data_9E4Q
# 
_entry.id   9E4Q 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   9E4Q         pdb_00009e4q 10.2210/pdb9e4q/pdb 
WWPDB D_1000289425 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2024-12-04 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9E4Q 
_pdbx_database_status.recvd_initial_deposition_date   2024-10-25 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB 'A DARPin fused to the 1TEL crystallization chaperone via a helical Lys-Gln-Arg linker' 9DP8 unspecified 
PDB 'A DARPin fused to the 1TEL crystallization chaperone via a direct helical fusion'      9DAM unspecified 
PDB 'A DARPin fused to the 1TEL crystallization chaperone via a proline-alanine linker'     9DB5 unspecified 
PDB 'A DARPin fused to the 1TEL crystallization chaperone via a direct helical fusion'      9DVG unspecified 
# 
_pdbx_contact_author.id                 4 
_pdbx_contact_author.email              james.moody@byu.edu 
_pdbx_contact_author.name_first         James 
_pdbx_contact_author.name_last          Moody 
_pdbx_contact_author.name_mi            D 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-2266-5348 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Pedroza Romo, M.J.' 1 0000-0002-7441-3874 
'Noakes, E.'         2 0009-0007-6957-3295 
'Soleimani, S.'      3 ?                   
'Smith, T.'          4 ?                   
'Doukov, T.'         5 0000-0001-8625-2572 
'Moody, J.D.'        6 0000-0003-2266-5348 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Optimal TELSAM-Target Protein Linker Character is Target Protein Dependent' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Pedroza Romo, M.J.' 1  0000-0002-7441-3874 
primary 'Averett, J.C.'      2  0000-0002-2287-1590 
primary 'Keliiliki, A.'      3  0009-0005-0460-2062 
primary 'Wilson, E.W.'       4  0000-0001-5009-2685 
primary 'Smith, C.'          5  ?                   
primary 'Hansen, D.'         6  0009-0009-5764-5524 
primary 'Averett, B.'        7  ?                   
primary 'Gonzalez, J.'       8  ?                   
primary 'Noakes, E.'         9  0009-0007-6957-3295 
primary 'Nickles, R.'        10 ?                   
primary 'Soleimani, S.'      11 ?                   
primary 'Doukov, T.'         12 0000-0001-8625-2572 
primary 'Moody, J.D.'        13 0000-0003-2266-5348 
# 
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 'Transcription factor ETV6,DARPin' 45603.230 1  ? ? ? ? 
2 non-polymer syn 'SULFATE ION'                      96.063    3  ? ? ? ? 
3 water       nat water                              18.015    12 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'ETS translocation variant 6,ETS-related protein Tel1,Tel' 
# 
_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       
;GSIRLPAHLRLQPIYWSRDDVAQWLKWAENEFSLRPIDSNTFEMNGKALLLLTKEDFRYRSPHSGDELYELLQHILKQRP
GGGGSTSIRLPAHLRLQPIYWSRDDVAQWLKWAENEFSLRPIDSNTFEMNGKALLLLTKEDFRYRSPHSGDVLYELLQHI
LKQRPGGGGSTSIRLPAHLRLQPIYWSRDDVAQWLKWAENEFSLRPIDSNTFEMNGKALLLLTKEDFRYRSPHSGDVLYE
LLQHILGGGDLGKKLLEAARAGQDDEVRILMANGADVNATDNDGYTPLHLAASNGHLEIVEVLLKNGADVNASDLTGITP
LHAAAATGHLEIVEVLLKHGADVNAYDNDGHTPLHLAAKYGHLEIVEVLLKHGADVNAQDKFGKTAFDISIDNGNEDLAE
ILQKLN
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GSIRLPAHLRLQPIYWSRDDVAQWLKWAENEFSLRPIDSNTFEMNGKALLLLTKEDFRYRSPHSGDELYELLQHILKQRP
GGGGSTSIRLPAHLRLQPIYWSRDDVAQWLKWAENEFSLRPIDSNTFEMNGKALLLLTKEDFRYRSPHSGDVLYELLQHI
LKQRPGGGGSTSIRLPAHLRLQPIYWSRDDVAQWLKWAENEFSLRPIDSNTFEMNGKALLLLTKEDFRYRSPHSGDVLYE
LLQHILGGGDLGKKLLEAARAGQDDEVRILMANGADVNATDNDGYTPLHLAASNGHLEIVEVLLKNGADVNASDLTGITP
LHAAAATGHLEIVEVLLKHGADVNAYDNDGHTPLHLAAKYGHLEIVEVLLKHGADVNAQDKFGKTAFDISIDNGNEDLAE
ILQKLN
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'SULFATE ION' SO4 
3 water         HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   SER n 
1 3   ILE n 
1 4   ARG n 
1 5   LEU n 
1 6   PRO n 
1 7   ALA n 
1 8   HIS n 
1 9   LEU n 
1 10  ARG n 
1 11  LEU n 
1 12  GLN n 
1 13  PRO n 
1 14  ILE n 
1 15  TYR n 
1 16  TRP n 
1 17  SER n 
1 18  ARG n 
1 19  ASP n 
1 20  ASP n 
1 21  VAL n 
1 22  ALA n 
1 23  GLN n 
1 24  TRP n 
1 25  LEU n 
1 26  LYS n 
1 27  TRP n 
1 28  ALA n 
1 29  GLU n 
1 30  ASN n 
1 31  GLU n 
1 32  PHE n 
1 33  SER n 
1 34  LEU n 
1 35  ARG n 
1 36  PRO n 
1 37  ILE n 
1 38  ASP n 
1 39  SER n 
1 40  ASN n 
1 41  THR n 
1 42  PHE n 
1 43  GLU n 
1 44  MET n 
1 45  ASN n 
1 46  GLY n 
1 47  LYS n 
1 48  ALA n 
1 49  LEU n 
1 50  LEU n 
1 51  LEU n 
1 52  LEU n 
1 53  THR n 
1 54  LYS n 
1 55  GLU n 
1 56  ASP n 
1 57  PHE n 
1 58  ARG n 
1 59  TYR n 
1 60  ARG n 
1 61  SER n 
1 62  PRO n 
1 63  HIS n 
1 64  SER n 
1 65  GLY n 
1 66  ASP n 
1 67  GLU n 
1 68  LEU n 
1 69  TYR n 
1 70  GLU n 
1 71  LEU n 
1 72  LEU n 
1 73  GLN n 
1 74  HIS n 
1 75  ILE n 
1 76  LEU n 
1 77  LYS n 
1 78  GLN n 
1 79  ARG n 
1 80  PRO n 
1 81  GLY n 
1 82  GLY n 
1 83  GLY n 
1 84  GLY n 
1 85  SER n 
1 86  THR n 
1 87  SER n 
1 88  ILE n 
1 89  ARG n 
1 90  LEU n 
1 91  PRO n 
1 92  ALA n 
1 93  HIS n 
1 94  LEU n 
1 95  ARG n 
1 96  LEU n 
1 97  GLN n 
1 98  PRO n 
1 99  ILE n 
1 100 TYR n 
1 101 TRP n 
1 102 SER n 
1 103 ARG n 
1 104 ASP n 
1 105 ASP n 
1 106 VAL n 
1 107 ALA n 
1 108 GLN n 
1 109 TRP n 
1 110 LEU n 
1 111 LYS n 
1 112 TRP n 
1 113 ALA n 
1 114 GLU n 
1 115 ASN n 
1 116 GLU n 
1 117 PHE n 
1 118 SER n 
1 119 LEU n 
1 120 ARG n 
1 121 PRO n 
1 122 ILE n 
1 123 ASP n 
1 124 SER n 
1 125 ASN n 
1 126 THR n 
1 127 PHE n 
1 128 GLU n 
1 129 MET n 
1 130 ASN n 
1 131 GLY n 
1 132 LYS n 
1 133 ALA n 
1 134 LEU n 
1 135 LEU n 
1 136 LEU n 
1 137 LEU n 
1 138 THR n 
1 139 LYS n 
1 140 GLU n 
1 141 ASP n 
1 142 PHE n 
1 143 ARG n 
1 144 TYR n 
1 145 ARG n 
1 146 SER n 
1 147 PRO n 
1 148 HIS n 
1 149 SER n 
1 150 GLY n 
1 151 ASP n 
1 152 VAL n 
1 153 LEU n 
1 154 TYR n 
1 155 GLU n 
1 156 LEU n 
1 157 LEU n 
1 158 GLN n 
1 159 HIS n 
1 160 ILE n 
1 161 LEU n 
1 162 LYS n 
1 163 GLN n 
1 164 ARG n 
1 165 PRO n 
1 166 GLY n 
1 167 GLY n 
1 168 GLY n 
1 169 GLY n 
1 170 SER n 
1 171 THR n 
1 172 SER n 
1 173 ILE n 
1 174 ARG n 
1 175 LEU n 
1 176 PRO n 
1 177 ALA n 
1 178 HIS n 
1 179 LEU n 
1 180 ARG n 
1 181 LEU n 
1 182 GLN n 
1 183 PRO n 
1 184 ILE n 
1 185 TYR n 
1 186 TRP n 
1 187 SER n 
1 188 ARG n 
1 189 ASP n 
1 190 ASP n 
1 191 VAL n 
1 192 ALA n 
1 193 GLN n 
1 194 TRP n 
1 195 LEU n 
1 196 LYS n 
1 197 TRP n 
1 198 ALA n 
1 199 GLU n 
1 200 ASN n 
1 201 GLU n 
1 202 PHE n 
1 203 SER n 
1 204 LEU n 
1 205 ARG n 
1 206 PRO n 
1 207 ILE n 
1 208 ASP n 
1 209 SER n 
1 210 ASN n 
1 211 THR n 
1 212 PHE n 
1 213 GLU n 
1 214 MET n 
1 215 ASN n 
1 216 GLY n 
1 217 LYS n 
1 218 ALA n 
1 219 LEU n 
1 220 LEU n 
1 221 LEU n 
1 222 LEU n 
1 223 THR n 
1 224 LYS n 
1 225 GLU n 
1 226 ASP n 
1 227 PHE n 
1 228 ARG n 
1 229 TYR n 
1 230 ARG n 
1 231 SER n 
1 232 PRO n 
1 233 HIS n 
1 234 SER n 
1 235 GLY n 
1 236 ASP n 
1 237 VAL n 
1 238 LEU n 
1 239 TYR n 
1 240 GLU n 
1 241 LEU n 
1 242 LEU n 
1 243 GLN n 
1 244 HIS n 
1 245 ILE n 
1 246 LEU n 
1 247 GLY n 
1 248 GLY n 
1 249 GLY n 
1 250 ASP n 
1 251 LEU n 
1 252 GLY n 
1 253 LYS n 
1 254 LYS n 
1 255 LEU n 
1 256 LEU n 
1 257 GLU n 
1 258 ALA n 
1 259 ALA n 
1 260 ARG n 
1 261 ALA n 
1 262 GLY n 
1 263 GLN n 
1 264 ASP n 
1 265 ASP n 
1 266 GLU n 
1 267 VAL n 
1 268 ARG n 
1 269 ILE n 
1 270 LEU n 
1 271 MET n 
1 272 ALA n 
1 273 ASN n 
1 274 GLY n 
1 275 ALA n 
1 276 ASP n 
1 277 VAL n 
1 278 ASN n 
1 279 ALA n 
1 280 THR n 
1 281 ASP n 
1 282 ASN n 
1 283 ASP n 
1 284 GLY n 
1 285 TYR n 
1 286 THR n 
1 287 PRO n 
1 288 LEU n 
1 289 HIS n 
1 290 LEU n 
1 291 ALA n 
1 292 ALA n 
1 293 SER n 
1 294 ASN n 
1 295 GLY n 
1 296 HIS n 
1 297 LEU n 
1 298 GLU n 
1 299 ILE n 
1 300 VAL n 
1 301 GLU n 
1 302 VAL n 
1 303 LEU n 
1 304 LEU n 
1 305 LYS n 
1 306 ASN n 
1 307 GLY n 
1 308 ALA n 
1 309 ASP n 
1 310 VAL n 
1 311 ASN n 
1 312 ALA n 
1 313 SER n 
1 314 ASP n 
1 315 LEU n 
1 316 THR n 
1 317 GLY n 
1 318 ILE n 
1 319 THR n 
1 320 PRO n 
1 321 LEU n 
1 322 HIS n 
1 323 ALA n 
1 324 ALA n 
1 325 ALA n 
1 326 ALA n 
1 327 THR n 
1 328 GLY n 
1 329 HIS n 
1 330 LEU n 
1 331 GLU n 
1 332 ILE n 
1 333 VAL n 
1 334 GLU n 
1 335 VAL n 
1 336 LEU n 
1 337 LEU n 
1 338 LYS n 
1 339 HIS n 
1 340 GLY n 
1 341 ALA n 
1 342 ASP n 
1 343 VAL n 
1 344 ASN n 
1 345 ALA n 
1 346 TYR n 
1 347 ASP n 
1 348 ASN n 
1 349 ASP n 
1 350 GLY n 
1 351 HIS n 
1 352 THR n 
1 353 PRO n 
1 354 LEU n 
1 355 HIS n 
1 356 LEU n 
1 357 ALA n 
1 358 ALA n 
1 359 LYS n 
1 360 TYR n 
1 361 GLY n 
1 362 HIS n 
1 363 LEU n 
1 364 GLU n 
1 365 ILE n 
1 366 VAL n 
1 367 GLU n 
1 368 VAL n 
1 369 LEU n 
1 370 LEU n 
1 371 LYS n 
1 372 HIS n 
1 373 GLY n 
1 374 ALA n 
1 375 ASP n 
1 376 VAL n 
1 377 ASN n 
1 378 ALA n 
1 379 GLN n 
1 380 ASP n 
1 381 LYS n 
1 382 PHE n 
1 383 GLY n 
1 384 LYS n 
1 385 THR n 
1 386 ALA n 
1 387 PHE n 
1 388 ASP n 
1 389 ILE n 
1 390 SER n 
1 391 ILE n 
1 392 ASP n 
1 393 ASN n 
1 394 GLY n 
1 395 ASN n 
1 396 GLU n 
1 397 ASP n 
1 398 LEU n 
1 399 ALA n 
1 400 GLU n 
1 401 ILE n 
1 402 LEU n 
1 403 GLN n 
1 404 LYS n 
1 405 LEU n 
1 406 ASN n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_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 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_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 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_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 
1 1 sample 'Biological sequence' 1   79  human ? 'ETV6, TEL, TEL1' ? ? ? ? ? ? 'Homo sapiens'        9606  ? ? ? ? ? ? ? ? 
'Escherichia coli B' 37762 ? ? ? ? ? ? B 'BL21(DE3)' ? ? ? ? ? ? ? ? ? ? ? ? ? 
1 2 sample 'Biological sequence' 80  164 human ? 'ETV6, TEL, TEL1' ? ? ? ? ? ? 'Homo sapiens'        9606  ? ? ? ? ? ? ? ? 
'Escherichia coli B' 37762 ? ? ? ? ? ? B 'BL21(DE3)' ? ? ? ? ? ? ? ? ? ? ? ? ? 
1 3 sample 'Biological sequence' 165 246 human ? 'ETV6, TEL, TEL1' ? ? ? ? ? ? 'Homo sapiens'        9606  ? ? ? ? ? ? ? ? 
'Escherichia coli B' 37762 ? ? ? ? ? ? B 'BL21(DE3)' ? ? ? ? ? ? ? ? ? ? ? ? ? 
1 4 sample 'Biological sequence' 247 406 ?     ? 'ETV6, TEL, TEL1' ? ? ? ? ? ? 'synthetic construct' 32630 ? ? ? ? ? ? ? ? 
'Escherichia coli B' 37762 ? ? ? ? ? ? B 'BL21(DE3)' ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
SO4 non-polymer         . 'SULFATE ION'   ? 'O4 S -2'        96.063  
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   ILE 3   3   ?   ?   ?   A . n 
A 1 4   ARG 4   4   ?   ?   ?   A . n 
A 1 5   LEU 5   5   ?   ?   ?   A . n 
A 1 6   PRO 6   6   ?   ?   ?   A . n 
A 1 7   ALA 7   7   ?   ?   ?   A . n 
A 1 8   HIS 8   8   ?   ?   ?   A . n 
A 1 9   LEU 9   9   ?   ?   ?   A . n 
A 1 10  ARG 10  10  ?   ?   ?   A . n 
A 1 11  LEU 11  11  ?   ?   ?   A . n 
A 1 12  GLN 12  12  12  GLN GLN A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  ILE 14  14  14  ILE ILE A . n 
A 1 15  TYR 15  15  15  TYR TYR A . n 
A 1 16  TRP 16  16  16  TRP TRP A . n 
A 1 17  SER 17  17  17  SER SER A . n 
A 1 18  ARG 18  18  18  ARG ARG A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  ASP 20  20  20  ASP ASP A . n 
A 1 21  VAL 21  21  21  VAL VAL A . n 
A 1 22  ALA 22  22  22  ALA ALA A . n 
A 1 23  GLN 23  23  23  GLN GLN A . n 
A 1 24  TRP 24  24  24  TRP TRP A . n 
A 1 25  LEU 25  25  25  LEU LEU A . n 
A 1 26  LYS 26  26  26  LYS LYS A . n 
A 1 27  TRP 27  27  27  TRP TRP A . n 
A 1 28  ALA 28  28  28  ALA ALA A . n 
A 1 29  GLU 29  29  29  GLU GLU A . n 
A 1 30  ASN 30  30  30  ASN ASN A . n 
A 1 31  GLU 31  31  31  GLU GLU A . n 
A 1 32  PHE 32  32  32  PHE PHE A . n 
A 1 33  SER 33  33  33  SER SER A . n 
A 1 34  LEU 34  34  34  LEU LEU A . n 
A 1 35  ARG 35  35  35  ARG ARG A . n 
A 1 36  PRO 36  36  36  PRO PRO A . n 
A 1 37  ILE 37  37  37  ILE ILE A . n 
A 1 38  ASP 38  38  38  ASP ASP A . n 
A 1 39  SER 39  39  39  SER SER A . n 
A 1 40  ASN 40  40  40  ASN ASN A . n 
A 1 41  THR 41  41  41  THR THR A . n 
A 1 42  PHE 42  42  42  PHE PHE A . n 
A 1 43  GLU 43  43  43  GLU GLU A . n 
A 1 44  MET 44  44  44  MET MET A . n 
A 1 45  ASN 45  45  45  ASN ASN A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  LYS 47  47  47  LYS LYS A . n 
A 1 48  ALA 48  48  48  ALA ALA A . n 
A 1 49  LEU 49  49  49  LEU LEU A . n 
A 1 50  LEU 50  50  50  LEU LEU A . n 
A 1 51  LEU 51  51  51  LEU LEU A . n 
A 1 52  LEU 52  52  52  LEU LEU A . n 
A 1 53  THR 53  53  53  THR THR A . n 
A 1 54  LYS 54  54  54  LYS LYS A . n 
A 1 55  GLU 55  55  55  GLU GLU A . n 
A 1 56  ASP 56  56  56  ASP ASP A . n 
A 1 57  PHE 57  57  57  PHE PHE A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  TYR 59  59  59  TYR TYR A . n 
A 1 60  ARG 60  60  60  ARG ARG A . n 
A 1 61  SER 61  61  61  SER SER A . n 
A 1 62  PRO 62  62  62  PRO PRO A . n 
A 1 63  HIS 63  63  63  HIS HIS A . n 
A 1 64  SER 64  64  64  SER SER A . n 
A 1 65  GLY 65  65  65  GLY GLY A . n 
A 1 66  ASP 66  66  66  ASP ASP A . n 
A 1 67  GLU 67  67  67  GLU GLU A . n 
A 1 68  LEU 68  68  68  LEU LEU A . n 
A 1 69  TYR 69  69  69  TYR TYR A . n 
A 1 70  GLU 70  70  70  GLU GLU A . n 
A 1 71  LEU 71  71  71  LEU LEU A . n 
A 1 72  LEU 72  72  72  LEU LEU A . n 
A 1 73  GLN 73  73  73  GLN GLN A . n 
A 1 74  HIS 74  74  74  HIS HIS A . n 
A 1 75  ILE 75  75  75  ILE ILE A . n 
A 1 76  LEU 76  76  76  LEU LEU A . n 
A 1 77  LYS 77  77  77  LYS LYS A . n 
A 1 78  GLN 78  78  78  GLN GLN A . n 
A 1 79  ARG 79  79  ?   ?   ?   A . n 
A 1 80  PRO 80  80  ?   ?   ?   A . n 
A 1 81  GLY 81  81  ?   ?   ?   A . n 
A 1 82  GLY 82  82  ?   ?   ?   A . n 
A 1 83  GLY 83  83  ?   ?   ?   A . n 
A 1 84  GLY 84  84  ?   ?   ?   A . n 
A 1 85  SER 85  85  ?   ?   ?   A . n 
A 1 86  THR 86  86  ?   ?   ?   A . n 
A 1 87  SER 87  87  ?   ?   ?   A . n 
A 1 88  ILE 88  88  88  ILE ILE A . n 
A 1 89  ARG 89  89  89  ARG ARG A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  PRO 91  91  91  PRO PRO A . n 
A 1 92  ALA 92  92  92  ALA ALA A . n 
A 1 93  HIS 93  93  93  HIS HIS A . n 
A 1 94  LEU 94  94  94  LEU LEU A . n 
A 1 95  ARG 95  95  95  ARG ARG A . n 
A 1 96  LEU 96  96  96  LEU LEU A . n 
A 1 97  GLN 97  97  97  GLN GLN A . n 
A 1 98  PRO 98  98  98  PRO PRO A . n 
A 1 99  ILE 99  99  99  ILE ILE A . n 
A 1 100 TYR 100 100 100 TYR TYR A . n 
A 1 101 TRP 101 101 101 TRP TRP A . n 
A 1 102 SER 102 102 102 SER SER A . n 
A 1 103 ARG 103 103 103 ARG ARG A . n 
A 1 104 ASP 104 104 104 ASP ASP A . n 
A 1 105 ASP 105 105 105 ASP ASP A . n 
A 1 106 VAL 106 106 106 VAL VAL A . n 
A 1 107 ALA 107 107 107 ALA ALA A . n 
A 1 108 GLN 108 108 108 GLN GLN A . n 
A 1 109 TRP 109 109 109 TRP TRP A . n 
A 1 110 LEU 110 110 110 LEU LEU A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 TRP 112 112 112 TRP TRP A . n 
A 1 113 ALA 113 113 113 ALA ALA A . n 
A 1 114 GLU 114 114 114 GLU GLU A . n 
A 1 115 ASN 115 115 115 ASN ASN A . n 
A 1 116 GLU 116 116 116 GLU GLU A . n 
A 1 117 PHE 117 117 117 PHE PHE A . n 
A 1 118 SER 118 118 118 SER SER A . n 
A 1 119 LEU 119 119 119 LEU LEU A . n 
A 1 120 ARG 120 120 120 ARG ARG A . n 
A 1 121 PRO 121 121 121 PRO PRO A . n 
A 1 122 ILE 122 122 122 ILE ILE A . n 
A 1 123 ASP 123 123 123 ASP ASP A . n 
A 1 124 SER 124 124 124 SER SER A . n 
A 1 125 ASN 125 125 125 ASN ASN A . n 
A 1 126 THR 126 126 126 THR THR A . n 
A 1 127 PHE 127 127 127 PHE PHE A . n 
A 1 128 GLU 128 128 128 GLU GLU A . n 
A 1 129 MET 129 129 129 MET MET A . n 
A 1 130 ASN 130 130 130 ASN ASN A . n 
A 1 131 GLY 131 131 131 GLY GLY A . n 
A 1 132 LYS 132 132 132 LYS LYS A . n 
A 1 133 ALA 133 133 133 ALA ALA A . n 
A 1 134 LEU 134 134 134 LEU LEU A . n 
A 1 135 LEU 135 135 135 LEU LEU A . n 
A 1 136 LEU 136 136 136 LEU LEU A . n 
A 1 137 LEU 137 137 137 LEU LEU A . n 
A 1 138 THR 138 138 138 THR THR A . n 
A 1 139 LYS 139 139 139 LYS LYS A . n 
A 1 140 GLU 140 140 140 GLU GLU A . n 
A 1 141 ASP 141 141 141 ASP ASP A . n 
A 1 142 PHE 142 142 142 PHE PHE A . n 
A 1 143 ARG 143 143 143 ARG ARG A . n 
A 1 144 TYR 144 144 144 TYR TYR A . n 
A 1 145 ARG 145 145 145 ARG ARG A . n 
A 1 146 SER 146 146 146 SER SER A . n 
A 1 147 PRO 147 147 147 PRO PRO A . n 
A 1 148 HIS 148 148 148 HIS HIS A . n 
A 1 149 SER 149 149 149 SER SER A . n 
A 1 150 GLY 150 150 150 GLY GLY A . n 
A 1 151 ASP 151 151 151 ASP ASP A . n 
A 1 152 VAL 152 152 152 VAL VAL A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 TYR 154 154 154 TYR TYR A . n 
A 1 155 GLU 155 155 155 GLU GLU A . n 
A 1 156 LEU 156 156 156 LEU LEU A . n 
A 1 157 LEU 157 157 157 LEU LEU A . n 
A 1 158 GLN 158 158 158 GLN GLN A . n 
A 1 159 HIS 159 159 159 HIS HIS A . n 
A 1 160 ILE 160 160 160 ILE ILE A . n 
A 1 161 LEU 161 161 161 LEU LEU A . n 
A 1 162 LYS 162 162 162 LYS LYS A . n 
A 1 163 GLN 163 163 163 GLN GLN A . n 
A 1 164 ARG 164 164 164 ARG ARG A . n 
A 1 165 PRO 165 165 ?   ?   ?   A . n 
A 1 166 GLY 166 166 ?   ?   ?   A . n 
A 1 167 GLY 167 167 ?   ?   ?   A . n 
A 1 168 GLY 168 168 ?   ?   ?   A . n 
A 1 169 GLY 169 169 ?   ?   ?   A . n 
A 1 170 SER 170 170 ?   ?   ?   A . n 
A 1 171 THR 171 171 ?   ?   ?   A . n 
A 1 172 SER 172 172 ?   ?   ?   A . n 
A 1 173 ILE 173 173 ?   ?   ?   A . n 
A 1 174 ARG 174 174 ?   ?   ?   A . n 
A 1 175 LEU 175 175 175 LEU LEU A . n 
A 1 176 PRO 176 176 176 PRO PRO A . n 
A 1 177 ALA 177 177 177 ALA ALA A . n 
A 1 178 HIS 178 178 178 HIS HIS A . n 
A 1 179 LEU 179 179 179 LEU LEU A . n 
A 1 180 ARG 180 180 180 ARG ARG A . n 
A 1 181 LEU 181 181 181 LEU LEU A . n 
A 1 182 GLN 182 182 182 GLN GLN A . n 
A 1 183 PRO 183 183 183 PRO PRO A . n 
A 1 184 ILE 184 184 184 ILE ILE A . n 
A 1 185 TYR 185 185 185 TYR TYR A . n 
A 1 186 TRP 186 186 186 TRP TRP A . n 
A 1 187 SER 187 187 187 SER SER A . n 
A 1 188 ARG 188 188 188 ARG ARG A . n 
A 1 189 ASP 189 189 189 ASP ASP A . n 
A 1 190 ASP 190 190 190 ASP ASP A . n 
A 1 191 VAL 191 191 191 VAL VAL A . n 
A 1 192 ALA 192 192 192 ALA ALA A . n 
A 1 193 GLN 193 193 193 GLN GLN A . n 
A 1 194 TRP 194 194 194 TRP TRP A . n 
A 1 195 LEU 195 195 195 LEU LEU A . n 
A 1 196 LYS 196 196 196 LYS LYS A . n 
A 1 197 TRP 197 197 197 TRP TRP A . n 
A 1 198 ALA 198 198 198 ALA ALA A . n 
A 1 199 GLU 199 199 199 GLU GLU A . n 
A 1 200 ASN 200 200 200 ASN ASN A . n 
A 1 201 GLU 201 201 201 GLU GLU A . n 
A 1 202 PHE 202 202 202 PHE PHE A . n 
A 1 203 SER 203 203 203 SER SER A . n 
A 1 204 LEU 204 204 204 LEU LEU A . n 
A 1 205 ARG 205 205 205 ARG ARG A . n 
A 1 206 PRO 206 206 206 PRO PRO A . n 
A 1 207 ILE 207 207 207 ILE ILE A . n 
A 1 208 ASP 208 208 208 ASP ASP A . n 
A 1 209 SER 209 209 209 SER SER A . n 
A 1 210 ASN 210 210 210 ASN ASN A . n 
A 1 211 THR 211 211 211 THR THR A . n 
A 1 212 PHE 212 212 212 PHE PHE A . n 
A 1 213 GLU 213 213 213 GLU GLU A . n 
A 1 214 MET 214 214 214 MET MET A . n 
A 1 215 ASN 215 215 215 ASN ASN A . n 
A 1 216 GLY 216 216 216 GLY GLY A . n 
A 1 217 LYS 217 217 217 LYS LYS A . n 
A 1 218 ALA 218 218 218 ALA ALA A . n 
A 1 219 LEU 219 219 219 LEU LEU A . n 
A 1 220 LEU 220 220 220 LEU LEU A . n 
A 1 221 LEU 221 221 221 LEU LEU A . n 
A 1 222 LEU 222 222 222 LEU LEU A . n 
A 1 223 THR 223 223 223 THR THR A . n 
A 1 224 LYS 224 224 224 LYS LYS A . n 
A 1 225 GLU 225 225 225 GLU GLU A . n 
A 1 226 ASP 226 226 226 ASP ASP A . n 
A 1 227 PHE 227 227 227 PHE PHE A . n 
A 1 228 ARG 228 228 228 ARG ARG A . n 
A 1 229 TYR 229 229 229 TYR TYR A . n 
A 1 230 ARG 230 230 230 ARG ARG A . n 
A 1 231 SER 231 231 231 SER SER A . n 
A 1 232 PRO 232 232 232 PRO PRO A . n 
A 1 233 HIS 233 233 233 HIS HIS A . n 
A 1 234 SER 234 234 234 SER SER A . n 
A 1 235 GLY 235 235 235 GLY GLY A . n 
A 1 236 ASP 236 236 236 ASP ASP A . n 
A 1 237 VAL 237 237 237 VAL VAL A . n 
A 1 238 LEU 238 238 238 LEU LEU A . n 
A 1 239 TYR 239 239 239 TYR TYR A . n 
A 1 240 GLU 240 240 240 GLU GLU A . n 
A 1 241 LEU 241 241 241 LEU LEU A . n 
A 1 242 LEU 242 242 242 LEU LEU A . n 
A 1 243 GLN 243 243 243 GLN GLN A . n 
A 1 244 HIS 244 244 244 HIS HIS A . n 
A 1 245 ILE 245 245 245 ILE ILE A . n 
A 1 246 LEU 246 246 246 LEU LEU A . n 
A 1 247 GLY 247 247 247 GLY GLY A . n 
A 1 248 GLY 248 248 ?   ?   ?   A . n 
A 1 249 GLY 249 249 ?   ?   ?   A . n 
A 1 250 ASP 250 250 ?   ?   ?   A . n 
A 1 251 LEU 251 251 251 LEU LEU A . n 
A 1 252 GLY 252 252 252 GLY GLY A . n 
A 1 253 LYS 253 253 253 LYS LYS A . n 
A 1 254 LYS 254 254 254 LYS LYS A . n 
A 1 255 LEU 255 255 255 LEU LEU A . n 
A 1 256 LEU 256 256 256 LEU LEU A . n 
A 1 257 GLU 257 257 257 GLU GLU A . n 
A 1 258 ALA 258 258 258 ALA ALA A . n 
A 1 259 ALA 259 259 259 ALA ALA A . n 
A 1 260 ARG 260 260 260 ARG ARG A . n 
A 1 261 ALA 261 261 261 ALA ALA A . n 
A 1 262 GLY 262 262 262 GLY GLY A . n 
A 1 263 GLN 263 263 263 GLN GLN A . n 
A 1 264 ASP 264 264 264 ASP ASP A . n 
A 1 265 ASP 265 265 265 ASP ASP A . n 
A 1 266 GLU 266 266 266 GLU GLU A . n 
A 1 267 VAL 267 267 267 VAL VAL A . n 
A 1 268 ARG 268 268 268 ARG ARG A . n 
A 1 269 ILE 269 269 269 ILE ILE A . n 
A 1 270 LEU 270 270 270 LEU LEU A . n 
A 1 271 MET 271 271 271 MET MET A . n 
A 1 272 ALA 272 272 272 ALA ALA A . n 
A 1 273 ASN 273 273 273 ASN ASN A . n 
A 1 274 GLY 274 274 274 GLY GLY A . n 
A 1 275 ALA 275 275 275 ALA ALA A . n 
A 1 276 ASP 276 276 276 ASP ASP A . n 
A 1 277 VAL 277 277 277 VAL VAL A . n 
A 1 278 ASN 278 278 278 ASN ASN A . n 
A 1 279 ALA 279 279 279 ALA ALA A . n 
A 1 280 THR 280 280 280 THR THR A . n 
A 1 281 ASP 281 281 281 ASP ASP A . n 
A 1 282 ASN 282 282 282 ASN ASN A . n 
A 1 283 ASP 283 283 283 ASP ASP A . n 
A 1 284 GLY 284 284 284 GLY GLY A . n 
A 1 285 TYR 285 285 285 TYR TYR A . n 
A 1 286 THR 286 286 286 THR THR A . n 
A 1 287 PRO 287 287 287 PRO PRO A . n 
A 1 288 LEU 288 288 288 LEU LEU A . n 
A 1 289 HIS 289 289 289 HIS HIS A . n 
A 1 290 LEU 290 290 290 LEU LEU A . n 
A 1 291 ALA 291 291 291 ALA ALA A . n 
A 1 292 ALA 292 292 292 ALA ALA A . n 
A 1 293 SER 293 293 293 SER SER A . n 
A 1 294 ASN 294 294 294 ASN ASN A . n 
A 1 295 GLY 295 295 295 GLY GLY A . n 
A 1 296 HIS 296 296 296 HIS HIS A . n 
A 1 297 LEU 297 297 297 LEU LEU A . n 
A 1 298 GLU 298 298 298 GLU GLU A . n 
A 1 299 ILE 299 299 299 ILE ILE A . n 
A 1 300 VAL 300 300 300 VAL VAL A . n 
A 1 301 GLU 301 301 301 GLU GLU A . n 
A 1 302 VAL 302 302 302 VAL VAL A . n 
A 1 303 LEU 303 303 303 LEU LEU A . n 
A 1 304 LEU 304 304 304 LEU LEU A . n 
A 1 305 LYS 305 305 305 LYS LYS A . n 
A 1 306 ASN 306 306 306 ASN ASN A . n 
A 1 307 GLY 307 307 307 GLY GLY A . n 
A 1 308 ALA 308 308 308 ALA ALA A . n 
A 1 309 ASP 309 309 309 ASP ASP A . n 
A 1 310 VAL 310 310 310 VAL VAL A . n 
A 1 311 ASN 311 311 311 ASN ASN A . n 
A 1 312 ALA 312 312 312 ALA ALA A . n 
A 1 313 SER 313 313 313 SER SER A . n 
A 1 314 ASP 314 314 314 ASP ASP A . n 
A 1 315 LEU 315 315 315 LEU LEU A . n 
A 1 316 THR 316 316 316 THR THR A . n 
A 1 317 GLY 317 317 317 GLY GLY A . n 
A 1 318 ILE 318 318 318 ILE ILE A . n 
A 1 319 THR 319 319 319 THR THR A . n 
A 1 320 PRO 320 320 320 PRO PRO A . n 
A 1 321 LEU 321 321 321 LEU LEU A . n 
A 1 322 HIS 322 322 322 HIS HIS A . n 
A 1 323 ALA 323 323 323 ALA ALA A . n 
A 1 324 ALA 324 324 324 ALA ALA A . n 
A 1 325 ALA 325 325 325 ALA ALA A . n 
A 1 326 ALA 326 326 326 ALA ALA A . n 
A 1 327 THR 327 327 327 THR THR A . n 
A 1 328 GLY 328 328 328 GLY GLY A . n 
A 1 329 HIS 329 329 329 HIS HIS A . n 
A 1 330 LEU 330 330 330 LEU LEU A . n 
A 1 331 GLU 331 331 331 GLU GLU A . n 
A 1 332 ILE 332 332 332 ILE ILE A . n 
A 1 333 VAL 333 333 333 VAL VAL A . n 
A 1 334 GLU 334 334 334 GLU GLU A . n 
A 1 335 VAL 335 335 335 VAL VAL A . n 
A 1 336 LEU 336 336 336 LEU LEU A . n 
A 1 337 LEU 337 337 337 LEU LEU A . n 
A 1 338 LYS 338 338 338 LYS LYS A . n 
A 1 339 HIS 339 339 339 HIS HIS A . n 
A 1 340 GLY 340 340 340 GLY GLY A . n 
A 1 341 ALA 341 341 341 ALA ALA A . n 
A 1 342 ASP 342 342 342 ASP ASP A . n 
A 1 343 VAL 343 343 343 VAL VAL A . n 
A 1 344 ASN 344 344 344 ASN ASN A . n 
A 1 345 ALA 345 345 345 ALA ALA A . n 
A 1 346 TYR 346 346 346 TYR TYR A . n 
A 1 347 ASP 347 347 347 ASP ASP A . n 
A 1 348 ASN 348 348 348 ASN ASN A . n 
A 1 349 ASP 349 349 349 ASP ASP A . n 
A 1 350 GLY 350 350 350 GLY GLY A . n 
A 1 351 HIS 351 351 351 HIS HIS A . n 
A 1 352 THR 352 352 352 THR THR A . n 
A 1 353 PRO 353 353 353 PRO PRO A . n 
A 1 354 LEU 354 354 354 LEU LEU A . n 
A 1 355 HIS 355 355 355 HIS HIS A . n 
A 1 356 LEU 356 356 356 LEU LEU A . n 
A 1 357 ALA 357 357 357 ALA ALA A . n 
A 1 358 ALA 358 358 358 ALA ALA A . n 
A 1 359 LYS 359 359 359 LYS LYS A . n 
A 1 360 TYR 360 360 360 TYR TYR A . n 
A 1 361 GLY 361 361 361 GLY GLY A . n 
A 1 362 HIS 362 362 362 HIS HIS A . n 
A 1 363 LEU 363 363 363 LEU LEU A . n 
A 1 364 GLU 364 364 364 GLU GLU A . n 
A 1 365 ILE 365 365 365 ILE ILE A . n 
A 1 366 VAL 366 366 366 VAL VAL A . n 
A 1 367 GLU 367 367 367 GLU GLU A . n 
A 1 368 VAL 368 368 368 VAL VAL A . n 
A 1 369 LEU 369 369 369 LEU LEU A . n 
A 1 370 LEU 370 370 370 LEU LEU A . n 
A 1 371 LYS 371 371 371 LYS LYS A . n 
A 1 372 HIS 372 372 372 HIS HIS A . n 
A 1 373 GLY 373 373 373 GLY GLY A . n 
A 1 374 ALA 374 374 374 ALA ALA A . n 
A 1 375 ASP 375 375 375 ASP ASP A . n 
A 1 376 VAL 376 376 376 VAL VAL A . n 
A 1 377 ASN 377 377 377 ASN ASN A . n 
A 1 378 ALA 378 378 378 ALA ALA A . n 
A 1 379 GLN 379 379 379 GLN GLN A . n 
A 1 380 ASP 380 380 380 ASP ASP A . n 
A 1 381 LYS 381 381 381 LYS LYS A . n 
A 1 382 PHE 382 382 382 PHE PHE A . n 
A 1 383 GLY 383 383 383 GLY GLY A . n 
A 1 384 LYS 384 384 384 LYS LYS A . n 
A 1 385 THR 385 385 385 THR THR A . n 
A 1 386 ALA 386 386 386 ALA ALA A . n 
A 1 387 PHE 387 387 387 PHE PHE A . n 
A 1 388 ASP 388 388 388 ASP ASP A . n 
A 1 389 ILE 389 389 389 ILE ILE A . n 
A 1 390 SER 390 390 390 SER SER A . n 
A 1 391 ILE 391 391 391 ILE ILE A . n 
A 1 392 ASP 392 392 392 ASP ASP A . n 
A 1 393 ASN 393 393 393 ASN ASN A . n 
A 1 394 GLY 394 394 394 GLY GLY A . n 
A 1 395 ASN 395 395 395 ASN ASN A . n 
A 1 396 GLU 396 396 396 GLU GLU A . n 
A 1 397 ASP 397 397 397 ASP ASP A . n 
A 1 398 LEU 398 398 398 LEU LEU A . n 
A 1 399 ALA 399 399 399 ALA ALA A . n 
A 1 400 GLU 400 400 400 GLU GLU A . n 
A 1 401 ILE 401 401 401 ILE ILE A . n 
A 1 402 LEU 402 402 402 LEU LEU A . n 
A 1 403 GLN 403 403 ?   ?   ?   A . n 
A 1 404 LYS 404 404 ?   ?   ?   A . n 
A 1 405 LEU 405 405 ?   ?   ?   A . n 
A 1 406 ASN 406 406 ?   ?   ?   A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 SO4 1  501 1  SO4 SO4 A . 
C 2 SO4 1  502 2  SO4 SO4 A . 
D 2 SO4 1  503 3  SO4 SO4 A . 
E 3 HOH 1  601 5  HOH HOH A . 
E 3 HOH 2  602 11 HOH HOH A . 
E 3 HOH 3  603 16 HOH HOH A . 
E 3 HOH 4  604 3  HOH HOH A . 
E 3 HOH 5  605 2  HOH HOH A . 
E 3 HOH 6  606 1  HOH HOH A . 
E 3 HOH 7  607 8  HOH HOH A . 
E 3 HOH 8  608 14 HOH HOH A . 
E 3 HOH 9  609 19 HOH HOH A . 
E 3 HOH 10 610 7  HOH HOH A . 
E 3 HOH 11 611 21 HOH HOH A . 
E 3 HOH 12 612 9  HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A GLN 12  ? CG  ? A GLN 12  CG  
2   1 Y 1 A GLN 12  ? CD  ? A GLN 12  CD  
3   1 Y 1 A GLN 12  ? OE1 ? A GLN 12  OE1 
4   1 Y 1 A GLN 12  ? NE2 ? A GLN 12  NE2 
5   1 Y 1 A ILE 14  ? CD1 ? A ILE 14  CD1 
6   1 Y 1 A SER 17  ? OG  ? A SER 17  OG  
7   1 Y 1 A ARG 18  ? CG  ? A ARG 18  CG  
8   1 Y 1 A ARG 18  ? CD  ? A ARG 18  CD  
9   1 Y 1 A ARG 18  ? NE  ? A ARG 18  NE  
10  1 Y 1 A ARG 18  ? CZ  ? A ARG 18  CZ  
11  1 Y 1 A ARG 18  ? NH1 ? A ARG 18  NH1 
12  1 Y 1 A ARG 18  ? NH2 ? A ARG 18  NH2 
13  1 Y 1 A GLN 23  ? CG  ? A GLN 23  CG  
14  1 Y 1 A GLN 23  ? CD  ? A GLN 23  CD  
15  1 Y 1 A GLN 23  ? OE1 ? A GLN 23  OE1 
16  1 Y 1 A GLN 23  ? NE2 ? A GLN 23  NE2 
17  1 Y 1 A LYS 26  ? CG  ? A LYS 26  CG  
18  1 Y 1 A LYS 26  ? CD  ? A LYS 26  CD  
19  1 Y 1 A LYS 26  ? CE  ? A LYS 26  CE  
20  1 Y 1 A LYS 26  ? NZ  ? A LYS 26  NZ  
21  1 Y 1 A SER 33  ? OG  ? A SER 33  OG  
22  1 Y 1 A ILE 37  ? CG1 ? A ILE 37  CG1 
23  1 Y 1 A ILE 37  ? CG2 ? A ILE 37  CG2 
24  1 Y 1 A ILE 37  ? CD1 ? A ILE 37  CD1 
25  1 Y 1 A SER 39  ? OG  ? A SER 39  OG  
26  1 Y 1 A ASN 40  ? CG  ? A ASN 40  CG  
27  1 Y 1 A ASN 40  ? OD1 ? A ASN 40  OD1 
28  1 Y 1 A ASN 40  ? ND2 ? A ASN 40  ND2 
29  1 Y 1 A GLU 43  ? CG  ? A GLU 43  CG  
30  1 Y 1 A GLU 43  ? CD  ? A GLU 43  CD  
31  1 Y 1 A GLU 43  ? OE1 ? A GLU 43  OE1 
32  1 Y 1 A GLU 43  ? OE2 ? A GLU 43  OE2 
33  1 Y 1 A LYS 47  ? CG  ? A LYS 47  CG  
34  1 Y 1 A LYS 47  ? CD  ? A LYS 47  CD  
35  1 Y 1 A LYS 47  ? CE  ? A LYS 47  CE  
36  1 Y 1 A LYS 47  ? NZ  ? A LYS 47  NZ  
37  1 Y 1 A LEU 50  ? CD1 ? A LEU 50  CD1 
38  1 Y 1 A LEU 50  ? CD2 ? A LEU 50  CD2 
39  1 Y 1 A LYS 54  ? CE  ? A LYS 54  CE  
40  1 Y 1 A LYS 54  ? NZ  ? A LYS 54  NZ  
41  1 Y 1 A GLU 55  ? CG  ? A GLU 55  CG  
42  1 Y 1 A GLU 55  ? CD  ? A GLU 55  CD  
43  1 Y 1 A GLU 55  ? OE1 ? A GLU 55  OE1 
44  1 Y 1 A GLU 55  ? OE2 ? A GLU 55  OE2 
45  1 Y 1 A TYR 59  ? CG  ? A TYR 59  CG  
46  1 Y 1 A TYR 59  ? CD1 ? A TYR 59  CD1 
47  1 Y 1 A TYR 59  ? CD2 ? A TYR 59  CD2 
48  1 Y 1 A TYR 59  ? CE1 ? A TYR 59  CE1 
49  1 Y 1 A TYR 59  ? CE2 ? A TYR 59  CE2 
50  1 Y 1 A TYR 59  ? CZ  ? A TYR 59  CZ  
51  1 Y 1 A TYR 59  ? OH  ? A TYR 59  OH  
52  1 Y 1 A SER 64  ? OG  ? A SER 64  OG  
53  1 Y 1 A ASP 66  ? CG  ? A ASP 66  CG  
54  1 Y 1 A ASP 66  ? OD1 ? A ASP 66  OD1 
55  1 Y 1 A ASP 66  ? OD2 ? A ASP 66  OD2 
56  1 Y 1 A GLU 67  ? CG  ? A GLU 67  CG  
57  1 Y 1 A GLU 67  ? CD  ? A GLU 67  CD  
58  1 Y 1 A GLU 67  ? OE1 ? A GLU 67  OE1 
59  1 Y 1 A GLU 67  ? OE2 ? A GLU 67  OE2 
60  1 Y 1 A LEU 71  ? CD1 ? A LEU 71  CD1 
61  1 Y 1 A LEU 71  ? CD2 ? A LEU 71  CD2 
62  1 Y 1 A LEU 72  ? CD1 ? A LEU 72  CD1 
63  1 Y 1 A LEU 72  ? CD2 ? A LEU 72  CD2 
64  1 Y 1 A ILE 75  ? CD1 ? A ILE 75  CD1 
65  1 Y 1 A LEU 76  ? CG  ? A LEU 76  CG  
66  1 Y 1 A LEU 76  ? CD1 ? A LEU 76  CD1 
67  1 Y 1 A LEU 76  ? CD2 ? A LEU 76  CD2 
68  1 Y 1 A LYS 77  ? CG  ? A LYS 77  CG  
69  1 Y 1 A LYS 77  ? CD  ? A LYS 77  CD  
70  1 Y 1 A LYS 77  ? CE  ? A LYS 77  CE  
71  1 Y 1 A LYS 77  ? NZ  ? A LYS 77  NZ  
72  1 Y 1 A GLN 78  ? CG  ? A GLN 78  CG  
73  1 Y 1 A GLN 78  ? CD  ? A GLN 78  CD  
74  1 Y 1 A GLN 78  ? OE1 ? A GLN 78  OE1 
75  1 Y 1 A GLN 78  ? NE2 ? A GLN 78  NE2 
76  1 Y 1 A ILE 88  ? CG1 ? A ILE 88  CG1 
77  1 Y 1 A ILE 88  ? CG2 ? A ILE 88  CG2 
78  1 Y 1 A ILE 88  ? CD1 ? A ILE 88  CD1 
79  1 Y 1 A ARG 89  ? CG  ? A ARG 89  CG  
80  1 Y 1 A ARG 89  ? CD  ? A ARG 89  CD  
81  1 Y 1 A ARG 89  ? NE  ? A ARG 89  NE  
82  1 Y 1 A ARG 89  ? CZ  ? A ARG 89  CZ  
83  1 Y 1 A ARG 89  ? NH1 ? A ARG 89  NH1 
84  1 Y 1 A ARG 89  ? NH2 ? A ARG 89  NH2 
85  1 Y 1 A LEU 90  ? CG  ? A LEU 90  CG  
86  1 Y 1 A LEU 90  ? CD1 ? A LEU 90  CD1 
87  1 Y 1 A LEU 90  ? CD2 ? A LEU 90  CD2 
88  1 Y 1 A HIS 93  ? ND1 ? A HIS 93  ND1 
89  1 Y 1 A HIS 93  ? CD2 ? A HIS 93  CD2 
90  1 Y 1 A HIS 93  ? CE1 ? A HIS 93  CE1 
91  1 Y 1 A HIS 93  ? NE2 ? A HIS 93  NE2 
92  1 Y 1 A ARG 95  ? CG  ? A ARG 95  CG  
93  1 Y 1 A ARG 95  ? CD  ? A ARG 95  CD  
94  1 Y 1 A ARG 95  ? NE  ? A ARG 95  NE  
95  1 Y 1 A ARG 95  ? CZ  ? A ARG 95  CZ  
96  1 Y 1 A ARG 95  ? NH1 ? A ARG 95  NH1 
97  1 Y 1 A ARG 95  ? NH2 ? A ARG 95  NH2 
98  1 Y 1 A ILE 99  ? CD1 ? A ILE 99  CD1 
99  1 Y 1 A LYS 111 ? CG  ? A LYS 111 CG  
100 1 Y 1 A LYS 111 ? CD  ? A LYS 111 CD  
101 1 Y 1 A LYS 111 ? CE  ? A LYS 111 CE  
102 1 Y 1 A LYS 111 ? NZ  ? A LYS 111 NZ  
103 1 Y 1 A ASN 115 ? CG  ? A ASN 115 CG  
104 1 Y 1 A ASN 115 ? OD1 ? A ASN 115 OD1 
105 1 Y 1 A ASN 115 ? ND2 ? A ASN 115 ND2 
106 1 Y 1 A ARG 120 ? CG  ? A ARG 120 CG  
107 1 Y 1 A ARG 120 ? CD  ? A ARG 120 CD  
108 1 Y 1 A ARG 120 ? NE  ? A ARG 120 NE  
109 1 Y 1 A ARG 120 ? CZ  ? A ARG 120 CZ  
110 1 Y 1 A ARG 120 ? NH1 ? A ARG 120 NH1 
111 1 Y 1 A ARG 120 ? NH2 ? A ARG 120 NH2 
112 1 Y 1 A ILE 122 ? CD1 ? A ILE 122 CD1 
113 1 Y 1 A SER 124 ? OG  ? A SER 124 OG  
114 1 Y 1 A ASN 125 ? CG  ? A ASN 125 CG  
115 1 Y 1 A ASN 125 ? OD1 ? A ASN 125 OD1 
116 1 Y 1 A ASN 125 ? ND2 ? A ASN 125 ND2 
117 1 Y 1 A LYS 132 ? CG  ? A LYS 132 CG  
118 1 Y 1 A LYS 132 ? CD  ? A LYS 132 CD  
119 1 Y 1 A LYS 132 ? CE  ? A LYS 132 CE  
120 1 Y 1 A LYS 132 ? NZ  ? A LYS 132 NZ  
121 1 Y 1 A LYS 139 ? CG  ? A LYS 139 CG  
122 1 Y 1 A LYS 139 ? CD  ? A LYS 139 CD  
123 1 Y 1 A LYS 139 ? CE  ? A LYS 139 CE  
124 1 Y 1 A LYS 139 ? NZ  ? A LYS 139 NZ  
125 1 Y 1 A GLU 140 ? CG  ? A GLU 140 CG  
126 1 Y 1 A GLU 140 ? CD  ? A GLU 140 CD  
127 1 Y 1 A GLU 140 ? OE1 ? A GLU 140 OE1 
128 1 Y 1 A GLU 140 ? OE2 ? A GLU 140 OE2 
129 1 Y 1 A SER 146 ? OG  ? A SER 146 OG  
130 1 Y 1 A SER 149 ? OG  ? A SER 149 OG  
131 1 Y 1 A VAL 152 ? CG1 ? A VAL 152 CG1 
132 1 Y 1 A VAL 152 ? CG2 ? A VAL 152 CG2 
133 1 Y 1 A ILE 160 ? CD1 ? A ILE 160 CD1 
134 1 Y 1 A LYS 162 ? CG  ? A LYS 162 CG  
135 1 Y 1 A LYS 162 ? CD  ? A LYS 162 CD  
136 1 Y 1 A LYS 162 ? CE  ? A LYS 162 CE  
137 1 Y 1 A LYS 162 ? NZ  ? A LYS 162 NZ  
138 1 Y 1 A ARG 164 ? CG  ? A ARG 164 CG  
139 1 Y 1 A ARG 164 ? CD  ? A ARG 164 CD  
140 1 Y 1 A ARG 164 ? NE  ? A ARG 164 NE  
141 1 Y 1 A ARG 164 ? CZ  ? A ARG 164 CZ  
142 1 Y 1 A ARG 164 ? NH1 ? A ARG 164 NH1 
143 1 Y 1 A ARG 164 ? NH2 ? A ARG 164 NH2 
144 1 Y 1 A LEU 175 ? CG  ? A LEU 175 CG  
145 1 Y 1 A LEU 175 ? CD1 ? A LEU 175 CD1 
146 1 Y 1 A LEU 175 ? CD2 ? A LEU 175 CD2 
147 1 Y 1 A HIS 178 ? CG  ? A HIS 178 CG  
148 1 Y 1 A HIS 178 ? ND1 ? A HIS 178 ND1 
149 1 Y 1 A HIS 178 ? CD2 ? A HIS 178 CD2 
150 1 Y 1 A HIS 178 ? CE1 ? A HIS 178 CE1 
151 1 Y 1 A HIS 178 ? NE2 ? A HIS 178 NE2 
152 1 Y 1 A LEU 181 ? CG  ? A LEU 181 CG  
153 1 Y 1 A LEU 181 ? CD1 ? A LEU 181 CD1 
154 1 Y 1 A LEU 181 ? CD2 ? A LEU 181 CD2 
155 1 Y 1 A ASP 190 ? CG  ? A ASP 190 CG  
156 1 Y 1 A ASP 190 ? OD1 ? A ASP 190 OD1 
157 1 Y 1 A ASP 190 ? OD2 ? A ASP 190 OD2 
158 1 Y 1 A GLN 193 ? OE1 ? A GLN 193 OE1 
159 1 Y 1 A GLN 193 ? NE2 ? A GLN 193 NE2 
160 1 Y 1 A LYS 196 ? CG  ? A LYS 196 CG  
161 1 Y 1 A LYS 196 ? CD  ? A LYS 196 CD  
162 1 Y 1 A LYS 196 ? CE  ? A LYS 196 CE  
163 1 Y 1 A LYS 196 ? NZ  ? A LYS 196 NZ  
164 1 Y 1 A SER 209 ? OG  ? A SER 209 OG  
165 1 Y 1 A ASN 210 ? CG  ? A ASN 210 CG  
166 1 Y 1 A ASN 210 ? OD1 ? A ASN 210 OD1 
167 1 Y 1 A ASN 210 ? ND2 ? A ASN 210 ND2 
168 1 Y 1 A GLU 213 ? CG  ? A GLU 213 CG  
169 1 Y 1 A GLU 213 ? CD  ? A GLU 213 CD  
170 1 Y 1 A GLU 213 ? OE1 ? A GLU 213 OE1 
171 1 Y 1 A GLU 213 ? OE2 ? A GLU 213 OE2 
172 1 Y 1 A LYS 217 ? CG  ? A LYS 217 CG  
173 1 Y 1 A LYS 217 ? CD  ? A LYS 217 CD  
174 1 Y 1 A LYS 217 ? CE  ? A LYS 217 CE  
175 1 Y 1 A LYS 217 ? NZ  ? A LYS 217 NZ  
176 1 Y 1 A LYS 224 ? CG  ? A LYS 224 CG  
177 1 Y 1 A LYS 224 ? CD  ? A LYS 224 CD  
178 1 Y 1 A LYS 224 ? CE  ? A LYS 224 CE  
179 1 Y 1 A LYS 224 ? NZ  ? A LYS 224 NZ  
180 1 Y 1 A GLU 225 ? CG  ? A GLU 225 CG  
181 1 Y 1 A GLU 225 ? CD  ? A GLU 225 CD  
182 1 Y 1 A GLU 225 ? OE1 ? A GLU 225 OE1 
183 1 Y 1 A GLU 225 ? OE2 ? A GLU 225 OE2 
184 1 Y 1 A TYR 229 ? CG  ? A TYR 229 CG  
185 1 Y 1 A TYR 229 ? CD1 ? A TYR 229 CD1 
186 1 Y 1 A TYR 229 ? CD2 ? A TYR 229 CD2 
187 1 Y 1 A TYR 229 ? CE1 ? A TYR 229 CE1 
188 1 Y 1 A TYR 229 ? CE2 ? A TYR 229 CE2 
189 1 Y 1 A TYR 229 ? CZ  ? A TYR 229 CZ  
190 1 Y 1 A TYR 229 ? OH  ? A TYR 229 OH  
191 1 Y 1 A HIS 244 ? CG  ? A HIS 244 CG  
192 1 Y 1 A HIS 244 ? ND1 ? A HIS 244 ND1 
193 1 Y 1 A HIS 244 ? CD2 ? A HIS 244 CD2 
194 1 Y 1 A HIS 244 ? CE1 ? A HIS 244 CE1 
195 1 Y 1 A HIS 244 ? NE2 ? A HIS 244 NE2 
196 1 Y 1 A ILE 245 ? CD1 ? A ILE 245 CD1 
197 1 Y 1 A LEU 251 ? CG  ? A LEU 251 CG  
198 1 Y 1 A LEU 251 ? CD1 ? A LEU 251 CD1 
199 1 Y 1 A LEU 251 ? CD2 ? A LEU 251 CD2 
200 1 Y 1 A LYS 253 ? CG  ? A LYS 253 CG  
201 1 Y 1 A LYS 253 ? CD  ? A LYS 253 CD  
202 1 Y 1 A LYS 253 ? CE  ? A LYS 253 CE  
203 1 Y 1 A LYS 253 ? NZ  ? A LYS 253 NZ  
204 1 Y 1 A LYS 254 ? CG  ? A LYS 254 CG  
205 1 Y 1 A LYS 254 ? CD  ? A LYS 254 CD  
206 1 Y 1 A LYS 254 ? CE  ? A LYS 254 CE  
207 1 Y 1 A LYS 254 ? NZ  ? A LYS 254 NZ  
208 1 Y 1 A LEU 255 ? CG  ? A LEU 255 CG  
209 1 Y 1 A LEU 255 ? CD1 ? A LEU 255 CD1 
210 1 Y 1 A LEU 255 ? CD2 ? A LEU 255 CD2 
211 1 Y 1 A LEU 256 ? CG  ? A LEU 256 CG  
212 1 Y 1 A LEU 256 ? CD1 ? A LEU 256 CD1 
213 1 Y 1 A LEU 256 ? CD2 ? A LEU 256 CD2 
214 1 Y 1 A GLU 257 ? CG  ? A GLU 257 CG  
215 1 Y 1 A GLU 257 ? CD  ? A GLU 257 CD  
216 1 Y 1 A GLU 257 ? OE1 ? A GLU 257 OE1 
217 1 Y 1 A GLU 257 ? OE2 ? A GLU 257 OE2 
218 1 Y 1 A ARG 260 ? CG  ? A ARG 260 CG  
219 1 Y 1 A ARG 260 ? CD  ? A ARG 260 CD  
220 1 Y 1 A ARG 260 ? NE  ? A ARG 260 NE  
221 1 Y 1 A ARG 260 ? CZ  ? A ARG 260 CZ  
222 1 Y 1 A ARG 260 ? NH1 ? A ARG 260 NH1 
223 1 Y 1 A ARG 260 ? NH2 ? A ARG 260 NH2 
224 1 Y 1 A GLN 263 ? CG  ? A GLN 263 CG  
225 1 Y 1 A GLN 263 ? CD  ? A GLN 263 CD  
226 1 Y 1 A GLN 263 ? OE1 ? A GLN 263 OE1 
227 1 Y 1 A GLN 263 ? NE2 ? A GLN 263 NE2 
228 1 Y 1 A ASP 264 ? CG  ? A ASP 264 CG  
229 1 Y 1 A ASP 264 ? OD1 ? A ASP 264 OD1 
230 1 Y 1 A ASP 264 ? OD2 ? A ASP 264 OD2 
231 1 Y 1 A ASP 265 ? CG  ? A ASP 265 CG  
232 1 Y 1 A ASP 265 ? OD1 ? A ASP 265 OD1 
233 1 Y 1 A ASP 265 ? OD2 ? A ASP 265 OD2 
234 1 Y 1 A GLU 266 ? CG  ? A GLU 266 CG  
235 1 Y 1 A GLU 266 ? CD  ? A GLU 266 CD  
236 1 Y 1 A GLU 266 ? OE1 ? A GLU 266 OE1 
237 1 Y 1 A GLU 266 ? OE2 ? A GLU 266 OE2 
238 1 Y 1 A VAL 267 ? CG1 ? A VAL 267 CG1 
239 1 Y 1 A VAL 267 ? CG2 ? A VAL 267 CG2 
240 1 Y 1 A ILE 269 ? CG1 ? A ILE 269 CG1 
241 1 Y 1 A ILE 269 ? CG2 ? A ILE 269 CG2 
242 1 Y 1 A ILE 269 ? CD1 ? A ILE 269 CD1 
243 1 Y 1 A LEU 270 ? CG  ? A LEU 270 CG  
244 1 Y 1 A LEU 270 ? CD1 ? A LEU 270 CD1 
245 1 Y 1 A LEU 270 ? CD2 ? A LEU 270 CD2 
246 1 Y 1 A ASN 282 ? CG  ? A ASN 282 CG  
247 1 Y 1 A ASN 282 ? OD1 ? A ASN 282 OD1 
248 1 Y 1 A ASN 282 ? ND2 ? A ASN 282 ND2 
249 1 Y 1 A LEU 297 ? CG  ? A LEU 297 CG  
250 1 Y 1 A LEU 297 ? CD1 ? A LEU 297 CD1 
251 1 Y 1 A LEU 297 ? CD2 ? A LEU 297 CD2 
252 1 Y 1 A GLU 298 ? CG  ? A GLU 298 CG  
253 1 Y 1 A GLU 298 ? CD  ? A GLU 298 CD  
254 1 Y 1 A GLU 298 ? OE1 ? A GLU 298 OE1 
255 1 Y 1 A GLU 298 ? OE2 ? A GLU 298 OE2 
256 1 Y 1 A ILE 299 ? CG1 ? A ILE 299 CG1 
257 1 Y 1 A ILE 299 ? CG2 ? A ILE 299 CG2 
258 1 Y 1 A ILE 299 ? CD1 ? A ILE 299 CD1 
259 1 Y 1 A VAL 300 ? CG1 ? A VAL 300 CG1 
260 1 Y 1 A VAL 300 ? CG2 ? A VAL 300 CG2 
261 1 Y 1 A LYS 305 ? CG  ? A LYS 305 CG  
262 1 Y 1 A LYS 305 ? CD  ? A LYS 305 CD  
263 1 Y 1 A LYS 305 ? CE  ? A LYS 305 CE  
264 1 Y 1 A LYS 305 ? NZ  ? A LYS 305 NZ  
265 1 Y 1 A VAL 310 ? CG1 ? A VAL 310 CG1 
266 1 Y 1 A VAL 310 ? CG2 ? A VAL 310 CG2 
267 1 Y 1 A SER 313 ? OG  ? A SER 313 OG  
268 1 Y 1 A LEU 315 ? CG  ? A LEU 315 CG  
269 1 Y 1 A LEU 315 ? CD1 ? A LEU 315 CD1 
270 1 Y 1 A LEU 315 ? CD2 ? A LEU 315 CD2 
271 1 Y 1 A ILE 318 ? CD1 ? A ILE 318 CD1 
272 1 Y 1 A LEU 330 ? CG  ? A LEU 330 CG  
273 1 Y 1 A LEU 330 ? CD1 ? A LEU 330 CD1 
274 1 Y 1 A LEU 330 ? CD2 ? A LEU 330 CD2 
275 1 Y 1 A GLU 331 ? CG  ? A GLU 331 CG  
276 1 Y 1 A GLU 331 ? CD  ? A GLU 331 CD  
277 1 Y 1 A GLU 331 ? OE1 ? A GLU 331 OE1 
278 1 Y 1 A GLU 331 ? OE2 ? A GLU 331 OE2 
279 1 Y 1 A ILE 332 ? CD1 ? A ILE 332 CD1 
280 1 Y 1 A GLU 334 ? CG  ? A GLU 334 CG  
281 1 Y 1 A GLU 334 ? CD  ? A GLU 334 CD  
282 1 Y 1 A GLU 334 ? OE1 ? A GLU 334 OE1 
283 1 Y 1 A GLU 334 ? OE2 ? A GLU 334 OE2 
284 1 Y 1 A TYR 346 ? CG  ? A TYR 346 CG  
285 1 Y 1 A TYR 346 ? CD1 ? A TYR 346 CD1 
286 1 Y 1 A TYR 346 ? CD2 ? A TYR 346 CD2 
287 1 Y 1 A TYR 346 ? CE1 ? A TYR 346 CE1 
288 1 Y 1 A TYR 346 ? CE2 ? A TYR 346 CE2 
289 1 Y 1 A TYR 346 ? CZ  ? A TYR 346 CZ  
290 1 Y 1 A TYR 346 ? OH  ? A TYR 346 OH  
291 1 Y 1 A THR 352 ? OG1 ? A THR 352 OG1 
292 1 Y 1 A THR 352 ? CG2 ? A THR 352 CG2 
293 1 Y 1 A LEU 354 ? CD1 ? A LEU 354 CD1 
294 1 Y 1 A LEU 354 ? CD2 ? A LEU 354 CD2 
295 1 Y 1 A HIS 355 ? ND1 ? A HIS 355 ND1 
296 1 Y 1 A HIS 355 ? CD2 ? A HIS 355 CD2 
297 1 Y 1 A HIS 355 ? CE1 ? A HIS 355 CE1 
298 1 Y 1 A HIS 355 ? NE2 ? A HIS 355 NE2 
299 1 Y 1 A LEU 356 ? CD1 ? A LEU 356 CD1 
300 1 Y 1 A LEU 356 ? CD2 ? A LEU 356 CD2 
301 1 Y 1 A LYS 359 ? CG  ? A LYS 359 CG  
302 1 Y 1 A LYS 359 ? CD  ? A LYS 359 CD  
303 1 Y 1 A LYS 359 ? CE  ? A LYS 359 CE  
304 1 Y 1 A LYS 359 ? NZ  ? A LYS 359 NZ  
305 1 Y 1 A LEU 363 ? CG  ? A LEU 363 CG  
306 1 Y 1 A LEU 363 ? CD1 ? A LEU 363 CD1 
307 1 Y 1 A LEU 363 ? CD2 ? A LEU 363 CD2 
308 1 Y 1 A ILE 365 ? CD1 ? A ILE 365 CD1 
309 1 Y 1 A VAL 366 ? CG1 ? A VAL 366 CG1 
310 1 Y 1 A VAL 366 ? CG2 ? A VAL 366 CG2 
311 1 Y 1 A GLU 367 ? CG  ? A GLU 367 CG  
312 1 Y 1 A GLU 367 ? CD  ? A GLU 367 CD  
313 1 Y 1 A GLU 367 ? OE1 ? A GLU 367 OE1 
314 1 Y 1 A GLU 367 ? OE2 ? A GLU 367 OE2 
315 1 Y 1 A VAL 368 ? CG1 ? A VAL 368 CG1 
316 1 Y 1 A VAL 368 ? CG2 ? A VAL 368 CG2 
317 1 Y 1 A LEU 370 ? CD1 ? A LEU 370 CD1 
318 1 Y 1 A LEU 370 ? CD2 ? A LEU 370 CD2 
319 1 Y 1 A LYS 371 ? CG  ? A LYS 371 CG  
320 1 Y 1 A LYS 371 ? CD  ? A LYS 371 CD  
321 1 Y 1 A LYS 371 ? CE  ? A LYS 371 CE  
322 1 Y 1 A LYS 371 ? NZ  ? A LYS 371 NZ  
323 1 Y 1 A VAL 376 ? CG1 ? A VAL 376 CG1 
324 1 Y 1 A VAL 376 ? CG2 ? A VAL 376 CG2 
325 1 Y 1 A ASN 377 ? CG  ? A ASN 377 CG  
326 1 Y 1 A ASN 377 ? OD1 ? A ASN 377 OD1 
327 1 Y 1 A ASN 377 ? ND2 ? A ASN 377 ND2 
328 1 Y 1 A GLN 379 ? CG  ? A GLN 379 CG  
329 1 Y 1 A GLN 379 ? CD  ? A GLN 379 CD  
330 1 Y 1 A GLN 379 ? OE1 ? A GLN 379 OE1 
331 1 Y 1 A GLN 379 ? NE2 ? A GLN 379 NE2 
332 1 Y 1 A LYS 381 ? CG  ? A LYS 381 CG  
333 1 Y 1 A LYS 381 ? CD  ? A LYS 381 CD  
334 1 Y 1 A LYS 381 ? CE  ? A LYS 381 CE  
335 1 Y 1 A LYS 381 ? NZ  ? A LYS 381 NZ  
336 1 Y 1 A PHE 382 ? CD1 ? A PHE 382 CD1 
337 1 Y 1 A PHE 382 ? CD2 ? A PHE 382 CD2 
338 1 Y 1 A PHE 382 ? CE1 ? A PHE 382 CE1 
339 1 Y 1 A PHE 382 ? CE2 ? A PHE 382 CE2 
340 1 Y 1 A PHE 382 ? CZ  ? A PHE 382 CZ  
341 1 Y 1 A LYS 384 ? CG  ? A LYS 384 CG  
342 1 Y 1 A LYS 384 ? CD  ? A LYS 384 CD  
343 1 Y 1 A LYS 384 ? CE  ? A LYS 384 CE  
344 1 Y 1 A LYS 384 ? NZ  ? A LYS 384 NZ  
345 1 Y 1 A PHE 387 ? CG  ? A PHE 387 CG  
346 1 Y 1 A PHE 387 ? CD1 ? A PHE 387 CD1 
347 1 Y 1 A PHE 387 ? CD2 ? A PHE 387 CD2 
348 1 Y 1 A PHE 387 ? CE1 ? A PHE 387 CE1 
349 1 Y 1 A PHE 387 ? CE2 ? A PHE 387 CE2 
350 1 Y 1 A PHE 387 ? CZ  ? A PHE 387 CZ  
351 1 Y 1 A ASP 388 ? OD1 ? A ASP 388 OD1 
352 1 Y 1 A ASP 388 ? OD2 ? A ASP 388 OD2 
353 1 Y 1 A ILE 389 ? CG1 ? A ILE 389 CG1 
354 1 Y 1 A ILE 389 ? CG2 ? A ILE 389 CG2 
355 1 Y 1 A ILE 389 ? CD1 ? A ILE 389 CD1 
356 1 Y 1 A SER 390 ? OG  ? A SER 390 OG  
357 1 Y 1 A ILE 391 ? CG1 ? A ILE 391 CG1 
358 1 Y 1 A ILE 391 ? CG2 ? A ILE 391 CG2 
359 1 Y 1 A ILE 391 ? CD1 ? A ILE 391 CD1 
360 1 Y 1 A ASP 392 ? CG  ? A ASP 392 CG  
361 1 Y 1 A ASP 392 ? OD1 ? A ASP 392 OD1 
362 1 Y 1 A ASP 392 ? OD2 ? A ASP 392 OD2 
363 1 Y 1 A ASN 393 ? CG  ? A ASN 393 CG  
364 1 Y 1 A ASN 393 ? OD1 ? A ASN 393 OD1 
365 1 Y 1 A ASN 393 ? ND2 ? A ASN 393 ND2 
366 1 Y 1 A ASN 395 ? CG  ? A ASN 395 CG  
367 1 Y 1 A ASN 395 ? OD1 ? A ASN 395 OD1 
368 1 Y 1 A ASN 395 ? ND2 ? A ASN 395 ND2 
369 1 Y 1 A GLU 396 ? CG  ? A GLU 396 CG  
370 1 Y 1 A GLU 396 ? CD  ? A GLU 396 CD  
371 1 Y 1 A GLU 396 ? OE1 ? A GLU 396 OE1 
372 1 Y 1 A GLU 396 ? OE2 ? A GLU 396 OE2 
373 1 Y 1 A ASP 397 ? CG  ? A ASP 397 CG  
374 1 Y 1 A ASP 397 ? OD1 ? A ASP 397 OD1 
375 1 Y 1 A ASP 397 ? OD2 ? A ASP 397 OD2 
376 1 Y 1 A LEU 398 ? CG  ? A LEU 398 CG  
377 1 Y 1 A LEU 398 ? CD1 ? A LEU 398 CD1 
378 1 Y 1 A LEU 398 ? CD2 ? A LEU 398 CD2 
379 1 Y 1 A GLU 400 ? CG  ? A GLU 400 CG  
380 1 Y 1 A GLU 400 ? CD  ? A GLU 400 CD  
381 1 Y 1 A GLU 400 ? OE1 ? A GLU 400 OE1 
382 1 Y 1 A GLU 400 ? OE2 ? A GLU 400 OE2 
383 1 Y 1 A ILE 401 ? CD1 ? A ILE 401 CD1 
384 1 Y 1 A LEU 402 ? CG  ? A LEU 402 CG  
385 1 Y 1 A LEU 402 ? CD1 ? A LEU 402 CD1 
386 1 Y 1 A LEU 402 ? CD2 ? A LEU 402 CD2 
# 
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 
? 'model building' ? ? ? ? ? ? ? ? ? ? ? Coot     ? ? ? .           1 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.20.1_4487 2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS      ? ? ? .           3 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .           4 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .           5 
# 
_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                     9E4Q 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     46.140 
_cell.length_a_esd                 ? 
_cell.length_b                     85.500 
_cell.length_b_esd                 ? 
_cell.length_c                     120.675 
_cell.length_c_esd                 ? 
_cell.volume                       476059.255 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9E4Q 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            'P 2ac 2ab' 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_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                   9E4Q 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          38.52 
_exptl_crystal.description                  'Needles with a hexagonal cross section' 
_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              6.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.05 M Ammonium sulfate, 0.05 M BIS-TRIS pH 6.5, Polyethylene glycol 600' 
_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                      'Mirror: Rh coated flat bent M0, toroidal focusing post-monochromator M1' 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-12-08 
_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                    'Si(111) and Si(220) double crystal' 
_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   0.97946 
_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                        'SSRL BEAMLINE BL9-2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97946 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL9-2 
_diffrn_source.pdbx_synchrotron_site       SSRL 
# 
_reflns.B_iso_Wilson_estimate                          80.00 
_reflns.entry_id                                       9E4Q 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              3.58 
_reflns.d_resolution_low                               42.75 
_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                                     6014 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.59 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                12.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.55 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.2945 
_reflns.pdbx_Rpim_I_all                                0.08171 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.993 
_reflns.pdbx_CC_star                                   0.998 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.2825 
_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                                    3.58 
_reflns_shell.d_res_low                                     3.708 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.36 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             586 
_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                               11.5 
_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                               1.187 
_reflns_shell.pdbx_Rpim_I_all                               0.3483 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.828 
_reflns_shell.pdbx_CC_star                                  0.952 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          98.99 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.132 
_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                               68.68 
_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                                 9E4Q 
_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                            3.58 
_refine.ls_d_res_low                             42.75 
_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                     6014 
_refine.ls_number_reflns_R_free                  310 
_refine.ls_number_reflns_R_work                  5704 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.65 
_refine.ls_percent_reflns_R_free                 5.15 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2711 
_refine.ls_R_factor_R_free                       0.3244 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2684 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_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                 31.7155 
_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                            0.4587 
_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                       3.58 
_refine_hist.d_res_low                        42.75 
_refine_hist.number_atoms_solvent             12 
_refine_hist.number_atoms_total               2612 
_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        2585 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         15 
_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' ? 0.0033 ? 2667 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.5038 ? 3671 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0382 ? 421  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0042 ? 488  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 9.1621 ? 838  ? 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' 3.58 4.51  . . 174 2768 99.76 . . . . 0.2724 . . . . . . . . . . . 0.3278 
'X-RAY DIFFRACTION' 4.51 42.75 . . 136 2936 99.55 . . . . 0.2658 . . . . . . . . . . . 0.3214 
# 
_struct.entry_id                     9E4Q 
_struct.title                        'A DARPin fused to the 3TEL crystallization chaperone via a gly-gly-gly fusion' 
_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        9E4Q 
_struct_keywords.text            'TELSAM, DARPin, ETV6, Designed Ankyrin Repeat Protein, PROTEIN BINDING' 
_struct_keywords.pdbx_keywords   'PROTEIN BINDING' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP ETV6_HUMAN P41212 ? 1 SIRLPAHLRLQPIYWSRDDVAQWLKWAENEFSLRPIDSNTFEMNGKALLLLTKEDFRYRSPHSGDVLYELLQHILKQR 47  
2 UNP ETV6_HUMAN P41212 ? 1 SIRLPAHLRLQPIYWSRDDVAQWLKWAENEFSLRPIDSNTFEMNGKALLLLTKEDFRYRSPHSGDVLYELLQHIL    47  
3 PDB 9E4Q       9E4Q   ? 1 ?                                                                              247 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9E4Q A 2   ? 79  ? P41212 47  ? 124 ? 2   79  
2 1 9E4Q A 87  ? 164 ? P41212 47  ? 124 ? 87  164 
3 2 9E4Q A 172 ? 246 ? P41212 47  ? 121 ? 172 246 
4 3 9E4Q A 247 ? 406 ? 9E4Q   247 ? 406 ? 247 406 
# 
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 9E4Q GLY A 1   ? UNP P41212 ?   ?   'expression tag'      1   1  
1 9E4Q GLU A 67  ? UNP P41212 VAL 112 'engineered mutation' 67  2  
1 9E4Q PRO A 80  ? UNP P41212 ?   ?   linker                80  3  
1 9E4Q GLY A 81  ? UNP P41212 ?   ?   linker                81  4  
1 9E4Q GLY A 82  ? UNP P41212 ?   ?   linker                82  5  
1 9E4Q GLY A 83  ? UNP P41212 ?   ?   linker                83  6  
1 9E4Q GLY A 84  ? UNP P41212 ?   ?   linker                84  7  
1 9E4Q SER A 85  ? UNP P41212 ?   ?   linker                85  8  
1 9E4Q THR A 86  ? UNP P41212 ?   ?   linker                86  9  
2 9E4Q PRO A 165 ? UNP P41212 ?   ?   linker                165 10 
2 9E4Q GLY A 166 ? UNP P41212 ?   ?   linker                166 11 
2 9E4Q GLY A 167 ? UNP P41212 ?   ?   linker                167 12 
2 9E4Q GLY A 168 ? UNP P41212 ?   ?   linker                168 13 
2 9E4Q GLY A 169 ? UNP P41212 ?   ?   linker                169 14 
2 9E4Q SER A 170 ? UNP P41212 ?   ?   linker                170 15 
2 9E4Q THR A 171 ? UNP P41212 ?   ?   linker                171 16 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLN A 12  ? TRP A 16  ? GLN A 12  TRP A 16  5 ? 5  
HELX_P HELX_P2  AA2 SER A 17  ? PHE A 32  ? SER A 17  PHE A 32  1 ? 16 
HELX_P HELX_P3  AA3 ASP A 38  ? GLU A 43  ? ASP A 38  GLU A 43  5 ? 6  
HELX_P HELX_P4  AA4 ASN A 45  ? LEU A 52  ? ASN A 45  LEU A 52  1 ? 8  
HELX_P HELX_P5  AA5 THR A 53  ? SER A 61  ? THR A 53  SER A 61  1 ? 9  
HELX_P HELX_P6  AA6 SER A 64  ? GLN A 78  ? SER A 64  GLN A 78  1 ? 15 
HELX_P HELX_P7  AA7 PRO A 91  ? ARG A 95  ? PRO A 91  ARG A 95  5 ? 5  
HELX_P HELX_P8  AA8 GLN A 97  ? TRP A 101 ? GLN A 97  TRP A 101 5 ? 5  
HELX_P HELX_P9  AA9 SER A 102 ? SER A 118 ? SER A 102 SER A 118 1 ? 17 
HELX_P HELX_P10 AB1 ASP A 123 ? GLU A 128 ? ASP A 123 GLU A 128 5 ? 6  
HELX_P HELX_P11 AB2 ASN A 130 ? LEU A 137 ? ASN A 130 LEU A 137 1 ? 8  
HELX_P HELX_P12 AB3 THR A 138 ? SER A 146 ? THR A 138 SER A 146 1 ? 9  
HELX_P HELX_P13 AB4 SER A 149 ? GLN A 163 ? SER A 149 GLN A 163 1 ? 15 
HELX_P HELX_P14 AB5 PRO A 176 ? ARG A 180 ? PRO A 176 ARG A 180 5 ? 5  
HELX_P HELX_P15 AB6 GLN A 182 ? TRP A 186 ? GLN A 182 TRP A 186 5 ? 5  
HELX_P HELX_P16 AB7 SER A 187 ? PHE A 202 ? SER A 187 PHE A 202 1 ? 16 
HELX_P HELX_P17 AB8 ASP A 208 ? GLU A 213 ? ASP A 208 GLU A 213 5 ? 6  
HELX_P HELX_P18 AB9 ASN A 215 ? LEU A 222 ? ASN A 215 LEU A 222 1 ? 8  
HELX_P HELX_P19 AC1 THR A 223 ? SER A 231 ? THR A 223 SER A 231 1 ? 9  
HELX_P HELX_P20 AC2 SER A 234 ? GLY A 247 ? SER A 234 GLY A 247 1 ? 14 
HELX_P HELX_P21 AC3 GLY A 252 ? GLU A 257 ? GLY A 252 GLU A 257 1 ? 6  
HELX_P HELX_P22 AC4 ALA A 258 ? GLY A 262 ? ALA A 258 GLY A 262 5 ? 5  
HELX_P HELX_P23 AC5 GLN A 263 ? GLY A 274 ? GLN A 263 GLY A 274 1 ? 12 
HELX_P HELX_P24 AC6 THR A 286 ? ASN A 294 ? THR A 286 ASN A 294 1 ? 9  
HELX_P HELX_P25 AC7 HIS A 296 ? ASN A 306 ? HIS A 296 ASN A 306 1 ? 11 
HELX_P HELX_P26 AC8 THR A 319 ? THR A 327 ? THR A 319 THR A 327 1 ? 9  
HELX_P HELX_P27 AC9 HIS A 329 ? HIS A 339 ? HIS A 329 HIS A 339 1 ? 11 
HELX_P HELX_P28 AD1 THR A 352 ? TYR A 360 ? THR A 352 TYR A 360 1 ? 9  
HELX_P HELX_P29 AD2 HIS A 362 ? HIS A 372 ? HIS A 362 HIS A 372 1 ? 11 
HELX_P HELX_P30 AD3 THR A 385 ? ASN A 393 ? THR A 385 ASN A 393 1 ? 9  
HELX_P HELX_P31 AD4 ASN A 395 ? GLU A 400 ? ASN A 395 GLU A 400 1 ? 6  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_pdbx_entry_details.entry_id                   9E4Q 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     N 
_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 SER A 64  ? ? -140.79 23.60   
2 1 ASN A 278 ? ? -100.34 40.13   
3 1 ASP A 347 ? ? -79.41  -168.90 
4 1 GLU A 400 ? ? -68.58  66.62   
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 x+1/2,-y+1/2,-z 
3 -x,y+1/2,-z+1/2 
4 -x+1/2,-y,z+1/2 
# 
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 15.8497879467 40.9735747868  -1.22883278851 0.492208274935 ? -0.0737203879328  ? 0.0309585808832  
? 0.347713769908 ? 0.0997938495436  ? 0.739455529676 ? 2.70099129769 ? -0.726966112718 ? -2.57164679889 ? 2.39602670729 ? 
2.15687140773    ? 6.38042154093 ? 0.415216165568 ? -0.0240413426834 ? 0.455727819096 ? -0.331919013305 ? -0.0692816444081  ? 
0.182394325233  ? -1.30782913879  ? 0.062182110665  ? -0.488988286211 ? 
2 'X-RAY DIFFRACTION' ? refined 26.159392157  23.185417572   -17.9548641589 0.3101812146   ? 0.00576891541365  ? 0.00391080897388 
? 0.47022566461  ? -0.037305495762  ? 0.393742846188 ? 1.30298304699 ? -0.477494309633 ? -0.90811783983 ? 6.05528675295 ? 
-0.0501862941211 ? 2.70230083182 ? 0.14806392224  ? 0.161453171047   ? 0.234082527046 ? 0.196960198541  ? -0.00540064980557 ? 
-0.365959147272 ? -0.102673845228 ? 0.0162637022249 ? -0.133694284153 ? 
3 'X-RAY DIFFRACTION' ? refined 11.2888060372 -8.76748447105 -19.0027002886 0.492703429503 ? -0.00828757531962 ? 0.106810150317   
? 0.533960253232 ? -0.0164749705078 ? 0.58497643553  ? 1.97359701513 ? 3.20409407978   ? 0.390808904291 ? 4.74752210372 ? 
0.253162109395   ? 6.42047828523 ? 0.342379500108 ? -0.490462220368  ? 0.214720339859 ? 1.08936926096   ? -0.2219140073     ? 
0.27693710698   ? -0.269746895377 ? -0.162469985634 ? -0.160017332447 ? 
# 
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 12  ? A 82  A 102 ? ? 
;chain 'A' and (resid 12 through 102 )
;
2 'X-RAY DIFFRACTION' 2 A 83  A 103 ? A 228 A 261 ? ? 
;chain 'A' and (resid 103 through 261 )
;
3 'X-RAY DIFFRACTION' 3 A 229 A 262 ? A 369 A 402 ? ? 
;chain 'A' and (resid 262 through 402 )
;
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 611 ? 6.14 . 
2 1 O ? A HOH 612 ? 7.35 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY 1   ? A GLY 1   
2  1 Y 1 A SER 2   ? A SER 2   
3  1 Y 1 A ILE 3   ? A ILE 3   
4  1 Y 1 A ARG 4   ? A ARG 4   
5  1 Y 1 A LEU 5   ? A LEU 5   
6  1 Y 1 A PRO 6   ? A PRO 6   
7  1 Y 1 A ALA 7   ? A ALA 7   
8  1 Y 1 A HIS 8   ? A HIS 8   
9  1 Y 1 A LEU 9   ? A LEU 9   
10 1 Y 1 A ARG 10  ? A ARG 10  
11 1 Y 1 A LEU 11  ? A LEU 11  
12 1 Y 1 A ARG 79  ? A ARG 79  
13 1 Y 1 A PRO 80  ? A PRO 80  
14 1 Y 1 A GLY 81  ? A GLY 81  
15 1 Y 1 A GLY 82  ? A GLY 82  
16 1 Y 1 A GLY 83  ? A GLY 83  
17 1 Y 1 A GLY 84  ? A GLY 84  
18 1 Y 1 A SER 85  ? A SER 85  
19 1 Y 1 A THR 86  ? A THR 86  
20 1 Y 1 A SER 87  ? A SER 87  
21 1 Y 1 A PRO 165 ? A PRO 165 
22 1 Y 1 A GLY 166 ? A GLY 166 
23 1 Y 1 A GLY 167 ? A GLY 167 
24 1 Y 1 A GLY 168 ? A GLY 168 
25 1 Y 1 A GLY 169 ? A GLY 169 
26 1 Y 1 A SER 170 ? A SER 170 
27 1 Y 1 A THR 171 ? A THR 171 
28 1 Y 1 A SER 172 ? A SER 172 
29 1 Y 1 A ILE 173 ? A ILE 173 
30 1 Y 1 A ARG 174 ? A ARG 174 
31 1 Y 1 A GLY 248 ? A GLY 248 
32 1 Y 1 A GLY 249 ? A GLY 249 
33 1 Y 1 A ASP 250 ? A ASP 250 
34 1 Y 1 A GLN 403 ? A GLN 403 
35 1 Y 1 A LYS 404 ? A LYS 404 
36 1 Y 1 A LEU 405 ? A LEU 405 
37 1 Y 1 A ASN 406 ? A ASN 406 
# 
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  
GLN N    N N N 74  
GLN CA   C N S 75  
GLN C    C N N 76  
GLN O    O N N 77  
GLN CB   C N N 78  
GLN CG   C N N 79  
GLN CD   C N N 80  
GLN OE1  O N N 81  
GLN NE2  N N N 82  
GLN OXT  O N N 83  
GLN H    H N N 84  
GLN H2   H N N 85  
GLN HA   H N N 86  
GLN HB2  H N N 87  
GLN HB3  H N N 88  
GLN HG2  H N N 89  
GLN HG3  H N N 90  
GLN HE21 H N N 91  
GLN HE22 H N N 92  
GLN HXT  H N N 93  
GLU N    N N N 94  
GLU CA   C N S 95  
GLU C    C N N 96  
GLU O    O N N 97  
GLU CB   C N N 98  
GLU CG   C N N 99  
GLU CD   C N N 100 
GLU OE1  O N N 101 
GLU OE2  O N N 102 
GLU OXT  O N N 103 
GLU H    H N N 104 
GLU H2   H N N 105 
GLU HA   H N N 106 
GLU HB2  H N N 107 
GLU HB3  H N N 108 
GLU HG2  H N N 109 
GLU HG3  H N N 110 
GLU HE2  H N N 111 
GLU HXT  H N N 112 
GLY N    N N N 113 
GLY CA   C N N 114 
GLY C    C N N 115 
GLY O    O N N 116 
GLY OXT  O N N 117 
GLY H    H N N 118 
GLY H2   H N N 119 
GLY HA2  H N N 120 
GLY HA3  H N N 121 
GLY HXT  H N N 122 
HIS N    N N N 123 
HIS CA   C N S 124 
HIS C    C N N 125 
HIS O    O N N 126 
HIS CB   C N N 127 
HIS CG   C Y N 128 
HIS ND1  N Y N 129 
HIS CD2  C Y N 130 
HIS CE1  C Y N 131 
HIS NE2  N Y N 132 
HIS OXT  O N N 133 
HIS H    H N N 134 
HIS H2   H N N 135 
HIS HA   H N N 136 
HIS HB2  H N N 137 
HIS HB3  H N N 138 
HIS HD1  H N N 139 
HIS HD2  H N N 140 
HIS HE1  H N N 141 
HIS HE2  H N N 142 
HIS HXT  H N N 143 
HOH O    O N N 144 
HOH H1   H N N 145 
HOH H2   H N N 146 
ILE N    N N N 147 
ILE CA   C N S 148 
ILE C    C N N 149 
ILE O    O N N 150 
ILE CB   C N S 151 
ILE CG1  C N N 152 
ILE CG2  C N N 153 
ILE CD1  C N N 154 
ILE OXT  O N N 155 
ILE H    H N N 156 
ILE H2   H N N 157 
ILE HA   H N N 158 
ILE HB   H N N 159 
ILE HG12 H N N 160 
ILE HG13 H N N 161 
ILE HG21 H N N 162 
ILE HG22 H N N 163 
ILE HG23 H N N 164 
ILE HD11 H N N 165 
ILE HD12 H N N 166 
ILE HD13 H N N 167 
ILE HXT  H N N 168 
LEU N    N N N 169 
LEU CA   C N S 170 
LEU C    C N N 171 
LEU O    O N N 172 
LEU CB   C N N 173 
LEU CG   C N N 174 
LEU CD1  C N N 175 
LEU CD2  C N N 176 
LEU OXT  O N N 177 
LEU H    H N N 178 
LEU H2   H N N 179 
LEU HA   H N N 180 
LEU HB2  H N N 181 
LEU HB3  H N N 182 
LEU HG   H N N 183 
LEU HD11 H N N 184 
LEU HD12 H N N 185 
LEU HD13 H N N 186 
LEU HD21 H N N 187 
LEU HD22 H N N 188 
LEU HD23 H N N 189 
LEU HXT  H N N 190 
LYS N    N N N 191 
LYS CA   C N S 192 
LYS C    C N N 193 
LYS O    O N N 194 
LYS CB   C N N 195 
LYS CG   C N N 196 
LYS CD   C N N 197 
LYS CE   C N N 198 
LYS NZ   N N N 199 
LYS OXT  O N N 200 
LYS H    H N N 201 
LYS H2   H N N 202 
LYS HA   H N N 203 
LYS HB2  H N N 204 
LYS HB3  H N N 205 
LYS HG2  H N N 206 
LYS HG3  H N N 207 
LYS HD2  H N N 208 
LYS HD3  H N N 209 
LYS HE2  H N N 210 
LYS HE3  H N N 211 
LYS HZ1  H N N 212 
LYS HZ2  H N N 213 
LYS HZ3  H N N 214 
LYS HXT  H N N 215 
MET N    N N N 216 
MET CA   C N S 217 
MET C    C N N 218 
MET O    O N N 219 
MET CB   C N N 220 
MET CG   C N N 221 
MET SD   S N N 222 
MET CE   C N N 223 
MET OXT  O N N 224 
MET H    H N N 225 
MET H2   H N N 226 
MET HA   H N N 227 
MET HB2  H N N 228 
MET HB3  H N N 229 
MET HG2  H N N 230 
MET HG3  H N N 231 
MET HE1  H N N 232 
MET HE2  H N N 233 
MET HE3  H N N 234 
MET HXT  H N N 235 
PHE N    N N N 236 
PHE CA   C N S 237 
PHE C    C N N 238 
PHE O    O N N 239 
PHE CB   C N N 240 
PHE CG   C Y N 241 
PHE CD1  C Y N 242 
PHE CD2  C Y N 243 
PHE CE1  C Y N 244 
PHE CE2  C Y N 245 
PHE CZ   C Y N 246 
PHE OXT  O N N 247 
PHE H    H N N 248 
PHE H2   H N N 249 
PHE HA   H N N 250 
PHE HB2  H N N 251 
PHE HB3  H N N 252 
PHE HD1  H N N 253 
PHE HD2  H N N 254 
PHE HE1  H N N 255 
PHE HE2  H N N 256 
PHE HZ   H N N 257 
PHE HXT  H N N 258 
PRO N    N N N 259 
PRO CA   C N S 260 
PRO C    C N N 261 
PRO O    O N N 262 
PRO CB   C N N 263 
PRO CG   C N N 264 
PRO CD   C N N 265 
PRO OXT  O N N 266 
PRO H    H N N 267 
PRO HA   H N N 268 
PRO HB2  H N N 269 
PRO HB3  H N N 270 
PRO HG2  H N N 271 
PRO HG3  H N N 272 
PRO HD2  H N N 273 
PRO HD3  H N N 274 
PRO HXT  H N N 275 
SER N    N N N 276 
SER CA   C N S 277 
SER C    C N N 278 
SER O    O N N 279 
SER CB   C N N 280 
SER OG   O N N 281 
SER OXT  O N N 282 
SER H    H N N 283 
SER H2   H N N 284 
SER HA   H N N 285 
SER HB2  H N N 286 
SER HB3  H N N 287 
SER HG   H N N 288 
SER HXT  H N N 289 
SO4 S    S N N 290 
SO4 O1   O N N 291 
SO4 O2   O N N 292 
SO4 O3   O N N 293 
SO4 O4   O N N 294 
THR N    N N N 295 
THR CA   C N S 296 
THR C    C N N 297 
THR O    O N N 298 
THR CB   C N R 299 
THR OG1  O N N 300 
THR CG2  C N N 301 
THR OXT  O N N 302 
THR H    H N N 303 
THR H2   H N N 304 
THR HA   H N N 305 
THR HB   H N N 306 
THR HG1  H N N 307 
THR HG21 H N N 308 
THR HG22 H N N 309 
THR HG23 H N N 310 
THR HXT  H N N 311 
TRP N    N N N 312 
TRP CA   C N S 313 
TRP C    C N N 314 
TRP O    O N N 315 
TRP CB   C N N 316 
TRP CG   C Y N 317 
TRP CD1  C Y N 318 
TRP CD2  C Y N 319 
TRP NE1  N Y N 320 
TRP CE2  C Y N 321 
TRP CE3  C Y N 322 
TRP CZ2  C Y N 323 
TRP CZ3  C Y N 324 
TRP CH2  C Y N 325 
TRP OXT  O N N 326 
TRP H    H N N 327 
TRP H2   H N N 328 
TRP HA   H N N 329 
TRP HB2  H N N 330 
TRP HB3  H N N 331 
TRP HD1  H N N 332 
TRP HE1  H N N 333 
TRP HE3  H N N 334 
TRP HZ2  H N N 335 
TRP HZ3  H N N 336 
TRP HH2  H N N 337 
TRP HXT  H N N 338 
TYR N    N N N 339 
TYR CA   C N S 340 
TYR C    C N N 341 
TYR O    O N N 342 
TYR CB   C N N 343 
TYR CG   C Y N 344 
TYR CD1  C Y N 345 
TYR CD2  C Y N 346 
TYR CE1  C Y N 347 
TYR CE2  C Y N 348 
TYR CZ   C Y N 349 
TYR OH   O N N 350 
TYR OXT  O N N 351 
TYR H    H N N 352 
TYR H2   H N N 353 
TYR HA   H N N 354 
TYR HB2  H N N 355 
TYR HB3  H N N 356 
TYR HD1  H N N 357 
TYR HD2  H N N 358 
TYR HE1  H N N 359 
TYR HE2  H N N 360 
TYR HH   H N N 361 
TYR HXT  H N N 362 
VAL N    N N N 363 
VAL CA   C N S 364 
VAL C    C N N 365 
VAL O    O N N 366 
VAL CB   C N N 367 
VAL CG1  C N N 368 
VAL CG2  C N N 369 
VAL OXT  O N N 370 
VAL H    H N N 371 
VAL H2   H N N 372 
VAL HA   H N N 373 
VAL HB   H N N 374 
VAL HG11 H N N 375 
VAL HG12 H N N 376 
VAL HG13 H N N 377 
VAL HG21 H N N 378 
VAL HG22 H N N 379 
VAL HG23 H N N 380 
VAL HXT  H N N 381 
# 
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  
GLN N   CA   sing N N 70  
GLN N   H    sing N N 71  
GLN N   H2   sing N N 72  
GLN CA  C    sing N N 73  
GLN CA  CB   sing N N 74  
GLN CA  HA   sing N N 75  
GLN C   O    doub N N 76  
GLN C   OXT  sing N N 77  
GLN CB  CG   sing N N 78  
GLN CB  HB2  sing N N 79  
GLN CB  HB3  sing N N 80  
GLN CG  CD   sing N N 81  
GLN CG  HG2  sing N N 82  
GLN CG  HG3  sing N N 83  
GLN CD  OE1  doub N N 84  
GLN CD  NE2  sing N N 85  
GLN NE2 HE21 sing N N 86  
GLN NE2 HE22 sing N N 87  
GLN OXT HXT  sing N N 88  
GLU N   CA   sing N N 89  
GLU N   H    sing N N 90  
GLU N   H2   sing N N 91  
GLU CA  C    sing N N 92  
GLU CA  CB   sing N N 93  
GLU CA  HA   sing N N 94  
GLU C   O    doub N N 95  
GLU C   OXT  sing N N 96  
GLU CB  CG   sing N N 97  
GLU CB  HB2  sing N N 98  
GLU CB  HB3  sing N N 99  
GLU CG  CD   sing N N 100 
GLU CG  HG2  sing N N 101 
GLU CG  HG3  sing N N 102 
GLU CD  OE1  doub N N 103 
GLU CD  OE2  sing N N 104 
GLU OE2 HE2  sing N N 105 
GLU OXT HXT  sing N N 106 
GLY N   CA   sing N N 107 
GLY N   H    sing N N 108 
GLY N   H2   sing N N 109 
GLY CA  C    sing N N 110 
GLY CA  HA2  sing N N 111 
GLY CA  HA3  sing N N 112 
GLY C   O    doub N N 113 
GLY C   OXT  sing N N 114 
GLY OXT HXT  sing N N 115 
HIS N   CA   sing N N 116 
HIS N   H    sing N N 117 
HIS N   H2   sing N N 118 
HIS CA  C    sing N N 119 
HIS CA  CB   sing N N 120 
HIS CA  HA   sing N N 121 
HIS C   O    doub N N 122 
HIS C   OXT  sing N N 123 
HIS CB  CG   sing N N 124 
HIS CB  HB2  sing N N 125 
HIS CB  HB3  sing N N 126 
HIS CG  ND1  sing Y N 127 
HIS CG  CD2  doub Y N 128 
HIS ND1 CE1  doub Y N 129 
HIS ND1 HD1  sing N N 130 
HIS CD2 NE2  sing Y N 131 
HIS CD2 HD2  sing N N 132 
HIS CE1 NE2  sing Y N 133 
HIS CE1 HE1  sing N N 134 
HIS NE2 HE2  sing N N 135 
HIS OXT HXT  sing N N 136 
HOH O   H1   sing N N 137 
HOH O   H2   sing N N 138 
ILE N   CA   sing N N 139 
ILE N   H    sing N N 140 
ILE N   H2   sing N N 141 
ILE CA  C    sing N N 142 
ILE CA  CB   sing N N 143 
ILE CA  HA   sing N N 144 
ILE C   O    doub N N 145 
ILE C   OXT  sing N N 146 
ILE CB  CG1  sing N N 147 
ILE CB  CG2  sing N N 148 
ILE CB  HB   sing N N 149 
ILE CG1 CD1  sing N N 150 
ILE CG1 HG12 sing N N 151 
ILE CG1 HG13 sing N N 152 
ILE CG2 HG21 sing N N 153 
ILE CG2 HG22 sing N N 154 
ILE CG2 HG23 sing N N 155 
ILE CD1 HD11 sing N N 156 
ILE CD1 HD12 sing N N 157 
ILE CD1 HD13 sing N N 158 
ILE OXT HXT  sing N N 159 
LEU N   CA   sing N N 160 
LEU N   H    sing N N 161 
LEU N   H2   sing N N 162 
LEU CA  C    sing N N 163 
LEU CA  CB   sing N N 164 
LEU CA  HA   sing N N 165 
LEU C   O    doub N N 166 
LEU C   OXT  sing N N 167 
LEU CB  CG   sing N N 168 
LEU CB  HB2  sing N N 169 
LEU CB  HB3  sing N N 170 
LEU CG  CD1  sing N N 171 
LEU CG  CD2  sing N N 172 
LEU CG  HG   sing N N 173 
LEU CD1 HD11 sing N N 174 
LEU CD1 HD12 sing N N 175 
LEU CD1 HD13 sing N N 176 
LEU CD2 HD21 sing N N 177 
LEU CD2 HD22 sing N N 178 
LEU CD2 HD23 sing N N 179 
LEU OXT HXT  sing N N 180 
LYS N   CA   sing N N 181 
LYS N   H    sing N N 182 
LYS N   H2   sing N N 183 
LYS CA  C    sing N N 184 
LYS CA  CB   sing N N 185 
LYS CA  HA   sing N N 186 
LYS C   O    doub N N 187 
LYS C   OXT  sing N N 188 
LYS CB  CG   sing N N 189 
LYS CB  HB2  sing N N 190 
LYS CB  HB3  sing N N 191 
LYS CG  CD   sing N N 192 
LYS CG  HG2  sing N N 193 
LYS CG  HG3  sing N N 194 
LYS CD  CE   sing N N 195 
LYS CD  HD2  sing N N 196 
LYS CD  HD3  sing N N 197 
LYS CE  NZ   sing N N 198 
LYS CE  HE2  sing N N 199 
LYS CE  HE3  sing N N 200 
LYS NZ  HZ1  sing N N 201 
LYS NZ  HZ2  sing N N 202 
LYS NZ  HZ3  sing N N 203 
LYS OXT HXT  sing N N 204 
MET N   CA   sing N N 205 
MET N   H    sing N N 206 
MET N   H2   sing N N 207 
MET CA  C    sing N N 208 
MET CA  CB   sing N N 209 
MET CA  HA   sing N N 210 
MET C   O    doub N N 211 
MET C   OXT  sing N N 212 
MET CB  CG   sing N N 213 
MET CB  HB2  sing N N 214 
MET CB  HB3  sing N N 215 
MET CG  SD   sing N N 216 
MET CG  HG2  sing N N 217 
MET CG  HG3  sing N N 218 
MET SD  CE   sing N N 219 
MET CE  HE1  sing N N 220 
MET CE  HE2  sing N N 221 
MET CE  HE3  sing N N 222 
MET OXT HXT  sing N N 223 
PHE N   CA   sing N N 224 
PHE N   H    sing N N 225 
PHE N   H2   sing N N 226 
PHE CA  C    sing N N 227 
PHE CA  CB   sing N N 228 
PHE CA  HA   sing N N 229 
PHE C   O    doub N N 230 
PHE C   OXT  sing N N 231 
PHE CB  CG   sing N N 232 
PHE CB  HB2  sing N N 233 
PHE CB  HB3  sing N N 234 
PHE CG  CD1  doub Y N 235 
PHE CG  CD2  sing Y N 236 
PHE CD1 CE1  sing Y N 237 
PHE CD1 HD1  sing N N 238 
PHE CD2 CE2  doub Y N 239 
PHE CD2 HD2  sing N N 240 
PHE CE1 CZ   doub Y N 241 
PHE CE1 HE1  sing N N 242 
PHE CE2 CZ   sing Y N 243 
PHE CE2 HE2  sing N N 244 
PHE CZ  HZ   sing N N 245 
PHE OXT HXT  sing N N 246 
PRO N   CA   sing N N 247 
PRO N   CD   sing N N 248 
PRO N   H    sing N N 249 
PRO CA  C    sing N N 250 
PRO CA  CB   sing N N 251 
PRO CA  HA   sing N N 252 
PRO C   O    doub N N 253 
PRO C   OXT  sing N N 254 
PRO CB  CG   sing N N 255 
PRO CB  HB2  sing N N 256 
PRO CB  HB3  sing N N 257 
PRO CG  CD   sing N N 258 
PRO CG  HG2  sing N N 259 
PRO CG  HG3  sing N N 260 
PRO CD  HD2  sing N N 261 
PRO CD  HD3  sing N N 262 
PRO OXT HXT  sing N N 263 
SER N   CA   sing N N 264 
SER N   H    sing N N 265 
SER N   H2   sing N N 266 
SER CA  C    sing N N 267 
SER CA  CB   sing N N 268 
SER CA  HA   sing N N 269 
SER C   O    doub N N 270 
SER C   OXT  sing N N 271 
SER CB  OG   sing N N 272 
SER CB  HB2  sing N N 273 
SER CB  HB3  sing N N 274 
SER OG  HG   sing N N 275 
SER OXT HXT  sing N N 276 
SO4 S   O1   doub N N 277 
SO4 S   O2   doub N N 278 
SO4 S   O3   sing N N 279 
SO4 S   O4   sing N N 280 
THR N   CA   sing N N 281 
THR N   H    sing N N 282 
THR N   H2   sing N N 283 
THR CA  C    sing N N 284 
THR CA  CB   sing N N 285 
THR CA  HA   sing N N 286 
THR C   O    doub N N 287 
THR C   OXT  sing N N 288 
THR CB  OG1  sing N N 289 
THR CB  CG2  sing N N 290 
THR CB  HB   sing N N 291 
THR OG1 HG1  sing N N 292 
THR CG2 HG21 sing N N 293 
THR CG2 HG22 sing N N 294 
THR CG2 HG23 sing N N 295 
THR OXT HXT  sing N N 296 
TRP N   CA   sing N N 297 
TRP N   H    sing N N 298 
TRP N   H2   sing N N 299 
TRP CA  C    sing N N 300 
TRP CA  CB   sing N N 301 
TRP CA  HA   sing N N 302 
TRP C   O    doub N N 303 
TRP C   OXT  sing N N 304 
TRP CB  CG   sing N N 305 
TRP CB  HB2  sing N N 306 
TRP CB  HB3  sing N N 307 
TRP CG  CD1  doub Y N 308 
TRP CG  CD2  sing Y N 309 
TRP CD1 NE1  sing Y N 310 
TRP CD1 HD1  sing N N 311 
TRP CD2 CE2  doub Y N 312 
TRP CD2 CE3  sing Y N 313 
TRP NE1 CE2  sing Y N 314 
TRP NE1 HE1  sing N N 315 
TRP CE2 CZ2  sing Y N 316 
TRP CE3 CZ3  doub Y N 317 
TRP CE3 HE3  sing N N 318 
TRP CZ2 CH2  doub Y N 319 
TRP CZ2 HZ2  sing N N 320 
TRP CZ3 CH2  sing Y N 321 
TRP CZ3 HZ3  sing N N 322 
TRP CH2 HH2  sing N N 323 
TRP OXT HXT  sing N N 324 
TYR N   CA   sing N N 325 
TYR N   H    sing N N 326 
TYR N   H2   sing N N 327 
TYR CA  C    sing N N 328 
TYR CA  CB   sing N N 329 
TYR CA  HA   sing N N 330 
TYR C   O    doub N N 331 
TYR C   OXT  sing N N 332 
TYR CB  CG   sing N N 333 
TYR CB  HB2  sing N N 334 
TYR CB  HB3  sing N N 335 
TYR CG  CD1  doub Y N 336 
TYR CG  CD2  sing Y N 337 
TYR CD1 CE1  sing Y N 338 
TYR CD1 HD1  sing N N 339 
TYR CD2 CE2  doub Y N 340 
TYR CD2 HD2  sing N N 341 
TYR CE1 CZ   doub Y N 342 
TYR CE1 HE1  sing N N 343 
TYR CE2 CZ   sing Y N 344 
TYR CE2 HE2  sing N N 345 
TYR CZ  OH   sing N N 346 
TYR OH  HH   sing N N 347 
TYR OXT HXT  sing N N 348 
VAL N   CA   sing N N 349 
VAL N   H    sing N N 350 
VAL N   H2   sing N N 351 
VAL CA  C    sing N N 352 
VAL CA  CB   sing N N 353 
VAL CA  HA   sing N N 354 
VAL C   O    doub N N 355 
VAL C   OXT  sing N N 356 
VAL CB  CG1  sing N N 357 
VAL CB  CG2  sing N N 358 
VAL CB  HB   sing N N 359 
VAL CG1 HG11 sing N N 360 
VAL CG1 HG12 sing N N 361 
VAL CG1 HG13 sing N N 362 
VAL CG2 HG21 sing N N 363 
VAL CG2 HG22 sing N N 364 
VAL CG2 HG23 sing N N 365 
VAL OXT HXT  sing N N 366 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           1R15GM146209 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   7N2B 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 21 21 21' 
_space_group.name_Hall        'P 2ac 2ab' 
_space_group.IT_number        19 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9E4Q 
_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]   0.021673 
_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]   0.011696 
_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]   0.008287 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C   ? ? 5.96793  ? ? ? 14.89577 ? ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N   ? ? 6.96715  ? ? ? 11.43723 ? ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O   ? ? 7.96527  ? ? ? 9.05267  ? ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O1- ? ? 8.95260  ? ? ? 12.67477 ? ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S   ? ? 15.91112 ? ? ? 10.84690 ? ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . GLN A 1 12  ? 8.06600  52.44200  -1.37400  1.000 82.12111  ?  12  GLN A N   1 
ATOM   2    C CA  . GLN A 1 12  ? 7.91900  51.01600  -1.64000  1.000 75.97847  ?  12  GLN A CA  1 
ATOM   3    C C   . GLN A 1 12  ? 9.28000  50.35000  -1.83100  1.000 72.97317  ?  12  GLN A C   1 
ATOM   4    O O   . GLN A 1 12  ? 10.21800 50.97300  -2.33300  1.000 75.04610  ?  12  GLN A O   1 
ATOM   5    C CB  . GLN A 1 12  ? 7.04000  50.78900  -2.87100  1.000 75.76447  ?  12  GLN A CB  1 
ATOM   6    N N   . PRO A 1 13  ? 9.38400  49.08100  -1.42800  1.000 68.83523  ?  13  PRO A N   1 
ATOM   7    C CA  . PRO A 1 13  ? 10.68400 48.39700  -1.49300  1.000 66.33740  ?  13  PRO A CA  1 
ATOM   8    C C   . PRO A 1 13  ? 11.29000 48.37600  -2.87900  1.000 71.24703  ?  13  PRO A C   1 
ATOM   9    O O   . PRO A 1 13  ? 12.51700 48.28700  -3.00300  1.000 70.75171  ?  13  PRO A O   1 
ATOM   10   C CB  . PRO A 1 13  ? 10.35500 46.98300  -1.00200  1.000 65.72758  ?  13  PRO A CB  1 
ATOM   11   C CG  . PRO A 1 13  ? 9.17300  47.16300  -0.12100  1.000 65.75029  ?  13  PRO A CG  1 
ATOM   12   C CD  . PRO A 1 13  ? 8.36500  48.26600  -0.74700  1.000 71.32970  ?  13  PRO A CD  1 
ATOM   13   N N   . ILE A 1 14  ? 10.46700 48.45700  -3.92700  1.000 72.55469  ?  14  ILE A N   1 
ATOM   14   C CA  . ILE A 1 14  ? 10.99900 48.46800  -5.28500  1.000 70.12307  ?  14  ILE A CA  1 
ATOM   15   C C   . ILE A 1 14  ? 11.99200 49.60600  -5.46300  1.000 70.27088  ?  14  ILE A C   1 
ATOM   16   O O   . ILE A 1 14  ? 12.99100 49.46800  -6.18000  1.000 69.44559  ?  14  ILE A O   1 
ATOM   17   C CB  . ILE A 1 14  ? 9.84600  48.55400  -6.30400  1.000 70.41732  ?  14  ILE A CB  1 
ATOM   18   C CG1 . ILE A 1 14  ? 10.40000 48.65900  -7.72700  1.000 71.10684  ?  14  ILE A CG1 1 
ATOM   19   C CG2 . ILE A 1 14  ? 8.90900  49.71100  -5.96200  1.000 73.31917  ?  14  ILE A CG2 1 
ATOM   20   N N   . TYR A 1 15  ? 11.75800 50.72600  -4.79400  1.000 72.90206  ?  15  TYR A N   1 
ATOM   21   C CA  . TYR A 1 15  ? 12.62300 51.88800  -4.90200  1.000 75.09576  ?  15  TYR A CA  1 
ATOM   22   C C   . TYR A 1 15  ? 13.81400 51.84300  -3.95200  1.000 74.37013  ?  15  TYR A C   1 
ATOM   23   O O   . TYR A 1 15  ? 14.64800 52.75300  -3.98800  1.000 78.30197  ?  15  TYR A O   1 
ATOM   24   C CB  . TYR A 1 15  ? 11.80700 53.15800  -4.65600  1.000 79.19326  ?  15  TYR A CB  1 
ATOM   25   C CG  . TYR A 1 15  ? 10.46300 53.17600  -5.35700  1.000 81.14354  ?  15  TYR A CG  1 
ATOM   26   C CD1 . TYR A 1 15  ? 10.38200 53.24900  -6.74300  1.000 86.91266  ?  15  TYR A CD1 1 
ATOM   27   C CD2 . TYR A 1 15  ? 9.27700  53.12500  -4.63500  1.000 82.17551  ?  15  TYR A CD2 1 
ATOM   28   C CE1 . TYR A 1 15  ? 9.15900  53.27500  -7.39000  1.000 90.84109  ?  15  TYR A CE1 1 
ATOM   29   C CE2 . TYR A 1 15  ? 8.04800  53.15000  -5.27400  1.000 87.72007  ?  15  TYR A CE2 1 
ATOM   30   C CZ  . TYR A 1 15  ? 7.99500  53.22400  -6.65100  1.000 93.89264  ?  15  TYR A CZ  1 
ATOM   31   O OH  . TYR A 1 15  ? 6.77500  53.24900  -7.29100  1.000 99.05826  ?  15  TYR A OH  1 
ATOM   32   N N   . TRP A 1 16  ? 13.92400 50.81700  -3.11400  1.000 69.80635  ?  16  TRP A N   1 
ATOM   33   C CA  . TRP A 1 16  ? 15.02500 50.76300  -2.16400  1.000 68.67430  ?  16  TRP A CA  1 
ATOM   34   C C   . TRP A 1 16  ? 16.35000 50.51200  -2.87500  1.000 68.79791  ?  16  TRP A C   1 
ATOM   35   O O   . TRP A 1 16  ? 16.40500 49.90900  -3.95000  1.000 69.80584  ?  16  TRP A O   1 
ATOM   36   C CB  . TRP A 1 16  ? 14.78300 49.67500  -1.12200  1.000 71.08984  ?  16  TRP A CB  1 
ATOM   37   C CG  . TRP A 1 16  ? 13.59400 49.92000  -0.24600  1.000 71.49540  ?  16  TRP A CG  1 
ATOM   38   C CD1 . TRP A 1 16  ? 12.76100 51.00100  -0.26800  1.000 72.88358  ?  16  TRP A CD1 1 
ATOM   39   C CD2 . TRP A 1 16  ? 13.10200 49.05600  0.78300   1.000 70.27069  ?  16  TRP A CD2 1 
ATOM   40   N NE1 . TRP A 1 16  ? 11.78000 50.86300  0.68400   1.000 74.25511  ?  16  TRP A NE1 1 
ATOM   41   C CE2 . TRP A 1 16  ? 11.96800 49.67700  1.34300   1.000 72.90806  ?  16  TRP A CE2 1 
ATOM   42   C CE3 . TRP A 1 16  ? 13.50800 47.81500  1.28200   1.000 66.43501  ?  16  TRP A CE3 1 
ATOM   43   C CZ2 . TRP A 1 16  ? 11.23700 49.09800  2.37700   1.000 75.14385  ?  16  TRP A CZ2 1 
ATOM   44   C CZ3 . TRP A 1 16  ? 12.78400 47.24300  2.30900   1.000 61.39703  ?  16  TRP A CZ3 1 
ATOM   45   C CH2 . TRP A 1 16  ? 11.66100 47.88200  2.84500   1.000 67.40977  ?  16  TRP A CH2 1 
ATOM   46   N N   . SER A 1 17  ? 17.42300 50.99400  -2.26100  1.000 67.33435  ?  17  SER A N   1 
ATOM   47   C CA  . SER A 1 17  ? 18.78100 50.77500  -2.73000  1.000 66.94942  ?  17  SER A CA  1 
ATOM   48   C C   . SER A 1 17  ? 19.49500 49.82800  -1.77400  1.000 71.41476  ?  17  SER A C   1 
ATOM   49   O O   . SER A 1 17  ? 18.94600 49.41200  -0.74900  1.000 72.18520  ?  17  SER A O   1 
ATOM   50   C CB  . SER A 1 17  ? 19.53000 52.10100  -2.85800  1.000 70.58404  ?  17  SER A CB  1 
ATOM   51   N N   . ARG A 1 18  ? 20.73500 49.48000  -2.12900  1.000 66.71242  ?  18  ARG A N   1 
ATOM   52   C CA  . ARG A 1 18  ? 21.53400 48.62400  -1.25900  1.000 64.39401  ?  18  ARG A CA  1 
ATOM   53   C C   . ARG A 1 18  ? 21.63900 49.22300  0.13300   1.000 69.03951  ?  18  ARG A C   1 
ATOM   54   O O   . ARG A 1 18  ? 21.60200 48.50000  1.13500   1.000 71.93801  ?  18  ARG A O   1 
ATOM   55   C CB  . ARG A 1 18  ? 22.92300 48.40600  -1.85700  1.000 64.37132  ?  18  ARG A CB  1 
ATOM   56   N N   . ASP A 1 19  ? 21.75100 50.55000  0.21400   1.000 70.70255  ?  19  ASP A N   1 
ATOM   57   C CA  . ASP A 1 19  ? 21.70800 51.21700  1.50900   1.000 74.17720  ?  19  ASP A CA  1 
ATOM   58   C C   . ASP A 1 19  ? 20.33000 51.07300  2.14700   1.000 70.56175  ?  19  ASP A C   1 
ATOM   59   O O   . ASP A 1 19  ? 20.22000 50.80200  3.34800   1.000 68.87665  ?  19  ASP A O   1 
ATOM   60   C CB  . ASP A 1 19  ? 22.08500 52.69200  1.34200   1.000 79.96686  ?  19  ASP A CB  1 
ATOM   61   C CG  . ASP A 1 19  ? 22.26300 53.41500  2.67100   1.000 89.76432  ?  19  ASP A CG  1 
ATOM   62   O OD1 . ASP A 1 19  ? 22.22200 52.75800  3.73400   1.000 87.04465  ?  19  ASP A OD1 1 
ATOM   63   O OD2 . ASP A 1 19  ? 22.44300 54.65200  2.65000   1.000 95.21838  -1 19  ASP A OD2 1 
ATOM   64   N N   . ASP A 1 20  ? 19.26600 51.23000  1.35800   1.000 71.62221  ?  20  ASP A N   1 
ATOM   65   C CA  . ASP A 1 20  ? 17.92300 51.12500  1.91400   1.000 69.35405  ?  20  ASP A CA  1 
ATOM   66   C C   . ASP A 1 20  ? 17.62400 49.70300  2.35800   1.000 69.54943  ?  20  ASP A C   1 
ATOM   67   O O   . ASP A 1 20  ? 16.96900 49.49100  3.38600   1.000 70.77980  ?  20  ASP A O   1 
ATOM   68   C CB  . ASP A 1 20  ? 16.89400 51.58000  0.88900   1.000 71.51735  ?  20  ASP A CB  1 
ATOM   69   C CG  . ASP A 1 20  ? 17.22300 52.92700  0.29900   1.000 81.20599  ?  20  ASP A CG  1 
ATOM   70   O OD1 . ASP A 1 20  ? 18.15700 53.58700  0.80300   1.000 85.66801  ?  20  ASP A OD1 1 
ATOM   71   O OD2 . ASP A 1 20  ? 16.56400 53.31500  -0.68600  1.000 85.78148  -1 20  ASP A OD2 1 
ATOM   72   N N   . VAL A 1 21  ? 18.08200 48.71700  1.58800   1.000 70.01269  ?  21  VAL A N   1 
ATOM   73   C CA  . VAL A 1 21  ? 17.89400 47.32600  1.98300   1.000 66.28803  ?  21  VAL A CA  1 
ATOM   74   C C   . VAL A 1 21  ? 18.59500 47.05500  3.30700   1.000 63.45080  ?  21  VAL A C   1 
ATOM   75   O O   . VAL A 1 21  ? 18.02600 46.43000  4.20900   1.000 61.98673  ?  21  VAL A O   1 
ATOM   76   C CB  . VAL A 1 21  ? 18.38300 46.38400  0.86700   1.000 62.50704  ?  21  VAL A CB  1 
ATOM   77   C CG1 . VAL A 1 21  ? 18.37800 44.95000  1.34100   1.000 60.39064  ?  21  VAL A CG1 1 
ATOM   78   C CG2 . VAL A 1 21  ? 17.49400 46.52600  -0.35600  1.000 64.54176  ?  21  VAL A CG2 1 
ATOM   79   N N   . ALA A 1 22  ? 19.82400 47.55800  3.46000   1.000 68.62688  ?  22  ALA A N   1 
ATOM   80   C CA  . ALA A 1 22  ? 20.60400 47.27500  4.66100   1.000 64.64899  ?  22  ALA A CA  1 
ATOM   81   C C   . ALA A 1 22  ? 19.98500 47.91000  5.90300   1.000 64.37824  ?  22  ALA A C   1 
ATOM   82   O O   . ALA A 1 22  ? 20.02000 47.31900  6.98900   1.000 64.09397  ?  22  ALA A O   1 
ATOM   83   C CB  . ALA A 1 22  ? 22.04300 47.75100  4.47500   1.000 60.98202  ?  22  ALA A CB  1 
ATOM   84   N N   . GLN A 1 23  ? 19.42300 49.11400  5.77000   1.000 62.25823  ?  23  GLN A N   1 
ATOM   85   C CA  . GLN A 1 23  ? 18.76700 49.74000  6.91500   1.000 64.39252  ?  23  GLN A CA  1 
ATOM   86   C C   . GLN A 1 23  ? 17.55200 48.93400  7.35400   1.000 64.23861  ?  23  GLN A C   1 
ATOM   87   O O   . GLN A 1 23  ? 17.29800 48.78100  8.55600   1.000 64.01919  ?  23  GLN A O   1 
ATOM   88   C CB  . GLN A 1 23  ? 18.36800 51.17700  6.58100   1.000 64.99605  ?  23  GLN A CB  1 
ATOM   89   N N   . TRP A 1 24  ? 16.79300 48.40400  6.39300   1.000 64.17536  ?  24  TRP A N   1 
ATOM   90   C CA  . TRP A 1 24  ? 15.65700 47.55600  6.73300   1.000 61.22320  ?  24  TRP A CA  1 
ATOM   91   C C   . TRP A 1 24  ? 16.09700 46.30900  7.48600   1.000 62.03354  ?  24  TRP A C   1 
ATOM   92   O O   . TRP A 1 24  ? 15.32500 45.76100  8.28200   1.000 61.51076  ?  24  TRP A O   1 
ATOM   93   C CB  . TRP A 1 24  ? 14.89600 47.18200  5.46200   1.000 61.74495  ?  24  TRP A CB  1 
ATOM   94   C CG  . TRP A 1 24  ? 13.84700 46.13300  5.65600   1.000 60.68566  ?  24  TRP A CG  1 
ATOM   95   C CD1 . TRP A 1 24  ? 12.70300 46.24300  6.38900   1.000 61.04462  ?  24  TRP A CD1 1 
ATOM   96   C CD2 . TRP A 1 24  ? 13.82600 44.82300  5.07400   1.000 57.11101  ?  24  TRP A CD2 1 
ATOM   97   N NE1 . TRP A 1 24  ? 11.97900 45.07700  6.31600   1.000 59.73174  ?  24  TRP A NE1 1 
ATOM   98   C CE2 . TRP A 1 24  ? 12.64700 44.19000  5.51300   1.000 55.44917  ?  24  TRP A CE2 1 
ATOM   99   C CE3 . TRP A 1 24  ? 14.69500 44.12200  4.23300   1.000 54.83618  ?  24  TRP A CE3 1 
ATOM   100  C CZ2 . TRP A 1 24  ? 12.31300 42.89300  5.13900   1.000 53.41015  ?  24  TRP A CZ2 1 
ATOM   101  C CZ3 . TRP A 1 24  ? 14.36200 42.83500  3.86300   1.000 50.80655  ?  24  TRP A CZ3 1 
ATOM   102  C CH2 . TRP A 1 24  ? 13.18200 42.23400  4.31500   1.000 54.10867  ?  24  TRP A CH2 1 
ATOM   103  N N   . LEU A 1 25  ? 17.33000 45.85100  7.25900   1.000 63.66887  ?  25  LEU A N   1 
ATOM   104  C CA  . LEU A 1 25  ? 17.81800 44.67000  7.96300   1.000 62.56467  ?  25  LEU A CA  1 
ATOM   105  C C   . LEU A 1 25  ? 18.10900 44.98900  9.42300   1.000 64.26878  ?  25  LEU A C   1 
ATOM   106  O O   . LEU A 1 25  ? 17.65100 44.27900  10.32800  1.000 67.50445  ?  25  LEU A O   1 
ATOM   107  C CB  . LEU A 1 25  ? 19.06800 44.11900  7.27500   1.000 63.19536  ?  25  LEU A CB  1 
ATOM   108  C CG  . LEU A 1 25  ? 19.00100 43.84100  5.77200   1.000 61.56907  ?  25  LEU A CG  1 
ATOM   109  C CD1 . LEU A 1 25  ? 20.35500 43.36900  5.25300   1.000 63.05798  ?  25  LEU A CD1 1 
ATOM   110  C CD2 . LEU A 1 25  ? 17.90000 42.84900  5.43000   1.000 59.82101  ?  25  LEU A CD2 1 
ATOM   111  N N   . LYS A 1 26  ? 18.87300 46.05600  9.67500   1.000 62.14632  ?  26  LYS A N   1 
ATOM   112  C CA  . LYS A 1 26  ? 19.18500 46.42300  11.05200  1.000 63.07691  ?  26  LYS A CA  1 
ATOM   113  C C   . LYS A 1 26  ? 17.93900 46.84700  11.81400  1.000 63.42334  ?  26  LYS A C   1 
ATOM   114  O O   . LYS A 1 26  ? 17.87500 46.67200  13.03600  1.000 66.43539  ?  26  LYS A O   1 
ATOM   115  C CB  . LYS A 1 26  ? 20.22700 47.54000  11.07800  1.000 60.79421  ?  26  LYS A CB  1 
ATOM   116  N N   . TRP A 1 27  ? 16.94500 47.40100  11.11700  1.000 58.92743  ?  27  TRP A N   1 
ATOM   117  C CA  . TRP A 1 27  ? 15.69800 47.76700  11.77800  1.000 61.65729  ?  27  TRP A CA  1 
ATOM   118  C C   . TRP A 1 27  ? 14.97200 46.52600  12.28200  1.000 61.54319  ?  27  TRP A C   1 
ATOM   119  O O   . TRP A 1 27  ? 14.57000 46.45600  13.45000  1.000 65.36430  ?  27  TRP A O   1 
ATOM   120  C CB  . TRP A 1 27  ? 14.81000 48.56800  10.82200  1.000 60.38225  ?  27  TRP A CB  1 
ATOM   121  C CG  . TRP A 1 27  ? 13.37500 48.63500  11.25800  1.000 64.36048  ?  27  TRP A CG  1 
ATOM   122  C CD1 . TRP A 1 27  ? 12.82400 49.52400  12.13800  1.000 67.55475  ?  27  TRP A CD1 1 
ATOM   123  C CD2 . TRP A 1 27  ? 12.31200 47.76500  10.85100  1.000 66.61684  ?  27  TRP A CD2 1 
ATOM   124  N NE1 . TRP A 1 27  ? 11.48300 49.26700  12.29400  1.000 70.87058  ?  27  TRP A NE1 1 
ATOM   125  C CE2 . TRP A 1 27  ? 11.14400 48.19100  11.51600  1.000 70.38077  ?  27  TRP A CE2 1 
ATOM   126  C CE3 . TRP A 1 27  ? 12.23300 46.67000  9.98600   1.000 65.24140  ?  27  TRP A CE3 1 
ATOM   127  C CZ2 . TRP A 1 27  ? 9.91400  47.55900  11.34200  1.000 68.85150  ?  27  TRP A CZ2 1 
ATOM   128  C CZ3 . TRP A 1 27  ? 11.01200 46.04500  9.81600   1.000 64.80525  ?  27  TRP A CZ3 1 
ATOM   129  C CH2 . TRP A 1 27  ? 9.86900  46.49100  10.49000  1.000 65.54312  ?  27  TRP A CH2 1 
ATOM   130  N N   . ALA A 1 28  ? 14.80000 45.52900  11.41300  1.000 63.23923  ?  28  ALA A N   1 
ATOM   131  C CA  . ALA A 1 28  ? 14.14500 44.29600  11.83300  1.000 58.85015  ?  28  ALA A CA  1 
ATOM   132  C C   . ALA A 1 28  ? 14.96800 43.57500  12.88900  1.000 63.08663  ?  28  ALA A C   1 
ATOM   133  O O   . ALA A 1 28  ? 14.41200 42.97400  13.81600  1.000 66.99326  ?  28  ALA A O   1 
ATOM   134  C CB  . ALA A 1 28  ? 13.90100 43.39200  10.62600  1.000 55.13246  ?  28  ALA A CB  1 
ATOM   135  N N   . GLU A 1 29  ? 16.29600 43.63300  12.76900  1.000 56.70884  ?  29  GLU A N   1 
ATOM   136  C CA  . GLU A 1 29  ? 17.16100 42.98900  13.75100  1.000 61.02856  ?  29  GLU A CA  1 
ATOM   137  C C   . GLU A 1 29  ? 16.90100 43.51200  15.15800  1.000 63.82558  ?  29  GLU A C   1 
ATOM   138  O O   . GLU A 1 29  ? 17.01000 42.75700  16.13200  1.000 65.43495  ?  29  GLU A O   1 
ATOM   139  C CB  . GLU A 1 29  ? 18.62200 43.18900  13.35300  1.000 61.90934  ?  29  GLU A CB  1 
ATOM   140  C CG  . GLU A 1 29  ? 19.62000 42.77900  14.40800  1.000 69.24229  ?  29  GLU A CG  1 
ATOM   141  C CD  . GLU A 1 29  ? 21.03500 43.12900  14.01400  1.000 75.70389  ?  29  GLU A CD  1 
ATOM   142  O OE1 . GLU A 1 29  ? 21.30800 43.20300  12.79600  1.000 72.00411  ?  29  GLU A OE1 1 
ATOM   143  O OE2 . GLU A 1 29  ? 21.86900 43.34900  14.91900  1.000 80.13515  -1 29  GLU A OE2 1 
ATOM   144  N N   . ASN A 1 30  ? 16.53700 44.78600  15.28500  1.000 66.11346  ?  30  ASN A N   1 
ATOM   145  C CA  . ASN A 1 30  ? 16.17400 45.34700  16.58000  1.000 70.22963  ?  30  ASN A CA  1 
ATOM   146  C C   . ASN A 1 30  ? 14.68400 45.20600  16.86000  1.000 70.43372  ?  30  ASN A C   1 
ATOM   147  O O   . ASN A 1 30  ? 14.29300 44.89000  17.98900  1.000 75.45885  ?  30  ASN A O   1 
ATOM   148  C CB  . ASN A 1 30  ? 16.57500 46.82500  16.64900  1.000 72.64553  ?  30  ASN A CB  1 
ATOM   149  C CG  . ASN A 1 30  ? 18.03500 47.05200  16.30800  1.000 74.63706  ?  30  ASN A CG  1 
ATOM   150  O OD1 . ASN A 1 30  ? 18.74700 46.12500  15.91600  1.000 76.75751  ?  30  ASN A OD1 1 
ATOM   151  N ND2 . ASN A 1 30  ? 18.49000 48.29200  16.45700  1.000 73.10629  ?  30  ASN A ND2 1 
ATOM   152  N N   . GLU A 1 31  ? 13.84600 45.42700  15.84500  1.000 72.82500  ?  31  GLU A N   1 
ATOM   153  C CA  . GLU A 1 31  ? 12.40300 45.42900  16.06300  1.000 76.56299  ?  31  GLU A CA  1 
ATOM   154  C C   . GLU A 1 31  ? 11.90000 44.04700  16.46100  1.000 73.42832  ?  31  GLU A C   1 
ATOM   155  O O   . GLU A 1 31  ? 11.07800 43.91800  17.37400  1.000 75.40861  ?  31  GLU A O   1 
ATOM   156  C CB  . GLU A 1 31  ? 11.68900 45.92400  14.80500  1.000 78.03493  ?  31  GLU A CB  1 
ATOM   157  C CG  . GLU A 1 31  ? 10.17700 45.72800  14.81000  1.000 84.68907  ?  31  GLU A CG  1 
ATOM   158  C CD  . GLU A 1 31  ? 9.45300  46.69400  15.73700  1.000 92.98127  ?  31  GLU A CD  1 
ATOM   159  O OE1 . GLU A 1 31  ? 10.08500 47.66000  16.21600  1.000 93.88854  ?  31  GLU A OE1 1 
ATOM   160  O OE2 . GLU A 1 31  ? 8.24600  46.48400  15.98600  1.000 96.79435  -1 31  GLU A OE2 1 
ATOM   161  N N   . PHE A 1 32  ? 12.38400 43.00300  15.79200  1.000 63.20838  ?  32  PHE A N   1 
ATOM   162  C CA  . PHE A 1 32  ? 11.98900 41.63200  16.07600  1.000 61.96642  ?  32  PHE A CA  1 
ATOM   163  C C   . PHE A 1 32  ? 13.04300 40.87300  16.86200  1.000 65.55409  ?  32  PHE A C   1 
ATOM   164  O O   . PHE A 1 32  ? 12.86900 39.67700  17.12100  1.000 63.91719  ?  32  PHE A O   1 
ATOM   165  C CB  . PHE A 1 32  ? 11.67800 40.89100  14.78100  1.000 56.10886  ?  32  PHE A CB  1 
ATOM   166  C CG  . PHE A 1 32  ? 10.75600 41.63300  13.87100  1.000 57.26380  ?  32  PHE A CG  1 
ATOM   167  C CD1 . PHE A 1 32  ? 9.39800  41.67600  14.13000  1.000 55.87292  ?  32  PHE A CD1 1 
ATOM   168  C CD2 . PHE A 1 32  ? 11.24300 42.28700  12.75400  1.000 60.08849  ?  32  PHE A CD2 1 
ATOM   169  C CE1 . PHE A 1 32  ? 8.54200  42.36000  13.29400  1.000 56.73184  ?  32  PHE A CE1 1 
ATOM   170  C CE2 . PHE A 1 32  ? 10.39100 42.97400  11.91300  1.000 61.98434  ?  32  PHE A CE2 1 
ATOM   171  C CZ  . PHE A 1 32  ? 9.03900  43.01000  12.18300  1.000 61.11604  ?  32  PHE A CZ  1 
ATOM   172  N N   . SER A 1 33  ? 14.13100 41.54200  17.24100  1.000 65.83711  ?  33  SER A N   1 
ATOM   173  C CA  . SER A 1 33  ? 15.20200 40.92400  18.01500  1.000 65.82598  ?  33  SER A CA  1 
ATOM   174  C C   . SER A 1 33  ? 15.74700 39.70200  17.28900  1.000 62.37399  ?  33  SER A C   1 
ATOM   175  O O   . SER A 1 33  ? 15.94900 38.63700  17.87400  1.000 64.31957  ?  33  SER A O   1 
ATOM   176  C CB  . SER A 1 33  ? 14.72900 40.56300  19.41900  1.000 69.09754  ?  33  SER A CB  1 
ATOM   177  N N   . LEU A 1 34  ? 15.95200 39.85500  15.98600  1.000 61.11827  ?  34  LEU A N   1 
ATOM   178  C CA  . LEU A 1 34  ? 16.55400 38.79300  15.20700  1.000 63.23262  ?  34  LEU A CA  1 
ATOM   179  C C   . LEU A 1 34  ? 18.04000 38.69900  15.52200  1.000 67.24841  ?  34  LEU A C   1 
ATOM   180  O O   . LEU A 1 34  ? 18.65900 39.64100  16.02800  1.000 68.05729  ?  34  LEU A O   1 
ATOM   181  C CB  . LEU A 1 34  ? 16.34100 39.03200  13.71500  1.000 56.18485  ?  34  LEU A CB  1 
ATOM   182  C CG  . LEU A 1 34  ? 14.90900 39.40800  13.34100  1.000 53.05946  ?  34  LEU A CG  1 
ATOM   183  C CD1 . LEU A 1 34  ? 14.79400 39.65800  11.84500  1.000 53.34225  ?  34  LEU A CD1 1 
ATOM   184  C CD2 . LEU A 1 34  ? 13.93600 38.33200  13.79500  1.000 56.26722  ?  34  LEU A CD2 1 
ATOM   185  N N   . ARG A 1 35  ? 18.60400 37.53400  15.23900  1.000 65.56495  ?  35  ARG A N   1 
ATOM   186  C CA  . ARG A 1 35  ? 20.03600 37.35700  15.39800  1.000 69.98348  ?  35  ARG A CA  1 
ATOM   187  C C   . ARG A 1 35  ? 20.75600 38.28100  14.42100  1.000 72.23974  ?  35  ARG A C   1 
ATOM   188  O O   . ARG A 1 35  ? 20.37500 38.35000  13.24400  1.000 73.91587  ?  35  ARG A O   1 
ATOM   189  C CB  . ARG A 1 35  ? 20.43100 35.90100  15.16000  1.000 72.55305  ?  35  ARG A CB  1 
ATOM   190  C CG  . ARG A 1 35  ? 21.92900 35.62900  15.22500  1.000 73.51454  ?  35  ARG A CG  1 
ATOM   191  C CD  . ARG A 1 35  ? 22.50800 35.41300  13.83500  1.000 78.53835  ?  35  ARG A CD  1 
ATOM   192  N NE  . ARG A 1 35  ? 23.89300 34.95800  13.86500  1.000 81.95531  ?  35  ARG A NE  1 
ATOM   193  C CZ  . ARG A 1 35  ? 24.60200 34.65500  12.78500  1.000 84.25938  ?  35  ARG A CZ  1 
ATOM   194  N NH1 . ARG A 1 35  ? 24.08900 34.76300  11.56800  1.000 80.89480  ?  35  ARG A NH1 1 
ATOM   195  N NH2 . ARG A 1 35  ? 25.85500 34.23300  12.92800  1.000 87.80794  ?  35  ARG A NH2 1 
ATOM   196  N N   . PRO A 1 36  ? 21.77200 39.01700  14.86900  1.000 72.43534  ?  36  PRO A N   1 
ATOM   197  C CA  . PRO A 1 36  ? 22.40200 40.02700  14.01000  1.000 73.22600  ?  36  PRO A CA  1 
ATOM   198  C C   . PRO A 1 36  ? 22.91300 39.44100  12.70400  1.000 72.59823  ?  36  PRO A C   1 
ATOM   199  O O   . PRO A 1 36  ? 23.45700 38.33500  12.66400  1.000 75.49760  ?  36  PRO A O   1 
ATOM   200  C CB  . PRO A 1 36  ? 23.55000 40.55300  14.87700  1.000 77.31052  ?  36  PRO A CB  1 
ATOM   201  C CG  . PRO A 1 36  ? 23.08000 40.32800  16.27400  1.000 80.38105  ?  36  PRO A CG  1 
ATOM   202  C CD  . PRO A 1 36  ? 22.30900 39.04100  16.23800  1.000 79.73291  ?  36  PRO A CD  1 
ATOM   203  N N   . ILE A 1 37  ? 22.73800 40.20000  11.62800  1.000 67.85960  ?  37  ILE A N   1 
ATOM   204  C CA  . ILE A 1 37  ? 23.11500 39.76200  10.29100  1.000 70.77139  ?  37  ILE A CA  1 
ATOM   205  C C   . ILE A 1 37  ? 23.96300 40.84500  9.64100   1.000 70.84838  ?  37  ILE A C   1 
ATOM   206  O O   . ILE A 1 37  ? 23.68600 42.03900  9.79600   1.000 73.25112  ?  37  ILE A O   1 
ATOM   207  C CB  . ILE A 1 37  ? 21.87600 39.44700  9.42800   1.000 69.58606  ?  37  ILE A CB  1 
ATOM   208  N N   . ASP A 1 38  ? 25.00200 40.42600  8.92300   1.000 66.83637  ?  38  ASP A N   1 
ATOM   209  C CA  . ASP A 1 38  ? 25.81900 41.36700  8.17100   1.000 69.01231  ?  38  ASP A CA  1 
ATOM   210  C C   . ASP A 1 38  ? 25.02300 41.93300  7.00200   1.000 72.81242  ?  38  ASP A C   1 
ATOM   211  O O   . ASP A 1 38  ? 24.21200 41.23500  6.38800   1.000 72.24896  ?  38  ASP A O   1 
ATOM   212  C CB  . ASP A 1 38  ? 27.08700 40.68600  7.65500   1.000 70.34738  ?  38  ASP A CB  1 
ATOM   213  C CG  . ASP A 1 38  ? 27.96200 41.62200  6.83000   1.000 76.10851  ?  38  ASP A CG  1 
ATOM   214  O OD1 . ASP A 1 38  ? 27.78900 42.85600  6.93100   1.000 78.89914  ?  38  ASP A OD1 1 
ATOM   215  O OD2 . ASP A 1 38  ? 28.81700 41.12300  6.06600   1.000 75.24901  -1 38  ASP A OD2 1 
ATOM   216  N N   . SER A 1 39  ? 25.26300 43.21100  6.69300   1.000 74.39826  ?  39  SER A N   1 
ATOM   217  C CA  . SER A 1 39  ? 24.61600 43.83600  5.54500   1.000 71.42220  ?  39  SER A CA  1 
ATOM   218  C C   . SER A 1 39  ? 25.01700 43.17700  4.23300   1.000 66.09468  ?  39  SER A C   1 
ATOM   219  O O   . SER A 1 39  ? 24.28000 43.28500  3.24600   1.000 62.66406  ?  39  SER A O   1 
ATOM   220  C CB  . SER A 1 39  ? 24.95000 45.32800  5.49700   1.000 73.54967  ?  39  SER A CB  1 
ATOM   221  N N   . ASN A 1 40  ? 26.16700 42.50100  4.20100   1.000 67.01338  ?  40  ASN A N   1 
ATOM   222  C CA  . ASN A 1 40  ? 26.58600 41.75300  3.02300   1.000 68.56822  ?  40  ASN A CA  1 
ATOM   223  C C   . ASN A 1 40  ? 25.66200 40.58200  2.71000   1.000 64.64505  ?  40  ASN A C   1 
ATOM   224  O O   . ASN A 1 40  ? 25.78700 39.99000  1.63300   1.000 63.90819  ?  40  ASN A O   1 
ATOM   225  C CB  . ASN A 1 40  ? 28.01700 41.24700  3.20800   1.000 69.83542  ?  40  ASN A CB  1 
ATOM   226  N N   . THR A 1 41  ? 24.74700 40.23500  3.61800   1.000 61.50897  ?  41  THR A N   1 
ATOM   227  C CA  . THR A 1 41  ? 23.81500 39.14500  3.34800   1.000 60.82483  ?  41  THR A CA  1 
ATOM   228  C C   . THR A 1 41  ? 22.87200 39.49500  2.20300   1.000 58.92851  ?  41  THR A C   1 
ATOM   229  O O   . THR A 1 41  ? 22.53400 38.63400  1.38300   1.000 60.52737  ?  41  THR A O   1 
ATOM   230  C CB  . THR A 1 41  ? 23.03000 38.80600  4.61700   1.000 63.07615  ?  41  THR A CB  1 
ATOM   231  O OG1 . THR A 1 41  ? 23.94100 38.64800  5.71400   1.000 67.40289  ?  41  THR A OG1 1 
ATOM   232  C CG2 . THR A 1 41  ? 22.24500 37.51800  4.43800   1.000 62.16899  ?  41  THR A CG2 1 
ATOM   233  N N   . PHE A 1 42  ? 22.44700 40.75600  2.11900   1.000 59.62771  ?  42  PHE A N   1 
ATOM   234  C CA  . PHE A 1 42  ? 21.53300 41.22900  1.07600   1.000 57.40825  ?  42  PHE A CA  1 
ATOM   235  C C   . PHE A 1 42  ? 22.11900 42.51100  0.49200   1.000 57.52306  ?  42  PHE A C   1 
ATOM   236  O O   . PHE A 1 42  ? 21.70400 43.62000  0.83900   1.000 58.42245  ?  42  PHE A O   1 
ATOM   237  C CB  . PHE A 1 42  ? 20.13100 41.44600  1.63400   1.000 57.10115  ?  42  PHE A CB  1 
ATOM   238  C CG  . PHE A 1 42  ? 19.48400 40.19800  2.17300   1.000 56.54185  ?  42  PHE A CG  1 
ATOM   239  C CD1 . PHE A 1 42  ? 18.73400 39.37700  1.34500   1.000 57.23411  ?  42  PHE A CD1 1 
ATOM   240  C CD2 . PHE A 1 42  ? 19.63000 39.84100  3.50300   1.000 56.00957  ?  42  PHE A CD2 1 
ATOM   241  C CE1 . PHE A 1 42  ? 18.12600 38.23400  1.83900   1.000 57.41072  ?  42  PHE A CE1 1 
ATOM   242  C CE2 . PHE A 1 42  ? 19.03100 38.69700  4.00000   1.000 54.23373  ?  42  PHE A CE2 1 
ATOM   243  C CZ  . PHE A 1 42  ? 18.28100 37.89200  3.16600   1.000 57.02212  ?  42  PHE A CZ  1 
ATOM   244  N N   . GLU A 1 43  ? 23.09200 42.35300  -0.39800  1.000 57.42056  ?  43  GLU A N   1 
ATOM   245  C CA  . GLU A 1 43  ? 23.74700 43.48000  -1.05700  1.000 56.71292  ?  43  GLU A CA  1 
ATOM   246  C C   . GLU A 1 43  ? 23.10300 43.64300  -2.43000  1.000 59.58394  ?  43  GLU A C   1 
ATOM   247  O O   . GLU A 1 43  ? 23.60200 43.13400  -3.43400  1.000 58.35190  ?  43  GLU A O   1 
ATOM   248  C CB  . GLU A 1 43  ? 25.25100 43.25100  -1.15000  1.000 55.14143  ?  43  GLU A CB  1 
ATOM   249  N N   . MET A 1 44  ? 21.98500 44.36400  -2.47100  1.000 61.07851  ?  44  MET A N   1 
ATOM   250  C CA  . MET A 1 44  ? 21.20300 44.49800  -3.69400  1.000 61.50053  ?  44  MET A CA  1 
ATOM   251  C C   . MET A 1 44  ? 20.18400 45.61400  -3.50200  1.000 64.39372  ?  44  MET A C   1 
ATOM   252  O O   . MET A 1 44  ? 19.96200 46.09100  -2.38600  1.000 63.45151  ?  44  MET A O   1 
ATOM   253  C CB  . MET A 1 44  ? 20.50400 43.18600  -4.04100  1.000 56.05846  ?  44  MET A CB  1 
ATOM   254  C CG  . MET A 1 44  ? 19.41000 42.82500  -3.06000  1.000 57.93711  ?  44  MET A CG  1 
ATOM   255  S SD  . MET A 1 44  ? 18.84200 41.13200  -3.23300  1.000 57.89537  ?  44  MET A SD  1 
ATOM   256  C CE  . MET A 1 44  ? 20.33500 40.25300  -2.78600  1.000 57.07944  ?  44  MET A CE  1 
ATOM   257  N N   . ASN A 1 45  ? 19.56500 46.02400  -4.60700  1.000 67.06841  ?  45  ASN A N   1 
ATOM   258  C CA  . ASN A 1 45  ? 18.47600 46.98400  -4.53900  1.000 65.47592  ?  45  ASN A CA  1 
ATOM   259  C C   . ASN A 1 45  ? 17.16600 46.25500  -4.25800  1.000 66.07827  ?  45  ASN A C   1 
ATOM   260  O O   . ASN A 1 45  ? 17.09600 45.02300  -4.27400  1.000 66.28783  ?  45  ASN A O   1 
ATOM   261  C CB  . ASN A 1 45  ? 18.36800 47.78500  -5.83700  1.000 67.83300  ?  45  ASN A CB  1 
ATOM   262  C CG  . ASN A 1 45  ? 17.93300 46.93500  -7.01900  1.000 72.17683  ?  45  ASN A CG  1 
ATOM   263  O OD1 . ASN A 1 45  ? 18.01500 45.70700  -6.98400  1.000 72.20204  ?  45  ASN A OD1 1 
ATOM   264  N ND2 . ASN A 1 45  ? 17.47300 47.59100  -8.08000  1.000 72.08439  ?  45  ASN A ND2 1 
ATOM   265  N N   . GLY A 1 46  ? 16.11100 47.03100  -4.01300  1.000 65.20300  ?  46  GLY A N   1 
ATOM   266  C CA  . GLY A 1 46  ? 14.82100 46.42900  -3.72700  1.000 64.48707  ?  46  GLY A CA  1 
ATOM   267  C C   . GLY A 1 46  ? 14.27900 45.59800  -4.87200  1.000 65.34458  ?  46  GLY A C   1 
ATOM   268  O O   . GLY A 1 46  ? 13.55800 44.62100  -4.64700  1.000 63.55143  ?  46  GLY A O   1 
ATOM   269  N N   . LYS A 1 47  ? 14.61300 45.96800  -6.11200  1.000 66.92149  ?  47  LYS A N   1 
ATOM   270  C CA  . LYS A 1 47  ? 14.17300 45.18000  -7.25700  1.000 62.89329  ?  47  LYS A CA  1 
ATOM   271  C C   . LYS A 1 47  ? 14.77900 43.78600  -7.22300  1.000 63.20157  ?  47  LYS A C   1 
ATOM   272  O O   . LYS A 1 47  ? 14.08900 42.79300  -7.48200  1.000 64.04782  ?  47  LYS A O   1 
ATOM   273  C CB  . LYS A 1 47  ? 14.53600 45.88900  -8.56000  1.000 63.49181  ?  47  LYS A CB  1 
ATOM   274  N N   . ALA A 1 48  ? 16.06800 43.69000  -6.89200  1.000 59.41371  ?  48  ALA A N   1 
ATOM   275  C CA  . ALA A 1 48  ? 16.69600 42.38000  -6.77900  1.000 60.13606  ?  48  ALA A CA  1 
ATOM   276  C C   . ALA A 1 48  ? 16.11000 41.58400  -5.62000  1.000 56.97843  ?  48  ALA A C   1 
ATOM   277  O O   . ALA A 1 48  ? 15.91600 40.36700  -5.73100  1.000 57.80620  ?  48  ALA A O   1 
ATOM   278  C CB  . ALA A 1 48  ? 18.20500 42.53000  -6.61600  1.000 61.68259  ?  48  ALA A CB  1 
ATOM   279  N N   . LEU A 1 49  ? 15.85000 42.24700  -4.50300  1.000 58.07014  ?  49  LEU A N   1 
ATOM   280  C CA  . LEU A 1 49  ? 15.33800 41.54100  -3.33800  1.000 56.77260  ?  49  LEU A CA  1 
ATOM   281  C C   . LEU A 1 49  ? 14.02100 40.87700  -3.67800  1.000 58.40781  ?  49  LEU A C   1 
ATOM   282  O O   . LEU A 1 49  ? 13.74300 39.76800  -3.22700  1.000 57.61472  ?  49  LEU A O   1 
ATOM   283  C CB  . LEU A 1 49  ? 15.15900 42.49600  -2.16200  1.000 57.36684  ?  49  LEU A CB  1 
ATOM   284  C CG  . LEU A 1 49  ? 14.99400 41.83400  -0.79600  1.000 54.02153  ?  49  LEU A CG  1 
ATOM   285  C CD1 . LEU A 1 49  ? 16.20900 40.97200  -0.49100  1.000 53.62137  ?  49  LEU A CD1 1 
ATOM   286  C CD2 . LEU A 1 49  ? 14.79800 42.88500  0.28400   1.000 53.15480  ?  49  LEU A CD2 1 
ATOM   287  N N   . LEU A 1 50  ? 13.20900 41.54900  -4.48200  1.000 54.33619  ?  50  LEU A N   1 
ATOM   288  C CA  . LEU A 1 50  ? 11.91600 40.99800  -4.85600  1.000 55.21795  ?  50  LEU A CA  1 
ATOM   289  C C   . LEU A 1 50  ? 12.08400 39.72100  -5.65200  1.000 55.05592  ?  50  LEU A C   1 
ATOM   290  O O   . LEU A 1 50  ? 11.35800 38.75200  -5.44100  1.000 56.54455  ?  50  LEU A O   1 
ATOM   291  C CB  . LEU A 1 50  ? 11.12100 42.01500  -5.67000  1.000 58.19152  ?  50  LEU A CB  1 
ATOM   292  C CG  . LEU A 1 50  ? 10.75500 43.31200  -4.94900  1.000 59.98177  ?  50  LEU A CG  1 
ATOM   293  N N   . LEU A 1 51  ? 13.04200 39.71300  -6.56900  1.000 53.69445  ?  51  LEU A N   1 
ATOM   294  C CA  . LEU A 1 51  ? 13.26700 38.53500  -7.39800  1.000 56.79328  ?  51  LEU A CA  1 
ATOM   295  C C   . LEU A 1 51  ? 13.56700 37.30500  -6.55700  1.000 53.73757  ?  51  LEU A C   1 
ATOM   296  O O   . LEU A 1 51  ? 13.28800 36.18100  -6.98800  1.000 54.67562  ?  51  LEU A O   1 
ATOM   297  C CB  . LEU A 1 51  ? 14.41700 38.78000  -8.37200  1.000 55.69297  ?  51  LEU A CB  1 
ATOM   298  C CG  . LEU A 1 51  ? 14.27400 39.96700  -9.31400  1.000 55.90896  ?  51  LEU A CG  1 
ATOM   299  C CD1 . LEU A 1 51  ? 15.46800 40.02400  -10.25100 1.000 60.18660  ?  51  LEU A CD1 1 
ATOM   300  C CD2 . LEU A 1 51  ? 12.96800 39.87800  -10.08500 1.000 59.23090  ?  51  LEU A CD2 1 
ATOM   301  N N   . LEU A 1 52  ? 14.09200 37.51600  -5.35700  1.000 50.61248  ?  52  LEU A N   1 
ATOM   302  C CA  . LEU A 1 52  ? 14.46700 36.39900  -4.49800  1.000 52.00112  ?  52  LEU A CA  1 
ATOM   303  C C   . LEU A 1 52  ? 13.28800 35.65900  -3.89900  1.000 53.56890  ?  52  LEU A C   1 
ATOM   304  O O   . LEU A 1 52  ? 12.31200 36.27500  -3.47600  1.000 58.64712  ?  52  LEU A O   1 
ATOM   305  C CB  . LEU A 1 52  ? 15.36700 36.89300  -3.36500  1.000 52.17022  ?  52  LEU A CB  1 
ATOM   306  C CG  . LEU A 1 52  ? 16.60300 37.69700  -3.76200  1.000 55.77174  ?  52  LEU A CG  1 
ATOM   307  C CD1 . LEU A 1 52  ? 17.46400 37.94600  -2.53400  1.000 52.39539  ?  52  LEU A CD1 1 
ATOM   308  C CD2 . LEU A 1 52  ? 17.39300 36.95800  -4.82900  1.000 57.60634  ?  52  LEU A CD2 1 
ATOM   309  N N   . THR A 1 53  ? 13.37500 34.33900  -3.86000  1.000 50.75546  ?  53  THR A N   1 
ATOM   310  C CA  . THR A 1 53  ? 12.33700 33.52400  -3.25400  1.000 50.40510  ?  53  THR A CA  1 
ATOM   311  C C   . THR A 1 53  ? 12.65000 33.30700  -1.78100  1.000 54.37791  ?  53  THR A C   1 
ATOM   312  O O   . THR A 1 53  ? 13.77500 33.52600  -1.32600  1.000 55.91978  ?  53  THR A O   1 
ATOM   313  C CB  . THR A 1 53  ? 12.22300 32.17700  -3.96400  1.000 52.86151  ?  53  THR A CB  1 
ATOM   314  O OG1 . THR A 1 53  ? 13.38700 31.38900  -3.68100  1.000 55.37591  ?  53  THR A OG1 1 
ATOM   315  C CG2 . THR A 1 53  ? 12.12700 32.38900  -5.45500  1.000 55.05816  ?  53  THR A CG2 1 
ATOM   316  N N   . LYS A 1 54  ? 11.63500 32.86100  -1.03500  1.000 54.88238  ?  54  LYS A N   1 
ATOM   317  C CA  . LYS A 1 54  ? 11.82500 32.62900  0.39300   1.000 53.06364  ?  54  LYS A CA  1 
ATOM   318  C C   . LYS A 1 54  ? 12.93500 31.62100  0.64600   1.000 53.59846  ?  54  LYS A C   1 
ATOM   319  O O   . LYS A 1 54  ? 13.65700 31.73400  1.64400   1.000 55.20099  ?  54  LYS A O   1 
ATOM   320  C CB  . LYS A 1 54  ? 10.51700 32.16800  1.04300   1.000 46.84944  ?  54  LYS A CB  1 
ATOM   321  C CG  . LYS A 1 54  ? 10.59900 32.01900  2.56600   1.000 44.65123  ?  54  LYS A CG  1 
ATOM   322  C CD  . LYS A 1 54  ? 9.24100  31.73400  3.19900   1.000 44.84027  ?  54  LYS A CD  1 
ATOM   323  N N   . GLU A 1 55  ? 13.10100 30.64400  -0.25000  1.000 48.18647  ?  55  GLU A N   1 
ATOM   324  C CA  . GLU A 1 55  ? 14.22900 29.72600  -0.13200  1.000 50.75945  ?  55  GLU A CA  1 
ATOM   325  C C   . GLU A 1 55  ? 15.55900 30.45600  -0.28400  1.000 56.32807  ?  55  GLU A C   1 
ATOM   326  O O   . GLU A 1 55  ? 16.54900 30.08100  0.35400   1.000 59.31615  ?  55  GLU A O   1 
ATOM   327  C CB  . GLU A 1 55  ? 14.10400 28.61200  -1.17300  1.000 47.21682  ?  55  GLU A CB  1 
ATOM   328  N N   . ASP A 1 56  ? 15.59900 31.50500  -1.11100  1.000 59.85131  ?  56  ASP A N   1 
ATOM   329  C CA  . ASP A 1 56  ? 16.81800 32.29800  -1.24100  1.000 59.81955  ?  56  ASP A CA  1 
ATOM   330  C C   . ASP A 1 56  ? 17.06500 33.13400  0.01000   1.000 61.60657  ?  56  ASP A C   1 
ATOM   331  O O   . ASP A 1 56  ? 18.21700 33.33500  0.40900   1.000 63.62275  ?  56  ASP A O   1 
ATOM   332  C CB  . ASP A 1 56  ? 16.74000 33.19400  -2.48000  1.000 59.14643  ?  56  ASP A CB  1 
ATOM   333  C CG  . ASP A 1 56  ? 16.36000 32.43200  -3.73500  1.000 58.83209  ?  56  ASP A CG  1 
ATOM   334  O OD1 . ASP A 1 56  ? 16.24300 31.19200  -3.66800  1.000 60.96208  ?  56  ASP A OD1 1 
ATOM   335  O OD2 . ASP A 1 56  ? 16.16500 33.07900  -4.78700  1.000 58.45101  -1 56  ASP A OD2 1 
ATOM   336  N N   . PHE A 1 57  ? 15.99500 33.64100  0.63200   1.000 63.13231  ?  57  PHE A N   1 
ATOM   337  C CA  . PHE A 1 57  ? 16.14100 34.34700  1.90200   1.000 62.37534  ?  57  PHE A CA  1 
ATOM   338  C C   . PHE A 1 57  ? 16.65500 33.41400  2.99100   1.000 63.86719  ?  57  PHE A C   1 
ATOM   339  O O   . PHE A 1 57  ? 17.49900 33.80500  3.80600   1.000 64.92502  ?  57  PHE A O   1 
ATOM   340  C CB  . PHE A 1 57  ? 14.80700 34.96500  2.32400   1.000 60.94016  ?  57  PHE A CB  1 
ATOM   341  C CG  . PHE A 1 57  ? 14.45100 36.21700  1.57400   1.000 61.11633  ?  57  PHE A CG  1 
ATOM   342  C CD1 . PHE A 1 57  ? 13.91600 36.15000  0.30000   1.000 62.42452  ?  57  PHE A CD1 1 
ATOM   343  C CD2 . PHE A 1 57  ? 14.64400 37.46100  2.15100   1.000 61.73820  ?  57  PHE A CD2 1 
ATOM   344  C CE1 . PHE A 1 57  ? 13.58600 37.30000  -0.39000  1.000 64.94824  ?  57  PHE A CE1 1 
ATOM   345  C CE2 . PHE A 1 57  ? 14.31800 38.61500  1.46800   1.000 63.87605  ?  57  PHE A CE2 1 
ATOM   346  C CZ  . PHE A 1 57  ? 13.78700 38.53400  0.19500   1.000 65.74759  ?  57  PHE A CZ  1 
ATOM   347  N N   . ARG A 1 58  ? 16.15000 32.17900  3.02200   1.000 59.30165  ?  58  ARG A N   1 
ATOM   348  C CA  . ARG A 1 58  ? 16.60800 31.21400  4.01500   1.000 55.32636  ?  58  ARG A CA  1 
ATOM   349  C C   . ARG A 1 58  ? 18.08900 30.90600  3.84000   1.000 58.69815  ?  58  ARG A C   1 
ATOM   350  O O   . ARG A 1 58  ? 18.84800 30.87600  4.81600   1.000 59.43670  ?  58  ARG A O   1 
ATOM   351  C CB  . ARG A 1 58  ? 15.78200 29.93200  3.92300   1.000 48.32258  ?  58  ARG A CB  1 
ATOM   352  C CG  . ARG A 1 58  ? 14.33800 30.07400  4.36200   1.000 44.98933  ?  58  ARG A CG  1 
ATOM   353  C CD  . ARG A 1 58  ? 13.68800 28.70600  4.45100   1.000 42.42826  ?  58  ARG A CD  1 
ATOM   354  N NE  . ARG A 1 58  ? 12.29600 28.76500  4.87800   1.000 42.45940  ?  58  ARG A NE  1 
ATOM   355  C CZ  . ARG A 1 58  ? 11.26000 28.72800  4.05300   1.000 42.23609  ?  58  ARG A CZ  1 
ATOM   356  N NH1 . ARG A 1 58  ? 11.42200 28.61600  2.74500   1.000 46.51975  ?  58  ARG A NH1 1 
ATOM   357  N NH2 . ARG A 1 58  ? 10.02900 28.79600  4.55300   1.000 46.77686  ?  58  ARG A NH2 1 
ATOM   358  N N   . TYR A 1 59  ? 18.52200 30.68000  2.59600   1.000 56.16819  ?  59  TYR A N   1 
ATOM   359  C CA  . TYR A 1 59  ? 19.91900 30.33400  2.34900   1.000 58.36934  ?  59  TYR A CA  1 
ATOM   360  C C   . TYR A 1 59  ? 20.85400 31.47800  2.72500   1.000 61.92374  ?  59  TYR A C   1 
ATOM   361  O O   . TYR A 1 59  ? 21.95600 31.24300  3.23700   1.000 67.18978  ?  59  TYR A O   1 
ATOM   362  C CB  . TYR A 1 59  ? 20.11600 29.94600  0.88300   1.000 58.82422  ?  59  TYR A CB  1 
ATOM   363  N N   . ARG A 1 60  ? 20.43600 32.72100  2.48300   1.000 61.80577  ?  60  ARG A N   1 
ATOM   364  C CA  . ARG A 1 60  ? 21.30200 33.86100  2.77300   1.000 61.81940  ?  60  ARG A CA  1 
ATOM   365  C C   . ARG A 1 60  ? 21.51200 34.03000  4.27700   1.000 60.72358  ?  60  ARG A C   1 
ATOM   366  O O   . ARG A 1 60  ? 22.63500 33.89700  4.77300   1.000 60.31115  ?  60  ARG A O   1 
ATOM   367  C CB  . ARG A 1 60  ? 20.73100 35.13300  2.13500   1.000 59.17302  ?  60  ARG A CB  1 
ATOM   368  C CG  . ARG A 1 60  ? 20.88700 35.17700  0.61000   1.000 58.83218  ?  60  ARG A CG  1 
ATOM   369  C CD  . ARG A 1 60  ? 20.40400 36.49000  0.00300   1.000 57.41915  ?  60  ARG A CD  1 
ATOM   370  N NE  . ARG A 1 60  ? 20.70800 36.58600  -1.42200  1.000 58.23621  ?  60  ARG A NE  1 
ATOM   371  C CZ  . ARG A 1 60  ? 21.78800 37.16800  -1.92900  1.000 58.14061  ?  60  ARG A CZ  1 
ATOM   372  N NH1 . ARG A 1 60  ? 22.69400 37.74400  -1.15500  1.000 57.43243  ?  60  ARG A NH1 1 
ATOM   373  N NH2 . ARG A 1 60  ? 21.96200 37.17600  -3.24700  1.000 58.90915  ?  60  ARG A NH2 1 
ATOM   374  N N   . SER A 1 61  ? 20.44200 34.31700  5.02500   1.000 59.75796  ?  61  SER A N   1 
ATOM   375  C CA  . SER A 1 61  ? 20.51200 34.46800  6.48000   1.000 59.31951  ?  61  SER A CA  1 
ATOM   376  C C   . SER A 1 61  ? 19.67600 33.37000  7.11700   1.000 57.96339  ?  61  SER A C   1 
ATOM   377  O O   . SER A 1 61  ? 18.46600 33.54600  7.33100   1.000 56.97080  ?  61  SER A O   1 
ATOM   378  C CB  . SER A 1 61  ? 20.00900 35.83100  6.94200   1.000 60.48649  ?  61  SER A CB  1 
ATOM   379  O OG  . SER A 1 61  ? 18.64000 35.99100  6.61800   1.000 60.00698  ?  61  SER A OG  1 
ATOM   380  N N   . PRO A 1 62  ? 20.28000 32.23400  7.46100   1.000 61.79774  ?  62  PRO A N   1 
ATOM   381  C CA  . PRO A 1 62  ? 19.47900 31.11900  7.98700   1.000 58.56755  ?  62  PRO A CA  1 
ATOM   382  C C   . PRO A 1 62  ? 18.74300 31.46800  9.26300   1.000 60.12267  ?  62  PRO A C   1 
ATOM   383  O O   . PRO A 1 62  ? 17.61200 31.01200  9.46500   1.000 58.65915  ?  62  PRO A O   1 
ATOM   384  C CB  . PRO A 1 62  ? 20.52400 30.01900  8.21900   1.000 57.58579  ?  62  PRO A CB  1 
ATOM   385  C CG  . PRO A 1 62  ? 21.70000 30.41500  7.35900   1.000 61.09383  ?  62  PRO A CG  1 
ATOM   386  C CD  . PRO A 1 62  ? 21.71000 31.90600  7.37000   1.000 61.78610  ?  62  PRO A CD  1 
ATOM   387  N N   . HIS A 1 63  ? 19.35000 32.29100  10.12100  1.000 62.32240  ?  63  HIS A N   1 
ATOM   388  C CA  . HIS A 1 63  ? 18.77400 32.55100  11.43500  1.000 61.39783  ?  63  HIS A CA  1 
ATOM   389  C C   . HIS A 1 63  ? 17.48900 33.36100  11.33200  1.000 57.53656  ?  63  HIS A C   1 
ATOM   390  O O   . HIS A 1 63  ? 16.54400 33.13900  12.09700  1.000 56.50860  ?  63  HIS A O   1 
ATOM   391  C CB  . HIS A 1 63  ? 19.78500 33.28200  12.31200  1.000 66.45848  ?  63  HIS A CB  1 
ATOM   392  C CG  . HIS A 1 63  ? 21.04900 32.51700  12.54600  1.000 71.36049  ?  63  HIS A CG  1 
ATOM   393  N ND1 . HIS A 1 63  ? 22.07300 32.47700  11.62500  1.000 74.04693  ?  63  HIS A ND1 1 
ATOM   394  C CD2 . HIS A 1 63  ? 21.45700 31.76700  13.59700  1.000 75.60554  ?  63  HIS A CD2 1 
ATOM   395  C CE1 . HIS A 1 63  ? 23.05900 31.73500  12.09900  1.000 78.29153  ?  63  HIS A CE1 1 
ATOM   396  N NE2 . HIS A 1 63  ? 22.71000 31.29200  13.29400  1.000 78.04800  ?  63  HIS A NE2 1 
ATOM   397  N N   . SER A 1 64  ? 17.43200 34.30900  10.40400  1.000 55.66471  ?  64  SER A N   1 
ATOM   398  C CA  . SER A 1 64  ? 16.26800 35.17900  10.35300  1.000 55.39017  ?  64  SER A CA  1 
ATOM   399  C C   . SER A 1 64  ? 15.85000 35.47500  8.92000   1.000 52.43146  ?  64  SER A C   1 
ATOM   400  O O   . SER A 1 64  ? 15.19300 36.48600  8.65900   1.000 49.78159  ?  64  SER A O   1 
ATOM   401  C CB  . SER A 1 64  ? 16.53200 36.47900  11.11300  1.000 56.87667  ?  64  SER A CB  1 
ATOM   402  N N   . GLY A 1 65  ? 16.21200 34.60300  7.98100   1.000 53.36160  ?  65  GLY A N   1 
ATOM   403  C CA  . GLY A 1 65  ? 15.76900 34.79900  6.61100   1.000 53.76804  ?  65  GLY A CA  1 
ATOM   404  C C   . GLY A 1 65  ? 14.27200 34.63500  6.45700   1.000 51.73128  ?  65  GLY A C   1 
ATOM   405  O O   . GLY A 1 65  ? 13.62800 35.39300  5.72500   1.000 50.51071  ?  65  GLY A O   1 
ATOM   406  N N   . ASP A 1 66  ? 13.69500 33.65100  7.15200   1.000 50.16122  ?  66  ASP A N   1 
ATOM   407  C CA  . ASP A 1 66  ? 12.26700 33.38900  7.02400   1.000 48.85186  ?  66  ASP A CA  1 
ATOM   408  C C   . ASP A 1 66  ? 11.45500 34.62000  7.39700   1.000 49.72570  ?  66  ASP A C   1 
ATOM   409  O O   . ASP A 1 66  ? 10.62000 35.08900  6.61500   1.000 47.16776  ?  66  ASP A O   1 
ATOM   410  C CB  . ASP A 1 66  ? 11.87300 32.19600  7.89700   1.000 47.09519  ?  66  ASP A CB  1 
ATOM   411  N N   . GLU A 1 67  ? 11.71200 35.17400  8.58100   1.000 48.92170  ?  67  GLU A N   1 
ATOM   412  C CA  . GLU A 1 67  ? 10.92300 36.30400  9.05400   1.000 47.83421  ?  67  GLU A CA  1 
ATOM   413  C C   . GLU A 1 67  ? 11.17100 37.53100  8.18300   1.000 49.72770  ?  67  GLU A C   1 
ATOM   414  O O   . GLU A 1 67  ? 10.24700 38.30500  7.90500   1.000 53.58823  ?  67  GLU A O   1 
ATOM   415  C CB  . GLU A 1 67  ? 11.25000 36.61600  10.51600  1.000 46.12495  ?  67  GLU A CB  1 
ATOM   416  N N   . LEU A 1 68  ? 12.41000 37.71800  7.71600   1.000 50.45995  ?  68  LEU A N   1 
ATOM   417  C CA  . LEU A 1 68  ? 12.69100 38.83900  6.82300   1.000 49.65590  ?  68  LEU A CA  1 
ATOM   418  C C   . LEU A 1 68  ? 11.85700 38.75700  5.55400   1.000 51.90908  ?  68  LEU A C   1 
ATOM   419  O O   . LEU A 1 68  ? 11.29500 39.76200  5.10700   1.000 52.27438  ?  68  LEU A O   1 
ATOM   420  C CB  . LEU A 1 68  ? 14.17500 38.88700  6.47200   1.000 46.25546  ?  68  LEU A CB  1 
ATOM   421  C CG  . LEU A 1 68  ? 15.08200 39.43600  7.56500   1.000 48.25423  ?  68  LEU A CG  1 
ATOM   422  C CD1 . LEU A 1 68  ? 16.52200 39.38400  7.10500   1.000 52.39874  ?  68  LEU A CD1 1 
ATOM   423  C CD2 . LEU A 1 68  ? 14.67000 40.85200  7.91500   1.000 51.35827  ?  68  LEU A CD2 1 
ATOM   424  N N   . TYR A 1 69  ? 11.74800 37.56200  4.99100   1.000 49.94914  ?  69  TYR A N   1 
ATOM   425  C CA  . TYR A 1 69  ? 10.92800 37.38500  3.80600   1.000 50.47807  ?  69  TYR A CA  1 
ATOM   426  C C   . TYR A 1 69  ? 9.49500  37.74500  4.12200   1.000 52.61775  ?  69  TYR A C   1 
ATOM   427  O O   . TYR A 1 69  ? 8.87300  38.52600  3.40700   1.000 56.18666  ?  69  TYR A O   1 
ATOM   428  C CB  . TYR A 1 69  ? 11.00000 35.94400  3.32400   1.000 50.83686  ?  69  TYR A CB  1 
ATOM   429  C CG  . TYR A 1 69  ? 10.16000 35.66100  2.10400   1.000 52.42740  ?  69  TYR A CG  1 
ATOM   430  C CD1 . TYR A 1 69  ? 10.66000 35.87900  0.83000   1.000 54.99963  ?  69  TYR A CD1 1 
ATOM   431  C CD2 . TYR A 1 69  ? 8.86900  35.17000  2.22600   1.000 50.75677  ?  69  TYR A CD2 1 
ATOM   432  C CE1 . TYR A 1 69  ? 9.89900  35.61800  -0.29100  1.000 56.77276  ?  69  TYR A CE1 1 
ATOM   433  C CE2 . TYR A 1 69  ? 8.09900  34.90600  1.11100   1.000 52.39696  ?  69  TYR A CE2 1 
ATOM   434  C CZ  . TYR A 1 69  ? 8.61900  35.13100  -0.14400  1.000 57.13944  ?  69  TYR A CZ  1 
ATOM   435  O OH  . TYR A 1 69  ? 7.85600  34.87100  -1.25700  1.000 64.29699  ?  69  TYR A OH  1 
ATOM   436  N N   . GLU A 1 70  ? 8.96500  37.18100  5.20100   1.000 52.29131  ?  70  GLU A N   1 
ATOM   437  C CA  . GLU A 1 70  ? 7.57600  37.44000  5.55500   1.000 54.68297  ?  70  GLU A CA  1 
ATOM   438  C C   . GLU A 1 70  ? 7.35300  38.92000  5.83300   1.000 55.88260  ?  70  GLU A C   1 
ATOM   439  O O   . GLU A 1 70  ? 6.30100  39.47200  5.49000   1.000 60.49868  ?  70  GLU A O   1 
ATOM   440  C CB  . GLU A 1 70  ? 7.17100  36.59400  6.76200   1.000 52.39858  ?  70  GLU A CB  1 
ATOM   441  C CG  . GLU A 1 70  ? 7.44700  35.10600  6.60400   1.000 50.34975  ?  70  GLU A CG  1 
ATOM   442  C CD  . GLU A 1 70  ? 6.72500  34.47400  5.42300   1.000 53.43234  ?  70  GLU A CD  1 
ATOM   443  O OE1 . GLU A 1 70  ? 5.66500  34.99100  5.00700   1.000 52.15588  ?  70  GLU A OE1 1 
ATOM   444  O OE2 . GLU A 1 70  ? 7.22300  33.44500  4.91400   1.000 54.34721  -1 70  GLU A OE2 1 
ATOM   445  N N   . LEU A 1 71  ? 8.33900  39.58200  6.44500   1.000 54.82018  ?  71  LEU A N   1 
ATOM   446  C CA  . LEU A 1 71  ? 8.23800  41.02100  6.66700   1.000 61.08714  ?  71  LEU A CA  1 
ATOM   447  C C   . LEU A 1 71  ? 8.11100  41.76500  5.34400   1.000 64.32445  ?  71  LEU A C   1 
ATOM   448  O O   . LEU A 1 71  ? 7.24200  42.63000  5.18400   1.000 65.16071  ?  71  LEU A O   1 
ATOM   449  C CB  . LEU A 1 71  ? 9.45200  41.52400  7.45100   1.000 54.31413  ?  71  LEU A CB  1 
ATOM   450  C CG  . LEU A 1 71  ? 9.52100  41.20200  8.94500   1.000 51.26412  ?  71  LEU A CG  1 
ATOM   451  N N   . LEU A 1 72  ? 8.97100  41.43100  4.38000   1.000 61.88429  ?  72  LEU A N   1 
ATOM   452  C CA  . LEU A 1 72  ? 8.89700  42.06800  3.07100   1.000 60.58387  ?  72  LEU A CA  1 
ATOM   453  C C   . LEU A 1 72  ? 7.52600  41.85200  2.44400   1.000 66.20903  ?  72  LEU A C   1 
ATOM   454  O O   . LEU A 1 72  ? 6.90400  42.79500  1.94100   1.000 69.78270  ?  72  LEU A O   1 
ATOM   455  C CB  . LEU A 1 72  ? 10.00800 41.53300  2.16700   1.000 54.30959  ?  72  LEU A CB  1 
ATOM   456  C CG  . LEU A 1 72  ? 10.08800 42.12100  0.75700   1.000 55.80677  ?  72  LEU A CG  1 
ATOM   457  N N   . GLN A 1 73  ? 7.03600  40.62400  2.51300   1.000 64.10385  ?  73  GLN A N   1 
ATOM   458  C CA  . GLN A 1 73  ? 5.71600  40.34400  1.98100   1.000 67.70922  ?  73  GLN A CA  1 
ATOM   459  C C   . GLN A 1 73  ? 4.67600  41.20400  2.68700   1.000 70.97173  ?  73  GLN A C   1 
ATOM   460  O O   . GLN A 1 73  ? 3.81000  41.79300  2.04100   1.000 71.60508  ?  73  GLN A O   1 
ATOM   461  C CB  . GLN A 1 73  ? 5.38800  38.86200  2.12800   1.000 64.03575  ?  73  GLN A CB  1 
ATOM   462  C CG  . GLN A 1 73  ? 6.41500  37.95400  1.47400   1.000 61.62626  ?  73  GLN A CG  1 
ATOM   463  C CD  . GLN A 1 73  ? 6.59000  38.24900  -0.00200  1.000 62.53409  ?  73  GLN A CD  1 
ATOM   464  O OE1 . GLN A 1 73  ? 5.64500  38.64500  -0.68500  1.000 61.69133  ?  73  GLN A OE1 1 
ATOM   465  N NE2 . GLN A 1 73  ? 7.80200  38.05200  -0.50500  1.000 64.87945  ?  73  GLN A NE2 1 
ATOM   466  N N   . HIS A 1 74  ? 4.76500  41.29000  4.01000   1.000 80.26802  ?  74  HIS A N   1 
ATOM   467  C CA  . HIS A 1 74  ? 3.81300  42.10800  4.75600   1.000 82.54690  ?  74  HIS A CA  1 
ATOM   468  C C   . HIS A 1 74  ? 3.94000  43.58100  4.38200   1.000 84.72382  ?  74  HIS A C   1 
ATOM   469  O O   . HIS A 1 74  ? 2.94000  44.30900  4.36200   1.000 86.82031  ?  74  HIS A O   1 
ATOM   470  C CB  . HIS A 1 74  ? 4.00500  41.91200  6.26100   1.000 81.32203  ?  74  HIS A CB  1 
ATOM   471  C CG  . HIS A 1 74  ? 3.42300  40.63400  6.78900   1.000 82.53291  ?  74  HIS A CG  1 
ATOM   472  N ND1 . HIS A 1 74  ? 4.13600  39.45500  6.83600   1.000 84.55490  ?  74  HIS A ND1 1 
ATOM   473  C CD2 . HIS A 1 74  ? 2.20000  40.35200  7.29800   1.000 82.52041  ?  74  HIS A CD2 1 
ATOM   474  C CE1 . HIS A 1 74  ? 3.37800  38.50200  7.34900   1.000 80.80940  ?  74  HIS A CE1 1 
ATOM   475  N NE2 . HIS A 1 74  ? 2.19700  39.02000  7.63800   1.000 80.54571  ?  74  HIS A NE2 1 
ATOM   476  N N   . ILE A 1 75  ? 5.15800  44.03900  4.08100   1.000 76.41555  ?  75  ILE A N   1 
ATOM   477  C CA  . ILE A 1 75  ? 5.33300  45.41600  3.62800   1.000 75.40289  ?  75  ILE A CA  1 
ATOM   478  C C   . ILE A 1 75  ? 4.71500  45.60000  2.24800   1.000 75.19816  ?  75  ILE A C   1 
ATOM   479  O O   . ILE A 1 75  ? 4.14000  46.65200  1.94200   1.000 76.22691  ?  75  ILE A O   1 
ATOM   480  C CB  . ILE A 1 75  ? 6.82400  45.80100  3.63700   1.000 65.67379  ?  75  ILE A CB  1 
ATOM   481  C CG1 . ILE A 1 75  ? 7.36100  45.84600  5.06900   1.000 67.55062  ?  75  ILE A CG1 1 
ATOM   482  C CG2 . ILE A 1 75  ? 7.03500  47.14400  2.96000   1.000 67.44686  ?  75  ILE A CG2 1 
ATOM   483  N N   . LEU A 1 76  ? 4.81300  44.57400  1.39800   1.000 72.48344  ?  76  LEU A N   1 
ATOM   484  C CA  . LEU A 1 76  ? 4.25000  44.64700  0.05500   1.000 72.92352  ?  76  LEU A CA  1 
ATOM   485  C C   . LEU A 1 76  ? 2.72700  44.68300  0.07300   1.000 77.71504  ?  76  LEU A C   1 
ATOM   486  O O   . LEU A 1 76  ? 2.11400  45.25400  -0.83700  1.000 78.37999  ?  76  LEU A O   1 
ATOM   487  C CB  . LEU A 1 76  ? 4.74300  43.46100  -0.78000  1.000 66.50430  ?  76  LEU A CB  1 
ATOM   488  N N   . LYS A 1 77  ? 2.10200  44.08900  1.09100   1.000 77.97257  ?  77  LYS A N   1 
ATOM   489  C CA  . LYS A 1 77  ? 0.64600  44.06100  1.15700   1.000 80.95833  ?  77  LYS A CA  1 
ATOM   490  C C   . LYS A 1 77  ? 0.05600  45.38500  1.63600   1.000 88.15182  ?  77  LYS A C   1 
ATOM   491  O O   . LYS A 1 77  ? -1.07000 45.72500  1.25500   1.000 89.54930  ?  77  LYS A O   1 
ATOM   492  C CB  . LYS A 1 77  ? 0.18300  42.92800  2.07400   1.000 80.57167  ?  77  LYS A CB  1 
ATOM   493  N N   . GLN A 1 78  ? 0.78200  46.13800  2.45900   1.000 99.22937  ?  78  GLN A N   1 
ATOM   494  C CA  . GLN A 1 78  ? 0.27500  47.40800  2.97900   1.000 101.25279 ?  78  GLN A CA  1 
ATOM   495  C C   . GLN A 1 78  ? 0.29300  48.50800  1.92000   1.000 102.03696 ?  78  GLN A C   1 
ATOM   496  O O   . GLN A 1 78  ? 0.88600  48.35300  0.85100   1.000 103.82021 ?  78  GLN A O   1 
ATOM   497  C CB  . GLN A 1 78  ? 1.08800  47.85000  4.19800   1.000 100.89223 ?  78  GLN A CB  1 
ATOM   498  N N   . ILE A 1 88  ? 11.72000 43.84100  -17.02300 1.000 74.33959  ?  88  ILE A N   1 
ATOM   499  C CA  . ILE A 1 88  ? 12.33700 43.82800  -18.34200 1.000 80.37123  ?  88  ILE A CA  1 
ATOM   500  C C   . ILE A 1 88  ? 13.49000 44.83000  -18.41300 1.000 81.55423  ?  88  ILE A C   1 
ATOM   501  O O   . ILE A 1 88  ? 14.45200 44.73000  -17.65000 1.000 80.48450  ?  88  ILE A O   1 
ATOM   502  C CB  . ILE A 1 88  ? 11.29600 44.11100  -19.43800 1.000 85.92864  ?  88  ILE A CB  1 
ATOM   503  N N   . ARG A 1 89  ? 13.38400 45.78800  -19.33900 1.000 81.86013  ?  89  ARG A N   1 
ATOM   504  C CA  . ARG A 1 89  ? 14.40000 46.82300  -19.55600 1.000 78.85645  ?  89  ARG A CA  1 
ATOM   505  C C   . ARG A 1 89  ? 15.75500 46.22700  -19.93400 1.000 78.26241  ?  89  ARG A C   1 
ATOM   506  O O   . ARG A 1 89  ? 16.80400 46.76100  -19.56500 1.000 77.03686  ?  89  ARG A O   1 
ATOM   507  C CB  . ARG A 1 89  ? 14.54100 47.73800  -18.33400 1.000 78.11507  ?  89  ARG A CB  1 
ATOM   508  N N   . LEU A 1 90  ? 15.74200 45.12400  -20.67800 1.000 79.76399  ?  90  LEU A N   1 
ATOM   509  C CA  . LEU A 1 90  ? 16.98800 44.51600  -21.11900 1.000 79.39742  ?  90  LEU A CA  1 
ATOM   510  C C   . LEU A 1 90  ? 17.63200 45.37500  -22.20500 1.000 82.22942  ?  90  LEU A C   1 
ATOM   511  O O   . LEU A 1 90  ? 16.92600 45.97000  -23.02900 1.000 81.27267  ?  90  LEU A O   1 
ATOM   512  C CB  . LEU A 1 90  ? 16.74200 43.10300  -21.64600 1.000 76.24941  ?  90  LEU A CB  1 
ATOM   513  N N   . PRO A 1 91  ? 18.96300 45.46400  -22.22900 1.000 82.19603  ?  91  PRO A N   1 
ATOM   514  C CA  . PRO A 1 91  ? 19.62900 46.27000  -23.25700 1.000 81.27646  ?  91  PRO A CA  1 
ATOM   515  C C   . PRO A 1 91  ? 19.29700 45.77200  -24.65400 1.000 85.26484  ?  91  PRO A C   1 
ATOM   516  O O   . PRO A 1 91  ? 18.96400 44.60300  -24.86200 1.000 85.16011  ?  91  PRO A O   1 
ATOM   517  C CB  . PRO A 1 91  ? 21.11900 46.09200  -22.94000 1.000 80.24171  ?  91  PRO A CB  1 
ATOM   518  C CG  . PRO A 1 91  ? 21.15500 45.71000  -21.50400 1.000 79.02917  ?  91  PRO A CG  1 
ATOM   519  C CD  . PRO A 1 91  ? 19.92400 44.88300  -21.27800 1.000 79.55679  ?  91  PRO A CD  1 
ATOM   520  N N   . ALA A 1 92  ? 19.38600 46.68700  -25.62000 1.000 86.39902  ?  92  ALA A N   1 
ATOM   521  C CA  . ALA A 1 92  ? 19.11500 46.32000  -27.00400 1.000 88.63830  ?  92  ALA A CA  1 
ATOM   522  C C   . ALA A 1 92  ? 20.07700 45.24600  -27.49100 1.000 87.13941  ?  92  ALA A C   1 
ATOM   523  O O   . ALA A 1 92  ? 19.68700 44.36700  -28.26700 1.000 87.68131  ?  92  ALA A O   1 
ATOM   524  C CB  . ALA A 1 92  ? 19.19400 47.55600  -27.89600 1.000 95.05718  ?  92  ALA A CB  1 
ATOM   525  N N   . HIS A 1 93  ? 21.33100 45.29000  -27.03700 1.000 86.18087  ?  93  HIS A N   1 
ATOM   526  C CA  . HIS A 1 93  ? 22.29700 44.27100  -27.43300 1.000 85.94303  ?  93  HIS A CA  1 
ATOM   527  C C   . HIS A 1 93  ? 21.90800 42.89100  -26.91600 1.000 86.97806  ?  93  HIS A C   1 
ATOM   528  O O   . HIS A 1 93  ? 22.27400 41.87600  -27.52100 1.000 85.70030  ?  93  HIS A O   1 
ATOM   529  C CB  . HIS A 1 93  ? 23.69200 44.65400  -26.93500 1.000 85.27275  ?  93  HIS A CB  1 
ATOM   530  C CG  . HIS A 1 93  ? 23.77800 44.82500  -25.45000 1.000 83.00703  ?  93  HIS A CG  1 
ATOM   531  N N   . LEU A 1 94  ? 21.16000 42.83100  -25.81300 1.000 87.49334  ?  94  LEU A N   1 
ATOM   532  C CA  . LEU A 1 94  ? 20.74300 41.57200  -25.20800 1.000 88.97455  ?  94  LEU A CA  1 
ATOM   533  C C   . LEU A 1 94  ? 19.23500 41.35800  -25.29800 1.000 88.78691  ?  94  LEU A C   1 
ATOM   534  O O   . LEU A 1 94  ? 18.67600 40.57900  -24.52100 1.000 85.82162  ?  94  LEU A O   1 
ATOM   535  C CB  . LEU A 1 94  ? 21.20100 41.51200  -23.75100 1.000 87.00384  ?  94  LEU A CB  1 
ATOM   536  C CG  . LEU A 1 94  ? 22.67000 41.86600  -23.51300 1.000 84.99298  ?  94  LEU A CG  1 
ATOM   537  C CD1 . LEU A 1 94  ? 22.94500 42.02600  -22.03200 1.000 82.73214  ?  94  LEU A CD1 1 
ATOM   538  C CD2 . LEU A 1 94  ? 23.58400 40.81200  -24.11700 1.000 83.92568  ?  94  LEU A CD2 1 
ATOM   539  N N   . ARG A 1 95  ? 18.56500 42.03900  -26.23100 1.000 85.25259  ?  95  ARG A N   1 
ATOM   540  C CA  . ARG A 1 95  ? 17.12100 41.88600  -26.36800 1.000 85.15283  ?  95  ARG A CA  1 
ATOM   541  C C   . ARG A 1 95  ? 16.73600 40.55300  -26.99800 1.000 84.57831  ?  95  ARG A C   1 
ATOM   542  O O   . ARG A 1 95  ? 15.56500 40.16600  -26.92800 1.000 87.75552  ?  95  ARG A O   1 
ATOM   543  C CB  . ARG A 1 95  ? 16.54500 43.03900  -27.19100 1.000 85.55959  ?  95  ARG A CB  1 
ATOM   544  N N   . LEU A 1 96  ? 17.68700 39.84600  -27.60600 1.000 82.03157  ?  96  LEU A N   1 
ATOM   545  C CA  . LEU A 1 96  ? 17.40500 38.54400  -28.19000 1.000 80.79765  ?  96  LEU A CA  1 
ATOM   546  C C   . LEU A 1 96  ? 17.16900 37.50800  -27.09100 1.000 80.34827  ?  96  LEU A C   1 
ATOM   547  O O   . LEU A 1 96  ? 17.37600 37.76200  -25.90100 1.000 79.68300  ?  96  LEU A O   1 
ATOM   548  C CB  . LEU A 1 96  ? 18.54500 38.10900  -29.11800 1.000 80.98875  ?  96  LEU A CB  1 
ATOM   549  C CG  . LEU A 1 96  ? 19.92900 37.74300  -28.56500 1.000 79.97442  ?  96  LEU A CG  1 
ATOM   550  C CD1 . LEU A 1 96  ? 20.74700 37.02600  -29.63100 1.000 80.50980  ?  96  LEU A CD1 1 
ATOM   551  C CD2 . LEU A 1 96  ? 20.69000 38.96700  -28.06400 1.000 82.47285  ?  96  LEU A CD2 1 
ATOM   552  N N   . GLN A 1 97  ? 16.71600 36.32700  -27.50400 1.000 78.53987  ?  97  GLN A N   1 
ATOM   553  C CA  . GLN A 1 97  ? 16.40000 35.28300  -26.54300 1.000 78.93103  ?  97  GLN A CA  1 
ATOM   554  C C   . GLN A 1 97  ? 17.67900 34.66200  -25.98400 1.000 77.12770  ?  97  GLN A C   1 
ATOM   555  O O   . GLN A 1 97  ? 18.68900 34.56100  -26.68700 1.000 78.35685  ?  97  GLN A O   1 
ATOM   556  C CB  . GLN A 1 97  ? 15.53700 34.20200  -27.18400 1.000 80.95255  ?  97  GLN A CB  1 
ATOM   557  C CG  . GLN A 1 97  ? 14.23400 34.72500  -27.75100 1.000 86.27550  ?  97  GLN A CG  1 
ATOM   558  C CD  . GLN A 1 97  ? 13.37900 33.62700  -28.34500 1.000 95.67338  ?  97  GLN A CD  1 
ATOM   559  O OE1 . GLN A 1 97  ? 13.68900 32.44300  -28.21300 1.000 97.59241  ?  97  GLN A OE1 1 
ATOM   560  N NE2 . GLN A 1 97  ? 12.29700 34.01500  -29.01100 1.000 101.04051 ?  97  GLN A NE2 1 
ATOM   561  N N   . PRO A 1 98  ? 17.65900 34.24000  -24.71800 1.000 71.71924  ?  98  PRO A N   1 
ATOM   562  C CA  . PRO A 1 98  ? 18.90200 33.77200  -24.08700 1.000 71.12051  ?  98  PRO A CA  1 
ATOM   563  C C   . PRO A 1 98  ? 19.48700 32.54200  -24.74700 1.000 71.89268  ?  98  PRO A C   1 
ATOM   564  O O   . PRO A 1 98  ? 20.70100 32.32300  -24.65800 1.000 72.52584  ?  98  PRO A O   1 
ATOM   565  C CB  . PRO A 1 98  ? 18.47300 33.48700  -22.64100 1.000 66.85304  ?  98  PRO A CB  1 
ATOM   566  C CG  . PRO A 1 98  ? 17.25100 34.32300  -22.43800 1.000 66.93263  ?  98  PRO A CG  1 
ATOM   567  C CD  . PRO A 1 98  ? 16.54500 34.30500  -23.75900 1.000 70.66417  ?  98  PRO A CD  1 
ATOM   568  N N   . ILE A 1 99  ? 18.66400 31.73300  -25.41600 1.000 73.26343  ?  99  ILE A N   1 
ATOM   569  C CA  . ILE A 1 99  ? 19.18800 30.54600  -26.08000 1.000 73.07773  ?  99  ILE A CA  1 
ATOM   570  C C   . ILE A 1 99  ? 20.19100 30.93100  -27.16300 1.000 75.56147  ?  99  ILE A C   1 
ATOM   571  O O   . ILE A 1 99  ? 21.10600 30.16000  -27.47500 1.000 74.95064  ?  99  ILE A O   1 
ATOM   572  C CB  . ILE A 1 99  ? 18.02200 29.70400  -26.63600 1.000 68.25144  ?  99  ILE A CB  1 
ATOM   573  C CG1 . ILE A 1 99  ? 18.54100 28.45500  -27.35000 1.000 68.30065  ?  99  ILE A CG1 1 
ATOM   574  C CG2 . ILE A 1 99  ? 17.15600 30.54500  -27.55700 1.000 76.53915  ?  99  ILE A CG2 1 
ATOM   575  N N   . TYR A 1 100 ? 20.06200 32.13200  -27.72900 1.000 74.19109  ?  100 TYR A N   1 
ATOM   576  C CA  . TYR A 1 100 ? 20.97900 32.61700  -28.75500 1.000 77.50342  ?  100 TYR A CA  1 
ATOM   577  C C   . TYR A 1 100 ? 22.10100 33.49000  -28.20400 1.000 78.67346  ?  100 TYR A C   1 
ATOM   578  O O   . TYR A 1 100 ? 22.89400 34.02100  -28.98900 1.000 80.65326  ?  100 TYR A O   1 
ATOM   579  C CB  . TYR A 1 100 ? 20.21500 33.39800  -29.83100 1.000 81.12368  ?  100 TYR A CB  1 
ATOM   580  C CG  . TYR A 1 100 ? 18.90900 32.77200  -30.27200 1.000 81.29020  ?  100 TYR A CG  1 
ATOM   581  C CD1 . TYR A 1 100 ? 18.89300 31.58500  -30.99500 1.000 83.37616  ?  100 TYR A CD1 1 
ATOM   582  C CD2 . TYR A 1 100 ? 17.69100 33.36700  -29.96600 1.000 84.52282  ?  100 TYR A CD2 1 
ATOM   583  C CE1 . TYR A 1 100 ? 17.70100 31.01000  -31.40700 1.000 83.88745  ?  100 TYR A CE1 1 
ATOM   584  C CE2 . TYR A 1 100 ? 16.49100 32.79700  -30.37200 1.000 89.46672  ?  100 TYR A CE2 1 
ATOM   585  C CZ  . TYR A 1 100 ? 16.50300 31.61700  -31.09200 1.000 87.62134  ?  100 TYR A CZ  1 
ATOM   586  O OH  . TYR A 1 100 ? 15.31800 31.04100  -31.50000 1.000 86.08473  ?  100 TYR A OH  1 
ATOM   587  N N   . TRP A 1 101 ? 22.18700 33.66000  -26.88700 1.000 75.41561  ?  101 TRP A N   1 
ATOM   588  C CA  . TRP A 1 101 ? 23.25400 34.46400  -26.30400 1.000 75.54430  ?  101 TRP A CA  1 
ATOM   589  C C   . TRP A 1 101 ? 24.59800 33.77400  -26.50300 1.000 73.61791  ?  101 TRP A C   1 
ATOM   590  O O   . TRP A 1 101 ? 24.77200 32.61900  -26.10100 1.000 76.06174  ?  101 TRP A O   1 
ATOM   591  C CB  . TRP A 1 101 ? 22.99600 34.69000  -24.81800 1.000 74.57564  ?  101 TRP A CB  1 
ATOM   592  C CG  . TRP A 1 101 ? 21.86600 35.61400  -24.52400 1.000 71.73127  ?  101 TRP A CG  1 
ATOM   593  C CD1 . TRP A 1 101 ? 21.04100 36.22100  -25.42400 1.000 73.45131  ?  101 TRP A CD1 1 
ATOM   594  C CD2 . TRP A 1 101 ? 21.42800 36.03200  -23.23100 1.000 68.77589  ?  101 TRP A CD2 1 
ATOM   595  N NE1 . TRP A 1 101 ? 20.11700 36.99600  -24.76800 1.000 73.80936  ?  101 TRP A NE1 1 
ATOM   596  C CE2 . TRP A 1 101 ? 20.33400 36.89600  -23.41900 1.000 70.00127  ?  101 TRP A CE2 1 
ATOM   597  C CE3 . TRP A 1 101 ? 21.85600 35.75700  -21.92900 1.000 68.41737  ?  101 TRP A CE3 1 
ATOM   598  C CZ2 . TRP A 1 101 ? 19.66200 37.48900  -22.35500 1.000 71.87787  ?  101 TRP A CZ2 1 
ATOM   599  C CZ3 . TRP A 1 101 ? 21.18900 36.34600  -20.87400 1.000 66.43137  ?  101 TRP A CZ3 1 
ATOM   600  C CH2 . TRP A 1 101 ? 20.10400 37.20200  -21.09200 1.000 68.07730  ?  101 TRP A CH2 1 
ATOM   601  N N   . SER A 1 102 ? 25.54500 34.47400  -27.12100 1.000 75.29917  ?  102 SER A N   1 
ATOM   602  C CA  . SER A 1 102 ? 26.90000 33.95400  -27.17200 1.000 75.82789  ?  102 SER A CA  1 
ATOM   603  C C   . SER A 1 102 ? 27.56000 34.12200  -25.81100 1.000 74.35993  ?  102 SER A C   1 
ATOM   604  O O   . SER A 1 102 ? 26.99800 34.71500  -24.88700 1.000 77.38204  ?  102 SER A O   1 
ATOM   605  C CB  . SER A 1 102 ? 27.72700 34.67000  -28.23600 1.000 78.31114  ?  102 SER A CB  1 
ATOM   606  O OG  . SER A 1 102 ? 28.01200 36.00000  -27.84200 1.000 78.75154  ?  102 SER A OG  1 
ATOM   607  N N   . ARG A 1 103 ? 28.78300 33.60400  -25.69400 1.000 58.99702  ?  103 ARG A N   1 
ATOM   608  C CA  . ARG A 1 103 ? 29.49000 33.71400  -24.42300 1.000 57.17908  ?  103 ARG A CA  1 
ATOM   609  C C   . ARG A 1 103 ? 29.74900 35.16500  -24.05000 1.000 58.05184  ?  103 ARG A C   1 
ATOM   610  O O   . ARG A 1 103 ? 29.74700 35.51000  -22.86300 1.000 61.69250  ?  103 ARG A O   1 
ATOM   611  C CB  . ARG A 1 103 ? 30.80100 32.93800  -24.47800 1.000 55.38821  ?  103 ARG A CB  1 
ATOM   612  C CG  . ARG A 1 103 ? 31.44100 32.75700  -23.11800 1.000 59.03511  ?  103 ARG A CG  1 
ATOM   613  C CD  . ARG A 1 103 ? 32.46100 31.64400  -23.15300 1.000 58.49973  ?  103 ARG A CD  1 
ATOM   614  N NE  . ARG A 1 103 ? 33.64000 32.00900  -23.92600 1.000 56.07172  ?  103 ARG A NE  1 
ATOM   615  C CZ  . ARG A 1 103 ? 34.64500 31.18300  -24.18300 1.000 57.63654  ?  103 ARG A CZ  1 
ATOM   616  N NH1 . ARG A 1 103 ? 34.63500 29.93000  -23.75800 1.000 55.75740  ?  103 ARG A NH1 1 
ATOM   617  N NH2 . ARG A 1 103 ? 35.68500 31.62500  -24.88500 1.000 58.67198  ?  103 ARG A NH2 1 
ATOM   618  N N   . ASP A 1 104 ? 29.96600 36.02500  -25.04300 1.000 59.21980  ?  104 ASP A N   1 
ATOM   619  C CA  . ASP A 1 104 ? 30.15200 37.44600  -24.77300 1.000 59.18581  ?  104 ASP A CA  1 
ATOM   620  C C   . ASP A 1 104 ? 28.85600 38.08600  -24.29400 1.000 60.99049  ?  104 ASP A C   1 
ATOM   621  O O   . ASP A 1 104 ? 28.86600 38.90800  -23.37200 1.000 66.03612  ?  104 ASP A O   1 
ATOM   622  C CB  . ASP A 1 104 ? 30.66600 38.13600  -26.03300 1.000 61.43124  ?  104 ASP A CB  1 
ATOM   623  C CG  . ASP A 1 104 ? 31.85200 37.41500  -26.64400 1.000 62.45930  ?  104 ASP A CG  1 
ATOM   624  O OD1 . ASP A 1 104 ? 32.48700 36.60900  -25.93100 1.000 63.24076  ?  104 ASP A OD1 1 
ATOM   625  O OD2 . ASP A 1 104 ? 32.11500 37.61500  -27.85000 1.000 61.78005  -1 104 ASP A OD2 1 
ATOM   626  N N   . ASP A 1 105 ? 27.72900 37.71300  -24.90600 1.000 59.52962  ?  105 ASP A N   1 
ATOM   627  C CA  . ASP A 1 105 ? 26.44000 38.26900  -24.50500 1.000 62.30806  ?  105 ASP A CA  1 
ATOM   628  C C   . ASP A 1 105 ? 26.12900 37.95700  -23.04700 1.000 66.71733  ?  105 ASP A C   1 
ATOM   629  O O   . ASP A 1 105 ? 25.57900 38.80000  -22.32800 1.000 71.30414  ?  105 ASP A O   1 
ATOM   630  C CB  . ASP A 1 105 ? 25.33700 37.72800  -25.41100 1.000 64.25714  ?  105 ASP A CB  1 
ATOM   631  C CG  . ASP A 1 105 ? 25.62000 37.97100  -26.87500 1.000 68.59566  ?  105 ASP A CG  1 
ATOM   632  O OD1 . ASP A 1 105 ? 26.60300 38.67700  -27.18000 1.000 71.99459  ?  105 ASP A OD1 1 
ATOM   633  O OD2 . ASP A 1 105 ? 24.86300 37.45400  -27.72300 1.000 71.81439  -1 105 ASP A OD2 1 
ATOM   634  N N   . VAL A 1 106 ? 26.46900 36.74900  -22.59500 1.000 67.00477  ?  106 VAL A N   1 
ATOM   635  C CA  . VAL A 1 106 ? 26.24400 36.39100  -21.19800 1.000 64.23065  ?  106 VAL A CA  1 
ATOM   636  C C   . VAL A 1 106 ? 27.04300 37.30800  -20.28300 1.000 66.60833  ?  106 VAL A C   1 
ATOM   637  O O   . VAL A 1 106 ? 26.56600 37.71500  -19.21700 1.000 68.44781  ?  106 VAL A O   1 
ATOM   638  C CB  . VAL A 1 106 ? 26.59200 34.90900  -20.96300 1.000 60.28928  ?  106 VAL A CB  1 
ATOM   639  C CG1 . VAL A 1 106 ? 26.33900 34.52400  -19.51400 1.000 62.60792  ?  106 VAL A CG1 1 
ATOM   640  C CG2 . VAL A 1 106 ? 25.78700 34.02300  -21.90000 1.000 62.72941  ?  106 VAL A CG2 1 
ATOM   641  N N   . ALA A 1 107 ? 28.26400 37.66400  -20.69300 1.000 70.27358  ?  107 ALA A N   1 
ATOM   642  C CA  . ALA A 1 107 ? 29.09900 38.53500  -19.87300 1.000 66.98954  ?  107 ALA A CA  1 
ATOM   643  C C   . ALA A 1 107 ? 28.47600 39.91700  -19.72100 1.000 71.78827  ?  107 ALA A C   1 
ATOM   644  O O   . ALA A 1 107 ? 28.48700 40.49100  -18.62600 1.000 72.42327  ?  107 ALA A O   1 
ATOM   645  C CB  . ALA A 1 107 ? 30.49900 38.64000  -20.47400 1.000 62.37735  ?  107 ALA A CB  1 
ATOM   646  N N   . GLN A 1 108 ? 27.93100 40.46800  -20.80900 1.000 72.47157  ?  108 GLN A N   1 
ATOM   647  C CA  . GLN A 1 108 ? 27.25600 41.75700  -20.71800 1.000 74.36063  ?  108 GLN A CA  1 
ATOM   648  C C   . GLN A 1 108 ? 26.02600 41.66700  -19.82900 1.000 74.58534  ?  108 GLN A C   1 
ATOM   649  O O   . GLN A 1 108 ? 25.73700 42.59100  -19.05900 1.000 75.96231  ?  108 GLN A O   1 
ATOM   650  C CB  . GLN A 1 108 ? 26.86600 42.26000  -22.11100 1.000 77.21384  ?  108 GLN A CB  1 
ATOM   651  C CG  . GLN A 1 108 ? 27.82500 41.88200  -23.22900 1.000 80.26665  ?  108 GLN A CG  1 
ATOM   652  C CD  . GLN A 1 108 ? 29.21400 42.46300  -23.04100 1.000 86.35713  ?  108 GLN A CD  1 
ATOM   653  O OE1 . GLN A 1 108 ? 29.40000 43.45000  -22.33100 1.000 89.37466  ?  108 GLN A OE1 1 
ATOM   654  N NE2 . GLN A 1 108 ? 30.20100 41.84800  -23.68600 1.000 83.55439  ?  108 GLN A NE2 1 
ATOM   655  N N   . TRP A 1 109 ? 25.29000 40.55800  -19.92100 1.000 66.09597  ?  109 TRP A N   1 
ATOM   656  C CA  . TRP A 1 109 ? 24.11900 40.37300  -19.07100 1.000 66.37515  ?  109 TRP A CA  1 
ATOM   657  C C   . TRP A 1 109 ? 24.51800 40.34600  -17.60200 1.000 66.81556  ?  109 TRP A C   1 
ATOM   658  O O   . TRP A 1 109 ? 23.84600 40.94600  -16.75500 1.000 66.43406  ?  109 TRP A O   1 
ATOM   659  C CB  . TRP A 1 109 ? 23.38300 39.09100  -19.47300 1.000 63.76232  ?  109 TRP A CB  1 
ATOM   660  C CG  . TRP A 1 109 ? 22.38700 38.58300  -18.46300 1.000 60.22662  ?  109 TRP A CG  1 
ATOM   661  C CD1 . TRP A 1 109 ? 21.17600 39.13700  -18.15500 1.000 56.64498  ?  109 TRP A CD1 1 
ATOM   662  C CD2 . TRP A 1 109 ? 22.51100 37.41300  -17.64300 1.000 59.51540  ?  109 TRP A CD2 1 
ATOM   663  N NE1 . TRP A 1 109 ? 20.54400 38.38800  -17.19100 1.000 57.63332  ?  109 TRP A NE1 1 
ATOM   664  C CE2 . TRP A 1 109 ? 21.34200 37.32600  -16.85900 1.000 59.02921  ?  109 TRP A CE2 1 
ATOM   665  C CE3 . TRP A 1 109 ? 23.49800 36.43300  -17.49100 1.000 58.19624  ?  109 TRP A CE3 1 
ATOM   666  C CZ2 . TRP A 1 109 ? 21.13400 36.30100  -15.93900 1.000 56.36724  ?  109 TRP A CZ2 1 
ATOM   667  C CZ3 . TRP A 1 109 ? 23.28800 35.41600  -16.57700 1.000 56.21533  ?  109 TRP A CZ3 1 
ATOM   668  C CH2 . TRP A 1 109 ? 22.11700 35.35800  -15.81400 1.000 55.20864  ?  109 TRP A CH2 1 
ATOM   669  N N   . LEU A 1 110 ? 25.63000 39.67500  -17.28400 1.000 65.21272  ?  110 LEU A N   1 
ATOM   670  C CA  . LEU A 1 110 ? 26.13000 39.68100  -15.91400 1.000 65.94394  ?  110 LEU A CA  1 
ATOM   671  C C   . LEU A 1 110 ? 26.54700 41.08200  -15.49100 1.000 67.86819  ?  110 LEU A C   1 
ATOM   672  O O   . LEU A 1 110 ? 26.20500 41.53700  -14.39300 1.000 68.89149  ?  110 LEU A O   1 
ATOM   673  C CB  . LEU A 1 110 ? 27.30600 38.71500  -15.77900 1.000 63.50514  ?  110 LEU A CB  1 
ATOM   674  C CG  . LEU A 1 110 ? 27.00000 37.23800  -16.01900 1.000 61.23757  ?  110 LEU A CG  1 
ATOM   675  C CD1 . LEU A 1 110 ? 28.28500 36.43000  -16.11700 1.000 64.64864  ?  110 LEU A CD1 1 
ATOM   676  C CD2 . LEU A 1 110 ? 26.10500 36.69800  -14.92100 1.000 62.43538  ?  110 LEU A CD2 1 
ATOM   677  N N   . LYS A 1 111 ? 27.28700 41.78100  -16.35300 1.000 66.81248  ?  111 LYS A N   1 
ATOM   678  C CA  . LYS A 1 111 ? 27.72900 43.12700  -16.01300 1.000 67.28639  ?  111 LYS A CA  1 
ATOM   679  C C   . LYS A 1 111 ? 26.55200 44.09200  -15.94400 1.000 71.01021  ?  111 LYS A C   1 
ATOM   680  O O   . LYS A 1 111 ? 26.53700 44.99600  -15.10100 1.000 75.32757  ?  111 LYS A O   1 
ATOM   681  C CB  . LYS A 1 111 ? 28.77100 43.60500  -17.02300 1.000 67.69900  ?  111 LYS A CB  1 
ATOM   682  N N   . TRP A 1 112 ? 25.54800 43.90900  -16.80700 1.000 67.57440  ?  112 TRP A N   1 
ATOM   683  C CA  . TRP A 1 112 ? 24.40600 44.82000  -16.80300 1.000 70.60891  ?  112 TRP A CA  1 
ATOM   684  C C   . TRP A 1 112 ? 23.55900 44.63200  -15.55000 1.000 73.75282  ?  112 TRP A C   1 
ATOM   685  O O   . TRP A 1 112 ? 23.26400 45.60000  -14.83800 1.000 76.42411  ?  112 TRP A O   1 
ATOM   686  C CB  . TRP A 1 112 ? 23.55300 44.61900  -18.05500 1.000 69.73900  ?  112 TRP A CB  1 
ATOM   687  C CG  . TRP A 1 112 ? 22.20700 45.28200  -17.97300 1.000 71.50606  ?  112 TRP A CG  1 
ATOM   688  C CD1 . TRP A 1 112 ? 21.92400 46.59900  -18.20500 1.000 77.67486  ?  112 TRP A CD1 1 
ATOM   689  C CD2 . TRP A 1 112 ? 20.96300 44.66300  -17.62600 1.000 68.57621  ?  112 TRP A CD2 1 
ATOM   690  N NE1 . TRP A 1 112 ? 20.58200 46.83400  -18.03200 1.000 78.64790  ?  112 TRP A NE1 1 
ATOM   691  C CE2 . TRP A 1 112 ? 19.97000 45.66100  -17.67400 1.000 73.14043  ?  112 TRP A CE2 1 
ATOM   692  C CE3 . TRP A 1 112 ? 20.59300 43.36200  -17.28100 1.000 68.80481  ?  112 TRP A CE3 1 
ATOM   693  C CZ2 . TRP A 1 112 ? 18.63300 45.39700  -17.39100 1.000 72.77918  ?  112 TRP A CZ2 1 
ATOM   694  C CZ3 . TRP A 1 112 ? 19.26500 43.10300  -17.00100 1.000 69.31676  ?  112 TRP A CZ3 1 
ATOM   695  C CH2 . TRP A 1 112 ? 18.30200 44.11500  -17.05700 1.000 70.40710  ?  112 TRP A CH2 1 
ATOM   696  N N   . ALA A 1 113 ? 23.15200 43.39000  -15.26900 1.000 73.17650  ?  113 ALA A N   1 
ATOM   697  C CA  . ALA A 1 113 ? 22.37700 43.12700  -14.06000 1.000 70.39928  ?  113 ALA A CA  1 
ATOM   698  C C   . ALA A 1 113 ? 23.13000 43.56300  -12.81500 1.000 70.81205  ?  113 ALA A C   1 
ATOM   699  O O   . ALA A 1 113 ? 22.51100 43.95000  -11.81800 1.000 73.52709  ?  113 ALA A O   1 
ATOM   700  C CB  . ALA A 1 113 ? 22.02200 41.64500  -13.96800 1.000 62.88916  ?  113 ALA A CB  1 
ATOM   701  N N   . GLU A 1 114 ? 24.46000 43.50900  -12.85600 1.000 70.39012  ?  114 GLU A N   1 
ATOM   702  C CA  . GLU A 1 114 ? 25.25700 44.01000  -11.74500 1.000 72.20711  ?  114 GLU A CA  1 
ATOM   703  C C   . GLU A 1 114 ? 24.97000 45.48400  -11.49300 1.000 73.67580  ?  114 GLU A C   1 
ATOM   704  O O   . GLU A 1 114 ? 24.69800 45.89100  -10.35800 1.000 77.24328  ?  114 GLU A O   1 
ATOM   705  C CB  . GLU A 1 114 ? 26.73800 43.77500  -12.03100 1.000 69.96566  ?  114 GLU A CB  1 
ATOM   706  C CG  . GLU A 1 114 ? 27.67900 44.45300  -11.06700 1.000 72.74493  ?  114 GLU A CG  1 
ATOM   707  C CD  . GLU A 1 114 ? 29.12600 44.20400  -11.42300 1.000 75.92761  ?  114 GLU A CD  1 
ATOM   708  O OE1 . GLU A 1 114 ? 29.40500 43.18300  -12.08500 1.000 76.60988  ?  114 GLU A OE1 1 
ATOM   709  O OE2 . GLU A 1 114 ? 29.98100 45.03800  -11.06300 1.000 80.06102  -1 114 GLU A OE2 1 
ATOM   710  N N   . ASN A 1 115 ? 25.00900 46.30000  -12.54600 1.000 75.84692  ?  115 ASN A N   1 
ATOM   711  C CA  . ASN A 1 115 ? 24.67000 47.71000  -12.39300 1.000 81.25585  ?  115 ASN A CA  1 
ATOM   712  C C   . ASN A 1 115 ? 23.16900 47.91900  -12.25800 1.000 82.03666  ?  115 ASN A C   1 
ATOM   713  O O   . ASN A 1 115 ? 22.73500 48.91500  -11.66700 1.000 85.72238  ?  115 ASN A O   1 
ATOM   714  C CB  . ASN A 1 115 ? 25.20600 48.51500  -13.57800 1.000 78.22482  ?  115 ASN A CB  1 
ATOM   715  N N   . GLU A 1 116 ? 22.36700 46.99500  -12.79100 1.000 76.79444  ?  116 GLU A N   1 
ATOM   716  C CA  . GLU A 1 116 ? 20.91900 47.15000  -12.72500 1.000 77.32256  ?  116 GLU A CA  1 
ATOM   717  C C   . GLU A 1 116 ? 20.40100 46.90400  -11.31600 1.000 78.88127  ?  116 GLU A C   1 
ATOM   718  O O   . GLU A 1 116 ? 19.48700 47.59700  -10.85300 1.000 79.00187  ?  116 GLU A O   1 
ATOM   719  C CB  . GLU A 1 116 ? 20.24500 46.19900  -13.71400 1.000 74.03784  ?  116 GLU A CB  1 
ATOM   720  C CG  . GLU A 1 116 ? 18.72600 46.28300  -13.73300 1.000 74.38038  ?  116 GLU A CG  1 
ATOM   721  C CD  . GLU A 1 116 ? 18.21800 47.53200  -14.43300 1.000 80.49786  ?  116 GLU A CD  1 
ATOM   722  O OE1 . GLU A 1 116 ? 19.03200 48.24200  -15.06100 1.000 81.51729  ?  116 GLU A OE1 1 
ATOM   723  O OE2 . GLU A 1 116 ? 16.99900 47.79800  -14.36500 1.000 82.95304  -1 116 GLU A OE2 1 
ATOM   724  N N   . PHE A 1 117 ? 20.97100 45.92600  -10.61600 1.000 79.52074  ?  117 PHE A N   1 
ATOM   725  C CA  . PHE A 1 117 ? 20.50900 45.55500  -9.28700  1.000 77.79775  ?  117 PHE A CA  1 
ATOM   726  C C   . PHE A 1 117 ? 21.51900 45.89100  -8.19800  1.000 80.77718  ?  117 PHE A C   1 
ATOM   727  O O   . PHE A 1 117 ? 21.31000 45.51200  -7.04100  1.000 80.53717  ?  117 PHE A O   1 
ATOM   728  C CB  . PHE A 1 117 ? 20.16300 44.06500  -9.25300  1.000 71.09046  ?  117 PHE A CB  1 
ATOM   729  C CG  . PHE A 1 117 ? 19.10600 43.67200  -10.24300 1.000 68.77306  ?  117 PHE A CG  1 
ATOM   730  C CD1 . PHE A 1 117 ? 17.76200 43.82600  -9.94300  1.000 66.34001  ?  117 PHE A CD1 1 
ATOM   731  C CD2 . PHE A 1 117 ? 19.45800 43.16800  -11.48400 1.000 69.13472  ?  117 PHE A CD2 1 
ATOM   732  C CE1 . PHE A 1 117 ? 16.78900 43.47100  -10.85700 1.000 65.99582  ?  117 PHE A CE1 1 
ATOM   733  C CE2 . PHE A 1 117 ? 18.48900 42.81200  -12.40400 1.000 67.25264  ?  117 PHE A CE2 1 
ATOM   734  C CZ  . PHE A 1 117 ? 17.15400 42.96300  -12.09100 1.000 65.98015  ?  117 PHE A CZ  1 
ATOM   735  N N   . SER A 1 118 ? 22.59600 46.60000  -8.53300  1.000 98.18679  ?  118 SER A N   1 
ATOM   736  C CA  . SER A 1 118 ? 23.60800 47.00800  -7.55900  1.000 99.25704  ?  118 SER A CA  1 
ATOM   737  C C   . SER A 1 118 ? 24.12400 45.80600  -6.76700  1.000 99.16902  ?  118 SER A C   1 
ATOM   738  O O   . SER A 1 118 ? 24.09500 45.77500  -5.53600  1.000 99.69856  ?  118 SER A O   1 
ATOM   739  C CB  . SER A 1 118 ? 23.06400 48.09700  -6.62900  1.000 99.88064  ?  118 SER A CB  1 
ATOM   740  O OG  . SER A 1 118 ? 21.96800 47.63300  -5.85600  1.000 99.31927  ?  118 SER A OG  1 
ATOM   741  N N   . LEU A 1 119 ? 24.59500 44.79800  -7.49400  1.000 80.49212  ?  119 LEU A N   1 
ATOM   742  C CA  . LEU A 1 119 ? 25.06400 43.55900  -6.89700  1.000 78.02605  ?  119 LEU A CA  1 
ATOM   743  C C   . LEU A 1 119 ? 26.57800 43.60200  -6.69600  1.000 78.03176  ?  119 LEU A C   1 
ATOM   744  O O   . LEU A 1 119 ? 27.25600 44.55600  -7.08400  1.000 75.41478  ?  119 LEU A O   1 
ATOM   745  C CB  . LEU A 1 119 ? 24.66500 42.36500  -7.76100  1.000 71.87597  ?  119 LEU A CB  1 
ATOM   746  C CG  . LEU A 1 119 ? 23.18900 42.28100  -8.15100  1.000 71.23883  ?  119 LEU A CG  1 
ATOM   747  C CD1 . LEU A 1 119 ? 22.98500 41.19700  -9.18800  1.000 65.94674  ?  119 LEU A CD1 1 
ATOM   748  C CD2 . LEU A 1 119 ? 22.34100 41.99300  -6.92300  1.000 75.14212  ?  119 LEU A CD2 1 
ATOM   749  N N   . ARG A 1 120 ? 27.10600 42.55300  -6.06700  1.000 80.48064  ?  120 ARG A N   1 
ATOM   750  C CA  . ARG A 1 120 ? 28.54600 42.40000  -5.95700  1.000 77.53921  ?  120 ARG A CA  1 
ATOM   751  C C   . ARG A 1 120 ? 29.14900 42.20400  -7.34600  1.000 79.71486  ?  120 ARG A C   1 
ATOM   752  O O   . ARG A 1 120 ? 28.50300 41.64500  -8.23700  1.000 79.14898  ?  120 ARG A O   1 
ATOM   753  C CB  . ARG A 1 120 ? 28.90000 41.21500  -5.06500  1.000 84.24656  ?  120 ARG A CB  1 
ATOM   754  N N   . PRO A 1 121 ? 30.38700 42.65500  -7.55600  1.000 78.30704  ?  121 PRO A N   1 
ATOM   755  C CA  . PRO A 1 121 ? 30.97000 42.63100  -8.90700  1.000 77.11492  ?  121 PRO A CA  1 
ATOM   756  C C   . PRO A 1 121 ? 31.17500 41.22600  -9.45200  1.000 75.35845  ?  121 PRO A C   1 
ATOM   757  O O   . PRO A 1 121 ? 32.09000 40.50800  -9.03700  1.000 74.47786  ?  121 PRO A O   1 
ATOM   758  C CB  . PRO A 1 121 ? 32.30900 43.35900  -8.72400  1.000 81.72072  ?  121 PRO A CB  1 
ATOM   759  C CG  . PRO A 1 121 ? 32.17300 44.11400  -7.42900  1.000 84.95111  ?  121 PRO A CG  1 
ATOM   760  C CD  . PRO A 1 121 ? 31.28800 43.27500  -6.57200  1.000 83.14597  ?  121 PRO A CD  1 
ATOM   761  N N   . ILE A 1 122 ? 30.32700 40.83400  -10.39600 1.000 73.64545  ?  122 ILE A N   1 
ATOM   762  C CA  . ILE A 1 122 ? 30.40100 39.50400  -10.98700 1.000 74.56152  ?  122 ILE A CA  1 
ATOM   763  C C   . ILE A 1 122 ? 31.54200 39.45900  -11.99200 1.000 75.19924  ?  122 ILE A C   1 
ATOM   764  O O   . ILE A 1 122 ? 31.60500 40.27500  -12.91900 1.000 72.83035  ?  122 ILE A O   1 
ATOM   765  C CB  . ILE A 1 122 ? 29.06500 39.13100  -11.64800 1.000 72.89908  ?  122 ILE A CB  1 
ATOM   766  C CG1 . ILE A 1 122 ? 27.94800 39.10300  -10.60400 1.000 73.09489  ?  122 ILE A CG1 1 
ATOM   767  C CG2 . ILE A 1 122 ? 29.18000 37.79400  -12.36900 1.000 71.98676  ?  122 ILE A CG2 1 
ATOM   768  N N   . ASP A 1 123 ? 32.45200 38.50900  -11.80300 1.000 76.73564  ?  123 ASP A N   1 
ATOM   769  C CA  . ASP A 1 123 ? 33.51100 38.28300  -12.77100 1.000 75.47183  ?  123 ASP A CA  1 
ATOM   770  C C   . ASP A 1 123 ? 32.95300 37.64100  -14.03400 1.000 76.29230  ?  123 ASP A C   1 
ATOM   771  O O   . ASP A 1 123 ? 32.02500 36.82900  -13.99100 1.000 73.04093  ?  123 ASP A O   1 
ATOM   772  C CB  . ASP A 1 123 ? 34.59800 37.39100  -12.17700 1.000 73.36559  ?  123 ASP A CB  1 
ATOM   773  C CG  . ASP A 1 123 ? 35.75300 37.16300  -13.13100 1.000 76.81442  ?  123 ASP A CG  1 
ATOM   774  O OD1 . ASP A 1 123 ? 35.87300 37.91100  -14.12700 1.000 81.60173  ?  123 ASP A OD1 1 
ATOM   775  O OD2 . ASP A 1 123 ? 36.54400 36.23200  -12.88100 1.000 77.03485  -1 123 ASP A OD2 1 
ATOM   776  N N   . SER A 1 124 ? 33.53300 38.02000  -15.17500 1.000 82.66899  ?  124 SER A N   1 
ATOM   777  C CA  . SER A 1 124 ? 33.11900 37.42400  -16.43800 1.000 77.60808  ?  124 SER A CA  1 
ATOM   778  C C   . SER A 1 124 ? 33.36400 35.92000  -16.44400 1.000 75.90852  ?  124 SER A C   1 
ATOM   779  O O   . SER A 1 124 ? 32.61800 35.17100  -17.08600 1.000 73.23279  ?  124 SER A O   1 
ATOM   780  C CB  . SER A 1 124 ? 33.84500 38.09800  -17.60100 1.000 75.09314  ?  124 SER A CB  1 
ATOM   781  N N   . ASN A 1 125 ? 34.38400 35.45900  -15.71700 1.000 71.55320  ?  125 ASN A N   1 
ATOM   782  C CA  . ASN A 1 125 ? 34.68200 34.03400  -15.63000 1.000 71.18033  ?  125 ASN A CA  1 
ATOM   783  C C   . ASN A 1 125 ? 33.61700 33.25100  -14.87600 1.000 69.37519  ?  125 ASN A C   1 
ATOM   784  O O   . ASN A 1 125 ? 33.67300 32.01600  -14.87000 1.000 67.01626  ?  125 ASN A O   1 
ATOM   785  C CB  . ASN A 1 125 ? 36.04200 33.82300  -14.96200 1.000 71.06439  ?  125 ASN A CB  1 
ATOM   786  N N   . THR A 1 126 ? 32.65400 33.93100  -14.25100 1.000 69.24238  ?  126 THR A N   1 
ATOM   787  C CA  . THR A 1 126 ? 31.64100 33.23400  -13.46700 1.000 67.58633  ?  126 THR A CA  1 
ATOM   788  C C   . THR A 1 126 ? 30.78400 32.32900  -14.34100 1.000 63.50501  ?  126 THR A C   1 
ATOM   789  O O   . THR A 1 126 ? 30.43800 31.21200  -13.94100 1.000 62.34319  ?  126 THR A O   1 
ATOM   790  C CB  . THR A 1 126 ? 30.77700 34.25200  -12.72800 1.000 67.89572  ?  126 THR A CB  1 
ATOM   791  O OG1 . THR A 1 126 ? 31.62200 35.11500  -11.95800 1.000 68.30590  ?  126 THR A OG1 1 
ATOM   792  C CG2 . THR A 1 126 ? 29.79600 33.55400  -11.81100 1.000 66.44856  ?  126 THR A CG2 1 
ATOM   793  N N   . PHE A 1 127 ? 30.43700 32.78600  -15.54100 1.000 62.16269  ?  127 PHE A N   1 
ATOM   794  C CA  . PHE A 1 127 ? 29.62300 32.01200  -16.47800 1.000 60.26912  ?  127 PHE A CA  1 
ATOM   795  C C   . PHE A 1 127 ? 30.35600 31.98800  -17.81500 1.000 62.01612  ?  127 PHE A C   1 
ATOM   796  O O   . PHE A 1 127 ? 30.08200 32.79000  -18.71000 1.000 61.07521  ?  127 PHE A O   1 
ATOM   797  C CB  . PHE A 1 127 ? 28.22600 32.60000  -16.59700 1.000 59.24506  ?  127 PHE A CB  1 
ATOM   798  C CG  . PHE A 1 127 ? 27.39700 32.43800  -15.35800 1.000 59.71384  ?  127 PHE A CG  1 
ATOM   799  C CD1 . PHE A 1 127 ? 26.67700 31.27600  -15.14200 1.000 59.55007  ?  127 PHE A CD1 1 
ATOM   800  C CD2 . PHE A 1 127 ? 27.34500 33.44000  -14.40500 1.000 60.27889  ?  127 PHE A CD2 1 
ATOM   801  C CE1 . PHE A 1 127 ? 25.90900 31.12200  -14.00500 1.000 63.53945  ?  127 PHE A CE1 1 
ATOM   802  C CE2 . PHE A 1 127 ? 26.58200 33.29200  -13.26500 1.000 60.56567  ?  127 PHE A CE2 1 
ATOM   803  C CZ  . PHE A 1 127 ? 25.86300 32.13100  -13.06300 1.000 65.80232  ?  127 PHE A CZ  1 
ATOM   804  N N   . GLU A 1 128 ? 31.29900 31.05500  -17.94400 1.000 60.01132  ?  128 GLU A N   1 
ATOM   805  C CA  . GLU A 1 128 ? 32.07600 30.89500  -19.17200 1.000 57.00751  ?  128 GLU A CA  1 
ATOM   806  C C   . GLU A 1 128 ? 31.38100 29.86800  -20.05800 1.000 55.19017  ?  128 GLU A C   1 
ATOM   807  O O   . GLU A 1 128 ? 31.80100 28.71600  -20.18200 1.000 54.55654  ?  128 GLU A O   1 
ATOM   808  C CB  . GLU A 1 128 ? 33.50000 30.47700  -18.84500 1.000 56.16032  ?  128 GLU A CB  1 
ATOM   809  C CG  . GLU A 1 128 ? 34.31200 31.54600  -18.16400 1.000 61.63595  ?  128 GLU A CG  1 
ATOM   810  C CD  . GLU A 1 128 ? 35.50200 30.97500  -17.43100 1.000 64.95850  ?  128 GLU A CD  1 
ATOM   811  O OE1 . GLU A 1 128 ? 35.45900 29.77900  -17.07600 1.000 64.58693  ?  128 GLU A OE1 1 
ATOM   812  O OE2 . GLU A 1 128 ? 36.48000 31.72000  -17.20800 1.000 66.45492  -1 128 GLU A OE2 1 
ATOM   813  N N   . MET A 1 129 ? 30.30100 30.30800  -20.69900 1.000 53.61340  ?  129 MET A N   1 
ATOM   814  C CA  . MET A 1 129 ? 29.46600 29.40500  -21.48000 1.000 52.83446  ?  129 MET A CA  1 
ATOM   815  C C   . MET A 1 129 ? 28.57700 30.22700  -22.40400 1.000 52.87499  ?  129 MET A C   1 
ATOM   816  O O   . MET A 1 129 ? 28.43600 31.44100  -22.24200 1.000 57.42440  ?  129 MET A O   1 
ATOM   817  C CB  . MET A 1 129 ? 28.62300 28.51600  -20.56300 1.000 55.83937  ?  129 MET A CB  1 
ATOM   818  C CG  . MET A 1 129 ? 27.54800 29.27200  -19.79500 1.000 54.31517  ?  129 MET A CG  1 
ATOM   819  S SD  . MET A 1 129 ? 26.93900 28.36100  -18.36900 1.000 50.49673  ?  129 MET A SD  1 
ATOM   820  C CE  . MET A 1 129 ? 28.42000 28.32300  -17.36500 1.000 53.93282  ?  129 MET A CE  1 
ATOM   821  N N   . ASN A 1 130 ? 27.96900 29.54800  -23.37400 1.000 50.97062  ?  130 ASN A N   1 
ATOM   822  C CA  . ASN A 1 130 ? 27.00300 30.19700  -24.24600 1.000 52.61462  ?  130 ASN A CA  1 
ATOM   823  C C   . ASN A 1 130 ? 25.66900 30.36600  -23.52100 1.000 53.45526  ?  130 ASN A C   1 
ATOM   824  O O   . ASN A 1 130 ? 25.51900 30.02100  -22.34700 1.000 57.37719  ?  130 ASN A O   1 
ATOM   825  C CB  . ASN A 1 130 ? 26.82600 29.39800  -25.53300 1.000 54.85435  ?  130 ASN A CB  1 
ATOM   826  C CG  . ASN A 1 130 ? 26.03200 28.12800  -25.32100 1.000 59.37377  ?  130 ASN A CG  1 
ATOM   827  O OD1 . ASN A 1 130 ? 26.02800 27.56200  -24.22900 1.000 61.90771  ?  130 ASN A OD1 1 
ATOM   828  N ND2 . ASN A 1 130 ? 25.34600 27.67500  -26.36300 1.000 60.91152  ?  130 ASN A ND2 1 
ATOM   829  N N   . GLY A 1 131 ? 24.67400 30.89100  -24.23800 1.000 55.90709  ?  131 GLY A N   1 
ATOM   830  C CA  . GLY A 1 131 ? 23.35800 31.07000  -23.65000 1.000 57.40858  ?  131 GLY A CA  1 
ATOM   831  C C   . GLY A 1 131 ? 22.62100 29.77300  -23.38100 1.000 56.36067  ?  131 GLY A C   1 
ATOM   832  O O   . GLY A 1 131 ? 21.86800 29.67900  -22.40700 1.000 56.22214  ?  131 GLY A O   1 
ATOM   833  N N   . LYS A 1 132 ? 22.81900 28.75800  -24.22500 1.000 62.46654  ?  132 LYS A N   1 
ATOM   834  C CA  . LYS A 1 132 ? 22.14800 27.48200  -23.99900 1.000 62.08160  ?  132 LYS A CA  1 
ATOM   835  C C   . LYS A 1 132 ? 22.63700 26.82800  -22.71300 1.000 62.73528  ?  132 LYS A C   1 
ATOM   836  O O   . LYS A 1 132 ? 21.83500 26.34700  -21.90500 1.000 63.55880  ?  132 LYS A O   1 
ATOM   837  C CB  . LYS A 1 132 ? 22.36200 26.55300  -25.19400 1.000 62.51018  ?  132 LYS A CB  1 
ATOM   838  N N   . ALA A 1 133 ? 23.95600 26.80500  -22.50200 1.000 54.76296  ?  133 ALA A N   1 
ATOM   839  C CA  . ALA A 1 133 ? 24.49500 26.19900  -21.28800 1.000 51.10395  ?  133 ALA A CA  1 
ATOM   840  C C   . ALA A 1 133 ? 24.00100 26.92300  -20.04600 1.000 51.92406  ?  133 ALA A C   1 
ATOM   841  O O   . ALA A 1 133 ? 23.73600 26.29500  -19.01400 1.000 56.04586  ?  133 ALA A O   1 
ATOM   842  C CB  . ALA A 1 133 ? 26.02100 26.19700  -21.33200 1.000 49.29411  ?  133 ALA A CB  1 
ATOM   843  N N   . LEU A 1 134 ? 23.87100 28.24800  -20.12500 1.000 49.64145  ?  134 LEU A N   1 
ATOM   844  C CA  . LEU A 1 134 ? 23.32000 29.00000  -19.00600 1.000 47.90003  ?  134 LEU A CA  1 
ATOM   845  C C   . LEU A 1 134 ? 21.93200 28.49200  -18.64400 1.000 49.98457  ?  134 LEU A C   1 
ATOM   846  O O   . LEU A 1 134 ? 21.56600 28.44000  -17.46300 1.000 57.10037  ?  134 LEU A O   1 
ATOM   847  C CB  . LEU A 1 134 ? 23.27400 30.48600  -19.35400 1.000 47.12589  ?  134 LEU A CB  1 
ATOM   848  C CG  . LEU A 1 134 ? 22.77600 31.43500  -18.27000 1.000 48.03770  ?  134 LEU A CG  1 
ATOM   849  C CD1 . LEU A 1 134 ? 23.84300 31.60500  -17.19900 1.000 56.19090  ?  134 LEU A CD1 1 
ATOM   850  C CD2 . LEU A 1 134 ? 22.38100 32.76700  -18.87900 1.000 49.99717  ?  134 LEU A CD2 1 
ATOM   851  N N   . LEU A 1 135 ? 21.14700 28.09600  -19.64700 1.000 45.26117  ?  135 LEU A N   1 
ATOM   852  C CA  . LEU A 1 135 ? 19.81700 27.57500  -19.36400 1.000 45.34970  ?  135 LEU A CA  1 
ATOM   853  C C   . LEU A 1 135 ? 19.87800 26.18800  -18.74300 1.000 52.25206  ?  135 LEU A C   1 
ATOM   854  O O   . LEU A 1 135 ? 18.98300 25.81600  -17.97600 1.000 56.96047  ?  135 LEU A O   1 
ATOM   855  C CB  . LEU A 1 135 ? 18.97800 27.55100  -20.63900 1.000 45.82911  ?  135 LEU A CB  1 
ATOM   856  C CG  . LEU A 1 135 ? 18.92500 28.86200  -21.42300 1.000 47.90217  ?  135 LEU A CG  1 
ATOM   857  C CD1 . LEU A 1 135 ? 18.15400 28.69400  -22.72000 1.000 55.04861  ?  135 LEU A CD1 1 
ATOM   858  C CD2 . LEU A 1 135 ? 18.30300 29.94700  -20.57600 1.000 48.78837  ?  135 LEU A CD2 1 
ATOM   859  N N   . LEU A 1 136 ? 20.92000 25.41300  -19.05400 1.000 46.06522  ?  136 LEU A N   1 
ATOM   860  C CA  . LEU A 1 136 ? 21.02000 24.07100  -18.49300 1.000 47.75248  ?  136 LEU A CA  1 
ATOM   861  C C   . LEU A 1 136 ? 21.28500 24.10000  -16.99500 1.000 49.70837  ?  136 LEU A C   1 
ATOM   862  O O   . LEU A 1 136 ? 20.82200 23.21200  -16.27000 1.000 50.83067  ?  136 LEU A O   1 
ATOM   863  C CB  . LEU A 1 136 ? 22.12200 23.27300  -19.19100 1.000 46.43665  ?  136 LEU A CB  1 
ATOM   864  C CG  . LEU A 1 136 ? 22.00200 23.04200  -20.69400 1.000 49.03014  ?  136 LEU A CG  1 
ATOM   865  C CD1 . LEU A 1 136 ? 23.13900 22.15100  -21.17100 1.000 47.24090  ?  136 LEU A CD1 1 
ATOM   866  C CD2 . LEU A 1 136 ? 20.65000 22.44500  -21.04400 1.000 50.06210  ?  136 LEU A CD2 1 
ATOM   867  N N   . LEU A 1 137 ? 22.02500 25.09700  -16.51500 1.000 47.73704  ?  137 LEU A N   1 
ATOM   868  C CA  . LEU A 1 137 ? 22.38700 25.13800  -15.10600 1.000 52.35336  ?  137 LEU A CA  1 
ATOM   869  C C   . LEU A 1 137 ? 21.15300 25.27500  -14.22600 1.000 55.22080  ?  137 LEU A C   1 
ATOM   870  O O   . LEU A 1 137 ? 20.21100 26.00200  -14.55200 1.000 56.37909  ?  137 LEU A O   1 
ATOM   871  C CB  . LEU A 1 137 ? 23.34600 26.29500  -14.83300 1.000 52.76559  ?  137 LEU A CB  1 
ATOM   872  C CG  . LEU A 1 137 ? 24.70200 26.22700  -15.52300 1.000 53.90782  ?  137 LEU A CG  1 
ATOM   873  C CD1 . LEU A 1 137 ? 25.61200 27.32900  -15.00800 1.000 53.78353  ?  137 LEU A CD1 1 
ATOM   874  C CD2 . LEU A 1 137 ? 25.31100 24.86000  -15.27900 1.000 55.48948  ?  137 LEU A CD2 1 
ATOM   875  N N   . THR A 1 138 ? 21.16400 24.56200  -13.10600 1.000 56.62084  ?  138 THR A N   1 
ATOM   876  C CA  . THR A 1 138 ? 20.12100 24.69300  -12.10500 1.000 54.09322  ?  138 THR A CA  1 
ATOM   877  C C   . THR A 1 138 ? 20.42300 25.87100  -11.18500 1.000 58.20986  ?  138 THR A C   1 
ATOM   878  O O   . THR A 1 138 ? 21.52000 26.43800  -11.19400 1.000 59.59818  ?  138 THR A O   1 
ATOM   879  C CB  . THR A 1 138 ? 19.99000 23.41200  -11.28600 1.000 55.08766  ?  138 THR A CB  1 
ATOM   880  O OG1 . THR A 1 138 ? 21.19500 23.19800  -10.53900 1.000 57.07941  ?  138 THR A OG1 1 
ATOM   881  C CG2 . THR A 1 138 ? 19.74300 22.22600  -12.19700 1.000 56.87025  ?  138 THR A CG2 1 
ATOM   882  N N   . LYS A 1 139 ? 19.42700 26.22900  -10.37200 1.000 57.87155  ?  139 LYS A N   1 
ATOM   883  C CA  . LYS A 1 139 ? 19.58700 27.35500  -9.45900  1.000 57.28145  ?  139 LYS A CA  1 
ATOM   884  C C   . LYS A 1 139 ? 20.79000 27.16100  -8.54700  1.000 61.44428  ?  139 LYS A C   1 
ATOM   885  O O   . LYS A 1 139 ? 21.50400 28.12300  -8.24100  1.000 64.29031  ?  139 LYS A O   1 
ATOM   886  C CB  . LYS A 1 139 ? 18.31300 27.55000  -8.63700  1.000 55.10823  ?  139 LYS A CB  1 
ATOM   887  N N   . GLU A 1 140 ? 21.04200 25.92200  -8.11700  1.000 59.04914  ?  140 GLU A N   1 
ATOM   888  C CA  . GLU A 1 140 ? 22.20400 25.66000  -7.27400  1.000 61.66219  ?  140 GLU A CA  1 
ATOM   889  C C   . GLU A 1 140 ? 23.50000 26.01800  -7.99200  1.000 66.01016  ?  140 GLU A C   1 
ATOM   890  O O   . GLU A 1 140 ? 24.38900 26.64400  -7.40400  1.000 70.76587  ?  140 GLU A O   1 
ATOM   891  C CB  . GLU A 1 140 ? 22.21500 24.19700  -6.83500  1.000 59.84015  ?  140 GLU A CB  1 
ATOM   892  N N   . ASP A 1 141 ? 23.61700 25.64900  -9.27100  1.000 59.87899  ?  141 ASP A N   1 
ATOM   893  C CA  . ASP A 1 141 ? 24.82700 25.96200  -10.02600 1.000 62.74362  ?  141 ASP A CA  1 
ATOM   894  C C   . ASP A 1 141 ? 25.06700 27.46400  -10.09100 1.000 67.39957  ?  141 ASP A C   1 
ATOM   895  O O   . ASP A 1 141 ? 26.21100 27.92200  -9.98600  1.000 67.27568  ?  141 ASP A O   1 
ATOM   896  C CB  . ASP A 1 141 ? 24.73500 25.36800  -11.43000 1.000 62.32127  ?  141 ASP A CB  1 
ATOM   897  C CG  . ASP A 1 141 ? 24.52200 23.86800  -11.41200 1.000 63.22509  ?  141 ASP A CG  1 
ATOM   898  O OD1 . ASP A 1 141 ? 25.37300 23.15400  -10.84200 1.000 62.44987  ?  141 ASP A OD1 1 
ATOM   899  O OD2 . ASP A 1 141 ? 23.49200 23.40600  -11.94500 1.000 63.83964  -1 141 ASP A OD2 1 
ATOM   900  N N   . PHE A 1 142 ? 24.00100 28.24900  -10.26500 1.000 70.83505  ?  142 PHE A N   1 
ATOM   901  C CA  . PHE A 1 142 ? 24.14100 29.69900  -10.19900 1.000 71.16535  ?  142 PHE A CA  1 
ATOM   902  C C   . PHE A 1 142 ? 24.65800 30.13200  -8.83500  1.000 72.18184  ?  142 PHE A C   1 
ATOM   903  O O   . PHE A 1 142 ? 25.54400 30.98900  -8.74200  1.000 76.17783  ?  142 PHE A O   1 
ATOM   904  C CB  . PHE A 1 142 ? 22.80500 30.37700  -10.50200 1.000 70.34534  ?  142 PHE A CB  1 
ATOM   905  C CG  . PHE A 1 142 ? 22.41600 30.33400  -11.95000 1.000 68.94065  ?  142 PHE A CG  1 
ATOM   906  C CD1 . PHE A 1 142 ? 22.05100 29.14200  -12.55300 1.000 68.60228  ?  142 PHE A CD1 1 
ATOM   907  C CD2 . PHE A 1 142 ? 22.40900 31.49100  -12.71100 1.000 68.30555  ?  142 PHE A CD2 1 
ATOM   908  C CE1 . PHE A 1 142 ? 21.68900 29.10400  -13.88800 1.000 66.24946  ?  142 PHE A CE1 1 
ATOM   909  C CE2 . PHE A 1 142 ? 22.05000 31.45800  -14.04600 1.000 68.78439  ?  142 PHE A CE2 1 
ATOM   910  C CZ  . PHE A 1 142 ? 21.69000 30.26200  -14.63500 1.000 66.58056  ?  142 PHE A CZ  1 
ATOM   911  N N   . ARG A 1 143 ? 24.12700 29.53800  -7.76400  1.000 68.44279  ?  143 ARG A N   1 
ATOM   912  C CA  . ARG A 1 143 ? 24.53000 29.94000  -6.42200  1.000 64.63650  ?  143 ARG A CA  1 
ATOM   913  C C   . ARG A 1 143 ? 25.99100 29.60900  -6.16200  1.000 69.66069  ?  143 ARG A C   1 
ATOM   914  O O   . ARG A 1 143 ? 26.70800 30.39300  -5.53000  1.000 69.78577  ?  143 ARG A O   1 
ATOM   915  C CB  . ARG A 1 143 ? 23.64000 29.26900  -5.38200  1.000 60.05601  ?  143 ARG A CB  1 
ATOM   916  C CG  . ARG A 1 143 ? 22.17800 29.64600  -5.49800  1.000 59.77455  ?  143 ARG A CG  1 
ATOM   917  C CD  . ARG A 1 143 ? 21.33100 28.91300  -4.47300  1.000 58.50422  ?  143 ARG A CD  1 
ATOM   918  N NE  . ARG A 1 143 ? 19.91100 29.19000  -4.65400  1.000 61.63025  ?  143 ARG A NE  1 
ATOM   919  C CZ  . ARG A 1 143 ? 18.95000 28.72200  -3.86900  1.000 65.71589  ?  143 ARG A CZ  1 
ATOM   920  N NH1 . ARG A 1 143 ? 19.22200 27.95900  -2.82300  1.000 68.22568  ?  143 ARG A NH1 1 
ATOM   921  N NH2 . ARG A 1 143 ? 17.68500 29.03100  -4.13800  1.000 68.90740  ?  143 ARG A NH2 1 
ATOM   922  N N   . TYR A 1 144 ? 26.45100 28.45100  -6.63700  1.000 82.47209  ?  144 TYR A N   1 
ATOM   923  C CA  . TYR A 1 144 ? 27.85700 28.10200  -6.47800  1.000 81.99008  ?  144 TYR A CA  1 
ATOM   924  C C   . TYR A 1 144 ? 28.74600 29.07200  -7.24100  1.000 82.64387  ?  144 TYR A C   1 
ATOM   925  O O   . TYR A 1 144 ? 29.76900 29.53200  -6.72000  1.000 83.08392  ?  144 TYR A O   1 
ATOM   926  C CB  . TYR A 1 144 ? 28.10400 26.67100  -6.95200  1.000 80.59064  ?  144 TYR A CB  1 
ATOM   927  C CG  . TYR A 1 144 ? 27.16900 25.64700  -6.35400  1.000 87.85667  ?  144 TYR A CG  1 
ATOM   928  C CD1 . TYR A 1 144 ? 26.76500 25.72900  -5.02800  1.000 85.73464  ?  144 TYR A CD1 1 
ATOM   929  C CD2 . TYR A 1 144 ? 26.68600 24.59500  -7.11900  1.000 88.15729  ?  144 TYR A CD2 1 
ATOM   930  C CE1 . TYR A 1 144 ? 25.90600 24.79000  -4.48100  1.000 89.93280  ?  144 TYR A CE1 1 
ATOM   931  C CE2 . TYR A 1 144 ? 25.82700 23.65500  -6.58000  1.000 86.03249  ?  144 TYR A CE2 1 
ATOM   932  C CZ  . TYR A 1 144 ? 25.44100 23.75400  -5.26400  1.000 89.72331  ?  144 TYR A CZ  1 
ATOM   933  O OH  . TYR A 1 144 ? 24.58600 22.81200  -4.73500  1.000 90.39725  ?  144 TYR A OH  1 
ATOM   934  N N   . ARG A 1 145 ? 28.36500 29.40400  -8.47500  1.000 70.26803  ?  145 ARG A N   1 
ATOM   935  C CA  . ARG A 1 145 ? 29.18700 30.29700  -9.28400  1.000 67.42218  ?  145 ARG A CA  1 
ATOM   936  C C   . ARG A 1 145 ? 29.18000 31.71700  -8.72700  1.000 64.65620  ?  145 ARG A C   1 
ATOM   937  O O   . ARG A 1 145 ? 30.23700 32.34600  -8.60200  1.000 65.86471  ?  145 ARG A O   1 
ATOM   938  C CB  . ARG A 1 145 ? 28.71500 30.26900  -10.74100 1.000 66.00514  ?  145 ARG A CB  1 
ATOM   939  C CG  . ARG A 1 145 ? 28.94500 28.92700  -11.44000 1.000 62.48447  ?  145 ARG A CG  1 
ATOM   940  C CD  . ARG A 1 145 ? 28.41100 28.90400  -12.86900 1.000 59.96004  ?  145 ARG A CD  1 
ATOM   941  N NE  . ARG A 1 145 ? 28.83800 27.71200  -13.59800 1.000 59.02608  ?  145 ARG A NE  1 
ATOM   942  C CZ  . ARG A 1 145 ? 29.93000 27.64200  -14.34900 1.000 57.71997  ?  145 ARG A CZ  1 
ATOM   943  N NH1 . ARG A 1 145 ? 30.72000 28.69000  -14.52100 1.000 59.44945  ?  145 ARG A NH1 1 
ATOM   944  N NH2 . ARG A 1 145 ? 30.23700 26.49300  -14.94600 1.000 52.90898  ?  145 ARG A NH2 1 
ATOM   945  N N   . SER A 1 146 ? 28.00100 32.23800  -8.37700  1.000 62.41644  ?  146 SER A N   1 
ATOM   946  C CA  . SER A 1 146 ? 27.84800 33.58900  -7.83900  1.000 62.29443  ?  146 SER A CA  1 
ATOM   947  C C   . SER A 1 146 ? 27.23400 33.47900  -6.45100  1.000 71.56580  ?  146 SER A C   1 
ATOM   948  O O   . SER A 1 146 ? 26.01100 33.59700  -6.29000  1.000 72.89536  ?  146 SER A O   1 
ATOM   949  C CB  . SER A 1 146 ? 26.99300 34.46700  -8.74800  1.000 61.66843  ?  146 SER A CB  1 
ATOM   950  N N   . PRO A 1 147 ? 28.05100 33.24700  -5.42400  1.000 71.54434  ?  147 PRO A N   1 
ATOM   951  C CA  . PRO A 1 147 ? 27.50500 33.12800  -4.06600  1.000 63.76911  ?  147 PRO A CA  1 
ATOM   952  C C   . PRO A 1 147 ? 26.91300 34.41900  -3.53100  1.000 70.47556  ?  147 PRO A C   1 
ATOM   953  O O   . PRO A 1 147 ? 26.17800 34.37500  -2.53600  1.000 72.98061  ?  147 PRO A O   1 
ATOM   954  C CB  . PRO A 1 147 ? 28.71700 32.68600  -3.24200  1.000 65.79654  ?  147 PRO A CB  1 
ATOM   955  C CG  . PRO A 1 147 ? 29.88800 33.22200  -4.00800  1.000 66.63069  ?  147 PRO A CG  1 
ATOM   956  C CD  . PRO A 1 147 ? 29.51900 33.15900  -5.45000  1.000 68.24245  ?  147 PRO A CD  1 
ATOM   957  N N   . HIS A 1 148 ? 27.19200 35.55900  -4.15800  1.000 77.80701  ?  148 HIS A N   1 
ATOM   958  C CA  . HIS A 1 148 ? 26.66300 36.83400  -3.70000  1.000 80.10323  ?  148 HIS A CA  1 
ATOM   959  C C   . HIS A 1 148 ? 25.51700 37.34700  -4.55100  1.000 78.03822  ?  148 HIS A C   1 
ATOM   960  O O   . HIS A 1 148 ? 24.69100 38.12300  -4.06000  1.000 78.32598  ?  148 HIS A O   1 
ATOM   961  C CB  . HIS A 1 148 ? 27.76700 37.89100  -3.66600  1.000 82.95640  ?  148 HIS A CB  1 
ATOM   962  C CG  . HIS A 1 148 ? 28.99800 37.44800  -2.94400  1.000 85.44614  ?  148 HIS A CG  1 
ATOM   963  N ND1 . HIS A 1 148 ? 30.02800 36.78200  -3.57200  1.000 89.20260  ?  148 HIS A ND1 1 
ATOM   964  C CD2 . HIS A 1 148 ? 29.36100 37.56700  -1.64400  1.000 84.96712  ?  148 HIS A CD2 1 
ATOM   965  C CE1 . HIS A 1 148 ? 30.97600 36.51300  -2.69100  1.000 90.95002  ?  148 HIS A CE1 1 
ATOM   966  N NE2 . HIS A 1 148 ? 30.59600 36.97800  -1.51400  1.000 87.65220  ?  148 HIS A NE2 1 
ATOM   967  N N   . SER A 1 149 ? 25.43900 36.93600  -5.81400  1.000 73.06993  ?  149 SER A N   1 
ATOM   968  C CA  . SER A 1 149 ? 24.38100 37.43700  -6.68100  1.000 71.38616  ?  149 SER A CA  1 
ATOM   969  C C   . SER A 1 149 ? 23.74600 36.33000  -7.51600  1.000 69.91913  ?  149 SER A C   1 
ATOM   970  O O   . SER A 1 149 ? 23.03100 36.62600  -8.47800  1.000 70.08182  ?  149 SER A O   1 
ATOM   971  C CB  . SER A 1 149 ? 24.92500 38.54500  -7.58800  1.000 73.16818  ?  149 SER A CB  1 
ATOM   972  N N   . GLY A 1 150 ? 23.96800 35.06500  -7.16000  1.000 65.57792  ?  150 GLY A N   1 
ATOM   973  C CA  . GLY A 1 150 ? 23.49300 33.97600  -8.00100  1.000 66.28402  ?  150 GLY A CA  1 
ATOM   974  C C   . GLY A 1 150 ? 21.98100 33.89300  -8.08100  1.000 65.18707  ?  150 GLY A C   1 
ATOM   975  O O   . GLY A 1 150 ? 21.41100 33.81200  -9.17300  1.000 69.01694  ?  150 GLY A O   1 
ATOM   976  N N   . ASP A 1 151 ? 21.31100 33.90200  -6.92800  1.000 59.41624  ?  151 ASP A N   1 
ATOM   977  C CA  . ASP A 1 151 ? 19.85800 33.77400  -6.92600  1.000 59.68848  ?  151 ASP A CA  1 
ATOM   978  C C   . ASP A 1 151 ? 19.20300 34.89200  -7.72700  1.000 65.05772  ?  151 ASP A C   1 
ATOM   979  O O   . ASP A 1 151 ? 18.28700 34.64200  -8.52000  1.000 64.98085  ?  151 ASP A O   1 
ATOM   980  C CB  . ASP A 1 151 ? 19.33800 33.75100  -5.49000  1.000 61.25120  ?  151 ASP A CB  1 
ATOM   981  C CG  . ASP A 1 151 ? 19.99700 34.79900  -4.61600  1.000 65.92598  ?  151 ASP A CG  1 
ATOM   982  O OD1 . ASP A 1 151 ? 20.78500 35.61100  -5.14600  1.000 68.52903  ?  151 ASP A OD1 1 
ATOM   983  O OD2 . ASP A 1 151 ? 19.74200 34.79900  -3.39300  1.000 66.17394  -1 151 ASP A OD2 1 
ATOM   984  N N   . VAL A 1 152 ? 19.66700 36.13000  -7.54500  1.000 66.41186  ?  152 VAL A N   1 
ATOM   985  C CA  . VAL A 1 152 ? 19.14600 37.23700  -8.34100  1.000 63.34885  ?  152 VAL A CA  1 
ATOM   986  C C   . VAL A 1 152 ? 19.46000 37.02100  -9.81600  1.000 62.98870  ?  152 VAL A C   1 
ATOM   987  O O   . VAL A 1 152 ? 18.59200 37.18400  -10.68200 1.000 64.76171  ?  152 VAL A O   1 
ATOM   988  C CB  . VAL A 1 152 ? 19.70700 38.57600  -7.82800  1.000 63.33231  ?  152 VAL A CB  1 
ATOM   989  N N   . LEU A 1 153 ? 20.69800 36.63000  -10.12400 1.000 63.30545  ?  153 LEU A N   1 
ATOM   990  C CA  . LEU A 1 153 ? 21.08000 36.34500  -11.50300 1.000 62.23756  ?  153 LEU A CA  1 
ATOM   991  C C   . LEU A 1 153 ? 20.40300 35.10400  -12.05800 1.000 64.45061  ?  153 LEU A C   1 
ATOM   992  O O   . LEU A 1 153 ? 20.54800 34.81900  -13.25100 1.000 63.96347  ?  153 LEU A O   1 
ATOM   993  C CB  . LEU A 1 153 ? 22.59500 36.19200  -11.60900 1.000 58.70790  ?  153 LEU A CB  1 
ATOM   994  C CG  . LEU A 1 153 ? 23.35100 37.51800  -11.58100 1.000 61.17673  ?  153 LEU A CG  1 
ATOM   995  C CD1 . LEU A 1 153 ? 24.85200 37.28600  -11.49600 1.000 66.37586  ?  153 LEU A CD1 1 
ATOM   996  C CD2 . LEU A 1 153 ? 22.98700 38.35800  -12.79000 1.000 61.16649  ?  153 LEU A CD2 1 
ATOM   997  N N   . TYR A 1 154 ? 19.67800 34.35400  -11.23300 1.000 60.79567  ?  154 TYR A N   1 
ATOM   998  C CA  . TYR A 1 154 ? 18.93800 33.19200  -11.69800 1.000 58.70628  ?  154 TYR A CA  1 
ATOM   999  C C   . TYR A 1 154 ? 17.47600 33.51700  -11.96900 1.000 59.99382  ?  154 TYR A C   1 
ATOM   1000 O O   . TYR A 1 154 ? 16.96400 33.20900  -13.04900 1.000 59.57071  ?  154 TYR A O   1 
ATOM   1001 C CB  . TYR A 1 154 ? 19.03500 32.06200  -10.67300 1.000 60.79774  ?  154 TYR A CB  1 
ATOM   1002 C CG  . TYR A 1 154 ? 18.27600 30.82000  -11.06900 1.000 61.80117  ?  154 TYR A CG  1 
ATOM   1003 C CD1 . TYR A 1 154 ? 18.83100 29.89500  -11.93900 1.000 63.47084  ?  154 TYR A CD1 1 
ATOM   1004 C CD2 . TYR A 1 154 ? 17.00000 30.57600  -10.57800 1.000 61.99082  ?  154 TYR A CD2 1 
ATOM   1005 C CE1 . TYR A 1 154 ? 18.14200 28.75500  -12.30600 1.000 63.27047  ?  154 TYR A CE1 1 
ATOM   1006 C CE2 . TYR A 1 154 ? 16.30200 29.44100  -10.94000 1.000 60.90463  ?  154 TYR A CE2 1 
ATOM   1007 C CZ  . TYR A 1 154 ? 16.87800 28.53300  -11.80200 1.000 59.51095  ?  154 TYR A CZ  1 
ATOM   1008 O OH  . TYR A 1 154 ? 16.18600 27.40100  -12.16300 1.000 61.43617  ?  154 TYR A OH  1 
ATOM   1009 N N   . GLU A 1 155 ? 16.79200 34.13100  -11.00200 1.000 60.25323  ?  155 GLU A N   1 
ATOM   1010 C CA  . GLU A 1 155 ? 15.38900 34.47500  -11.19800 1.000 61.64461  ?  155 GLU A CA  1 
ATOM   1011 C C   . GLU A 1 155 ? 15.21700 35.49500  -12.31200 1.000 60.71500  ?  155 GLU A C   1 
ATOM   1012 O O   . GLU A 1 155 ? 14.19400 35.48600  -13.00800 1.000 59.38331  ?  155 GLU A O   1 
ATOM   1013 C CB  . GLU A 1 155 ? 14.78500 34.99800  -9.89200  1.000 60.82546  ?  155 GLU A CB  1 
ATOM   1014 C CG  . GLU A 1 155 ? 15.09000 34.12700  -8.68100  1.000 60.13165  ?  155 GLU A CG  1 
ATOM   1015 C CD  . GLU A 1 155 ? 14.46000 32.74400  -8.77500  1.000 63.50099  ?  155 GLU A CD  1 
ATOM   1016 O OE1 . GLU A 1 155 ? 13.43700 32.59900  -9.47800  1.000 62.11073  ?  155 GLU A OE1 1 
ATOM   1017 O OE2 . GLU A 1 155 ? 14.99400 31.79800  -8.15200  1.000 63.18675  -1 155 GLU A OE2 1 
ATOM   1018 N N   . LEU A 1 156 ? 16.20400 36.37400  -12.50000 1.000 59.85792  ?  156 LEU A N   1 
ATOM   1019 C CA  . LEU A 1 156 ? 16.13800 37.32900  -13.59900 1.000 62.50377  ?  156 LEU A CA  1 
ATOM   1020 C C   . LEU A 1 156 ? 16.07400 36.61000  -14.93700 1.000 60.48091  ?  156 LEU A C   1 
ATOM   1021 O O   . LEU A 1 156 ? 15.28500 36.98000  -15.81600 1.000 59.05103  ?  156 LEU A O   1 
ATOM   1022 C CB  . LEU A 1 156 ? 17.34400 38.26400  -13.55500 1.000 64.31646  ?  156 LEU A CB  1 
ATOM   1023 C CG  . LEU A 1 156 ? 17.49600 39.21800  -14.73900 1.000 66.71285  ?  156 LEU A CG  1 
ATOM   1024 C CD1 . LEU A 1 156 ? 16.31900 40.18500  -14.81100 1.000 68.13421  ?  156 LEU A CD1 1 
ATOM   1025 C CD2 . LEU A 1 156 ? 18.80800 39.96700  -14.63500 1.000 66.04357  ?  156 LEU A CD2 1 
ATOM   1026 N N   . LEU A 1 157 ? 16.89400 35.57300  -15.10300 1.000 59.52635  ?  157 LEU A N   1 
ATOM   1027 C CA  . LEU A 1 157 ? 16.84200 34.77000  -16.31700 1.000 56.49560  ?  157 LEU A CA  1 
ATOM   1028 C C   . LEU A 1 157 ? 15.44000 34.21700  -16.54000 1.000 56.42677  ?  157 LEU A C   1 
ATOM   1029 O O   . LEU A 1 157 ? 14.88000 34.33900  -17.63400 1.000 57.64795  ?  157 LEU A O   1 
ATOM   1030 C CB  . LEU A 1 157 ? 17.86600 33.64200  -16.23200 1.000 54.31960  ?  157 LEU A CB  1 
ATOM   1031 C CG  . LEU A 1 157 ? 17.87900 32.64900  -17.39000 1.000 52.39448  ?  157 LEU A CG  1 
ATOM   1032 C CD1 . LEU A 1 157 ? 18.22800 33.35700  -18.68800 1.000 52.89865  ?  157 LEU A CD1 1 
ATOM   1033 C CD2 . LEU A 1 157 ? 18.85100 31.51600  -17.10600 1.000 54.53633  ?  157 LEU A CD2 1 
ATOM   1034 N N   . GLN A 1 158 ? 14.84300 33.63600  -15.49500 1.000 56.75827  ?  158 GLN A N   1 
ATOM   1035 C CA  . GLN A 1 158 ? 13.50700 33.06200  -15.62800 1.000 55.28769  ?  158 GLN A CA  1 
ATOM   1036 C C   . GLN A 1 158 ? 12.48900 34.11100  -16.04900 1.000 57.67673  ?  158 GLN A C   1 
ATOM   1037 O O   . GLN A 1 158 ? 11.61200 33.83700  -16.87600 1.000 58.83363  ?  158 GLN A O   1 
ATOM   1038 C CB  . GLN A 1 158 ? 13.08700 32.40600  -14.31700 1.000 56.44463  ?  158 GLN A CB  1 
ATOM   1039 C CG  . GLN A 1 158 ? 14.21100 31.65800  -13.63700 1.000 57.70380  ?  158 GLN A CG  1 
ATOM   1040 C CD  . GLN A 1 158 ? 14.83100 30.61100  -14.53600 1.000 56.50783  ?  158 GLN A CD  1 
ATOM   1041 O OE1 . GLN A 1 158 ? 14.13900 29.95600  -15.31900 1.000 54.88412  ?  158 GLN A OE1 1 
ATOM   1042 N NE2 . GLN A 1 158 ? 16.14500 30.45000  -14.43400 1.000 58.69312  ?  158 GLN A NE2 1 
ATOM   1043 N N   . HIS A 1 159 ? 12.58100 35.31800  -15.48700 1.000 60.65546  ?  159 HIS A N   1 
ATOM   1044 C CA  . HIS A 1 159 ? 11.69900 36.39200  -15.93200 1.000 63.80726  ?  159 HIS A CA  1 
ATOM   1045 C C   . HIS A 1 159 ? 11.97500 36.76500  -17.38300 1.000 64.48261  ?  159 HIS A C   1 
ATOM   1046 O O   . HIS A 1 159 ? 11.03900 36.98000  -18.16200 1.000 64.80086  ?  159 HIS A O   1 
ATOM   1047 C CB  . HIS A 1 159 ? 11.84600 37.60600  -15.01800 1.000 66.24217  ?  159 HIS A CB  1 
ATOM   1048 C CG  . HIS A 1 159 ? 11.42000 37.35300  -13.60500 1.000 68.34033  ?  159 HIS A CG  1 
ATOM   1049 N ND1 . HIS A 1 159 ? 12.29200 36.92000  -12.62900 1.000 67.38364  ?  159 HIS A ND1 1 
ATOM   1050 C CD2 . HIS A 1 159 ? 10.21700 37.49200  -12.99800 1.000 68.73081  ?  159 HIS A CD2 1 
ATOM   1051 C CE1 . HIS A 1 159 ? 11.64200 36.79100  -11.48600 1.000 66.87121  ?  159 HIS A CE1 1 
ATOM   1052 N NE2 . HIS A 1 159 ? 10.38100 37.13400  -11.68300 1.000 66.37680  ?  159 HIS A NE2 1 
ATOM   1053 N N   . ILE A 1 160 ? 13.25100 36.84500  -17.76300 1.000 62.56263  ?  160 ILE A N   1 
ATOM   1054 C CA  . ILE A 1 160 ? 13.59700 37.04500  -19.16600 1.000 62.50221  ?  160 ILE A CA  1 
ATOM   1055 C C   . ILE A 1 160 ? 13.04700 35.90700  -20.01300 1.000 64.19331  ?  160 ILE A C   1 
ATOM   1056 O O   . ILE A 1 160 ? 12.50400 36.12800  -21.10300 1.000 69.47712  ?  160 ILE A O   1 
ATOM   1057 C CB  . ILE A 1 160 ? 15.12200 37.17900  -19.32700 1.000 55.88107  ?  160 ILE A CB  1 
ATOM   1058 C CG1 . ILE A 1 160 ? 15.62700 38.43300  -18.61600 1.000 60.56926  ?  160 ILE A CG1 1 
ATOM   1059 C CG2 . ILE A 1 160 ? 15.50300 37.21100  -20.79700 1.000 56.55534  ?  160 ILE A CG2 1 
ATOM   1060 N N   . LEU A 1 161 ? 13.17800 34.67000  -19.52700 1.000 59.67473  ?  161 LEU A N   1 
ATOM   1061 C CA  . LEU A 1 161 ? 12.62600 33.53300  -20.25300 1.000 56.11421  ?  161 LEU A CA  1 
ATOM   1062 C C   . LEU A 1 161 ? 11.11400 33.63500  -20.36800 1.000 63.24122  ?  161 LEU A C   1 
ATOM   1063 O O   . LEU A 1 161 ? 10.53500 33.20200  -21.37100 1.000 70.99178  ?  161 LEU A O   1 
ATOM   1064 C CB  . LEU A 1 161 ? 13.01900 32.22500  -19.56800 1.000 52.81887  ?  161 LEU A CB  1 
ATOM   1065 C CG  . LEU A 1 161 ? 14.51300 31.90200  -19.54000 1.000 51.27492  ?  161 LEU A CG  1 
ATOM   1066 C CD1 . LEU A 1 161 ? 14.79700 30.68700  -18.67800 1.000 50.58017  ?  161 LEU A CD1 1 
ATOM   1067 C CD2 . LEU A 1 161 ? 15.03300 31.69300  -20.94300 1.000 52.18636  ?  161 LEU A CD2 1 
ATOM   1068 N N   . LYS A 1 162 ? 10.45900 34.20700  -19.35700 1.000 60.80266  ?  162 LYS A N   1 
ATOM   1069 C CA  . LYS A 1 162 ? 9.01900  34.40800  -19.44300 1.000 65.22314  ?  162 LYS A CA  1 
ATOM   1070 C C   . LYS A 1 162 ? 8.67700  35.47000  -20.48000 1.000 75.15416  ?  162 LYS A C   1 
ATOM   1071 O O   . LYS A 1 162 ? 7.67400  35.35000  -21.19200 1.000 80.27673  ?  162 LYS A O   1 
ATOM   1072 C CB  . LYS A 1 162 ? 8.45000  34.80200  -18.07900 1.000 64.44616  ?  162 LYS A CB  1 
ATOM   1073 N N   . GLN A 1 163 ? 9.50100  36.51000  -20.58500 1.000 79.67421  ?  163 GLN A N   1 
ATOM   1074 C CA  . GLN A 1 163 ? 9.28200  37.54500  -21.58800 1.000 81.32918  ?  163 GLN A CA  1 
ATOM   1075 C C   . GLN A 1 163 ? 9.54900  36.98000  -22.97700 1.000 84.79874  ?  163 GLN A C   1 
ATOM   1076 O O   . GLN A 1 163 ? 10.65700 36.51200  -23.26100 1.000 84.06452  ?  163 GLN A O   1 
ATOM   1077 C CB  . GLN A 1 163 ? 10.18100 38.74700  -21.31400 1.000 84.37580  ?  163 GLN A CB  1 
ATOM   1078 C CG  . GLN A 1 163 ? 9.96700  39.39500  -19.95400 1.000 85.26566  ?  163 GLN A CG  1 
ATOM   1079 C CD  . GLN A 1 163 ? 11.04200 40.41200  -19.62100 1.000 89.33615  ?  163 GLN A CD  1 
ATOM   1080 O OE1 . GLN A 1 163 ? 11.19700 40.81600  -18.46800 1.000 90.35637  ?  163 GLN A OE1 1 
ATOM   1081 N NE2 . GLN A 1 163 ? 11.80100 40.82100  -20.63200 1.000 90.32346  ?  163 GLN A NE2 1 
ATOM   1082 N N   . ARG A 1 164 ? 8.53200  37.02300  -23.83700 1.000 97.11166  ?  164 ARG A N   1 
ATOM   1083 C CA  . ARG A 1 164 ? 8.60600  36.47900  -25.19200 1.000 101.31855 ?  164 ARG A CA  1 
ATOM   1084 C C   . ARG A 1 164 ? 9.05800  35.01900  -25.16200 1.000 97.69879  ?  164 ARG A C   1 
ATOM   1085 O O   . ARG A 1 164 ? 10.06900 34.63300  -25.75200 1.000 97.45148  ?  164 ARG A O   1 
ATOM   1086 C CB  . ARG A 1 164 ? 9.55700  37.31000  -26.05600 1.000 104.29208 ?  164 ARG A CB  1 
ATOM   1087 N N   . LEU A 1 175 ? 22.83900 15.49200  -30.80700 1.000 81.11565  ?  175 LEU A N   1 
ATOM   1088 C CA  . LEU A 1 175 ? 24.07100 14.82000  -30.42600 1.000 76.88281  ?  175 LEU A CA  1 
ATOM   1089 C C   . LEU A 1 175 ? 24.80800 14.32700  -31.67200 1.000 77.15308  ?  175 LEU A C   1 
ATOM   1090 O O   . LEU A 1 175 ? 24.18300 13.99700  -32.68300 1.000 77.47057  ?  175 LEU A O   1 
ATOM   1091 C CB  . LEU A 1 175 ? 23.77400 13.64900  -29.49100 1.000 67.68403  ?  175 LEU A CB  1 
ATOM   1092 N N   . PRO A 1 176 ? 26.14000 14.28000  -31.63000 1.000 75.77129  ?  176 PRO A N   1 
ATOM   1093 C CA  . PRO A 1 176 ? 26.89200 13.78600  -32.78800 1.000 78.06107  ?  176 PRO A CA  1 
ATOM   1094 C C   . PRO A 1 176 ? 26.58600 12.32200  -33.06400 1.000 82.14661  ?  176 PRO A C   1 
ATOM   1095 O O   . PRO A 1 176 ? 26.25700 11.55100  -32.16000 1.000 81.55909  ?  176 PRO A O   1 
ATOM   1096 C CB  . PRO A 1 176 ? 28.35500 13.98200  -32.37200 1.000 74.23714  ?  176 PRO A CB  1 
ATOM   1097 C CG  . PRO A 1 176 ? 28.32100 14.01200  -30.88200 1.000 76.24760  ?  176 PRO A CG  1 
ATOM   1098 C CD  . PRO A 1 176 ? 27.02800 14.68200  -30.52700 1.000 74.62494  ?  176 PRO A CD  1 
ATOM   1099 N N   . ALA A 1 177 ? 26.70500 11.94300  -34.33900 1.000 85.79080  ?  177 ALA A N   1 
ATOM   1100 C CA  . ALA A 1 177 ? 26.38200 10.57800  -34.74000 1.000 86.33508  ?  177 ALA A CA  1 
ATOM   1101 C C   . ALA A 1 177 ? 27.33300 9.56000   -34.12000 1.000 86.98232  ?  177 ALA A C   1 
ATOM   1102 O O   . ALA A 1 177 ? 26.92500 8.42600   -33.84400 1.000 89.80301  ?  177 ALA A O   1 
ATOM   1103 C CB  . ALA A 1 177 ? 26.39400 10.46400  -36.26300 1.000 87.83943  ?  177 ALA A CB  1 
ATOM   1104 N N   . HIS A 1 178 ? 28.59400 9.94000   -33.88600 1.000 80.76230  ?  178 HIS A N   1 
ATOM   1105 C CA  . HIS A 1 178 ? 29.53600 9.02900   -33.24400 1.000 78.26040  ?  178 HIS A CA  1 
ATOM   1106 C C   . HIS A 1 178 ? 29.13400 8.70500   -31.81200 1.000 75.68170  ?  178 HIS A C   1 
ATOM   1107 O O   . HIS A 1 178 ? 29.63100 7.72500   -31.24600 1.000 77.09144  ?  178 HIS A O   1 
ATOM   1108 C CB  . HIS A 1 178 ? 30.94600 9.62500   -33.26500 1.000 74.73520  ?  178 HIS A CB  1 
ATOM   1109 N N   . LEU A 1 179 ? 28.24100 9.50200   -31.22100 1.000 73.13688  ?  179 LEU A N   1 
ATOM   1110 C CA  . LEU A 1 179 ? 27.79800 9.32300   -29.84400 1.000 67.62038  ?  179 LEU A CA  1 
ATOM   1111 C C   . LEU A 1 179 ? 26.28600 9.17200   -29.73800 1.000 66.31364  ?  179 LEU A C   1 
ATOM   1112 O O   . LEU A 1 179 ? 25.71600 9.42100   -28.67200 1.000 64.87530  ?  179 LEU A O   1 
ATOM   1113 C CB  . LEU A 1 179 ? 28.26700 10.49400  -28.98200 1.000 62.22232  ?  179 LEU A CB  1 
ATOM   1114 C CG  . LEU A 1 179 ? 29.74900 10.45000  -28.63300 1.000 61.41289  ?  179 LEU A CG  1 
ATOM   1115 C CD1 . LEU A 1 179 ? 30.34200 11.84500  -28.64900 1.000 58.61732  ?  179 LEU A CD1 1 
ATOM   1116 C CD2 . LEU A 1 179 ? 29.92100 9.79200   -27.27600 1.000 60.67313  ?  179 LEU A CD2 1 
ATOM   1117 N N   . ARG A 1 180 ? 25.62300 8.77000   -30.82200 1.000 64.88528  ?  180 ARG A N   1 
ATOM   1118 C CA  . ARG A 1 180 ? 24.17900 8.58100   -30.77100 1.000 64.58412  ?  180 ARG A CA  1 
ATOM   1119 C C   . ARG A 1 180 ? 23.78200 7.38000   -29.92400 1.000 63.08282  ?  180 ARG A C   1 
ATOM   1120 O O   . ARG A 1 180 ? 22.58800 7.19000   -29.67200 1.000 63.74737  ?  180 ARG A O   1 
ATOM   1121 C CB  . ARG A 1 180 ? 23.61800 8.43100   -32.18600 1.000 68.85745  ?  180 ARG A CB  1 
ATOM   1122 C CG  . ARG A 1 180 ? 22.19200 8.93300   -32.34800 1.000 69.38571  ?  180 ARG A CG  1 
ATOM   1123 C CD  . ARG A 1 180 ? 22.10600 10.42600  -32.08500 1.000 72.65507  ?  180 ARG A CD  1 
ATOM   1124 N NE  . ARG A 1 180 ? 22.99500 11.18600  -32.95600 1.000 75.51785  ?  180 ARG A NE  1 
ATOM   1125 C CZ  . ARG A 1 180 ? 22.66100 11.64000  -34.15700 1.000 78.70129  ?  180 ARG A CZ  1 
ATOM   1126 N NH1 . ARG A 1 180 ? 21.45900 11.42500  -34.66900 1.000 77.12167  ?  180 ARG A NH1 1 
ATOM   1127 N NH2 . ARG A 1 180 ? 23.55500 12.32700  -34.86500 1.000 82.71581  ?  180 ARG A NH2 1 
ATOM   1128 N N   . LEU A 1 181 ? 24.74400 6.57400   -29.48300 1.000 63.73912  ?  181 LEU A N   1 
ATOM   1129 C CA  . LEU A 1 181 ? 24.43500 5.44200   -28.62800 1.000 62.95647  ?  181 LEU A CA  1 
ATOM   1130 C C   . LEU A 1 181 ? 24.13200 5.92000   -27.21000 1.000 65.01912  ?  181 LEU A C   1 
ATOM   1131 O O   . LEU A 1 181 ? 24.44100 7.05200   -26.83000 1.000 64.16984  ?  181 LEU A O   1 
ATOM   1132 C CB  . LEU A 1 181 ? 25.59400 4.44400   -28.61500 1.000 58.00796  ?  181 LEU A CB  1 
ATOM   1133 N N   . GLN A 1 182 ? 23.51800 5.03800   -26.42700 1.000 64.16161  ?  182 GLN A N   1 
ATOM   1134 C CA  . GLN A 1 182 ? 23.15100 5.37400   -25.05600 1.000 58.41858  ?  182 GLN A CA  1 
ATOM   1135 C C   . GLN A 1 182 ? 24.41200 5.53800   -24.20900 1.000 57.84490  ?  182 GLN A C   1 
ATOM   1136 O O   . GLN A 1 182 ? 25.35300 4.75100   -24.34000 1.000 59.69140  ?  182 GLN A O   1 
ATOM   1137 C CB  . GLN A 1 182 ? 22.24500 4.30000   -24.45100 1.000 59.86542  ?  182 GLN A CB  1 
ATOM   1138 C CG  . GLN A 1 182 ? 20.92700 4.08000   -25.18700 1.000 64.35828  ?  182 GLN A CG  1 
ATOM   1139 C CD  . GLN A 1 182 ? 21.09500 3.40100   -26.54100 1.000 71.55986  ?  182 GLN A CD  1 
ATOM   1140 O OE1 . GLN A 1 182 ? 22.02400 2.62000   -26.74900 1.000 71.72567  ?  182 GLN A OE1 1 
ATOM   1141 N NE2 . GLN A 1 182 ? 20.22600 3.74500   -27.48500 1.000 72.62918  ?  182 GLN A NE2 1 
ATOM   1142 N N   . PRO A 1 183 ? 24.46600 6.55300   -23.34200 1.000 57.46585  ?  183 PRO A N   1 
ATOM   1143 C CA  . PRO A 1 183 ? 25.69000 6.79300   -22.55700 1.000 58.09847  ?  183 PRO A CA  1 
ATOM   1144 C C   . PRO A 1 183 ? 26.19200 5.57400   -21.80300 1.000 58.73411  ?  183 PRO A C   1 
ATOM   1145 O O   . PRO A 1 183 ? 27.40600 5.42500   -21.62500 1.000 59.48355  ?  183 PRO A O   1 
ATOM   1146 C CB  . PRO A 1 183 ? 25.25800 7.90300   -21.59600 1.000 58.16523  ?  183 PRO A CB  1 
ATOM   1147 C CG  . PRO A 1 183 ? 24.24000 8.67500   -22.36300 1.000 57.98374  ?  183 PRO A CG  1 
ATOM   1148 C CD  . PRO A 1 183 ? 23.50100 7.65900   -23.21300 1.000 62.15074  ?  183 PRO A CD  1 
ATOM   1149 N N   . ILE A 1 184 ? 25.28900 4.70100   -21.34800 1.000 60.68031  ?  184 ILE A N   1 
ATOM   1150 C CA  . ILE A 1 184 ? 25.69300 3.48400   -20.64700 1.000 60.32036  ?  184 ILE A CA  1 
ATOM   1151 C C   . ILE A 1 184 ? 26.63000 2.64600   -21.50600 1.000 58.57572  ?  184 ILE A C   1 
ATOM   1152 O O   . ILE A 1 184 ? 27.48400 1.91600   -20.98800 1.000 59.14145  ?  184 ILE A O   1 
ATOM   1153 C CB  . ILE A 1 184 ? 24.43700 2.69200   -20.22100 1.000 57.42964  ?  184 ILE A CB  1 
ATOM   1154 C CG1 . ILE A 1 184 ? 24.80800 1.31700   -19.66500 1.000 55.07867  ?  184 ILE A CG1 1 
ATOM   1155 C CG2 . ILE A 1 184 ? 23.46700 2.56100   -21.38700 1.000 59.82211  ?  184 ILE A CG2 1 
ATOM   1156 C CD1 . ILE A 1 184 ? 23.61700 0.45400   -19.33600 1.000 58.36562  ?  184 ILE A CD1 1 
ATOM   1157 N N   . TYR A 1 185 ? 26.50900 2.75400   -22.82600 1.000 55.81060  ?  185 TYR A N   1 
ATOM   1158 C CA  . TYR A 1 185 ? 27.34900 2.00600   -23.74700 1.000 58.38881  ?  185 TYR A CA  1 
ATOM   1159 C C   . TYR A 1 185 ? 28.49000 2.83800   -24.33200 1.000 58.94377  ?  185 TYR A C   1 
ATOM   1160 O O   . TYR A 1 185 ? 29.14000 2.38700   -25.27900 1.000 59.67275  ?  185 TYR A O   1 
ATOM   1161 C CB  . TYR A 1 185 ? 26.49700 1.41800   -24.87700 1.000 60.84796  ?  185 TYR A CB  1 
ATOM   1162 C CG  . TYR A 1 185 ? 25.22900 0.72700   -24.41500 1.000 61.18424  ?  185 TYR A CG  1 
ATOM   1163 C CD1 . TYR A 1 185 ? 25.28600 -0.42500  -23.64300 1.000 62.56827  ?  185 TYR A CD1 1 
ATOM   1164 C CD2 . TYR A 1 185 ? 23.97500 1.21700   -24.76500 1.000 61.82765  ?  185 TYR A CD2 1 
ATOM   1165 C CE1 . TYR A 1 185 ? 24.13400 -1.06400  -23.21900 1.000 62.06900  ?  185 TYR A CE1 1 
ATOM   1166 C CE2 . TYR A 1 185 ? 22.81300 0.58300   -24.34600 1.000 61.90544  ?  185 TYR A CE2 1 
ATOM   1167 C CZ  . TYR A 1 185 ? 22.90200 -0.55800  -23.57200 1.000 62.79835  ?  185 TYR A CZ  1 
ATOM   1168 O OH  . TYR A 1 185 ? 21.76200 -1.20100  -23.14500 1.000 64.65641  ?  185 TYR A OH  1 
ATOM   1169 N N   . TRP A 1 186 ? 28.76000 4.02800   -23.79600 1.000 59.40980  ?  186 TRP A N   1 
ATOM   1170 C CA  . TRP A 1 186 ? 29.84600 4.83700   -24.33900 1.000 58.37983  ?  186 TRP A CA  1 
ATOM   1171 C C   . TRP A 1 186 ? 31.20200 4.28600   -23.91600 1.000 58.92528  ?  186 TRP A C   1 
ATOM   1172 O O   . TRP A 1 186 ? 31.35500 3.68600   -22.84900 1.000 62.00255  ?  186 TRP A O   1 
ATOM   1173 C CB  . TRP A 1 186 ? 29.73500 6.29100   -23.88700 1.000 58.10466  ?  186 TRP A CB  1 
ATOM   1174 C CG  . TRP A 1 186 ? 28.64200 7.05500   -24.54800 1.000 57.66435  ?  186 TRP A CG  1 
ATOM   1175 C CD1 . TRP A 1 186 ? 27.76300 6.59100   -25.48000 1.000 58.43000  ?  186 TRP A CD1 1 
ATOM   1176 C CD2 . TRP A 1 186 ? 28.28600 8.41900   -24.30400 1.000 58.79358  ?  186 TRP A CD2 1 
ATOM   1177 N NE1 . TRP A 1 186 ? 26.88800 7.58500   -25.84100 1.000 59.16779  ?  186 TRP A NE1 1 
ATOM   1178 C CE2 . TRP A 1 186 ? 27.18700 8.71800   -25.13100 1.000 59.54846  ?  186 TRP A CE2 1 
ATOM   1179 C CE3 . TRP A 1 186 ? 28.79200 9.41800   -23.46600 1.000 57.38427  ?  186 TRP A CE3 1 
ATOM   1180 C CZ2 . TRP A 1 186 ? 26.58500 9.97400   -25.14800 1.000 58.47968  ?  186 TRP A CZ2 1 
ATOM   1181 C CZ3 . TRP A 1 186 ? 28.19300 10.66500  -23.48400 1.000 54.32365  ?  186 TRP A CZ3 1 
ATOM   1182 C CH2 . TRP A 1 186 ? 27.10100 10.93200  -24.31900 1.000 55.45690  ?  186 TRP A CH2 1 
ATOM   1183 N N   . SER A 1 187 ? 32.19500 4.50900   -24.76600 1.000 58.65332  ?  187 SER A N   1 
ATOM   1184 C CA  . SER A 1 187 ? 33.55000 4.06200   -24.50100 1.000 63.33187  ?  187 SER A CA  1 
ATOM   1185 C C   . SER A 1 187 ? 34.36100 5.18800   -23.87500 1.000 66.86337  ?  187 SER A C   1 
ATOM   1186 O O   . SER A 1 187 ? 33.92100 6.33600   -23.79500 1.000 67.80744  ?  187 SER A O   1 
ATOM   1187 C CB  . SER A 1 187 ? 34.21900 3.58700   -25.78800 1.000 71.79132  ?  187 SER A CB  1 
ATOM   1188 O OG  . SER A 1 187 ? 34.43700 4.67500   -26.67000 1.000 74.78448  ?  187 SER A OG  1 
ATOM   1189 N N   . ARG A 1 188 ? 35.56800 4.84300   -23.42800 1.000 65.39046  ?  188 ARG A N   1 
ATOM   1190 C CA  . ARG A 1 188 ? 36.45400 5.85700   -22.87000 1.000 69.88613  ?  188 ARG A CA  1 
ATOM   1191 C C   . ARG A 1 188 ? 36.78400 6.91200   -23.91400 1.000 72.02368  ?  188 ARG A C   1 
ATOM   1192 O O   . ARG A 1 188 ? 36.83400 8.10900   -23.60900 1.000 72.65464  ?  188 ARG A O   1 
ATOM   1193 C CB  . ARG A 1 188 ? 37.72900 5.20700   -22.33200 1.000 71.71112  ?  188 ARG A CB  1 
ATOM   1194 C CG  . ARG A 1 188 ? 38.68800 6.17200   -21.65700 1.000 70.07868  ?  188 ARG A CG  1 
ATOM   1195 C CD  . ARG A 1 188 ? 39.94400 5.46100   -21.17100 1.000 68.84845  ?  188 ARG A CD  1 
ATOM   1196 N NE  . ARG A 1 188 ? 40.81800 6.37000   -20.44300 1.000 72.56557  ?  188 ARG A NE  1 
ATOM   1197 C CZ  . ARG A 1 188 ? 41.79400 7.07800   -20.99400 1.000 78.48889  ?  188 ARG A CZ  1 
ATOM   1198 N NH1 . ARG A 1 188 ? 42.08000 6.97700   -22.28200 1.000 82.78695  ?  188 ARG A NH1 1 
ATOM   1199 N NH2 . ARG A 1 188 ? 42.49800 7.91400   -20.23400 1.000 80.02425  ?  188 ARG A NH2 1 
ATOM   1200 N N   . ASP A 1 189 ? 36.99800 6.48500   -25.16000 1.000 82.49703  ?  189 ASP A N   1 
ATOM   1201 C CA  . ASP A 1 189 ? 37.20500 7.44400   -26.23700 1.000 82.16811  ?  189 ASP A CA  1 
ATOM   1202 C C   . ASP A 1 189 ? 35.91800 8.18200   -26.56900 1.000 80.48659  ?  189 ASP A C   1 
ATOM   1203 O O   . ASP A 1 189 ? 35.95900 9.35400   -26.95800 1.000 79.55466  ?  189 ASP A O   1 
ATOM   1204 C CB  . ASP A 1 189 ? 37.74300 6.73100   -27.47600 1.000 83.12315  ?  189 ASP A CB  1 
ATOM   1205 C CG  . ASP A 1 189 ? 38.96200 5.88700   -27.17300 1.000 90.49036  ?  189 ASP A CG  1 
ATOM   1206 O OD1 . ASP A 1 189 ? 39.41800 5.89900   -26.00900 1.000 94.18769  ?  189 ASP A OD1 1 
ATOM   1207 O OD2 . ASP A 1 189 ? 39.46400 5.21500   -28.09900 1.000 95.53320  -1 189 ASP A OD2 1 
ATOM   1208 N N   . ASP A 1 190 ? 34.77100 7.51900   -26.41400 1.000 68.26458  ?  190 ASP A N   1 
ATOM   1209 C CA  . ASP A 1 190 ? 33.50000 8.18200   -26.67700 1.000 67.46853  ?  190 ASP A CA  1 
ATOM   1210 C C   . ASP A 1 190 ? 33.25900 9.31900   -25.68900 1.000 65.49687  ?  190 ASP A C   1 
ATOM   1211 O O   . ASP A 1 190 ? 32.80000 10.40000  -26.07800 1.000 63.34046  ?  190 ASP A O   1 
ATOM   1212 C CB  . ASP A 1 190 ? 32.36000 7.16400   -26.63300 1.000 65.19034  ?  190 ASP A CB  1 
ATOM   1213 N N   . VAL A 1 191 ? 33.58200 9.10200   -24.41100 1.000 66.51302  ?  191 VAL A N   1 
ATOM   1214 C CA  . VAL A 1 191 ? 33.41100 10.15200  -23.40700 1.000 65.07366  ?  191 VAL A CA  1 
ATOM   1215 C C   . VAL A 1 191 ? 34.24800 11.37500  -23.76300 1.000 64.73860  ?  191 VAL A C   1 
ATOM   1216 O O   . VAL A 1 191 ? 33.80500 12.52100  -23.60200 1.000 60.55260  ?  191 VAL A O   1 
ATOM   1217 C CB  . VAL A 1 191 ? 33.76100 9.60900   -22.00700 1.000 60.36382  ?  191 VAL A CB  1 
ATOM   1218 C CG1 . VAL A 1 191 ? 33.71300 10.71700  -20.96600 1.000 56.56599  ?  191 VAL A CG1 1 
ATOM   1219 C CG2 . VAL A 1 191 ? 32.81200 8.48600   -21.63000 1.000 63.81512  ?  191 VAL A CG2 1 
ATOM   1220 N N   . ALA A 1 192 ? 35.46400 11.15300  -24.26700 1.000 64.87909  ?  192 ALA A N   1 
ATOM   1221 C CA  . ALA A 1 192 ? 36.33500 12.26500  -24.62800 1.000 58.50410  ?  192 ALA A CA  1 
ATOM   1222 C C   . ALA A 1 192 ? 35.73500 13.08800  -25.75900 1.000 57.58291  ?  192 ALA A C   1 
ATOM   1223 O O   . ALA A 1 192 ? 35.72600 14.32300  -25.70400 1.000 60.83043  ?  192 ALA A O   1 
ATOM   1224 C CB  . ALA A 1 192 ? 37.72000 11.74800  -25.01400 1.000 63.31938  ?  192 ALA A CB  1 
ATOM   1225 N N   . GLN A 1 193 ? 35.23800 12.42000  -26.80200 1.000 58.43384  ?  193 GLN A N   1 
ATOM   1226 C CA  . GLN A 1 193 ? 34.63100 13.15300  -27.90900 1.000 58.22047  ?  193 GLN A CA  1 
ATOM   1227 C C   . GLN A 1 193 ? 33.37000 13.88700  -27.46800 1.000 58.18564  ?  193 GLN A C   1 
ATOM   1228 O O   . GLN A 1 193 ? 33.07000 14.96600  -27.99300 1.000 54.27067  ?  193 GLN A O   1 
ATOM   1229 C CB  . GLN A 1 193 ? 34.32300 12.20700  -29.07200 1.000 58.27659  ?  193 GLN A CB  1 
ATOM   1230 C CG  . GLN A 1 193 ? 35.50200 11.97100  -30.01400 1.000 58.51656  ?  193 GLN A CG  1 
ATOM   1231 C CD  . GLN A 1 193 ? 35.57900 10.54200  -30.51800 1.000 59.84761  ?  193 GLN A CD  1 
ATOM   1232 N N   . TRP A 1 194 ? 32.63200 13.32800  -26.50300 1.000 57.72222  ?  194 TRP A N   1 
ATOM   1233 C CA  . TRP A 1 194 ? 31.45000 14.01200  -25.98300 1.000 54.37719  ?  194 TRP A CA  1 
ATOM   1234 C C   . TRP A 1 194 ? 31.82900 15.32700  -25.32100 1.000 55.18740  ?  194 TRP A C   1 
ATOM   1235 O O   . TRP A 1 194 ? 31.13200 16.33800  -25.47800 1.000 53.43849  ?  194 TRP A O   1 
ATOM   1236 C CB  . TRP A 1 194 ? 30.71200 13.10900  -24.99400 1.000 54.09432  ?  194 TRP A CB  1 
ATOM   1237 C CG  . TRP A 1 194 ? 29.67100 13.82000  -24.16200 1.000 49.34425  ?  194 TRP A CG  1 
ATOM   1238 C CD1 . TRP A 1 194 ? 28.47200 14.30700  -24.59300 1.000 48.88589  ?  194 TRP A CD1 1 
ATOM   1239 C CD2 . TRP A 1 194 ? 29.73300 14.10100  -22.75600 1.000 50.86913  ?  194 TRP A CD2 1 
ATOM   1240 N NE1 . TRP A 1 194 ? 27.78800 14.87900  -23.54900 1.000 47.82589  ?  194 TRP A NE1 1 
ATOM   1241 C CE2 . TRP A 1 194 ? 28.54000 14.76700  -22.41000 1.000 49.89991  ?  194 TRP A CE2 1 
ATOM   1242 C CE3 . TRP A 1 194 ? 30.68300 13.85800  -21.75800 1.000 51.62891  ?  194 TRP A CE3 1 
ATOM   1243 C CZ2 . TRP A 1 194 ? 28.27100 15.19300  -21.11100 1.000 47.96554  ?  194 TRP A CZ2 1 
ATOM   1244 C CZ3 . TRP A 1 194 ? 30.41300 14.28100  -20.46700 1.000 46.59019  ?  194 TRP A CZ3 1 
ATOM   1245 C CH2 . TRP A 1 194 ? 29.21700 14.94100  -20.15700 1.000 47.60570  ?  194 TRP A CH2 1 
ATOM   1246 N N   . LEU A 1 195 ? 32.93200 15.33200  -24.57400 1.000 53.31419  ?  195 LEU A N   1 
ATOM   1247 C CA  . LEU A 1 195 ? 33.40500 16.56700  -23.96700 1.000 53.29941  ?  195 LEU A CA  1 
ATOM   1248 C C   . LEU A 1 195 ? 33.73500 17.59900  -25.03700 1.000 51.29278  ?  195 LEU A C   1 
ATOM   1249 O O   . LEU A 1 195 ? 33.27100 18.74400  -24.97700 1.000 54.05535  ?  195 LEU A O   1 
ATOM   1250 C CB  . LEU A 1 195 ? 34.62300 16.27300  -23.09200 1.000 56.03170  ?  195 LEU A CB  1 
ATOM   1251 C CG  . LEU A 1 195 ? 34.41000 15.24000  -21.98100 1.000 54.61791  ?  195 LEU A CG  1 
ATOM   1252 C CD1 . LEU A 1 195 ? 35.74700 14.75200  -21.45900 1.000 56.37725  ?  195 LEU A CD1 1 
ATOM   1253 C CD2 . LEU A 1 195 ? 33.57500 15.81600  -20.85100 1.000 54.07444  ?  195 LEU A CD2 1 
ATOM   1254 N N   . LYS A 1 196 ? 34.51400 17.19600  -26.04500 1.000 52.25380  ?  196 LYS A N   1 
ATOM   1255 C CA  . LYS A 1 196 ? 34.90200 18.11700  -27.10800 1.000 52.69106  ?  196 LYS A CA  1 
ATOM   1256 C C   . LYS A 1 196 ? 33.68500 18.65800  -27.84600 1.000 54.53182  ?  196 LYS A C   1 
ATOM   1257 O O   . LYS A 1 196 ? 33.65200 19.83500  -28.22500 1.000 57.57828  ?  196 LYS A O   1 
ATOM   1258 C CB  . LYS A 1 196 ? 35.85000 17.41800  -28.07900 1.000 54.51089  ?  196 LYS A CB  1 
ATOM   1259 N N   . TRP A 1 197 ? 32.67300 17.81500  -28.05800 1.000 52.61534  ?  197 TRP A N   1 
ATOM   1260 C CA  . TRP A 1 197 ? 31.43800 18.29000  -28.67000 1.000 53.36780  ?  197 TRP A CA  1 
ATOM   1261 C C   . TRP A 1 197 ? 30.73800 19.28800  -27.76100 1.000 54.97273  ?  197 TRP A C   1 
ATOM   1262 O O   . TRP A 1 197 ? 30.27600 20.34200  -28.21100 1.000 59.27717  ?  197 TRP A O   1 
ATOM   1263 C CB  . TRP A 1 197 ? 30.51400 17.11300  -28.97700 1.000 53.26500  ?  197 TRP A CB  1 
ATOM   1264 C CG  . TRP A 1 197 ? 29.12500 17.53200  -29.35100 1.000 57.40622  ?  197 TRP A CG  1 
ATOM   1265 C CD1 . TRP A 1 197 ? 28.69800 17.93500  -30.58300 1.000 61.69626  ?  197 TRP A CD1 1 
ATOM   1266 C CD2 . TRP A 1 197 ? 27.97900 17.58500  -28.49300 1.000 56.30252  ?  197 TRP A CD2 1 
ATOM   1267 N NE1 . TRP A 1 197 ? 27.36000 18.23900  -30.54400 1.000 65.60756  ?  197 TRP A NE1 1 
ATOM   1268 C CE2 . TRP A 1 197 ? 26.89400 18.03200  -29.27300 1.000 62.08816  ?  197 TRP A CE2 1 
ATOM   1269 C CE3 . TRP A 1 197 ? 27.76500 17.30000  -27.14300 1.000 54.12772  ?  197 TRP A CE3 1 
ATOM   1270 C CZ2 . TRP A 1 197 ? 25.61500 18.20000  -28.74700 1.000 62.32871  ?  197 TRP A CZ2 1 
ATOM   1271 C CZ3 . TRP A 1 197 ? 26.49400 17.46700  -26.62400 1.000 55.11672  ?  197 TRP A CZ3 1 
ATOM   1272 C CH2 . TRP A 1 197 ? 25.43600 17.91300  -27.42400 1.000 58.84432  ?  197 TRP A CH2 1 
ATOM   1273 N N   . ALA A 1 198 ? 30.65500 18.96700  -26.46900 1.000 55.60143  ?  198 ALA A N   1 
ATOM   1274 C CA  . ALA A 1 198 ? 30.00100 19.86000  -25.52200 1.000 55.45875  ?  198 ALA A CA  1 
ATOM   1275 C C   . ALA A 1 198 ? 30.71500 21.20000  -25.44900 1.000 61.96148  ?  198 ALA A C   1 
ATOM   1276 O O   . ALA A 1 198 ? 30.07100 22.25100  -25.35200 1.000 62.04017  ?  198 ALA A O   1 
ATOM   1277 C CB  . ALA A 1 198 ? 29.95200 19.20800  -24.14400 1.000 49.00146  ?  198 ALA A CB  1 
ATOM   1278 N N   . GLU A 1 199 ? 32.04700 21.18200  -25.49900 1.000 61.07298  ?  199 GLU A N   1 
ATOM   1279 C CA  . GLU A 1 199 ? 32.80600 22.42400  -25.42000 1.000 61.39740  ?  199 GLU A CA  1 
ATOM   1280 C C   . GLU A 1 199 ? 32.47400 23.34100  -26.58700 1.000 63.69360  ?  199 GLU A C   1 
ATOM   1281 O O   . GLU A 1 199 ? 32.23700 24.54000  -26.40300 1.000 70.87687  ?  199 GLU A O   1 
ATOM   1282 C CB  . GLU A 1 199 ? 34.30100 22.12300  -25.38400 1.000 61.56731  ?  199 GLU A CB  1 
ATOM   1283 C CG  . GLU A 1 199 ? 35.16400 23.35300  -25.56400 1.000 64.92026  ?  199 GLU A CG  1 
ATOM   1284 C CD  . GLU A 1 199 ? 36.63900 23.03900  -25.48900 1.000 71.92883  ?  199 GLU A CD  1 
ATOM   1285 O OE1 . GLU A 1 199 ? 36.98600 21.91700  -25.06400 1.000 74.98482  ?  199 GLU A OE1 1 
ATOM   1286 O OE2 . GLU A 1 199 ? 37.45300 23.91700  -25.84800 1.000 75.16775  -1 199 GLU A OE2 1 
ATOM   1287 N N   . ASN A 1 200 ? 32.44200 22.79200  -27.80000 1.000 62.76831  ?  200 ASN A N   1 
ATOM   1288 C CA  . ASN A 1 200 ? 32.10700 23.61500  -28.95500 1.000 65.65437  ?  200 ASN A CA  1 
ATOM   1289 C C   . ASN A 1 200 ? 30.62300 23.95600  -28.97200 1.000 68.34927  ?  200 ASN A C   1 
ATOM   1290 O O   . ASN A 1 200 ? 30.23900 25.05900  -29.37800 1.000 72.14370  ?  200 ASN A O   1 
ATOM   1291 C CB  . ASN A 1 200 ? 32.51300 22.90000  -30.24200 1.000 69.53029  ?  200 ASN A CB  1 
ATOM   1292 C CG  . ASN A 1 200 ? 33.95200 22.43100  -30.21300 1.000 71.05070  ?  200 ASN A CG  1 
ATOM   1293 O OD1 . ASN A 1 200 ? 34.59100 22.42100  -29.16100 1.000 70.40661  ?  200 ASN A OD1 1 
ATOM   1294 N ND2 . ASN A 1 200 ? 34.47200 22.04100  -31.37100 1.000 69.78335  ?  200 ASN A ND2 1 
ATOM   1295 N N   . GLU A 1 201 ? 29.77700 23.02700  -28.51800 1.000 67.18422  ?  201 GLU A N   1 
ATOM   1296 C CA  . GLU A 1 201 ? 28.33500 23.24400  -28.58600 1.000 67.68465  ?  201 GLU A CA  1 
ATOM   1297 C C   . GLU A 1 201 ? 27.88700 24.33200  -27.61800 1.000 66.61659  ?  201 GLU A C   1 
ATOM   1298 O O   . GLU A 1 201 ? 27.01900 25.14500  -27.95100 1.000 68.97964  ?  201 GLU A O   1 
ATOM   1299 C CB  . GLU A 1 201 ? 27.59200 21.93500  -28.30800 1.000 66.62523  ?  201 GLU A CB  1 
ATOM   1300 C CG  . GLU A 1 201 ? 26.07000 22.04500  -28.31100 1.000 67.65705  ?  201 GLU A CG  1 
ATOM   1301 C CD  . GLU A 1 201 ? 25.48500 22.19900  -29.70800 1.000 78.23953  ?  201 GLU A CD  1 
ATOM   1302 O OE1 . GLU A 1 201 ? 26.24600 22.11000  -30.69500 1.000 81.12171  ?  201 GLU A OE1 1 
ATOM   1303 O OE2 . GLU A 1 201 ? 24.25700 22.40500  -29.82100 1.000 87.13315  -1 201 GLU A OE2 1 
ATOM   1304 N N   . PHE A 1 202 ? 28.46900 24.37100  -26.42100 1.000 60.28803  ?  202 PHE A N   1 
ATOM   1305 C CA  . PHE A 1 202 ? 28.05400 25.31200  -25.39000 1.000 54.35572  ?  202 PHE A CA  1 
ATOM   1306 C C   . PHE A 1 202 ? 29.07300 26.41300  -25.13600 1.000 56.56789  ?  202 PHE A C   1 
ATOM   1307 O O   . PHE A 1 202 ? 28.97100 27.11100  -24.12100 1.000 56.42839  ?  202 PHE A O   1 
ATOM   1308 C CB  . PHE A 1 202 ? 27.75400 24.57100  -24.08900 1.000 49.36170  ?  202 PHE A CB  1 
ATOM   1309 C CG  . PHE A 1 202 ? 26.72600 23.49200  -24.23300 1.000 51.47694  ?  202 PHE A CG  1 
ATOM   1310 C CD1 . PHE A 1 202 ? 25.38100 23.80900  -24.31600 1.000 51.88385  ?  202 PHE A CD1 1 
ATOM   1311 C CD2 . PHE A 1 202 ? 27.10200 22.16100  -24.29700 1.000 53.26782  ?  202 PHE A CD2 1 
ATOM   1312 C CE1 . PHE A 1 202 ? 24.42800 22.81700  -24.45100 1.000 51.55211  ?  202 PHE A CE1 1 
ATOM   1313 C CE2 . PHE A 1 202 ? 26.15400 21.16400  -24.43300 1.000 52.42791  ?  202 PHE A CE2 1 
ATOM   1314 C CZ  . PHE A 1 202 ? 24.81600 21.49300  -24.51000 1.000 51.33519  ?  202 PHE A CZ  1 
ATOM   1315 N N   . SER A 1 203 ? 30.04400 26.59200  -26.02900 1.000 55.71226  ?  203 SER A N   1 
ATOM   1316 C CA  . SER A 1 203 ? 31.05200 27.64300  -25.88400 1.000 56.73798  ?  203 SER A CA  1 
ATOM   1317 C C   . SER A 1 203 ? 31.77100 27.53500  -24.54000 1.000 56.16306  ?  203 SER A C   1 
ATOM   1318 O O   . SER A 1 203 ? 32.00700 28.53500  -23.86100 1.000 57.23865  ?  203 SER A O   1 
ATOM   1319 C CB  . SER A 1 203 ? 30.42800 29.03300  -26.05500 1.000 60.52312  ?  203 SER A CB  1 
ATOM   1320 O OG  . SER A 1 203 ? 29.78600 29.17300  -27.31200 1.000 62.72795  ?  203 SER A OG  1 
ATOM   1321 N N   . LEU A 1 204 ? 32.10800 26.31100  -24.14100 1.000 55.26952  ?  204 LEU A N   1 
ATOM   1322 C CA  . LEU A 1 204 ? 32.77300 26.09500  -22.86600 1.000 53.90634  ?  204 LEU A CA  1 
ATOM   1323 C C   . LEU A 1 204 ? 34.27700 26.31700  -22.99400 1.000 56.11054  ?  204 LEU A C   1 
ATOM   1324 O O   . LEU A 1 204 ? 34.83300 26.38000  -24.09400 1.000 59.02634  ?  204 LEU A O   1 
ATOM   1325 C CB  . LEU A 1 204 ? 32.49900 24.68400  -22.34500 1.000 52.38751  ?  204 LEU A CB  1 
ATOM   1326 C CG  . LEU A 1 204 ? 31.02500 24.29300  -22.25500 1.000 53.08275  ?  204 LEU A CG  1 
ATOM   1327 C CD1 . LEU A 1 204 ? 30.87900 22.83900  -21.84400 1.000 50.70334  ?  204 LEU A CD1 1 
ATOM   1328 C CD2 . LEU A 1 204 ? 30.29300 25.20400  -21.28200 1.000 52.95191  ?  204 LEU A CD2 1 
ATOM   1329 N N   . ARG A 1 205 ? 34.93500 26.44200  -21.84300 1.000 51.48055  ?  205 ARG A N   1 
ATOM   1330 C CA  . ARG A 1 205 ? 36.38200 26.56100  -21.82200 1.000 52.97418  ?  205 ARG A CA  1 
ATOM   1331 C C   . ARG A 1 205 ? 37.01000 25.25200  -22.29800 1.000 55.22586  ?  205 ARG A C   1 
ATOM   1332 O O   . ARG A 1 205 ? 36.36200 24.20400  -22.27400 1.000 57.18141  ?  205 ARG A O   1 
ATOM   1333 C CB  . ARG A 1 205 ? 36.86800 26.90000  -20.41400 1.000 54.74066  ?  205 ARG A CB  1 
ATOM   1334 C CG  . ARG A 1 205 ? 36.14400 28.06100  -19.75400 1.000 56.42162  ?  205 ARG A CG  1 
ATOM   1335 C CD  . ARG A 1 205 ? 36.36500 29.38300  -20.48400 1.000 59.50632  ?  205 ARG A CD  1 
ATOM   1336 N NE  . ARG A 1 205 ? 37.77400 29.70900  -20.67700 1.000 60.70433  ?  205 ARG A NE  1 
ATOM   1337 C CZ  . ARG A 1 205 ? 38.38500 29.71300  -21.85500 1.000 62.37323  ?  205 ARG A CZ  1 
ATOM   1338 N NH1 . ARG A 1 205 ? 37.73500 29.43000  -22.97200 1.000 60.08485  ?  205 ARG A NH1 1 
ATOM   1339 N NH2 . ARG A 1 205 ? 39.67900 30.01800  -21.91500 1.000 63.43955  ?  205 ARG A NH2 1 
ATOM   1340 N N   . PRO A 1 206 ? 38.26200 25.28800  -22.75700 1.000 56.77876  ?  206 PRO A N   1 
ATOM   1341 C CA  . PRO A 1 206 ? 38.93300 24.04600  -23.16300 1.000 56.65172  ?  206 PRO A CA  1 
ATOM   1342 C C   . PRO A 1 206 ? 38.91800 22.99700  -22.05900 1.000 57.84525  ?  206 PRO A C   1 
ATOM   1343 O O   . PRO A 1 206 ? 39.32300 23.25200  -20.92100 1.000 56.27083  ?  206 PRO A O   1 
ATOM   1344 C CB  . PRO A 1 206 ? 40.35600 24.51100  -23.48800 1.000 58.89541  ?  206 PRO A CB  1 
ATOM   1345 C CG  . PRO A 1 206 ? 40.17200 25.91600  -23.95300 1.000 58.57873  ?  206 PRO A CG  1 
ATOM   1346 C CD  . PRO A 1 206 ? 39.07900 26.47500  -23.07400 1.000 59.91609  ?  206 PRO A CD  1 
ATOM   1347 N N   . ILE A 1 207 ? 38.43900 21.80400  -22.40700 1.000 59.08699  ?  207 ILE A N   1 
ATOM   1348 C CA  . ILE A 1 207 ? 38.30000 20.68600  -21.47600 1.000 57.95844  ?  207 ILE A CA  1 
ATOM   1349 C C   . ILE A 1 207 ? 39.37400 19.65600  -21.79800 1.000 53.74533  ?  207 ILE A C   1 
ATOM   1350 O O   . ILE A 1 207 ? 39.52600 19.24900  -22.95600 1.000 55.20122  ?  207 ILE A O   1 
ATOM   1351 C CB  . ILE A 1 207 ? 36.89600 20.06200  -21.54900 1.000 56.11875  ?  207 ILE A CB  1 
ATOM   1352 C CG1 . ILE A 1 207 ? 35.82400 21.12800  -21.31800 1.000 55.79302  ?  207 ILE A CG1 1 
ATOM   1353 C CG2 . ILE A 1 207 ? 36.73600 18.93700  -20.53500 1.000 55.89322  ?  207 ILE A CG2 1 
ATOM   1354 C CD1 . ILE A 1 207 ? 34.40900 20.60700  -21.42700 1.000 52.25526  ?  207 ILE A CD1 1 
ATOM   1355 N N   . ASP A 1 208 ? 40.12400 19.24300  -20.78100 1.000 54.62566  ?  208 ASP A N   1 
ATOM   1356 C CA  . ASP A 1 208 ? 41.08000 18.16300  -20.96500 1.000 57.51070  ?  208 ASP A CA  1 
ATOM   1357 C C   . ASP A 1 208 ? 40.35600 16.82100  -21.00700 1.000 61.95921  ?  208 ASP A C   1 
ATOM   1358 O O   . ASP A 1 208 ? 39.38300 16.59900  -20.28000 1.000 62.92521  ?  208 ASP A O   1 
ATOM   1359 C CB  . ASP A 1 208 ? 42.11300 18.17500  -19.84100 1.000 58.84405  ?  208 ASP A CB  1 
ATOM   1360 C CG  . ASP A 1 208 ? 43.14700 17.08400  -19.99400 1.000 63.74072  ?  208 ASP A CG  1 
ATOM   1361 O OD1 . ASP A 1 208 ? 43.26600 16.52700  -21.10500 1.000 64.78480  ?  208 ASP A OD1 1 
ATOM   1362 O OD2 . ASP A 1 208 ? 43.83500 16.77400  -18.99900 1.000 69.64926  -1 208 ASP A OD2 1 
ATOM   1363 N N   . SER A 1 209 ? 40.83600 15.91800  -21.86800 1.000 62.02301  ?  209 SER A N   1 
ATOM   1364 C CA  . SER A 1 209 ? 40.18200 14.62100  -22.02400 1.000 63.92346  ?  209 SER A CA  1 
ATOM   1365 C C   . SER A 1 209 ? 40.34500 13.75100  -20.78400 1.000 63.52469  ?  209 SER A C   1 
ATOM   1366 O O   . SER A 1 209 ? 39.46600 12.93700  -20.47900 1.000 64.82939  ?  209 SER A O   1 
ATOM   1367 C CB  . SER A 1 209 ? 40.73300 13.89500  -23.25100 1.000 66.03154  ?  209 SER A CB  1 
ATOM   1368 N N   . ASN A 1 210 ? 41.45200 13.90300  -20.06300 1.000 60.69087  ?  210 ASN A N   1 
ATOM   1369 C CA  . ASN A 1 210 ? 41.64900 13.14800  -18.83300 1.000 64.90672  ?  210 ASN A CA  1 
ATOM   1370 C C   . ASN A 1 210 ? 40.73000 13.60300  -17.70300 1.000 66.15250  ?  210 ASN A C   1 
ATOM   1371 O O   . ASN A 1 210 ? 40.77600 13.00300  -16.62200 1.000 63.31519  ?  210 ASN A O   1 
ATOM   1372 C CB  . ASN A 1 210 ? 43.10900 13.24800  -18.39000 1.000 63.41611  ?  210 ASN A CB  1 
ATOM   1373 N N   . THR A 1 211 ? 39.90600 14.63400  -17.92100 1.000 66.45765  ?  211 THR A N   1 
ATOM   1374 C CA  . THR A 1 211 ? 38.98700 15.08800  -16.88200 1.000 64.32262  ?  211 THR A CA  1 
ATOM   1375 C C   . THR A 1 211 ? 37.97700 14.01000  -16.51800 1.000 66.23377  ?  211 THR A C   1 
ATOM   1376 O O   . THR A 1 211 ? 37.57700 13.89400  -15.35400 1.000 65.93964  ?  211 THR A O   1 
ATOM   1377 C CB  . THR A 1 211 ? 38.26200 16.35600  -17.34100 1.000 63.09376  ?  211 THR A CB  1 
ATOM   1378 O OG1 . THR A 1 211 ? 39.22300 17.33300  -17.75800 1.000 66.17113  ?  211 THR A OG1 1 
ATOM   1379 C CG2 . THR A 1 211 ? 37.42500 16.93600  -16.21800 1.000 64.00467  ?  211 THR A CG2 1 
ATOM   1380 N N   . PHE A 1 212 ? 37.55500 13.21100  -17.49600 1.000 61.37547  ?  212 PHE A N   1 
ATOM   1381 C CA  . PHE A 1 212 ? 36.64800 12.09300  -17.26900 1.000 58.09411  ?  212 PHE A CA  1 
ATOM   1382 C C   . PHE A 1 212 ? 37.22600 10.86800  -17.97500 1.000 59.44149  ?  212 PHE A C   1 
ATOM   1383 O O   . PHE A 1 212 ? 36.64200 10.34700  -18.92600 1.000 60.14842  ?  212 PHE A O   1 
ATOM   1384 C CB  . PHE A 1 212 ? 35.24200 12.41400  -17.76100 1.000 54.88210  ?  212 PHE A CB  1 
ATOM   1385 C CG  . PHE A 1 212 ? 34.62600 13.61000  -17.10000 1.000 58.07112  ?  212 PHE A CG  1 
ATOM   1386 C CD1 . PHE A 1 212 ? 33.94100 13.48100  -15.90600 1.000 59.08195  ?  212 PHE A CD1 1 
ATOM   1387 C CD2 . PHE A 1 212 ? 34.72500 14.86300  -17.67600 1.000 57.61313  ?  212 PHE A CD2 1 
ATOM   1388 C CE1 . PHE A 1 212 ? 33.36400 14.58000  -15.30100 1.000 58.35586  ?  212 PHE A CE1 1 
ATOM   1389 C CE2 . PHE A 1 212 ? 34.15300 15.96500  -17.07400 1.000 56.16823  ?  212 PHE A CE2 1 
ATOM   1390 C CZ  . PHE A 1 212 ? 33.47400 15.82300  -15.88300 1.000 56.42299  ?  212 PHE A CZ  1 
ATOM   1391 N N   . GLU A 1 213 ? 38.38500 10.40900  -17.50100 1.000 60.56122  ?  213 GLU A N   1 
ATOM   1392 C CA  . GLU A 1 213 ? 39.06500 9.25300   -18.08500 1.000 62.50787  ?  213 GLU A CA  1 
ATOM   1393 C C   . GLU A 1 213 ? 38.40200 7.97800   -17.56900 1.000 59.02369  ?  213 GLU A C   1 
ATOM   1394 O O   . GLU A 1 213 ? 38.88700 7.30600   -16.65500 1.000 60.38988  ?  213 GLU A O   1 
ATOM   1395 C CB  . GLU A 1 213 ? 40.55300 9.28400   -17.75800 1.000 60.88379  ?  213 GLU A CB  1 
ATOM   1396 N N   . MET A 1 214 ? 37.27600 7.63200   -18.18700 1.000 59.91959  ?  214 MET A N   1 
ATOM   1397 C CA  . MET A 1 214 ? 36.48300 6.47600   -17.77900 1.000 61.57947  ?  214 MET A CA  1 
ATOM   1398 C C   . MET A 1 214 ? 35.50500 6.13300   -18.89700 1.000 64.08433  ?  214 MET A C   1 
ATOM   1399 O O   . MET A 1 214 ? 35.43300 6.81800   -19.92200 1.000 62.95759  ?  214 MET A O   1 
ATOM   1400 C CB  . MET A 1 214 ? 35.74400 6.75500   -16.47400 1.000 59.61631  ?  214 MET A CB  1 
ATOM   1401 C CG  . MET A 1 214 ? 34.71100 7.86100   -16.59500 1.000 58.41678  ?  214 MET A CG  1 
ATOM   1402 S SD  . MET A 1 214 ? 34.21500 8.49800   -14.98600 1.000 63.23464  ?  214 MET A SD  1 
ATOM   1403 C CE  . MET A 1 214 ? 35.76900 9.16800   -14.40300 1.000 60.66735  ?  214 MET A CE  1 
ATOM   1404 N N   . ASN A 1 215 ? 34.74100 5.06900   -18.68000 1.000 72.25897  ?  215 ASN A N   1 
ATOM   1405 C CA  . ASN A 1 215 ? 33.68900 4.67100   -19.59900 1.000 71.97760  ?  215 ASN A CA  1 
ATOM   1406 C C   . ASN A 1 215 ? 32.37600 5.34100   -19.24200 1.000 70.71570  ?  215 ASN A C   1 
ATOM   1407 O O   . ASN A 1 215 ? 32.19500 5.86900   -18.14400 1.000 70.63489  ?  215 ASN A O   1 
ATOM   1408 C CB  . ASN A 1 215 ? 33.50800 3.16100   -19.59000 1.000 73.43579  ?  215 ASN A CB  1 
ATOM   1409 C CG  . ASN A 1 215 ? 34.52500 2.47300   -20.43700 1.000 78.33095  ?  215 ASN A CG  1 
ATOM   1410 O OD1 . ASN A 1 215 ? 35.35500 3.13200   -21.05800 1.000 82.26685  ?  215 ASN A OD1 1 
ATOM   1411 N ND2 . ASN A 1 215 ? 34.48400 1.15000   -20.47100 1.000 82.61846  ?  215 ASN A ND2 1 
ATOM   1412 N N   . GLY A 1 216 ? 31.44500 5.29400   -20.19300 1.000 63.34359  ?  216 GLY A N   1 
ATOM   1413 C CA  . GLY A 1 216 ? 30.16500 5.95100   -19.99200 1.000 60.23095  ?  216 GLY A CA  1 
ATOM   1414 C C   . GLY A 1 216 ? 29.45000 5.46900   -18.75000 1.000 61.04754  ?  216 GLY A C   1 
ATOM   1415 O O   . GLY A 1 216 ? 28.79800 6.25000   -18.05500 1.000 62.05954  ?  216 GLY A O   1 
ATOM   1416 N N   . LYS A 1 217 ? 29.57000 4.17500   -18.44600 1.000 58.79388  ?  217 LYS A N   1 
ATOM   1417 C CA  . LYS A 1 217 ? 29.00100 3.66000   -17.20700 1.000 58.42454  ?  217 LYS A CA  1 
ATOM   1418 C C   . LYS A 1 217 ? 29.61600 4.35800   -16.00100 1.000 59.93224  ?  217 LYS A C   1 
ATOM   1419 O O   . LYS A 1 217 ? 28.90100 4.83200   -15.11100 1.000 64.51669  ?  217 LYS A O   1 
ATOM   1420 C CB  . LYS A 1 217 ? 29.20300 2.14700   -17.12500 1.000 57.35826  ?  217 LYS A CB  1 
ATOM   1421 N N   . ALA A 1 218 ? 30.94700 4.45300   -15.96800 1.000 57.71147  ?  218 ALA A N   1 
ATOM   1422 C CA  . ALA A 1 218 ? 31.60300 5.11200   -14.84300 1.000 59.11907  ?  218 ALA A CA  1 
ATOM   1423 C C   . ALA A 1 218 ? 31.22900 6.58600   -14.77600 1.000 62.38616  ?  218 ALA A C   1 
ATOM   1424 O O   . ALA A 1 218 ? 31.08400 7.14800   -13.68300 1.000 59.84788  ?  218 ALA A O   1 
ATOM   1425 C CB  . ALA A 1 218 ? 33.11500 4.94500   -14.94700 1.000 59.14486  ?  218 ALA A CB  1 
ATOM   1426 N N   . LEU A 1 219 ? 31.06700 7.22700   -15.93600 1.000 61.55640  ?  219 LEU A N   1 
ATOM   1427 C CA  . LEU A 1 219 ? 30.67400 8.63100   -15.96000 1.000 53.74898  ?  219 LEU A CA  1 
ATOM   1428 C C   . LEU A 1 219 ? 29.29400 8.82200   -15.34500 1.000 52.67697  ?  219 LEU A C   1 
ATOM   1429 O O   . LEU A 1 219 ? 29.03800 9.82400   -14.66600 1.000 57.71291  ?  219 LEU A O   1 
ATOM   1430 C CB  . LEU A 1 219 ? 30.69500 9.15400   -17.39400 1.000 52.48440  ?  219 LEU A CB  1 
ATOM   1431 C CG  . LEU A 1 219 ? 30.32000 10.62400  -17.55500 1.000 50.40550  ?  219 LEU A CG  1 
ATOM   1432 C CD1 . LEU A 1 219 ? 31.39700 11.47700  -16.93500 1.000 53.43444  ?  219 LEU A CD1 1 
ATOM   1433 C CD2 . LEU A 1 219 ? 30.12200 10.98700  -19.01200 1.000 52.99616  ?  219 LEU A CD2 1 
ATOM   1434 N N   . LEU A 1 220 ? 28.39000 7.86700   -15.57100 1.000 52.12357  ?  220 LEU A N   1 
ATOM   1435 C CA  . LEU A 1 220 ? 27.07000 7.94800   -14.95700 1.000 51.20766  ?  220 LEU A CA  1 
ATOM   1436 C C   . LEU A 1 220 ? 27.16000 7.87500   -13.43900 1.000 55.91141  ?  220 LEU A C   1 
ATOM   1437 O O   . LEU A 1 220 ? 26.45200 8.60500   -12.73400 1.000 58.52137  ?  220 LEU A O   1 
ATOM   1438 C CB  . LEU A 1 220 ? 26.16600 6.84100   -15.50000 1.000 51.45355  ?  220 LEU A CB  1 
ATOM   1439 C CG  . LEU A 1 220 ? 25.91300 6.83300   -17.01000 1.000 53.31506  ?  220 LEU A CG  1 
ATOM   1440 C CD1 . LEU A 1 220 ? 25.09900 5.61800   -17.42800 1.000 55.15769  ?  220 LEU A CD1 1 
ATOM   1441 C CD2 . LEU A 1 220 ? 25.20500 8.11000   -17.42600 1.000 51.02801  ?  220 LEU A CD2 1 
ATOM   1442 N N   . LEU A 1 221 ? 28.03900 7.01300   -12.91700 1.000 53.86816  ?  221 LEU A N   1 
ATOM   1443 C CA  . LEU A 1 221 ? 28.14200 6.84000   -11.46900 1.000 55.53020  ?  221 LEU A CA  1 
ATOM   1444 C C   . LEU A 1 221 ? 28.56700 8.12200   -10.76700 1.000 54.92452  ?  221 LEU A C   1 
ATOM   1445 O O   . LEU A 1 221 ? 28.21700 8.33200   -9.59900  1.000 53.88195  ?  221 LEU A O   1 
ATOM   1446 C CB  . LEU A 1 221 ? 29.12500 5.71700   -11.14100 1.000 56.35414  ?  221 LEU A CB  1 
ATOM   1447 C CG  . LEU A 1 221 ? 28.84500 4.36700   -11.80000 1.000 58.15816  ?  221 LEU A CG  1 
ATOM   1448 C CD1 . LEU A 1 221 ? 29.93000 3.35600   -11.47000 1.000 59.67246  ?  221 LEU A CD1 1 
ATOM   1449 C CD2 . LEU A 1 221 ? 27.48500 3.85100   -11.37200 1.000 60.89582  ?  221 LEU A CD2 1 
ATOM   1450 N N   . LEU A 1 222 ? 29.31900 8.98200   -11.45000 1.000 54.00561  ?  222 LEU A N   1 
ATOM   1451 C CA  . LEU A 1 222 ? 29.80800 10.19900  -10.82100 1.000 52.86481  ?  222 LEU A CA  1 
ATOM   1452 C C   . LEU A 1 222 ? 28.64500 11.10100  -10.42900 1.000 54.78029  ?  222 LEU A C   1 
ATOM   1453 O O   . LEU A 1 222 ? 27.66500 11.23800  -11.16600 1.000 55.25653  ?  222 LEU A O   1 
ATOM   1454 C CB  . LEU A 1 222 ? 30.76600 10.94000  -11.75900 1.000 52.40309  ?  222 LEU A CB  1 
ATOM   1455 C CG  . LEU A 1 222 ? 32.06200 10.25200  -12.20100 1.000 53.58851  ?  222 LEU A CG  1 
ATOM   1456 C CD1 . LEU A 1 222 ? 32.86500 11.16000  -13.11800 1.000 54.78675  ?  222 LEU A CD1 1 
ATOM   1457 C CD2 . LEU A 1 222 ? 32.89600 9.85900   -10.99800 1.000 55.06985  ?  222 LEU A CD2 1 
ATOM   1458 N N   . THR A 1 223 ? 28.75200 11.69800  -9.24700  1.000 54.48750  ?  223 THR A N   1 
ATOM   1459 C CA  . THR A 1 223 ? 27.76100 12.64500  -8.76600  1.000 54.06594  ?  223 THR A CA  1 
ATOM   1460 C C   . THR A 1 223 ? 28.06400 14.04400  -9.29400  1.000 60.14812  ?  223 THR A C   1 
ATOM   1461 O O   . THR A 1 223 ? 29.16400 14.33000  -9.77300  1.000 62.04852  ?  223 THR A O   1 
ATOM   1462 C CB  . THR A 1 223 ? 27.73000 12.65500  -7.24100  1.000 52.37855  ?  223 THR A CB  1 
ATOM   1463 O OG1 . THR A 1 223 ? 28.99800 13.10000  -6.74700  1.000 54.41442  ?  223 THR A OG1 1 
ATOM   1464 C CG2 . THR A 1 223 ? 27.45000 11.26700  -6.71400  1.000 53.25366  ?  223 THR A CG2 1 
ATOM   1465 N N   . LYS A 1 224 ? 27.06400 14.92500  -9.19200  1.000 57.52339  ?  224 LYS A N   1 
ATOM   1466 C CA  . LYS A 1 224 ? 27.22400 16.29000  -9.68500  1.000 55.50179  ?  224 LYS A CA  1 
ATOM   1467 C C   . LYS A 1 224 ? 28.37300 17.00900  -8.99200  1.000 55.06394  ?  224 LYS A C   1 
ATOM   1468 O O   . LYS A 1 224 ? 29.01100 17.87900  -9.59600  1.000 56.65503  ?  224 LYS A O   1 
ATOM   1469 C CB  . LYS A 1 224 ? 25.92400 17.07400  -9.50700  1.000 53.63128  ?  224 LYS A CB  1 
ATOM   1470 N N   . GLU A 1 225 ? 28.66000 16.65700  -7.73500  1.000 56.02312  ?  225 GLU A N   1 
ATOM   1471 C CA  . GLU A 1 225 ? 29.81100 17.24100  -7.05300  1.000 58.01024  ?  225 GLU A CA  1 
ATOM   1472 C C   . GLU A 1 225 ? 31.12700 16.77200  -7.66500  1.000 61.33628  ?  225 GLU A C   1 
ATOM   1473 O O   . GLU A 1 225 ? 32.10800 17.52500  -7.66500  1.000 63.26904  ?  225 GLU A O   1 
ATOM   1474 C CB  . GLU A 1 225 ? 29.76700 16.91200  -5.56000  1.000 54.77955  ?  225 GLU A CB  1 
ATOM   1475 N N   . ASP A 1 226 ? 31.17300 15.53900  -8.18600  1.000 57.68974  ?  226 ASP A N   1 
ATOM   1476 C CA  . ASP A 1 226 ? 32.37400 15.06900  -8.87500  1.000 57.80166  ?  226 ASP A CA  1 
ATOM   1477 C C   . ASP A 1 226 ? 32.58700 15.82100  -10.18700 1.000 57.75672  ?  226 ASP A C   1 
ATOM   1478 O O   . ASP A 1 226 ? 33.72100 16.18800  -10.52100 1.000 56.57167  ?  226 ASP A O   1 
ATOM   1479 C CB  . ASP A 1 226 ? 32.28600 13.55900  -9.12200  1.000 58.18718  ?  226 ASP A CB  1 
ATOM   1480 C CG  . ASP A 1 226 ? 31.95300 12.77600  -7.86200  1.000 57.73859  ?  226 ASP A CG  1 
ATOM   1481 O OD1 . ASP A 1 226 ? 32.03200 13.36000  -6.76200  1.000 61.50840  ?  226 ASP A OD1 1 
ATOM   1482 O OD2 . ASP A 1 226 ? 31.58800 11.58600  -7.97300  1.000 58.59527  -1 226 ASP A OD2 1 
ATOM   1483 N N   . PHE A 1 227 ? 31.51000 16.05900  -10.94100 1.000 59.32190  ?  227 PHE A N   1 
ATOM   1484 C CA  . PHE A 1 227 ? 31.62100 16.84900  -12.16300 1.000 56.57672  ?  227 PHE A CA  1 
ATOM   1485 C C   . PHE A 1 227 ? 32.12900 18.25500  -11.86700 1.000 58.26774  ?  227 PHE A C   1 
ATOM   1486 O O   . PHE A 1 227 ? 32.99000 18.77400  -12.58600 1.000 58.97799  ?  227 PHE A O   1 
ATOM   1487 C CB  . PHE A 1 227 ? 30.27100 16.90900  -12.88000 1.000 57.14098  ?  227 PHE A CB  1 
ATOM   1488 C CG  . PHE A 1 227 ? 29.89700 15.63500  -13.59000 1.000 57.79110  ?  227 PHE A CG  1 
ATOM   1489 C CD1 . PHE A 1 227 ? 29.44500 14.53500  -12.88200 1.000 56.56104  ?  227 PHE A CD1 1 
ATOM   1490 C CD2 . PHE A 1 227 ? 29.98900 15.54500  -14.97000 1.000 55.69624  ?  227 PHE A CD2 1 
ATOM   1491 C CE1 . PHE A 1 227 ? 29.09500 13.36800  -13.53700 1.000 55.56764  ?  227 PHE A CE1 1 
ATOM   1492 C CE2 . PHE A 1 227 ? 29.64500 14.38300  -15.62800 1.000 52.52414  ?  227 PHE A CE2 1 
ATOM   1493 C CZ  . PHE A 1 227 ? 29.19600 13.29300  -14.91000 1.000 55.19595  ?  227 PHE A CZ  1 
ATOM   1494 N N   . ARG A 1 228 ? 31.60700 18.88700  -10.81100 1.000 59.67213  ?  228 ARG A N   1 
ATOM   1495 C CA  . ARG A 1 228 ? 32.07900 20.21900  -10.44600 1.000 54.72558  ?  228 ARG A CA  1 
ATOM   1496 C C   . ARG A 1 228 ? 33.54600 20.20300  -10.04800 1.000 55.03214  ?  228 ARG A C   1 
ATOM   1497 O O   . ARG A 1 228 ? 34.26100 21.18700  -10.27200 1.000 56.71312  ?  228 ARG A O   1 
ATOM   1498 C CB  . ARG A 1 228 ? 31.24700 20.79300  -9.29900  1.000 51.78095  ?  228 ARG A CB  1 
ATOM   1499 C CG  . ARG A 1 228 ? 29.80900 21.10700  -9.64900  1.000 53.77055  ?  228 ARG A CG  1 
ATOM   1500 C CD  . ARG A 1 228 ? 29.12600 21.85200  -8.51300  1.000 52.67139  ?  228 ARG A CD  1 
ATOM   1501 N NE  . ARG A 1 228 ? 27.73900 22.15800  -8.83300  1.000 57.07493  ?  228 ARG A NE  1 
ATOM   1502 C CZ  . ARG A 1 228 ? 26.72200 21.34500  -8.58400  1.000 61.93182  ?  228 ARG A CZ  1 
ATOM   1503 N NH1 . ARG A 1 228 ? 26.89800 20.18400  -7.97600  1.000 61.48914  ?  228 ARG A NH1 1 
ATOM   1504 N NH2 . ARG A 1 228 ? 25.49500 21.70900  -8.94800  1.000 65.32210  ?  228 ARG A NH2 1 
ATOM   1505 N N   . TYR A 1 229 ? 34.01100 19.10600  -9.45100  1.000 53.05196  ?  229 TYR A N   1 
ATOM   1506 C CA  . TYR A 1 229 ? 35.41000 19.01900  -9.05800  1.000 54.70020  ?  229 TYR A CA  1 
ATOM   1507 C C   . TYR A 1 229 ? 36.30500 18.71600  -10.25200 1.000 58.53890  ?  229 TYR A C   1 
ATOM   1508 O O   . TYR A 1 229 ? 37.39800 19.28100  -10.37200 1.000 62.13184  ?  229 TYR A O   1 
ATOM   1509 C CB  . TYR A 1 229 ? 35.58900 17.95600  -7.97200  1.000 55.73716  ?  229 TYR A CB  1 
ATOM   1510 N N   . ARG A 1 230 ? 35.86300 17.83400  -11.14700 1.000 57.34172  ?  230 ARG A N   1 
ATOM   1511 C CA  . ARG A 1 230 ? 36.68400 17.49800  -12.30400 1.000 58.46351  ?  230 ARG A CA  1 
ATOM   1512 C C   . ARG A 1 230 ? 36.81100 18.68600  -13.25100 1.000 61.39333  ?  230 ARG A C   1 
ATOM   1513 O O   . ARG A 1 230 ? 37.92000 19.04900  -13.65900 1.000 65.83554  ?  230 ARG A O   1 
ATOM   1514 C CB  . ARG A 1 230 ? 36.10500 16.27300  -13.01100 1.000 60.12996  ?  230 ARG A CB  1 
ATOM   1515 C CG  . ARG A 1 230 ? 36.26400 14.99700  -12.19700 1.000 61.79037  ?  230 ARG A CG  1 
ATOM   1516 C CD  . ARG A 1 230 ? 35.57200 13.81100  -12.83800 1.000 62.38462  ?  230 ARG A CD  1 
ATOM   1517 N NE  . ARG A 1 230 ? 35.77900 12.58500  -12.07800 1.000 65.41931  ?  230 ARG A NE  1 
ATOM   1518 C CZ  . ARG A 1 230 ? 36.74000 11.70500  -12.32100 1.000 64.84947  ?  230 ARG A CZ  1 
ATOM   1519 N NH1 . ARG A 1 230 ? 37.58500 11.86500  -13.32800 1.000 62.02036  ?  230 ARG A NH1 1 
ATOM   1520 N NH2 . ARG A 1 230 ? 36.85300 10.63600  -11.53900 1.000 65.09701  ?  230 ARG A NH2 1 
ATOM   1521 N N   . SER A 1 231 ? 35.68700 19.31700  -13.59900 1.000 57.99451  ?  231 SER A N   1 
ATOM   1522 C CA  . SER A 1 231 ? 35.66800 20.50300  -14.45700 1.000 55.29947  ?  231 SER A CA  1 
ATOM   1523 C C   . SER A 1 231 ? 34.99700 21.64800  -13.71400 1.000 56.02944  ?  231 SER A C   1 
ATOM   1524 O O   . SER A 1 231 ? 33.77700 21.83900  -13.81600 1.000 55.11401  ?  231 SER A O   1 
ATOM   1525 C CB  . SER A 1 231 ? 34.94700 20.23600  -15.77300 1.000 57.25666  ?  231 SER A CB  1 
ATOM   1526 O OG  . SER A 1 231 ? 34.88500 21.42700  -16.54300 1.000 56.65549  ?  231 SER A OG  1 
ATOM   1527 N N   . PRO A 1 232 ? 35.75300 22.44000  -12.96000 1.000 54.13684  ?  232 PRO A N   1 
ATOM   1528 C CA  . PRO A 1 232 ? 35.13900 23.58100  -12.27000 1.000 54.20515  ?  232 PRO A CA  1 
ATOM   1529 C C   . PRO A 1 232 ? 34.59300 24.62200  -13.22200 1.000 54.18835  ?  232 PRO A C   1 
ATOM   1530 O O   . PRO A 1 232 ? 33.70400 25.39000  -12.83600 1.000 59.83905  ?  232 PRO A O   1 
ATOM   1531 C CB  . PRO A 1 232 ? 36.28900 24.13800  -11.42300 1.000 59.00868  ?  232 PRO A CB  1 
ATOM   1532 C CG  . PRO A 1 232 ? 37.25600 22.99300  -11.28800 1.000 56.72485  ?  232 PRO A CG  1 
ATOM   1533 C CD  . PRO A 1 232 ? 37.16600 22.25900  -12.58800 1.000 55.66510  ?  232 PRO A CD  1 
ATOM   1534 N N   . HIS A 1 233 ? 35.08100 24.66700  -14.46500 1.000 55.01896  ?  233 HIS A N   1 
ATOM   1535 C CA  . HIS A 1 233 ? 34.59400 25.66300  -15.41300 1.000 55.77857  ?  233 HIS A CA  1 
ATOM   1536 C C   . HIS A 1 233 ? 33.29100 25.22100  -16.06800 1.000 55.91876  ?  233 HIS A C   1 
ATOM   1537 O O   . HIS A 1 233 ? 32.40500 26.04800  -16.31700 1.000 53.71319  ?  233 HIS A O   1 
ATOM   1538 C CB  . HIS A 1 233 ? 35.64900 25.94600  -16.47700 1.000 54.26361  ?  233 HIS A CB  1 
ATOM   1539 C CG  . HIS A 1 233 ? 36.87600 26.61300  -15.94300 1.000 54.09741  ?  233 HIS A CG  1 
ATOM   1540 N ND1 . HIS A 1 233 ? 37.04700 27.98000  -15.95200 1.000 55.59723  ?  233 HIS A ND1 1 
ATOM   1541 C CD2 . HIS A 1 233 ? 38.00100 26.09700  -15.39400 1.000 57.91039  ?  233 HIS A CD2 1 
ATOM   1542 C CE1 . HIS A 1 233 ? 38.22400 28.27800  -15.42800 1.000 59.38730  ?  233 HIS A CE1 1 
ATOM   1543 N NE2 . HIS A 1 233 ? 38.82200 27.15300  -15.08100 1.000 61.36797  ?  233 HIS A NE2 1 
ATOM   1544 N N   . SER A 1 234 ? 33.15000 23.92300  -16.35000 1.000 54.25908  ?  234 SER A N   1 
ATOM   1545 C CA  . SER A 1 234 ? 32.01600 23.44600  -17.12900 1.000 51.57661  ?  234 SER A CA  1 
ATOM   1546 C C   . SER A 1 234 ? 31.36900 22.17700  -16.58200 1.000 51.76172  ?  234 SER A C   1 
ATOM   1547 O O   . SER A 1 234 ? 30.40100 21.70100  -17.18200 1.000 50.91019  ?  234 SER A O   1 
ATOM   1548 C CB  . SER A 1 234 ? 32.45400 23.21800  -18.58800 1.000 51.17523  ?  234 SER A CB  1 
ATOM   1549 O OG  . SER A 1 234 ? 33.15500 24.34400  -19.09700 1.000 49.91590  ?  234 SER A OG  1 
ATOM   1550 N N   . GLY A 1 235 ? 31.85000 21.62600  -15.46200 1.000 56.75026  ?  235 GLY A N   1 
ATOM   1551 C CA  . GLY A 1 235 ? 31.30000 20.37800  -14.95200 1.000 55.30405  ?  235 GLY A CA  1 
ATOM   1552 C C   . GLY A 1 235 ? 29.81700 20.43500  -14.64100 1.000 54.27961  ?  235 GLY A C   1 
ATOM   1553 O O   . GLY A 1 235 ? 29.10200 19.44600  -14.82800 1.000 52.83406  ?  235 GLY A O   1 
ATOM   1554 N N   . ASP A 1 236 ? 29.33200 21.57800  -14.16100 1.000 52.97079  ?  236 ASP A N   1 
ATOM   1555 C CA  . ASP A 1 236 ? 27.89800 21.72100  -13.93600 1.000 53.63426  ?  236 ASP A CA  1 
ATOM   1556 C C   . ASP A 1 236 ? 27.12400 21.65000  -15.24500 1.000 50.72754  ?  236 ASP A C   1 
ATOM   1557 O O   . ASP A 1 236 ? 26.06800 21.01200  -15.31200 1.000 53.39710  ?  236 ASP A O   1 
ATOM   1558 C CB  . ASP A 1 236 ? 27.61700 23.02700  -13.19500 1.000 56.75122  ?  236 ASP A CB  1 
ATOM   1559 C CG  . ASP A 1 236 ? 28.38600 24.19500  -13.76900 1.000 58.54689  ?  236 ASP A CG  1 
ATOM   1560 O OD1 . ASP A 1 236 ? 29.04900 24.01700  -14.81300 1.000 55.83810  ?  236 ASP A OD1 1 
ATOM   1561 O OD2 . ASP A 1 236 ? 28.34200 25.28600  -13.16100 1.000 60.61091  -1 236 ASP A OD2 1 
ATOM   1562 N N   . VAL A 1 237 ? 27.63000 22.29300  -16.29600 1.000 49.88447  ?  237 VAL A N   1 
ATOM   1563 C CA  . VAL A 1 237 ? 26.99500 22.16800  -17.60400 1.000 51.07279  ?  237 VAL A CA  1 
ATOM   1564 C C   . VAL A 1 237 ? 27.08900 20.72900  -18.09500 1.000 52.36181  ?  237 VAL A C   1 
ATOM   1565 O O   . VAL A 1 237 ? 26.08900 20.13000  -18.51000 1.000 51.67348  ?  237 VAL A O   1 
ATOM   1566 C CB  . VAL A 1 237 ? 27.62800 23.14800  -18.60600 1.000 49.59039  ?  237 VAL A CB  1 
ATOM   1567 C CG1 . VAL A 1 237 ? 27.01300 22.96300  -19.98500 1.000 46.37821  ?  237 VAL A CG1 1 
ATOM   1568 C CG2 . VAL A 1 237 ? 27.47700 24.57400  -18.12100 1.000 51.03822  ?  237 VAL A CG2 1 
ATOM   1569 N N   . LEU A 1 238 ? 28.29400 20.14900  -18.03500 1.000 50.11446  ?  238 LEU A N   1 
ATOM   1570 C CA  . LEU A 1 238 ? 28.50300 18.79500  -18.54500 1.000 48.34269  ?  238 LEU A CA  1 
ATOM   1571 C C   . LEU A 1 238 ? 27.60000 17.78900  -17.85100 1.000 49.95276  ?  238 LEU A C   1 
ATOM   1572 O O   . LEU A 1 238 ? 27.00400 16.92600  -18.50700 1.000 50.67911  ?  238 LEU A O   1 
ATOM   1573 C CB  . LEU A 1 238 ? 29.96600 18.38900  -18.37700 1.000 46.29255  ?  238 LEU A CB  1 
ATOM   1574 C CG  . LEU A 1 238 ? 31.00100 19.20000  -19.14400 1.000 47.15731  ?  238 LEU A CG  1 
ATOM   1575 C CD1 . LEU A 1 238 ? 32.39400 18.82300  -18.68800 1.000 48.66620  ?  238 LEU A CD1 1 
ATOM   1576 C CD2 . LEU A 1 238 ? 30.83000 18.95400  -20.62800 1.000 48.43618  ?  238 LEU A CD2 1 
ATOM   1577 N N   . TYR A 1 239 ? 27.48900 17.88100  -16.52500 1.000 50.38034  ?  239 TYR A N   1 
ATOM   1578 C CA  . TYR A 1 239 ? 26.62500 16.96800  -15.79000 1.000 51.40952  ?  239 TYR A CA  1 
ATOM   1579 C C   . TYR A 1 239 ? 25.19600 17.03500  -16.31000 1.000 55.97715  ?  239 TYR A C   1 
ATOM   1580 O O   . TYR A 1 239 ? 24.60400 16.00700  -16.65800 1.000 56.95658  ?  239 TYR A O   1 
ATOM   1581 C CB  . TYR A 1 239 ? 26.67100 17.29200  -14.29800 1.000 55.84238  ?  239 TYR A CB  1 
ATOM   1582 C CG  . TYR A 1 239 ? 25.73800 16.45600  -13.44700 1.000 57.00475  ?  239 TYR A CG  1 
ATOM   1583 C CD1 . TYR A 1 239 ? 26.14400 15.22600  -12.95000 1.000 57.85886  ?  239 TYR A CD1 1 
ATOM   1584 C CD2 . TYR A 1 239 ? 24.45200 16.89200  -13.14400 1.000 54.91048  ?  239 TYR A CD2 1 
ATOM   1585 C CE1 . TYR A 1 239 ? 25.30700 14.46000  -12.17100 1.000 56.25272  ?  239 TYR A CE1 1 
ATOM   1586 C CE2 . TYR A 1 239 ? 23.60300 16.12600  -12.36900 1.000 53.74589  ?  239 TYR A CE2 1 
ATOM   1587 C CZ  . TYR A 1 239 ? 24.04100 14.90900  -11.88600 1.000 55.01743  ?  239 TYR A CZ  1 
ATOM   1588 O OH  . TYR A 1 239 ? 23.22100 14.12500  -11.11100 1.000 56.48313  ?  239 TYR A OH  1 
ATOM   1589 N N   . GLU A 1 240 ? 24.62600 18.24400  -16.37900 1.000 51.88965  ?  240 GLU A N   1 
ATOM   1590 C CA  . GLU A 1 240 ? 23.24500 18.39100  -16.84200 1.000 52.97728  ?  240 GLU A CA  1 
ATOM   1591 C C   . GLU A 1 240 ? 23.08600 17.90100  -18.27300 1.000 52.15798  ?  240 GLU A C   1 
ATOM   1592 O O   . GLU A 1 240 ? 22.07400 17.27600  -18.61500 1.000 51.26780  ?  240 GLU A O   1 
ATOM   1593 C CB  . GLU A 1 240 ? 22.79400 19.84900  -16.71700 1.000 51.44989  ?  240 GLU A CB  1 
ATOM   1594 C CG  . GLU A 1 240 ? 22.98500 20.45600  -15.33100 1.000 53.66706  ?  240 GLU A CG  1 
ATOM   1595 C CD  . GLU A 1 240 ? 22.24000 19.70800  -14.23200 1.000 58.80671  ?  240 GLU A CD  1 
ATOM   1596 O OE1 . GLU A 1 240 ? 21.27200 18.97700  -14.53600 1.000 55.39472  ?  240 GLU A OE1 1 
ATOM   1597 O OE2 . GLU A 1 240 ? 22.66000 19.82100  -13.05800 1.000 65.91889  -1 240 GLU A OE2 1 
ATOM   1598 N N   . LEU A 1 241 ? 24.07700 18.18000  -19.12300 1.000 51.00474  ?  241 LEU A N   1 
ATOM   1599 C CA  . LEU A 1 241 ? 24.05600 17.67500  -20.49100 1.000 49.71724  ?  241 LEU A CA  1 
ATOM   1600 C C   . LEU A 1 241 ? 23.85500 16.16600  -20.52100 1.000 50.77718  ?  241 LEU A C   1 
ATOM   1601 O O   . LEU A 1 241 ? 23.01300 15.65200  -21.26700 1.000 49.89074  ?  241 LEU A O   1 
ATOM   1602 C CB  . LEU A 1 241 ? 25.35200 18.06400  -21.19600 1.000 47.48659  ?  241 LEU A CB  1 
ATOM   1603 C CG  . LEU A 1 241 ? 25.51500 17.46500  -22.58900 1.000 47.60042  ?  241 LEU A CG  1 
ATOM   1604 C CD1 . LEU A 1 241 ? 24.35300 17.84700  -23.49000 1.000 51.30815  ?  241 LEU A CD1 1 
ATOM   1605 C CD2 . LEU A 1 241 ? 26.82700 17.93000  -23.17700 1.000 47.62277  ?  241 LEU A CD2 1 
ATOM   1606 N N   . LEU A 1 242 ? 24.61400 15.44200  -19.69800 1.000 50.43299  ?  242 LEU A N   1 
ATOM   1607 C CA  . LEU A 1 242 ? 24.46700 13.99400  -19.64100 1.000 50.52271  ?  242 LEU A CA  1 
ATOM   1608 C C   . LEU A 1 242 ? 23.06100 13.59300  -19.20900 1.000 50.77025  ?  242 LEU A C   1 
ATOM   1609 O O   . LEU A 1 242 ? 22.50500 12.62000  -19.72900 1.000 52.94321  ?  242 LEU A O   1 
ATOM   1610 C CB  . LEU A 1 242 ? 25.51800 13.40600  -18.70300 1.000 49.75263  ?  242 LEU A CB  1 
ATOM   1611 C CG  . LEU A 1 242 ? 25.52600 11.88700  -18.57900 1.000 49.78250  ?  242 LEU A CG  1 
ATOM   1612 C CD1 . LEU A 1 242 ? 25.69200 11.25900  -19.95000 1.000 50.20711  ?  242 LEU A CD1 1 
ATOM   1613 C CD2 . LEU A 1 242 ? 26.64500 11.45300  -17.63800 1.000 53.49128  ?  242 LEU A CD2 1 
ATOM   1614 N N   . GLN A 1 243 ? 22.46400 14.33800  -18.27600 1.000 47.04505  ?  243 GLN A N   1 
ATOM   1615 C CA  . GLN A 1 243 ? 21.10800 14.02500  -17.83300 1.000 49.90250  ?  243 GLN A CA  1 
ATOM   1616 C C   . GLN A 1 243 ? 20.10500 14.14600  -18.97100 1.000 49.31243  ?  243 GLN A C   1 
ATOM   1617 O O   . GLN A 1 243 ? 19.20600 13.30900  -19.11100 1.000 50.83684  ?  243 GLN A O   1 
ATOM   1618 C CB  . GLN A 1 243 ? 20.70400 14.93800  -16.67500 1.000 52.07466  ?  243 GLN A CB  1 
ATOM   1619 C CG  . GLN A 1 243 ? 21.79300 15.17400  -15.65100 1.000 57.59066  ?  243 GLN A CG  1 
ATOM   1620 C CD  . GLN A 1 243 ? 22.39500 13.88900  -15.11700 1.000 60.90939  ?  243 GLN A CD  1 
ATOM   1621 O OE1 . GLN A 1 243 ? 21.70100 12.88700  -14.91800 1.000 59.59459  ?  243 GLN A OE1 1 
ATOM   1622 N NE2 . GLN A 1 243 ? 23.70700 13.90100  -14.92100 1.000 62.50525  ?  243 GLN A NE2 1 
ATOM   1623 N N   . HIS A 1 244 ? 20.24000 15.18400  -19.79300 1.000 50.19244  ?  244 HIS A N   1 
ATOM   1624 C CA  . HIS A 1 244 ? 19.32300 15.34900  -20.91000 1.000 47.11585  ?  244 HIS A CA  1 
ATOM   1625 C C   . HIS A 1 244 ? 19.50500 14.23500  -21.93600 1.000 55.65611  ?  244 HIS A C   1 
ATOM   1626 O O   . HIS A 1 244 ? 18.52500 13.76500  -22.52500 1.000 60.08632  ?  244 HIS A O   1 
ATOM   1627 C CB  . HIS A 1 244 ? 19.52100 16.72000  -21.55500 1.000 49.30164  ?  244 HIS A CB  1 
ATOM   1628 N N   . ILE A 1 245 ? 20.74500 13.78200  -22.14900 1.000 48.23390  ?  245 ILE A N   1 
ATOM   1629 C CA  . ILE A 1 245 ? 20.98200 12.69400  -23.09600 1.000 51.26644  ?  245 ILE A CA  1 
ATOM   1630 C C   . ILE A 1 245 ? 20.32900 11.40500  -22.60500 1.000 55.86417  ?  245 ILE A C   1 
ATOM   1631 O O   . ILE A 1 245 ? 19.79200 10.62200  -23.40300 1.000 58.88377  ?  245 ILE A O   1 
ATOM   1632 C CB  . ILE A 1 245 ? 22.49400 12.51300  -23.35700 1.000 52.35545  ?  245 ILE A CB  1 
ATOM   1633 C CG1 . ILE A 1 245 ? 23.11800 13.81300  -23.87000 1.000 47.24420  ?  245 ILE A CG1 1 
ATOM   1634 C CG2 . ILE A 1 245 ? 22.76200 11.40100  -24.35600 1.000 56.73492  ?  245 ILE A CG2 1 
ATOM   1635 N N   . LEU A 1 246 ? 20.36300 11.19200  -21.28600 1.000 58.88421  ?  246 LEU A N   1 
ATOM   1636 C CA  . LEU A 1 246 ? 19.76700 9.96400   -20.69200 1.000 55.96340  ?  246 LEU A CA  1 
ATOM   1637 C C   . LEU A 1 246 ? 18.25000 9.98000   -20.90100 1.000 60.81744  ?  246 LEU A C   1 
ATOM   1638 O O   . LEU A 1 246 ? 17.63500 8.90000   -20.82500 1.000 65.94600  ?  246 LEU A O   1 
ATOM   1639 C CB  . LEU A 1 246 ? 20.11000 9.92600   -19.20000 1.000 49.61426  ?  246 LEU A CB  1 
ATOM   1640 C CG  . LEU A 1 246 ? 21.59800 9.82000   -18.87400 1.000 51.30140  ?  246 LEU A CG  1 
ATOM   1641 C CD1 . LEU A 1 246 ? 21.81500 9.69900   -17.37400 1.000 53.80911  ?  246 LEU A CD1 1 
ATOM   1642 C CD2 . LEU A 1 246 ? 22.22200 8.63800   -19.59600 1.000 51.08591  ?  246 LEU A CD2 1 
ATOM   1643 N N   . GLY A 1 247 ? 17.67500 11.16000  -21.15000 1.000 58.66432  ?  247 GLY A N   1 
ATOM   1644 C CA  . GLY A 1 247 ? 16.21600 11.27600  -21.33900 1.000 59.81350  ?  247 GLY A CA  1 
ATOM   1645 C C   . GLY A 1 247 ? 15.86100 12.38200  -22.31700 1.000 66.93849  ?  247 GLY A C   1 
ATOM   1646 O O   . GLY A 1 247 ? 15.19000 13.33500  -21.87800 1.000 72.68164  ?  247 GLY A O   1 
ATOM   1647 N N   . LEU A 1 251 ? 12.87900 15.76800  -22.63800 1.000 68.52128  ?  251 LEU A N   1 
ATOM   1648 C CA  . LEU A 1 251 ? 11.51800 16.36500  -22.68400 1.000 70.75829  ?  251 LEU A CA  1 
ATOM   1649 C C   . LEU A 1 251 ? 10.59100 15.43600  -23.47200 1.000 73.40690  ?  251 LEU A C   1 
ATOM   1650 O O   . LEU A 1 251 ? 9.64800  14.89300  -22.86600 1.000 75.01145  ?  251 LEU A O   1 
ATOM   1651 C CB  . LEU A 1 251 ? 11.60300 17.74500  -23.34300 1.000 70.84256  ?  251 LEU A CB  1 
ATOM   1652 N N   . GLY A 1 252 ? 10.85300 15.26400  -24.77100 1.000 63.67731  ?  252 GLY A N   1 
ATOM   1653 C CA  . GLY A 1 252 ? 10.04500 14.33800  -25.58700 1.000 64.01808  ?  252 GLY A CA  1 
ATOM   1654 C C   . GLY A 1 252 ? 10.11200 12.93600  -25.01400 1.000 62.77476  ?  252 GLY A C   1 
ATOM   1655 O O   . GLY A 1 252 ? 9.07200  12.25200  -25.00600 1.000 65.20635  ?  252 GLY A O   1 
ATOM   1656 N N   . LYS A 1 253 ? 11.29200 12.52700  -24.54200 1.000 62.66682  ?  253 LYS A N   1 
ATOM   1657 C CA  . LYS A 1 253 ? 11.44500 11.19200  -23.90700 1.000 65.20507  ?  253 LYS A CA  1 
ATOM   1658 C C   . LYS A 1 253 ? 10.60400 11.15200  -22.62800 1.000 66.63859  ?  253 LYS A C   1 
ATOM   1659 O O   . LYS A 1 253 ? 9.91400  10.14000  -22.40800 1.000 68.34834  ?  253 LYS A O   1 
ATOM   1660 C CB  . LYS A 1 253 ? 12.91900 10.92100  -23.59700 1.000 63.20411  ?  253 LYS A CB  1 
ATOM   1661 N N   . LYS A 1 254 ? 10.65800 12.22100  -21.82900 1.000 62.72113  ?  254 LYS A N   1 
ATOM   1662 C CA  . LYS A 1 254 ? 9.86100  12.28400  -20.57600 1.000 56.26529  ?  254 LYS A CA  1 
ATOM   1663 C C   . LYS A 1 254 ? 8.39100  12.06500  -20.93300 1.000 61.04278  ?  254 LYS A C   1 
ATOM   1664 O O   . LYS A 1 254 ? 7.69800  11.35900  -20.17700 1.000 64.57082  ?  254 LYS A O   1 
ATOM   1665 C CB  . LYS A 1 254 ? 10.06400 13.63400  -19.88200 1.000 54.29643  ?  254 LYS A CB  1 
ATOM   1666 N N   . LEU A 1 255 ? 7.94200  12.64600  -22.04800 1.000 61.29332  ?  255 LEU A N   1 
ATOM   1667 C CA  . LEU A 1 255 ? 6.54400  12.43800  -22.50700 1.000 66.47554  ?  255 LEU A CA  1 
ATOM   1668 C C   . LEU A 1 255 ? 6.42800  11.02800  -23.09500 1.000 71.30333  ?  255 LEU A C   1 
ATOM   1669 O O   . LEU A 1 255 ? 5.39500  10.37300  -22.86300 1.000 74.61409  ?  255 LEU A O   1 
ATOM   1670 C CB  . LEU A 1 255 ? 6.20200  13.50300  -23.55200 1.000 67.75119  ?  255 LEU A CB  1 
ATOM   1671 N N   . LEU A 1 256 ? 7.45900  10.58900  -23.82200 1.000 76.68408  ?  256 LEU A N   1 
ATOM   1672 C CA  A LEU A 1 256 ? 7.35600  9.27000   -24.43600 0.580 77.98083  ?  256 LEU A CA  1 
ATOM   1673 C CA  B LEU A 1 256 ? 7.35600  9.27000   -24.43600 0.420 77.20360  ?  256 LEU A CA  1 
ATOM   1674 C C   . LEU A 1 256 ? 7.30900  8.16500   -23.38500 1.000 77.46803  ?  256 LEU A C   1 
ATOM   1675 O O   . LEU A 1 256 ? 6.63400  7.14100   -23.57500 1.000 79.14002  ?  256 LEU A O   1 
ATOM   1676 C CB  A LEU A 1 256 ? 8.52500  9.06800   -25.39000 0.580 77.44188  ?  256 LEU A CB  1 
ATOM   1677 C CB  B LEU A 1 256 ? 8.52400  9.06900   -25.39000 0.420 77.41842  ?  256 LEU A CB  1 
ATOM   1678 N N   . GLU A 1 257 ? 8.01000  8.35600   -22.26800 1.000 71.05346  ?  257 GLU A N   1 
ATOM   1679 C CA  . GLU A 1 257 ? 7.98300  7.36400   -21.19900 1.000 68.50588  ?  257 GLU A CA  1 
ATOM   1680 C C   . GLU A 1 257 ? 6.56300  7.05000   -20.73500 1.000 73.25654  ?  257 GLU A C   1 
ATOM   1681 O O   . GLU A 1 257 ? 6.31800  5.96400   -20.19400 1.000 71.66184  ?  257 GLU A O   1 
ATOM   1682 C CB  . GLU A 1 257 ? 8.83900  7.86500   -20.03400 1.000 60.40369  ?  257 GLU A CB  1 
ATOM   1683 N N   . ALA A 1 258 ? 5.61300  7.95800   -20.98600 1.000 70.51170  ?  258 ALA A N   1 
ATOM   1684 C CA  . ALA A 1 258 ? 4.20200  7.76600   -20.66200 1.000 69.80152  ?  258 ALA A CA  1 
ATOM   1685 C C   . ALA A 1 258 ? 3.59200  6.66300   -21.51600 1.000 73.20024  ?  258 ALA A C   1 
ATOM   1686 O O   . ALA A 1 258 ? 2.40600  6.34000   -21.37700 1.000 76.99297  ?  258 ALA A O   1 
ATOM   1687 C CB  . ALA A 1 258 ? 3.42300  9.07500   -20.82400 1.000 68.23723  ?  258 ALA A CB  1 
ATOM   1688 N N   . ALA A 1 259 ? 4.39700  6.08100   -22.40100 1.000 73.38505  ?  259 ALA A N   1 
ATOM   1689 C CA  . ALA A 1 259 ? 4.00200  4.86900   -23.10600 1.000 74.41026  ?  259 ALA A CA  1 
ATOM   1690 C C   . ALA A 1 259 ? 3.63700  3.73700   -22.15100 1.000 74.81592  ?  259 ALA A C   1 
ATOM   1691 O O   . ALA A 1 259 ? 2.87500  2.84000   -22.53500 1.000 77.17522  ?  259 ALA A O   1 
ATOM   1692 C CB  . ALA A 1 259 ? 5.13500  4.43100   -24.04500 1.000 74.52959  ?  259 ALA A CB  1 
ATOM   1693 N N   . ARG A 1 260 ? 4.16400  3.76000   -20.92200 1.000 72.03144  ?  260 ARG A N   1 
ATOM   1694 C CA  . ARG A 1 260 ? 3.66300  2.88000   -19.87300 1.000 77.03515  ?  260 ARG A CA  1 
ATOM   1695 C C   . ARG A 1 260 ? 2.14300  2.90900   -19.78600 1.000 81.80927  ?  260 ARG A C   1 
ATOM   1696 O O   . ARG A 1 260 ? 1.50900  1.85700   -19.65900 1.000 81.55086  ?  260 ARG A O   1 
ATOM   1697 C CB  . ARG A 1 260 ? 4.26300  3.28200   -18.52400 1.000 74.43664  ?  260 ARG A CB  1 
ATOM   1698 N N   . ALA A 1 261 ? 1.53900  4.10400   -19.83200 1.000 81.37778  ?  261 ALA A N   1 
ATOM   1699 C CA  . ALA A 1 261 ? 0.08600  4.21600   -19.73900 1.000 80.81836  ?  261 ALA A CA  1 
ATOM   1700 C C   . ALA A 1 261 ? -0.62900 3.52700   -20.89200 1.000 85.82690  ?  261 ALA A C   1 
ATOM   1701 O O   . ALA A 1 261 ? -1.83800 3.29100   -20.80000 1.000 89.57010  ?  261 ALA A O   1 
ATOM   1702 C CB  . ALA A 1 261 ? -0.33100 5.68700   -19.69800 1.000 79.65754  ?  261 ALA A CB  1 
ATOM   1703 N N   . GLY A 1 262 ? 0.08000  3.22500   -21.97500 1.000 92.29448  ?  262 GLY A N   1 
ATOM   1704 C CA  . GLY A 1 262 ? -0.51500 2.58800   -23.12500 1.000 92.07760  ?  262 GLY A CA  1 
ATOM   1705 C C   . GLY A 1 262 ? -1.04100 3.52100   -24.19200 1.000 96.59955  ?  262 GLY A C   1 
ATOM   1706 O O   . GLY A 1 262 ? -1.77600 3.06600   -25.07600 1.000 100.86883 ?  262 GLY A O   1 
ATOM   1707 N N   . GLN A 1 263 ? -0.69000 4.80700   -24.14200 1.000 97.20126  ?  263 GLN A N   1 
ATOM   1708 C CA  . GLN A 1 263 ? -1.10100 5.77600   -25.15700 1.000 99.67117  ?  263 GLN A CA  1 
ATOM   1709 C C   . GLN A 1 263 ? -0.26100 5.54000   -26.40900 1.000 102.21266 ?  263 GLN A C   1 
ATOM   1710 O O   . GLN A 1 263 ? 0.72600  6.22800   -26.68400 1.000 105.37493 ?  263 GLN A O   1 
ATOM   1711 C CB  . GLN A 1 263 ? -0.95400 7.19700   -24.63700 1.000 100.85340 ?  263 GLN A CB  1 
ATOM   1712 N N   . ASP A 1 264 ? -0.68000 4.53400   -27.18000 1.000 92.37565  ?  264 ASP A N   1 
ATOM   1713 C CA  . ASP A 1 264 ? 0.08300  4.10400   -28.34500 1.000 86.76912  ?  264 ASP A CA  1 
ATOM   1714 C C   . ASP A 1 264 ? 0.18700  5.22100   -29.37600 1.000 87.98659  ?  264 ASP A C   1 
ATOM   1715 O O   . ASP A 1 264 ? 1.27600  5.51400   -29.88700 1.000 87.45894  ?  264 ASP A O   1 
ATOM   1716 C CB  . ASP A 1 264 ? -0.56600 2.85600   -28.94700 1.000 80.79286  ?  264 ASP A CB  1 
ATOM   1717 N N   . ASP A 1 265 ? -0.93900 5.86600   -29.68400 1.000 89.39298  ?  265 ASP A N   1 
ATOM   1718 C CA  . ASP A 1 265 ? -0.91900 6.97300   -30.63600 1.000 86.91124  ?  265 ASP A CA  1 
ATOM   1719 C C   . ASP A 1 265 ? 0.03000  8.07800   -30.18100 1.000 88.57417  ?  265 ASP A C   1 
ATOM   1720 O O   . ASP A 1 265 ? 0.76000  8.65000   -30.99900 1.000 92.55405  ?  265 ASP A O   1 
ATOM   1721 C CB  . ASP A 1 265 ? -2.33500 7.51400   -30.83500 1.000 91.15975  ?  265 ASP A CB  1 
ATOM   1722 N N   . GLU A 1 266 ? 0.05100  8.38100   -28.87700 1.000 89.48636  ?  266 GLU A N   1 
ATOM   1723 C CA  . GLU A 1 266 ? 0.98700  9.38200   -28.36800 1.000 90.03636  ?  266 GLU A CA  1 
ATOM   1724 C C   . GLU A 1 266 ? 2.43600  8.91300   -28.46600 1.000 86.76916  ?  266 GLU A C   1 
ATOM   1725 O O   . GLU A 1 266 ? 3.34400  9.74000   -28.61500 1.000 84.82750  ?  266 GLU A O   1 
ATOM   1726 C CB  . GLU A 1 266 ? 0.64400  9.73900   -26.92000 1.000 90.21900  ?  266 GLU A CB  1 
ATOM   1727 N N   . VAL A 1 267 ? 2.67600  7.60000   -28.38100 1.000 85.44014  ?  267 VAL A N   1 
ATOM   1728 C CA  . VAL A 1 267 ? 4.03500  7.08400   -28.53600 1.000 84.50850  ?  267 VAL A CA  1 
ATOM   1729 C C   . VAL A 1 267 ? 4.49800  7.22700   -29.97900 1.000 82.93247  ?  267 VAL A C   1 
ATOM   1730 O O   . VAL A 1 267 ? 5.63700  7.63300   -30.24400 1.000 83.03507  ?  267 VAL A O   1 
ATOM   1731 C CB  . VAL A 1 267 ? 4.11500  5.62300   -28.05900 1.000 78.08878  ?  267 VAL A CB  1 
ATOM   1732 N N   . ARG A 1 268 ? 3.63200  6.88300   -30.93500 1.000 81.42503  ?  268 ARG A N   1 
ATOM   1733 C CA  . ARG A 1 268 ? 3.96500  7.08200   -32.34100 1.000 81.89730  ?  268 ARG A CA  1 
ATOM   1734 C C   . ARG A 1 268 ? 4.20000  8.55600   -32.63500 1.000 80.99202  ?  268 ARG A C   1 
ATOM   1735 O O   . ARG A 1 268 ? 5.18600  8.92400   -33.28400 1.000 81.31222  ?  268 ARG A O   1 
ATOM   1736 C CB  . ARG A 1 268 ? 2.85400  6.52200   -33.23000 1.000 82.35526  ?  268 ARG A CB  1 
ATOM   1737 C CG  . ARG A 1 268 ? 2.64700  5.01900   -33.12000 1.000 81.57019  ?  268 ARG A CG  1 
ATOM   1738 C CD  . ARG A 1 268 ? 1.49300  4.56300   -34.00300 1.000 82.92366  ?  268 ARG A CD  1 
ATOM   1739 N NE  . ARG A 1 268 ? 1.30100  3.11900   -33.96900 1.000 78.34190  ?  268 ARG A NE  1 
ATOM   1740 C CZ  . ARG A 1 268 ? 1.91100  2.26700   -34.78100 1.000 80.19583  ?  268 ARG A CZ  1 
ATOM   1741 N NH1 . ARG A 1 268 ? 2.76400  2.68400   -35.70500 1.000 78.27969  ?  268 ARG A NH1 1 
ATOM   1742 N NH2 . ARG A 1 268 ? 1.66000  0.96600   -34.66600 1.000 84.39118  ?  268 ARG A NH2 1 
ATOM   1743 N N   . ILE A 1 269 ? 3.30400  9.41800   -32.15000 1.000 82.81512  ?  269 ILE A N   1 
ATOM   1744 C CA  . ILE A 1 269 ? 3.45500  10.85300  -32.36600 1.000 86.18345  ?  269 ILE A CA  1 
ATOM   1745 C C   . ILE A 1 269 ? 4.76600  11.34600  -31.76900 1.000 88.34781  ?  269 ILE A C   1 
ATOM   1746 O O   . ILE A 1 269 ? 5.49100  12.13200  -32.39100 1.000 88.57161  ?  269 ILE A O   1 
ATOM   1747 C CB  . ILE A 1 269 ? 2.24400  11.60700  -31.78600 1.000 90.44967  ?  269 ILE A CB  1 
ATOM   1748 N N   . LEU A 1 270 ? 5.10600  10.87500  -30.56600 1.000 86.63934  ?  270 LEU A N   1 
ATOM   1749 C CA  . LEU A 1 270 ? 6.35300  11.29500  -29.93400 1.000 85.82268  ?  270 LEU A CA  1 
ATOM   1750 C C   . LEU A 1 270 ? 7.56300  10.81400  -30.72800 1.000 86.91474  ?  270 LEU A C   1 
ATOM   1751 O O   . LEU A 1 270 ? 8.49600  11.58300  -30.98800 1.000 85.70169  ?  270 LEU A O   1 
ATOM   1752 C CB  . LEU A 1 270 ? 6.40600  10.78900  -28.49000 1.000 82.98916  ?  270 LEU A CB  1 
ATOM   1753 N N   . MET A 1 271 ? 7.56300  9.54100   -31.13300 1.000 82.92610  ?  271 MET A N   1 
ATOM   1754 C CA  . MET A 1 271 ? 8.67900  9.01700   -31.91900 1.000 82.00413  ?  271 MET A CA  1 
ATOM   1755 C C   . MET A 1 271 ? 8.77300  9.69400   -33.27700 1.000 82.70134  ?  271 MET A C   1 
ATOM   1756 O O   . MET A 1 271 ? 9.87500  9.98400   -33.75900 1.000 84.71341  ?  271 MET A O   1 
ATOM   1757 C CB  . MET A 1 271 ? 8.55200  7.50500   -32.07900 1.000 73.93286  ?  271 MET A CB  1 
ATOM   1758 C CG  . MET A 1 271 ? 8.75600  6.74700   -30.79000 1.000 75.13420  ?  271 MET A CG  1 
ATOM   1759 S SD  . MET A 1 271 ? 8.54400  4.97700   -31.00800 1.000 83.50720  ?  271 MET A SD  1 
ATOM   1760 C CE  . MET A 1 271 ? 6.80200  4.90200   -31.42100 1.000 77.07887  ?  271 MET A CE  1 
ATOM   1761 N N   . ALA A 1 272 ? 7.62900  9.94200   -33.91500 1.000 81.53038  ?  272 ALA A N   1 
ATOM   1762 C CA  . ALA A 1 272 ? 7.63200  10.68900  -35.16900 1.000 82.61687  ?  272 ALA A CA  1 
ATOM   1763 C C   . ALA A 1 272 ? 8.29700  12.04700  -34.99400 1.000 85.90983  ?  272 ALA A C   1 
ATOM   1764 O O   . ALA A 1 272 ? 9.07600  12.48100  -35.84800 1.000 85.77895  ?  272 ALA A O   1 
ATOM   1765 C CB  . ALA A 1 272 ? 6.20100  10.85400  -35.67800 1.000 81.43989  ?  272 ALA A CB  1 
ATOM   1766 N N   . ASN A 1 273 ? 8.01400  12.72500  -33.88000 1.000 87.50605  ?  273 ASN A N   1 
ATOM   1767 C CA  . ASN A 1 273 ? 8.68500  13.98300  -33.58000 1.000 91.31879  ?  273 ASN A CA  1 
ATOM   1768 C C   . ASN A 1 273 ? 10.14800 13.77600  -33.21000 1.000 91.99279  ?  273 ASN A C   1 
ATOM   1769 O O   . ASN A 1 273 ? 10.91400 14.74600  -33.20100 1.000 89.24315  ?  273 ASN A O   1 
ATOM   1770 C CB  . ASN A 1 273 ? 7.95100  14.71600  -32.45300 1.000 93.72570  ?  273 ASN A CB  1 
ATOM   1771 C CG  . ASN A 1 273 ? 6.46300  14.89800  -32.73400 1.000 92.71374  ?  273 ASN A CG  1 
ATOM   1772 O OD1 . ASN A 1 273 ? 6.01400  14.76200  -33.87200 1.000 93.15728  ?  273 ASN A OD1 1 
ATOM   1773 N ND2 . ASN A 1 273 ? 5.68700  15.17500  -31.68900 1.000 95.36328  ?  273 ASN A ND2 1 
ATOM   1774 N N   . GLY A 1 274 ? 10.54300 12.54200  -32.91400 1.000 101.48099 ?  274 GLY A N   1 
ATOM   1775 C CA  . GLY A 1 274 ? 11.90500 12.24200  -32.52900 1.000 101.14079 ?  274 GLY A CA  1 
ATOM   1776 C C   . GLY A 1 274 ? 12.06500 12.14800  -31.02700 1.000 102.52312 ?  274 GLY A C   1 
ATOM   1777 O O   . GLY A 1 274 ? 11.81600 13.12000  -30.31000 1.000 112.40979 ?  274 GLY A O   1 
ATOM   1778 N N   . ALA A 1 275 ? 12.48700 10.98700  -30.54200 1.000 83.86189  ?  275 ALA A N   1 
ATOM   1779 C CA  . ALA A 1 275 ? 12.67800 10.79700  -29.11500 1.000 83.90559  ?  275 ALA A CA  1 
ATOM   1780 C C   . ALA A 1 275 ? 13.64300 9.64100   -28.90500 1.000 85.69406  ?  275 ALA A C   1 
ATOM   1781 O O   . ALA A 1 275 ? 13.73700 8.73700   -29.73900 1.000 88.34109  ?  275 ALA A O   1 
ATOM   1782 C CB  . ALA A 1 275 ? 11.34900 10.52800  -28.40400 1.000 82.84270  ?  275 ALA A CB  1 
ATOM   1783 N N   . ASP A 1 276 ? 14.36200 9.68400   -27.78800 1.000 82.48440  ?  276 ASP A N   1 
ATOM   1784 C CA  . ASP A 1 276 ? 15.28200 8.61300   -27.42700 1.000 81.09953  ?  276 ASP A CA  1 
ATOM   1785 C C   . ASP A 1 276 ? 14.44600 7.40600   -27.02700 1.000 79.96283  ?  276 ASP A C   1 
ATOM   1786 O O   . ASP A 1 276 ? 13.88100 7.36000   -25.93100 1.000 80.51724  ?  276 ASP A O   1 
ATOM   1787 C CB  . ASP A 1 276 ? 16.20200 9.06100   -26.29200 1.000 82.35550  ?  276 ASP A CB  1 
ATOM   1788 C CG  . ASP A 1 276 ? 17.15800 7.96900   -25.83400 1.000 88.46732  ?  276 ASP A CG  1 
ATOM   1789 O OD1 . ASP A 1 276 ? 17.22200 6.90500   -26.48400 1.000 89.40289  ?  276 ASP A OD1 1 
ATOM   1790 O OD2 . ASP A 1 276 ? 17.85200 8.17400   -24.81400 1.000 87.50221  -1 276 ASP A OD2 1 
ATOM   1791 N N   . VAL A 1 277 ? 14.34900 6.42500   -27.92500 1.000 69.88045  ?  277 VAL A N   1 
ATOM   1792 C CA  . VAL A 1 277 ? 13.59200 5.21500   -27.63000 1.000 70.75435  ?  277 VAL A CA  1 
ATOM   1793 C C   . VAL A 1 277 ? 14.21500 4.47500   -26.45600 1.000 73.04031  ?  277 VAL A C   1 
ATOM   1794 O O   . VAL A 1 277 ? 13.52800 3.73200   -25.74000 1.000 71.23178  ?  277 VAL A O   1 
ATOM   1795 C CB  . VAL A 1 277 ? 13.50400 4.32900   -28.88900 1.000 67.83907  ?  277 VAL A CB  1 
ATOM   1796 C CG1 . VAL A 1 277 ? 12.53100 3.17000   -28.67700 1.000 65.55462  ?  277 VAL A CG1 1 
ATOM   1797 C CG2 . VAL A 1 277 ? 13.11500 5.16800   -30.10700 1.000 71.66311  ?  277 VAL A CG2 1 
ATOM   1798 N N   . ASN A 1 278 ? 15.51300 4.66800   -26.23000 1.000 69.76366  ?  278 ASN A N   1 
ATOM   1799 C CA  . ASN A 1 278 ? 16.20900 4.10000   -25.07800 1.000 68.17781  ?  278 ASN A CA  1 
ATOM   1800 C C   . ASN A 1 278 ? 16.39500 5.12500   -23.97200 1.000 72.01385  ?  278 ASN A C   1 
ATOM   1801 O O   . ASN A 1 278 ? 17.44200 5.17600   -23.31900 1.000 74.65954  ?  278 ASN A O   1 
ATOM   1802 C CB  . ASN A 1 278 ? 17.54600 3.50600   -25.50100 1.000 65.60769  ?  278 ASN A CB  1 
ATOM   1803 C CG  . ASN A 1 278 ? 17.38600 2.40300   -26.51600 1.000 66.70774  ?  278 ASN A CG  1 
ATOM   1804 O OD1 . ASN A 1 278 ? 16.32700 2.26000   -27.11700 1.000 67.20535  ?  278 ASN A OD1 1 
ATOM   1805 N ND2 . ASN A 1 278 ? 18.43300 1.60900   -26.70800 1.000 65.21543  ?  278 ASN A ND2 1 
ATOM   1806 N N   . ALA A 1 279 ? 15.37600 5.94600   -23.74000 1.000 74.18446  ?  279 ALA A N   1 
ATOM   1807 C CA  . ALA A 1 279 ? 15.42200 6.92100   -22.66500 1.000 71.15665  ?  279 ALA A CA  1 
ATOM   1808 C C   . ALA A 1 279 ? 15.43000 6.21600   -21.31600 1.000 71.25652  ?  279 ALA A C   1 
ATOM   1809 O O   . ALA A 1 279 ? 15.14100 5.02600   -21.20300 1.000 76.15587  ?  279 ALA A O   1 
ATOM   1810 C CB  . ALA A 1 279 ? 14.23200 7.86900   -22.75100 1.000 72.91755  ?  279 ALA A CB  1 
ATOM   1811 N N   . THR A 1 280 ? 15.76400 6.97000   -20.27500 1.000 73.23922  ?  280 THR A N   1 
ATOM   1812 C CA  . THR A 1 280 ? 15.84900 6.41700   -18.93200 1.000 73.68655  ?  280 THR A CA  1 
ATOM   1813 C C   . THR A 1 280 ? 15.22300 7.39300   -17.94700 1.000 75.95736  ?  280 THR A C   1 
ATOM   1814 O O   . THR A 1 280 ? 15.59100 8.57100   -17.91700 1.000 77.66362  ?  280 THR A O   1 
ATOM   1815 C CB  . THR A 1 280 ? 17.30700 6.12700   -18.54800 1.000 73.89270  ?  280 THR A CB  1 
ATOM   1816 O OG1 . THR A 1 280 ? 18.07300 7.33300   -18.63500 1.000 77.78303  ?  280 THR A OG1 1 
ATOM   1817 C CG2 . THR A 1 280 ? 17.91100 5.07000   -19.47100 1.000 71.52403  ?  280 THR A CG2 1 
ATOM   1818 N N   . ASP A 1 281 ? 14.27100 6.90400   -17.15700 1.000 79.10262  ?  281 ASP A N   1 
ATOM   1819 C CA  . ASP A 1 281 ? 13.59900 7.72800   -16.16100 1.000 78.27099  ?  281 ASP A CA  1 
ATOM   1820 C C   . ASP A 1 281 ? 14.51500 7.93500   -14.95600 1.000 81.79764  ?  281 ASP A C   1 
ATOM   1821 O O   . ASP A 1 281 ? 15.69900 7.58600   -14.97300 1.000 79.29780  ?  281 ASP A O   1 
ATOM   1822 C CB  . ASP A 1 281 ? 12.26700 7.09900   -15.76300 1.000 77.92652  ?  281 ASP A CB  1 
ATOM   1823 C CG  . ASP A 1 281 ? 12.43500 5.82900   -14.94300 1.000 81.25503  ?  281 ASP A CG  1 
ATOM   1824 O OD1 . ASP A 1 281 ? 13.48900 5.16200   -15.04600 1.000 82.75847  ?  281 ASP A OD1 1 
ATOM   1825 O OD2 . ASP A 1 281 ? 11.51400 5.51900   -14.16000 1.000 84.64047  -1 281 ASP A OD2 1 
ATOM   1826 N N   . ASN A 1 282 ? 13.96100 8.50700   -13.88300 1.000 91.69412  ?  282 ASN A N   1 
ATOM   1827 C CA  . ASN A 1 282 ? 14.74300 8.75100   -12.67700 1.000 91.42628  ?  282 ASN A CA  1 
ATOM   1828 C C   . ASN A 1 282 ? 15.19300 7.45800   -12.01200 1.000 92.18062  ?  282 ASN A C   1 
ATOM   1829 O O   . ASN A 1 282 ? 16.15500 7.47700   -11.23700 1.000 95.29043  ?  282 ASN A O   1 
ATOM   1830 C CB  . ASN A 1 282 ? 13.93600 9.59200   -11.68600 1.000 87.67599  ?  282 ASN A CB  1 
ATOM   1831 N N   . ASP A 1 283 ? 14.52100 6.34200   -12.29400 1.000 88.43603  ?  283 ASP A N   1 
ATOM   1832 C CA  . ASP A 1 283 ? 14.90200 5.03600   -11.77700 1.000 85.99563  ?  283 ASP A CA  1 
ATOM   1833 C C   . ASP A 1 283 ? 15.60200 4.16800   -12.82000 1.000 81.53058  ?  283 ASP A C   1 
ATOM   1834 O O   . ASP A 1 283 ? 15.97500 3.03200   -12.51300 1.000 80.89828  ?  283 ASP A O   1 
ATOM   1835 C CB  . ASP A 1 283 ? 13.66900 4.31000   -11.22500 1.000 86.44283  ?  283 ASP A CB  1 
ATOM   1836 C CG  . ASP A 1 283 ? 12.93800 5.11700   -10.16000 1.000 92.45644  ?  283 ASP A CG  1 
ATOM   1837 O OD1 . ASP A 1 283 ? 13.42200 6.20900   -9.79200  1.000 94.47444  ?  283 ASP A OD1 1 
ATOM   1838 O OD2 . ASP A 1 283 ? 11.87500 4.65900   -9.69000  1.000 97.95209  -1 283 ASP A OD2 1 
ATOM   1839 N N   . GLY A 1 284 ? 15.79100 4.67300   -14.03800 1.000 81.74229  ?  284 GLY A N   1 
ATOM   1840 C CA  . GLY A 1 284 ? 16.56100 3.97100   -15.04500 1.000 77.16759  ?  284 GLY A CA  1 
ATOM   1841 C C   . GLY A 1 284 ? 15.75600 2.96900   -15.84200 1.000 78.63765  ?  284 GLY A C   1 
ATOM   1842 O O   . GLY A 1 284 ? 16.20700 1.84400   -16.07700 1.000 84.64336  ?  284 GLY A O   1 
ATOM   1843 N N   . TYR A 1 285 ? 14.56300 3.37300   -16.26900 1.000 74.15062  ?  285 TYR A N   1 
ATOM   1844 C CA  . TYR A 1 285 ? 13.66100 2.51600   -17.02400 1.000 76.16254  ?  285 TYR A CA  1 
ATOM   1845 C C   . TYR A 1 285 ? 13.42500 3.10100   -18.40700 1.000 73.86066  ?  285 TYR A C   1 
ATOM   1846 O O   . TYR A 1 285 ? 13.06000 4.27100   -18.53700 1.000 74.42806  ?  285 TYR A O   1 
ATOM   1847 C CB  . TYR A 1 285 ? 12.32800 2.34200   -16.29100 1.000 76.28743  ?  285 TYR A CB  1 
ATOM   1848 C CG  . TYR A 1 285 ? 12.45000 1.51600   -15.03600 1.000 82.91792  ?  285 TYR A CG  1 
ATOM   1849 C CD1 . TYR A 1 285 ? 12.72600 2.11000   -13.81200 1.000 84.64337  ?  285 TYR A CD1 1 
ATOM   1850 C CD2 . TYR A 1 285 ? 12.32100 0.13500   -15.07900 1.000 85.60741  ?  285 TYR A CD2 1 
ATOM   1851 C CE1 . TYR A 1 285 ? 12.85000 1.35100   -12.66100 1.000 90.36194  ?  285 TYR A CE1 1 
ATOM   1852 C CE2 . TYR A 1 285 ? 12.44600 -0.63100  -13.93600 1.000 90.06442  ?  285 TYR A CE2 1 
ATOM   1853 C CZ  . TYR A 1 285 ? 12.71100 -0.01900  -12.72900 1.000 94.94134  ?  285 TYR A CZ  1 
ATOM   1854 O OH  . TYR A 1 285 ? 12.83500 -0.78700  -11.59100 1.000 94.19429  ?  285 TYR A OH  1 
ATOM   1855 N N   . THR A 1 286 ? 13.62700 2.28100   -19.42800 1.000 74.45019  ?  286 THR A N   1 
ATOM   1856 C CA  . THR A 1 286 ? 13.30500 2.64300   -20.79600 1.000 73.68714  ?  286 THR A CA  1 
ATOM   1857 C C   . THR A 1 286 ? 11.79700 2.59100   -21.02400 1.000 71.81506  ?  286 THR A C   1 
ATOM   1858 O O   . THR A 1 286 ? 11.05900 2.01600   -20.22100 1.000 71.48220  ?  286 THR A O   1 
ATOM   1859 C CB  . THR A 1 286 ? 14.02100 1.70200   -21.76100 1.000 74.60462  ?  286 THR A CB  1 
ATOM   1860 O OG1 . THR A 1 286 ? 13.50500 0.37400   -21.60300 1.000 73.97320  ?  286 THR A OG1 1 
ATOM   1861 C CG2 . THR A 1 286 ? 15.52700 1.69600   -21.48900 1.000 74.59894  ?  286 THR A CG2 1 
ATOM   1862 N N   . PRO A 1 287 ? 11.30600 3.22800   -22.09100 1.000 71.23965  ?  287 PRO A N   1 
ATOM   1863 C CA  . PRO A 1 287 ? 9.91500  2.99000   -22.50700 1.000 69.54690  ?  287 PRO A CA  1 
ATOM   1864 C C   . PRO A 1 287 ? 9.57600  1.52200   -22.66800 1.000 68.01490  ?  287 PRO A C   1 
ATOM   1865 O O   . PRO A 1 287 ? 8.43400  1.12100   -22.40800 1.000 68.02219  ?  287 PRO A O   1 
ATOM   1866 C CB  . PRO A 1 287 ? 9.82900  3.73100   -23.84700 1.000 68.12812  ?  287 PRO A CB  1 
ATOM   1867 C CG  . PRO A 1 287 ? 10.81700 4.82800   -23.72400 1.000 73.76834  ?  287 PRO A CG  1 
ATOM   1868 C CD  . PRO A 1 287 ? 11.94700 4.29200   -22.88700 1.000 73.50971  ?  287 PRO A CD  1 
ATOM   1869 N N   . LEU A 1 288 ? 10.54000 0.70900   -23.10200 1.000 69.72354  ?  288 LEU A N   1 
ATOM   1870 C CA  . LEU A 1 288 ? 10.32600 -0.72800  -23.21600 1.000 65.04677  ?  288 LEU A CA  1 
ATOM   1871 C C   . LEU A 1 288 ? 10.03200 -1.35400  -21.85900 1.000 66.64723  ?  288 LEU A C   1 
ATOM   1872 O O   . LEU A 1 288 ? 9.05200  -2.09000  -21.70400 1.000 65.70497  ?  288 LEU A O   1 
ATOM   1873 C CB  . LEU A 1 288 ? 11.55300 -1.37500  -23.85000 1.000 62.05953  ?  288 LEU A CB  1 
ATOM   1874 C CG  . LEU A 1 288 ? 11.36200 -2.83200  -24.23700 1.000 60.07275  ?  288 LEU A CG  1 
ATOM   1875 C CD1 . LEU A 1 288 ? 10.13000 -2.95300  -25.11200 1.000 57.99370  ?  288 LEU A CD1 1 
ATOM   1876 C CD2 . LEU A 1 288 ? 12.59600 -3.35600  -24.95100 1.000 57.30851  ?  288 LEU A CD2 1 
ATOM   1877 N N   . HIS A 1 289 ? 10.88500 -1.08300  -20.86600 1.000 66.00593  ?  289 HIS A N   1 
ATOM   1878 C CA  . HIS A 1 289 ? 10.63800 -1.56400  -19.50900 1.000 67.20683  ?  289 HIS A CA  1 
ATOM   1879 C C   . HIS A 1 289 ? 9.21100  -1.27000  -19.07600 1.000 66.32977  ?  289 HIS A C   1 
ATOM   1880 O O   . HIS A 1 289 ? 8.49300  -2.15700  -18.60000 1.000 64.77571  ?  289 HIS A O   1 
ATOM   1881 C CB  . HIS A 1 289 ? 11.61500 -0.91000  -18.52600 1.000 70.55454  ?  289 HIS A CB  1 
ATOM   1882 C CG  . HIS A 1 289 ? 12.99000 -1.49600  -18.55000 1.000 73.40886  ?  289 HIS A CG  1 
ATOM   1883 N ND1 . HIS A 1 289 ? 14.01900 -0.95400  -19.28800 1.000 74.46372  ?  289 HIS A ND1 1 
ATOM   1884 C CD2 . HIS A 1 289 ? 13.50800 -2.57500  -17.91800 1.000 75.49358  ?  289 HIS A CD2 1 
ATOM   1885 C CE1 . HIS A 1 289 ? 15.11000 -1.67800  -19.11400 1.000 76.54597  ?  289 HIS A CE1 1 
ATOM   1886 N NE2 . HIS A 1 289 ? 14.82600 -2.66700  -18.28800 1.000 78.75866  ?  289 HIS A NE2 1 
ATOM   1887 N N   . LEU A 1 290 ? 8.78500  -0.01800  -19.24100 1.000 73.18290  ?  290 LEU A N   1 
ATOM   1888 C CA  . LEU A 1 290 ? 7.48000  0.40200   -18.74900 1.000 72.40231  ?  290 LEU A CA  1 
ATOM   1889 C C   . LEU A 1 290 ? 6.35500  -0.19500  -19.58300 1.000 75.15622  ?  290 LEU A C   1 
ATOM   1890 O O   . LEU A 1 290 ? 5.31000  -0.57700  -19.04300 1.000 75.27813  ?  290 LEU A O   1 
ATOM   1891 C CB  . LEU A 1 290 ? 7.39800  1.92400   -18.74700 1.000 67.44425  ?  290 LEU A CB  1 
ATOM   1892 C CG  . LEU A 1 290 ? 8.59400  2.65400   -18.13900 1.000 68.95481  ?  290 LEU A CG  1 
ATOM   1893 C CD1 . LEU A 1 290 ? 8.45400  4.14200   -18.35700 1.000 71.68063  ?  290 LEU A CD1 1 
ATOM   1894 C CD2 . LEU A 1 290 ? 8.71600  2.34300   -16.65900 1.000 70.07813  ?  290 LEU A CD2 1 
ATOM   1895 N N   . ALA A 1 291 ? 6.54600  -0.28100  -20.90100 1.000 68.88249  ?  291 ALA A N   1 
ATOM   1896 C CA  . ALA A 1 291 ? 5.50900  -0.84400  -21.75900 1.000 68.51369  ?  291 ALA A CA  1 
ATOM   1897 C C   . ALA A 1 291 ? 5.39500  -2.35000  -21.57000 1.000 69.68804  ?  291 ALA A C   1 
ATOM   1898 O O   . ALA A 1 291 ? 4.28900  -2.90300  -21.60900 1.000 71.89559  ?  291 ALA A O   1 
ATOM   1899 C CB  . ALA A 1 291 ? 5.79300  -0.50400  -23.22200 1.000 69.09055  ?  291 ALA A CB  1 
ATOM   1900 N N   . ALA A 1 292 ? 6.52500  -3.03100  -21.36200 1.000 69.75716  ?  292 ALA A N   1 
ATOM   1901 C CA  . ALA A 1 292 ? 6.49000  -4.47400  -21.14900 1.000 70.37570  ?  292 ALA A CA  1 
ATOM   1902 C C   . ALA A 1 292 ? 5.83700  -4.81900  -19.81800 1.000 70.69210  ?  292 ALA A C   1 
ATOM   1903 O O   . ALA A 1 292 ? 5.09900  -5.80600  -19.72000 1.000 71.26996  ?  292 ALA A O   1 
ATOM   1904 C CB  . ALA A 1 292 ? 7.90400  -5.05100  -21.21500 1.000 68.50786  ?  292 ALA A CB  1 
ATOM   1905 N N   . SER A 1 293 ? 6.09600  -4.01800  -18.78300 1.000 69.28007  ?  293 SER A N   1 
ATOM   1906 C CA  A SER A 1 293 ? 5.51700  -4.29200  -17.47500 0.420 70.13670  ?  293 SER A CA  1 
ATOM   1907 C CA  B SER A 1 293 ? 5.51700  -4.29200  -17.47500 0.330 70.32323  ?  293 SER A CA  1 
ATOM   1908 C CA  C SER A 1 293 ? 5.51900  -4.27300  -17.46900 0.250 73.36838  ?  293 SER A CA  1 
ATOM   1909 C C   . SER A 1 293 ? 4.01800  -4.02600  -17.43700 1.000 70.16660  ?  293 SER A C   1 
ATOM   1910 O O   . SER A 1 293 ? 3.32700  -4.58000  -16.57700 1.000 74.06333  ?  293 SER A O   1 
ATOM   1911 C CB  A SER A 1 293 ? 6.22100  -3.46000  -16.40100 0.420 71.80128  ?  293 SER A CB  1 
ATOM   1912 C CB  B SER A 1 293 ? 6.22100  -3.45900  -16.40200 0.330 74.00131  ?  293 SER A CB  1 
ATOM   1913 C CB  C SER A 1 293 ? 6.20000  -3.39700  -16.41700 0.250 72.58560  ?  293 SER A CB  1 
ATOM   1914 O OG  A SER A 1 293 ? 6.11000  -2.07400  -16.67000 0.420 72.05020  ?  293 SER A OG  1 
ATOM   1915 O OG  B SER A 1 293 ? 6.11200  -2.07300  -16.67500 0.330 72.03716  ?  293 SER A OG  1 
ATOM   1916 O OG  C SER A 1 293 ? 7.60600  -3.41200  -16.57300 0.250 71.64796  ?  293 SER A OG  1 
ATOM   1917 N N   . ASN A 1 294 ? 3.50100  -3.20200  -18.34600 1.000 70.10515  ?  294 ASN A N   1 
ATOM   1918 C CA  . ASN A 1 294 ? 2.08800  -2.85300  -18.36700 1.000 72.05900  ?  294 ASN A CA  1 
ATOM   1919 C C   . ASN A 1 294 ? 1.32100  -3.53900  -19.49300 1.000 75.97919  ?  294 ASN A C   1 
ATOM   1920 O O   . ASN A 1 294 ? 0.15700  -3.20000  -19.73100 1.000 76.57606  ?  294 ASN A O   1 
ATOM   1921 C CB  . ASN A 1 294 ? 1.93300  -1.33300  -18.46200 1.000 76.05710  ?  294 ASN A CB  1 
ATOM   1922 C CG  . ASN A 1 294 ? 2.70100  -0.59800  -17.37400 1.000 76.69527  ?  294 ASN A CG  1 
ATOM   1923 O OD1 . ASN A 1 294 ? 3.43300  -1.20500  -16.59100 1.000 75.48188  ?  294 ASN A OD1 1 
ATOM   1924 N ND2 . ASN A 1 294 ? 2.54800  0.71900   -17.33200 1.000 78.58514  ?  294 ASN A ND2 1 
ATOM   1925 N N   . GLY A 1 295 ? 1.93900  -4.49200  -20.18500 1.000 83.56331  ?  295 GLY A N   1 
ATOM   1926 C CA  . GLY A 1 295 ? 1.24700  -5.26300  -21.20100 1.000 83.01866  ?  295 GLY A CA  1 
ATOM   1927 C C   . GLY A 1 295 ? 0.78100  -4.45600  -22.39400 1.000 84.80722  ?  295 GLY A C   1 
ATOM   1928 O O   . GLY A 1 295 ? -0.42100 -4.35500  -22.65300 1.000 91.33676  ?  295 GLY A O   1 
ATOM   1929 N N   . HIS A 1 296 ? 1.72500  -3.87400  -23.13300 1.000 75.70223  ?  296 HIS A N   1 
ATOM   1930 C CA  . HIS A 1 296 ? 1.42400  -3.10100  -24.33900 1.000 75.32836  ?  296 HIS A CA  1 
ATOM   1931 C C   . HIS A 1 296 ? 2.26900  -3.67800  -25.46800 1.000 73.50531  ?  296 HIS A C   1 
ATOM   1932 O O   . HIS A 1 296 ? 3.28700  -3.09900  -25.85700 1.000 71.23291  ?  296 HIS A O   1 
ATOM   1933 C CB  . HIS A 1 296 ? 1.68900  -1.61800  -24.12100 1.000 77.72047  ?  296 HIS A CB  1 
ATOM   1934 C CG  . HIS A 1 296 ? 0.94600  -1.04300  -22.95800 1.000 81.21165  ?  296 HIS A CG  1 
ATOM   1935 N ND1 . HIS A 1 296 ? -0.42700 -1.10500  -22.85100 1.000 83.03861  ?  296 HIS A ND1 1 
ATOM   1936 C CD2 . HIS A 1 296 ? 1.38100  -0.39900  -21.85000 1.000 79.52229  ?  296 HIS A CD2 1 
ATOM   1937 C CE1 . HIS A 1 296 ? -0.80500 -0.52400  -21.72700 1.000 80.73952  ?  296 HIS A CE1 1 
ATOM   1938 N NE2 . HIS A 1 296 ? 0.27300  -0.08500  -21.10200 1.000 80.46735  ?  296 HIS A NE2 1 
ATOM   1939 N N   . LEU A 1 297 ? 1.84200  -4.83300  -25.98600 1.000 75.07530  ?  297 LEU A N   1 
ATOM   1940 C CA  . LEU A 1 297 ? 2.58800  -5.48200  -27.05800 1.000 71.24180  ?  297 LEU A CA  1 
ATOM   1941 C C   . LEU A 1 297 ? 2.71700  -4.56500  -28.26800 1.000 69.81935  ?  297 LEU A C   1 
ATOM   1942 O O   . LEU A 1 297 ? 3.77100  -4.52500  -28.91400 1.000 69.65374  ?  297 LEU A O   1 
ATOM   1943 C CB  . LEU A 1 297 ? 1.91900  -6.80200  -27.44600 1.000 64.66580  ?  297 LEU A CB  1 
ATOM   1944 N N   . GLU A 1 298 ? 1.66000  -3.81300  -28.58300 1.000 68.27213  ?  298 GLU A N   1 
ATOM   1945 C CA  . GLU A 1 298 ? 1.75600  -2.82600  -29.65400 1.000 69.16988  ?  298 GLU A CA  1 
ATOM   1946 C C   . GLU A 1 298 ? 2.89100  -1.84500  -29.38700 1.000 68.52463  ?  298 GLU A C   1 
ATOM   1947 O O   . GLU A 1 298 ? 3.67300  -1.52700  -30.29000 1.000 68.79523  ?  298 GLU A O   1 
ATOM   1948 C CB  . GLU A 1 298 ? 0.42400  -2.08900  -29.81000 1.000 69.66159  ?  298 GLU A CB  1 
ATOM   1949 N N   . ILE A 1 299 ? 3.01100  -1.37500  -28.14300 1.000 69.24953  ?  299 ILE A N   1 
ATOM   1950 C CA  . ILE A 1 299 ? 4.11000  -0.48500  -27.78600 1.000 68.06849  ?  299 ILE A CA  1 
ATOM   1951 C C   . ILE A 1 299 ? 5.42000  -1.26200  -27.68300 1.000 66.64323  ?  299 ILE A C   1 
ATOM   1952 O O   . ILE A 1 299 ? 6.46800  -0.79600  -28.15100 1.000 66.19609  ?  299 ILE A O   1 
ATOM   1953 C CB  . ILE A 1 299 ? 3.78700  0.27200   -26.48300 1.000 66.38215  ?  299 ILE A CB  1 
ATOM   1954 N N   . VAL A 1 300 ? 5.38400  -2.46100  -27.08900 1.000 68.85693  ?  300 VAL A N   1 
ATOM   1955 C CA  . VAL A 1 300 ? 6.59100  -3.27100  -26.94300 1.000 65.83553  ?  300 VAL A CA  1 
ATOM   1956 C C   . VAL A 1 300 ? 7.19000  -3.66500  -28.28800 1.000 68.64196  ?  300 VAL A C   1 
ATOM   1957 O O   . VAL A 1 300 ? 8.39000  -3.95000  -28.37000 1.000 65.15559  ?  300 VAL A O   1 
ATOM   1958 C CB  . VAL A 1 300 ? 6.28800  -4.53100  -26.10100 1.000 57.52824  ?  300 VAL A CB  1 
ATOM   1959 N N   . GLU A 1 301 ? 6.38200  -3.70100  -29.34800 1.000 72.07659  ?  301 GLU A N   1 
ATOM   1960 C CA  . GLU A 1 301 ? 6.88300  -4.04300  -30.67500 1.000 71.50618  ?  301 GLU A CA  1 
ATOM   1961 C C   . GLU A 1 301 ? 7.31900  -2.81800  -31.47100 1.000 72.04600  ?  301 GLU A C   1 
ATOM   1962 O O   . GLU A 1 301 ? 8.32400  -2.88100  -32.19200 1.000 72.12768  ?  301 GLU A O   1 
ATOM   1963 C CB  . GLU A 1 301 ? 5.82500  -4.82400  -31.45800 1.000 69.99301  ?  301 GLU A CB  1 
ATOM   1964 C CG  . GLU A 1 301 ? 5.55900  -6.22100  -30.92700 1.000 72.59701  ?  301 GLU A CG  1 
ATOM   1965 C CD  . GLU A 1 301 ? 4.28900  -6.82000  -31.48900 1.000 76.32936  ?  301 GLU A CD  1 
ATOM   1966 O OE1 . GLU A 1 301 ? 3.63000  -6.14400  -32.30500 1.000 76.21578  ?  301 GLU A OE1 1 
ATOM   1967 O OE2 . GLU A 1 301 ? 3.93800  -7.95500  -31.10400 1.000 78.69043  -1 301 GLU A OE2 1 
ATOM   1968 N N   . VAL A 1 302 ? 6.59000  -1.70400  -31.36500 1.000 67.49082  ?  302 VAL A N   1 
ATOM   1969 C CA  . VAL A 1 302 ? 6.95700  -0.51900  -32.13300 1.000 64.89920  ?  302 VAL A CA  1 
ATOM   1970 C C   . VAL A 1 302 ? 8.24600  0.08900   -31.59400 1.000 65.95388  ?  302 VAL A C   1 
ATOM   1971 O O   . VAL A 1 302 ? 9.06200  0.61900   -32.35900 1.000 67.04020  ?  302 VAL A O   1 
ATOM   1972 C CB  . VAL A 1 302 ? 5.79800  0.50000   -32.15500 1.000 63.87133  ?  302 VAL A CB  1 
ATOM   1973 C CG1 . VAL A 1 302 ? 5.49200  1.01300   -30.76300 1.000 66.77247  ?  302 VAL A CG1 1 
ATOM   1974 C CG2 . VAL A 1 302 ? 6.13200  1.66100   -33.08000 1.000 66.40107  ?  302 VAL A CG2 1 
ATOM   1975 N N   . LEU A 1 303 ? 8.46700  0.00100   -30.27900 1.000 61.79124  ?  303 LEU A N   1 
ATOM   1976 C CA  . LEU A 1 303 ? 9.70700  0.52100   -29.71000 1.000 61.88904  ?  303 LEU A CA  1 
ATOM   1977 C C   . LEU A 1 303 ? 10.90700 -0.27800  -30.19700 1.000 60.63213  ?  303 LEU A C   1 
ATOM   1978 O O   . LEU A 1 303 ? 11.94700 0.29600   -30.54200 1.000 63.44331  ?  303 LEU A O   1 
ATOM   1979 C CB  . LEU A 1 303 ? 9.63400  0.51600   -28.18400 1.000 63.39736  ?  303 LEU A CB  1 
ATOM   1980 C CG  . LEU A 1 303 ? 8.58300  1.43000   -27.54700 1.000 66.91946  ?  303 LEU A CG  1 
ATOM   1981 C CD1 . LEU A 1 303 ? 8.49300  1.18500   -26.04400 1.000 66.01022  ?  303 LEU A CD1 1 
ATOM   1982 C CD2 . LEU A 1 303 ? 8.88700  2.89300   -27.85300 1.000 64.47971  ?  303 LEU A CD2 1 
ATOM   1983 N N   . LEU A 1 304 ? 10.77600 -1.60500  -30.24900 1.000 63.68547  ?  304 LEU A N   1 
ATOM   1984 C CA  . LEU A 1 304 ? 11.86000 -2.44000  -30.76000 1.000 60.71839  ?  304 LEU A CA  1 
ATOM   1985 C C   . LEU A 1 304 ? 12.14900 -2.14100  -32.22500 1.000 60.57862  ?  304 LEU A C   1 
ATOM   1986 O O   . LEU A 1 304 ? 13.31500 -2.03600  -32.62500 1.000 59.06347  ?  304 LEU A O   1 
ATOM   1987 C CB  . LEU A 1 304 ? 11.50500 -3.91200  -30.57500 1.000 56.10996  ?  304 LEU A CB  1 
ATOM   1988 C CG  . LEU A 1 304 ? 11.46200 -4.37600  -29.12500 1.000 51.51410  ?  304 LEU A CG  1 
ATOM   1989 C CD1 . LEU A 1 304 ? 11.00600 -5.81400  -29.07500 1.000 52.11443  ?  304 LEU A CD1 1 
ATOM   1990 C CD2 . LEU A 1 304 ? 12.82200 -4.20400  -28.45900 1.000 53.54827  ?  304 LEU A CD2 1 
ATOM   1991 N N   . LYS A 1 305 ? 11.10100 -2.00000  -33.04000 1.000 58.71361  ?  305 LYS A N   1 
ATOM   1992 C CA  . LYS A 1 305 ? 11.29900 -1.69900  -34.45400 1.000 57.41419  ?  305 LYS A CA  1 
ATOM   1993 C C   . LYS A 1 305 ? 11.98400 -0.35100  -34.64000 1.000 55.46105  ?  305 LYS A C   1 
ATOM   1994 O O   . LYS A 1 305 ? 12.82100 -0.19400  -35.53500 1.000 54.12192  ?  305 LYS A O   1 
ATOM   1995 C CB  . LYS A 1 305 ? 9.96100  -1.72600  -35.19300 1.000 58.35401  ?  305 LYS A CB  1 
ATOM   1996 N N   . ASN A 1 306 ? 11.64400 0.63200   -33.80400 1.000 58.73490  ?  306 ASN A N   1 
ATOM   1997 C CA  . ASN A 1 306 ? 12.23000 1.96700   -33.86600 1.000 62.10619  ?  306 ASN A CA  1 
ATOM   1998 C C   . ASN A 1 306 ? 13.56100 2.07700   -33.12300 1.000 59.71698  ?  306 ASN A C   1 
ATOM   1999 O O   . ASN A 1 306 ? 14.07300 3.18900   -32.95900 1.000 60.77532  ?  306 ASN A O   1 
ATOM   2000 C CB  . ASN A 1 306 ? 11.24100 3.00800   -33.32600 1.000 62.16084  ?  306 ASN A CB  1 
ATOM   2001 C CG  . ASN A 1 306 ? 9.91400  2.98900   -34.06700 1.000 65.70083  ?  306 ASN A CG  1 
ATOM   2002 O OD1 . ASN A 1 306 ? 9.69500  2.15800   -34.94600 1.000 67.68258  ?  306 ASN A OD1 1 
ATOM   2003 N ND2 . ASN A 1 306 ? 9.02000  3.90300   -33.70900 1.000 72.54921  ?  306 ASN A ND2 1 
ATOM   2004 N N   . GLY A 1 307 ? 14.13300 0.95400   -32.68800 1.000 57.40027  ?  307 GLY A N   1 
ATOM   2005 C CA  . GLY A 1 307 ? 15.42100 0.95300   -32.02300 1.000 57.17117  ?  307 GLY A CA  1 
ATOM   2006 C C   . GLY A 1 307 ? 15.33500 1.01400   -30.50900 1.000 59.11954  ?  307 GLY A C   1 
ATOM   2007 O O   . GLY A 1 307 ? 15.60600 2.06000   -29.91400 1.000 61.84724  ?  307 GLY A O   1 
ATOM   2008 N N   . ALA A 1 308 ? 14.96100 -0.09600  -29.87600 1.000 59.44391  ?  308 ALA A N   1 
ATOM   2009 C CA  . ALA A 1 308 ? 14.89700 -0.19100  -28.42600 1.000 56.52886  ?  308 ALA A CA  1 
ATOM   2010 C C   . ALA A 1 308 ? 15.81700 -1.30400  -27.95900 1.000 54.69240  ?  308 ALA A C   1 
ATOM   2011 O O   . ALA A 1 308 ? 15.84300 -2.38500  -28.55300 1.000 55.52094  ?  308 ALA A O   1 
ATOM   2012 C CB  . ALA A 1 308 ? 13.47300 -0.46100  -27.93700 1.000 58.33509  ?  308 ALA A CB  1 
ATOM   2013 N N   . ASP A 1 309 ? 16.57700 -1.03300  -26.90500 1.000 54.39649  ?  309 ASP A N   1 
ATOM   2014 C CA  . ASP A 1 309 ? 17.46700 -2.03000  -26.32500 1.000 52.97311  ?  309 ASP A CA  1 
ATOM   2015 C C   . ASP A 1 309 ? 16.62200 -3.10000  -25.65100 1.000 56.76604  ?  309 ASP A C   1 
ATOM   2016 O O   . ASP A 1 309 ? 16.12100 -2.90600  -24.54200 1.000 57.74419  ?  309 ASP A O   1 
ATOM   2017 C CB  . ASP A 1 309 ? 18.42600 -1.36700  -25.34000 1.000 55.42101  ?  309 ASP A CB  1 
ATOM   2018 C CG  . ASP A 1 309 ? 19.61500 -2.23900  -25.00400 1.000 56.43586  ?  309 ASP A CG  1 
ATOM   2019 O OD1 . ASP A 1 309 ? 19.41800 -3.40900  -24.61700 1.000 58.75067  ?  309 ASP A OD1 1 
ATOM   2020 O OD2 . ASP A 1 309 ? 20.75700 -1.75500  -25.14600 1.000 60.91595  -1 309 ASP A OD2 1 
ATOM   2021 N N   . VAL A 1 310 ? 16.45200 -4.23500  -26.33400 1.000 53.29117  ?  310 VAL A N   1 
ATOM   2022 C CA  . VAL A 1 310 ? 15.64200 -5.32300  -25.80000 1.000 55.66838  ?  310 VAL A CA  1 
ATOM   2023 C C   . VAL A 1 310 ? 16.25200 -5.88700  -24.52700 1.000 61.49499  ?  310 VAL A C   1 
ATOM   2024 O O   . VAL A 1 310 ? 15.54300 -6.48800  -23.71300 1.000 61.57759  ?  310 VAL A O   1 
ATOM   2025 C CB  . VAL A 1 310 ? 15.45600 -6.41600  -26.87400 1.000 45.48432  ?  310 VAL A CB  1 
ATOM   2026 N N   . ASN A 1 311 ? 17.55700 -5.68800  -24.32700 1.000 57.40018  ?  311 ASN A N   1 
ATOM   2027 C CA  . ASN A 1 311 ? 18.27500 -6.14200  -23.14300 1.000 61.86120  ?  311 ASN A CA  1 
ATOM   2028 C C   . ASN A 1 311 ? 18.67900 -4.99300  -22.22800 1.000 66.01794  ?  311 ASN A C   1 
ATOM   2029 O O   . ASN A 1 311 ? 19.63300 -5.13100  -21.45500 1.000 67.56616  ?  311 ASN A O   1 
ATOM   2030 C CB  . ASN A 1 311 ? 19.50700 -6.94500  -23.55600 1.000 59.24870  ?  311 ASN A CB  1 
ATOM   2031 C CG  . ASN A 1 311 ? 19.14400 -8.17600  -24.33100 1.000 61.26496  ?  311 ASN A CG  1 
ATOM   2032 O OD1 . ASN A 1 311 ? 17.99600 -8.33700  -24.73200 1.000 62.74951  ?  311 ASN A OD1 1 
ATOM   2033 N ND2 . ASN A 1 311 ? 20.10900 -9.06100  -24.54100 1.000 65.45116  ?  311 ASN A ND2 1 
ATOM   2034 N N   . ALA A 1 312 ? 17.97300 -3.86600  -22.30000 1.000 67.77769  ?  312 ALA A N   1 
ATOM   2035 C CA  . ALA A 1 312 ? 18.33000 -2.70600  -21.49700 1.000 66.49504  ?  312 ALA A CA  1 
ATOM   2036 C C   . ALA A 1 312 ? 18.38300 -3.07000  -20.02200 1.000 70.57143  ?  312 ALA A C   1 
ATOM   2037 O O   . ALA A 1 312 ? 17.54100 -3.82000  -19.51900 1.000 71.96654  ?  312 ALA A O   1 
ATOM   2038 C CB  . ALA A 1 312 ? 17.32300 -1.57700  -21.72500 1.000 69.63115  ?  312 ALA A CB  1 
ATOM   2039 N N   . SER A 1 313 ? 19.39100 -2.54100  -19.33600 1.000 71.88618  ?  313 SER A N   1 
ATOM   2040 C CA  . SER A 1 313 ? 19.66800 -2.87700  -17.94500 1.000 77.17607  ?  313 SER A CA  1 
ATOM   2041 C C   . SER A 1 313 ? 19.13400 -1.76200  -17.05700 1.000 83.25937  ?  313 SER A C   1 
ATOM   2042 O O   . SER A 1 313 ? 19.66900 -0.64800  -17.05800 1.000 86.54894  ?  313 SER A O   1 
ATOM   2043 C CB  . SER A 1 313 ? 21.16400 -3.07900  -17.71900 1.000 77.59813  ?  313 SER A CB  1 
ATOM   2044 N N   . ASP A 1 314 ? 18.07500 -2.05900  -16.31100 1.000 89.06888  ?  314 ASP A N   1 
ATOM   2045 C CA  . ASP A 1 314 ? 17.60100 -1.12900  -15.30200 1.000 89.27891  ?  314 ASP A CA  1 
ATOM   2046 C C   . ASP A 1 314 ? 18.68800 -0.91000  -14.25200 1.000 89.30790  ?  314 ASP A C   1 
ATOM   2047 O O   . ASP A 1 314 ? 19.64800 -1.67900  -14.14300 1.000 87.99119  ?  314 ASP A O   1 
ATOM   2048 C CB  . ASP A 1 314 ? 16.31900 -1.65700  -14.65700 1.000 88.23659  ?  314 ASP A CB  1 
ATOM   2049 C CG  . ASP A 1 314 ? 15.85000 -0.80300  -13.50700 1.000 91.42439  ?  314 ASP A CG  1 
ATOM   2050 O OD1 . ASP A 1 314 ? 15.84700 0.43600   -13.65500 1.000 92.41371  ?  314 ASP A OD1 1 
ATOM   2051 O OD2 . ASP A 1 314 ? 15.50300 -1.37100  -12.45000 1.000 92.30978  -1 314 ASP A OD2 1 
ATOM   2052 N N   . LEU A 1 315 ? 18.54000 0.17600   -13.48900 1.000 83.73166  ?  315 LEU A N   1 
ATOM   2053 C CA  . LEU A 1 315 ? 19.46200 0.44400   -12.39200 1.000 82.96148  ?  315 LEU A CA  1 
ATOM   2054 C C   . LEU A 1 315 ? 19.63200 -0.77300  -11.49000 1.000 82.74960  ?  315 LEU A C   1 
ATOM   2055 O O   . LEU A 1 315 ? 20.72200 -1.00100  -10.95400 1.000 82.66050  ?  315 LEU A O   1 
ATOM   2056 C CB  . LEU A 1 315 ? 18.97300 1.64800   -11.58500 1.000 80.33570  ?  315 LEU A CB  1 
ATOM   2057 N N   . THR A 1 316 ? 18.58100 -1.57300  -11.32700 1.000 81.95173  ?  316 THR A N   1 
ATOM   2058 C CA  . THR A 1 316 ? 18.65900 -2.81500  -10.57100 1.000 83.60114  ?  316 THR A CA  1 
ATOM   2059 C C   . THR A 1 316 ? 19.09100 -3.99600  -11.43000 1.000 85.30813  ?  316 THR A C   1 
ATOM   2060 O O   . THR A 1 316 ? 18.93800 -5.14300  -11.00300 1.000 88.91569  ?  316 THR A O   1 
ATOM   2061 C CB  . THR A 1 316 ? 17.30900 -3.12800  -9.91900  1.000 80.32565  ?  316 THR A CB  1 
ATOM   2062 O OG1 . THR A 1 316 ? 16.32600 -3.35500  -10.93500 1.000 84.06925  ?  316 THR A OG1 1 
ATOM   2063 C CG2 . THR A 1 316 ? 16.85500 -1.96300  -9.05900  1.000 78.59152  ?  316 THR A CG2 1 
ATOM   2064 N N   . GLY A 1 317 ? 19.62600 -3.74400  -12.62400 1.000 83.99638  ?  317 GLY A N   1 
ATOM   2065 C CA  . GLY A 1 317 ? 19.96100 -4.80400  -13.55000 1.000 85.49979  ?  317 GLY A CA  1 
ATOM   2066 C C   . GLY A 1 317 ? 18.77600 -5.47600  -14.20500 1.000 83.01464  ?  317 GLY A C   1 
ATOM   2067 O O   . GLY A 1 317 ? 18.96900 -6.44200  -14.95400 1.000 82.55102  ?  317 GLY A O   1 
ATOM   2068 N N   . ILE A 1 318 ? 17.55900 -4.99800  -13.95100 1.000 81.72600  ?  318 ILE A N   1 
ATOM   2069 C CA  . ILE A 1 318 ? 16.36800 -5.61300  -14.51900 1.000 79.64339  ?  318 ILE A CA  1 
ATOM   2070 C C   . ILE A 1 318 ? 16.29000 -5.30200  -16.00800 1.000 80.53102  ?  318 ILE A C   1 
ATOM   2071 O O   . ILE A 1 318 ? 16.49100 -4.15700  -16.43300 1.000 81.83586  ?  318 ILE A O   1 
ATOM   2072 C CB  . ILE A 1 318 ? 15.11500 -5.12300  -13.77700 1.000 76.03949  ?  318 ILE A CB  1 
ATOM   2073 C CG1 . ILE A 1 318 ? 15.00000 -5.81400  -12.41600 1.000 76.17696  ?  318 ILE A CG1 1 
ATOM   2074 C CG2 . ILE A 1 318 ? 13.86700 -5.35000  -14.61200 1.000 76.02832  ?  318 ILE A CG2 1 
ATOM   2075 N N   . THR A 1 319 ? 16.00500 -6.32900  -16.81100 1.000 75.66074  ?  319 THR A N   1 
ATOM   2076 C CA  . THR A 1 319 ? 15.80000 -6.20800  -18.24300 1.000 70.75739  ?  319 THR A CA  1 
ATOM   2077 C C   . THR A 1 319 ? 14.31400 -6.11700  -18.56400 1.000 68.97306  ?  319 THR A C   1 
ATOM   2078 O O   . THR A 1 319 ? 13.46400 -6.42400  -17.72000 1.000 69.23517  ?  319 THR A O   1 
ATOM   2079 C CB  . THR A 1 319 ? 16.41300 -7.41000  -18.96900 1.000 70.25045  ?  319 THR A CB  1 
ATOM   2080 O OG1 . THR A 1 319 ? 15.66600 -8.58700  -18.64100 1.000 71.85469  ?  319 THR A OG1 1 
ATOM   2081 C CG2 . THR A 1 319 ? 17.86200 -7.61200  -18.53400 1.000 71.87440  ?  319 THR A CG2 1 
ATOM   2082 N N   . PRO A 1 320 ? 13.95700 -5.66900  -19.77200 1.000 65.29288  ?  320 PRO A N   1 
ATOM   2083 C CA  . PRO A 1 320 ? 12.53900 -5.70800  -20.16700 1.000 62.86657  ?  320 PRO A CA  1 
ATOM   2084 C C   . PRO A 1 320 ? 11.91700 -7.08500  -20.02600 1.000 60.44147  ?  320 PRO A C   1 
ATOM   2085 O O   . PRO A 1 320 ? 10.74600 -7.19800  -19.64800 1.000 61.47601  ?  320 PRO A O   1 
ATOM   2086 C CB  . PRO A 1 320 ? 12.58200 -5.25100  -21.62900 1.000 61.17025  ?  320 PRO A CB  1 
ATOM   2087 C CG  . PRO A 1 320 ? 13.76400 -4.33800  -21.68600 1.000 64.58376  ?  320 PRO A CG  1 
ATOM   2088 C CD  . PRO A 1 320 ? 14.78300 -4.94500  -20.75500 1.000 65.57603  ?  320 PRO A CD  1 
ATOM   2089 N N   . LEU A 1 321 ? 12.67700 -8.13800  -20.33000 1.000 64.04051  ?  321 LEU A N   1 
ATOM   2090 C CA  . LEU A 1 321 ? 12.19300 -9.49700  -20.12100 1.000 62.47160  ?  321 LEU A CA  1 
ATOM   2091 C C   . LEU A 1 321 ? 11.94500 -9.76900  -18.64200 1.000 70.28024  ?  321 LEU A C   1 
ATOM   2092 O O   . LEU A 1 321 ? 10.89600 -10.30800 -18.26600 1.000 70.31608  ?  321 LEU A O   1 
ATOM   2093 C CB  . LEU A 1 321 ? 13.19900 -10.49200 -20.69900 1.000 59.11056  ?  321 LEU A CB  1 
ATOM   2094 C CG  . LEU A 1 321 ? 12.82100 -11.95600 -20.50100 1.000 54.59156  ?  321 LEU A CG  1 
ATOM   2095 C CD1 . LEU A 1 321 ? 11.48500 -12.23000 -21.15800 1.000 53.93709  ?  321 LEU A CD1 1 
ATOM   2096 C CD2 . LEU A 1 321 ? 13.89500 -12.88700 -21.04600 1.000 61.69335  ?  321 LEU A CD2 1 
ATOM   2097 N N   . HIS A 1 322 ? 12.90900 -9.40300  -17.78900 1.000 65.16744  ?  322 HIS A N   1 
ATOM   2098 C CA  . HIS A 1 322 ? 12.73200 -9.52700  -16.34300 1.000 65.89958  ?  322 HIS A CA  1 
ATOM   2099 C C   . HIS A 1 322 ? 11.41200 -8.92000  -15.89000 1.000 66.11940  ?  322 HIS A C   1 
ATOM   2100 O O   . HIS A 1 322 ? 10.71900 -9.48200  -15.03300 1.000 67.92174  ?  322 HIS A O   1 
ATOM   2101 C CB  . HIS A 1 322 ? 13.89600 -8.85100  -15.61100 1.000 69.44720  ?  322 HIS A CB  1 
ATOM   2102 C CG  . HIS A 1 322 ? 15.11700 -9.70600  -15.46900 1.000 72.89428  ?  322 HIS A CG  1 
ATOM   2103 N ND1 . HIS A 1 322 ? 16.17500 -9.65300  -16.35200 1.000 73.88518  ?  322 HIS A ND1 1 
ATOM   2104 C CD2 . HIS A 1 322 ? 15.46100 -10.61100 -14.52300 1.000 74.64713  ?  322 HIS A CD2 1 
ATOM   2105 C CE1 . HIS A 1 322 ? 17.10700 -10.50700 -15.96800 1.000 74.35182  ?  322 HIS A CE1 1 
ATOM   2106 N NE2 . HIS A 1 322 ? 16.70100 -11.09800 -14.85900 1.000 74.00054  ?  322 HIS A NE2 1 
ATOM   2107 N N   . ALA A 1 323 ? 11.05700 -7.76400  -16.45400 1.000 65.27593  ?  323 ALA A N   1 
ATOM   2108 C CA  . ALA A 1 323 ? 9.80000  -7.10700  -16.11900 1.000 65.32877  ?  323 ALA A CA  1 
ATOM   2109 C C   . ALA A 1 323 ? 8.60700  -7.87600  -16.67400 1.000 70.84467  ?  323 ALA A C   1 
ATOM   2110 O O   . ALA A 1 323 ? 7.65700  -8.18100  -15.94300 1.000 69.84023  ?  323 ALA A O   1 
ATOM   2111 C CB  . ALA A 1 323 ? 9.80800  -5.67700  -16.65500 1.000 68.99470  ?  323 ALA A CB  1 
ATOM   2112 N N   . ALA A 1 324 ? 8.63300  -8.18400  -17.97300 1.000 66.50691  ?  324 ALA A N   1 
ATOM   2113 C CA  . ALA A 1 324 ? 7.50800  -8.87800  -18.59200 1.000 68.76959  ?  324 ALA A CA  1 
ATOM   2114 C C   . ALA A 1 324 ? 7.30400  -10.26400 -17.99800 1.000 70.95112  ?  324 ALA A C   1 
ATOM   2115 O O   . ALA A 1 324 ? 6.16700  -10.74300 -17.91800 1.000 72.70710  ?  324 ALA A O   1 
ATOM   2116 C CB  . ALA A 1 324 ? 7.71500  -8.97600  -20.10300 1.000 68.26193  ?  324 ALA A CB  1 
ATOM   2117 N N   . ALA A 1 325 ? 8.38600  -10.92400 -17.58100 1.000 71.68748  ?  325 ALA A N   1 
ATOM   2118 C CA  . ALA A 1 325 ? 8.25300  -12.24400 -16.97400 1.000 68.43805  ?  325 ALA A CA  1 
ATOM   2119 C C   . ALA A 1 325 ? 7.50500  -12.16100 -15.65000 1.000 68.37396  ?  325 ALA A C   1 
ATOM   2120 O O   . ALA A 1 325 ? 6.58700  -12.94800 -15.39300 1.000 69.85014  ?  325 ALA A O   1 
ATOM   2121 C CB  . ALA A 1 325 ? 9.63200  -12.87400 -16.77800 1.000 65.18440  ?  325 ALA A CB  1 
ATOM   2122 N N   . ALA A 1 326 ? 7.87900  -11.20300 -14.80000 1.000 66.65876  ?  326 ALA A N   1 
ATOM   2123 C CA  . ALA A 1 326 ? 7.22700  -11.07300 -13.50200 1.000 70.95533  ?  326 ALA A CA  1 
ATOM   2124 C C   . ALA A 1 326 ? 5.78700  -10.59900 -13.65200 1.000 71.02345  ?  326 ALA A C   1 
ATOM   2125 O O   . ALA A 1 326 ? 4.89500  -11.07400 -12.94000 1.000 73.29893  ?  326 ALA A O   1 
ATOM   2126 C CB  . ALA A 1 326 ? 8.02000  -10.11800 -12.61000 1.000 67.18571  ?  326 ALA A CB  1 
ATOM   2127 N N   . THR A 1 327 ? 5.54000  -9.67000  -14.57300 1.000 68.94696  ?  327 THR A N   1 
ATOM   2128 C CA  . THR A 1 327 ? 4.19000  -9.17500  -14.80700 1.000 71.64250  ?  327 THR A CA  1 
ATOM   2129 C C   . THR A 1 327 ? 3.32500  -10.16200 -15.58400 1.000 76.90387  ?  327 THR A C   1 
ATOM   2130 O O   . THR A 1 327 ? 2.14300  -9.87900  -15.81100 1.000 78.15610  ?  327 THR A O   1 
ATOM   2131 C CB  . THR A 1 327 ? 4.24000  -7.82800  -15.53700 1.000 70.82634  ?  327 THR A CB  1 
ATOM   2132 O OG1 . THR A 1 327 ? 4.88700  -7.98600  -16.80600 1.000 72.46694  ?  327 THR A OG1 1 
ATOM   2133 C CG2 . THR A 1 327 ? 5.00200  -6.80100  -14.71100 1.000 68.84361  ?  327 THR A CG2 1 
ATOM   2134 N N   . GLY A 1 328 ? 3.87900  -11.30400 -15.99100 1.000 83.50167  ?  328 GLY A N   1 
ATOM   2135 C CA  . GLY A 1 328 ? 3.09500  -12.34500 -16.62600 1.000 83.36283  ?  328 GLY A CA  1 
ATOM   2136 C C   . GLY A 1 328 ? 2.63800  -12.04900 -18.03400 1.000 82.19799  ?  328 GLY A C   1 
ATOM   2137 O O   . GLY A 1 328 ? 1.64100  -12.61900 -18.48300 1.000 84.95456  ?  328 GLY A O   1 
ATOM   2138 N N   . HIS A 1 329 ? 3.33400  -11.17000 -18.74900 1.000 73.69282  ?  329 HIS A N   1 
ATOM   2139 C CA  . HIS A 1 329 ? 2.96200  -10.82300 -20.11900 1.000 70.98448  ?  329 HIS A CA  1 
ATOM   2140 C C   . HIS A 1 329 ? 3.74100  -11.73200 -21.05600 1.000 67.22823  ?  329 HIS A C   1 
ATOM   2141 O O   . HIS A 1 329 ? 4.81500  -11.38600 -21.54900 1.000 64.35219  ?  329 HIS A O   1 
ATOM   2142 C CB  . HIS A 1 329 ? 3.22200  -9.34800  -20.38300 1.000 69.94806  ?  329 HIS A CB  1 
ATOM   2143 C CG  . HIS A 1 329 ? 2.39900  -8.44300  -19.52400 1.000 70.50979  ?  329 HIS A CG  1 
ATOM   2144 N ND1 . HIS A 1 329 ? 2.94900  -7.60000  -18.58400 1.000 70.68013  ?  329 HIS A ND1 1 
ATOM   2145 C CD2 . HIS A 1 329 ? 1.05900  -8.25900  -19.45700 1.000 70.82749  ?  329 HIS A CD2 1 
ATOM   2146 C CE1 . HIS A 1 329 ? 1.98400  -6.93300  -17.97700 1.000 71.56971  ?  329 HIS A CE1 1 
ATOM   2147 N NE2 . HIS A 1 329 ? 0.82800  -7.31400  -18.48900 1.000 71.92646  ?  329 HIS A NE2 1 
ATOM   2148 N N   . LEU A 1 330 ? 3.18200  -12.92000 -21.29500 1.000 63.49212  ?  330 LEU A N   1 
ATOM   2149 C CA  . LEU A 1 330 ? 3.89100  -13.93200 -22.06700 1.000 60.91839  ?  330 LEU A CA  1 
ATOM   2150 C C   . LEU A 1 330 ? 4.10400  -13.48400 -23.50500 1.000 57.37889  ?  330 LEU A C   1 
ATOM   2151 O O   . LEU A 1 330 ? 5.17800  -13.70800 -24.07800 1.000 56.35831  ?  330 LEU A O   1 
ATOM   2152 C CB  . LEU A 1 330 ? 3.12600  -15.25600 -22.01900 1.000 61.11046  ?  330 LEU A CB  1 
ATOM   2153 N N   . GLU A 1 331 ? 3.09500  -12.85100 -24.10700 1.000 56.90201  ?  331 GLU A N   1 
ATOM   2154 C CA  . GLU A 1 331 ? 3.23500  -12.39400 -25.48400 1.000 55.30266  ?  331 GLU A CA  1 
ATOM   2155 C C   . GLU A 1 331 ? 4.41500  -11.43800 -25.62400 1.000 62.78268  ?  331 GLU A C   1 
ATOM   2156 O O   . GLU A 1 331 ? 5.19900  -11.54400 -26.57300 1.000 58.42018  ?  331 GLU A O   1 
ATOM   2157 C CB  . GLU A 1 331 ? 1.93500  -11.74200 -25.95400 1.000 53.71089  ?  331 GLU A CB  1 
ATOM   2158 N N   . ILE A 1 332 ? 4.57300  -10.51700 -24.66800 1.000 63.91940  ?  332 ILE A N   1 
ATOM   2159 C CA  . ILE A 1 332 ? 5.73500  -9.63100  -24.66400 1.000 60.55000  ?  332 ILE A CA  1 
ATOM   2160 C C   . ILE A 1 332 ? 7.01300  -10.42900 -24.43200 1.000 58.37014  ?  332 ILE A C   1 
ATOM   2161 O O   . ILE A 1 332 ? 8.06900  -10.11700 -24.99600 1.000 55.54198  ?  332 ILE A O   1 
ATOM   2162 C CB  . ILE A 1 332 ? 5.55400  -8.52700  -23.60500 1.000 62.89120  ?  332 ILE A CB  1 
ATOM   2163 C CG1 . ILE A 1 332 ? 4.25600  -7.75500  -23.85300 1.000 61.97669  ?  332 ILE A CG1 1 
ATOM   2164 C CG2 . ILE A 1 332 ? 6.74800  -7.58400  -23.60100 1.000 66.68104  ?  332 ILE A CG2 1 
ATOM   2165 N N   . VAL A 1 333 ? 6.93300  -11.47300 -23.60200 1.000 61.26883  ?  333 VAL A N   1 
ATOM   2166 C CA  . VAL A 1 333 ? 8.08900  -12.32800 -23.33600 1.000 58.07484  ?  333 VAL A CA  1 
ATOM   2167 C C   . VAL A 1 333 ? 8.55300  -13.01300 -24.61400 1.000 55.22922  ?  333 VAL A C   1 
ATOM   2168 O O   . VAL A 1 333 ? 9.74600  -13.02000 -24.94300 1.000 51.23251  ?  333 VAL A O   1 
ATOM   2169 C CB  . VAL A 1 333 ? 7.74800  -13.35500 -22.24400 1.000 55.95958  ?  333 VAL A CB  1 
ATOM   2170 C CG1 . VAL A 1 333 ? 8.76800  -14.47400 -22.23700 1.000 58.34263  ?  333 VAL A CG1 1 
ATOM   2171 C CG2 . VAL A 1 333 ? 7.68800  -12.68100 -20.88600 1.000 60.19378  ?  333 VAL A CG2 1 
ATOM   2172 N N   . GLU A 1 334 ? 7.61400  -13.61400 -25.34700 1.000 51.59795  ?  334 GLU A N   1 
ATOM   2173 C CA  . GLU A 1 334 ? 7.95900  -14.24800 -26.61300 1.000 53.44828  ?  334 GLU A CA  1 
ATOM   2174 C C   . GLU A 1 334 ? 8.54000  -13.23700 -27.59500 1.000 52.72449  ?  334 GLU A C   1 
ATOM   2175 O O   . GLU A 1 334 ? 9.48500  -13.54800 -28.32900 1.000 53.16146  ?  334 GLU A O   1 
ATOM   2176 C CB  . GLU A 1 334 ? 6.72700  -14.93700 -27.20400 1.000 52.32382  ?  334 GLU A CB  1 
ATOM   2177 N N   . VAL A 1 335 ? 7.99900  -12.01500 -27.61000 1.000 55.46349  ?  335 VAL A N   1 
ATOM   2178 C CA  . VAL A 1 335 ? 8.48700  -10.98900 -28.53000 1.000 55.42572  ?  335 VAL A CA  1 
ATOM   2179 C C   . VAL A 1 335 ? 9.92100  -10.60600 -28.19300 1.000 54.71504  ?  335 VAL A C   1 
ATOM   2180 O O   . VAL A 1 335 ? 10.79300 -10.56600 -29.06900 1.000 55.55264  ?  335 VAL A O   1 
ATOM   2181 C CB  . VAL A 1 335 ? 7.56000  -9.76000  -28.50800 1.000 54.87642  ?  335 VAL A CB  1 
ATOM   2182 C CG1 . VAL A 1 335 ? 8.23800  -8.57100  -29.17600 1.000 54.60801  ?  335 VAL A CG1 1 
ATOM   2183 C CG2 . VAL A 1 335 ? 6.24800  -10.07400 -29.20000 1.000 54.94163  ?  335 VAL A CG2 1 
ATOM   2184 N N   . LEU A 1 336 ? 10.18100 -10.30100 -26.92000 1.000 50.94822  ?  336 LEU A N   1 
ATOM   2185 C CA  . LEU A 1 336 ? 11.53100 -9.92600  -26.51300 1.000 51.86154  ?  336 LEU A CA  1 
ATOM   2186 C C   . LEU A 1 336 ? 12.51900 -11.04300 -26.81900 1.000 51.65996  ?  336 LEU A C   1 
ATOM   2187 O O   . LEU A 1 336 ? 13.59600 -10.79900 -27.37400 1.000 54.15693  ?  336 LEU A O   1 
ATOM   2188 C CB  . LEU A 1 336 ? 11.54200 -9.56300  -25.02700 1.000 51.31507  ?  336 LEU A CB  1 
ATOM   2189 C CG  . LEU A 1 336 ? 10.67900 -8.35100  -24.65000 1.000 51.99992  ?  336 LEU A CG  1 
ATOM   2190 C CD1 . LEU A 1 336 ? 10.51900 -8.24000  -23.14800 1.000 56.17101  ?  336 LEU A CD1 1 
ATOM   2191 C CD2 . LEU A 1 336 ? 11.28700 -7.07500  -25.20100 1.000 51.58618  ?  336 LEU A CD2 1 
ATOM   2192 N N   . LEU A 1 337 ? 12.15500 -12.28500 -26.49200 1.000 51.00695  ?  337 LEU A N   1 
ATOM   2193 C CA  . LEU A 1 337 ? 13.00700 -13.41200 -26.85200 1.000 54.35979  ?  337 LEU A CA  1 
ATOM   2194 C C   . LEU A 1 337 ? 13.15300 -13.52800 -28.36300 1.000 55.26637  ?  337 LEU A C   1 
ATOM   2195 O O   . LEU A 1 337 ? 14.23000 -13.86600 -28.86800 1.000 54.91422  ?  337 LEU A O   1 
ATOM   2196 C CB  . LEU A 1 337 ? 12.44100 -14.70000 -26.26600 1.000 54.00483  ?  337 LEU A CB  1 
ATOM   2197 C CG  . LEU A 1 337 ? 12.36200 -14.75700 -24.74600 1.000 54.91161  ?  337 LEU A CG  1 
ATOM   2198 C CD1 . LEU A 1 337 ? 11.45800 -15.90100 -24.35100 1.000 58.22367  ?  337 LEU A CD1 1 
ATOM   2199 C CD2 . LEU A 1 337 ? 13.74300 -14.91500 -24.13600 1.000 57.30935  ?  337 LEU A CD2 1 
ATOM   2200 N N   . LYS A 1 338 ? 12.07900 -13.24600 -29.10200 1.000 52.70257  ?  338 LYS A N   1 
ATOM   2201 C CA  . LYS A 1 338 ? 12.14300 -13.28000 -30.56000 1.000 53.26439  ?  338 LYS A CA  1 
ATOM   2202 C C   . LYS A 1 338 ? 13.04000 -12.17600 -31.10200 1.000 51.41138  ?  338 LYS A C   1 
ATOM   2203 O O   . LYS A 1 338 ? 13.78800 -12.39100 -32.06200 1.000 50.22212  ?  338 LYS A O   1 
ATOM   2204 C CB  . LYS A 1 338 ? 10.73400 -13.15800 -31.13800 1.000 54.99029  ?  338 LYS A CB  1 
ATOM   2205 C CG  . LYS A 1 338 ? 10.62900 -13.31600 -32.64100 1.000 57.29814  ?  338 LYS A CG  1 
ATOM   2206 C CD  . LYS A 1 338 ? 9.22400  -12.93800 -33.09500 1.000 59.62819  ?  338 LYS A CD  1 
ATOM   2207 C CE  . LYS A 1 338 ? 8.70500  -13.87400 -34.17900 1.000 53.52777  ?  338 LYS A CE  1 
ATOM   2208 N NZ  . LYS A 1 338 ? 7.36100  -13.46900 -34.69000 1.000 47.87252  ?  338 LYS A NZ  1 
ATOM   2209 N N   . HIS A 1 339 ? 12.97600 -10.99000 -30.50500 1.000 51.89846  ?  339 HIS A N   1 
ATOM   2210 C CA  . HIS A 1 339 ? 13.79400 -9.86000  -30.91900 1.000 55.58855  ?  339 HIS A CA  1 
ATOM   2211 C C   . HIS A 1 339 ? 15.09800 -9.76700  -30.13900 1.000 57.81419  ?  339 HIS A C   1 
ATOM   2212 O O   . HIS A 1 339 ? 15.68400 -8.68300  -30.05500 1.000 61.10940  ?  339 HIS A O   1 
ATOM   2213 C CB  . HIS A 1 339 ? 13.00000 -8.56100  -30.78700 1.000 53.25439  ?  339 HIS A CB  1 
ATOM   2214 C CG  . HIS A 1 339 ? 11.82800 -8.48600  -31.71300 1.000 54.69080  ?  339 HIS A CG  1 
ATOM   2215 N ND1 . HIS A 1 339 ? 10.66700 -9.19900  -31.50200 1.000 57.25144  ?  339 HIS A ND1 1 
ATOM   2216 C CD2 . HIS A 1 339 ? 11.63800 -7.78700  -32.85600 1.000 51.55326  ?  339 HIS A CD2 1 
ATOM   2217 C CE1 . HIS A 1 339 ? 9.81300  -8.94500  -32.47800 1.000 57.10298  ?  339 HIS A CE1 1 
ATOM   2218 N NE2 . HIS A 1 339 ? 10.37700 -8.08900  -33.31200 1.000 55.02063  ?  339 HIS A NE2 1 
ATOM   2219 N N   . GLY A 1 340 ? 15.55700 -10.87700 -29.57000 1.000 61.94329  ?  340 GLY A N   1 
ATOM   2220 C CA  . GLY A 1 340 ? 16.83800 -10.91300 -28.89600 1.000 62.24655  ?  340 GLY A CA  1 
ATOM   2221 C C   . GLY A 1 340 ? 16.79300 -10.40300 -27.47000 1.000 61.41787  ?  340 GLY A C   1 
ATOM   2222 O O   . GLY A 1 340 ? 17.03200 -9.21900  -27.22900 1.000 63.14751  ?  340 GLY A O   1 
ATOM   2223 N N   . ALA A 1 341 ? 16.48800 -11.29200 -26.52200 1.000 64.70393  ?  341 ALA A N   1 
ATOM   2224 C CA  . ALA A 1 341 ? 16.48200 -10.97800 -25.10100 1.000 66.78039  ?  341 ALA A CA  1 
ATOM   2225 C C   . ALA A 1 341 ? 17.27300 -12.03200 -24.34200 1.000 69.01256  ?  341 ALA A C   1 
ATOM   2226 O O   . ALA A 1 341 ? 17.14900 -13.23000 -24.61600 1.000 69.26970  ?  341 ALA A O   1 
ATOM   2227 C CB  . ALA A 1 341 ? 15.06200 -10.90400 -24.53800 1.000 66.08636  ?  341 ALA A CB  1 
ATOM   2228 N N   . ASP A 1 342 ? 18.08000 -11.58200 -23.38800 1.000 70.88454  ?  342 ASP A N   1 
ATOM   2229 C CA  . ASP A 1 342 ? 18.90300 -12.48700 -22.59900 1.000 74.01675  ?  342 ASP A CA  1 
ATOM   2230 C C   . ASP A 1 342 ? 17.98500 -13.23200 -21.64200 1.000 77.44294  ?  342 ASP A C   1 
ATOM   2231 O O   . ASP A 1 342 ? 17.60100 -12.70900 -20.59400 1.000 81.59261  ?  342 ASP A O   1 
ATOM   2232 C CB  . ASP A 1 342 ? 19.98700 -11.71700 -21.84700 1.000 80.41713  ?  342 ASP A CB  1 
ATOM   2233 C CG  . ASP A 1 342 ? 20.96600 -12.63300 -21.13500 1.000 86.96382  ?  342 ASP A CG  1 
ATOM   2234 O OD1 . ASP A 1 342 ? 20.80400 -13.86800 -21.21900 1.000 85.69684  ?  342 ASP A OD1 1 
ATOM   2235 O OD2 . ASP A 1 342 ? 21.90100 -12.11800 -20.48600 1.000 93.12071  -1 342 ASP A OD2 1 
ATOM   2236 N N   . VAL A 1 343 ? 17.62100 -14.45800 -22.01200 1.000 68.71515  ?  343 VAL A N   1 
ATOM   2237 C CA  . VAL A 1 343 ? 16.81300 -15.28900 -21.13700 1.000 70.49080  ?  343 VAL A CA  1 
ATOM   2238 C C   . VAL A 1 343 ? 17.55400 -15.59800 -19.83900 1.000 73.35258  ?  343 VAL A C   1 
ATOM   2239 O O   . VAL A 1 343 ? 16.92200 -15.88500 -18.81700 1.000 76.79559  ?  343 VAL A O   1 
ATOM   2240 C CB  . VAL A 1 343 ? 16.39600 -16.56700 -21.90300 1.000 67.79921  ?  343 VAL A CB  1 
ATOM   2241 C CG1 . VAL A 1 343 ? 17.62600 -17.35500 -22.33100 1.000 68.30949  ?  343 VAL A CG1 1 
ATOM   2242 C CG2 . VAL A 1 343 ? 15.43700 -17.42600 -21.08200 1.000 73.48175  ?  343 VAL A CG2 1 
ATOM   2243 N N   . ASN A 1 344 ? 18.88500 -15.49800 -19.84100 1.000 71.31691  ?  344 ASN A N   1 
ATOM   2244 C CA  . ASN A 1 344 ? 19.69900 -15.82600 -18.67700 1.000 71.33441  ?  344 ASN A CA  1 
ATOM   2245 C C   . ASN A 1 344 ? 20.38700 -14.59900 -18.08400 1.000 71.78240  ?  344 ASN A C   1 
ATOM   2246 O O   . ASN A 1 344 ? 21.46600 -14.70900 -17.49700 1.000 70.79251  ?  344 ASN A O   1 
ATOM   2247 C CB  . ASN A 1 344 ? 20.73300 -16.89500 -19.02700 1.000 67.67901  ?  344 ASN A CB  1 
ATOM   2248 C CG  . ASN A 1 344 ? 20.09800 -18.22100 -19.39700 1.000 69.94845  ?  344 ASN A CG  1 
ATOM   2249 O OD1 . ASN A 1 344 ? 18.88000 -18.38200 -19.32200 1.000 69.70390  ?  344 ASN A OD1 1 
ATOM   2250 N ND2 . ASN A 1 344 ? 20.92500 -19.18600 -19.78400 1.000 72.66097  ?  344 ASN A ND2 1 
ATOM   2251 N N   . ALA A 1 345 ? 19.77700 -13.42700 -18.23100 1.000 72.31967  ?  345 ALA A N   1 
ATOM   2252 C CA  . ALA A 1 345 ? 20.31800 -12.23400 -17.60200 1.000 71.64141  ?  345 ALA A CA  1 
ATOM   2253 C C   . ALA A 1 345 ? 20.06900 -12.27900 -16.10200 1.000 74.57408  ?  345 ALA A C   1 
ATOM   2254 O O   . ALA A 1 345 ? 19.24900 -13.05400 -15.60500 1.000 77.48195  ?  345 ALA A O   1 
ATOM   2255 C CB  . ALA A 1 345 ? 19.69200 -10.97500 -18.20100 1.000 74.05140  ?  345 ALA A CB  1 
ATOM   2256 N N   . TYR A 1 346 ? 20.79000 -11.43600 -15.37800 1.000 73.23571  ?  346 TYR A N   1 
ATOM   2257 C CA  . TYR A 1 346 ? 20.69400 -11.41700 -13.93000 1.000 78.59929  ?  346 TYR A CA  1 
ATOM   2258 C C   . TYR A 1 346 ? 20.66100 -9.97900  -13.44700 1.000 83.07140  ?  346 TYR A C   1 
ATOM   2259 O O   . TYR A 1 346 ? 21.42300 -9.13500  -13.92700 1.000 83.48574  ?  346 TYR A O   1 
ATOM   2260 C CB  . TYR A 1 346 ? 21.86100 -12.17300 -13.28600 1.000 79.97637  ?  346 TYR A CB  1 
ATOM   2261 N N   . ASP A 1 347 ? 19.76300 -9.70800  -12.50600 1.000 87.70478  ?  347 ASP A N   1 
ATOM   2262 C CA  . ASP A 1 347 ? 19.64200 -8.38800  -11.90500 1.000 90.93262  ?  347 ASP A CA  1 
ATOM   2263 C C   . ASP A 1 347 ? 20.73400 -8.21000  -10.84900 1.000 94.45237  ?  347 ASP A C   1 
ATOM   2264 O O   . ASP A 1 347 ? 21.66500 -9.01200  -10.74200 1.000 96.76321  ?  347 ASP A O   1 
ATOM   2265 C CB  . ASP A 1 347 ? 18.23700 -8.19400  -11.33800 1.000 90.41390  ?  347 ASP A CB  1 
ATOM   2266 C CG  . ASP A 1 347 ? 17.91500 -9.15600  -10.20000 1.000 93.03582  ?  347 ASP A CG  1 
ATOM   2267 O OD1 . ASP A 1 347 ? 18.70100 -10.09200 -9.94000  1.000 95.37156  ?  347 ASP A OD1 1 
ATOM   2268 O OD2 . ASP A 1 347 ? 16.87600 -8.94800  -9.53900  1.000 91.04888  -1 347 ASP A OD2 1 
ATOM   2269 N N   . ASN A 1 348 ? 20.62700 -7.14900  -10.04500 1.000 96.23411  ?  348 ASN A N   1 
ATOM   2270 C CA  . ASN A 1 348 ? 21.62600 -6.90400  -9.01200  1.000 95.73196  ?  348 ASN A CA  1 
ATOM   2271 C C   . ASN A 1 348 ? 21.53200 -7.90300  -7.86800  1.000 91.23530  ?  348 ASN A C   1 
ATOM   2272 O O   . ASN A 1 348 ? 22.48400 -8.02700  -7.09100  1.000 90.76612  ?  348 ASN A O   1 
ATOM   2273 C CB  . ASN A 1 348 ? 21.49400 -5.48100  -8.47200  1.000 96.95398  ?  348 ASN A CB  1 
ATOM   2274 C CG  . ASN A 1 348 ? 21.80800 -4.42900  -9.51700  1.000 99.92417  ?  348 ASN A CG  1 
ATOM   2275 O OD1 . ASN A 1 348 ? 22.00300 -4.74000  -10.69300 1.000 95.38306  ?  348 ASN A OD1 1 
ATOM   2276 N ND2 . ASN A 1 348 ? 21.86400 -3.17300  -9.09000  1.000 103.75185 ?  348 ASN A ND2 1 
ATOM   2277 N N   . ASP A 1 349 ? 20.41300 -8.61500  -7.74800  1.000 87.91263  ?  349 ASP A N   1 
ATOM   2278 C CA  . ASP A 1 349 ? 20.24600 -9.65200  -6.74100  1.000 84.71902  ?  349 ASP A CA  1 
ATOM   2279 C C   . ASP A 1 349 ? 20.47600 -11.05100 -7.30000  1.000 87.96726  ?  349 ASP A C   1 
ATOM   2280 O O   . ASP A 1 349 ? 20.12300 -12.03600 -6.64300  1.000 86.14281  ?  349 ASP A O   1 
ATOM   2281 C CB  . ASP A 1 349 ? 18.85300 -9.55700  -6.11800  1.000 82.40377  ?  349 ASP A CB  1 
ATOM   2282 C CG  . ASP A 1 349 ? 18.54500 -8.17200  -5.59500  1.000 85.34832  ?  349 ASP A CG  1 
ATOM   2283 O OD1 . ASP A 1 349 ? 19.46700 -7.32700  -5.56800  1.000 85.48814  ?  349 ASP A OD1 1 
ATOM   2284 O OD2 . ASP A 1 349 ? 17.38100 -7.92600  -5.21300  1.000 85.12574  -1 349 ASP A OD2 1 
ATOM   2285 N N   . GLY A 1 350 ? 21.04900 -11.15900 -8.49600  1.000 98.21358  ?  350 GLY A N   1 
ATOM   2286 C CA  . GLY A 1 350 ? 21.33600 -12.45800 -9.07800  1.000 99.24252  ?  350 GLY A CA  1 
ATOM   2287 C C   . GLY A 1 350 ? 20.11900 -13.24400 -9.51600  1.000 98.08625  ?  350 GLY A C   1 
ATOM   2288 O O   . GLY A 1 350 ? 20.14300 -14.47800 -9.47300  1.000 103.78373 ?  350 GLY A O   1 
ATOM   2289 N N   . HIS A 1 351 ? 19.05800 -12.56700 -9.94600  1.000 84.61836  ?  351 HIS A N   1 
ATOM   2290 C CA  . HIS A 1 351 ? 17.82000 -13.22500 -10.33900 1.000 80.58231  ?  351 HIS A CA  1 
ATOM   2291 C C   . HIS A 1 351 ? 17.69000 -13.24300 -11.85700 1.000 80.17901  ?  351 HIS A C   1 
ATOM   2292 O O   . HIS A 1 351 ? 17.71700 -12.19000 -12.50500 1.000 81.22678  ?  351 HIS A O   1 
ATOM   2293 C CB  . HIS A 1 351 ? 16.60900 -12.53100 -9.71300  1.000 78.11864  ?  351 HIS A CB  1 
ATOM   2294 C CG  . HIS A 1 351 ? 16.47200 -12.77200 -8.24200  1.000 86.03575  ?  351 HIS A CG  1 
ATOM   2295 N ND1 . HIS A 1 351 ? 16.93500 -11.88200 -7.29700  1.000 87.88607  ?  351 HIS A ND1 1 
ATOM   2296 C CD2 . HIS A 1 351 ? 15.93100 -13.80500 -7.55300  1.000 84.49793  ?  351 HIS A CD2 1 
ATOM   2297 C CE1 . HIS A 1 351 ? 16.68200 -12.35300 -6.08900  1.000 84.63981  ?  351 HIS A CE1 1 
ATOM   2298 N NE2 . HIS A 1 351 ? 16.07400 -13.51900 -6.21600  1.000 81.49730  ?  351 HIS A NE2 1 
ATOM   2299 N N   . THR A 1 352 ? 17.54000 -14.43500 -12.41200 1.000 78.98818  ?  352 THR A N   1 
ATOM   2300 C CA  . THR A 1 352 ? 17.27000 -14.61100 -13.82400 1.000 70.90823  ?  352 THR A CA  1 
ATOM   2301 C C   . THR A 1 352 ? 15.79200 -14.35300 -14.09800 1.000 70.50319  ?  352 THR A C   1 
ATOM   2302 O O   . THR A 1 352 ? 14.97700 -14.36000 -13.17500 1.000 69.66915  ?  352 THR A O   1 
ATOM   2303 C CB  . THR A 1 352 ? 17.65500 -16.02100 -14.25700 1.000 69.90160  ?  352 THR A CB  1 
ATOM   2304 N N   . PRO A 1 353 ? 15.42500 -14.09200 -15.36200 1.000 74.53456  ?  353 PRO A N   1 
ATOM   2305 C CA  . PRO A 1 353 ? 13.99700 -13.95100 -15.69100 1.000 72.32003  ?  353 PRO A CA  1 
ATOM   2306 C C   . PRO A 1 353 ? 13.16100 -15.13200 -15.23900 1.000 69.24893  ?  353 PRO A C   1 
ATOM   2307 O O   . PRO A 1 353 ? 12.01200 -14.95300 -14.82000 1.000 67.83662  ?  353 PRO A O   1 
ATOM   2308 C CB  . PRO A 1 353 ? 14.00700 -13.82100 -17.21900 1.000 70.58430  ?  353 PRO A CB  1 
ATOM   2309 C CG  . PRO A 1 353 ? 15.31900 -13.18800 -17.51800 1.000 71.54156  ?  353 PRO A CG  1 
ATOM   2310 C CD  . PRO A 1 353 ? 16.28500 -13.76400 -16.51400 1.000 74.76871  ?  353 PRO A CD  1 
ATOM   2311 N N   . LEU A 1 354 ? 13.72000 -16.34000 -15.31500 1.000 70.35182  ?  354 LEU A N   1 
ATOM   2312 C CA  . LEU A 1 354 ? 13.02400 -17.52100 -14.82200 1.000 72.92297  ?  354 LEU A CA  1 
ATOM   2313 C C   . LEU A 1 354 ? 12.77100 -17.42600 -13.32100 1.000 73.52909  ?  354 LEU A C   1 
ATOM   2314 O O   . LEU A 1 354 ? 11.67300 -17.74200 -12.84500 1.000 72.70596  ?  354 LEU A O   1 
ATOM   2315 C CB  . LEU A 1 354 ? 13.83300 -18.77200 -15.15900 1.000 69.61291  ?  354 LEU A CB  1 
ATOM   2316 C CG  . LEU A 1 354 ? 13.21100 -20.10600 -14.75600 1.000 67.96072  ?  354 LEU A CG  1 
ATOM   2317 N N   . HIS A 1 355 ? 13.78100 -17.00000 -12.55700 1.000 72.73745  ?  355 HIS A N   1 
ATOM   2318 C CA  . HIS A 1 355 ? 13.59800 -16.83300 -11.11800 1.000 71.31893  ?  355 HIS A CA  1 
ATOM   2319 C C   . HIS A 1 355 ? 12.46200 -15.86200 -10.82800 1.000 71.25158  ?  355 HIS A C   1 
ATOM   2320 O O   . HIS A 1 355 ? 11.57600 -16.14800 -10.01200 1.000 71.39769  ?  355 HIS A O   1 
ATOM   2321 C CB  . HIS A 1 355 ? 14.89400 -16.34900 -10.46300 1.000 72.59049  ?  355 HIS A CB  1 
ATOM   2322 C CG  . HIS A 1 355 ? 16.13300 -16.77400 -11.18600 1.000 72.46688  ?  355 HIS A CG  1 
ATOM   2323 N N   . LEU A 1 356 ? 12.46600 -14.70700 -11.49800 1.000 72.96951  ?  356 LEU A N   1 
ATOM   2324 C CA  . LEU A 1 356 ? 11.38000 -13.75000 -11.32100 1.000 69.65273  ?  356 LEU A CA  1 
ATOM   2325 C C   . LEU A 1 356 ? 10.05000 -14.34900 -11.75200 1.000 73.32577  ?  356 LEU A C   1 
ATOM   2326 O O   . LEU A 1 356 ? 9.01900  -14.12000 -11.10800 1.000 75.58472  ?  356 LEU A O   1 
ATOM   2327 C CB  . LEU A 1 356 ? 11.67500 -12.47200 -12.10200 1.000 68.57627  ?  356 LEU A CB  1 
ATOM   2328 C CG  . LEU A 1 356 ? 13.02300 -11.83500 -11.77100 1.000 69.95373  ?  356 LEU A CG  1 
ATOM   2329 N N   . ALA A 1 357 ? 10.05300 -15.12900 -12.83300 1.000 70.25811  ?  357 ALA A N   1 
ATOM   2330 C CA  . ALA A 1 357 ? 8.83300  -15.81000 -13.24800 1.000 70.47443  ?  357 ALA A CA  1 
ATOM   2331 C C   . ALA A 1 357 ? 8.37100  -16.78800 -12.17600 1.000 77.25585  ?  357 ALA A C   1 
ATOM   2332 O O   . ALA A 1 357 ? 7.21700  -16.74200 -11.73500 1.000 80.16217  ?  357 ALA A O   1 
ATOM   2333 C CB  . ALA A 1 357 ? 9.05600  -16.52500 -14.58000 1.000 69.69592  ?  357 ALA A CB  1 
ATOM   2334 N N   . ALA A 1 358 ? 9.27500  -17.66100 -11.72000 1.000 79.72207  ?  358 ALA A N   1 
ATOM   2335 C CA  . ALA A 1 358 ? 8.91000  -18.66500 -10.72400 1.000 81.77915  ?  358 ALA A CA  1 
ATOM   2336 C C   . ALA A 1 358 ? 8.46800  -18.03300 -9.41100  1.000 80.83052  ?  358 ALA A C   1 
ATOM   2337 O O   . ALA A 1 358 ? 7.64300  -18.61100 -8.69200  1.000 80.29706  ?  358 ALA A O   1 
ATOM   2338 C CB  . ALA A 1 358 ? 10.08400 -19.61400 -10.48200 1.000 80.47427  ?  358 ALA A CB  1 
ATOM   2339 N N   . LYS A 1 359 ? 9.00300  -16.85600 -9.07700  1.000 82.36055  ?  359 LYS A N   1 
ATOM   2340 C CA  . LYS A 1 359 ? 8.59900  -16.18800 -7.84500  1.000 82.40014  ?  359 LYS A CA  1 
ATOM   2341 C C   . LYS A 1 359 ? 7.13100  -15.78000 -7.88000  1.000 84.54650  ?  359 LYS A C   1 
ATOM   2342 O O   . LYS A 1 359 ? 6.45800  -15.81200 -6.84400  1.000 86.29589  ?  359 LYS A O   1 
ATOM   2343 C CB  . LYS A 1 359 ? 9.48300  -14.96800 -7.59600  1.000 80.16801  ?  359 LYS A CB  1 
ATOM   2344 N N   . TYR A 1 360 ? 6.61600  -15.40100 -9.05100  1.000 76.35819  ?  360 TYR A N   1 
ATOM   2345 C CA  . TYR A 1 360 ? 5.22300  -14.99800 -9.20300  1.000 74.33743  ?  360 TYR A CA  1 
ATOM   2346 C C   . TYR A 1 360 ? 4.40400  -16.04300 -9.95600  1.000 74.42685  ?  360 TYR A C   1 
ATOM   2347 O O   . TYR A 1 360 ? 3.40500  -15.71000 -10.59700 1.000 76.42991  ?  360 TYR A O   1 
ATOM   2348 C CB  . TYR A 1 360 ? 5.13400  -13.63600 -9.89600  1.000 72.59801  ?  360 TYR A CB  1 
ATOM   2349 C CG  . TYR A 1 360 ? 5.91200  -12.53600 -9.19600  1.000 75.34258  ?  360 TYR A CG  1 
ATOM   2350 C CD1 . TYR A 1 360 ? 5.35200  -11.82200 -8.14000  1.000 74.49545  ?  360 TYR A CD1 1 
ATOM   2351 C CD2 . TYR A 1 360 ? 7.20300  -12.21100 -9.58800  1.000 74.68042  ?  360 TYR A CD2 1 
ATOM   2352 C CE1 . TYR A 1 360 ? 6.06000  -10.82000 -7.49300  1.000 73.19640  ?  360 TYR A CE1 1 
ATOM   2353 C CE2 . TYR A 1 360 ? 7.91900  -11.20900 -8.94700  1.000 74.97952  ?  360 TYR A CE2 1 
ATOM   2354 C CZ  . TYR A 1 360 ? 7.34300  -10.51800 -7.90100  1.000 72.52727  ?  360 TYR A CZ  1 
ATOM   2355 O OH  . TYR A 1 360 ? 8.04900  -9.52200  -7.26200  1.000 73.58278  ?  360 TYR A OH  1 
ATOM   2356 N N   . GLY A 1 361 ? 4.80100  -17.31000 -9.87600  1.000 72.21751  ?  361 GLY A N   1 
ATOM   2357 C CA  . GLY A 1 361 ? 4.11000  -18.34900 -10.61200 1.000 72.08132  ?  361 GLY A CA  1 
ATOM   2358 C C   . GLY A 1 361 ? 4.44500  -18.31100 -12.08900 1.000 80.24466  ?  361 GLY A C   1 
ATOM   2359 O O   . GLY A 1 361 ? 5.55100  -18.69400 -12.48300 1.000 81.24304  ?  361 GLY A O   1 
ATOM   2360 N N   . HIS A 1 362 ? 3.49500  -17.85100 -12.90500 1.000 82.57613  ?  362 HIS A N   1 
ATOM   2361 C CA  . HIS A 1 362 ? 3.67200  -17.66500 -14.34900 1.000 80.44310  ?  362 HIS A CA  1 
ATOM   2362 C C   . HIS A 1 362 ? 4.39300  -18.84600 -14.98500 1.000 78.83878  ?  362 HIS A C   1 
ATOM   2363 O O   . HIS A 1 362 ? 5.33700  -18.69100 -15.76400 1.000 77.56612  ?  362 HIS A O   1 
ATOM   2364 C CB  . HIS A 1 362 ? 4.41000  -16.36500 -14.65100 1.000 76.71855  ?  362 HIS A CB  1 
ATOM   2365 C CG  . HIS A 1 362 ? 3.79700  -15.16700 -14.00600 1.000 76.44327  ?  362 HIS A CG  1 
ATOM   2366 N ND1 . HIS A 1 362 ? 2.50300  -14.77000 -14.25900 1.000 78.20609  ?  362 HIS A ND1 1 
ATOM   2367 C CD2 . HIS A 1 362 ? 4.30800  -14.26100 -13.14000 1.000 77.52114  ?  362 HIS A CD2 1 
ATOM   2368 C CE1 . HIS A 1 362 ? 2.23500  -13.68200 -13.55800 1.000 80.18671  ?  362 HIS A CE1 1 
ATOM   2369 N NE2 . HIS A 1 362 ? 3.31500  -13.35100 -12.87400 1.000 79.93664  ?  362 HIS A NE2 1 
ATOM   2370 N N   . LEU A 1 363 ? 3.93800  -20.04900 -14.62900 1.000 77.48530  ?  363 LEU A N   1 
ATOM   2371 C CA  . LEU A 1 363 ? 4.56800  -21.25600 -15.14800 1.000 78.99034  ?  363 LEU A CA  1 
ATOM   2372 C C   . LEU A 1 363 ? 4.57100  -21.26400 -16.67100 1.000 75.56810  ?  363 LEU A C   1 
ATOM   2373 O O   . LEU A 1 363 ? 5.51800  -21.76400 -17.28900 1.000 73.73860  ?  363 LEU A O   1 
ATOM   2374 C CB  . LEU A 1 363 ? 3.85900  -22.49300 -14.59500 1.000 80.72982  ?  363 LEU A CB  1 
ATOM   2375 N N   . GLU A 1 364 ? 3.53600  -20.68800 -17.28600 1.000 76.18378  ?  364 GLU A N   1 
ATOM   2376 C CA  . GLU A 1 364 ? 3.49500  -20.57000 -18.73900 1.000 73.47162  ?  364 GLU A CA  1 
ATOM   2377 C C   . GLU A 1 364 ? 4.65800  -19.72500 -19.24300 1.000 68.99061  ?  364 GLU A C   1 
ATOM   2378 O O   . GLU A 1 364 ? 5.36200  -20.10600 -20.18600 1.000 64.55945  ?  364 GLU A O   1 
ATOM   2379 C CB  . GLU A 1 364 ? 2.15900  -19.96200 -19.17100 1.000 74.78489  ?  364 GLU A CB  1 
ATOM   2380 C CG  . GLU A 1 364 ? 0.95900  -20.39700 -18.32400 1.000 77.55984  ?  364 GLU A CG  1 
ATOM   2381 C CD  . GLU A 1 364 ? 0.80300  -19.57300 -17.04600 1.000 78.68475  ?  364 GLU A CD  1 
ATOM   2382 O OE1 . GLU A 1 364 ? 1.60000  -18.63300 -16.83800 1.000 79.11474  ?  364 GLU A OE1 1 
ATOM   2383 O OE2 . GLU A 1 364 ? -0.10800 -19.87300 -16.24400 1.000 75.14871  -1 364 GLU A OE2 1 
ATOM   2384 N N   . ILE A 1 365 ? 4.87600  -18.56700 -18.61600 1.000 72.19407  ?  365 ILE A N   1 
ATOM   2385 C CA  . ILE A 1 365 ? 6.02700  -17.73900 -18.96000 1.000 70.81472  ?  365 ILE A CA  1 
ATOM   2386 C C   . ILE A 1 365 ? 7.31900  -18.48100 -18.64800 1.000 71.11480  ?  365 ILE A C   1 
ATOM   2387 O O   . ILE A 1 365 ? 8.29400  -18.40500 -19.40400 1.000 70.46697  ?  365 ILE A O   1 
ATOM   2388 C CB  . ILE A 1 365 ? 5.95100  -16.38700 -18.22500 1.000 68.28629  ?  365 ILE A CB  1 
ATOM   2389 C CG1 . ILE A 1 365 ? 4.66200  -15.64800 -18.59500 1.000 67.57607  ?  365 ILE A CG1 1 
ATOM   2390 C CG2 . ILE A 1 365 ? 7.15900  -15.52700 -18.55600 1.000 63.40970  ?  365 ILE A CG2 1 
ATOM   2391 N N   . VAL A 1 366 ? 7.34200  -19.22600 -17.53900 1.000 72.30032  ?  366 VAL A N   1 
ATOM   2392 C CA  . VAL A 1 366 ? 8.53200  -20.00000 -17.19200 1.000 73.38269  ?  366 VAL A CA  1 
ATOM   2393 C C   . VAL A 1 366 ? 8.82700  -21.03000 -18.27500 1.000 72.72389  ?  366 VAL A C   1 
ATOM   2394 O O   . VAL A 1 366 ? 9.98900  -21.26800 -18.62500 1.000 75.88467  ?  366 VAL A O   1 
ATOM   2395 C CB  . VAL A 1 366 ? 8.36200  -20.65900 -15.81200 1.000 69.07013  ?  366 VAL A CB  1 
ATOM   2396 N N   . GLU A 1 367 ? 7.78200  -21.64600 -18.83100 1.000 71.19637  ?  367 GLU A N   1 
ATOM   2397 C CA  . GLU A 1 367 ? 7.98700  -22.61500 -19.90100 1.000 68.70346  ?  367 GLU A CA  1 
ATOM   2398 C C   . GLU A 1 367 ? 8.59700  -21.95500 -21.13000 1.000 67.90351  ?  367 GLU A C   1 
ATOM   2399 O O   . GLU A 1 367 ? 9.52200  -22.50100 -21.74200 1.000 67.64968  ?  367 GLU A O   1 
ATOM   2400 C CB  . GLU A 1 367 ? 6.66600  -23.29700 -20.25600 1.000 64.97454  ?  367 GLU A CB  1 
ATOM   2401 N N   . VAL A 1 368 ? 8.09500  -20.77600 -21.50500 1.000 69.90659  ?  368 VAL A N   1 
ATOM   2402 C CA  . VAL A 1 368 ? 8.64000  -20.07600 -22.66400 1.000 67.16097  ?  368 VAL A CA  1 
ATOM   2403 C C   . VAL A 1 368 ? 10.11100 -19.76000 -22.44500 1.000 72.21590  ?  368 VAL A C   1 
ATOM   2404 O O   . VAL A 1 368 ? 10.94200 -19.93600 -23.34500 1.000 72.72266  ?  368 VAL A O   1 
ATOM   2405 C CB  . VAL A 1 368 ? 7.82500  -18.80300 -22.95400 1.000 57.98447  ?  368 VAL A CB  1 
ATOM   2406 N N   . LEU A 1 369 ? 10.45900 -19.29700 -21.24100 1.000 74.05743  ?  369 LEU A N   1 
ATOM   2407 C CA  . LEU A 1 369 ? 11.85700 -19.01500 -20.93500 1.000 75.68630  ?  369 LEU A CA  1 
ATOM   2408 C C   . LEU A 1 369 ? 12.70200 -20.27500 -21.03000 1.000 75.92093  ?  369 LEU A C   1 
ATOM   2409 O O   . LEU A 1 369 ? 13.80500 -20.25100 -21.58700 1.000 78.15418  ?  369 LEU A O   1 
ATOM   2410 C CB  . LEU A 1 369 ? 11.98000 -18.39500 -19.54400 1.000 75.75726  ?  369 LEU A CB  1 
ATOM   2411 C CG  . LEU A 1 369 ? 11.19400 -17.10500 -19.32400 1.000 74.97190  ?  369 LEU A CG  1 
ATOM   2412 C CD1 . LEU A 1 369 ? 11.30400 -16.63200 -17.87600 1.000 74.59448  ?  369 LEU A CD1 1 
ATOM   2413 C CD2 . LEU A 1 369 ? 11.66200 -16.03800 -20.30000 1.000 72.63994  ?  369 LEU A CD2 1 
ATOM   2414 N N   . LEU A 1 370 ? 12.20100 -21.38900 -20.49200 1.000 71.85141  ?  370 LEU A N   1 
ATOM   2415 C CA  . LEU A 1 370 ? 12.93300 -22.64300 -20.60800 1.000 73.54927  ?  370 LEU A CA  1 
ATOM   2416 C C   . LEU A 1 370 ? 13.04600 -23.07500 -22.06500 1.000 73.58267  ?  370 LEU A C   1 
ATOM   2417 O O   . LEU A 1 370 ? 14.10000 -23.55800 -22.49700 1.000 72.79784  ?  370 LEU A O   1 
ATOM   2418 C CB  . LEU A 1 370 ? 12.26100 -23.72800 -19.76700 1.000 68.99262  ?  370 LEU A CB  1 
ATOM   2419 C CG  . LEU A 1 370 ? 12.30000 -23.54300 -18.24800 1.000 65.65587  ?  370 LEU A CG  1 
ATOM   2420 N N   . LYS A 1 371 ? 11.97800 -22.88900 -22.84600 1.000 71.76301  ?  371 LYS A N   1 
ATOM   2421 C CA  . LYS A 1 371 ? 12.02300 -23.24100 -24.26000 1.000 68.58640  ?  371 LYS A CA  1 
ATOM   2422 C C   . LYS A 1 371 ? 12.96200 -22.33900 -25.04700 1.000 68.99838  ?  371 LYS A C   1 
ATOM   2423 O O   . LYS A 1 371 ? 13.31600 -22.67300 -26.18300 1.000 68.91494  ?  371 LYS A O   1 
ATOM   2424 C CB  . LYS A 1 371 ? 10.62100 -23.18800 -24.86800 1.000 64.99594  ?  371 LYS A CB  1 
ATOM   2425 N N   . HIS A 1 372 ? 13.37100 -21.20800 -24.47300 1.000 67.43775  ?  372 HIS A N   1 
ATOM   2426 C CA  . HIS A 1 372 ? 14.34400 -20.32200 -25.09600 1.000 65.86007  ?  372 HIS A CA  1 
ATOM   2427 C C   . HIS A 1 372 ? 15.71700 -20.41000 -24.44000 1.000 65.90157  ?  372 HIS A C   1 
ATOM   2428 O O   . HIS A 1 372 ? 16.57400 -19.56200 -24.70500 1.000 64.52104  ?  372 HIS A O   1 
ATOM   2429 C CB  . HIS A 1 372 ? 13.83900 -18.87900 -25.07700 1.000 64.67508  ?  372 HIS A CB  1 
ATOM   2430 C CG  . HIS A 1 372 ? 12.76200 -18.60100 -26.07900 1.000 64.14358  ?  372 HIS A CG  1 
ATOM   2431 N ND1 . HIS A 1 372 ? 11.45900 -19.01300 -25.90200 1.000 64.94023  ?  372 HIS A ND1 1 
ATOM   2432 C CD2 . HIS A 1 372 ? 12.79400 -17.96200 -27.27200 1.000 62.45267  ?  372 HIS A CD2 1 
ATOM   2433 C CE1 . HIS A 1 372 ? 10.73500 -18.63900 -26.94200 1.000 65.61345  ?  372 HIS A CE1 1 
ATOM   2434 N NE2 . HIS A 1 372 ? 11.52100 -17.99800 -27.78800 1.000 64.96103  ?  372 HIS A NE2 1 
ATOM   2435 N N   . GLY A 1 373 ? 15.94400 -21.40900 -23.58700 1.000 65.95154  ?  373 GLY A N   1 
ATOM   2436 C CA  . GLY A 1 373 ? 17.26100 -21.64500 -23.02300 1.000 68.84776  ?  373 GLY A CA  1 
ATOM   2437 C C   . GLY A 1 373 ? 17.50600 -21.01700 -21.66500 1.000 73.53068  ?  373 GLY A C   1 
ATOM   2438 O O   . GLY A 1 373 ? 18.55200 -20.39900 -21.44200 1.000 71.88265  ?  373 GLY A O   1 
ATOM   2439 N N   . ALA A 1 374 ? 16.55800 -21.17700 -20.74400 1.000 75.51494  ?  374 ALA A N   1 
ATOM   2440 C CA  . ALA A 1 374 ? 16.71000 -20.64900 -19.39400 1.000 71.62955  ?  374 ALA A CA  1 
ATOM   2441 C C   . ALA A 1 374 ? 17.62800 -21.54700 -18.57400 1.000 74.21431  ?  374 ALA A C   1 
ATOM   2442 O O   . ALA A 1 374 ? 17.62400 -22.77200 -18.72800 1.000 75.98644  ?  374 ALA A O   1 
ATOM   2443 C CB  . ALA A 1 374 ? 15.34700 -20.52400 -18.71200 1.000 73.11557  ?  374 ALA A CB  1 
ATOM   2444 N N   . ASP A 1 375 ? 18.41700 -20.93200 -17.69700 1.000 73.55505  ?  375 ASP A N   1 
ATOM   2445 C CA  . ASP A 1 375 ? 19.34400 -21.68300 -16.86200 1.000 73.35233  ?  375 ASP A CA  1 
ATOM   2446 C C   . ASP A 1 375 ? 18.59100 -22.29700 -15.68400 1.000 78.17176  ?  375 ASP A C   1 
ATOM   2447 O O   . ASP A 1 375 ? 17.89600 -21.58900 -14.94600 1.000 78.98891  ?  375 ASP A O   1 
ATOM   2448 C CB  . ASP A 1 375 ? 20.46600 -20.76600 -16.37000 1.000 75.09166  ?  375 ASP A CB  1 
ATOM   2449 C CG  . ASP A 1 375 ? 21.56400 -21.51800 -15.64000 1.000 81.17213  ?  375 ASP A CG  1 
ATOM   2450 O OD1 . ASP A 1 375 ? 21.55400 -22.76900 -15.65200 1.000 84.17417  ?  375 ASP A OD1 1 
ATOM   2451 O OD2 . ASP A 1 375 ? 22.43600 -20.85300 -15.04300 1.000 86.70281  -1 375 ASP A OD2 1 
ATOM   2452 N N   . VAL A 1 376 ? 18.72300 -23.61900 -15.51400 1.000 80.86540  ?  376 VAL A N   1 
ATOM   2453 C CA  . VAL A 1 376 ? 18.07200 -24.30300 -14.39700 1.000 74.59908  ?  376 VAL A CA  1 
ATOM   2454 C C   . VAL A 1 376 ? 18.65300 -23.84700 -13.06800 1.000 79.20893  ?  376 VAL A C   1 
ATOM   2455 O O   . VAL A 1 376 ? 17.93400 -23.76100 -12.06400 1.000 82.62057  ?  376 VAL A O   1 
ATOM   2456 C CB  . VAL A 1 376 ? 18.19100 -25.83000 -14.55200 1.000 76.06998  ?  376 VAL A CB  1 
ATOM   2457 N N   . ASN A 1 377 ? 19.95200 -23.56400 -13.02800 1.000 80.72236  ?  377 ASN A N   1 
ATOM   2458 C CA  . ASN A 1 377 ? 20.59600 -23.01000 -11.83900 1.000 83.10319  ?  377 ASN A CA  1 
ATOM   2459 C C   . ASN A 1 377 ? 20.33700 -21.51100 -11.81900 1.000 85.60639  ?  377 ASN A C   1 
ATOM   2460 O O   . ASN A 1 377 ? 21.05300 -20.73800 -12.45700 1.000 85.44382  ?  377 ASN A O   1 
ATOM   2461 C CB  . ASN A 1 377 ? 22.09000 -23.31200 -11.84300 1.000 80.86320  ?  377 ASN A CB  1 
ATOM   2462 N N   . ALA A 1 378 ? 19.30500 -21.09300 -11.08000 1.000 92.93663  ?  378 ALA A N   1 
ATOM   2463 C CA  . ALA A 1 378 ? 18.95600 -19.67800 -11.03100 1.000 95.02892  ?  378 ALA A CA  1 
ATOM   2464 C C   . ALA A 1 378 ? 20.05000 -18.82900 -10.40100 1.000 101.04003 ?  378 ALA A C   1 
ATOM   2465 O O   . ALA A 1 378 ? 20.02800 -17.60400 -10.56200 1.000 102.87927 ?  378 ALA A O   1 
ATOM   2466 C CB  . ALA A 1 378 ? 17.65200 -19.47900 -10.26600 1.000 92.98772  ?  378 ALA A CB  1 
ATOM   2467 N N   . GLN A 1 379 ? 20.98700 -19.44800 -9.68000  1.000 91.75897  ?  379 GLN A N   1 
ATOM   2468 C CA  . GLN A 1 379 ? 22.15600 -18.75600 -9.13100  1.000 93.69167  ?  379 GLN A CA  1 
ATOM   2469 C C   . GLN A 1 379 ? 21.75500 -17.49800 -8.36400  1.000 95.50840  ?  379 GLN A C   1 
ATOM   2470 O O   . GLN A 1 379 ? 22.37700 -16.44100 -8.49100  1.000 98.00162  ?  379 GLN A O   1 
ATOM   2471 C CB  . GLN A 1 379 ? 23.16000 -18.42300 -10.23500 1.000 94.66064  ?  379 GLN A CB  1 
ATOM   2472 N N   . ASP A 1 380 ? 20.69500 -17.61400 -7.56900  1.000 93.35800  ?  380 ASP A N   1 
ATOM   2473 C CA  . ASP A 1 380 ? 20.22600 -16.50000 -6.76200  1.000 92.60967  ?  380 ASP A CA  1 
ATOM   2474 C C   . ASP A 1 380 ? 21.33000 -16.02600 -5.81500  1.000 93.92405  ?  380 ASP A C   1 
ATOM   2475 O O   . ASP A 1 380 ? 22.27800 -16.75500 -5.50900  1.000 91.31223  ?  380 ASP A O   1 
ATOM   2476 C CB  . ASP A 1 380 ? 18.98500 -16.91900 -5.97300  1.000 92.01149  ?  380 ASP A CB  1 
ATOM   2477 C CG  . ASP A 1 380 ? 18.31200 -15.75800 -5.27900  1.000 93.61854  ?  380 ASP A CG  1 
ATOM   2478 O OD1 . ASP A 1 380 ? 18.70000 -14.60200 -5.54300  1.000 94.78446  ?  380 ASP A OD1 1 
ATOM   2479 O OD2 . ASP A 1 380 ? 17.40400 -16.00500 -4.45700  1.000 94.44311  -1 380 ASP A OD2 1 
ATOM   2480 N N   . LYS A 1 381 ? 21.20200 -14.77600 -5.35300  1.000 96.12632  ?  381 LYS A N   1 
ATOM   2481 C CA  . LYS A 1 381 ? 22.13700 -14.24200 -4.36600  1.000 92.51419  ?  381 LYS A CA  1 
ATOM   2482 C C   . LYS A 1 381 ? 22.17700 -15.09000 -3.10500  1.000 96.37879  ?  381 LYS A C   1 
ATOM   2483 O O   . LYS A 1 381 ? 23.16700 -15.04400 -2.36500  1.000 102.00122 ?  381 LYS A O   1 
ATOM   2484 C CB  . LYS A 1 381 ? 21.77300 -12.80100 -4.00400  1.000 90.65083  ?  381 LYS A CB  1 
ATOM   2485 N N   . PHE A 1 382 ? 21.11900 -15.85300 -2.84000  1.000 94.21632  ?  382 PHE A N   1 
ATOM   2486 C CA  . PHE A 1 382 ? 21.10300 -16.84700 -1.77900  1.000 96.37938  ?  382 PHE A CA  1 
ATOM   2487 C C   . PHE A 1 382 ? 21.34900 -18.25500 -2.31100  1.000 96.06164  ?  382 PHE A C   1 
ATOM   2488 O O   . PHE A 1 382 ? 21.05300 -19.23400 -1.61800  1.000 101.22988 ?  382 PHE A O   1 
ATOM   2489 C CB  . PHE A 1 382 ? 19.77600 -16.78400 -1.02400  1.000 98.50642  ?  382 PHE A CB  1 
ATOM   2490 C CG  . PHE A 1 382 ? 19.38700 -15.39700 -0.59700  1.000 99.14070  ?  382 PHE A CG  1 
ATOM   2491 N N   . GLY A 1 383 ? 21.87900 -18.37600 -3.52700  1.000 91.84736  ?  383 GLY A N   1 
ATOM   2492 C CA  . GLY A 1 383 ? 22.14300 -19.67000 -4.12400  1.000 90.98024  ?  383 GLY A CA  1 
ATOM   2493 C C   . GLY A 1 383 ? 20.92100 -20.43200 -4.58300  1.000 88.51786  ?  383 GLY A C   1 
ATOM   2494 O O   . GLY A 1 383 ? 21.06600 -21.55400 -5.08600  1.000 89.26785  ?  383 GLY A O   1 
ATOM   2495 N N   . LYS A 1 384 ? 19.72900 -19.86000 -4.44100  1.000 87.43733  ?  384 LYS A N   1 
ATOM   2496 C CA  . LYS A 1 384 ? 18.50300 -20.56900 -4.77500  1.000 85.41079  ?  384 LYS A CA  1 
ATOM   2497 C C   . LYS A 1 384 ? 18.37000 -20.75700 -6.28100  1.000 83.52891  ?  384 LYS A C   1 
ATOM   2498 O O   . LYS A 1 384 ? 18.73600 -19.88400 -7.07200  1.000 83.64894  ?  384 LYS A O   1 
ATOM   2499 C CB  . LYS A 1 384 ? 17.29200 -19.80700 -4.23600  1.000 84.13804  ?  384 LYS A CB  1 
ATOM   2500 N N   . THR A 1 385 ? 17.84500 -21.91400 -6.67100  1.000 83.16918  ?  385 THR A N   1 
ATOM   2501 C CA  . THR A 1 385 ? 17.53600 -22.18700 -8.06100  1.000 80.14567  ?  385 THR A CA  1 
ATOM   2502 C C   . THR A 1 385 ? 16.08700 -21.80700 -8.34200  1.000 80.53888  ?  385 THR A C   1 
ATOM   2503 O O   . THR A 1 385 ? 15.33100 -21.41300 -7.44900  1.000 79.61506  ?  385 THR A O   1 
ATOM   2504 C CB  . THR A 1 385 ? 17.79000 -23.65500 -8.39400  1.000 80.84008  ?  385 THR A CB  1 
ATOM   2505 O OG1 . THR A 1 385 ? 16.82300 -24.46900 -7.72000  1.000 81.72705  ?  385 THR A OG1 1 
ATOM   2506 C CG2 . THR A 1 385 ? 19.18700 -24.06200 -7.95300  1.000 82.97089  ?  385 THR A CG2 1 
ATOM   2507 N N   . ALA A 1 386 ? 15.69100 -21.92100 -9.60900  1.000 77.93174  ?  386 ALA A N   1 
ATOM   2508 C CA  . ALA A 1 386 ? 14.31700 -21.60200 -9.97000  1.000 75.21703  ?  386 ALA A CA  1 
ATOM   2509 C C   . ALA A 1 386 ? 13.34100 -22.55800 -9.29900  1.000 78.34450  ?  386 ALA A C   1 
ATOM   2510 O O   . ALA A 1 386 ? 12.30100 -22.13200 -8.78400  1.000 78.73364  ?  386 ALA A O   1 
ATOM   2511 C CB  . ALA A 1 386 ? 14.15200 -21.63000 -11.48800 1.000 74.53230  ?  386 ALA A CB  1 
ATOM   2512 N N   . PHE A 1 387 ? 13.66600 -23.85500 -9.28000  1.000 79.88181  ?  387 PHE A N   1 
ATOM   2513 C CA  . PHE A 1 387 ? 12.79800 -24.82200 -8.61400  1.000 80.04765  ?  387 PHE A CA  1 
ATOM   2514 C C   . PHE A 1 387 ? 12.69100 -24.52800 -7.12500  1.000 79.85510  ?  387 PHE A C   1 
ATOM   2515 O O   . PHE A 1 387 ? 11.61800 -24.67900 -6.53000  1.000 80.25415  ?  387 PHE A O   1 
ATOM   2516 C CB  . PHE A 1 387 ? 13.31500 -26.24300 -8.83700  1.000 80.06131  ?  387 PHE A CB  1 
ATOM   2517 N N   . ASP A 1 388 ? 13.79500 -24.10800 -6.50600  1.000 80.86499  ?  388 ASP A N   1 
ATOM   2518 C CA  . ASP A 1 388 ? 13.75100 -23.76400 -5.09100  1.000 83.57497  ?  388 ASP A CA  1 
ATOM   2519 C C   . ASP A 1 388 ? 12.76000 -22.63400 -4.83800  1.000 82.72414  ?  388 ASP A C   1 
ATOM   2520 O O   . ASP A 1 388 ? 12.04000 -22.64500 -3.83300  1.000 86.23851  ?  388 ASP A O   1 
ATOM   2521 C CB  . ASP A 1 388 ? 15.14900 -23.39100 -4.59800  1.000 85.56980  ?  388 ASP A CB  1 
ATOM   2522 C CG  . ASP A 1 388 ? 16.13500 -24.53900 -4.71600  1.000 88.42473  ?  388 ASP A CG  1 
ATOM   2523 N N   . ILE A 1 389 ? 12.68800 -21.66700 -5.75600  1.000 81.30550  ?  389 ILE A N   1 
ATOM   2524 C CA  . ILE A 1 389 ? 11.73100 -20.57500 -5.60400  1.000 81.83546  ?  389 ILE A CA  1 
ATOM   2525 C C   . ILE A 1 389 ? 10.30500 -21.09900 -5.71400  1.000 84.32123  ?  389 ILE A C   1 
ATOM   2526 O O   . ILE A 1 389 ? 9.40700  -20.65400 -4.98900  1.000 84.71664  ?  389 ILE A O   1 
ATOM   2527 C CB  . ILE A 1 389 ? 12.01300 -19.47000 -6.63800  1.000 76.73172  ?  389 ILE A CB  1 
ATOM   2528 N N   . SER A 1 390 ? 10.07700 -22.05700 -6.61500  1.000 80.36930  ?  390 SER A N   1 
ATOM   2529 C CA  . SER A 1 390 ? 8.74500  -22.63200 -6.76500  1.000 81.69705  ?  390 SER A CA  1 
ATOM   2530 C C   . SER A 1 390 ? 8.35500  -23.47600 -5.55800  1.000 86.00246  ?  390 SER A C   1 
ATOM   2531 O O   . SER A 1 390 ? 7.16500  -23.59200 -5.24300  1.000 87.01444  ?  390 SER A O   1 
ATOM   2532 C CB  . SER A 1 390 ? 8.68000  -23.46900 -8.04200  1.000 79.76415  ?  390 SER A CB  1 
ATOM   2533 N N   . ILE A 1 391 ? 9.33500  -24.07100 -4.87700  1.000 83.73350  ?  391 ILE A N   1 
ATOM   2534 C CA  . ILE A 1 391 ? 9.03600  -24.86500 -3.69100  1.000 88.26465  ?  391 ILE A CA  1 
ATOM   2535 C C   . ILE A 1 391 ? 8.62800  -23.96300 -2.53300  1.000 96.59980  ?  391 ILE A C   1 
ATOM   2536 O O   . ILE A 1 391 ? 7.67500  -24.26200 -1.80300  1.000 97.13308  ?  391 ILE A O   1 
ATOM   2537 C CB  . ILE A 1 391 ? 10.24000 -25.75100 -3.32300  1.000 91.06480  ?  391 ILE A CB  1 
ATOM   2538 N N   . ASP A 1 392 ? 9.33800  -22.84600 -2.34500  1.000 110.63443 ?  392 ASP A N   1 
ATOM   2539 C CA  . ASP A 1 392 ? 8.98200  -21.91100 -1.28100  1.000 113.71946 ?  392 ASP A CA  1 
ATOM   2540 C C   . ASP A 1 392 ? 7.61800  -21.27100 -1.51300  1.000 113.10589 ?  392 ASP A C   1 
ATOM   2541 O O   . ASP A 1 392 ? 6.90000  -20.99000 -0.54700  1.000 118.51254 ?  392 ASP A O   1 
ATOM   2542 C CB  . ASP A 1 392 ? 10.05600 -20.82900 -1.15300  1.000 116.56578 ?  392 ASP A CB  1 
ATOM   2543 N N   . ASN A 1 393 ? 7.24700  -21.03700 -2.77200  1.000 99.73915  ?  393 ASN A N   1 
ATOM   2544 C CA  . ASN A 1 393 ? 5.93700  -20.50200 -3.11300  1.000 98.70555  ?  393 ASN A CA  1 
ATOM   2545 C C   . ASN A 1 393 ? 4.84800  -21.56700 -3.12500  1.000 100.27308 ?  393 ASN A C   1 
ATOM   2546 O O   . ASN A 1 393 ? 3.67900  -21.23000 -3.34600  1.000 104.22099 ?  393 ASN A O   1 
ATOM   2547 C CB  . ASN A 1 393 ? 5.98700  -19.81200 -4.48000  1.000 94.43443  ?  393 ASN A CB  1 
ATOM   2548 N N   . GLY A 1 394 ? 5.19600  -22.83200 -2.90500  1.000 95.80970  ?  394 GLY A N   1 
ATOM   2549 C CA  . GLY A 1 394 ? 4.20300  -23.88700 -2.89300  1.000 91.99314  ?  394 GLY A CA  1 
ATOM   2550 C C   . GLY A 1 394 ? 3.53800  -24.14200 -4.22500  1.000 90.80686  ?  394 GLY A C   1 
ATOM   2551 O O   . GLY A 1 394 ? 2.40900  -24.63300 -4.26300  1.000 90.57118  ?  394 GLY A O   1 
ATOM   2552 N N   . ASN A 1 395 ? 4.21500  -23.82000 -5.32700  1.000 103.53470 ?  395 ASN A N   1 
ATOM   2553 C CA  . ASN A 1 395 ? 3.67900  -24.02800 -6.67000  1.000 100.77043 ?  395 ASN A CA  1 
ATOM   2554 C C   . ASN A 1 395 ? 4.23500  -25.34700 -7.19100  1.000 100.62762 ?  395 ASN A C   1 
ATOM   2555 O O   . ASN A 1 395 ? 5.29400  -25.39200 -7.81800  1.000 100.59281 ?  395 ASN A O   1 
ATOM   2556 C CB  . ASN A 1 395 ? 4.03700  -22.85900 -7.58000  1.000 98.65028  ?  395 ASN A CB  1 
ATOM   2557 N N   . GLU A 1 396 ? 3.50200  -26.43200 -6.92700  1.000 92.60634  ?  396 GLU A N   1 
ATOM   2558 C CA  . GLU A 1 396 ? 3.95700  -27.76000 -7.33500  1.000 87.71183  ?  396 GLU A CA  1 
ATOM   2559 C C   . GLU A 1 396 ? 4.04300  -27.88900 -8.84900  1.000 88.10329  ?  396 GLU A C   1 
ATOM   2560 O O   . GLU A 1 396 ? 4.91700  -28.59800 -9.36000  1.000 88.50547  ?  396 GLU A O   1 
ATOM   2561 C CB  . GLU A 1 396 ? 3.02200  -28.82500 -6.76100  1.000 88.97433  ?  396 GLU A CB  1 
ATOM   2562 N N   . ASP A 1 397 ? 3.15700  -27.21100 -9.58200  1.000 88.81029  ?  397 ASP A N   1 
ATOM   2563 C CA  . ASP A 1 397 ? 3.20600  -27.27400 -11.03900 1.000 88.75712  ?  397 ASP A CA  1 
ATOM   2564 C C   . ASP A 1 397 ? 4.51000  -26.68800 -11.56100 1.000 88.60639  ?  397 ASP A C   1 
ATOM   2565 O O   . ASP A 1 397 ? 5.17300  -27.29000 -12.41200 1.000 87.36698  ?  397 ASP A O   1 
ATOM   2566 C CB  . ASP A 1 397 ? 2.00100  -26.54700 -11.64200 1.000 88.70580  ?  397 ASP A CB  1 
ATOM   2567 N N   . LEU A 1 398 ? 4.89800  -25.51200 -11.05600 1.000 90.56109  ?  398 LEU A N   1 
ATOM   2568 C CA  . LEU A 1 398 ? 6.18800  -24.93800 -11.42900 1.000 89.62463  ?  398 LEU A CA  1 
ATOM   2569 C C   . LEU A 1 398 ? 7.33800  -25.80500 -10.93100 1.000 86.07596  ?  398 LEU A C   1 
ATOM   2570 O O   . LEU A 1 398 ? 8.37100  -25.92300 -11.60100 1.000 87.11918  ?  398 LEU A O   1 
ATOM   2571 C CB  . LEU A 1 398 ? 6.31100  -23.51300 -10.88500 1.000 88.65272  ?  398 LEU A CB  1 
ATOM   2572 N N   . ALA A 1 399 ? 7.17600  -26.42800 -9.76100  1.000 83.02794  ?  399 ALA A N   1 
ATOM   2573 C CA  . ALA A 1 399 ? 8.19000  -27.36200 -9.27800  1.000 83.59904  ?  399 ALA A CA  1 
ATOM   2574 C C   . ALA A 1 399 ? 8.32500  -28.55400 -10.21700 1.000 81.96110  ?  399 ALA A C   1 
ATOM   2575 O O   . ALA A 1 399 ? 9.43900  -29.01200 -10.49700 1.000 81.95518  ?  399 ALA A O   1 
ATOM   2576 C CB  . ALA A 1 399 ? 7.84800  -27.82900 -7.86300  1.000 87.42513  ?  399 ALA A CB  1 
ATOM   2577 N N   . GLU A 1 400 ? 7.20400  -29.07000 -10.71900 1.000 81.53955  ?  400 GLU A N   1 
ATOM   2578 C CA  . GLU A 1 400 ? 7.24700  -30.11600 -11.73200 1.000 79.06810  ?  400 GLU A CA  1 
ATOM   2579 C C   . GLU A 1 400 ? 7.78700  -29.54600 -13.03500 1.000 78.74754  ?  400 GLU A C   1 
ATOM   2580 O O   . GLU A 1 400 ? 7.06400  -29.45100 -14.03100 1.000 78.43304  ?  400 GLU A O   1 
ATOM   2581 C CB  . GLU A 1 400 ? 5.86400  -30.72500 -11.95100 1.000 77.99186  ?  400 GLU A CB  1 
ATOM   2582 N N   . ILE A 1 401 ? 9.06300  -29.15600 -13.03000 1.000 79.42484  ?  401 ILE A N   1 
ATOM   2583 C CA  . ILE A 1 401 ? 9.66900  -28.58000 -14.22500 1.000 78.98096  ?  401 ILE A CA  1 
ATOM   2584 C C   . ILE A 1 401 ? 9.65900  -29.59400 -15.35800 1.000 83.91552  ?  401 ILE A C   1 
ATOM   2585 O O   . ILE A 1 401 ? 9.49400  -29.23800 -16.53100 1.000 81.58008  ?  401 ILE A O   1 
ATOM   2586 C CB  . ILE A 1 401 ? 11.09400 -28.07300 -13.91800 1.000 74.48262  ?  401 ILE A CB  1 
ATOM   2587 C CG1 . ILE A 1 401 ? 11.96800 -29.19100 -13.34000 1.000 77.10627  ?  401 ILE A CG1 1 
ATOM   2588 C CG2 . ILE A 1 401 ? 11.04700 -26.88500 -12.97600 1.000 74.09108  ?  401 ILE A CG2 1 
ATOM   2589 N N   . LEU A 1 402 ? 9.80200  -30.87000 -15.02400 1.000 85.66345  ?  402 LEU A N   1 
ATOM   2590 C CA  . LEU A 1 402 ? 9.82300  -31.92900 -16.01700 1.000 88.07223  ?  402 LEU A CA  1 
ATOM   2591 C C   . LEU A 1 402 ? 8.93500  -33.08100 -15.56100 1.000 92.05894  ?  402 LEU A C   1 
ATOM   2592 O O   . LEU A 1 402 ? 8.13100  -32.92500 -14.64000 1.000 91.14088  ?  402 LEU A O   1 
ATOM   2593 C CB  . LEU A 1 402 ? 11.25600 -32.40400 -16.25300 1.000 88.97159  ?  402 LEU A CB  1 
HETATM 2594 S S   . SO4 B 2 .   ? 7.74000  55.08600  0.63600   1.000 127.13348 ?  501 SO4 A S   1 
HETATM 2595 O O1  . SO4 B 2 .   ? 8.81600  55.02300  -0.35000  1.000 104.80348 ?  501 SO4 A O1  1 
HETATM 2596 O O2  . SO4 B 2 .   ? 6.46200  55.19600  -0.06200  1.000 113.55348 ?  501 SO4 A O2  1 
HETATM 2597 O O3  . SO4 B 2 .   ? 7.75500  53.87500  1.45200   1.000 120.71348 ?  501 SO4 A O3  1 
HETATM 2598 O O4  . SO4 B 2 .   ? 7.93400  56.25100  1.49700   1.000 124.28348 ?  501 SO4 A O4  1 
HETATM 2599 S S   . SO4 C 2 .   ? 36.99300 1.74600   -23.71100 1.000 89.23348  ?  502 SO4 A S   1 
HETATM 2600 O O1  . SO4 C 2 .   ? 37.48700 0.60400   -24.47500 1.000 86.52348  ?  502 SO4 A O1  1 
HETATM 2601 O O2  . SO4 C 2 .   ? 35.59100 1.50800   -23.37200 1.000 75.84348  ?  502 SO4 A O2  1 
HETATM 2602 O O3  . SO4 C 2 .   ? 37.79800 1.87700   -22.50400 1.000 78.75348  ?  502 SO4 A O3  1 
HETATM 2603 O O4  . SO4 C 2 .   ? 37.11500 2.98100   -24.48400 1.000 83.25348  ?  502 SO4 A O4  1 
HETATM 2604 S S   . SO4 D 2 .   ? 7.70600  37.20200  -4.94900  1.000 107.97348 ?  503 SO4 A S   1 
HETATM 2605 O O1  . SO4 D 2 .   ? 8.01100  35.81100  -5.35100  1.000 100.54348 ?  503 SO4 A O1  1 
HETATM 2606 O O2  . SO4 D 2 .   ? 7.75600  38.08300  -6.13700  1.000 101.37348 ?  503 SO4 A O2  1 
HETATM 2607 O O3  . SO4 D 2 .   ? 6.35600  37.26000  -4.34700  1.000 98.23348  ?  503 SO4 A O3  1 
HETATM 2608 O O4  . SO4 D 2 .   ? 8.70700  37.65800  -3.96000  1.000 77.80348  ?  503 SO4 A O4  1 
HETATM 2609 O O   . HOH E 3 .   ? 21.91600 34.49600  9.55100   1.000 50.54348  ?  601 HOH A O   1 
HETATM 2610 O O   . HOH E 3 .   ? 31.39500 24.25900  -11.22000 1.000 43.77348  ?  602 HOH A O   1 
HETATM 2611 O O   . HOH E 3 .   ? 24.18900 50.43600  -9.46300  1.000 58.77348  ?  603 HOH A O   1 
HETATM 2612 O O   . HOH E 3 .   ? 13.65200 28.63300  -5.03200  1.000 27.14348  ?  604 HOH A O   1 
HETATM 2613 O O   . HOH E 3 .   ? -1.19800 -4.42300  -26.46100 1.000 66.88348  ?  605 HOH A O   1 
HETATM 2614 O O   . HOH E 3 .   ? 21.05600 21.26400  -8.09600  1.000 46.67348  ?  606 HOH A O   1 
HETATM 2615 O O   . HOH E 3 .   ? 22.17100 51.34600  -5.25200  1.000 40.07348  ?  607 HOH A O   1 
HETATM 2616 O O   . HOH E 3 .   ? 22.091   40.195    -31.681   1.000 38.77348  ?  608 HOH A O   1 
HETATM 2617 O O   . HOH E 3 .   ? 10.55600 53.41200  8.77800   1.000 52.24348  ?  609 HOH A O   1 
HETATM 2618 O O   . HOH E 3 .   ? 34.61900 42.22600  -18.82600 1.000 32.37348  ?  610 HOH A O   1 
HETATM 2619 O O   . HOH E 3 .   ? 14.57000 50.88900  20.41300  1.000 32.49348  ?  611 HOH A O   1 
HETATM 2620 O O   . HOH E 3 .   ? 10.60800 46.14300  -26.78200 1.000 31.03348  ?  612 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   . GLN A 12  ? 1.37082 0.56449 1.18491 0.26208  0.17690  0.16115  12  GLN A N   
2    C CA  . GLN A 12  ? 1.23328 0.53394 1.11961 0.26010  0.14232  0.16089  12  GLN A CA  
3    C C   . GLN A 12  ? 1.18464 0.50217 1.08584 0.19799  0.14231  0.15604  12  GLN A C   
4    O O   . GLN A 12  ? 1.25735 0.49308 1.10098 0.17577  0.16689  0.16256  12  GLN A O   
5    C CB  . GLN A 12  ? 1.22197 0.55519 1.10155 0.32140  0.11676  0.17808  12  GLN A CB  
6    N N   . PRO A 13  ? 1.07224 0.49452 1.04867 0.17076  0.11704  0.14384  13  PRO A N   
7    C CA  . PRO A 13  ? 1.02657 0.47301 1.02094 0.11535  0.11622  0.13754  13  PRO A CA  
8    C C   . PRO A 13  ? 1.11075 0.52782 1.06850 0.11700  0.11559  0.15300  13  PRO A C   
9    O O   . PRO A 13  ? 1.11245 0.51495 1.06085 0.07154  0.12760  0.14809  13  PRO A O   
10   C CB  . PRO A 13  ? 0.95405 0.51444 1.02886 0.10557  0.08688  0.12718  13  PRO A CB  
11   C CG  . PRO A 13  ? 0.93945 0.52140 1.03736 0.13296  0.08477  0.11970  13  PRO A CG  
12   C CD  . PRO A 13  ? 1.04941 0.56625 1.09454 0.18615  0.09366  0.13290  13  PRO A CD  
13   N N   . ILE A 14  ? 1.13578 0.54882 1.07215 0.16910  0.10188  0.17002  14  ILE A N   
14   C CA  . ILE A 14  ? 1.12952 0.51094 1.02390 0.17421  0.10199  0.18601  14  ILE A CA  
15   C C   . ILE A 14  ? 1.19625 0.46001 1.01372 0.14883  0.14248  0.19124  14  ILE A C   
16   O O   . ILE A 14  ? 1.19906 0.44389 0.99567 0.11905  0.15103  0.19454  14  ILE A O   
17   C CB  . ILE A 14  ? 1.13688 0.52818 1.01047 0.24233  0.08212  0.20285  14  ILE A CB  
18   C CG1 . ILE A 14  ? 1.17814 0.52692 0.99668 0.25043  0.08476  0.22111  14  ILE A CG1 
19   C CG2 . ILE A 14  ? 1.20994 0.53715 1.03870 0.29206  0.09690  0.20990  14  ILE A CG2 
20   N N   . TYR A 15  ? 1.26643 0.45918 1.04434 0.15450  0.16840  0.18727  15  TYR A N   
21   C CA  . TYR A 15  ? 1.34230 0.45462 1.05638 0.12243  0.20332  0.18071  15  TYR A CA  
22   C C   . TYR A 15  ? 1.32367 0.44166 1.06039 0.05247  0.22273  0.15609  15  TYR A C   
23   O O   . TYR A 15  ? 1.40626 0.47090 1.09796 0.01944  0.25288  0.14499  15  TYR A O   
24   C CB  . TYR A 15  ? 1.43213 0.48171 1.09514 0.15934  0.22073  0.18312  15  TYR A CB  
25   C CG  . TYR A 15  ? 1.45422 0.52181 1.10705 0.23278  0.19692  0.20194  15  TYR A CG  
26   C CD1 . TYR A 15  ? 1.54494 0.60073 1.15662 0.26262  0.18917  0.22004  15  TYR A CD1 
27   C CD2 . TYR A 15  ? 1.44401 0.54860 1.12968 0.27189  0.18214  0.19873  15  TYR A CD2 
28   C CE1 . TYR A 15  ? 1.58727 0.67308 1.19119 0.32896  0.16554  0.23316  15  TYR A CE1 
29   C CE2 . TYR A 15  ? 1.50406 0.64274 1.18616 0.33747  0.15869  0.21058  15  TYR A CE2 
30   C CZ  . TYR A 15  ? 1.59806 0.72988 1.23956 0.36543  0.14959  0.22715  15  TYR A CZ  
31   O OH  . TYR A 15  ? 1.64921 0.82609 1.28846 0.42896  0.12508  0.23526  15  TYR A OH  
32   N N   . TRP A 16  ? 1.21984 0.40693 1.02556 0.02970  0.20718  0.14545  16  TRP A N   
33   C CA  . TRP A 16  ? 1.19029 0.39921 1.01981 -0.03370 0.22161  0.11900  16  TRP A CA  
34   C C   . TRP A 16  ? 1.18842 0.41285 1.01274 -0.07647 0.22693  0.11270  16  TRP A C   
35   O O   . TRP A 16  ? 1.19636 0.43464 1.02131 -0.06220 0.21288  0.12946  16  TRP A O   
36   C CB  . TRP A 16  ? 1.15939 0.47277 1.06893 -0.04248 0.19380  0.10623  16  TRP A CB  
37   C CG  . TRP A 16  ? 1.15893 0.47583 1.08174 -0.00916 0.18898  0.10484  16  TRP A CG  
38   C CD1 . TRP A 16  ? 1.22091 0.45509 1.09324 0.02868  0.20778  0.11358  16  TRP A CD1 
39   C CD2 . TRP A 16  ? 1.09170 0.49805 1.08022 -0.00909 0.16583  0.09395  16  TRP A CD2 
40   N NE1 . TRP A 16  ? 1.21309 0.48717 1.12110 0.05137  0.19651  0.10689  16  TRP A NE1 
41   C CE2 . TRP A 16  ? 1.13780 0.51596 1.11641 0.02673  0.17175  0.09479  16  TRP A CE2 
42   C CE3 . TRP A 16  ? 0.99037 0.49331 1.04055 -0.03371 0.14290  0.08438  16  TRP A CE3 
43   C CZ2 . TRP A 16  ? 1.12610 0.57222 1.15680 0.03410  0.15638  0.08493  16  TRP A CZ2 
44   C CZ3 . TRP A 16  ? 0.89181 0.45360 0.98739 -0.02483 0.12891  0.07686  16  TRP A CZ3 
45   C CH2 . TRP A 16  ? 0.97983 0.51461 1.06683 0.00661  0.13603  0.07648  16  TRP A CH2 
46   N N   . SER A 17  ? 1.17042 0.39767 0.99031 -0.12779 0.24764  0.08623  17  SER A N   
47   C CA  . SER A 17  ? 1.15388 0.41196 0.97794 -0.17183 0.25378  0.07280  17  SER A CA  
48   C C   . SER A 17  ? 1.15611 0.51032 1.04701 -0.21003 0.23851  0.05065  17  SER A C   
49   O O   . SER A 17  ? 1.14204 0.53020 1.07047 -0.20489 0.22658  0.04604  17  SER A O   
50   C CB  . SER A 17  ? 1.24031 0.43555 1.00601 -0.19767 0.29098  0.05648  17  SER A CB  
51   N N   . ARG A 18  ? 1.07609 0.47770 0.98097 -0.24564 0.23914  0.03654  18  ARG A N   
52   C CA  . ARG A 18  ? 0.99402 0.49497 0.95768 -0.27729 0.22373  0.01411  18  ARG A CA  
53   C C   . ARG A 18  ? 1.04895 0.55862 1.01562 -0.29752 0.23489  -0.01167 18  ARG A C   
54   O O   . ARG A 18  ? 1.04730 0.62558 1.06044 -0.30325 0.21725  -0.02150 18  ARG A O   
55   C CB  . ARG A 18  ? 0.97683 0.52258 0.94641 -0.30895 0.22732  -0.00081 18  ARG A CB  
56   N N   . ASP A 19  ? 1.11123 0.54974 1.02541 -0.30764 0.26599  -0.02310 19  ASP A N   
57   C CA  . ASP A 19  ? 1.15786 0.59258 1.06795 -0.32432 0.27989  -0.04705 19  ASP A CA  
58   C C   . ASP A 19  ? 1.11632 0.52836 1.03635 -0.28985 0.26922  -0.03116 19  ASP A C   
59   O O   . ASP A 19  ? 1.06960 0.52677 1.02063 -0.30011 0.26185  -0.04677 19  ASP A O   
60   C CB  . ASP A 19  ? 1.27925 0.63340 1.12573 -0.34158 0.32023  -0.06190 19  ASP A CB  
61   C CG  . ASP A 19  ? 1.40465 0.76063 1.24535 -0.36736 0.33864  -0.09303 19  ASP A CG  
62   O OD1 . ASP A 19  ? 1.33109 0.75845 1.21776 -0.37436 0.31868  -0.10509 19  ASP A OD1 
63   O OD2 . ASP A 19  ? 1.51566 0.79975 1.30245 -0.38076 0.37507  -0.10593 19  ASP A OD2 
64   N N   . ASP A 20  ? 1.16019 0.50692 1.05420 -0.24632 0.26796  -0.00101 20  ASP A N   
65   C CA  . ASP A 20  ? 1.13462 0.46165 1.03887 -0.20861 0.25923  0.01279  20  ASP A CA  
66   C C   . ASP A 20  ? 1.08449 0.50022 1.05785 -0.20162 0.22691  0.01766  20  ASP A C   
67   O O   . ASP A 20  ? 1.07985 0.52944 1.08002 -0.18874 0.21590  0.01234  20  ASP A O   
68   C CB  . ASP A 20  ? 1.20144 0.45275 1.06314 -0.15638 0.26167  0.04300  20  ASP A CB  
69   C CG  . ASP A 20  ? 1.37609 0.54343 1.16594 -0.15909 0.29334  0.04129  20  ASP A CG  
70   O OD1 . ASP A 20  ? 1.43974 0.60144 1.21382 -0.20249 0.31714  0.01444  20  ASP A OD1 
71   O OD2 . ASP A 20  ? 1.46686 0.57722 1.21522 -0.11694 0.29526  0.06587  20  ASP A OD2 
72   N N   . VAL A 21  ? 1.06120 0.53545 1.06351 -0.20169 0.20463  0.02721  21  VAL A N   
73   C CA  . VAL A 21  ? 0.95856 0.53616 1.02392 -0.18906 0.16825  0.03055  21  VAL A CA  
74   C C   . VAL A 21  ? 0.89203 0.53266 0.98614 -0.22266 0.16683  0.00443  21  VAL A C   
75   O O   . VAL A 21  ? 0.84601 0.53633 0.97287 -0.20730 0.14928  0.00430  21  VAL A O   
76   C CB  . VAL A 21  ? 0.89054 0.50979 0.97465 -0.18620 0.14973  0.04316  21  VAL A CB  
77   C CG1 . VAL A 21  ? 0.81154 0.52884 0.95419 -0.17929 0.11860  0.04356  21  VAL A CG1 
78   C CG2 . VAL A 21  ? 0.94094 0.51140 0.99995 -0.14509 0.14505  0.06935  21  VAL A CG2 
79   N N   . ALA A 22  ? 0.96267 0.60271 1.04214 -0.26916 0.18710  -0.01986 22  ALA A N   
80   C CA  . ALA A 22  ? 0.87864 0.59259 0.98514 -0.30010 0.18309  -0.04771 22  ALA A CA  
81   C C   . ALA A 22  ? 0.88587 0.57796 0.98224 -0.29981 0.19382  -0.06075 22  ALA A C   
82   O O   . ALA A 22  ? 0.84953 0.61054 0.97521 -0.30010 0.17794  -0.07102 22  ALA A O   
83   C CB  . ALA A 22  ? 0.83037 0.56501 0.92167 -0.33966 0.19683  -0.07319 22  ALA A CB  
84   N N   . GLN A 23  ? 0.90727 0.50049 0.95777 -0.29719 0.22223  -0.06013 23  GLN A N   
85   C CA  . GLN A 23  ? 0.94678 0.51397 0.98587 -0.29402 0.23410  -0.07237 23  GLN A CA  
86   C C   . GLN A 23  ? 0.92139 0.52581 0.99357 -0.24774 0.20664  -0.05200 23  GLN A C   
87   O O   . GLN A 23  ? 0.90122 0.54211 0.98911 -0.24930 0.20214  -0.06453 23  GLN A O   
88   C CB  . GLN A 23  ? 1.01190 0.46801 0.98965 -0.28743 0.26687  -0.07168 23  GLN A CB  
89   N N   . TRP A 24  ? 0.91913 0.51768 1.00156 -0.20816 0.18946  -0.02276 24  TRP A N   
90   C CA  . TRP A 24  ? 0.85535 0.49707 0.97378 -0.16935 0.16526  -0.00718 24  TRP A CA  
91   C C   . TRP A 24  ? 0.81919 0.55627 0.98153 -0.17960 0.14231  -0.01276 24  TRP A C   
92   O O   . TRP A 24  ? 0.79371 0.56411 0.97931 -0.16140 0.13166  -0.00990 24  TRP A O   
93   C CB  . TRP A 24  ? 0.86479 0.49353 0.98771 -0.13058 0.15097  0.01985  24  TRP A CB  
94   C CG  . TRP A 24  ? 0.81739 0.50409 0.98429 -0.09813 0.12608  0.03182  24  TRP A CG  
95   C CD1 . TRP A 24  ? 0.81761 0.50624 0.99557 -0.07414 0.12645  0.03095  24  TRP A CD1 
96   C CD2 . TRP A 24  ? 0.73901 0.48745 0.94349 -0.08845 0.10086  0.04409  24  TRP A CD2 
97   N NE1 . TRP A 24  ? 0.76599 0.51613 0.98741 -0.05358 0.10428  0.04034  24  TRP A NE1 
98   C CE2 . TRP A 24  ? 0.69529 0.47950 0.93202 -0.06220 0.08889  0.04856  24  TRP A CE2 
99   C CE3 . TRP A 24  ? 0.69809 0.47403 0.91140 -0.10091 0.08965  0.04983  24  TRP A CE3 
100  C CZ2 . TRP A 24  ? 0.63780 0.47882 0.91272 -0.05112 0.06840  0.05745  24  TRP A CZ2 
101  C CZ3 . TRP A 24  ? 0.61630 0.44743 0.86669 -0.08612 0.06760  0.06029  24  TRP A CZ3 
102  C CH2 . TRP A 24  ? 0.63852 0.49919 0.91817 -0.06292 0.05818  0.06354  24  TRP A CH2 
103  N N   . LEU A 25  ? 0.82259 0.60291 0.99363 -0.20683 0.13639  -0.02085 25  LEU A N   
104  C CA  . LEU A 25  ? 0.76838 0.63543 0.97336 -0.21055 0.11548  -0.02458 25  LEU A CA  
105  C C   . LEU A 25  ? 0.78318 0.67566 0.98308 -0.22992 0.12285  -0.04850 25  LEU A C   
106  O O   . LEU A 25  ? 0.80521 0.73761 1.02204 -0.21439 0.11091  -0.04505 25  LEU A O   
107  C CB  . LEU A 25  ? 0.75863 0.66883 0.97368 -0.22914 0.10696  -0.02751 25  LEU A CB  
108  C CG  . LEU A 25  ? 0.74548 0.63273 0.96113 -0.21590 0.10142  -0.00731 25  LEU A CG  
109  C CD1 . LEU A 25  ? 0.74526 0.68008 0.97057 -0.23861 0.09635  -0.01555 25  LEU A CD1 
110  C CD2 . LEU A 25  ? 0.71072 0.61105 0.95116 -0.17733 0.08150  0.01707  25  LEU A CD2 
111  N N   . LYS A 26  ? 0.77298 0.64158 0.94671 -0.26574 0.14470  -0.07460 26  LYS A N   
112  C CA  . LYS A 26  ? 0.77770 0.67428 0.94466 -0.28705 0.15226  -0.10196 26  LYS A CA  
113  C C   . LYS A 26  ? 0.79947 0.65404 0.95629 -0.26636 0.16084  -0.09804 26  LYS A C   
114  O O   . LYS A 26  ? 0.82375 0.71660 0.98389 -0.26882 0.15774  -0.11085 26  LYS A O   
115  C CB  . LYS A 26  ? 0.76432 0.64057 0.90501 -0.33506 0.17817  -0.13551 26  LYS A CB  
116  N N   . TRP A 27  ? 0.77220 0.55172 0.91506 -0.24330 0.17154  -0.08097 27  TRP A N   
117  C CA  . TRP A 27  ? 0.81988 0.56562 0.95720 -0.21866 0.17908  -0.07725 27  TRP A CA  
118  C C   . TRP A 27  ? 0.78614 0.59267 0.95956 -0.19062 0.15564  -0.06155 27  TRP A C   
119  O O   . TRP A 27  ? 0.82744 0.65338 1.00273 -0.18862 0.15793  -0.07071 27  TRP A O   
120  C CB  . TRP A 27  ? 0.83978 0.50018 0.95429 -0.19255 0.19306  -0.06127 27  TRP A CB  
121  C CG  . TRP A 27  ? 0.89276 0.53789 1.01475 -0.15500 0.19305  -0.05183 27  TRP A CG  
122  C CD1 . TRP A 27  ? 0.95429 0.55808 1.05440 -0.15322 0.21405  -0.06633 27  TRP A CD1 
123  C CD2 . TRP A 27  ? 0.89945 0.57641 1.05527 -0.11582 0.17251  -0.02949 27  TRP A CD2 
124  N NE1 . TRP A 27  ? 0.98745 0.59812 1.10719 -0.11316 0.20724  -0.05352 27  TRP A NE1 
125  C CE2 . TRP A 27  ? 0.95365 0.61160 1.10890 -0.09139 0.18205  -0.03223 27  TRP A CE2 
126  C CE3 . TRP A 27  ? 0.85684 0.57822 1.04382 -0.10098 0.14872  -0.01037 27  TRP A CE3 
127  C CZ2 . TRP A 27  ? 0.91302 0.60195 1.10107 -0.05459 0.16849  -0.01841 27  TRP A CZ2 
128  C CZ3 . TRP A 27  ? 0.83258 0.58002 1.04971 -0.06648 0.13609  0.00276  27  TRP A CZ3 
129  C CH2 . TRP A 27  ? 0.84558 0.58010 1.06467 -0.04444 0.14592  -0.00218 27  TRP A CH2 
130  N N   . ALA A 28  ? 0.78985 0.62373 0.98922 -0.17075 0.13569  -0.03902 28  ALA A N   
131  C CA  . ALA A 28  ? 0.70702 0.59163 0.93738 -0.14870 0.11837  -0.02551 28  ALA A CA  
132  C C   . ALA A 28  ? 0.73910 0.68499 0.97291 -0.16415 0.11010  -0.03551 28  ALA A C   
133  O O   . ALA A 28  ? 0.77774 0.74866 1.01904 -0.15237 0.10747  -0.03285 28  ALA A O   
134  C CB  . ALA A 28  ? 0.64725 0.54597 0.90156 -0.12946 0.10153  -0.00338 28  ALA A CB  
135  N N   . GLU A 29  ? 0.65200 0.62454 0.87814 -0.18913 0.10695  -0.04789 29  GLU A N   
136  C CA  . GLU A 29  ? 0.68444 0.72365 0.91072 -0.19870 0.09691  -0.05892 29  GLU A CA  
137  C C   . GLU A 29  ? 0.72500 0.76673 0.93335 -0.20603 0.10795  -0.07754 29  GLU A C   
138  O O   . GLU A 29  ? 0.73008 0.81908 0.93707 -0.19724 0.09893  -0.07708 29  GLU A O   
139  C CB  . GLU A 29  ? 0.68568 0.75818 0.90841 -0.22631 0.09409  -0.07590 29  GLU A CB  
140  C CG  . GLU A 29  ? 0.75426 0.90329 0.97334 -0.23643 0.08431  -0.09450 29  GLU A CG  
141  C CD  . GLU A 29  ? 0.82238 1.01195 1.04207 -0.26739 0.08417  -0.11834 29  GLU A CD  
142  O OE1 . GLU A 29  ? 0.78023 0.94761 1.00799 -0.27362 0.08593  -0.11083 29  GLU A OE1 
143  O OE2 . GLU A 29  ? 0.86191 1.10904 1.07381 -0.28647 0.08317  -0.14679 29  GLU A OE2 
144  N N   . ASN A 30  ? 0.77855 0.76520 0.96826 -0.21975 0.12904  -0.09315 30  ASN A N   
145  C CA  . ASN A 30  ? 0.83837 0.82009 1.00994 -0.22620 0.14208  -0.11180 30  ASN A CA  
146  C C   . ASN A 30  ? 0.84899 0.79930 1.02787 -0.19645 0.14724  -0.09558 30  ASN A C   
147  O O   . ASN A 30  ? 0.90640 0.87975 1.08094 -0.18992 0.14832  -0.09931 30  ASN A O   
148  C CB  . ASN A 30  ? 0.89412 0.82816 1.03792 -0.25870 0.16679  -0.14097 30  ASN A CB  
149  C CG  . ASN A 30  ? 0.90992 0.87673 1.04921 -0.29453 0.16629  -0.16253 30  ASN A CG  
150  O OD1 . ASN A 30  ? 0.91071 0.93629 1.06944 -0.29089 0.14554  -0.15360 30  ASN A OD1 
151  N ND2 . ASN A 30  ? 0.91200 0.84064 1.02507 -0.33048 0.19169  -0.19325 30  ASN A ND2 
152  N N   . GLU A 31  ? 0.89170 0.79435 1.08096 -0.17734 0.15067  -0.07884 31  GLU A N   
153  C CA  . GLU A 31  ? 0.94326 0.82289 1.14290 -0.14955 0.15713  -0.06894 31  GLU A CA  
154  C C   . GLU A 31  ? 0.87870 0.80813 1.10310 -0.13209 0.14360  -0.05313 31  GLU A C   
155  O O   . GLU A 31  ? 0.90173 0.83606 1.12739 -0.12259 0.15187  -0.05573 31  GLU A O   
156  C CB  . GLU A 31  ? 0.97687 0.80625 1.18184 -0.12875 0.16044  -0.05550 31  GLU A CB  
157  C CG  . GLU A 31  ? 1.05526 0.88085 1.28169 -0.09515 0.16182  -0.04499 31  GLU A CG  
158  C CD  . GLU A 31  ? 1.17753 0.96898 1.38635 -0.08985 0.18321  -0.06070 31  GLU A CD  
159  O OE1 . GLU A 31  ? 1.21191 0.96810 1.38733 -0.11205 0.19919  -0.07927 31  GLU A OE1 
160  O OE2 . GLU A 31  ? 1.21559 1.01739 1.44476 -0.06496 0.18570  -0.05696 31  GLU A OE2 
161  N N   . PHE A 32  ? 0.73282 0.69486 0.97395 -0.12873 0.12604  -0.03745 32  PHE A N   
162  C CA  . PHE A 32  ? 0.69923 0.69756 0.95765 -0.11421 0.11734  -0.02186 32  PHE A CA  
163  C C   . PHE A 32  ? 0.73530 0.77784 0.97761 -0.12253 0.10861  -0.02316 32  PHE A C   
164  O O   . PHE A 32  ? 0.70578 0.77033 0.95246 -0.10969 0.10393  -0.00840 32  PHE A O   
165  C CB  . PHE A 32  ? 0.61523 0.61563 0.90102 -0.10054 0.10593  -0.00320 32  PHE A CB  
166  C CG  . PHE A 32  ? 0.63727 0.60258 0.93592 -0.08717 0.11035  -0.00157 32  PHE A CG  
167  C CD1 . PHE A 32  ? 0.61555 0.57661 0.93076 -0.06960 0.11915  -0.00224 32  PHE A CD1 
168  C CD2 . PHE A 32  ? 0.68424 0.62279 0.97606 -0.08988 0.10656  0.00022  32  PHE A CD2 
169  C CE1 . PHE A 32  ? 0.63109 0.56772 0.95674 -0.05033 0.12113  -0.00123 32  PHE A CE1 
170  C CE2 . PHE A 32  ? 0.71849 0.62245 1.01418 -0.07068 0.11024  0.00402  32  PHE A CE2 
171  C CZ  . PHE A 32  ? 0.70102 0.60700 1.01411 -0.04850 0.11601  0.00329  32  PHE A CZ  
172  N N   . SER A 33  ? 0.74129 0.79747 0.96274 -0.14293 0.10781  -0.04184 33  SER A N   
173  C CA  . SER A 33  ? 0.72887 0.83877 0.93345 -0.14711 0.09714  -0.04688 33  SER A CA  
174  C C   . SER A 33  ? 0.67146 0.80970 0.88877 -0.13370 0.08038  -0.02678 33  SER A C   
175  O O   . SER A 33  ? 0.69008 0.85746 0.89631 -0.11751 0.07393  -0.01517 33  SER A O   
176  C CB  . SER A 33  ? 0.77275 0.89544 0.95720 -0.13734 0.10394  -0.04794 33  SER A CB  
177  N N   . LEU A 34  ? 0.65423 0.77749 0.89050 -0.13832 0.07538  -0.02162 34  LEU A N   
178  C CA  . LEU A 34  ? 0.66858 0.81724 0.91673 -0.12793 0.06060  -0.00562 34  LEU A CA  
179  C C   . LEU A 34  ? 0.70483 0.90981 0.94050 -0.13712 0.04919  -0.01909 34  LEU A C   
180  O O   . LEU A 34  ? 0.71341 0.93556 0.93689 -0.15923 0.05311  -0.04454 34  LEU A O   
181  C CB  . LEU A 34  ? 0.58240 0.70055 0.85182 -0.13033 0.05898  0.00221  34  LEU A CB  
182  C CG  . LEU A 34  ? 0.55419 0.62539 0.83644 -0.12074 0.06904  0.00917  34  LEU A CG  
183  C CD1 . LEU A 34  ? 0.56129 0.60747 0.85800 -0.11919 0.06514  0.01684  34  LEU A CD1 
184  C CD2 . LEU A 34  ? 0.58989 0.66584 0.88216 -0.10186 0.07117  0.02330  34  LEU A CD2 
185  N N   . ARG A 35  ? 0.67198 0.90868 0.91051 -0.11947 0.03613  -0.00405 35  ARG A N   
186  C CA  . ARG A 35  ? 0.70899 1.00963 0.94043 -0.12247 0.02291  -0.01674 35  ARG A CA  
187  C C   . ARG A 35  ? 0.73133 1.03523 0.97821 -0.15175 0.02372  -0.03504 35  ARG A C   
188  O O   . ARG A 35  ? 0.76053 1.02405 1.02388 -0.15431 0.02659  -0.02349 35  ARG A O   
189  C CB  . ARG A 35  ? 0.73405 1.05883 0.96380 -0.09227 0.01078  0.00563  35  ARG A CB  
190  C CG  . ARG A 35  ? 0.72263 1.12239 0.94820 -0.08811 -0.00495 -0.00682 35  ARG A CG  
191  C CD  . ARG A 35  ? 0.77617 1.18137 1.02656 -0.09332 -0.01114 -0.00326 35  ARG A CD  
192  N NE  . ARG A 35  ? 0.79395 1.27655 1.04343 -0.08304 -0.02625 -0.01335 35  ARG A NE  
193  C CZ  . ARG A 35  ? 0.81008 1.31250 1.07889 -0.08422 -0.03264 -0.01259 35  ARG A CZ  
194  N NH1 . ARG A 35  ? 0.77910 1.22796 1.06658 -0.09601 -0.02584 -0.00164 35  ARG A NH1 
195  N NH2 . ARG A 35  ? 0.82847 1.41071 1.09713 -0.07122 -0.04653 -0.02408 35  ARG A NH2 
196  N N   . PRO A 36  ? 0.72061 1.07109 0.96051 -0.17568 0.02330  -0.06519 36  PRO A N   
197  C CA  . PRO A 36  ? 0.72994 1.07299 0.97933 -0.21073 0.03180  -0.08625 36  PRO A CA  
198  C C   . PRO A 36  ? 0.71313 1.06361 0.98166 -0.20569 0.02350  -0.07301 36  PRO A C   
199  O O   . PRO A 36  ? 0.73147 1.13086 1.00624 -0.18207 0.00745  -0.06187 36  PRO A O   
200  C CB  . PRO A 36  ? 0.76025 1.17619 1.00100 -0.23469 0.03024  -0.12363 36  PRO A CB  
201  C CG  . PRO A 36  ? 0.80097 1.23179 1.02135 -0.21715 0.02738  -0.12348 36  PRO A CG  
202  C CD  . PRO A 36  ? 0.80015 1.20951 1.01983 -0.17437 0.01816  -0.08436 36  PRO A CD  
203  N N   . ILE A 37  ? 0.66916 0.96678 0.94241 -0.22589 0.03605  -0.07383 37  ILE A N   
204  C CA  . ILE A 37  ? 0.70205 0.99662 0.99033 -0.22324 0.03099  -0.06124 37  ILE A CA  
205  C C   . ILE A 37  ? 0.70594 0.99520 0.99078 -0.26346 0.04612  -0.08659 37  ILE A C   
206  O O   . ILE A 37  ? 0.75859 0.99867 1.02595 -0.28872 0.06632  -0.10186 37  ILE A O   
207  C CB  . ILE A 37  ? 0.70804 0.93457 1.00135 -0.20177 0.03203  -0.03092 37  ILE A CB  
208  N N   . ASP A 38  ? 0.63466 0.97122 0.93360 -0.26992 0.03938  -0.09202 38  ASP A N   
209  C CA  . ASP A 38  ? 0.66599 0.99472 0.96144 -0.31057 0.05734  -0.11544 38  ASP A CA  
210  C C   . ASP A 38  ? 0.75168 0.98229 1.03257 -0.31243 0.07269  -0.09577 38  ASP A C   
211  O O   . ASP A 38  ? 0.75284 0.95277 1.03952 -0.28040 0.06168  -0.06468 38  ASP A O   
212  C CB  . ASP A 38  ? 0.64960 1.05758 0.96570 -0.31285 0.04602  -0.12509 38  ASP A CB  
213  C CG  . ASP A 38  ? 0.73835 1.11854 1.03489 -0.33997 0.06465  -0.14307 38  ASP A CG  
214  O OD1 . ASP A 38  ? 0.80236 1.12357 1.07187 -0.36592 0.08773  -0.15736 38  ASP A OD1 
215  O OD2 . ASP A 38  ? 0.71283 1.12757 1.01872 -0.33475 0.05846  -0.14295 38  ASP A OD2 
216  N N   . SER A 39  ? 0.79697 0.97624 1.05359 -0.34720 0.09897  -0.11439 39  SER A N   
217  C CA  . SER A 39  ? 0.79920 0.88260 1.03192 -0.34543 0.11523  -0.09564 39  SER A CA  
218  C C   . SER A 39  ? 0.72548 0.81777 0.96805 -0.33566 0.10660  -0.07917 39  SER A C   
219  O O   . SER A 39  ? 0.70820 0.73439 0.93836 -0.32325 0.11191  -0.05630 39  SER A O   
220  C CB  . SER A 39  ? 0.86104 0.88261 1.05090 -0.37218 0.14442  -0.11587 39  SER A CB  
221  N N   . ASN A 40  ? 0.70355 0.87662 0.96603 -0.33805 0.09357  -0.09095 40  ASN A N   
222  C CA  . ASN A 40  ? 0.71381 0.90285 0.98862 -0.32734 0.08464  -0.07680 40  ASN A CA  
223  C C   . ASN A 40  ? 0.65623 0.84665 0.95334 -0.29307 0.06487  -0.04629 40  ASN A C   
224  O O   . ASN A 40  ? 0.64521 0.83441 0.94859 -0.28198 0.05877  -0.03174 40  ASN A O   
225  C CB  . ASN A 40  ? 0.69439 0.97343 0.98560 -0.33167 0.07498  -0.09796 40  ASN A CB  
226  N N   . THR A 41  ? 0.61645 0.80304 0.91758 -0.26788 0.05355  -0.03487 41  THR A N   
227  C CA  . THR A 41  ? 0.60643 0.78444 0.92020 -0.22880 0.03567  -0.00576 41  THR A CA  
228  C C   . THR A 41  ? 0.61146 0.71613 0.91142 -0.21883 0.04135  0.01378  41  THR A C   
229  O O   . THR A 41  ? 0.62775 0.73318 0.93883 -0.19768 0.02954  0.03178  41  THR A O   
230  C CB  . THR A 41  ? 0.63099 0.81702 0.94860 -0.20937 0.02799  -0.00101 41  THR A CB  
231  O OG1 . THR A 41  ? 0.66172 0.91523 0.98405 -0.21779 0.02349  -0.02095 41  THR A OG1 
232  C CG2 . THR A 41  ? 0.61393 0.80180 0.94641 -0.17465 0.01286  0.02382  41  THR A CG2 
233  N N   . PHE A 42  ? 0.65086 0.69141 0.92331 -0.23203 0.06008  0.00964  42  PHE A N   
234  C CA  . PHE A 42  ? 0.65359 0.62285 0.90481 -0.21671 0.06593  0.02817  42  PHE A CA  
235  C C   . PHE A 42  ? 0.68656 0.59932 0.89973 -0.24610 0.09290  0.01725  42  PHE A C   
236  O O   . PHE A 42  ? 0.72794 0.58059 0.91126 -0.25320 0.11223  0.01213  42  PHE A O   
237  C CB  . PHE A 42  ? 0.66164 0.59738 0.91057 -0.19129 0.06341  0.03870  42  PHE A CB  
238  C CG  . PHE A 42  ? 0.62780 0.61034 0.91019 -0.16637 0.04272  0.04848  42  PHE A CG  
239  C CD1 . PHE A 42  ? 0.63094 0.61563 0.92807 -0.14107 0.02911  0.06594  42  PHE A CD1 
240  C CD2 . PHE A 42  ? 0.60338 0.62594 0.89879 -0.16956 0.03920  0.03879  42  PHE A CD2 
241  C CE1 . PHE A 42  ? 0.61233 0.63221 0.93681 -0.12327 0.01606  0.07240  42  PHE A CE1 
242  C CE2 . PHE A 42  ? 0.56290 0.61677 0.88096 -0.14769 0.02559  0.04893  42  PHE A CE2 
243  C CZ  . PHE A 42  ? 0.59465 0.64449 0.92745 -0.12657 0.01581  0.06515  42  PHE A CZ  
244  N N   . GLU A 43  ? 0.68087 0.60868 0.89217 -0.26376 0.09729  0.01308  43  GLU A N   
245  C CA  . GLU A 43  ? 0.70353 0.57558 0.87572 -0.29606 0.12739  0.00211  43  GLU A CA  
246  C C   . GLU A 43  ? 0.77244 0.57757 0.91391 -0.27255 0.12999  0.02804  43  GLU A C   
247  O O   . GLU A 43  ? 0.75045 0.57189 0.89477 -0.27334 0.12574  0.03410  43  GLU A O   
248  C CB  . GLU A 43  ? 0.65712 0.59577 0.84224 -0.32204 0.12781  -0.01995 43  GLU A CB  
249  N N   . MET A 44  ? 0.82617 0.55827 0.93626 -0.24873 0.13675  0.04275  44  MET A N   
250  C CA  . MET A 44  ? 0.86062 0.53624 0.93988 -0.21608 0.13463  0.06854  44  MET A CA  
251  C C   . MET A 44  ? 0.93995 0.53062 0.97609 -0.19462 0.15009  0.07776  44  MET A C   
252  O O   . MET A 44  ? 0.92953 0.51282 0.96853 -0.20245 0.15821  0.06533  44  MET A O   
253  C CB  . MET A 44  ? 0.75850 0.49280 0.87866 -0.18057 0.09989  0.08448  44  MET A CB  
254  C CG  . MET A 44  ? 0.76402 0.52359 0.91374 -0.15521 0.08287  0.08713  44  MET A CG  
255  S SD  . MET A 44  ? 0.71945 0.55723 0.92308 -0.12897 0.04880  0.09656  44  MET A SD  
256  C CE  . MET A 44  ? 0.67556 0.58319 0.91001 -0.16080 0.04554  0.08076  44  MET A CE  
257  N N   . ASN A 45  ? 1.00925 0.53651 1.00253 -0.16426 0.15407  0.09965  45  ASN A N   
258  C CA  . ASN A 45  ? 1.02895 0.47909 0.97975 -0.13058 0.16490  0.11232  45  ASN A CA  
259  C C   . ASN A 45  ? 1.00543 0.50778 0.99747 -0.08545 0.13197  0.12278  45  ASN A C   
260  O O   . ASN A 45  ? 0.96255 0.54792 1.00816 -0.08140 0.10394  0.12231  45  ASN A O   
261  C CB  . ASN A 45  ? 1.11373 0.47118 0.99243 -0.11130 0.18440  0.13222  45  ASN A CB  
262  C CG  . ASN A 45  ? 1.15322 0.54737 1.04181 -0.07638 0.15624  0.15178  45  ASN A CG  
263  O OD1 . ASN A 45  ? 1.10285 0.58878 1.05172 -0.07905 0.12748  0.14719  45  ASN A OD1 
264  N ND2 . ASN A 45  ? 1.19841 0.51759 1.02288 -0.04229 0.16598  0.17329  45  ASN A ND2 
265  N N   . GLY A 46  ? 1.02042 0.47161 0.98539 -0.05134 0.13813  0.13089  46  GLY A N   
266  C CA  . GLY A 46  ? 0.98036 0.48445 0.98541 -0.01038 0.11029  0.13669  46  GLY A CA  
267  C C   . GLY A 46  ? 0.97184 0.51884 0.99212 0.02194  0.08323  0.15108  46  GLY A C   
268  O O   . GLY A 46  ? 0.90591 0.52879 0.97997 0.03729  0.05723  0.14814  46  GLY A O   
269  N N   . LYS A 47  ? 1.02450 0.52276 0.99546 0.03074  0.09107  0.16507  47  LYS A N   
270  C CA  . LYS A 47  ? 0.95518 0.49708 0.93740 0.05922  0.06540  0.17638  47  LYS A CA  
271  C C   . LYS A 47  ? 0.90991 0.53832 0.95314 0.02959  0.04630  0.16552  47  LYS A C   
272  O O   . LYS A 47  ? 0.88385 0.58030 0.96938 0.04841  0.01999  0.16466  47  LYS A O   
273  C CB  . LYS A 47  ? 1.01230 0.47859 0.92151 0.07194  0.08094  0.19383  47  LYS A CB  
274  N N   . ALA A 48  ? 0.86047 0.48865 0.90832 -0.01657 0.06076  0.15508  48  ALA A N   
275  C CA  . ALA A 48  ? 0.82537 0.53234 0.92719 -0.04009 0.04436  0.14532  48  ALA A CA  
276  C C   . ALA A 48  ? 0.74558 0.51510 0.90424 -0.03788 0.02842  0.13550  48  ALA A C   
277  O O   . ALA A 48  ? 0.72120 0.55290 0.92227 -0.03427 0.00883  0.13339  48  ALA A O   
278  C CB  . ALA A 48  ? 0.84962 0.55012 0.94392 -0.08608 0.06355  0.13381  48  ALA A CB  
279  N N   . LEU A 49  ? 0.76701 0.51606 0.92332 -0.04178 0.03965  0.12873  49  LEU A N   
280  C CA  . LEU A 49  ? 0.71678 0.51947 0.92085 -0.04162 0.02836  0.11960  49  LEU A CA  
281  C C   . LEU A 49  ? 0.71584 0.55572 0.94767 -0.00742 0.00809  0.12462  49  LEU A C   
282  O O   . LEU A 49  ? 0.67189 0.56896 0.94824 -0.01060 -0.00442 0.11855  49  LEU A O   
283  C CB  . LEU A 49  ? 0.74026 0.50882 0.93060 -0.04794 0.04518  0.11145  49  LEU A CB  
284  C CG  . LEU A 49  ? 0.66702 0.48668 0.89887 -0.05784 0.03909  0.09999  49  LEU A CG  
285  C CD1 . LEU A 49  ? 0.63929 0.50553 0.89254 -0.08786 0.03517  0.09205  49  LEU A CD1 
286  C CD2 . LEU A 49  ? 0.67525 0.45658 0.88782 -0.06348 0.05714  0.09086  49  LEU A CD2 
287  N N   . LEU A 50  ? 0.68448 0.49245 0.88759 0.02585  0.00635  0.13443  50  LEU A N   
288  C CA  . LEU A 50  ? 0.67088 0.52520 0.90195 0.05926  -0.01351 0.13445  50  LEU A CA  
289  C C   . LEU A 50  ? 0.64057 0.54983 0.90148 0.05277  -0.03063 0.13242  50  LEU A C   
290  O O   . LEU A 50  ? 0.62477 0.59282 0.93085 0.05647  -0.04344 0.12296  50  LEU A O   
291  C CB  . LEU A 50  ? 0.73704 0.54956 0.92441 0.10200  -0.01343 0.14584  50  LEU A CB  
292  C CG  . LEU A 50  ? 0.79172 0.54256 0.94475 0.11698  0.00522  0.14824  50  LEU A CG  
293  N N   . LEU A 51  ? 0.63933 0.52716 0.87365 0.04091  -0.02792 0.13954  51  LEU A N   
294  C CA  . LEU A 51  ? 0.65530 0.58955 0.91303 0.03492  -0.04220 0.13713  51  LEU A CA  
295  C C   . LEU A 51  ? 0.58402 0.56719 0.89058 0.01011  -0.04512 0.12598  51  LEU A C   
296  O O   . LEU A 51  ? 0.57125 0.59900 0.90717 0.01021  -0.05670 0.12008  51  LEU A O   
297  C CB  . LEU A 51  ? 0.66553 0.56532 0.88523 0.02141  -0.03433 0.14548  51  LEU A CB  
298  C CG  . LEU A 51  ? 0.70974 0.54690 0.86765 0.04510  -0.02655 0.15974  51  LEU A CG  
299  C CD1 . LEU A 51  ? 0.78455 0.59322 0.90904 0.02519  -0.01606 0.16561  51  LEU A CD1 
300  C CD2 . LEU A 51  ? 0.74342 0.60647 0.90061 0.08854  -0.04624 0.16305  51  LEU A CD2 
301  N N   . LEU A 52  ? 0.54634 0.51906 0.85765 -0.00939 -0.03340 0.12243  52  LEU A N   
302  C CA  . LEU A 52  ? 0.53916 0.55065 0.88599 -0.02822 -0.03429 0.11488  52  LEU A CA  
303  C C   . LEU A 52  ? 0.53493 0.58221 0.91824 -0.01840 -0.04005 0.10746  52  LEU A C   
304  O O   . LEU A 52  ? 0.60009 0.64271 0.98552 -0.00310 -0.03903 0.10503  52  LEU A O   
305  C CB  . LEU A 52  ? 0.54967 0.54545 0.88711 -0.04918 -0.02119 0.11173  52  LEU A CB  
306  C CG  . LEU A 52  ? 0.61700 0.58100 0.92107 -0.06747 -0.00993 0.11283  52  LEU A CG  
307  C CD1 . LEU A 52  ? 0.57172 0.54203 0.87704 -0.09085 0.00057  0.10298  52  LEU A CD1 
308  C CD2 . LEU A 52  ? 0.63365 0.61587 0.93926 -0.07421 -0.01549 0.11529  52  LEU A CD2 
309  N N   . THR A 53  ? 0.47929 0.55975 0.88944 -0.02756 -0.04324 0.10276  53  THR A N   
310  C CA  . THR A 53  ? 0.45398 0.56425 0.89693 -0.02543 -0.04267 0.09339  53  THR A CA  
311  C C   . THR A 53  ? 0.50445 0.61016 0.95150 -0.03746 -0.03125 0.09303  53  THR A C   
312  O O   . THR A 53  ? 0.53449 0.62611 0.96410 -0.04792 -0.02701 0.09814  53  THR A O   
313  C CB  . THR A 53  ? 0.46893 0.60718 0.93238 -0.03094 -0.04661 0.08713  53  THR A CB  
314  O OG1 . THR A 53  ? 0.50488 0.63627 0.96289 -0.04536 -0.04058 0.09206  53  THR A OG1 
315  C CG2 . THR A 53  ? 0.49794 0.64244 0.95157 -0.01993 -0.05889 0.08751  53  THR A CG2 
316  N N   . LYS A 54  ? 0.49767 0.62006 0.96755 -0.03610 -0.02565 0.08502  54  LYS A N   
317  C CA  . LYS A 54  ? 0.47704 0.59329 0.94585 -0.04489 -0.01367 0.08546  54  LYS A CA  
318  C C   . LYS A 54  ? 0.48716 0.60183 0.94750 -0.05495 -0.00990 0.09158  54  LYS A C   
319  O O   . LYS A 54  ? 0.51483 0.62252 0.96004 -0.05883 -0.00468 0.09561  54  LYS A O   
320  C CB  . LYS A 54  ? 0.38404 0.51797 0.87806 -0.04406 -0.00481 0.07484  54  LYS A CB  
321  C CG  . LYS A 54  ? 0.36213 0.48539 0.84903 -0.05091 0.00944  0.07614  54  LYS A CG  
322  C CD  . LYS A 54  ? 0.35132 0.49048 0.86193 -0.05180 0.02144  0.06397  54  LYS A CD  
323  N N   . GLU A 55  ? 0.41329 0.53645 0.88113 -0.05686 -0.01263 0.09132  55  GLU A N   
324  C CA  . GLU A 55  ? 0.45109 0.57052 0.90702 -0.06046 -0.00925 0.09815  55  GLU A CA  
325  C C   . GLU A 55  ? 0.52836 0.64688 0.96496 -0.06180 -0.01637 0.10388  55  GLU A C   
326  O O   . GLU A 55  ? 0.56850 0.69211 0.99314 -0.06165 -0.01370 0.10798  55  GLU A O   
327  C CB  . GLU A 55  ? 0.40104 0.52565 0.86734 -0.06239 -0.00909 0.09465  55  GLU A CB  
328  N N   . ASP A 56  ? 0.57669 0.68973 1.00766 -0.06247 -0.02384 0.10306  56  ASP A N   
329  C CA  . ASP A 56  ? 0.58399 0.69316 0.99572 -0.07007 -0.02530 0.10474  56  ASP A CA  
330  C C   . ASP A 56  ? 0.61168 0.71627 1.01282 -0.07597 -0.01927 0.10151  56  ASP A C   
331  O O   . ASP A 56  ? 0.63655 0.75363 1.02719 -0.08523 -0.01782 0.09846  56  ASP A O   
332  C CB  . ASP A 56  ? 0.58512 0.67726 0.98492 -0.06957 -0.02970 0.10585  56  ASP A CB  
333  C CG  . ASP A 56  ? 0.57516 0.67598 0.98421 -0.06265 -0.03705 0.10676  56  ASP A CG  
334  O OD1 . ASP A 56  ? 0.59111 0.70845 1.01672 -0.06198 -0.03663 0.10489  56  ASP A OD1 
335  O OD2 . ASP A 56  ? 0.57916 0.66693 0.97478 -0.05736 -0.04163 0.10891  56  ASP A OD2 
336  N N   . PHE A 57  ? 0.63396 0.72601 1.03877 -0.07111 -0.01544 0.09936  57  PHE A N   
337  C CA  . PHE A 57  ? 0.62940 0.71685 1.02374 -0.07688 -0.00836 0.09459  57  PHE A CA  
338  C C   . PHE A 57  ? 0.64065 0.75069 1.03532 -0.07658 -0.00602 0.09535  57  PHE A C   
339  O O   . PHE A 57  ? 0.65436 0.77661 1.03589 -0.08384 -0.00427 0.09012  57  PHE A O   
340  C CB  . PHE A 57  ? 0.61496 0.68591 1.01457 -0.06853 -0.00376 0.09185  57  PHE A CB  
341  C CG  . PHE A 57  ? 0.63164 0.67298 1.01751 -0.06365 -0.00350 0.09159  57  PHE A CG  
342  C CD1 . PHE A 57  ? 0.64776 0.68621 1.03789 -0.05105 -0.01131 0.09595  57  PHE A CD1 
343  C CD2 . PHE A 57  ? 0.65629 0.66945 1.02002 -0.07004 0.00612  0.08660  57  PHE A CD2 
344  C CE1 . PHE A 57  ? 0.69795 0.70345 1.06634 -0.03999 -0.01018 0.09867  57  PHE A CE1 
345  C CE2 . PHE A 57  ? 0.70408 0.67703 1.04589 -0.06214 0.01049  0.08851  57  PHE A CE2 
346  C CZ  . PHE A 57  ? 0.72941 0.69723 1.07147 -0.04457 0.00201  0.09622  57  PHE A CZ  
347  N N   . ARG A 58  ? 0.57742 0.69229 0.98349 -0.06772 -0.00440 0.10071  58  ARG A N   
348  C CA  . ARG A 58  ? 0.52675 0.65212 0.92328 -0.06160 0.00058  0.10516  58  ARG A CA  
349  C C   . ARG A 58  ? 0.56534 0.71415 0.95077 -0.05983 -0.00607 0.10673  58  ARG A C   
350  O O   . ARG A 58  ? 0.57294 0.74192 0.94347 -0.05566 -0.00630 0.10549  58  ARG A O   
351  C CB  . ARG A 58  ? 0.43901 0.55267 0.84436 -0.05500 0.00913  0.11007  58  ARG A CB  
352  C CG  . ARG A 58  ? 0.39607 0.49848 0.81484 -0.05758 0.01876  0.10480  58  ARG A CG  
353  C CD  . ARG A 58  ? 0.36626 0.45647 0.78934 -0.05697 0.03325  0.10640  58  ARG A CD  
354  N NE  . ARG A 58  ? 0.36198 0.44935 0.80193 -0.06291 0.04524  0.09737  58  ARG A NE  
355  C CZ  . ARG A 58  ? 0.34557 0.44489 0.81431 -0.06865 0.04492  0.08580  58  ARG A CZ  
356  N NH1 . ARG A 58  ? 0.39236 0.50245 0.87273 -0.06879 0.03309  0.08331  58  ARG A NH1 
357  N NH2 . ARG A 58  ? 0.39489 0.50102 0.88139 -0.07385 0.05677  0.07462  58  ARG A NH2 
358  N N   . TYR A 59  ? 0.52974 0.68207 0.92232 -0.06163 -0.01194 0.10777  59  TYR A N   
359  C CA  . TYR A 59  ? 0.55040 0.73105 0.93632 -0.05894 -0.01739 0.10728  59  TYR A CA  
360  C C   . TYR A 59  ? 0.58941 0.79494 0.96847 -0.07285 -0.02032 0.09545  59  TYR A C   
361  O O   . TYR A 59  ? 0.64529 0.88967 1.01794 -0.06845 -0.02386 0.09063  59  TYR A O   
362  C CB  . TYR A 59  ? 0.55427 0.73166 0.94912 -0.06040 -0.02117 0.10909  59  TYR A CB  
363  N N   . ARG A 60  ? 0.59511 0.77965 0.97358 -0.08904 -0.01745 0.08885  60  ARG A N   
364  C CA  . ARG A 60  ? 0.59339 0.79288 0.96258 -0.10874 -0.01468 0.07406  60  ARG A CA  
365  C C   . ARG A 60  ? 0.57430 0.79752 0.93540 -0.10843 -0.01331 0.06586  60  ARG A C   
366  O O   . ARG A 60  ? 0.55401 0.82536 0.91218 -0.11034 -0.01727 0.05555  60  ARG A O   
367  C CB  . ARG A 60  ? 0.57716 0.73266 0.93848 -0.12315 -0.00729 0.07113  60  ARG A CB  
368  C CG  . ARG A 60  ? 0.57875 0.71750 0.93910 -0.12602 -0.00827 0.07620  60  ARG A CG  
369  C CD  . ARG A 60  ? 0.58410 0.67239 0.92518 -0.13519 0.00116  0.07556  60  ARG A CD  
370  N NE  . ARG A 60  ? 0.60293 0.67498 0.93480 -0.13806 0.00177  0.08041  60  ARG A NE  
371  C CZ  . ARG A 60  ? 0.60702 0.67787 0.92418 -0.16000 0.01152  0.07155  60  ARG A CZ  
372  N NH1 . ARG A 60  ? 0.59308 0.68304 0.90605 -0.18358 0.02127  0.05414  60  ARG A NH1 
373  N NH2 . ARG A 60  ? 0.62656 0.67933 0.93239 -0.16014 0.01285  0.07799  60  ARG A NH2 
374  N N   . SER A 61  ? 0.57242 0.76828 0.92983 -0.10465 -0.00808 0.06865  61  SER A N   
375  C CA  . SER A 61  ? 0.56448 0.77880 0.91059 -0.10326 -0.00582 0.06148  61  SER A CA  
376  C C   . SER A 61  ? 0.55133 0.75516 0.89585 -0.08072 -0.00440 0.07644  61  SER A C   
377  O O   . SER A 61  ? 0.54845 0.71950 0.89668 -0.07925 0.00288  0.08027  61  SER A O   
378  C CB  . SER A 61  ? 0.59099 0.77827 0.92895 -0.12057 0.00391  0.04931  61  SER A CB  
379  O OG  . SER A 61  ? 0.59799 0.74004 0.94197 -0.11269 0.00890  0.05909  61  SER A OG  
380  N N   . PRO A 62  ? 0.59413 0.82344 0.93046 -0.06208 -0.00870 0.08435  62  PRO A N   
381  C CA  . PRO A 62  ? 0.56403 0.76961 0.89166 -0.04236 -0.00132 0.09978  62  PRO A CA  
382  C C   . PRO A 62  ? 0.59217 0.78566 0.90656 -0.04227 0.00748  0.09774  62  PRO A C   
383  O O   . PRO A 62  ? 0.58414 0.74445 0.90019 -0.03829 0.01891  0.10559  62  PRO A O   
384  C CB  . PRO A 62  ? 0.54791 0.78177 0.85832 -0.01904 -0.00636 0.10780  62  PRO A CB  
385  C CG  . PRO A 62  ? 0.57495 0.84814 0.89820 -0.02799 -0.01792 0.09705  62  PRO A CG  
386  C CD  . PRO A 62  ? 0.57868 0.85801 0.91090 -0.05652 -0.01819 0.07896  62  PRO A CD  
387  N N   . HIS A 63  ? 0.61442 0.83693 0.91661 -0.04928 0.00394  0.08430  63  HIS A N   
388  C CA  . HIS A 63  ? 0.61105 0.82626 0.89553 -0.04714 0.01230  0.08171  63  HIS A CA  
389  C C   . HIS A 63  ? 0.57005 0.74657 0.86950 -0.06146 0.02266  0.07729  63  HIS A C   
390  O O   . HIS A 63  ? 0.56626 0.72195 0.85886 -0.05599 0.03420  0.08153  63  HIS A O   
391  C CB  . HIS A 63  ? 0.66472 0.92692 0.93348 -0.05367 0.00531  0.06375  63  HIS A CB  
392  C CG  . HIS A 63  ? 0.71441 1.02873 0.96823 -0.03392 -0.00676 0.06534  63  HIS A CG  
393  N ND1 . HIS A 63  ? 0.73187 1.08060 1.00097 -0.03778 -0.01733 0.05919  63  HIS A ND1 
394  C CD2 . HIS A 63  ? 0.77012 1.10998 0.99257 -0.00653 -0.00964 0.07234  63  HIS A CD2 
395  C CE1 . HIS A 63  ? 0.77465 1.17353 1.02654 -0.01258 -0.02734 0.06091  63  HIS A CE1 
396  N NE2 . HIS A 63  ? 0.78381 1.17686 1.00479 0.00879  -0.02347 0.06995  63  HIS A NE2 
397  N N   . SER A 64  ? 0.54410 0.70990 0.86101 -0.07768 0.02022  0.06875  64  SER A N   
398  C CA  . SER A 64  ? 0.54877 0.68057 0.87523 -0.08474 0.02931  0.06401  64  SER A CA  
399  C C   . SER A 64  ? 0.51202 0.62213 0.85801 -0.08705 0.02626  0.06729  64  SER A C   
400  O O   . SER A 64  ? 0.48617 0.57028 0.83502 -0.09106 0.03129  0.06155  64  SER A O   
401  C CB  . SER A 64  ? 0.57253 0.70414 0.88438 -0.10010 0.03444  0.04609  64  SER A CB  
402  N N   . GLY A 65  ? 0.51761 0.63655 0.87333 -0.08153 0.01858  0.07672  65  GLY A N   
403  C CA  . GLY A 65  ? 0.52334 0.62498 0.89462 -0.08132 0.01480  0.07999  65  GLY A CA  
404  C C   . GLY A 65  ? 0.49681 0.58298 0.88577 -0.07198 0.01976  0.08224  65  GLY A C   
405  O O   . GLY A 65  ? 0.48437 0.55458 0.88022 -0.06889 0.01850  0.07995  65  GLY A O   
406  N N   . ASP A 66  ? 0.47333 0.56499 0.86758 -0.06636 0.02702  0.08569  66  ASP A N   
407  C CA  . ASP A 66  ? 0.45083 0.53825 0.86707 -0.06162 0.03408  0.08296  66  ASP A CA  
408  C C   . ASP A 66  ? 0.46417 0.54196 0.88322 -0.05922 0.03833  0.07399  66  ASP A C   
409  O O   . ASP A 66  ? 0.42653 0.50343 0.86220 -0.05127 0.03497  0.07011  66  ASP A O   
410  C CB  . ASP A 66  ? 0.42928 0.51687 0.84326 -0.06109 0.04788  0.08630  66  ASP A CB  
411  N N   . GLU A 67  ? 0.46232 0.53398 0.86250 -0.06336 0.04551  0.06993  67  GLU A N   
412  C CA  . GLU A 67  ? 0.45324 0.51115 0.85309 -0.06012 0.05292  0.06051  67  GLU A CA  
413  C C   . GLU A 67  ? 0.48757 0.52320 0.87865 -0.05801 0.04726  0.05838  67  GLU A C   
414  O O   . GLU A 67  ? 0.53933 0.56070 0.93608 -0.04529 0.05028  0.05437  67  GLU A O   
415  C CB  . GLU A 67  ? 0.43989 0.49542 0.81722 -0.06713 0.06262  0.05488  67  GLU A CB  
416  N N   . LEU A 68  ? 0.50380 0.53497 0.87848 -0.06876 0.04082  0.06085  68  LEU A N   
417  C CA  . LEU A 68  ? 0.50901 0.50928 0.86841 -0.06938 0.04030  0.05983  68  LEU A CA  
418  C C   . LEU A 68  ? 0.53419 0.53002 0.90809 -0.05056 0.03273  0.06701  68  LEU A C   
419  O O   . LEU A 68  ? 0.55280 0.51835 0.91504 -0.03680 0.03618  0.06665  68  LEU A O   
420  C CB  . LEU A 68  ? 0.47000 0.47399 0.81351 -0.08789 0.03673  0.05900  68  LEU A CB  
421  C CG  . LEU A 68  ? 0.50030 0.50899 0.82415 -0.10790 0.04463  0.04551  68  LEU A CG  
422  C CD1 . LEU A 68  ? 0.54944 0.57631 0.86517 -0.12630 0.04039  0.04113  68  LEU A CD1 
423  C CD2 . LEU A 68  ? 0.56143 0.52562 0.86433 -0.11196 0.05984  0.03509  68  LEU A CD2 
424  N N   . TYR A 69  ? 0.49206 0.51751 0.88827 -0.04776 0.02331  0.07265  69  TYR A N   
425  C CA  . TYR A 69  ? 0.49080 0.52385 0.90328 -0.03090 0.01458  0.07562  69  TYR A CA  
426  C C   . TYR A 69  ? 0.50991 0.55041 0.93892 -0.01275 0.01858  0.06841  69  TYR A C   
427  O O   . TYR A 69  ? 0.56060 0.58968 0.98456 0.00819  0.01482  0.06878  69  TYR A O   
428  C CB  . TYR A 69  ? 0.47725 0.54220 0.91212 -0.03545 0.00757  0.07828  69  TYR A CB  
429  C CG  . TYR A 69  ? 0.48489 0.56811 0.93900 -0.02114 -0.00224 0.07680  69  TYR A CG  
430  C CD1 . TYR A 69  ? 0.52483 0.59900 0.96591 -0.01639 -0.01241 0.08320  69  TYR A CD1 
431  C CD2 . TYR A 69  ? 0.44301 0.55746 0.92805 -0.01353 -0.00054 0.06654  69  TYR A CD2 
432  C CE1 . TYR A 69  ? 0.53490 0.63145 0.99076 -0.00149 -0.02308 0.08045  69  TYR A CE1 
433  C CE2 . TYR A 69  ? 0.44750 0.59090 0.95244 -0.00099 -0.01098 0.06054  69  TYR A CE2 
434  C CZ  . TYR A 69  ? 0.51573 0.65051 1.00479 0.00646  -0.02347 0.06804  69  TYR A CZ  
435  O OH  . TYR A 69  ? 0.58938 0.75817 1.09544 0.02081  -0.03549 0.06079  69  TYR A OH  
436  N N   . GLU A 70  ? 0.49347 0.55368 0.93968 -0.01840 0.02729  0.06176  70  GLU A N   
437  C CA  . GLU A 70  ? 0.51116 0.58793 0.97861 -0.00312 0.03295  0.05154  70  GLU A CA  
438  C C   . GLU A 70  ? 0.54552 0.58776 0.99000 0.01181  0.03871  0.04963  70  GLU A C   
439  O O   . GLU A 70  ? 0.59796 0.64803 1.05268 0.03693  0.03733  0.04446  70  GLU A O   
440  C CB  . GLU A 70  ? 0.47051 0.56681 0.95358 -0.01632 0.04630  0.04487  70  GLU A CB  
441  C CG  . GLU A 70  ? 0.43416 0.54912 0.92979 -0.03127 0.04685  0.04790  70  GLU A CG  
442  C CD  . GLU A 70  ? 0.45229 0.59928 0.97861 -0.02611 0.03886  0.04152  70  GLU A CD  
443  O OE1 . GLU A 70  ? 0.42103 0.59216 0.96849 -0.00980 0.03502  0.03076  70  GLU A OE1 
444  O OE2 . GLU A 70  ? 0.46181 0.61281 0.99033 -0.03704 0.03652  0.04576  70  GLU A OE2 
445  N N   . LEU A 71  ? 0.55528 0.56037 0.96727 -0.00244 0.04621  0.05190  71  LEU A N   
446  C CA  . LEU A 71  ? 0.65949 0.61915 1.04239 0.00793  0.05618  0.04894  71  LEU A CA  
447  C C   . LEU A 71  ? 0.71624 0.64682 1.08097 0.03046  0.05000  0.05698  71  LEU A C   
448  O O   . LEU A 71  ? 0.73641 0.64727 1.09213 0.05897  0.05423  0.05563  71  LEU A O   
449  C CB  . LEU A 71  ? 0.59422 0.52380 0.94566 -0.01838 0.06624  0.04565  71  LEU A CB  
450  C CG  . LEU A 71  ? 0.54862 0.49591 0.90328 -0.03393 0.07529  0.03650  71  LEU A CG  
451  N N   . LEU A 72  ? 0.68960 0.61639 1.04534 0.02109  0.04073  0.06601  72  LEU A N   
452  C CA  . LEU A 72  ? 0.69110 0.58767 1.02314 0.04299  0.03562  0.07565  72  LEU A CA  
453  C C   . LEU A 72  ? 0.74146 0.67519 1.09899 0.07885  0.02350  0.07472  72  LEU A C   
454  O O   . LEU A 72  ? 0.80381 0.70932 1.13829 0.11243  0.02473  0.07873  72  LEU A O   
455  C CB  . LEU A 72  ? 0.61383 0.51152 0.93817 0.02468  0.02751  0.08372  72  LEU A CB  
456  C CG  . LEU A 72  ? 0.65499 0.51768 0.94774 0.04418  0.02368  0.09536  72  LEU A CG  
457  N N   . GLN A 73  ? 0.67836 0.67584 1.08146 0.07267  0.01365  0.06766  73  GLN A N   
458  C CA  . GLN A 73  ? 0.69650 0.74480 1.13134 0.10123  0.00280  0.05985  73  GLN A CA  
459  C C   . GLN A 73  ? 0.73792 0.78393 1.17475 0.12691  0.01184  0.05144  73  GLN A C   
460  O O   . GLN A 73  ? 0.74367 0.79952 1.17748 0.16614  0.00469  0.05058  73  GLN A O   
461  C CB  . GLN A 73  ? 0.61290 0.72458 1.09559 0.08102  -0.00180 0.04889  73  GLN A CB  
462  C CG  . GLN A 73  ? 0.58334 0.69509 1.06309 0.05794  -0.00893 0.05668  73  GLN A CG  
463  C CD  . GLN A 73  ? 0.60314 0.70834 1.06454 0.07668  -0.02355 0.06506  73  GLN A CD  
464  O OE1 . GLN A 73  ? 0.58323 0.71118 1.04958 0.10837  -0.03317 0.06095  73  GLN A OE1 
465  N NE2 . GLN A 73  ? 0.64952 0.72736 1.08825 0.05928  -0.02532 0.07618  73  GLN A NE2 
466  N N   . HIS A 74  ? 0.85870 0.89316 1.29797 0.10810  0.02742  0.04503  74  HIS A N   
467  C CA  . HIS A 74  ? 0.88849 0.91892 1.32900 0.13101  0.03846  0.03571  74  HIS A CA  
468  C C   . HIS A 74  ? 0.95664 0.91690 1.34557 0.15982  0.04492  0.04547  74  HIS A C   
469  O O   . HIS A 74  ? 0.98355 0.94487 1.37036 0.19864  0.04725  0.04113  74  HIS A O   
470  C CB  . HIS A 74  ? 0.87237 0.89882 1.31868 0.10253  0.05523  0.02741  74  HIS A CB  
471  C CG  . HIS A 74  ? 0.85090 0.94076 1.34421 0.08521  0.05617  0.01570  74  HIS A CG  
472  N ND1 . HIS A 74  ? 0.86888 0.97263 1.37119 0.05446  0.05376  0.01975  74  HIS A ND1 
473  C CD2 . HIS A 74  ? 0.82189 0.96090 1.35261 0.09371  0.06277  -0.00078 74  HIS A CD2 
474  C CE1 . HIS A 74  ? 0.79414 0.94379 1.33246 0.04381  0.06100  0.00761  74  HIS A CE1 
475  N NE2 . HIS A 74  ? 0.77565 0.95062 1.33410 0.06466  0.06685  -0.00629 74  HIS A NE2 
476  N N   . ILE A 75  ? 0.88709 0.78440 1.23195 0.14200  0.05031  0.05765  75  ILE A N   
477  C CA  . ILE A 75  ? 0.92008 0.73742 1.20747 0.16601  0.06178  0.06757  75  ILE A CA  
478  C C   . ILE A 75  ? 0.91869 0.74300 1.19550 0.21078  0.04660  0.07820  75  ILE A C   
479  O O   . ILE A 75  ? 0.95844 0.73895 1.19889 0.25355  0.05334  0.08414  75  ILE A O   
480  C CB  . ILE A 75  ? 0.83229 0.58559 1.07742 0.12859  0.07477  0.07365  75  ILE A CB  
481  C CG1 . ILE A 75  ? 0.85706 0.60412 1.10544 0.09151  0.09021  0.06029  75  ILE A CG1 
482  C CG2 . ILE A 75  ? 0.90724 0.56873 1.08671 0.15046  0.09052  0.08492  75  ILE A CG2 
483  N N   . LEU A 76  ? 0.85666 0.73569 1.16169 0.20439  0.02633  0.08042  76  LEU A N   
484  C CA  . LEU A 76  ? 0.85932 0.75621 1.15524 0.24592  0.00905  0.08844  76  LEU A CA  
485  C C   . LEU A 76  ? 0.88730 0.84885 1.21667 0.29076  -0.00144 0.07604  76  LEU A C   
486  O O   . LEU A 76  ? 0.90430 0.86433 1.20945 0.34131  -0.01122 0.08311  76  LEU A O   
487  C CB  . LEU A 76  ? 0.75356 0.69839 1.07492 0.22290  -0.00882 0.08959  76  LEU A CB  
488  N N   . LYS A 77  ? 0.85306 0.87383 1.23572 0.27491  0.00123  0.05691  77  LYS A N   
489  C CA  . LYS A 77  ? 0.85270 0.94802 1.27532 0.31269  -0.00704 0.03980  77  LYS A CA  
490  C C   . LYS A 77  ? 0.97022 1.01913 1.36002 0.35538  0.00688  0.04173  77  LYS A C   
491  O O   . LYS A 77  ? 0.96850 1.06400 1.36997 0.40709  -0.00311 0.03422  77  LYS A O   
492  C CB  . LYS A 77  ? 0.80035 0.97171 1.28930 0.27671  -0.00411 0.01722  77  LYS A CB  
493  N N   . GLN A 78  ? 1.15333 1.11485 1.50208 0.33625  0.03012  0.04947  78  GLN A N   
494  C CA  . GLN A 78  ? 1.20956 1.11534 1.52225 0.37365  0.04803  0.05019  78  GLN A CA  
495  C C   . GLN A 78  ? 1.26698 1.09927 1.51069 0.42581  0.04891  0.07084  78  GLN A C   
496  O O   . GLN A 78  ? 1.30464 1.11779 1.52226 0.42535  0.03835  0.08606  78  GLN A O   
497  C CB  . GLN A 78  ? 1.23679 1.07165 1.52500 0.33182  0.07462  0.04840  78  GLN A CB  
498  N N   . ILE A 88  ? 1.15350 0.75591 0.91516 0.30758  -0.04407 0.26505  88  ILE A N   
499  C CA  . ILE A 88  ? 1.25984 0.83013 0.96377 0.31018  -0.03921 0.27830  88  ILE A CA  
500  C C   . ILE A 88  ? 1.34095 0.78756 0.97017 0.28291  0.00456  0.29527  88  ILE A C   
501  O O   . ILE A 88  ? 1.32173 0.75501 0.98131 0.22629  0.02500  0.28408  88  ILE A O   
502  C CB  . ILE A 88  ? 1.34310 0.92605 0.99574 0.38123  -0.06126 0.29151  88  ILE A CB  
503  N N   . ARG A 89  ? 1.40357 0.76853 0.93821 0.32017  0.01959  0.31759  89  ARG A N   
504  C CA  . ARG A 89  ? 1.42373 0.68205 0.89041 0.28794  0.06430  0.32454  89  ARG A CA  
505  C C   . ARG A 89  ? 1.41999 0.66643 0.88720 0.23401  0.08101  0.32326  89  ARG A C   
506  O O   . ARG A 89  ? 1.42850 0.61730 0.88126 0.18341  0.11757  0.31659  89  ARG A O   
507  C CB  . ARG A 89  ? 1.43155 0.63549 0.90098 0.26457  0.09200  0.31677  89  ARG A CB  
508  N N   . LEU A 90  ? 1.40339 0.72641 0.90087 0.23795  0.05310  0.31956  90  LEU A N   
509  C CA  . LEU A 90  ? 1.38976 0.72570 0.90128 0.18474  0.06590  0.30999  90  LEU A CA  
510  C C   . LEU A 90  ? 1.49782 0.72513 0.90139 0.18815  0.10104  0.33219  90  LEU A C   
511  O O   . LEU A 90  ? 1.51316 0.71586 0.85897 0.23755  0.09527  0.34477  90  LEU A O   
512  C CB  . LEU A 90  ? 1.28939 0.74172 0.86602 0.18696  0.02714  0.29478  90  LEU A CB  
513  N N   . PRO A 91  ? 1.51235 0.70295 0.90777 0.12933  0.13538  0.32466  91  PRO A N   
514  C CA  . PRO A 91  ? 1.55042 0.66887 0.86884 0.12087  0.16798  0.33059  91  PRO A CA  
515  C C   . PRO A 91  ? 1.60851 0.74534 0.88583 0.15950  0.14789  0.34552  91  PRO A C   
516  O O   . PRO A 91  ? 1.56435 0.78439 0.88696 0.17165  0.11244  0.34286  91  PRO A O   
517  C CB  . PRO A 91  ? 1.52886 0.64519 0.87476 0.04621  0.19959  0.31143  91  PRO A CB  
518  C CG  . PRO A 91  ? 1.47248 0.63409 0.89618 0.01800  0.19198  0.29541  91  PRO A CG  
519  C CD  . PRO A 91  ? 1.43291 0.67859 0.91130 0.06437  0.14209  0.29715  91  PRO A CD  
520  N N   . ALA A 92  ? 1.67276 0.74062 0.86939 0.17766  0.17016  0.35557  92  ALA A N   
521  C CA  . ALA A 92  ? 1.71208 0.79370 0.86208 0.21419  0.15385  0.36847  92  ALA A CA  
522  C C   . ALA A 92  ? 1.67327 0.79313 0.84449 0.17315  0.15472  0.36283  92  ALA A C   
523  O O   . ALA A 92  ? 1.66160 0.83786 0.83203 0.20096  0.12398  0.36799  92  ALA A O   
524  C CB  . ALA A 92  ? 1.85615 0.84441 0.91118 0.23525  0.18531  0.37970  92  ALA A CB  
525  N N   . HIS A 93  ? 1.66083 0.75947 0.85418 0.10676  0.18915  0.34845  93  HIS A N   
526  C CA  . HIS A 93  ? 1.63576 0.77550 0.85418 0.06446  0.19336  0.33980  93  HIS A CA  
527  C C   . HIS A 93  ? 1.56345 0.84235 0.89898 0.06301  0.14475  0.31582  93  HIS A C   
528  O O   . HIS A 93  ? 1.51223 0.86083 0.88316 0.05042  0.12945  0.30279  93  HIS A O   
529  C CB  . HIS A 93  ? 1.62708 0.74453 0.86836 -0.00728 0.23632  0.31780  93  HIS A CB  
530  C CG  . HIS A 93  ? 1.57052 0.70660 0.87677 -0.03594 0.23908  0.30117  93  HIS A CG  
531  N N   . LEU A 94  ? 1.53819 0.85466 0.93150 0.07561  0.12271  0.30914  94  LEU A N   
532  C CA  . LEU A 94  ? 1.48097 0.91839 0.98127 0.07250  0.08194  0.28641  94  LEU A CA  
533  C C   . LEU A 94  ? 1.46070 0.94292 0.96987 0.13160  0.04154  0.29184  94  LEU A C   
534  O O   . LEU A 94  ? 1.36788 0.93268 0.96027 0.13101  0.01334  0.27422  94  LEU A O   
535  C CB  . LEU A 94  ? 1.42456 0.88471 0.99647 0.03104  0.09018  0.26846  94  LEU A CB  
536  C CG  . LEU A 94  ? 1.41322 0.83664 0.97949 -0.02807 0.13134  0.25842  94  LEU A CG  
537  C CD1 . LEU A 94  ? 1.35976 0.80001 0.98368 -0.05941 0.13817  0.24233  94  LEU A CD1 
538  C CD2 . LEU A 94  ? 1.36597 0.85364 0.96918 -0.05731 0.12834  0.24240  94  LEU A CD2 
539  N N   . ARG A 95  ? 1.46185 0.89278 0.88458 0.18364  0.03949  0.31494  95  ARG A N   
540  C CA  . ARG A 95  ? 1.44035 0.92462 0.87045 0.24352  0.00023  0.31721  95  ARG A CA  
541  C C   . ARG A 95  ? 1.37683 0.97460 0.86216 0.24870  -0.03737 0.29657  95  ARG A C   
542  O O   . ARG A 95  ? 1.38097 1.05238 0.90096 0.28533  -0.07251 0.28699  95  ARG A O   
543  C CB  . ARG A 95  ? 1.51328 0.90994 0.82765 0.30433  0.00911  0.34875  95  ARG A CB  
544  N N   . LEU A 96  ? 1.33562 0.95072 0.83049 0.21157  -0.02893 0.28686  96  LEU A N   
545  C CA  . LEU A 96  ? 1.26926 0.98519 0.81550 0.21085  -0.05990 0.26451  96  LEU A CA  
546  C C   . LEU A 96  ? 1.19782 0.99955 0.85549 0.18299  -0.07831 0.23684  96  LEU A C   
547  O O   . LEU A 96  ? 1.18252 0.96755 0.87752 0.16107  -0.06661 0.23547  96  LEU A O   
548  C CB  . LEU A 96  ? 1.28395 0.98718 0.80608 0.17898  -0.04174 0.26200  96  LEU A CB  
549  C CG  . LEU A 96  ? 1.25926 0.95425 0.82515 0.11648  -0.01400 0.25031  96  LEU A CG  
550  C CD1 . LEU A 96  ? 1.26348 0.97760 0.81793 0.09595  -0.00733 0.24165  96  LEU A CD1 
551  C CD2 . LEU A 96  ? 1.33964 0.93568 0.85828 0.09572  0.02657  0.26739  96  LEU A CD2 
552  N N   . GLN A 97  ? 1.12870 1.02014 0.83532 0.18385  -0.10555 0.21380  97  GLN A N   
553  C CA  . GLN A 97  ? 1.07620 1.04279 0.88003 0.15995  -0.12046 0.18769  97  GLN A CA  
554  C C   . GLN A 97  ? 1.04096 1.00135 0.88819 0.10671  -0.09902 0.17883  97  GLN A C   
555  O O   . GLN A 97  ? 1.07458 1.00989 0.89273 0.08724  -0.08197 0.18192  97  GLN A O   
556  C CB  . GLN A 97  ? 1.05941 1.11820 0.89822 0.17296  -0.15097 0.16246  97  GLN A CB  
557  C CG  . GLN A 97  ? 1.12928 1.21644 0.93236 0.22870  -0.17660 0.16571  97  GLN A CG  
558  C CD  . GLN A 97  ? 1.20004 1.39065 1.04447 0.23546  -0.20608 0.13352  97  GLN A CD  
559  O OE1 . GLN A 97  ? 1.19029 1.42436 1.09342 0.19644  -0.20520 0.10862  97  GLN A OE1 
560  N NE2 . GLN A 97  ? 1.26549 1.49656 1.07702 0.28614  -0.23118 0.13227  97  GLN A NE2 
561  N N   . PRO A 98  ? 0.94137 0.92709 0.85654 0.08495  -0.09928 0.16738  98  PRO A N   
562  C CA  . PRO A 98  ? 0.92382 0.90354 0.87489 0.04135  -0.07914 0.16100  98  PRO A CA  
563  C C   . PRO A 98  ? 0.91146 0.93302 0.88712 0.02183  -0.08078 0.14396  98  PRO A C   
564  O O   . PRO A 98  ? 0.92122 0.93060 0.90383 -0.00727 -0.06132 0.14218  98  PRO A O   
565  C CB  . PRO A 98  ? 0.83962 0.84621 0.85428 0.03281  -0.08496 0.15199  98  PRO A CB  
566  C CG  . PRO A 98  ? 0.85030 0.84736 0.84548 0.06856  -0.09781 0.16105  98  PRO A CG  
567  C CD  . PRO A 98  ? 0.90445 0.92050 0.85997 0.10160  -0.11537 0.16161  98  PRO A CD  
568  N N   . ILE A 99  ? 0.90690 0.98066 0.89611 0.03689  -0.10250 0.12882  99  ILE A N   
569  C CA  . ILE A 99  ? 0.88652 0.99476 0.89535 0.01845  -0.10187 0.11082  99  ILE A CA  
570  C C   . ILE A 99  ? 0.95011 1.02019 0.90069 0.01307  -0.08500 0.12174  99  ILE A C   
571  O O   . ILE A 99  ? 0.93356 1.01524 0.89898 -0.00998 -0.07370 0.11112  99  ILE A O   
572  C CB  . ILE A 99  ? 0.79752 0.96860 0.82712 0.03374  -0.12677 0.08884  99  ILE A CB  
573  C CG1 . ILE A 99  ? 0.78273 0.98343 0.82895 0.01355  -0.12338 0.06797  99  ILE A CG1 
574  C CG2 . ILE A 99  ? 0.92178 1.09232 0.89404 0.07271  -0.14328 0.09854  99  ILE A CG2 
575  N N   . TYR A 100 ? 0.97286 0.99266 0.85340 0.03483  -0.08010 0.14340  100 TYR A N   
576  C CA  . TYR A 100 ? 1.05213 1.02509 0.86755 0.02917  -0.05931 0.15578  100 TYR A CA  
577  C C   . TYR A 100 ? 1.09374 1.00505 0.89044 0.00295  -0.02661 0.16953  100 TYR A C   
578  O O   . TYR A 100 ? 1.15360 1.01819 0.89267 -0.00606 -0.00329 0.17977  100 TYR A O   
579  C CB  . TYR A 100 ? 1.13345 1.07948 0.86941 0.07039  -0.06907 0.17215  100 TYR A CB  
580  C CG  . TYR A 100 ? 1.10682 1.12212 0.85972 0.10153  -0.10442 0.15667  100 TYR A CG  
581  C CD1 . TYR A 100 ? 1.10489 1.18004 0.88299 0.09201  -0.11638 0.13222  100 TYR A CD1 
582  C CD2 . TYR A 100 ? 1.14729 1.17217 0.89202 0.13961  -0.12457 0.16328  100 TYR A CD2 
583  C CE1 . TYR A 100 ? 1.08213 1.22744 0.87777 0.11530  -0.14691 0.11225  100 TYR A CE1 
584  C CE2 . TYR A 100 ? 1.17756 1.27922 0.94254 0.16628  -0.15692 0.14385  100 TYR A CE2 
585  C CZ  . TYR A 100 ? 1.12498 1.28812 0.91611 0.15171  -0.16769 0.11703  100 TYR A CZ  
586  O OH  . TYR A 100 ? 1.07044 1.31635 0.88403 0.17287  -0.19801 0.09203  100 TYR A OH  
587  N N   . TRP A 101 ? 1.03732 0.94873 0.87939 -0.01143 -0.02259 0.16788  101 TRP A N   
588  C CA  . TRP A 101 ? 1.05900 0.92239 0.88895 -0.04056 0.00844  0.17477  101 TRP A CA  
589  C C   . TRP A 101 ? 1.01746 0.90662 0.87306 -0.07582 0.02584  0.15991  101 TRP A C   
590  O O   . TRP A 101 ? 1.00724 0.95637 0.92640 -0.08470 0.01414  0.14231  101 TRP A O   
591  C CB  . TRP A 101 ? 1.02893 0.89857 0.90604 -0.04692 0.00543  0.17255  101 TRP A CB  
592  C CG  . TRP A 101 ? 1.01529 0.84849 0.86168 -0.01529 -0.00359 0.18807  101 TRP A CG  
593  C CD1 . TRP A 101 ? 1.06935 0.86963 0.85183 0.02252  -0.01143 0.20400  101 TRP A CD1 
594  C CD2 . TRP A 101 ? 0.96944 0.79783 0.84591 -0.01467 -0.00589 0.18881  101 TRP A CD2 
595  N NE1 . TRP A 101 ? 1.08549 0.86113 0.85780 0.04859  -0.01827 0.21463  101 TRP A NE1 
596  C CE2 . TRP A 101 ? 1.01274 0.80392 0.84307 0.02431  -0.01427 0.20505  101 TRP A CE2 
597  C CE3 . TRP A 101 ? 0.93683 0.79045 0.87227 -0.04061 -0.00188 0.17716  101 TRP A CE3 
598  C CZ2 . TRP A 101 ? 1.03669 0.81371 0.88063 0.03576  -0.01724 0.20901  101 TRP A CZ2 
599  C CZ3 . TRP A 101 ? 0.91272 0.75173 0.85964 -0.03109 -0.00516 0.18127  101 TRP A CZ3 
600  C CH2 . TRP A 101 ? 0.96115 0.76149 0.86399 0.00558  -0.01205 0.19658  101 TRP A CH2 
601  N N   . SER A 102 ? 1.07158 0.91383 0.87561 -0.09485 0.05600  0.16639  102 SER A N   
602  C CA  . SER A 102 ? 1.05886 0.93069 0.89156 -0.13016 0.07568  0.14992  102 SER A CA  
603  C C   . SER A 102 ? 1.01715 0.90715 0.90103 -0.15703 0.08639  0.13958  102 SER A C   
604  O O   . SER A 102 ? 1.05989 0.93011 0.95016 -0.15106 0.08164  0.14635  102 SER A O   
605  C CB  . SER A 102 ? 1.13110 0.95044 0.89393 -0.14669 0.10841  0.15683  102 SER A CB  
606  O OG  . SER A 102 ? 1.17402 0.92433 0.89386 -0.16283 0.13719  0.16781  102 SER A OG  
607  N N   . ARG A 103 ? 0.70511 0.74696 0.78955 0.02767  0.17598  0.04489  103 ARG A N   
608  C CA  . ARG A 103 ? 0.66425 0.71685 0.79144 0.01052  0.16697  0.03144  103 ARG A CA  
609  C C   . ARG A 103 ? 0.68213 0.70636 0.81722 0.00280  0.18131  0.03322  103 ARG A C   
610  O O   . ARG A 103 ? 0.72433 0.74644 0.87327 -0.00690 0.16808  0.02342  103 ARG A O   
611  C CB  . ARG A 103 ? 0.62129 0.69366 0.78955 -0.00086 0.16983  0.02317  103 ARG A CB  
612  C CG  . ARG A 103 ? 0.64816 0.73687 0.85804 -0.01623 0.14936  0.00813  103 ARG A CG  
613  C CD  . ARG A 103 ? 0.61938 0.73561 0.86773 -0.02128 0.14416  0.00075  103 ARG A CD  
614  N NE  . ARG A 103 ? 0.57670 0.69134 0.86243 -0.02804 0.17169  0.00404  103 ARG A NE  
615  C CZ  . ARG A 103 ? 0.57544 0.71231 0.90217 -0.03066 0.17649  0.00013  103 ARG A CZ  
616  N NH1 . ARG A 103 ? 0.54228 0.70248 0.87377 -0.02637 0.15419  -0.00692 103 ARG A NH1 
617  N NH2 . ARG A 103 ? 0.57679 0.71050 0.94199 -0.03714 0.20700  0.00393  103 ARG A NH2 
618  N N   . ASP A 104 ? 0.71109 0.70730 0.83169 0.00695  0.20911  0.04546  104 ASP A N   
619  C CA  . ASP A 104 ? 0.72086 0.68370 0.84423 0.00003  0.22584  0.04821  104 ASP A CA  
620  C C   . ASP A 104 ? 0.76074 0.70670 0.84991 0.01285  0.21681  0.05309  104 ASP A C   
621  O O   . ASP A 104 ? 0.82834 0.75590 0.92484 0.00399  0.21615  0.04692  104 ASP A O   
622  C CB  . ASP A 104 ? 0.76395 0.69585 0.87431 0.00308  0.26140  0.06193  104 ASP A CB  
623  C CG  . ASP A 104 ? 0.76074 0.70885 0.90358 -0.00594 0.27604  0.05901  104 ASP A CG  
624  O OD1 . ASP A 104 ? 0.74373 0.72693 0.93221 -0.01829 0.25843  0.04490  104 ASP A OD1 
625  O OD2 . ASP A 104 ? 0.76825 0.69158 0.88754 0.00140  0.30561  0.07153  104 ASP A OD2 
626  N N   . ASP A 105 ? 0.75247 0.70370 0.80569 0.03381  0.20948  0.06367  105 ASP A N   
627  C CA  . ASP A 105 ? 0.79900 0.73977 0.82865 0.04864  0.20195  0.06960  105 ASP A CA  
628  C C   . ASP A 105 ? 0.84388 0.79991 0.89116 0.04022  0.18252  0.05515  105 ASP A C   
629  O O   . ASP A 105 ? 0.91223 0.84607 0.95093 0.04318  0.18590  0.05520  105 ASP A O   
630  C CB  . ASP A 105 ? 0.82954 0.78298 0.82896 0.07092  0.19130  0.08157  105 ASP A CB  
631  C CG  . ASP A 105 ? 0.90269 0.83283 0.87081 0.08098  0.20867  0.09595  105 ASP A CG  
632  O OD1 . ASP A 105 ? 0.95420 0.85590 0.92537 0.07160  0.23453  0.09840  105 ASP A OD1 
633  O OD2 . ASP A 105 ? 0.95083 0.88814 0.88964 0.09767  0.19668  0.10454  105 ASP A OD2 
634  N N   . VAL A 106 ? 0.83026 0.81853 0.89709 0.03090  0.16394  0.04316  106 VAL A N   
635  C CA  . VAL A 106 ? 0.78977 0.78550 0.86520 0.02302  0.14630  0.02968  106 VAL A CA  
636  C C   . VAL A 106 ? 0.82552 0.79307 0.91222 0.00606  0.15096  0.01979  106 VAL A C   
637  O O   . VAL A 106 ? 0.85955 0.80787 0.93329 0.00475  0.14622  0.01354  106 VAL A O   
638  C CB  . VAL A 106 ? 0.72312 0.75330 0.81429 0.01664  0.12660  0.01977  106 VAL A CB  
639  C CG1 . VAL A 106 ? 0.75275 0.78283 0.84324 0.00998  0.10941  0.00708  106 VAL A CG1 
640  C CG2 . VAL A 106 ? 0.75094 0.80430 0.82819 0.03132  0.12144  0.02812  106 VAL A CG2 
641  N N   . ALA A 107 ? 0.86582 0.82768 0.97657 -0.00772 0.16155  0.01785  107 ALA A N   
642  C CA  . ALA A 107 ? 0.82717 0.76349 0.95463 -0.02710 0.16311  0.00690  107 ALA A CA  
643  C C   . ALA A 107 ? 0.91233 0.80392 1.01137 -0.02162 0.18082  0.01319  107 ALA A C   
644  O O   . ALA A 107 ? 0.93212 0.79664 1.02299 -0.03137 0.17481  0.00240  107 ALA A O   
645  C CB  . ALA A 107 ? 0.75248 0.69596 0.92161 -0.04299 0.17438  0.00492  107 ALA A CB  
646  N N   . GLN A 108 ? 0.93206 0.81051 1.01101 -0.00496 0.20240  0.03070  108 GLN A N   
647  C CA  . GLN A 108 ? 0.98014 0.81473 1.03050 0.00452  0.22018  0.03888  108 GLN A CA  
648  C C   . GLN A 108 ? 0.99132 0.82345 1.01913 0.01790  0.20922  0.03714  108 GLN A C   
649  O O   . GLN A 108 ? 1.02741 0.82079 1.03802 0.01682  0.21744  0.03361  108 GLN A O   
650  C CB  . GLN A 108 ? 1.02801 0.84879 1.05698 0.02361  0.24221  0.05990  108 GLN A CB  
651  C CG  . GLN A 108 ? 1.05788 0.89027 1.10162 0.01743  0.25351  0.06478  108 GLN A CG  
652  C CD  . GLN A 108 ? 1.12965 0.94469 1.20684 -0.00890 0.26853  0.05551  108 GLN A CD  
653  O OE1 . GLN A 108 ? 1.17842 0.96017 1.25724 -0.02059 0.27520  0.04917  108 GLN A OE1 
654  N NE2 . GLN A 108 ? 1.07713 0.91393 1.18362 -0.01879 0.27480  0.05422  108 GLN A NE2 
655  N N   . TRP A 109 ? 0.87098 0.74145 0.89891 0.03008  0.19314  0.03926  109 TRP A N   
656  C CA  . TRP A 109 ? 0.87885 0.75040 0.89271 0.04186  0.18611  0.03762  109 TRP A CA  
657  C C   . TRP A 109 ? 0.89222 0.74453 0.90194 0.02443  0.17646  0.01906  109 TRP A C   
658  O O   . TRP A 109 ? 0.90542 0.72596 0.89281 0.02984  0.18423  0.01678  109 TRP A O   
659  C CB  . TRP A 109 ? 0.82763 0.74591 0.84914 0.05360  0.17026  0.04167  109 TRP A CB  
660  C CG  . TRP A 109 ? 0.78141 0.70797 0.79896 0.05951  0.16233  0.03631  109 TRP A CG  
661  C CD1 . TRP A 109 ? 0.74314 0.65727 0.75184 0.07702  0.17349  0.04389  109 TRP A CD1 
662  C CD2 . TRP A 109 ? 0.76396 0.71046 0.78689 0.04897  0.14490  0.02322  109 TRP A CD2 
663  N NE1 . TRP A 109 ? 0.75172 0.67667 0.76141 0.07668  0.16694  0.03598  109 TRP A NE1 
664  C CE2 . TRP A 109 ? 0.76204 0.70434 0.77646 0.05950  0.14906  0.02342  109 TRP A CE2 
665  C CE3 . TRP A 109 ? 0.73707 0.70250 0.77162 0.03291  0.12779  0.01211  109 TRP A CE3 
666  C CZ2 . TRP A 109 ? 0.72613 0.67799 0.73758 0.05334  0.13829  0.01305  109 TRP A CZ2 
667  C CZ3 . TRP A 109 ? 0.70989 0.68543 0.74061 0.02834  0.11380  0.00214  109 TRP A CZ3 
668  C CH2 . TRP A 109 ? 0.70487 0.67147 0.72133 0.03792  0.11981  0.00271  109 TRP A CH2 
669  N N   . LEU A 110 ? 0.86053 0.72800 0.88926 0.00444  0.15951  0.00577  110 LEU A N   
670  C CA  . LEU A 110 ? 0.88043 0.72473 0.90041 -0.01263 0.14517  -0.01231 110 LEU A CA  
671  C C   . LEU A 110 ? 0.92654 0.71871 0.93343 -0.02364 0.15797  -0.01743 110 LEU A C   
672  O O   . LEU A 110 ? 0.96340 0.71564 0.93853 -0.02599 0.15747  -0.02645 110 LEU A O   
673  C CB  . LEU A 110 ? 0.82984 0.70371 0.87936 -0.02988 0.12180  -0.02386 110 LEU A CB  
674  C CG  . LEU A 110 ? 0.78329 0.70190 0.84156 -0.02164 0.10745  -0.02192 110 LEU A CG  
675  C CD1 . LEU A 110 ? 0.80537 0.75201 0.89898 -0.03620 0.08942  -0.03053 110 LEU A CD1 
676  C CD2 . LEU A 110 ? 0.81196 0.72062 0.83968 -0.01549 0.09815  -0.02754 110 LEU A CD2 
677  N N   . LYS A 111 ? 0.90805 0.69482 0.93570 -0.03098 0.17183  -0.01202 111 LYS A N   
678  C CA  . LYS A 111 ? 0.93465 0.66954 0.95238 -0.04388 0.18557  -0.01724 111 LYS A CA  
679  C C   . LYS A 111 ? 1.00866 0.70247 0.98693 -0.02407 0.20901  -0.00662 111 LYS A C   
680  O O   . LYS A 111 ? 1.08950 0.73133 1.04128 -0.03157 0.21548  -0.01555 111 LYS A O   
681  C CB  . LYS A 111 ? 0.92710 0.66568 0.97947 -0.05628 0.19986  -0.01238 111 LYS A CB  
682  N N   . TRP A 112 ? 0.95966 0.67449 0.93337 0.00196  0.22067  0.01204  112 TRP A N   
683  C CA  . TRP A 112 ? 1.01929 0.69984 0.96369 0.02424  0.24252  0.02410  112 TRP A CA  
684  C C   . TRP A 112 ? 1.07233 0.73748 0.99246 0.03048  0.23844  0.01550  112 TRP A C   
685  O O   . TRP A 112 ? 1.13408 0.74528 1.02441 0.03189  0.25415  0.01172  112 TRP A O   
686  C CB  . TRP A 112 ? 0.99645 0.70708 0.94623 0.05120  0.25003  0.04612  112 TRP A CB  
687  C CG  . TRP A 112 ? 1.03241 0.72223 0.96226 0.07863  0.26606  0.05905  112 TRP A CG  
688  C CD1 . TRP A 112 ? 1.13368 0.77472 1.04289 0.09063  0.29093  0.06972  112 TRP A CD1 
689  C CD2 . TRP A 112 ? 0.98488 0.70208 0.91862 0.09806  0.26009  0.06305  112 TRP A CD2 
690  N NE1 . TRP A 112 ? 1.14922 0.78784 1.05121 0.11833  0.29977  0.08063  112 TRP A NE1 
691  C CE2 . TRP A 112 ? 1.05730 0.74421 0.97749 0.12253  0.28159  0.07652  112 TRP A CE2 
692  C CE3 . TRP A 112 ? 0.96694 0.73033 0.91701 0.09702  0.24039  0.05682  112 TRP A CE3 
693  C CZ2 . TRP A 112 ? 1.04294 0.74938 0.97296 0.14570  0.28392  0.08377  112 TRP A CZ2 
694  C CZ3 . TRP A 112 ? 0.96574 0.74558 0.92240 0.11793  0.24379  0.06357  112 TRP A CZ3 
695  C CH2 . TRP A 112 ? 0.99031 0.74424 0.94059 0.14190  0.26536  0.07683  112 TRP A CH2 
696  N N   . ALA A 113 ? 1.04794 0.75510 0.97733 0.03441  0.22048  0.01244  113 ALA A N   
697  C CA  . ALA A 113 ? 1.02690 0.71654 0.93142 0.03949  0.22026  0.00444  113 ALA A CA  
698  C C   . ALA A 113 ? 1.06028 0.69694 0.93331 0.01757  0.21419  -0.01572 113 ALA A C   
699  O O   . ALA A 113 ? 1.12211 0.71411 0.95748 0.02291  0.22581  -0.02129 113 ALA A O   
700  C CB  . ALA A 113 ? 0.90938 0.65024 0.82989 0.04234  0.20149  0.00291  113 ALA A CB  
701  N N   . GLU A 114 ? 1.04906 0.68828 0.93717 -0.00693 0.19601  -0.02707 114 GLU A N   
702  C CA  . GLU A 114 ? 1.09819 0.68621 0.95915 -0.02977 0.18479  -0.04713 114 GLU A CA  
703  C C   . GLU A 114 ? 1.15008 0.67144 0.97782 -0.02757 0.21104  -0.04674 114 GLU A C   
704  O O   . GLU A 114 ? 1.23002 0.69523 1.00964 -0.03024 0.21413  -0.05850 114 GLU A O   
705  C CB  . GLU A 114 ? 1.04921 0.66036 0.94881 -0.05547 0.16159  -0.05707 114 GLU A CB  
706  C CG  . GLU A 114 ? 1.10707 0.66779 0.98912 -0.08183 0.14662  -0.07773 114 GLU A CG  
707  C CD  . GLU A 114 ? 1.11858 0.71161 1.05471 -0.10641 0.12419  -0.08630 114 GLU A CD  
708  O OE1 . GLU A 114 ? 1.09346 0.74680 1.07057 -0.10262 0.11415  -0.07987 114 GLU A OE1 
709  O OE2 . GLU A 114 ? 1.18115 0.73896 1.12185 -0.12964 0.11797  -0.09953 114 GLU A OE2 
710  N N   . ASN A 115 ? 1.17147 0.69202 1.01835 -0.02156 0.23210  -0.03286 115 ASN A N   
711  C CA  . ASN A 115 ? 1.27260 0.72751 1.08725 -0.01646 0.26033  -0.03015 115 ASN A CA  
712  C C   . ASN A 115 ? 1.29528 0.73678 1.08497 0.01574  0.28459  -0.01657 115 ASN A C   
713  O O   . ASN A 115 ? 1.37623 0.75406 1.12677 0.02161  0.30674  -0.01882 115 ASN A O   
714  C CB  . ASN A 115 ? 1.22637 0.67952 1.06630 -0.01938 0.27718  -0.01823 115 ASN A CB  
715  N N   . GLU A 116 ? 1.20113 0.70108 1.01563 0.03647  0.28122  -0.00298 116 GLU A N   
716  C CA  . GLU A 116 ? 1.21175 0.70877 1.01738 0.06745  0.30323  0.01081  116 GLU A CA  
717  C C   . GLU A 116 ? 1.25510 0.71825 1.02378 0.06744  0.30698  -0.00245 116 GLU A C   
718  O O   . GLU A 116 ? 1.27879 0.70027 1.02265 0.08596  0.33488  0.00227  116 GLU A O   
719  C CB  . GLU A 116 ? 1.13153 0.70261 0.97896 0.08652  0.29459  0.02748  116 GLU A CB  
720  C CG  . GLU A 116 ? 1.13049 0.71089 0.98473 0.11865  0.31361  0.04254  116 GLU A CG  
721  C CD  . GLU A 116 ? 1.21831 0.77045 1.06980 0.14132  0.33830  0.06042  116 GLU A CD  
722  O OE1 . GLU A 116 ? 1.24134 0.77058 1.08536 0.13216  0.34097  0.06295  116 GLU A OE1 
723  O OE2 . GLU A 116 ? 1.24666 0.79925 1.10593 0.16911  0.35619  0.07269  116 GLU A OE2 
724  N N   . PHE A 117 ? 1.26124 0.73735 1.02283 0.04833  0.28108  -0.01843 117 PHE A N   
725  C CA  . PHE A 117 ? 1.26548 0.70628 0.98419 0.04841  0.28397  -0.03053 117 PHE A CA  
726  C C   . PHE A 117 ? 1.34106 0.71874 1.00936 0.02149  0.26827  -0.05394 117 PHE A C   
727  O O   . PHE A 117 ? 1.36607 0.70667 0.98731 0.01874  0.26589  -0.06607 117 PHE A O   
728  C CB  . PHE A 117 ? 1.15324 0.65287 0.89500 0.05189  0.26722  -0.02900 117 PHE A CB  
729  C CG  . PHE A 117 ? 1.08726 0.64784 0.87797 0.07666  0.27852  -0.00825 117 PHE A CG  
730  C CD1 . PHE A 117 ? 1.05898 0.61219 0.84945 0.10080  0.30689  0.00142  117 PHE A CD1 
731  C CD2 . PHE A 117 ? 1.05527 0.67865 0.89288 0.07599  0.26070  0.00134  117 PHE A CD2 
732  C CE1 . PHE A 117 ? 1.01762 0.63025 0.85966 0.12278  0.31220  0.01976  117 PHE A CE1 
733  C CE2 . PHE A 117 ? 1.00058 0.67633 0.87839 0.09799  0.26596  0.01919  117 PHE A CE2 
734  C CZ  . PHE A 117 ? 0.98367 0.65659 0.86668 0.12092  0.28923  0.02820  117 PHE A CZ  
735  N N   . SER A 118 ? 1.56449 0.92604 1.24012 0.00135  0.25757  -0.06069 118 SER A N   
736  C CA  . SER A 118 ? 1.61146 0.91412 1.24573 -0.02662 0.23798  -0.08406 118 SER A CA  
737  C C   . SER A 118 ? 1.60918 0.92769 1.23110 -0.04052 0.20167  -0.09873 118 SER A C   
738  O O   . SER A 118 ? 1.65633 0.91629 1.21547 -0.04660 0.19467  -0.11410 118 SER A O   
739  C CB  . SER A 118 ? 1.67283 0.88346 1.23873 -0.02147 0.26509  -0.09137 118 SER A CB  
740  O OG  . SER A 118 ? 1.68460 0.87673 1.21235 -0.00147 0.28251  -0.08921 118 SER A OG  
741  N N   . LEU A 119 ? 1.32893 0.72288 1.00653 -0.04412 0.17917  -0.09336 119 LEU A N   
742  C CA  . LEU A 119 ? 1.29151 0.70827 0.96486 -0.05365 0.14516  -0.10391 119 LEU A CA  
743  C C   . LEU A 119 ? 1.28669 0.70203 0.97613 -0.08319 0.10721  -0.12106 119 LEU A C   
744  O O   . LEU A 119 ? 1.25125 0.65278 0.96139 -0.09793 0.10934  -0.12453 119 LEU A O   
745  C CB  . LEU A 119 ? 1.17005 0.66717 0.89374 -0.03944 0.14312  -0.08875 119 LEU A CB  
746  C CG  . LEU A 119 ? 1.15541 0.66880 0.88254 -0.01126 0.17662  -0.07068 119 LEU A CG  
747  C CD1 . LEU A 119 ? 1.04316 0.63693 0.82559 -0.00215 0.16920  -0.05742 119 LEU A CD1 
748  C CD2 . LEU A 119 ? 1.23934 0.70678 0.90894 -0.00221 0.18848  -0.07637 119 LEU A CD2 
749  N N   . ARG A 120 ? 1.31558 0.74459 0.99773 -0.09166 0.07224  -0.13164 120 ARG A N   
750  C CA  . ARG A 120 ? 1.26297 0.70659 0.97658 -0.11712 0.03165  -0.14616 120 ARG A CA  
751  C C   . ARG A 120 ? 1.23625 0.75517 1.03738 -0.12013 0.03372  -0.13451 120 ARG A C   
752  O O   . ARG A 120 ? 1.20336 0.77143 1.03251 -0.10155 0.05295  -0.11700 120 ARG A O   
753  C CB  . ARG A 120 ? 1.35534 0.80157 1.04408 -0.12012 -0.00615 -0.15666 120 ARG A CB  
754  N N   . PRO A 121 ? 1.20114 0.72797 1.04620 -0.14389 0.01481  -0.14430 121 PRO A N   
755  C CA  . PRO A 121 ? 1.13927 0.72713 1.06361 -0.14704 0.02555  -0.13269 121 PRO A CA  
756  C C   . PRO A 121 ? 1.07884 0.73773 1.04671 -0.13817 0.01157  -0.12496 121 PRO A C   
757  O O   . PRO A 121 ? 1.05193 0.73304 1.04484 -0.15020 -0.02413 -0.13602 121 PRO A O   
758  C CB  . PRO A 121 ? 1.19003 0.76426 1.15073 -0.17781 0.00507  -0.14881 121 PRO A CB  
759  C CG  . PRO A 121 ? 1.28145 0.77532 1.17098 -0.18853 -0.00736 -0.16665 121 PRO A CG  
760  C CD  . PRO A 121 ? 1.28667 0.76238 1.11011 -0.16973 -0.01536 -0.16684 121 PRO A CD  
761  N N   . ILE A 122 ? 1.04269 0.73582 1.01968 -0.11658 0.03838  -0.10605 122 ILE A N   
762  C CA  . ILE A 122 ? 1.02218 0.77717 1.03365 -0.10695 0.02918  -0.09825 122 ILE A CA  
763  C C   . ILE A 122 ? 0.99148 0.79082 1.07493 -0.11873 0.02850  -0.09568 122 ILE A C   
764  O O   . ILE A 122 ? 0.95458 0.75329 1.05935 -0.11947 0.05601  -0.08621 122 ILE A O   
765  C CB  . ILE A 122 ? 1.00079 0.77356 0.99548 -0.08131 0.05575  -0.08037 122 ILE A CB  
766  C CG1 . ILE A 122 ? 1.03796 0.76954 0.96978 -0.06979 0.05996  -0.08295 122 ILE A CG1 
767  C CG2 . ILE A 122 ? 0.95758 0.79061 0.98698 -0.07337 0.04734  -0.07311 122 ILE A CG2 
768  N N   . ASP A 123 ? 0.98686 0.82164 1.10711 -0.12687 -0.00089 -0.10345 123 ASP A N   
769  C CA  . ASP A 123 ? 0.93058 0.81248 1.12452 -0.13526 0.00181  -0.10004 123 ASP A CA  
770  C C   . ASP A 123 ? 0.92492 0.84469 1.12915 -0.11570 0.02779  -0.08170 123 ASP A C   
771  O O   . ASP A 123 ? 0.89207 0.82051 1.06265 -0.09814 0.02718  -0.07557 123 ASP A O   
772  C CB  . ASP A 123 ? 0.88146 0.79173 1.11437 -0.14613 -0.03780 -0.11284 123 ASP A CB  
773  C CG  . ASP A 123 ? 0.88039 0.84023 1.19797 -0.15467 -0.03213 -0.10979 123 ASP A CG  
774  O OD1 . ASP A 123 ? 0.93182 0.89352 1.27516 -0.15785 0.00180  -0.10063 123 ASP A OD1 
775  O OD2 . ASP A 123 ? 0.85844 0.85265 1.21588 -0.15703 -0.05980 -0.11592 123 ASP A OD2 
776  N N   . SER A 124 ? 0.98426 0.92304 1.23374 -0.11974 0.05148  -0.07330 124 SER A N   
777  C CA  . SER A 124 ? 0.90858 0.87740 1.16278 -0.10218 0.07450  -0.05683 124 SER A CA  
778  C C   . SER A 124 ? 0.86703 0.87799 1.13916 -0.09548 0.05469  -0.05866 124 SER A C   
779  O O   . SER A 124 ? 0.83442 0.86208 1.08601 -0.07811 0.06367  -0.04828 124 SER A O   
780  C CB  . SER A 124 ? 0.86171 0.83496 1.15653 -0.10901 0.10488  -0.04843 124 SER A CB  
781  N N   . ASN A 125 ? 0.79427 0.82077 1.10366 -0.10869 0.02581  -0.07204 125 ASN A N   
782  C CA  . ASN A 125 ? 0.77205 0.83424 1.09823 -0.10141 0.00574  -0.07401 125 ASN A CA  
783  C C   . ASN A 125 ? 0.77307 0.82317 1.03970 -0.08804 -0.01030 -0.07494 125 ASN A C   
784  O O   . ASN A 125 ? 0.73370 0.80826 1.00435 -0.07959 -0.02297 -0.07470 125 ASN A O   
785  C CB  . ASN A 125 ? 0.74578 0.82554 1.12881 -0.11747 -0.02469 -0.08776 125 ASN A CB  
786  N N   . THR A 126 ? 0.80246 0.81325 1.01518 -0.08567 -0.00683 -0.07567 126 THR A N   
787  C CA  . THR A 126 ? 0.80453 0.80021 0.96323 -0.07419 -0.01746 -0.07671 126 THR A CA  
788  C C   . THR A 126 ? 0.74645 0.76925 0.89720 -0.05710 -0.00183 -0.06430 126 THR A C   
789  O O   . THR A 126 ? 0.73500 0.76572 0.86804 -0.05003 -0.01477 -0.06584 126 THR A O   
790  C CB  . THR A 126 ? 0.84205 0.78843 0.94925 -0.07411 -0.00903 -0.07882 126 THR A CB  
791  O OG1 . THR A 126 ? 0.85567 0.77232 0.96732 -0.09217 -0.02510 -0.09201 126 THR A OG1 
792  C CG2 . THR A 126 ? 0.84840 0.77464 0.90170 -0.06366 -0.01654 -0.08066 126 THR A CG2 
793  N N   . PHE A 127 ? 0.72256 0.75618 0.88316 -0.05061 0.02496  -0.05214 127 PHE A N   
794  C CA  . PHE A 127 ? 0.69383 0.75075 0.84537 -0.03543 0.03711  -0.04096 127 PHE A CA  
795  C C   . PHE A 127 ? 0.69650 0.77661 0.88322 -0.03538 0.05286  -0.03365 127 PHE A C   
796  O O   . PHE A 127 ? 0.68890 0.76068 0.87100 -0.03084 0.07545  -0.02343 127 PHE A O   
797  C CB  . PHE A 127 ? 0.69858 0.73811 0.81435 -0.02357 0.05309  -0.03207 127 PHE A CB  
798  C CG  . PHE A 127 ? 0.72375 0.74091 0.80420 -0.02117 0.04410  -0.03796 127 PHE A CG  
799  C CD1 . PHE A 127 ? 0.72167 0.75282 0.78814 -0.01360 0.03727  -0.03764 127 PHE A CD1 
800  C CD2 . PHE A 127 ? 0.75164 0.72876 0.80993 -0.02708 0.04504  -0.04415 127 PHE A CD2 
801  C CE1 . PHE A 127 ? 0.79183 0.79798 0.82440 -0.01137 0.03453  -0.04223 127 PHE A CE1 
802  C CE2 . PHE A 127 ? 0.77762 0.72688 0.79671 -0.02388 0.04143  -0.04928 127 PHE A CE2 
803  C CZ  . PHE A 127 ? 0.84306 0.80709 0.85004 -0.01576 0.03756  -0.04780 127 PHE A CZ  
804  N N   . GLU A 128 ? 0.65180 0.75722 0.87113 -0.03902 0.04250  -0.03831 128 GLU A N   
805  C CA  . GLU A 128 ? 0.59602 0.72106 0.84895 -0.03839 0.06086  -0.03209 128 GLU A CA  
806  C C   . GLU A 128 ? 0.57630 0.71531 0.80536 -0.02388 0.06742  -0.02445 128 GLU A C   
807  O O   . GLU A 128 ? 0.55735 0.71591 0.79964 -0.02131 0.05976  -0.02757 128 GLU A O   
808  C CB  . GLU A 128 ? 0.56022 0.70546 0.86816 -0.04912 0.04825  -0.04116 128 GLU A CB  
809  C CG  . GLU A 128 ? 0.62275 0.75629 0.96285 -0.06625 0.04134  -0.04932 128 GLU A CG  
810  C CD  . GLU A 128 ? 0.64082 0.79578 1.03153 -0.07566 0.01403  -0.06101 128 GLU A CD  
811  O OE1 . GLU A 128 ? 0.63363 0.80296 1.01742 -0.06721 -0.00504 -0.06372 128 GLU A OE1 
812  O OE2 . GLU A 128 ? 0.64293 0.79989 1.08217 -0.09145 0.01063  -0.06742 128 GLU A OE2 
813  N N   . MET A 129 ? 0.57226 0.69923 0.76557 -0.01393 0.08073  -0.01443 129 MET A N   
814  C CA  . MET A 129 ? 0.56812 0.70525 0.73410 -0.00136 0.08169  -0.00842 129 MET A CA  
815  C C   . MET A 129 ? 0.58348 0.70567 0.71986 0.00905  0.09760  0.00430  129 MET A C   
816  O O   . MET A 129 ? 0.64870 0.75132 0.78184 0.00797  0.10707  0.00837  129 MET A O   
817  C CB  . MET A 129 ? 0.60995 0.75355 0.75815 0.00095  0.06068  -0.01462 129 MET A CB  
818  C CG  . MET A 129 ? 0.60346 0.73062 0.72965 0.00315  0.05824  -0.01345 129 MET A CG  
819  S SD  . MET A 129 ? 0.56090 0.68611 0.67164 0.00131  0.03839  -0.02311 129 MET A SD  
820  C CE  . MET A 129 ? 0.59943 0.71758 0.73220 -0.01169 0.02266  -0.03519 129 MET A CE  
821  N N   . ASN A 130 ? 0.56532 0.69387 0.67746 0.01972  0.09871  0.01041  130 ASN A N   
822  C CA  . ASN A 130 ? 0.60120 0.71654 0.68138 0.03229  0.10649  0.02279  130 ASN A CA  
823  C C   . ASN A 130 ? 0.61391 0.73322 0.68393 0.03794  0.09268  0.02329  130 ASN A C   
824  O O   . ASN A 130 ? 0.65723 0.78378 0.73906 0.03141  0.08102  0.01416  130 ASN A O   
825  C CB  . ASN A 130 ? 0.63780 0.75487 0.69155 0.04115  0.10833  0.02785  130 ASN A CB  
826  C CG  . ASN A 130 ? 0.69094 0.82834 0.73665 0.04279  0.08681  0.02151  130 ASN A CG  
827  O OD1 . ASN A 130 ? 0.71195 0.86329 0.77697 0.03535  0.07442  0.01191  130 ASN A OD1 
828  N ND2 . ASN A 130 ? 0.72175 0.85698 0.73564 0.05210  0.08170  0.02665  130 ASN A ND2 
829  N N   . GLY A 131 ? 0.65479 0.76742 0.70201 0.05149  0.09468  0.03470  131 GLY A N   
830  C CA  . GLY A 131 ? 0.67170 0.79168 0.71789 0.05888  0.08456  0.03662  131 GLY A CA  
831  C C   . GLY A 131 ? 0.64833 0.79431 0.69881 0.05784  0.06630  0.02994  131 GLY A C   
832  O O   . GLY A 131 ? 0.64053 0.79378 0.70188 0.05707  0.06110  0.02615  131 GLY A O   
833  N N   . LYS A 132 ? 0.72581 0.88179 0.76585 0.05735  0.05904  0.02816  132 LYS A N   
834  C CA  . LYS A 132 ? 0.71256 0.88992 0.75635 0.05424  0.04253  0.02090  132 LYS A CA  
835  C C   . LYS A 132 ? 0.71419 0.89503 0.77444 0.04218  0.04037  0.00902  132 LYS A C   
836  O O   . LYS A 132 ? 0.71901 0.90909 0.78684 0.03992  0.03333  0.00464  132 LYS A O   
837  C CB  . LYS A 132 ? 0.72456 0.90358 0.74696 0.05548  0.03646  0.02029  132 LYS A CB  
838  N N   . ALA A 133 ? 0.61400 0.78604 0.68070 0.03484  0.04655  0.00411  133 ALA A N   
839  C CA  . ALA A 133 ? 0.56366 0.73576 0.64230 0.02526  0.04003  -0.00660 133 ALA A CA  
840  C C   . ALA A 133 ? 0.57752 0.73785 0.65750 0.02355  0.04045  -0.00831 133 ALA A C   
841  O O   . ALA A 133 ? 0.63175 0.78929 0.70845 0.01930  0.03332  -0.01530 133 ALA A O   
842  C CB  . ALA A 133 ? 0.53692 0.70496 0.63107 0.01902  0.04437  -0.01061 133 ALA A CB  
843  N N   . LEU A 134 ? 0.55314 0.70038 0.63263 0.02743  0.05103  -0.00177 134 LEU A N   
844  C CA  . LEU A 134 ? 0.53840 0.66819 0.61339 0.02742  0.05488  -0.00314 134 LEU A CA  
845  C C   . LEU A 134 ? 0.56235 0.70217 0.63466 0.03319  0.05306  -0.00190 134 LEU A C   
846  O O   . LEU A 134 ? 0.65964 0.78506 0.72485 0.03041  0.05502  -0.00720 134 LEU A O   
847  C CB  . LEU A 134 ? 0.53504 0.64747 0.60806 0.03300  0.06892  0.00532  134 LEU A CB  
848  C CG  . LEU A 134 ? 0.55819 0.64461 0.62242 0.03403  0.07708  0.00411  134 LEU A CG  
849  C CD1 . LEU A 134 ? 0.67056 0.73373 0.73071 0.01991  0.07198  -0.00791 134 LEU A CD1 
850  C CD2 . LEU A 134 ? 0.58881 0.66108 0.64977 0.04462  0.09222  0.01576  134 LEU A CD2 
851  N N   . LEU A 135 ? 0.49325 0.65565 0.57082 0.04074  0.04948  0.00471  135 LEU A N   
852  C CA  . LEU A 135 ? 0.48615 0.66400 0.57293 0.04444  0.04716  0.00549  135 LEU A CA  
853  C C   . LEU A 135 ? 0.57264 0.75518 0.65752 0.03448  0.03977  -0.00454 135 LEU A C   
854  O O   . LEU A 135 ? 0.63000 0.81359 0.72065 0.03349  0.04399  -0.00660 135 LEU A O   
855  C CB  . LEU A 135 ? 0.48159 0.68285 0.57685 0.05439  0.03979  0.01447  135 LEU A CB  
856  C CG  . LEU A 135 ? 0.51238 0.70499 0.60269 0.06703  0.04586  0.02652  135 LEU A CG  
857  C CD1 . LEU A 135 ? 0.59624 0.80842 0.68693 0.07760  0.03234  0.03491  135 LEU A CD1 
858  C CD2 . LEU A 135 ? 0.52514 0.70444 0.62415 0.07426  0.06002  0.03096  135 LEU A CD2 
859  N N   . LEU A 136 ? 0.49668 0.67954 0.57405 0.02784  0.03153  -0.01020 136 LEU A N   
860  C CA  . LEU A 136 ? 0.51975 0.70266 0.59197 0.02005  0.02476  -0.01885 136 LEU A CA  
861  C C   . LEU A 136 ? 0.55748 0.71439 0.61682 0.01531  0.02798  -0.02504 136 LEU A C   
862  O O   . LEU A 136 ? 0.57665 0.72685 0.62783 0.01147  0.02822  -0.02956 136 LEU A O   
863  C CB  . LEU A 136 ? 0.50316 0.69003 0.57119 0.01676  0.01695  -0.02267 136 LEU A CB  
864  C CG  . LEU A 136 ? 0.53133 0.73344 0.59815 0.02091  0.01390  -0.01827 136 LEU A CG  
865  C CD1 . LEU A 136 ? 0.51176 0.71097 0.57221 0.01795  0.01143  -0.02330 136 LEU A CD1 
866  C CD2 . LEU A 136 ? 0.53785 0.75614 0.60814 0.02126  0.00719  -0.01762 136 LEU A CD2 
867  N N   . LEU A 137 ? 0.54096 0.67848 0.59435 0.01492  0.03034  -0.02568 137 LEU A N   
868  C CA  . LEU A 137 ? 0.61704 0.72302 0.64913 0.01021  0.02877  -0.03279 137 LEU A CA  
869  C C   . LEU A 137 ? 0.66325 0.75265 0.68224 0.01292  0.04258  -0.03176 137 LEU A C   
870  O O   . LEU A 137 ? 0.67045 0.76879 0.70291 0.01965  0.05531  -0.02471 137 LEU A O   
871  C CB  . LEU A 137 ? 0.62908 0.71661 0.65916 0.00763  0.02702  -0.03459 137 LEU A CB  
872  C CG  . LEU A 137 ? 0.63242 0.73369 0.68214 0.00352  0.01691  -0.03634 137 LEU A CG  
873  C CD1 . LEU A 137 ? 0.63725 0.71754 0.68874 -0.00254 0.01398  -0.04034 137 LEU A CD1 
874  C CD2 . LEU A 137 ? 0.65112 0.75773 0.69950 0.00065  0.00257  -0.04253 137 LEU A CD2 
875  N N   . THR A 138 ? 0.69867 0.76162 0.69104 0.00895  0.04143  -0.03811 138 THR A N   
876  C CA  . THR A 138 ? 0.68170 0.71852 0.65507 0.01106  0.05960  -0.03778 138 THR A CA  
877  C C   . THR A 138 ? 0.75746 0.75269 0.70156 0.01207  0.06524  -0.04046 138 THR A C   
878  O O   . THR A 138 ? 0.77998 0.76596 0.71853 0.00852  0.05100  -0.04431 138 THR A O   
879  C CB  . THR A 138 ? 0.70968 0.72608 0.65732 0.00673  0.05938  -0.04278 138 THR A CB  
880  O OG1 . THR A 138 ? 0.75695 0.74165 0.67016 0.00339  0.04157  -0.04996 138 THR A OG1 
881  C CG2 . THR A 138 ? 0.71139 0.76406 0.68536 0.00396  0.05343  -0.04167 138 THR A CG2 
882  N N   . LYS A 139 ? 0.76820 0.73614 0.69451 0.01629  0.08775  -0.03895 139 LYS A N   
883  C CA  . LYS A 139 ? 0.78873 0.70859 0.67912 0.01772  0.09647  -0.04222 139 LYS A CA  
884  C C   . LYS A 139 ? 0.87057 0.74911 0.71492 0.00994  0.07489  -0.05283 139 LYS A C   
885  O O   . LYS A 139 ? 0.92085 0.77371 0.74818 0.00676  0.06646  -0.05769 139 LYS A O   
886  C CB  . LYS A 139 ? 0.77650 0.66749 0.64987 0.02432  0.12825  -0.03937 139 LYS A CB  
887  N N   . GLU A 140 ? 0.84931 0.72017 0.67411 0.00674  0.06378  -0.05662 140 GLU A N   
888  C CA  . GLU A 140 ? 0.90865 0.74246 0.69177 0.00153  0.03777  -0.06589 140 GLU A CA  
889  C C   . GLU A 140 ? 0.94226 0.80600 0.75983 -0.00372 0.01089  -0.06881 140 GLU A C   
890  O O   . GLU A 140 ? 1.01910 0.85387 0.81582 -0.00888 -0.00729 -0.07645 140 GLU A O   
891  C CB  . GLU A 140 ? 0.89673 0.72015 0.65677 0.00159  0.03119  -0.06718 140 GLU A CB  
892  N N   . ASP A 141 ? 0.82842 0.74784 0.69887 -0.00309 0.00907  -0.06320 141 ASP A N   
893  C CA  . ASP A 141 ? 0.84307 0.79079 0.75011 -0.00761 -0.00959 -0.06483 141 ASP A CA  
894  C C   . ASP A 141 ? 0.90382 0.84013 0.81693 -0.01088 -0.00476 -0.06555 141 ASP A C   
895  O O   . ASP A 141 ? 0.90024 0.83231 0.82362 -0.01842 -0.02318 -0.07175 141 ASP A O   
896  C CB  . ASP A 141 ? 0.80508 0.80540 0.75744 -0.00482 -0.00536 -0.05781 141 ASP A CB  
897  C CG  . ASP A 141 ? 0.81585 0.82445 0.76197 -0.00294 -0.00953 -0.05805 141 ASP A CG  
898  O OD1 . ASP A 141 ? 0.81520 0.81010 0.74750 -0.00438 -0.02863 -0.06366 141 ASP A OD1 
899  O OD2 . ASP A 141 ? 0.81433 0.84150 0.76978 0.00001  0.00521  -0.05277 141 ASP A OD2 
900  N N   . PHE A 142 ? 0.94988 0.88109 0.86044 -0.00532 0.02012  -0.05923 142 PHE A N   
901  C CA  . PHE A 142 ? 0.96229 0.87195 0.86972 -0.00740 0.02783  -0.05988 142 PHE A CA  
902  C C   . PHE A 142 ? 1.01047 0.86289 0.86922 -0.01457 0.01562  -0.07163 142 PHE A C   
903  O O   . PHE A 142 ? 1.06441 0.90285 0.92715 -0.02352 0.00370  -0.07786 142 PHE A O   
904  C CB  . PHE A 142 ? 0.95094 0.86087 0.86099 0.00327  0.05732  -0.05025 142 PHE A CB  
905  C CG  . PHE A 142 ? 0.90101 0.86170 0.85672 0.01011  0.06446  -0.03888 142 PHE A CG  
906  C CD1 . PHE A 142 ? 0.87775 0.87572 0.85310 0.01280  0.06020  -0.03526 142 PHE A CD1 
907  C CD2 . PHE A 142 ? 0.88562 0.85094 0.85874 0.01398  0.07495  -0.03193 142 PHE A CD2 
908  C CE1 . PHE A 142 ? 0.82342 0.86171 0.83205 0.01901  0.06346  -0.02582 142 PHE A CE1 
909  C CE2 . PHE A 142 ? 0.86790 0.87263 0.87296 0.02182  0.07942  -0.02096 142 PHE A CE2 
910  C CZ  . PHE A 142 ? 0.82249 0.86343 0.84384 0.02424  0.07227  -0.01833 142 PHE A CZ  
911  N N   . ARG A 143 ? 0.99190 0.80692 0.80169 -0.01155 0.01819  -0.07522 143 ARG A N   
912  C CA  . ARG A 143 ? 0.98567 0.73559 0.73463 -0.01697 0.00624  -0.08659 143 ARG A CA  
913  C C   . ARG A 143 ? 1.04766 0.79836 0.80077 -0.02715 -0.03416 -0.09646 143 ARG A C   
914  O O   . ARG A 143 ? 1.06905 0.78316 0.79933 -0.03622 -0.05205 -0.10670 143 ARG A O   
915  C CB  . ARG A 143 ? 0.96196 0.66753 0.65236 -0.01018 0.02091  -0.08691 143 ARG A CB  
916  C CG  . ARG A 143 ? 0.95875 0.66169 0.65072 -0.00006 0.06253  -0.07783 143 ARG A CG  
917  C CD  . ARG A 143 ? 0.97510 0.63389 0.61391 0.00552  0.08180  -0.07785 143 ARG A CD  
918  N NE  . ARG A 143 ? 1.00612 0.67262 0.66293 0.01543  0.12313  -0.06839 143 ARG A NE  
919  C CZ  . ARG A 143 ? 1.08081 0.71244 0.70366 0.02108  0.15188  -0.06633 143 ARG A CZ  
920  N NH1 . ARG A 143 ? 1.15194 0.73072 0.70961 0.01850  0.14527  -0.07256 143 ARG A NH1 
921  N NH2 . ARG A 143 ? 1.10445 0.75325 0.76047 0.03028  0.18889  -0.05721 143 ARG A NH2 
922  N N   . TYR A 144 ? 1.18590 0.97745 0.97021 -0.02573 -0.04977 -0.09396 144 TYR A N   
923  C CA  . TYR A 144 ? 1.17098 0.97163 0.97263 -0.03303 -0.08787 -0.10190 144 TYR A CA  
924  C C   . TYR A 144 ? 1.15040 0.98100 1.00869 -0.04294 -0.09448 -0.10386 144 TYR A C   
925  O O   . TYR A 144 ? 1.16095 0.97484 1.02102 -0.05344 -0.12244 -0.11431 144 TYR A O   
926  C CB  . TYR A 144 ? 1.13151 0.97103 0.95954 -0.02708 -0.09715 -0.09725 144 TYR A CB  
927  C CG  . TYR A 144 ? 1.24865 1.06195 1.02755 -0.01836 -0.08529 -0.09389 144 TYR A CG  
928  C CD1 . TYR A 144 ? 1.26945 1.01540 0.97268 -0.01684 -0.08529 -0.09901 144 TYR A CD1 
929  C CD2 . TYR A 144 ? 1.23115 1.08218 1.03624 -0.01244 -0.07217 -0.08596 144 TYR A CD2 
930  C CE1 . TYR A 144 ? 1.34682 1.06497 1.00524 -0.00951 -0.06927 -0.09520 144 TYR A CE1 
931  C CE2 . TYR A 144 ? 1.22604 1.05225 0.99055 -0.00671 -0.05896 -0.08318 144 TYR A CE2 
932  C CZ  . TYR A 144 ? 1.31846 1.07902 1.01159 -0.00519 -0.05593 -0.08725 144 TYR A CZ  
933  O OH  . TYR A 144 ? 1.34956 1.08223 1.00289 -0.00009 -0.03790 -0.08374 144 TYR A OH  
934  N N   . ARG A 145 ? 0.96454 0.83679 0.86854 -0.04019 -0.06932 -0.09396 145 ARG A N   
935  C CA  . ARG A 145 ? 0.90264 0.80015 0.85894 -0.04915 -0.06953 -0.09405 145 ARG A CA  
936  C C   . ARG A 145 ? 0.89064 0.74371 0.82230 -0.05781 -0.06525 -0.10049 145 ARG A C   
937  O O   . ARG A 145 ? 0.89948 0.74845 0.85464 -0.07150 -0.08353 -0.10910 145 ARG A O   
938  C CB  . ARG A 145 ? 0.85573 0.79896 0.85321 -0.04189 -0.04284 -0.08081 145 ARG A CB  
939  C CG  . ARG A 145 ? 0.78724 0.77348 0.81341 -0.03592 -0.04818 -0.07621 145 ARG A CG  
940  C CD  . ARG A 145 ? 0.73387 0.75632 0.78802 -0.02857 -0.02380 -0.06406 145 ARG A CD  
941  N NE  . ARG A 145 ? 0.70116 0.75941 0.78216 -0.02484 -0.02907 -0.06154 145 ARG A NE  
942  C CZ  . ARG A 145 ? 0.66096 0.74562 0.78651 -0.02851 -0.03165 -0.06130 145 ARG A CZ  
943  N NH1 . ARG A 145 ? 0.67393 0.75707 0.82781 -0.03758 -0.02941 -0.06316 145 ARG A NH1 
944  N NH2 . ARG A 145 ? 0.58544 0.69636 0.72850 -0.02326 -0.03380 -0.05926 145 ARG A NH2 
945  N N   . SER A 146 ? 0.88867 0.70713 0.77574 -0.05039 -0.04039 -0.09688 146 SER A N   
946  C CA  . SER A 146 ? 0.91428 0.68278 0.76985 -0.05626 -0.03086 -0.10244 146 SER A CA  
947  C C   . SER A 146 ? 1.07870 0.78391 0.85657 -0.05269 -0.03191 -0.10971 146 SER A C   
948  O O   . SER A 146 ? 1.11198 0.79782 0.85989 -0.04067 -0.00172 -0.10279 146 SER A O   
949  C CB  . SER A 146 ? 0.89705 0.67612 0.76995 -0.04785 0.00528  -0.09006 146 SER A CB  
950  N N   . PRO A 147 ? 1.10176 0.77161 0.84499 -0.06211 -0.06592 -0.12338 147 PRO A N   
951  C CA  . PRO A 147 ? 1.05620 0.65460 0.71213 -0.05811 -0.06639 -0.13046 147 PRO A CA  
952  C C   . PRO A 147 ? 1.17832 0.71455 0.78488 -0.05910 -0.04265 -0.13461 147 PRO A C   
953  O O   . PRO A 147 ? 1.25541 0.73011 0.78742 -0.05206 -0.02885 -0.13739 147 PRO A O   
954  C CB  . PRO A 147 ? 1.09552 0.67316 0.73128 -0.06868 -0.11579 -0.14435 147 PRO A CB  
955  C CG  . PRO A 147 ? 1.06556 0.68869 0.77742 -0.08315 -0.13605 -0.14820 147 PRO A CG  
956  C CD  . PRO A 147 ? 1.04017 0.73040 0.82234 -0.07656 -0.10553 -0.13305 147 PRO A CD  
957  N N   . HIS A 148 ? 1.25598 0.80160 0.89872 -0.06682 -0.03393 -0.13463 148 HIS A N   
958  C CA  . HIS A 148 ? 1.32095 0.80475 0.91785 -0.06722 -0.00973 -0.13845 148 HIS A CA  
959  C C   . HIS A 148 ? 1.27856 0.78439 0.90215 -0.05176 0.03625  -0.12219 148 HIS A C   
960  O O   . HIS A 148 ? 1.31514 0.76795 0.89295 -0.04402 0.06551  -0.12178 148 HIS A O   
961  C CB  . HIS A 148 ? 1.35930 0.82362 0.96905 -0.08780 -0.03174 -0.15134 148 HIS A CB  
962  C CG  . HIS A 148 ? 1.39800 0.85076 0.99780 -0.10400 -0.08344 -0.16749 148 HIS A CG  
963  N ND1 . HIS A 148 ? 1.39908 0.91812 1.07209 -0.11170 -0.11301 -0.16706 148 HIS A ND1 
964  C CD2 . HIS A 148 ? 1.44094 0.82196 0.96546 -0.11263 -0.11223 -0.18437 148 HIS A CD2 
965  C CE1 . HIS A 148 ? 1.43684 0.93095 1.08790 -0.12388 -0.15956 -0.18249 148 HIS A CE1 
966  N NE2 . HIS A 148 ? 1.45441 0.86358 1.01239 -0.12503 -0.16220 -0.19348 148 HIS A NE2 
967  N N   . SER A 149 ? 1.16732 0.74724 0.86177 -0.04582 0.04292  -0.10868 149 SER A N   
968  C CA  . SER A 149 ? 1.12960 0.73192 0.85083 -0.03008 0.08052  -0.09274 149 SER A CA  
969  C C   . SER A 149 ? 1.07501 0.74266 0.83894 -0.01721 0.08702  -0.07906 149 SER A C   
970  O O   . SER A 149 ? 1.05429 0.75486 0.85364 -0.00493 0.10911  -0.06512 149 SER A O   
971  C CB  . SER A 149 ? 1.13511 0.74923 0.89571 -0.03676 0.08587  -0.08949 149 SER A CB  
972  N N   . GLY A 150 ? 1.01677 0.70002 0.77488 -0.01932 0.06719  -0.08287 150 GLY A N   
973  C CA  . GLY A 150 ? 0.99164 0.73557 0.79128 -0.01039 0.07024  -0.07188 150 GLY A CA  
974  C C   . GLY A 150 ? 0.97653 0.72509 0.77520 0.00616  0.10266  -0.06078 150 GLY A C   
975  O O   . GLY A 150 ? 0.99332 0.79075 0.83826 0.01532  0.11342  -0.04854 150 GLY A O   
976  N N   . ASP A 151 ? 0.93822 0.63474 0.68458 0.01046  0.11851  -0.06494 151 ASP A N   
977  C CA  . ASP A 151 ? 0.93705 0.63987 0.69097 0.02589  0.15210  -0.05461 151 ASP A CA  
978  C C   . ASP A 151 ? 0.98818 0.70692 0.77679 0.03773  0.17488  -0.04335 151 ASP A C   
979  O O   . ASP A 151 ? 0.95583 0.72201 0.79114 0.04978  0.18781  -0.03091 151 ASP A O   
980  C CB  . ASP A 151 ? 1.00288 0.63566 0.68873 0.02840  0.17102  -0.06137 151 ASP A CB  
981  C CG  . ASP A 151 ? 1.10639 0.66689 0.73161 0.02098  0.16632  -0.07346 151 ASP A CG  
982  O OD1 . ASP A 151 ? 1.13033 0.69876 0.77471 0.01342  0.15118  -0.07599 151 ASP A OD1 
983  O OD2 . ASP A 151 ? 1.15582 0.64745 0.71104 0.02181  0.17811  -0.08098 151 ASP A OD2 
984  N N   . VAL A 152 ? 1.02631 0.70442 0.79262 0.03455  0.17812  -0.04757 152 VAL A N   
985  C CA  . VAL A 152 ? 0.97440 0.66255 0.77001 0.04683  0.19876  -0.03598 152 VAL A CA  
986  C C   . VAL A 152 ? 0.92817 0.68286 0.78225 0.04767  0.18373  -0.02596 152 VAL A C   
987  O O   . VAL A 152 ? 0.92622 0.71650 0.81793 0.06345  0.19704  -0.01167 152 VAL A O   
988  C CB  . VAL A 152 ? 1.00893 0.63336 0.76405 0.04038  0.20440  -0.04410 152 VAL A CB  
989  N N   . LEU A 153 ? 0.92417 0.69507 0.78608 0.03166  0.15559  -0.03313 153 LEU A N   
990  C CA  . LEU A 153 ? 0.87605 0.70302 0.78568 0.03195  0.14396  -0.02446 153 LEU A CA  
991  C C   . LEU A 153 ? 0.87700 0.75636 0.81548 0.03952  0.13925  -0.01749 153 LEU A C   
992  O O   . LEU A 153 ? 0.84533 0.76785 0.81715 0.04214  0.13135  -0.00964 153 LEU A O   
993  C CB  . LEU A 153 ? 0.82855 0.65843 0.74365 0.01300  0.11885  -0.03449 153 LEU A CB  
994  C CG  . LEU A 153 ? 0.87469 0.66791 0.78184 0.00371  0.12275  -0.03863 153 LEU A CG  
995  C CD1 . LEU A 153 ? 0.93456 0.73241 0.85500 -0.01701 0.09631  -0.05062 153 LEU A CD1 
996  C CD2 . LEU A 153 ? 0.86138 0.66933 0.79334 0.01539  0.14206  -0.02330 153 LEU A CD2 
997  N N   . TYR A 154 ? 0.83807 0.71041 0.76148 0.04227  0.14498  -0.02056 154 TYR A N   
998  C CA  . TYR A 154 ? 0.78643 0.70515 0.73899 0.04766  0.14259  -0.01486 154 TYR A CA  
999  C C   . TYR A 154 ? 0.78874 0.72363 0.76712 0.06511  0.16573  -0.00286 154 TYR A C   
1000 O O   . TYR A 154 ? 0.75384 0.73696 0.77262 0.07272  0.16031  0.00676  154 TYR A O   
1001 C CB  . TYR A 154 ? 0.82747 0.73003 0.75253 0.03919  0.13599  -0.02481 154 TYR A CB  
1002 C CG  . TYR A 154 ? 0.81649 0.76144 0.77023 0.04201  0.13530  -0.02041 154 TYR A CG  
1003 C CD1 . TYR A 154 ? 0.81632 0.80203 0.79326 0.03613  0.11338  -0.02061 154 TYR A CD1 
1004 C CD2 . TYR A 154 ? 0.81786 0.76019 0.77732 0.04992  0.15863  -0.01648 154 TYR A CD2 
1005 C CE1 . TYR A 154 ? 0.79453 0.81455 0.79491 0.03681  0.11188  -0.01805 154 TYR A CE1 
1006 C CE2 . TYR A 154 ? 0.78076 0.76197 0.77137 0.04970  0.15767  -0.01354 154 TYR A CE2 
1007 C CZ  . TYR A 154 ? 0.74463 0.76323 0.75329 0.04254  0.13287  -0.01485 154 TYR A CZ  
1008 O OH  . TYR A 154 ? 0.74826 0.80106 0.78498 0.04055  0.13115  -0.01333 154 TYR A OH  
1009 N N   . GLU A 155 ? 0.81327 0.70705 0.76904 0.07220  0.19102  -0.00345 155 GLU A N   
1010 C CA  . GLU A 155 ? 0.81412 0.72494 0.80315 0.09051  0.21532  0.00842  155 GLU A CA  
1011 C C   . GLU A 155 ? 0.78622 0.71678 0.80389 0.10401  0.21571  0.02104  155 GLU A C   
1012 O O   . GLU A 155 ? 0.74095 0.71150 0.80385 0.11926  0.22030  0.03317  155 GLU A O   
1013 C CB  . GLU A 155 ? 0.83419 0.68844 0.78845 0.09632  0.24742  0.00497  155 GLU A CB  
1014 C CG  . GLU A 155 ? 0.85390 0.67033 0.76049 0.08337  0.24781  -0.00781 155 GLU A CG  
1015 C CD  . GLU A 155 ? 0.87246 0.73012 0.81017 0.08111  0.24632  -0.00603 155 GLU A CD  
1016 O OE1 . GLU A 155 ? 0.81861 0.72580 0.81551 0.09180  0.25493  0.00469  155 GLU A OE1 
1017 O OE2 . GLU A 155 ? 0.88591 0.72542 0.78948 0.06853  0.23498  -0.01542 155 GLU A OE2 
1018 N N   . LEU A 156 ? 0.79320 0.69516 0.78597 0.09859  0.21004  0.01860  156 LEU A N   
1019 C CA  . LEU A 156 ? 0.81628 0.72995 0.82862 0.11110  0.21137  0.03140  156 LEU A CA  
1020 C C   . LEU A 156 ? 0.75883 0.73140 0.80777 0.11398  0.18960  0.03971  156 LEU A C   
1021 O O   . LEU A 156 ? 0.72281 0.72079 0.80006 0.13195  0.19117  0.05386  156 LEU A O   
1022 C CB  . LEU A 156 ? 0.86420 0.73545 0.84409 0.09998  0.20944  0.02560  156 LEU A CB  
1023 C CG  . LEU A 156 ? 0.88899 0.76466 0.88113 0.11013  0.21162  0.03865  156 LEU A CG  
1024 C CD1 . LEU A 156 ? 0.90823 0.77120 0.90936 0.13498  0.23571  0.05237  156 LEU A CD1 
1025 C CD2 . LEU A 156 ? 0.90271 0.73841 0.86824 0.09340  0.20983  0.03042  156 LEU A CD2 
1026 N N   . LEU A 157 ? 0.74142 0.73300 0.78731 0.09751  0.16821  0.03103  157 LEU A N   
1027 C CA  . LEU A 157 ? 0.67778 0.71861 0.75019 0.09902  0.14842  0.03684  157 LEU A CA  
1028 C C   . LEU A 157 ? 0.65186 0.73123 0.76087 0.11160  0.14888  0.04416  157 LEU A C   
1029 O O   . LEU A 157 ? 0.64916 0.75887 0.78233 0.12460  0.13972  0.05569  157 LEU A O   
1030 C CB  . LEU A 157 ? 0.65033 0.70049 0.71308 0.08010  0.12978  0.02496  157 LEU A CB  
1031 C CG  . LEU A 157 ? 0.60494 0.69881 0.68700 0.07955  0.11061  0.02818  157 LEU A CG  
1032 C CD1 . LEU A 157 ? 0.61024 0.70778 0.69188 0.08752  0.10768  0.03875  157 LEU A CD1 
1033 C CD2 . LEU A 157 ? 0.63410 0.73167 0.70636 0.06259  0.09643  0.01596  157 LEU A CD2 
1034 N N   . GLN A 158 ? 0.65575 0.73171 0.76909 0.10804  0.15976  0.03772  158 GLN A N   
1035 C CA  . GLN A 158 ? 0.60926 0.72426 0.76716 0.11715  0.16251  0.04351  158 GLN A CA  
1036 C C   . GLN A 158 ? 0.62597 0.75052 0.81496 0.14017  0.17450  0.05814  158 GLN A C   
1037 O O   . GLN A 158 ? 0.61054 0.78074 0.84413 0.15071  0.16211  0.06697  158 GLN A O   
1038 C CB  . GLN A 158 ? 0.63135 0.72961 0.78368 0.10943  0.18060  0.03469  158 GLN A CB  
1039 C CG  . GLN A 158 ? 0.67132 0.74197 0.77920 0.08992  0.17164  0.02072  158 GLN A CG  
1040 C CD  . GLN A 158 ? 0.64196 0.74731 0.75777 0.07932  0.14298  0.01758  158 GLN A CD  
1041 O OE1 . GLN A 158 ? 0.59447 0.74352 0.74736 0.08188  0.13252  0.02205  158 GLN A OE1 
1042 N NE2 . GLN A 158 ? 0.68750 0.77265 0.76993 0.06737  0.12974  0.00941  158 GLN A NE2 
1043 N N   . HIS A 159 ? 0.68609 0.76640 0.85215 0.14877  0.19708  0.06071  159 HIS A N   
1044 C CA  . HIS A 159 ? 0.71554 0.80036 0.90848 0.17337  0.20895  0.07596  159 HIS A CA  
1045 C C   . HIS A 159 ? 0.71630 0.82109 0.91266 0.18238  0.18571  0.08706  159 HIS A C   
1046 O O   . HIS A 159 ? 0.69639 0.83432 0.93143 0.20195  0.17767  0.10051  159 HIS A O   
1047 C CB  . HIS A 159 ? 0.77810 0.80202 0.93678 0.17955  0.23959  0.07516  159 HIS A CB  
1048 C CG  . HIS A 159 ? 0.81776 0.81310 0.96576 0.17509  0.26670  0.06611  159 HIS A CG  
1049 N ND1 . HIS A 159 ? 0.83599 0.79116 0.93313 0.15426  0.26794  0.05020  159 HIS A ND1 
1050 C CD2 . HIS A 159 ? 0.81177 0.80875 0.99094 0.18991  0.29520  0.07128  159 HIS A CD2 
1051 C CE1 . HIS A 159 ? 0.84142 0.76941 0.92997 0.15636  0.29618  0.04597  159 HIS A CE1 
1052 N NE2 . HIS A 159 ? 0.80970 0.76273 0.94959 0.17749  0.31587  0.05854  159 HIS A NE2 
1053 N N   . ILE A 160 ? 0.71243 0.79586 0.86881 0.16897  0.17487  0.08197  160 ILE A N   
1054 C CA  . ILE A 160 ? 0.70882 0.80580 0.86018 0.17554  0.15533  0.09182  160 ILE A CA  
1055 C C   . ILE A 160 ? 0.70240 0.85307 0.88358 0.17593  0.12803  0.09360  160 ILE A C   
1056 O O   . ILE A 160 ? 0.75800 0.92958 0.95223 0.19254  0.11230  0.10640  160 ILE A O   
1057 C CB  . ILE A 160 ? 0.64916 0.71529 0.75878 0.15775  0.15301  0.08418  160 ILE A CB  
1058 C CG1 . ILE A 160 ? 0.73613 0.74729 0.81794 0.15703  0.17710  0.08270  160 ILE A CG1 
1059 C CG2 . ILE A 160 ? 0.65732 0.73444 0.75708 0.16327  0.13650  0.09386  160 ILE A CG2 
1060 N N   . LEU A 161 ? 0.63644 0.80603 0.82490 0.15775  0.12060  0.08059  161 LEU A N   
1061 C CA  . LEU A 161 ? 0.56625 0.78319 0.78264 0.15538  0.09547  0.08012  161 LEU A CA  
1062 C C   . LEU A 161 ? 0.62619 0.87931 0.89737 0.17291  0.09338  0.08972  161 LEU A C   
1063 O O   . LEU A 161 ? 0.70413 0.99419 0.99905 0.17925  0.06694  0.09515  161 LEU A O   
1064 C CB  . LEU A 161 ? 0.52341 0.74705 0.73642 0.13294  0.09270  0.06444  161 LEU A CB  
1065 C CG  . LEU A 161 ? 0.52678 0.72492 0.69651 0.11588  0.08883  0.05459  161 LEU A CG  
1066 C CD1 . LEU A 161 ? 0.51860 0.71826 0.68495 0.09755  0.08816  0.04052  161 LEU A CD1 
1067 C CD2 . LEU A 161 ? 0.53946 0.74865 0.69473 0.11704  0.06825  0.05886  161 LEU A CD2 
1068 N N   . LYS A 162 ? 0.59191 0.83380 0.88451 0.18120  0.12065  0.09166  162 LYS A N   
1069 C CA  . LYS A 162 ? 0.61496 0.89325 0.96997 0.20018  0.12244  0.10208  162 LYS A CA  
1070 C C   . LYS A 162 ? 0.73808 1.01927 1.09817 0.22599  0.11058  0.11948  162 LYS A C   
1071 O O   . LYS A 162 ? 0.77197 1.09704 1.18113 0.24072  0.08958  0.12884  162 LYS A O   
1072 C CB  . LYS A 162 ? 0.60594 0.86417 0.97855 0.20425  0.16116  0.10032  162 LYS A CB  
1073 N N   . GLN A 163 ? 0.82802 1.06133 1.13791 0.23163  0.12237  0.12408  163 GLN A N   
1074 C CA  . GLN A 163 ? 0.85382 1.07942 1.15689 0.25658  0.11323  0.14162  163 GLN A CA  
1075 C C   . GLN A 163 ? 0.89660 1.14284 1.18252 0.25524  0.07543  0.14484  163 GLN A C   
1076 O O   . GLN A 163 ? 0.90827 1.13668 1.14912 0.23644  0.06956  0.13599  163 GLN A O   
1077 C CB  . GLN A 163 ? 0.93094 1.09394 1.18102 0.25894  0.13865  0.14418  163 GLN A CB  
1078 C CG  . GLN A 163 ? 0.95186 1.08228 1.20556 0.26065  0.17629  0.14010  163 GLN A CG  
1079 C CD  . GLN A 163 ? 1.04440 1.10960 1.24037 0.25476  0.19772  0.13752  163 GLN A CD  
1080 O OE1 . GLN A 163 ? 1.07516 1.10249 1.25548 0.24852  0.22526  0.12919  163 GLN A OE1 
1081 N NE2 . GLN A 163 ? 1.07399 1.12219 1.23570 0.25562  0.18572  0.14407  163 GLN A NE2 
1082 N N   . ARG A 164 ? 1.02877 1.31073 1.35030 0.27594  0.04957  0.15740  164 ARG A N   
1083 C CA  . ARG A 164 ? 1.08319 1.38174 1.38472 0.27721  0.01005  0.16074  164 ARG A CA  
1084 C C   . ARG A 164 ? 1.03211 1.35127 1.32873 0.24821  -0.00433 0.14283  164 ARG A C   
1085 O O   . ARG A 164 ? 1.05436 1.35116 1.29719 0.23548  -0.01225 0.13745  164 ARG A O   
1086 C CB  . ARG A 164 ? 1.16204 1.40897 1.39162 0.28539  0.01173  0.17030  164 ARG A CB  
1087 N N   . LEU A 175 ? 1.06821 1.15656 0.85726 0.02332  -0.01874 -0.05087 175 LEU A N   
1088 C CA  . LEU A 175 ? 1.01560 1.09252 0.81308 0.02427  0.00417  -0.05489 175 LEU A CA  
1089 C C   . LEU A 175 ? 1.05172 1.08543 0.79431 0.03106  0.02088  -0.05720 175 LEU A C   
1090 O O   . LEU A 175 ? 1.08202 1.08981 0.77170 0.03009  0.00785  -0.06120 175 LEU A O   
1091 C CB  . LEU A 175 ? 0.88910 0.97532 0.70726 0.01343  -0.00455 -0.06521 175 LEU A CB  
1092 N N   . PRO A 176 ? 1.03381 1.05727 0.78787 0.03833  0.04987  -0.05491 176 PRO A N   
1093 C CA  . PRO A 176 ? 1.09477 1.07342 0.79778 0.04612  0.07275  -0.05679 176 PRO A CA  
1094 C C   . PRO A 176 ? 1.16779 1.11998 0.83343 0.04027  0.06456  -0.07014 176 PRO A C   
1095 O O   . PRO A 176 ? 1.14496 1.11513 0.83879 0.03153  0.05125  -0.07737 176 PRO A O   
1096 C CB  . PRO A 176 ? 1.02876 1.01519 0.77673 0.05371  0.10458  -0.05200 176 PRO A CB  
1097 C CG  . PRO A 176 ? 1.01817 1.04763 0.83126 0.04738  0.09038  -0.05297 176 PRO A CG  
1098 C CD  . PRO A 176 ? 0.98948 1.04076 0.80517 0.03996  0.06279  -0.05077 176 PRO A CD  
1099 N N   . ALA A 177 ? 1.25376 1.15642 0.84948 0.04514  0.07439  -0.07346 177 ALA A N   
1100 C CA  . ALA A 177 ? 1.28761 1.15577 0.83696 0.03872  0.06651  -0.08746 177 ALA A CA  
1101 C C   . ALA A 177 ? 1.28771 1.15230 0.86492 0.04136  0.08855  -0.09269 177 ALA A C   
1102 O O   . ALA A 177 ? 1.33040 1.18435 0.89736 0.03248  0.07664  -0.10399 177 ALA A O   
1103 C CB  . ALA A 177 ? 1.35721 1.16414 0.81615 0.04485  0.07435  -0.08991 177 ALA A CB  
1104 N N   . HIS A 178 ? 1.19321 1.06657 0.80882 0.05352  0.11996  -0.08448 178 HIS A N   
1105 C CA  . HIS A 178 ? 1.14931 1.02413 0.80009 0.05895  0.13804  -0.08782 178 HIS A CA  
1106 C C   . HIS A 178 ? 1.08543 1.00020 0.78993 0.05017  0.11423  -0.09022 178 HIS A C   
1107 O O   . HIS A 178 ? 1.09961 1.00894 0.82058 0.05327  0.12058  -0.09470 178 HIS A O   
1108 C CB  . HIS A 178 ? 1.08712 0.97130 0.78117 0.07326  0.17327  -0.07787 178 HIS A CB  
1109 N N   . LEU A 179 ? 1.03349 0.98357 0.76181 0.04071  0.08882  -0.08674 179 LEU A N   
1110 C CA  . LEU A 179 ? 0.93766 0.92064 0.71097 0.03258  0.06934  -0.08798 179 LEU A CA  
1111 C C   . LEU A 179 ? 0.92460 0.91385 0.68117 0.01708  0.04072  -0.09379 179 LEU A C   
1112 O O   . LEU A 179 ? 0.88408 0.90334 0.67754 0.00998  0.02614  -0.09217 179 LEU A O   
1113 C CB  . LEU A 179 ? 0.83677 0.85936 0.66804 0.03648  0.07018  -0.07777 179 LEU A CB  
1114 C CG  . LEU A 179 ? 0.81138 0.83937 0.68265 0.04874  0.09164  -0.07372 179 LEU A CG  
1115 C CD1 . LEU A 179 ? 0.75611 0.80749 0.66360 0.05295  0.10146  -0.06383 179 LEU A CD1 
1116 C CD2 . LEU A 179 ? 0.78612 0.82791 0.69128 0.04791  0.07946  -0.07627 179 LEU A CD2 
1117 N N   . ARG A 180 ? 0.93437 0.89441 0.63656 0.01159  0.03245  -0.10083 180 ARG A N   
1118 C CA  . ARG A 180 ? 0.92956 0.89936 0.62498 -0.00429 0.00299  -0.10728 180 ARG A CA  
1119 C C   . ARG A 180 ? 0.90746 0.87413 0.61528 -0.01629 -0.00314 -0.11678 180 ARG A C   
1120 O O   . ARG A 180 ? 0.90812 0.88862 0.62536 -0.03145 -0.02468 -0.12204 180 ARG A O   
1121 C CB  . ARG A 180 ? 1.01631 0.95236 0.64761 -0.00742 -0.00893 -0.11353 180 ARG A CB  
1122 C CG  . ARG A 180 ? 1.01309 0.97320 0.65005 -0.01856 -0.04268 -0.11429 180 ARG A CG  
1123 C CD  . ARG A 180 ? 1.03037 1.02727 0.70293 -0.00978 -0.04427 -0.09977 180 ARG A CD  
1124 N NE  . ARG A 180 ? 1.08564 1.05928 0.72442 0.00598  -0.02477 -0.09095 180 ARG A NE  
1125 C CZ  . ARG A 180 ? 1.15243 1.10054 0.73731 0.01103  -0.03466 -0.08874 180 ARG A CZ  
1126 N NH1 . ARG A 180 ? 1.14107 1.08708 0.70212 0.00185  -0.06894 -0.09530 180 ARG A NH1 
1127 N NH2 . ARG A 180 ? 1.22210 1.14447 0.77626 0.02566  -0.00998 -0.07958 180 ARG A NH2 
1128 N N   . LEU A 181 ? 0.92101 0.86931 0.63148 -0.00935 0.01614  -0.11848 181 LEU A N   
1129 C CA  . LEU A 181 ? 0.91177 0.85073 0.62956 -0.01880 0.01311  -0.12583 181 LEU A CA  
1130 C C   . LEU A 181 ? 0.90815 0.88421 0.67806 -0.02175 0.00646  -0.11906 181 LEU A C   
1131 O O   . LEU A 181 ? 0.87684 0.88297 0.67836 -0.01401 0.00726  -0.10907 181 LEU A O   
1132 C CB  . LEU A 181 ? 0.86601 0.77012 0.56791 -0.00690 0.03567  -0.12831 181 LEU A CB  
1133 N N   . GLN A 182 ? 0.89856 0.86656 0.67272 -0.03355 0.00175  -0.12493 182 GLN A N   
1134 C CA  . GLN A 182 ? 0.80498 0.79725 0.61741 -0.03685 -0.00163 -0.11927 182 GLN A CA  
1135 C C   . GLN A 182 ? 0.79183 0.78457 0.62144 -0.01973 0.00979  -0.11118 182 GLN A C   
1136 O O   . GLN A 182 ? 0.82899 0.79556 0.64346 -0.00940 0.02109  -0.11280 182 GLN A O   
1137 C CB  . GLN A 182 ? 0.83061 0.80564 0.63836 -0.05350 -0.00418 -0.12721 182 GLN A CB  
1138 C CG  . GLN A 182 ? 0.88805 0.86714 0.69014 -0.07354 -0.01930 -0.13664 182 GLN A CG  
1139 C CD  . GLN A 182 ? 1.00561 0.95215 0.76119 -0.07595 -0.02240 -0.14692 182 GLN A CD  
1140 O OE1 . GLN A 182 ? 1.03019 0.94018 0.75488 -0.06677 -0.00775 -0.14976 182 GLN A OE1 
1141 N NE2 . GLN A 182 ? 1.01789 0.97549 0.76620 -0.08641 -0.04193 -0.15207 182 GLN A NE2 
1142 N N   . PRO A 183 ? 0.76681 0.78784 0.62878 -0.01594 0.00598  -0.10275 183 PRO A N   
1143 C CA  . PRO A 183 ? 0.76780 0.79112 0.64855 -0.00057 0.01100  -0.09595 183 PRO A CA  
1144 C C   . PRO A 183 ? 0.79043 0.78287 0.65833 0.00490  0.01520  -0.09801 183 PRO A C   
1145 O O   . PRO A 183 ? 0.79793 0.78586 0.67632 0.02063  0.01950  -0.09440 183 PRO A O   
1146 C CB  . PRO A 183 ? 0.75135 0.80054 0.65812 -0.00338 0.00297  -0.08970 183 PRO A CB  
1147 C CG  . PRO A 183 ? 0.74085 0.81127 0.65099 -0.01279 -0.00205 -0.08985 183 PRO A CG  
1148 C CD  . PRO A 183 ? 0.80852 0.86108 0.69185 -0.02373 -0.00375 -0.09895 183 PRO A CD  
1149 N N   . ILE A 184 ? 0.82888 0.79955 0.67715 -0.00730 0.01448  -0.10321 184 ILE A N   
1150 C CA  . ILE A 184 ? 0.84340 0.77672 0.67178 -0.00179 0.01994  -0.10448 184 ILE A CA  
1151 C C   . ILE A 184 ? 0.83457 0.74442 0.64662 0.00991  0.03008  -0.10783 184 ILE A C   
1152 O O   . ILE A 184 ? 0.85119 0.73770 0.65822 0.02430  0.03441  -0.10522 184 ILE A O   
1153 C CB  . ILE A 184 ? 0.82073 0.73163 0.62970 -0.02047 0.02200  -0.11039 184 ILE A CB  
1154 C CG1 . ILE A 184 ? 0.81687 0.67967 0.59620 -0.01530 0.03065  -0.11203 184 ILE A CG1 
1155 C CG2 . ILE A 184 ? 0.85113 0.76822 0.65361 -0.03808 0.01992  -0.11964 184 ILE A CG2 
1156 C CD1 . ILE A 184 ? 0.87392 0.70947 0.63424 -0.03556 0.03714  -0.11849 184 ILE A CD1 
1157 N N   . TYR A 185 ? 0.80227 0.71482 0.60346 0.00582  0.03440  -0.11309 185 TYR A N   
1158 C CA  . TYR A 185 ? 0.85125 0.73613 0.63112 0.01695  0.04869  -0.11687 185 TYR A CA  
1159 C C   . TYR A 185 ? 0.84277 0.74945 0.64738 0.03373  0.05718  -0.11031 185 TYR A C   
1160 O O   . TYR A 185 ? 0.86520 0.74995 0.65215 0.04298  0.07363  -0.11313 185 TYR A O   
1161 C CB  . TYR A 185 ? 0.90452 0.76417 0.64325 0.00126  0.05009  -0.12860 185 TYR A CB  
1162 C CG  . TYR A 185 ? 0.91852 0.76335 0.64286 -0.02024 0.04143  -0.13620 185 TYR A CG  
1163 C CD1 . TYR A 185 ? 0.95307 0.76196 0.66228 -0.02022 0.04864  -0.13823 185 TYR A CD1 
1164 C CD2 . TYR A 185 ? 0.91821 0.78412 0.64684 -0.04021 0.02702  -0.14090 185 TYR A CD2 
1165 C CE1 . TYR A 185 ? 0.95555 0.74842 0.65438 -0.04149 0.04513  -0.14502 185 TYR A CE1 
1166 C CE2 . TYR A 185 ? 0.92328 0.77936 0.64949 -0.06131 0.02125  -0.14807 185 TYR A CE2 
1167 C CZ  . TYR A 185 ? 0.95210 0.77071 0.66325 -0.06286 0.03213  -0.15029 185 TYR A CZ  
1168 O OH  . TYR A 185 ? 0.97987 0.78589 0.69089 -0.08524 0.03080  -0.15721 185 TYR A OH  
1169 N N   . TRP A 186 ? 0.82252 0.76802 0.66677 0.03744  0.04910  -0.10198 186 TRP A N   
1170 C CA  . TRP A 186 ? 0.79281 0.75903 0.66632 0.05104  0.05945  -0.09591 186 TRP A CA  
1171 C C   . TRP A 186 ? 0.79269 0.75330 0.69290 0.07098  0.06808  -0.09188 186 TRP A C   
1172 O O   . TRP A 186 ? 0.83295 0.78463 0.73823 0.07597  0.05812  -0.09045 186 TRP A O   
1173 C CB  . TRP A 186 ? 0.76405 0.77072 0.67295 0.04749  0.04821  -0.08903 186 TRP A CB  
1174 C CG  . TRP A 186 ? 0.76053 0.77794 0.65252 0.03368  0.04295  -0.09043 186 TRP A CG  
1175 C CD1 . TRP A 186 ? 0.79051 0.78805 0.64152 0.02354  0.04294  -0.09757 186 TRP A CD1 
1176 C CD2 . TRP A 186 ? 0.75635 0.80550 0.67204 0.02914  0.03429  -0.08456 186 TRP A CD2 
1177 N NE1 . TRP A 186 ? 0.79299 0.81115 0.64397 0.01447  0.03282  -0.09563 186 TRP A NE1 
1178 C CE2 . TRP A 186 ? 0.77454 0.82358 0.66445 0.01838  0.02943  -0.08722 186 TRP A CE2 
1179 C CE3 . TRP A 186 ? 0.71670 0.79190 0.67174 0.03321  0.02892  -0.07776 186 TRP A CE3 
1180 C CZ2 . TRP A 186 ? 0.74785 0.82245 0.65166 0.01394  0.02155  -0.08188 186 TRP A CZ2 
1181 C CZ3 . TRP A 186 ? 0.66734 0.76436 0.63236 0.02692  0.02313  -0.07360 186 TRP A CZ3 
1182 C CH2 . TRP A 186 ? 0.68996 0.78687 0.63028 0.01851  0.02057  -0.07496 186 TRP A CH2 
1183 N N   . SER A 187 ? 0.78193 0.74662 0.70001 0.08348  0.08744  -0.08934 187 SER A N   
1184 C CA  . SER A 187 ? 0.82807 0.79404 0.78421 0.10417  0.09764  -0.08487 187 SER A CA  
1185 C C   . SER A 187 ? 0.83590 0.84706 0.85754 0.10991  0.08813  -0.07685 187 SER A C   
1186 O O   . SER A 187 ? 0.83611 0.87244 0.86782 0.09837  0.07887  -0.07489 187 SER A O   
1187 C CB  . SER A 187 ? 0.94776 0.88947 0.89051 0.11532  0.12958  -0.08690 187 SER A CB  
1188 O OG  . SER A 187 ? 0.97558 0.93526 0.93063 0.11318  0.14392  -0.08379 187 SER A OG  
1189 N N   . ARG A 188 ? 0.79845 0.81905 0.86704 0.12821  0.08954  -0.07244 188 ARG A N   
1190 C CA  . ARG A 188 ? 0.81786 0.88184 0.95566 0.13298  0.07872  -0.06619 188 ARG A CA  
1191 C C   . ARG A 188 ? 0.82997 0.91445 0.99215 0.12894  0.10146  -0.06400 188 ARG A C   
1192 O O   . ARG A 188 ? 0.81690 0.93220 1.01145 0.12053  0.09110  -0.06106 188 ARG A O   
1193 C CB  . ARG A 188 ? 0.82102 0.89279 1.01088 0.15488  0.07543  -0.06208 188 ARG A CB  
1194 C CG  . ARG A 188 ? 0.75892 0.87688 1.02687 0.15880  0.05788  -0.05703 188 ARG A CG  
1195 C CD  . ARG A 188 ? 0.72086 0.84906 1.04601 0.18225  0.05125  -0.05282 188 ARG A CD  
1196 N NE  . ARG A 188 ? 0.72716 0.90063 1.12937 0.18373  0.02727  -0.04947 188 ARG A NE  
1197 C CZ  . ARG A 188 ? 0.76409 0.97525 1.24288 0.18629  0.04399  -0.04685 188 ARG A CZ  
1198 N NH1 . ARG A 188 ? 0.81769 1.02402 1.30382 0.19022  0.08807  -0.04600 188 ARG A NH1 
1199 N NH2 . ARG A 188 ? 0.74725 0.99840 1.29491 0.18402  0.01677  -0.04546 188 ARG A NH2 
1200 N N   . ASP A 189 ? 0.97753 1.03880 1.11819 0.13484  0.13440  -0.06543 189 ASP A N   
1201 C CA  . ASP A 189 ? 0.96846 1.03737 1.11619 0.13106  0.15995  -0.06276 189 ASP A CA  
1202 C C   . ASP A 189 ? 0.96696 1.02930 1.06187 0.11246  0.15002  -0.06488 189 ASP A C   
1203 O O   . ASP A 189 ? 0.94442 1.02385 1.05445 0.10651  0.15717  -0.06061 189 ASP A O   
1204 C CB  . ASP A 189 ? 0.99896 1.03422 1.12512 0.14361  0.19987  -0.06389 189 ASP A CB  
1205 C CG  . ASP A 189 ? 1.07276 1.11282 1.25264 0.16478  0.21166  -0.06142 189 ASP A CG  
1206 O OD1 . ASP A 189 ? 1.09054 1.16231 1.32585 0.16971  0.18495  -0.05851 189 ASP A OD1 
1207 O OD2 . ASP A 189 ? 1.15183 1.16142 1.31658 0.17761  0.24720  -0.06225 189 ASP A OD2 
1208 N N   . ASP A 190 ? 0.83967 0.87765 0.87642 0.10336  0.13389  -0.07107 190 ASP A N   
1209 C CA  . ASP A 190 ? 0.84378 0.88039 0.83933 0.08674  0.12127  -0.07287 190 ASP A CA  
1210 C C   . ASP A 190 ? 0.79417 0.86766 0.82675 0.07861  0.09892  -0.06837 190 ASP A C   
1211 O O   . ASP A 190 ? 0.76484 0.84930 0.79251 0.07084  0.09900  -0.06527 190 ASP A O   
1212 C CB  . ASP A 190 ? 0.84389 0.85076 0.78228 0.07754  0.10829  -0.08114 190 ASP A CB  
1213 N N   . VAL A 191 ? 0.79135 0.87931 0.85653 0.08145  0.07980  -0.06776 191 VAL A N   
1214 C CA  . VAL A 191 ? 0.75435 0.86981 0.84834 0.07415  0.05870  -0.06463 191 VAL A CA  
1215 C C   . VAL A 191 ? 0.72542 0.86717 0.86718 0.07547  0.07000  -0.05920 191 VAL A C   
1216 O O   . VAL A 191 ? 0.66625 0.82212 0.81235 0.06598  0.06317  -0.05678 191 VAL A O   
1217 C CB  . VAL A 191 ? 0.68807 0.80513 0.80035 0.07945  0.03615  -0.06514 191 VAL A CB  
1218 C CG1 . VAL A 191 ? 0.62438 0.76321 0.76165 0.07265  0.01485  -0.06290 191 VAL A CG1 
1219 C CG2 . VAL A 191 ? 0.75915 0.84547 0.82006 0.07576  0.02844  -0.06981 191 VAL A CG2 
1220 N N   . ALA A 192 ? 0.71262 0.85964 0.89285 0.08726  0.09024  -0.05702 192 ALA A N   
1221 C CA  . ALA A 192 ? 0.60628 0.77753 0.83908 0.08734  0.10548  -0.05192 192 ALA A CA  
1222 C C   . ALA A 192 ? 0.61098 0.76991 0.80699 0.08017  0.12567  -0.04907 192 ALA A C   
1223 O O   . ALA A 192 ? 0.64008 0.81491 0.85628 0.07256  0.12533  -0.04516 192 ALA A O   
1224 C CB  . ALA A 192 ? 0.64738 0.82587 0.93260 0.10221  0.12822  -0.04995 192 ALA A CB  
1225 N N   . GLN A 193 ? 0.65203 0.77828 0.78991 0.08297  0.14244  -0.05107 193 GLN A N   
1226 C CA  . GLN A 193 ? 0.67019 0.77861 0.76332 0.07814  0.15762  -0.04797 193 GLN A CA  
1227 C C   . GLN A 193 ? 0.67534 0.79178 0.74367 0.06590  0.13131  -0.04771 193 GLN A C   
1228 O O   . GLN A 193 ? 0.62952 0.74546 0.68705 0.06225  0.13808  -0.04223 193 GLN A O   
1229 C CB  . GLN A 193 ? 0.70688 0.77278 0.73458 0.08341  0.17551  -0.05181 193 GLN A CB  
1230 C CG  . GLN A 193 ? 0.71223 0.75998 0.75115 0.09622  0.21645  -0.04899 193 GLN A CG  
1231 C CD  . GLN A 193 ? 0.75542 0.76594 0.75258 0.10499  0.22884  -0.05570 193 GLN A CD  
1232 N N   . TRP A 194 ? 0.67064 0.79217 0.73038 0.06055  0.10390  -0.05277 194 TRP A N   
1233 C CA  . TRP A 194 ? 0.63008 0.76116 0.67485 0.05000  0.08211  -0.05223 194 TRP A CA  
1234 C C   . TRP A 194 ? 0.61745 0.77324 0.70619 0.04676  0.07797  -0.04702 194 TRP A C   
1235 O O   . TRP A 194 ? 0.59806 0.75715 0.67521 0.04153  0.07513  -0.04299 194 TRP A O   
1236 C CB  . TRP A 194 ? 0.63158 0.76024 0.66351 0.04516  0.05967  -0.05833 194 TRP A CB  
1237 C CG  . TRP A 194 ? 0.56739 0.70899 0.59847 0.03569  0.04048  -0.05737 194 TRP A CG  
1238 C CD1 . TRP A 194 ? 0.57019 0.71184 0.57541 0.02917  0.03517  -0.05614 194 TRP A CD1 
1239 C CD2 . TRP A 194 ? 0.57469 0.72778 0.63033 0.03308  0.02483  -0.05749 194 TRP A CD2 
1240 N NE1 . TRP A 194 ? 0.54856 0.70291 0.56569 0.02316  0.02123  -0.05509 194 TRP A NE1 
1241 C CE2 . TRP A 194 ? 0.56515 0.72303 0.60779 0.02500  0.01549  -0.05624 194 TRP A CE2 
1242 C CE3 . TRP A 194 ? 0.57301 0.73032 0.65834 0.03778  0.01661  -0.05848 194 TRP A CE3 
1243 C CZ2 . TRP A 194 ? 0.53612 0.69771 0.58864 0.02117  0.00281  -0.05630 194 TRP A CZ2 
1244 C CZ3 . TRP A 194 ? 0.50665 0.66635 0.59721 0.03347  -0.00088 -0.05889 194 TRP A CZ3 
1245 C CH2 . TRP A 194 ? 0.52603 0.68535 0.59741 0.02506  -0.00540 -0.05798 194 TRP A CH2 
1246 N N   . LEU A 195 ? 0.57123 0.74324 0.71123 0.05005  0.07606  -0.04732 195 LEU A N   
1247 C CA  . LEU A 195 ? 0.54970 0.74231 0.73312 0.04516  0.07124  -0.04414 195 LEU A CA  
1248 C C   . LEU A 195 ? 0.52265 0.71367 0.71257 0.04476  0.09725  -0.03758 195 LEU A C   
1249 O O   . LEU A 195 ? 0.55816 0.75144 0.74426 0.03840  0.09530  -0.03377 195 LEU A O   
1250 C CB  . LEU A 195 ? 0.55950 0.76968 0.79977 0.04916  0.06170  -0.04656 195 LEU A CB  
1251 C CG  . LEU A 195 ? 0.54717 0.75199 0.77607 0.05200  0.03603  -0.05170 195 LEU A CG  
1252 C CD1 . LEU A 195 ? 0.54635 0.76576 0.82996 0.06105  0.02912  -0.05279 195 LEU A CD1 
1253 C CD2 . LEU A 195 ? 0.54705 0.74983 0.75771 0.04296  0.01189  -0.05339 195 LEU A CD2 
1254 N N   . LYS A 196 ? 0.53617 0.71794 0.73130 0.05251  0.12479  -0.03564 196 LYS A N   
1255 C CA  . LYS A 196 ? 0.54447 0.71696 0.74059 0.05311  0.15524  -0.02848 196 LYS A CA  
1256 C C   . LYS A 196 ? 0.59706 0.74692 0.72798 0.05109  0.15522  -0.02434 196 LYS A C   
1257 O O   . LYS A 196 ? 0.63730 0.78275 0.76767 0.04847  0.16717  -0.01740 196 LYS A O   
1258 C CB  . LYS A 196 ? 0.57012 0.72848 0.77256 0.06342  0.18853  -0.02742 196 LYS A CB  
1259 N N   . TRP A 197 ? 0.59565 0.73039 0.67310 0.05232  0.14081  -0.02841 197 TRP A N   
1260 C CA  . TRP A 197 ? 0.62883 0.74758 0.65132 0.05073  0.13309  -0.02499 197 TRP A CA  
1261 C C   . TRP A 197 ? 0.63661 0.77544 0.67666 0.04373  0.11276  -0.02258 197 TRP A C   
1262 O O   . TRP A 197 ? 0.69917 0.83082 0.72228 0.04418  0.11689  -0.01522 197 TRP A O   
1263 C CB  . TRP A 197 ? 0.64944 0.75240 0.62199 0.05087  0.11793  -0.03180 197 TRP A CB  
1264 C CG  . TRP A 197 ? 0.71810 0.81492 0.64816 0.04797  0.09988  -0.02967 197 TRP A CG  
1265 C CD1 . TRP A 197 ? 0.79836 0.86865 0.67717 0.05285  0.10652  -0.02446 197 TRP A CD1 
1266 C CD2 . TRP A 197 ? 0.69527 0.81200 0.63197 0.04083  0.07216  -0.03216 197 TRP A CD2 
1267 N NE1 . TRP A 197 ? 0.85215 0.92946 0.71118 0.04969  0.08078  -0.02354 197 TRP A NE1 
1268 C CE2 . TRP A 197 ? 0.78472 0.89201 0.68234 0.04197  0.06178  -0.02823 197 TRP A CE2 
1269 C CE3 . TRP A 197 ? 0.64930 0.78789 0.61942 0.03450  0.05629  -0.03686 197 TRP A CE3 
1270 C CZ2 . TRP A 197 ? 0.78020 0.90561 0.68240 0.03680  0.03759  -0.02891 197 TRP A CZ2 
1271 C CZ3 . TRP A 197 ? 0.65899 0.80943 0.62576 0.02885  0.03633  -0.03753 197 TRP A CZ3 
1272 C CH2 . TRP A 197 ? 0.71675 0.86376 0.65530 0.02991  0.02786  -0.03360 197 TRP A CH2 
1273 N N   . ALA A 198 ? 0.62802 0.78703 0.69756 0.03852  0.09202  -0.02831 198 ALA A N   
1274 C CA  . ALA A 198 ? 0.61775 0.78987 0.69956 0.03243  0.07538  -0.02696 198 ALA A CA  
1275 C C   . ALA A 198 ? 0.68782 0.86452 0.80191 0.03026  0.08808  -0.02132 198 ALA A C   
1276 O O   . ALA A 198 ? 0.69230 0.86690 0.79804 0.02834  0.08563  -0.01638 198 ALA A O   
1277 C CB  . ALA A 198 ? 0.52600 0.70952 0.62631 0.02822  0.05455  -0.03428 198 ALA A CB  
1278 N N   . GLU A 199 ? 0.66098 0.84373 0.81578 0.03048  0.10271  -0.02198 199 GLU A N   
1279 C CA  . GLU A 199 ? 0.65073 0.83826 0.84383 0.02553  0.11581  -0.01784 199 GLU A CA  
1280 C C   . GLU A 199 ? 0.69782 0.86371 0.85853 0.02876  0.13886  -0.00793 199 GLU A C   
1281 O O   . GLU A 199 ? 0.78907 0.95092 0.95301 0.02468  0.14061  -0.00324 199 GLU A O   
1282 C CB  . GLU A 199 ? 0.62894 0.83040 0.87994 0.02527  0.12885  -0.02038 199 GLU A CB  
1283 C CG  . GLU A 199 ? 0.65566 0.86045 0.95056 0.01855  0.14896  -0.01602 199 GLU A CG  
1284 C CD  . GLU A 199 ? 0.71392 0.93919 1.07986 0.01763  0.16077  -0.01889 199 GLU A CD  
1285 O OE1 . GLU A 199 ? 0.74244 0.98126 1.12539 0.02311  0.14698  -0.02457 199 GLU A OE1 
1286 O OE2 . GLU A 199 ? 0.74003 0.96783 1.14818 0.01169  0.18450  -0.01513 199 GLU A OE2 
1287 N N   . ASN A 200 ? 0.70540 0.85130 0.82821 0.03700  0.15681  -0.00450 200 ASN A N   
1288 C CA  . ASN A 200 ? 0.76577 0.88302 0.84577 0.04226  0.17728  0.00582  200 ASN A CA  
1289 C C   . ASN A 200 ? 0.81744 0.92835 0.85117 0.04498  0.15490  0.00906  200 ASN A C   
1290 O O   . ASN A 200 ? 0.87720 0.97254 0.89139 0.04784  0.16228  0.01828  200 ASN A O   
1291 C CB  . ASN A 200 ? 0.83631 0.92601 0.87951 0.05105  0.20264  0.00795  200 ASN A CB  
1292 C CG  . ASN A 200 ? 0.83456 0.93395 0.93109 0.05045  0.22669  0.00476  200 ASN A CG  
1293 O OD1 . ASN A 200 ? 0.79391 0.92539 0.95583 0.04354  0.21592  -0.00066 200 ASN A OD1 
1294 N ND2 . ASN A 200 ? 0.83776 0.90754 0.90615 0.05860  0.25920  0.00818  200 ASN A ND2 
1295 N N   . GLU A 201 ? 0.80336 0.92621 0.82313 0.04445  0.12840  0.00199  201 GLU A N   
1296 C CA  . GLU A 201 ? 0.82170 0.94328 0.80673 0.04719  0.10738  0.00473  201 GLU A CA  
1297 C C   . GLU A 201 ? 0.79502 0.93014 0.80597 0.04350  0.09825  0.00759  201 GLU A C   
1298 O O   . GLU A 201 ? 0.83498 0.96219 0.82374 0.04914  0.09448  0.01557  201 GLU A O   
1299 C CB  . GLU A 201 ? 0.80939 0.94089 0.78118 0.04500  0.08470  -0.00442 201 GLU A CB  
1300 C CG  . GLU A 201 ? 0.82783 0.96531 0.77752 0.04623  0.06151  -0.00285 201 GLU A CG  
1301 C CD  . GLU A 201 ? 0.98739 1.10127 0.88409 0.05495  0.06025  0.00362  201 GLU A CD  
1302 O OE1 . GLU A 201 ? 1.04295 1.12935 0.90996 0.05996  0.07989  0.00625  201 GLU A OE1 
1303 O OE2 . GLU A 201 ? 1.10183 1.22290 0.98594 0.05753  0.03944  0.00622  201 GLU A OE2 
1304 N N   . PHE A 202 ? 0.69461 0.84660 0.74946 0.03522  0.09394  0.00124  202 PHE A N   
1305 C CA  . PHE A 202 ? 0.61128 0.76969 0.68430 0.03100  0.08515  0.00179  202 PHE A CA  
1306 C C   . PHE A 202 ? 0.63065 0.78352 0.73515 0.02536  0.10084  0.00392  202 PHE A C   
1307 O O   . PHE A 202 ? 0.62256 0.77720 0.74427 0.01954  0.09314  0.00141  202 PHE A O   
1308 C CB  . PHE A 202 ? 0.53802 0.71164 0.62585 0.02510  0.06442  -0.00794 202 PHE A CB  
1309 C CG  . PHE A 202 ? 0.57118 0.75021 0.63450 0.02766  0.05048  -0.01091 202 PHE A CG  
1310 C CD1 . PHE A 202 ? 0.58114 0.76256 0.62765 0.03133  0.04194  -0.00670 202 PHE A CD1 
1311 C CD2 . PHE A 202 ? 0.59373 0.77546 0.65475 0.02630  0.04637  -0.01797 202 PHE A CD2 
1312 C CE1 . PHE A 202 ? 0.57917 0.76824 0.61133 0.03115  0.02842  -0.01037 202 PHE A CE1 
1313 C CE2 . PHE A 202 ? 0.58966 0.77350 0.62887 0.02618  0.03421  -0.02173 202 PHE A CE2 
1314 C CZ  . PHE A 202 ? 0.57827 0.76709 0.60515 0.02739  0.02471  -0.01836 202 PHE A CZ  
1315 N N   . SER A 203 ? 0.62071 0.76375 0.73236 0.02614  0.12428  0.00802  203 SER A N   
1316 C CA  . SER A 203 ? 0.62321 0.76121 0.77137 0.01854  0.14222  0.00993  203 SER A CA  
1317 C C   . SER A 203 ? 0.59248 0.75051 0.79096 0.00682  0.12594  -0.00112 203 SER A C   
1318 O O   . SER A 203 ? 0.60026 0.75429 0.82026 -0.00182 0.12442  -0.00268 203 SER A O   
1319 C CB  . SER A 203 ? 0.68508 0.80212 0.81240 0.02078  0.15039  0.01924  203 SER A CB  
1320 O OG  . SER A 203 ? 0.73699 0.83220 0.81418 0.03351  0.16192  0.03048  203 SER A OG  
1321 N N   . LEU A 204 ? 0.57051 0.74604 0.78344 0.00696  0.11194  -0.00905 204 LEU A N   
1322 C CA  . LEU A 204 ? 0.53434 0.72574 0.78811 -0.00164 0.09135  -0.01914 204 LEU A CA  
1323 C C   . LEU A 204 ? 0.53784 0.74158 0.85252 -0.00841 0.10415  -0.02115 204 LEU A C   
1324 O O   . LEU A 204 ? 0.57251 0.77294 0.89729 -0.00533 0.13299  -0.01499 204 LEU A O   
1325 C CB  . LEU A 204 ? 0.51565 0.71699 0.75785 0.00297  0.07053  -0.02569 204 LEU A CB  
1326 C CG  . LEU A 204 ? 0.54429 0.73721 0.73540 0.00814  0.05981  -0.02447 204 LEU A CG  
1327 C CD1 . LEU A 204 ? 0.51537 0.71414 0.69699 0.01128  0.04449  -0.03077 204 LEU A CD1 
1328 C CD2 . LEU A 204 ? 0.54912 0.73319 0.72962 0.00351  0.04854  -0.02531 204 LEU A CD2 
1329 N N   . ARG A 205 ? 0.46135 0.67764 0.81703 -0.01777 0.08238  -0.03001 205 ARG A N   
1330 C CA  . ARG A 205 ? 0.45005 0.68570 0.87702 -0.02516 0.08804  -0.03350 205 ARG A CA  
1331 C C   . ARG A 205 ? 0.46535 0.71878 0.91421 -0.01514 0.09391  -0.03372 205 ARG A C   
1332 O O   . ARG A 205 ? 0.50475 0.75456 0.91332 -0.00519 0.08364  -0.03436 205 ARG A O   
1333 C CB  . ARG A 205 ? 0.45856 0.70213 0.91920 -0.03682 0.05477  -0.04424 205 ARG A CB  
1334 C CG  . ARG A 205 ? 0.49894 0.71783 0.92700 -0.04559 0.04606  -0.04598 205 ARG A CG  
1335 C CD  . ARG A 205 ? 0.53736 0.74368 0.97993 -0.05391 0.07598  -0.03989 205 ARG A CD  
1336 N NE  . ARG A 205 ? 0.52022 0.74587 1.04039 -0.06550 0.08599  -0.04288 205 ARG A NE  
1337 C CZ  . ARG A 205 ? 0.52907 0.76179 1.07903 -0.06325 0.12214  -0.03502 205 ARG A CZ  
1338 N NH1 . ARG A 205 ? 0.52156 0.73916 1.02223 -0.04960 0.14921  -0.02401 205 ARG A NH1 
1339 N NH2 . ARG A 205 ? 0.50875 0.76206 1.13960 -0.07525 0.13159  -0.03849 205 ARG A NH2 
1340 N N   . PRO A 206 ? 0.45729 0.72846 0.97159 -0.01756 0.11315  -0.03309 206 PRO A N   
1341 C CA  . PRO A 206 ? 0.44164 0.72878 0.98209 -0.00626 0.12103  -0.03330 206 PRO A CA  
1342 C C   . PRO A 206 ? 0.45187 0.75177 0.99422 -0.00103 0.08183  -0.04117 206 PRO A C   
1343 O O   . PRO A 206 ? 0.41642 0.72912 0.99250 -0.00868 0.04998  -0.04837 206 PRO A O   
1344 C CB  . PRO A 206 ? 0.43300 0.74248 1.06227 -0.01304 0.14333  -0.03276 206 PRO A CB  
1345 C CG  . PRO A 206 ? 0.43815 0.72882 1.05875 -0.02450 0.16680  -0.02753 206 PRO A CG  
1346 C CD  . PRO A 206 ? 0.47857 0.75269 1.04527 -0.03011 0.13567  -0.03097 206 PRO A CD  
1347 N N   . ILE A 207 ? 0.48454 0.77563 0.98487 0.01206  0.08386  -0.03992 207 ILE A N   
1348 C CA  . ILE A 207 ? 0.47308 0.76735 0.96172 0.01915  0.05175  -0.04568 207 ILE A CA  
1349 C C   . ILE A 207 ? 0.39734 0.70922 0.93552 0.03095  0.06098  -0.04563 207 ILE A C   
1350 O O   . ILE A 207 ? 0.42034 0.72517 0.95189 0.03886  0.09546  -0.04079 207 ILE A O   
1351 C CB  . ILE A 207 ? 0.48595 0.75472 0.89159 0.02401  0.04687  -0.04495 207 ILE A CB  
1352 C CG1 . ILE A 207 ? 0.50058 0.75439 0.86491 0.01464  0.04215  -0.04361 207 ILE A CG1 
1353 C CG2 . ILE A 207 ? 0.48936 0.75508 0.87925 0.03027  0.01690  -0.05032 207 ILE A CG2 
1354 C CD1 . ILE A 207 ? 0.48536 0.71975 0.78035 0.01824  0.03834  -0.04261 207 ILE A CD1 
1355 N N   . ASP A 208 ? 0.38626 0.71772 0.97155 0.03344  0.03027  -0.05079 208 ASP A N   
1356 C CA  . ASP A 208 ? 0.40139 0.74963 1.03412 0.04803  0.03513  -0.05024 208 ASP A CA  
1357 C C   . ASP A 208 ? 0.48781 0.81142 1.05494 0.06133  0.03199  -0.05011 208 ASP A C   
1358 O O   . ASP A 208 ? 0.52705 0.83023 1.03359 0.05888  0.00770  -0.05289 208 ASP A O   
1359 C CB  . ASP A 208 ? 0.38413 0.76154 1.09014 0.04782  -0.00201 -0.05531 208 ASP A CB  
1360 C CG  . ASP A 208 ? 0.41954 0.81795 1.18437 0.06553  0.00155  -0.05368 208 ASP A CG  
1361 O OD1 . ASP A 208 ? 0.43564 0.82824 1.19764 0.07567  0.04179  -0.04868 208 ASP A OD1 
1362 O OD2 . ASP A 208 ? 0.47273 0.89020 1.28343 0.07059  -0.03654 -0.05730 208 ASP A OD2 
1363 N N   . SER A 209 ? 0.48497 0.80737 1.06425 0.07505  0.05962  -0.04709 209 SER A N   
1364 C CA  . SER A 209 ? 0.53935 0.83383 1.05562 0.08647  0.06055  -0.04771 209 SER A CA  
1365 C C   . SER A 209 ? 0.53296 0.82804 1.05264 0.09517  0.02216  -0.05097 209 SER A C   
1366 O O   . SER A 209 ? 0.58103 0.84764 1.03454 0.09813  0.01162  -0.05270 209 SER A O   
1367 C CB  . SER A 209 ? 0.56539 0.85224 1.09126 0.09958  0.10166  -0.04436 209 SER A CB  
1368 N N   . ASN A 210 ? 0.46184 0.78692 1.05722 0.09922  0.00033  -0.05172 210 ASN A N   
1369 C CA  . ASN A 210 ? 0.51686 0.83832 1.11098 0.10908  -0.04060 -0.05395 210 ASN A CA  
1370 C C   . ASN A 210 ? 0.55900 0.85969 1.09480 0.09726  -0.07529 -0.05795 210 ASN A C   
1371 O O   . ASN A 210 ? 0.53342 0.82072 1.05155 0.10513  -0.10952 -0.05947 210 ASN A O   
1372 C CB  . ASN A 210 ? 0.45075 0.81219 1.14659 0.11698  -0.05913 -0.05379 210 ASN A CB  
1373 N N   . THR A 211 ? 0.57616 0.86986 1.07907 0.08031  -0.06574 -0.05902 211 THR A N   
1374 C CA  . THR A 211 ? 0.57565 0.84627 1.02205 0.07007  -0.09252 -0.06254 211 THR A CA  
1375 C C   . THR A 211 ? 0.63771 0.87184 1.00703 0.07629  -0.09691 -0.06245 211 THR A C   
1376 O O   . THR A 211 ? 0.65484 0.86575 0.98481 0.07552  -0.12485 -0.06485 211 THR A O   
1377 C CB  . THR A 211 ? 0.56646 0.83605 0.99477 0.05351  -0.07520 -0.06237 211 THR A CB  
1378 O OG1 . THR A 211 ? 0.57146 0.87112 1.07161 0.04671  -0.06588 -0.06206 211 THR A OG1 
1379 C CG2 . THR A 211 ? 0.60235 0.84857 0.98096 0.04380  -0.10025 -0.06612 211 THR A CG2 
1380 N N   . PHE A 212 ? 0.58790 0.81215 0.93194 0.08173  -0.06853 -0.06010 212 PHE A N   
1381 C CA  . PHE A 212 ? 0.57980 0.76978 0.85774 0.08612  -0.06916 -0.06065 212 PHE A CA  
1382 C C   . PHE A 212 ? 0.59395 0.78047 0.88409 0.10163  -0.05207 -0.05893 212 PHE A C   
1383 O O   . PHE A 212 ? 0.61913 0.79069 0.87555 0.10086  -0.02645 -0.05919 212 PHE A O   
1384 C CB  . PHE A 212 ? 0.56247 0.73724 0.78556 0.07312  -0.05256 -0.06131 212 PHE A CB  
1385 C CG  . PHE A 212 ? 0.60695 0.78216 0.81733 0.06002  -0.06480 -0.06235 212 PHE A CG  
1386 C CD1 . PHE A 212 ? 0.64292 0.79220 0.80973 0.05712  -0.08448 -0.06428 212 PHE A CD1 
1387 C CD2 . PHE A 212 ? 0.58508 0.78099 0.82297 0.05133  -0.05336 -0.06100 212 PHE A CD2 
1388 C CE1 . PHE A 212 ? 0.64030 0.78493 0.79203 0.04628  -0.09198 -0.06543 212 PHE A CE1 
1389 C CE2 . PHE A 212 ? 0.57265 0.76474 0.79676 0.04041  -0.06259 -0.06196 212 PHE A CE2 
1390 C CZ  . PHE A 212 ? 0.59855 0.76527 0.78000 0.03814  -0.08174 -0.06447 212 PHE A CZ  
1391 N N   . GLU A 213 ? 0.58795 0.78666 0.92644 0.11640  -0.06769 -0.05746 213 GLU A N   
1392 C CA  . GLU A 213 ? 0.60743 0.80267 0.96492 0.13448  -0.05104 -0.05514 213 GLU A CA  
1393 C C   . GLU A 213 ? 0.59973 0.75199 0.89091 0.14194  -0.05884 -0.05563 213 GLU A C   
1394 O O   . GLU A 213 ? 0.61970 0.76073 0.91411 0.15606  -0.08339 -0.05368 213 GLU A O   
1395 C CB  . GLU A 213 ? 0.54693 0.77556 0.99082 0.14882  -0.06568 -0.05257 213 GLU A CB  
1396 N N   . MET A 214 ? 0.64018 0.76616 0.87033 0.13226  -0.03794 -0.05816 214 MET A N   
1397 C CA  . MET A 214 ? 0.69740 0.77994 0.86241 0.13433  -0.04054 -0.05959 214 MET A CA  
1398 C C   . MET A 214 ? 0.75030 0.81444 0.87017 0.12339  -0.01194 -0.06357 214 MET A C   
1399 O O   . MET A 214 ? 0.72576 0.80794 0.85840 0.11595  0.00694  -0.06443 214 MET A O   
1400 C CB  . MET A 214 ? 0.69159 0.75625 0.81730 0.12576  -0.06742 -0.06006 214 MET A CB  
1401 C CG  . MET A 214 ? 0.67948 0.75357 0.78653 0.10488  -0.06338 -0.06258 214 MET A CG  
1402 S SD  . MET A 214 ? 0.75593 0.81369 0.83301 0.09792  -0.09356 -0.06257 214 MET A SD  
1403 C CE  . MET A 214 ? 0.69137 0.77909 0.83462 0.10898  -0.12224 -0.06087 214 MET A CE  
1404 N N   . ASN A 215 ? 0.88544 0.91021 0.94986 0.12199  -0.01015 -0.06613 215 ASN A N   
1405 C CA  . ASN A 215 ? 0.90422 0.90827 0.92233 0.10885  0.00995  -0.07165 215 ASN A CA  
1406 C C   . ASN A 215 ? 0.89719 0.90299 0.88669 0.08847  0.00142  -0.07390 215 ASN A C   
1407 O O   . ASN A 215 ? 0.89407 0.90433 0.88540 0.08553  -0.01732 -0.07145 215 ASN A O   
1408 C CB  . ASN A 215 ? 0.95138 0.91069 0.92816 0.11531  0.01806  -0.07437 215 ASN A CB  
1409 C CG  . ASN A 215 ? 1.00943 0.96200 1.00479 0.13293  0.03806  -0.07395 215 ASN A CG  
1410 O OD1 . ASN A 215 ? 1.03374 1.01665 1.07537 0.13971  0.04801  -0.07141 215 ASN A OD1 
1411 N ND2 . ASN A 215 ? 1.08959 0.99971 1.04983 0.14075  0.04725  -0.07622 215 ASN A ND2 
1412 N N   . GLY A 216 ? 0.81520 0.81485 0.77672 0.07505  0.01524  -0.07883 216 GLY A N   
1413 C CA  . GLY A 216 ? 0.77932 0.78600 0.72318 0.05678  0.00887  -0.08055 216 GLY A CA  
1414 C C   . GLY A 216 ? 0.80633 0.78944 0.72376 0.05125  -0.00172 -0.08078 216 GLY A C   
1415 O O   . GLY A 216 ? 0.81576 0.80868 0.73355 0.04244  -0.01019 -0.07911 216 GLY A O   
1416 N N   . LYS A 217 ? 0.79866 0.74545 0.68979 0.05722  0.00156  -0.08239 217 LYS A N   
1417 C CA  . LYS A 217 ? 0.81438 0.73029 0.67520 0.05398  -0.00519 -0.08123 217 LYS A CA  
1418 C C   . LYS A 217 ? 0.82691 0.74933 0.70092 0.06388  -0.02404 -0.07482 217 LYS A C   
1419 O O   . LYS A 217 ? 0.89309 0.80800 0.75025 0.05536  -0.02964 -0.07359 217 LYS A O   
1420 C CB  . LYS A 217 ? 0.82635 0.69736 0.65564 0.06166  0.00269  -0.08285 217 LYS A CB  
1421 N N   . ALA A 218 ? 0.78381 0.71955 0.68941 0.08173  -0.03398 -0.07113 218 ALA A N   
1422 C CA  . ALA A 218 ? 0.79508 0.73664 0.71454 0.09050  -0.05759 -0.06646 218 ALA A CA  
1423 C C   . ALA A 218 ? 0.81958 0.79246 0.75835 0.07797  -0.06259 -0.06694 218 ALA A C   
1424 O O   . ALA A 218 ? 0.79581 0.75824 0.71990 0.07635  -0.07816 -0.06540 218 ALA A O   
1425 C CB  . ALA A 218 ? 0.77528 0.73311 0.73884 0.11104  -0.06840 -0.06309 218 ALA A CB  
1426 N N   . LEU A 219 ? 0.78920 0.79473 0.75493 0.06992  -0.04877 -0.06890 219 LEU A N   
1427 C CA  . LEU A 219 ? 0.67580 0.70813 0.65829 0.05903  -0.05099 -0.06858 219 LEU A CA  
1428 C C   . LEU A 219 ? 0.68044 0.69516 0.62588 0.04554  -0.04830 -0.06966 219 LEU A C   
1429 O O   . LEU A 219 ? 0.74260 0.76181 0.68842 0.04084  -0.05589 -0.06846 219 LEU A O   
1430 C CB  . LEU A 219 ? 0.64125 0.70321 0.64971 0.05469  -0.03457 -0.06933 219 LEU A CB  
1431 C CG  . LEU A 219 ? 0.60063 0.68826 0.62630 0.04522  -0.03457 -0.06783 219 LEU A CG  
1432 C CD1 . LEU A 219 ? 0.62132 0.72510 0.68385 0.05083  -0.04927 -0.06567 219 LEU A CD1 
1433 C CD2 . LEU A 219 ? 0.62458 0.72993 0.65910 0.04141  -0.01710 -0.06775 219 LEU A CD2 
1434 N N   . LEU A 220 ? 0.69068 0.68384 0.60593 0.03871  -0.03577 -0.07231 220 LEU A N   
1435 C CA  . LEU A 220 ? 0.69350 0.67062 0.58153 0.02576  -0.02964 -0.07309 220 LEU A CA  
1436 C C   . LEU A 220 ? 0.77513 0.71708 0.63217 0.03086  -0.03926 -0.07026 220 LEU A C   
1437 O O   . LEU A 220 ? 0.81425 0.75018 0.65912 0.02391  -0.03730 -0.06925 220 LEU A O   
1438 C CB  . LEU A 220 ? 0.70882 0.66935 0.57683 0.01589  -0.01502 -0.07745 220 LEU A CB  
1439 C CG  . LEU A 220 ? 0.71834 0.70401 0.60338 0.00941  -0.00767 -0.08160 220 LEU A CG  
1440 C CD1 . LEU A 220 ? 0.75732 0.71958 0.61884 -0.00148 0.00251  -0.08780 220 LEU A CD1 
1441 C CD2 . LEU A 220 ? 0.67046 0.69061 0.57776 0.00075  -0.00794 -0.08039 220 LEU A CD2 
1442 N N   . LEU A 221 ? 0.76383 0.67847 0.60444 0.04461  -0.04959 -0.06854 221 LEU A N   
1443 C CA  . LEU A 221 ? 0.81320 0.68458 0.61211 0.05141  -0.06117 -0.06538 221 LEU A CA  
1444 C C   . LEU A 221 ? 0.79936 0.68092 0.60660 0.05353  -0.07956 -0.06431 221 LEU A C   
1445 O O   . LEU A 221 ? 0.81304 0.65705 0.57718 0.05330  -0.08406 -0.06295 221 LEU A O   
1446 C CB  . LEU A 221 ? 0.83830 0.68105 0.62185 0.06918  -0.07320 -0.06270 221 LEU A CB  
1447 C CG  . LEU A 221 ? 0.87164 0.69592 0.64219 0.06871  -0.05503 -0.06425 221 LEU A CG  
1448 C CD1 . LEU A 221 ? 0.90371 0.70044 0.66313 0.09013  -0.06757 -0.06033 221 LEU A CD1 
1449 C CD2 . LEU A 221 ? 0.93312 0.72057 0.66007 0.05373  -0.03458 -0.06549 221 LEU A CD2 
1450 N N   . LEU A 222 ? 0.75577 0.68223 0.61397 0.05506  -0.08855 -0.06523 222 LEU A N   
1451 C CA  . LEU A 222 ? 0.73471 0.66981 0.60411 0.05544  -0.10725 -0.06549 222 LEU A CA  
1452 C C   . LEU A 222 ? 0.76931 0.69593 0.61617 0.04242  -0.09444 -0.06628 222 LEU A C   
1453 O O   . LEU A 222 ? 0.76601 0.71058 0.62290 0.03207  -0.07254 -0.06660 222 LEU A O   
1454 C CB  . LEU A 222 ? 0.69050 0.67611 0.62447 0.05696  -0.11290 -0.06627 222 LEU A CB  
1455 C CG  . LEU A 222 ? 0.68740 0.68928 0.65944 0.07117  -0.12314 -0.06515 222 LEU A CG  
1456 C CD1 . LEU A 222 ? 0.66470 0.71497 0.70197 0.06959  -0.12118 -0.06565 222 LEU A CD1 
1457 C CD2 . LEU A 222 ? 0.72061 0.69507 0.67672 0.08472  -0.15376 -0.06391 222 LEU A CD2 
1458 N N   . THR A 223 ? 0.78635 0.68278 0.60115 0.04393  -0.10904 -0.06670 223 THR A N   
1459 C CA  . THR A 223 ? 0.79293 0.67623 0.58510 0.03402  -0.09584 -0.06737 223 THR A CA  
1460 C C   . THR A 223 ? 0.84206 0.76475 0.67854 0.02864  -0.09987 -0.06911 223 THR A C   
1461 O O   . THR A 223 ? 0.84179 0.79470 0.72108 0.03229  -0.11632 -0.07020 223 THR A O   
1462 C CB  . THR A 223 ? 0.81411 0.63608 0.53996 0.03851  -0.10705 -0.06757 223 THR A CB  
1463 O OG1 . THR A 223 ? 0.83879 0.65849 0.57022 0.04615  -0.14228 -0.07003 223 THR A OG1 
1464 C CG2 . THR A 223 ? 0.85657 0.63308 0.53374 0.04461  -0.10054 -0.06456 223 THR A CG2 
1465 N N   . LYS A 224 ? 0.81245 0.73292 0.64025 0.02024  -0.08219 -0.06889 224 LYS A N   
1466 C CA  . LYS A 224 ? 0.76452 0.71582 0.62848 0.01530  -0.08224 -0.06967 224 LYS A CA  
1467 C C   . LYS A 224 ? 0.76256 0.70287 0.62676 0.01750  -0.11007 -0.07369 224 LYS A C   
1468 O O   . LYS A 224 ? 0.75679 0.72980 0.66604 0.01430  -0.11570 -0.07479 224 LYS A O   
1469 C CB  . LYS A 224 ? 0.74872 0.69131 0.59771 0.00881  -0.05876 -0.06809 224 LYS A CB  
1470 N N   . GLU A 225 ? 0.80776 0.69980 0.62106 0.02246  -0.12848 -0.07607 225 GLU A N   
1471 C CA  . GLU A 225 ? 0.83643 0.71730 0.65039 0.02419  -0.16233 -0.08120 225 GLU A CA  
1472 C C   . GLU A 225 ? 0.84587 0.76646 0.71816 0.03023  -0.18425 -0.08137 225 GLU A C   
1473 O O   . GLU A 225 ? 0.85090 0.79100 0.76204 0.02745  -0.20604 -0.08548 225 GLU A O   
1474 C CB  . GLU A 225 ? 0.84451 0.65705 0.57981 0.02969  -0.17943 -0.08345 225 GLU A CB  
1475 N N   . ASP A 226 ? 0.79272 0.72459 0.67464 0.03814  -0.17723 -0.07726 226 ASP A N   
1476 C CA  . ASP A 226 ? 0.76116 0.73191 0.70312 0.04565  -0.19100 -0.07657 226 ASP A CA  
1477 C C   . ASP A 226 ? 0.72065 0.74494 0.72890 0.03834  -0.17322 -0.07602 226 ASP A C   
1478 O O   . ASP A 226 ? 0.67593 0.73179 0.74174 0.03942  -0.18684 -0.07753 226 ASP A O   
1479 C CB  . ASP A 226 ? 0.77364 0.73537 0.70185 0.05645  -0.18333 -0.07243 226 ASP A CB  
1480 C CG  . ASP A 226 ? 0.81299 0.71389 0.66692 0.06394  -0.19497 -0.07136 226 ASP A CG  
1481 O OD1 . ASP A 226 ? 0.88556 0.75141 0.70007 0.06319  -0.21528 -0.07421 226 ASP A OD1 
1482 O OD2 . ASP A 226 ? 0.83808 0.72068 0.66760 0.07012  -0.18229 -0.06783 226 ASP A OD2 
1483 N N   . PHE A 227 ? 0.73947 0.77318 0.74132 0.03121  -0.14276 -0.07349 227 PHE A N   
1484 C CA  . PHE A 227 ? 0.67439 0.74935 0.72592 0.02530  -0.12538 -0.07191 227 PHE A CA  
1485 C C   . PHE A 227 ? 0.68585 0.76749 0.76057 0.01753  -0.13601 -0.07506 227 PHE A C   
1486 O O   . PHE A 227 ? 0.66548 0.77971 0.79570 0.01539  -0.13460 -0.07492 227 PHE A O   
1487 C CB  . PHE A 227 ? 0.68674 0.76485 0.71950 0.02007  -0.09705 -0.06857 227 PHE A CB  
1488 C CG  . PHE A 227 ? 0.69612 0.77777 0.72191 0.02439  -0.08423 -0.06664 227 PHE A CG  
1489 C CD1 . PHE A 227 ? 0.70481 0.75485 0.68940 0.02777  -0.08691 -0.06726 227 PHE A CD1 
1490 C CD2 . PHE A 227 ? 0.65032 0.76072 0.70516 0.02460  -0.06826 -0.06450 227 PHE A CD2 
1491 C CE1 . PHE A 227 ? 0.69476 0.74439 0.67217 0.02982  -0.07472 -0.06662 227 PHE A CE1 
1492 C CE2 . PHE A 227 ? 0.61497 0.72293 0.65778 0.02737  -0.05768 -0.06434 227 PHE A CE2 
1493 C CZ  . PHE A 227 ? 0.67067 0.74944 0.67708 0.02925  -0.06132 -0.06583 227 PHE A CZ  
1494 N N   . ARG A 228 ? 0.72971 0.77668 0.76088 0.01269  -0.14410 -0.07820 228 ARG A N   
1495 C CA  . ARG A 228 ? 0.66252 0.70787 0.70893 0.00403  -0.15550 -0.08275 228 ARG A CA  
1496 C C   . ARG A 228 ? 0.64971 0.70583 0.73543 0.00506  -0.18862 -0.08792 228 ARG A C   
1497 O O   . ARG A 228 ? 0.64921 0.72510 0.78053 -0.00355 -0.19438 -0.09121 228 ARG A O   
1498 C CB  . ARG A 228 ? 0.66294 0.65929 0.64521 0.00012  -0.15745 -0.08602 228 ARG A CB  
1499 C CG  . ARG A 228 ? 0.69840 0.68889 0.65574 -0.00184 -0.12432 -0.08109 228 ARG A CG  
1500 C CD  . ARG A 228 ? 0.71986 0.66085 0.62056 -0.00518 -0.12264 -0.08459 228 ARG A CD  
1501 N NE  . ARG A 228 ? 0.78077 0.72026 0.66757 -0.00539 -0.08989 -0.07914 228 ARG A NE  
1502 C CZ  . ARG A 228 ? 0.85811 0.78163 0.71338 -0.00150 -0.07348 -0.07575 228 ARG A CZ  
1503 N NH1 . ARG A 228 ? 0.87056 0.77081 0.69494 0.00305  -0.08431 -0.07686 228 ARG A NH1 
1504 N NH2 . ARG A 228 ? 0.89804 0.82854 0.75536 -0.00198 -0.04527 -0.07079 228 ARG A NH2 
1505 N N   . TYR A 229 ? 0.63366 0.67675 0.70532 0.01554  -0.21111 -0.08849 229 TYR A N   
1506 C CA  . TYR A 229 ? 0.63513 0.69228 0.75095 0.01878  -0.24688 -0.09284 229 TYR A CA  
1507 C C   . TYR A 229 ? 0.63753 0.74967 0.83701 0.02251  -0.23577 -0.08926 229 TYR A C   
1508 O O   . TYR A 229 ? 0.65110 0.79289 0.91674 0.01780  -0.25097 -0.09279 229 TYR A O   
1509 C CB  . TYR A 229 ? 0.67708 0.69642 0.74426 0.03171  -0.27653 -0.09339 229 TYR A CB  
1510 N N   . ARG A 230 ? 0.61883 0.74290 0.81699 0.03022  -0.20792 -0.08279 230 ARG A N   
1511 C CA  . ARG A 230 ? 0.59505 0.76297 0.86332 0.03529  -0.19238 -0.07927 230 ARG A CA  
1512 C C   . ARG A 230 ? 0.60768 0.80411 0.92087 0.02312  -0.16859 -0.07861 230 ARG A C   
1513 O O   . ARG A 230 ? 0.62888 0.85823 1.01435 0.02123  -0.17007 -0.07941 230 ARG A O   
1514 C CB  . ARG A 230 ? 0.62604 0.78961 0.86901 0.04551  -0.16839 -0.07387 230 ARG A CB  
1515 C CG  . ARG A 230 ? 0.66623 0.80382 0.87770 0.05965  -0.18980 -0.07341 230 ARG A CG  
1516 C CD  . ARG A 230 ? 0.68849 0.81426 0.86758 0.06683  -0.16490 -0.06938 230 ARG A CD  
1517 N NE  . ARG A 230 ? 0.74669 0.84352 0.89543 0.08113  -0.18306 -0.06811 230 ARG A NE  
1518 C CZ  . ARG A 230 ? 0.72296 0.83234 0.90869 0.09656  -0.18893 -0.06571 230 ARG A CZ  
1519 N NH1 . ARG A 230 ? 0.64967 0.80071 0.90611 0.09938  -0.17483 -0.06460 230 ARG A NH1 
1520 N NH2 . ARG A 230 ? 0.74915 0.82530 0.89894 0.11066  -0.20673 -0.06365 230 ARG A NH2 
1521 N N   . SER A 231 ? 0.58229 0.76552 0.85572 0.01525  -0.14569 -0.07659 231 SER A N   
1522 C CA  . SER A 231 ? 0.53256 0.73333 0.83524 0.00498  -0.12233 -0.07461 231 SER A CA  
1523 C C   . SER A 231 ? 0.56258 0.73734 0.82895 -0.00596 -0.12868 -0.07805 231 SER A C   
1524 O O   . SER A 231 ? 0.57316 0.72967 0.79125 -0.00659 -0.11223 -0.07491 231 SER A O   
1525 C CB  . SER A 231 ? 0.55899 0.76762 0.84889 0.00853  -0.08683 -0.06747 231 SER A CB  
1526 O OG  . SER A 231 ? 0.54219 0.75996 0.85050 0.00027  -0.06530 -0.06433 231 SER A OG  
1527 N N   . PRO A 232 ? 0.53186 0.70334 0.82176 -0.01478 -0.15234 -0.08490 232 PRO A N   
1528 C CA  . PRO A 232 ? 0.55610 0.69633 0.80712 -0.02529 -0.15576 -0.08900 232 PRO A CA  
1529 C C   . PRO A 232 ? 0.55149 0.69826 0.80915 -0.03163 -0.12225 -0.08357 232 PRO A C   
1530 O O   . PRO A 232 ? 0.64711 0.76544 0.86106 -0.03568 -0.11532 -0.08391 232 PRO A O   
1531 C CB  . PRO A 232 ? 0.60594 0.74497 0.89116 -0.03462 -0.19064 -0.09877 232 PRO A CB  
1532 C CG  . PRO A 232 ? 0.55685 0.71844 0.88000 -0.02447 -0.21402 -0.09945 232 PRO A CG  
1533 C CD  . PRO A 232 ? 0.52408 0.71670 0.87424 -0.01501 -0.18075 -0.09016 232 PRO A CD  
1534 N N   . HIS A 233 ? 0.53458 0.71387 0.84202 -0.03100 -0.09931 -0.07778 233 HIS A N   
1535 C CA  . HIS A 233 ? 0.54386 0.72384 0.85164 -0.03519 -0.06783 -0.07123 233 HIS A CA  
1536 C C   . HIS A 233 ? 0.56341 0.73723 0.82402 -0.02534 -0.04678 -0.06308 233 HIS A C   
1537 O O   . HIS A 233 ? 0.54908 0.70892 0.78286 -0.02640 -0.03105 -0.05859 233 HIS A O   
1538 C CB  . HIS A 233 ? 0.49293 0.70230 0.86654 -0.03857 -0.04890 -0.06783 233 HIS A CB  
1539 C CG  . HIS A 233 ? 0.46796 0.68735 0.90015 -0.05168 -0.06647 -0.07582 233 HIS A CG  
1540 N ND1 . HIS A 233 ? 0.48554 0.69414 0.93276 -0.06584 -0.05804 -0.07767 233 HIS A ND1 
1541 C CD2 . HIS A 233 ? 0.49240 0.73220 0.97572 -0.05309 -0.09358 -0.08270 233 HIS A CD2 
1542 C CE1 . HIS A 233 ? 0.50897 0.73170 1.01577 -0.07774 -0.07973 -0.08649 233 HIS A CE1 
1543 N NE2 . HIS A 233 ? 0.51865 0.76257 1.05049 -0.06961 -0.10304 -0.08947 233 HIS A NE2 
1544 N N   . SER A 234 ? 0.54208 0.72560 0.79392 -0.01563 -0.04742 -0.06131 234 SER A N   
1545 C CA  . SER A 234 ? 0.52047 0.70243 0.73678 -0.00830 -0.02913 -0.05466 234 SER A CA  
1546 C C   . SER A 234 ? 0.53793 0.71014 0.71864 -0.00209 -0.04051 -0.05686 234 SER A C   
1547 O O   . SER A 234 ? 0.53577 0.70785 0.69074 0.00206  -0.02831 -0.05281 234 SER A O   
1548 C CB  . SER A 234 ? 0.50076 0.70202 0.74164 -0.00387 -0.00617 -0.04857 234 SER A CB  
1549 O OG  . SER A 234 ? 0.47124 0.67831 0.74703 -0.01003 0.00821  -0.04594 234 SER A OG  
1550 N N   . GLY A 235 ? 0.60607 0.76737 0.78281 -0.00160 -0.06428 -0.06309 235 GLY A N   
1551 C CA  . GLY A 235 ? 0.60477 0.75124 0.74529 0.00460  -0.07203 -0.06430 235 GLY A CA  
1552 C C   . GLY A 235 ? 0.61418 0.74058 0.70762 0.00333  -0.06257 -0.06252 235 GLY A C   
1553 O O   . GLY A 235 ? 0.60430 0.72721 0.67594 0.00676  -0.05639 -0.06119 235 GLY A O   
1554 N N   . ASP A 236 ? 0.60670 0.71901 0.68695 -0.00183 -0.05991 -0.06270 236 ASP A N   
1555 C CA  . ASP A 236 ? 0.63158 0.72897 0.67731 -0.00173 -0.04657 -0.05995 236 ASP A CA  
1556 C C   . ASP A 236 ? 0.58279 0.70475 0.63987 0.00062  -0.02805 -0.05332 236 ASP A C   
1557 O O   . ASP A 236 ? 0.62282 0.74359 0.66243 0.00192  -0.02110 -0.05175 236 ASP A O   
1558 C CB  . ASP A 236 ? 0.68360 0.75828 0.71440 -0.00596 -0.04498 -0.06130 236 ASP A CB  
1559 C CG  . ASP A 236 ? 0.69051 0.77873 0.75528 -0.01033 -0.04292 -0.06048 236 ASP A CG  
1560 O OD1 . ASP A 236 ? 0.63501 0.75136 0.73522 -0.00946 -0.03884 -0.05762 236 ASP A OD1 
1561 O OD2 . ASP A 236 ? 0.72767 0.79395 0.78133 -0.01496 -0.04317 -0.06291 236 ASP A OD2 
1562 N N   . VAL A 237 ? 0.55615 0.69801 0.64123 0.00080  -0.02031 -0.04949 237 VAL A N   
1563 C CA  . VAL A 237 ? 0.56450 0.72399 0.65204 0.00443  -0.00655 -0.04326 237 VAL A CA  
1564 C C   . VAL A 237 ? 0.57977 0.74653 0.66321 0.00697  -0.00896 -0.04535 237 VAL A C   
1565 O O   . VAL A 237 ? 0.57523 0.74497 0.64316 0.00765  -0.00554 -0.04422 237 VAL A O   
1566 C CB  . VAL A 237 ? 0.53487 0.70466 0.64468 0.00501  0.00459  -0.03809 237 VAL A CB  
1567 C CG1 . VAL A 237 ? 0.49359 0.67393 0.59464 0.01040  0.01596  -0.03155 237 VAL A CG1 
1568 C CG2 . VAL A 237 ? 0.55695 0.71454 0.66773 0.00202  0.00843  -0.03623 237 VAL A CG2 
1569 N N   . LEU A 238 ? 0.54497 0.71416 0.64499 0.00829  -0.01539 -0.04886 238 LEU A N   
1570 C CA  . LEU A 238 ? 0.52313 0.69493 0.61875 0.01222  -0.01499 -0.05078 238 LEU A CA  
1571 C C   . LEU A 238 ? 0.55854 0.71526 0.62418 0.01099  -0.02111 -0.05400 238 LEU A C   
1572 O O   . LEU A 238 ? 0.57211 0.72951 0.62396 0.01096  -0.01595 -0.05454 238 LEU A O   
1573 C CB  . LEU A 238 ? 0.48605 0.66250 0.61036 0.01596  -0.02150 -0.05351 238 LEU A CB  
1574 C CG  . LEU A 238 ? 0.47852 0.67132 0.64193 0.01628  -0.01074 -0.05062 238 LEU A CG  
1575 C CD1 . LEU A 238 ? 0.48165 0.68297 0.68447 0.01945  -0.02133 -0.05403 238 LEU A CD1 
1576 C CD2 . LEU A 238 ? 0.49597 0.69289 0.65149 0.02013  0.01010  -0.04637 238 LEU A CD2 
1577 N N   . TYR A 239 ? 0.57454 0.71308 0.62660 0.00923  -0.03122 -0.05657 239 TYR A N   
1578 C CA  . TYR A 239 ? 0.60477 0.72282 0.62573 0.00767  -0.03223 -0.05879 239 TYR A CA  
1579 C C   . TYR A 239 ? 0.66214 0.78824 0.67650 0.00317  -0.01972 -0.05643 239 TYR A C   
1580 O O   . TYR A 239 ? 0.67811 0.80309 0.68289 0.00078  -0.01629 -0.05817 239 TYR A O   
1581 C CB  . TYR A 239 ? 0.67779 0.76746 0.67651 0.00709  -0.04177 -0.06096 239 TYR A CB  
1582 C CG  . TYR A 239 ? 0.71448 0.77534 0.67610 0.00540  -0.03718 -0.06214 239 TYR A CG  
1583 C CD1 . TYR A 239 ? 0.73972 0.77843 0.68022 0.00921  -0.04493 -0.06436 239 TYR A CD1 
1584 C CD2 . TYR A 239 ? 0.69419 0.74831 0.64385 0.00075  -0.02253 -0.06032 239 TYR A CD2 
1585 C CE1 . TYR A 239 ? 0.74226 0.74905 0.64604 0.00706  -0.03699 -0.06478 239 TYR A CE1 
1586 C CE2 . TYR A 239 ? 0.69859 0.72509 0.61842 -0.00180 -0.01321 -0.06106 239 TYR A CE2 
1587 C CZ  . TYR A 239 ? 0.73161 0.73260 0.62620 0.00068  -0.01987 -0.06332 239 TYR A CZ  
1588 O OH  . TYR A 239 ? 0.77226 0.73999 0.63385 -0.00237 -0.00726 -0.06345 239 TYR A OH  
1589 N N   . GLU A 240 ? 0.60500 0.73931 0.62726 0.00201  -0.01373 -0.05261 240 GLU A N   
1590 C CA  . GLU A 240 ? 0.61403 0.76033 0.63853 -0.00042 -0.00460 -0.04953 240 GLU A CA  
1591 C C   . GLU A 240 ? 0.59439 0.76074 0.62664 -0.00021 -0.00488 -0.04869 240 GLU A C   
1592 O O   . GLU A 240 ? 0.58141 0.75431 0.61222 -0.00439 -0.00406 -0.04984 240 GLU A O   
1593 C CB  . GLU A 240 ? 0.59034 0.74071 0.62381 0.00162  0.00184  -0.04439 240 GLU A CB  
1594 C CG  . GLU A 240 ? 0.63273 0.75574 0.65064 0.00118  0.00255  -0.04630 240 GLU A CG  
1595 C CD  . GLU A 240 ? 0.71394 0.81259 0.70786 -0.00159 0.00789  -0.04920 240 GLU A CD  
1596 O OE1 . GLU A 240 ? 0.66537 0.77431 0.66506 -0.00443 0.01502  -0.04861 240 GLU A OE1 
1597 O OE2 . GLU A 240 ? 0.82382 0.88975 0.79104 -0.00151 0.00455  -0.05245 240 GLU A OE2 
1598 N N   . LEU A 241 ? 0.57490 0.74846 0.61459 0.00401  -0.00543 -0.04714 241 LEU A N   
1599 C CA  . LEU A 241 ? 0.55723 0.73942 0.59238 0.00534  -0.00427 -0.04689 241 LEU A CA  
1600 C C   . LEU A 241 ? 0.57864 0.75164 0.59901 0.00133  -0.00754 -0.05348 241 LEU A C   
1601 O O   . LEU A 241 ? 0.56894 0.74619 0.58049 -0.00256 -0.00986 -0.05529 241 LEU A O   
1602 C CB  . LEU A 241 ? 0.52591 0.70908 0.56929 0.01084  0.00135  -0.04466 241 LEU A CB  
1603 C CG  . LEU A 241 ? 0.53295 0.71427 0.56137 0.01367  0.00633  -0.04492 241 LEU A CG  
1604 C CD1 . LEU A 241 ? 0.58309 0.76999 0.59640 0.01354  0.00338  -0.04121 241 LEU A CD1 
1605 C CD2 . LEU A 241 ? 0.52957 0.70954 0.57034 0.01937  0.01844  -0.04179 241 LEU A CD2 
1606 N N   . LEU A 242 ? 0.58054 0.73855 0.59713 0.00222  -0.00946 -0.05732 242 LEU A N   
1607 C CA  . LEU A 242 ? 0.59242 0.73534 0.59187 -0.00080 -0.01053 -0.06309 242 LEU A CA  
1608 C C   . LEU A 242 ? 0.59885 0.73887 0.59132 -0.01022 -0.01002 -0.06520 242 LEU A C   
1609 O O   . LEU A 242 ? 0.63116 0.76676 0.61368 -0.01654 -0.01020 -0.06993 242 LEU A O   
1610 C CB  . LEU A 242 ? 0.58974 0.71468 0.58596 0.00458  -0.01432 -0.06497 242 LEU A CB  
1611 C CG  . LEU A 242 ? 0.60447 0.70715 0.57988 0.00399  -0.01381 -0.06991 242 LEU A CG  
1612 C CD1 . LEU A 242 ? 0.61104 0.71564 0.58096 0.00473  -0.00817 -0.07276 242 LEU A CD1 
1613 C CD2 . LEU A 242 ? 0.65776 0.74310 0.63156 0.01311  -0.02089 -0.06979 242 LEU A CD2 
1614 N N   . GLN A 243 ? 0.54919 0.69009 0.54822 -0.01194 -0.00768 -0.06221 243 GLN A N   
1615 C CA  . GLN A 243 ? 0.58501 0.72510 0.58596 -0.02068 -0.00218 -0.06339 243 GLN A CA  
1616 C C   . GLN A 243 ? 0.56304 0.72930 0.58130 -0.02563 -0.00557 -0.06324 243 GLN A C   
1617 O O   . GLN A 243 ? 0.58060 0.74822 0.60275 -0.03549 -0.00547 -0.06771 243 GLN A O   
1618 C CB  . GLN A 243 ? 0.61399 0.74708 0.61753 -0.01931 0.00518  -0.05949 243 GLN A CB  
1619 C CG  . GLN A 243 ? 0.69887 0.80650 0.68282 -0.01307 0.00201  -0.05943 243 GLN A CG  
1620 C CD  . GLN A 243 ? 0.75868 0.83816 0.71743 -0.01262 -0.00153 -0.06352 243 GLN A CD  
1621 O OE1 . GLN A 243 ? 0.75049 0.81609 0.69774 -0.01905 0.00574  -0.06607 243 GLN A OE1 
1622 N NE2 . GLN A 243 ? 0.78330 0.85468 0.73694 -0.00483 -0.01283 -0.06393 243 GLN A NE2 
1623 N N   . HIS A 244 ? 0.56453 0.74971 0.59285 -0.01916 -0.00982 -0.05815 244 HIS A N   
1624 C CA  . HIS A 244 ? 0.51461 0.72157 0.55401 -0.02138 -0.01794 -0.05717 244 HIS A CA  
1625 C C   . HIS A 244 ? 0.63200 0.83128 0.65140 -0.02609 -0.02600 -0.06412 244 HIS A C   
1626 O O   . HIS A 244 ? 0.68289 0.89222 0.70790 -0.03424 -0.03562 -0.06806 244 HIS A O   
1627 C CB  . HIS A 244 ? 0.53598 0.75608 0.58117 -0.01111 -0.01964 -0.04883 244 HIS A CB  
1628 N N   . ILE A 245 ? 0.55155 0.73193 0.54919 -0.02123 -0.02234 -0.06629 245 ILE A N   
1629 C CA  . ILE A 245 ? 0.60334 0.76864 0.57591 -0.02440 -0.02601 -0.07336 245 ILE A CA  
1630 C C   . ILE A 245 ? 0.66690 0.81980 0.63588 -0.03695 -0.02676 -0.08170 245 ILE A C   
1631 O O   . ILE A 245 ? 0.71138 0.85857 0.66736 -0.04566 -0.03465 -0.08892 245 ILE A O   
1632 C CB  . ILE A 245 ? 0.62809 0.77614 0.58504 -0.01437 -0.01714 -0.07291 245 ILE A CB  
1633 C CG1 . ILE A 245 ? 0.55739 0.71622 0.52146 -0.00426 -0.01279 -0.06463 245 ILE A CG1 
1634 C CG2 . ILE A 245 ? 0.70122 0.82725 0.62719 -0.01585 -0.01660 -0.08022 245 ILE A CG2 
1635 N N   . LEU A 246 ? 0.70556 0.84962 0.68216 -0.03848 -0.01844 -0.08099 246 LEU A N   
1636 C CA  . LEU A 246 ? 0.67675 0.80226 0.64734 -0.05045 -0.01419 -0.08773 246 LEU A CA  
1637 C C   . LEU A 246 ? 0.72250 0.86933 0.71895 -0.06425 -0.01909 -0.09030 246 LEU A C   
1638 O O   . LEU A 246 ? 0.79208 0.92658 0.78698 -0.07797 -0.01744 -0.09782 246 LEU A O   
1639 C CB  . LEU A 246 ? 0.60401 0.71054 0.57056 -0.04678 -0.00351 -0.08437 246 LEU A CB  
1640 C CG  . LEU A 246 ? 0.63774 0.72540 0.58608 -0.03333 -0.00339 -0.08232 246 LEU A CG  
1641 C CD1 . LEU A 246 ? 0.68184 0.74466 0.61800 -0.03015 0.00192  -0.07972 246 LEU A CD1 
1642 C CD2 . LEU A 246 ? 0.64863 0.71661 0.57580 -0.03211 -0.00361 -0.08818 246 LEU A CD2 
1643 N N   . GLY A 247 ? 0.67621 0.85377 0.69900 -0.06060 -0.02468 -0.08413 247 GLY A N   
1644 C CA  . GLY A 247 ? 0.66953 0.87439 0.72872 -0.07144 -0.03123 -0.08536 247 GLY A CA  
1645 C C   . GLY A 247 ? 0.74488 0.97946 0.81902 -0.06357 -0.04678 -0.07965 247 GLY A C   
1646 O O   . GLY A 247 ? 0.79872 1.05645 0.90640 -0.05933 -0.04312 -0.07240 247 GLY A O   
1647 N N   . LEU A 251 ? 0.68774 1.02691 0.88884 -0.04424 -0.06422 -0.05465 251 LEU A N   
1648 C CA  . LEU A 251 ? 0.68329 1.06175 0.94345 -0.04232 -0.07123 -0.04935 251 LEU A CA  
1649 C C   . LEU A 251 ? 0.70090 1.10114 0.98709 -0.05738 -0.09654 -0.05844 251 LEU A C   
1650 O O   . LEU A 251 ? 0.69857 1.11692 1.03460 -0.07084 -0.08861 -0.06272 251 LEU A O   
1651 C CB  . LEU A 251 ? 0.68199 1.07120 0.93850 -0.02244 -0.08120 -0.03746 251 LEU A CB  
1652 N N   . GLY A 252 ? 0.59084 0.98588 0.84273 -0.05588 -0.12492 -0.06168 252 GLY A N   
1653 C CA  . GLY A 252 ? 0.58538 0.99445 0.85256 -0.07185 -0.15404 -0.07261 252 GLY A CA  
1654 C C   . GLY A 252 ? 0.57710 0.96692 0.84113 -0.09355 -0.14077 -0.08566 252 GLY A C   
1655 O O   . GLY A 252 ? 0.58467 0.99669 0.89618 -0.11134 -0.15103 -0.09371 252 GLY A O   
1656 N N   . LYS A 253 ? 0.60598 0.95585 0.81922 -0.09197 -0.11884 -0.08738 253 LYS A N   
1657 C CA  . LYS A 253 ? 0.65006 0.97401 0.85343 -0.10972 -0.10319 -0.09811 253 LYS A CA  
1658 C C   . LYS A 253 ? 0.64448 0.98416 0.90332 -0.11800 -0.07890 -0.09583 253 LYS A C   
1659 O O   . LYS A 253 ? 0.65752 0.99751 0.94189 -0.13823 -0.07605 -0.10512 253 LYS A O   
1660 C CB  . LYS A 253 ? 0.65939 0.94008 0.80200 -0.10124 -0.08550 -0.09767 253 LYS A CB  
1661 N N   . LYS A 254 ? 0.58691 0.93496 0.86124 -0.10336 -0.05999 -0.08418 254 LYS A N   
1662 C CA  . LYS A 254 ? 0.48689 0.84320 0.80773 -0.10872 -0.03143 -0.08091 254 LYS A CA  
1663 C C   . LYS A 254 ? 0.50765 0.90824 0.90345 -0.12259 -0.04365 -0.08458 254 LYS A C   
1664 O O   . LYS A 254 ? 0.54069 0.94061 0.97210 -0.13874 -0.02258 -0.08891 254 LYS A O   
1665 C CB  . LYS A 254 ? 0.46024 0.81887 0.78391 -0.08909 -0.01392 -0.06817 254 LYS A CB  
1666 N N   . LEU A 255 ? 0.49122 0.92734 0.91030 -0.11632 -0.07682 -0.08265 255 LEU A N   
1667 C CA  . LEU A 255 ? 0.51492 0.99885 1.01199 -0.12926 -0.09721 -0.08684 255 LEU A CA  
1668 C C   . LEU A 255 ? 0.58412 1.05561 1.06947 -0.15411 -0.11607 -0.10326 255 LEU A C   
1669 O O   . LEU A 255 ? 0.59680 1.09176 1.14644 -0.17469 -0.11416 -0.11040 255 LEU A O   
1670 C CB  . LEU A 255 ? 0.51371 1.03264 1.02789 -0.11194 -0.13181 -0.07903 255 LEU A CB  
1671 N N   . LEU A 256 ? 0.69080 1.12464 1.09821 -0.15245 -0.13108 -0.10914 256 LEU A N   
1672 C CA  A LEU A 256 ? 0.71916 1.13499 1.10876 -0.17532 -0.14901 -0.12549 256 LEU A CA  
1673 C CA  B LEU A 256 ? 0.70932 1.12515 1.09892 -0.17532 -0.14901 -0.12549 256 LEU A CA  
1674 C C   . LEU A 256 ? 0.71938 1.10873 1.11532 -0.19455 -0.11541 -0.13244 256 LEU A C   
1675 O O   . LEU A 256 ? 0.73108 1.12201 1.15387 -0.21954 -0.12359 -0.14536 256 LEU A O   
1676 C CB  A LEU A 256 ? 0.75567 1.13055 1.05622 -0.16664 -0.16540 -0.12931 256 LEU A CB  
1677 C CB  B LEU A 256 ? 0.75533 1.13026 1.05595 -0.16663 -0.16541 -0.12930 256 LEU A CB  
1678 N N   . GLU A 257 ? 0.65636 1.01776 1.02559 -0.18368 -0.07837 -0.12418 257 GLU A N   
1679 C CA  . GLU A 257 ? 0.63590 0.96464 1.00238 -0.19877 -0.04455 -0.12854 257 GLU A CA  
1680 C C   . GLU A 257 ? 0.65682 1.01773 1.10887 -0.21949 -0.03267 -0.13180 257 GLU A C   
1681 O O   . GLU A 257 ? 0.64434 0.97893 1.09956 -0.23968 -0.01170 -0.13942 257 GLU A O   
1682 C CB  . GLU A 257 ? 0.55654 0.85410 0.88442 -0.18044 -0.01119 -0.11719 257 GLU A CB  
1683 N N   . ALA A 258 ? 0.57909 0.99635 1.10368 -0.21490 -0.04559 -0.12608 258 ALA A N   
1684 C CA  . ALA A 258 ? 0.52355 0.98242 1.14616 -0.23335 -0.03668 -0.12859 258 ALA A CA  
1685 C C   . ALA A 258 ? 0.55372 1.02354 1.20401 -0.26216 -0.06658 -0.14565 258 ALA A C   
1686 O O   . ALA A 258 ? 0.55977 1.06664 1.29897 -0.28258 -0.06399 -0.15065 258 ALA A O   
1687 C CB  . ALA A 258 ? 0.46028 0.97846 1.15396 -0.21689 -0.04725 -0.11728 258 ALA A CB  
1688 N N   . ALA A 259 ? 0.59201 1.02824 1.16805 -0.26452 -0.09397 -0.15519 259 ALA A N   
1689 C CA  . ALA A 259 ? 0.60638 1.03376 1.18711 -0.29359 -0.11761 -0.17360 259 ALA A CA  
1690 C C   . ALA A 259 ? 0.61344 1.01341 1.21582 -0.31914 -0.07881 -0.18056 259 ALA A C   
1691 O O   . ALA A 259 ? 0.62659 1.03497 1.27074 -0.34878 -0.09303 -0.19540 259 ALA A O   
1692 C CB  . ALA A 259 ? 0.65775 1.03725 1.13679 -0.28765 -0.14160 -0.18118 259 ALA A CB  
1693 N N   . ARG A 260 ? 0.60054 0.96407 1.17225 -0.30873 -0.03101 -0.17040 260 ARG A N   
1694 C CA  . ARG A 260 ? 0.66317 1.00176 1.26206 -0.32994 0.01228  -0.17316 260 ARG A CA  
1695 C C   . ARG A 260 ? 0.66411 1.06080 1.38346 -0.35184 0.01505  -0.17645 260 ARG A C   
1696 O O   . ARG A 260 ? 0.65617 1.03939 1.40300 -0.37854 0.02540  -0.18490 260 ARG A O   
1697 C CB  . ARG A 260 ? 0.65657 0.95729 1.21439 -0.30984 0.06011  -0.15815 260 ARG A CB  
1698 N N   . ALA A 261 ? 0.61761 1.07290 1.40148 -0.33559 0.00663  -0.16527 261 ALA A N   
1699 C CA  . ALA A 261 ? 0.56616 1.06586 1.43870 -0.34145 0.00759  -0.15674 261 ALA A CA  
1700 C C   . ALA A 261 ? 0.61274 1.13574 1.51255 -0.36245 -0.04047 -0.16712 261 ALA A C   
1701 O O   . ALA A 261 ? 0.62565 1.17994 1.59767 -0.37543 -0.03796 -0.16433 261 ALA A O   
1702 C CB  . ALA A 261 ? 0.51954 1.07009 1.43699 -0.31376 0.00312  -0.14033 261 ALA A CB  
1703 N N   . GLY A 262 ? 0.99907 0.99778 1.50991 0.35487  0.28550  -0.09872 262 GLY A N   
1704 C CA  . GLY A 262 ? 0.94806 1.02231 1.52815 0.35579  0.25281  -0.06973 262 GLY A CA  
1705 C C   . GLY A 262 ? 0.99862 1.05658 1.61514 0.38943  0.21863  -0.05335 262 GLY A C   
1706 O O   . GLY A 262 ? 1.01036 1.13621 1.68599 0.39202  0.19301  -0.03088 262 GLY A O   
1707 N N   . GLN A 263 ? 1.05099 1.01543 1.62679 0.41240  0.21569  -0.06320 263 GLN A N   
1708 C CA  . GLN A 263 ? 1.08628 1.01711 1.68365 0.44411  0.17903  -0.04643 263 GLN A CA  
1709 C C   . GLN A 263 ? 1.13019 1.03635 1.71708 0.41715  0.13794  -0.01528 263 GLN A C   
1710 O O   . GLN A 263 ? 1.22374 1.03577 1.74426 0.40436  0.12291  -0.01378 263 GLN A O   
1711 C CB  . GLN A 263 ? 1.15349 0.98083 1.69765 0.47323  0.18924  -0.06848 263 GLN A CB  
1712 N N   . ASP A 264 ? 0.95831 0.95112 1.60042 0.40048  0.11760  0.00874  264 ASP A N   
1713 C CA  . ASP A 264 ? 0.89616 0.87942 1.52125 0.36364  0.07908  0.03613  264 ASP A CA  
1714 C C   . ASP A 264 ? 0.94353 0.85052 1.54904 0.37612  0.03731  0.05464  264 ASP A C   
1715 O O   . ASP A 264 ? 0.98557 0.82383 1.51364 0.34049  0.01531  0.05940  264 ASP A O   
1716 C CB  . ASP A 264 ? 0.76353 0.85164 1.45459 0.34673  0.06802  0.05761  264 ASP A CB  
1717 N N   . ASP A 265 ? 0.94066 0.86011 1.59576 0.41867  0.02357  0.06279  265 ASP A N   
1718 C CA  . ASP A 265 ? 0.94450 0.78346 1.57428 0.43271  -0.01892 0.08194  265 ASP A CA  
1719 C C   . ASP A 265 ? 1.03667 0.74712 1.58162 0.43583  -0.01150 0.06403  265 ASP A C   
1720 O O   . ASP A 265 ? 1.13517 0.76251 1.61895 0.41189  -0.04714 0.07926  265 ASP A O   
1721 C CB  . ASP A 265 ? 0.96781 0.84425 1.65159 0.48062  -0.02993 0.08762  265 ASP A CB  
1722 N N   . GLU A 266 ? 1.06231 0.75298 1.58479 0.45503  0.03380  0.02982  266 GLU A N   
1723 C CA  . GLU A 266 ? 1.14161 0.70673 1.57263 0.45066  0.04471  0.01080  266 GLU A CA  
1724 C C   . GLU A 266 ? 1.13656 0.67986 1.48042 0.38199  0.03847  0.00965  266 GLU A C   
1725 O O   . GLU A 266 ? 1.17597 0.61881 1.42828 0.35837  0.02472  0.00617  266 GLU A O   
1726 C CB  . GLU A 266 ? 1.15153 0.70918 1.56720 0.47690  0.09341  -0.02761 266 GLU A CB  
1727 N N   . VAL A 267 ? 1.08032 0.71628 1.44973 0.34886  0.04806  0.01193  267 VAL A N   
1728 C CA  . VAL A 267 ? 1.09456 0.72191 1.39446 0.28823  0.04042  0.01132  267 VAL A CA  
1729 C C   . VAL A 267 ? 1.09125 0.69311 1.36670 0.25683  -0.00590 0.03753  267 VAL A C   
1730 O O   . VAL A 267 ? 1.14017 0.68014 1.33464 0.21644  -0.01857 0.03460  267 VAL A O   
1731 C CB  . VAL A 267 ? 0.96847 0.69500 1.30354 0.26684  0.06191  0.00708  267 VAL A CB  
1732 N N   . ARG A 268 ? 1.03336 0.68488 1.37553 0.26987  -0.03165 0.06337  268 ARG A N   
1733 C CA  . ARG A 268 ? 1.05937 0.67917 1.37318 0.23825  -0.07684 0.08935  268 ARG A CA  
1734 C C   . ARG A 268 ? 1.11084 0.60905 1.35744 0.24660  -0.09981 0.09157  268 ARG A C   
1735 O O   . ARG A 268 ? 1.16198 0.59847 1.32905 0.20000  -0.12150 0.09603  268 ARG A O   
1736 C CB  . ARG A 268 ? 1.01355 0.70489 1.41069 0.25292  -0.10171 0.11809  268 ARG A CB  
1737 C CG  . ARG A 268 ? 0.94861 0.75105 1.39963 0.23526  -0.08396 0.11925  268 ARG A CG  
1738 C CD  . ARG A 268 ? 0.91773 0.78678 1.44621 0.24667  -0.11065 0.14897  268 ARG A CD  
1739 N NE  . ARG A 268 ? 0.81431 0.77965 1.38267 0.22376  -0.09539 0.15120  268 ARG A NE  
1740 C CZ  . ARG A 268 ? 0.84206 0.82388 1.38114 0.17263  -0.10841 0.16158  268 ARG A CZ  
1741 N NH1 . ARG A 268 ? 0.86130 0.77878 1.33419 0.13568  -0.13506 0.16973  268 ARG A NH1 
1742 N NH2 . ARG A 268 ? 0.85762 0.91859 1.43027 0.15623  -0.09262 0.16241  268 ARG A NH2 
1743 N N   . ILE A 269 ? 1.13706 0.59718 1.41235 0.30528  -0.09376 0.08698  269 ILE A N   
1744 C CA  . ILE A 269 ? 1.24544 0.57661 1.45253 0.31902  -0.11532 0.08855  269 ILE A CA  
1745 C C   . ILE A 269 ? 1.33658 0.58718 1.43305 0.27856  -0.09772 0.06439  269 ILE A C   
1746 O O   . ILE A 269 ? 1.40044 0.55606 1.40882 0.24484  -0.12554 0.07149  269 ILE A O   
1747 C CB  . ILE A 269 ? 1.28683 0.59712 1.55273 0.39680  -0.10347 0.08219  269 ILE A CB  
1748 N N   . LEU A 270 ? 1.30278 0.59102 1.39811 0.27590  -0.05323 0.03669  270 LEU A N   
1749 C CA  . LEU A 270 ? 1.34847 0.57013 1.34227 0.23460  -0.03775 0.01485  270 LEU A CA  
1750 C C   . LEU A 270 ? 1.37286 0.61124 1.31826 0.16480  -0.05939 0.02416  270 LEU A C   
1751 O O   . LEU A 270 ? 1.41671 0.57106 1.26851 0.12511  -0.07378 0.02123  270 LEU A O   
1752 C CB  . LEU A 270 ? 1.29348 0.55955 1.30018 0.24399  0.01079  -0.01342 270 LEU A CB  
1753 N N   . MET A 271 ? 1.26616 0.61197 1.27268 0.14748  -0.06037 0.03410  271 MET A N   
1754 C CA  . MET A 271 ? 1.25901 0.62794 1.22883 0.08484  -0.07652 0.04002  271 MET A CA  
1755 C C   . MET A 271 ? 1.30366 0.60820 1.23041 0.05986  -0.11851 0.06199  271 MET A C   
1756 O O   . MET A 271 ? 1.36704 0.63283 1.21885 0.00486  -0.13030 0.05921  271 MET A O   
1757 C CB  . MET A 271 ? 1.09252 0.58039 1.13621 0.07716  -0.06730 0.04536  271 MET A CB  
1758 C CG  . MET A 271 ? 1.08125 0.62628 1.14723 0.08550  -0.03003 0.02432  271 MET A CG  
1759 S SD  . MET A 271 ? 1.12021 0.78879 1.26389 0.07786  -0.02210 0.03229  271 MET A SD  
1760 C CE  . MET A 271 ? 0.99958 0.70135 1.22771 0.12743  -0.03072 0.05269  271 MET A CE  
1761 N N   . ALA A 272 ? 1.27651 0.57176 1.24952 0.09673  -0.14274 0.08459  272 ALA A N   
1762 C CA  . ALA A 272 ? 1.33200 0.55111 1.25595 0.07450  -0.18767 0.10838  272 ALA A CA  
1763 C C   . ALA A 272 ? 1.45350 0.54141 1.26928 0.05858  -0.19589 0.09868  272 ALA A C   
1764 O O   . ALA A 272 ? 1.49851 0.52709 1.23361 0.00355  -0.22153 0.10644  272 ALA A O   
1765 C CB  . ALA A 272 ? 1.29077 0.51675 1.28682 0.12698  -0.21412 0.13468  272 ALA A CB  
1766 N N   . ASN A 273 ? 1.49353 0.53162 1.29968 0.10192  -0.17218 0.08008  273 ASN A N   
1767 C CA  . ASN A 273 ? 1.62266 0.53045 1.31659 0.08395  -0.17513 0.06765  273 ASN A CA  
1768 C C   . ASN A 273 ? 1.65181 0.56907 1.27442 0.01735  -0.15659 0.04698  273 ASN A C   
1769 O O   . ASN A 273 ? 1.68552 0.50264 1.20267 -0.01883 -0.16442 0.03955  273 ASN A O   
1770 C CB  . ASN A 273 ? 1.66910 0.52031 1.37174 0.14907  -0.14994 0.05052  273 ASN A CB  
1771 C CG  . ASN A 273 ? 1.61651 0.49259 1.41360 0.21918  -0.16077 0.06807  273 ASN A CG  
1772 O OD1 . ASN A 273 ? 1.60327 0.50303 1.43325 0.21618  -0.19738 0.09718  273 ASN A OD1 
1773 N ND2 . ASN A 273 ? 1.63226 0.51431 1.47680 0.27859  -0.12603 0.04979  273 ASN A ND2 
1774 N N   . GLY A 274 ? 1.71341 0.75033 1.39207 0.00037  -0.13373 0.03834  274 GLY A N   
1775 C CA  . GLY A 274 ? 1.71664 0.78037 1.34589 -0.05676 -0.11743 0.01969  274 GLY A CA  
1776 C C   . GLY A 274 ? 1.72890 0.80706 1.35945 -0.03774 -0.07990 -0.00511 274 GLY A C   
1777 O O   . GLY A 274 ? 1.90090 0.88828 1.48188 -0.01462 -0.07013 -0.01621 274 GLY A O   
1778 N N   . ALA A 275 ? 1.44014 0.62503 1.12121 -0.04872 -0.05929 -0.01396 275 ALA A N   
1779 C CA  . ALA A 275 ? 1.43575 0.63790 1.11439 -0.03736 -0.02669 -0.03528 275 ALA A CA  
1780 C C   . ALA A 275 ? 1.41552 0.71977 1.12069 -0.07361 -0.01831 -0.04121 275 ALA A C   
1781 O O   . ALA A 275 ? 1.40657 0.78590 1.16409 -0.08516 -0.02881 -0.02978 275 ALA A O   
1782 C CB  . ALA A 275 ? 1.39095 0.61603 1.14067 0.02856  -0.00437 -0.03767 275 ALA A CB  
1783 N N   . ASP A 276 ? 1.38837 0.69094 1.05473 -0.09152 -0.00036 -0.05893 276 ASP A N   
1784 C CA  . ASP A 276 ? 1.33023 0.72715 1.02403 -0.11986 0.00570  -0.06439 276 ASP A CA  
1785 C C   . ASP A 276 ? 1.25894 0.73726 1.04202 -0.07838 0.02142  -0.06065 276 ASP A C   
1786 O O   . ASP A 276 ? 1.26666 0.73714 1.05549 -0.04982 0.04349  -0.06987 276 ASP A O   
1787 C CB  . ASP A 276 ? 1.37930 0.74635 1.00349 -0.15048 0.01605  -0.08133 276 ASP A CB  
1788 C CG  . ASP A 276 ? 1.41316 0.87837 1.06983 -0.17555 0.01802  -0.08511 276 ASP A CG  
1789 O OD1 . ASP A 276 ? 1.37329 0.92338 1.10023 -0.17197 0.01213  -0.07657 276 ASP A OD1 
1790 O OD2 . ASP A 276 ? 1.42024 0.87451 1.02994 -0.19900 0.02426  -0.09622 276 ASP A OD2 
1791 N N   . VAL A 277 ? 1.08522 0.63782 0.93210 -0.07861 0.01152  -0.04801 277 VAL A N   
1792 C CA  . VAL A 277 ? 1.04509 0.67322 0.97003 -0.04604 0.02448  -0.04320 277 VAL A CA  
1793 C C   . VAL A 277 ? 1.05900 0.73159 0.98461 -0.05455 0.03944  -0.05472 277 VAL A C   
1794 O O   . VAL A 277 ? 1.01104 0.71924 0.97620 -0.02726 0.05583  -0.05541 277 VAL A O   
1795 C CB  . VAL A 277 ? 0.97009 0.65895 0.94854 -0.05345 0.00982  -0.02807 277 VAL A CB  
1796 C CG1 . VAL A 277 ? 0.89471 0.64905 0.94701 -0.02003 0.02171  -0.02086 277 VAL A CG1 
1797 C CG2 . VAL A 277 ? 1.04252 0.67783 1.00252 -0.05811 -0.01187 -0.01491 277 VAL A CG2 
1798 N N   . ASN A 278 ? 1.03279 0.70468 0.91323 -0.09479 0.03236  -0.06296 278 ASN A N   
1799 C CA  . ASN A 278 ? 1.00371 0.71031 0.87643 -0.10659 0.03994  -0.07165 278 ASN A CA  
1800 C C   . ASN A 278 ? 1.10205 0.73548 0.89867 -0.11701 0.04974  -0.08456 278 ASN A C   
1801 O O   . ASN A 278 ? 1.14616 0.78657 0.90399 -0.15041 0.04473  -0.09121 278 ASN A O   
1802 C CB  . ASN A 278 ? 0.94616 0.71587 0.83076 -0.14299 0.02453  -0.07172 278 ASN A CB  
1803 C CG  . ASN A 278 ? 0.91410 0.75160 0.86889 -0.13315 0.01954  -0.06216 278 ASN A CG  
1804 O OD1 . ASN A 278 ? 0.91248 0.74308 0.89794 -0.10755 0.02247  -0.05299 278 ASN A OD1 
1805 N ND2 . ASN A 278 ? 0.86419 0.76816 0.84553 -0.15331 0.01203  -0.06455 278 ASN A ND2 
1806 N N   . ALA A 279 ? 1.16033 0.72307 0.93528 -0.08846 0.06390  -0.08856 279 ALA A N   
1807 C CA  . ALA A 279 ? 1.17454 0.65664 0.87245 -0.09511 0.07877  -0.10356 279 ALA A CA  
1808 C C   . ALA A 279 ? 1.16587 0.67778 0.86377 -0.09396 0.09601  -0.11118 279 ALA A C   
1809 O O   . ALA A 279 ? 1.18245 0.76814 0.94299 -0.07855 0.09844  -0.10433 279 ALA A O   
1810 C CB  . ALA A 279 ? 1.22700 0.63005 0.91349 -0.05580 0.09304  -0.10774 279 ALA A CB  
1811 N N   . THR A 280 ? 1.23969 0.68566 0.85741 -0.11435 0.10734  -0.12518 280 THR A N   
1812 C CA  . THR A 280 ? 1.24664 0.70740 0.84571 -0.12267 0.12158  -0.13234 280 THR A CA  
1813 C C   . THR A 280 ? 1.33085 0.69575 0.85943 -0.11446 0.15212  -0.15163 280 THR A C   
1814 O O   . THR A 280 ? 1.40656 0.68651 0.85779 -0.13451 0.15191  -0.16065 280 THR A O   
1815 C CB  . THR A 280 ? 1.24907 0.74362 0.81490 -0.17336 0.09806  -0.12855 280 THR A CB  
1816 O OG1 . THR A 280 ? 1.34799 0.77472 0.83269 -0.21106 0.08940  -0.13533 280 THR A OG1 
1817 C CG2 . THR A 280 ? 1.16007 0.75410 0.80341 -0.17606 0.07285  -0.11305 280 THR A CG2 
1818 N N   . ASP A 281 ? 1.35946 0.73499 0.91110 -0.08693 0.18027  -0.15940 281 ASP A N   
1819 C CA  . ASP A 281 ? 1.39764 0.68817 0.88813 -0.07670 0.21668  -0.18189 281 ASP A CA  
1820 C C   . ASP A 281 ? 1.48826 0.73758 0.88210 -0.12829 0.21799  -0.19118 281 ASP A C   
1821 O O   . ASP A 281 ? 1.45033 0.73555 0.82708 -0.17005 0.18689  -0.17894 281 ASP A O   
1822 C CB  . ASP A 281 ? 1.36083 0.68723 0.91280 -0.03404 0.24886  -0.18874 281 ASP A CB  
1823 C CG  . ASP A 281 ? 1.37673 0.76915 0.94145 -0.05367 0.24959  -0.18380 281 ASP A CG  
1824 O OD1 . ASP A 281 ? 1.38079 0.81887 0.94478 -0.08610 0.21710  -0.16801 281 ASP A OD1 
1825 O OD2 . ASP A 281 ? 1.41588 0.81161 0.98846 -0.03739 0.28324  -0.19667 281 ASP A OD2 
1826 N N   . ASN A 282 ? 1.65955 0.83455 0.98986 -0.12659 0.25487  -0.21367 282 ASN A N   
1827 C CA  . ASN A 282 ? 1.70693 0.83259 0.93426 -0.17970 0.25792  -0.22304 282 ASN A CA  
1828 C C   . ASN A 282 ? 1.68384 0.88865 0.92996 -0.20549 0.24222  -0.20984 282 ASN A C   
1829 O O   . ASN A 282 ? 1.75303 0.94109 0.92648 -0.25715 0.22621  -0.20739 282 ASN A O   
1830 C CB  . ASN A 282 ? 1.71679 0.74254 0.87195 -0.17057 0.30687  -0.25298 282 ASN A CB  
1831 N N   . ASP A 283 ? 1.57847 0.86525 0.91644 -0.17243 0.24400  -0.20000 283 ASP A N   
1832 C CA  . ASP A 283 ? 1.51680 0.87447 0.87617 -0.19194 0.22530  -0.18487 283 ASP A CA  
1833 C C   . ASP A 283 ? 1.40341 0.85196 0.84242 -0.18766 0.18306  -0.15958 283 ASP A C   
1834 O O   . ASP A 283 ? 1.36752 0.87506 0.83118 -0.19860 0.16284  -0.14497 283 ASP A O   
1835 C CB  . ASP A 283 ? 1.50443 0.88322 0.89679 -0.16540 0.25933  -0.19317 283 ASP A CB  
1836 C CG  . ASP A 283 ? 1.63386 0.92784 0.95122 -0.16913 0.30791  -0.22261 283 ASP A CG  
1837 O OD1 . ASP A 283 ? 1.71575 0.92648 0.94737 -0.19393 0.31374  -0.23572 283 ASP A OD1 
1838 O OD2 . ASP A 283 ? 1.69021 0.99983 1.03170 -0.14943 0.34243  -0.23420 283 ASP A OD2 
1839 N N   . GLY A 284 ? 1.39157 0.84742 0.86685 -0.17301 0.16974  -0.15482 284 GLY A N   
1840 C CA  . GLY A 284 ? 1.28534 0.82058 0.82610 -0.17499 0.13349  -0.13511 284 GLY A CA  
1841 C C   . GLY A 284 ? 1.24914 0.85203 0.88670 -0.13395 0.13539  -0.12469 284 GLY A C   
1842 O O   . GLY A 284 ? 1.28550 0.95899 0.97157 -0.13579 0.11327  -0.10984 284 GLY A O   
1843 N N   . TYR A 285 ? 1.19029 0.77089 0.85621 -0.09660 0.16081  -0.13216 285 TYR A N   
1844 C CA  . TYR A 285 ? 1.16633 0.80754 0.91996 -0.06010 0.16433  -0.12237 285 TYR A CA  
1845 C C   . TYR A 285 ? 1.12482 0.76368 0.91787 -0.03955 0.15520  -0.11686 285 TYR A C   
1846 O O   . TYR A 285 ? 1.16427 0.73718 0.92647 -0.02883 0.16699  -0.12703 285 TYR A O   
1847 C CB  . TYR A 285 ? 1.16746 0.80002 0.93109 -0.03434 0.20143  -0.13397 285 TYR A CB  
1848 C CG  . TYR A 285 ? 1.25950 0.90212 0.98888 -0.05716 0.20846  -0.13602 285 TYR A CG  
1849 C CD1 . TYR A 285 ? 1.33168 0.91065 0.97373 -0.08491 0.22388  -0.15146 285 TYR A CD1 
1850 C CD2 . TYR A 285 ? 1.25643 0.96447 1.03179 -0.05507 0.19758  -0.12159 285 TYR A CD2 
1851 C CE1 . TYR A 285 ? 1.41613 0.99876 1.01846 -0.11115 0.22686  -0.15131 285 TYR A CE1 
1852 C CE2 . TYR A 285 ? 1.32585 1.03442 1.06176 -0.07868 0.19963  -0.12111 285 TYR A CE2 
1853 C CZ  . TYR A 285 ? 1.43689 1.08390 1.08655 -0.10749 0.21328  -0.13532 285 TYR A CZ  
1854 O OH  . TYR A 285 ? 1.44451 1.08700 1.04745 -0.13576 0.21223  -0.13292 285 TYR A OH  
1855 N N   . THR A 286 ? 1.08961 0.79378 0.94537 -0.03512 0.13386  -0.10081 286 THR A N   
1856 C CA  . THR A 286 ? 1.06525 0.77342 0.96111 -0.01861 0.12352  -0.09266 286 THR A CA  
1857 C C   . THR A 286 ? 1.02208 0.73719 0.96938 0.02335  0.14330  -0.09176 286 THR A C   
1858 O O   . THR A 286 ? 1.00561 0.74144 0.96895 0.03723  0.16514  -0.09675 286 THR A O   
1859 C CB  . THR A 286 ? 1.03900 0.81498 0.98066 -0.03169 0.09798  -0.07809 286 THR A CB  
1860 O OG1 . THR A 286 ? 0.99414 0.82928 0.98722 -0.01669 0.10270  -0.07036 286 THR A OG1 
1861 C CG2 . THR A 286 ? 1.04852 0.83347 0.95242 -0.07076 0.07897  -0.07997 286 THR A CG2 
1862 N N   . PRO A 287 ? 1.01250 0.71010 0.98418 0.04194  0.13526  -0.08531 287 PRO A N   
1863 C CA  . PRO A 287 ? 0.95877 0.68582 0.99788 0.08110  0.14609  -0.07902 287 PRO A CA  
1864 C C   . PRO A 287 ? 0.89170 0.70242 0.99013 0.08240  0.14493  -0.06738 287 PRO A C   
1865 O O   . PRO A 287 ? 0.86626 0.70918 1.00910 0.10737  0.16377  -0.06767 287 PRO A O   
1866 C CB  . PRO A 287 ? 0.94574 0.64667 0.99615 0.08785  0.12279  -0.06693 287 PRO A CB  
1867 C CG  . PRO A 287 ? 1.06933 0.69362 1.03991 0.06230  0.11442  -0.07601 287 PRO A CG  
1868 C CD  . PRO A 287 ? 1.07275 0.71583 1.00446 0.02613  0.11556  -0.08355 287 PRO A CD  
1869 N N   . LEU A 288 ? 0.90092 0.74743 1.00083 0.05557  0.12419  -0.05810 288 LEU A N   
1870 C CA  . LEU A 288 ? 0.80460 0.71792 0.94896 0.05463  0.12248  -0.04788 288 LEU A CA  
1871 C C   . LEU A 288 ? 0.82655 0.74943 0.95631 0.05480  0.14367  -0.05645 288 LEU A C   
1872 O O   . LEU A 288 ? 0.79010 0.74984 0.95655 0.06819  0.15742  -0.05289 288 LEU A O   
1873 C CB  . LEU A 288 ? 0.75857 0.69824 0.90117 0.02805  0.09860  -0.04060 288 LEU A CB  
1874 C CG  . LEU A 288 ? 0.69954 0.69718 0.88577 0.02843  0.09414  -0.02918 288 LEU A CG  
1875 C CD1 . LEU A 288 ? 0.65014 0.66875 0.88461 0.04689  0.09683  -0.01804 288 LEU A CD1 
1876 C CD2 . LEU A 288 ? 0.65629 0.67659 0.84458 0.00669  0.07381  -0.02572 288 LEU A CD2 
1877 N N   . HIS A 289 ? 0.84898 0.73863 0.92032 0.03479  0.14523  -0.06703 289 HIS A N   
1878 C CA  . HIS A 289 ? 0.87495 0.76114 0.91747 0.02870  0.16435  -0.07547 289 HIS A CA  
1879 C C   . HIS A 289 ? 0.85890 0.74126 0.92006 0.05389  0.19788  -0.08577 289 HIS A C   
1880 O O   . HIS A 289 ? 0.82157 0.73839 0.90122 0.05587  0.21291  -0.08502 289 HIS A O   
1881 C CB  . HIS A 289 ? 0.95927 0.79454 0.92694 0.00299  0.16267  -0.08675 289 HIS A CB  
1882 C CG  . HIS A 289 ? 0.99328 0.84936 0.94656 -0.02408 0.13215  -0.07738 289 HIS A CG  
1883 N ND1 . HIS A 289 ? 1.00949 0.86260 0.95719 -0.03830 0.10997  -0.07491 289 HIS A ND1 
1884 C CD2 . HIS A 289 ? 1.01375 0.89554 0.95912 -0.03890 0.11945  -0.07005 289 HIS A CD2 
1885 C CE1 . HIS A 289 ? 1.02568 0.91107 0.97164 -0.05820 0.08684  -0.06782 289 HIS A CE1 
1886 N NE2 . HIS A 289 ? 1.04922 0.94936 0.99390 -0.05667 0.09013  -0.06366 289 HIS A NE2 
1887 N N   . LEU A 290 ? 0.96136 0.80144 1.01782 0.07325  0.21024  -0.09617 290 LEU A N   
1888 C CA  . LEU A 290 ? 0.94597 0.78165 1.02333 0.10159  0.24549  -0.11028 290 LEU A CA  
1889 C C   . LEU A 290 ? 0.93009 0.83289 1.09262 0.12698  0.24606  -0.09755 290 LEU A C   
1890 O O   . LEU A 290 ? 0.91017 0.84766 1.10240 0.13923  0.27402  -0.10517 290 LEU A O   
1891 C CB  . LEU A 290 ? 0.91680 0.68076 0.96501 0.11937  0.25568  -0.12458 290 LEU A CB  
1892 C CG  . LEU A 290 ? 0.99022 0.68167 0.94808 0.08874  0.24958  -0.13468 290 LEU A CG  
1893 C CD1 . LEU A 290 ? 1.06060 0.67402 0.98892 0.10732  0.25624  -0.14620 290 LEU A CD1 
1894 C CD2 . LEU A 290 ? 1.02906 0.70362 0.92997 0.06543  0.27404  -0.15037 290 LEU A CD2 
1895 N N   . ALA A 291 ? 0.83132 0.75472 1.03118 0.13078  0.21594  -0.07846 291 ALA A N   
1896 C CA  . ALA A 291 ? 0.78038 0.76640 1.05643 0.14932  0.21203  -0.06356 291 ALA A CA  
1897 C C   . ALA A 291 ? 0.77116 0.81476 1.06191 0.12969  0.21252  -0.05473 291 ALA A C   
1898 O O   . ALA A 291 ? 0.76512 0.86146 1.10512 0.14021  0.22611  -0.05097 291 ALA A O   
1899 C CB  . ALA A 291 ? 0.78135 0.76375 1.08003 0.15166  0.17847  -0.04527 291 ALA A CB  
1900 N N   . ALA A 292 ? 0.78928 0.82342 1.03775 0.10091  0.19683  -0.05107 292 ALA A N   
1901 C CA  . ALA A 292 ? 0.78244 0.85658 1.03494 0.08312  0.19469  -0.04232 292 ALA A CA  
1902 C C   . ALA A 292 ? 0.79253 0.87009 1.02335 0.07802  0.22534  -0.05545 292 ALA A C   
1903 O O   . ALA A 292 ? 0.77885 0.89829 1.03079 0.07176  0.23400  -0.04962 292 ALA A O   
1904 C CB  . ALA A 292 ? 0.77567 0.83559 0.99172 0.05940  0.16903  -0.03612 292 ALA A CB  
1905 N N   . SER A 293 ? 0.80675 0.83716 0.98842 0.07569  0.24305  -0.07391 293 SER A N   
1906 C CA  A SER A 293 ? 0.82909 0.85616 0.97962 0.06491  0.27514  -0.08909 293 SER A CA  
1907 C CA  B SER A 293 ? 0.83145 0.85853 0.98198 0.06491  0.27514  -0.08909 293 SER A CA  
1908 C CA  C SER A 293 ? 0.87038 0.89676 1.02053 0.06508  0.27535  -0.08935 293 SER A CA  
1909 C C   . SER A 293 ? 0.79829 0.86461 1.00310 0.08901  0.30929  -0.09956 293 SER A C   
1910 O O   . SER A 293 ? 0.84397 0.93112 1.03898 0.07636  0.33693  -0.10932 293 SER A O   
1911 C CB  A SER A 293 ? 0.89728 0.85760 0.97324 0.05162  0.28573  -0.10698 293 SER A CB  
1912 C CB  B SER A 293 ? 0.92513 0.88544 1.00114 0.05165  0.28572  -0.10698 293 SER A CB  
1913 C CB  C SER A 293 ? 0.90718 0.86654 0.98421 0.05300  0.28649  -0.10759 293 SER A CB  
1914 O OG  A SER A 293 ? 0.91072 0.83507 0.99179 0.07551  0.29532  -0.11906 293 SER A OG  
1915 O OG  B SER A 293 ? 0.91050 0.83487 0.99171 0.07556  0.29520  -0.11899 293 SER A OG  
1916 O OG  C SER A 293 ? 0.91795 0.84846 0.95588 0.03398  0.25254  -0.09790 293 SER A OG  
1917 N N   . ASN A 294 ? 0.77424 0.85299 1.03644 0.12208  0.30695  -0.09739 294 ASN A N   
1918 C CA  . ASN A 294 ? 0.76258 0.88582 1.08952 0.15157  0.33636  -0.10675 294 ASN A CA  
1919 C C   . ASN A 294 ? 0.76136 0.95926 1.16624 0.16006  0.31935  -0.08460 294 ASN A C   
1920 O O   . ASN A 294 ? 0.72998 0.97590 1.20367 0.18792  0.33576  -0.08770 294 ASN A O   
1921 C CB  . ASN A 294 ? 0.82553 0.90321 1.16109 0.18735  0.34666  -0.12109 294 ASN A CB  
1922 C CG  . ASN A 294 ? 0.88972 0.88556 1.13880 0.17440  0.36382  -0.14341 294 ASN A CG  
1923 O OD1 . ASN A 294 ? 0.90280 0.87824 1.08693 0.13762  0.36273  -0.14545 294 ASN A OD1 
1924 N ND2 . ASN A 294 ? 0.93282 0.87637 1.17669 0.20352  0.37719  -0.15896 294 ASN A ND2 
1925 N N   . GLY A 295 ? 0.85645 1.06582 1.25275 0.13657  0.28722  -0.06287 295 GLY A N   
1926 C CA  . GLY A 295 ? 0.80819 1.08203 1.26411 0.13547  0.27180  -0.04180 295 GLY A CA  
1927 C C   . GLY A 295 ? 0.80448 1.09476 1.32305 0.16520  0.25352  -0.02962 295 GLY A C   
1928 O O   . GLY A 295 ? 0.84498 1.19359 1.43181 0.18473  0.26361  -0.02662 295 GLY A O   
1929 N N   . HIS A 296 ? 0.71322 0.95411 1.20901 0.16681  0.22490  -0.02174 296 HIS A N   
1930 C CA  . HIS A 296 ? 0.69343 0.93510 1.23361 0.18877  0.20058  -0.00705 296 HIS A CA  
1931 C C   . HIS A 296 ? 0.67895 0.91277 1.20114 0.16185  0.16509  0.01318  296 HIS A C   
1932 O O   . HIS A 296 ? 0.68109 0.86128 1.16415 0.15543  0.14705  0.01307  296 HIS A O   
1933 C CB  . HIS A 296 ? 0.75213 0.92831 1.27258 0.21569  0.20420  -0.02081 296 HIS A CB  
1934 C CG  . HIS A 296 ? 0.79355 0.96826 1.32386 0.24177  0.24449  -0.04555 296 HIS A CG  
1935 N ND1 . HIS A 296 ? 0.77144 1.01198 1.37166 0.26578  0.26260  -0.04785 296 HIS A ND1 
1936 C CD2 . HIS A 296 ? 0.81058 0.92653 1.28438 0.24372  0.27024  -0.07056 296 HIS A CD2 
1937 C CE1 . HIS A 296 ? 0.75505 0.97653 1.33616 0.28066  0.29648  -0.07487 296 HIS A CE1 
1938 N NE2 . HIS A 296 ? 0.80029 0.94401 1.31310 0.27124  0.30866  -0.08965 296 HIS A NE2 
1939 N N   . LEU A 297 ? 0.67272 0.95961 1.22019 0.14303  0.15752  0.02889  297 LEU A N   
1940 C CA  . LEU A 297 ? 0.63277 0.91219 1.16190 0.11616  0.12917  0.04526  297 LEU A CA  
1941 C C   . LEU A 297 ? 0.61841 0.87411 1.16030 0.12339  0.10121  0.05807  297 LEU A C   
1942 O O   . LEU A 297 ? 0.64084 0.86009 1.14559 0.10399  0.08271  0.06089  297 LEU A O   
1943 C CB  . LEU A 297 ? 0.52331 0.85823 1.07547 0.09512  0.12754  0.05998  297 LEU A CB  
1944 N N   . GLU A 298 ? 0.57467 0.85065 1.16871 0.15063  0.09727  0.06571  298 GLU A N   
1945 C CA  . GLU A 298 ? 0.59628 0.83721 1.19465 0.15868  0.06739  0.07910  298 GLU A CA  
1946 C C   . GLU A 298 ? 0.63435 0.79638 1.17290 0.15977  0.06574  0.06429  298 GLU A C   
1947 O O   . GLU A 298 ? 0.66221 0.78463 1.16706 0.13966  0.04097  0.07236  298 GLU A O   
1948 C CB  . GLU A 298 ? 0.56924 0.84102 1.23657 0.19662  0.06394  0.08787  298 GLU A CB  
1949 N N   . ILE A 299 ? 0.65815 0.79593 1.17709 0.17760  0.09314  0.04174  299 ILE A N   
1950 C CA  . ILE A 299 ? 0.68961 0.75242 1.14425 0.17269  0.09281  0.02706  299 ILE A CA  
1951 C C   . ILE A 299 ? 0.69011 0.74679 1.09525 0.13490  0.08971  0.02240  299 ILE A C   
1952 O O   . ILE A 299 ? 0.71332 0.72681 1.07502 0.11531  0.07316  0.02156  299 ILE A O   
1953 C CB  . ILE A 299 ? 0.68146 0.71571 1.12506 0.20063  0.12420  0.00390  299 ILE A CB  
1954 N N   . VAL A 300 ? 0.70146 0.80179 1.11300 0.12366  0.10451  0.01953  300 VAL A N   
1955 C CA  . VAL A 300 ? 0.67719 0.77452 1.04974 0.09426  0.10002  0.01578  300 VAL A CA  
1956 C C   . VAL A 300 ? 0.71058 0.81387 1.08362 0.07098  0.07509  0.02923  300 VAL A C   
1957 O O   . VAL A 300 ? 0.68087 0.77251 1.02223 0.04967  0.06841  0.02358  300 VAL A O   
1958 C CB  . VAL A 300 ? 0.55715 0.69341 0.93525 0.08859  0.11735  0.01328  300 VAL A CB  
1959 N N   . GLU A 301 ? 0.73519 0.85912 1.14427 0.07291  0.06149  0.04648  301 GLU A N   
1960 C CA  . GLU A 301 ? 0.73004 0.85425 1.13261 0.04594  0.03987  0.05840  301 GLU A CA  
1961 C C   . GLU A 301 ? 0.76132 0.83674 1.13935 0.03952  0.02007  0.06117  301 GLU A C   
1962 O O   . GLU A 301 ? 0.77785 0.83737 1.12531 0.01038  0.00918  0.05940  301 GLU A O   
1963 C CB  . GLU A 301 ? 0.68248 0.85108 1.12586 0.04141  0.03248  0.07785  301 GLU A CB  
1964 C CG  . GLU A 301 ? 0.69860 0.90809 1.15167 0.03476  0.04834  0.07694  301 GLU A CG  
1965 C CD  . GLU A 301 ? 0.71676 0.97253 1.21088 0.03150  0.04364  0.09578  301 GLU A CD  
1966 O OE1 . GLU A 301 ? 0.70504 0.96522 1.22559 0.03651  0.02556  0.11086  301 GLU A OE1 
1967 O OE2 . GLU A 301 ? 0.73536 1.02160 1.23291 0.02225  0.05586  0.09676  301 GLU A OE2 
1968 N N   . VAL A 302 ? 0.70882 0.75783 1.09769 0.06545  0.01572  0.06461  302 VAL A N   
1969 C CA  . VAL A 302 ? 0.70641 0.69677 1.06270 0.05792  -0.00648 0.06938  302 VAL A CA  
1970 C C   . VAL A 302 ? 0.75548 0.69825 1.05222 0.04281  -0.00032 0.05002  302 VAL A C   
1971 O O   . VAL A 302 ? 0.79577 0.70072 1.05073 0.01449  -0.01706 0.05081  302 VAL A O   
1972 C CB  . VAL A 302 ? 0.69086 0.65978 1.07617 0.09512  -0.01505 0.07914  302 VAL A CB  
1973 C CG1 . VAL A 302 ? 0.73090 0.68659 1.11956 0.13002  0.01258  0.05996  302 VAL A CG1 
1974 C CG2 . VAL A 302 ? 0.76004 0.65858 1.10432 0.08409  -0.04430 0.08854  302 VAL A CG2 
1975 N N   . LEU A 303 ? 0.70480 0.65016 0.99283 0.05589  0.02321  0.03267  303 LEU A N   
1976 C CA  . LEU A 303 ? 0.73794 0.64446 0.96911 0.03726  0.02720  0.01572  303 LEU A CA  
1977 C C   . LEU A 303 ? 0.71670 0.65198 0.93506 0.00088  0.02078  0.01304  303 LEU A C   
1978 O O   . LEU A 303 ? 0.77583 0.68260 0.95213 -0.02670 0.01132  0.00649  303 LEU A O   
1979 C CB  . LEU A 303 ? 0.76104 0.66502 0.98276 0.05505  0.05228  -0.00043 303 LEU A CB  
1980 C CG  . LEU A 303 ? 0.81493 0.68445 1.04325 0.09164  0.06635  -0.00544 303 LEU A CG  
1981 C CD1 . LEU A 303 ? 0.80548 0.68026 1.02235 0.10165  0.09553  -0.02280 303 LEU A CD1 
1982 C CD2 . LEU A 303 ? 0.82745 0.61575 1.00673 0.09093  0.05408  -0.00837 303 LEU A CD2 
1983 N N   . LEU A 304 ? 0.72485 0.71620 0.97870 -0.00021 0.02671  0.01705  304 LEU A N   
1984 C CA  . LEU A 304 ? 0.67922 0.69911 0.92870 -0.02860 0.02285  0.01301  304 LEU A CA  
1985 C C   . LEU A 304 ? 0.68538 0.69282 0.92352 -0.05642 0.00622  0.02007  304 LEU A C   
1986 O O   . LEU A 304 ? 0.67492 0.68112 0.88810 -0.08541 0.00290  0.01004  304 LEU A O   
1987 C CB  . LEU A 304 ? 0.59276 0.66175 0.87741 -0.02121 0.03204  0.01717  304 LEU A CB  
1988 C CG  . LEU A 304 ? 0.53099 0.61085 0.81546 -0.00388 0.04698  0.00928  304 LEU A CG  
1989 C CD1 . LEU A 304 ? 0.51714 0.63486 0.82811 -0.00009 0.05310  0.01605  304 LEU A CD1 
1990 C CD2 . LEU A 304 ? 0.56946 0.64185 0.82329 -0.01665 0.04573  -0.00494 304 LEU A CD2 
1991 N N   . LYS A 305 ? 0.65811 0.65888 0.91386 -0.05090 -0.00488 0.03740  305 LYS A N   
1992 C CA  . LYS A 305 ? 0.65462 0.63602 0.89084 -0.08229 -0.02328 0.04646  305 LYS A CA  
1993 C C   . LYS A 305 ? 0.66694 0.58998 0.85035 -0.10030 -0.03472 0.04048  305 LYS A C   
1994 O O   . LYS A 305 ? 0.66472 0.57623 0.81543 -0.13965 -0.04242 0.03668  305 LYS A O   
1995 C CB  . LYS A 305 ? 0.65658 0.63982 0.92079 -0.07208 -0.03830 0.06984  305 LYS A CB  
1996 N N   . ASN A 306 ? 0.72668 0.60898 0.89600 -0.07485 -0.03400 0.03806  306 ASN A N   
1997 C CA  . ASN A 306 ? 0.81221 0.62620 0.92134 -0.09135 -0.04464 0.03240  306 ASN A CA  
1998 C C   . ASN A 306 ? 0.79245 0.60955 0.86697 -0.11266 -0.03219 0.01091  306 ASN A C   
1999 O O   . ASN A 306 ? 0.84393 0.60308 0.86218 -0.12812 -0.03812 0.00417  306 ASN A O   
2000 C CB  . ASN A 306 ? 0.83237 0.59174 0.93771 -0.05277 -0.04855 0.03832  306 ASN A CB  
2001 C CG  . ASN A 306 ? 0.86210 0.62476 1.00947 -0.02948 -0.06540 0.06152  306 ASN A CG  
2002 O OD1 . ASN A 306 ? 0.86421 0.66875 1.03867 -0.04560 -0.07400 0.07418  306 ASN A OD1 
2003 N ND2 . ASN A 306 ? 0.96132 0.68023 1.11499 0.00869  -0.07023 0.06693  306 ASN A ND2 
2004 N N   . GLY A 307 ? 0.73165 0.61282 0.83649 -0.11504 -0.01756 0.00129  307 GLY A N   
2005 C CA  . GLY A 307 ? 0.73091 0.62804 0.81329 -0.13518 -0.01004 -0.01653 307 GLY A CA  
2006 C C   . GLY A 307 ? 0.75762 0.65113 0.83752 -0.10989 0.00242  -0.02425 307 GLY A C   
2007 O O   . GLY A 307 ? 0.82542 0.66791 0.85658 -0.11577 0.00192  -0.03145 307 GLY A O   
2008 N N   . ALA A 308 ? 0.73153 0.67199 0.85508 -0.08587 0.01371  -0.02299 308 ALA A N   
2009 C CA  . ALA A 308 ? 0.69715 0.63639 0.81430 -0.06758 0.02586  -0.03011 308 ALA A CA  
2010 C C   . ALA A 308 ? 0.64872 0.64398 0.78536 -0.07571 0.02710  -0.03574 308 ALA A C   
2011 O O   . ALA A 308 ? 0.63129 0.67105 0.80720 -0.07405 0.02642  -0.03120 308 ALA A O   
2012 C CB  . ALA A 308 ? 0.71094 0.64851 0.85702 -0.03076 0.03817  -0.02287 308 ALA A CB  
2013 N N   . ASP A 309 ? 0.65704 0.64613 0.76366 -0.08487 0.02736  -0.04504 309 ASP A N   
2014 C CA  . ASP A 309 ? 0.61593 0.65552 0.74129 -0.08926 0.02346  -0.04825 309 ASP A CA  
2015 C C   . ASP A 309 ? 0.65020 0.70492 0.80173 -0.06132 0.03207  -0.04118 309 ASP A C   
2016 O O   . ASP A 309 ? 0.67938 0.70776 0.80688 -0.05113 0.04063  -0.04237 309 ASP A O   
2017 C CB  . ASP A 309 ? 0.66631 0.69201 0.74742 -0.11006 0.01745  -0.05703 309 ASP A CB  
2018 C CG  . ASP A 309 ? 0.65096 0.73664 0.75670 -0.11985 0.00538  -0.05922 309 ASP A CG  
2019 O OD1 . ASP A 309 ? 0.65973 0.77449 0.79804 -0.09913 0.00498  -0.05328 309 ASP A OD1 
2020 O OD2 . ASP A 309 ? 0.70567 0.81010 0.79875 -0.14878 -0.00492 -0.06660 309 ASP A OD2 
2021 N N   . VAL A 310 ? 0.57907 0.67206 0.77369 -0.05264 0.03149  -0.03490 310 VAL A N   
2022 C CA  . VAL A 310 ? 0.59899 0.70348 0.81267 -0.03156 0.03870  -0.02726 310 VAL A CA  
2023 C C   . VAL A 310 ? 0.67537 0.78708 0.87408 -0.03083 0.03325  -0.02903 310 VAL A C   
2024 O O   . VAL A 310 ? 0.68119 0.78493 0.87354 -0.01891 0.04020  -0.02415 310 VAL A O   
2025 C CB  . VAL A 310 ? 0.44653 0.58232 0.69935 -0.02809 0.03800  -0.02079 310 VAL A CB  
2026 N N   . ASN A 311 ? 0.62072 0.74850 0.81172 -0.04657 0.01940  -0.03523 311 ASN A N   
2027 C CA  . ASN A 311 ? 0.67939 0.81556 0.85550 -0.04909 0.00699  -0.03434 311 ASN A CA  
2028 C C   . ASN A 311 ? 0.75955 0.86474 0.88409 -0.06861 0.00425  -0.04045 311 ASN A C   
2029 O O   . ASN A 311 ? 0.77872 0.89841 0.89007 -0.08096 -0.01266 -0.04001 311 ASN A O   
2030 C CB  . ASN A 311 ? 0.61588 0.80427 0.83103 -0.05037 -0.00995 -0.03542 311 ASN A CB  
2031 C CG  . ASN A 311 ? 0.62127 0.82929 0.87723 -0.03152 -0.00575 -0.03082 311 ASN A CG  
2032 O OD1 . ASN A 311 ? 0.64694 0.83453 0.90273 -0.02316 0.00844  -0.02596 311 ASN A OD1 
2033 N ND2 . ASN A 311 ? 0.64920 0.89693 0.94071 -0.02455 -0.01801 -0.03255 311 ASN A ND2 
2034 N N   . ALA A 312 ? 0.80721 0.86730 0.90073 -0.07170 0.01915  -0.04558 312 ALA A N   
2035 C CA  . ALA A 312 ? 0.82457 0.84267 0.85927 -0.09238 0.01940  -0.05334 312 ALA A CA  
2036 C C   . ALA A 312 ? 0.89293 0.89651 0.89195 -0.09681 0.01707  -0.05150 312 ALA A C   
2037 O O   . ALA A 312 ? 0.91050 0.90923 0.91467 -0.07992 0.02705  -0.04677 312 ALA A O   
2038 C CB  . ALA A 312 ? 0.89229 0.85325 0.90012 -0.08519 0.03885  -0.05905 312 ALA A CB  
2039 N N   . SER A 313 ? 0.92559 0.92203 0.88372 -0.12472 0.00260  -0.05462 313 SER A N   
2040 C CA  . SER A 313 ? 1.01052 0.99404 0.92778 -0.13765 -0.00687 -0.05066 313 SER A CA  
2041 C C   . SER A 313 ? 1.13761 1.04739 0.97847 -0.15290 0.01327  -0.06134 313 SER A C   
2042 O O   . SER A 313 ? 1.20332 1.08371 1.00144 -0.17750 0.01171  -0.06933 313 SER A O   
2043 C CB  . SER A 313 ? 0.99867 1.02768 0.92202 -0.16092 -0.03952 -0.04535 313 SER A CB  
2044 N N   . ASP A 314 ? 1.22867 1.10637 1.04918 -0.14027 0.03435  -0.06313 314 ASP A N   
2045 C CA  . ASP A 314 ? 1.28004 1.08724 1.02491 -0.15529 0.05697  -0.07608 314 ASP A CA  
2046 C C   . ASP A 314 ? 1.30750 1.09813 0.98767 -0.19621 0.03530  -0.07387 314 ASP A C   
2047 O O   . ASP A 314 ? 1.26738 1.10697 0.96892 -0.20711 0.00209  -0.05996 314 ASP A O   
2048 C CB  . ASP A 314 ? 1.27432 1.06346 1.01480 -0.13763 0.08490  -0.07966 314 ASP A CB  
2049 C CG  . ASP A 314 ? 1.36537 1.08276 1.02559 -0.15469 0.11271  -0.09630 314 ASP A CG  
2050 O OD1 . ASP A 314 ? 1.40498 1.07452 1.03180 -0.15854 0.12628  -0.10963 314 ASP A OD1 
2051 O OD2 . ASP A 314 ? 1.39334 1.09641 1.01760 -0.16666 0.12137  -0.09673 314 ASP A OD2 
2052 N N   . LEU A 315 ? 1.28730 1.00675 0.88737 -0.21892 0.05363  -0.08781 315 LEU A N   
2053 C CA  . LEU A 315 ? 1.31094 1.00520 0.83602 -0.26424 0.03478  -0.08569 315 LEU A CA  
2054 C C   . LEU A 315 ? 1.30086 1.02026 0.82298 -0.27244 0.01458  -0.07065 315 LEU A C   
2055 O O   . LEU A 315 ? 1.30048 1.03974 0.80051 -0.30316 -0.02122 -0.05803 315 LEU A O   
2056 C CB  . LEU A 315 ? 1.34074 0.94044 0.77121 -0.28463 0.06693  -0.10567 315 LEU A CB  
2057 N N   . THR A 316 ? 1.28338 1.00325 0.82716 -0.24704 0.03422  -0.07034 316 THR A N   
2058 C CA  . THR A 316 ? 1.30023 1.03718 0.83905 -0.25357 0.01380  -0.05446 316 THR A CA  
2059 C C   . THR A 316 ? 1.26770 1.07904 0.89458 -0.22599 -0.01640 -0.03620 316 THR A C   
2060 O O   . THR A 316 ? 1.30851 1.12958 0.94030 -0.22132 -0.03030 -0.02286 316 THR A O   
2061 C CB  . THR A 316 ? 1.28153 0.97949 0.79099 -0.24672 0.05156  -0.06431 316 THR A CB  
2062 O OG1 . THR A 316 ? 1.29467 1.02212 0.87746 -0.20463 0.07622  -0.06942 316 THR A OG1 
2063 C CG2 . THR A 316 ? 1.31392 0.93541 0.73679 -0.27139 0.08741  -0.08667 316 THR A CG2 
2064 N N   . GLY A 317 ? 1.21450 1.07232 0.90466 -0.20982 -0.02570 -0.03635 317 GLY A N   
2065 C CA  . GLY A 317 ? 1.18344 1.10752 0.95764 -0.18160 -0.04621 -0.02403 317 GLY A CA  
2066 C C   . GLY A 317 ? 1.13507 1.06546 0.95364 -0.14747 -0.02169 -0.02520 317 GLY A C   
2067 O O   . GLY A 317 ? 1.09332 1.06946 0.97378 -0.12514 -0.03590 -0.01569 317 GLY A O   
2068 N N   . ILE A 318 ? 1.14262 1.03015 0.93245 -0.14330 0.01537  -0.03732 318 ILE A N   
2069 C CA  . ILE A 318 ? 1.09801 0.99779 0.93029 -0.11493 0.03831  -0.03765 318 ILE A CA  
2070 C C   . ILE A 318 ? 1.07606 1.00960 0.97415 -0.09176 0.04257  -0.03999 318 ILE A C   
2071 O O   . ILE A 318 ? 1.09971 1.01875 0.99093 -0.09593 0.04912  -0.04967 318 ILE A O   
2072 C CB  . ILE A 318 ? 1.08214 0.93589 0.87112 -0.11755 0.07793  -0.05188 318 ILE A CB  
2073 C CG1 . ILE A 318 ? 1.11402 0.93912 0.84124 -0.14184 0.07539  -0.04746 318 ILE A CG1 
2074 C CG2 . ILE A 318 ? 1.05591 0.93206 0.90076 -0.08737 0.10418  -0.05505 318 ILE A CG2 
2075 N N   . THR A 319 ? 0.98289 0.95479 0.93708 -0.07091 0.03788  -0.03068 319 THR A N   
2076 C CA  . THR A 319 ? 0.89148 0.89316 0.90382 -0.05240 0.04244  -0.03126 319 THR A CA  
2077 C C   . THR A 319 ? 0.86587 0.85970 0.89509 -0.03496 0.07182  -0.03461 319 THR A C   
2078 O O   . THR A 319 ? 0.88272 0.85968 0.88822 -0.03552 0.08922  -0.03633 319 THR A O   
2079 C CB  . THR A 319 ? 0.85401 0.90043 0.91476 -0.04248 0.02062  -0.02020 319 THR A CB  
2080 O OG1 . THR A 319 ? 0.87475 0.91885 0.93655 -0.03349 0.02462  -0.01150 319 THR A OG1 
2081 C CG2 . THR A 319 ? 0.87075 0.93510 0.92505 -0.05534 -0.01007 -0.01623 319 THR A CG2 
2082 N N   . PRO A 320 ? 0.80111 0.80891 0.87082 -0.02168 0.07753  -0.03553 320 PRO A N   
2083 C CA  . PRO A 320 ? 0.75912 0.77222 0.85731 -0.00337 0.09994  -0.03503 320 PRO A CA  
2084 C C   . PRO A 320 ? 0.71475 0.75223 0.82952 0.00026  0.10251  -0.02543 320 PRO A C   
2085 O O   . PRO A 320 ? 0.72685 0.76507 0.84389 0.00624  0.12484  -0.02763 320 PRO A O   
2086 C CB  . PRO A 320 ? 0.71918 0.74754 0.85746 0.00447  0.09271  -0.03179 320 PRO A CB  
2087 C CG  . PRO A 320 ? 0.77817 0.78705 0.88867 -0.01135 0.07908  -0.03846 320 PRO A CG  
2088 C CD  . PRO A 320 ? 0.79742 0.81264 0.88153 -0.02703 0.06439  -0.03774 320 PRO A CD  
2089 N N   . LEU A 321 ? 0.75008 0.80710 0.87607 -0.00364 0.08096  -0.01577 321 LEU A N   
2090 C CA  . LEU A 321 ? 0.72662 0.79287 0.85415 -0.00351 0.08046  -0.00606 321 LEU A CA  
2091 C C   . LEU A 321 ? 0.85260 0.89069 0.92704 -0.01664 0.08712  -0.00775 321 LEU A C   
2092 O O   . LEU A 321 ? 0.85604 0.89373 0.92192 -0.01993 0.10447  -0.00628 321 LEU A O   
2093 C CB  . LEU A 321 ? 0.67270 0.75494 0.81829 -0.00173 0.05529  0.00243  321 LEU A CB  
2094 C CG  . LEU A 321 ? 0.61967 0.69768 0.75688 -0.00203 0.05107  0.01327  321 LEU A CG  
2095 C CD1 . LEU A 321 ? 0.59968 0.69144 0.75824 -0.00015 0.07111  0.01661  321 LEU A CD1 
2096 C CD2 . LEU A 321 ? 0.70040 0.78752 0.85615 0.00540  0.02717  0.01900  321 LEU A CD2 
2097 N N   . HIS A 322 ? 0.80873 0.82392 0.84342 -0.02904 0.07301  -0.01066 322 HIS A N   
2098 C CA  . HIS A 322 ? 0.85035 0.83071 0.82282 -0.04814 0.07841  -0.01272 322 HIS A CA  
2099 C C   . HIS A 322 ? 0.86158 0.83013 0.82053 -0.04940 0.11726  -0.02596 322 HIS A C   
2100 O O   . HIS A 322 ? 0.90070 0.85535 0.82466 -0.06342 0.13153  -0.02672 322 HIS A O   
2101 C CB  . HIS A 322 ? 0.91636 0.87413 0.84819 -0.06436 0.05988  -0.01560 322 HIS A CB  
2102 C CG  . HIS A 322 ? 0.95712 0.92428 0.88826 -0.06829 0.02034  -0.00127 322 HIS A CG  
2103 N ND1 . HIS A 322 ? 0.94257 0.94482 0.91991 -0.05758 -0.00188 0.00152  322 HIS A ND1 
2104 C CD2 . HIS A 322 ? 0.99994 0.94595 0.89036 -0.08136 -0.00184 0.01085  322 HIS A CD2 
2105 C CE1 . HIS A 322 ? 0.94730 0.95598 0.92175 -0.05896 -0.03502 0.01394  322 HIS A CE1 
2106 N NE2 . HIS A 322 ? 0.97344 0.94464 0.89360 -0.07270 -0.03837 0.02146  322 HIS A NE2 
2107 N N   . ALA A 323 ? 0.84044 0.81346 0.82628 -0.03508 0.13486  -0.03717 323 ALA A N   
2108 C CA  . ALA A 323 ? 0.84264 0.81009 0.82947 -0.02801 0.17283  -0.05167 323 ALA A CA  
2109 C C   . ALA A 323 ? 0.88275 0.89187 0.91715 -0.01692 0.18704  -0.04576 323 ALA A C   
2110 O O   . ALA A 323 ? 0.87390 0.88640 0.89331 -0.02528 0.21301  -0.05259 323 ALA A O   
2111 C CB  . ALA A 323 ? 0.88781 0.84218 0.89150 -0.01151 0.18190  -0.06282 323 ALA A CB  
2112 N N   . ALA A 324 ? 0.79856 0.84084 0.88756 -0.00241 0.17138  -0.03379 324 ALA A N   
2113 C CA  . ALA A 324 ? 0.79887 0.88218 0.93188 0.00405  0.18202  -0.02630 324 ALA A CA  
2114 C C   . ALA A 324 ? 0.83676 0.92024 0.93882 -0.01680 0.17986  -0.01800 324 ALA A C   
2115 O O   . ALA A 324 ? 0.84581 0.95571 0.96101 -0.02208 0.19973  -0.01765 324 ALA A O   
2116 C CB  . ALA A 324 ? 0.76663 0.87609 0.95093 0.01647  0.16235  -0.01409 324 ALA A CB  
2117 N N   . ALA A 325 ? 0.86954 0.92403 0.93023 -0.02964 0.15436  -0.01057 325 ALA A N   
2118 C CA  . ALA A 325 ? 0.84659 0.88668 0.86706 -0.04981 0.14765  -0.00092 325 ALA A CA  
2119 C C   . ALA A 325 ? 0.86872 0.89055 0.83863 -0.07153 0.17440  -0.01181 325 ALA A C   
2120 O O   . ALA A 325 ? 0.88839 0.91997 0.84563 -0.08782 0.18913  -0.00940 325 ALA A O   
2121 C CB  . ALA A 325 ? 0.82512 0.83561 0.81598 -0.05355 0.11082  0.00990  325 ALA A CB  
2122 N N   . ALA A 326 ? 0.86782 0.86154 0.80337 -0.07634 0.18295  -0.02516 326 ALA A N   
2123 C CA  . ALA A 326 ? 0.94862 0.91929 0.82808 -0.10096 0.21202  -0.03889 326 ALA A CA  
2124 C C   . ALA A 326 ? 0.92154 0.93333 0.84370 -0.09136 0.25587  -0.05457 326 ALA A C   
2125 O O   . ALA A 326 ? 0.95706 0.97512 0.85285 -0.11381 0.28196  -0.06160 326 ALA A O   
2126 C CB  . ALA A 326 ? 0.93338 0.85869 0.76069 -0.11085 0.21087  -0.05016 326 ALA A CB  
2127 N N   . THR A 327 ? 0.86310 0.90476 0.85181 -0.05915 0.26346  -0.05991 327 THR A N   
2128 C CA  . THR A 327 ? 0.86362 0.95144 0.90703 -0.04268 0.30038  -0.07286 327 THR A CA  
2129 C C   . THR A 327 ? 0.89537 1.03956 0.98707 -0.04421 0.29883  -0.05873 327 THR A C   
2130 O O   . THR A 327 ? 0.87604 1.07188 1.02166 -0.03231 0.32654  -0.06671 327 THR A O   
2131 C CB  . THR A 327 ? 0.83533 0.92688 0.92887 -0.00684 0.30306  -0.08041 327 THR A CB  
2132 O OG1 . THR A 327 ? 0.84001 0.94278 0.97063 0.00663  0.26701  -0.06125 327 THR A OG1 
2133 C CG2 . THR A 327 ? 0.84946 0.88003 0.88625 -0.01026 0.30881  -0.09645 327 THR A CG2 
2134 N N   . GLY A 328 ? 0.98775 1.12322 1.06171 -0.05850 0.26726  -0.03835 328 GLY A N   
2135 C CA  . GLY A 328 ? 0.96327 1.13983 1.06431 -0.06862 0.26579  -0.02485 328 GLY A CA  
2136 C C   . GLY A 328 ? 0.90481 1.13179 1.08655 -0.04387 0.25939  -0.01599 328 GLY A C   
2137 O O   . GLY A 328 ? 0.91279 1.18785 1.12724 -0.05247 0.26804  -0.00898 328 GLY A O   
2138 N N   . HIS A 329 ? 0.79105 1.00755 1.00139 -0.01782 0.24298  -0.01515 329 HIS A N   
2139 C CA  . HIS A 329 ? 0.72088 0.97648 0.99973 0.00238  0.23274  -0.00506 329 HIS A CA  
2140 C C   . HIS A 329 ? 0.68030 0.92312 0.95095 -0.00689 0.20065  0.01297  329 HIS A C   
2141 O O   . HIS A 329 ? 0.65415 0.87019 0.92074 0.00243  0.17960  0.01489  329 HIS A O   
2142 C CB  . HIS A 329 ? 0.70272 0.94653 1.00846 0.03157  0.23382  -0.01469 329 HIS A CB  
2143 C CG  . HIS A 329 ? 0.70326 0.95577 1.02002 0.04533  0.26883  -0.03485 329 HIS A CG  
2144 N ND1 . HIS A 329 ? 0.73677 0.93970 1.00906 0.04882  0.28144  -0.05303 329 HIS A ND1 
2145 C CD2 . HIS A 329 ? 0.67201 0.97884 1.04028 0.05609  0.29584  -0.04125 329 HIS A CD2 
2146 C CE1 . HIS A 329 ? 0.73572 0.95545 1.02815 0.06246  0.31742  -0.07165 329 HIS A CE1 
2147 N NE2 . HIS A 329 ? 0.69660 0.98381 1.05247 0.06918  0.32700  -0.06531 329 HIS A NE2 
2148 N N   . LEU A 330 ? 0.62837 0.89004 0.89400 -0.02772 0.19928  0.02466  330 LEU A N   
2149 C CA  . LEU A 330 ? 0.60907 0.84895 0.85660 -0.03818 0.17337  0.03906  330 LEU A CA  
2150 C C   . LEU A 330 ? 0.54313 0.79956 0.83745 -0.02453 0.15746  0.04691  330 LEU A C   
2151 O O   . LEU A 330 ? 0.54345 0.77200 0.82590 -0.02235 0.13760  0.04993  330 LEU A O   
2152 C CB  . LEU A 330 ? 0.61621 0.86536 0.84035 -0.06679 0.17758  0.04935  330 LEU A CB  
2153 N N   . GLU A 331 ? 0.50368 0.80650 0.85183 -0.01618 0.16540  0.05020  331 GLU A N   
2154 C CA  . GLU A 331 ? 0.46748 0.78089 0.85288 -0.00812 0.14745  0.05989  331 GLU A CA  
2155 C C   . GLU A 331 ? 0.57685 0.85396 0.95464 0.00864  0.13593  0.05136  331 GLU A C   
2156 O O   . GLU A 331 ? 0.52777 0.78927 0.90266 0.00412  0.11781  0.05639  331 GLU A O   
2157 C CB  . GLU A 331 ? 0.40872 0.77705 0.85500 0.00167  0.15427  0.06607  331 GLU A CB  
2158 N N   . ILE A 332 ? 0.59919 0.86102 0.96843 0.02397  0.14818  0.03694  332 ILE A N   
2159 C CA  . ILE A 332 ? 0.57493 0.79922 0.92647 0.03351  0.13765  0.02824  332 ILE A CA  
2160 C C   . ILE A 332 ? 0.57033 0.76630 0.88118 0.02080  0.12389  0.02719  332 ILE A C   
2161 O O   . ILE A 332 ? 0.54086 0.72139 0.84809 0.02097  0.10826  0.02553  332 ILE A O   
2162 C CB  . ILE A 332 ? 0.61345 0.82104 0.95508 0.04865  0.15618  0.01229  332 ILE A CB  
2163 C CG1 . ILE A 332 ? 0.57461 0.81359 0.96663 0.06847  0.17047  0.01217  332 ILE A CG1 
2164 C CG2 . ILE A 332 ? 0.68397 0.84988 0.99972 0.05257  0.14439  0.00401  332 ILE A CG2 
2165 N N   . VAL A 333 ? 0.61932 0.80898 0.89964 0.00918  0.12875  0.02822  333 VAL A N   
2166 C CA  . VAL A 333 ? 0.59972 0.76169 0.84517 0.00165  0.11232  0.02940  333 VAL A CA  
2167 C C   . VAL A 333 ? 0.55649 0.72335 0.81862 -0.00161 0.09721  0.03752  333 VAL A C   
2168 O O   . VAL A 333 ? 0.51031 0.66573 0.77056 0.00186  0.08283  0.03381  333 VAL A O   
2169 C CB  . VAL A 333 ? 0.59210 0.73843 0.79568 -0.01207 0.11807  0.03190  333 VAL A CB  
2170 C CG1 . VAL A 333 ? 0.64125 0.75895 0.81655 -0.01627 0.09646  0.03812  333 VAL A CG1 
2171 C CG2 . VAL A 333 ? 0.66151 0.79134 0.83423 -0.01351 0.13121  0.02057  333 VAL A CG2 
2172 N N   . GLU A 334 ? 0.49888 0.68490 0.77671 -0.01091 0.10174  0.04763  334 GLU A N   
2173 C CA  . GLU A 334 ? 0.51959 0.70483 0.80637 -0.01850 0.09096  0.05404  334 GLU A CA  
2174 C C   . GLU A 334 ? 0.49930 0.69149 0.81250 -0.01309 0.08333  0.04996  334 GLU A C   
2175 O O   . GLU A 334 ? 0.50861 0.69113 0.82015 -0.01665 0.07454  0.04660  334 GLU A O   
2176 C CB  . GLU A 334 ? 0.49629 0.70128 0.79050 -0.03532 0.09698  0.06684  334 GLU A CB  
2177 N N   . VAL A 335 ? 0.52204 0.72798 0.85734 -0.00493 0.08742  0.04903  335 VAL A N   
2178 C CA  . VAL A 335 ? 0.51745 0.72060 0.86787 -0.00375 0.07803  0.04675  335 VAL A CA  
2179 C C   . VAL A 335 ? 0.52100 0.70475 0.85318 -0.00092 0.07165  0.03355  335 VAL A C   
2180 O O   . VAL A 335 ? 0.53179 0.71338 0.86558 -0.01002 0.06319  0.02984  335 VAL A O   
2181 C CB  . VAL A 335 ? 0.49954 0.71195 0.87356 0.00850  0.08186  0.04933  335 VAL A CB  
2182 C CG1 . VAL A 335 ? 0.50322 0.69558 0.87605 0.00914  0.07034  0.04527  335 VAL A CG1 
2183 C CG2 . VAL A 335 ? 0.47979 0.72343 0.88432 0.00335  0.08178  0.06498  335 VAL A CG2 
2184 N N   . LEU A 336 ? 0.48340 0.65551 0.79689 0.00817  0.07623  0.02573  336 LEU A N   
2185 C CA  . LEU A 336 ? 0.50492 0.66433 0.80125 0.00765  0.06749  0.01497  336 LEU A CA  
2186 C C   . LEU A 336 ? 0.50016 0.66552 0.79717 0.00367  0.05769  0.01395  336 LEU A C   
2187 O O   . LEU A 336 ? 0.52678 0.69943 0.83151 -0.00116 0.04975  0.00633  336 LEU A O   
2188 C CB  . LEU A 336 ? 0.51295 0.65553 0.78127 0.01302  0.07324  0.00896  336 LEU A CB  
2189 C CG  . LEU A 336 ? 0.52607 0.65719 0.79250 0.02074  0.08716  0.00476  336 LEU A CG  
2190 C CD1 . LEU A 336 ? 0.59650 0.70882 0.82892 0.02167  0.09886  -0.00248 336 LEU A CD1 
2191 C CD2 . LEU A 336 ? 0.52704 0.64227 0.79073 0.01883  0.07996  -0.00142 336 LEU A CD2 
2192 N N   . LEU A 337 ? 0.49595 0.65747 0.78462 0.00527  0.05911  0.02065  337 LEU A N   
2193 C CA  . LEU A 337 ? 0.53850 0.69820 0.82872 0.00653  0.05059  0.01948  337 LEU A CA  
2194 C C   . LEU A 337 ? 0.53935 0.71001 0.85050 -0.00257 0.05301  0.01751  337 LEU A C   
2195 O O   . LEU A 337 ? 0.52893 0.70627 0.85129 -0.00134 0.04882  0.00834  337 LEU A O   
2196 C CB  . LEU A 337 ? 0.54834 0.68859 0.81501 0.00736  0.05131  0.02858  337 LEU A CB  
2197 C CG  . LEU A 337 ? 0.57625 0.69887 0.81127 0.01024  0.04798  0.03067  337 LEU A CG  
2198 C CD1 . LEU A 337 ? 0.63493 0.73667 0.84063 0.00228  0.05251  0.04097  337 LEU A CD1 
2199 C CD2 . LEU A 337 ? 0.61073 0.72674 0.84002 0.01986  0.02903  0.02620  337 LEU A CD2 
2200 N N   . LYS A 338 ? 0.50344 0.67820 0.82082 -0.01310 0.05982  0.02566  338 LYS A N   
2201 C CA  . LYS A 338 ? 0.50537 0.68502 0.83341 -0.02866 0.06071  0.02547  338 LYS A CA  
2202 C C   . LYS A 338 ? 0.47636 0.66370 0.81334 -0.03497 0.05655  0.01473  338 LYS A C   
2203 O O   . LYS A 338 ? 0.45841 0.65013 0.79967 -0.04734 0.05802  0.00605  338 LYS A O   
2204 C CB  . LYS A 338 ? 0.52417 0.70869 0.85652 -0.04024 0.06339  0.04041  338 LYS A CB  
2205 C CG  . LYS A 338 ? 0.55339 0.73698 0.88671 -0.06309 0.06199  0.04422  338 LYS A CG  
2206 C CD  . LYS A 338 ? 0.57544 0.77094 0.91922 -0.07303 0.05814  0.06214  338 LYS A CD  
2207 C CE  . LYS A 338 ? 0.50363 0.69495 0.83523 -0.09949 0.05818  0.07227  338 LYS A CE  
2208 N NZ  . LYS A 338 ? 0.41996 0.63142 0.76756 -0.11140 0.04936  0.09241  338 LYS A NZ  
2209 N N   . HIS A 339 ? 0.48372 0.66948 0.81870 -0.02950 0.05332  0.01367  339 HIS A N   
2210 C CA  . HIS A 339 ? 0.53128 0.71681 0.86402 -0.03981 0.04828  0.00420  339 HIS A CA  
2211 C C   . HIS A 339 ? 0.55703 0.75235 0.88730 -0.03492 0.04428  -0.00911 339 HIS A C   
2212 O O   . HIS A 339 ? 0.60300 0.79557 0.92331 -0.04370 0.03987  -0.01629 339 HIS A O   
2213 C CB  . HIS A 339 ? 0.50967 0.67836 0.83539 -0.03777 0.04579  0.01055  339 HIS A CB  
2214 C CG  . HIS A 339 ? 0.52536 0.69161 0.86103 -0.04378 0.04382  0.02516  339 HIS A CG  
2215 N ND1 . HIS A 339 ? 0.54956 0.72708 0.89865 -0.03525 0.04875  0.03731  339 HIS A ND1 
2216 C CD2 . HIS A 339 ? 0.49050 0.64541 0.82287 -0.06069 0.03478  0.03114  339 HIS A CD2 
2217 C CE1 . HIS A 339 ? 0.54353 0.72294 0.90319 -0.04505 0.04189  0.05077  339 HIS A CE1 
2218 N NE2 . HIS A 339 ? 0.52672 0.68901 0.87481 -0.05993 0.03202  0.04816  339 HIS A NE2 
2219 N N   . GLY A 340 ? 0.60408 0.80866 0.94082 -0.02249 0.04330  -0.01116 340 GLY A N   
2220 C CA  . GLY A 340 ? 0.60040 0.82207 0.94261 -0.01701 0.03480  -0.02134 340 GLY A CA  
2221 C C   . GLY A 340 ? 0.60136 0.81049 0.92176 -0.00976 0.02792  -0.01822 340 GLY A C   
2222 O O   . GLY A 340 ? 0.63001 0.83367 0.93564 -0.01977 0.02593  -0.02281 340 GLY A O   
2223 N N   . ALA A 341 ? 0.65027 0.84788 0.96031 0.00386  0.02451  -0.01070 341 ALA A N   
2224 C CA  . ALA A 341 ? 0.69152 0.87301 0.97282 0.00637  0.01823  -0.00796 341 ALA A CA  
2225 C C   . ALA A 341 ? 0.71880 0.90388 0.99948 0.01686  0.00130  -0.00468 341 ALA A C   
2226 O O   . ALA A 341 ? 0.72052 0.90120 1.01020 0.02759  -0.00016 0.00021  341 ALA A O   
2227 C CB  . ALA A 341 ? 0.69914 0.85466 0.95718 0.00806  0.03164  -0.00031 341 ALA A CB  
2228 N N   . ASP A 342 ? 0.74625 0.93463 1.01241 0.01273  -0.01354 -0.00624 342 ASP A N   
2229 C CA  . ASP A 342 ? 0.78457 0.97684 1.05089 0.02298  -0.03656 -0.00029 342 ASP A CA  
2230 C C   . ASP A 342 ? 0.85624 1.00558 1.08066 0.02523  -0.03695 0.01214  342 ASP A C   
2231 O O   . ASP A 342 ? 0.93125 1.05585 1.11304 0.01265  -0.03586 0.01480  342 ASP A O   
2232 C CB  . ASP A 342 ? 0.86190 1.07237 1.12122 0.01178  -0.05519 -0.00325 342 ASP A CB  
2233 C CG  . ASP A 342 ? 0.93682 1.16045 1.20696 0.02430  -0.08549 0.00497  342 ASP A CG  
2234 O OD1 . ASP A 342 ? 0.92206 1.13253 1.20150 0.04412  -0.09133 0.01220  342 ASP A OD1 
2235 O OD2 . ASP A 342 ? 1.00880 1.25339 1.27598 0.01363  -0.10566 0.00529  342 ASP A OD2 
2236 N N   . VAL A 343 ? 0.74799 0.88445 0.97842 0.03761  -0.03646 0.01845  343 VAL A N   
2237 C CA  . VAL A 343 ? 0.79994 0.89350 0.98490 0.03499  -0.03843 0.03061  343 VAL A CA  
2238 C C   . VAL A 343 ? 0.85296 0.92754 1.00656 0.03437  -0.06723 0.03955  343 VAL A C   
2239 O O   . VAL A 343 ? 0.92774 0.96269 1.02745 0.02149  -0.06882 0.04833  343 VAL A O   
2240 C CB  . VAL A 343 ? 0.76839 0.84670 0.96096 0.04536  -0.03413 0.03539  343 VAL A CB  
2241 C CG1 . VAL A 343 ? 0.75948 0.84962 0.98635 0.06771  -0.05371 0.03338  343 VAL A CG1 
2242 C CG2 . VAL A 343 ? 0.87440 0.90533 1.01224 0.03561  -0.03370 0.04794  343 VAL A CG2 
2243 N N   . ASN A 344 ? 0.80640 0.91153 0.99179 0.04461  -0.09066 0.03759  344 ASN A N   
2244 C CA  . ASN A 344 ? 0.81835 0.91136 0.98067 0.04483  -0.12525 0.04915  344 ASN A CA  
2245 C C   . ASN A 344 ? 0.81814 0.93536 0.97390 0.02624  -0.13430 0.04479  344 ASN A C   
2246 O O   . ASN A 344 ? 0.79727 0.93186 0.96066 0.02829  -0.16717 0.05191  344 ASN A O   
2247 C CB  . ASN A 344 ? 0.75151 0.86158 0.95840 0.07457  -0.15178 0.05355  344 ASN A CB  
2248 C CG  . ASN A 344 ? 0.79885 0.86567 0.99320 0.09021  -0.14735 0.05999  344 ASN A CG  
2249 O OD1 . ASN A 344 ? 0.82324 0.85153 0.97366 0.07468  -0.12686 0.06312  344 ASN A OD1 
2250 N ND2 . ASN A 344 ? 0.81849 0.89137 1.05093 0.12064  -0.16617 0.06134  344 ASN A ND2 
2251 N N   . ALA A 345 ? 0.83024 0.94693 0.97064 0.00779  -0.10710 0.03384  345 ALA A N   
2252 C CA  . ALA A 345 ? 0.82686 0.95080 0.94438 -0.01472 -0.11297 0.02919  345 ALA A CA  
2253 C C   . ALA A 345 ? 0.90420 0.98000 0.94927 -0.03531 -0.12509 0.03963  345 ALA A C   
2254 O O   . ALA A 345 ? 0.96673 1.00173 0.97550 -0.03556 -0.12089 0.04778  345 ALA A O   
2255 C CB  . ALA A 345 ? 0.85817 0.98195 0.97349 -0.02604 -0.08040 0.01428  345 ALA A CB  
2256 N N   . TYR A 346 ? 0.89548 0.97404 0.91310 -0.05802 -0.13992 0.03906  346 TYR A N   
2257 C CA  . TYR A 346 ? 1.00473 1.03564 0.94605 -0.08434 -0.15377 0.04871  346 TYR A CA  
2258 C C   . TYR A 346 ? 1.08310 1.09587 0.97737 -0.11527 -0.13724 0.03641  346 TYR A C   
2259 O O   . TYR A 346 ? 1.06819 1.11562 0.98826 -0.12115 -0.14082 0.02856  346 TYR A O   
2260 C CB  . TYR A 346 ? 1.01627 1.06103 0.96144 -0.08316 -0.20464 0.06776  346 TYR A CB  
2261 N N   . ASP A 347 ? 1.18527 1.14050 1.00661 -0.13692 -0.11681 0.03315  347 ASP A N   
2262 C CA  . ASP A 347 ? 1.25673 1.17858 1.01972 -0.16692 -0.09752 0.01971  347 ASP A CA  
2263 C C   . ASP A 347 ? 1.32134 1.23338 1.03405 -0.20019 -0.13543 0.03110  347 ASP A C   
2264 O O   . ASP A 347 ? 1.33086 1.27495 1.07075 -0.19446 -0.17865 0.04930  347 ASP A O   
2265 C CB  . ASP A 347 ? 1.28570 1.15405 0.99556 -0.17536 -0.05608 0.00828  347 ASP A CB  
2266 C CG  . ASP A 347 ? 1.35199 1.18099 1.00195 -0.19378 -0.06767 0.02089  347 ASP A CG  
2267 O OD1 . ASP A 347 ? 1.37684 1.21585 1.03100 -0.19341 -0.11084 0.04140  347 ASP A OD1 
2268 O OD2 . ASP A 347 ? 1.35918 1.14506 0.95520 -0.20988 -0.03335 0.00960  347 ASP A OD2 
2269 N N   . ASN A 348 ? 1.38440 1.25014 1.02192 -0.23558 -0.12033 0.02064  348 ASN A N   
2270 C CA  . ASN A 348 ? 1.40180 1.25416 0.98141 -0.27498 -0.15650 0.03209  348 ASN A CA  
2271 C C   . ASN A 348 ? 1.37572 1.19128 0.89953 -0.29211 -0.18210 0.05103  348 ASN A C   
2272 O O   . ASN A 348 ? 1.38100 1.19654 0.87116 -0.31958 -0.22616 0.06854  348 ASN A O   
2273 C CB  . ASN A 348 ? 1.46019 1.26108 0.96253 -0.31215 -0.13011 0.01404  348 ASN A CB  
2274 C CG  . ASN A 348 ? 1.47495 1.30355 1.01816 -0.30342 -0.11515 -0.00099 348 ASN A CG  
2275 O OD1 . ASN A 348 ? 1.36893 1.25618 0.99901 -0.27009 -0.11889 -0.00006 348 ASN A OD1 
2276 N ND2 . ASN A 348 ? 1.56333 1.34278 1.03599 -0.33677 -0.09779 -0.01539 348 ASN A ND2 
2277 N N   . ASP A 349 ? 1.34847 1.13281 0.85900 -0.27989 -0.15777 0.04914  349 ASP A N   
2278 C CA  . ASP A 349 ? 1.34117 1.08414 0.79362 -0.29780 -0.18150 0.06759  349 ASP A CA  
2279 C C   . ASP A 349 ? 1.35010 1.12554 0.86671 -0.26080 -0.21356 0.08748  349 ASP A C   
2280 O O   . ASP A 349 ? 1.35610 1.09007 0.82686 -0.26989 -0.22865 0.10223  349 ASP A O   
2281 C CB  . ASP A 349 ? 1.35543 1.03749 0.73805 -0.31709 -0.13252 0.05151  349 ASP A CB  
2282 C CG  . ASP A 349 ? 1.42686 1.06951 0.74648 -0.34826 -0.09415 0.02764  349 ASP A CG  
2283 O OD1 . ASP A 349 ? 1.42806 1.07958 0.74052 -0.36345 -0.11145 0.02717  349 ASP A OD1 
2284 O OD2 . ASP A 349 ? 1.45156 1.05437 0.72846 -0.35816 -0.04543 0.00820  349 ASP A OD2 
2285 N N   . GLY A 350 ? 1.42476 1.26709 1.03981 -0.22167 -0.22260 0.08697  350 GLY A N   
2286 C CA  . GLY A 350 ? 1.40813 1.27784 1.08479 -0.18409 -0.25050 0.10286  350 GLY A CA  
2287 C C   . GLY A 350 ? 1.40007 1.24584 1.08092 -0.16511 -0.21942 0.09850  350 GLY A C   
2288 O O   . GLY A 350 ? 1.47665 1.30656 1.16009 -0.14974 -0.24453 0.11538  350 GLY A O   
2289 N N   . HIS A 351 ? 1.23051 1.07259 0.91201 -0.16583 -0.16716 0.07706  351 HIS A N   
2290 C CA  . HIS A 351 ? 1.18321 1.00999 0.86856 -0.15356 -0.13563 0.07247  351 HIS A CA  
2291 C C   . HIS A 351 ? 1.13007 1.00977 0.90660 -0.11558 -0.11847 0.06369  351 HIS A C   
2292 O O   . HIS A 351 ? 1.12141 1.03145 0.93338 -0.10986 -0.09685 0.04818  351 HIS A O   
2293 C CB  . HIS A 351 ? 1.18427 0.97416 0.80973 -0.18092 -0.08867 0.05504  351 HIS A CB  
2294 C CG  . HIS A 351 ? 1.33891 1.06693 0.86313 -0.22328 -0.09830 0.06246  351 HIS A CG  
2295 N ND1 . HIS A 351 ? 1.39238 1.09246 0.85444 -0.25758 -0.10280 0.05819  351 HIS A ND1 
2296 C CD2 . HIS A 351 ? 1.35390 1.03709 0.81954 -0.24218 -0.10479 0.07407  351 HIS A CD2 
2297 C CE1 . HIS A 351 ? 1.40144 1.04300 0.77149 -0.29612 -0.11121 0.06664  351 HIS A CE1 
2298 N NE2 . HIS A 351 ? 1.36548 0.99556 0.73549 -0.28785 -0.11298 0.07653  351 HIS A NE2 
2299 N N   . THR A 352 ? 1.10426 0.98698 0.90995 -0.09307 -0.12857 0.07385  352 THR A N   
2300 C CA  . THR A 352 ? 0.96420 0.88678 0.84321 -0.06305 -0.11018 0.06623  352 THR A CA  
2301 C C   . THR A 352 ? 0.96469 0.87930 0.83481 -0.06948 -0.06456 0.05440  352 THR A C   
2302 O O   . THR A 352 ? 0.98672 0.86448 0.79591 -0.09394 -0.04853 0.05316  352 THR A O   
2303 C CB  . THR A 352 ? 0.94436 0.86343 0.84816 -0.03900 -0.13700 0.08066  352 THR A CB  
2304 N N   . PRO A 353 ? 0.98289 0.93495 0.91413 -0.04973 -0.04302 0.04519  353 PRO A N   
2305 C CA  . PRO A 353 ? 0.95380 0.90701 0.88702 -0.05295 -0.00455 0.03712  353 PRO A CA  
2306 C C   . PRO A 353 ? 0.93880 0.86098 0.83136 -0.06505 -0.00132 0.04681  353 PRO A C   
2307 O O   . PRO A 353 ? 0.93212 0.84677 0.79860 -0.08160 0.02878  0.04001  353 PRO A O   
2308 C CB  . PRO A 353 ? 0.89390 0.88930 0.89869 -0.02992 0.00302  0.03286  353 PRO A CB  
2309 C CG  . PRO A 353 ? 0.88903 0.90726 0.92197 -0.02205 -0.01711 0.02935  353 PRO A CG  
2310 C CD  . PRO A 353 ? 0.94799 0.94581 0.94706 -0.02823 -0.05153 0.04053  353 PRO A CD  
2311 N N   . LEU A 354 ? 0.96132 0.86448 0.84725 -0.05743 -0.03123 0.06172  354 LEU A N   
2312 C CA  . LEU A 354 ? 1.02593 0.88626 0.85855 -0.07360 -0.03319 0.07290  354 LEU A CA  
2313 C C   . LEU A 354 ? 1.07548 0.89188 0.82641 -0.10739 -0.03396 0.07507  354 LEU A C   
2314 O O   . LEU A 354 ? 1.08663 0.88312 0.79275 -0.13285 -0.01044 0.07306  354 LEU A O   
2315 C CB  . LEU A 354 ? 0.99041 0.82725 0.82731 -0.05495 -0.06936 0.08840  354 LEU A CB  
2316 C CG  . LEU A 354 ? 1.00949 0.78900 0.78370 -0.07139 -0.07659 0.10211  354 LEU A CG  
2317 N N   . HIS A 355 ? 1.07783 0.88019 0.80567 -0.11235 -0.06060 0.07891  355 HIS A N   
2318 C CA  . HIS A 355 ? 1.10405 0.85984 0.74590 -0.15010 -0.06172 0.08048  355 HIS A CA  
2319 C C   . HIS A 355 ? 1.10400 0.87106 0.73218 -0.16955 -0.01040 0.05883  355 HIS A C   
2320 O O   . HIS A 355 ? 1.13734 0.87298 0.70247 -0.20156 0.01004  0.05567  355 HIS A O   
2321 C CB  . HIS A 355 ? 1.12809 0.87583 0.75419 -0.15392 -0.09837 0.08752  355 HIS A CB  
2322 C CG  . HIS A 355 ? 1.09635 0.87233 0.78473 -0.11909 -0.13866 0.09950  355 HIS A CG  
2323 N N   . LEU A 356 ? 1.09176 0.90252 0.77823 -0.15050 0.01170  0.04281  356 LEU A N   
2324 C CA  . LEU A 356 ? 1.04634 0.86893 0.73122 -0.15971 0.06060  0.02119  356 LEU A CA  
2325 C C   . LEU A 356 ? 1.07991 0.92271 0.78342 -0.16004 0.09064  0.01821  356 LEU A C   
2326 O O   . LEU A 356 ? 1.12023 0.95884 0.79280 -0.18154 0.12708  0.00470  356 LEU A O   
2327 C CB  . LEU A 356 ? 1.00080 0.85912 0.74566 -0.13509 0.07235  0.00785  356 LEU A CB  
2328 C CG  . LEU A 356 ? 1.02753 0.87353 0.75687 -0.13869 0.04269  0.01046  356 LEU A CG  
2329 N N   . ALA A 357 ? 1.01670 0.88332 0.76947 -0.13906 0.07725  0.02964  357 ALA A N   
2330 C CA  . ALA A 357 ? 1.00942 0.89453 0.77376 -0.14544 0.10074  0.03006  357 ALA A CA  
2331 C C   . ALA A 357 ? 1.13902 0.97739 0.81896 -0.18384 0.10000  0.03704  357 ALA A C   
2332 O O   . ALA A 357 ? 1.17902 1.02805 0.83873 -0.20755 0.13610  0.02589  357 ALA A O   
2333 C CB  . ALA A 357 ? 0.97405 0.88114 0.79293 -0.12114 0.08294  0.04207  357 ALA A CB  
2334 N N   . ALA A 358 ? 1.20467 0.99077 0.83363 -0.19139 0.05842  0.05524  358 ALA A N   
2335 C CA  . ALA A 358 ? 1.28050 1.00899 0.81775 -0.23090 0.05076  0.06542  358 ALA A CA  
2336 C C   . ALA A 358 ? 1.29817 1.00480 0.76822 -0.26933 0.07614  0.05142  358 ALA A C   
2337 O O   . ALA A 358 ? 1.32301 1.00203 0.72588 -0.30952 0.09298  0.05027  358 ALA A O   
2338 C CB  . ALA A 358 ? 1.29575 0.96743 0.79447 -0.22550 -0.00507 0.08929  358 ALA A CB  
2339 N N   . LYS A 359 ? 1.31132 1.02623 0.79177 -0.26184 0.08099  0.03944  359 LYS A N   
2340 C CA  . LYS A 359 ? 1.34324 1.03200 0.75559 -0.29927 0.10951  0.02277  359 LYS A CA  
2341 C C   . LYS A 359 ? 1.34949 1.07990 0.78300 -0.30877 0.17012  -0.00160 359 LYS A C   
2342 O O   . LYS A 359 ? 1.40346 1.10869 0.76670 -0.35084 0.19858  -0.01387 359 LYS A O   
2343 C CB  . LYS A 359 ? 1.31326 0.99991 0.73285 -0.28861 0.10323  0.01416  359 LYS A CB  
2344 N N   . TYR A 360 ? 1.19181 0.98783 0.72163 -0.27184 0.19014  -0.00895 360 TYR A N   
2345 C CA  . TYR A 360 ? 1.13554 0.98462 0.70432 -0.27341 0.24384  -0.03025 360 TYR A CA  
2346 C C   . TYR A 360 ? 1.11472 0.99910 0.71407 -0.27609 0.24606  -0.01920 360 TYR A C   
2347 O O   . TYR A 360 ? 1.09508 1.04506 0.76384 -0.26171 0.27861  -0.03038 360 TYR A O   
2348 C CB  . TYR A 360 ? 1.07012 0.96591 0.72236 -0.23195 0.26579  -0.04723 360 TYR A CB  
2349 C CG  . TYR A 360 ? 1.12976 0.98634 0.74658 -0.23220 0.26605  -0.05955 360 TYR A CG  
2350 C CD1 . TYR A 360 ? 1.14101 0.97882 0.71065 -0.25554 0.30868  -0.08510 360 TYR A CD1 
2351 C CD2 . TYR A 360 ? 1.12365 0.96240 0.75146 -0.21239 0.22584  -0.04718 360 TYR A CD2 
2352 C CE1 . TYR A 360 ? 1.15359 0.94719 0.68034 -0.26059 0.30958  -0.09666 360 TYR A CE1 
2353 C CE2 . TYR A 360 ? 1.15231 0.95483 0.74174 -0.21870 0.22473  -0.05744 360 TYR A CE2 
2354 C CZ  . TYR A 360 ? 1.14822 0.92399 0.68349 -0.24351 0.26590  -0.08153 360 TYR A CZ  
2355 O OH  . TYR A 360 ? 1.19213 0.92404 0.67964 -0.25411 0.26555  -0.09207 360 TYR A OH  
2356 N N   . GLY A 361 ? 1.11976 0.95873 0.66545 -0.29539 0.21039  0.00339  361 GLY A N   
2357 C CA  . GLY A 361 ? 1.10520 0.96567 0.66789 -0.30176 0.20947  0.01515  361 GLY A CA  
2358 C C   . GLY A 361 ? 1.16598 1.06555 0.81740 -0.25712 0.19148  0.02484  361 GLY A C   
2359 O O   . GLY A 361 ? 1.19028 1.05592 0.84066 -0.23710 0.15082  0.04054  361 GLY A O   
2360 N N   . HIS A 362 ? 1.14549 1.11778 0.87425 -0.24242 0.22139  0.01529  362 HIS A N   
2361 C CA  . HIS A 362 ? 1.07681 1.09015 0.88951 -0.20484 0.20890  0.02265  362 HIS A CA  
2362 C C   . HIS A 362 ? 1.07725 1.04957 0.86869 -0.20261 0.16974  0.04444  362 HIS A C   
2363 O O   . HIS A 362 ? 1.05028 1.01847 0.87841 -0.17137 0.14480  0.05060  362 HIS A O   
2364 C CB  . HIS A 362 ? 1.00828 1.03478 0.87190 -0.16725 0.20544  0.01331  362 HIS A CB  
2365 C CG  . HIS A 362 ? 0.99145 1.04355 0.86950 -0.16520 0.24346  -0.00962 362 HIS A CG  
2366 N ND1 . HIS A 362 ? 0.97491 1.09036 0.90621 -0.16237 0.28055  -0.02166 362 HIS A ND1 
2367 C CD2 . HIS A 362 ? 1.02533 1.04736 0.87276 -0.16428 0.25061  -0.02356 362 HIS A CD2 
2368 C CE1 . HIS A 362 ? 0.99729 1.11798 0.93146 -0.15617 0.31130  -0.04389 362 HIS A CE1 
2369 N NE2 . HIS A 362 ? 1.03276 1.09310 0.91137 -0.15936 0.29459  -0.04569 362 HIS A NE2 
2370 N N   . LEU A 363 ? 1.09281 1.03119 0.82009 -0.23796 0.16616  0.05468  363 LEU A N   
2371 C CA  . LEU A 363 ? 1.13981 1.02569 0.83577 -0.23641 0.13073  0.07425  363 LEU A CA  
2372 C C   . LEU A 363 ? 1.05848 0.98424 0.82853 -0.20923 0.12695  0.07861  363 LEU A C   
2373 O O   . LEU A 363 ? 1.04562 0.93737 0.81874 -0.18782 0.09807  0.08824  363 LEU A O   
2374 C CB  . LEU A 363 ? 1.20477 1.04682 0.81577 -0.28378 0.13225  0.08364  363 LEU A CB  
2375 N N   . GLU A 364 ? 1.02148 1.02022 0.85293 -0.20959 0.15570  0.07109  364 GLU A N   
2376 C CA  . GLU A 364 ? 0.95164 0.98903 0.85091 -0.18816 0.15137  0.07590  364 GLU A CA  
2377 C C   . GLU A 364 ? 0.87904 0.91725 0.82504 -0.14750 0.13478  0.07171  364 GLU A C   
2378 O O   . GLU A 364 ? 0.82275 0.84560 0.78461 -0.13154 0.11501  0.07860  364 GLU A O   
2379 C CB  . GLU A 364 ? 0.92058 1.04037 0.88054 -0.19496 0.18173  0.06992  364 GLU A CB  
2380 C CG  . GLU A 364 ? 0.96138 1.10078 0.88477 -0.23620 0.20815  0.06622  364 GLU A CG  
2381 C CD  . GLU A 364 ? 0.97739 1.12403 0.88825 -0.23827 0.23222  0.04782  364 GLU A CD  
2382 O OE1 . GLU A 364 ? 0.98045 1.11527 0.91028 -0.20765 0.22706  0.03922  364 GLU A OE1 
2383 O OE2 . GLU A 364 ? 0.93884 1.10078 0.81569 -0.27433 0.25776  0.04086  364 GLU A OE2 
2384 N N   . ILE A 365 ? 0.90815 0.96245 0.87245 -0.13339 0.14475  0.05877  365 ILE A N   
2385 C CA  . ILE A 365 ? 0.88056 0.93197 0.87811 -0.10177 0.12860  0.05434  365 ILE A CA  
2386 C C   . ILE A 365 ? 0.91781 0.91161 0.87262 -0.09669 0.09595  0.06239  365 ILE A C   
2387 O O   . ILE A 365 ? 0.89927 0.89271 0.88544 -0.07362 0.07716  0.06382  365 ILE A O   
2388 C CB  . ILE A 365 ? 0.83850 0.90726 0.84881 -0.09358 0.14695  0.03854  365 ILE A CB  
2389 C CG1 . ILE A 365 ? 0.79179 0.92026 0.85554 -0.09050 0.17824  0.03025  365 ILE A CG1 
2390 C CG2 . ILE A 365 ? 0.77026 0.83304 0.80598 -0.06770 0.12932  0.03442  365 ILE A CG2 
2391 N N   . VAL A 366 ? 0.97288 0.91814 0.85606 -0.11887 0.08802  0.06786  366 VAL A N   
2392 C CA  . VAL A 366 ? 1.01887 0.90706 0.86227 -0.11156 0.05198  0.07847  366 VAL A CA  
2393 C C   . VAL A 366 ? 1.01180 0.88363 0.86775 -0.09940 0.03638  0.08815  366 VAL A C   
2394 O O   . VAL A 366 ? 1.05176 0.90715 0.92436 -0.07385 0.01112  0.09098  366 VAL A O   
2395 C CB  . VAL A 366 ? 1.01296 0.84404 0.76736 -0.14290 0.04414  0.08536  366 VAL A CB  
2396 N N   . GLU A 367 ? 0.99264 0.87091 0.84159 -0.11865 0.05273  0.09208  367 GLU A N   
2397 C CA  . GLU A 367 ? 0.96733 0.82330 0.81979 -0.11166 0.04193  0.09960  367 GLU A CA  
2398 C C   . GLU A 367 ? 0.91792 0.81627 0.84583 -0.08212 0.04231  0.09201  367 GLU A C   
2399 O O   . GLU A 367 ? 0.92016 0.79355 0.85667 -0.06186 0.02536  0.09298  367 GLU A O   
2400 C CB  . GLU A 367 ? 0.92745 0.78695 0.75434 -0.14566 0.06072  0.10547  367 GLU A CB  
2401 N N   . VAL A 368 ? 0.90484 0.86495 0.88633 -0.07959 0.06199  0.08356  368 VAL A N   
2402 C CA  . VAL A 368 ? 0.83729 0.83295 0.88156 -0.05782 0.06160  0.07696  368 VAL A CA  
2403 C C   . VAL A 368 ? 0.90060 0.88525 0.95802 -0.03208 0.04145  0.07108  368 VAL A C   
2404 O O   . VAL A 368 ? 0.89681 0.88345 0.98287 -0.01565 0.03280  0.06755  368 VAL A O   
2405 C CB  . VAL A 368 ? 0.68570 0.73986 0.77759 -0.05897 0.08210  0.07084  368 VAL A CB  
2406 N N   . LEU A 369 ? 0.93423 0.90960 0.97001 -0.03122 0.03450  0.06921  369 LEU A N   
2407 C CA  . LEU A 369 ? 0.95274 0.92307 0.99992 -0.01097 0.01185  0.06580  369 LEU A CA  
2408 C C   . LEU A 369 ? 0.97475 0.90445 1.00546 0.00275  -0.01292 0.07322  369 LEU A C   
2409 O O   . LEU A 369 ? 0.98509 0.92919 1.05522 0.02578  -0.02585 0.06785  369 LEU A O   
2410 C CB  . LEU A 369 ? 0.96855 0.92816 0.98172 -0.02019 0.00736  0.06486  369 LEU A CB  
2411 C CG  . LEU A 369 ? 0.94373 0.93513 0.96973 -0.02964 0.03406  0.05444  369 LEU A CG  
2412 C CD1 . LEU A 369 ? 0.96279 0.93104 0.94042 -0.04382 0.03239  0.05198  369 LEU A CD1 
2413 C CD2 . LEU A 369 ? 0.88112 0.91287 0.96599 -0.01313 0.03812  0.04481  369 LEU A CD2 
2414 N N   . LEU A 370 ? 0.96021 0.83769 0.93212 -0.01122 -0.01923 0.08470  370 LEU A N   
2415 C CA  . LEU A 370 ? 1.00545 0.83222 0.95687 0.00499  -0.04342 0.09234  370 LEU A CA  
2416 C C   . LEU A 370 ? 0.99044 0.82626 0.97910 0.01785  -0.03274 0.08576  370 LEU A C   
2417 O O   . LEU A 370 ? 0.97593 0.80117 0.98889 0.04575  -0.04761 0.08199  370 LEU A O   
2418 C CB  . LEU A 370 ? 0.99836 0.75651 0.86653 -0.01858 -0.05175 0.10677  370 LEU A CB  
2419 C CG  . LEU A 370 ? 0.98286 0.71436 0.79741 -0.03498 -0.06726 0.11456  370 LEU A CG  
2420 N N   . LYS A 371 ? 0.95771 0.81580 0.95315 -0.00285 -0.00663 0.08362  371 LYS A N   
2421 C CA  . LYS A 371 ? 0.90654 0.77047 0.92896 0.00156  0.00461  0.07760  371 LYS A CA  
2422 C C   . LYS A 371 ? 0.87186 0.78721 0.96256 0.02262  0.00716  0.06321  371 LYS A C   
2423 O O   . LYS A 371 ? 0.86340 0.77936 0.97570 0.02903  0.01454  0.05515  371 LYS A O   
2424 C CB  . LYS A 371 ? 0.85866 0.73931 0.87157 -0.03031 0.02754  0.08185  371 LYS A CB  
2425 N N   . HIS A 372 ? 0.82973 0.78439 0.94820 0.02919  0.00276  0.05876  372 HIS A N   
2426 C CA  . HIS A 372 ? 0.77528 0.77646 0.95064 0.04433  0.00295  0.04526  372 HIS A CA  
2427 C C   . HIS A 372 ? 0.76993 0.77313 0.96091 0.06906  -0.02122 0.04220  372 HIS A C   
2428 O O   . HIS A 372 ? 0.72276 0.77083 0.95791 0.07723  -0.02305 0.03129  372 HIS A O   
2429 C CB  . HIS A 372 ? 0.73942 0.78315 0.93480 0.03140  0.01547  0.04174  372 HIS A CB  
2430 C CG  . HIS A 372 ? 0.72432 0.78377 0.92907 0.01352  0.03552  0.04293  372 HIS A CG  
2431 N ND1 . HIS A 372 ? 0.74825 0.79496 0.92422 -0.00492 0.04552  0.05353  372 HIS A ND1 
2432 C CD2 . HIS A 372 ? 0.68210 0.77027 0.92054 0.00841  0.04503  0.03621  372 HIS A CD2 
2433 C CE1 . HIS A 372 ? 0.74157 0.81269 0.93876 -0.01802 0.05818  0.05460  372 HIS A CE1 
2434 N NE2 . HIS A 372 ? 0.71497 0.80673 0.94653 -0.01067 0.05716  0.04487  372 HIS A NE2 
2435 N N   . GLY A 373 ? 0.79863 0.75445 0.95279 0.07894  -0.04212 0.05281  373 GLY A N   
2436 C CA  . GLY A 373 ? 0.82797 0.78613 1.00180 0.10562  -0.07062 0.05293  373 GLY A CA  
2437 C C   . GLY A 373 ? 0.89290 0.85501 1.04592 0.09856  -0.09119 0.06156  373 GLY A C   
2438 O O   . GLY A 373 ? 0.84587 0.84860 1.03674 0.10999  -0.10634 0.05662  373 GLY A O   
2439 N N   . ALA A 374 ? 0.95300 0.87370 1.04253 0.07566  -0.09105 0.07374  374 ALA A N   
2440 C CA  . ALA A 374 ? 0.91783 0.83087 0.97290 0.06257  -0.10830 0.08150  374 ALA A CA  
2441 C C   . ALA A 374 ? 0.97081 0.84502 1.00397 0.07923  -0.14985 0.09574  374 ALA A C   
2442 O O   . ALA A 374 ? 1.01650 0.84179 1.02884 0.09259  -0.16191 0.10395  374 ALA A O   
2443 C CB  . ALA A 374 ? 0.96685 0.85072 0.96049 0.02932  -0.08909 0.08652  374 ALA A CB  
2444 N N   . ASP A 375 ? 0.95612 0.84805 0.99058 0.07755  -0.17394 0.09978  375 ASP A N   
2445 C CA  . ASP A 375 ? 0.96944 0.83029 0.98732 0.09312  -0.22013 0.11639  375 ASP A CA  
2446 C C   . ASP A 375 ? 1.08913 0.87127 1.00976 0.06528  -0.23356 0.13461  375 ASP A C   
2447 O O   . ASP A 375 ? 1.11773 0.89299 0.99049 0.02979  -0.21841 0.13375  375 ASP A O   
2448 C CB  . ASP A 375 ? 0.96200 0.87582 1.01532 0.09525  -0.24328 0.11559  375 ASP A CB  
2449 C CG  . ASP A 375 ? 1.04416 0.94104 1.09897 0.11682  -0.29657 0.13402  375 ASP A CG  
2450 O OD1 . ASP A 375 ? 1.10640 0.94899 1.14284 0.13789  -0.31523 0.14554  375 ASP A OD1 
2451 O OD2 . ASP A 375 ? 1.09570 1.03098 1.16763 0.11185  -0.32194 0.13811  375 ASP A OD2 
2452 N N   . VAL A 376 ? 1.15564 0.87390 1.04298 0.08013  -0.26050 0.14980  376 VAL A N   
2453 C CA  . VAL A 376 ? 1.13836 0.77270 0.92336 0.04965  -0.27727 0.16868  376 VAL A CA  
2454 C C   . VAL A 376 ? 1.21266 0.83744 0.95948 0.03136  -0.31252 0.18246  376 VAL A C   
2455 O O   . VAL A 376 ? 1.29980 0.87847 0.96094 -0.01138 -0.30979 0.18992  376 VAL A O   
2456 C CB  . VAL A 376 ? 1.19314 0.75089 0.94628 0.07133  -0.30303 0.18307  376 VAL A CB  
2457 N N   . ASN A 377 ? 1.19713 0.86614 1.00381 0.05945  -0.34564 0.18575  377 ASN A N   
2458 C CA  . ASN A 377 ? 1.23682 0.90735 1.01337 0.03912  -0.38095 0.19903  377 ASN A CA  
2459 C C   . ASN A 377 ? 1.24424 0.97330 1.03511 0.01149  -0.34502 0.18015  377 ASN A C   
2460 O O   . ASN A 377 ? 1.19072 0.99518 1.06057 0.02971  -0.33888 0.16697  377 ASN A O   
2461 C CB  . ASN A 377 ? 1.17545 0.87937 1.01762 0.07989  -0.43221 0.21071  377 ASN A CB  
2462 N N   . ALA A 378 ? 1.37608 1.06764 1.08744 -0.03376 -0.31974 0.17751  378 ALA A N   
2463 C CA  . ALA A 378 ? 1.38620 1.12054 1.10392 -0.05789 -0.28248 0.15807  378 ALA A CA  
2464 C C   . ALA A 378 ? 1.44961 1.21442 1.17503 -0.06708 -0.31178 0.16210  378 ALA A C   
2465 O O   . ALA A 378 ? 1.45281 1.25864 1.19749 -0.07931 -0.28466 0.14476  378 ALA A O   
2466 C CB  . ALA A 378 ? 1.40554 1.09155 1.03602 -0.10271 -0.24913 0.15303  378 ALA A CB  
2467 N N   . GLN A 379 ? 1.34560 1.08805 1.05277 -0.06318 -0.36831 0.18571  379 GLN A N   
2468 C CA  . GLN A 379 ? 1.35247 1.13251 1.07488 -0.07128 -0.40441 0.19323  379 GLN A CA  
2469 C C   . GLN A 379 ? 1.39988 1.17027 1.05873 -0.12132 -0.37909 0.18211  379 GLN A C   
2470 O O   . GLN A 379 ? 1.40300 1.22561 1.09500 -0.12783 -0.37605 0.17209  379 GLN A O   
2471 C CB  . GLN A 379 ? 1.29498 1.16702 1.13467 -0.03081 -0.40761 0.18231  379 GLN A CB  
2472 N N   . ASP A 380 ? 1.42781 1.12829 0.99108 -0.15886 -0.35822 0.18211  380 ASP A N   
2473 C CA  . ASP A 380 ? 1.44862 1.12812 0.94201 -0.20676 -0.32945 0.16896  380 ASP A CA  
2474 C C   . ASP A 380 ? 1.47757 1.15543 0.93568 -0.23441 -0.37582 0.18436  380 ASP A C   
2475 O O   . ASP A 380 ? 1.44130 1.11897 0.90919 -0.22301 -0.43544 0.21055  380 ASP A O   
2476 C CB  . ASP A 380 ? 1.49920 1.10334 0.89347 -0.24388 -0.30382 0.16779  380 ASP A CB  
2477 C CG  . ASP A 380 ? 1.54766 1.13201 0.87741 -0.28813 -0.25949 0.14647  380 ASP A CG  
2478 O OD1 . ASP A 380 ? 1.53769 1.16237 0.90132 -0.28619 -0.24447 0.13134  380 ASP A OD1 
2479 O OD2 . ASP A 380 ? 1.60734 1.13247 0.84859 -0.32647 -0.23866 0.14375  380 ASP A OD2 
2480 N N   . LYS A 381 ? 1.52016 1.19571 0.93649 -0.27111 -0.34886 0.16806  381 LYS A N   
2481 C CA  . LYS A 381 ? 1.49493 1.16058 0.85961 -0.30928 -0.38891 0.18175  381 LYS A CA  
2482 C C   . LYS A 381 ? 1.60218 1.19228 0.86749 -0.34471 -0.43294 0.20938  381 LYS A C   
2483 O O   . LYS A 381 ? 1.68399 1.27099 0.92061 -0.36742 -0.48748 0.23185  381 LYS A O   
2484 C CB  . LYS A 381 ? 1.49289 1.14541 0.80602 -0.34874 -0.34427 0.15675  381 LYS A CB  
2485 N N   . PHE A 382 ? 1.61413 1.14303 0.82263 -0.35397 -0.41210 0.20919  382 PHE A N   
2486 C CA  . PHE A 382 ? 1.69964 1.14956 0.81278 -0.38503 -0.45597 0.23729  382 PHE A CA  
2487 C C   . PHE A 382 ? 1.68044 1.12709 0.84237 -0.33811 -0.49591 0.25993  382 PHE A C   
2488 O O   . PHE A 382 ? 1.79873 1.16807 0.87948 -0.35883 -0.52336 0.28081  382 PHE A O   
2489 C CB  . PHE A 382 ? 1.78811 1.16436 0.79032 -0.43585 -0.40666 0.22172  382 PHE A CB  
2490 C CG  . PHE A 382 ? 1.81133 1.18604 0.76952 -0.47516 -0.35578 0.19303  382 PHE A CG  
2491 N N   . GLY A 383 ? 1.56028 1.08287 0.84663 -0.27761 -0.49835 0.25513  383 GLY A N   
2492 C CA  . GLY A 383 ? 1.53347 1.05219 0.87118 -0.22832 -0.53087 0.27229  383 GLY A CA  
2493 C C   . GLY A 383 ? 1.52395 0.99960 0.83973 -0.22124 -0.49075 0.26254  383 GLY A C   
2494 O O   . GLY A 383 ? 1.52880 0.98777 0.87520 -0.18285 -0.51467 0.27567  383 GLY A O   
2495 N N   . LYS A 384 ? 1.53256 0.99130 0.79836 -0.25650 -0.43015 0.23928  384 LYS A N   
2496 C CA  . LYS A 384 ? 1.52829 0.95032 0.76662 -0.25898 -0.39239 0.23098  384 LYS A CA  
2497 C C   . LYS A 384 ? 1.44715 0.93038 0.79619 -0.20404 -0.36600 0.21667  384 LYS A C   
2498 O O   . LYS A 384 ? 1.39435 0.95352 0.83041 -0.17833 -0.34596 0.19948  384 LYS A O   
2499 C CB  . LYS A 384 ? 1.54098 0.94506 0.71082 -0.30907 -0.33206 0.20717  384 LYS A CB  
2500 N N   . THR A 385 ? 1.46004 0.90339 0.79662 -0.19080 -0.36681 0.22426  385 THR A N   
2501 C CA  . THR A 385 ? 1.37858 0.86606 0.80053 -0.14861 -0.33756 0.21046  385 THR A CA  
2502 C C   . THR A 385 ? 1.38616 0.88294 0.79101 -0.17401 -0.27294 0.18796  385 THR A C   
2503 O O   . THR A 385 ? 1.40901 0.87763 0.73837 -0.22107 -0.24947 0.18170  385 THR A O   
2504 C CB  . THR A 385 ? 1.40605 0.84214 0.82337 -0.11963 -0.37353 0.23020  385 THR A CB  
2505 O OG1 . THR A 385 ? 1.48234 0.83215 0.79077 -0.16056 -0.36998 0.24019  385 THR A OG1 
2506 C CG2 . THR A 385 ? 1.43231 0.85627 0.86394 -0.09397 -0.44183 0.25461  385 THR A CG2 
2507 N N   . ALA A 386 ? 1.31448 0.85429 0.79228 -0.14323 -0.24320 0.17497  386 ALA A N   
2508 C CA  . ALA A 386 ? 1.27503 0.83356 0.74932 -0.16321 -0.18610 0.15596  386 ALA A CA  
2509 C C   . ALA A 386 ? 1.37065 0.85860 0.74749 -0.20357 -0.18094 0.16504  386 ALA A C   
2510 O O   . ALA A 386 ? 1.38981 0.87845 0.72326 -0.24251 -0.14156 0.15193  386 ALA A O   
2511 C CB  . ALA A 386 ? 1.21718 0.83092 0.78379 -0.12519 -0.16320 0.14463  386 ALA A CB  
2512 N N   . PHE A 387 ? 1.42389 0.84831 0.76294 -0.19582 -0.21974 0.18649  387 PHE A N   
2513 C CA  . PHE A 387 ? 1.48731 0.83370 0.72044 -0.23983 -0.21938 0.19721  387 PHE A CA  
2514 C C   . PHE A 387 ? 1.53360 0.83299 0.66754 -0.29204 -0.22783 0.20242  387 PHE A C   
2515 O O   . PHE A 387 ? 1.57387 0.84434 0.63108 -0.34270 -0.19788 0.19626  387 PHE A O   
2516 C CB  . PHE A 387 ? 1.52161 0.79452 0.72583 -0.21867 -0.26601 0.22098  387 PHE A CB  
2517 N N   . ASP A 388 ? 1.54899 0.84227 0.68124 -0.28430 -0.26774 0.21321  388 ASP A N   
2518 C CA  . ASP A 388 ? 1.63242 0.87822 0.66483 -0.33829 -0.27669 0.21812  388 ASP A CA  
2519 C C   . ASP A 388 ? 1.60810 0.89884 0.63620 -0.37174 -0.21102 0.18757  388 ASP A C   
2520 O O   . ASP A 388 ? 1.70049 0.94584 0.63034 -0.42898 -0.19194 0.18320  388 ASP A O   
2521 C CB  . ASP A 388 ? 1.65357 0.89933 0.69836 -0.32270 -0.33091 0.23460  388 ASP A CB  
2522 C CG  . ASP A 388 ? 1.70389 0.90323 0.75262 -0.28775 -0.39924 0.26570  388 ASP A CG  
2523 N N   . ILE A 389 ? 1.52657 0.90376 0.65891 -0.33680 -0.17475 0.16530  389 ILE A N   
2524 C CA  . ILE A 389 ? 1.51686 0.93688 0.65563 -0.35920 -0.11220 0.13543  389 ILE A CA  
2525 C C   . ILE A 389 ? 1.55812 0.97636 0.66934 -0.38610 -0.06807 0.12467  389 ILE A C   
2526 O O   . ILE A 389 ? 1.58065 0.99677 0.64143 -0.42844 -0.02524 0.10622  389 ILE A O   
2527 C CB  . ILE A 389 ? 1.38530 0.89000 0.64016 -0.31295 -0.09000 0.11742  389 ILE A CB  
2528 N N   . SER A 390 ? 1.49694 0.91720 0.63953 -0.36430 -0.07638 0.13484  390 SER A N   
2529 C CA  . SER A 390 ? 1.52227 0.94406 0.63778 -0.39390 -0.03842 0.12716  390 SER A CA  
2530 C C   . SER A 390 ? 1.65054 0.98573 0.63143 -0.45600 -0.04964 0.13871  390 SER A C   
2531 O O   . SER A 390 ? 1.67480 1.01688 0.61448 -0.49944 -0.00651 0.12477  390 SER A O   
2532 C CB  . SER A 390 ? 1.47392 0.91029 0.64646 -0.35930 -0.04807 0.13669  390 SER A CB  
2533 N N   . ILE A 391 ? 1.67163 0.92681 0.58305 -0.46270 -0.10804 0.16442  391 ILE A N   
2534 C CA  . ILE A 391 ? 1.79527 0.96808 0.59030 -0.51925 -0.12471 0.17145  391 ILE A CA  
2535 C C   . ILE A 391 ? 1.91203 1.09275 0.66557 -0.56517 -0.09155 0.14728  391 ILE A C   
2536 O O   . ILE A 391 ? 1.93895 1.10571 0.64596 -0.61297 -0.06449 0.12829  391 ILE A O   
2537 C CB  . ILE A 391 ? 1.86685 0.96347 0.62973 -0.50256 -0.20034 0.20055  391 ILE A CB  
2538 N N   . ASP A 392 ? 2.07758 1.27934 0.84668 -0.55291 -0.09278 0.14576  392 ASP A N   
2539 C CA  . ASP A 392 ? 2.12818 1.33344 0.85919 -0.59434 -0.05764 0.11971  392 ASP A CA  
2540 C C   . ASP A 392 ? 2.08545 1.35835 0.85371 -0.60569 0.02064  0.08360  392 ASP A C   
2541 O O   . ASP A 392 ? 2.16934 1.43515 0.89844 -0.64922 0.05425  0.05787  392 ASP A O   
2542 C CB  . ASP A 392 ? 2.15706 1.37189 0.90002 -0.57653 -0.07554 0.12466  392 ASP A CB  
2543 N N   . ASN A 393 ? 1.86668 1.20702 0.71594 -0.56667 0.04936  0.08084  393 ASN A N   
2544 C CA  . ASN A 393 ? 1.80941 1.22588 0.71507 -0.56908 0.11907  0.04837  393 ASN A CA  
2545 C C   . ASN A 393 ? 1.83075 1.25159 0.72758 -0.59470 0.13055  0.04319  393 ASN A C   
2546 O O   . ASN A 393 ? 1.84037 1.33075 0.78880 -0.59835 0.18354  0.01679  393 ASN A O   
2547 C CB  . ASN A 393 ? 1.68024 1.18374 0.72410 -0.50308 0.13338  0.04034  393 ASN A CB  
2548 N N   . GLY A 394 ? 1.81777 1.16790 0.65466 -0.61059 0.08062  0.06692  394 GLY A N   
2549 C CA  . GLY A 394 ? 1.77750 1.12280 0.59502 -0.63973 0.08814  0.06164  394 GLY A CA  
2550 C C   . GLY A 394 ? 1.71369 1.12650 0.61005 -0.61123 0.11017  0.06207  394 GLY A C   
2551 O O   . GLY A 394 ? 1.69864 1.14169 0.60097 -0.63637 0.13533  0.04745  394 GLY A O   
2552 N N   . ASN A 395 ? 1.84630 1.28409 0.80345 -0.56199 0.09966  0.07880  395 ASN A N   
2553 C CA  . ASN A 395 ? 1.76505 1.26410 0.79967 -0.53544 0.11750  0.08130  395 ASN A CA  
2554 C C   . ASN A 395 ? 1.79726 1.22760 0.79853 -0.52526 0.06652  0.10983  395 ASN A C   
2555 O O   . ASN A 395 ? 1.79415 1.20345 0.82446 -0.48168 0.03082  0.12874  395 ASN A O   
2556 C CB  . ASN A 395 ? 1.67457 1.24997 0.82372 -0.47936 0.13300  0.07253  395 ASN A CB  
2557 N N   . GLU A 396 ? 1.72073 1.12173 0.67616 -0.55936 0.06149  0.10647  396 GLU A N   
2558 C CA  . GLU A 396 ? 1.69713 1.02267 0.61285 -0.55171 0.01525  0.12883  396 GLU A CA  
2559 C C   . GLU A 396 ? 1.66616 1.02759 0.65377 -0.51097 0.01777  0.13949  396 GLU A C   
2560 O O   . GLU A 396 ? 1.69562 0.99589 0.67129 -0.48154 -0.02327 0.16069  396 GLU A O   
2561 C CB  . GLU A 396 ? 1.74657 1.03722 0.59683 -0.60274 0.01563  0.11860  396 GLU A CB  
2562 N N   . ASP A 397 ? 1.61584 1.07600 0.68254 -0.50711 0.06448  0.12402  397 ASP A N   
2563 C CA  . ASP A 397 ? 1.57968 1.07636 0.71633 -0.47357 0.06771  0.13317  397 ASP A CA  
2564 C C   . ASP A 397 ? 1.55482 1.05411 0.75771 -0.41189 0.04083  0.13889  397 ASP A C   
2565 O O   . ASP A 397 ? 1.54261 1.01139 0.76554 -0.37852 0.01235  0.15120  397 ASP A O   
2566 C CB  . ASP A 397 ? 1.51120 1.12449 0.73474 -0.47769 0.11845  0.11288  397 ASP A CB  
2567 N N   . LEU A 398 ? 1.55320 1.09196 0.79576 -0.39463 0.04991  0.12578  398 LEU A N   
2568 C CA  . LEU A 398 ? 1.51823 1.06366 0.82344 -0.33958 0.02134  0.12827  398 LEU A CA  
2569 C C   . LEU A 398 ? 1.52741 0.97689 0.76620 -0.33156 -0.03416 0.15049  398 LEU A C   
2570 O O   . LEU A 398 ? 1.52538 0.97029 0.81447 -0.28425 -0.06440 0.15804  398 LEU A O   
2571 C CB  . LEU A 398 ? 1.47560 1.07291 0.81989 -0.33185 0.04296  0.10986  398 LEU A CB  
2572 N N   . ALA A 399 ? 1.55207 0.92453 0.67809 -0.37780 -0.04885 0.16115  399 ALA A N   
2573 C CA  . ALA A 399 ? 1.61576 0.88831 0.67231 -0.37105 -0.10711 0.18618  399 ALA A CA  
2574 C C   . ALA A 399 ? 1.61117 0.83751 0.66547 -0.34970 -0.12831 0.20013  399 ALA A C   
2575 O O   . ALA A 399 ? 1.61903 0.80477 0.69013 -0.30632 -0.17166 0.21403  399 ALA A O   
2576 C CB  . ALA A 399 ? 1.73484 0.92727 0.65964 -0.43301 -0.11789 0.19545  399 ALA A CB  
2577 N N   . GLU A 400 ? 1.61021 0.84323 0.64469 -0.38001 -0.09738 0.19571  400 GLU A N   
2578 C CA  . GLU A 400 ? 1.59292 0.78508 0.62622 -0.36250 -0.11026 0.20551  400 GLU A CA  
2579 C C   . GLU A 400 ? 1.52179 0.78913 0.68112 -0.30294 -0.10221 0.19470  400 GLU A C   
2580 O O   . GLU A 400 ? 1.48323 0.80573 0.69114 -0.30490 -0.07010 0.18481  400 GLU A O   
2581 C CB  . GLU A 400 ? 1.58212 0.79198 0.58923 -0.40780 -0.07773 0.19250  400 GLU A CB  
2582 N N   . ILE A 401 ? 1.51164 0.78356 0.72259 -0.25354 -0.13232 0.19699  401 ILE A N   
2583 C CA  . ILE A 401 ? 1.44410 0.78659 0.77022 -0.20081 -0.12480 0.18532  401 ILE A CA  
2584 C C   . ILE A 401 ? 1.51803 0.82380 0.84658 -0.18441 -0.12734 0.18893  401 ILE A C   
2585 O O   . ILE A 401 ? 1.44290 0.81025 0.84652 -0.16641 -0.10250 0.17653  401 ILE A O   
2586 C CB  . ILE A 401 ? 1.36819 0.72042 0.74139 -0.15654 -0.15932 0.18788  401 ILE A CB  
2587 C CG1 . ILE A 401 ? 1.45700 0.70758 0.76511 -0.14281 -0.21289 0.20993  401 ILE A CG1 
2588 C CG2 . ILE A 401 ? 1.34639 0.74457 0.72416 -0.17501 -0.14902 0.18034  401 ILE A CG2 
2589 N N   . LEU A 402 ? 1.60607 0.80404 0.84471 -0.19379 -0.15714 0.20602  402 LEU A N   
2590 C CA  . LEU A 402 ? 1.65975 0.80284 0.88375 -0.18014 -0.16040 0.20919  402 LEU A CA  
2591 C C   . LEU A 402 ? 1.78540 0.83068 0.88175 -0.23412 -0.16413 0.22337  402 LEU A C   
2592 O O   . LEU A 402 ? 1.78539 0.84406 0.83349 -0.28266 -0.15246 0.22076  402 LEU A O   
2593 C CB  . LEU A 402 ? 1.67630 0.77376 0.93046 -0.11888 -0.19997 0.21457  402 LEU A CB  
# 
