data_9BLV
# 
_entry.id   9BLV 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9BLV         pdb_00009blv 10.2210/pdb9blv/pdb 
WWPDB D_1000283660 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-02-12 
# 
_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                        9BLV 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-01 
_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           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              plp@uga.edu 
_pdbx_contact_author.name_first         Robert 
_pdbx_contact_author.name_last          Phillips 
_pdbx_contact_author.name_mi            S 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-8710-562X 
# 
_audit_author.name               'Phillips, R.S.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   0000-0001-8710-562X 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Acs Catalysis' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2155-5435 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            14 
_citation.language                  ? 
_citation.page_first                11498 
_citation.page_last                 11511 
_citation.title                     
'Structural Snapshots of Proteus vulgaris Tryptophan Indole-Lyase Reveal Insights into the Catalytic Mechanism.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acscatal.4c03232 
_citation.pdbx_database_id_PubMed   39114092 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Phillips, R.S.' 1 0000-0001-8710-562X 
primary 'Brown, S.M.'    2 ?                   
primary 'Patel, R.S.'    3 ?                   
# 
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 Tryptophanase                                                                                          52558.984 
4   4.1.99.1 ? ? ? 
2 non-polymer syn 'POTASSIUM ION'                                                                                        39.098    
4   ?        ? ? ? 
3 non-polymer syn BENZIMIDAZOLE                                                                                          118.136   
2   ?        ? ? ? 
4 non-polymer syn '2-{[(E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}prop-2-enoic acid' 316.204   
2   ?        ? ? ? 
5 non-polymer syn 'DIMETHYL SULFOXIDE'                                                                                   78.133    
2   ?        ? ? ? 
6 non-polymer syn '[3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHYL]-L-TRYPTOPHANE'                           433.352   
1   ?        ? ? ? 
7 non-polymer nat 'N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-tryptophan'                     435.368   
1   ?        ? ? ? 
8 water       nat water                                                                                                  18.015    
934 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'L-tryptophan indole-lyase,TNase' 
# 
_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       
;MAKRIVEPFRIKMVEKIRVPSREEREAALKEAGYNPFLLPSSAVYIDLLTDSGTNAMSDHQWAAMITGDEAYAGSRNYYD
LKDKAKELFNYDYIIPAHQGRGAENILFPVLLKYKQKEGKAKNPVFISNFHFDTTAAHVELNGCKAINIVTEKAFDSETY
DDWKGDFDIKKLKENIAQHGADNIVAIVSTVTCNSAGGQPVSMSNLKEVYEIAKQHGIFVVMDSARFCENAYFIKARDPK
YKNATIKEVIFDMYKYADALTMSAKKDPLLNIGGLVAIRDNEEIFTLARQRCVPMEGFVTYGGLAGRDMAAMVQGLEEGT
EEEYLHYRIGQVKYLGDRLREAGIPIQYPTGGHAVFVDCKKLVPQIPGDQFPAQAVINALYLESGVRAVEIGSFLLGRDP
ATGEQKHADMEFMRLTIARRVYTNDHMDYIADALIGLKEKFATLKGLEFEYEPPVLRHFTARLKPIE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MAKRIVEPFRIKMVEKIRVPSREEREAALKEAGYNPFLLPSSAVYIDLLTDSGTNAMSDHQWAAMITGDEAYAGSRNYYD
LKDKAKELFNYDYIIPAHQGRGAENILFPVLLKYKQKEGKAKNPVFISNFHFDTTAAHVELNGCKAINIVTEKAFDSETY
DDWKGDFDIKKLKENIAQHGADNIVAIVSTVTCNSAGGQPVSMSNLKEVYEIAKQHGIFVVMDSARFCENAYFIKARDPK
YKNATIKEVIFDMYKYADALTMSAKKDPLLNIGGLVAIRDNEEIFTLARQRCVPMEGFVTYGGLAGRDMAAMVQGLEEGT
EEEYLHYRIGQVKYLGDRLREAGIPIQYPTGGHAVFVDCKKLVPQIPGDQFPAQAVINALYLESGVRAVEIGSFLLGRDP
ATGEQKHADMEFMRLTIARRVYTNDHMDYIADALIGLKEKFATLKGLEFEYEPPVLRHFTARLKPIE
;
_entity_poly.pdbx_strand_id                 A,B,C,D 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'POTASSIUM ION'                                                                                        K     
3 BENZIMIDAZOLE                                                                                          BZI   
4 '2-{[(E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}prop-2-enoic acid' 0JO   
5 'DIMETHYL SULFOXIDE'                                                                                   DMS   
6 '[3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHYL]-L-TRYPTOPHANE'                           PLT   
7 'N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-tryptophan'                     A1A2Z 
8 water                                                                                                  HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ALA n 
1 3   LYS n 
1 4   ARG n 
1 5   ILE n 
1 6   VAL n 
1 7   GLU n 
1 8   PRO n 
1 9   PHE n 
1 10  ARG n 
1 11  ILE n 
1 12  LYS n 
1 13  MET n 
1 14  VAL n 
1 15  GLU n 
1 16  LYS n 
1 17  ILE n 
1 18  ARG n 
1 19  VAL n 
1 20  PRO n 
1 21  SER n 
1 22  ARG n 
1 23  GLU n 
1 24  GLU n 
1 25  ARG n 
1 26  GLU n 
1 27  ALA n 
1 28  ALA n 
1 29  LEU n 
1 30  LYS n 
1 31  GLU n 
1 32  ALA n 
1 33  GLY n 
1 34  TYR n 
1 35  ASN n 
1 36  PRO n 
1 37  PHE n 
1 38  LEU n 
1 39  LEU n 
1 40  PRO n 
1 41  SER n 
1 42  SER n 
1 43  ALA n 
1 44  VAL n 
1 45  TYR n 
1 46  ILE n 
1 47  ASP n 
1 48  LEU n 
1 49  LEU n 
1 50  THR n 
1 51  ASP n 
1 52  SER n 
1 53  GLY n 
1 54  THR n 
1 55  ASN n 
1 56  ALA n 
1 57  MET n 
1 58  SER n 
1 59  ASP n 
1 60  HIS n 
1 61  GLN n 
1 62  TRP n 
1 63  ALA n 
1 64  ALA n 
1 65  MET n 
1 66  ILE n 
1 67  THR n 
1 68  GLY n 
1 69  ASP n 
1 70  GLU n 
1 71  ALA n 
1 72  TYR n 
1 73  ALA n 
1 74  GLY n 
1 75  SER n 
1 76  ARG n 
1 77  ASN n 
1 78  TYR n 
1 79  TYR n 
1 80  ASP n 
1 81  LEU n 
1 82  LYS n 
1 83  ASP n 
1 84  LYS n 
1 85  ALA n 
1 86  LYS n 
1 87  GLU n 
1 88  LEU n 
1 89  PHE n 
1 90  ASN n 
1 91  TYR n 
1 92  ASP n 
1 93  TYR n 
1 94  ILE n 
1 95  ILE n 
1 96  PRO n 
1 97  ALA n 
1 98  HIS n 
1 99  GLN n 
1 100 GLY n 
1 101 ARG n 
1 102 GLY n 
1 103 ALA n 
1 104 GLU n 
1 105 ASN n 
1 106 ILE n 
1 107 LEU n 
1 108 PHE n 
1 109 PRO n 
1 110 VAL n 
1 111 LEU n 
1 112 LEU n 
1 113 LYS n 
1 114 TYR n 
1 115 LYS n 
1 116 GLN n 
1 117 LYS n 
1 118 GLU n 
1 119 GLY n 
1 120 LYS n 
1 121 ALA n 
1 122 LYS n 
1 123 ASN n 
1 124 PRO n 
1 125 VAL n 
1 126 PHE n 
1 127 ILE n 
1 128 SER n 
1 129 ASN n 
1 130 PHE n 
1 131 HIS n 
1 132 PHE n 
1 133 ASP n 
1 134 THR n 
1 135 THR n 
1 136 ALA n 
1 137 ALA n 
1 138 HIS n 
1 139 VAL n 
1 140 GLU n 
1 141 LEU n 
1 142 ASN n 
1 143 GLY n 
1 144 CYS n 
1 145 LYS n 
1 146 ALA n 
1 147 ILE n 
1 148 ASN n 
1 149 ILE n 
1 150 VAL n 
1 151 THR n 
1 152 GLU n 
1 153 LYS n 
1 154 ALA n 
1 155 PHE n 
1 156 ASP n 
1 157 SER n 
1 158 GLU n 
1 159 THR n 
1 160 TYR n 
1 161 ASP n 
1 162 ASP n 
1 163 TRP n 
1 164 LYS n 
1 165 GLY n 
1 166 ASP n 
1 167 PHE n 
1 168 ASP n 
1 169 ILE n 
1 170 LYS n 
1 171 LYS n 
1 172 LEU n 
1 173 LYS n 
1 174 GLU n 
1 175 ASN n 
1 176 ILE n 
1 177 ALA n 
1 178 GLN n 
1 179 HIS n 
1 180 GLY n 
1 181 ALA n 
1 182 ASP n 
1 183 ASN n 
1 184 ILE n 
1 185 VAL n 
1 186 ALA n 
1 187 ILE n 
1 188 VAL n 
1 189 SER n 
1 190 THR n 
1 191 VAL n 
1 192 THR n 
1 193 CYS n 
1 194 ASN n 
1 195 SER n 
1 196 ALA n 
1 197 GLY n 
1 198 GLY n 
1 199 GLN n 
1 200 PRO n 
1 201 VAL n 
1 202 SER n 
1 203 MET n 
1 204 SER n 
1 205 ASN n 
1 206 LEU n 
1 207 LYS n 
1 208 GLU n 
1 209 VAL n 
1 210 TYR n 
1 211 GLU n 
1 212 ILE n 
1 213 ALA n 
1 214 LYS n 
1 215 GLN n 
1 216 HIS n 
1 217 GLY n 
1 218 ILE n 
1 219 PHE n 
1 220 VAL n 
1 221 VAL n 
1 222 MET n 
1 223 ASP n 
1 224 SER n 
1 225 ALA n 
1 226 ARG n 
1 227 PHE n 
1 228 CYS n 
1 229 GLU n 
1 230 ASN n 
1 231 ALA n 
1 232 TYR n 
1 233 PHE n 
1 234 ILE n 
1 235 LYS n 
1 236 ALA n 
1 237 ARG n 
1 238 ASP n 
1 239 PRO n 
1 240 LYS n 
1 241 TYR n 
1 242 LYS n 
1 243 ASN n 
1 244 ALA n 
1 245 THR n 
1 246 ILE n 
1 247 LYS n 
1 248 GLU n 
1 249 VAL n 
1 250 ILE n 
1 251 PHE n 
1 252 ASP n 
1 253 MET n 
1 254 TYR n 
1 255 LYS n 
1 256 TYR n 
1 257 ALA n 
1 258 ASP n 
1 259 ALA n 
1 260 LEU n 
1 261 THR n 
1 262 MET n 
1 263 SER n 
1 264 ALA n 
1 265 LYS n 
1 266 LYS n 
1 267 ASP n 
1 268 PRO n 
1 269 LEU n 
1 270 LEU n 
1 271 ASN n 
1 272 ILE n 
1 273 GLY n 
1 274 GLY n 
1 275 LEU n 
1 276 VAL n 
1 277 ALA n 
1 278 ILE n 
1 279 ARG n 
1 280 ASP n 
1 281 ASN n 
1 282 GLU n 
1 283 GLU n 
1 284 ILE n 
1 285 PHE n 
1 286 THR n 
1 287 LEU n 
1 288 ALA n 
1 289 ARG n 
1 290 GLN n 
1 291 ARG n 
1 292 CYS n 
1 293 VAL n 
1 294 PRO n 
1 295 MET n 
1 296 GLU n 
1 297 GLY n 
1 298 PHE n 
1 299 VAL n 
1 300 THR n 
1 301 TYR n 
1 302 GLY n 
1 303 GLY n 
1 304 LEU n 
1 305 ALA n 
1 306 GLY n 
1 307 ARG n 
1 308 ASP n 
1 309 MET n 
1 310 ALA n 
1 311 ALA n 
1 312 MET n 
1 313 VAL n 
1 314 GLN n 
1 315 GLY n 
1 316 LEU n 
1 317 GLU n 
1 318 GLU n 
1 319 GLY n 
1 320 THR n 
1 321 GLU n 
1 322 GLU n 
1 323 GLU n 
1 324 TYR n 
1 325 LEU n 
1 326 HIS n 
1 327 TYR n 
1 328 ARG n 
1 329 ILE n 
1 330 GLY n 
1 331 GLN n 
1 332 VAL n 
1 333 LYS n 
1 334 TYR n 
1 335 LEU n 
1 336 GLY n 
1 337 ASP n 
1 338 ARG n 
1 339 LEU n 
1 340 ARG n 
1 341 GLU n 
1 342 ALA n 
1 343 GLY n 
1 344 ILE n 
1 345 PRO n 
1 346 ILE n 
1 347 GLN n 
1 348 TYR n 
1 349 PRO n 
1 350 THR n 
1 351 GLY n 
1 352 GLY n 
1 353 HIS n 
1 354 ALA n 
1 355 VAL n 
1 356 PHE n 
1 357 VAL n 
1 358 ASP n 
1 359 CYS n 
1 360 LYS n 
1 361 LYS n 
1 362 LEU n 
1 363 VAL n 
1 364 PRO n 
1 365 GLN n 
1 366 ILE n 
1 367 PRO n 
1 368 GLY n 
1 369 ASP n 
1 370 GLN n 
1 371 PHE n 
1 372 PRO n 
1 373 ALA n 
1 374 GLN n 
1 375 ALA n 
1 376 VAL n 
1 377 ILE n 
1 378 ASN n 
1 379 ALA n 
1 380 LEU n 
1 381 TYR n 
1 382 LEU n 
1 383 GLU n 
1 384 SER n 
1 385 GLY n 
1 386 VAL n 
1 387 ARG n 
1 388 ALA n 
1 389 VAL n 
1 390 GLU n 
1 391 ILE n 
1 392 GLY n 
1 393 SER n 
1 394 PHE n 
1 395 LEU n 
1 396 LEU n 
1 397 GLY n 
1 398 ARG n 
1 399 ASP n 
1 400 PRO n 
1 401 ALA n 
1 402 THR n 
1 403 GLY n 
1 404 GLU n 
1 405 GLN n 
1 406 LYS n 
1 407 HIS n 
1 408 ALA n 
1 409 ASP n 
1 410 MET n 
1 411 GLU n 
1 412 PHE n 
1 413 MET n 
1 414 ARG n 
1 415 LEU n 
1 416 THR n 
1 417 ILE n 
1 418 ALA n 
1 419 ARG n 
1 420 ARG n 
1 421 VAL n 
1 422 TYR n 
1 423 THR n 
1 424 ASN n 
1 425 ASP n 
1 426 HIS n 
1 427 MET n 
1 428 ASP n 
1 429 TYR n 
1 430 ILE n 
1 431 ALA n 
1 432 ASP n 
1 433 ALA n 
1 434 LEU n 
1 435 ILE n 
1 436 GLY n 
1 437 LEU n 
1 438 LYS n 
1 439 GLU n 
1 440 LYS n 
1 441 PHE n 
1 442 ALA n 
1 443 THR n 
1 444 LEU n 
1 445 LYS n 
1 446 GLY n 
1 447 LEU n 
1 448 GLU n 
1 449 PHE n 
1 450 GLU n 
1 451 TYR n 
1 452 GLU n 
1 453 PRO n 
1 454 PRO n 
1 455 VAL n 
1 456 LEU n 
1 457 ARG n 
1 458 HIS n 
1 459 PHE n 
1 460 THR n 
1 461 ALA n 
1 462 ARG n 
1 463 LEU n 
1 464 LYS n 
1 465 PRO n 
1 466 ILE n 
1 467 GLU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   467 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 tnaA 
_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      'Proteus vulgaris' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     585 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
0JO   non-polymer         . '2-{[(E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}prop-2-enoic acid' 
? 'C11 H13 N2 O7 P' 316.204 
A1A2Z non-polymer         n 'N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-tryptophan'                     
? 'C19 H22 N3 O7 P' 435.368 
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 
BZI   non-polymer         . BENZIMIDAZOLE                                                                                          
? 'C7 H6 N2'        118.136 
CYS   'L-peptide linking' y CYSTEINE                                                                                               
? 'C3 H7 N O2 S'    121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                                                                   
? 'C2 H6 O S'       78.133  
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 
K     non-polymer         . 'POTASSIUM ION'                                                                                        
? 'K 1'             39.098  
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 
PLT   non-polymer         . '[3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHYL]-L-TRYPTOPHANE'                           
? 'C19 H20 N3 O7 P' 433.352 
PRO   'L-peptide linking' y PROLINE                                                                                                
? 'C5 H9 N O2'      115.130 
SER   'L-peptide linking' y SERINE                                                                                                 
? 'C3 H7 N O3'      105.093 
THR   'L-peptide linking' y THREONINE                                                                                              
? 'C4 H9 N O3'      119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                                             
? 'C11 H12 N2 O2'   204.225 
TYR   'L-peptide linking' y TYROSINE                                                                                               
? 'C9 H11 N O3'     181.189 
VAL   'L-peptide linking' y VALINE                                                                                                 
? 'C5 H11 N O2'     117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   ALA 2   2   2   ALA ALA A . n 
A 1 3   LYS 3   3   3   LYS LYS A . n 
A 1 4   ARG 4   4   4   ARG ARG A . n 
A 1 5   ILE 5   5   5   ILE ILE A . n 
A 1 6   VAL 6   6   6   VAL VAL A . n 
A 1 7   GLU 7   7   7   GLU GLU A . n 
A 1 8   PRO 8   8   8   PRO PRO A . n 
A 1 9   PHE 9   9   9   PHE PHE A . n 
A 1 10  ARG 10  10  10  ARG ARG A . n 
A 1 11  ILE 11  11  11  ILE ILE A . n 
A 1 12  LYS 12  12  12  LYS LYS A . n 
A 1 13  MET 13  13  13  MET MET A . n 
A 1 14  VAL 14  14  14  VAL VAL A . n 
A 1 15  GLU 15  15  15  GLU GLU A . n 
A 1 16  LYS 16  16  16  LYS LYS A . n 
A 1 17  ILE 17  17  17  ILE ILE A . n 
A 1 18  ARG 18  18  18  ARG ARG A . n 
A 1 19  VAL 19  19  19  VAL VAL A . n 
A 1 20  PRO 20  20  20  PRO PRO A . n 
A 1 21  SER 21  21  21  SER SER A . n 
A 1 22  ARG 22  22  22  ARG ARG A . n 
A 1 23  GLU 23  23  23  GLU GLU A . n 
A 1 24  GLU 24  24  24  GLU GLU A . n 
A 1 25  ARG 25  25  25  ARG ARG A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  ALA 28  28  28  ALA ALA A . n 
A 1 29  LEU 29  29  29  LEU LEU A . n 
A 1 30  LYS 30  30  30  LYS LYS A . n 
A 1 31  GLU 31  31  31  GLU GLU A . n 
A 1 32  ALA 32  32  32  ALA ALA A . n 
A 1 33  GLY 33  33  33  GLY GLY A . n 
A 1 34  TYR 34  34  34  TYR TYR A . n 
A 1 35  ASN 35  35  35  ASN ASN A . n 
A 1 36  PRO 36  36  36  PRO PRO A . n 
A 1 37  PHE 37  37  37  PHE PHE A . n 
A 1 38  LEU 38  38  38  LEU LEU A . n 
A 1 39  LEU 39  39  39  LEU LEU A . n 
A 1 40  PRO 40  40  40  PRO PRO A . n 
A 1 41  SER 41  41  41  SER SER A . n 
A 1 42  SER 42  42  42  SER SER A . n 
A 1 43  ALA 43  43  43  ALA ALA A . n 
A 1 44  VAL 44  44  44  VAL VAL A . n 
A 1 45  TYR 45  45  45  TYR TYR A . n 
A 1 46  ILE 46  46  46  ILE ILE A . n 
A 1 47  ASP 47  47  47  ASP ASP A . n 
A 1 48  LEU 48  48  48  LEU LEU A . n 
A 1 49  LEU 49  49  49  LEU LEU A . n 
A 1 50  THR 50  50  50  THR THR A . n 
A 1 51  ASP 51  51  51  ASP ASP A . n 
A 1 52  SER 52  52  52  SER SER A . n 
A 1 53  GLY 53  53  53  GLY GLY A . n 
A 1 54  THR 54  54  54  THR THR A . n 
A 1 55  ASN 55  55  55  ASN ASN A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  MET 57  57  57  MET MET A . n 
A 1 58  SER 58  58  58  SER SER A . n 
A 1 59  ASP 59  59  59  ASP ASP A . n 
A 1 60  HIS 60  60  60  HIS HIS A . n 
A 1 61  GLN 61  61  61  GLN GLN A . n 
A 1 62  TRP 62  62  62  TRP TRP A . n 
A 1 63  ALA 63  63  63  ALA ALA A . n 
A 1 64  ALA 64  64  64  ALA ALA A . n 
A 1 65  MET 65  65  65  MET MET A . n 
A 1 66  ILE 66  66  66  ILE ILE A . n 
A 1 67  THR 67  67  67  THR THR A . n 
A 1 68  GLY 68  68  68  GLY GLY A . n 
A 1 69  ASP 69  69  69  ASP ASP A . n 
A 1 70  GLU 70  70  70  GLU GLU A . n 
A 1 71  ALA 71  71  71  ALA ALA A . n 
A 1 72  TYR 72  72  72  TYR TYR A . n 
A 1 73  ALA 73  73  73  ALA ALA A . n 
A 1 74  GLY 74  74  74  GLY GLY A . n 
A 1 75  SER 75  75  75  SER SER A . n 
A 1 76  ARG 76  76  76  ARG ARG A . n 
A 1 77  ASN 77  77  77  ASN ASN A . n 
A 1 78  TYR 78  78  78  TYR TYR A . n 
A 1 79  TYR 79  79  79  TYR TYR A . n 
A 1 80  ASP 80  80  80  ASP ASP A . n 
A 1 81  LEU 81  81  81  LEU LEU A . n 
A 1 82  LYS 82  82  82  LYS LYS A . n 
A 1 83  ASP 83  83  83  ASP ASP A . n 
A 1 84  LYS 84  84  84  LYS LYS A . n 
A 1 85  ALA 85  85  85  ALA ALA A . n 
A 1 86  LYS 86  86  86  LYS LYS A . n 
A 1 87  GLU 87  87  87  GLU GLU A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  PHE 89  89  89  PHE PHE A . n 
A 1 90  ASN 90  90  90  ASN ASN A . n 
A 1 91  TYR 91  91  91  TYR TYR A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  TYR 93  93  93  TYR TYR A . n 
A 1 94  ILE 94  94  94  ILE ILE A . n 
A 1 95  ILE 95  95  95  ILE ILE A . n 
A 1 96  PRO 96  96  96  PRO PRO A . n 
A 1 97  ALA 97  97  97  ALA ALA A . n 
A 1 98  HIS 98  98  98  HIS HIS A . n 
A 1 99  GLN 99  99  99  GLN GLN A . n 
A 1 100 GLY 100 100 100 GLY GLY A . n 
A 1 101 ARG 101 101 101 ARG ARG A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 ALA 103 103 103 ALA ALA A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 ASN 105 105 105 ASN ASN A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 LEU 107 107 107 LEU LEU A . n 
A 1 108 PHE 108 108 108 PHE PHE A . n 
A 1 109 PRO 109 109 109 PRO PRO A . n 
A 1 110 VAL 110 110 110 VAL VAL A . n 
A 1 111 LEU 111 111 111 LEU LEU A . n 
A 1 112 LEU 112 112 112 LEU LEU A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 LYS 115 115 115 LYS LYS A . n 
A 1 116 GLN 116 116 116 GLN GLN A . n 
A 1 117 LYS 117 117 117 LYS LYS A . n 
A 1 118 GLU 118 118 118 GLU GLU A . n 
A 1 119 GLY 119 119 119 GLY GLY A . n 
A 1 120 LYS 120 120 120 LYS LYS A . n 
A 1 121 ALA 121 121 121 ALA ALA A . n 
A 1 122 LYS 122 122 122 LYS LYS A . n 
A 1 123 ASN 123 123 123 ASN ASN A . n 
A 1 124 PRO 124 124 124 PRO PRO A . n 
A 1 125 VAL 125 125 125 VAL VAL A . n 
A 1 126 PHE 126 126 126 PHE PHE A . n 
A 1 127 ILE 127 127 127 ILE ILE A . n 
A 1 128 SER 128 128 128 SER SER A . n 
A 1 129 ASN 129 129 129 ASN ASN A . n 
A 1 130 PHE 130 130 130 PHE PHE A . n 
A 1 131 HIS 131 131 131 HIS HIS A . n 
A 1 132 PHE 132 132 132 PHE PHE A . n 
A 1 133 ASP 133 133 133 ASP ASP A . n 
A 1 134 THR 134 134 134 THR THR A . n 
A 1 135 THR 135 135 135 THR THR A . n 
A 1 136 ALA 136 136 136 ALA ALA A . n 
A 1 137 ALA 137 137 137 ALA ALA A . n 
A 1 138 HIS 138 138 138 HIS HIS A . n 
A 1 139 VAL 139 139 139 VAL VAL A . n 
A 1 140 GLU 140 140 140 GLU GLU A . n 
A 1 141 LEU 141 141 141 LEU LEU A . n 
A 1 142 ASN 142 142 142 ASN ASN A . n 
A 1 143 GLY 143 143 143 GLY GLY A . n 
A 1 144 CYS 144 144 144 CYS CYS A . n 
A 1 145 LYS 145 145 145 LYS LYS A . n 
A 1 146 ALA 146 146 146 ALA ALA A . n 
A 1 147 ILE 147 147 147 ILE ILE A . n 
A 1 148 ASN 148 148 148 ASN ASN A . n 
A 1 149 ILE 149 149 149 ILE ILE A . n 
A 1 150 VAL 150 150 150 VAL VAL A . n 
A 1 151 THR 151 151 151 THR THR A . n 
A 1 152 GLU 152 152 152 GLU GLU A . n 
A 1 153 LYS 153 153 153 LYS LYS A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 PHE 155 155 155 PHE PHE A . n 
A 1 156 ASP 156 156 156 ASP ASP A . n 
A 1 157 SER 157 157 157 SER SER A . n 
A 1 158 GLU 158 158 158 GLU GLU A . n 
A 1 159 THR 159 159 159 THR THR A . n 
A 1 160 TYR 160 160 160 TYR TYR A . n 
A 1 161 ASP 161 161 161 ASP ASP A . n 
A 1 162 ASP 162 162 162 ASP ASP A . n 
A 1 163 TRP 163 163 163 TRP TRP A . n 
A 1 164 LYS 164 164 164 LYS LYS A . n 
A 1 165 GLY 165 165 165 GLY GLY A . n 
A 1 166 ASP 166 166 166 ASP ASP A . n 
A 1 167 PHE 167 167 167 PHE PHE A . n 
A 1 168 ASP 168 168 168 ASP ASP A . n 
A 1 169 ILE 169 169 169 ILE ILE A . n 
A 1 170 LYS 170 170 170 LYS LYS A . n 
A 1 171 LYS 171 171 171 LYS LYS A . n 
A 1 172 LEU 172 172 172 LEU LEU A . n 
A 1 173 LYS 173 173 173 LYS LYS A . n 
A 1 174 GLU 174 174 174 GLU GLU A . n 
A 1 175 ASN 175 175 175 ASN ASN A . n 
A 1 176 ILE 176 176 176 ILE ILE A . n 
A 1 177 ALA 177 177 177 ALA ALA A . n 
A 1 178 GLN 178 178 178 GLN GLN A . n 
A 1 179 HIS 179 179 179 HIS HIS A . n 
A 1 180 GLY 180 180 180 GLY GLY A . n 
A 1 181 ALA 181 181 181 ALA ALA A . n 
A 1 182 ASP 182 182 182 ASP ASP A . n 
A 1 183 ASN 183 183 183 ASN ASN A . n 
A 1 184 ILE 184 184 184 ILE ILE A . n 
A 1 185 VAL 185 185 185 VAL VAL A . n 
A 1 186 ALA 186 186 186 ALA ALA A . n 
A 1 187 ILE 187 187 187 ILE ILE A . n 
A 1 188 VAL 188 188 188 VAL VAL A . n 
A 1 189 SER 189 189 189 SER SER A . n 
A 1 190 THR 190 190 190 THR THR A . n 
A 1 191 VAL 191 191 191 VAL VAL A . n 
A 1 192 THR 192 192 192 THR THR A . n 
A 1 193 CYS 193 193 193 CYS CYS A . n 
A 1 194 ASN 194 194 194 ASN ASN A . n 
A 1 195 SER 195 195 195 SER SER A . n 
A 1 196 ALA 196 196 196 ALA ALA A . n 
A 1 197 GLY 197 197 197 GLY GLY A . n 
A 1 198 GLY 198 198 198 GLY GLY A . n 
A 1 199 GLN 199 199 199 GLN GLN A . n 
A 1 200 PRO 200 200 200 PRO PRO A . n 
A 1 201 VAL 201 201 201 VAL VAL A . n 
A 1 202 SER 202 202 202 SER SER A . n 
A 1 203 MET 203 203 203 MET MET A . n 
A 1 204 SER 204 204 204 SER SER A . n 
A 1 205 ASN 205 205 205 ASN ASN A . n 
A 1 206 LEU 206 206 206 LEU LEU A . n 
A 1 207 LYS 207 207 207 LYS LYS A . n 
A 1 208 GLU 208 208 208 GLU GLU A . n 
A 1 209 VAL 209 209 209 VAL VAL A . n 
A 1 210 TYR 210 210 210 TYR TYR A . n 
A 1 211 GLU 211 211 211 GLU GLU A . n 
A 1 212 ILE 212 212 212 ILE ILE A . n 
A 1 213 ALA 213 213 213 ALA ALA A . n 
A 1 214 LYS 214 214 214 LYS LYS A . n 
A 1 215 GLN 215 215 215 GLN GLN A . n 
A 1 216 HIS 216 216 216 HIS HIS A . n 
A 1 217 GLY 217 217 217 GLY GLY A . n 
A 1 218 ILE 218 218 218 ILE ILE A . n 
A 1 219 PHE 219 219 219 PHE PHE A . n 
A 1 220 VAL 220 220 220 VAL VAL A . n 
A 1 221 VAL 221 221 221 VAL VAL A . n 
A 1 222 MET 222 222 222 MET MET A . n 
A 1 223 ASP 223 223 223 ASP ASP A . n 
A 1 224 SER 224 224 224 SER SER A . n 
A 1 225 ALA 225 225 225 ALA ALA A . n 
A 1 226 ARG 226 226 226 ARG ARG A . n 
A 1 227 PHE 227 227 227 PHE PHE A . n 
A 1 228 CYS 228 228 228 CYS CYS A . n 
A 1 229 GLU 229 229 229 GLU GLU A . n 
A 1 230 ASN 230 230 230 ASN ASN A . n 
A 1 231 ALA 231 231 231 ALA ALA A . n 
A 1 232 TYR 232 232 232 TYR TYR A . n 
A 1 233 PHE 233 233 233 PHE PHE A . n 
A 1 234 ILE 234 234 234 ILE ILE A . n 
A 1 235 LYS 235 235 235 LYS LYS A . n 
A 1 236 ALA 236 236 236 ALA ALA A . n 
A 1 237 ARG 237 237 237 ARG ARG A . n 
A 1 238 ASP 238 238 238 ASP ASP A . n 
A 1 239 PRO 239 239 239 PRO PRO A . n 
A 1 240 LYS 240 240 240 LYS LYS A . n 
A 1 241 TYR 241 241 241 TYR TYR A . n 
A 1 242 LYS 242 242 242 LYS LYS A . n 
A 1 243 ASN 243 243 243 ASN ASN A . n 
A 1 244 ALA 244 244 244 ALA ALA A . n 
A 1 245 THR 245 245 245 THR THR A . n 
A 1 246 ILE 246 246 246 ILE ILE A . n 
A 1 247 LYS 247 247 247 LYS LYS A . n 
A 1 248 GLU 248 248 248 GLU GLU A . n 
A 1 249 VAL 249 249 249 VAL VAL A . n 
A 1 250 ILE 250 250 250 ILE ILE A . n 
A 1 251 PHE 251 251 251 PHE PHE A . n 
A 1 252 ASP 252 252 252 ASP ASP A . n 
A 1 253 MET 253 253 253 MET MET A . n 
A 1 254 TYR 254 254 254 TYR TYR A . n 
A 1 255 LYS 255 255 255 LYS LYS A . n 
A 1 256 TYR 256 256 256 TYR TYR A . n 
A 1 257 ALA 257 257 257 ALA ALA A . n 
A 1 258 ASP 258 258 258 ASP ASP A . n 
A 1 259 ALA 259 259 259 ALA ALA A . n 
A 1 260 LEU 260 260 260 LEU LEU A . n 
A 1 261 THR 261 261 261 THR THR A . n 
A 1 262 MET 262 262 262 MET MET A . n 
A 1 263 SER 263 263 263 SER SER A . n 
A 1 264 ALA 264 264 264 ALA ALA A . n 
A 1 265 LYS 265 265 265 LYS LYS A . n 
A 1 266 LYS 266 266 266 LYS LYS A . n 
A 1 267 ASP 267 267 267 ASP ASP A . n 
A 1 268 PRO 268 268 268 PRO PRO A . n 
A 1 269 LEU 269 269 269 LEU LEU A . n 
A 1 270 LEU 270 270 270 LEU LEU A . n 
A 1 271 ASN 271 271 271 ASN ASN A . n 
A 1 272 ILE 272 272 272 ILE ILE A . n 
A 1 273 GLY 273 273 273 GLY GLY A . n 
A 1 274 GLY 274 274 274 GLY GLY A . n 
A 1 275 LEU 275 275 275 LEU LEU A . n 
A 1 276 VAL 276 276 276 VAL VAL A . n 
A 1 277 ALA 277 277 277 ALA ALA A . n 
A 1 278 ILE 278 278 278 ILE ILE A . n 
A 1 279 ARG 279 279 279 ARG ARG A . n 
A 1 280 ASP 280 280 280 ASP ASP A . n 
A 1 281 ASN 281 281 281 ASN ASN A . n 
A 1 282 GLU 282 282 282 GLU GLU A . n 
A 1 283 GLU 283 283 283 GLU GLU A . n 
A 1 284 ILE 284 284 284 ILE ILE A . n 
A 1 285 PHE 285 285 285 PHE PHE A . n 
A 1 286 THR 286 286 286 THR THR A . n 
A 1 287 LEU 287 287 287 LEU LEU A . n 
A 1 288 ALA 288 288 288 ALA ALA A . n 
A 1 289 ARG 289 289 289 ARG ARG A . n 
A 1 290 GLN 290 290 290 GLN GLN A . n 
A 1 291 ARG 291 291 291 ARG ARG A . n 
A 1 292 CYS 292 292 292 CYS CYS A . n 
A 1 293 VAL 293 293 293 VAL VAL A . n 
A 1 294 PRO 294 294 294 PRO PRO A . n 
A 1 295 MET 295 295 295 MET MET A . n 
A 1 296 GLU 296 296 296 GLU GLU A . n 
A 1 297 GLY 297 297 297 GLY GLY A . n 
A 1 298 PHE 298 298 298 PHE PHE A . n 
A 1 299 VAL 299 299 299 VAL VAL A . n 
A 1 300 THR 300 300 300 THR THR A . n 
A 1 301 TYR 301 301 301 TYR TYR A . n 
A 1 302 GLY 302 302 302 GLY GLY A . n 
A 1 303 GLY 303 303 303 GLY GLY A . n 
A 1 304 LEU 304 304 304 LEU LEU A . n 
A 1 305 ALA 305 305 305 ALA ALA A . n 
A 1 306 GLY 306 306 306 GLY GLY A . n 
A 1 307 ARG 307 307 307 ARG ARG A . n 
A 1 308 ASP 308 308 308 ASP ASP A . n 
A 1 309 MET 309 309 309 MET MET A . n 
A 1 310 ALA 310 310 310 ALA ALA A . n 
A 1 311 ALA 311 311 311 ALA ALA A . n 
A 1 312 MET 312 312 312 MET MET A . n 
A 1 313 VAL 313 313 313 VAL VAL A . n 
A 1 314 GLN 314 314 314 GLN GLN A . n 
A 1 315 GLY 315 315 315 GLY GLY A . n 
A 1 316 LEU 316 316 316 LEU LEU A . n 
A 1 317 GLU 317 317 317 GLU GLU A . n 
A 1 318 GLU 318 318 318 GLU GLU A . n 
A 1 319 GLY 319 319 319 GLY GLY A . n 
A 1 320 THR 320 320 320 THR THR A . n 
A 1 321 GLU 321 321 321 GLU GLU A . n 
A 1 322 GLU 322 322 322 GLU GLU A . n 
A 1 323 GLU 323 323 323 GLU GLU A . n 
A 1 324 TYR 324 324 324 TYR TYR A . n 
A 1 325 LEU 325 325 325 LEU LEU A . n 
A 1 326 HIS 326 326 326 HIS HIS A . n 
A 1 327 TYR 327 327 327 TYR TYR A . n 
A 1 328 ARG 328 328 328 ARG ARG A . n 
A 1 329 ILE 329 329 329 ILE ILE A . n 
A 1 330 GLY 330 330 330 GLY GLY A . n 
A 1 331 GLN 331 331 331 GLN GLN A . n 
A 1 332 VAL 332 332 332 VAL VAL A . n 
A 1 333 LYS 333 333 333 LYS LYS A . n 
A 1 334 TYR 334 334 334 TYR TYR A . n 
A 1 335 LEU 335 335 335 LEU LEU A . n 
A 1 336 GLY 336 336 336 GLY GLY A . n 
A 1 337 ASP 337 337 337 ASP ASP A . n 
A 1 338 ARG 338 338 338 ARG ARG A . n 
A 1 339 LEU 339 339 339 LEU LEU A . n 
A 1 340 ARG 340 340 340 ARG ARG A . n 
A 1 341 GLU 341 341 341 GLU GLU A . n 
A 1 342 ALA 342 342 342 ALA ALA A . n 
A 1 343 GLY 343 343 343 GLY GLY A . n 
A 1 344 ILE 344 344 344 ILE ILE A . n 
A 1 345 PRO 345 345 345 PRO PRO A . n 
A 1 346 ILE 346 346 346 ILE ILE A . n 
A 1 347 GLN 347 347 347 GLN GLN A . n 
A 1 348 TYR 348 348 348 TYR TYR A . n 
A 1 349 PRO 349 349 349 PRO PRO A . n 
A 1 350 THR 350 350 350 THR THR A . n 
A 1 351 GLY 351 351 351 GLY GLY A . n 
A 1 352 GLY 352 352 352 GLY GLY A . n 
A 1 353 HIS 353 353 353 HIS HIS A . n 
A 1 354 ALA 354 354 354 ALA ALA A . n 
A 1 355 VAL 355 355 355 VAL VAL A . n 
A 1 356 PHE 356 356 356 PHE PHE A . n 
A 1 357 VAL 357 357 357 VAL VAL A . n 
A 1 358 ASP 358 358 358 ASP ASP A . n 
A 1 359 CYS 359 359 359 CYS CYS A . n 
A 1 360 LYS 360 360 360 LYS LYS A . n 
A 1 361 LYS 361 361 361 LYS LYS A . n 
A 1 362 LEU 362 362 362 LEU LEU A . n 
A 1 363 VAL 363 363 363 VAL VAL A . n 
A 1 364 PRO 364 364 364 PRO PRO A . n 
A 1 365 GLN 365 365 365 GLN GLN A . n 
A 1 366 ILE 366 366 366 ILE ILE A . n 
A 1 367 PRO 367 367 367 PRO PRO A . n 
A 1 368 GLY 368 368 368 GLY GLY A . n 
A 1 369 ASP 369 369 369 ASP ASP A . n 
A 1 370 GLN 370 370 370 GLN GLN A . n 
A 1 371 PHE 371 371 371 PHE PHE A . n 
A 1 372 PRO 372 372 372 PRO PRO A . n 
A 1 373 ALA 373 373 373 ALA ALA A . n 
A 1 374 GLN 374 374 374 GLN GLN A . n 
A 1 375 ALA 375 375 375 ALA ALA A . n 
A 1 376 VAL 376 376 376 VAL VAL A . n 
A 1 377 ILE 377 377 377 ILE ILE A . n 
A 1 378 ASN 378 378 378 ASN ASN A . n 
A 1 379 ALA 379 379 379 ALA ALA A . n 
A 1 380 LEU 380 380 380 LEU LEU A . n 
A 1 381 TYR 381 381 381 TYR TYR A . n 
A 1 382 LEU 382 382 382 LEU LEU A . n 
A 1 383 GLU 383 383 383 GLU GLU A . n 
A 1 384 SER 384 384 384 SER SER A . n 
A 1 385 GLY 385 385 385 GLY GLY A . n 
A 1 386 VAL 386 386 386 VAL VAL A . n 
A 1 387 ARG 387 387 387 ARG ARG A . n 
A 1 388 ALA 388 388 388 ALA ALA A . n 
A 1 389 VAL 389 389 389 VAL VAL A . n 
A 1 390 GLU 390 390 390 GLU GLU A . n 
A 1 391 ILE 391 391 391 ILE ILE A . n 
A 1 392 GLY 392 392 392 GLY GLY A . n 
A 1 393 SER 393 393 393 SER SER A . n 
A 1 394 PHE 394 394 394 PHE PHE A . n 
A 1 395 LEU 395 395 395 LEU LEU A . n 
A 1 396 LEU 396 396 396 LEU LEU A . n 
A 1 397 GLY 397 397 397 GLY GLY A . n 
A 1 398 ARG 398 398 ?   ?   ?   A . n 
A 1 399 ASP 399 399 ?   ?   ?   A . n 
A 1 400 PRO 400 400 ?   ?   ?   A . n 
A 1 401 ALA 401 401 ?   ?   ?   A . n 
A 1 402 THR 402 402 ?   ?   ?   A . n 
A 1 403 GLY 403 403 ?   ?   ?   A . n 
A 1 404 GLU 404 404 ?   ?   ?   A . n 
A 1 405 GLN 405 405 405 GLN GLN A . n 
A 1 406 LYS 406 406 406 LYS LYS A . n 
A 1 407 HIS 407 407 407 HIS HIS A . n 
A 1 408 ALA 408 408 408 ALA ALA A . n 
A 1 409 ASP 409 409 409 ASP ASP A . n 
A 1 410 MET 410 410 410 MET MET A . n 
A 1 411 GLU 411 411 411 GLU GLU A . n 
A 1 412 PHE 412 412 412 PHE PHE A . n 
A 1 413 MET 413 413 413 MET MET A . n 
A 1 414 ARG 414 414 414 ARG ARG A . n 
A 1 415 LEU 415 415 415 LEU LEU A . n 
A 1 416 THR 416 416 416 THR THR A . n 
A 1 417 ILE 417 417 417 ILE ILE A . n 
A 1 418 ALA 418 418 418 ALA ALA A . n 
A 1 419 ARG 419 419 419 ARG ARG A . n 
A 1 420 ARG 420 420 420 ARG ARG A . n 
A 1 421 VAL 421 421 421 VAL VAL A . n 
A 1 422 TYR 422 422 422 TYR TYR A . n 
A 1 423 THR 423 423 423 THR THR A . n 
A 1 424 ASN 424 424 424 ASN ASN A . n 
A 1 425 ASP 425 425 425 ASP ASP A . n 
A 1 426 HIS 426 426 426 HIS HIS A . n 
A 1 427 MET 427 427 427 MET MET A . n 
A 1 428 ASP 428 428 428 ASP ASP A . n 
A 1 429 TYR 429 429 429 TYR TYR A . n 
A 1 430 ILE 430 430 430 ILE ILE A . n 
A 1 431 ALA 431 431 431 ALA ALA A . n 
A 1 432 ASP 432 432 432 ASP ASP A . n 
A 1 433 ALA 433 433 433 ALA ALA A . n 
A 1 434 LEU 434 434 434 LEU LEU A . n 
A 1 435 ILE 435 435 435 ILE ILE A . n 
A 1 436 GLY 436 436 436 GLY GLY A . n 
A 1 437 LEU 437 437 437 LEU LEU A . n 
A 1 438 LYS 438 438 438 LYS LYS A . n 
A 1 439 GLU 439 439 439 GLU GLU A . n 
A 1 440 LYS 440 440 440 LYS LYS A . n 
A 1 441 PHE 441 441 441 PHE PHE A . n 
A 1 442 ALA 442 442 442 ALA ALA A . n 
A 1 443 THR 443 443 443 THR THR A . n 
A 1 444 LEU 444 444 444 LEU LEU A . n 
A 1 445 LYS 445 445 445 LYS LYS A . n 
A 1 446 GLY 446 446 446 GLY GLY A . n 
A 1 447 LEU 447 447 447 LEU LEU A . n 
A 1 448 GLU 448 448 448 GLU GLU A . n 
A 1 449 PHE 449 449 449 PHE PHE A . n 
A 1 450 GLU 450 450 450 GLU GLU A . n 
A 1 451 TYR 451 451 451 TYR TYR A . n 
A 1 452 GLU 452 452 452 GLU GLU A . n 
A 1 453 PRO 453 453 453 PRO PRO A . n 
A 1 454 PRO 454 454 454 PRO PRO A . n 
A 1 455 VAL 455 455 455 VAL VAL A . n 
A 1 456 LEU 456 456 456 LEU LEU A . n 
A 1 457 ARG 457 457 457 ARG ARG A . n 
A 1 458 HIS 458 458 458 HIS HIS A . n 
A 1 459 PHE 459 459 459 PHE PHE A . n 
A 1 460 THR 460 460 460 THR THR A . n 
A 1 461 ALA 461 461 461 ALA ALA A . n 
A 1 462 ARG 462 462 462 ARG ARG A . n 
A 1 463 LEU 463 463 463 LEU LEU A . n 
A 1 464 LYS 464 464 464 LYS LYS A . n 
A 1 465 PRO 465 465 465 PRO PRO A . n 
A 1 466 ILE 466 466 466 ILE ILE A . n 
A 1 467 GLU 467 467 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   ALA 2   2   2   ALA ALA B . n 
B 1 3   LYS 3   3   3   LYS LYS B . n 
B 1 4   ARG 4   4   4   ARG ARG B . n 
B 1 5   ILE 5   5   5   ILE ILE B . n 
B 1 6   VAL 6   6   6   VAL VAL B . n 
B 1 7   GLU 7   7   7   GLU GLU B . n 
B 1 8   PRO 8   8   8   PRO PRO B . n 
B 1 9   PHE 9   9   9   PHE PHE B . n 
B 1 10  ARG 10  10  10  ARG ARG B . n 
B 1 11  ILE 11  11  11  ILE ILE B . n 
B 1 12  LYS 12  12  12  LYS LYS B . n 
B 1 13  MET 13  13  13  MET MET B . n 
B 1 14  VAL 14  14  14  VAL VAL B . n 
B 1 15  GLU 15  15  15  GLU GLU B . n 
B 1 16  LYS 16  16  16  LYS LYS B . n 
B 1 17  ILE 17  17  17  ILE ILE B . n 
B 1 18  ARG 18  18  18  ARG ARG B . n 
B 1 19  VAL 19  19  19  VAL VAL B . n 
B 1 20  PRO 20  20  20  PRO PRO B . n 
B 1 21  SER 21  21  21  SER SER B . n 
B 1 22  ARG 22  22  22  ARG ARG B . n 
B 1 23  GLU 23  23  23  GLU GLU B . n 
B 1 24  GLU 24  24  24  GLU GLU B . n 
B 1 25  ARG 25  25  25  ARG ARG B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  ALA 27  27  27  ALA ALA B . n 
B 1 28  ALA 28  28  28  ALA ALA B . n 
B 1 29  LEU 29  29  29  LEU LEU B . n 
B 1 30  LYS 30  30  30  LYS LYS B . n 
B 1 31  GLU 31  31  31  GLU GLU B . n 
B 1 32  ALA 32  32  32  ALA ALA B . n 
B 1 33  GLY 33  33  33  GLY GLY B . n 
B 1 34  TYR 34  34  34  TYR TYR B . n 
B 1 35  ASN 35  35  35  ASN ASN B . n 
B 1 36  PRO 36  36  36  PRO PRO B . n 
B 1 37  PHE 37  37  37  PHE PHE B . n 
B 1 38  LEU 38  38  38  LEU LEU B . n 
B 1 39  LEU 39  39  39  LEU LEU B . n 
B 1 40  PRO 40  40  40  PRO PRO B . n 
B 1 41  SER 41  41  41  SER SER B . n 
B 1 42  SER 42  42  42  SER SER B . n 
B 1 43  ALA 43  43  43  ALA ALA B . n 
B 1 44  VAL 44  44  44  VAL VAL B . n 
B 1 45  TYR 45  45  45  TYR TYR B . n 
B 1 46  ILE 46  46  46  ILE ILE B . n 
B 1 47  ASP 47  47  47  ASP ASP B . n 
B 1 48  LEU 48  48  48  LEU LEU B . n 
B 1 49  LEU 49  49  49  LEU LEU B . n 
B 1 50  THR 50  50  50  THR THR B . n 
B 1 51  ASP 51  51  51  ASP ASP B . n 
B 1 52  SER 52  52  52  SER SER B . n 
B 1 53  GLY 53  53  53  GLY GLY B . n 
B 1 54  THR 54  54  54  THR THR B . n 
B 1 55  ASN 55  55  55  ASN ASN B . n 
B 1 56  ALA 56  56  56  ALA ALA B . n 
B 1 57  MET 57  57  57  MET MET B . n 
B 1 58  SER 58  58  58  SER SER B . n 
B 1 59  ASP 59  59  59  ASP ASP B . n 
B 1 60  HIS 60  60  60  HIS HIS B . n 
B 1 61  GLN 61  61  61  GLN GLN B . n 
B 1 62  TRP 62  62  62  TRP TRP B . n 
B 1 63  ALA 63  63  63  ALA ALA B . n 
B 1 64  ALA 64  64  64  ALA ALA B . n 
B 1 65  MET 65  65  65  MET MET B . n 
B 1 66  ILE 66  66  66  ILE ILE B . n 
B 1 67  THR 67  67  67  THR THR B . n 
B 1 68  GLY 68  68  68  GLY GLY B . n 
B 1 69  ASP 69  69  69  ASP ASP B . n 
B 1 70  GLU 70  70  70  GLU GLU B . n 
B 1 71  ALA 71  71  71  ALA ALA B . n 
B 1 72  TYR 72  72  72  TYR TYR B . n 
B 1 73  ALA 73  73  73  ALA ALA B . n 
B 1 74  GLY 74  74  74  GLY GLY B . n 
B 1 75  SER 75  75  75  SER SER B . n 
B 1 76  ARG 76  76  76  ARG ARG B . n 
B 1 77  ASN 77  77  77  ASN ASN B . n 
B 1 78  TYR 78  78  78  TYR TYR B . n 
B 1 79  TYR 79  79  79  TYR TYR B . n 
B 1 80  ASP 80  80  80  ASP ASP B . n 
B 1 81  LEU 81  81  81  LEU LEU B . n 
B 1 82  LYS 82  82  82  LYS LYS B . n 
B 1 83  ASP 83  83  83  ASP ASP B . n 
B 1 84  LYS 84  84  84  LYS LYS B . n 
B 1 85  ALA 85  85  85  ALA ALA B . n 
B 1 86  LYS 86  86  86  LYS LYS B . n 
B 1 87  GLU 87  87  87  GLU GLU B . n 
B 1 88  LEU 88  88  88  LEU LEU B . n 
B 1 89  PHE 89  89  89  PHE PHE B . n 
B 1 90  ASN 90  90  90  ASN ASN B . n 
B 1 91  TYR 91  91  91  TYR TYR B . n 
B 1 92  ASP 92  92  92  ASP ASP B . n 
B 1 93  TYR 93  93  93  TYR TYR B . n 
B 1 94  ILE 94  94  94  ILE ILE B . n 
B 1 95  ILE 95  95  95  ILE ILE B . n 
B 1 96  PRO 96  96  96  PRO PRO B . n 
B 1 97  ALA 97  97  97  ALA ALA B . n 
B 1 98  HIS 98  98  98  HIS HIS B . n 
B 1 99  GLN 99  99  99  GLN GLN B . n 
B 1 100 GLY 100 100 100 GLY GLY B . n 
B 1 101 ARG 101 101 101 ARG ARG B . n 
B 1 102 GLY 102 102 102 GLY GLY B . n 
B 1 103 ALA 103 103 103 ALA ALA B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 ASN 105 105 105 ASN ASN B . n 
B 1 106 ILE 106 106 106 ILE ILE B . n 
B 1 107 LEU 107 107 107 LEU LEU B . n 
B 1 108 PHE 108 108 108 PHE PHE B . n 
B 1 109 PRO 109 109 109 PRO PRO B . n 
B 1 110 VAL 110 110 110 VAL VAL B . n 
B 1 111 LEU 111 111 111 LEU LEU B . n 
B 1 112 LEU 112 112 112 LEU LEU B . n 
B 1 113 LYS 113 113 113 LYS LYS B . n 
B 1 114 TYR 114 114 114 TYR TYR B . n 
B 1 115 LYS 115 115 115 LYS LYS B . n 
B 1 116 GLN 116 116 116 GLN GLN B . n 
B 1 117 LYS 117 117 117 LYS LYS B . n 
B 1 118 GLU 118 118 118 GLU GLU B . n 
B 1 119 GLY 119 119 119 GLY GLY B . n 
B 1 120 LYS 120 120 120 LYS LYS B . n 
B 1 121 ALA 121 121 121 ALA ALA B . n 
B 1 122 LYS 122 122 122 LYS LYS B . n 
B 1 123 ASN 123 123 123 ASN ASN B . n 
B 1 124 PRO 124 124 124 PRO PRO B . n 
B 1 125 VAL 125 125 125 VAL VAL B . n 
B 1 126 PHE 126 126 126 PHE PHE B . n 
B 1 127 ILE 127 127 127 ILE ILE B . n 
B 1 128 SER 128 128 128 SER SER B . n 
B 1 129 ASN 129 129 129 ASN ASN B . n 
B 1 130 PHE 130 130 130 PHE PHE B . n 
B 1 131 HIS 131 131 131 HIS HIS B . n 
B 1 132 PHE 132 132 132 PHE PHE B . n 
B 1 133 ASP 133 133 133 ASP ASP B . n 
B 1 134 THR 134 134 134 THR THR B . n 
B 1 135 THR 135 135 135 THR THR B . n 
B 1 136 ALA 136 136 136 ALA ALA B . n 
B 1 137 ALA 137 137 137 ALA ALA B . n 
B 1 138 HIS 138 138 138 HIS HIS B . n 
B 1 139 VAL 139 139 139 VAL VAL B . n 
B 1 140 GLU 140 140 140 GLU GLU B . n 
B 1 141 LEU 141 141 141 LEU LEU B . n 
B 1 142 ASN 142 142 142 ASN ASN B . n 
B 1 143 GLY 143 143 143 GLY GLY B . n 
B 1 144 CYS 144 144 144 CYS CYS B . n 
B 1 145 LYS 145 145 145 LYS LYS B . n 
B 1 146 ALA 146 146 146 ALA ALA B . n 
B 1 147 ILE 147 147 147 ILE ILE B . n 
B 1 148 ASN 148 148 148 ASN ASN B . n 
B 1 149 ILE 149 149 149 ILE ILE B . n 
B 1 150 VAL 150 150 150 VAL VAL B . n 
B 1 151 THR 151 151 151 THR THR B . n 
B 1 152 GLU 152 152 152 GLU GLU B . n 
B 1 153 LYS 153 153 153 LYS LYS B . n 
B 1 154 ALA 154 154 154 ALA ALA B . n 
B 1 155 PHE 155 155 155 PHE PHE B . n 
B 1 156 ASP 156 156 156 ASP ASP B . n 
B 1 157 SER 157 157 157 SER SER B . n 
B 1 158 GLU 158 158 158 GLU GLU B . n 
B 1 159 THR 159 159 159 THR THR B . n 
B 1 160 TYR 160 160 160 TYR TYR B . n 
B 1 161 ASP 161 161 161 ASP ASP B . n 
B 1 162 ASP 162 162 162 ASP ASP B . n 
B 1 163 TRP 163 163 163 TRP TRP B . n 
B 1 164 LYS 164 164 164 LYS LYS B . n 
B 1 165 GLY 165 165 165 GLY GLY B . n 
B 1 166 ASP 166 166 166 ASP ASP B . n 
B 1 167 PHE 167 167 167 PHE PHE B . n 
B 1 168 ASP 168 168 168 ASP ASP B . n 
B 1 169 ILE 169 169 169 ILE ILE B . n 
B 1 170 LYS 170 170 170 LYS LYS B . n 
B 1 171 LYS 171 171 171 LYS LYS B . n 
B 1 172 LEU 172 172 172 LEU LEU B . n 
B 1 173 LYS 173 173 173 LYS LYS B . n 
B 1 174 GLU 174 174 174 GLU GLU B . n 
B 1 175 ASN 175 175 175 ASN ASN B . n 
B 1 176 ILE 176 176 176 ILE ILE B . n 
B 1 177 ALA 177 177 177 ALA ALA B . n 
B 1 178 GLN 178 178 178 GLN GLN B . n 
B 1 179 HIS 179 179 179 HIS HIS B . n 
B 1 180 GLY 180 180 180 GLY GLY B . n 
B 1 181 ALA 181 181 181 ALA ALA B . n 
B 1 182 ASP 182 182 182 ASP ASP B . n 
B 1 183 ASN 183 183 183 ASN ASN B . n 
B 1 184 ILE 184 184 184 ILE ILE B . n 
B 1 185 VAL 185 185 185 VAL VAL B . n 
B 1 186 ALA 186 186 186 ALA ALA B . n 
B 1 187 ILE 187 187 187 ILE ILE B . n 
B 1 188 VAL 188 188 188 VAL VAL B . n 
B 1 189 SER 189 189 189 SER SER B . n 
B 1 190 THR 190 190 190 THR THR B . n 
B 1 191 VAL 191 191 191 VAL VAL B . n 
B 1 192 THR 192 192 192 THR THR B . n 
B 1 193 CYS 193 193 193 CYS CYS B . n 
B 1 194 ASN 194 194 194 ASN ASN B . n 
B 1 195 SER 195 195 195 SER SER B . n 
B 1 196 ALA 196 196 196 ALA ALA B . n 
B 1 197 GLY 197 197 197 GLY GLY B . n 
B 1 198 GLY 198 198 198 GLY GLY B . n 
B 1 199 GLN 199 199 199 GLN GLN B . n 
B 1 200 PRO 200 200 200 PRO PRO B . n 
B 1 201 VAL 201 201 201 VAL VAL B . n 
B 1 202 SER 202 202 202 SER SER B . n 
B 1 203 MET 203 203 203 MET MET B . n 
B 1 204 SER 204 204 204 SER SER B . n 
B 1 205 ASN 205 205 205 ASN ASN B . n 
B 1 206 LEU 206 206 206 LEU LEU B . n 
B 1 207 LYS 207 207 207 LYS LYS B . n 
B 1 208 GLU 208 208 208 GLU GLU B . n 
B 1 209 VAL 209 209 209 VAL VAL B . n 
B 1 210 TYR 210 210 210 TYR TYR B . n 
B 1 211 GLU 211 211 211 GLU GLU B . n 
B 1 212 ILE 212 212 212 ILE ILE B . n 
B 1 213 ALA 213 213 213 ALA ALA B . n 
B 1 214 LYS 214 214 214 LYS LYS B . n 
B 1 215 GLN 215 215 215 GLN GLN B . n 
B 1 216 HIS 216 216 216 HIS HIS B . n 
B 1 217 GLY 217 217 217 GLY GLY B . n 
B 1 218 ILE 218 218 218 ILE ILE B . n 
B 1 219 PHE 219 219 219 PHE PHE B . n 
B 1 220 VAL 220 220 220 VAL VAL B . n 
B 1 221 VAL 221 221 221 VAL VAL B . n 
B 1 222 MET 222 222 222 MET MET B . n 
B 1 223 ASP 223 223 223 ASP ASP B . n 
B 1 224 SER 224 224 224 SER SER B . n 
B 1 225 ALA 225 225 225 ALA ALA B . n 
B 1 226 ARG 226 226 226 ARG ARG B . n 
B 1 227 PHE 227 227 227 PHE PHE B . n 
B 1 228 CYS 228 228 228 CYS CYS B . n 
B 1 229 GLU 229 229 229 GLU GLU B . n 
B 1 230 ASN 230 230 230 ASN ASN B . n 
B 1 231 ALA 231 231 231 ALA ALA B . n 
B 1 232 TYR 232 232 232 TYR TYR B . n 
B 1 233 PHE 233 233 233 PHE PHE B . n 
B 1 234 ILE 234 234 234 ILE ILE B . n 
B 1 235 LYS 235 235 235 LYS LYS B . n 
B 1 236 ALA 236 236 236 ALA ALA B . n 
B 1 237 ARG 237 237 237 ARG ARG B . n 
B 1 238 ASP 238 238 238 ASP ASP B . n 
B 1 239 PRO 239 239 239 PRO PRO B . n 
B 1 240 LYS 240 240 240 LYS LYS B . n 
B 1 241 TYR 241 241 241 TYR TYR B . n 
B 1 242 LYS 242 242 242 LYS LYS B . n 
B 1 243 ASN 243 243 243 ASN ASN B . n 
B 1 244 ALA 244 244 244 ALA ALA B . n 
B 1 245 THR 245 245 245 THR THR B . n 
B 1 246 ILE 246 246 246 ILE ILE B . n 
B 1 247 LYS 247 247 247 LYS LYS B . n 
B 1 248 GLU 248 248 248 GLU GLU B . n 
B 1 249 VAL 249 249 249 VAL VAL B . n 
B 1 250 ILE 250 250 250 ILE ILE B . n 
B 1 251 PHE 251 251 251 PHE PHE B . n 
B 1 252 ASP 252 252 252 ASP ASP B . n 
B 1 253 MET 253 253 253 MET MET B . n 
B 1 254 TYR 254 254 254 TYR TYR B . n 
B 1 255 LYS 255 255 255 LYS LYS B . n 
B 1 256 TYR 256 256 256 TYR TYR B . n 
B 1 257 ALA 257 257 257 ALA ALA B . n 
B 1 258 ASP 258 258 258 ASP ASP B . n 
B 1 259 ALA 259 259 259 ALA ALA B . n 
B 1 260 LEU 260 260 260 LEU LEU B . n 
B 1 261 THR 261 261 261 THR THR B . n 
B 1 262 MET 262 262 262 MET MET B . n 
B 1 263 SER 263 263 263 SER SER B . n 
B 1 264 ALA 264 264 264 ALA ALA B . n 
B 1 265 LYS 265 265 265 LYS LYS B . n 
B 1 266 LYS 266 266 266 LYS LYS B . n 
B 1 267 ASP 267 267 267 ASP ASP B . n 
B 1 268 PRO 268 268 268 PRO PRO B . n 
B 1 269 LEU 269 269 269 LEU LEU B . n 
B 1 270 LEU 270 270 270 LEU LEU B . n 
B 1 271 ASN 271 271 271 ASN ASN B . n 
B 1 272 ILE 272 272 272 ILE ILE B . n 
B 1 273 GLY 273 273 273 GLY GLY B . n 
B 1 274 GLY 274 274 274 GLY GLY B . n 
B 1 275 LEU 275 275 275 LEU LEU B . n 
B 1 276 VAL 276 276 276 VAL VAL B . n 
B 1 277 ALA 277 277 277 ALA ALA B . n 
B 1 278 ILE 278 278 278 ILE ILE B . n 
B 1 279 ARG 279 279 279 ARG ARG B . n 
B 1 280 ASP 280 280 280 ASP ASP B . n 
B 1 281 ASN 281 281 281 ASN ASN B . n 
B 1 282 GLU 282 282 282 GLU GLU B . n 
B 1 283 GLU 283 283 283 GLU GLU B . n 
B 1 284 ILE 284 284 284 ILE ILE B . n 
B 1 285 PHE 285 285 285 PHE PHE B . n 
B 1 286 THR 286 286 286 THR THR B . n 
B 1 287 LEU 287 287 287 LEU LEU B . n 
B 1 288 ALA 288 288 288 ALA ALA B . n 
B 1 289 ARG 289 289 289 ARG ARG B . n 
B 1 290 GLN 290 290 290 GLN GLN B . n 
B 1 291 ARG 291 291 291 ARG ARG B . n 
B 1 292 CYS 292 292 292 CYS CYS B . n 
B 1 293 VAL 293 293 293 VAL VAL B . n 
B 1 294 PRO 294 294 294 PRO PRO B . n 
B 1 295 MET 295 295 295 MET MET B . n 
B 1 296 GLU 296 296 296 GLU GLU B . n 
B 1 297 GLY 297 297 297 GLY GLY B . n 
B 1 298 PHE 298 298 298 PHE PHE B . n 
B 1 299 VAL 299 299 299 VAL VAL B . n 
B 1 300 THR 300 300 300 THR THR B . n 
B 1 301 TYR 301 301 301 TYR TYR B . n 
B 1 302 GLY 302 302 302 GLY GLY B . n 
B 1 303 GLY 303 303 303 GLY GLY B . n 
B 1 304 LEU 304 304 304 LEU LEU B . n 
B 1 305 ALA 305 305 305 ALA ALA B . n 
B 1 306 GLY 306 306 306 GLY GLY B . n 
B 1 307 ARG 307 307 307 ARG ARG B . n 
B 1 308 ASP 308 308 308 ASP ASP B . n 
B 1 309 MET 309 309 309 MET MET B . n 
B 1 310 ALA 310 310 310 ALA ALA B . n 
B 1 311 ALA 311 311 311 ALA ALA B . n 
B 1 312 MET 312 312 312 MET MET B . n 
B 1 313 VAL 313 313 313 VAL VAL B . n 
B 1 314 GLN 314 314 314 GLN GLN B . n 
B 1 315 GLY 315 315 315 GLY GLY B . n 
B 1 316 LEU 316 316 316 LEU LEU B . n 
B 1 317 GLU 317 317 317 GLU GLU B . n 
B 1 318 GLU 318 318 318 GLU GLU B . n 
B 1 319 GLY 319 319 319 GLY GLY B . n 
B 1 320 THR 320 320 320 THR THR B . n 
B 1 321 GLU 321 321 321 GLU GLU B . n 
B 1 322 GLU 322 322 322 GLU GLU B . n 
B 1 323 GLU 323 323 323 GLU GLU B . n 
B 1 324 TYR 324 324 324 TYR TYR B . n 
B 1 325 LEU 325 325 325 LEU LEU B . n 
B 1 326 HIS 326 326 326 HIS HIS B . n 
B 1 327 TYR 327 327 327 TYR TYR B . n 
B 1 328 ARG 328 328 328 ARG ARG B . n 
B 1 329 ILE 329 329 329 ILE ILE B . n 
B 1 330 GLY 330 330 330 GLY GLY B . n 
B 1 331 GLN 331 331 331 GLN GLN B . n 
B 1 332 VAL 332 332 332 VAL VAL B . n 
B 1 333 LYS 333 333 333 LYS LYS B . n 
B 1 334 TYR 334 334 334 TYR TYR B . n 
B 1 335 LEU 335 335 335 LEU LEU B . n 
B 1 336 GLY 336 336 336 GLY GLY B . n 
B 1 337 ASP 337 337 337 ASP ASP B . n 
B 1 338 ARG 338 338 338 ARG ARG B . n 
B 1 339 LEU 339 339 339 LEU LEU B . n 
B 1 340 ARG 340 340 340 ARG ARG B . n 
B 1 341 GLU 341 341 341 GLU GLU B . n 
B 1 342 ALA 342 342 342 ALA ALA B . n 
B 1 343 GLY 343 343 343 GLY GLY B . n 
B 1 344 ILE 344 344 344 ILE ILE B . n 
B 1 345 PRO 345 345 345 PRO PRO B . n 
B 1 346 ILE 346 346 346 ILE ILE B . n 
B 1 347 GLN 347 347 347 GLN GLN B . n 
B 1 348 TYR 348 348 348 TYR TYR B . n 
B 1 349 PRO 349 349 349 PRO PRO B . n 
B 1 350 THR 350 350 350 THR THR B . n 
B 1 351 GLY 351 351 351 GLY GLY B . n 
B 1 352 GLY 352 352 352 GLY GLY B . n 
B 1 353 HIS 353 353 353 HIS HIS B . n 
B 1 354 ALA 354 354 354 ALA ALA B . n 
B 1 355 VAL 355 355 355 VAL VAL B . n 
B 1 356 PHE 356 356 356 PHE PHE B . n 
B 1 357 VAL 357 357 357 VAL VAL B . n 
B 1 358 ASP 358 358 358 ASP ASP B . n 
B 1 359 CYS 359 359 359 CYS CYS B . n 
B 1 360 LYS 360 360 360 LYS LYS B . n 
B 1 361 LYS 361 361 361 LYS LYS B . n 
B 1 362 LEU 362 362 362 LEU LEU B . n 
B 1 363 VAL 363 363 363 VAL VAL B . n 
B 1 364 PRO 364 364 364 PRO PRO B . n 
B 1 365 GLN 365 365 365 GLN GLN B . n 
B 1 366 ILE 366 366 366 ILE ILE B . n 
B 1 367 PRO 367 367 367 PRO PRO B . n 
B 1 368 GLY 368 368 368 GLY GLY B . n 
B 1 369 ASP 369 369 369 ASP ASP B . n 
B 1 370 GLN 370 370 370 GLN GLN B . n 
B 1 371 PHE 371 371 371 PHE PHE B . n 
B 1 372 PRO 372 372 372 PRO PRO B . n 
B 1 373 ALA 373 373 373 ALA ALA B . n 
B 1 374 GLN 374 374 374 GLN GLN B . n 
B 1 375 ALA 375 375 375 ALA ALA B . n 
B 1 376 VAL 376 376 376 VAL VAL B . n 
B 1 377 ILE 377 377 377 ILE ILE B . n 
B 1 378 ASN 378 378 378 ASN ASN B . n 
B 1 379 ALA 379 379 379 ALA ALA B . n 
B 1 380 LEU 380 380 380 LEU LEU B . n 
B 1 381 TYR 381 381 381 TYR TYR B . n 
B 1 382 LEU 382 382 382 LEU LEU B . n 
B 1 383 GLU 383 383 383 GLU GLU B . n 
B 1 384 SER 384 384 384 SER SER B . n 
B 1 385 GLY 385 385 385 GLY GLY B . n 
B 1 386 VAL 386 386 386 VAL VAL B . n 
B 1 387 ARG 387 387 387 ARG ARG B . n 
B 1 388 ALA 388 388 388 ALA ALA B . n 
B 1 389 VAL 389 389 389 VAL VAL B . n 
B 1 390 GLU 390 390 390 GLU GLU B . n 
B 1 391 ILE 391 391 391 ILE ILE B . n 
B 1 392 GLY 392 392 392 GLY GLY B . n 
B 1 393 SER 393 393 393 SER SER B . n 
B 1 394 PHE 394 394 394 PHE PHE B . n 
B 1 395 LEU 395 395 395 LEU LEU B . n 
B 1 396 LEU 396 396 396 LEU LEU B . n 
B 1 397 GLY 397 397 397 GLY GLY B . n 
B 1 398 ARG 398 398 398 ARG ARG B . n 
B 1 399 ASP 399 399 399 ASP ASP B . n 
B 1 400 PRO 400 400 400 PRO PRO B . n 
B 1 401 ALA 401 401 401 ALA ALA B . n 
B 1 402 THR 402 402 402 THR THR B . n 
B 1 403 GLY 403 403 403 GLY GLY B . n 
B 1 404 GLU 404 404 404 GLU GLU B . n 
B 1 405 GLN 405 405 405 GLN GLN B . n 
B 1 406 LYS 406 406 406 LYS LYS B . n 
B 1 407 HIS 407 407 407 HIS HIS B . n 
B 1 408 ALA 408 408 408 ALA ALA B . n 
B 1 409 ASP 409 409 409 ASP ASP B . n 
B 1 410 MET 410 410 410 MET MET B . n 
B 1 411 GLU 411 411 411 GLU GLU B . n 
B 1 412 PHE 412 412 412 PHE PHE B . n 
B 1 413 MET 413 413 413 MET MET B . n 
B 1 414 ARG 414 414 414 ARG ARG B . n 
B 1 415 LEU 415 415 415 LEU LEU B . n 
B 1 416 THR 416 416 416 THR THR B . n 
B 1 417 ILE 417 417 417 ILE ILE B . n 
B 1 418 ALA 418 418 418 ALA ALA B . n 
B 1 419 ARG 419 419 419 ARG ARG B . n 
B 1 420 ARG 420 420 420 ARG ARG B . n 
B 1 421 VAL 421 421 421 VAL VAL B . n 
B 1 422 TYR 422 422 422 TYR TYR B . n 
B 1 423 THR 423 423 423 THR THR B . n 
B 1 424 ASN 424 424 424 ASN ASN B . n 
B 1 425 ASP 425 425 425 ASP ASP B . n 
B 1 426 HIS 426 426 426 HIS HIS B . n 
B 1 427 MET 427 427 427 MET MET B . n 
B 1 428 ASP 428 428 428 ASP ASP B . n 
B 1 429 TYR 429 429 429 TYR TYR B . n 
B 1 430 ILE 430 430 430 ILE ILE B . n 
B 1 431 ALA 431 431 431 ALA ALA B . n 
B 1 432 ASP 432 432 432 ASP ASP B . n 
B 1 433 ALA 433 433 433 ALA ALA B . n 
B 1 434 LEU 434 434 434 LEU LEU B . n 
B 1 435 ILE 435 435 435 ILE ILE B . n 
B 1 436 GLY 436 436 436 GLY GLY B . n 
B 1 437 LEU 437 437 437 LEU LEU B . n 
B 1 438 LYS 438 438 438 LYS LYS B . n 
B 1 439 GLU 439 439 439 GLU GLU B . n 
B 1 440 LYS 440 440 440 LYS LYS B . n 
B 1 441 PHE 441 441 441 PHE PHE B . n 
B 1 442 ALA 442 442 442 ALA ALA B . n 
B 1 443 THR 443 443 443 THR THR B . n 
B 1 444 LEU 444 444 444 LEU LEU B . n 
B 1 445 LYS 445 445 445 LYS LYS B . n 
B 1 446 GLY 446 446 446 GLY GLY B . n 
B 1 447 LEU 447 447 447 LEU LEU B . n 
B 1 448 GLU 448 448 448 GLU GLU B . n 
B 1 449 PHE 449 449 449 PHE PHE B . n 
B 1 450 GLU 450 450 450 GLU GLU B . n 
B 1 451 TYR 451 451 451 TYR TYR B . n 
B 1 452 GLU 452 452 452 GLU GLU B . n 
B 1 453 PRO 453 453 453 PRO PRO B . n 
B 1 454 PRO 454 454 454 PRO PRO B . n 
B 1 455 VAL 455 455 455 VAL VAL B . n 
B 1 456 LEU 456 456 456 LEU LEU B . n 
B 1 457 ARG 457 457 457 ARG ARG B . n 
B 1 458 HIS 458 458 458 HIS HIS B . n 
B 1 459 PHE 459 459 459 PHE PHE B . n 
B 1 460 THR 460 460 460 THR THR B . n 
B 1 461 ALA 461 461 461 ALA ALA B . n 
B 1 462 ARG 462 462 462 ARG ARG B . n 
B 1 463 LEU 463 463 463 LEU LEU B . n 
B 1 464 LYS 464 464 464 LYS LYS B . n 
B 1 465 PRO 465 465 465 PRO PRO B . n 
B 1 466 ILE 466 466 466 ILE ILE B . n 
B 1 467 GLU 467 467 ?   ?   ?   B . n 
C 1 1   MET 1   1   ?   ?   ?   C . n 
C 1 2   ALA 2   2   2   ALA ALA C . n 
C 1 3   LYS 3   3   3   LYS LYS C . n 
C 1 4   ARG 4   4   4   ARG ARG C . n 
C 1 5   ILE 5   5   5   ILE ILE C . n 
C 1 6   VAL 6   6   6   VAL VAL C . n 
C 1 7   GLU 7   7   7   GLU GLU C . n 
C 1 8   PRO 8   8   8   PRO PRO C . n 
C 1 9   PHE 9   9   9   PHE PHE C . n 
C 1 10  ARG 10  10  10  ARG ARG C . n 
C 1 11  ILE 11  11  11  ILE ILE C . n 
C 1 12  LYS 12  12  12  LYS LYS C . n 
C 1 13  MET 13  13  13  MET MET C . n 
C 1 14  VAL 14  14  14  VAL VAL C . n 
C 1 15  GLU 15  15  15  GLU GLU C . n 
C 1 16  LYS 16  16  16  LYS LYS C . n 
C 1 17  ILE 17  17  17  ILE ILE C . n 
C 1 18  ARG 18  18  18  ARG ARG C . n 
C 1 19  VAL 19  19  19  VAL VAL C . n 
C 1 20  PRO 20  20  20  PRO PRO C . n 
C 1 21  SER 21  21  21  SER SER C . n 
C 1 22  ARG 22  22  22  ARG ARG C . n 
C 1 23  GLU 23  23  23  GLU GLU C . n 
C 1 24  GLU 24  24  24  GLU GLU C . n 
C 1 25  ARG 25  25  25  ARG ARG C . n 
C 1 26  GLU 26  26  26  GLU GLU C . n 
C 1 27  ALA 27  27  27  ALA ALA C . n 
C 1 28  ALA 28  28  28  ALA ALA C . n 
C 1 29  LEU 29  29  29  LEU LEU C . n 
C 1 30  LYS 30  30  30  LYS LYS C . n 
C 1 31  GLU 31  31  31  GLU GLU C . n 
C 1 32  ALA 32  32  32  ALA ALA C . n 
C 1 33  GLY 33  33  33  GLY GLY C . n 
C 1 34  TYR 34  34  34  TYR TYR C . n 
C 1 35  ASN 35  35  35  ASN ASN C . n 
C 1 36  PRO 36  36  36  PRO PRO C . n 
C 1 37  PHE 37  37  37  PHE PHE C . n 
C 1 38  LEU 38  38  38  LEU LEU C . n 
C 1 39  LEU 39  39  39  LEU LEU C . n 
C 1 40  PRO 40  40  40  PRO PRO C . n 
C 1 41  SER 41  41  41  SER SER C . n 
C 1 42  SER 42  42  42  SER SER C . n 
C 1 43  ALA 43  43  43  ALA ALA C . n 
C 1 44  VAL 44  44  44  VAL VAL C . n 
C 1 45  TYR 45  45  45  TYR TYR C . n 
C 1 46  ILE 46  46  46  ILE ILE C . n 
C 1 47  ASP 47  47  47  ASP ASP C . n 
C 1 48  LEU 48  48  48  LEU LEU C . n 
C 1 49  LEU 49  49  49  LEU LEU C . n 
C 1 50  THR 50  50  50  THR THR C . n 
C 1 51  ASP 51  51  51  ASP ASP C . n 
C 1 52  SER 52  52  52  SER SER C . n 
C 1 53  GLY 53  53  53  GLY GLY C . n 
C 1 54  THR 54  54  54  THR THR C . n 
C 1 55  ASN 55  55  55  ASN ASN C . n 
C 1 56  ALA 56  56  56  ALA ALA C . n 
C 1 57  MET 57  57  57  MET MET C . n 
C 1 58  SER 58  58  58  SER SER C . n 
C 1 59  ASP 59  59  59  ASP ASP C . n 
C 1 60  HIS 60  60  60  HIS HIS C . n 
C 1 61  GLN 61  61  61  GLN GLN C . n 
C 1 62  TRP 62  62  62  TRP TRP C . n 
C 1 63  ALA 63  63  63  ALA ALA C . n 
C 1 64  ALA 64  64  64  ALA ALA C . n 
C 1 65  MET 65  65  65  MET MET C . n 
C 1 66  ILE 66  66  66  ILE ILE C . n 
C 1 67  THR 67  67  67  THR THR C . n 
C 1 68  GLY 68  68  68  GLY GLY C . n 
C 1 69  ASP 69  69  69  ASP ASP C . n 
C 1 70  GLU 70  70  70  GLU GLU C . n 
C 1 71  ALA 71  71  71  ALA ALA C . n 
C 1 72  TYR 72  72  72  TYR TYR C . n 
C 1 73  ALA 73  73  73  ALA ALA C . n 
C 1 74  GLY 74  74  74  GLY GLY C . n 
C 1 75  SER 75  75  75  SER SER C . n 
C 1 76  ARG 76  76  76  ARG ARG C . n 
C 1 77  ASN 77  77  77  ASN ASN C . n 
C 1 78  TYR 78  78  78  TYR TYR C . n 
C 1 79  TYR 79  79  79  TYR TYR C . n 
C 1 80  ASP 80  80  80  ASP ASP C . n 
C 1 81  LEU 81  81  81  LEU LEU C . n 
C 1 82  LYS 82  82  82  LYS LYS C . n 
C 1 83  ASP 83  83  83  ASP ASP C . n 
C 1 84  LYS 84  84  84  LYS LYS C . n 
C 1 85  ALA 85  85  85  ALA ALA C . n 
C 1 86  LYS 86  86  86  LYS LYS C . n 
C 1 87  GLU 87  87  87  GLU GLU C . n 
C 1 88  LEU 88  88  88  LEU LEU C . n 
C 1 89  PHE 89  89  89  PHE PHE C . n 
C 1 90  ASN 90  90  90  ASN ASN C . n 
C 1 91  TYR 91  91  91  TYR TYR C . n 
C 1 92  ASP 92  92  92  ASP ASP C . n 
C 1 93  TYR 93  93  93  TYR TYR C . n 
C 1 94  ILE 94  94  94  ILE ILE C . n 
C 1 95  ILE 95  95  95  ILE ILE C . n 
C 1 96  PRO 96  96  96  PRO PRO C . n 
C 1 97  ALA 97  97  97  ALA ALA C . n 
C 1 98  HIS 98  98  98  HIS HIS C . n 
C 1 99  GLN 99  99  99  GLN GLN C . n 
C 1 100 GLY 100 100 100 GLY GLY C . n 
C 1 101 ARG 101 101 101 ARG ARG C . n 
C 1 102 GLY 102 102 102 GLY GLY C . n 
C 1 103 ALA 103 103 103 ALA ALA C . n 
C 1 104 GLU 104 104 104 GLU GLU C . n 
C 1 105 ASN 105 105 105 ASN ASN C . n 
C 1 106 ILE 106 106 106 ILE ILE C . n 
C 1 107 LEU 107 107 107 LEU LEU C . n 
C 1 108 PHE 108 108 108 PHE PHE C . n 
C 1 109 PRO 109 109 109 PRO PRO C . n 
C 1 110 VAL 110 110 110 VAL VAL C . n 
C 1 111 LEU 111 111 111 LEU LEU C . n 
C 1 112 LEU 112 112 112 LEU LEU C . n 
C 1 113 LYS 113 113 113 LYS LYS C . n 
C 1 114 TYR 114 114 114 TYR TYR C . n 
C 1 115 LYS 115 115 115 LYS LYS C . n 
C 1 116 GLN 116 116 116 GLN GLN C . n 
C 1 117 LYS 117 117 117 LYS LYS C . n 
C 1 118 GLU 118 118 118 GLU GLU C . n 
C 1 119 GLY 119 119 119 GLY GLY C . n 
C 1 120 LYS 120 120 120 LYS LYS C . n 
C 1 121 ALA 121 121 121 ALA ALA C . n 
C 1 122 LYS 122 122 122 LYS LYS C . n 
C 1 123 ASN 123 123 123 ASN ASN C . n 
C 1 124 PRO 124 124 124 PRO PRO C . n 
C 1 125 VAL 125 125 125 VAL VAL C . n 
C 1 126 PHE 126 126 126 PHE PHE C . n 
C 1 127 ILE 127 127 127 ILE ILE C . n 
C 1 128 SER 128 128 128 SER SER C . n 
C 1 129 ASN 129 129 129 ASN ASN C . n 
C 1 130 PHE 130 130 130 PHE PHE C . n 
C 1 131 HIS 131 131 131 HIS HIS C . n 
C 1 132 PHE 132 132 132 PHE PHE C . n 
C 1 133 ASP 133 133 133 ASP ASP C . n 
C 1 134 THR 134 134 134 THR THR C . n 
C 1 135 THR 135 135 135 THR THR C . n 
C 1 136 ALA 136 136 136 ALA ALA C . n 
C 1 137 ALA 137 137 137 ALA ALA C . n 
C 1 138 HIS 138 138 138 HIS HIS C . n 
C 1 139 VAL 139 139 139 VAL VAL C . n 
C 1 140 GLU 140 140 140 GLU GLU C . n 
C 1 141 LEU 141 141 141 LEU LEU C . n 
C 1 142 ASN 142 142 142 ASN ASN C . n 
C 1 143 GLY 143 143 143 GLY GLY C . n 
C 1 144 CYS 144 144 144 CYS CYS C . n 
C 1 145 LYS 145 145 145 LYS LYS C . n 
C 1 146 ALA 146 146 146 ALA ALA C . n 
C 1 147 ILE 147 147 147 ILE ILE C . n 
C 1 148 ASN 148 148 148 ASN ASN C . n 
C 1 149 ILE 149 149 149 ILE ILE C . n 
C 1 150 VAL 150 150 150 VAL VAL C . n 
C 1 151 THR 151 151 151 THR THR C . n 
C 1 152 GLU 152 152 152 GLU GLU C . n 
C 1 153 LYS 153 153 153 LYS LYS C . n 
C 1 154 ALA 154 154 154 ALA ALA C . n 
C 1 155 PHE 155 155 155 PHE PHE C . n 
C 1 156 ASP 156 156 156 ASP ASP C . n 
C 1 157 SER 157 157 157 SER SER C . n 
C 1 158 GLU 158 158 158 GLU GLU C . n 
C 1 159 THR 159 159 159 THR THR C . n 
C 1 160 TYR 160 160 160 TYR TYR C . n 
C 1 161 ASP 161 161 161 ASP ASP C . n 
C 1 162 ASP 162 162 162 ASP ASP C . n 
C 1 163 TRP 163 163 163 TRP TRP C . n 
C 1 164 LYS 164 164 164 LYS LYS C . n 
C 1 165 GLY 165 165 165 GLY GLY C . n 
C 1 166 ASP 166 166 166 ASP ASP C . n 
C 1 167 PHE 167 167 167 PHE PHE C . n 
C 1 168 ASP 168 168 168 ASP ASP C . n 
C 1 169 ILE 169 169 169 ILE ILE C . n 
C 1 170 LYS 170 170 170 LYS LYS C . n 
C 1 171 LYS 171 171 171 LYS LYS C . n 
C 1 172 LEU 172 172 172 LEU LEU C . n 
C 1 173 LYS 173 173 173 LYS LYS C . n 
C 1 174 GLU 174 174 174 GLU GLU C . n 
C 1 175 ASN 175 175 175 ASN ASN C . n 
C 1 176 ILE 176 176 176 ILE ILE C . n 
C 1 177 ALA 177 177 177 ALA ALA C . n 
C 1 178 GLN 178 178 178 GLN GLN C . n 
C 1 179 HIS 179 179 179 HIS HIS C . n 
C 1 180 GLY 180 180 180 GLY GLY C . n 
C 1 181 ALA 181 181 181 ALA ALA C . n 
C 1 182 ASP 182 182 182 ASP ASP C . n 
C 1 183 ASN 183 183 183 ASN ASN C . n 
C 1 184 ILE 184 184 184 ILE ILE C . n 
C 1 185 VAL 185 185 185 VAL VAL C . n 
C 1 186 ALA 186 186 186 ALA ALA C . n 
C 1 187 ILE 187 187 187 ILE ILE C . n 
C 1 188 VAL 188 188 188 VAL VAL C . n 
C 1 189 SER 189 189 189 SER SER C . n 
C 1 190 THR 190 190 190 THR THR C . n 
C 1 191 VAL 191 191 191 VAL VAL C . n 
C 1 192 THR 192 192 192 THR THR C . n 
C 1 193 CYS 193 193 193 CYS CYS C . n 
C 1 194 ASN 194 194 194 ASN ASN C . n 
C 1 195 SER 195 195 195 SER SER C . n 
C 1 196 ALA 196 196 196 ALA ALA C . n 
C 1 197 GLY 197 197 197 GLY GLY C . n 
C 1 198 GLY 198 198 198 GLY GLY C . n 
C 1 199 GLN 199 199 199 GLN GLN C . n 
C 1 200 PRO 200 200 200 PRO PRO C . n 
C 1 201 VAL 201 201 201 VAL VAL C . n 
C 1 202 SER 202 202 202 SER SER C . n 
C 1 203 MET 203 203 203 MET MET C . n 
C 1 204 SER 204 204 204 SER SER C . n 
C 1 205 ASN 205 205 205 ASN ASN C . n 
C 1 206 LEU 206 206 206 LEU LEU C . n 
C 1 207 LYS 207 207 207 LYS LYS C . n 
C 1 208 GLU 208 208 208 GLU GLU C . n 
C 1 209 VAL 209 209 209 VAL VAL C . n 
C 1 210 TYR 210 210 210 TYR TYR C . n 
C 1 211 GLU 211 211 211 GLU GLU C . n 
C 1 212 ILE 212 212 212 ILE ILE C . n 
C 1 213 ALA 213 213 213 ALA ALA C . n 
C 1 214 LYS 214 214 214 LYS LYS C . n 
C 1 215 GLN 215 215 215 GLN GLN C . n 
C 1 216 HIS 216 216 216 HIS HIS C . n 
C 1 217 GLY 217 217 217 GLY GLY C . n 
C 1 218 ILE 218 218 218 ILE ILE C . n 
C 1 219 PHE 219 219 219 PHE PHE C . n 
C 1 220 VAL 220 220 220 VAL VAL C . n 
C 1 221 VAL 221 221 221 VAL VAL C . n 
C 1 222 MET 222 222 222 MET MET C . n 
C 1 223 ASP 223 223 223 ASP ASP C . n 
C 1 224 SER 224 224 224 SER SER C . n 
C 1 225 ALA 225 225 225 ALA ALA C . n 
C 1 226 ARG 226 226 226 ARG ARG C . n 
C 1 227 PHE 227 227 227 PHE PHE C . n 
C 1 228 CYS 228 228 228 CYS CYS C . n 
C 1 229 GLU 229 229 229 GLU GLU C . n 
C 1 230 ASN 230 230 230 ASN ASN C . n 
C 1 231 ALA 231 231 231 ALA ALA C . n 
C 1 232 TYR 232 232 232 TYR TYR C . n 
C 1 233 PHE 233 233 233 PHE PHE C . n 
C 1 234 ILE 234 234 234 ILE ILE C . n 
C 1 235 LYS 235 235 235 LYS LYS C . n 
C 1 236 ALA 236 236 236 ALA ALA C . n 
C 1 237 ARG 237 237 237 ARG ARG C . n 
C 1 238 ASP 238 238 238 ASP ASP C . n 
C 1 239 PRO 239 239 239 PRO PRO C . n 
C 1 240 LYS 240 240 240 LYS LYS C . n 
C 1 241 TYR 241 241 241 TYR TYR C . n 
C 1 242 LYS 242 242 242 LYS LYS C . n 
C 1 243 ASN 243 243 243 ASN ASN C . n 
C 1 244 ALA 244 244 244 ALA ALA C . n 
C 1 245 THR 245 245 245 THR THR C . n 
C 1 246 ILE 246 246 246 ILE ILE C . n 
C 1 247 LYS 247 247 247 LYS LYS C . n 
C 1 248 GLU 248 248 248 GLU GLU C . n 
C 1 249 VAL 249 249 249 VAL VAL C . n 
C 1 250 ILE 250 250 250 ILE ILE C . n 
C 1 251 PHE 251 251 251 PHE PHE C . n 
C 1 252 ASP 252 252 252 ASP ASP C . n 
C 1 253 MET 253 253 253 MET MET C . n 
C 1 254 TYR 254 254 254 TYR TYR C . n 
C 1 255 LYS 255 255 255 LYS LYS C . n 
C 1 256 TYR 256 256 256 TYR TYR C . n 
C 1 257 ALA 257 257 257 ALA ALA C . n 
C 1 258 ASP 258 258 258 ASP ASP C . n 
C 1 259 ALA 259 259 259 ALA ALA C . n 
C 1 260 LEU 260 260 260 LEU LEU C . n 
C 1 261 THR 261 261 261 THR THR C . n 
C 1 262 MET 262 262 262 MET MET C . n 
C 1 263 SER 263 263 263 SER SER C . n 
C 1 264 ALA 264 264 264 ALA ALA C . n 
C 1 265 LYS 265 265 265 LYS LYS C . n 
C 1 266 LYS 266 266 266 LYS LYS C . n 
C 1 267 ASP 267 267 267 ASP ASP C . n 
C 1 268 PRO 268 268 268 PRO PRO C . n 
C 1 269 LEU 269 269 269 LEU LEU C . n 
C 1 270 LEU 270 270 270 LEU LEU C . n 
C 1 271 ASN 271 271 271 ASN ASN C . n 
C 1 272 ILE 272 272 272 ILE ILE C . n 
C 1 273 GLY 273 273 273 GLY GLY C . n 
C 1 274 GLY 274 274 274 GLY GLY C . n 
C 1 275 LEU 275 275 275 LEU LEU C . n 
C 1 276 VAL 276 276 276 VAL VAL C . n 
C 1 277 ALA 277 277 277 ALA ALA C . n 
C 1 278 ILE 278 278 278 ILE ILE C . n 
C 1 279 ARG 279 279 279 ARG ARG C . n 
C 1 280 ASP 280 280 280 ASP ASP C . n 
C 1 281 ASN 281 281 281 ASN ASN C . n 
C 1 282 GLU 282 282 282 GLU GLU C . n 
C 1 283 GLU 283 283 283 GLU GLU C . n 
C 1 284 ILE 284 284 284 ILE ILE C . n 
C 1 285 PHE 285 285 285 PHE PHE C . n 
C 1 286 THR 286 286 286 THR THR C . n 
C 1 287 LEU 287 287 287 LEU LEU C . n 
C 1 288 ALA 288 288 288 ALA ALA C . n 
C 1 289 ARG 289 289 289 ARG ARG C . n 
C 1 290 GLN 290 290 290 GLN GLN C . n 
C 1 291 ARG 291 291 291 ARG ARG C . n 
C 1 292 CYS 292 292 292 CYS CYS C . n 
C 1 293 VAL 293 293 293 VAL VAL C . n 
C 1 294 PRO 294 294 294 PRO PRO C . n 
C 1 295 MET 295 295 295 MET MET C . n 
C 1 296 GLU 296 296 296 GLU GLU C . n 
C 1 297 GLY 297 297 297 GLY GLY C . n 
C 1 298 PHE 298 298 298 PHE PHE C . n 
C 1 299 VAL 299 299 299 VAL VAL C . n 
C 1 300 THR 300 300 300 THR THR C . n 
C 1 301 TYR 301 301 301 TYR TYR C . n 
C 1 302 GLY 302 302 302 GLY GLY C . n 
C 1 303 GLY 303 303 303 GLY GLY C . n 
C 1 304 LEU 304 304 304 LEU LEU C . n 
C 1 305 ALA 305 305 305 ALA ALA C . n 
C 1 306 GLY 306 306 306 GLY GLY C . n 
C 1 307 ARG 307 307 307 ARG ARG C . n 
C 1 308 ASP 308 308 308 ASP ASP C . n 
C 1 309 MET 309 309 309 MET MET C . n 
C 1 310 ALA 310 310 310 ALA ALA C . n 
C 1 311 ALA 311 311 311 ALA ALA C . n 
C 1 312 MET 312 312 312 MET MET C . n 
C 1 313 VAL 313 313 313 VAL VAL C . n 
C 1 314 GLN 314 314 314 GLN GLN C . n 
C 1 315 GLY 315 315 315 GLY GLY C . n 
C 1 316 LEU 316 316 316 LEU LEU C . n 
C 1 317 GLU 317 317 317 GLU GLU C . n 
C 1 318 GLU 318 318 318 GLU GLU C . n 
C 1 319 GLY 319 319 319 GLY GLY C . n 
C 1 320 THR 320 320 320 THR THR C . n 
C 1 321 GLU 321 321 321 GLU GLU C . n 
C 1 322 GLU 322 322 322 GLU GLU C . n 
C 1 323 GLU 323 323 323 GLU GLU C . n 
C 1 324 TYR 324 324 324 TYR TYR C . n 
C 1 325 LEU 325 325 325 LEU LEU C . n 
C 1 326 HIS 326 326 326 HIS HIS C . n 
C 1 327 TYR 327 327 327 TYR TYR C . n 
C 1 328 ARG 328 328 328 ARG ARG C . n 
C 1 329 ILE 329 329 329 ILE ILE C . n 
C 1 330 GLY 330 330 330 GLY GLY C . n 
C 1 331 GLN 331 331 331 GLN GLN C . n 
C 1 332 VAL 332 332 332 VAL VAL C . n 
C 1 333 LYS 333 333 333 LYS LYS C . n 
C 1 334 TYR 334 334 334 TYR TYR C . n 
C 1 335 LEU 335 335 335 LEU LEU C . n 
C 1 336 GLY 336 336 336 GLY GLY C . n 
C 1 337 ASP 337 337 337 ASP ASP C . n 
C 1 338 ARG 338 338 338 ARG ARG C . n 
C 1 339 LEU 339 339 339 LEU LEU C . n 
C 1 340 ARG 340 340 340 ARG ARG C . n 
C 1 341 GLU 341 341 341 GLU GLU C . n 
C 1 342 ALA 342 342 342 ALA ALA C . n 
C 1 343 GLY 343 343 343 GLY GLY C . n 
C 1 344 ILE 344 344 344 ILE ILE C . n 
C 1 345 PRO 345 345 345 PRO PRO C . n 
C 1 346 ILE 346 346 346 ILE ILE C . n 
C 1 347 GLN 347 347 347 GLN GLN C . n 
C 1 348 TYR 348 348 348 TYR TYR C . n 
C 1 349 PRO 349 349 349 PRO PRO C . n 
C 1 350 THR 350 350 350 THR THR C . n 
C 1 351 GLY 351 351 351 GLY GLY C . n 
C 1 352 GLY 352 352 352 GLY GLY C . n 
C 1 353 HIS 353 353 353 HIS HIS C . n 
C 1 354 ALA 354 354 354 ALA ALA C . n 
C 1 355 VAL 355 355 355 VAL VAL C . n 
C 1 356 PHE 356 356 356 PHE PHE C . n 
C 1 357 VAL 357 357 357 VAL VAL C . n 
C 1 358 ASP 358 358 358 ASP ASP C . n 
C 1 359 CYS 359 359 359 CYS CYS C . n 
C 1 360 LYS 360 360 360 LYS LYS C . n 
C 1 361 LYS 361 361 361 LYS LYS C . n 
C 1 362 LEU 362 362 362 LEU LEU C . n 
C 1 363 VAL 363 363 363 VAL VAL C . n 
C 1 364 PRO 364 364 364 PRO PRO C . n 
C 1 365 GLN 365 365 365 GLN GLN C . n 
C 1 366 ILE 366 366 366 ILE ILE C . n 
C 1 367 PRO 367 367 367 PRO PRO C . n 
C 1 368 GLY 368 368 368 GLY GLY C . n 
C 1 369 ASP 369 369 369 ASP ASP C . n 
C 1 370 GLN 370 370 370 GLN GLN C . n 
C 1 371 PHE 371 371 371 PHE PHE C . n 
C 1 372 PRO 372 372 372 PRO PRO C . n 
C 1 373 ALA 373 373 373 ALA ALA C . n 
C 1 374 GLN 374 374 374 GLN GLN C . n 
C 1 375 ALA 375 375 375 ALA ALA C . n 
C 1 376 VAL 376 376 376 VAL VAL C . n 
C 1 377 ILE 377 377 377 ILE ILE C . n 
C 1 378 ASN 378 378 378 ASN ASN C . n 
C 1 379 ALA 379 379 379 ALA ALA C . n 
C 1 380 LEU 380 380 380 LEU LEU C . n 
C 1 381 TYR 381 381 381 TYR TYR C . n 
C 1 382 LEU 382 382 382 LEU LEU C . n 
C 1 383 GLU 383 383 383 GLU GLU C . n 
C 1 384 SER 384 384 384 SER SER C . n 
C 1 385 GLY 385 385 385 GLY GLY C . n 
C 1 386 VAL 386 386 386 VAL VAL C . n 
C 1 387 ARG 387 387 387 ARG ARG C . n 
C 1 388 ALA 388 388 388 ALA ALA C . n 
C 1 389 VAL 389 389 389 VAL VAL C . n 
C 1 390 GLU 390 390 390 GLU GLU C . n 
C 1 391 ILE 391 391 391 ILE ILE C . n 
C 1 392 GLY 392 392 392 GLY GLY C . n 
C 1 393 SER 393 393 393 SER SER C . n 
C 1 394 PHE 394 394 394 PHE PHE C . n 
C 1 395 LEU 395 395 395 LEU LEU C . n 
C 1 396 LEU 396 396 396 LEU LEU C . n 
C 1 397 GLY 397 397 397 GLY GLY C . n 
C 1 398 ARG 398 398 398 ARG ARG C . n 
C 1 399 ASP 399 399 ?   ?   ?   C . n 
C 1 400 PRO 400 400 ?   ?   ?   C . n 
C 1 401 ALA 401 401 ?   ?   ?   C . n 
C 1 402 THR 402 402 ?   ?   ?   C . n 
C 1 403 GLY 403 403 ?   ?   ?   C . n 
C 1 404 GLU 404 404 ?   ?   ?   C . n 
C 1 405 GLN 405 405 ?   ?   ?   C . n 
C 1 406 LYS 406 406 406 LYS LYS C . n 
C 1 407 HIS 407 407 407 HIS HIS C . n 
C 1 408 ALA 408 408 408 ALA ALA C . n 
C 1 409 ASP 409 409 409 ASP ASP C . n 
C 1 410 MET 410 410 410 MET MET C . n 
C 1 411 GLU 411 411 411 GLU GLU C . n 
C 1 412 PHE 412 412 412 PHE PHE C . n 
C 1 413 MET 413 413 413 MET MET C . n 
C 1 414 ARG 414 414 414 ARG ARG C . n 
C 1 415 LEU 415 415 415 LEU LEU C . n 
C 1 416 THR 416 416 416 THR THR C . n 
C 1 417 ILE 417 417 417 ILE ILE C . n 
C 1 418 ALA 418 418 418 ALA ALA C . n 
C 1 419 ARG 419 419 419 ARG ARG C . n 
C 1 420 ARG 420 420 420 ARG ARG C . n 
C 1 421 VAL 421 421 421 VAL VAL C . n 
C 1 422 TYR 422 422 422 TYR TYR C . n 
C 1 423 THR 423 423 423 THR THR C . n 
C 1 424 ASN 424 424 424 ASN ASN C . n 
C 1 425 ASP 425 425 425 ASP ASP C . n 
C 1 426 HIS 426 426 426 HIS HIS C . n 
C 1 427 MET 427 427 427 MET MET C . n 
C 1 428 ASP 428 428 428 ASP ASP C . n 
C 1 429 TYR 429 429 429 TYR TYR C . n 
C 1 430 ILE 430 430 430 ILE ILE C . n 
C 1 431 ALA 431 431 431 ALA ALA C . n 
C 1 432 ASP 432 432 432 ASP ASP C . n 
C 1 433 ALA 433 433 433 ALA ALA C . n 
C 1 434 LEU 434 434 434 LEU LEU C . n 
C 1 435 ILE 435 435 435 ILE ILE C . n 
C 1 436 GLY 436 436 436 GLY GLY C . n 
C 1 437 LEU 437 437 437 LEU LEU C . n 
C 1 438 LYS 438 438 438 LYS LYS C . n 
C 1 439 GLU 439 439 439 GLU GLU C . n 
C 1 440 LYS 440 440 440 LYS LYS C . n 
C 1 441 PHE 441 441 441 PHE PHE C . n 
C 1 442 ALA 442 442 442 ALA ALA C . n 
C 1 443 THR 443 443 443 THR THR C . n 
C 1 444 LEU 444 444 444 LEU LEU C . n 
C 1 445 LYS 445 445 445 LYS LYS C . n 
C 1 446 GLY 446 446 446 GLY GLY C . n 
C 1 447 LEU 447 447 447 LEU LEU C . n 
C 1 448 GLU 448 448 448 GLU GLU C . n 
C 1 449 PHE 449 449 449 PHE PHE C . n 
C 1 450 GLU 450 450 450 GLU GLU C . n 
C 1 451 TYR 451 451 451 TYR TYR C . n 
C 1 452 GLU 452 452 452 GLU GLU C . n 
C 1 453 PRO 453 453 453 PRO PRO C . n 
C 1 454 PRO 454 454 454 PRO PRO C . n 
C 1 455 VAL 455 455 455 VAL VAL C . n 
C 1 456 LEU 456 456 456 LEU LEU C . n 
C 1 457 ARG 457 457 457 ARG ARG C . n 
C 1 458 HIS 458 458 458 HIS HIS C . n 
C 1 459 PHE 459 459 459 PHE PHE C . n 
C 1 460 THR 460 460 460 THR THR C . n 
C 1 461 ALA 461 461 461 ALA ALA C . n 
C 1 462 ARG 462 462 462 ARG ARG C . n 
C 1 463 LEU 463 463 463 LEU LEU C . n 
C 1 464 LYS 464 464 464 LYS LYS C . n 
C 1 465 PRO 465 465 465 PRO PRO C . n 
C 1 466 ILE 466 466 466 ILE ILE C . n 
C 1 467 GLU 467 467 ?   ?   ?   C . n 
D 1 1   MET 1   1   ?   ?   ?   D . n 
D 1 2   ALA 2   2   2   ALA ALA D . n 
D 1 3   LYS 3   3   3   LYS LYS D . n 
D 1 4   ARG 4   4   4   ARG ARG D . n 
D 1 5   ILE 5   5   5   ILE ILE D . n 
D 1 6   VAL 6   6   6   VAL VAL D . n 
D 1 7   GLU 7   7   7   GLU GLU D . n 
D 1 8   PRO 8   8   8   PRO PRO D . n 
D 1 9   PHE 9   9   9   PHE PHE D . n 
D 1 10  ARG 10  10  10  ARG ARG D . n 
D 1 11  ILE 11  11  11  ILE ILE D . n 
D 1 12  LYS 12  12  12  LYS LYS D . n 
D 1 13  MET 13  13  13  MET MET D . n 
D 1 14  VAL 14  14  14  VAL VAL D . n 
D 1 15  GLU 15  15  15  GLU GLU D . n 
D 1 16  LYS 16  16  16  LYS LYS D . n 
D 1 17  ILE 17  17  17  ILE ILE D . n 
D 1 18  ARG 18  18  18  ARG ARG D . n 
D 1 19  VAL 19  19  19  VAL VAL D . n 
D 1 20  PRO 20  20  20  PRO PRO D . n 
D 1 21  SER 21  21  21  SER SER D . n 
D 1 22  ARG 22  22  22  ARG ARG D . n 
D 1 23  GLU 23  23  23  GLU GLU D . n 
D 1 24  GLU 24  24  24  GLU GLU D . n 
D 1 25  ARG 25  25  25  ARG ARG D . n 
D 1 26  GLU 26  26  26  GLU GLU D . n 
D 1 27  ALA 27  27  27  ALA ALA D . n 
D 1 28  ALA 28  28  28  ALA ALA D . n 
D 1 29  LEU 29  29  29  LEU LEU D . n 
D 1 30  LYS 30  30  30  LYS LYS D . n 
D 1 31  GLU 31  31  31  GLU GLU D . n 
D 1 32  ALA 32  32  32  ALA ALA D . n 
D 1 33  GLY 33  33  33  GLY GLY D . n 
D 1 34  TYR 34  34  34  TYR TYR D . n 
D 1 35  ASN 35  35  35  ASN ASN D . n 
D 1 36  PRO 36  36  36  PRO PRO D . n 
D 1 37  PHE 37  37  37  PHE PHE D . n 
D 1 38  LEU 38  38  38  LEU LEU D . n 
D 1 39  LEU 39  39  39  LEU LEU D . n 
D 1 40  PRO 40  40  40  PRO PRO D . n 
D 1 41  SER 41  41  41  SER SER D . n 
D 1 42  SER 42  42  42  SER SER D . n 
D 1 43  ALA 43  43  43  ALA ALA D . n 
D 1 44  VAL 44  44  44  VAL VAL D . n 
D 1 45  TYR 45  45  45  TYR TYR D . n 
D 1 46  ILE 46  46  46  ILE ILE D . n 
D 1 47  ASP 47  47  47  ASP ASP D . n 
D 1 48  LEU 48  48  48  LEU LEU D . n 
D 1 49  LEU 49  49  49  LEU LEU D . n 
D 1 50  THR 50  50  50  THR THR D . n 
D 1 51  ASP 51  51  51  ASP ASP D . n 
D 1 52  SER 52  52  52  SER SER D . n 
D 1 53  GLY 53  53  53  GLY GLY D . n 
D 1 54  THR 54  54  54  THR THR D . n 
D 1 55  ASN 55  55  55  ASN ASN D . n 
D 1 56  ALA 56  56  56  ALA ALA D . n 
D 1 57  MET 57  57  57  MET MET D . n 
D 1 58  SER 58  58  58  SER SER D . n 
D 1 59  ASP 59  59  59  ASP ASP D . n 
D 1 60  HIS 60  60  60  HIS HIS D . n 
D 1 61  GLN 61  61  61  GLN GLN D . n 
D 1 62  TRP 62  62  62  TRP TRP D . n 
D 1 63  ALA 63  63  63  ALA ALA D . n 
D 1 64  ALA 64  64  64  ALA ALA D . n 
D 1 65  MET 65  65  65  MET MET D . n 
D 1 66  ILE 66  66  66  ILE ILE D . n 
D 1 67  THR 67  67  67  THR THR D . n 
D 1 68  GLY 68  68  68  GLY GLY D . n 
D 1 69  ASP 69  69  69  ASP ASP D . n 
D 1 70  GLU 70  70  70  GLU GLU D . n 
D 1 71  ALA 71  71  71  ALA ALA D . n 
D 1 72  TYR 72  72  72  TYR TYR D . n 
D 1 73  ALA 73  73  73  ALA ALA D . n 
D 1 74  GLY 74  74  74  GLY GLY D . n 
D 1 75  SER 75  75  75  SER SER D . n 
D 1 76  ARG 76  76  76  ARG ARG D . n 
D 1 77  ASN 77  77  77  ASN ASN D . n 
D 1 78  TYR 78  78  78  TYR TYR D . n 
D 1 79  TYR 79  79  79  TYR TYR D . n 
D 1 80  ASP 80  80  80  ASP ASP D . n 
D 1 81  LEU 81  81  81  LEU LEU D . n 
D 1 82  LYS 82  82  82  LYS LYS D . n 
D 1 83  ASP 83  83  83  ASP ASP D . n 
D 1 84  LYS 84  84  84  LYS LYS D . n 
D 1 85  ALA 85  85  85  ALA ALA D . n 
D 1 86  LYS 86  86  86  LYS LYS D . n 
D 1 87  GLU 87  87  87  GLU GLU D . n 
D 1 88  LEU 88  88  88  LEU LEU D . n 
D 1 89  PHE 89  89  89  PHE PHE D . n 
D 1 90  ASN 90  90  90  ASN ASN D . n 
D 1 91  TYR 91  91  91  TYR TYR D . n 
D 1 92  ASP 92  92  92  ASP ASP D . n 
D 1 93  TYR 93  93  93  TYR TYR D . n 
D 1 94  ILE 94  94  94  ILE ILE D . n 
D 1 95  ILE 95  95  95  ILE ILE D . n 
D 1 96  PRO 96  96  96  PRO PRO D . n 
D 1 97  ALA 97  97  97  ALA ALA D . n 
D 1 98  HIS 98  98  98  HIS HIS D . n 
D 1 99  GLN 99  99  99  GLN GLN D . n 
D 1 100 GLY 100 100 100 GLY GLY D . n 
D 1 101 ARG 101 101 101 ARG ARG D . n 
D 1 102 GLY 102 102 102 GLY GLY D . n 
D 1 103 ALA 103 103 103 ALA ALA D . n 
D 1 104 GLU 104 104 104 GLU GLU D . n 
D 1 105 ASN 105 105 105 ASN ASN D . n 
D 1 106 ILE 106 106 106 ILE ILE D . n 
D 1 107 LEU 107 107 107 LEU LEU D . n 
D 1 108 PHE 108 108 108 PHE PHE D . n 
D 1 109 PRO 109 109 109 PRO PRO D . n 
D 1 110 VAL 110 110 110 VAL VAL D . n 
D 1 111 LEU 111 111 111 LEU LEU D . n 
D 1 112 LEU 112 112 112 LEU LEU D . n 
D 1 113 LYS 113 113 113 LYS LYS D . n 
D 1 114 TYR 114 114 114 TYR TYR D . n 
D 1 115 LYS 115 115 115 LYS LYS D . n 
D 1 116 GLN 116 116 116 GLN GLN D . n 
D 1 117 LYS 117 117 117 LYS LYS D . n 
D 1 118 GLU 118 118 118 GLU GLU D . n 
D 1 119 GLY 119 119 119 GLY GLY D . n 
D 1 120 LYS 120 120 120 LYS LYS D . n 
D 1 121 ALA 121 121 121 ALA ALA D . n 
D 1 122 LYS 122 122 122 LYS LYS D . n 
D 1 123 ASN 123 123 123 ASN ASN D . n 
D 1 124 PRO 124 124 124 PRO PRO D . n 
D 1 125 VAL 125 125 125 VAL VAL D . n 
D 1 126 PHE 126 126 126 PHE PHE D . n 
D 1 127 ILE 127 127 127 ILE ILE D . n 
D 1 128 SER 128 128 128 SER SER D . n 
D 1 129 ASN 129 129 129 ASN ASN D . n 
D 1 130 PHE 130 130 130 PHE PHE D . n 
D 1 131 HIS 131 131 131 HIS HIS D . n 
D 1 132 PHE 132 132 132 PHE PHE D . n 
D 1 133 ASP 133 133 133 ASP ASP D . n 
D 1 134 THR 134 134 134 THR THR D . n 
D 1 135 THR 135 135 135 THR THR D . n 
D 1 136 ALA 136 136 136 ALA ALA D . n 
D 1 137 ALA 137 137 137 ALA ALA D . n 
D 1 138 HIS 138 138 138 HIS HIS D . n 
D 1 139 VAL 139 139 139 VAL VAL D . n 
D 1 140 GLU 140 140 140 GLU GLU D . n 
D 1 141 LEU 141 141 141 LEU LEU D . n 
D 1 142 ASN 142 142 142 ASN ASN D . n 
D 1 143 GLY 143 143 143 GLY GLY D . n 
D 1 144 CYS 144 144 144 CYS CYS D . n 
D 1 145 LYS 145 145 145 LYS LYS D . n 
D 1 146 ALA 146 146 146 ALA ALA D . n 
D 1 147 ILE 147 147 147 ILE ILE D . n 
D 1 148 ASN 148 148 148 ASN ASN D . n 
D 1 149 ILE 149 149 149 ILE ILE D . n 
D 1 150 VAL 150 150 150 VAL VAL D . n 
D 1 151 THR 151 151 151 THR THR D . n 
D 1 152 GLU 152 152 152 GLU GLU D . n 
D 1 153 LYS 153 153 153 LYS LYS D . n 
D 1 154 ALA 154 154 154 ALA ALA D . n 
D 1 155 PHE 155 155 155 PHE PHE D . n 
D 1 156 ASP 156 156 156 ASP ASP D . n 
D 1 157 SER 157 157 157 SER SER D . n 
D 1 158 GLU 158 158 158 GLU GLU D . n 
D 1 159 THR 159 159 159 THR THR D . n 
D 1 160 TYR 160 160 160 TYR TYR D . n 
D 1 161 ASP 161 161 161 ASP ASP D . n 
D 1 162 ASP 162 162 162 ASP ASP D . n 
D 1 163 TRP 163 163 163 TRP TRP D . n 
D 1 164 LYS 164 164 164 LYS LYS D . n 
D 1 165 GLY 165 165 165 GLY GLY D . n 
D 1 166 ASP 166 166 166 ASP ASP D . n 
D 1 167 PHE 167 167 167 PHE PHE D . n 
D 1 168 ASP 168 168 168 ASP ASP D . n 
D 1 169 ILE 169 169 169 ILE ILE D . n 
D 1 170 LYS 170 170 170 LYS LYS D . n 
D 1 171 LYS 171 171 171 LYS LYS D . n 
D 1 172 LEU 172 172 172 LEU LEU D . n 
D 1 173 LYS 173 173 173 LYS LYS D . n 
D 1 174 GLU 174 174 174 GLU GLU D . n 
D 1 175 ASN 175 175 175 ASN ASN D . n 
D 1 176 ILE 176 176 176 ILE ILE D . n 
D 1 177 ALA 177 177 177 ALA ALA D . n 
D 1 178 GLN 178 178 178 GLN GLN D . n 
D 1 179 HIS 179 179 179 HIS HIS D . n 
D 1 180 GLY 180 180 180 GLY GLY D . n 
D 1 181 ALA 181 181 181 ALA ALA D . n 
D 1 182 ASP 182 182 182 ASP ASP D . n 
D 1 183 ASN 183 183 183 ASN ASN D . n 
D 1 184 ILE 184 184 184 ILE ILE D . n 
D 1 185 VAL 185 185 185 VAL VAL D . n 
D 1 186 ALA 186 186 186 ALA ALA D . n 
D 1 187 ILE 187 187 187 ILE ILE D . n 
D 1 188 VAL 188 188 188 VAL VAL D . n 
D 1 189 SER 189 189 189 SER SER D . n 
D 1 190 THR 190 190 190 THR THR D . n 
D 1 191 VAL 191 191 191 VAL VAL D . n 
D 1 192 THR 192 192 192 THR THR D . n 
D 1 193 CYS 193 193 193 CYS CYS D . n 
D 1 194 ASN 194 194 194 ASN ASN D . n 
D 1 195 SER 195 195 195 SER SER D . n 
D 1 196 ALA 196 196 196 ALA ALA D . n 
D 1 197 GLY 197 197 197 GLY GLY D . n 
D 1 198 GLY 198 198 198 GLY GLY D . n 
D 1 199 GLN 199 199 199 GLN GLN D . n 
D 1 200 PRO 200 200 200 PRO PRO D . n 
D 1 201 VAL 201 201 201 VAL VAL D . n 
D 1 202 SER 202 202 202 SER SER D . n 
D 1 203 MET 203 203 203 MET MET D . n 
D 1 204 SER 204 204 204 SER SER D . n 
D 1 205 ASN 205 205 205 ASN ASN D . n 
D 1 206 LEU 206 206 206 LEU LEU D . n 
D 1 207 LYS 207 207 207 LYS LYS D . n 
D 1 208 GLU 208 208 208 GLU GLU D . n 
D 1 209 VAL 209 209 209 VAL VAL D . n 
D 1 210 TYR 210 210 210 TYR TYR D . n 
D 1 211 GLU 211 211 211 GLU GLU D . n 
D 1 212 ILE 212 212 212 ILE ILE D . n 
D 1 213 ALA 213 213 213 ALA ALA D . n 
D 1 214 LYS 214 214 214 LYS LYS D . n 
D 1 215 GLN 215 215 215 GLN GLN D . n 
D 1 216 HIS 216 216 216 HIS HIS D . n 
D 1 217 GLY 217 217 217 GLY GLY D . n 
D 1 218 ILE 218 218 218 ILE ILE D . n 
D 1 219 PHE 219 219 219 PHE PHE D . n 
D 1 220 VAL 220 220 220 VAL VAL D . n 
D 1 221 VAL 221 221 221 VAL VAL D . n 
D 1 222 MET 222 222 222 MET MET D . n 
D 1 223 ASP 223 223 223 ASP ASP D . n 
D 1 224 SER 224 224 224 SER SER D . n 
D 1 225 ALA 225 225 225 ALA ALA D . n 
D 1 226 ARG 226 226 226 ARG ARG D . n 
D 1 227 PHE 227 227 227 PHE PHE D . n 
D 1 228 CYS 228 228 228 CYS CYS D . n 
D 1 229 GLU 229 229 229 GLU GLU D . n 
D 1 230 ASN 230 230 230 ASN ASN D . n 
D 1 231 ALA 231 231 231 ALA ALA D . n 
D 1 232 TYR 232 232 232 TYR TYR D . n 
D 1 233 PHE 233 233 233 PHE PHE D . n 
D 1 234 ILE 234 234 234 ILE ILE D . n 
D 1 235 LYS 235 235 235 LYS LYS D . n 
D 1 236 ALA 236 236 236 ALA ALA D . n 
D 1 237 ARG 237 237 237 ARG ARG D . n 
D 1 238 ASP 238 238 238 ASP ASP D . n 
D 1 239 PRO 239 239 239 PRO PRO D . n 
D 1 240 LYS 240 240 240 LYS LYS D . n 
D 1 241 TYR 241 241 241 TYR TYR D . n 
D 1 242 LYS 242 242 242 LYS LYS D . n 
D 1 243 ASN 243 243 243 ASN ASN D . n 
D 1 244 ALA 244 244 244 ALA ALA D . n 
D 1 245 THR 245 245 245 THR THR D . n 
D 1 246 ILE 246 246 246 ILE ILE D . n 
D 1 247 LYS 247 247 247 LYS LYS D . n 
D 1 248 GLU 248 248 248 GLU GLU D . n 
D 1 249 VAL 249 249 249 VAL VAL D . n 
D 1 250 ILE 250 250 250 ILE ILE D . n 
D 1 251 PHE 251 251 251 PHE PHE D . n 
D 1 252 ASP 252 252 252 ASP ASP D . n 
D 1 253 MET 253 253 253 MET MET D . n 
D 1 254 TYR 254 254 254 TYR TYR D . n 
D 1 255 LYS 255 255 255 LYS LYS D . n 
D 1 256 TYR 256 256 256 TYR TYR D . n 
D 1 257 ALA 257 257 257 ALA ALA D . n 
D 1 258 ASP 258 258 258 ASP ASP D . n 
D 1 259 ALA 259 259 259 ALA ALA D . n 
D 1 260 LEU 260 260 260 LEU LEU D . n 
D 1 261 THR 261 261 261 THR THR D . n 
D 1 262 MET 262 262 262 MET MET D . n 
D 1 263 SER 263 263 263 SER SER D . n 
D 1 264 ALA 264 264 264 ALA ALA D . n 
D 1 265 LYS 265 265 265 LYS LYS D . n 
D 1 266 LYS 266 266 266 LYS LYS D . n 
D 1 267 ASP 267 267 267 ASP ASP D . n 
D 1 268 PRO 268 268 268 PRO PRO D . n 
D 1 269 LEU 269 269 269 LEU LEU D . n 
D 1 270 LEU 270 270 270 LEU LEU D . n 
D 1 271 ASN 271 271 271 ASN ASN D . n 
D 1 272 ILE 272 272 272 ILE ILE D . n 
D 1 273 GLY 273 273 273 GLY GLY D . n 
D 1 274 GLY 274 274 274 GLY GLY D . n 
D 1 275 LEU 275 275 275 LEU LEU D . n 
D 1 276 VAL 276 276 276 VAL VAL D . n 
D 1 277 ALA 277 277 277 ALA ALA D . n 
D 1 278 ILE 278 278 278 ILE ILE D . n 
D 1 279 ARG 279 279 279 ARG ARG D . n 
D 1 280 ASP 280 280 280 ASP ASP D . n 
D 1 281 ASN 281 281 281 ASN ASN D . n 
D 1 282 GLU 282 282 282 GLU GLU D . n 
D 1 283 GLU 283 283 283 GLU GLU D . n 
D 1 284 ILE 284 284 284 ILE ILE D . n 
D 1 285 PHE 285 285 285 PHE PHE D . n 
D 1 286 THR 286 286 286 THR THR D . n 
D 1 287 LEU 287 287 287 LEU LEU D . n 
D 1 288 ALA 288 288 288 ALA ALA D . n 
D 1 289 ARG 289 289 289 ARG ARG D . n 
D 1 290 GLN 290 290 290 GLN GLN D . n 
D 1 291 ARG 291 291 291 ARG ARG D . n 
D 1 292 CYS 292 292 292 CYS CYS D . n 
D 1 293 VAL 293 293 293 VAL VAL D . n 
D 1 294 PRO 294 294 294 PRO PRO D . n 
D 1 295 MET 295 295 295 MET MET D . n 
D 1 296 GLU 296 296 296 GLU GLU D . n 
D 1 297 GLY 297 297 297 GLY GLY D . n 
D 1 298 PHE 298 298 298 PHE PHE D . n 
D 1 299 VAL 299 299 299 VAL VAL D . n 
D 1 300 THR 300 300 300 THR THR D . n 
D 1 301 TYR 301 301 301 TYR TYR D . n 
D 1 302 GLY 302 302 302 GLY GLY D . n 
D 1 303 GLY 303 303 303 GLY GLY D . n 
D 1 304 LEU 304 304 304 LEU LEU D . n 
D 1 305 ALA 305 305 305 ALA ALA D . n 
D 1 306 GLY 306 306 306 GLY GLY D . n 
D 1 307 ARG 307 307 307 ARG ARG D . n 
D 1 308 ASP 308 308 308 ASP ASP D . n 
D 1 309 MET 309 309 309 MET MET D . n 
D 1 310 ALA 310 310 310 ALA ALA D . n 
D 1 311 ALA 311 311 311 ALA ALA D . n 
D 1 312 MET 312 312 312 MET MET D . n 
D 1 313 VAL 313 313 313 VAL VAL D . n 
D 1 314 GLN 314 314 314 GLN GLN D . n 
D 1 315 GLY 315 315 315 GLY GLY D . n 
D 1 316 LEU 316 316 316 LEU LEU D . n 
D 1 317 GLU 317 317 317 GLU GLU D . n 
D 1 318 GLU 318 318 318 GLU GLU D . n 
D 1 319 GLY 319 319 319 GLY GLY D . n 
D 1 320 THR 320 320 320 THR THR D . n 
D 1 321 GLU 321 321 321 GLU GLU D . n 
D 1 322 GLU 322 322 322 GLU GLU D . n 
D 1 323 GLU 323 323 323 GLU GLU D . n 
D 1 324 TYR 324 324 324 TYR TYR D . n 
D 1 325 LEU 325 325 325 LEU LEU D . n 
D 1 326 HIS 326 326 326 HIS HIS D . n 
D 1 327 TYR 327 327 327 TYR TYR D . n 
D 1 328 ARG 328 328 328 ARG ARG D . n 
D 1 329 ILE 329 329 329 ILE ILE D . n 
D 1 330 GLY 330 330 330 GLY GLY D . n 
D 1 331 GLN 331 331 331 GLN GLN D . n 
D 1 332 VAL 332 332 332 VAL VAL D . n 
D 1 333 LYS 333 333 333 LYS LYS D . n 
D 1 334 TYR 334 334 334 TYR TYR D . n 
D 1 335 LEU 335 335 335 LEU LEU D . n 
D 1 336 GLY 336 336 336 GLY GLY D . n 
D 1 337 ASP 337 337 337 ASP ASP D . n 
D 1 338 ARG 338 338 338 ARG ARG D . n 
D 1 339 LEU 339 339 339 LEU LEU D . n 
D 1 340 ARG 340 340 340 ARG ARG D . n 
D 1 341 GLU 341 341 341 GLU GLU D . n 
D 1 342 ALA 342 342 342 ALA ALA D . n 
D 1 343 GLY 343 343 343 GLY GLY D . n 
D 1 344 ILE 344 344 344 ILE ILE D . n 
D 1 345 PRO 345 345 345 PRO PRO D . n 
D 1 346 ILE 346 346 346 ILE ILE D . n 
D 1 347 GLN 347 347 347 GLN GLN D . n 
D 1 348 TYR 348 348 348 TYR TYR D . n 
D 1 349 PRO 349 349 349 PRO PRO D . n 
D 1 350 THR 350 350 350 THR THR D . n 
D 1 351 GLY 351 351 351 GLY GLY D . n 
D 1 352 GLY 352 352 352 GLY GLY D . n 
D 1 353 HIS 353 353 353 HIS HIS D . n 
D 1 354 ALA 354 354 354 ALA ALA D . n 
D 1 355 VAL 355 355 355 VAL VAL D . n 
D 1 356 PHE 356 356 356 PHE PHE D . n 
D 1 357 VAL 357 357 357 VAL VAL D . n 
D 1 358 ASP 358 358 358 ASP ASP D . n 
D 1 359 CYS 359 359 359 CYS CYS D . n 
D 1 360 LYS 360 360 360 LYS LYS D . n 
D 1 361 LYS 361 361 361 LYS LYS D . n 
D 1 362 LEU 362 362 362 LEU LEU D . n 
D 1 363 VAL 363 363 363 VAL VAL D . n 
D 1 364 PRO 364 364 364 PRO PRO D . n 
D 1 365 GLN 365 365 365 GLN GLN D . n 
D 1 366 ILE 366 366 366 ILE ILE D . n 
D 1 367 PRO 367 367 367 PRO PRO D . n 
D 1 368 GLY 368 368 368 GLY GLY D . n 
D 1 369 ASP 369 369 369 ASP ASP D . n 
D 1 370 GLN 370 370 370 GLN GLN D . n 
D 1 371 PHE 371 371 371 PHE PHE D . n 
D 1 372 PRO 372 372 372 PRO PRO D . n 
D 1 373 ALA 373 373 373 ALA ALA D . n 
D 1 374 GLN 374 374 374 GLN GLN D . n 
D 1 375 ALA 375 375 375 ALA ALA D . n 
D 1 376 VAL 376 376 376 VAL VAL D . n 
D 1 377 ILE 377 377 377 ILE ILE D . n 
D 1 378 ASN 378 378 378 ASN ASN D . n 
D 1 379 ALA 379 379 379 ALA ALA D . n 
D 1 380 LEU 380 380 380 LEU LEU D . n 
D 1 381 TYR 381 381 381 TYR TYR D . n 
D 1 382 LEU 382 382 382 LEU LEU D . n 
D 1 383 GLU 383 383 383 GLU GLU D . n 
D 1 384 SER 384 384 384 SER SER D . n 
D 1 385 GLY 385 385 385 GLY GLY D . n 
D 1 386 VAL 386 386 386 VAL VAL D . n 
D 1 387 ARG 387 387 387 ARG ARG D . n 
D 1 388 ALA 388 388 388 ALA ALA D . n 
D 1 389 VAL 389 389 389 VAL VAL D . n 
D 1 390 GLU 390 390 390 GLU GLU D . n 
D 1 391 ILE 391 391 391 ILE ILE D . n 
D 1 392 GLY 392 392 392 GLY GLY D . n 
D 1 393 SER 393 393 393 SER SER D . n 
D 1 394 PHE 394 394 394 PHE PHE D . n 
D 1 395 LEU 395 395 395 LEU LEU D . n 
D 1 396 LEU 396 396 396 LEU LEU D . n 
D 1 397 GLY 397 397 397 GLY GLY D . n 
D 1 398 ARG 398 398 398 ARG ARG D . n 
D 1 399 ASP 399 399 ?   ?   ?   D . n 
D 1 400 PRO 400 400 ?   ?   ?   D . n 
D 1 401 ALA 401 401 ?   ?   ?   D . n 
D 1 402 THR 402 402 ?   ?   ?   D . n 
D 1 403 GLY 403 403 ?   ?   ?   D . n 
D 1 404 GLU 404 404 ?   ?   ?   D . n 
D 1 405 GLN 405 405 405 GLN GLN D . n 
D 1 406 LYS 406 406 406 LYS LYS D . n 
D 1 407 HIS 407 407 407 HIS HIS D . n 
D 1 408 ALA 408 408 408 ALA ALA D . n 
D 1 409 ASP 409 409 409 ASP ASP D . n 
D 1 410 MET 410 410 410 MET MET D . n 
D 1 411 GLU 411 411 411 GLU GLU D . n 
D 1 412 PHE 412 412 412 PHE PHE D . n 
D 1 413 MET 413 413 413 MET MET D . n 
D 1 414 ARG 414 414 414 ARG ARG D . n 
D 1 415 LEU 415 415 415 LEU LEU D . n 
D 1 416 THR 416 416 416 THR THR D . n 
D 1 417 ILE 417 417 417 ILE ILE D . n 
D 1 418 ALA 418 418 418 ALA ALA D . n 
D 1 419 ARG 419 419 419 ARG ARG D . n 
D 1 420 ARG 420 420 420 ARG ARG D . n 
D 1 421 VAL 421 421 421 VAL VAL D . n 
D 1 422 TYR 422 422 422 TYR TYR D . n 
D 1 423 THR 423 423 423 THR THR D . n 
D 1 424 ASN 424 424 424 ASN ASN D . n 
D 1 425 ASP 425 425 425 ASP ASP D . n 
D 1 426 HIS 426 426 426 HIS HIS D . n 
D 1 427 MET 427 427 427 MET MET D . n 
D 1 428 ASP 428 428 428 ASP ASP D . n 
D 1 429 TYR 429 429 429 TYR TYR D . n 
D 1 430 ILE 430 430 430 ILE ILE D . n 
D 1 431 ALA 431 431 431 ALA ALA D . n 
D 1 432 ASP 432 432 432 ASP ASP D . n 
D 1 433 ALA 433 433 433 ALA ALA D . n 
D 1 434 LEU 434 434 434 LEU LEU D . n 
D 1 435 ILE 435 435 435 ILE ILE D . n 
D 1 436 GLY 436 436 436 GLY GLY D . n 
D 1 437 LEU 437 437 437 LEU LEU D . n 
D 1 438 LYS 438 438 438 LYS LYS D . n 
D 1 439 GLU 439 439 439 GLU GLU D . n 
D 1 440 LYS 440 440 440 LYS LYS D . n 
D 1 441 PHE 441 441 441 PHE PHE D . n 
D 1 442 ALA 442 442 442 ALA ALA D . n 
D 1 443 THR 443 443 443 THR THR D . n 
D 1 444 LEU 444 444 444 LEU LEU D . n 
D 1 445 LYS 445 445 445 LYS LYS D . n 
D 1 446 GLY 446 446 446 GLY GLY D . n 
D 1 447 LEU 447 447 447 LEU LEU D . n 
D 1 448 GLU 448 448 448 GLU GLU D . n 
D 1 449 PHE 449 449 449 PHE PHE D . n 
D 1 450 GLU 450 450 450 GLU GLU D . n 
D 1 451 TYR 451 451 451 TYR TYR D . n 
D 1 452 GLU 452 452 452 GLU GLU D . n 
D 1 453 PRO 453 453 453 PRO PRO D . n 
D 1 454 PRO 454 454 454 PRO PRO D . n 
D 1 455 VAL 455 455 455 VAL VAL D . n 
D 1 456 LEU 456 456 456 LEU LEU D . n 
D 1 457 ARG 457 457 457 ARG ARG D . n 
D 1 458 HIS 458 458 458 HIS HIS D . n 
D 1 459 PHE 459 459 459 PHE PHE D . n 
D 1 460 THR 460 460 460 THR THR D . n 
D 1 461 ALA 461 461 461 ALA ALA D . n 
D 1 462 ARG 462 462 462 ARG ARG D . n 
D 1 463 LEU 463 463 463 LEU LEU D . n 
D 1 464 LYS 464 464 464 LYS LYS D . n 
D 1 465 PRO 465 465 465 PRO PRO D . n 
D 1 466 ILE 466 466 ?   ?   ?   D . n 
D 1 467 GLU 467 467 ?   ?   ?   D . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 0JO   ? ? 0JO   ? ? 'SUBJECT OF INVESTIGATION' ? 
2 A1A2Z ? ? A1A2Z ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E 2 K     1   501 1   K     K   A . 
F 2 K     1   502 2   K     K   A . 
G 3 BZI   1   503 4   BZI   BZI A . 
H 4 0JO   1   504 5   0JO   0JO A . 
I 5 DMS   1   505 6   DMS   DMS A . 
J 5 DMS   1   501 7   DMS   DMS B . 
K 6 PLT   1   502 8   PLT   PLT B . 
L 2 K     1   501 9   K     K   C . 
M 2 K     1   502 10  K     K   C . 
N 7 A1A2Z 1   503 11  A1A2Z LIG C . 
O 3 BZI   1   501 12  BZI   BZI D . 
P 4 0JO   1   502 13  0JO   0JO D . 
Q 8 HOH   1   601 717 HOH   HOH A . 
Q 8 HOH   2   602 309 HOH   HOH A . 
Q 8 HOH   3   603 715 HOH   HOH A . 
Q 8 HOH   4   604 405 HOH   HOH A . 
Q 8 HOH   5   605 113 HOH   HOH A . 
Q 8 HOH   6   606 394 HOH   HOH A . 
Q 8 HOH   7   607 564 HOH   HOH A . 
Q 8 HOH   8   608 98  HOH   HOH A . 
Q 8 HOH   9   609 505 HOH   HOH A . 
Q 8 HOH   10  610 832 HOH   HOH A . 
Q 8 HOH   11  611 563 HOH   HOH A . 
Q 8 HOH   12  612 406 HOH   HOH A . 
Q 8 HOH   13  613 891 HOH   HOH A . 
Q 8 HOH   14  614 681 HOH   HOH A . 
Q 8 HOH   15  615 430 HOH   HOH A . 
Q 8 HOH   16  616 698 HOH   HOH A . 
Q 8 HOH   17  617 565 HOH   HOH A . 
Q 8 HOH   18  618 743 HOH   HOH A . 
Q 8 HOH   19  619 520 HOH   HOH A . 
Q 8 HOH   20  620 91  HOH   HOH A . 
Q 8 HOH   21  621 271 HOH   HOH A . 
Q 8 HOH   22  622 396 HOH   HOH A . 
Q 8 HOH   23  623 859 HOH   HOH A . 
Q 8 HOH   24  624 102 HOH   HOH A . 
Q 8 HOH   25  625 644 HOH   HOH A . 
Q 8 HOH   26  626 813 HOH   HOH A . 
Q 8 HOH   27  627 444 HOH   HOH A . 
Q 8 HOH   28  628 872 HOH   HOH A . 
Q 8 HOH   29  629 690 HOH   HOH A . 
Q 8 HOH   30  630 525 HOH   HOH A . 
Q 8 HOH   31  631 114 HOH   HOH A . 
Q 8 HOH   32  632 97  HOH   HOH A . 
Q 8 HOH   33  633 552 HOH   HOH A . 
Q 8 HOH   34  634 25  HOH   HOH A . 
Q 8 HOH   35  635 560 HOH   HOH A . 
Q 8 HOH   36  636 366 HOH   HOH A . 
Q 8 HOH   37  637 135 HOH   HOH A . 
Q 8 HOH   38  638 54  HOH   HOH A . 
Q 8 HOH   39  639 79  HOH   HOH A . 
Q 8 HOH   40  640 231 HOH   HOH A . 
Q 8 HOH   41  641 296 HOH   HOH A . 
Q 8 HOH   42  642 40  HOH   HOH A . 
Q 8 HOH   43  643 329 HOH   HOH A . 
Q 8 HOH   44  644 619 HOH   HOH A . 
Q 8 HOH   45  645 90  HOH   HOH A . 
Q 8 HOH   46  646 270 HOH   HOH A . 
Q 8 HOH   47  647 915 HOH   HOH A . 
Q 8 HOH   48  648 469 HOH   HOH A . 
Q 8 HOH   49  649 273 HOH   HOH A . 
Q 8 HOH   50  650 555 HOH   HOH A . 
Q 8 HOH   51  651 723 HOH   HOH A . 
Q 8 HOH   52  652 326 HOH   HOH A . 
Q 8 HOH   53  653 227 HOH   HOH A . 
Q 8 HOH   54  654 403 HOH   HOH A . 
Q 8 HOH   55  655 569 HOH   HOH A . 
Q 8 HOH   56  656 111 HOH   HOH A . 
Q 8 HOH   57  657 179 HOH   HOH A . 
Q 8 HOH   58  658 23  HOH   HOH A . 
Q 8 HOH   59  659 856 HOH   HOH A . 
Q 8 HOH   60  660 363 HOH   HOH A . 
Q 8 HOH   61  661 22  HOH   HOH A . 
Q 8 HOH   62  662 13  HOH   HOH A . 
Q 8 HOH   63  663 41  HOH   HOH A . 
Q 8 HOH   64  664 6   HOH   HOH A . 
Q 8 HOH   65  665 104 HOH   HOH A . 
Q 8 HOH   66  666 201 HOH   HOH A . 
Q 8 HOH   67  667 42  HOH   HOH A . 
Q 8 HOH   68  668 15  HOH   HOH A . 
Q 8 HOH   69  669 501 HOH   HOH A . 
Q 8 HOH   70  670 653 HOH   HOH A . 
Q 8 HOH   71  671 876 HOH   HOH A . 
Q 8 HOH   72  672 434 HOH   HOH A . 
Q 8 HOH   73  673 237 HOH   HOH A . 
Q 8 HOH   74  674 852 HOH   HOH A . 
Q 8 HOH   75  675 482 HOH   HOH A . 
Q 8 HOH   76  676 361 HOH   HOH A . 
Q 8 HOH   77  677 339 HOH   HOH A . 
Q 8 HOH   78  678 433 HOH   HOH A . 
Q 8 HOH   79  679 451 HOH   HOH A . 
Q 8 HOH   80  680 423 HOH   HOH A . 
Q 8 HOH   81  681 519 HOH   HOH A . 
Q 8 HOH   82  682 30  HOH   HOH A . 
Q 8 HOH   83  683 243 HOH   HOH A . 
Q 8 HOH   84  684 183 HOH   HOH A . 
Q 8 HOH   85  685 27  HOH   HOH A . 
Q 8 HOH   86  686 348 HOH   HOH A . 
Q 8 HOH   87  687 393 HOH   HOH A . 
Q 8 HOH   88  688 108 HOH   HOH A . 
Q 8 HOH   89  689 291 HOH   HOH A . 
Q 8 HOH   90  690 490 HOH   HOH A . 
Q 8 HOH   91  691 5   HOH   HOH A . 
Q 8 HOH   92  692 173 HOH   HOH A . 
Q 8 HOH   93  693 562 HOH   HOH A . 
Q 8 HOH   94  694 337 HOH   HOH A . 
Q 8 HOH   95  695 432 HOH   HOH A . 
Q 8 HOH   96  696 532 HOH   HOH A . 
Q 8 HOH   97  697 665 HOH   HOH A . 
Q 8 HOH   98  698 146 HOH   HOH A . 
Q 8 HOH   99  699 37  HOH   HOH A . 
Q 8 HOH   100 700 139 HOH   HOH A . 
Q 8 HOH   101 701 739 HOH   HOH A . 
Q 8 HOH   102 702 94  HOH   HOH A . 
Q 8 HOH   103 703 47  HOH   HOH A . 
Q 8 HOH   104 704 374 HOH   HOH A . 
Q 8 HOH   105 705 509 HOH   HOH A . 
Q 8 HOH   106 706 661 HOH   HOH A . 
Q 8 HOH   107 707 352 HOH   HOH A . 
Q 8 HOH   108 708 196 HOH   HOH A . 
Q 8 HOH   109 709 747 HOH   HOH A . 
Q 8 HOH   110 710 535 HOH   HOH A . 
Q 8 HOH   111 711 200 HOH   HOH A . 
Q 8 HOH   112 712 44  HOH   HOH A . 
Q 8 HOH   113 713 467 HOH   HOH A . 
Q 8 HOH   114 714 647 HOH   HOH A . 
Q 8 HOH   115 715 145 HOH   HOH A . 
Q 8 HOH   116 716 203 HOH   HOH A . 
Q 8 HOH   117 717 307 HOH   HOH A . 
Q 8 HOH   118 718 422 HOH   HOH A . 
Q 8 HOH   119 719 496 HOH   HOH A . 
Q 8 HOH   120 720 150 HOH   HOH A . 
Q 8 HOH   121 721 76  HOH   HOH A . 
Q 8 HOH   122 722 308 HOH   HOH A . 
Q 8 HOH   123 723 342 HOH   HOH A . 
Q 8 HOH   124 724 741 HOH   HOH A . 
Q 8 HOH   125 725 202 HOH   HOH A . 
Q 8 HOH   126 726 272 HOH   HOH A . 
Q 8 HOH   127 727 542 HOH   HOH A . 
Q 8 HOH   128 728 334 HOH   HOH A . 
Q 8 HOH   129 729 214 HOH   HOH A . 
Q 8 HOH   130 730 226 HOH   HOH A . 
Q 8 HOH   131 731 372 HOH   HOH A . 
Q 8 HOH   132 732 667 HOH   HOH A . 
Q 8 HOH   133 733 445 HOH   HOH A . 
Q 8 HOH   134 734 194 HOH   HOH A . 
Q 8 HOH   135 735 691 HOH   HOH A . 
Q 8 HOH   136 736 692 HOH   HOH A . 
Q 8 HOH   137 737 541 HOH   HOH A . 
Q 8 HOH   138 738 404 HOH   HOH A . 
Q 8 HOH   139 739 17  HOH   HOH A . 
Q 8 HOH   140 740 187 HOH   HOH A . 
Q 8 HOH   141 741 460 HOH   HOH A . 
Q 8 HOH   142 742 491 HOH   HOH A . 
Q 8 HOH   143 743 57  HOH   HOH A . 
Q 8 HOH   144 744 524 HOH   HOH A . 
Q 8 HOH   145 745 160 HOH   HOH A . 
Q 8 HOH   146 746 158 HOH   HOH A . 
Q 8 HOH   147 747 671 HOH   HOH A . 
Q 8 HOH   148 748 545 HOH   HOH A . 
Q 8 HOH   149 749 547 HOH   HOH A . 
Q 8 HOH   150 750 702 HOH   HOH A . 
Q 8 HOH   151 751 756 HOH   HOH A . 
Q 8 HOH   152 752 254 HOH   HOH A . 
Q 8 HOH   153 753 686 HOH   HOH A . 
Q 8 HOH   154 754 823 HOH   HOH A . 
Q 8 HOH   155 755 101 HOH   HOH A . 
Q 8 HOH   156 756 646 HOH   HOH A . 
Q 8 HOH   157 757 131 HOH   HOH A . 
Q 8 HOH   158 758 238 HOH   HOH A . 
Q 8 HOH   159 759 362 HOH   HOH A . 
Q 8 HOH   160 760 589 HOH   HOH A . 
Q 8 HOH   161 761 874 HOH   HOH A . 
Q 8 HOH   162 762 236 HOH   HOH A . 
Q 8 HOH   163 763 486 HOH   HOH A . 
Q 8 HOH   164 764 418 HOH   HOH A . 
Q 8 HOH   165 765 401 HOH   HOH A . 
Q 8 HOH   166 766 816 HOH   HOH A . 
Q 8 HOH   167 767 817 HOH   HOH A . 
Q 8 HOH   168 768 371 HOH   HOH A . 
Q 8 HOH   169 769 579 HOH   HOH A . 
Q 8 HOH   170 770 696 HOH   HOH A . 
Q 8 HOH   171 771 224 HOH   HOH A . 
Q 8 HOH   172 772 657 HOH   HOH A . 
Q 8 HOH   173 773 208 HOH   HOH A . 
Q 8 HOH   174 774 142 HOH   HOH A . 
Q 8 HOH   175 775 663 HOH   HOH A . 
Q 8 HOH   176 776 819 HOH   HOH A . 
Q 8 HOH   177 777 735 HOH   HOH A . 
Q 8 HOH   178 778 895 HOH   HOH A . 
Q 8 HOH   179 779 441 HOH   HOH A . 
Q 8 HOH   180 780 293 HOH   HOH A . 
Q 8 HOH   181 781 380 HOH   HOH A . 
Q 8 HOH   182 782 592 HOH   HOH A . 
Q 8 HOH   183 783 229 HOH   HOH A . 
Q 8 HOH   184 784 578 HOH   HOH A . 
Q 8 HOH   185 785 497 HOH   HOH A . 
Q 8 HOH   186 786 103 HOH   HOH A . 
Q 8 HOH   187 787 354 HOH   HOH A . 
Q 8 HOH   188 788 771 HOH   HOH A . 
Q 8 HOH   189 789 786 HOH   HOH A . 
Q 8 HOH   190 790 794 HOH   HOH A . 
Q 8 HOH   191 791 283 HOH   HOH A . 
Q 8 HOH   192 792 634 HOH   HOH A . 
Q 8 HOH   193 793 637 HOH   HOH A . 
Q 8 HOH   194 794 887 HOH   HOH A . 
Q 8 HOH   195 795 72  HOH   HOH A . 
Q 8 HOH   196 796 642 HOH   HOH A . 
Q 8 HOH   197 797 900 HOH   HOH A . 
Q 8 HOH   198 798 217 HOH   HOH A . 
Q 8 HOH   199 799 893 HOH   HOH A . 
Q 8 HOH   200 800 744 HOH   HOH A . 
Q 8 HOH   201 801 854 HOH   HOH A . 
Q 8 HOH   202 802 602 HOH   HOH A . 
Q 8 HOH   203 803 55  HOH   HOH A . 
Q 8 HOH   204 804 279 HOH   HOH A . 
Q 8 HOH   205 805 623 HOH   HOH A . 
Q 8 HOH   206 806 595 HOH   HOH A . 
Q 8 HOH   207 807 593 HOH   HOH A . 
Q 8 HOH   208 808 796 HOH   HOH A . 
Q 8 HOH   209 809 806 HOH   HOH A . 
Q 8 HOH   210 810 571 HOH   HOH A . 
Q 8 HOH   211 811 781 HOH   HOH A . 
Q 8 HOH   212 812 920 HOH   HOH A . 
R 8 HOH   1   601 719 HOH   HOH B . 
R 8 HOH   2   602 709 HOH   HOH B . 
R 8 HOH   3   603 833 HOH   HOH B . 
R 8 HOH   4   604 837 HOH   HOH B . 
R 8 HOH   5   605 773 HOH   HOH B . 
R 8 HOH   6   606 853 HOH   HOH B . 
R 8 HOH   7   607 540 HOH   HOH B . 
R 8 HOH   8   608 277 HOH   HOH B . 
R 8 HOH   9   609 463 HOH   HOH B . 
R 8 HOH   10  610 369 HOH   HOH B . 
R 8 HOH   11  611 620 HOH   HOH B . 
R 8 HOH   12  612 464 HOH   HOH B . 
R 8 HOH   13  613 585 HOH   HOH B . 
R 8 HOH   14  614 652 HOH   HOH B . 
R 8 HOH   15  615 622 HOH   HOH B . 
R 8 HOH   16  616 636 HOH   HOH B . 
R 8 HOH   17  617 927 HOH   HOH B . 
R 8 HOH   18  618 316 HOH   HOH B . 
R 8 HOH   19  619 628 HOH   HOH B . 
R 8 HOH   20  620 262 HOH   HOH B . 
R 8 HOH   21  621 379 HOH   HOH B . 
R 8 HOH   22  622 689 HOH   HOH B . 
R 8 HOH   23  623 193 HOH   HOH B . 
R 8 HOH   24  624 82  HOH   HOH B . 
R 8 HOH   25  625 725 HOH   HOH B . 
R 8 HOH   26  626 123 HOH   HOH B . 
R 8 HOH   27  627 584 HOH   HOH B . 
R 8 HOH   28  628 398 HOH   HOH B . 
R 8 HOH   29  629 284 HOH   HOH B . 
R 8 HOH   30  630 63  HOH   HOH B . 
R 8 HOH   31  631 516 HOH   HOH B . 
R 8 HOH   32  632 20  HOH   HOH B . 
R 8 HOH   33  633 174 HOH   HOH B . 
R 8 HOH   34  634 471 HOH   HOH B . 
R 8 HOH   35  635 475 HOH   HOH B . 
R 8 HOH   36  636 378 HOH   HOH B . 
R 8 HOH   37  637 522 HOH   HOH B . 
R 8 HOH   38  638 287 HOH   HOH B . 
R 8 HOH   39  639 132 HOH   HOH B . 
R 8 HOH   40  640 180 HOH   HOH B . 
R 8 HOH   41  641 655 HOH   HOH B . 
R 8 HOH   42  642 480 HOH   HOH B . 
R 8 HOH   43  643 536 HOH   HOH B . 
R 8 HOH   44  644 299 HOH   HOH B . 
R 8 HOH   45  645 754 HOH   HOH B . 
R 8 HOH   46  646 827 HOH   HOH B . 
R 8 HOH   47  647 256 HOH   HOH B . 
R 8 HOH   48  648 858 HOH   HOH B . 
R 8 HOH   49  649 459 HOH   HOH B . 
R 8 HOH   50  650 120 HOH   HOH B . 
R 8 HOH   51  651 268 HOH   HOH B . 
R 8 HOH   52  652 195 HOH   HOH B . 
R 8 HOH   53  653 239 HOH   HOH B . 
R 8 HOH   54  654 718 HOH   HOH B . 
R 8 HOH   55  655 340 HOH   HOH B . 
R 8 HOH   56  656 96  HOH   HOH B . 
R 8 HOH   57  657 504 HOH   HOH B . 
R 8 HOH   58  658 51  HOH   HOH B . 
R 8 HOH   59  659 77  HOH   HOH B . 
R 8 HOH   60  660 798 HOH   HOH B . 
R 8 HOH   61  661 888 HOH   HOH B . 
R 8 HOH   62  662 336 HOH   HOH B . 
R 8 HOH   63  663 359 HOH   HOH B . 
R 8 HOH   64  664 365 HOH   HOH B . 
R 8 HOH   65  665 553 HOH   HOH B . 
R 8 HOH   66  666 720 HOH   HOH B . 
R 8 HOH   67  667 488 HOH   HOH B . 
R 8 HOH   68  668 878 HOH   HOH B . 
R 8 HOH   69  669 358 HOH   HOH B . 
R 8 HOH   70  670 693 HOH   HOH B . 
R 8 HOH   71  671 518 HOH   HOH B . 
R 8 HOH   72  672 503 HOH   HOH B . 
R 8 HOH   73  673 192 HOH   HOH B . 
R 8 HOH   74  674 659 HOH   HOH B . 
R 8 HOH   75  675 35  HOH   HOH B . 
R 8 HOH   76  676 521 HOH   HOH B . 
R 8 HOH   77  677 119 HOH   HOH B . 
R 8 HOH   78  678 561 HOH   HOH B . 
R 8 HOH   79  679 440 HOH   HOH B . 
R 8 HOH   80  680 687 HOH   HOH B . 
R 8 HOH   81  681 165 HOH   HOH B . 
R 8 HOH   82  682 417 HOH   HOH B . 
R 8 HOH   83  683 275 HOH   HOH B . 
R 8 HOH   84  684 466 HOH   HOH B . 
R 8 HOH   85  685 34  HOH   HOH B . 
R 8 HOH   86  686 494 HOH   HOH B . 
R 8 HOH   87  687 514 HOH   HOH B . 
R 8 HOH   88  688 573 HOH   HOH B . 
R 8 HOH   89  689 442 HOH   HOH B . 
R 8 HOH   90  690 191 HOH   HOH B . 
R 8 HOH   91  691 297 HOH   HOH B . 
R 8 HOH   92  692 677 HOH   HOH B . 
R 8 HOH   93  693 43  HOH   HOH B . 
R 8 HOH   94  694 24  HOH   HOH B . 
R 8 HOH   95  695 318 HOH   HOH B . 
R 8 HOH   96  696 703 HOH   HOH B . 
R 8 HOH   97  697 1   HOH   HOH B . 
R 8 HOH   98  698 576 HOH   HOH B . 
R 8 HOH   99  699 479 HOH   HOH B . 
R 8 HOH   100 700 258 HOH   HOH B . 
R 8 HOH   101 701 149 HOH   HOH B . 
R 8 HOH   102 702 707 HOH   HOH B . 
R 8 HOH   103 703 175 HOH   HOH B . 
R 8 HOH   104 704 31  HOH   HOH B . 
R 8 HOH   105 705 391 HOH   HOH B . 
R 8 HOH   106 706 317 HOH   HOH B . 
R 8 HOH   107 707 415 HOH   HOH B . 
R 8 HOH   108 708 242 HOH   HOH B . 
R 8 HOH   109 709 81  HOH   HOH B . 
R 8 HOH   110 710 477 HOH   HOH B . 
R 8 HOH   111 711 288 HOH   HOH B . 
R 8 HOH   112 712 7   HOH   HOH B . 
R 8 HOH   113 713 383 HOH   HOH B . 
R 8 HOH   114 714 86  HOH   HOH B . 
R 8 HOH   115 715 151 HOH   HOH B . 
R 8 HOH   116 716 215 HOH   HOH B . 
R 8 HOH   117 717 557 HOH   HOH B . 
R 8 HOH   118 718 839 HOH   HOH B . 
R 8 HOH   119 719 87  HOH   HOH B . 
R 8 HOH   120 720 127 HOH   HOH B . 
R 8 HOH   121 721 3   HOH   HOH B . 
R 8 HOH   122 722 331 HOH   HOH B . 
R 8 HOH   123 723 476 HOH   HOH B . 
R 8 HOH   124 724 414 HOH   HOH B . 
R 8 HOH   125 725 375 HOH   HOH B . 
R 8 HOH   126 726 382 HOH   HOH B . 
R 8 HOH   127 727 551 HOH   HOH B . 
R 8 HOH   128 728 240 HOH   HOH B . 
R 8 HOH   129 729 513 HOH   HOH B . 
R 8 HOH   130 730 320 HOH   HOH B . 
R 8 HOH   131 731 130 HOH   HOH B . 
R 8 HOH   132 732 112 HOH   HOH B . 
R 8 HOH   133 733 473 HOH   HOH B . 
R 8 HOH   134 734 407 HOH   HOH B . 
R 8 HOH   135 735 388 HOH   HOH B . 
R 8 HOH   136 736 126 HOH   HOH B . 
R 8 HOH   137 737 700 HOH   HOH B . 
R 8 HOH   138 738 452 HOH   HOH B . 
R 8 HOH   139 739 570 HOH   HOH B . 
R 8 HOH   140 740 474 HOH   HOH B . 
R 8 HOH   141 741 478 HOH   HOH B . 
R 8 HOH   142 742 211 HOH   HOH B . 
R 8 HOH   143 743 259 HOH   HOH B . 
R 8 HOH   144 744 745 HOH   HOH B . 
R 8 HOH   145 745 924 HOH   HOH B . 
R 8 HOH   146 746 472 HOH   HOH B . 
R 8 HOH   147 747 311 HOH   HOH B . 
R 8 HOH   148 748 868 HOH   HOH B . 
R 8 HOH   149 749 59  HOH   HOH B . 
R 8 HOH   150 750 651 HOH   HOH B . 
R 8 HOH   151 751 315 HOH   HOH B . 
R 8 HOH   152 752 748 HOH   HOH B . 
R 8 HOH   153 753 437 HOH   HOH B . 
R 8 HOH   154 754 62  HOH   HOH B . 
R 8 HOH   155 755 190 HOH   HOH B . 
R 8 HOH   156 756 484 HOH   HOH B . 
R 8 HOH   157 757 453 HOH   HOH B . 
R 8 HOH   158 758 873 HOH   HOH B . 
R 8 HOH   159 759 850 HOH   HOH B . 
R 8 HOH   160 760 48  HOH   HOH B . 
R 8 HOH   161 761 188 HOH   HOH B . 
R 8 HOH   162 762 93  HOH   HOH B . 
R 8 HOH   163 763 679 HOH   HOH B . 
R 8 HOH   164 764 559 HOH   HOH B . 
R 8 HOH   165 765 439 HOH   HOH B . 
R 8 HOH   166 766 306 HOH   HOH B . 
R 8 HOH   167 767 750 HOH   HOH B . 
R 8 HOH   168 768 485 HOH   HOH B . 
R 8 HOH   169 769 909 HOH   HOH B . 
R 8 HOH   170 770 609 HOH   HOH B . 
R 8 HOH   171 771 209 HOH   HOH B . 
R 8 HOH   172 772 539 HOH   HOH B . 
R 8 HOH   173 773 567 HOH   HOH B . 
R 8 HOH   174 774 428 HOH   HOH B . 
R 8 HOH   175 775 508 HOH   HOH B . 
R 8 HOH   176 776 935 HOH   HOH B . 
R 8 HOH   177 777 510 HOH   HOH B . 
R 8 HOH   178 778 921 HOH   HOH B . 
R 8 HOH   179 779 790 HOH   HOH B . 
R 8 HOH   180 780 727 HOH   HOH B . 
R 8 HOH   181 781 387 HOH   HOH B . 
R 8 HOH   182 782 435 HOH   HOH B . 
R 8 HOH   183 783 892 HOH   HOH B . 
R 8 HOH   184 784 820 HOH   HOH B . 
R 8 HOH   185 785 92  HOH   HOH B . 
R 8 HOH   186 786 511 HOH   HOH B . 
R 8 HOH   187 787 763 HOH   HOH B . 
R 8 HOH   188 788 782 HOH   HOH B . 
R 8 HOH   189 789 688 HOH   HOH B . 
R 8 HOH   190 790 594 HOH   HOH B . 
R 8 HOH   191 791 605 HOH   HOH B . 
R 8 HOH   192 792 9   HOH   HOH B . 
R 8 HOH   193 793 343 HOH   HOH B . 
R 8 HOH   194 794 566 HOH   HOH B . 
R 8 HOH   195 795 811 HOH   HOH B . 
R 8 HOH   196 796 789 HOH   HOH B . 
R 8 HOH   197 797 899 HOH   HOH B . 
R 8 HOH   198 798 713 HOH   HOH B . 
R 8 HOH   199 799 606 HOH   HOH B . 
R 8 HOH   200 800 629 HOH   HOH B . 
R 8 HOH   201 801 147 HOH   HOH B . 
R 8 HOH   202 802 266 HOH   HOH B . 
R 8 HOH   203 803 660 HOH   HOH B . 
R 8 HOH   204 804 186 HOH   HOH B . 
R 8 HOH   205 805 760 HOH   HOH B . 
R 8 HOH   206 806 711 HOH   HOH B . 
R 8 HOH   207 807 599 HOH   HOH B . 
R 8 HOH   208 808 889 HOH   HOH B . 
R 8 HOH   209 809 810 HOH   HOH B . 
R 8 HOH   210 810 864 HOH   HOH B . 
R 8 HOH   211 811 481 HOH   HOH B . 
R 8 HOH   212 812 923 HOH   HOH B . 
R 8 HOH   213 813 848 HOH   HOH B . 
R 8 HOH   214 814 603 HOH   HOH B . 
R 8 HOH   215 815 807 HOH   HOH B . 
R 8 HOH   216 816 838 HOH   HOH B . 
R 8 HOH   217 817 800 HOH   HOH B . 
R 8 HOH   218 818 774 HOH   HOH B . 
R 8 HOH   219 819 809 HOH   HOH B . 
R 8 HOH   220 820 801 HOH   HOH B . 
R 8 HOH   221 821 844 HOH   HOH B . 
R 8 HOH   222 822 255 HOH   HOH B . 
R 8 HOH   223 823 577 HOH   HOH B . 
R 8 HOH   224 824 805 HOH   HOH B . 
R 8 HOH   225 825 912 HOH   HOH B . 
R 8 HOH   226 826 778 HOH   HOH B . 
R 8 HOH   227 827 916 HOH   HOH B . 
S 8 HOH   1   601 558 HOH   HOH C . 
S 8 HOH   2   602 930 HOH   HOH C . 
S 8 HOH   3   603 499 HOH   HOH C . 
S 8 HOH   4   604 842 HOH   HOH C . 
S 8 HOH   5   605 834 HOH   HOH C . 
S 8 HOH   6   606 836 HOH   HOH C . 
S 8 HOH   7   607 356 HOH   HOH C . 
S 8 HOH   8   608 913 HOH   HOH C . 
S 8 HOH   9   609 699 HOH   HOH C . 
S 8 HOH   10  610 410 HOH   HOH C . 
S 8 HOH   11  611 716 HOH   HOH C . 
S 8 HOH   12  612 860 HOH   HOH C . 
S 8 HOH   13  613 767 HOH   HOH C . 
S 8 HOH   14  614 347 HOH   HOH C . 
S 8 HOH   15  615 769 HOH   HOH C . 
S 8 HOH   16  616 621 HOH   HOH C . 
S 8 HOH   17  617 506 HOH   HOH C . 
S 8 HOH   18  618 697 HOH   HOH C . 
S 8 HOH   19  619 70  HOH   HOH C . 
S 8 HOH   20  620 395 HOH   HOH C . 
S 8 HOH   21  621 762 HOH   HOH C . 
S 8 HOH   22  622 370 HOH   HOH C . 
S 8 HOH   23  623 926 HOH   HOH C . 
S 8 HOH   24  624 528 HOH   HOH C . 
S 8 HOH   25  625 732 HOH   HOH C . 
S 8 HOH   26  626 327 HOH   HOH C . 
S 8 HOH   27  627 74  HOH   HOH C . 
S 8 HOH   28  628 178 HOH   HOH C . 
S 8 HOH   29  629 99  HOH   HOH C . 
S 8 HOH   30  630 705 HOH   HOH C . 
S 8 HOH   31  631 305 HOH   HOH C . 
S 8 HOH   32  632 456 HOH   HOH C . 
S 8 HOH   33  633 534 HOH   HOH C . 
S 8 HOH   34  634 280 HOH   HOH C . 
S 8 HOH   35  635 840 HOH   HOH C . 
S 8 HOH   36  636 323 HOH   HOH C . 
S 8 HOH   37  637 155 HOH   HOH C . 
S 8 HOH   38  638 10  HOH   HOH C . 
S 8 HOH   39  639 73  HOH   HOH C . 
S 8 HOH   40  640 198 HOH   HOH C . 
S 8 HOH   41  641 866 HOH   HOH C . 
S 8 HOH   42  642 385 HOH   HOH C . 
S 8 HOH   43  643 575 HOH   HOH C . 
S 8 HOH   44  644 281 HOH   HOH C . 
S 8 HOH   45  645 877 HOH   HOH C . 
S 8 HOH   46  646 932 HOH   HOH C . 
S 8 HOH   47  647 53  HOH   HOH C . 
S 8 HOH   48  648 220 HOH   HOH C . 
S 8 HOH   49  649 124 HOH   HOH C . 
S 8 HOH   50  650 225 HOH   HOH C . 
S 8 HOH   51  651 32  HOH   HOH C . 
S 8 HOH   52  652 869 HOH   HOH C . 
S 8 HOH   53  653 282 HOH   HOH C . 
S 8 HOH   54  654 286 HOH   HOH C . 
S 8 HOH   55  655 304 HOH   HOH C . 
S 8 HOH   56  656 624 HOH   HOH C . 
S 8 HOH   57  657 588 HOH   HOH C . 
S 8 HOH   58  658 166 HOH   HOH C . 
S 8 HOH   59  659 627 HOH   HOH C . 
S 8 HOH   60  660 399 HOH   HOH C . 
S 8 HOH   61  661 914 HOH   HOH C . 
S 8 HOH   62  662 269 HOH   HOH C . 
S 8 HOH   63  663 232 HOH   HOH C . 
S 8 HOH   64  664 695 HOH   HOH C . 
S 8 HOH   65  665 746 HOH   HOH C . 
S 8 HOH   66  666 845 HOH   HOH C . 
S 8 HOH   67  667 685 HOH   HOH C . 
S 8 HOH   68  668 381 HOH   HOH C . 
S 8 HOH   69  669 164 HOH   HOH C . 
S 8 HOH   70  670 241 HOH   HOH C . 
S 8 HOH   71  671 169 HOH   HOH C . 
S 8 HOH   72  672 502 HOH   HOH C . 
S 8 HOH   73  673 116 HOH   HOH C . 
S 8 HOH   74  674 292 HOH   HOH C . 
S 8 HOH   75  675 457 HOH   HOH C . 
S 8 HOH   76  676 670 HOH   HOH C . 
S 8 HOH   77  677 572 HOH   HOH C . 
S 8 HOH   78  678 107 HOH   HOH C . 
S 8 HOH   79  679 276 HOH   HOH C . 
S 8 HOH   80  680 171 HOH   HOH C . 
S 8 HOH   81  681 344 HOH   HOH C . 
S 8 HOH   82  682 728 HOH   HOH C . 
S 8 HOH   83  683 538 HOH   HOH C . 
S 8 HOH   84  684 614 HOH   HOH C . 
S 8 HOH   85  685 325 HOH   HOH C . 
S 8 HOH   86  686 549 HOH   HOH C . 
S 8 HOH   87  687 2   HOH   HOH C . 
S 8 HOH   88  688 507 HOH   HOH C . 
S 8 HOH   89  689 815 HOH   HOH C . 
S 8 HOH   90  690 252 HOH   HOH C . 
S 8 HOH   91  691 45  HOH   HOH C . 
S 8 HOH   92  692 129 HOH   HOH C . 
S 8 HOH   93  693 300 HOH   HOH C . 
S 8 HOH   94  694 544 HOH   HOH C . 
S 8 HOH   95  695 751 HOH   HOH C . 
S 8 HOH   96  696 821 HOH   HOH C . 
S 8 HOH   97  697 568 HOH   HOH C . 
S 8 HOH   98  698 461 HOH   HOH C . 
S 8 HOH   99  699 729 HOH   HOH C . 
S 8 HOH   100 700 574 HOH   HOH C . 
S 8 HOH   101 701 294 HOH   HOH C . 
S 8 HOH   102 702 156 HOH   HOH C . 
S 8 HOH   103 703 314 HOH   HOH C . 
S 8 HOH   104 704 136 HOH   HOH C . 
S 8 HOH   105 705 556 HOH   HOH C . 
S 8 HOH   106 706 134 HOH   HOH C . 
S 8 HOH   107 707 650 HOH   HOH C . 
S 8 HOH   108 708 489 HOH   HOH C . 
S 8 HOH   109 709 8   HOH   HOH C . 
S 8 HOH   110 710 701 HOH   HOH C . 
S 8 HOH   111 711 397 HOH   HOH C . 
S 8 HOH   112 712 29  HOH   HOH C . 
S 8 HOH   113 713 742 HOH   HOH C . 
S 8 HOH   114 714 141 HOH   HOH C . 
S 8 HOH   115 715 161 HOH   HOH C . 
S 8 HOH   116 716 163 HOH   HOH C . 
S 8 HOH   117 717 787 HOH   HOH C . 
S 8 HOH   118 718 847 HOH   HOH C . 
S 8 HOH   119 719 483 HOH   HOH C . 
S 8 HOH   120 720 184 HOH   HOH C . 
S 8 HOH   121 721 731 HOH   HOH C . 
S 8 HOH   122 722 757 HOH   HOH C . 
S 8 HOH   123 723 738 HOH   HOH C . 
S 8 HOH   124 724 89  HOH   HOH C . 
S 8 HOH   125 725 353 HOH   HOH C . 
S 8 HOH   126 726 492 HOH   HOH C . 
S 8 HOH   127 727 199 HOH   HOH C . 
S 8 HOH   128 728 197 HOH   HOH C . 
S 8 HOH   129 729 295 HOH   HOH C . 
S 8 HOH   130 730 357 HOH   HOH C . 
S 8 HOH   131 731 219 HOH   HOH C . 
S 8 HOH   132 732 658 HOH   HOH C . 
S 8 HOH   133 733 666 HOH   HOH C . 
S 8 HOH   134 734 447 HOH   HOH C . 
S 8 HOH   135 735 648 HOH   HOH C . 
S 8 HOH   136 736 80  HOH   HOH C . 
S 8 HOH   137 737 835 HOH   HOH C . 
S 8 HOH   138 738 260 HOH   HOH C . 
S 8 HOH   139 739 60  HOH   HOH C . 
S 8 HOH   140 740 425 HOH   HOH C . 
S 8 HOH   141 741 118 HOH   HOH C . 
S 8 HOH   142 742 182 HOH   HOH C . 
S 8 HOH   143 743 826 HOH   HOH C . 
S 8 HOH   144 744 641 HOH   HOH C . 
S 8 HOH   145 745 84  HOH   HOH C . 
S 8 HOH   146 746 303 HOH   HOH C . 
S 8 HOH   147 747 436 HOH   HOH C . 
S 8 HOH   148 748 332 HOH   HOH C . 
S 8 HOH   149 749 523 HOH   HOH C . 
S 8 HOH   150 750 500 HOH   HOH C . 
S 8 HOH   151 751 88  HOH   HOH C . 
S 8 HOH   152 752 515 HOH   HOH C . 
S 8 HOH   153 753 825 HOH   HOH C . 
S 8 HOH   154 754 400 HOH   HOH C . 
S 8 HOH   155 755 245 HOH   HOH C . 
S 8 HOH   156 756 704 HOH   HOH C . 
S 8 HOH   157 757 726 HOH   HOH C . 
S 8 HOH   158 758 247 HOH   HOH C . 
S 8 HOH   159 759 427 HOH   HOH C . 
S 8 HOH   160 760 324 HOH   HOH C . 
S 8 HOH   161 761 802 HOH   HOH C . 
S 8 HOH   162 762 384 HOH   HOH C . 
S 8 HOH   163 763 143 HOH   HOH C . 
S 8 HOH   164 764 420 HOH   HOH C . 
S 8 HOH   165 765 449 HOH   HOH C . 
S 8 HOH   166 766 548 HOH   HOH C . 
S 8 HOH   167 767 581 HOH   HOH C . 
S 8 HOH   168 768 638 HOH   HOH C . 
S 8 HOH   169 769 470 HOH   HOH C . 
S 8 HOH   170 770 253 HOH   HOH C . 
S 8 HOH   171 771 465 HOH   HOH C . 
S 8 HOH   172 772 846 HOH   HOH C . 
S 8 HOH   173 773 706 HOH   HOH C . 
S 8 HOH   174 774 908 HOH   HOH C . 
S 8 HOH   175 775 529 HOH   HOH C . 
S 8 HOH   176 776 929 HOH   HOH C . 
S 8 HOH   177 777 443 HOH   HOH C . 
S 8 HOH   178 778 46  HOH   HOH C . 
S 8 HOH   179 779 678 HOH   HOH C . 
S 8 HOH   180 780 56  HOH   HOH C . 
S 8 HOH   181 781 487 HOH   HOH C . 
S 8 HOH   182 782 458 HOH   HOH C . 
S 8 HOH   183 783 533 HOH   HOH C . 
S 8 HOH   184 784 818 HOH   HOH C . 
S 8 HOH   185 785 870 HOH   HOH C . 
S 8 HOH   186 786 234 HOH   HOH C . 
S 8 HOH   187 787 351 HOH   HOH C . 
S 8 HOH   188 788 233 HOH   HOH C . 
S 8 HOH   189 789 333 HOH   HOH C . 
S 8 HOH   190 790 462 HOH   HOH C . 
S 8 HOH   191 791 330 HOH   HOH C . 
S 8 HOH   192 792 669 HOH   HOH C . 
S 8 HOH   193 793 776 HOH   HOH C . 
S 8 HOH   194 794 904 HOH   HOH C . 
S 8 HOH   195 795 766 HOH   HOH C . 
S 8 HOH   196 796 865 HOH   HOH C . 
S 8 HOH   197 797 768 HOH   HOH C . 
S 8 HOH   198 798 918 HOH   HOH C . 
S 8 HOH   199 799 265 HOH   HOH C . 
S 8 HOH   200 800 204 HOH   HOH C . 
S 8 HOH   201 801 546 HOH   HOH C . 
S 8 HOH   202 802 613 HOH   HOH C . 
S 8 HOH   203 803 512 HOH   HOH C . 
S 8 HOH   204 804 875 HOH   HOH C . 
S 8 HOH   205 805 791 HOH   HOH C . 
S 8 HOH   206 806 285 HOH   HOH C . 
S 8 HOH   207 807 785 HOH   HOH C . 
S 8 HOH   208 808 761 HOH   HOH C . 
S 8 HOH   209 809 879 HOH   HOH C . 
S 8 HOH   210 810 580 HOH   HOH C . 
S 8 HOH   211 811 694 HOH   HOH C . 
S 8 HOH   212 812 861 HOH   HOH C . 
S 8 HOH   213 813 250 HOH   HOH C . 
S 8 HOH   214 814 897 HOH   HOH C . 
S 8 HOH   215 815 645 HOH   HOH C . 
S 8 HOH   216 816 360 HOH   HOH C . 
S 8 HOH   217 817 783 HOH   HOH C . 
S 8 HOH   218 818 896 HOH   HOH C . 
S 8 HOH   219 819 301 HOH   HOH C . 
S 8 HOH   220 820 828 HOH   HOH C . 
S 8 HOH   221 821 882 HOH   HOH C . 
S 8 HOH   222 822 803 HOH   HOH C . 
S 8 HOH   223 823 493 HOH   HOH C . 
S 8 HOH   224 824 772 HOH   HOH C . 
S 8 HOH   225 825 910 HOH   HOH C . 
S 8 HOH   226 826 901 HOH   HOH C . 
S 8 HOH   227 827 898 HOH   HOH C . 
S 8 HOH   228 828 590 HOH   HOH C . 
S 8 HOH   229 829 712 HOH   HOH C . 
S 8 HOH   230 830 863 HOH   HOH C . 
S 8 HOH   231 831 758 HOH   HOH C . 
S 8 HOH   232 832 106 HOH   HOH C . 
S 8 HOH   233 833 601 HOH   HOH C . 
S 8 HOH   234 834 765 HOH   HOH C . 
S 8 HOH   235 835 267 HOH   HOH C . 
S 8 HOH   236 836 886 HOH   HOH C . 
S 8 HOH   237 837 345 HOH   HOH C . 
S 8 HOH   238 838 633 HOH   HOH C . 
S 8 HOH   239 839 799 HOH   HOH C . 
S 8 HOH   240 840 714 HOH   HOH C . 
S 8 HOH   241 841 784 HOH   HOH C . 
S 8 HOH   242 842 596 HOH   HOH C . 
S 8 HOH   243 843 804 HOH   HOH C . 
S 8 HOH   244 844 632 HOH   HOH C . 
S 8 HOH   245 845 617 HOH   HOH C . 
S 8 HOH   246 846 612 HOH   HOH C . 
S 8 HOH   247 847 797 HOH   HOH C . 
S 8 HOH   248 848 902 HOH   HOH C . 
S 8 HOH   249 849 604 HOH   HOH C . 
S 8 HOH   250 850 792 HOH   HOH C . 
S 8 HOH   251 851 905 HOH   HOH C . 
S 8 HOH   252 852 611 HOH   HOH C . 
S 8 HOH   253 853 170 HOH   HOH C . 
S 8 HOH   254 854 600 HOH   HOH C . 
S 8 HOH   255 855 777 HOH   HOH C . 
S 8 HOH   256 856 616 HOH   HOH C . 
S 8 HOH   257 857 883 HOH   HOH C . 
S 8 HOH   258 858 884 HOH   HOH C . 
S 8 HOH   259 859 591 HOH   HOH C . 
S 8 HOH   260 860 907 HOH   HOH C . 
S 8 HOH   261 861 618 HOH   HOH C . 
T 8 HOH   1   601 855 HOH   HOH D . 
T 8 HOH   2   602 498 HOH   HOH D . 
T 8 HOH   3   603 880 HOH   HOH D . 
T 8 HOH   4   604 737 HOH   HOH D . 
T 8 HOH   5   605 221 HOH   HOH D . 
T 8 HOH   6   606 911 HOH   HOH D . 
T 8 HOH   7   607 413 HOH   HOH D . 
T 8 HOH   8   608 78  HOH   HOH D . 
T 8 HOH   9   609 419 HOH   HOH D . 
T 8 HOH   10  610 121 HOH   HOH D . 
T 8 HOH   11  611 248 HOH   HOH D . 
T 8 HOH   12  612 50  HOH   HOH D . 
T 8 HOH   13  613 153 HOH   HOH D . 
T 8 HOH   14  614 335 HOH   HOH D . 
T 8 HOH   15  615 722 HOH   HOH D . 
T 8 HOH   16  616 740 HOH   HOH D . 
T 8 HOH   17  617 216 HOH   HOH D . 
T 8 HOH   18  618 635 HOH   HOH D . 
T 8 HOH   19  619 495 HOH   HOH D . 
T 8 HOH   20  620 736 HOH   HOH D . 
T 8 HOH   21  621 934 HOH   HOH D . 
T 8 HOH   22  622 52  HOH   HOH D . 
T 8 HOH   23  623 626 HOH   HOH D . 
T 8 HOH   24  624 793 HOH   HOH D . 
T 8 HOH   25  625 662 HOH   HOH D . 
T 8 HOH   26  626 157 HOH   HOH D . 
T 8 HOH   27  627 550 HOH   HOH D . 
T 8 HOH   28  628 261 HOH   HOH D . 
T 8 HOH   29  629 583 HOH   HOH D . 
T 8 HOH   30  630 843 HOH   HOH D . 
T 8 HOH   31  631 919 HOH   HOH D . 
T 8 HOH   32  632 338 HOH   HOH D . 
T 8 HOH   33  633 206 HOH   HOH D . 
T 8 HOH   34  634 903 HOH   HOH D . 
T 8 HOH   35  635 625 HOH   HOH D . 
T 8 HOH   36  636 65  HOH   HOH D . 
T 8 HOH   37  637 526 HOH   HOH D . 
T 8 HOH   38  638 12  HOH   HOH D . 
T 8 HOH   39  639 450 HOH   HOH D . 
T 8 HOH   40  640 376 HOH   HOH D . 
T 8 HOH   41  641 117 HOH   HOH D . 
T 8 HOH   42  642 66  HOH   HOH D . 
T 8 HOH   43  643 829 HOH   HOH D . 
T 8 HOH   44  644 122 HOH   HOH D . 
T 8 HOH   45  645 530 HOH   HOH D . 
T 8 HOH   46  646 4   HOH   HOH D . 
T 8 HOH   47  647 251 HOH   HOH D . 
T 8 HOH   48  648 274 HOH   HOH D . 
T 8 HOH   49  649 83  HOH   HOH D . 
T 8 HOH   50  650 871 HOH   HOH D . 
T 8 HOH   51  651 319 HOH   HOH D . 
T 8 HOH   52  652 11  HOH   HOH D . 
T 8 HOH   53  653 390 HOH   HOH D . 
T 8 HOH   54  654 38  HOH   HOH D . 
T 8 HOH   55  655 749 HOH   HOH D . 
T 8 HOH   56  656 100 HOH   HOH D . 
T 8 HOH   57  657 322 HOH   HOH D . 
T 8 HOH   58  658 222 HOH   HOH D . 
T 8 HOH   59  659 368 HOH   HOH D . 
T 8 HOH   60  660 448 HOH   HOH D . 
T 8 HOH   61  661 128 HOH   HOH D . 
T 8 HOH   62  662 64  HOH   HOH D . 
T 8 HOH   63  663 167 HOH   HOH D . 
T 8 HOH   64  664 172 HOH   HOH D . 
T 8 HOH   65  665 734 HOH   HOH D . 
T 8 HOH   66  666 49  HOH   HOH D . 
T 8 HOH   67  667 673 HOH   HOH D . 
T 8 HOH   68  668 152 HOH   HOH D . 
T 8 HOH   69  669 26  HOH   HOH D . 
T 8 HOH   70  670 649 HOH   HOH D . 
T 8 HOH   71  671 341 HOH   HOH D . 
T 8 HOH   72  672 416 HOH   HOH D . 
T 8 HOH   73  673 438 HOH   HOH D . 
T 8 HOH   74  674 33  HOH   HOH D . 
T 8 HOH   75  675 75  HOH   HOH D . 
T 8 HOH   76  676 21  HOH   HOH D . 
T 8 HOH   77  677 672 HOH   HOH D . 
T 8 HOH   78  678 402 HOH   HOH D . 
T 8 HOH   79  679 752 HOH   HOH D . 
T 8 HOH   80  680 176 HOH   HOH D . 
T 8 HOH   81  681 933 HOH   HOH D . 
T 8 HOH   82  682 708 HOH   HOH D . 
T 8 HOH   83  683 814 HOH   HOH D . 
T 8 HOH   84  684 312 HOH   HOH D . 
T 8 HOH   85  685 349 HOH   HOH D . 
T 8 HOH   86  686 58  HOH   HOH D . 
T 8 HOH   87  687 654 HOH   HOH D . 
T 8 HOH   88  688 412 HOH   HOH D . 
T 8 HOH   89  689 426 HOH   HOH D . 
T 8 HOH   90  690 39  HOH   HOH D . 
T 8 HOH   91  691 531 HOH   HOH D . 
T 8 HOH   92  692 411 HOH   HOH D . 
T 8 HOH   93  693 230 HOH   HOH D . 
T 8 HOH   94  694 313 HOH   HOH D . 
T 8 HOH   95  695 289 HOH   HOH D . 
T 8 HOH   96  696 133 HOH   HOH D . 
T 8 HOH   97  697 210 HOH   HOH D . 
T 8 HOH   98  698 205 HOH   HOH D . 
T 8 HOH   99  699 675 HOH   HOH D . 
T 8 HOH   100 700 373 HOH   HOH D . 
T 8 HOH   101 701 639 HOH   HOH D . 
T 8 HOH   102 702 115 HOH   HOH D . 
T 8 HOH   103 703 517 HOH   HOH D . 
T 8 HOH   104 704 922 HOH   HOH D . 
T 8 HOH   105 705 61  HOH   HOH D . 
T 8 HOH   106 706 389 HOH   HOH D . 
T 8 HOH   107 707 830 HOH   HOH D . 
T 8 HOH   108 708 377 HOH   HOH D . 
T 8 HOH   109 709 16  HOH   HOH D . 
T 8 HOH   110 710 105 HOH   HOH D . 
T 8 HOH   111 711 228 HOH   HOH D . 
T 8 HOH   112 712 137 HOH   HOH D . 
T 8 HOH   113 713 680 HOH   HOH D . 
T 8 HOH   114 714 19  HOH   HOH D . 
T 8 HOH   115 715 85  HOH   HOH D . 
T 8 HOH   116 716 684 HOH   HOH D . 
T 8 HOH   117 717 218 HOH   HOH D . 
T 8 HOH   118 718 36  HOH   HOH D . 
T 8 HOH   119 719 263 HOH   HOH D . 
T 8 HOH   120 720 392 HOH   HOH D . 
T 8 HOH   121 721 140 HOH   HOH D . 
T 8 HOH   122 722 824 HOH   HOH D . 
T 8 HOH   123 723 302 HOH   HOH D . 
T 8 HOH   124 724 246 HOH   HOH D . 
T 8 HOH   125 725 753 HOH   HOH D . 
T 8 HOH   126 726 867 HOH   HOH D . 
T 8 HOH   127 727 543 HOH   HOH D . 
T 8 HOH   128 728 148 HOH   HOH D . 
T 8 HOH   129 729 162 HOH   HOH D . 
T 8 HOH   130 730 68  HOH   HOH D . 
T 8 HOH   131 731 181 HOH   HOH D . 
T 8 HOH   132 732 125 HOH   HOH D . 
T 8 HOH   133 733 159 HOH   HOH D . 
T 8 HOH   134 734 346 HOH   HOH D . 
T 8 HOH   135 735 350 HOH   HOH D . 
T 8 HOH   136 736 640 HOH   HOH D . 
T 8 HOH   137 737 455 HOH   HOH D . 
T 8 HOH   138 738 367 HOH   HOH D . 
T 8 HOH   139 739 207 HOH   HOH D . 
T 8 HOH   140 740 71  HOH   HOH D . 
T 8 HOH   141 741 235 HOH   HOH D . 
T 8 HOH   142 742 759 HOH   HOH D . 
T 8 HOH   143 743 586 HOH   HOH D . 
T 8 HOH   144 744 674 HOH   HOH D . 
T 8 HOH   145 745 409 HOH   HOH D . 
T 8 HOH   146 746 249 HOH   HOH D . 
T 8 HOH   147 747 278 HOH   HOH D . 
T 8 HOH   148 748 831 HOH   HOH D . 
T 8 HOH   149 749 244 HOH   HOH D . 
T 8 HOH   150 750 109 HOH   HOH D . 
T 8 HOH   151 751 527 HOH   HOH D . 
T 8 HOH   152 752 643 HOH   HOH D . 
T 8 HOH   153 753 408 HOH   HOH D . 
T 8 HOH   154 754 14  HOH   HOH D . 
T 8 HOH   155 755 310 HOH   HOH D . 
T 8 HOH   156 756 454 HOH   HOH D . 
T 8 HOH   157 757 554 HOH   HOH D . 
T 8 HOH   158 758 110 HOH   HOH D . 
T 8 HOH   159 759 676 HOH   HOH D . 
T 8 HOH   160 760 721 HOH   HOH D . 
T 8 HOH   161 761 668 HOH   HOH D . 
T 8 HOH   162 762 95  HOH   HOH D . 
T 8 HOH   163 763 138 HOH   HOH D . 
T 8 HOH   164 764 664 HOH   HOH D . 
T 8 HOH   165 765 67  HOH   HOH D . 
T 8 HOH   166 766 223 HOH   HOH D . 
T 8 HOH   167 767 386 HOH   HOH D . 
T 8 HOH   168 768 421 HOH   HOH D . 
T 8 HOH   169 769 862 HOH   HOH D . 
T 8 HOH   170 770 446 HOH   HOH D . 
T 8 HOH   171 771 168 HOH   HOH D . 
T 8 HOH   172 772 710 HOH   HOH D . 
T 8 HOH   173 773 822 HOH   HOH D . 
T 8 HOH   174 774 733 HOH   HOH D . 
T 8 HOH   175 775 189 HOH   HOH D . 
T 8 HOH   176 776 298 HOH   HOH D . 
T 8 HOH   177 777 537 HOH   HOH D . 
T 8 HOH   178 778 18  HOH   HOH D . 
T 8 HOH   179 779 587 HOH   HOH D . 
T 8 HOH   180 780 631 HOH   HOH D . 
T 8 HOH   181 781 928 HOH   HOH D . 
T 8 HOH   182 782 468 HOH   HOH D . 
T 8 HOH   183 783 290 HOH   HOH D . 
T 8 HOH   184 784 212 HOH   HOH D . 
T 8 HOH   185 785 851 HOH   HOH D . 
T 8 HOH   186 786 355 HOH   HOH D . 
T 8 HOH   187 787 321 HOH   HOH D . 
T 8 HOH   188 788 780 HOH   HOH D . 
T 8 HOH   189 789 770 HOH   HOH D . 
T 8 HOH   190 790 429 HOH   HOH D . 
T 8 HOH   191 791 328 HOH   HOH D . 
T 8 HOH   192 792 424 HOH   HOH D . 
T 8 HOH   193 793 682 HOH   HOH D . 
T 8 HOH   194 794 598 HOH   HOH D . 
T 8 HOH   195 795 656 HOH   HOH D . 
T 8 HOH   196 796 849 HOH   HOH D . 
T 8 HOH   197 797 608 HOH   HOH D . 
T 8 HOH   198 798 730 HOH   HOH D . 
T 8 HOH   199 799 683 HOH   HOH D . 
T 8 HOH   200 800 28  HOH   HOH D . 
T 8 HOH   201 801 177 HOH   HOH D . 
T 8 HOH   202 802 364 HOH   HOH D . 
T 8 HOH   203 803 775 HOH   HOH D . 
T 8 HOH   204 804 755 HOH   HOH D . 
T 8 HOH   205 805 630 HOH   HOH D . 
T 8 HOH   206 806 154 HOH   HOH D . 
T 8 HOH   207 807 213 HOH   HOH D . 
T 8 HOH   208 808 885 HOH   HOH D . 
T 8 HOH   209 809 881 HOH   HOH D . 
T 8 HOH   210 810 812 HOH   HOH D . 
T 8 HOH   211 811 931 HOH   HOH D . 
T 8 HOH   212 812 808 HOH   HOH D . 
T 8 HOH   213 813 936 HOH   HOH D . 
T 8 HOH   214 814 610 HOH   HOH D . 
T 8 HOH   215 815 925 HOH   HOH D . 
T 8 HOH   216 816 597 HOH   HOH D . 
T 8 HOH   217 817 264 HOH   HOH D . 
T 8 HOH   218 818 779 HOH   HOH D . 
T 8 HOH   219 819 257 HOH   HOH D . 
T 8 HOH   220 820 724 HOH   HOH D . 
T 8 HOH   221 821 764 HOH   HOH D . 
T 8 HOH   222 822 69  HOH   HOH D . 
T 8 HOH   223 823 841 HOH   HOH D . 
T 8 HOH   224 824 917 HOH   HOH D . 
T 8 HOH   225 825 144 HOH   HOH D . 
T 8 HOH   226 826 607 HOH   HOH D . 
T 8 HOH   227 827 795 HOH   HOH D . 
T 8 HOH   228 828 788 HOH   HOH D . 
T 8 HOH   229 829 615 HOH   HOH D . 
T 8 HOH   230 830 857 HOH   HOH D . 
T 8 HOH   231 831 185 HOH   HOH D . 
T 8 HOH   232 832 431 HOH   HOH D . 
T 8 HOH   233 833 582 HOH   HOH D . 
T 8 HOH   234 834 890 HOH   HOH D . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.21.1_5286 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless  ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .           4 
? 'model building' ? ? ? ? ? ? ? ? ? ? ? Coot     ? ? ? .           5 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9BLV 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     113.523 
_cell.length_a_esd                 ? 
_cell.length_b                     109.962 
_cell.length_b_esd                 ? 
_cell.length_c                     144.982 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        16 
_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                         9BLV 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_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                   9BLV 
_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             2.18 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          43.56 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_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    '0.1 M potassium phosphate, pH 8, 0.2 M CsCl, 22% PEG 4000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-03-01 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0000 
_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                        'APS BEAMLINE 22-ID' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0000 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   22-ID 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          19.86 
_reflns.entry_id                                       9BLV 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.776 
_reflns.d_resolution_low                               56.76 
_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                                     94968 
_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                           94.4 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          5.4 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.994 
_reflns.pdbx_CC_star                                   0.998 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.776 
_reflns_shell.d_res_low                                     1.80 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.6 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4748 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.666 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_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                                 9BLV 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.78 
_refine.ls_d_res_low                             56.76 
_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                     94874 
_refine.ls_number_reflns_R_free                  4846 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    54.33 
_refine.ls_percent_reflns_R_free                 5.11 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2003 
_refine.ls_R_factor_R_free                       0.2474 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1978 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 33.72 
_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                            0.21 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.78 
_refine_hist.d_res_low                        56.76 
_refine_hist.number_atoms_solvent             936 
_refine_hist.number_atoms_total               15632 
_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        14564 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         132 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
_refine_ls_restr.pdbx_refine_id            'X-RAY DIFFRACTION' 
_refine_ls_restr.criterion                 ? 
_refine_ls_restr.dev_ideal                 0.007 
_refine_ls_restr.dev_ideal_target          ? 
_refine_ls_restr.number                    2678 
_refine_ls_restr.rejects                   ? 
_refine_ls_restr.type                      f_plane_restr 
_refine_ls_restr.weight                    ? 
_refine_ls_restr.pdbx_restraint_function   ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.776 
_refine_ls_shell.d_res_low                        1.80 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             3 
_refine_ls_shell.number_reflns_R_work             48 
_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                  0.3153 
_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                  0.6909 
# 
_struct.entry_id                     9BLV 
_struct.title                        'Proteus vulgaris tryptophan indole-lyase complexed with L-Trp and benzimidazole' 
_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        9BLV 
_struct_keywords.text            
;pyridoxal-5'-phosphate, reaction intermediates, reaction mechanism, aminotransferase fold, LYASE
;
_struct_keywords.pdbx_keywords   LYASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 1 ? 
E N N 2 ? 
F N N 2 ? 
G N N 3 ? 
H N N 4 ? 
I N N 5 ? 
J N N 5 ? 
K N N 6 ? 
L N N 2 ? 
M N N 2 ? 
N N N 7 ? 
O N N 3 ? 
P N N 4 ? 
Q N N 8 ? 
R N N 8 ? 
S N N 8 ? 
T N N 8 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    TNAA_PROVU 
_struct_ref.pdbx_db_accession          P28796 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MAKRIVEPFRIKMVEKIRVPSREEREAALKEAGYNPFLLPSSAVYIDLLTDSGTNAMSDHQWAAMITGDEAYAGSRNYYD
LKDKAKELFNYDYIIPAHQGRGAENILFPVLLKYKQKEGKAKNPVFISNFHFDTTAAHVELNGCKAINIVTEKAFDSETY
DDWKGDFDIKKLKENIAQHGADNIVAIVSTVTCNSAGGQPVSMSNLKEVYEIAKQHGIFVVMDSARFCENAYFIKARDPK
YKNATIKEVIFDMYKYADALTMSAKKDPLLNIGGLVAIRDNEEIFTLARQRCVPMEGFVTYGGLAGRDMAAMVQGLEEGT
EEEYLHYRIGQVKYLGDRLREAGIPIQYPTGGHAVFVDCKKLVPQIPGDQFPAQAVINALYLESGVRAVEIGSFLLGRDP
ATGEQKHADMEFMRLTIARRVYTNDHMDYIADALIGLKEKFATLKGLEFEYEPPVLRHFTARLKPIE
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9BLV A 1 ? 467 ? P28796 1 ? 467 ? 1 467 
2 1 9BLV B 1 ? 467 ? P28796 1 ? 467 ? 1 467 
3 1 9BLV C 1 ? 467 ? P28796 1 ? 467 ? 1 467 
4 1 9BLV D 1 ? 467 ? P28796 1 ? 467 ? 1 467 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 19130 ? 
1 MORE         -67   ? 
1 'SSA (A^2)'  56550 ? 
# 
_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,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 21  ? ALA A 32  ? SER A 21  ALA A 32  1 ? 12 
HELX_P HELX_P2  AA2 ASN A 35  ? LEU A 39  ? ASN A 35  LEU A 39  5 ? 5  
HELX_P HELX_P3  AA3 PRO A 40  ? VAL A 44  ? PRO A 40  VAL A 44  5 ? 5  
HELX_P HELX_P4  AA4 ASP A 59  ? THR A 67  ? ASP A 59  THR A 67  1 ? 9  
HELX_P HELX_P5  AA5 SER A 75  ? ASN A 90  ? SER A 75  ASN A 90  1 ? 16 
HELX_P HELX_P6  AA6 GLN A 99  ? GLN A 116 ? GLN A 99  GLN A 116 1 ? 18 
HELX_P HELX_P7  AA7 PHE A 132 ? ASN A 142 ? PHE A 132 ASN A 142 1 ? 11 
HELX_P HELX_P8  AA8 THR A 151 ? ASP A 156 ? THR A 151 ASP A 156 5 ? 6  
HELX_P HELX_P9  AA9 ASP A 168 ? GLY A 180 ? ASP A 168 GLY A 180 1 ? 13 
HELX_P HELX_P10 AB1 SER A 202 ? GLY A 217 ? SER A 202 GLY A 217 1 ? 16 
HELX_P HELX_P11 AB2 ARG A 226 ? ASP A 238 ? ARG A 226 ASP A 238 1 ? 13 
HELX_P HELX_P12 AB3 THR A 245 ? TYR A 254 ? THR A 245 TYR A 254 1 ? 10 
HELX_P HELX_P13 AB4 LYS A 255 ? ALA A 257 ? LYS A 255 ALA A 257 5 ? 3  
HELX_P HELX_P14 AB5 ASN A 281 ? GLU A 296 ? ASN A 281 GLU A 296 1 ? 16 
HELX_P HELX_P15 AB6 ALA A 305 ? GLY A 319 ? ALA A 305 GLY A 319 1 ? 15 
HELX_P HELX_P16 AB7 GLU A 321 ? ALA A 342 ? GLU A 321 ALA A 342 1 ? 22 
HELX_P HELX_P17 AB8 CYS A 359 ? VAL A 363 ? CYS A 359 VAL A 363 1 ? 5  
HELX_P HELX_P18 AB9 PRO A 367 ? GLN A 370 ? PRO A 367 GLN A 370 5 ? 4  
HELX_P HELX_P19 AC1 PHE A 371 ? GLY A 385 ? PHE A 371 GLY A 385 1 ? 15 
HELX_P HELX_P20 AC2 GLY A 392 ? GLY A 397 ? GLY A 392 GLY A 397 1 ? 6  
HELX_P HELX_P21 AC3 THR A 423 ? GLY A 436 ? THR A 423 GLY A 436 1 ? 14 
HELX_P HELX_P22 AC4 LEU A 456 ? THR A 460 ? LEU A 456 THR A 460 5 ? 5  
HELX_P HELX_P23 AC5 SER B 21  ? ALA B 32  ? SER B 21  ALA B 32  1 ? 12 
HELX_P HELX_P24 AC6 ASN B 35  ? LEU B 39  ? ASN B 35  LEU B 39  5 ? 5  
HELX_P HELX_P25 AC7 PRO B 40  ? VAL B 44  ? PRO B 40  VAL B 44  5 ? 5  
HELX_P HELX_P26 AC8 ASP B 59  ? THR B 67  ? ASP B 59  THR B 67  1 ? 9  
HELX_P HELX_P27 AC9 SER B 75  ? ASN B 90  ? SER B 75  ASN B 90  1 ? 16 
HELX_P HELX_P28 AD1 GLN B 99  ? LYS B 117 ? GLN B 99  LYS B 117 1 ? 19 
HELX_P HELX_P29 AD2 GLU B 118 ? LYS B 120 ? GLU B 118 LYS B 120 5 ? 3  
HELX_P HELX_P30 AD3 PHE B 132 ? ASN B 142 ? PHE B 132 ASN B 142 1 ? 11 
HELX_P HELX_P31 AD4 THR B 151 ? ASP B 156 ? THR B 151 ASP B 156 5 ? 6  
HELX_P HELX_P32 AD5 ASP B 168 ? GLY B 180 ? ASP B 168 GLY B 180 1 ? 13 
HELX_P HELX_P33 AD6 SER B 202 ? HIS B 216 ? SER B 202 HIS B 216 1 ? 15 
HELX_P HELX_P34 AD7 ARG B 226 ? ASP B 238 ? ARG B 226 ASP B 238 1 ? 13 
HELX_P HELX_P35 AD8 PRO B 239 ? LYS B 242 ? PRO B 239 LYS B 242 5 ? 4  
HELX_P HELX_P36 AD9 THR B 245 ? TYR B 254 ? THR B 245 TYR B 254 1 ? 10 
HELX_P HELX_P37 AE1 LYS B 255 ? ALA B 257 ? LYS B 255 ALA B 257 5 ? 3  
HELX_P HELX_P38 AE2 ASN B 281 ? GLU B 296 ? ASN B 281 GLU B 296 1 ? 16 
HELX_P HELX_P39 AE3 ALA B 305 ? GLY B 319 ? ALA B 305 GLY B 319 1 ? 15 
HELX_P HELX_P40 AE4 GLU B 321 ? ALA B 342 ? GLU B 321 ALA B 342 1 ? 22 
HELX_P HELX_P41 AE5 PRO B 367 ? GLN B 370 ? PRO B 367 GLN B 370 5 ? 4  
HELX_P HELX_P42 AE6 PHE B 371 ? GLY B 385 ? PHE B 371 GLY B 385 1 ? 15 
HELX_P HELX_P43 AE7 GLY B 392 ? GLY B 397 ? GLY B 392 GLY B 397 1 ? 6  
HELX_P HELX_P44 AE8 THR B 423 ? GLY B 436 ? THR B 423 GLY B 436 1 ? 14 
HELX_P HELX_P45 AE9 LEU B 437 ? ALA B 442 ? LEU B 437 ALA B 442 1 ? 6  
HELX_P HELX_P46 AF1 LEU B 456 ? ALA B 461 ? LEU B 456 ALA B 461 1 ? 6  
HELX_P HELX_P47 AF2 SER C 21  ? ALA C 32  ? SER C 21  ALA C 32  1 ? 12 
HELX_P HELX_P48 AF3 ASN C 35  ? LEU C 39  ? ASN C 35  LEU C 39  5 ? 5  
HELX_P HELX_P49 AF4 PRO C 40  ? VAL C 44  ? PRO C 40  VAL C 44  5 ? 5  
HELX_P HELX_P50 AF5 ASP C 59  ? THR C 67  ? ASP C 59  THR C 67  1 ? 9  
HELX_P HELX_P51 AF6 SER C 75  ? ASN C 90  ? SER C 75  ASN C 90  1 ? 16 
HELX_P HELX_P52 AF7 GLN C 99  ? GLN C 116 ? GLN C 99  GLN C 116 1 ? 18 
HELX_P HELX_P53 AF8 LYS C 117 ? LYS C 120 ? LYS C 117 LYS C 120 5 ? 4  
HELX_P HELX_P54 AF9 PHE C 132 ? ASN C 142 ? PHE C 132 ASN C 142 1 ? 11 
HELX_P HELX_P55 AG1 THR C 151 ? ASP C 156 ? THR C 151 ASP C 156 5 ? 6  
HELX_P HELX_P56 AG2 ASP C 168 ? GLY C 180 ? ASP C 168 GLY C 180 1 ? 13 
HELX_P HELX_P57 AG3 SER C 202 ? HIS C 216 ? SER C 202 HIS C 216 1 ? 15 
HELX_P HELX_P58 AG4 ARG C 226 ? ASP C 238 ? ARG C 226 ASP C 238 1 ? 13 
HELX_P HELX_P59 AG5 PRO C 239 ? LYS C 242 ? PRO C 239 LYS C 242 5 ? 4  
HELX_P HELX_P60 AG6 THR C 245 ? TYR C 254 ? THR C 245 TYR C 254 1 ? 10 
HELX_P HELX_P61 AG7 LYS C 255 ? ALA C 257 ? LYS C 255 ALA C 257 5 ? 3  
HELX_P HELX_P62 AG8 ASN C 281 ? GLU C 296 ? ASN C 281 GLU C 296 1 ? 16 
HELX_P HELX_P63 AG9 ALA C 305 ? GLY C 319 ? ALA C 305 GLY C 319 1 ? 15 
HELX_P HELX_P64 AH1 GLU C 321 ? ALA C 342 ? GLU C 321 ALA C 342 1 ? 22 
HELX_P HELX_P65 AH2 PRO C 367 ? GLN C 370 ? PRO C 367 GLN C 370 5 ? 4  
HELX_P HELX_P66 AH3 PHE C 371 ? GLY C 385 ? PHE C 371 GLY C 385 1 ? 15 
HELX_P HELX_P67 AH4 GLY C 392 ? GLY C 397 ? GLY C 392 GLY C 397 1 ? 6  
HELX_P HELX_P68 AH5 THR C 423 ? LEU C 437 ? THR C 423 LEU C 437 1 ? 15 
HELX_P HELX_P69 AH6 LYS C 438 ? LEU C 444 ? LYS C 438 LEU C 444 5 ? 7  
HELX_P HELX_P70 AH7 LEU C 456 ? THR C 460 ? LEU C 456 THR C 460 5 ? 5  
HELX_P HELX_P71 AH8 SER D 21  ? GLY D 33  ? SER D 21  GLY D 33  1 ? 13 
HELX_P HELX_P72 AH9 ASN D 35  ? LEU D 39  ? ASN D 35  LEU D 39  5 ? 5  
HELX_P HELX_P73 AI1 PRO D 40  ? VAL D 44  ? PRO D 40  VAL D 44  5 ? 5  
HELX_P HELX_P74 AI2 ASP D 59  ? THR D 67  ? ASP D 59  THR D 67  1 ? 9  
HELX_P HELX_P75 AI3 SER D 75  ? ASN D 90  ? SER D 75  ASN D 90  1 ? 16 
HELX_P HELX_P76 AI4 GLN D 99  ? GLN D 116 ? GLN D 99  GLN D 116 1 ? 18 
HELX_P HELX_P77 AI5 LYS D 117 ? LYS D 120 ? LYS D 117 LYS D 120 5 ? 4  
HELX_P HELX_P78 AI6 PHE D 132 ? ASN D 142 ? PHE D 132 ASN D 142 1 ? 11 
HELX_P HELX_P79 AI7 THR D 151 ? ASP D 156 ? THR D 151 ASP D 156 5 ? 6  
HELX_P HELX_P80 AI8 ASP D 168 ? GLY D 180 ? ASP D 168 GLY D 180 1 ? 13 
HELX_P HELX_P81 AI9 SER D 202 ? HIS D 216 ? SER D 202 HIS D 216 1 ? 15 
HELX_P HELX_P82 AJ1 ARG D 226 ? ASP D 238 ? ARG D 226 ASP D 238 1 ? 13 
HELX_P HELX_P83 AJ2 PRO D 239 ? LYS D 242 ? PRO D 239 LYS D 242 5 ? 4  
HELX_P HELX_P84 AJ3 THR D 245 ? TYR D 254 ? THR D 245 TYR D 254 1 ? 10 
HELX_P HELX_P85 AJ4 LYS D 255 ? ALA D 257 ? LYS D 255 ALA D 257 5 ? 3  
HELX_P HELX_P86 AJ5 ASN D 281 ? GLU D 296 ? ASN D 281 GLU D 296 1 ? 16 
HELX_P HELX_P87 AJ6 ALA D 305 ? GLY D 319 ? ALA D 305 GLY D 319 1 ? 15 
HELX_P HELX_P88 AJ7 GLU D 321 ? ALA D 342 ? GLU D 321 ALA D 342 1 ? 22 
HELX_P HELX_P89 AJ8 PHE D 371 ? GLY D 385 ? PHE D 371 GLY D 385 1 ? 15 
HELX_P HELX_P90 AJ9 GLY D 392 ? GLY D 397 ? GLY D 392 GLY D 397 1 ? 6  
HELX_P HELX_P91 AK1 THR D 423 ? LEU D 437 ? THR D 423 LEU D 437 1 ? 15 
HELX_P HELX_P92 AK2 LEU D 456 ? ALA D 461 ? LEU D 456 ALA D 461 1 ? 6  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1  covale one ? C LYS 266 NZ  ? ? ? 1_555 N A1A2Z .   C4A ? ? C LYS 266 C A1A2Z 503 1_555 ? ? ? ? ? ? ? 1.434 ? ? 
metalc1  metalc ?   ? A GLY 53  O   ? ? ? 1_555 E K     .   K   ? ? A GLY 53  A K     501 1_555 ? ? ? ? ? ? ? 2.876 ? ? 
metalc2  metalc ?   ? A GLU 70  O   ? ? ? 1_555 F K     .   K   ? ? A GLU 70  A K     502 1_555 ? ? ? ? ? ? ? 3.033 ? ? 
metalc3  metalc ?   ? A GLU 70  OE1 ? ? ? 1_555 F K     .   K   ? ? A GLU 70  A K     502 1_555 ? ? ? ? ? ? ? 2.681 ? ? 
metalc4  metalc ?   ? A ASN 271 O   ? ? ? 1_555 E K     .   K   ? ? A ASN 271 A K     501 1_555 ? ? ? ? ? ? ? 2.948 ? ? 
metalc5  metalc ?   ? E K   .   K   ? ? ? 1_555 Q HOH   .   O   ? ? A K   501 A HOH   620 1_555 ? ? ? ? ? ? ? 2.867 ? ? 
metalc6  metalc ?   ? E K   .   K   ? ? ? 1_555 Q HOH   .   O   ? ? A K   501 A HOH   758 1_555 ? ? ? ? ? ? ? 2.954 ? ? 
metalc7  metalc ?   ? E K   .   K   ? ? ? 1_555 B GLU   70  O   ? ? A K   501 B GLU   70  1_555 ? ? ? ? ? ? ? 3.009 ? ? 
metalc8  metalc ?   ? E K   .   K   ? ? ? 1_555 B GLU   70  OE1 ? ? A K   501 B GLU   70  1_555 ? ? ? ? ? ? ? 2.756 ? ? 
metalc9  metalc ?   ? E K   .   K   ? ? ? 1_555 R HOH   .   O   ? ? A K   501 B HOH   703 1_555 ? ? ? ? ? ? ? 2.837 ? ? 
metalc10 metalc ?   ? F K   .   K   ? ? ? 1_555 Q HOH   .   O   ? ? A K   502 A HOH   743 1_555 ? ? ? ? ? ? ? 2.761 ? ? 
metalc11 metalc ?   ? F K   .   K   ? ? ? 1_555 B GLY   53  O   ? ? A K   502 B GLY   53  1_555 ? ? ? ? ? ? ? 2.866 ? ? 
metalc12 metalc ?   ? F K   .   K   ? ? ? 1_555 B ASN   271 O   ? ? A K   502 B ASN   271 1_555 ? ? ? ? ? ? ? 2.963 ? ? 
metalc13 metalc ?   ? F K   .   K   ? ? ? 1_555 R HOH   .   O   ? ? A K   502 B HOH   700 1_555 ? ? ? ? ? ? ? 2.739 ? ? 
metalc14 metalc ?   ? F K   .   K   ? ? ? 1_555 R HOH   .   O   ? ? A K   502 B HOH   742 1_555 ? ? ? ? ? ? ? 3.029 ? ? 
metalc15 metalc ?   ? C GLY 53  O   ? ? ? 1_555 M K     .   K   ? ? C GLY 53  C K     502 1_555 ? ? ? ? ? ? ? 2.907 ? ? 
metalc16 metalc ?   ? C GLU 70  O   ? ? ? 1_555 L K     .   K   ? ? C GLU 70  C K     501 1_555 ? ? ? ? ? ? ? 3.088 ? ? 
metalc17 metalc ?   ? C GLU 70  OE1 ? ? ? 1_555 L K     .   K   ? ? C GLU 70  C K     501 1_555 ? ? ? ? ? ? ? 2.777 ? ? 
metalc18 metalc ?   ? C ASN 271 O   ? ? ? 1_555 M K     .   K   ? ? C ASN 271 C K     502 1_555 ? ? ? ? ? ? ? 2.972 ? ? 
metalc19 metalc ?   ? L K   .   K   ? ? ? 1_555 S HOH   .   O   ? ? C K   501 C HOH   680 1_555 ? ? ? ? ? ? ? 2.838 ? ? 
metalc20 metalc ?   ? L K   .   K   ? ? ? 1_555 S HOH   .   O   ? ? C K   501 C HOH   741 1_555 ? ? ? ? ? ? ? 2.789 ? ? 
metalc21 metalc ?   ? L K   .   K   ? ? ? 1_555 D GLY   53  O   ? ? C K   501 D GLY   53  1_555 ? ? ? ? ? ? ? 2.681 ? ? 
metalc22 metalc ?   ? L K   .   K   ? ? ? 1_555 D ASN   271 O   ? ? C K   501 D ASN   271 1_555 ? ? ? ? ? ? ? 2.901 ? ? 
metalc23 metalc ?   ? L K   .   K   ? ? ? 1_555 T HOH   .   O   ? ? C K   501 D HOH   711 1_555 ? ? ? ? ? ? ? 3.085 ? ? 
metalc24 metalc ?   ? M K   .   K   ? ? ? 1_555 S HOH   .   O   ? ? C K   502 C HOH   702 1_555 ? ? ? ? ? ? ? 3.001 ? ? 
metalc25 metalc ?   ? M K   .   K   ? ? ? 1_555 D GLU   70  O   ? ? C K   502 D GLU   70  1_555 ? ? ? ? ? ? ? 3.142 ? ? 
metalc26 metalc ?   ? M K   .   K   ? ? ? 1_555 D GLU   70  OE1 ? ? C K   502 D GLU   70  1_555 ? ? ? ? ? ? ? 2.698 ? ? 
metalc27 metalc ?   ? M K   .   K   ? ? ? 1_555 T HOH   .   O   ? ? C K   502 D HOH   696 1_555 ? ? ? ? ? ? ? 2.653 ? ? 
metalc28 metalc ?   ? M K   .   K   ? ? ? 1_555 T HOH   .   O   ? ? C K   502 D HOH   723 1_555 ? ? ? ? ? ? ? 2.816 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
covale ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  O   ? A GLY 53  ? A GLY 53  ? 1_555 K ? E K . ? A K 501 ? 1_555 O   ? A ASN 271 ? A ASN 271 ? 1_555 80.9  ? 
2  O   ? A GLY 53  ? A GLY 53  ? 1_555 K ? E K . ? A K 501 ? 1_555 O   ? Q HOH .   ? A HOH 620 ? 1_555 73.0  ? 
3  O   ? A ASN 271 ? A ASN 271 ? 1_555 K ? E K . ? A K 501 ? 1_555 O   ? Q HOH .   ? A HOH 620 ? 1_555 109.5 ? 
4  O   ? A GLY 53  ? A GLY 53  ? 1_555 K ? E K . ? A K 501 ? 1_555 O   ? Q HOH .   ? A HOH 758 ? 1_555 116.7 ? 
5  O   ? A ASN 271 ? A ASN 271 ? 1_555 K ? E K . ? A K 501 ? 1_555 O   ? Q HOH .   ? A HOH 758 ? 1_555 88.3  ? 
6  O   ? Q HOH .   ? A HOH 620 ? 1_555 K ? E K . ? A K 501 ? 1_555 O   ? Q HOH .   ? A HOH 758 ? 1_555 52.7  ? 
7  O   ? A GLY 53  ? A GLY 53  ? 1_555 K ? E K . ? A K 501 ? 1_555 O   ? B GLU 70  ? B GLU 70  ? 1_555 77.7  ? 
8  O   ? A ASN 271 ? A ASN 271 ? 1_555 K ? E K . ? A K 501 ? 1_555 O   ? B GLU 70  ? B GLU 70  ? 1_555 158.6 ? 
9  O   ? Q HOH .   ? A HOH 620 ? 1_555 K ? E K . ? A K 501 ? 1_555 O   ? B GLU 70  ? B GLU 70  ? 1_555 63.2  ? 
10 O   ? Q HOH .   ? A HOH 758 ? 1_555 K ? E K . ? A K 501 ? 1_555 O   ? B GLU 70  ? B GLU 70  ? 1_555 100.5 ? 
11 O   ? A GLY 53  ? A GLY 53  ? 1_555 K ? E K . ? A K 501 ? 1_555 OE1 ? B GLU 70  ? B GLU 70  ? 1_555 93.8  ? 
12 O   ? A ASN 271 ? A ASN 271 ? 1_555 K ? E K . ? A K 501 ? 1_555 OE1 ? B GLU 70  ? B GLU 70  ? 1_555 93.4  ? 
13 O   ? Q HOH .   ? A HOH 620 ? 1_555 K ? E K . ? A K 501 ? 1_555 OE1 ? B GLU 70  ? B GLU 70  ? 1_555 150.8 ? 
14 O   ? Q HOH .   ? A HOH 758 ? 1_555 K ? E K . ? A K 501 ? 1_555 OE1 ? B GLU 70  ? B GLU 70  ? 1_555 149.3 ? 
15 O   ? B GLU 70  ? B GLU 70  ? 1_555 K ? E K . ? A K 501 ? 1_555 OE1 ? B GLU 70  ? B GLU 70  ? 1_555 88.9  ? 
16 O   ? A GLY 53  ? A GLY 53  ? 1_555 K ? E K . ? A K 501 ? 1_555 O   ? R HOH .   ? B HOH 703 ? 1_555 167.3 ? 
17 O   ? A ASN 271 ? A ASN 271 ? 1_555 K ? E K . ? A K 501 ? 1_555 O   ? R HOH .   ? B HOH 703 ? 1_555 109.8 ? 
18 O   ? Q HOH .   ? A HOH 620 ? 1_555 K ? E K . ? A K 501 ? 1_555 O   ? R HOH .   ? B HOH 703 ? 1_555 96.5  ? 
19 O   ? Q HOH .   ? A HOH 758 ? 1_555 K ? E K . ? A K 501 ? 1_555 O   ? R HOH .   ? B HOH 703 ? 1_555 58.6  ? 
20 O   ? B GLU 70  ? B GLU 70  ? 1_555 K ? E K . ? A K 501 ? 1_555 O   ? R HOH .   ? B HOH 703 ? 1_555 91.4  ? 
21 OE1 ? B GLU 70  ? B GLU 70  ? 1_555 K ? E K . ? A K 501 ? 1_555 O   ? R HOH .   ? B HOH 703 ? 1_555 92.3  ? 
22 O   ? A GLU 70  ? A GLU 70  ? 1_555 K ? F K . ? A K 502 ? 1_555 OE1 ? A GLU 70  ? A GLU 70  ? 1_555 87.6  ? 
23 O   ? A GLU 70  ? A GLU 70  ? 1_555 K ? F K . ? A K 502 ? 1_555 O   ? Q HOH .   ? A HOH 743 ? 1_555 88.4  ? 
24 OE1 ? A GLU 70  ? A GLU 70  ? 1_555 K ? F K . ? A K 502 ? 1_555 O   ? Q HOH .   ? A HOH 743 ? 1_555 89.1  ? 
25 O   ? A GLU 70  ? A GLU 70  ? 1_555 K ? F K . ? A K 502 ? 1_555 O   ? B GLY 53  ? B GLY 53  ? 1_555 84.7  ? 
26 OE1 ? A GLU 70  ? A GLU 70  ? 1_555 K ? F K . ? A K 502 ? 1_555 O   ? B GLY 53  ? B GLY 53  ? 1_555 94.5  ? 
27 O   ? Q HOH .   ? A HOH 743 ? 1_555 K ? F K . ? A K 502 ? 1_555 O   ? B GLY 53  ? B GLY 53  ? 1_555 172.1 ? 
28 O   ? A GLU 70  ? A GLU 70  ? 1_555 K ? F K . ? A K 502 ? 1_555 O   ? B ASN 271 ? B ASN 271 ? 1_555 162.2 ? 
29 OE1 ? A GLU 70  ? A GLU 70  ? 1_555 K ? F K . ? A K 502 ? 1_555 O   ? B ASN 271 ? B ASN 271 ? 1_555 94.9  ? 
30 O   ? Q HOH .   ? A HOH 743 ? 1_555 K ? F K . ? A K 502 ? 1_555 O   ? B ASN 271 ? B ASN 271 ? 1_555 109.3 ? 
31 O   ? B GLY 53  ? B GLY 53  ? 1_555 K ? F K . ? A K 502 ? 1_555 O   ? B ASN 271 ? B ASN 271 ? 1_555 77.5  ? 
32 O   ? A GLU 70  ? A GLU 70  ? 1_555 K ? F K . ? A K 502 ? 1_555 O   ? R HOH .   ? B HOH 700 ? 1_555 59.8  ? 
33 OE1 ? A GLU 70  ? A GLU 70  ? 1_555 K ? F K . ? A K 502 ? 1_555 O   ? R HOH .   ? B HOH 700 ? 1_555 147.2 ? 
34 O   ? Q HOH .   ? A HOH 743 ? 1_555 K ? F K . ? A K 502 ? 1_555 O   ? R HOH .   ? B HOH 700 ? 1_555 92.5  ? 
35 O   ? B GLY 53  ? B GLY 53  ? 1_555 K ? F K . ? A K 502 ? 1_555 O   ? R HOH .   ? B HOH 700 ? 1_555 80.7  ? 
36 O   ? B ASN 271 ? B ASN 271 ? 1_555 K ? F K . ? A K 502 ? 1_555 O   ? R HOH .   ? B HOH 700 ? 1_555 115.2 ? 
37 O   ? A GLU 70  ? A GLU 70  ? 1_555 K ? F K . ? A K 502 ? 1_555 O   ? R HOH .   ? B HOH 742 ? 1_555 97.0  ? 
38 OE1 ? A GLU 70  ? A GLU 70  ? 1_555 K ? F K . ? A K 502 ? 1_555 O   ? R HOH .   ? B HOH 742 ? 1_555 148.2 ? 
39 O   ? Q HOH .   ? A HOH 743 ? 1_555 K ? F K . ? A K 502 ? 1_555 O   ? R HOH .   ? B HOH 742 ? 1_555 59.8  ? 
40 O   ? B GLY 53  ? B GLY 53  ? 1_555 K ? F K . ? A K 502 ? 1_555 O   ? R HOH .   ? B HOH 742 ? 1_555 117.2 ? 
41 O   ? B ASN 271 ? B ASN 271 ? 1_555 K ? F K . ? A K 502 ? 1_555 O   ? R HOH .   ? B HOH 742 ? 1_555 90.1  ? 
42 O   ? R HOH .   ? B HOH 700 ? 1_555 K ? F K . ? A K 502 ? 1_555 O   ? R HOH .   ? B HOH 742 ? 1_555 49.8  ? 
43 O   ? C GLY 53  ? C GLY 53  ? 1_555 K ? M K . ? C K 502 ? 1_555 O   ? C ASN 271 ? C ASN 271 ? 1_555 80.2  ? 
44 O   ? C GLY 53  ? C GLY 53  ? 1_555 K ? M K . ? C K 502 ? 1_555 O   ? S HOH .   ? C HOH 702 ? 1_555 116.1 ? 
45 O   ? C ASN 271 ? C ASN 271 ? 1_555 K ? M K . ? C K 502 ? 1_555 O   ? S HOH .   ? C HOH 702 ? 1_555 87.7  ? 
46 O   ? C GLY 53  ? C GLY 53  ? 1_555 K ? M K . ? C K 502 ? 1_555 O   ? D GLU 70  ? D GLU 70  ? 1_555 81.0  ? 
47 O   ? C ASN 271 ? C ASN 271 ? 1_555 K ? M K . ? C K 502 ? 1_555 O   ? D GLU 70  ? D GLU 70  ? 1_555 161.2 ? 
48 O   ? S HOH .   ? C HOH 702 ? 1_555 K ? M K . ? C K 502 ? 1_555 O   ? D GLU 70  ? D GLU 70  ? 1_555 100.8 ? 
49 O   ? C GLY 53  ? C GLY 53  ? 1_555 K ? M K . ? C K 502 ? 1_555 OE1 ? D GLU 70  ? D GLU 70  ? 1_555 92.8  ? 
50 O   ? C ASN 271 ? C ASN 271 ? 1_555 K ? M K . ? C K 502 ? 1_555 OE1 ? D GLU 70  ? D GLU 70  ? 1_555 93.1  ? 
51 O   ? S HOH .   ? C HOH 702 ? 1_555 K ? M K . ? C K 502 ? 1_555 OE1 ? D GLU 70  ? D GLU 70  ? 1_555 150.7 ? 
52 O   ? D GLU 70  ? D GLU 70  ? 1_555 K ? M K . ? C K 502 ? 1_555 OE1 ? D GLU 70  ? D GLU 70  ? 1_555 87.7  ? 
53 O   ? C GLY 53  ? C GLY 53  ? 1_555 K ? M K . ? C K 502 ? 1_555 O   ? T HOH .   ? D HOH 696 ? 1_555 174.1 ? 
54 O   ? C ASN 271 ? C ASN 271 ? 1_555 K ? M K . ? C K 502 ? 1_555 O   ? T HOH .   ? D HOH 696 ? 1_555 105.2 ? 
55 O   ? S HOH .   ? C HOH 702 ? 1_555 K ? M K . ? C K 502 ? 1_555 O   ? T HOH .   ? D HOH 696 ? 1_555 62.3  ? 
56 O   ? D GLU 70  ? D GLU 70  ? 1_555 K ? M K . ? C K 502 ? 1_555 O   ? T HOH .   ? D HOH 696 ? 1_555 93.6  ? 
57 OE1 ? D GLU 70  ? D GLU 70  ? 1_555 K ? M K . ? C K 502 ? 1_555 O   ? T HOH .   ? D HOH 696 ? 1_555 89.4  ? 
58 O   ? C GLY 53  ? C GLY 53  ? 1_555 K ? M K . ? C K 502 ? 1_555 O   ? T HOH .   ? D HOH 723 ? 1_555 83.1  ? 
59 O   ? C ASN 271 ? C ASN 271 ? 1_555 K ? M K . ? C K 502 ? 1_555 O   ? T HOH .   ? D HOH 723 ? 1_555 120.9 ? 
60 O   ? S HOH .   ? C HOH 702 ? 1_555 K ? M K . ? C K 502 ? 1_555 O   ? T HOH .   ? D HOH 723 ? 1_555 51.3  ? 
61 O   ? D GLU 70  ? D GLU 70  ? 1_555 K ? M K . ? C K 502 ? 1_555 O   ? T HOH .   ? D HOH 723 ? 1_555 56.6  ? 
62 OE1 ? D GLU 70  ? D GLU 70  ? 1_555 K ? M K . ? C K 502 ? 1_555 O   ? T HOH .   ? D HOH 723 ? 1_555 144.2 ? 
63 O   ? T HOH .   ? D HOH 696 ? 1_555 K ? M K . ? C K 502 ? 1_555 O   ? T HOH .   ? D HOH 723 ? 1_555 91.9  ? 
64 O   ? C GLU 70  ? C GLU 70  ? 1_555 K ? L K . ? C K 501 ? 1_555 OE1 ? C GLU 70  ? C GLU 70  ? 1_555 86.4  ? 
65 O   ? C GLU 70  ? C GLU 70  ? 1_555 K ? L K . ? C K 501 ? 1_555 O   ? S HOH .   ? C HOH 680 ? 1_555 93.5  ? 
66 OE1 ? C GLU 70  ? C GLU 70  ? 1_555 K ? L K . ? C K 501 ? 1_555 O   ? S HOH .   ? C HOH 680 ? 1_555 89.7  ? 
67 O   ? C GLU 70  ? C GLU 70  ? 1_555 K ? L K . ? C K 501 ? 1_555 O   ? S HOH .   ? C HOH 741 ? 1_555 58.5  ? 
68 OE1 ? C GLU 70  ? C GLU 70  ? 1_555 K ? L K . ? C K 501 ? 1_555 O   ? S HOH .   ? C HOH 741 ? 1_555 144.9 ? 
69 O   ? S HOH .   ? C HOH 680 ? 1_555 K ? L K . ? C K 501 ? 1_555 O   ? S HOH .   ? C HOH 741 ? 1_555 90.0  ? 
70 O   ? C GLU 70  ? C GLU 70  ? 1_555 K ? L K . ? C K 501 ? 1_555 O   ? D GLY 53  ? D GLY 53  ? 1_555 80.7  ? 
71 OE1 ? C GLU 70  ? C GLU 70  ? 1_555 K ? L K . ? C K 501 ? 1_555 O   ? D GLY 53  ? D GLY 53  ? 1_555 97.9  ? 
72 O   ? S HOH .   ? C HOH 680 ? 1_555 K ? L K . ? C K 501 ? 1_555 O   ? D GLY 53  ? D GLY 53  ? 1_555 170.1 ? 
73 O   ? S HOH .   ? C HOH 741 ? 1_555 K ? L K . ? C K 501 ? 1_555 O   ? D GLY 53  ? D GLY 53  ? 1_555 80.2  ? 
74 O   ? C GLU 70  ? C GLU 70  ? 1_555 K ? L K . ? C K 501 ? 1_555 O   ? D ASN 271 ? D ASN 271 ? 1_555 163.1 ? 
75 OE1 ? C GLU 70  ? C GLU 70  ? 1_555 K ? L K . ? C K 501 ? 1_555 O   ? D ASN 271 ? D ASN 271 ? 1_555 93.4  ? 
76 O   ? S HOH .   ? C HOH 680 ? 1_555 K ? L K . ? C K 501 ? 1_555 O   ? D ASN 271 ? D ASN 271 ? 1_555 103.4 ? 
77 O   ? S HOH .   ? C HOH 741 ? 1_555 K ? L K . ? C K 501 ? 1_555 O   ? D ASN 271 ? D ASN 271 ? 1_555 120.7 ? 
78 O   ? D GLY 53  ? D GLY 53  ? 1_555 K ? L K . ? C K 501 ? 1_555 O   ? D ASN 271 ? D ASN 271 ? 1_555 82.5  ? 
79 O   ? C GLU 70  ? C GLU 70  ? 1_555 K ? L K . ? C K 501 ? 1_555 O   ? T HOH .   ? D HOH 711 ? 1_555 100.1 ? 
80 OE1 ? C GLU 70  ? C GLU 70  ? 1_555 K ? L K . ? C K 501 ? 1_555 O   ? T HOH .   ? D HOH 711 ? 1_555 146.4 ? 
81 O   ? S HOH .   ? C HOH 680 ? 1_555 K ? L K . ? C K 501 ? 1_555 O   ? T HOH .   ? D HOH 711 ? 1_555 57.2  ? 
82 O   ? S HOH .   ? C HOH 741 ? 1_555 K ? L K . ? C K 501 ? 1_555 O   ? T HOH .   ? D HOH 711 ? 1_555 50.8  ? 
83 O   ? D GLY 53  ? D GLY 53  ? 1_555 K ? L K . ? C K 501 ? 1_555 O   ? T HOH .   ? D HOH 711 ? 1_555 115.7 ? 
84 O   ? D ASN 271 ? D ASN 271 ? 1_555 K ? L K . ? C K 501 ? 1_555 O   ? T HOH .   ? D HOH 711 ? 1_555 89.4  ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      A1A2Z 
_pdbx_modification_feature.label_asym_id                      N 
_pdbx_modification_feature.label_seq_id                       . 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     LYS 
_pdbx_modification_feature.modified_residue_label_asym_id     C 
_pdbx_modification_feature.modified_residue_label_seq_id      266 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       A1A2Z 
_pdbx_modification_feature.auth_asym_id                       C 
_pdbx_modification_feature.auth_seq_id                        503 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      LYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      C 
_pdbx_modification_feature.modified_residue_auth_seq_id       266 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               C4A 
_pdbx_modification_feature.modified_residue_id_linking_atom   NZ 
_pdbx_modification_feature.modified_residue_id                LYS 
_pdbx_modification_feature.ref_pcm_id                         1 
_pdbx_modification_feature.ref_comp_id                        A1A2Z 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Covalent chemical modification' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 VAL 191 A . ? VAL 191 A THR 192 A ? THR 192 A 1 -14.80 
2 TYR 348 A . ? TYR 348 A PRO 349 A ? PRO 349 A 1 4.31   
3 VAL 191 B . ? VAL 191 B THR 192 B ? THR 192 B 1 -15.45 
4 TYR 348 B . ? TYR 348 B PRO 349 B ? PRO 349 B 1 -0.04  
5 VAL 191 C . ? VAL 191 C THR 192 C ? THR 192 C 1 -16.04 
6 TYR 348 C . ? TYR 348 C PRO 349 C ? PRO 349 C 1 -1.52  
7 VAL 191 D . ? VAL 191 D THR 192 D ? THR 192 D 1 -16.87 
8 TYR 348 D . ? TYR 348 D PRO 349 D ? PRO 349 D 1 -2.04  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 7 ? 
AA3 ? 3 ? 
AA4 ? 2 ? 
AA5 ? 4 ? 
AA6 ? 7 ? 
AA7 ? 3 ? 
AA8 ? 2 ? 
AA9 ? 7 ? 
AB1 ? 3 ? 
AB2 ? 2 ? 
AB3 ? 7 ? 
AB4 ? 3 ? 
AB5 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? anti-parallel 
AA1 3 4 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA2 5 6 ? parallel      
AA2 6 7 ? parallel      
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? anti-parallel 
AA5 3 4 ? parallel      
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? parallel      
AA6 4 5 ? parallel      
AA6 5 6 ? parallel      
AA6 6 7 ? parallel      
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AA9 3 4 ? parallel      
AA9 4 5 ? parallel      
AA9 5 6 ? parallel      
AA9 6 7 ? parallel      
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB3 2 3 ? anti-parallel 
AB3 3 4 ? parallel      
AB3 4 5 ? parallel      
AB3 5 6 ? parallel      
AB3 6 7 ? parallel      
AB4 1 2 ? anti-parallel 
AB4 2 3 ? anti-parallel 
AB5 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 MET A 57  ? SER A 58  ? MET A 57  SER A 58  
AA1 2 PHE C 9   ? LYS C 16  ? PHE C 9   LYS C 16  
AA1 3 PHE A 9   ? LYS A 16  ? PHE A 9   LYS A 16  
AA1 4 MET C 57  ? SER C 58  ? MET C 57  SER C 58  
AA2 1 TYR A 93  ? ALA A 97  ? TYR A 93  ALA A 97  
AA2 2 GLY A 274 ? ILE A 278 ? GLY A 274 ILE A 278 
AA2 3 ALA A 259 ? SER A 263 ? ALA A 259 SER A 263 
AA2 4 VAL A 220 ? ASP A 223 ? VAL A 220 ASP A 223 
AA2 5 ILE A 184 ? THR A 190 ? ILE A 184 THR A 190 
AA2 6 VAL A 125 ? SER A 128 ? VAL A 125 SER A 128 
AA2 7 LYS A 145 ? ASN A 148 ? LYS A 145 ASN A 148 
AA3 1 ALA A 354 ? ASP A 358 ? ALA A 354 ASP A 358 
AA3 2 PHE A 412 ? THR A 416 ? PHE A 412 THR A 416 
AA3 3 VAL A 389 ? ILE A 391 ? VAL A 389 ILE A 391 
AA4 1 LEU A 447 ? TYR A 451 ? LEU A 447 TYR A 451 
AA4 2 ARG A 462 ? PRO A 465 ? ARG A 462 PRO A 465 
AA5 1 MET B 57  ? SER B 58  ? MET B 57  SER B 58  
AA5 2 PHE D 9   ? LYS D 16  ? PHE D 9   LYS D 16  
AA5 3 PHE B 9   ? LYS B 16  ? PHE B 9   LYS B 16  
AA5 4 MET D 57  ? SER D 58  ? MET D 57  SER D 58  
AA6 1 TYR B 93  ? ALA B 97  ? TYR B 93  ALA B 97  
AA6 2 GLY B 274 ? ILE B 278 ? GLY B 274 ILE B 278 
AA6 3 ALA B 259 ? SER B 263 ? ALA B 259 SER B 263 
AA6 4 VAL B 220 ? ASP B 223 ? VAL B 220 ASP B 223 
AA6 5 ILE B 184 ? THR B 190 ? ILE B 184 THR B 190 
AA6 6 VAL B 125 ? SER B 128 ? VAL B 125 SER B 128 
AA6 7 LYS B 145 ? ASN B 148 ? LYS B 145 ASN B 148 
AA7 1 ALA B 354 ? ASP B 358 ? ALA B 354 ASP B 358 
AA7 2 PHE B 412 ? THR B 416 ? PHE B 412 THR B 416 
AA7 3 VAL B 389 ? ILE B 391 ? VAL B 389 ILE B 391 
AA8 1 LEU B 447 ? TYR B 451 ? LEU B 447 TYR B 451 
AA8 2 ARG B 462 ? PRO B 465 ? ARG B 462 PRO B 465 
AA9 1 TYR C 93  ? ALA C 97  ? TYR C 93  ALA C 97  
AA9 2 GLY C 274 ? ILE C 278 ? GLY C 274 ILE C 278 
AA9 3 ALA C 259 ? SER C 263 ? ALA C 259 SER C 263 
AA9 4 PHE C 219 ? ASP C 223 ? PHE C 219 ASP C 223 
AA9 5 ILE C 184 ? THR C 190 ? ILE C 184 THR C 190 
AA9 6 VAL C 125 ? SER C 128 ? VAL C 125 SER C 128 
AA9 7 LYS C 145 ? ASN C 148 ? LYS C 145 ASN C 148 
AB1 1 ALA C 354 ? ASP C 358 ? ALA C 354 ASP C 358 
AB1 2 PHE C 412 ? THR C 416 ? PHE C 412 THR C 416 
AB1 3 VAL C 389 ? ILE C 391 ? VAL C 389 ILE C 391 
AB2 1 LEU C 447 ? TYR C 451 ? LEU C 447 TYR C 451 
AB2 2 ARG C 462 ? PRO C 465 ? ARG C 462 PRO C 465 
AB3 1 TYR D 93  ? ALA D 97  ? TYR D 93  ALA D 97  
AB3 2 GLY D 274 ? ILE D 278 ? GLY D 274 ILE D 278 
AB3 3 ALA D 259 ? SER D 263 ? ALA D 259 SER D 263 
AB3 4 VAL D 220 ? ASP D 223 ? VAL D 220 ASP D 223 
AB3 5 ILE D 184 ? THR D 190 ? ILE D 184 THR D 190 
AB3 6 VAL D 125 ? SER D 128 ? VAL D 125 SER D 128 
AB3 7 LYS D 145 ? ASN D 148 ? LYS D 145 ASN D 148 
AB4 1 ALA D 354 ? VAL D 357 ? ALA D 354 VAL D 357 
AB4 2 PHE D 412 ? THR D 416 ? PHE D 412 THR D 416 
AB4 3 VAL D 389 ? ILE D 391 ? VAL D 389 ILE D 391 
AB5 1 GLU D 448 ? TYR D 451 ? GLU D 448 TYR D 451 
AB5 2 ARG D 462 ? LYS D 464 ? ARG D 462 LYS D 464 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N MET A 57  ? N MET A 57  O VAL C 14  ? O VAL C 14  
AA1 2 3 O GLU C 15  ? O GLU C 15  N ARG A 10  ? N ARG A 10  
AA1 3 4 N VAL A 14  ? N VAL A 14  O MET C 57  ? O MET C 57  
AA2 1 2 N ILE A 95  ? N ILE A 95  O VAL A 276 ? O VAL A 276 
AA2 2 3 O ALA A 277 ? O ALA A 277 N LEU A 260 ? N LEU A 260 
AA2 3 4 O ALA A 259 ? O ALA A 259 N MET A 222 ? N MET A 222 
AA2 4 5 O VAL A 221 ? O VAL A 221 N ILE A 187 ? N ILE A 187 
AA2 5 6 O VAL A 185 ? O VAL A 185 N VAL A 125 ? N VAL A 125 
AA2 6 7 N PHE A 126 ? N PHE A 126 O LYS A 145 ? O LYS A 145 
AA3 1 2 N VAL A 357 ? N VAL A 357 O MET A 413 ? O MET A 413 
AA3 2 3 O ARG A 414 ? O ARG A 414 N VAL A 389 ? N VAL A 389 
AA4 1 2 N GLU A 450 ? N GLU A 450 O ARG A 462 ? O ARG A 462 
AA5 1 2 N MET B 57  ? N MET B 57  O VAL D 14  ? O VAL D 14  
AA5 2 3 O LYS D 12  ? O LYS D 12  N MET B 13  ? N MET B 13  
AA5 3 4 N VAL B 14  ? N VAL B 14  O MET D 57  ? O MET D 57  
AA6 1 2 N ILE B 95  ? N ILE B 95  O VAL B 276 ? O VAL B 276 
AA6 2 3 O ALA B 277 ? O ALA B 277 N LEU B 260 ? N LEU B 260 
AA6 3 4 O ALA B 259 ? O ALA B 259 N MET B 222 ? N MET B 222 
AA6 4 5 O VAL B 221 ? O VAL B 221 N ILE B 187 ? N ILE B 187 
AA6 5 6 O VAL B 188 ? O VAL B 188 N ILE B 127 ? N ILE B 127 
AA6 6 7 N PHE B 126 ? N PHE B 126 O ILE B 147 ? O ILE B 147 
AA7 1 2 N VAL B 355 ? N VAL B 355 O LEU B 415 ? O LEU B 415 
AA7 2 3 O ARG B 414 ? O ARG B 414 N VAL B 389 ? N VAL B 389 
AA8 1 2 N GLU B 448 ? N GLU B 448 O LYS B 464 ? O LYS B 464 
AA9 1 2 N ILE C 95  ? N ILE C 95  O VAL C 276 ? O VAL C 276 
AA9 2 3 O ALA C 277 ? O ALA C 277 N LEU C 260 ? N LEU C 260 
AA9 3 4 O ALA C 259 ? O ALA C 259 N MET C 222 ? N MET C 222 
AA9 4 5 O VAL C 221 ? O VAL C 221 N ILE C 187 ? N ILE C 187 
AA9 5 6 O VAL C 188 ? O VAL C 188 N ILE C 127 ? N ILE C 127 
AA9 6 7 N PHE C 126 ? N PHE C 126 O LYS C 145 ? O LYS C 145 
AB1 1 2 N VAL C 355 ? N VAL C 355 O LEU C 415 ? O LEU C 415 
AB1 2 3 O PHE C 412 ? O PHE C 412 N ILE C 391 ? N ILE C 391 
AB2 1 2 N GLU C 450 ? N GLU C 450 O ARG C 462 ? O ARG C 462 
AB3 1 2 N ILE D 95  ? N ILE D 95  O VAL D 276 ? O VAL D 276 
AB3 2 3 O ALA D 277 ? O ALA D 277 N LEU D 260 ? N LEU D 260 
AB3 3 4 O ALA D 259 ? O ALA D 259 N MET D 222 ? N MET D 222 
AB3 4 5 O VAL D 221 ? O VAL D 221 N SER D 189 ? N SER D 189 
AB3 5 6 O VAL D 185 ? O VAL D 185 N VAL D 125 ? N VAL D 125 
AB3 6 7 N SER D 128 ? N SER D 128 O ILE D 147 ? O ILE D 147 
AB4 1 2 N VAL D 355 ? N VAL D 355 O LEU D 415 ? O LEU D 415 
AB4 2 3 O ARG D 414 ? O ARG D 414 N VAL D 389 ? N VAL D 389 
AB5 1 2 N GLU D 448 ? N GLU D 448 O LYS D 464 ? O LYS D 464 
# 
_pdbx_entry_details.entry_id                   9BLV 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
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 PRO A 8   ? ? -86.54  35.72   
2  1 TYR A 45  ? ? -88.25  -83.05  
3  1 GLN A 99  ? ? -168.89 -167.31 
4  1 LYS A 120 ? ? -110.02 -168.28 
5  1 PHE A 130 ? ? -167.76 111.31  
6  1 LYS A 266 ? ? -109.11 -106.43 
7  1 ASP A 280 ? ? -152.83 4.35    
8  1 TYR A 301 ? ? -140.34 -26.87  
9  1 PHE A 371 ? ? 57.42   79.02   
10 1 SER A 384 ? ? -144.29 -12.72  
11 1 PRO B 8   ? ? -89.81  44.24   
12 1 TYR B 45  ? ? -88.50  -85.44  
13 1 GLN B 99  ? ? -173.45 -171.74 
14 1 PHE B 130 ? ? -164.11 114.01  
15 1 LYS B 266 ? ? -107.42 -106.40 
16 1 ASP B 280 ? ? -145.53 -7.36   
17 1 PHE B 371 ? ? 55.86   77.85   
18 1 SER B 384 ? ? -141.42 -11.50  
19 1 ILE B 391 ? ? -118.14 76.00   
20 1 GLU B 411 ? ? -157.33 75.21   
21 1 PRO C 8   ? ? -86.34  39.22   
22 1 TYR C 45  ? ? -96.70  -75.13  
23 1 LYS C 266 ? ? -104.04 -105.27 
24 1 PRO C 268 ? ? -69.38  6.66    
25 1 ASP C 280 ? ? -151.83 -4.39   
26 1 HIS C 353 ? ? -141.93 -6.20   
27 1 PHE C 371 ? ? 63.53   70.50   
28 1 PRO D 8   ? ? -83.92  40.20   
29 1 TYR D 45  ? ? -80.32  -85.53  
30 1 GLN D 99  ? ? -167.98 -168.90 
31 1 GLU D 118 ? ? 59.99   12.91   
32 1 PHE D 130 ? ? -161.96 117.35  
33 1 LYS D 266 ? ? -107.65 -107.62 
34 1 ASP D 280 ? ? -152.61 12.80   
35 1 TYR D 301 ? ? -142.91 -28.74  
36 1 PRO D 367 ? ? -77.27  -161.39 
37 1 PHE D 371 ? ? 63.84   72.35   
38 1 SER D 384 ? ? -141.38 -22.34  
39 1 GLU D 411 ? ? -109.89 61.08   
# 
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 -26.2697 -9.7960  50.9901 0.0951 ? -0.0254 ? 0.0029  ? 0.2097 ? 0.0851  ? 0.1284 ? 1.1463 ? 
0.0696  ? -0.0869 ? 0.3456 ? 0.1176  ? 0.9547 ? -0.0335 ? 0.1291  ? 0.1288  ? -0.0323 ? 0.0608  ? 0.1144  ? 0.0127  ? -0.3146 ? 
-0.0052 ? 
2  'X-RAY DIFFRACTION' ? refined -34.7426 5.0389   62.7588 0.0804 ? 0.0354  ? 0.0291  ? 0.4292 ? 0.1000  ? 0.2744 ? 0.7808 ? 
-0.1167 ? -0.1190 ? 0.8963 ? 0.0028  ? 0.1703 ? -0.1207 ? 0.1651  ? 0.2785  ? -0.0231 ? 0.2484  ? 0.2257  ? 0.0386  ? -0.3697 ? 
-0.0013 ? 
3  'X-RAY DIFFRACTION' ? refined -37.8895 15.0362  53.7085 0.2487 ? 0.0981  ? 0.0129  ? 0.7549 ? 0.3339  ? 0.6412 ? 1.1000 ? 
-0.3962 ? 0.8676  ? 0.4845 ? -0.2081 ? 0.7912 ? -0.2025 ? 0.1929  ? 0.6853  ? 0.0240  ? 0.1810  ? 0.1424  ? -0.2431 ? -0.3913 ? 
-0.0448 ? 
4  'X-RAY DIFFRACTION' ? refined -1.7420  -0.5685  39.0868 0.1185 ? -0.0081 ? -0.0219 ? 0.1015 ? 0.0924  ? 0.1097 ? 0.7836 ? 
0.1502  ? -0.3030 ? 0.5677 ? -0.4278 ? 1.6123 ? -0.0652 ? 0.0746  ? 0.1148  ? -0.0984 ? 0.0496  ? 0.0373  ? 0.0938  ? -0.0090 ? 
0.0517  ? 
5  'X-RAY DIFFRACTION' ? refined -21.9724 6.8972   23.5924 0.2038 ? -0.0013 ? -0.0568 ? 0.5766 ? 0.2173  ? 0.2727 ? 1.0996 ? 
0.0227  ? 1.0478  ? 0.9572 ? -0.0055 ? 2.8024 ? -0.0544 ? 0.1942  ? 0.1793  ? -0.1738 ? 0.1343  ? 0.2472  ? -0.2161 ? -0.1877 ? 
0.1948  ? 
6  'X-RAY DIFFRACTION' ? refined -7.5294  12.3277  26.4126 0.2114 ? 0.0148  ? -0.0705 ? 0.3582 ? 0.3816  ? 0.1549 ? 0.1671 ? 
0.1441  ? -0.1500 ? 0.1634 ? -0.1042 ? 0.2956 ? -0.0408 ? 0.4574  ? 0.3338  ? -0.1714 ? 0.2263  ? 0.2237  ? -0.2242 ? -0.3623 ? 
0.2787  ? 
7  'X-RAY DIFFRACTION' ? refined 2.3531   -9.1290  17.5886 0.3246 ? -0.1828 ? 0.0327  ? 0.4558 ? 0.0590  ? 0.0499 ? 0.6732 ? 
-0.0294 ? -0.6267 ? 0.7604 ? -0.8571 ? 1.6091 ? -0.2490 ? 0.5071  ? -0.1055 ? -0.5134 ? 0.3148  ? 0.1678  ? 0.4999  ? -0.5163 ? 
0.4151  ? 
8  'X-RAY DIFFRACTION' ? refined -1.0753  -11.9004 20.2398 0.3222 ? -0.1356 ? -0.0918 ? 0.6355 ? 0.0600  ? 0.1144 ? 0.7058 ? 
0.2570  ? 0.7198  ? 0.6650 ? 0.2022  ? 1.1468 ? -0.0289 ? 0.4566  ? -0.0793 ? -0.3234 ? 0.0115  ? 0.2606  ? 0.4878  ? -0.4557 ? 
-0.3431 ? 
9  'X-RAY DIFFRACTION' ? refined 1.7241   -0.3848  71.5407 0.1541 ? 0.0809  ? 0.0282  ? 0.2471 ? 0.0387  ? 0.1712 ? 1.1754 ? 
-0.0531 ? -0.0189 ? 0.2668 ? 0.1827  ? 0.9927 ? -0.2668 ? -0.3127 ? -0.0629 ? 0.1063  ? 0.0465  ? 0.0534  ? 0.0979  ? -0.1918 ? 
0.0991  ? 
10 'X-RAY DIFFRACTION' ? refined 21.9861  7.1726   87.2989 0.2026 ? 0.0847  ? -0.0294 ? 0.2283 ? -0.1049 ? 0.1286 ? 0.2611 ? 
-0.5205 ? 0.5559  ? 1.4321 ? -0.0886 ? 3.8639 ? -0.0893 ? -0.3432 ? 0.1765  ? 0.2390  ? 0.1354  ? -0.1701 ? -0.1358 ? 0.2954  ? 
-0.0642 ? 
11 'X-RAY DIFFRACTION' ? refined 6.3983   11.5802  85.1458 0.1316 ? 0.1148  ? -0.0151 ? 0.4269 ? -0.1603 ? 0.1279 ? 0.3207 ? 
-0.2137 ? -0.0483 ? 0.1554 ? 0.0592  ? 0.2758 ? -0.1028 ? -0.4150 ? 0.3086  ? 0.1469  ? 0.0723  ? 0.0987  ? -0.1542 ? -0.3579 ? 
-0.0363 ? 
12 'X-RAY DIFFRACTION' ? refined 0.9242   -12.8695 94.6269 0.4822 ? 0.2540  ? 0.1059  ? 1.0114 ? 0.0874  ? 0.2856 ? 0.3868 ? 
0.4676  ? -0.4233 ? 0.8681 ? -0.3184 ? 0.5985 ? -0.1359 ? -0.6176 ? -0.0490 ? 0.5038  ? 0.1829  ? -0.0264 ? 0.2888  ? 0.5843  ? 
0.0443  ? 
13 'X-RAY DIFFRACTION' ? refined -9.5120  -5.5402  83.4641 0.1734 ? 0.0986  ? 0.0650  ? 0.5769 ? 0.0339  ? 0.1970 ? 1.7197 ? 
-0.0686 ? -0.6087 ? 0.5768 ? 0.3729  ? 0.4260 ? -0.1946 ? -0.5310 ? -0.3674 ? 0.2049  ? 0.0720  ? 0.0416  ? 0.1586  ? 0.1064  ? 
0.3326  ? 
14 'X-RAY DIFFRACTION' ? refined 5.3026   -19.7232 92.2242 0.6237 ? 0.0323  ? 0.0791  ? 0.7120 ? 0.2932  ? 0.5480 ? 1.8656 ? 
-0.2641 ? -1.2252 ? 1.1251 ? 1.3947  ? 2.1785 ? 0.0400  ? -0.6724 ? -0.8536 ? 0.8255  ? 0.0630  ? 0.3114  ? 0.4185  ? 0.0463  ? 
0.0360  ? 
15 'X-RAY DIFFRACTION' ? refined 16.6003  4.8919   51.0833 0.2039 ? -0.0857 ? 0.0221  ? 0.3462 ? -0.0129 ? 0.1653 ? 1.0203 ? 
0.0367  ? -0.4038 ? 0.3187 ? 0.0407  ? 1.3250 ? 0.1854  ? 0.0605  ? 0.3817  ? -0.0633 ? 0.1087  ? -0.0380 ? -0.3434 ? 0.3692  ? 
-0.1413 ? 
16 'X-RAY DIFFRACTION' ? refined 26.7487  -11.8983 71.0069 0.1302 ? 0.0011  ? -0.0511 ? 0.0674 ? -0.0060 ? 0.0759 ? 2.4554 ? 
0.3067  ? -0.1100 ? 0.9106 ? 0.2072  ? 0.6978 ? 0.1026  ? -0.0660 ? 0.0220  ? 0.0353  ? -0.0496 ? -0.0073 ? 0.0520  ? 0.0679  ? 
-0.0695 ? 
17 'X-RAY DIFFRACTION' ? refined 30.2687  -14.7302 61.8478 0.0577 ? 0.0240  ? -0.0627 ? 0.1698 ? -0.0870 ? 0.1062 ? 0.7650 ? 
-0.1667 ? 0.2964  ? 0.5209 ? 0.0748  ? 0.7079 ? 0.0849  ? 0.3490  ? -0.1498 ? 0.0019  ? 0.0213  ? -0.0442 ? 0.0880  ? 0.0904  ? 
-0.0466 ? 
18 'X-RAY DIFFRACTION' ? refined 33.1255  -1.5818  42.9259 0.1543 ? -0.0730 ? 0.0566  ? 0.6831 ? -0.0285 ? 0.1099 ? 0.6722 ? 
-0.1841 ? -0.6877 ? 0.1847 ? -0.0882 ? 1.2784 ? 0.0541  ? -0.0452 ? 0.1601  ? -0.0345 ? 0.0598  ? -0.1764 ? -0.2542 ? 0.5777  ? 
-0.2268 ? 
19 'X-RAY DIFFRACTION' ? refined 34.1787  11.1129  50.9916 0.2501 ? -0.2214 ? 0.0181  ? 0.8547 ? -0.1563 ? 0.3402 ? 1.4574 ? 
0.1227  ? 0.4958  ? 1.1112 ? 0.7618  ? 0.6350 ? 0.0952  ? -0.2379 ? 0.4970  ? 0.1046  ? 0.2850  ? -0.4383 ? -0.3639 ? 0.7553  ? 
0.6726  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1  'X-RAY DIFFRACTION' 1  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 2 through 341 )
;
2  'X-RAY DIFFRACTION' 2  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 342 through 437 )
;
3  'X-RAY DIFFRACTION' 3  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 438 through 466 )
;
4  'X-RAY DIFFRACTION' 4  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 2 through 99 )
;
5  'X-RAY DIFFRACTION' 5  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 100 through 141 )
;
6  'X-RAY DIFFRACTION' 6  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 142 through 341 )
;
7  'X-RAY DIFFRACTION' 7  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 342 through 396 )
;
8  'X-RAY DIFFRACTION' 8  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 397 through 466 )
;
9  'X-RAY DIFFRACTION' 9  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 2 through 99 )
;
10 'X-RAY DIFFRACTION' 10 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 100 through 141 )
;
11 'X-RAY DIFFRACTION' 11 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 142 through 358 )
;
12 'X-RAY DIFFRACTION' 12 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 359 through 411 )
;
13 'X-RAY DIFFRACTION' 13 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 412 through 438 )
;
14 'X-RAY DIFFRACTION' 14 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 439 through 466 )
;
15 'X-RAY DIFFRACTION' 15 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 2 through 75 )
;
16 'X-RAY DIFFRACTION' 16 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 76 through 141 )
;
17 'X-RAY DIFFRACTION' 17 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 142 through 321 )
;
18 'X-RAY DIFFRACTION' 18 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 322 through 367 )
;
19 'X-RAY DIFFRACTION' 19 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 368 through 465 )
;
# 
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 MET 1   ? A MET 1   
2  1 Y 1 A ARG 398 ? A ARG 398 
3  1 Y 1 A ASP 399 ? A ASP 399 
4  1 Y 1 A PRO 400 ? A PRO 400 
5  1 Y 1 A ALA 401 ? A ALA 401 
6  1 Y 1 A THR 402 ? A THR 402 
7  1 Y 1 A GLY 403 ? A GLY 403 
8  1 Y 1 A GLU 404 ? A GLU 404 
9  1 Y 1 A GLU 467 ? A GLU 467 
10 1 Y 1 B MET 1   ? B MET 1   
11 1 Y 1 B GLU 467 ? B GLU 467 
12 1 Y 1 C MET 1   ? C MET 1   
13 1 Y 1 C ASP 399 ? C ASP 399 
14 1 Y 1 C PRO 400 ? C PRO 400 
15 1 Y 1 C ALA 401 ? C ALA 401 
16 1 Y 1 C THR 402 ? C THR 402 
17 1 Y 1 C GLY 403 ? C GLY 403 
18 1 Y 1 C GLU 404 ? C GLU 404 
19 1 Y 1 C GLN 405 ? C GLN 405 
20 1 Y 1 C GLU 467 ? C GLU 467 
21 1 Y 1 D MET 1   ? D MET 1   
22 1 Y 1 D ASP 399 ? D ASP 399 
23 1 Y 1 D PRO 400 ? D PRO 400 
24 1 Y 1 D ALA 401 ? D ALA 401 
25 1 Y 1 D THR 402 ? D THR 402 
26 1 Y 1 D GLY 403 ? D GLY 403 
27 1 Y 1 D GLU 404 ? D GLU 404 
28 1 Y 1 D ILE 466 ? D ILE 466 
29 1 Y 1 D GLU 467 ? D GLU 467 
# 
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 
0JO   O    O N N 1   
0JO   C    C N N 2   
0JO   OXT  O N N 3   
0JO   CA   C N N 4   
0JO   CB   C N N 5   
0JO   N    N N N 6   
0JO   C4A  C N N 7   
0JO   C4   C Y N 8   
0JO   C3   C Y N 9   
0JO   O3   O N N 10  
0JO   C2   C Y N 11  
0JO   C2A  C N N 12  
0JO   N1   N Y N 13  
0JO   C6   C Y N 14  
0JO   C5   C Y N 15  
0JO   C5A  C N N 16  
0JO   OP4  O N N 17  
0JO   P    P N N 18  
0JO   OP3  O N N 19  
0JO   OP1  O N N 20  
0JO   OP2  O N N 21  
0JO   H1   H N N 22  
0JO   H2   H N N 23  
0JO   H3   H N N 24  
0JO   H4   H N N 25  
0JO   H5   H N N 26  
0JO   H6   H N N 27  
0JO   H7   H N N 28  
0JO   H8   H N N 29  
0JO   H9   H N N 30  
0JO   H10  H N N 31  
0JO   H11  H N N 32  
0JO   H12  H N N 33  
0JO   H13  H N N 34  
A1A2Z N    N N N 35  
A1A2Z N1   N Y N 36  
A1A2Z CG   C Y N 37  
A1A2Z CD1  C Y N 38  
A1A2Z CD2  C Y N 39  
A1A2Z CE2  C Y N 40  
A1A2Z CE3  C Y N 41  
A1A2Z CZ3  C Y N 42  
A1A2Z C2A  C N N 43  
A1A2Z C4   C Y N 44  
A1A2Z C5   C Y N 45  
A1A2Z CA   C N S 46  
A1A2Z CH2  C Y N 47  
A1A2Z C2   C Y N 48  
A1A2Z C3   C Y N 49  
A1A2Z C4A  C N N 50  
A1A2Z C5A  C N N 51  
A1A2Z C6   C Y N 52  
A1A2Z C    C N N 53  
A1A2Z CB   C N N 54  
A1A2Z CZ2  C Y N 55  
A1A2Z NE1  N Y N 56  
A1A2Z O    O N N 57  
A1A2Z OXT  O N N 58  
A1A2Z O3P  O N N 59  
A1A2Z O1P  O N N 60  
A1A2Z O3   O N N 61  
A1A2Z O2P  O N N 62  
A1A2Z O4P  O N N 63  
A1A2Z P    P N N 64  
A1A2Z H    H N N 65  
A1A2Z HD1  H N N 66  
A1A2Z HE3  H N N 67  
A1A2Z HZ3  H N N 68  
A1A2Z H2A1 H N N 69  
A1A2Z H2A2 H N N 70  
A1A2Z H2A3 H N N 71  
A1A2Z HA   H N N 72  
A1A2Z HH2  H N N 73  
A1A2Z H4A  H N N 74  
A1A2Z H4B  H N N 75  
A1A2Z H5A1 H N N 76  
A1A2Z H5A2 H N N 77  
A1A2Z H6   H N N 78  
A1A2Z HB2  H N N 79  
A1A2Z HB3  H N N 80  
A1A2Z HZ2  H N N 81  
A1A2Z HE1  H N N 82  
A1A2Z HXT  H N N 83  
A1A2Z HOP3 H N N 84  
A1A2Z HO3  H N N 85  
A1A2Z HOP2 H N N 86  
ALA   N    N N N 87  
ALA   CA   C N S 88  
ALA   C    C N N 89  
ALA   O    O N N 90  
ALA   CB   C N N 91  
ALA   OXT  O N N 92  
ALA   H    H N N 93  
ALA   H2   H N N 94  
ALA   HA   H N N 95  
ALA   HB1  H N N 96  
ALA   HB2  H N N 97  
ALA   HB3  H N N 98  
ALA   HXT  H N N 99  
ARG   N    N N N 100 
ARG   CA   C N S 101 
ARG   C    C N N 102 
ARG   O    O N N 103 
ARG   CB   C N N 104 
ARG   CG   C N N 105 
ARG   CD   C N N 106 
ARG   NE   N N N 107 
ARG   CZ   C N N 108 
ARG   NH1  N N N 109 
ARG   NH2  N N N 110 
ARG   OXT  O N N 111 
ARG   H    H N N 112 
ARG   H2   H N N 113 
ARG   HA   H N N 114 
ARG   HB2  H N N 115 
ARG   HB3  H N N 116 
ARG   HG2  H N N 117 
ARG   HG3  H N N 118 
ARG   HD2  H N N 119 
ARG   HD3  H N N 120 
ARG   HE   H N N 121 
ARG   HH11 H N N 122 
ARG   HH12 H N N 123 
ARG   HH21 H N N 124 
ARG   HH22 H N N 125 
ARG   HXT  H N N 126 
ASN   N    N N N 127 
ASN   CA   C N S 128 
ASN   C    C N N 129 
ASN   O    O N N 130 
ASN   CB   C N N 131 
ASN   CG   C N N 132 
ASN   OD1  O N N 133 
ASN   ND2  N N N 134 
ASN   OXT  O N N 135 
ASN   H    H N N 136 
ASN   H2   H N N 137 
ASN   HA   H N N 138 
ASN   HB2  H N N 139 
ASN   HB3  H N N 140 
ASN   HD21 H N N 141 
ASN   HD22 H N N 142 
ASN   HXT  H N N 143 
ASP   N    N N N 144 
ASP   CA   C N S 145 
ASP   C    C N N 146 
ASP   O    O N N 147 
ASP   CB   C N N 148 
ASP   CG   C N N 149 
ASP   OD1  O N N 150 
ASP   OD2  O N N 151 
ASP   OXT  O N N 152 
ASP   H    H N N 153 
ASP   H2   H N N 154 
ASP   HA   H N N 155 
ASP   HB2  H N N 156 
ASP   HB3  H N N 157 
ASP   HD2  H N N 158 
ASP   HXT  H N N 159 
BZI   N1   N Y N 160 
BZI   C2   C Y N 161 
BZI   N3   N Y N 162 
BZI   C3A  C Y N 163 
BZI   C4   C Y N 164 
BZI   C5   C Y N 165 
BZI   C6   C Y N 166 
BZI   C7   C Y N 167 
BZI   C7A  C Y N 168 
BZI   HN1  H N N 169 
BZI   H2   H N N 170 
BZI   H4   H N N 171 
BZI   H5   H N N 172 
BZI   H6   H N N 173 
BZI   H7   H N N 174 
CYS   N    N N N 175 
CYS   CA   C N R 176 
CYS   C    C N N 177 
CYS   O    O N N 178 
CYS   CB   C N N 179 
CYS   SG   S N N 180 
CYS   OXT  O N N 181 
CYS   H    H N N 182 
CYS   H2   H N N 183 
CYS   HA   H N N 184 
CYS   HB2  H N N 185 
CYS   HB3  H N N 186 
CYS   HG   H N N 187 
CYS   HXT  H N N 188 
DMS   S    S N N 189 
DMS   O    O N N 190 
DMS   C1   C N N 191 
DMS   C2   C N N 192 
DMS   H11  H N N 193 
DMS   H12  H N N 194 
DMS   H13  H N N 195 
DMS   H21  H N N 196 
DMS   H22  H N N 197 
DMS   H23  H N N 198 
GLN   N    N N N 199 
GLN   CA   C N S 200 
GLN   C    C N N 201 
GLN   O    O N N 202 
GLN   CB   C N N 203 
GLN   CG   C N N 204 
GLN   CD   C N N 205 
GLN   OE1  O N N 206 
GLN   NE2  N N N 207 
GLN   OXT  O N N 208 
GLN   H    H N N 209 
GLN   H2   H N N 210 
GLN   HA   H N N 211 
GLN   HB2  H N N 212 
GLN   HB3  H N N 213 
GLN   HG2  H N N 214 
GLN   HG3  H N N 215 
GLN   HE21 H N N 216 
GLN   HE22 H N N 217 
GLN   HXT  H N N 218 
GLU   N    N N N 219 
GLU   CA   C N S 220 
GLU   C    C N N 221 
GLU   O    O N N 222 
GLU   CB   C N N 223 
GLU   CG   C N N 224 
GLU   CD   C N N 225 
GLU   OE1  O N N 226 
GLU   OE2  O N N 227 
GLU   OXT  O N N 228 
GLU   H    H N N 229 
GLU   H2   H N N 230 
GLU   HA   H N N 231 
GLU   HB2  H N N 232 
GLU   HB3  H N N 233 
GLU   HG2  H N N 234 
GLU   HG3  H N N 235 
GLU   HE2  H N N 236 
GLU   HXT  H N N 237 
GLY   N    N N N 238 
GLY   CA   C N N 239 
GLY   C    C N N 240 
GLY   O    O N N 241 
GLY   OXT  O N N 242 
GLY   H    H N N 243 
GLY   H2   H N N 244 
GLY   HA2  H N N 245 
GLY   HA3  H N N 246 
GLY   HXT  H N N 247 
HIS   N    N N N 248 
HIS   CA   C N S 249 
HIS   C    C N N 250 
HIS   O    O N N 251 
HIS   CB   C N N 252 
HIS   CG   C Y N 253 
HIS   ND1  N Y N 254 
HIS   CD2  C Y N 255 
HIS   CE1  C Y N 256 
HIS   NE2  N Y N 257 
HIS   OXT  O N N 258 
HIS   H    H N N 259 
HIS   H2   H N N 260 
HIS   HA   H N N 261 
HIS   HB2  H N N 262 
HIS   HB3  H N N 263 
HIS   HD1  H N N 264 
HIS   HD2  H N N 265 
HIS   HE1  H N N 266 
HIS   HE2  H N N 267 
HIS   HXT  H N N 268 
HOH   O    O N N 269 
HOH   H1   H N N 270 
HOH   H2   H N N 271 
ILE   N    N N N 272 
ILE   CA   C N S 273 
ILE   C    C N N 274 
ILE   O    O N N 275 
ILE   CB   C N S 276 
ILE   CG1  C N N 277 
ILE   CG2  C N N 278 
ILE   CD1  C N N 279 
ILE   OXT  O N N 280 
ILE   H    H N N 281 
ILE   H2   H N N 282 
ILE   HA   H N N 283 
ILE   HB   H N N 284 
ILE   HG12 H N N 285 
ILE   HG13 H N N 286 
ILE   HG21 H N N 287 
ILE   HG22 H N N 288 
ILE   HG23 H N N 289 
ILE   HD11 H N N 290 
ILE   HD12 H N N 291 
ILE   HD13 H N N 292 
ILE   HXT  H N N 293 
K     K    K N N 294 
LEU   N    N N N 295 
LEU   CA   C N S 296 
LEU   C    C N N 297 
LEU   O    O N N 298 
LEU   CB   C N N 299 
LEU   CG   C N N 300 
LEU   CD1  C N N 301 
LEU   CD2  C N N 302 
LEU   OXT  O N N 303 
LEU   H    H N N 304 
LEU   H2   H N N 305 
LEU   HA   H N N 306 
LEU   HB2  H N N 307 
LEU   HB3  H N N 308 
LEU   HG   H N N 309 
LEU   HD11 H N N 310 
LEU   HD12 H N N 311 
LEU   HD13 H N N 312 
LEU   HD21 H N N 313 
LEU   HD22 H N N 314 
LEU   HD23 H N N 315 
LEU   HXT  H N N 316 
LYS   N    N N N 317 
LYS   CA   C N S 318 
LYS   C    C N N 319 
LYS   O    O N N 320 
LYS   CB   C N N 321 
LYS   CG   C N N 322 
LYS   CD   C N N 323 
LYS   CE   C N N 324 
LYS   NZ   N N N 325 
LYS   OXT  O N N 326 
LYS   H    H N N 327 
LYS   H2   H N N 328 
LYS   HA   H N N 329 
LYS   HB2  H N N 330 
LYS   HB3  H N N 331 
LYS   HG2  H N N 332 
LYS   HG3  H N N 333 
LYS   HD2  H N N 334 
LYS   HD3  H N N 335 
LYS   HE2  H N N 336 
LYS   HE3  H N N 337 
LYS   HZ1  H N N 338 
LYS   HZ2  H N N 339 
LYS   HZ3  H N N 340 
LYS   HXT  H N N 341 
MET   N    N N N 342 
MET   CA   C N S 343 
MET   C    C N N 344 
MET   O    O N N 345 
MET   CB   C N N 346 
MET   CG   C N N 347 
MET   SD   S N N 348 
MET   CE   C N N 349 
MET   OXT  O N N 350 
MET   H    H N N 351 
MET   H2   H N N 352 
MET   HA   H N N 353 
MET   HB2  H N N 354 
MET   HB3  H N N 355 
MET   HG2  H N N 356 
MET   HG3  H N N 357 
MET   HE1  H N N 358 
MET   HE2  H N N 359 
MET   HE3  H N N 360 
MET   HXT  H N N 361 
PHE   N    N N N 362 
PHE   CA   C N S 363 
PHE   C    C N N 364 
PHE   O    O N N 365 
PHE   CB   C N N 366 
PHE   CG   C Y N 367 
PHE   CD1  C Y N 368 
PHE   CD2  C Y N 369 
PHE   CE1  C Y N 370 
PHE   CE2  C Y N 371 
PHE   CZ   C Y N 372 
PHE   OXT  O N N 373 
PHE   H    H N N 374 
PHE   H2   H N N 375 
PHE   HA   H N N 376 
PHE   HB2  H N N 377 
PHE   HB3  H N N 378 
PHE   HD1  H N N 379 
PHE   HD2  H N N 380 
PHE   HE1  H N N 381 
PHE   HE2  H N N 382 
PHE   HZ   H N N 383 
PHE   HXT  H N N 384 
PLT   N1   N Y N 385 
PLT   C2   C Y N 386 
PLT   C2A  C N N 387 
PLT   C3   C Y N 388 
PLT   O3   O N N 389 
PLT   C4   C Y N 390 
PLT   C4A  C N N 391 
PLT   C5   C Y N 392 
PLT   C6   C Y N 393 
PLT   C5A  C N N 394 
PLT   O4P  O N N 395 
PLT   P    P N N 396 
PLT   O1P  O N N 397 
PLT   O2P  O N N 398 
PLT   O3P  O N N 399 
PLT   N    N N N 400 
PLT   CA   C N S 401 
PLT   C    C N N 402 
PLT   O    O N N 403 
PLT   OXT  O N N 404 
PLT   CB   C N N 405 
PLT   CG   C Y N 406 
PLT   CD1  C Y N 407 
PLT   NE1  N Y N 408 
PLT   CE2  C Y N 409 
PLT   CZ2  C Y N 410 
PLT   CH2  C Y N 411 
PLT   CZ3  C Y N 412 
PLT   CE3  C Y N 413 
PLT   CD2  C Y N 414 
PLT   H2A1 H N N 415 
PLT   H2A2 H N N 416 
PLT   H2A3 H N N 417 
PLT   HO3  H N N 418 
PLT   H4A  H N N 419 
PLT   H6   H N N 420 
PLT   H5A1 H N N 421 
PLT   H5A2 H N N 422 
PLT   HOP2 H N N 423 
PLT   HOP3 H N N 424 
PLT   HA   H N N 425 
PLT   HXT  H N N 426 
PLT   HB1  H N N 427 
PLT   HB2  H N N 428 
PLT   HD1  H N N 429 
PLT   HNE  H N N 430 
PLT   HZ2  H N N 431 
PLT   HH2  H N N 432 
PLT   HZ3  H N N 433 
PLT   HE3  H N N 434 
PRO   N    N N N 435 
PRO   CA   C N S 436 
PRO   C    C N N 437 
PRO   O    O N N 438 
PRO   CB   C N N 439 
PRO   CG   C N N 440 
PRO   CD   C N N 441 
PRO   OXT  O N N 442 
PRO   H    H N N 443 
PRO   HA   H N N 444 
PRO   HB2  H N N 445 
PRO   HB3  H N N 446 
PRO   HG2  H N N 447 
PRO   HG3  H N N 448 
PRO   HD2  H N N 449 
PRO   HD3  H N N 450 
PRO   HXT  H N N 451 
SER   N    N N N 452 
SER   CA   C N S 453 
SER   C    C N N 454 
SER   O    O N N 455 
SER   CB   C N N 456 
SER   OG   O N N 457 
SER   OXT  O N N 458 
SER   H    H N N 459 
SER   H2   H N N 460 
SER   HA   H N N 461 
SER   HB2  H N N 462 
SER   HB3  H N N 463 
SER   HG   H N N 464 
SER   HXT  H N N 465 
THR   N    N N N 466 
THR   CA   C N S 467 
THR   C    C N N 468 
THR   O    O N N 469 
THR   CB   C N R 470 
THR   OG1  O N N 471 
THR   CG2  C N N 472 
THR   OXT  O N N 473 
THR   H    H N N 474 
THR   H2   H N N 475 
THR   HA   H N N 476 
THR   HB   H N N 477 
THR   HG1  H N N 478 
THR   HG21 H N N 479 
THR   HG22 H N N 480 
THR   HG23 H N N 481 
THR   HXT  H N N 482 
TRP   N    N N N 483 
TRP   CA   C N S 484 
TRP   C    C N N 485 
TRP   O    O N N 486 
TRP   CB   C N N 487 
TRP   CG   C Y N 488 
TRP   CD1  C Y N 489 
TRP   CD2  C Y N 490 
TRP   NE1  N Y N 491 
TRP   CE2  C Y N 492 
TRP   CE3  C Y N 493 
TRP   CZ2  C Y N 494 
TRP   CZ3  C Y N 495 
TRP   CH2  C Y N 496 
TRP   OXT  O N N 497 
TRP   H    H N N 498 
TRP   H2   H N N 499 
TRP   HA   H N N 500 
TRP   HB2  H N N 501 
TRP   HB3  H N N 502 
TRP   HD1  H N N 503 
TRP   HE1  H N N 504 
TRP   HE3  H N N 505 
TRP   HZ2  H N N 506 
TRP   HZ3  H N N 507 
TRP   HH2  H N N 508 
TRP   HXT  H N N 509 
TYR   N    N N N 510 
TYR   CA   C N S 511 
TYR   C    C N N 512 
TYR   O    O N N 513 
TYR   CB   C N N 514 
TYR   CG   C Y N 515 
TYR   CD1  C Y N 516 
TYR   CD2  C Y N 517 
TYR   CE1  C Y N 518 
TYR   CE2  C Y N 519 
TYR   CZ   C Y N 520 
TYR   OH   O N N 521 
TYR   OXT  O N N 522 
TYR   H    H N N 523 
TYR   H2   H N N 524 
TYR   HA   H N N 525 
TYR   HB2  H N N 526 
TYR   HB3  H N N 527 
TYR   HD1  H N N 528 
TYR   HD2  H N N 529 
TYR   HE1  H N N 530 
TYR   HE2  H N N 531 
TYR   HH   H N N 532 
TYR   HXT  H N N 533 
VAL   N    N N N 534 
VAL   CA   C N S 535 
VAL   C    C N N 536 
VAL   O    O N N 537 
VAL   CB   C N N 538 
VAL   CG1  C N N 539 
VAL   CG2  C N N 540 
VAL   OXT  O N N 541 
VAL   H    H N N 542 
VAL   H2   H N N 543 
VAL   HA   H N N 544 
VAL   HB   H N N 545 
VAL   HG11 H N N 546 
VAL   HG12 H N N 547 
VAL   HG13 H N N 548 
VAL   HG21 H N N 549 
VAL   HG22 H N N 550 
VAL   HG23 H N N 551 
VAL   HXT  H N N 552 
# 
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 
0JO   O   C    doub N N 1   
0JO   OXT C    sing N N 2   
0JO   C   CA   sing N N 3   
0JO   CA  CB   doub N N 4   
0JO   CA  N    sing N N 5   
0JO   O3  C3   sing N N 6   
0JO   N   C4A  doub N N 7   
0JO   C4A C4   sing N N 8   
0JO   C3  C4   doub Y N 9   
0JO   C3  C2   sing Y N 10  
0JO   C2A C2   sing N N 11  
0JO   C4  C5   sing Y N 12  
0JO   C2  N1   doub Y N 13  
0JO   OP3 P    doub N N 14  
0JO   C5  C5A  sing N N 15  
0JO   C5  C6   doub Y N 16  
0JO   N1  C6   sing Y N 17  
0JO   OP4 C5A  sing N N 18  
0JO   OP4 P    sing N N 19  
0JO   OP1 P    sing N N 20  
0JO   P   OP2  sing N N 21  
0JO   OXT H1   sing N N 22  
0JO   CB  H2   sing N N 23  
0JO   CB  H3   sing N N 24  
0JO   C4A H4   sing N N 25  
0JO   O3  H5   sing N N 26  
0JO   C2A H6   sing N N 27  
0JO   C2A H7   sing N N 28  
0JO   C2A H8   sing N N 29  
0JO   C6  H9   sing N N 30  
0JO   C5A H10  sing N N 31  
0JO   C5A H11  sing N N 32  
0JO   OP1 H12  sing N N 33  
0JO   OP2 H13  sing N N 34  
A1A2Z O1P P    doub N N 35  
A1A2Z O2P P    sing N N 36  
A1A2Z P   O3P  sing N N 37  
A1A2Z P   O4P  sing N N 38  
A1A2Z O4P C5A  sing N N 39  
A1A2Z C5A C5   sing N N 40  
A1A2Z CB  CA   sing N N 41  
A1A2Z CB  CG   sing N N 42  
A1A2Z C4A C4   sing N N 43  
A1A2Z C4A N    sing N N 44  
A1A2Z CA  N    sing N N 45  
A1A2Z CA  C    sing N N 46  
A1A2Z C5  C4   doub Y N 47  
A1A2Z C5  C6   sing Y N 48  
A1A2Z C4  C3   sing Y N 49  
A1A2Z CG  CD1  doub Y N 50  
A1A2Z CG  CD2  sing Y N 51  
A1A2Z CD1 NE1  sing Y N 52  
A1A2Z O   C    doub N N 53  
A1A2Z C6  N1   doub Y N 54  
A1A2Z C   OXT  sing N N 55  
A1A2Z C3  O3   sing N N 56  
A1A2Z C3  C2   doub Y N 57  
A1A2Z CD2 CE3  doub Y N 58  
A1A2Z CD2 CE2  sing Y N 59  
A1A2Z NE1 CE2  sing Y N 60  
A1A2Z N1  C2   sing Y N 61  
A1A2Z CE3 CZ3  sing Y N 62  
A1A2Z C2  C2A  sing N N 63  
A1A2Z CE2 CZ2  doub Y N 64  
A1A2Z CZ3 CH2  doub Y N 65  
A1A2Z CZ2 CH2  sing Y N 66  
A1A2Z N   H    sing N N 67  
A1A2Z CD1 HD1  sing N N 68  
A1A2Z CE3 HE3  sing N N 69  
A1A2Z CZ3 HZ3  sing N N 70  
A1A2Z C2A H2A1 sing N N 71  
A1A2Z C2A H2A2 sing N N 72  
A1A2Z C2A H2A3 sing N N 73  
A1A2Z CA  HA   sing N N 74  
A1A2Z CH2 HH2  sing N N 75  
A1A2Z C4A H4A  sing N N 76  
A1A2Z C4A H4B  sing N N 77  
A1A2Z C5A H5A1 sing N N 78  
A1A2Z C5A H5A2 sing N N 79  
A1A2Z C6  H6   sing N N 80  
A1A2Z CB  HB2  sing N N 81  
A1A2Z CB  HB3  sing N N 82  
A1A2Z CZ2 HZ2  sing N N 83  
A1A2Z NE1 HE1  sing N N 84  
A1A2Z OXT HXT  sing N N 85  
A1A2Z O3P HOP3 sing N N 86  
A1A2Z O3  HO3  sing N N 87  
A1A2Z O2P HOP2 sing N N 88  
ALA   N   CA   sing N N 89  
ALA   N   H    sing N N 90  
ALA   N   H2   sing N N 91  
ALA   CA  C    sing N N 92  
ALA   CA  CB   sing N N 93  
ALA   CA  HA   sing N N 94  
ALA   C   O    doub N N 95  
ALA   C   OXT  sing N N 96  
ALA   CB  HB1  sing N N 97  
ALA   CB  HB2  sing N N 98  
ALA   CB  HB3  sing N N 99  
ALA   OXT HXT  sing N N 100 
ARG   N   CA   sing N N 101 
ARG   N   H    sing N N 102 
ARG   N   H2   sing N N 103 
ARG   CA  C    sing N N 104 
ARG   CA  CB   sing N N 105 
ARG   CA  HA   sing N N 106 
ARG   C   O    doub N N 107 
ARG   C   OXT  sing N N 108 
ARG   CB  CG   sing N N 109 
ARG   CB  HB2  sing N N 110 
ARG   CB  HB3  sing N N 111 
ARG   CG  CD   sing N N 112 
ARG   CG  HG2  sing N N 113 
ARG   CG  HG3  sing N N 114 
ARG   CD  NE   sing N N 115 
ARG   CD  HD2  sing N N 116 
ARG   CD  HD3  sing N N 117 
ARG   NE  CZ   sing N N 118 
ARG   NE  HE   sing N N 119 
ARG   CZ  NH1  sing N N 120 
ARG   CZ  NH2  doub N N 121 
ARG   NH1 HH11 sing N N 122 
ARG   NH1 HH12 sing N N 123 
ARG   NH2 HH21 sing N N 124 
ARG   NH2 HH22 sing N N 125 
ARG   OXT HXT  sing N N 126 
ASN   N   CA   sing N N 127 
ASN   N   H    sing N N 128 
ASN   N   H2   sing N N 129 
ASN   CA  C    sing N N 130 
ASN   CA  CB   sing N N 131 
ASN   CA  HA   sing N N 132 
ASN   C   O    doub N N 133 
ASN   C   OXT  sing N N 134 
ASN   CB  CG   sing N N 135 
ASN   CB  HB2  sing N N 136 
ASN   CB  HB3  sing N N 137 
ASN   CG  OD1  doub N N 138 
ASN   CG  ND2  sing N N 139 
ASN   ND2 HD21 sing N N 140 
ASN   ND2 HD22 sing N N 141 
ASN   OXT HXT  sing N N 142 
ASP   N   CA   sing N N 143 
ASP   N   H    sing N N 144 
ASP   N   H2   sing N N 145 
ASP   CA  C    sing N N 146 
ASP   CA  CB   sing N N 147 
ASP   CA  HA   sing N N 148 
ASP   C   O    doub N N 149 
ASP   C   OXT  sing N N 150 
ASP   CB  CG   sing N N 151 
ASP   CB  HB2  sing N N 152 
ASP   CB  HB3  sing N N 153 
ASP   CG  OD1  doub N N 154 
ASP   CG  OD2  sing N N 155 
ASP   OD2 HD2  sing N N 156 
ASP   OXT HXT  sing N N 157 
BZI   N1  C2   sing Y N 158 
BZI   N1  C7A  sing Y N 159 
BZI   N1  HN1  sing N N 160 
BZI   C2  N3   doub Y N 161 
BZI   C2  H2   sing N N 162 
BZI   N3  C3A  sing Y N 163 
BZI   C3A C4   doub Y N 164 
BZI   C3A C7A  sing Y N 165 
BZI   C4  C5   sing Y N 166 
BZI   C4  H4   sing N N 167 
BZI   C5  C6   doub Y N 168 
BZI   C5  H5   sing N N 169 
BZI   C6  C7   sing Y N 170 
BZI   C6  H6   sing N N 171 
BZI   C7  C7A  doub Y N 172 
BZI   C7  H7   sing N N 173 
CYS   N   CA   sing N N 174 
CYS   N   H    sing N N 175 
CYS   N   H2   sing N N 176 
CYS   CA  C    sing N N 177 
CYS   CA  CB   sing N N 178 
CYS   CA  HA   sing N N 179 
CYS   C   O    doub N N 180 
CYS   C   OXT  sing N N 181 
CYS   CB  SG   sing N N 182 
CYS   CB  HB2  sing N N 183 
CYS   CB  HB3  sing N N 184 
CYS   SG  HG   sing N N 185 
CYS   OXT HXT  sing N N 186 
DMS   S   O    doub N N 187 
DMS   S   C1   sing N N 188 
DMS   S   C2   sing N N 189 
DMS   C1  H11  sing N N 190 
DMS   C1  H12  sing N N 191 
DMS   C1  H13  sing N N 192 
DMS   C2  H21  sing N N 193 
DMS   C2  H22  sing N N 194 
DMS   C2  H23  sing N N 195 
GLN   N   CA   sing N N 196 
GLN   N   H    sing N N 197 
GLN   N   H2   sing N N 198 
GLN   CA  C    sing N N 199 
GLN   CA  CB   sing N N 200 
GLN   CA  HA   sing N N 201 
GLN   C   O    doub N N 202 
GLN   C   OXT  sing N N 203 
GLN   CB  CG   sing N N 204 
GLN   CB  HB2  sing N N 205 
GLN   CB  HB3  sing N N 206 
GLN   CG  CD   sing N N 207 
GLN   CG  HG2  sing N N 208 
GLN   CG  HG3  sing N N 209 
GLN   CD  OE1  doub N N 210 
GLN   CD  NE2  sing N N 211 
GLN   NE2 HE21 sing N N 212 
GLN   NE2 HE22 sing N N 213 
GLN   OXT HXT  sing N N 214 
GLU   N   CA   sing N N 215 
GLU   N   H    sing N N 216 
GLU   N   H2   sing N N 217 
GLU   CA  C    sing N N 218 
GLU   CA  CB   sing N N 219 
GLU   CA  HA   sing N N 220 
GLU   C   O    doub N N 221 
GLU   C   OXT  sing N N 222 
GLU   CB  CG   sing N N 223 
GLU   CB  HB2  sing N N 224 
GLU   CB  HB3  sing N N 225 
GLU   CG  CD   sing N N 226 
GLU   CG  HG2  sing N N 227 
GLU   CG  HG3  sing N N 228 
GLU   CD  OE1  doub N N 229 
GLU   CD  OE2  sing N N 230 
GLU   OE2 HE2  sing N N 231 
GLU   OXT HXT  sing N N 232 
GLY   N   CA   sing N N 233 
GLY   N   H    sing N N 234 
GLY   N   H2   sing N N 235 
GLY   CA  C    sing N N 236 
GLY   CA  HA2  sing N N 237 
GLY   CA  HA3  sing N N 238 
GLY   C   O    doub N N 239 
GLY   C   OXT  sing N N 240 
GLY   OXT HXT  sing N N 241 
HIS   N   CA   sing N N 242 
HIS   N   H    sing N N 243 
HIS   N   H2   sing N N 244 
HIS   CA  C    sing N N 245 
HIS   CA  CB   sing N N 246 
HIS   CA  HA   sing N N 247 
HIS   C   O    doub N N 248 
HIS   C   OXT  sing N N 249 
HIS   CB  CG   sing N N 250 
HIS   CB  HB2  sing N N 251 
HIS   CB  HB3  sing N N 252 
HIS   CG  ND1  sing Y N 253 
HIS   CG  CD2  doub Y N 254 
HIS   ND1 CE1  doub Y N 255 
HIS   ND1 HD1  sing N N 256 
HIS   CD2 NE2  sing Y N 257 
HIS   CD2 HD2  sing N N 258 
HIS   CE1 NE2  sing Y N 259 
HIS   CE1 HE1  sing N N 260 
HIS   NE2 HE2  sing N N 261 
HIS   OXT HXT  sing N N 262 
HOH   O   H1   sing N N 263 
HOH   O   H2   sing N N 264 
ILE   N   CA   sing N N 265 
ILE   N   H    sing N N 266 
ILE   N   H2   sing N N 267 
ILE   CA  C    sing N N 268 
ILE   CA  CB   sing N N 269 
ILE   CA  HA   sing N N 270 
ILE   C   O    doub N N 271 
ILE   C   OXT  sing N N 272 
ILE   CB  CG1  sing N N 273 
ILE   CB  CG2  sing N N 274 
ILE   CB  HB   sing N N 275 
ILE   CG1 CD1  sing N N 276 
ILE   CG1 HG12 sing N N 277 
ILE   CG1 HG13 sing N N 278 
ILE   CG2 HG21 sing N N 279 
ILE   CG2 HG22 sing N N 280 
ILE   CG2 HG23 sing N N 281 
ILE   CD1 HD11 sing N N 282 
ILE   CD1 HD12 sing N N 283 
ILE   CD1 HD13 sing N N 284 
ILE   OXT HXT  sing N N 285 
LEU   N   CA   sing N N 286 
LEU   N   H    sing N N 287 
LEU   N   H2   sing N N 288 
LEU   CA  C    sing N N 289 
LEU   CA  CB   sing N N 290 
LEU   CA  HA   sing N N 291 
LEU   C   O    doub N N 292 
LEU   C   OXT  sing N N 293 
LEU   CB  CG   sing N N 294 
LEU   CB  HB2  sing N N 295 
LEU   CB  HB3  sing N N 296 
LEU   CG  CD1  sing N N 297 
LEU   CG  CD2  sing N N 298 
LEU   CG  HG   sing N N 299 
LEU   CD1 HD11 sing N N 300 
LEU   CD1 HD12 sing N N 301 
LEU   CD1 HD13 sing N N 302 
LEU   CD2 HD21 sing N N 303 
LEU   CD2 HD22 sing N N 304 
LEU   CD2 HD23 sing N N 305 
LEU   OXT HXT  sing N N 306 
LYS   N   CA   sing N N 307 
LYS   N   H    sing N N 308 
LYS   N   H2   sing N N 309 
LYS   CA  C    sing N N 310 
LYS   CA  CB   sing N N 311 
LYS   CA  HA   sing N N 312 
LYS   C   O    doub N N 313 
LYS   C   OXT  sing N N 314 
LYS   CB  CG   sing N N 315 
LYS   CB  HB2  sing N N 316 
LYS   CB  HB3  sing N N 317 
LYS   CG  CD   sing N N 318 
LYS   CG  HG2  sing N N 319 
LYS   CG  HG3  sing N N 320 
LYS   CD  CE   sing N N 321 
LYS   CD  HD2  sing N N 322 
LYS   CD  HD3  sing N N 323 
LYS   CE  NZ   sing N N 324 
LYS   CE  HE2  sing N N 325 
LYS   CE  HE3  sing N N 326 
LYS   NZ  HZ1  sing N N 327 
LYS   NZ  HZ2  sing N N 328 
LYS   NZ  HZ3  sing N N 329 
LYS   OXT HXT  sing N N 330 
MET   N   CA   sing N N 331 
MET   N   H    sing N N 332 
MET   N   H2   sing N N 333 
MET   CA  C    sing N N 334 
MET   CA  CB   sing N N 335 
MET   CA  HA   sing N N 336 
MET   C   O    doub N N 337 
MET   C   OXT  sing N N 338 
MET   CB  CG   sing N N 339 
MET   CB  HB2  sing N N 340 
MET   CB  HB3  sing N N 341 
MET   CG  SD   sing N N 342 
MET   CG  HG2  sing N N 343 
MET   CG  HG3  sing N N 344 
MET   SD  CE   sing N N 345 
MET   CE  HE1  sing N N 346 
MET   CE  HE2  sing N N 347 
MET   CE  HE3  sing N N 348 
MET   OXT HXT  sing N N 349 
PHE   N   CA   sing N N 350 
PHE   N   H    sing N N 351 
PHE   N   H2   sing N N 352 
PHE   CA  C    sing N N 353 
PHE   CA  CB   sing N N 354 
PHE   CA  HA   sing N N 355 
PHE   C   O    doub N N 356 
PHE   C   OXT  sing N N 357 
PHE   CB  CG   sing N N 358 
PHE   CB  HB2  sing N N 359 
PHE   CB  HB3  sing N N 360 
PHE   CG  CD1  doub Y N 361 
PHE   CG  CD2  sing Y N 362 
PHE   CD1 CE1  sing Y N 363 
PHE   CD1 HD1  sing N N 364 
PHE   CD2 CE2  doub Y N 365 
PHE   CD2 HD2  sing N N 366 
PHE   CE1 CZ   doub Y N 367 
PHE   CE1 HE1  sing N N 368 
PHE   CE2 CZ   sing Y N 369 
PHE   CE2 HE2  sing N N 370 
PHE   CZ  HZ   sing N N 371 
PHE   OXT HXT  sing N N 372 
PLT   N1  C2   doub Y N 373 
PLT   N1  C6   sing Y N 374 
PLT   C2  C2A  sing N N 375 
PLT   C2  C3   sing Y N 376 
PLT   C2A H2A1 sing N N 377 
PLT   C2A H2A2 sing N N 378 
PLT   C2A H2A3 sing N N 379 
PLT   C3  O3   sing N N 380 
PLT   C3  C4   doub Y N 381 
PLT   O3  HO3  sing N N 382 
PLT   C4  C4A  sing N N 383 
PLT   C4  C5   sing Y N 384 
PLT   C4A N    doub N E 385 
PLT   C4A H4A  sing N N 386 
PLT   C5  C6   doub Y N 387 
PLT   C5  C5A  sing N N 388 
PLT   C6  H6   sing N N 389 
PLT   C5A O4P  sing N N 390 
PLT   C5A H5A1 sing N N 391 
PLT   C5A H5A2 sing N N 392 
PLT   O4P P    sing N N 393 
PLT   P   O1P  doub N N 394 
PLT   P   O2P  sing N N 395 
PLT   P   O3P  sing N N 396 
PLT   O2P HOP2 sing N N 397 
PLT   O3P HOP3 sing N N 398 
PLT   N   CA   sing N N 399 
PLT   CA  C    sing N N 400 
PLT   CA  CB   sing N N 401 
PLT   CA  HA   sing N N 402 
PLT   C   O    doub N N 403 
PLT   C   OXT  sing N N 404 
PLT   OXT HXT  sing N N 405 
PLT   CB  CG   sing N N 406 
PLT   CB  HB1  sing N N 407 
PLT   CB  HB2  sing N N 408 
PLT   CG  CD1  doub Y N 409 
PLT   CG  CD2  sing Y N 410 
PLT   CD1 NE1  sing Y N 411 
PLT   CD1 HD1  sing N N 412 
PLT   NE1 CE2  sing Y N 413 
PLT   NE1 HNE  sing N N 414 
PLT   CE2 CZ2  doub Y N 415 
PLT   CE2 CD2  sing Y N 416 
PLT   CZ2 CH2  sing Y N 417 
PLT   CZ2 HZ2  sing N N 418 
PLT   CH2 CZ3  doub Y N 419 
PLT   CH2 HH2  sing N N 420 
PLT   CZ3 CE3  sing Y N 421 
PLT   CZ3 HZ3  sing N N 422 
PLT   CE3 CD2  doub Y N 423 
PLT   CE3 HE3  sing N N 424 
PRO   N   CA   sing N N 425 
PRO   N   CD   sing N N 426 
PRO   N   H    sing N N 427 
PRO   CA  C    sing N N 428 
PRO   CA  CB   sing N N 429 
PRO   CA  HA   sing N N 430 
PRO   C   O    doub N N 431 
PRO   C   OXT  sing N N 432 
PRO   CB  CG   sing N N 433 
PRO   CB  HB2  sing N N 434 
PRO   CB  HB3  sing N N 435 
PRO   CG  CD   sing N N 436 
PRO   CG  HG2  sing N N 437 
PRO   CG  HG3  sing N N 438 
PRO   CD  HD2  sing N N 439 
PRO   CD  HD3  sing N N 440 
PRO   OXT HXT  sing N N 441 
SER   N   CA   sing N N 442 
SER   N   H    sing N N 443 
SER   N   H2   sing N N 444 
SER   CA  C    sing N N 445 
SER   CA  CB   sing N N 446 
SER   CA  HA   sing N N 447 
SER   C   O    doub N N 448 
SER   C   OXT  sing N N 449 
SER   CB  OG   sing N N 450 
SER   CB  HB2  sing N N 451 
SER   CB  HB3  sing N N 452 
SER   OG  HG   sing N N 453 
SER   OXT HXT  sing N N 454 
THR   N   CA   sing N N 455 
THR   N   H    sing N N 456 
THR   N   H2   sing N N 457 
THR   CA  C    sing N N 458 
THR   CA  CB   sing N N 459 
THR   CA  HA   sing N N 460 
THR   C   O    doub N N 461 
THR   C   OXT  sing N N 462 
THR   CB  OG1  sing N N 463 
THR   CB  CG2  sing N N 464 
THR   CB  HB   sing N N 465 
THR   OG1 HG1  sing N N 466 
THR   CG2 HG21 sing N N 467 
THR   CG2 HG22 sing N N 468 
THR   CG2 HG23 sing N N 469 
THR   OXT HXT  sing N N 470 
TRP   N   CA   sing N N 471 
TRP   N   H    sing N N 472 
TRP   N   H2   sing N N 473 
TRP   CA  C    sing N N 474 
TRP   CA  CB   sing N N 475 
TRP   CA  HA   sing N N 476 
TRP   C   O    doub N N 477 
TRP   C   OXT  sing N N 478 
TRP   CB  CG   sing N N 479 
TRP   CB  HB2  sing N N 480 
TRP   CB  HB3  sing N N 481 
TRP   CG  CD1  doub Y N 482 
TRP   CG  CD2  sing Y N 483 
TRP   CD1 NE1  sing Y N 484 
TRP   CD1 HD1  sing N N 485 
TRP   CD2 CE2  doub Y N 486 
TRP   CD2 CE3  sing Y N 487 
TRP   NE1 CE2  sing Y N 488 
TRP   NE1 HE1  sing N N 489 
TRP   CE2 CZ2  sing Y N 490 
TRP   CE3 CZ3  doub Y N 491 
TRP   CE3 HE3  sing N N 492 
TRP   CZ2 CH2  doub Y N 493 
TRP   CZ2 HZ2  sing N N 494 
TRP   CZ3 CH2  sing Y N 495 
TRP   CZ3 HZ3  sing N N 496 
TRP   CH2 HH2  sing N N 497 
TRP   OXT HXT  sing N N 498 
TYR   N   CA   sing N N 499 
TYR   N   H    sing N N 500 
TYR   N   H2   sing N N 501 
TYR   CA  C    sing N N 502 
TYR   CA  CB   sing N N 503 
TYR   CA  HA   sing N N 504 
TYR   C   O    doub N N 505 
TYR   C   OXT  sing N N 506 
TYR   CB  CG   sing N N 507 
TYR   CB  HB2  sing N N 508 
TYR   CB  HB3  sing N N 509 
TYR   CG  CD1  doub Y N 510 
TYR   CG  CD2  sing Y N 511 
TYR   CD1 CE1  sing Y N 512 
TYR   CD1 HD1  sing N N 513 
TYR   CD2 CE2  doub Y N 514 
TYR   CD2 HD2  sing N N 515 
TYR   CE1 CZ   doub Y N 516 
TYR   CE1 HE1  sing N N 517 
TYR   CE2 CZ   sing Y N 518 
TYR   CE2 HE2  sing N N 519 
TYR   CZ  OH   sing N N 520 
TYR   OH  HH   sing N N 521 
TYR   OXT HXT  sing N N 522 
VAL   N   CA   sing N N 523 
VAL   N   H    sing N N 524 
VAL   N   H2   sing N N 525 
VAL   CA  C    sing N N 526 
VAL   CA  CB   sing N N 527 
VAL   CA  HA   sing N N 528 
VAL   C   O    doub N N 529 
VAL   C   OXT  sing N N 530 
VAL   CB  CG1  sing N N 531 
VAL   CB  CG2  sing N N 532 
VAL   CB  HB   sing N N 533 
VAL   CG1 HG11 sing N N 534 
VAL   CG1 HG12 sing N N 535 
VAL   CG1 HG13 sing N N 536 
VAL   CG2 HG21 sing N N 537 
VAL   CG2 HG22 sing N N 538 
VAL   CG2 HG23 sing N N 539 
VAL   OXT HXT  sing N N 540 
# 
_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           GM137008 
_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   5W19 
_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                    9BLV 
_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]   0.008809 
_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]   0.009094 
_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]   0.006897 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356  2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
K ? ? 16.37977 2.54835 ? ? 4.54127  84.28225 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032  2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882  3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
P ? ? 9.51135  5.44231 ? ? 1.42069  35.72801 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732  6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N N   . ALA   A 1 2   ? -31.021 -5.263  79.280  1.00 30.24  ?  2   ALA   A N   1 
ATOM   2     C CA  . ALA   A 1 2   ? -30.147 -5.248  78.112  1.00 29.93  ?  2   ALA   A CA  1 
ATOM   3     C C   . ALA   A 1 2   ? -28.789 -5.828  78.480  1.00 33.10  ?  2   ALA   A C   1 
ATOM   4     O O   . ALA   A 1 2   ? -28.251 -5.544  79.553  1.00 31.13  ?  2   ALA   A O   1 
ATOM   5     C CB  . ALA   A 1 2   ? -30.001 -3.831  77.565  1.00 26.66  ?  2   ALA   A CB  1 
ATOM   6     N N   . LYS   A 1 3   ? -28.237 -6.640  77.585  1.00 26.86  ?  3   LYS   A N   1 
ATOM   7     C CA  . LYS   A 1 3   ? -27.049 -7.438  77.860  1.00 26.66  ?  3   LYS   A CA  1 
ATOM   8     C C   . LYS   A 1 3   ? -25.904 -6.993  76.959  1.00 26.34  ?  3   LYS   A C   1 
ATOM   9     O O   . LYS   A 1 3   ? -25.990 -7.110  75.729  1.00 25.64  ?  3   LYS   A O   1 
ATOM   10    C CB  . LYS   A 1 3   ? -27.355 -8.923  77.655  1.00 29.72  ?  3   LYS   A CB  1 
ATOM   11    C CG  . LYS   A 1 3   ? -26.177 -9.858  77.866  1.00 32.38  ?  3   LYS   A CG  1 
ATOM   12    C CD  . LYS   A 1 3   ? -26.668 -11.288 78.005  1.00 37.10  ?  3   LYS   A CD  1 
ATOM   13    C CE  . LYS   A 1 3   ? -25.521 -12.275 78.090  1.00 52.32  ?  3   LYS   A CE  1 
ATOM   14    N NZ  . LYS   A 1 3   ? -26.024 -13.682 78.133  1.00 62.49  ?  3   LYS   A NZ  1 
ATOM   15    N N   . ARG   A 1 4   ? -24.885 -6.427  77.582  1.00 25.90  ?  4   ARG   A N   1 
ATOM   16    C CA  A ARG   A 1 4   ? -23.640 -6.119  76.824  0.66 22.63  ?  4   ARG   A CA  1 
ATOM   17    C CA  B ARG   A 1 4   ? -23.640 -6.116  76.826  0.34 22.72  ?  4   ARG   A CA  1 
ATOM   18    C C   . ARG   A 1 4   ? -22.689 -7.361  76.631  1.00 26.27  ?  4   ARG   A C   1 
ATOM   19    O O   . ARG   A 1 4   ? -22.286 -8.220  77.542  1.00 24.26  ?  4   ARG   A O   1 
ATOM   20    C CB  A ARG   A 1 4   ? -22.868 -5.004  77.529  0.66 25.14  ?  4   ARG   A CB  1 
ATOM   21    C CB  B ARG   A 1 4   ? -22.844 -5.047  77.573  0.34 25.15  ?  4   ARG   A CB  1 
ATOM   22    C CG  A ARG   A 1 4   ? -23.640 -3.728  77.814  0.66 26.05  ?  4   ARG   A CG  1 
ATOM   23    C CG  B ARG   A 1 4   ? -23.582 -3.739  77.778  0.34 26.02  ?  4   ARG   A CG  1 
ATOM   24    C CD  A ARG   A 1 4   ? -22.856 -2.825  78.741  0.66 27.12  ?  4   ARG   A CD  1 
ATOM   25    C CD  B ARG   A 1 4   ? -22.643 -2.674  78.315  0.34 26.84  ?  4   ARG   A CD  1 
ATOM   26    N NE  A ARG   A 1 4   ? -22.935 -1.426  78.312  0.66 27.48  ?  4   ARG   A NE  1 
ATOM   27    N NE  B ARG   A 1 4   ? -22.221 -2.959  79.682  0.34 27.26  ?  4   ARG   A NE  1 
ATOM   28    C CZ  A ARG   A 1 4   ? -21.930 -0.746  77.784  0.66 24.36  ?  4   ARG   A CZ  1 
ATOM   29    C CZ  B ARG   A 1 4   ? -22.607 -2.268  80.747  0.34 27.23  ?  4   ARG   A CZ  1 
ATOM   30    N NH1 A ARG   A 1 4   ? -20.726 -1.281  77.710  0.66 26.16  ?  4   ARG   A NH1 1 
ATOM   31    N NH1 B ARG   A 1 4   ? -23.416 -1.225  80.640  0.34 25.22  ?  4   ARG   A NH1 1 
ATOM   32    N NH2 A ARG   A 1 4   ? -22.130 0.473   77.333  0.66 24.82  ?  4   ARG   A NH2 1 
ATOM   33    N NH2 B ARG   A 1 4   ? -22.164 -2.630  81.948  0.34 25.88  ?  4   ARG   A NH2 1 
ATOM   34    N N   . ILE   A 1 5   ? -22.397 -7.597  75.361  1.00 21.39  ?  5   ILE   A N   1 
ATOM   35    C CA  . ILE   A 1 5   ? -21.565 -8.733  74.980  1.00 22.16  ?  5   ILE   A CA  1 
ATOM   36    C C   . ILE   A 1 5   ? -20.193 -8.210  74.580  1.00 22.92  ?  5   ILE   A C   1 
ATOM   37    O O   . ILE   A 1 5   ? -20.088 -7.269  73.782  1.00 24.17  ?  5   ILE   A O   1 
ATOM   38    C CB  . ILE   A 1 5   ? -22.205 -9.545  73.841  1.00 19.20  ?  5   ILE   A CB  1 
ATOM   39    C CG1 . ILE   A 1 5   ? -23.412 -10.318 74.377  1.00 25.51  ?  5   ILE   A CG1 1 
ATOM   40    C CG2 . ILE   A 1 5   ? -21.187 -10.476 73.227  1.00 21.95  ?  5   ILE   A CG2 1 
ATOM   41    C CD1 . ILE   A 1 5   ? -24.256 -10.962 73.301  1.00 26.13  ?  5   ILE   A CD1 1 
ATOM   42    N N   . VAL   A 1 6   ? -19.148 -8.828  75.121  1.00 17.04  ?  6   VAL   A N   1 
ATOM   43    C CA  . VAL   A 1 6   ? -17.781 -8.339  74.977  1.00 21.64  ?  6   VAL   A CA  1 
ATOM   44    C C   . VAL   A 1 6   ? -17.209 -8.734  73.617  1.00 21.65  ?  6   VAL   A C   1 
ATOM   45    O O   . VAL   A 1 6   ? -17.570 -9.762  73.030  1.00 18.59  ?  6   VAL   A O   1 
ATOM   46    C CB  . VAL   A 1 6   ? -16.920 -8.860  76.150  1.00 25.07  ?  6   VAL   A CB  1 
ATOM   47    C CG1 . VAL   A 1 6   ? -16.861 -10.388 76.153  1.00 22.24  ?  6   VAL   A CG1 1 
ATOM   48    C CG2 . VAL   A 1 6   ? -15.524 -8.243  76.139  1.00 21.03  ?  6   VAL   A CG2 1 
ATOM   49    N N   . GLU   A 1 7   ? -16.312 -7.889  73.110  1.00 21.30  ?  7   GLU   A N   1 
ATOM   50    C CA  . GLU   A 1 7   ? -15.695 -8.095  71.806  1.00 20.28  ?  7   GLU   A CA  1 
ATOM   51    C C   . GLU   A 1 7   ? -14.864 -9.378  71.790  1.00 23.65  ?  7   GLU   A C   1 
ATOM   52    O O   . GLU   A 1 7   ? -14.082 -9.618  72.719  1.00 26.48  ?  7   GLU   A O   1 
ATOM   53    C CB  . GLU   A 1 7   ? -14.799 -6.906  71.456  1.00 19.52  ?  7   GLU   A CB  1 
ATOM   54    C CG  . GLU   A 1 7   ? -15.526 -5.615  71.120  1.00 19.37  ?  7   GLU   A CG  1 
ATOM   55    C CD  . GLU   A 1 7   ? -16.144 -4.913  72.328  1.00 23.57  ?  7   GLU   A CD  1 
ATOM   56    O OE1 . GLU   A 1 7   ? -15.848 -5.291  73.488  1.00 23.48  ?  7   GLU   A OE1 1 
ATOM   57    O OE2 . GLU   A 1 7   ? -16.931 -3.963  72.112  1.00 24.39  ?  7   GLU   A OE2 1 
ATOM   58    N N   . PRO   A 1 8   ? -14.988 -10.215 70.760  1.00 18.71  ?  8   PRO   A N   1 
ATOM   59    C CA  . PRO   A 1 8   ? -14.068 -11.347 70.625  1.00 19.07  ?  8   PRO   A CA  1 
ATOM   60    C C   . PRO   A 1 8   ? -12.804 -10.935 69.884  1.00 19.47  ?  8   PRO   A C   1 
ATOM   61    O O   . PRO   A 1 8   ? -12.235 -11.706 69.105  1.00 20.27  ?  8   PRO   A O   1 
ATOM   62    C CB  . PRO   A 1 8   ? -14.893 -12.363 69.834  1.00 20.93  ?  8   PRO   A CB  1 
ATOM   63    C CG  . PRO   A 1 8   ? -15.736 -11.512 68.959  1.00 17.99  ?  8   PRO   A CG  1 
ATOM   64    C CD  . PRO   A 1 8   ? -16.077 -10.279 69.773  1.00 19.83  ?  8   PRO   A CD  1 
ATOM   65    N N   . PHE   A 1 9   ? -12.370 -9.702  70.126  1.00 18.22  ?  9   PHE   A N   1 
ATOM   66    C CA  . PHE   A 1 9   ? -11.185 -9.130  69.504  1.00 19.15  ?  9   PHE   A CA  1 
ATOM   67    C C   . PHE   A 1 9   ? -10.752 -7.958  70.365  1.00 16.14  ?  9   PHE   A C   1 
ATOM   68    O O   . PHE   A 1 9   ? -11.445 -7.576  71.308  1.00 20.70  ?  9   PHE   A O   1 
ATOM   69    C CB  . PHE   A 1 9   ? -11.461 -8.677  68.067  1.00 14.64  ?  9   PHE   A CB  1 
ATOM   70    C CG  . PHE   A 1 9   ? -12.627 -7.724  67.946  1.00 16.41  ?  9   PHE   A CG  1 
ATOM   71    C CD1 . PHE   A 1 9   ? -12.476 -6.370  68.223  1.00 13.17  ?  9   PHE   A CD1 1 
ATOM   72    C CD2 . PHE   A 1 9   ? -13.874 -8.189  67.554  1.00 14.45  ?  9   PHE   A CD2 1 
ATOM   73    C CE1 . PHE   A 1 9   ? -13.557 -5.501  68.116  1.00 20.07  ?  9   PHE   A CE1 1 
ATOM   74    C CE2 . PHE   A 1 9   ? -14.954 -7.331  67.451  1.00 16.95  ?  9   PHE   A CE2 1 
ATOM   75    C CZ  . PHE   A 1 9   ? -14.798 -5.984  67.724  1.00 16.25  ?  9   PHE   A CZ  1 
ATOM   76    N N   . ARG   A 1 10  ? -9.609  -7.373  70.026  1.00 18.27  ?  10  ARG   A N   1 
ATOM   77    C CA  . ARG   A 1 10  ? -9.221  -6.107  70.628  1.00 18.77  ?  10  ARG   A CA  1 
ATOM   78    C C   . ARG   A 1 10  ? -8.888  -5.127  69.515  1.00 18.43  ?  10  ARG   A C   1 
ATOM   79    O O   . ARG   A 1 10  ? -8.791  -5.496  68.344  1.00 15.22  ?  10  ARG   A O   1 
ATOM   80    C CB  . ARG   A 1 10  ? -8.049  -6.263  71.613  1.00 20.16  ?  10  ARG   A CB  1 
ATOM   81    C CG  . ARG   A 1 10  ? -6.836  -6.922  71.043  1.00 19.59  ?  10  ARG   A CG  1 
ATOM   82    C CD  . ARG   A 1 10  ? -5.834  -7.281  72.127  1.00 25.79  ?  10  ARG   A CD  1 
ATOM   83    N NE  . ARG   A 1 10  ? -4.691  -7.972  71.540  1.00 29.38  ?  10  ARG   A NE  1 
ATOM   84    C CZ  . ARG   A 1 10  ? -3.911  -8.828  72.186  1.00 29.84  ?  10  ARG   A CZ  1 
ATOM   85    N NH1 . ARG   A 1 10  ? -4.114  -9.127  73.461  1.00 27.38  ?  10  ARG   A NH1 1 
ATOM   86    N NH2 . ARG   A 1 10  ? -2.909  -9.409  71.532  1.00 31.37  ?  10  ARG   A NH2 1 
ATOM   87    N N   . ILE   A 1 11  ? -8.739  -3.861  69.887  1.00 17.41  ?  11  ILE   A N   1 
ATOM   88    C CA  . ILE   A 1 11  ? -8.547  -2.800  68.907  1.00 13.79  ?  11  ILE   A CA  1 
ATOM   89    C C   . ILE   A 1 11  ? -7.076  -2.740  68.527  1.00 18.84  ?  11  ILE   A C   1 
ATOM   90    O O   . ILE   A 1 11  ? -6.194  -2.763  69.395  1.00 17.58  ?  11  ILE   A O   1 
ATOM   91    C CB  . ILE   A 1 11  ? -9.035  -1.455  69.471  1.00 16.99  ?  11  ILE   A CB  1 
ATOM   92    C CG1 . ILE   A 1 11  ? -10.502 -1.567  69.887  1.00 14.16  ?  11  ILE   A CG1 1 
ATOM   93    C CG2 . ILE   A 1 11  ? -8.820  -0.326  68.465  1.00 14.15  ?  11  ILE   A CG2 1 
ATOM   94    C CD1 . ILE   A 1 11  ? -10.985 -0.415  70.727  1.00 16.73  ?  11  ILE   A CD1 1 
ATOM   95    N N   . LYS   A 1 12  ? -6.803  -2.683  67.221  1.00 16.87  ?  12  LYS   A N   1 
ATOM   96    C CA  . LYS   A 1 12  ? -5.441  -2.520  66.736  1.00 15.53  ?  12  LYS   A CA  1 
ATOM   97    C C   . LYS   A 1 12  ? -5.194  -1.176  66.068  1.00 17.80  ?  12  LYS   A C   1 
ATOM   98    O O   . LYS   A 1 12  ? -4.044  -0.729  66.023  1.00 19.18  ?  12  LYS   A O   1 
ATOM   99    C CB  . LYS   A 1 12  ? -5.075  -3.647  65.757  1.00 17.62  ?  12  LYS   A CB  1 
ATOM   100   C CG  . LYS   A 1 12  ? -3.560  -3.744  65.493  1.00 21.01  ?  12  LYS   A CG  1 
ATOM   101   C CD  . LYS   A 1 12  ? -3.180  -5.081  64.878  1.00 24.81  ?  12  LYS   A CD  1 
ATOM   102   C CE  . LYS   A 1 12  ? -1.685  -5.182  64.598  1.00 25.22  ?  12  LYS   A CE  1 
ATOM   103   N NZ  . LYS   A 1 12  ? -1.309  -6.615  64.465  1.00 23.06  ?  12  LYS   A NZ  1 
ATOM   104   N N   . MET   A 1 13  ? -6.227  -0.513  65.561  1.00 13.84  ?  13  MET   A N   1 
ATOM   105   C CA  . MET   A 1 13  ? -6.031  0.812   64.997  1.00 15.05  ?  13  MET   A CA  1 
ATOM   106   C C   . MET   A 1 13  ? -7.304  1.611   65.206  1.00 14.18  ?  13  MET   A C   1 
ATOM   107   O O   . MET   A 1 13  ? -8.404  1.070   65.093  1.00 14.49  ?  13  MET   A O   1 
ATOM   108   C CB  . MET   A 1 13  ? -5.662  0.744   63.507  1.00 13.90  ?  13  MET   A CB  1 
ATOM   109   C CG  . MET   A 1 13  ? -5.334  2.096   62.886  1.00 17.10  ?  13  MET   A CG  1 
ATOM   110   S SD  . MET   A 1 13  ? -5.186  2.006   61.089  1.00 26.53  ?  13  MET   A SD  1 
ATOM   111   C CE  . MET   A 1 13  ? -4.025  0.668   60.963  1.00 14.18  ?  13  MET   A CE  1 
ATOM   112   N N   . VAL   A 1 14  ? -7.151  2.894   65.517  1.00 16.42  ?  14  VAL   A N   1 
ATOM   113   C CA  . VAL   A 1 14  ? -8.291  3.740   65.834  1.00 16.32  ?  14  VAL   A CA  1 
ATOM   114   C C   . VAL   A 1 14  ? -8.405  4.844   64.794  1.00 13.17  ?  14  VAL   A C   1 
ATOM   115   O O   . VAL   A 1 14  ? -7.468  5.137   64.054  1.00 16.31  ?  14  VAL   A O   1 
ATOM   116   C CB  . VAL   A 1 14  ? -8.193  4.336   67.255  1.00 16.10  ?  14  VAL   A CB  1 
ATOM   117   C CG1 . VAL   A 1 14  ? -8.084  3.223   68.273  1.00 17.26  ?  14  VAL   A CG1 1 
ATOM   118   C CG2 . VAL   A 1 14  ? -6.997  5.267   67.370  1.00 14.28  ?  14  VAL   A CG2 1 
ATOM   119   N N   . GLU   A 1 15  ? -9.583  5.458   64.755  1.00 17.39  ?  15  GLU   A N   1 
ATOM   120   C CA  . GLU   A 1 15  ? -9.889  6.541   63.835  1.00 17.92  ?  15  GLU   A CA  1 
ATOM   121   C C   . GLU   A 1 15  ? -10.610 7.631   64.611  1.00 18.76  ?  15  GLU   A C   1 
ATOM   122   O O   . GLU   A 1 15  ? -11.579 7.350   65.320  1.00 19.46  ?  15  GLU   A O   1 
ATOM   123   C CB  . GLU   A 1 15  ? -10.753 6.034   62.672  1.00 22.44  ?  15  GLU   A CB  1 
ATOM   124   C CG  . GLU   A 1 15  ? -11.356 7.118   61.806  1.00 24.91  ?  15  GLU   A CG  1 
ATOM   125   C CD  . GLU   A 1 15  ? -12.294 6.570   60.746  1.00 26.02  ?  15  GLU   A CD  1 
ATOM   126   O OE1 . GLU   A 1 15  ? -13.132 5.700   61.067  1.00 26.35  ?  15  GLU   A OE1 1 
ATOM   127   O OE2 . GLU   A 1 15  ? -12.195 7.012   59.583  1.00 33.36  ?  15  GLU   A OE2 1 
ATOM   128   N N   . LYS   A 1 16  ? -10.145 8.868   64.473  1.00 22.57  ?  16  LYS   A N   1 
ATOM   129   C CA  . LYS   A 1 16  ? -10.733 9.983   65.207  1.00 22.29  ?  16  LYS   A CA  1 
ATOM   130   C C   . LYS   A 1 16  ? -12.164 10.252  64.751  1.00 27.37  ?  16  LYS   A C   1 
ATOM   131   O O   . LYS   A 1 16  ? -12.475 10.208  63.559  1.00 26.03  ?  16  LYS   A O   1 
ATOM   132   C CB  . LYS   A 1 16  ? -9.881  11.237  65.014  1.00 30.73  ?  16  LYS   A CB  1 
ATOM   133   C CG  . LYS   A 1 16  ? -10.441 12.507  65.643  1.00 34.05  ?  16  LYS   A CG  1 
ATOM   134   C CD  . LYS   A 1 16  ? -9.910  12.718  67.053  1.00 39.49  ?  16  LYS   A CD  1 
ATOM   135   C CE  . LYS   A 1 16  ? -10.072 14.175  67.504  1.00 49.10  ?  16  LYS   A CE  1 
ATOM   136   N NZ  . LYS   A 1 16  ? -8.970  15.090  67.064  1.00 47.67  ?  16  LYS   A NZ  1 
ATOM   137   N N   . ILE   A 1 17  ? -13.047 10.516  65.716  1.00 26.30  ?  17  ILE   A N   1 
ATOM   138   C CA  . ILE   A 1 17  ? -14.383 11.029  65.449  1.00 26.89  ?  17  ILE   A CA  1 
ATOM   139   C C   . ILE   A 1 17  ? -14.640 12.150  66.442  1.00 30.60  ?  17  ILE   A C   1 
ATOM   140   O O   . ILE   A 1 17  ? -14.037 12.204  67.515  1.00 34.52  ?  17  ILE   A O   1 
ATOM   141   C CB  . ILE   A 1 17  ? -15.486 9.954   65.566  1.00 26.08  ?  17  ILE   A CB  1 
ATOM   142   C CG1 . ILE   A 1 17  ? -15.512 9.357   66.974  1.00 25.81  ?  17  ILE   A CG1 1 
ATOM   143   C CG2 . ILE   A 1 17  ? -15.294 8.877   64.515  1.00 28.50  ?  17  ILE   A CG2 1 
ATOM   144   C CD1 . ILE   A 1 17  ? -16.659 8.392   67.214  1.00 25.33  ?  17  ILE   A CD1 1 
ATOM   145   N N   . ARG   A 1 18  ? -15.544 13.058  66.075  1.00 33.29  ?  18  ARG   A N   1 
ATOM   146   C CA  . ARG   A 1 18  ? -15.845 14.206  66.922  1.00 33.53  ?  18  ARG   A CA  1 
ATOM   147   C C   . ARG   A 1 18  ? -17.330 14.519  66.854  1.00 33.46  ?  18  ARG   A C   1 
ATOM   148   O O   . ARG   A 1 18  ? -18.052 14.037  65.976  1.00 33.50  ?  18  ARG   A O   1 
ATOM   149   C CB  . ARG   A 1 18  ? -15.028 15.438  66.521  1.00 34.10  ?  18  ARG   A CB  1 
ATOM   150   C CG  . ARG   A 1 18  ? -15.286 15.902  65.107  1.00 36.68  ?  18  ARG   A CG  1 
ATOM   151   C CD  . ARG   A 1 18  ? -14.576 17.214  64.835  1.00 45.76  ?  18  ARG   A CD  1 
ATOM   152   N NE  . ARG   A 1 18  ? -15.132 18.309  65.623  1.00 43.80  ?  18  ARG   A NE  1 
ATOM   153   C CZ  . ARG   A 1 18  ? -16.063 19.142  65.184  1.00 44.29  ?  18  ARG   A CZ  1 
ATOM   154   N NH1 . ARG   A 1 18  ? -16.568 19.031  63.965  1.00 43.30  ?  18  ARG   A NH1 1 
ATOM   155   N NH2 . ARG   A 1 18  ? -16.501 20.111  65.987  1.00 50.64  ?  18  ARG   A NH2 1 
ATOM   156   N N   . VAL   A 1 19  ? -17.777 15.349  67.791  1.00 34.18  ?  19  VAL   A N   1 
ATOM   157   C CA  . VAL   A 1 19  ? -19.170 15.759  67.909  1.00 33.15  ?  19  VAL   A CA  1 
ATOM   158   C C   . VAL   A 1 19  ? -19.283 17.194  67.399  1.00 36.56  ?  19  VAL   A C   1 
ATOM   159   O O   . VAL   A 1 19  ? -18.759 18.121  68.035  1.00 36.47  ?  19  VAL   A O   1 
ATOM   160   C CB  . VAL   A 1 19  ? -19.675 15.644  69.353  1.00 33.34  ?  19  VAL   A CB  1 
ATOM   161   C CG1 . VAL   A 1 19  ? -21.168 15.967  69.422  1.00 36.20  ?  19  VAL   A CG1 1 
ATOM   162   C CG2 . VAL   A 1 19  ? -19.398 14.253  69.899  1.00 35.21  ?  19  VAL   A CG2 1 
ATOM   163   N N   . PRO   A 1 20  ? -19.951 17.428  66.273  1.00 37.37  ?  20  PRO   A N   1 
ATOM   164   C CA  . PRO   A 1 20  ? -20.163 18.807  65.815  1.00 38.43  ?  20  PRO   A CA  1 
ATOM   165   C C   . PRO   A 1 20  ? -21.111 19.557  66.740  1.00 37.86  ?  20  PRO   A C   1 
ATOM   166   O O   . PRO   A 1 20  ? -22.043 18.987  67.312  1.00 38.05  ?  20  PRO   A O   1 
ATOM   167   C CB  . PRO   A 1 20  ? -20.776 18.633  64.419  1.00 35.03  ?  20  PRO   A CB  1 
ATOM   168   C CG  . PRO   A 1 20  ? -20.498 17.194  64.037  1.00 40.33  ?  20  PRO   A CG  1 
ATOM   169   C CD  . PRO   A 1 20  ? -20.471 16.433  65.322  1.00 33.43  ?  20  PRO   A CD  1 
ATOM   170   N N   . SER   A 1 21  ? -20.863 20.854  66.882  1.00 39.95  ?  21  SER   A N   1 
ATOM   171   C CA  . SER   A 1 21  ? -21.727 21.687  67.701  1.00 39.29  ?  21  SER   A CA  1 
ATOM   172   C C   . SER   A 1 21  ? -23.113 21.793  67.078  1.00 40.35  ?  21  SER   A C   1 
ATOM   173   O O   . SER   A 1 21  ? -23.310 21.541  65.884  1.00 40.00  ?  21  SER   A O   1 
ATOM   174   C CB  . SER   A 1 21  ? -21.133 23.084  67.872  1.00 38.87  ?  21  SER   A CB  1 
ATOM   175   O OG  . SER   A 1 21  ? -21.127 23.781  66.640  1.00 38.73  ?  21  SER   A OG  1 
ATOM   176   N N   . ARG   A 1 22  ? -24.081 22.184  67.913  1.00 38.43  ?  22  ARG   A N   1 
ATOM   177   C CA  . ARG   A 1 22  ? -25.458 22.335  67.453  1.00 38.35  ?  22  ARG   A CA  1 
ATOM   178   C C   . ARG   A 1 22  ? -25.553 23.341  66.313  1.00 39.50  ?  22  ARG   A C   1 
ATOM   179   O O   . ARG   A 1 22  ? -26.342 23.157  65.379  1.00 43.05  ?  22  ARG   A O   1 
ATOM   180   C CB  . ARG   A 1 22  ? -26.351 22.748  68.626  1.00 37.41  ?  22  ARG   A CB  1 
ATOM   181   C CG  . ARG   A 1 22  ? -27.804 23.034  68.266  1.00 45.04  ?  22  ARG   A CG  1 
ATOM   182   C CD  . ARG   A 1 22  ? -28.450 21.852  67.557  1.00 48.74  ?  22  ARG   A CD  1 
ATOM   183   N NE  . ARG   A 1 22  ? -29.898 21.998  67.436  1.00 52.30  ?  22  ARG   A NE  1 
ATOM   184   C CZ  . ARG   A 1 22  ? -30.782 21.385  68.215  1.00 50.68  ?  22  ARG   A CZ  1 
ATOM   185   N NH1 . ARG   A 1 22  ? -30.401 20.567  69.185  1.00 49.32  ?  22  ARG   A NH1 1 
ATOM   186   N NH2 . ARG   A 1 22  ? -32.080 21.595  68.013  1.00 45.28  ?  22  ARG   A NH2 1 
ATOM   187   N N   . GLU   A 1 23  ? -24.750 24.407  66.365  1.00 42.12  ?  23  GLU   A N   1 
ATOM   188   C CA  . GLU   A 1 23  ? -24.695 25.352  65.252  1.00 45.19  ?  23  GLU   A CA  1 
ATOM   189   C C   . GLU   A 1 23  ? -24.265 24.656  63.964  1.00 41.87  ?  23  GLU   A C   1 
ATOM   190   O O   . GLU   A 1 23  ? -24.930 24.774  62.927  1.00 40.13  ?  23  GLU   A O   1 
ATOM   191   C CB  . GLU   A 1 23  ? -23.740 26.499  65.589  1.00 50.23  ?  23  GLU   A CB  1 
ATOM   192   C CG  . GLU   A 1 23  ? -23.443 27.452  64.427  1.00 55.37  ?  23  GLU   A CG  1 
ATOM   193   C CD  . GLU   A 1 23  ? -24.471 28.568  64.285  1.00 59.59  ?  23  GLU   A CD  1 
ATOM   194   O OE1 . GLU   A 1 23  ? -25.646 28.360  64.660  1.00 58.68  ?  23  GLU   A OE1 1 
ATOM   195   O OE2 . GLU   A 1 23  ? -24.099 29.661  63.803  1.00 62.01  ?  23  GLU   A OE2 1 
ATOM   196   N N   . GLU   A 1 24  ? -23.152 23.918  64.019  1.00 43.96  ?  24  GLU   A N   1 
ATOM   197   C CA  . GLU   A 1 24  ? -22.692 23.164  62.856  1.00 40.91  ?  24  GLU   A CA  1 
ATOM   198   C C   . GLU   A 1 24  ? -23.772 22.220  62.342  1.00 39.54  ?  24  GLU   A C   1 
ATOM   199   O O   . GLU   A 1 24  ? -24.011 22.140  61.130  1.00 41.56  ?  24  GLU   A O   1 
ATOM   200   C CB  . GLU   A 1 24  ? -21.427 22.379  63.207  1.00 40.54  ?  24  GLU   A CB  1 
ATOM   201   C CG  . GLU   A 1 24  ? -20.245 23.238  63.645  1.00 38.99  ?  24  GLU   A CG  1 
ATOM   202   C CD  . GLU   A 1 24  ? -19.024 22.409  64.020  1.00 45.66  ?  24  GLU   A CD  1 
ATOM   203   O OE1 . GLU   A 1 24  ? -18.795 21.349  63.388  1.00 52.74  ?  24  GLU   A OE1 1 
ATOM   204   O OE2 . GLU   A 1 24  ? -18.293 22.813  64.949  1.00 43.84  ?  24  GLU   A OE2 1 
ATOM   205   N N   . ARG   A 1 25  ? -24.444 21.505  63.246  1.00 39.72  ?  25  ARG   A N   1 
ATOM   206   C CA  A ARG   A 1 25  ? -25.459 20.547  62.817  0.20 40.29  ?  25  ARG   A CA  1 
ATOM   207   C CA  B ARG   A 1 25  ? -25.457 20.548  62.816  0.80 40.23  ?  25  ARG   A CA  1 
ATOM   208   C C   . ARG   A 1 25  ? -26.625 21.248  62.132  1.00 42.55  ?  25  ARG   A C   1 
ATOM   209   O O   . ARG   A 1 25  ? -27.115 20.782  61.097  1.00 42.40  ?  25  ARG   A O   1 
ATOM   210   C CB  A ARG   A 1 25  ? -25.950 19.726  64.009  0.20 39.71  ?  25  ARG   A CB  1 
ATOM   211   C CB  B ARG   A 1 25  ? -25.929 19.721  64.012  0.80 39.67  ?  25  ARG   A CB  1 
ATOM   212   C CG  A ARG   A 1 25  ? -24.848 18.992  64.758  0.20 39.30  ?  25  ARG   A CG  1 
ATOM   213   C CG  B ARG   A 1 25  ? -24.796 18.931  64.673  0.80 39.28  ?  25  ARG   A CG  1 
ATOM   214   C CD  A ARG   A 1 25  ? -25.420 17.970  65.727  0.20 38.13  ?  25  ARG   A CD  1 
ATOM   215   C CD  B ARG   A 1 25  ? -25.311 17.828  65.583  0.80 37.90  ?  25  ARG   A CD  1 
ATOM   216   N NE  A ARG   A 1 25  ? -24.616 17.851  66.938  0.20 38.70  ?  25  ARG   A NE  1 
ATOM   217   N NE  B ARG   A 1 25  ? -26.125 18.331  66.686  0.80 40.67  ?  25  ARG   A NE  1 
ATOM   218   C CZ  A ARG   A 1 25  ? -24.927 18.411  68.099  0.20 38.71  ?  25  ARG   A CZ  1 
ATOM   219   C CZ  B ARG   A 1 25  ? -25.670 18.566  67.910  0.80 39.31  ?  25  ARG   A CZ  1 
ATOM   220   N NH1 A ARG   A 1 25  ? -26.036 19.117  68.252  0.20 39.39  ?  25  ARG   A NH1 1 
ATOM   221   N NH1 B ARG   A 1 25  ? -24.396 18.390  68.219  0.80 37.56  ?  25  ARG   A NH1 1 
ATOM   222   N NH2 A ARG   A 1 25  ? -24.107 18.257  69.135  0.20 38.34  ?  25  ARG   A NH2 1 
ATOM   223   N NH2 B ARG   A 1 25  ? -26.518 18.982  68.848  0.80 37.41  ?  25  ARG   A NH2 1 
ATOM   224   N N   . GLU   A 1 26  ? -27.073 22.379  62.689  1.00 44.10  ?  26  GLU   A N   1 
ATOM   225   C CA  . GLU   A 1 26  ? -28.204 23.106  62.116  1.00 43.25  ?  26  GLU   A CA  1 
ATOM   226   C C   . GLU   A 1 26  ? -27.886 23.627  60.717  1.00 44.15  ?  26  GLU   A C   1 
ATOM   227   O O   . GLU   A 1 26  ? -28.709 23.508  59.799  1.00 42.38  ?  26  GLU   A O   1 
ATOM   228   C CB  . GLU   A 1 26  ? -28.600 24.257  63.042  1.00 40.30  ?  26  GLU   A CB  1 
ATOM   229   C CG  . GLU   A 1 26  ? -29.234 23.820  64.348  1.00 40.38  ?  26  GLU   A CG  1 
ATOM   230   C CD  . GLU   A 1 26  ? -30.733 23.658  64.232  1.00 47.83  ?  26  GLU   A CD  1 
ATOM   231   O OE1 . GLU   A 1 26  ? -31.256 23.813  63.108  1.00 54.83  ?  26  GLU   A OE1 1 
ATOM   232   O OE2 . GLU   A 1 26  ? -31.389 23.388  65.263  1.00 46.19  ?  26  GLU   A OE2 1 
ATOM   233   N N   . ALA   A 1 27  ? -26.701 24.218  60.538  1.00 40.82  ?  27  ALA   A N   1 
ATOM   234   C CA  . ALA   A 1 27  ? -26.303 24.701  59.218  1.00 38.93  ?  27  ALA   A CA  1 
ATOM   235   C C   . ALA   A 1 27  ? -26.110 23.550  58.239  1.00 45.58  ?  27  ALA   A C   1 
ATOM   236   O O   . ALA   A 1 27  ? -26.520 23.642  57.074  1.00 44.59  ?  27  ALA   A O   1 
ATOM   237   C CB  . ALA   A 1 27  ? -25.019 25.520  59.327  1.00 43.68  ?  27  ALA   A CB  1 
ATOM   238   N N   . ALA   A 1 28  ? -25.487 22.458  58.694  1.00 42.79  ?  28  ALA   A N   1 
ATOM   239   C CA  . ALA   A 1 28  ? -25.201 21.337  57.806  1.00 39.24  ?  28  ALA   A CA  1 
ATOM   240   C C   . ALA   A 1 28  ? -26.481 20.710  57.267  1.00 40.91  ?  28  ALA   A C   1 
ATOM   241   O O   . ALA   A 1 28  ? -26.553 20.346  56.087  1.00 42.02  ?  28  ALA   A O   1 
ATOM   242   C CB  . ALA   A 1 28  ? -24.360 20.293  58.543  1.00 35.94  ?  28  ALA   A CB  1 
ATOM   243   N N   . LEU   A 1 29  ? -27.503 20.571  58.116  1.00 42.01  ?  29  LEU   A N   1 
ATOM   244   C CA  . LEU   A 1 29  ? -28.739 19.925  57.682  1.00 41.28  ?  29  LEU   A CA  1 
ATOM   245   C C   . LEU   A 1 29  ? -29.519 20.812  56.717  1.00 41.63  ?  29  LEU   A C   1 
ATOM   246   O O   . LEU   A 1 29  ? -30.096 20.321  55.738  1.00 37.15  ?  29  LEU   A O   1 
ATOM   247   C CB  . LEU   A 1 29  ? -29.596 19.561  58.894  1.00 36.96  ?  29  LEU   A CB  1 
ATOM   248   C CG  . LEU   A 1 29  ? -30.858 18.756  58.583  1.00 38.53  ?  29  LEU   A CG  1 
ATOM   249   C CD1 . LEU   A 1 29  ? -30.499 17.421  57.948  1.00 39.25  ?  29  LEU   A CD1 1 
ATOM   250   C CD2 . LEU   A 1 29  ? -31.677 18.548  59.839  1.00 39.02  ?  29  LEU   A CD2 1 
ATOM   251   N N   . LYS   A 1 30  ? -29.549 22.121  56.974  1.00 42.78  ?  30  LYS   A N   1 
ATOM   252   C CA  . LYS   A 1 30  ? -30.143 23.036  56.007  1.00 41.64  ?  30  LYS   A CA  1 
ATOM   253   C C   . LYS   A 1 30  ? -29.352 23.033  54.707  1.00 39.81  ?  30  LYS   A C   1 
ATOM   254   O O   . LYS   A 1 30  ? -29.936 22.990  53.617  1.00 43.16  ?  30  LYS   A O   1 
ATOM   255   C CB  . LYS   A 1 30  ? -30.226 24.444  56.596  1.00 45.07  ?  30  LYS   A CB  1 
ATOM   256   C CG  . LYS   A 1 30  ? -31.159 24.552  57.796  1.00 47.70  ?  30  LYS   A CG  1 
ATOM   257   C CD  . LYS   A 1 30  ? -31.371 26.001  58.222  1.00 58.15  ?  30  LYS   A CD  1 
ATOM   258   C CE  . LYS   A 1 30  ? -32.250 26.088  59.466  1.00 58.95  ?  30  LYS   A CE  1 
ATOM   259   N NZ  . LYS   A 1 30  ? -32.549 27.496  59.852  1.00 61.46  ?  30  LYS   A NZ  1 
ATOM   260   N N   . GLU   A 1 31  ? -28.018 23.045  54.801  1.00 42.85  ?  31  GLU   A N   1 
ATOM   261   C CA  . GLU   A 1 31  ? -27.195 22.996  53.597  1.00 39.74  ?  31  GLU   A CA  1 
ATOM   262   C C   . GLU   A 1 31  ? -27.416 21.707  52.828  1.00 41.87  ?  31  GLU   A C   1 
ATOM   263   O O   . GLU   A 1 31  ? -27.380 21.708  51.593  1.00 48.93  ?  31  GLU   A O   1 
ATOM   264   C CB  . GLU   A 1 31  ? -25.716 23.149  53.948  1.00 36.44  ?  31  GLU   A CB  1 
ATOM   265   C CG  . GLU   A 1 31  ? -24.796 23.253  52.729  1.00 41.87  ?  31  GLU   A CG  1 
ATOM   266   C CD  . GLU   A 1 31  ? -25.204 24.364  51.766  1.00 56.39  ?  31  GLU   A CD  1 
ATOM   267   O OE1 . GLU   A 1 31  ? -25.611 25.460  52.230  1.00 53.74  ?  31  GLU   A OE1 1 
ATOM   268   O OE2 . GLU   A 1 31  ? -25.125 24.139  50.537  1.00 57.41  ?  31  GLU   A OE2 1 
ATOM   269   N N   . ALA   A 1 32  ? -27.664 20.607  53.533  1.00 43.45  ?  32  ALA   A N   1 
ATOM   270   C CA  . ALA   A 1 32  ? -27.905 19.316  52.906  1.00 39.01  ?  32  ALA   A CA  1 
ATOM   271   C C   . ALA   A 1 32  ? -29.342 19.150  52.436  1.00 38.50  ?  32  ALA   A C   1 
ATOM   272   O O   . ALA   A 1 32  ? -29.749 18.025  52.125  1.00 38.69  ?  32  ALA   A O   1 
ATOM   273   C CB  . ALA   A 1 32  ? -27.537 18.189  53.874  1.00 36.43  ?  32  ALA   A CB  1 
ATOM   274   N N   . GLY   A 1 33  ? -30.111 20.236  52.377  1.00 43.81  ?  33  GLY   A N   1 
ATOM   275   C CA  . GLY   A 1 33  ? -31.502 20.149  51.967  1.00 46.54  ?  33  GLY   A CA  1 
ATOM   276   C C   . GLY   A 1 33  ? -32.360 19.323  52.894  1.00 43.55  ?  33  GLY   A C   1 
ATOM   277   O O   . GLY   A 1 33  ? -33.312 18.681  52.437  1.00 43.26  ?  33  GLY   A O   1 
ATOM   278   N N   . TYR   A 1 34  ? -32.039 19.318  54.191  1.00 40.91  ?  34  TYR   A N   1 
ATOM   279   C CA  . TYR   A 1 34  ? -32.724 18.490  55.186  1.00 38.93  ?  34  TYR   A CA  1 
ATOM   280   C C   . TYR   A 1 34  ? -32.718 17.015  54.791  1.00 37.85  ?  34  TYR   A C   1 
ATOM   281   O O   . TYR   A 1 34  ? -33.634 16.262  55.130  1.00 35.73  ?  34  TYR   A O   1 
ATOM   282   C CB  . TYR   A 1 34  ? -34.151 18.986  55.429  1.00 47.45  ?  34  TYR   A CB  1 
ATOM   283   C CG  . TYR   A 1 34  ? -34.199 20.371  56.026  1.00 45.01  ?  34  TYR   A CG  1 
ATOM   284   C CD1 . TYR   A 1 34  ? -34.090 20.554  57.399  1.00 42.67  ?  34  TYR   A CD1 1 
ATOM   285   C CD2 . TYR   A 1 34  ? -34.338 21.492  55.220  1.00 45.35  ?  34  TYR   A CD2 1 
ATOM   286   C CE1 . TYR   A 1 34  ? -34.126 21.812  57.955  1.00 47.03  ?  34  TYR   A CE1 1 
ATOM   287   C CE2 . TYR   A 1 34  ? -34.375 22.760  55.765  1.00 51.85  ?  34  TYR   A CE2 1 
ATOM   288   C CZ  . TYR   A 1 34  ? -34.270 22.915  57.136  1.00 56.04  ?  34  TYR   A CZ  1 
ATOM   289   O OH  . TYR   A 1 34  ? -34.309 24.175  57.695  1.00 60.95  ?  34  TYR   A OH  1 
ATOM   290   N N   . ASN   A 1 35  ? -31.682 16.597  54.065  1.00 35.11  ?  35  ASN   A N   1 
ATOM   291   C CA  . ASN   A 1 35  ? -31.488 15.195  53.701  1.00 36.55  ?  35  ASN   A CA  1 
ATOM   292   C C   . ASN   A 1 35  ? -30.120 14.747  54.200  1.00 34.53  ?  35  ASN   A C   1 
ATOM   293   O O   . ASN   A 1 35  ? -29.091 15.086  53.587  1.00 34.74  ?  35  ASN   A O   1 
ATOM   294   C CB  . ASN   A 1 35  ? -31.604 14.996  52.191  1.00 32.23  ?  35  ASN   A CB  1 
ATOM   295   C CG  . ASN   A 1 35  ? -31.590 13.529  51.795  1.00 36.58  ?  35  ASN   A CG  1 
ATOM   296   O OD1 . ASN   A 1 35  ? -31.198 12.664  52.581  1.00 39.83  ?  35  ASN   A OD1 1 
ATOM   297   N ND2 . ASN   A 1 35  ? -32.012 13.241  50.569  1.00 36.50  ?  35  ASN   A ND2 1 
ATOM   298   N N   . PRO   A 1 36  ? -30.052 13.981  55.292  1.00 34.35  ?  36  PRO   A N   1 
ATOM   299   C CA  . PRO   A 1 36  ? -28.738 13.583  55.831  1.00 29.50  ?  36  PRO   A CA  1 
ATOM   300   C C   . PRO   A 1 36  ? -27.861 12.843  54.838  1.00 29.96  ?  36  PRO   A C   1 
ATOM   301   O O   . PRO   A 1 36  ? -26.644 12.764  55.051  1.00 30.82  ?  36  PRO   A O   1 
ATOM   302   C CB  . PRO   A 1 36  ? -29.095 12.701  57.038  1.00 28.70  ?  36  PRO   A CB  1 
ATOM   303   C CG  . PRO   A 1 36  ? -30.573 12.456  56.957  1.00 31.54  ?  36  PRO   A CG  1 
ATOM   304   C CD  . PRO   A 1 36  ? -31.163 13.574  56.167  1.00 34.16  ?  36  PRO   A CD  1 
ATOM   305   N N   . PHE   A 1 37  ? -28.429 12.310  53.756  1.00 29.08  ?  37  PHE   A N   1 
ATOM   306   C CA  . PHE   A 1 37  ? -27.604 11.727  52.707  1.00 29.73  ?  37  PHE   A CA  1 
ATOM   307   C C   . PHE   A 1 37  ? -26.700 12.761  52.047  1.00 29.87  ?  37  PHE   A C   1 
ATOM   308   O O   . PHE   A 1 37  ? -25.652 12.397  51.508  1.00 33.53  ?  37  PHE   A O   1 
ATOM   309   C CB  . PHE   A 1 37  ? -28.486 11.063  51.652  1.00 31.36  ?  37  PHE   A CB  1 
ATOM   310   C CG  . PHE   A 1 37  ? -28.417 9.564   51.656  1.00 30.05  ?  37  PHE   A CG  1 
ATOM   311   C CD1 . PHE   A 1 37  ? -27.276 8.909   51.223  1.00 30.71  ?  37  PHE   A CD1 1 
ATOM   312   C CD2 . PHE   A 1 37  ? -29.502 8.808   52.069  1.00 33.63  ?  37  PHE   A CD2 1 
ATOM   313   C CE1 . PHE   A 1 37  ? -27.215 7.528   51.217  1.00 29.51  ?  37  PHE   A CE1 1 
ATOM   314   C CE2 . PHE   A 1 37  ? -29.447 7.429   52.066  1.00 28.23  ?  37  PHE   A CE2 1 
ATOM   315   C CZ  . PHE   A 1 37  ? -28.303 6.787   51.636  1.00 25.46  ?  37  PHE   A CZ  1 
ATOM   316   N N   . LEU   A 1 38  ? -27.070 14.039  52.086  1.00 32.75  ?  38  LEU   A N   1 
ATOM   317   C CA  . LEU   A 1 38  ? -26.269 15.100  51.493  1.00 28.81  ?  38  LEU   A CA  1 
ATOM   318   C C   . LEU   A 1 38  ? -25.331 15.767  52.496  1.00 31.53  ?  38  LEU   A C   1 
ATOM   319   O O   . LEU   A 1 38  ? -24.706 16.778  52.159  1.00 30.64  ?  38  LEU   A O   1 
ATOM   320   C CB  . LEU   A 1 38  ? -27.182 16.147  50.850  1.00 26.90  ?  38  LEU   A CB  1 
ATOM   321   C CG  . LEU   A 1 38  ? -28.161 15.577  49.818  1.00 35.24  ?  38  LEU   A CG  1 
ATOM   322   C CD1 . LEU   A 1 38  ? -28.972 16.682  49.160  1.00 39.68  ?  38  LEU   A CD1 1 
ATOM   323   C CD2 . LEU   A 1 38  ? -27.441 14.743  48.766  1.00 35.69  ?  38  LEU   A CD2 1 
ATOM   324   N N   . LEU   A 1 39  ? -25.220 15.224  53.725  1.00 27.73  ?  39  LEU   A N   1 
ATOM   325   C CA  . LEU   A 1 39  ? -24.295 15.729  54.733  1.00 25.91  ?  39  LEU   A CA  1 
ATOM   326   C C   . LEU   A 1 39  ? -22.884 15.201  54.472  1.00 27.88  ?  39  LEU   A C   1 
ATOM   327   O O   . LEU   A 1 39  ? -22.716 14.034  54.108  1.00 22.00  ?  39  LEU   A O   1 
ATOM   328   C CB  . LEU   A 1 39  ? -24.733 15.300  56.129  1.00 27.33  ?  39  LEU   A CB  1 
ATOM   329   C CG  . LEU   A 1 39  ? -25.997 15.898  56.733  1.00 32.87  ?  39  LEU   A CG  1 
ATOM   330   C CD1 . LEU   A 1 39  ? -26.358 15.156  58.011  1.00 31.02  ?  39  LEU   A CD1 1 
ATOM   331   C CD2 . LEU   A 1 39  ? -25.785 17.373  57.017  1.00 30.93  ?  39  LEU   A CD2 1 
ATOM   332   N N   . PRO   A 1 40  ? -21.857 16.031  54.648  1.00 27.94  ?  40  PRO   A N   1 
ATOM   333   C CA  . PRO   A 1 40  ? -20.486 15.511  54.628  1.00 23.83  ?  40  PRO   A CA  1 
ATOM   334   C C   . PRO   A 1 40  ? -20.199 14.724  55.892  1.00 27.94  ?  40  PRO   A C   1 
ATOM   335   O O   . PRO   A 1 40  ? -20.754 15.003  56.958  1.00 30.03  ?  40  PRO   A O   1 
ATOM   336   C CB  . PRO   A 1 40  ? -19.625 16.777  54.556  1.00 23.30  ?  40  PRO   A CB  1 
ATOM   337   C CG  . PRO   A 1 40  ? -20.482 17.836  55.180  1.00 26.35  ?  40  PRO   A CG  1 
ATOM   338   C CD  . PRO   A 1 40  ? -21.891 17.500  54.778  1.00 24.64  ?  40  PRO   A CD  1 
ATOM   339   N N   . SER   A 1 41  ? -19.315 13.727  55.766  1.00 24.61  ?  41  SER   A N   1 
ATOM   340   C CA  . SER   A 1 41  ? -18.951 12.915  56.924  1.00 21.52  ?  41  SER   A CA  1 
ATOM   341   C C   . SER   A 1 41  ? -18.409 13.762  58.071  1.00 23.06  ?  41  SER   A C   1 
ATOM   342   O O   . SER   A 1 41  ? -18.581 13.406  59.241  1.00 22.62  ?  41  SER   A O   1 
ATOM   343   C CB  . SER   A 1 41  ? -17.914 11.876  56.524  1.00 22.55  ?  41  SER   A CB  1 
ATOM   344   O OG  . SER   A 1 41  ? -16.664 12.507  56.315  1.00 26.22  ?  41  SER   A OG  1 
ATOM   345   N N   . SER   A 1 42  ? -17.751 14.880  57.763  1.00 24.71  ?  42  SER   A N   1 
ATOM   346   C CA  . SER   A 1 42  ? -17.231 15.755  58.808  1.00 24.53  ?  42  SER   A CA  1 
ATOM   347   C C   . SER   A 1 42  ? -18.332 16.337  59.688  1.00 28.42  ?  42  SER   A C   1 
ATOM   348   O O   . SER   A 1 42  ? -18.045 16.789  60.802  1.00 35.25  ?  42  SER   A O   1 
ATOM   349   C CB  . SER   A 1 42  ? -16.426 16.888  58.181  1.00 22.37  ?  42  SER   A CB  1 
ATOM   350   O OG  . SER   A 1 42  ? -17.241 17.611  57.275  1.00 28.10  ?  42  SER   A OG  1 
ATOM   351   N N   . ALA   A 1 43  ? -19.576 16.356  59.215  1.00 23.84  ?  43  ALA   A N   1 
ATOM   352   C CA  . ALA   A 1 43  ? -20.684 16.866  60.008  1.00 28.87  ?  43  ALA   A CA  1 
ATOM   353   C C   . ALA   A 1 43  ? -21.386 15.775  60.807  1.00 27.22  ?  43  ALA   A C   1 
ATOM   354   O O   . ALA   A 1 43  ? -22.415 16.046  61.430  1.00 31.01  ?  43  ALA   A O   1 
ATOM   355   C CB  . ALA   A 1 43  ? -21.693 17.586  59.107  1.00 27.28  ?  43  ALA   A CB  1 
ATOM   356   N N   . VAL   A 1 44  ? -20.849 14.558  60.820  1.00 26.66  ?  44  VAL   A N   1 
ATOM   357   C CA  . VAL   A 1 44  ? -21.498 13.416  61.450  1.00 25.36  ?  44  VAL   A CA  1 
ATOM   358   C C   . VAL   A 1 44  ? -20.625 12.905  62.588  1.00 27.72  ?  44  VAL   A C   1 
ATOM   359   O O   . VAL   A 1 44  ? -19.401 12.815  62.453  1.00 25.67  ?  44  VAL   A O   1 
ATOM   360   C CB  . VAL   A 1 44  ? -21.773 12.303  60.421  1.00 25.19  ?  44  VAL   A CB  1 
ATOM   361   C CG1 . VAL   A 1 44  ? -22.419 11.100  61.092  1.00 24.08  ?  44  VAL   A CG1 1 
ATOM   362   C CG2 . VAL   A 1 44  ? -22.653 12.847  59.300  1.00 23.16  ?  44  VAL   A CG2 1 
ATOM   363   N N   . TYR   A 1 45  ? -21.258 12.578  63.713  1.00 27.31  ?  45  TYR   A N   1 
ATOM   364   C CA  . TYR   A 1 45  ? -20.542 12.019  64.851  1.00 24.63  ?  45  TYR   A CA  1 
ATOM   365   C C   . TYR   A 1 45  ? -20.474 10.501  64.721  1.00 25.53  ?  45  TYR   A C   1 
ATOM   366   O O   . TYR   A 1 45  ? -19.476 9.959   64.235  1.00 32.92  ?  45  TYR   A O   1 
ATOM   367   C CB  . TYR   A 1 45  ? -21.217 12.451  66.154  1.00 25.99  ?  45  TYR   A CB  1 
ATOM   368   C CG  . TYR   A 1 45  ? -20.680 11.783  67.397  1.00 27.55  ?  45  TYR   A CG  1 
ATOM   369   C CD1 . TYR   A 1 45  ? -19.324 11.545  67.552  1.00 23.76  ?  45  TYR   A CD1 1 
ATOM   370   C CD2 . TYR   A 1 45  ? -21.534 11.407  68.427  1.00 26.94  ?  45  TYR   A CD2 1 
ATOM   371   C CE1 . TYR   A 1 45  ? -18.835 10.935  68.686  1.00 29.19  ?  45  TYR   A CE1 1 
ATOM   372   C CE2 . TYR   A 1 45  ? -21.052 10.805  69.567  1.00 27.06  ?  45  TYR   A CE2 1 
ATOM   373   C CZ  . TYR   A 1 45  ? -19.704 10.568  69.693  1.00 27.78  ?  45  TYR   A CZ  1 
ATOM   374   O OH  . TYR   A 1 45  ? -19.218 9.957   70.831  1.00 29.90  ?  45  TYR   A OH  1 
ATOM   375   N N   . ILE   A 1 46  ? -21.528 9.808   65.134  1.00 22.58  ?  46  ILE   A N   1 
ATOM   376   C CA  . ILE   A 1 46  ? -21.643 8.363   64.973  1.00 20.11  ?  46  ILE   A CA  1 
ATOM   377   C C   . ILE   A 1 46  ? -22.524 8.100   63.759  1.00 18.79  ?  46  ILE   A C   1 
ATOM   378   O O   . ILE   A 1 46  ? -23.712 8.443   63.759  1.00 19.51  ?  46  ILE   A O   1 
ATOM   379   C CB  . ILE   A 1 46  ? -22.221 7.702   66.233  1.00 23.54  ?  46  ILE   A CB  1 
ATOM   380   C CG1 . ILE   A 1 46  ? -21.233 7.809   67.404  1.00 21.71  ?  46  ILE   A CG1 1 
ATOM   381   C CG2 . ILE   A 1 46  ? -22.599 6.252   65.942  1.00 20.04  ?  46  ILE   A CG2 1 
ATOM   382   C CD1 . ILE   A 1 46  ? -21.846 7.465   68.753  1.00 22.19  ?  46  ILE   A CD1 1 
ATOM   383   N N   . ASP   A 1 47  ? -21.957 7.482   62.730  1.00 18.36  ?  47  ASP   A N   1 
ATOM   384   C CA  . ASP   A 1 47  ? -22.607 7.398   61.422  1.00 22.64  ?  47  ASP   A CA  1 
ATOM   385   C C   . ASP   A 1 47  ? -23.321 6.058   61.302  1.00 16.17  ?  47  ASP   A C   1 
ATOM   386   O O   . ASP   A 1 47  ? -22.686 5.020   61.102  1.00 20.76  ?  47  ASP   A O   1 
ATOM   387   C CB  . ASP   A 1 47  ? -21.585 7.590   60.306  1.00 22.67  ?  47  ASP   A CB  1 
ATOM   388   C CG  . ASP   A 1 47  ? -22.203 8.148   59.042  1.00 19.44  ?  47  ASP   A CG  1 
ATOM   389   O OD1 . ASP   A 1 47  ? -23.444 8.171   58.955  1.00 17.29  ?  47  ASP   A OD1 1 
ATOM   390   O OD2 . ASP   A 1 47  ? -21.449 8.571   58.140  1.00 19.42  ?  47  ASP   A OD2 1 
ATOM   391   N N   . LEU   A 1 48  ? -24.647 6.086   61.426  1.00 21.22  ?  48  LEU   A N   1 
ATOM   392   C CA  . LEU   A 1 48  ? -25.495 4.906   61.294  1.00 16.87  ?  48  LEU   A CA  1 
ATOM   393   C C   . LEU   A 1 48  ? -26.262 4.903   59.978  1.00 19.77  ?  48  LEU   A C   1 
ATOM   394   O O   . LEU   A 1 48  ? -27.304 4.245   59.873  1.00 18.80  ?  48  LEU   A O   1 
ATOM   395   C CB  . LEU   A 1 48  ? -26.475 4.820   62.465  1.00 19.12  ?  48  LEU   A CB  1 
ATOM   396   C CG  . LEU   A 1 48  ? -25.910 5.005   63.874  1.00 17.61  ?  48  LEU   A CG  1 
ATOM   397   C CD1 . LEU   A 1 48  ? -27.003 4.804   64.909  1.00 16.98  ?  48  LEU   A CD1 1 
ATOM   398   C CD2 . LEU   A 1 48  ? -24.738 4.071   64.112  1.00 16.59  ?  48  LEU   A CD2 1 
ATOM   399   N N   . LEU   A 1 49  ? -25.780 5.650   58.982  1.00 19.43  ?  49  LEU   A N   1 
ATOM   400   C CA  . LEU   A 1 49  ? -26.448 5.677   57.685  1.00 21.01  ?  49  LEU   A CA  1 
ATOM   401   C C   . LEU   A 1 49  ? -26.549 4.280   57.087  1.00 21.59  ?  49  LEU   A C   1 
ATOM   402   O O   . LEU   A 1 49  ? -27.605 3.893   56.573  1.00 19.87  ?  49  LEU   A O   1 
ATOM   403   C CB  . LEU   A 1 49  ? -25.704 6.614   56.730  1.00 18.64  ?  49  LEU   A CB  1 
ATOM   404   C CG  . LEU   A 1 49  ? -26.487 7.038   55.482  1.00 20.06  ?  49  LEU   A CG  1 
ATOM   405   C CD1 . LEU   A 1 49  ? -27.642 7.954   55.855  1.00 23.38  ?  49  LEU   A CD1 1 
ATOM   406   C CD2 . LEU   A 1 49  ? -25.582 7.712   54.482  1.00 18.22  ?  49  LEU   A CD2 1 
ATOM   407   N N   . THR   A 1 50  ? -25.464 3.506   57.150  1.00 19.82  ?  50  THR   A N   1 
ATOM   408   C CA  . THR   A 1 50  ? -25.441 2.176   56.555  1.00 19.62  ?  50  THR   A CA  1 
ATOM   409   C C   . THR   A 1 50  ? -24.482 1.273   57.317  1.00 18.43  ?  50  THR   A C   1 
ATOM   410   O O   . THR   A 1 50  ? -23.607 1.733   58.054  1.00 17.57  ?  50  THR   A O   1 
ATOM   411   C CB  . THR   A 1 50  ? -25.017 2.220   55.079  1.00 25.96  ?  50  THR   A CB  1 
ATOM   412   O OG1 . THR   A 1 50  ? -25.224 0.929   54.489  1.00 26.39  ?  50  THR   A OG1 1 
ATOM   413   C CG2 . THR   A 1 50  ? -23.540 2.572   54.977  1.00 19.28  ?  50  THR   A CG2 1 
ATOM   414   N N   . ASP   A 1 51  ? -24.657 -0.031  57.121  1.00 19.65  ?  51  ASP   A N   1 
ATOM   415   C CA  . ASP   A 1 51  ? -23.652 -1.014  57.498  1.00 15.80  ?  51  ASP   A CA  1 
ATOM   416   C C   . ASP   A 1 51  ? -22.804 -1.436  56.310  1.00 17.13  ?  51  ASP   A C   1 
ATOM   417   O O   . ASP   A 1 51  ? -22.072 -2.425  56.401  1.00 17.88  ?  51  ASP   A O   1 
ATOM   418   C CB  . ASP   A 1 51  ? -24.310 -2.242  58.140  1.00 18.25  ?  51  ASP   A CB  1 
ATOM   419   C CG  . ASP   A 1 51  ? -25.225 -3.006  57.185  1.00 18.52  ?  51  ASP   A CG  1 
ATOM   420   O OD1 . ASP   A 1 51  ? -25.885 -2.382  56.324  1.00 19.50  ?  51  ASP   A OD1 1 
ATOM   421   O OD2 . ASP   A 1 51  ? -25.299 -4.246  57.317  1.00 15.90  ?  51  ASP   A OD2 1 
ATOM   422   N N   . SER   A 1 52  ? -22.864 -0.690  55.212  1.00 17.74  ?  52  SER   A N   1 
ATOM   423   C CA  . SER   A 1 52  ? -22.285 -1.107  53.942  1.00 18.25  ?  52  SER   A CA  1 
ATOM   424   C C   . SER   A 1 52  ? -20.962 -0.386  53.704  1.00 17.70  ?  52  SER   A C   1 
ATOM   425   O O   . SER   A 1 52  ? -20.932 0.844   53.548  1.00 19.24  ?  52  SER   A O   1 
ATOM   426   C CB  . SER   A 1 52  ? -23.259 -0.832  52.798  1.00 18.94  ?  52  SER   A CB  1 
ATOM   427   O OG  . SER   A 1 52  ? -22.832 -1.448  51.592  1.00 17.67  ?  52  SER   A OG  1 
ATOM   428   N N   . GLY   A 1 53  ? -19.877 -1.155  53.652  1.00 14.26  ?  53  GLY   A N   1 
ATOM   429   C CA  . GLY   A 1 53  ? -18.577 -0.613  53.332  1.00 11.18  ?  53  GLY   A CA  1 
ATOM   430   C C   . GLY   A 1 53  ? -17.915 0.176   54.437  1.00 15.10  ?  53  GLY   A C   1 
ATOM   431   O O   . GLY   A 1 53  ? -16.818 0.709   54.223  1.00 14.54  ?  53  GLY   A O   1 
ATOM   432   N N   . THR   A 1 54  ? -18.536 0.261   55.614  1.00 13.72  ?  54  THR   A N   1 
ATOM   433   C CA  . THR   A 1 54  ? -18.019 1.028   56.737  1.00 15.02  ?  54  THR   A CA  1 
ATOM   434   C C   . THR   A 1 54  ? -17.364 0.151   57.797  1.00 16.92  ?  54  THR   A C   1 
ATOM   435   O O   . THR   A 1 54  ? -17.021 0.646   58.878  1.00 17.08  ?  54  THR   A O   1 
ATOM   436   C CB  . THR   A 1 54  ? -19.150 1.838   57.361  1.00 17.98  ?  54  THR   A CB  1 
ATOM   437   O OG1 . THR   A 1 54  ? -20.279 0.980   57.560  1.00 16.36  ?  54  THR   A OG1 1 
ATOM   438   C CG2 . THR   A 1 54  ? -19.565 2.975   56.435  1.00 20.29  ?  54  THR   A CG2 1 
ATOM   439   N N   . ASN   A 1 55  ? -17.172 -1.131  57.506  1.00 13.89  ?  55  ASN   A N   1 
ATOM   440   C CA  . ASN   A 1 55  ? -16.716 -2.082  58.503  1.00 14.42  ?  55  ASN   A CA  1 
ATOM   441   C C   . ASN   A 1 55  ? -15.231 -1.909  58.804  1.00 12.75  ?  55  ASN   A C   1 
ATOM   442   O O   . ASN   A 1 55  ? -14.460 -1.392  57.989  1.00 13.70  ?  55  ASN   A O   1 
ATOM   443   C CB  . ASN   A 1 55  ? -16.983 -3.500  58.018  1.00 13.70  ?  55  ASN   A CB  1 
ATOM   444   C CG  . ASN   A 1 55  ? -18.386 -3.673  57.486  1.00 14.44  ?  55  ASN   A CG  1 
ATOM   445   O OD1 . ASN   A 1 55  ? -19.353 -3.693  58.243  1.00 13.57  ?  55  ASN   A OD1 1 
ATOM   446   N ND2 . ASN   A 1 55  ? -18.505 -3.807  56.174  1.00 14.28  ?  55  ASN   A ND2 1 
ATOM   447   N N   . ALA   A 1 56  ? -14.844 -2.327  60.012  1.00 14.01  ?  56  ALA   A N   1 
ATOM   448   C CA  . ALA   A 1 56  ? -13.445 -2.401  60.414  1.00 10.28  ?  56  ALA   A CA  1 
ATOM   449   C C   . ALA   A 1 56  ? -12.912 -3.778  60.052  1.00 12.44  ?  56  ALA   A C   1 
ATOM   450   O O   . ALA   A 1 56  ? -13.450 -4.802  60.501  1.00 14.05  ?  56  ALA   A O   1 
ATOM   451   C CB  . ALA   A 1 56  ? -13.271 -2.148  61.913  1.00 11.34  ?  56  ALA   A CB  1 
ATOM   452   N N   . MET   A 1 57  ? -11.853 -3.797  59.256  1.00 13.67  ?  57  MET   A N   1 
ATOM   453   C CA  . MET   A 1 57  ? -11.201 -5.025  58.854  1.00 15.54  ?  57  MET   A CA  1 
ATOM   454   C C   . MET   A 1 57  ? -10.232 -5.487  59.936  1.00 15.74  ?  57  MET   A C   1 
ATOM   455   O O   . MET   A 1 57  ? -9.957  -4.775  60.905  1.00 16.68  ?  57  MET   A O   1 
ATOM   456   C CB  . MET   A 1 57  ? -10.476 -4.828  57.527  1.00 12.82  ?  57  MET   A CB  1 
ATOM   457   C CG  . MET   A 1 57  ? -11.431 -4.593  56.361  1.00 12.58  ?  57  MET   A CG  1 
ATOM   458   S SD  . MET   A 1 57  ? -10.612 -4.857  54.786  1.00 14.91  ?  57  MET   A SD  1 
ATOM   459   C CE  . MET   A 1 57  ? -9.455  -3.498  54.730  1.00 12.69  ?  57  MET   A CE  1 
ATOM   460   N N   . SER   A 1 58  ? -9.709  -6.697  59.761  1.00 11.43  ?  58  SER   A N   1 
ATOM   461   C CA  . SER   A 1 58  ? -8.725  -7.247  60.678  1.00 14.52  ?  58  SER   A CA  1 
ATOM   462   C C   . SER   A 1 58  ? -7.321  -6.997  60.149  1.00 16.30  ?  58  SER   A C   1 
ATOM   463   O O   . SER   A 1 58  ? -7.119  -6.645  58.985  1.00 14.61  ?  58  SER   A O   1 
ATOM   464   C CB  . SER   A 1 58  ? -8.941  -8.748  60.872  1.00 16.44  ?  58  SER   A CB  1 
ATOM   465   O OG  . SER   A 1 58  ? -8.718  -9.432  59.653  1.00 16.02  ?  58  SER   A OG  1 
ATOM   466   N N   . ASP   A 1 59  ? -6.335  -7.195  61.028  1.00 15.74  ?  59  ASP   A N   1 
ATOM   467   C CA  . ASP   A 1 59  ? -4.957  -7.139  60.564  1.00 12.61  ?  59  ASP   A CA  1 
ATOM   468   C C   . ASP   A 1 59  ? -4.699  -8.193  59.497  1.00 13.56  ?  59  ASP   A C   1 
ATOM   469   O O   . ASP   A 1 59  ? -3.941  -7.943  58.554  1.00 15.35  ?  59  ASP   A O   1 
ATOM   470   C CB  . ASP   A 1 59  ? -3.985  -7.286  61.739  1.00 14.86  ?  59  ASP   A CB  1 
ATOM   471   C CG  . ASP   A 1 59  ? -4.309  -8.463  62.646  1.00 15.88  ?  59  ASP   A CG  1 
ATOM   472   O OD1 . ASP   A 1 59  ? -5.344  -9.137  62.435  1.00 21.76  ?  59  ASP   A OD1 1 
ATOM   473   O OD2 . ASP   A 1 59  ? -3.518  -8.709  63.584  1.00 21.16  ?  59  ASP   A OD2 1 
ATOM   474   N N   . HIS   A 1 60  ? -5.351  -9.353  59.603  1.00 14.05  ?  60  HIS   A N   1 
ATOM   475   C CA  . HIS   A 1 60  ? -5.207  -10.393 58.585  1.00 16.29  ?  60  HIS   A CA  1 
ATOM   476   C C   . HIS   A 1 60  ? -5.793  -9.959  57.252  1.00 14.81  ?  60  HIS   A C   1 
ATOM   477   O O   . HIS   A 1 60  ? -5.271  -10.319 56.189  1.00 13.44  ?  60  HIS   A O   1 
ATOM   478   C CB  . HIS   A 1 60  ? -5.875  -11.681 59.049  1.00 16.62  ?  60  HIS   A CB  1 
ATOM   479   C CG  . HIS   A 1 60  ? -5.086  -12.410 60.084  1.00 24.05  ?  60  HIS   A CG  1 
ATOM   480   N ND1 . HIS   A 1 60  ? -3.952  -13.131 59.779  1.00 26.14  ?  60  HIS   A ND1 1 
ATOM   481   C CD2 . HIS   A 1 60  ? -5.250  -12.511 61.423  1.00 24.92  ?  60  HIS   A CD2 1 
ATOM   482   C CE1 . HIS   A 1 60  ? -3.456  -13.652 60.888  1.00 30.97  ?  60  HIS   A CE1 1 
ATOM   483   N NE2 . HIS   A 1 60  ? -4.229  -13.295 61.898  1.00 24.13  ?  60  HIS   A NE2 1 
ATOM   484   N N   . GLN   A 1 61  ? -6.889  -9.202  57.283  1.00 15.00  ?  61  GLN   A N   1 
ATOM   485   C CA  . GLN   A 1 61  ? -7.437  -8.668  56.045  1.00 13.29  ?  61  GLN   A CA  1 
ATOM   486   C C   . GLN   A 1 61  ? -6.479  -7.672  55.416  1.00 14.69  ?  61  GLN   A C   1 
ATOM   487   O O   . GLN   A 1 61  ? -6.221  -7.727  54.209  1.00 15.10  ?  61  GLN   A O   1 
ATOM   488   C CB  . GLN   A 1 61  ? -8.788  -8.021  56.310  1.00 12.37  ?  61  GLN   A CB  1 
ATOM   489   C CG  . GLN   A 1 61  ? -9.921  -9.003  56.315  1.00 14.83  ?  61  GLN   A CG  1 
ATOM   490   C CD  . GLN   A 1 61  ? -11.228 -8.337  56.639  1.00 14.97  ?  61  GLN   A CD  1 
ATOM   491   O OE1 . GLN   A 1 61  ? -11.403 -7.836  57.738  1.00 12.74  ?  61  GLN   A OE1 1 
ATOM   492   N NE2 . GLN   A 1 61  ? -12.152 -8.308  55.675  1.00 12.69  ?  61  GLN   A NE2 1 
ATOM   493   N N   . TRP   A 1 62  ? -5.932  -6.758  56.224  1.00 14.05  ?  62  TRP   A N   1 
ATOM   494   C CA  . TRP   A 1 62  ? -4.956  -5.811  55.704  1.00 13.34  ?  62  TRP   A CA  1 
ATOM   495   C C   . TRP   A 1 62  ? -3.711  -6.524  55.197  1.00 16.17  ?  62  TRP   A C   1 
ATOM   496   O O   . TRP   A 1 62  ? -3.176  -6.170  54.137  1.00 14.77  ?  62  TRP   A O   1 
ATOM   497   C CB  . TRP   A 1 62  ? -4.605  -4.777  56.768  1.00 15.81  ?  62  TRP   A CB  1 
ATOM   498   C CG  . TRP   A 1 62  ? -5.622  -3.685  56.847  1.00 22.71  ?  62  TRP   A CG  1 
ATOM   499   C CD1 . TRP   A 1 62  ? -6.721  -3.637  57.664  1.00 22.50  ?  62  TRP   A CD1 1 
ATOM   500   C CD2 . TRP   A 1 62  ? -5.657  -2.488  56.059  1.00 24.09  ?  62  TRP   A CD2 1 
ATOM   501   N NE1 . TRP   A 1 62  ? -7.431  -2.478  57.438  1.00 21.45  ?  62  TRP   A NE1 1 
ATOM   502   C CE2 . TRP   A 1 62  ? -6.796  -1.754  56.461  1.00 25.79  ?  62  TRP   A CE2 1 
ATOM   503   C CE3 . TRP   A 1 62  ? -4.828  -1.957  55.063  1.00 24.95  ?  62  TRP   A CE3 1 
ATOM   504   C CZ2 . TRP   A 1 62  ? -7.131  -0.521  55.891  1.00 26.08  ?  62  TRP   A CZ2 1 
ATOM   505   C CZ3 . TRP   A 1 62  ? -5.164  -0.728  54.500  1.00 25.32  ?  62  TRP   A CZ3 1 
ATOM   506   C CH2 . TRP   A 1 62  ? -6.301  -0.027  54.916  1.00 22.91  ?  62  TRP   A CH2 1 
ATOM   507   N N   . ALA   A 1 63  ? -3.252  -7.556  55.910  1.00 12.32  ?  63  ALA   A N   1 
ATOM   508   C CA  . ALA   A 1 63  ? -2.100  -8.310  55.423  1.00 14.12  ?  63  ALA   A CA  1 
ATOM   509   C C   . ALA   A 1 63  ? -2.400  -8.971  54.081  1.00 11.53  ?  63  ALA   A C   1 
ATOM   510   O O   . ALA   A 1 63  ? -1.522  -9.057  53.213  1.00 13.61  ?  63  ALA   A O   1 
ATOM   511   C CB  . ALA   A 1 63  ? -1.674  -9.352  56.449  1.00 14.89  ?  63  ALA   A CB  1 
ATOM   512   N N   . ALA   A 1 64  ? -3.629  -9.454  53.890  1.00 17.81  ?  64  ALA   A N   1 
ATOM   513   C CA  . ALA   A 1 64  ? -3.991  -10.046 52.598  1.00 15.67  ?  64  ALA   A CA  1 
ATOM   514   C C   . ALA   A 1 64  ? -3.941  -9.013  51.479  1.00 16.12  ?  64  ALA   A C   1 
ATOM   515   O O   . ALA   A 1 64  ? -3.542  -9.321  50.345  1.00 14.81  ?  64  ALA   A O   1 
ATOM   516   C CB  . ALA   A 1 64  ? -5.382  -10.673 52.676  1.00 18.12  ?  64  ALA   A CB  1 
ATOM   517   N N   . MET   A 1 65  ? -4.368  -7.783  51.770  1.00 15.37  ?  65  MET   A N   1 
ATOM   518   C CA  . MET   A 1 65  ? -4.364  -6.747  50.746  1.00 14.90  ?  65  MET   A CA  1 
ATOM   519   C C   . MET   A 1 65  ? -2.949  -6.415  50.308  1.00 15.96  ?  65  MET   A C   1 
ATOM   520   O O   . MET   A 1 65  ? -2.699  -6.170  49.120  1.00 17.66  ?  65  MET   A O   1 
ATOM   521   C CB  . MET   A 1 65  ? -5.058  -5.495  51.272  1.00 12.65  ?  65  MET   A CB  1 
ATOM   522   C CG  . MET   A 1 65  ? -6.546  -5.651  51.466  1.00 18.30  ?  65  MET   A CG  1 
ATOM   523   S SD  . MET   A 1 65  ? -7.256  -4.083  51.969  1.00 25.44  ?  65  MET   A SD  1 
ATOM   524   C CE  . MET   A 1 65  ? -7.650  -3.404  50.397  1.00 16.37  ?  65  MET   A CE  1 
ATOM   525   N N   . ILE   A 1 66  ? -2.008  -6.406  51.258  1.00 15.77  ?  66  ILE   A N   1 
ATOM   526   C CA  . ILE   A 1 66  ? -0.640  -5.984  50.975  1.00 17.16  ?  66  ILE   A CA  1 
ATOM   527   C C   . ILE   A 1 66  ? 0.060   -6.966  50.049  1.00 13.64  ?  66  ILE   A C   1 
ATOM   528   O O   . ILE   A 1 66  ? 0.939   -6.579  49.271  1.00 16.14  ?  66  ILE   A O   1 
ATOM   529   C CB  . ILE   A 1 66  ? 0.137   -5.806  52.293  1.00 18.00  ?  66  ILE   A CB  1 
ATOM   530   C CG1 . ILE   A 1 66  ? -0.529  -4.741  53.153  1.00 21.38  ?  66  ILE   A CG1 1 
ATOM   531   C CG2 . ILE   A 1 66  ? 1.587   -5.439  52.020  1.00 19.50  ?  66  ILE   A CG2 1 
ATOM   532   C CD1 . ILE   A 1 66  ? -0.171  -4.848  54.615  1.00 24.77  ?  66  ILE   A CD1 1 
ATOM   533   N N   . THR   A 1 67  ? -0.296  -8.243  50.108  1.00 12.76  ?  67  THR   A N   1 
ATOM   534   C CA  . THR   A 1 67  ? 0.246   -9.206  49.167  1.00 13.37  ?  67  THR   A CA  1 
ATOM   535   C C   . THR   A 1 67  ? -0.721  -9.502  48.028  1.00 16.30  ?  67  THR   A C   1 
ATOM   536   O O   . THR   A 1 67  ? -0.512  -10.468 47.286  1.00 17.23  ?  67  THR   A O   1 
ATOM   537   C CB  . THR   A 1 67  ? 0.627   -10.490 49.893  1.00 14.88  ?  67  THR   A CB  1 
ATOM   538   O OG1 . THR   A 1 67  ? -0.459  -10.894 50.732  1.00 19.31  ?  67  THR   A OG1 1 
ATOM   539   C CG2 . THR   A 1 67  ? 1.846   -10.257 50.760  1.00 15.99  ?  67  THR   A CG2 1 
ATOM   540   N N   . GLY   A 1 68  ? -1.766  -8.689  47.873  1.00 15.93  ?  68  GLY   A N   1 
ATOM   541   C CA  . GLY   A 1 68  ? -2.722  -8.917  46.804  1.00 13.00  ?  68  GLY   A CA  1 
ATOM   542   C C   . GLY   A 1 68  ? -2.079  -8.848  45.434  1.00 14.45  ?  68  GLY   A C   1 
ATOM   543   O O   . GLY   A 1 68  ? -1.152  -8.077  45.183  1.00 15.67  ?  68  GLY   A O   1 
ATOM   544   N N   . ASP   A 1 69  ? -2.587  -9.672  44.535  1.00 13.75  ?  69  ASP   A N   1 
ATOM   545   C CA  . ASP   A 1 69  ? -2.059  -9.794  43.184  1.00 15.47  ?  69  ASP   A CA  1 
ATOM   546   C C   . ASP   A 1 69  ? -2.904  -8.922  42.261  1.00 18.15  ?  69  ASP   A C   1 
ATOM   547   O O   . ASP   A 1 69  ? -4.085  -9.210  42.031  1.00 17.61  ?  69  ASP   A O   1 
ATOM   548   C CB  . ASP   A 1 69  ? -2.075  -11.257 42.753  1.00 17.54  ?  69  ASP   A CB  1 
ATOM   549   C CG  . ASP   A 1 69  ? -1.612  -11.466 41.328  1.00 17.32  ?  69  ASP   A CG  1 
ATOM   550   O OD1 . ASP   A 1 69  ? -1.158  -10.502 40.668  1.00 18.20  ?  69  ASP   A OD1 1 
ATOM   551   O OD2 . ASP   A 1 69  ? -1.708  -12.622 40.860  1.00 19.46  ?  69  ASP   A OD2 1 
ATOM   552   N N   . GLU   A 1 70  ? -2.291  -7.870  41.722  1.00 15.98  ?  70  GLU   A N   1 
ATOM   553   C CA  . GLU   A 1 70  ? -2.982  -6.865  40.929  1.00 17.21  ?  70  GLU   A CA  1 
ATOM   554   C C   . GLU   A 1 70  ? -3.043  -7.196  39.440  1.00 18.52  ?  70  GLU   A C   1 
ATOM   555   O O   . GLU   A 1 70  ? -3.521  -6.359  38.660  1.00 17.44  ?  70  GLU   A O   1 
ATOM   556   C CB  . GLU   A 1 70  ? -2.318  -5.491  41.124  1.00 17.82  ?  70  GLU   A CB  1 
ATOM   557   C CG  . GLU   A 1 70  ? -2.484  -4.906  42.523  1.00 14.75  ?  70  GLU   A CG  1 
ATOM   558   C CD  . GLU   A 1 70  ? -3.941  -4.764  42.915  1.00 17.63  ?  70  GLU   A CD  1 
ATOM   559   O OE1 . GLU   A 1 70  ? -4.799  -4.671  42.009  1.00 15.93  ?  70  GLU   A OE1 1 
ATOM   560   O OE2 . GLU   A 1 70  ? -4.237  -4.743  44.126  1.00 15.59  ?  70  GLU   A OE2 1 
ATOM   561   N N   . ALA   A 1 71  ? -2.598  -8.392  39.039  1.00 16.22  ?  71  ALA   A N   1 
ATOM   562   C CA  . ALA   A 1 71  ? -2.586  -8.777  37.631  1.00 13.14  ?  71  ALA   A CA  1 
ATOM   563   C C   . ALA   A 1 71  ? -3.939  -8.537  36.975  1.00 13.85  ?  71  ALA   A C   1 
ATOM   564   O O   . ALA   A 1 71  ? -4.998  -8.696  37.590  1.00 19.91  ?  71  ALA   A O   1 
ATOM   565   C CB  . ALA   A 1 71  ? -2.202  -10.249 37.476  1.00 14.09  ?  71  ALA   A CB  1 
ATOM   566   N N   . TYR   A 1 72  ? -3.900  -8.162  35.700  1.00 18.41  ?  72  TYR   A N   1 
ATOM   567   C CA  . TYR   A 1 72  ? -5.140  -7.905  34.982  1.00 19.10  ?  72  TYR   A CA  1 
ATOM   568   C C   . TYR   A 1 72  ? -5.914  -9.193  34.742  1.00 17.71  ?  72  TYR   A C   1 
ATOM   569   O O   . TYR   A 1 72  ? -7.145  -9.218  34.869  1.00 19.66  ?  72  TYR   A O   1 
ATOM   570   C CB  . TYR   A 1 72  ? -4.852  -7.200  33.660  1.00 20.27  ?  72  TYR   A CB  1 
ATOM   571   C CG  . TYR   A 1 72  ? -6.098  -6.576  33.080  1.00 24.02  ?  72  TYR   A CG  1 
ATOM   572   C CD1 . TYR   A 1 72  ? -6.935  -7.302  32.241  1.00 20.88  ?  72  TYR   A CD1 1 
ATOM   573   C CD2 . TYR   A 1 72  ? -6.463  -5.274  33.407  1.00 21.34  ?  72  TYR   A CD2 1 
ATOM   574   C CE1 . TYR   A 1 72  ? -8.089  -6.742  31.729  1.00 23.79  ?  72  TYR   A CE1 1 
ATOM   575   C CE2 . TYR   A 1 72  ? -7.617  -4.706  32.896  1.00 22.66  ?  72  TYR   A CE2 1 
ATOM   576   C CZ  . TYR   A 1 72  ? -8.427  -5.446  32.062  1.00 23.04  ?  72  TYR   A CZ  1 
ATOM   577   O OH  . TYR   A 1 72  ? -9.584  -4.894  31.552  1.00 32.94  ?  72  TYR   A OH  1 
ATOM   578   N N   . ALA   A 1 73  ? -5.215  -10.271 34.396  1.00 19.27  ?  73  ALA   A N   1 
ATOM   579   C CA  . ALA   A 1 73  ? -5.845  -11.552 34.103  1.00 18.16  ?  73  ALA   A CA  1 
ATOM   580   C C   . ALA   A 1 73  ? -5.212  -12.632 34.964  1.00 18.71  ?  73  ALA   A C   1 
ATOM   581   O O   . ALA   A 1 73  ? -3.983  -12.719 35.050  1.00 18.55  ?  73  ALA   A O   1 
ATOM   582   C CB  . ALA   A 1 73  ? -5.695  -11.905 32.623  1.00 15.51  ?  73  ALA   A CB  1 
ATOM   583   N N   . GLY   A 1 74  ? -6.044  -13.448 35.604  1.00 15.84  ?  74  GLY   A N   1 
ATOM   584   C CA  . GLY   A 1 74  ? -5.533  -14.589 36.337  1.00 19.91  ?  74  GLY   A CA  1 
ATOM   585   C C   . GLY   A 1 74  ? -4.919  -14.279 37.684  1.00 18.69  ?  74  GLY   A C   1 
ATOM   586   O O   . GLY   A 1 74  ? -4.016  -14.996 38.124  1.00 18.50  ?  74  GLY   A O   1 
ATOM   587   N N   . SER   A 1 75  ? -5.383  -13.234 38.358  1.00 16.91  ?  75  SER   A N   1 
ATOM   588   C CA  . SER   A 1 75  ? -4.857  -12.912 39.675  1.00 16.38  ?  75  SER   A CA  1 
ATOM   589   C C   . SER   A 1 75  ? -4.962  -14.118 40.601  1.00 20.05  ?  75  SER   A C   1 
ATOM   590   O O   . SER   A 1 75  ? -5.951  -14.855 40.586  1.00 19.11  ?  75  SER   A O   1 
ATOM   591   C CB  . SER   A 1 75  ? -5.613  -11.719 40.262  1.00 18.73  ?  75  SER   A CB  1 
ATOM   592   O OG  . SER   A 1 75  ? -5.490  -11.677 41.679  1.00 21.11  ?  75  SER   A OG  1 
ATOM   593   N N   . ARG   A 1 76  ? -3.913  -14.328 41.394  1.00 19.15  ?  76  ARG   A N   1 
ATOM   594   C CA  A ARG   A 1 76  ? -3.898  -15.422 42.359  0.56 19.17  ?  76  ARG   A CA  1 
ATOM   595   C CA  B ARG   A 1 76  ? -3.926  -15.450 42.322  0.44 18.65  ?  76  ARG   A CA  1 
ATOM   596   C C   . ARG   A 1 76  ? -5.114  -15.376 43.276  1.00 19.54  ?  76  ARG   A C   1 
ATOM   597   O O   . ARG   A 1 76  ? -5.640  -16.419 43.682  1.00 20.76  ?  76  ARG   A O   1 
ATOM   598   C CB  A ARG   A 1 76  ? -2.598  -15.349 43.169  0.56 22.12  ?  76  ARG   A CB  1 
ATOM   599   C CB  B ARG   A 1 76  ? -2.602  -15.516 43.090  0.44 22.10  ?  76  ARG   A CB  1 
ATOM   600   C CG  A ARG   A 1 76  ? -2.390  -16.443 44.198  0.56 21.83  ?  76  ARG   A CG  1 
ATOM   601   C CG  B ARG   A 1 76  ? -2.430  -14.461 44.168  0.44 22.67  ?  76  ARG   A CG  1 
ATOM   602   C CD  A ARG   A 1 76  ? -1.177  -16.132 45.075  0.56 20.96  ?  76  ARG   A CD  1 
ATOM   603   C CD  B ARG   A 1 76  ? -1.037  -14.510 44.787  0.44 21.30  ?  76  ARG   A CD  1 
ATOM   604   N NE  A ARG   A 1 76  ? -1.453  -15.098 46.071  0.56 22.25  ?  76  ARG   A NE  1 
ATOM   605   N NE  B ARG   A 1 76  ? -0.105  -13.623 44.102  0.44 20.14  ?  76  ARG   A NE  1 
ATOM   606   C CZ  A ARG   A 1 76  ? -0.999  -13.851 46.018  0.56 19.17  ?  76  ARG   A CZ  1 
ATOM   607   C CZ  B ARG   A 1 76  ? 0.661   -13.982 43.083  0.44 19.58  ?  76  ARG   A CZ  1 
ATOM   608   N NH1 A ARG   A 1 76  ? -0.224  -13.437 45.029  0.56 19.56  ?  76  ARG   A NH1 1 
ATOM   609   N NH1 B ARG   A 1 76  ? 0.642   -15.217 42.607  0.44 18.17  ?  76  ARG   A NH1 1 
ATOM   610   N NH2 A ARG   A 1 76  ? -1.325  -13.001 46.986  0.56 18.21  ?  76  ARG   A NH2 1 
ATOM   611   N NH2 B ARG   A 1 76  ? 1.465   -13.080 42.528  0.44 20.22  ?  76  ARG   A NH2 1 
ATOM   612   N N   . ASN   A 1 77  ? -5.582  -14.174 43.613  1.00 15.19  ?  77  ASN   A N   1 
ATOM   613   C CA  . ASN   A 1 77  ? -6.705  -14.043 44.529  1.00 17.36  ?  77  ASN   A CA  1 
ATOM   614   C C   . ASN   A 1 77  ? -8.048  -14.345 43.881  1.00 17.38  ?  77  ASN   A C   1 
ATOM   615   O O   . ASN   A 1 77  ? -9.013  -14.629 44.603  1.00 15.52  ?  77  ASN   A O   1 
ATOM   616   C CB  . ASN   A 1 77  ? -6.711  -12.637 45.123  1.00 17.97  ?  77  ASN   A CB  1 
ATOM   617   C CG  . ASN   A 1 77  ? -5.348  -12.240 45.649  1.00 18.58  ?  77  ASN   A CG  1 
ATOM   618   O OD1 . ASN   A 1 77  ? -4.564  -11.593 44.952  1.00 17.32  ?  77  ASN   A OD1 1 
ATOM   619   N ND2 . ASN   A 1 77  ? -5.041  -12.665 46.869  1.00 15.26  ?  77  ASN   A ND2 1 
ATOM   620   N N   . TYR   A 1 78  ? -8.145  -14.266 42.550  1.00 16.60  ?  78  TYR   A N   1 
ATOM   621   C CA  . TYR   A 1 78  ? -9.360  -14.728 41.888  1.00 14.80  ?  78  TYR   A CA  1 
ATOM   622   C C   . TYR   A 1 78  ? -9.556  -16.216 42.133  1.00 14.82  ?  78  TYR   A C   1 
ATOM   623   O O   . TYR   A 1 78  ? -10.639 -16.661 42.529  1.00 19.43  ?  78  TYR   A O   1 
ATOM   624   C CB  . TYR   A 1 78  ? -9.301  -14.426 40.387  1.00 15.48  ?  78  TYR   A CB  1 
ATOM   625   C CG  . TYR   A 1 78  ? -10.309 -15.225 39.583  1.00 17.41  ?  78  TYR   A CG  1 
ATOM   626   C CD1 . TYR   A 1 78  ? -11.658 -14.889 39.593  1.00 15.13  ?  78  TYR   A CD1 1 
ATOM   627   C CD2 . TYR   A 1 78  ? -9.914  -16.328 38.836  1.00 17.61  ?  78  TYR   A CD2 1 
ATOM   628   C CE1 . TYR   A 1 78  ? -12.583 -15.627 38.875  1.00 14.34  ?  78  TYR   A CE1 1 
ATOM   629   C CE2 . TYR   A 1 78  ? -10.836 -17.066 38.107  1.00 16.87  ?  78  TYR   A CE2 1 
ATOM   630   C CZ  . TYR   A 1 78  ? -12.162 -16.711 38.137  1.00 15.66  ?  78  TYR   A CZ  1 
ATOM   631   O OH  . TYR   A 1 78  ? -13.071 -17.446 37.424  1.00 19.98  ?  78  TYR   A OH  1 
ATOM   632   N N   . TYR   A 1 79  ? -8.499  -17.000 41.927  1.00 17.20  ?  79  TYR   A N   1 
ATOM   633   C CA  . TYR   A 1 79  ? -8.587  -18.437 42.155  1.00 16.04  ?  79  TYR   A CA  1 
ATOM   634   C C   . TYR   A 1 79  ? -8.863  -18.753 43.622  1.00 19.40  ?  79  TYR   A C   1 
ATOM   635   O O   . TYR   A 1 79  ? -9.626  -19.679 43.924  1.00 18.69  ?  79  TYR   A O   1 
ATOM   636   C CB  . TYR   A 1 79  ? -7.304  -19.109 41.669  1.00 14.02  ?  79  TYR   A CB  1 
ATOM   637   C CG  . TYR   A 1 79  ? -7.067  -18.901 40.192  1.00 19.88  ?  79  TYR   A CG  1 
ATOM   638   C CD1 . TYR   A 1 79  ? -7.821  -19.591 39.249  1.00 22.34  ?  79  TYR   A CD1 1 
ATOM   639   C CD2 . TYR   A 1 79  ? -6.106  -18.006 39.731  1.00 21.15  ?  79  TYR   A CD2 1 
ATOM   640   C CE1 . TYR   A 1 79  ? -7.624  -19.402 37.884  1.00 17.26  ?  79  TYR   A CE1 1 
ATOM   641   C CE2 . TYR   A 1 79  ? -5.902  -17.817 38.359  1.00 23.49  ?  79  TYR   A CE2 1 
ATOM   642   C CZ  . TYR   A 1 79  ? -6.670  -18.523 37.451  1.00 19.54  ?  79  TYR   A CZ  1 
ATOM   643   O OH  . TYR   A 1 79  ? -6.496  -18.357 36.099  1.00 29.51  ?  79  TYR   A OH  1 
ATOM   644   N N   . ASP   A 1 80  ? -8.257  -17.992 44.547  1.00 15.58  ?  80  ASP   A N   1 
ATOM   645   C CA  . ASP   A 1 80  ? -8.564  -18.142 45.969  1.00 15.56  ?  80  ASP   A CA  1 
ATOM   646   C C   . ASP   A 1 80  ? -10.039 -17.873 46.247  1.00 18.70  ?  80  ASP   A C   1 
ATOM   647   O O   . ASP   A 1 80  ? -10.670 -18.576 47.045  1.00 15.73  ?  80  ASP   A O   1 
ATOM   648   C CB  . ASP   A 1 80  ? -7.705  -17.192 46.809  1.00 19.88  ?  80  ASP   A CB  1 
ATOM   649   C CG  . ASP   A 1 80  ? -6.258  -17.638 46.922  1.00 21.56  ?  80  ASP   A CG  1 
ATOM   650   O OD1 . ASP   A 1 80  ? -5.903  -18.694 46.358  1.00 26.44  ?  80  ASP   A OD1 1 
ATOM   651   O OD2 . ASP   A 1 80  ? -5.470  -16.930 47.592  1.00 26.75  ?  80  ASP   A OD2 1 
ATOM   652   N N   . LEU   A 1 81  ? -10.592 -16.833 45.620  1.00 19.59  ?  81  LEU   A N   1 
ATOM   653   C CA  . LEU   A 1 81  ? -12.009 -16.517 45.782  1.00 18.71  ?  81  LEU   A CA  1 
ATOM   654   C C   . LEU   A 1 81  ? -12.891 -17.621 45.209  1.00 18.37  ?  81  LEU   A C   1 
ATOM   655   O O   . LEU   A 1 81  ? -13.923 -17.975 45.795  1.00 19.22  ?  81  LEU   A O   1 
ATOM   656   C CB  . LEU   A 1 81  ? -12.310 -15.177 45.107  1.00 13.68  ?  81  LEU   A CB  1 
ATOM   657   C CG  . LEU   A 1 81  ? -13.688 -14.569 45.365  1.00 13.66  ?  81  LEU   A CG  1 
ATOM   658   C CD1 . LEU   A 1 81  ? -14.025 -14.550 46.844  1.00 14.98  ?  81  LEU   A CD1 1 
ATOM   659   C CD2 . LEU   A 1 81  ? -13.759 -13.163 44.776  1.00 16.19  ?  81  LEU   A CD2 1 
ATOM   660   N N   . LYS   A 1 82  ? -12.499 -18.175 44.063  1.00 17.58  ?  82  LYS   A N   1 
ATOM   661   C CA  . LYS   A 1 82  ? -13.264 -19.256 43.455  1.00 19.82  ?  82  LYS   A CA  1 
ATOM   662   C C   . LYS   A 1 82  ? -13.314 -20.466 44.375  1.00 20.13  ?  82  LYS   A C   1 
ATOM   663   O O   . LYS   A 1 82  ? -14.381 -21.051 44.602  1.00 20.95  ?  82  LYS   A O   1 
ATOM   664   C CB  . LYS   A 1 82  ? -12.645 -19.615 42.107  1.00 19.09  ?  82  LYS   A CB  1 
ATOM   665   C CG  . LYS   A 1 82  ? -13.407 -20.635 41.302  1.00 19.34  ?  82  LYS   A CG  1 
ATOM   666   C CD  . LYS   A 1 82  ? -12.782 -20.754 39.925  1.00 22.37  ?  82  LYS   A CD  1 
ATOM   667   C CE  . LYS   A 1 82  ? -12.551 -22.204 39.541  1.00 24.89  ?  82  LYS   A CE  1 
ATOM   668   N NZ  . LYS   A 1 82  ? -13.808 -22.965 39.425  1.00 22.02  ?  82  LYS   A NZ  1 
ATOM   669   N N   . ASP   A 1 83  ? -12.164 -20.848 44.925  1.00 19.77  ?  83  ASP   A N   1 
ATOM   670   C CA  . ASP   A 1 83  ? -12.126 -21.952 45.875  1.00 20.34  ?  83  ASP   A CA  1 
ATOM   671   C C   . ASP   A 1 83  ? -12.971 -21.655 47.101  1.00 18.65  ?  83  ASP   A C   1 
ATOM   672   O O   . ASP   A 1 83  ? -13.684 -22.535 47.600  1.00 22.12  ?  83  ASP   A O   1 
ATOM   673   C CB  . ASP   A 1 83  ? -10.685 -22.241 46.281  1.00 20.69  ?  83  ASP   A CB  1 
ATOM   674   C CG  . ASP   A 1 83  ? -9.816  -22.618 45.102  1.00 26.38  ?  83  ASP   A CG  1 
ATOM   675   O OD1 . ASP   A 1 83  ? -10.374 -23.029 44.059  1.00 26.44  ?  83  ASP   A OD1 1 
ATOM   676   O OD2 . ASP   A 1 83  ? -8.574  -22.505 45.218  1.00 31.06  ?  83  ASP   A OD2 1 
ATOM   677   N N   . LYS   A 1 84  ? -12.912 -20.421 47.603  1.00 17.67  ?  84  LYS   A N   1 
ATOM   678   C CA  . LYS   A 1 84  ? -13.668 -20.095 48.809  1.00 19.59  ?  84  LYS   A CA  1 
ATOM   679   C C   . LYS   A 1 84  ? -15.164 -20.206 48.557  1.00 21.60  ?  84  LYS   A C   1 
ATOM   680   O O   . LYS   A 1 84  ? -15.916 -20.690 49.417  1.00 24.34  ?  84  LYS   A O   1 
ATOM   681   C CB  . LYS   A 1 84  ? -13.304 -18.695 49.299  1.00 16.42  ?  84  LYS   A CB  1 
ATOM   682   C CG  . LYS   A 1 84  ? -13.780 -18.388 50.689  1.00 18.49  ?  84  LYS   A CG  1 
ATOM   683   C CD  . LYS   A 1 84  ? -13.059 -19.263 51.705  1.00 22.59  ?  84  LYS   A CD  1 
ATOM   684   C CE  . LYS   A 1 84  ? -13.507 -18.942 53.119  1.00 26.14  ?  84  LYS   A CE  1 
ATOM   685   N NZ  . LYS   A 1 84  ? -12.783 -19.751 54.144  1.00 29.75  ?  84  LYS   A NZ  1 
ATOM   686   N N   . ALA   A 1 85  ? -15.616 -19.770 47.379  1.00 19.33  ?  85  ALA   A N   1 
ATOM   687   C CA  . ALA   A 1 85  ? -17.025 -19.900 47.046  1.00 13.31  ?  85  ALA   A CA  1 
ATOM   688   C C   . ALA   A 1 85  ? -17.416 -21.360 46.902  1.00 18.89  ?  85  ALA   A C   1 
ATOM   689   O O   . ALA   A 1 85  ? -18.511 -21.759 47.311  1.00 20.46  ?  85  ALA   A O   1 
ATOM   690   C CB  . ALA   A 1 85  ? -17.338 -19.131 45.770  1.00 16.23  ?  85  ALA   A CB  1 
ATOM   691   N N   . LYS   A 1 86  ? -16.536 -22.175 46.321  1.00 20.16  ?  86  LYS   A N   1 
ATOM   692   C CA  . LYS   A 1 86  ? -16.799 -23.608 46.281  1.00 21.01  ?  86  LYS   A CA  1 
ATOM   693   C C   . LYS   A 1 86  ? -16.878 -24.181 47.688  1.00 24.24  ?  86  LYS   A C   1 
ATOM   694   O O   . LYS   A 1 86  ? -17.712 -25.051 47.970  1.00 25.77  ?  86  LYS   A O   1 
ATOM   695   C CB  . LYS   A 1 86  ? -15.713 -24.324 45.485  1.00 23.59  ?  86  LYS   A CB  1 
ATOM   696   C CG  . LYS   A 1 86  ? -15.896 -25.825 45.443  1.00 24.79  ?  86  LYS   A CG  1 
ATOM   697   C CD  . LYS   A 1 86  ? -17.235 -26.151 44.816  1.00 29.80  ?  86  LYS   A CD  1 
ATOM   698   C CE  . LYS   A 1 86  ? -17.359 -27.603 44.461  1.00 25.68  ?  86  LYS   A CE  1 
ATOM   699   N NZ  . LYS   A 1 86  ? -18.767 -27.905 44.102  1.00 26.14  ?  86  LYS   A NZ  1 
ATOM   700   N N   . GLU   A 1 87  ? -16.018 -23.700 48.587  1.00 21.81  ?  87  GLU   A N   1 
ATOM   701   C CA  . GLU   A 1 87  ? -16.004 -24.214 49.951  1.00 20.25  ?  87  GLU   A CA  1 
ATOM   702   C C   . GLU   A 1 87  ? -17.279 -23.839 50.697  1.00 24.44  ?  87  GLU   A C   1 
ATOM   703   O O   . GLU   A 1 87  ? -17.907 -24.687 51.343  1.00 27.46  ?  87  GLU   A O   1 
ATOM   704   C CB  . GLU   A 1 87  ? -14.782 -23.689 50.695  1.00 22.17  ?  87  GLU   A CB  1 
ATOM   705   C CG  . GLU   A 1 87  ? -14.875 -23.900 52.197  1.00 28.74  ?  87  GLU   A CG  1 
ATOM   706   C CD  . GLU   A 1 87  ? -13.957 -22.982 52.989  1.00 31.45  ?  87  GLU   A CD  1 
ATOM   707   O OE1 . GLU   A 1 87  ? -12.963 -22.475 52.419  1.00 31.63  ?  87  GLU   A OE1 1 
ATOM   708   O OE2 . GLU   A 1 87  ? -14.241 -22.767 54.189  1.00 33.17  ?  87  GLU   A OE2 1 
ATOM   709   N N   . LEU   A 1 88  ? -17.679 -22.568 50.622  1.00 22.08  ?  88  LEU   A N   1 
ATOM   710   C CA  . LEU   A 1 88  ? -18.784 -22.091 51.443  1.00 20.38  ?  88  LEU   A CA  1 
ATOM   711   C C   . LEU   A 1 88  ? -20.137 -22.522 50.899  1.00 22.64  ?  88  LEU   A C   1 
ATOM   712   O O   . LEU   A 1 88  ? -21.012 -22.936 51.669  1.00 17.21  ?  88  LEU   A O   1 
ATOM   713   C CB  . LEU   A 1 88  ? -18.739 -20.570 51.546  1.00 22.95  ?  88  LEU   A CB  1 
ATOM   714   C CG  . LEU   A 1 88  ? -17.676 -19.980 52.459  1.00 24.45  ?  88  LEU   A CG  1 
ATOM   715   C CD1 . LEU   A 1 88  ? -17.660 -18.474 52.287  1.00 19.10  ?  88  LEU   A CD1 1 
ATOM   716   C CD2 . LEU   A 1 88  ? -17.970 -20.373 53.903  1.00 27.13  ?  88  LEU   A CD2 1 
ATOM   717   N N   . PHE   A 1 89  ? -20.336 -22.405 49.585  1.00 22.95  ?  89  PHE   A N   1 
ATOM   718   C CA  . PHE   A 1 89  ? -21.655 -22.539 48.984  1.00 26.00  ?  89  PHE   A CA  1 
ATOM   719   C C   . PHE   A 1 89  ? -21.808 -23.775 48.121  1.00 24.52  ?  89  PHE   A C   1 
ATOM   720   O O   . PHE   A 1 89  ? -22.942 -24.104 47.747  1.00 21.56  ?  89  PHE   A O   1 
ATOM   721   C CB  . PHE   A 1 89  ? -21.982 -21.305 48.131  1.00 20.61  ?  89  PHE   A CB  1 
ATOM   722   C CG  . PHE   A 1 89  ? -21.641 -20.015 48.799  1.00 21.86  ?  89  PHE   A CG  1 
ATOM   723   C CD1 . PHE   A 1 89  ? -22.285 -19.635 49.966  1.00 21.52  ?  89  PHE   A CD1 1 
ATOM   724   C CD2 . PHE   A 1 89  ? -20.679 -19.175 48.261  1.00 19.87  ?  89  PHE   A CD2 1 
ATOM   725   C CE1 . PHE   A 1 89  ? -21.968 -18.438 50.590  1.00 21.61  ?  89  PHE   A CE1 1 
ATOM   726   C CE2 . PHE   A 1 89  ? -20.362 -17.981 48.875  1.00 18.55  ?  89  PHE   A CE2 1 
ATOM   727   C CZ  . PHE   A 1 89  ? -21.001 -17.612 50.040  1.00 18.30  ?  89  PHE   A CZ  1 
ATOM   728   N N   . ASN   A 1 90  ? -20.707 -24.456 47.797  1.00 20.48  ?  90  ASN   A N   1 
ATOM   729   C CA  . ASN   A 1 90  ? -20.707 -25.588 46.881  1.00 22.55  ?  90  ASN   A CA  1 
ATOM   730   C C   . ASN   A 1 90  ? -21.039 -25.146 45.464  1.00 26.15  ?  90  ASN   A C   1 
ATOM   731   O O   . ASN   A 1 90  ? -21.576 -25.924 44.671  1.00 32.84  ?  90  ASN   A O   1 
ATOM   732   C CB  . ASN   A 1 90  ? -21.670 -26.685 47.354  1.00 28.65  ?  90  ASN   A CB  1 
ATOM   733   C CG  . ASN   A 1 90  ? -21.272 -28.060 46.877  1.00 30.13  ?  90  ASN   A CG  1 
ATOM   734   O OD1 . ASN   A 1 90  ? -20.146 -28.275 46.429  1.00 28.72  ?  90  ASN   A OD1 1 
ATOM   735   N ND2 . ASN   A 1 90  ? -22.203 -29.009 46.975  1.00 26.75  ?  90  ASN   A ND2 1 
ATOM   736   N N   . TYR   A 1 91  ? -20.725 -23.892 45.139  1.00 21.75  ?  91  TYR   A N   1 
ATOM   737   C CA  . TYR   A 1 91  ? -20.984 -23.332 43.823  1.00 22.31  ?  91  TYR   A CA  1 
ATOM   738   C C   . TYR   A 1 91  ? -19.696 -23.350 43.013  1.00 22.34  ?  91  TYR   A C   1 
ATOM   739   O O   . TYR   A 1 91  ? -18.617 -23.055 43.536  1.00 19.73  ?  91  TYR   A O   1 
ATOM   740   C CB  . TYR   A 1 91  ? -21.532 -21.904 43.915  1.00 22.97  ?  91  TYR   A CB  1 
ATOM   741   C CG  . TYR   A 1 91  ? -22.946 -21.788 44.462  1.00 24.80  ?  91  TYR   A CG  1 
ATOM   742   C CD1 . TYR   A 1 91  ? -23.592 -22.883 45.027  1.00 20.36  ?  91  TYR   A CD1 1 
ATOM   743   C CD2 . TYR   A 1 91  ? -23.638 -20.579 44.408  1.00 23.39  ?  91  TYR   A CD2 1 
ATOM   744   C CE1 . TYR   A 1 91  ? -24.874 -22.782 45.530  1.00 22.37  ?  91  TYR   A CE1 1 
ATOM   745   C CE2 . TYR   A 1 91  ? -24.938 -20.470 44.914  1.00 21.64  ?  91  TYR   A CE2 1 
ATOM   746   C CZ  . TYR   A 1 91  ? -25.547 -21.577 45.474  1.00 21.30  ?  91  TYR   A CZ  1 
ATOM   747   O OH  . TYR   A 1 91  ? -26.832 -21.490 45.986  1.00 20.98  ?  91  TYR   A OH  1 
ATOM   748   N N   . ASP   A 1 92  ? -19.824 -23.695 41.731  1.00 24.46  ?  92  ASP   A N   1 
ATOM   749   C CA  . ASP   A 1 92  ? -18.696 -23.979 40.851  1.00 24.41  ?  92  ASP   A CA  1 
ATOM   750   C C   . ASP   A 1 92  ? -18.225 -22.782 40.033  1.00 25.44  ?  92  ASP   A C   1 
ATOM   751   O O   . ASP   A 1 92  ? -17.206 -22.894 39.347  1.00 28.28  ?  92  ASP   A O   1 
ATOM   752   C CB  . ASP   A 1 92  ? -19.063 -25.103 39.873  1.00 24.85  ?  92  ASP   A CB  1 
ATOM   753   C CG  . ASP   A 1 92  ? -19.243 -26.438 40.553  1.00 28.75  ?  92  ASP   A CG  1 
ATOM   754   O OD1 . ASP   A 1 92  ? -18.523 -26.714 41.534  1.00 30.60  ?  92  ASP   A OD1 1 
ATOM   755   O OD2 . ASP   A 1 92  ? -20.108 -27.217 40.103  1.00 33.14  ?  92  ASP   A OD2 1 
ATOM   756   N N   . TYR   A 1 93  ? -18.942 -21.664 40.046  1.00 24.49  ?  93  TYR   A N   1 
ATOM   757   C CA  . TYR   A 1 93  ? -18.617 -20.555 39.164  1.00 21.92  ?  93  TYR   A CA  1 
ATOM   758   C C   . TYR   A 1 93  ? -18.705 -19.248 39.930  1.00 23.42  ?  93  TYR   A C   1 
ATOM   759   O O   . TYR   A 1 93  ? -19.651 -19.037 40.692  1.00 23.37  ?  93  TYR   A O   1 
ATOM   760   C CB  . TYR   A 1 93  ? -19.558 -20.506 37.966  1.00 25.79  ?  93  TYR   A CB  1 
ATOM   761   C CG  . TYR   A 1 93  ? -19.559 -21.760 37.125  1.00 29.06  ?  93  TYR   A CG  1 
ATOM   762   C CD1 . TYR   A 1 93  ? -18.459 -22.091 36.347  1.00 32.59  ?  93  TYR   A CD1 1 
ATOM   763   C CD2 . TYR   A 1 93  ? -20.665 -22.602 37.090  1.00 28.74  ?  93  TYR   A CD2 1 
ATOM   764   C CE1 . TYR   A 1 93  ? -18.447 -23.232 35.564  1.00 32.62  ?  93  TYR   A CE1 1 
ATOM   765   C CE2 . TYR   A 1 93  ? -20.661 -23.750 36.308  1.00 32.42  ?  93  TYR   A CE2 1 
ATOM   766   C CZ  . TYR   A 1 93  ? -19.545 -24.059 35.550  1.00 33.35  ?  93  TYR   A CZ  1 
ATOM   767   O OH  . TYR   A 1 93  ? -19.515 -25.188 34.764  1.00 39.60  ?  93  TYR   A OH  1 
ATOM   768   N N   . ILE   A 1 94  ? -17.722 -18.370 39.724  1.00 21.32  ?  94  ILE   A N   1 
ATOM   769   C CA  . ILE   A 1 94  ? -17.717 -17.053 40.351  1.00 22.06  ?  94  ILE   A CA  1 
ATOM   770   C C   . ILE   A 1 94  ? -17.414 -15.979 39.314  1.00 21.73  ?  94  ILE   A C   1 
ATOM   771   O O   . ILE   A 1 94  ? -16.706 -16.213 38.328  1.00 19.39  ?  94  ILE   A O   1 
ATOM   772   C CB  . ILE   A 1 94  ? -16.715 -16.961 41.531  1.00 19.88  ?  94  ILE   A CB  1 
ATOM   773   C CG1 . ILE   A 1 94  ? -15.269 -17.107 41.058  1.00 17.93  ?  94  ILE   A CG1 1 
ATOM   774   C CG2 . ILE   A 1 94  ? -17.039 -18.005 42.562  1.00 22.59  ?  94  ILE   A CG2 1 
ATOM   775   C CD1 . ILE   A 1 94  ? -14.298 -16.309 41.913  1.00 18.79  ?  94  ILE   A CD1 1 
ATOM   776   N N   . ILE   A 1 95  ? -17.999 -14.800 39.532  1.00 18.90  ?  95  ILE   A N   1 
ATOM   777   C CA  . ILE   A 1 95  ? -17.628 -13.584 38.825  1.00 17.76  ?  95  ILE   A CA  1 
ATOM   778   C C   . ILE   A 1 95  ? -17.566 -12.490 39.882  1.00 23.40  ?  95  ILE   A C   1 
ATOM   779   O O   . ILE   A 1 95  ? -18.577 -12.204 40.531  1.00 23.91  ?  95  ILE   A O   1 
ATOM   780   C CB  . ILE   A 1 95  ? -18.631 -13.199 37.724  1.00 19.33  ?  95  ILE   A CB  1 
ATOM   781   C CG1 . ILE   A 1 95  ? -18.928 -14.380 36.807  1.00 19.76  ?  95  ILE   A CG1 1 
ATOM   782   C CG2 . ILE   A 1 95  ? -18.102 -12.035 36.905  1.00 16.27  ?  95  ILE   A CG2 1 
ATOM   783   C CD1 . ILE   A 1 95  ? -20.102 -14.121 35.901  1.00 23.50  ?  95  ILE   A CD1 1 
ATOM   784   N N   . PRO   A 1 96  ? -16.411 -11.881 40.133  1.00 18.02  ?  96  PRO   A N   1 
ATOM   785   C CA  . PRO   A 1 96  ? -16.367 -10.777 41.092  1.00 14.23  ?  96  PRO   A CA  1 
ATOM   786   C C   . PRO   A 1 96  ? -17.044 -9.542  40.518  1.00 17.45  ?  96  PRO   A C   1 
ATOM   787   O O   . PRO   A 1 96  ? -17.202 -9.383  39.307  1.00 15.98  ?  96  PRO   A O   1 
ATOM   788   C CB  . PRO   A 1 96  ? -14.867 -10.550 41.316  1.00 16.88  ?  96  PRO   A CB  1 
ATOM   789   C CG  . PRO   A 1 96  ? -14.206 -11.133 40.123  1.00 16.69  ?  96  PRO   A CG  1 
ATOM   790   C CD  . PRO   A 1 96  ? -15.069 -12.258 39.643  1.00 18.23  ?  96  PRO   A CD  1 
ATOM   791   N N   . ALA   A 1 97  ? -17.480 -8.671  41.423  1.00 19.47  ?  97  ALA   A N   1 
ATOM   792   C CA  . ALA   A 1 97  ? -18.130 -7.429  41.045  1.00 18.43  ?  97  ALA   A CA  1 
ATOM   793   C C   . ALA   A 1 97  ? -17.653 -6.352  42.001  1.00 19.00  ?  97  ALA   A C   1 
ATOM   794   O O   . ALA   A 1 97  ? -17.191 -6.648  43.105  1.00 21.44  ?  97  ALA   A O   1 
ATOM   795   C CB  . ALA   A 1 97  ? -19.660 -7.552  41.078  1.00 21.72  ?  97  ALA   A CB  1 
ATOM   796   N N   . HIS   A 1 98  ? -17.736 -5.091  41.570  1.00 15.81  ?  98  HIS   A N   1 
ATOM   797   C CA  . HIS   A 1 98  ? -17.195 -4.051  42.435  1.00 13.53  ?  98  HIS   A CA  1 
ATOM   798   C C   . HIS   A 1 98  ? -18.062 -3.867  43.672  1.00 16.57  ?  98  HIS   A C   1 
ATOM   799   O O   . HIS   A 1 98  ? -17.547 -3.484  44.727  1.00 16.05  ?  98  HIS   A O   1 
ATOM   800   C CB  . HIS   A 1 98  ? -17.007 -2.741  41.664  1.00 16.58  ?  98  HIS   A CB  1 
ATOM   801   C CG  . HIS   A 1 98  ? -18.269 -1.966  41.444  1.00 20.36  ?  98  HIS   A CG  1 
ATOM   802   N ND1 . HIS   A 1 98  ? -19.116 -2.206  40.384  1.00 21.31  ?  98  HIS   A ND1 1 
ATOM   803   C CD2 . HIS   A 1 98  ? -18.811 -0.936  42.134  1.00 20.35  ?  98  HIS   A CD2 1 
ATOM   804   C CE1 . HIS   A 1 98  ? -20.136 -1.368  40.440  1.00 23.11  ?  98  HIS   A CE1 1 
ATOM   805   N NE2 . HIS   A 1 98  ? -19.976 -0.588  41.494  1.00 21.32  ?  98  HIS   A NE2 1 
ATOM   806   N N   . GLN   A 1 99  ? -19.352 -4.183  43.588  1.00 16.11  ?  99  GLN   A N   1 
ATOM   807   C CA  . GLN   A 1 99  ? -20.193 -4.265  44.783  1.00 16.05  ?  99  GLN   A CA  1 
ATOM   808   C C   . GLN   A 1 99  ? -21.524 -4.907  44.406  1.00 17.33  ?  99  GLN   A C   1 
ATOM   809   O O   . GLN   A 1 99  ? -21.674 -5.466  43.313  1.00 15.36  ?  99  GLN   A O   1 
ATOM   810   C CB  . GLN   A 1 99  ? -20.374 -2.896  45.443  1.00 16.79  ?  99  GLN   A CB  1 
ATOM   811   C CG  . GLN   A 1 99  ? -21.056 -1.832  44.613  1.00 17.87  ?  99  GLN   A CG  1 
ATOM   812   C CD  . GLN   A 1 99  ? -21.109 -0.528  45.383  1.00 20.48  ?  99  GLN   A CD  1 
ATOM   813   O OE1 . GLN   A 1 99  ? -20.082 0.102   45.615  1.00 22.40  ?  99  GLN   A OE1 1 
ATOM   814   N NE2 . GLN   A 1 99  ? -22.296 -0.146  45.828  1.00 24.06  ?  99  GLN   A NE2 1 
ATOM   815   N N   . GLY   A 1 100 ? -22.497 -4.815  45.320  1.00 16.15  ?  100 GLY   A N   1 
ATOM   816   C CA  . GLY   A 1 100 ? -23.713 -5.611  45.190  1.00 17.92  ?  100 GLY   A CA  1 
ATOM   817   C C   . GLY   A 1 100 ? -24.528 -5.271  43.955  1.00 18.11  ?  100 GLY   A C   1 
ATOM   818   O O   . GLY   A 1 100 ? -24.982 -6.161  43.227  1.00 17.99  ?  100 GLY   A O   1 
ATOM   819   N N   . ARG   A 1 101 ? -24.744 -3.979  43.706  1.00 16.80  ?  101 ARG   A N   1 
ATOM   820   C CA  . ARG   A 1 101 ? -25.518 -3.603  42.535  1.00 16.43  ?  101 ARG   A CA  1 
ATOM   821   C C   . ARG   A 1 101 ? -24.746 -3.836  41.244  1.00 19.59  ?  101 ARG   A C   1 
ATOM   822   O O   . ARG   A 1 101 ? -25.359 -3.912  40.176  1.00 19.29  ?  101 ARG   A O   1 
ATOM   823   C CB  . ARG   A 1 101 ? -25.966 -2.145  42.644  1.00 19.02  ?  101 ARG   A CB  1 
ATOM   824   C CG  . ARG   A 1 101 ? -24.830 -1.140  42.626  1.00 19.37  ?  101 ARG   A CG  1 
ATOM   825   C CD  . ARG   A 1 101 ? -25.281 0.176   43.230  1.00 21.81  ?  101 ARG   A CD  1 
ATOM   826   N NE  . ARG   A 1 101 ? -25.287 0.103   44.689  1.00 23.26  ?  101 ARG   A NE  1 
ATOM   827   C CZ  . ARG   A 1 101 ? -25.605 1.108   45.493  1.00 20.75  ?  101 ARG   A CZ  1 
ATOM   828   N NH1 . ARG   A 1 101 ? -25.996 2.278   45.014  1.00 19.91  ?  101 ARG   A NH1 1 
ATOM   829   N NH2 . ARG   A 1 101 ? -25.513 0.939   46.810  1.00 20.86  ?  101 ARG   A NH2 1 
ATOM   830   N N   . GLY   A 1 102 ? -23.419 -3.957  41.309  1.00 18.19  ?  102 GLY   A N   1 
ATOM   831   C CA  . GLY   A 1 102 ? -22.691 -4.458  40.154  1.00 18.28  ?  102 GLY   A CA  1 
ATOM   832   C C   . GLY   A 1 102 ? -23.047 -5.902  39.866  1.00 19.39  ?  102 GLY   A C   1 
ATOM   833   O O   . GLY   A 1 102 ? -23.294 -6.276  38.718  1.00 20.14  ?  102 GLY   A O   1 
ATOM   834   N N   . ALA   A 1 103 ? -23.112 -6.724  40.916  1.00 21.81  ?  103 ALA   A N   1 
ATOM   835   C CA  . ALA   A 1 103 ? -23.517 -8.117  40.771  1.00 19.23  ?  103 ALA   A CA  1 
ATOM   836   C C   . ALA   A 1 103 ? -24.916 -8.232  40.174  1.00 23.25  ?  103 ALA   A C   1 
ATOM   837   O O   . ALA   A 1 103 ? -25.163 -9.080  39.305  1.00 21.56  ?  103 ALA   A O   1 
ATOM   838   C CB  . ALA   A 1 103 ? -23.445 -8.809  42.134  1.00 20.35  ?  103 ALA   A CB  1 
ATOM   839   N N   . GLU   A 1 104 ? -25.850 -7.389  40.632  1.00 23.74  ?  104 GLU   A N   1 
ATOM   840   C CA  . GLU   A 1 104 ? -27.194 -7.391  40.063  1.00 20.83  ?  104 GLU   A CA  1 
ATOM   841   C C   . GLU   A 1 104 ? -27.172 -6.969  38.596  1.00 25.81  ?  104 GLU   A C   1 
ATOM   842   O O   . GLU   A 1 104 ? -27.901 -7.530  37.766  1.00 25.66  ?  104 GLU   A O   1 
ATOM   843   C CB  . GLU   A 1 104 ? -28.105 -6.472  40.878  1.00 21.91  ?  104 GLU   A CB  1 
ATOM   844   C CG  . GLU   A 1 104 ? -28.299 -6.908  42.323  1.00 21.65  ?  104 GLU   A CG  1 
ATOM   845   C CD  . GLU   A 1 104 ? -28.783 -5.782  43.233  1.00 24.30  ?  104 GLU   A CD  1 
ATOM   846   O OE1 . GLU   A 1 104 ? -28.731 -4.599  42.830  1.00 26.33  ?  104 GLU   A OE1 1 
ATOM   847   O OE2 . GLU   A 1 104 ? -29.207 -6.079  44.368  1.00 26.90  ?  104 GLU   A OE2 1 
ATOM   848   N N   . ASN   A 1 105 ? -26.344 -5.974  38.257  1.00 21.38  ?  105 ASN   A N   1 
ATOM   849   C CA  . ASN   A 1 105 ? -26.259 -5.522  36.868  1.00 22.90  ?  105 ASN   A CA  1 
ATOM   850   C C   . ASN   A 1 105 ? -25.632 -6.585  35.974  1.00 21.92  ?  105 ASN   A C   1 
ATOM   851   O O   . ASN   A 1 105 ? -25.914 -6.628  34.775  1.00 28.31  ?  105 ASN   A O   1 
ATOM   852   C CB  . ASN   A 1 105 ? -25.462 -4.215  36.791  1.00 25.28  ?  105 ASN   A CB  1 
ATOM   853   C CG  . ASN   A 1 105 ? -25.558 -3.542  35.431  1.00 29.92  ?  105 ASN   A CG  1 
ATOM   854   O OD1 . ASN   A 1 105 ? -26.553 -3.688  34.727  1.00 27.55  ?  105 ASN   A OD1 1 
ATOM   855   N ND2 . ASN   A 1 105 ? -24.515 -2.804  35.053  1.00 27.56  ?  105 ASN   A ND2 1 
ATOM   856   N N   . ILE   A 1 106 ? -24.779 -7.448  36.534  1.00 26.65  ?  106 ILE   A N   1 
ATOM   857   C CA  . ILE   A 1 106 ? -24.215 -8.548  35.753  1.00 25.76  ?  106 ILE   A CA  1 
ATOM   858   C C   . ILE   A 1 106 ? -25.275 -9.610  35.477  1.00 27.70  ?  106 ILE   A C   1 
ATOM   859   O O   . ILE   A 1 106 ? -25.471 -10.027 34.330  1.00 29.66  ?  106 ILE   A O   1 
ATOM   860   C CB  . ILE   A 1 106 ? -22.993 -9.153  36.469  1.00 25.54  ?  106 ILE   A CB  1 
ATOM   861   C CG1 . ILE   A 1 106 ? -21.777 -8.236  36.337  1.00 22.51  ?  106 ILE   A CG1 1 
ATOM   862   C CG2 . ILE   A 1 106 ? -22.669 -10.529 35.903  1.00 24.55  ?  106 ILE   A CG2 1 
ATOM   863   C CD1 . ILE   A 1 106 ? -20.590 -8.693  37.163  1.00 19.01  ?  106 ILE   A CD1 1 
ATOM   864   N N   . LEU   A 1 107 ? -25.984 -10.051 36.519  1.00 24.67  ?  107 LEU   A N   1 
ATOM   865   C CA  . LEU   A 1 107 ? -26.780 -11.273 36.438  1.00 23.85  ?  107 LEU   A CA  1 
ATOM   866   C C   . LEU   A 1 107 ? -28.232 -11.043 36.029  1.00 26.79  ?  107 LEU   A C   1 
ATOM   867   O O   . LEU   A 1 107 ? -28.783 -11.836 35.255  1.00 23.04  ?  107 LEU   A O   1 
ATOM   868   C CB  . LEU   A 1 107 ? -26.736 -12.016 37.778  1.00 25.73  ?  107 LEU   A CB  1 
ATOM   869   C CG  . LEU   A 1 107 ? -27.514 -13.334 37.852  1.00 21.13  ?  107 LEU   A CG  1 
ATOM   870   C CD1 . LEU   A 1 107 ? -26.890 -14.376 36.927  1.00 21.44  ?  107 LEU   A CD1 1 
ATOM   871   C CD2 . LEU   A 1 107 ? -27.594 -13.839 39.288  1.00 20.27  ?  107 LEU   A CD2 1 
ATOM   872   N N   . PHE   A 1 108 ? -28.882 -9.994  36.530  1.00 24.53  ?  108 PHE   A N   1 
ATOM   873   C CA  . PHE   A 1 108 ? -30.307 -9.838  36.246  1.00 24.47  ?  108 PHE   A CA  1 
ATOM   874   C C   . PHE   A 1 108 ? -30.597 -9.700  34.752  1.00 24.52  ?  108 PHE   A C   1 
ATOM   875   O O   . PHE   A 1 108 ? -31.426 -10.471 34.239  1.00 22.87  ?  108 PHE   A O   1 
ATOM   876   C CB  . PHE   A 1 108 ? -30.886 -8.671  37.060  1.00 24.97  ?  108 PHE   A CB  1 
ATOM   877   C CG  . PHE   A 1 108 ? -31.074 -8.977  38.536  1.00 27.19  ?  108 PHE   A CG  1 
ATOM   878   C CD1 . PHE   A 1 108 ? -30.606 -10.160 39.092  1.00 25.84  ?  108 PHE   A CD1 1 
ATOM   879   C CD2 . PHE   A 1 108 ? -31.731 -8.078  39.362  1.00 28.64  ?  108 PHE   A CD2 1 
ATOM   880   C CE1 . PHE   A 1 108 ? -30.778 -10.434 40.446  1.00 30.10  ?  108 PHE   A CE1 1 
ATOM   881   C CE2 . PHE   A 1 108 ? -31.912 -8.350  40.718  1.00 29.27  ?  108 PHE   A CE2 1 
ATOM   882   C CZ  . PHE   A 1 108 ? -31.441 -9.527  41.261  1.00 25.12  ?  108 PHE   A CZ  1 
ATOM   883   N N   . PRO   A 1 109 ? -29.973 -8.784  33.996  1.00 27.62  ?  109 PRO   A N   1 
ATOM   884   C CA  . PRO   A 1 109 ? -30.289 -8.714  32.558  1.00 29.61  ?  109 PRO   A CA  1 
ATOM   885   C C   . PRO   A 1 109 ? -30.023 -10.017 31.831  1.00 28.95  ?  109 PRO   A C   1 
ATOM   886   O O   . PRO   A 1 109 ? -30.763 -10.369 30.907  1.00 29.53  ?  109 PRO   A O   1 
ATOM   887   C CB  . PRO   A 1 109 ? -29.380 -7.586  32.047  1.00 25.97  ?  109 PRO   A CB  1 
ATOM   888   C CG  . PRO   A 1 109 ? -29.051 -6.776  33.266  1.00 26.10  ?  109 PRO   A CG  1 
ATOM   889   C CD  . PRO   A 1 109 ? -28.963 -7.778  34.375  1.00 25.64  ?  109 PRO   A CD  1 
ATOM   890   N N   . VAL   A 1 110 ? -28.986 -10.748 32.234  1.00 24.82  ?  110 VAL   A N   1 
ATOM   891   C CA  . VAL   A 1 110 ? -28.720 -12.065 31.661  1.00 25.56  ?  110 VAL   A CA  1 
ATOM   892   C C   . VAL   A 1 110 ? -29.908 -12.992 31.887  1.00 29.92  ?  110 VAL   A C   1 
ATOM   893   O O   . VAL   A 1 110 ? -30.352 -13.696 30.972  1.00 26.13  ?  110 VAL   A O   1 
ATOM   894   C CB  . VAL   A 1 110 ? -27.430 -12.651 32.260  1.00 25.79  ?  110 VAL   A CB  1 
ATOM   895   C CG1 . VAL   A 1 110 ? -27.337 -14.132 31.963  1.00 30.10  ?  110 VAL   A CG1 1 
ATOM   896   C CG2 . VAL   A 1 110 ? -26.222 -11.910 31.730  1.00 25.83  ?  110 VAL   A CG2 1 
ATOM   897   N N   . LEU   A 1 111 ? -30.438 -13.007 33.117  1.00 29.06  ?  111 LEU   A N   1 
ATOM   898   C CA  . LEU   A 1 111 ? -31.579 -13.867 33.425  1.00 26.00  ?  111 LEU   A CA  1 
ATOM   899   C C   . LEU   A 1 111 ? -32.819 -13.446 32.648  1.00 28.01  ?  111 LEU   A C   1 
ATOM   900   O O   . LEU   A 1 111 ? -33.621 -14.299 32.252  1.00 22.81  ?  111 LEU   A O   1 
ATOM   901   C CB  . LEU   A 1 111 ? -31.869 -13.862 34.931  1.00 22.71  ?  111 LEU   A CB  1 
ATOM   902   C CG  . LEU   A 1 111 ? -30.830 -14.469 35.887  1.00 23.93  ?  111 LEU   A CG  1 
ATOM   903   C CD1 . LEU   A 1 111 ? -31.288 -14.348 37.335  1.00 25.56  ?  111 LEU   A CD1 1 
ATOM   904   C CD2 . LEU   A 1 111 ? -30.559 -15.917 35.540  1.00 25.74  ?  111 LEU   A CD2 1 
ATOM   905   N N   . LEU   A 1 112 ? -32.989 -12.145 32.409  1.00 26.40  ?  112 LEU   A N   1 
ATOM   906   C CA  . LEU   A 1 112 ? -34.137 -11.690 31.635  1.00 26.16  ?  112 LEU   A CA  1 
ATOM   907   C C   . LEU   A 1 112 ? -34.065 -12.189 30.197  1.00 31.26  ?  112 LEU   A C   1 
ATOM   908   O O   . LEU   A 1 112 ? -35.041 -12.732 29.669  1.00 29.52  ?  112 LEU   A O   1 
ATOM   909   C CB  . LEU   A 1 112 ? -34.229 -10.168 31.670  1.00 22.69  ?  112 LEU   A CB  1 
ATOM   910   C CG  . LEU   A 1 112 ? -35.336 -9.606  30.781  1.00 30.73  ?  112 LEU   A CG  1 
ATOM   911   C CD1 . LEU   A 1 112 ? -36.699 -10.125 31.210  1.00 31.00  ?  112 LEU   A CD1 1 
ATOM   912   C CD2 . LEU   A 1 112 ? -35.313 -8.097  30.791  1.00 31.65  ?  112 LEU   A CD2 1 
ATOM   913   N N   . LYS   A 1 113 ? -32.921 -12.022 29.539  1.00 30.55  ?  113 LYS   A N   1 
ATOM   914   C CA  . LYS   A 1 113 ? -32.863 -12.462 28.150  1.00 33.57  ?  113 LYS   A CA  1 
ATOM   915   C C   . LYS   A 1 113 ? -32.848 -13.982 28.046  1.00 33.24  ?  113 LYS   A C   1 
ATOM   916   O O   . LYS   A 1 113 ? -33.439 -14.540 27.116  1.00 33.19  ?  113 LYS   A O   1 
ATOM   917   C CB  . LYS   A 1 113 ? -31.665 -11.838 27.429  1.00 35.24  ?  113 LYS   A CB  1 
ATOM   918   C CG  . LYS   A 1 113 ? -30.331 -11.961 28.129  1.00 41.42  ?  113 LYS   A CG  1 
ATOM   919   C CD  . LYS   A 1 113 ? -29.280 -11.135 27.374  1.00 47.24  ?  113 LYS   A CD  1 
ATOM   920   C CE  . LYS   A 1 113 ? -27.901 -11.226 28.014  1.00 30.70  ?  113 LYS   A CE  1 
ATOM   921   N NZ  . LYS   A 1 113 ? -27.438 -12.636 28.098  1.00 34.49  ?  113 LYS   A NZ  1 
ATOM   922   N N   . TYR   A 1 114 ? -32.213 -14.668 28.996  1.00 29.46  ?  114 TYR   A N   1 
ATOM   923   C CA  . TYR   A 1 114 ? -32.292 -16.124 29.018  1.00 33.71  ?  114 TYR   A CA  1 
ATOM   924   C C   . TYR   A 1 114 ? -33.740 -16.602 29.115  1.00 37.50  ?  114 TYR   A C   1 
ATOM   925   O O   . TYR   A 1 114 ? -34.136 -17.548 28.426  1.00 36.45  ?  114 TYR   A O   1 
ATOM   926   C CB  . TYR   A 1 114 ? -31.468 -16.671 30.182  1.00 32.42  ?  114 TYR   A CB  1 
ATOM   927   C CG  . TYR   A 1 114 ? -31.366 -18.179 30.215  1.00 36.99  ?  114 TYR   A CG  1 
ATOM   928   C CD1 . TYR   A 1 114 ? -30.428 -18.848 29.438  1.00 42.64  ?  114 TYR   A CD1 1 
ATOM   929   C CD2 . TYR   A 1 114 ? -32.198 -18.932 31.031  1.00 44.11  ?  114 TYR   A CD2 1 
ATOM   930   C CE1 . TYR   A 1 114 ? -30.329 -20.225 29.469  1.00 42.21  ?  114 TYR   A CE1 1 
ATOM   931   C CE2 . TYR   A 1 114 ? -32.103 -20.309 31.070  1.00 44.13  ?  114 TYR   A CE2 1 
ATOM   932   C CZ  . TYR   A 1 114 ? -31.168 -20.949 30.287  1.00 44.74  ?  114 TYR   A CZ  1 
ATOM   933   O OH  . TYR   A 1 114 ? -31.075 -22.320 30.325  1.00 57.61  ?  114 TYR   A OH  1 
ATOM   934   N N   . LYS   A 1 115 ? -34.547 -15.956 29.962  1.00 35.41  ?  115 LYS   A N   1 
ATOM   935   C CA  . LYS   A 1 115 ? -35.916 -16.423 30.167  1.00 34.34  ?  115 LYS   A CA  1 
ATOM   936   C C   . LYS   A 1 115 ? -36.760 -16.234 28.915  1.00 37.22  ?  115 LYS   A C   1 
ATOM   937   O O   . LYS   A 1 115 ? -37.633 -17.056 28.619  1.00 37.88  ?  115 LYS   A O   1 
ATOM   938   C CB  . LYS   A 1 115 ? -36.552 -15.697 31.351  1.00 31.49  ?  115 LYS   A CB  1 
ATOM   939   C CG  . LYS   A 1 115 ? -37.928 -16.217 31.727  1.00 29.30  ?  115 LYS   A CG  1 
ATOM   940   C CD  . LYS   A 1 115 ? -37.838 -17.399 32.687  1.00 34.76  ?  115 LYS   A CD  1 
ATOM   941   C CE  . LYS   A 1 115 ? -39.219 -17.899 33.074  1.00 31.73  ?  115 LYS   A CE  1 
ATOM   942   N NZ  . LYS   A 1 115 ? -39.152 -18.972 34.103  1.00 26.70  ?  115 LYS   A NZ  1 
ATOM   943   N N   . GLN   A 1 116 ? -36.511 -15.165 28.159  1.00 38.71  ?  116 GLN   A N   1 
ATOM   944   C CA  . GLN   A 1 116 ? -37.319 -14.858 26.988  1.00 39.76  ?  116 GLN   A CA  1 
ATOM   945   C C   . GLN   A 1 116 ? -36.648 -15.264 25.682  1.00 38.75  ?  116 GLN   A C   1 
ATOM   946   O O   . GLN   A 1 116 ? -37.002 -14.735 24.623  1.00 44.17  ?  116 GLN   A O   1 
ATOM   947   C CB  . GLN   A 1 116 ? -37.682 -13.372 26.969  1.00 38.55  ?  116 GLN   A CB  1 
ATOM   948   C CG  . GLN   A 1 116 ? -36.537 -12.396 27.004  1.00 37.20  ?  116 GLN   A CG  1 
ATOM   949   C CD  . GLN   A 1 116 ? -37.037 -10.976 27.198  1.00 38.51  ?  116 GLN   A CD  1 
ATOM   950   O OE1 . GLN   A 1 116 ? -36.351 -10.007 26.863  1.00 39.58  ?  116 GLN   A OE1 1 
ATOM   951   N NE2 . GLN   A 1 116 ? -38.245 -10.847 27.740  1.00 33.50  ?  116 GLN   A NE2 1 
ATOM   952   N N   . LYS   A 1 117 ? -35.720 -16.221 25.727  1.00 38.32  ?  117 LYS   A N   1 
ATOM   953   C CA  . LYS   A 1 117 ? -35.013 -16.633 24.520  1.00 40.31  ?  117 LYS   A CA  1 
ATOM   954   C C   . LYS   A 1 117 ? -35.909 -17.382 23.543  1.00 48.48  ?  117 LYS   A C   1 
ATOM   955   O O   . LYS   A 1 117 ? -35.551 -17.505 22.365  1.00 53.48  ?  117 LYS   A O   1 
ATOM   956   C CB  . LYS   A 1 117 ? -33.808 -17.502 24.887  1.00 44.29  ?  117 LYS   A CB  1 
ATOM   957   C CG  . LYS   A 1 117 ? -34.178 -18.839 25.518  1.00 45.69  ?  117 LYS   A CG  1 
ATOM   958   C CD  . LYS   A 1 117 ? -32.971 -19.538 26.124  1.00 44.04  ?  117 LYS   A CD  1 
ATOM   959   C CE  . LYS   A 1 117 ? -31.949 -19.924 25.076  1.00 48.85  ?  117 LYS   A CE  1 
ATOM   960   N NZ  . LYS   A 1 117 ? -30.826 -20.677 25.697  1.00 52.51  ?  117 LYS   A NZ  1 
ATOM   961   N N   . GLU   A 1 118 ? -37.058 -17.884 23.996  1.00 48.68  ?  118 GLU   A N   1 
ATOM   962   C CA  . GLU   A 1 118 ? -37.990 -18.600 23.132  1.00 55.06  ?  118 GLU   A CA  1 
ATOM   963   C C   . GLU   A 1 118 ? -39.291 -17.828 22.935  1.00 58.44  ?  118 GLU   A C   1 
ATOM   964   O O   . GLU   A 1 118 ? -40.367 -18.423 22.831  1.00 59.88  ?  118 GLU   A O   1 
ATOM   965   C CB  . GLU   A 1 118 ? -38.272 -19.995 23.685  1.00 57.02  ?  118 GLU   A CB  1 
ATOM   966   C CG  . GLU   A 1 118 ? -37.270 -21.041 23.221  1.00 69.87  ?  118 GLU   A CG  1 
ATOM   967   C CD  . GLU   A 1 118 ? -37.410 -22.362 23.957  1.00 84.56  ?  118 GLU   A CD  1 
ATOM   968   O OE1 . GLU   A 1 118 ? -37.399 -22.355 25.208  1.00 80.66  ?  118 GLU   A OE1 1 
ATOM   969   O OE2 . GLU   A 1 118 ? -37.535 -23.409 23.284  1.00 94.58  ?  118 GLU   A OE2 1 
ATOM   970   N N   . GLY   A 1 119 ? -39.203 -16.500 22.883  1.00 49.77  ?  119 GLY   A N   1 
ATOM   971   C CA  . GLY   A 1 119 ? -40.370 -15.678 22.649  1.00 51.52  ?  119 GLY   A CA  1 
ATOM   972   C C   . GLY   A 1 119 ? -41.412 -15.702 23.742  1.00 50.09  ?  119 GLY   A C   1 
ATOM   973   O O   . GLY   A 1 119 ? -42.560 -15.325 23.490  1.00 52.64  ?  119 GLY   A O   1 
ATOM   974   N N   . LYS   A 1 120 ? -41.058 -16.138 24.950  1.00 45.55  ?  120 LYS   A N   1 
ATOM   975   C CA  . LYS   A 1 120 ? -41.974 -16.091 26.079  1.00 46.60  ?  120 LYS   A CA  1 
ATOM   976   C C   . LYS   A 1 120 ? -41.496 -15.037 27.076  1.00 36.79  ?  120 LYS   A C   1 
ATOM   977   O O   . LYS   A 1 120 ? -40.624 -14.220 26.772  1.00 38.11  ?  120 LYS   A O   1 
ATOM   978   C CB  . LYS   A 1 120 ? -42.115 -17.473 26.717  1.00 43.24  ?  120 LYS   A CB  1 
ATOM   979   C CG  . LYS   A 1 120 ? -40.860 -18.006 27.365  1.00 47.86  ?  120 LYS   A CG  1 
ATOM   980   C CD  . LYS   A 1 120 ? -41.164 -19.306 28.096  1.00 55.66  ?  120 LYS   A CD  1 
ATOM   981   C CE  . LYS   A 1 120 ? -40.028 -19.695 29.020  1.00 48.67  ?  120 LYS   A CE  1 
ATOM   982   N NZ  . LYS   A 1 120 ? -39.633 -18.551 29.883  1.00 43.16  ?  120 LYS   A NZ  1 
ATOM   983   N N   . ALA   A 1 121 ? -42.088 -15.042 28.268  1.00 36.51  ?  121 ALA   A N   1 
ATOM   984   C CA  . ALA   A 1 121 ? -41.793 -14.032 29.287  1.00 33.08  ?  121 ALA   A CA  1 
ATOM   985   C C   . ALA   A 1 121 ? -42.045 -12.623 28.753  1.00 36.66  ?  121 ALA   A C   1 
ATOM   986   O O   . ALA   A 1 121 ? -41.238 -11.712 28.951  1.00 36.39  ?  121 ALA   A O   1 
ATOM   987   C CB  . ALA   A 1 121 ? -40.361 -14.163 29.812  1.00 37.89  ?  121 ALA   A CB  1 
ATOM   988   N N   . LYS   A 1 122 ? -43.182 -12.444 28.071  1.00 35.88  ?  122 LYS   A N   1 
ATOM   989   C CA  . LYS   A 1 122 ? -43.542 -11.142 27.521  1.00 33.70  ?  122 LYS   A CA  1 
ATOM   990   C C   . LYS   A 1 122 ? -43.951 -10.147 28.600  1.00 32.34  ?  122 LYS   A C   1 
ATOM   991   O O   . LYS   A 1 122 ? -43.910 -8.938  28.351  1.00 35.34  ?  122 LYS   A O   1 
ATOM   992   C CB  . LYS   A 1 122 ? -44.680 -11.291 26.511  1.00 33.39  ?  122 LYS   A CB  1 
ATOM   993   C CG  . LYS   A 1 122 ? -44.584 -12.521 25.617  1.00 39.86  ?  122 LYS   A CG  1 
ATOM   994   C CD  . LYS   A 1 122 ? -43.523 -12.370 24.539  1.00 45.15  ?  122 LYS   A CD  1 
ATOM   995   C CE  . LYS   A 1 122 ? -44.009 -11.499 23.388  1.00 40.82  ?  122 LYS   A CE  1 
ATOM   996   N NZ  . LYS   A 1 122 ? -42.941 -11.287 22.367  1.00 49.49  ?  122 LYS   A NZ  1 
ATOM   997   N N   . ASN   A 1 123 ? -44.362 -10.626 29.778  1.00 31.63  ?  123 ASN   A N   1 
ATOM   998   C CA  . ASN   A 1 123 ? -44.687 -9.784  30.929  1.00 30.50  ?  123 ASN   A CA  1 
ATOM   999   C C   . ASN   A 1 123 ? -43.803 -10.213 32.097  1.00 31.10  ?  123 ASN   A C   1 
ATOM   1000  O O   . ASN   A 1 123 ? -44.282 -10.809 33.074  1.00 28.68  ?  123 ASN   A O   1 
ATOM   1001  C CB  . ASN   A 1 123 ? -46.164 -9.888  31.299  1.00 31.46  ?  123 ASN   A CB  1 
ATOM   1002  C CG  . ASN   A 1 123 ? -47.083 -9.675  30.109  1.00 37.57  ?  123 ASN   A CG  1 
ATOM   1003  O OD1 . ASN   A 1 123 ? -46.839 -8.809  29.265  1.00 36.93  ?  123 ASN   A OD1 1 
ATOM   1004  N ND2 . ASN   A 1 123 ? -48.145 -10.473 30.032  1.00 38.05  ?  123 ASN   A ND2 1 
ATOM   1005  N N   . PRO   A 1 124 ? -42.511 -9.908  32.036  1.00 31.43  ?  124 PRO   A N   1 
ATOM   1006  C CA  . PRO   A 1 124 ? -41.560 -10.515 32.974  1.00 30.74  ?  124 PRO   A CA  1 
ATOM   1007  C C   . PRO   A 1 124 ? -41.611 -9.888  34.360  1.00 30.41  ?  124 PRO   A C   1 
ATOM   1008  O O   . PRO   A 1 124 ? -41.709 -8.668  34.514  1.00 31.16  ?  124 PRO   A O   1 
ATOM   1009  C CB  . PRO   A 1 124 ? -40.211 -10.250 32.302  1.00 28.78  ?  124 PRO   A CB  1 
ATOM   1010  C CG  . PRO   A 1 124 ? -40.431 -8.957  31.593  1.00 28.98  ?  124 PRO   A CG  1 
ATOM   1011  C CD  . PRO   A 1 124 ? -41.843 -9.008  31.081  1.00 33.07  ?  124 PRO   A CD  1 
ATOM   1012  N N   . VAL   A 1 125 ? -41.524 -10.743 35.381  1.00 27.22  ?  125 VAL   A N   1 
ATOM   1013  C CA  . VAL   A 1 125 ? -41.535 -10.304 36.769  1.00 27.86  ?  125 VAL   A CA  1 
ATOM   1014  C C   . VAL   A 1 125 ? -40.428 -11.012 37.542  1.00 28.43  ?  125 VAL   A C   1 
ATOM   1015  O O   . VAL   A 1 125 ? -39.953 -12.087 37.161  1.00 23.10  ?  125 VAL   A O   1 
ATOM   1016  C CB  . VAL   A 1 125 ? -42.904 -10.551 37.447  1.00 33.07  ?  125 VAL   A CB  1 
ATOM   1017  C CG1 . VAL   A 1 125 ? -44.012 -9.843  36.685  1.00 32.59  ?  125 VAL   A CG1 1 
ATOM   1018  C CG2 . VAL   A 1 125 ? -43.197 -12.042 37.551  1.00 29.85  ?  125 VAL   A CG2 1 
ATOM   1019  N N   . PHE   A 1 126 ? -40.006 -10.368 38.634  1.00 26.57  ?  126 PHE   A N   1 
ATOM   1020  C CA  . PHE   A 1 126 ? -39.176 -10.963 39.672  1.00 25.23  ?  126 PHE   A CA  1 
ATOM   1021  C C   . PHE   A 1 126 ? -39.991 -11.045 40.957  1.00 27.05  ?  126 PHE   A C   1 
ATOM   1022  O O   . PHE   A 1 126 ? -40.761 -10.130 41.269  1.00 27.10  ?  126 PHE   A O   1 
ATOM   1023  C CB  . PHE   A 1 126 ? -37.918 -10.131 39.941  1.00 27.42  ?  126 PHE   A CB  1 
ATOM   1024  C CG  . PHE   A 1 126 ? -36.855 -10.226 38.874  1.00 31.28  ?  126 PHE   A CG  1 
ATOM   1025  C CD1 . PHE   A 1 126 ? -37.024 -9.626  37.641  1.00 28.34  ?  126 PHE   A CD1 1 
ATOM   1026  C CD2 . PHE   A 1 126 ? -35.650 -10.868 39.136  1.00 29.39  ?  126 PHE   A CD2 1 
ATOM   1027  C CE1 . PHE   A 1 126 ? -36.034 -9.697  36.679  1.00 26.75  ?  126 PHE   A CE1 1 
ATOM   1028  C CE2 . PHE   A 1 126 ? -34.653 -10.935 38.174  1.00 25.84  ?  126 PHE   A CE2 1 
ATOM   1029  C CZ  . PHE   A 1 126 ? -34.843 -10.349 36.952  1.00 26.74  ?  126 PHE   A CZ  1 
ATOM   1030  N N   . ILE   A 1 127 ? -39.820 -12.130 41.707  1.00 23.28  ?  127 ILE   A N   1 
ATOM   1031  C CA  . ILE   A 1 127 ? -40.526 -12.327 42.969  1.00 23.61  ?  127 ILE   A CA  1 
ATOM   1032  C C   . ILE   A 1 127 ? -39.504 -12.490 44.082  1.00 22.56  ?  127 ILE   A C   1 
ATOM   1033  O O   . ILE   A 1 127 ? -38.547 -13.259 43.945  1.00 27.23  ?  127 ILE   A O   1 
ATOM   1034  C CB  . ILE   A 1 127 ? -41.457 -13.548 42.918  1.00 25.20  ?  127 ILE   A CB  1 
ATOM   1035  C CG1 . ILE   A 1 127 ? -42.456 -13.416 41.773  1.00 31.39  ?  127 ILE   A CG1 1 
ATOM   1036  C CG2 . ILE   A 1 127 ? -42.192 -13.698 44.234  1.00 26.24  ?  127 ILE   A CG2 1 
ATOM   1037  C CD1 . ILE   A 1 127 ? -43.402 -14.589 41.680  1.00 25.13  ?  127 ILE   A CD1 1 
ATOM   1038  N N   . SER   A 1 128 ? -39.717 -11.790 45.190  1.00 21.41  ?  128 SER   A N   1 
ATOM   1039  C CA  . SER   A 1 128 ? -38.810 -11.863 46.322  1.00 21.60  ?  128 SER   A CA  1 
ATOM   1040  C C   . SER   A 1 128 ? -39.601 -11.787 47.619  1.00 20.91  ?  128 SER   A C   1 
ATOM   1041  O O   . SER   A 1 128 ? -40.719 -11.270 47.656  1.00 23.53  ?  128 SER   A O   1 
ATOM   1042  C CB  . SER   A 1 128 ? -37.779 -10.729 46.277  1.00 24.32  ?  128 SER   A CB  1 
ATOM   1043  O OG  . SER   A 1 128 ? -36.807 -10.892 47.294  1.00 22.97  ?  128 SER   A OG  1 
ATOM   1044  N N   . ASN   A 1 129 ? -39.007 -12.294 48.701  1.00 21.03  ?  129 ASN   A N   1 
ATOM   1045  C CA  . ASN   A 1 129 ? -39.563 -11.959 50.002  1.00 25.05  ?  129 ASN   A CA  1 
ATOM   1046  C C   . ASN   A 1 129 ? -39.577 -10.450 50.178  1.00 26.76  ?  129 ASN   A C   1 
ATOM   1047  O O   . ASN   A 1 129 ? -40.578 -9.883  50.632  1.00 23.62  ?  129 ASN   A O   1 
ATOM   1048  C CB  . ASN   A 1 129 ? -38.808 -12.663 51.138  1.00 20.34  ?  129 ASN   A CB  1 
ATOM   1049  C CG  . ASN   A 1 129 ? -37.304 -12.477 51.077  1.00 21.77  ?  129 ASN   A CG  1 
ATOM   1050  O OD1 . ASN   A 1 129 ? -36.728 -12.223 50.020  1.00 22.67  ?  129 ASN   A OD1 1 
ATOM   1051  N ND2 . ASN   A 1 129 ? -36.656 -12.636 52.224  1.00 24.40  ?  129 ASN   A ND2 1 
ATOM   1052  N N   . PHE   A 1 130 ? -38.500 -9.780  49.762  1.00 24.54  ?  130 PHE   A N   1 
ATOM   1053  C CA  . PHE   A 1 130 ? -38.503 -8.335  49.567  1.00 25.01  ?  130 PHE   A CA  1 
ATOM   1054  C C   . PHE   A 1 130 ? -37.256 -7.891  48.812  1.00 23.74  ?  130 PHE   A C   1 
ATOM   1055  O O   . PHE   A 1 130 ? -36.147 -7.979  49.346  1.00 25.34  ?  130 PHE   A O   1 
ATOM   1056  C CB  . PHE   A 1 130 ? -38.594 -7.596  50.906  1.00 26.72  ?  130 PHE   A CB  1 
ATOM   1057  C CG  . PHE   A 1 130 ? -39.415 -6.338  50.838  1.00 29.41  ?  130 PHE   A CG  1 
ATOM   1058  C CD1 . PHE   A 1 130 ? -38.947 -5.225  50.150  1.00 30.14  ?  130 PHE   A CD1 1 
ATOM   1059  C CD2 . PHE   A 1 130 ? -40.662 -6.274  51.442  1.00 33.04  ?  130 PHE   A CD2 1 
ATOM   1060  C CE1 . PHE   A 1 130 ? -39.696 -4.066  50.079  1.00 30.10  ?  130 PHE   A CE1 1 
ATOM   1061  C CE2 . PHE   A 1 130 ? -41.423 -5.117  51.371  1.00 34.14  ?  130 PHE   A CE2 1 
ATOM   1062  C CZ  . PHE   A 1 130 ? -40.935 -4.010  50.688  1.00 34.84  ?  130 PHE   A CZ  1 
ATOM   1063  N N   . HIS   A 1 131 ? -37.422 -7.434  47.570  1.00 25.37  ?  131 HIS   A N   1 
ATOM   1064  C CA  . HIS   A 1 131 ? -36.318 -6.820  46.837  1.00 23.88  ?  131 HIS   A CA  1 
ATOM   1065  C C   . HIS   A 1 131 ? -35.822 -5.581  47.573  1.00 24.05  ?  131 HIS   A C   1 
ATOM   1066  O O   . HIS   A 1 131 ? -36.609 -4.689  47.901  1.00 28.01  ?  131 HIS   A O   1 
ATOM   1067  C CB  . HIS   A 1 131 ? -36.760 -6.403  45.431  1.00 26.64  ?  131 HIS   A CB  1 
ATOM   1068  C CG  . HIS   A 1 131 ? -37.230 -7.525  44.557  1.00 26.01  ?  131 HIS   A CG  1 
ATOM   1069  N ND1 . HIS   A 1 131 ? -38.549 -7.916  44.493  1.00 24.28  ?  131 HIS   A ND1 1 
ATOM   1070  C CD2 . HIS   A 1 131 ? -36.565 -8.298  43.666  1.00 28.97  ?  131 HIS   A CD2 1 
ATOM   1071  C CE1 . HIS   A 1 131 ? -38.672 -8.901  43.620  1.00 24.71  ?  131 HIS   A CE1 1 
ATOM   1072  N NE2 . HIS   A 1 131 ? -37.483 -9.155  43.107  1.00 25.44  ?  131 HIS   A NE2 1 
ATOM   1073  N N   . PHE   A 1 132 ? -34.516 -5.498  47.807  1.00 25.95  ?  132 PHE   A N   1 
ATOM   1074  C CA  . PHE   A 1 132 ? -33.978 -4.241  48.304  1.00 27.50  ?  132 PHE   A CA  1 
ATOM   1075  C C   . PHE   A 1 132 ? -34.014 -3.204  47.183  1.00 26.92  ?  132 PHE   A C   1 
ATOM   1076  O O   . PHE   A 1 132 ? -34.349 -3.513  46.037  1.00 31.48  ?  132 PHE   A O   1 
ATOM   1077  C CB  . PHE   A 1 132 ? -32.559 -4.428  48.852  1.00 33.23  ?  132 PHE   A CB  1 
ATOM   1078  C CG  . PHE   A 1 132 ? -32.089 -3.276  49.704  1.00 33.34  ?  132 PHE   A CG  1 
ATOM   1079  C CD1 . PHE   A 1 132 ? -32.879 -2.805  50.745  1.00 34.12  ?  132 PHE   A CD1 1 
ATOM   1080  C CD2 . PHE   A 1 132 ? -30.883 -2.649  49.448  1.00 32.91  ?  132 PHE   A CD2 1 
ATOM   1081  C CE1 . PHE   A 1 132 ? -32.470 -1.732  51.520  1.00 35.10  ?  132 PHE   A CE1 1 
ATOM   1082  C CE2 . PHE   A 1 132 ? -30.468 -1.590  50.226  1.00 33.64  ?  132 PHE   A CE2 1 
ATOM   1083  C CZ  . PHE   A 1 132 ? -31.260 -1.129  51.261  1.00 30.63  ?  132 PHE   A CZ  1 
ATOM   1084  N N   . ASP   A 1 133 ? -33.659 -1.956  47.508  1.00 27.43  ?  133 ASP   A N   1 
ATOM   1085  C CA  . ASP   A 1 133 ? -33.962 -0.871  46.576  1.00 29.51  ?  133 ASP   A CA  1 
ATOM   1086  C C   . ASP   A 1 133 ? -33.157 -0.991  45.280  1.00 31.05  ?  133 ASP   A C   1 
ATOM   1087  O O   . ASP   A 1 133 ? -33.729 -0.903  44.190  1.00 26.90  ?  133 ASP   A O   1 
ATOM   1088  C CB  . ASP   A 1 133 ? -33.768 0.493   47.249  1.00 32.54  ?  133 ASP   A CB  1 
ATOM   1089  C CG  . ASP   A 1 133 ? -32.320 0.815   47.535  1.00 44.53  ?  133 ASP   A CG  1 
ATOM   1090  O OD1 . ASP   A 1 133 ? -31.543 -0.123  47.809  1.00 47.14  ?  133 ASP   A OD1 1 
ATOM   1091  O OD2 . ASP   A 1 133 ? -31.958 2.014   47.484  1.00 48.66  ?  133 ASP   A OD2 1 
ATOM   1092  N N   . THR   A 1 134 ? -31.837 -1.221  45.363  1.00 32.07  ?  134 THR   A N   1 
ATOM   1093  C CA  . THR   A 1 134 ? -31.052 -1.382  44.132  1.00 31.11  ?  134 THR   A CA  1 
ATOM   1094  C C   . THR   A 1 134 ? -31.489 -2.621  43.360  1.00 25.65  ?  134 THR   A C   1 
ATOM   1095  O O   . THR   A 1 134 ? -31.511 -2.621  42.123  1.00 25.87  ?  134 THR   A O   1 
ATOM   1096  C CB  . THR   A 1 134 ? -29.546 -1.469  44.432  1.00 32.29  ?  134 THR   A CB  1 
ATOM   1097  O OG1 . THR   A 1 134 ? -29.227 -2.759  44.983  1.00 24.48  ?  134 THR   A OG1 1 
ATOM   1098  C CG2 . THR   A 1 134 ? -29.105 -0.368  45.400  1.00 34.41  ?  134 THR   A CG2 1 
ATOM   1099  N N   . THR   A 1 135 ? -31.813 -3.696  44.080  1.00 27.72  ?  135 THR   A N   1 
ATOM   1100  C CA  . THR   A 1 135 ? -32.327 -4.907  43.452  1.00 28.62  ?  135 THR   A CA  1 
ATOM   1101  C C   . THR   A 1 135 ? -33.590 -4.611  42.654  1.00 29.19  ?  135 THR   A C   1 
ATOM   1102  O O   . THR   A 1 135 ? -33.662 -4.888  41.449  1.00 26.77  ?  135 THR   A O   1 
ATOM   1103  C CB  . THR   A 1 135 ? -32.598 -5.963  44.524  1.00 27.55  ?  135 THR   A CB  1 
ATOM   1104  O OG1 . THR   A 1 135 ? -31.528 -5.948  45.479  1.00 26.57  ?  135 THR   A OG1 1 
ATOM   1105  C CG2 . THR   A 1 135 ? -32.693 -7.350  43.901  1.00 26.86  ?  135 THR   A CG2 1 
ATOM   1106  N N   . ALA   A 1 136 ? -34.601 -4.037  43.317  1.00 26.03  ?  136 ALA   A N   1 
ATOM   1107  C CA  . ALA   A 1 136 ? -35.836 -3.676  42.632  1.00 25.95  ?  136 ALA   A CA  1 
ATOM   1108  C C   . ALA   A 1 136 ? -35.589 -2.679  41.506  1.00 31.44  ?  136 ALA   A C   1 
ATOM   1109  O O   . ALA   A 1 136 ? -36.261 -2.734  40.472  1.00 31.85  ?  136 ALA   A O   1 
ATOM   1110  C CB  . ALA   A 1 136 ? -36.841 -3.113  43.635  1.00 30.35  ?  136 ALA   A CB  1 
ATOM   1111  N N   . ALA   A 1 137 ? -34.628 -1.769  41.678  1.00 29.40  ?  137 ALA   A N   1 
ATOM   1112  C CA  . ALA   A 1 137 ? -34.340 -0.804  40.623  1.00 33.73  ?  137 ALA   A CA  1 
ATOM   1113  C C   . ALA   A 1 137 ? -33.791 -1.495  39.379  1.00 33.08  ?  137 ALA   A C   1 
ATOM   1114  O O   . ALA   A 1 137 ? -34.157 -1.140  38.252  1.00 31.16  ?  137 ALA   A O   1 
ATOM   1115  C CB  . ALA   A 1 137 ? -33.359 0.254   41.131  1.00 36.25  ?  137 ALA   A CB  1 
ATOM   1116  N N   . HIS   A 1 138 ? -32.919 -2.492  39.560  1.00 32.33  ?  138 HIS   A N   1 
ATOM   1117  C CA  . HIS   A 1 138 ? -32.409 -3.223  38.406  1.00 30.73  ?  138 HIS   A CA  1 
ATOM   1118  C C   . HIS   A 1 138 ? -33.497 -4.077  37.774  1.00 29.16  ?  138 HIS   A C   1 
ATOM   1119  O O   . HIS   A 1 138 ? -33.544 -4.215  36.547  1.00 29.10  ?  138 HIS   A O   1 
ATOM   1120  C CB  . HIS   A 1 138 ? -31.195 -4.070  38.805  1.00 28.74  ?  138 HIS   A CB  1 
ATOM   1121  C CG  . HIS   A 1 138 ? -29.938 -3.272  38.931  1.00 27.16  ?  138 HIS   A CG  1 
ATOM   1122  N ND1 . HIS   A 1 138 ? -29.271 -2.762  37.838  1.00 24.89  ?  138 HIS   A ND1 1 
ATOM   1123  C CD2 . HIS   A 1 138 ? -29.254 -2.850  40.020  1.00 26.58  ?  138 HIS   A CD2 1 
ATOM   1124  C CE1 . HIS   A 1 138 ? -28.219 -2.077  38.248  1.00 24.67  ?  138 HIS   A CE1 1 
ATOM   1125  N NE2 . HIS   A 1 138 ? -28.187 -2.113  39.567  1.00 24.90  ?  138 HIS   A NE2 1 
ATOM   1126  N N   . VAL   A 1 139 ? -34.383 -4.653  38.590  1.00 31.53  ?  139 VAL   A N   1 
ATOM   1127  C CA  . VAL   A 1 139 ? -35.539 -5.372  38.052  1.00 32.41  ?  139 VAL   A CA  1 
ATOM   1128  C C   . VAL   A 1 139 ? -36.343 -4.457  37.134  1.00 28.45  ?  139 VAL   A C   1 
ATOM   1129  O O   . VAL   A 1 139 ? -36.568 -4.760  35.957  1.00 28.70  ?  139 VAL   A O   1 
ATOM   1130  C CB  . VAL   A 1 139 ? -36.408 -5.929  39.195  1.00 30.38  ?  139 VAL   A CB  1 
ATOM   1131  C CG1 . VAL   A 1 139 ? -37.746 -6.379  38.671  1.00 30.46  ?  139 VAL   A CG1 1 
ATOM   1132  C CG2 . VAL   A 1 139 ? -35.706 -7.082  39.901  1.00 29.08  ?  139 VAL   A CG2 1 
ATOM   1133  N N   . GLU   A 1 140 ? -36.772 -3.309  37.662  1.00 32.15  ?  140 GLU   A N   1 
ATOM   1134  C CA  . GLU   A 1 140 ? -37.585 -2.382  36.885  1.00 27.90  ?  140 GLU   A CA  1 
ATOM   1135  C C   . GLU   A 1 140 ? -36.799 -1.758  35.741  1.00 34.68  ?  140 GLU   A C   1 
ATOM   1136  O O   . GLU   A 1 140 ? -37.362 -1.521  34.664  1.00 32.44  ?  140 GLU   A O   1 
ATOM   1137  C CB  . GLU   A 1 140 ? -38.148 -1.298  37.802  1.00 36.28  ?  140 GLU   A CB  1 
ATOM   1138  C CG  . GLU   A 1 140 ? -39.105 -1.826  38.870  1.00 34.07  ?  140 GLU   A CG  1 
ATOM   1139  C CD  . GLU   A 1 140 ? -39.287 -0.862  40.035  1.00 39.06  ?  140 GLU   A CD  1 
ATOM   1140  O OE1 . GLU   A 1 140 ? -38.552 0.144   40.103  1.00 43.77  ?  140 GLU   A OE1 1 
ATOM   1141  O OE2 . GLU   A 1 140 ? -40.166 -1.112  40.889  1.00 43.52  ?  140 GLU   A OE2 1 
ATOM   1142  N N   . LEU   A 1 141 ? -35.506 -1.490  35.943  1.00 30.80  ?  141 LEU   A N   1 
ATOM   1143  C CA  . LEU   A 1 141 ? -34.710 -0.891  34.875  1.00 31.42  ?  141 LEU   A CA  1 
ATOM   1144  C C   . LEU   A 1 141 ? -34.617 -1.812  33.672  1.00 33.55  ?  141 LEU   A C   1 
ATOM   1145  O O   . LEU   A 1 141 ? -34.414 -1.348  32.544  1.00 34.59  ?  141 LEU   A O   1 
ATOM   1146  C CB  . LEU   A 1 141 ? -33.312 -0.551  35.379  1.00 33.19  ?  141 LEU   A CB  1 
ATOM   1147  C CG  . LEU   A 1 141 ? -32.499 0.465   34.588  1.00 38.11  ?  141 LEU   A CG  1 
ATOM   1148  C CD1 . LEU   A 1 141 ? -33.289 1.734   34.392  1.00 38.67  ?  141 LEU   A CD1 1 
ATOM   1149  C CD2 . LEU   A 1 141 ? -31.235 0.752   35.353  1.00 40.77  ?  141 LEU   A CD2 1 
ATOM   1150  N N   . ASN   A 1 142 ? -34.757 -3.117  33.888  1.00 34.03  ?  142 ASN   A N   1 
ATOM   1151  C CA  . ASN   A 1 142 ? -34.784 -4.072  32.795  1.00 35.18  ?  142 ASN   A CA  1 
ATOM   1152  C C   . ASN   A 1 142 ? -36.203 -4.356  32.299  1.00 36.46  ?  142 ASN   A C   1 
ATOM   1153  O O   . ASN   A 1 142 ? -36.419 -5.340  31.583  1.00 37.16  ?  142 ASN   A O   1 
ATOM   1154  C CB  . ASN   A 1 142 ? -34.068 -5.358  33.213  1.00 26.18  ?  142 ASN   A CB  1 
ATOM   1155  C CG  . ASN   A 1 142 ? -32.552 -5.221  33.147  1.00 31.76  ?  142 ASN   A CG  1 
ATOM   1156  O OD1 . ASN   A 1 142 ? -31.959 -5.289  32.069  1.00 31.15  ?  142 ASN   A OD1 1 
ATOM   1157  N ND2 . ASN   A 1 142 ? -31.921 -5.015  34.299  1.00 29.08  ?  142 ASN   A ND2 1 
ATOM   1158  N N   . GLY   A 1 143 ? -37.167 -3.502  32.639  1.00 30.72  ?  143 GLY   A N   1 
ATOM   1159  C CA  . GLY   A 1 143 ? -38.509 -3.665  32.129  1.00 31.62  ?  143 GLY   A CA  1 
ATOM   1160  C C   . GLY   A 1 143 ? -39.322 -4.738  32.806  1.00 33.25  ?  143 GLY   A C   1 
ATOM   1161  O O   . GLY   A 1 143 ? -40.298 -5.215  32.223  1.00 40.63  ?  143 GLY   A O   1 
ATOM   1162  N N   . CYS   A 1 144 ? -38.962 -5.127  34.024  1.00 30.29  ?  144 CYS   A N   1 
ATOM   1163  C CA  . CYS   A 1 144 ? -39.671 -6.153  34.770  1.00 32.82  ?  144 CYS   A CA  1 
ATOM   1164  C C   . CYS   A 1 144 ? -40.387 -5.553  35.974  1.00 32.43  ?  144 CYS   A C   1 
ATOM   1165  O O   . CYS   A 1 144 ? -40.100 -4.433  36.405  1.00 36.16  ?  144 CYS   A O   1 
ATOM   1166  C CB  . CYS   A 1 144 ? -38.705 -7.246  35.243  1.00 30.40  ?  144 CYS   A CB  1 
ATOM   1167  S SG  . CYS   A 1 144 ? -37.800 -8.068  33.926  1.00 36.45  ?  144 CYS   A SG  1 
ATOM   1168  N N   . LYS   A 1 145 ? -41.316 -6.325  36.529  1.00 31.71  ?  145 LYS   A N   1 
ATOM   1169  C CA  . LYS   A 1 145 ? -41.986 -5.971  37.772  1.00 34.68  ?  145 LYS   A CA  1 
ATOM   1170  C C   . LYS   A 1 145 ? -41.295 -6.651  38.949  1.00 33.57  ?  145 LYS   A C   1 
ATOM   1171  O O   . LYS   A 1 145 ? -40.873 -7.809  38.850  1.00 29.41  ?  145 LYS   A O   1 
ATOM   1172  C CB  . LYS   A 1 145 ? -43.463 -6.366  37.725  1.00 36.62  ?  145 LYS   A CB  1 
ATOM   1173  C CG  . LYS   A 1 145 ? -44.227 -6.098  39.015  1.00 39.21  ?  145 LYS   A CG  1 
ATOM   1174  C CD  . LYS   A 1 145 ? -45.726 -6.333  38.825  1.00 42.72  ?  145 LYS   A CD  1 
ATOM   1175  C CE  . LYS   A 1 145 ? -46.517 -5.854  40.035  1.00 49.49  ?  145 LYS   A CE  1 
ATOM   1176  N NZ  . LYS   A 1 145 ? -46.193 -4.439  40.387  1.00 43.47  ?  145 LYS   A NZ  1 
ATOM   1177  N N   . ALA   A 1 146 ? -41.168 -5.920  40.058  1.00 30.94  ?  146 ALA   A N   1 
ATOM   1178  C CA  . ALA   A 1 146 ? -40.542 -6.426  41.277  1.00 31.36  ?  146 ALA   A CA  1 
ATOM   1179  C C   . ALA   A 1 146 ? -41.636 -6.648  42.309  1.00 32.13  ?  146 ALA   A C   1 
ATOM   1180  O O   . ALA   A 1 146 ? -42.164 -5.683  42.874  1.00 36.19  ?  146 ALA   A O   1 
ATOM   1181  C CB  . ALA   A 1 146 ? -39.482 -5.459  41.806  1.00 27.80  ?  146 ALA   A CB  1 
ATOM   1182  N N   . ILE   A 1 147 ? -41.966 -7.914  42.561  1.00 30.54  ?  147 ILE   A N   1 
ATOM   1183  C CA  . ILE   A 1 147 ? -43.045 -8.286  43.468  1.00 26.09  ?  147 ILE   A CA  1 
ATOM   1184  C C   . ILE   A 1 147 ? -42.435 -8.697  44.801  1.00 26.47  ?  147 ILE   A C   1 
ATOM   1185  O O   . ILE   A 1 147 ? -41.463 -9.460  44.837  1.00 27.04  ?  147 ILE   A O   1 
ATOM   1186  C CB  . ILE   A 1 147 ? -43.902 -9.417  42.870  1.00 28.88  ?  147 ILE   A CB  1 
ATOM   1187  C CG1 . ILE   A 1 147 ? -44.439 -9.008  41.494  1.00 33.86  ?  147 ILE   A CG1 1 
ATOM   1188  C CG2 . ILE   A 1 147 ? -45.049 -9.774  43.805  1.00 26.07  ?  147 ILE   A CG2 1 
ATOM   1189  C CD1 . ILE   A 1 147 ? -45.018 -10.156 40.678  1.00 32.56  ?  147 ILE   A CD1 1 
ATOM   1190  N N   . ASN   A 1 148 ? -42.996 -8.187  45.897  1.00 27.71  ?  148 ASN   A N   1 
ATOM   1191  C CA  . ASN   A 1 148 ? -42.532 -8.497  47.245  1.00 28.60  ?  148 ASN   A CA  1 
ATOM   1192  C C   . ASN   A 1 148 ? -43.633 -9.213  48.017  1.00 30.81  ?  148 ASN   A C   1 
ATOM   1193  O O   . ASN   A 1 148 ? -44.765 -8.721  48.087  1.00 30.09  ?  148 ASN   A O   1 
ATOM   1194  C CB  . ASN   A 1 148 ? -42.115 -7.226  47.988  1.00 28.32  ?  148 ASN   A CB  1 
ATOM   1195  C CG  . ASN   A 1 148 ? -41.017 -6.477  47.277  1.00 26.14  ?  148 ASN   A CG  1 
ATOM   1196  O OD1 . ASN   A 1 148 ? -40.023 -7.067  46.861  1.00 23.80  ?  148 ASN   A OD1 1 
ATOM   1197  N ND2 . ASN   A 1 148 ? -41.190 -5.171  47.124  1.00 26.58  ?  148 ASN   A ND2 1 
ATOM   1198  N N   . ILE   A 1 149 ? -43.298 -10.362 48.612  1.00 27.85  ?  149 ILE   A N   1 
ATOM   1199  C CA  . ILE   A 1 149 ? -44.289 -11.171 49.318  1.00 33.04  ?  149 ILE   A CA  1 
ATOM   1200  C C   . ILE   A 1 149 ? -43.767 -11.622 50.682  1.00 30.19  ?  149 ILE   A C   1 
ATOM   1201  O O   . ILE   A 1 149 ? -43.834 -12.810 51.027  1.00 27.61  ?  149 ILE   A O   1 
ATOM   1202  C CB  . ILE   A 1 149 ? -44.707 -12.380 48.461  1.00 27.92  ?  149 ILE   A CB  1 
ATOM   1203  C CG1 . ILE   A 1 149 ? -43.474 -13.138 47.975  1.00 30.14  ?  149 ILE   A CG1 1 
ATOM   1204  C CG2 . ILE   A 1 149 ? -45.536 -11.933 47.264  1.00 33.91  ?  149 ILE   A CG2 1 
ATOM   1205  C CD1 . ILE   A 1 149 ? -43.810 -14.442 47.306  1.00 26.14  ?  149 ILE   A CD1 1 
ATOM   1206  N N   . VAL   A 1 150 ? -43.271 -10.679 51.487  1.00 30.63  ?  150 VAL   A N   1 
ATOM   1207  C CA  . VAL   A 1 150 ? -42.799 -11.032 52.825  1.00 28.58  ?  150 VAL   A CA  1 
ATOM   1208  C C   . VAL   A 1 150 ? -43.982 -11.430 53.707  1.00 31.93  ?  150 VAL   A C   1 
ATOM   1209  O O   . VAL   A 1 150 ? -45.123 -10.984 53.510  1.00 25.28  ?  150 VAL   A O   1 
ATOM   1210  C CB  . VAL   A 1 150 ? -42.011 -9.870  53.459  1.00 26.75  ?  150 VAL   A CB  1 
ATOM   1211  C CG1 . VAL   A 1 150 ? -42.964 -8.796  53.974  1.00 30.18  ?  150 VAL   A CG1 1 
ATOM   1212  C CG2 . VAL   A 1 150 ? -41.117 -10.373 54.576  1.00 24.41  ?  150 VAL   A CG2 1 
ATOM   1213  N N   . THR   A 1 151 ? -43.703 -12.287 54.693  1.00 33.63  ?  151 THR   A N   1 
ATOM   1214  C CA  . THR   A 1 151 ? -44.723 -12.745 55.629  1.00 30.33  ?  151 THR   A CA  1 
ATOM   1215  C C   . THR   A 1 151 ? -45.438 -11.566 56.279  1.00 32.87  ?  151 THR   A C   1 
ATOM   1216  O O   . THR   A 1 151 ? -44.830 -10.538 56.584  1.00 34.59  ?  151 THR   A O   1 
ATOM   1217  C CB  . THR   A 1 151 ? -44.083 -13.634 56.703  1.00 29.88  ?  151 THR   A CB  1 
ATOM   1218  O OG1 . THR   A 1 151 ? -45.039 -13.921 57.733  1.00 37.90  ?  151 THR   A OG1 1 
ATOM   1219  C CG2 . THR   A 1 151 ? -42.891 -12.945 57.325  1.00 26.39  ?  151 THR   A CG2 1 
ATOM   1220  N N   . GLU   A 1 152 ? -46.748 -11.716 56.480  1.00 36.56  ?  152 GLU   A N   1 
ATOM   1221  C CA  . GLU   A 1 152 ? -47.506 -10.691 57.186  1.00 40.16  ?  152 GLU   A CA  1 
ATOM   1222  C C   . GLU   A 1 152 ? -46.977 -10.458 58.596  1.00 34.46  ?  152 GLU   A C   1 
ATOM   1223  O O   . GLU   A 1 152 ? -47.212 -9.386  59.166  1.00 32.31  ?  152 GLU   A O   1 
ATOM   1224  C CB  . GLU   A 1 152 ? -48.989 -11.074 57.228  1.00 41.74  ?  152 GLU   A CB  1 
ATOM   1225  C CG  . GLU   A 1 152 ? -49.620 -11.188 55.840  1.00 51.90  ?  152 GLU   A CG  1 
ATOM   1226  C CD  . GLU   A 1 152 ? -51.062 -11.679 55.872  1.00 63.88  ?  152 GLU   A CD  1 
ATOM   1227  O OE1 . GLU   A 1 152 ? -51.554 -12.020 56.974  1.00 59.09  ?  152 GLU   A OE1 1 
ATOM   1228  O OE2 . GLU   A 1 152 ? -51.699 -11.722 54.793  1.00 56.90  ?  152 GLU   A OE2 1 
ATOM   1229  N N   . LYS   A 1 153 ? -46.252 -11.429 59.158  1.00 31.30  ?  153 LYS   A N   1 
ATOM   1230  C CA  . LYS   A 1 153 ? -45.683 -11.259 60.490  1.00 34.18  ?  153 LYS   A CA  1 
ATOM   1231  C C   . LYS   A 1 153 ? -44.755 -10.055 60.553  1.00 32.20  ?  153 LYS   A C   1 
ATOM   1232  O O   . LYS   A 1 153 ? -44.617 -9.439  61.617  1.00 34.11  ?  153 LYS   A O   1 
ATOM   1233  C CB  . LYS   A 1 153 ? -44.934 -12.526 60.911  1.00 33.94  ?  153 LYS   A CB  1 
ATOM   1234  C CG  . LYS   A 1 153 ? -45.828 -13.694 61.291  1.00 32.18  ?  153 LYS   A CG  1 
ATOM   1235  C CD  . LYS   A 1 153 ? -46.505 -13.446 62.627  1.00 37.67  ?  153 LYS   A CD  1 
ATOM   1236  C CE  . LYS   A 1 153 ? -47.131 -14.719 63.183  1.00 48.07  ?  153 LYS   A CE  1 
ATOM   1237  N NZ  . LYS   A 1 153 ? -47.688 -14.532 64.566  1.00 50.98  ?  153 LYS   A NZ  1 
ATOM   1238  N N   . ALA   A 1 154 ? -44.124 -9.697  59.429  1.00 31.66  ?  154 ALA   A N   1 
ATOM   1239  C CA  . ALA   A 1 154 ? -43.192 -8.573  59.413  1.00 31.81  ?  154 ALA   A CA  1 
ATOM   1240  C C   . ALA   A 1 154 ? -43.873 -7.240  59.692  1.00 33.79  ?  154 ALA   A C   1 
ATOM   1241  O O   . ALA   A 1 154 ? -43.198 -6.289  60.099  1.00 31.60  ?  154 ALA   A O   1 
ATOM   1242  C CB  . ALA   A 1 154 ? -42.468 -8.503  58.068  1.00 29.25  ?  154 ALA   A CB  1 
ATOM   1243  N N   . PHE   A 1 155 ? -45.186 -7.149  59.493  1.00 31.60  ?  155 PHE   A N   1 
ATOM   1244  C CA  . PHE   A 1 155 ? -45.911 -5.893  59.634  1.00 33.39  ?  155 PHE   A CA  1 
ATOM   1245  C C   . PHE   A 1 155 ? -46.408 -5.643  61.053  1.00 41.87  ?  155 PHE   A C   1 
ATOM   1246  O O   . PHE   A 1 155 ? -46.903 -4.546  61.337  1.00 35.83  ?  155 PHE   A O   1 
ATOM   1247  C CB  . PHE   A 1 155 ? -47.098 -5.866  58.666  1.00 34.36  ?  155 PHE   A CB  1 
ATOM   1248  C CG  . PHE   A 1 155 ? -46.719 -6.132  57.232  1.00 39.65  ?  155 PHE   A CG  1 
ATOM   1249  C CD1 . PHE   A 1 155 ? -45.518 -5.674  56.718  1.00 45.89  ?  155 PHE   A CD1 1 
ATOM   1250  C CD2 . PHE   A 1 155 ? -47.563 -6.849  56.402  1.00 48.03  ?  155 PHE   A CD2 1 
ATOM   1251  C CE1 . PHE   A 1 155 ? -45.166 -5.923  55.397  1.00 42.95  ?  155 PHE   A CE1 1 
ATOM   1252  C CE2 . PHE   A 1 155 ? -47.216 -7.098  55.084  1.00 46.69  ?  155 PHE   A CE2 1 
ATOM   1253  C CZ  . PHE   A 1 155 ? -46.017 -6.635  54.585  1.00 41.20  ?  155 PHE   A CZ  1 
ATOM   1254  N N   . ASP   A 1 156 ? -46.297 -6.629  61.938  1.00 36.30  ?  156 ASP   A N   1 
ATOM   1255  C CA  . ASP   A 1 156 ? -46.671 -6.494  63.343  1.00 33.19  ?  156 ASP   A CA  1 
ATOM   1256  C C   . ASP   A 1 156 ? -45.363 -6.309  64.103  1.00 33.40  ?  156 ASP   A C   1 
ATOM   1257  O O   . ASP   A 1 156 ? -44.671 -7.282  64.409  1.00 34.92  ?  156 ASP   A O   1 
ATOM   1258  C CB  . ASP   A 1 156 ? -47.445 -7.726  63.805  1.00 34.58  ?  156 ASP   A CB  1 
ATOM   1259  C CG  . ASP   A 1 156 ? -48.059 -7.563  65.178  1.00 39.75  ?  156 ASP   A CG  1 
ATOM   1260  O OD1 . ASP   A 1 156 ? -47.578 -6.733  65.978  1.00 39.32  ?  156 ASP   A OD1 1 
ATOM   1261  O OD2 . ASP   A 1 156 ? -49.030 -8.292  65.471  1.00 50.17  ?  156 ASP   A OD2 1 
ATOM   1262  N N   . SER   A 1 157 ? -45.012 -5.051  64.385  1.00 33.55  ?  157 SER   A N   1 
ATOM   1263  C CA  . SER   A 1 157 ? -43.662 -4.739  64.853  1.00 38.65  ?  157 SER   A CA  1 
ATOM   1264  C C   . SER   A 1 157 ? -43.377 -5.368  66.209  1.00 36.29  ?  157 SER   A C   1 
ATOM   1265  O O   . SER   A 1 157 ? -42.422 -6.137  66.370  1.00 33.90  ?  157 SER   A O   1 
ATOM   1266  C CB  . SER   A 1 157 ? -43.466 -3.224  64.926  1.00 38.94  ?  157 SER   A CB  1 
ATOM   1267  O OG  . SER   A 1 157 ? -43.122 -2.695  63.663  1.00 37.06  ?  157 SER   A OG  1 
ATOM   1268  N N   . GLU   A 1 158 ? -44.192 -5.038  67.206  1.00 34.92  ?  158 GLU   A N   1 
ATOM   1269  C CA  . GLU   A 1 158 ? -43.888 -5.431  68.571  1.00 35.41  ?  158 GLU   A CA  1 
ATOM   1270  C C   . GLU   A 1 158 ? -44.080 -6.921  68.828  1.00 31.90  ?  158 GLU   A C   1 
ATOM   1271  O O   . GLU   A 1 158 ? -43.615 -7.415  69.859  1.00 33.50  ?  158 GLU   A O   1 
ATOM   1272  C CB  . GLU   A 1 158 ? -44.752 -4.621  69.538  1.00 40.27  ?  158 GLU   A CB  1 
ATOM   1273  C CG  . GLU   A 1 158 ? -44.520 -3.118  69.454  1.00 46.20  ?  158 GLU   A CG  1 
ATOM   1274  C CD  . GLU   A 1 158 ? -45.280 -2.460  68.312  1.00 58.73  ?  158 GLU   A CD  1 
ATOM   1275  O OE1 . GLU   A 1 158 ? -46.219 -3.091  67.766  1.00 57.48  ?  158 GLU   A OE1 1 
ATOM   1276  O OE2 . GLU   A 1 158 ? -44.935 -1.309  67.960  1.00 56.37  ?  158 GLU   A OE2 1 
ATOM   1277  N N   . THR   A 1 159 ? -44.737 -7.646  67.933  1.00 27.46  ?  159 THR   A N   1 
ATOM   1278  C CA  . THR   A 1 159 ? -45.052 -9.050  68.166  1.00 31.56  ?  159 THR   A CA  1 
ATOM   1279  C C   . THR   A 1 159 ? -43.897 -9.915  67.672  1.00 27.03  ?  159 THR   A C   1 
ATOM   1280  O O   . THR   A 1 159 ? -43.639 -9.990  66.468  1.00 29.43  ?  159 THR   A O   1 
ATOM   1281  C CB  . THR   A 1 159 ? -46.357 -9.425  67.471  1.00 33.15  ?  159 THR   A CB  1 
ATOM   1282  O OG1 . THR   A 1 159 ? -47.391 -8.531  67.895  1.00 33.93  ?  159 THR   A OG1 1 
ATOM   1283  C CG2 . THR   A 1 159 ? -46.755 -10.855 67.812  1.00 29.98  ?  159 THR   A CG2 1 
ATOM   1284  N N   . TYR   A 1 160 ? -43.217 -10.582 68.603  1.00 28.42  ?  160 TYR   A N   1 
ATOM   1285  C CA  . TYR   A 1 160 ? -42.109 -11.463 68.257  1.00 29.01  ?  160 TYR   A CA  1 
ATOM   1286  C C   . TYR   A 1 160 ? -42.534 -12.516 67.234  1.00 27.69  ?  160 TYR   A C   1 
ATOM   1287  O O   . TYR   A 1 160 ? -43.650 -13.039 67.276  1.00 29.73  ?  160 TYR   A O   1 
ATOM   1288  C CB  . TYR   A 1 160 ? -41.564 -12.148 69.521  1.00 27.83  ?  160 TYR   A CB  1 
ATOM   1289  C CG  . TYR   A 1 160 ? -40.419 -13.094 69.230  1.00 28.04  ?  160 TYR   A CG  1 
ATOM   1290  C CD1 . TYR   A 1 160 ? -40.654 -14.422 68.878  1.00 27.92  ?  160 TYR   A CD1 1 
ATOM   1291  C CD2 . TYR   A 1 160 ? -39.101 -12.654 69.271  1.00 32.96  ?  160 TYR   A CD2 1 
ATOM   1292  C CE1 . TYR   A 1 160 ? -39.606 -15.282 68.576  1.00 27.28  ?  160 TYR   A CE1 1 
ATOM   1293  C CE2 . TYR   A 1 160 ? -38.046 -13.514 68.982  1.00 29.87  ?  160 TYR   A CE2 1 
ATOM   1294  C CZ  . TYR   A 1 160 ? -38.310 -14.824 68.633  1.00 24.67  ?  160 TYR   A CZ  1 
ATOM   1295  O OH  . TYR   A 1 160 ? -37.268 -15.675 68.336  1.00 29.22  ?  160 TYR   A OH  1 
ATOM   1296  N N   . ASP   A 1 161 ? -41.634 -12.813 66.300  1.00 27.00  ?  161 ASP   A N   1 
ATOM   1297  C CA  . ASP   A 1 161 ? -41.730 -14.001 65.466  1.00 26.13  ?  161 ASP   A CA  1 
ATOM   1298  C C   . ASP   A 1 161 ? -40.319 -14.449 65.121  1.00 25.84  ?  161 ASP   A C   1 
ATOM   1299  O O   . ASP   A 1 161 ? -39.395 -13.631 65.045  1.00 21.86  ?  161 ASP   A O   1 
ATOM   1300  C CB  . ASP   A 1 161 ? -42.540 -13.760 64.191  1.00 29.70  ?  161 ASP   A CB  1 
ATOM   1301  C CG  . ASP   A 1 161 ? -42.875 -15.053 63.457  1.00 35.31  ?  161 ASP   A CG  1 
ATOM   1302  O OD1 . ASP   A 1 161 ? -42.032 -15.553 62.675  1.00 27.47  ?  161 ASP   A OD1 1 
ATOM   1303  O OD2 . ASP   A 1 161 ? -43.989 -15.579 63.680  1.00 36.48  ?  161 ASP   A OD2 1 
ATOM   1304  N N   . ASP   A 1 162 ? -40.160 -15.760 64.911  1.00 24.26  ?  162 ASP   A N   1 
ATOM   1305  C CA  . ASP   A 1 162 ? -38.828 -16.305 64.652  1.00 26.03  ?  162 ASP   A CA  1 
ATOM   1306  C C   . ASP   A 1 162 ? -38.294 -15.920 63.278  1.00 25.19  ?  162 ASP   A C   1 
ATOM   1307  O O   . ASP   A 1 162 ? -37.079 -15.744 63.118  1.00 23.75  ?  162 ASP   A O   1 
ATOM   1308  C CB  . ASP   A 1 162 ? -38.834 -17.828 64.771  1.00 28.58  ?  162 ASP   A CB  1 
ATOM   1309  C CG  . ASP   A 1 162 ? -38.626 -18.305 66.186  1.00 28.07  ?  162 ASP   A CG  1 
ATOM   1310  O OD1 . ASP   A 1 162 ? -38.112 -17.521 67.010  1.00 24.80  ?  162 ASP   A OD1 1 
ATOM   1311  O OD2 . ASP   A 1 162 ? -38.975 -19.474 66.464  1.00 32.31  ?  162 ASP   A OD2 1 
ATOM   1312  N N   . TRP   A 1 163 ? -39.166 -15.806 62.273  1.00 26.73  ?  163 TRP   A N   1 
ATOM   1313  C CA  . TRP   A 1 163 ? -38.737 -15.682 60.882  1.00 24.53  ?  163 TRP   A CA  1 
ATOM   1314  C C   . TRP   A 1 163 ? -39.525 -14.581 60.174  1.00 24.03  ?  163 TRP   A C   1 
ATOM   1315  O O   . TRP   A 1 163 ? -40.248 -14.830 59.211  1.00 25.25  ?  163 TRP   A O   1 
ATOM   1316  C CB  . TRP   A 1 163 ? -38.901 -17.012 60.153  1.00 25.55  ?  163 TRP   A CB  1 
ATOM   1317  C CG  . TRP   A 1 163 ? -38.501 -18.198 60.971  1.00 24.30  ?  163 TRP   A CG  1 
ATOM   1318  C CD1 . TRP   A 1 163 ? -39.334 -19.108 61.541  1.00 24.25  ?  163 TRP   A CD1 1 
ATOM   1319  C CD2 . TRP   A 1 163 ? -37.168 -18.598 61.324  1.00 25.92  ?  163 TRP   A CD2 1 
ATOM   1320  N NE1 . TRP   A 1 163 ? -38.609 -20.056 62.217  1.00 23.81  ?  163 TRP   A NE1 1 
ATOM   1321  C CE2 . TRP   A 1 163 ? -37.276 -19.764 62.102  1.00 22.28  ?  163 TRP   A CE2 1 
ATOM   1322  C CE3 . TRP   A 1 163 ? -35.892 -18.089 61.047  1.00 26.02  ?  163 TRP   A CE3 1 
ATOM   1323  C CZ2 . TRP   A 1 163 ? -36.158 -20.432 62.610  1.00 25.95  ?  163 TRP   A CZ2 1 
ATOM   1324  C CZ3 . TRP   A 1 163 ? -34.782 -18.754 61.553  1.00 18.35  ?  163 TRP   A CZ3 1 
ATOM   1325  C CH2 . TRP   A 1 163 ? -34.923 -19.910 62.323  1.00 21.30  ?  163 TRP   A CH2 1 
ATOM   1326  N N   . LYS   A 1 164 ? -39.355 -13.339 60.633  1.00 21.81  ?  164 LYS   A N   1 
ATOM   1327  C CA  . LYS   A 1 164 ? -40.069 -12.220 60.022  1.00 22.00  ?  164 LYS   A CA  1 
ATOM   1328  C C   . LYS   A 1 164 ? -39.584 -11.883 58.617  1.00 22.86  ?  164 LYS   A C   1 
ATOM   1329  O O   . LYS   A 1 164 ? -40.138 -10.961 58.003  1.00 23.61  ?  164 LYS   A O   1 
ATOM   1330  C CB  . LYS   A 1 164 ? -39.963 -10.980 60.906  1.00 24.15  ?  164 LYS   A CB  1 
ATOM   1331  C CG  . LYS   A 1 164 ? -40.868 -11.030 62.131  1.00 25.82  ?  164 LYS   A CG  1 
ATOM   1332  C CD  . LYS   A 1 164 ? -40.879 -9.703  62.868  1.00 27.10  ?  164 LYS   A CD  1 
ATOM   1333  C CE  . LYS   A 1 164 ? -41.981 -9.659  63.907  1.00 27.43  ?  164 LYS   A CE  1 
ATOM   1334  N NZ  . LYS   A 1 164 ? -42.077 -8.318  64.559  1.00 25.74  ?  164 LYS   A NZ  1 
ATOM   1335  N N   . GLY   A 1 165 ? -38.575 -12.576 58.096  1.00 21.58  ?  165 GLY   A N   1 
ATOM   1336  C CA  . GLY   A 1 165 ? -38.174 -12.407 56.719  1.00 21.71  ?  165 GLY   A CA  1 
ATOM   1337  C C   . GLY   A 1 165 ? -38.710 -13.446 55.765  1.00 23.76  ?  165 GLY   A C   1 
ATOM   1338  O O   . GLY   A 1 165 ? -38.389 -13.392 54.571  1.00 22.90  ?  165 GLY   A O   1 
ATOM   1339  N N   . ASP   A 1 166 ? -39.519 -14.388 56.250  1.00 22.41  ?  166 ASP   A N   1 
ATOM   1340  C CA  . ASP   A 1 166 ? -39.990 -15.491 55.423  1.00 23.52  ?  166 ASP   A CA  1 
ATOM   1341  C C   . ASP   A 1 166 ? -40.779 -14.984 54.222  1.00 26.85  ?  166 ASP   A C   1 
ATOM   1342  O O   . ASP   A 1 166 ? -41.394 -13.913 54.257  1.00 24.51  ?  166 ASP   A O   1 
ATOM   1343  C CB  . ASP   A 1 166 ? -40.882 -16.430 56.237  1.00 25.04  ?  166 ASP   A CB  1 
ATOM   1344  C CG  . ASP   A 1 166 ? -40.106 -17.492 56.979  1.00 25.68  ?  166 ASP   A CG  1 
ATOM   1345  O OD1 . ASP   A 1 166 ? -38.865 -17.580 56.825  1.00 23.10  ?  166 ASP   A OD1 1 
ATOM   1346  O OD2 . ASP   A 1 166 ? -40.754 -18.249 57.732  1.00 30.59  ?  166 ASP   A OD2 1 
ATOM   1347  N N   . PHE   A 1 167 ? -40.754 -15.775 53.150  1.00 24.05  ?  167 PHE   A N   1 
ATOM   1348  C CA  . PHE   A 1 167 ? -41.743 -15.629 52.094  1.00 27.75  ?  167 PHE   A CA  1 
ATOM   1349  C C   . PHE   A 1 167 ? -43.128 -15.954 52.633  1.00 30.16  ?  167 PHE   A C   1 
ATOM   1350  O O   . PHE   A 1 167 ? -43.290 -16.795 53.521  1.00 32.30  ?  167 PHE   A O   1 
ATOM   1351  C CB  . PHE   A 1 167 ? -41.451 -16.576 50.934  1.00 23.50  ?  167 PHE   A CB  1 
ATOM   1352  C CG  . PHE   A 1 167 ? -40.342 -16.136 50.038  1.00 21.91  ?  167 PHE   A CG  1 
ATOM   1353  C CD1 . PHE   A 1 167 ? -39.030 -16.190 50.457  1.00 22.62  ?  167 PHE   A CD1 1 
ATOM   1354  C CD2 . PHE   A 1 167 ? -40.613 -15.720 48.745  1.00 23.33  ?  167 PHE   A CD2 1 
ATOM   1355  C CE1 . PHE   A 1 167 ? -38.006 -15.806 49.611  1.00 22.84  ?  167 PHE   A CE1 1 
ATOM   1356  C CE2 . PHE   A 1 167 ? -39.591 -15.337 47.897  1.00 23.64  ?  167 PHE   A CE2 1 
ATOM   1357  C CZ  . PHE   A 1 167 ? -38.287 -15.383 48.331  1.00 20.46  ?  167 PHE   A CZ  1 
ATOM   1358  N N   . ASP   A 1 168 ? -44.135 -15.291 52.071  1.00 29.13  ?  168 ASP   A N   1 
ATOM   1359  C CA  . ASP   A 1 168 ? -45.531 -15.704 52.211  1.00 30.99  ?  168 ASP   A CA  1 
ATOM   1360  C C   . ASP   A 1 168 ? -45.779 -16.772 51.149  1.00 28.80  ?  168 ASP   A C   1 
ATOM   1361  O O   . ASP   A 1 168 ? -45.955 -16.459 49.971  1.00 29.73  ?  168 ASP   A O   1 
ATOM   1362  C CB  . ASP   A 1 168 ? -46.453 -14.497 52.046  1.00 29.67  ?  168 ASP   A CB  1 
ATOM   1363  C CG  . ASP   A 1 168 ? -47.935 -14.827 52.232  1.00 37.52  ?  168 ASP   A CG  1 
ATOM   1364  O OD1 . ASP   A 1 168 ? -48.406 -15.899 51.784  1.00 32.31  ?  168 ASP   A OD1 1 
ATOM   1365  O OD2 . ASP   A 1 168 ? -48.646 -13.971 52.809  1.00 39.51  ?  168 ASP   A OD2 1 
ATOM   1366  N N   . ILE   A 1 169 ? -45.793 -18.043 51.561  1.00 29.77  ?  169 ILE   A N   1 
ATOM   1367  C CA  . ILE   A 1 169 ? -45.828 -19.140 50.592  1.00 35.63  ?  169 ILE   A CA  1 
ATOM   1368  C C   . ILE   A 1 169 ? -47.124 -19.130 49.794  1.00 31.39  ?  169 ILE   A C   1 
ATOM   1369  O O   . ILE   A 1 169 ? -47.133 -19.474 48.607  1.00 33.19  ?  169 ILE   A O   1 
ATOM   1370  C CB  . ILE   A 1 169 ? -45.608 -20.491 51.309  1.00 37.21  ?  169 ILE   A CB  1 
ATOM   1371  C CG1 . ILE   A 1 169 ? -44.229 -20.517 51.981  1.00 38.50  ?  169 ILE   A CG1 1 
ATOM   1372  C CG2 . ILE   A 1 169 ? -45.757 -21.662 50.337  1.00 32.16  ?  169 ILE   A CG2 1 
ATOM   1373  C CD1 . ILE   A 1 169 ? -43.059 -20.387 51.016  1.00 28.86  ?  169 ILE   A CD1 1 
ATOM   1374  N N   . LYS   A 1 170 ? -48.233 -18.730 50.416  1.00 26.85  ?  170 LYS   A N   1 
ATOM   1375  C CA  . LYS   A 1 170 ? -49.494 -18.685 49.686  1.00 32.61  ?  170 LYS   A CA  1 
ATOM   1376  C C   . LYS   A 1 170 ? -49.467 -17.603 48.611  1.00 34.13  ?  170 LYS   A C   1 
ATOM   1377  O O   . LYS   A 1 170 ? -49.994 -17.801 47.508  1.00 34.05  ?  170 LYS   A O   1 
ATOM   1378  C CB  . LYS   A 1 170 ? -50.653 -18.470 50.659  1.00 31.96  ?  170 LYS   A CB  1 
ATOM   1379  C CG  . LYS   A 1 170 ? -52.024 -18.591 50.025  1.00 34.04  ?  170 LYS   A CG  1 
ATOM   1380  C CD  . LYS   A 1 170 ? -53.116 -18.365 51.058  1.00 41.01  ?  170 LYS   A CD  1 
ATOM   1381  C CE  . LYS   A 1 170 ? -54.503 -18.375 50.415  1.00 37.51  ?  170 LYS   A CE  1 
ATOM   1382  N NZ  . LYS   A 1 170 ? -55.578 -18.222 51.433  1.00 45.79  ?  170 LYS   A NZ  1 
ATOM   1383  N N   . LYS   A 1 171 ? -48.845 -16.456 48.904  1.00 30.20  ?  171 LYS   A N   1 
ATOM   1384  C CA  . LYS   A 1 171 ? -48.699 -15.420 47.887  1.00 31.43  ?  171 LYS   A CA  1 
ATOM   1385  C C   . LYS   A 1 171 ? -47.727 -15.841 46.792  1.00 30.25  ?  171 LYS   A C   1 
ATOM   1386  O O   . LYS   A 1 171 ? -47.895 -15.445 45.635  1.00 28.17  ?  171 LYS   A O   1 
ATOM   1387  C CB  . LYS   A 1 171 ? -48.231 -14.112 48.519  1.00 34.58  ?  171 LYS   A CB  1 
ATOM   1388  C CG  . LYS   A 1 171 ? -49.229 -13.458 49.457  1.00 32.95  ?  171 LYS   A CG  1 
ATOM   1389  C CD  . LYS   A 1 171 ? -48.630 -12.189 50.028  1.00 38.60  ?  171 LYS   A CD  1 
ATOM   1390  C CE  . LYS   A 1 171 ? -49.682 -11.238 50.576  1.00 43.56  ?  171 LYS   A CE  1 
ATOM   1391  N NZ  . LYS   A 1 171 ? -49.125 -9.849  50.728  1.00 42.82  ?  171 LYS   A NZ  1 
ATOM   1392  N N   . LEU   A 1 172 ? -46.700 -16.623 47.133  1.00 32.33  ?  172 LEU   A N   1 
ATOM   1393  C CA  . LEU   A 1 172 ? -45.801 -17.142 46.106  1.00 30.22  ?  172 LEU   A CA  1 
ATOM   1394  C C   . LEU   A 1 172 ? -46.554 -18.029 45.130  1.00 32.65  ?  172 LEU   A C   1 
ATOM   1395  O O   . LEU   A 1 172 ? -46.378 -17.917 43.911  1.00 27.43  ?  172 LEU   A O   1 
ATOM   1396  C CB  . LEU   A 1 172 ? -44.652 -17.919 46.744  1.00 29.94  ?  172 LEU   A CB  1 
ATOM   1397  C CG  . LEU   A 1 172 ? -43.717 -18.621 45.754  1.00 30.47  ?  172 LEU   A CG  1 
ATOM   1398  C CD1 . LEU   A 1 172 ? -43.025 -17.618 44.834  1.00 29.69  ?  172 LEU   A CD1 1 
ATOM   1399  C CD2 . LEU   A 1 172 ? -42.688 -19.487 46.484  1.00 27.11  ?  172 LEU   A CD2 1 
ATOM   1400  N N   . LYS   A 1 173 ? -47.405 -18.915 45.654  1.00 30.64  ?  173 LYS   A N   1 
ATOM   1401  C CA  . LYS   A 1 173 ? -48.225 -19.759 44.796  1.00 30.48  ?  173 LYS   A CA  1 
ATOM   1402  C C   . LYS   A 1 173 ? -49.227 -18.930 43.997  1.00 31.13  ?  173 LYS   A C   1 
ATOM   1403  O O   . LYS   A 1 173 ? -49.415 -19.165 42.798  1.00 31.63  ?  173 LYS   A O   1 
ATOM   1404  C CB  . LYS   A 1 173 ? -48.943 -20.808 45.645  1.00 34.48  ?  173 LYS   A CB  1 
ATOM   1405  C CG  . LYS   A 1 173 ? -48.026 -21.790 46.362  1.00 32.21  ?  173 LYS   A CG  1 
ATOM   1406  C CD  . LYS   A 1 173 ? -48.826 -22.658 47.331  1.00 42.29  ?  173 LYS   A CD  1 
ATOM   1407  C CE  . LYS   A 1 173 ? -47.948 -23.638 48.107  1.00 48.16  ?  173 LYS   A CE  1 
ATOM   1408  N NZ  . LYS   A 1 173 ? -47.443 -24.761 47.268  1.00 49.26  ?  173 LYS   A NZ  1 
ATOM   1409  N N   . GLU   A 1 174 ? -49.879 -17.955 44.643  1.00 32.57  ?  174 GLU   A N   1 
ATOM   1410  C CA  . GLU   A 1 174 ? -50.840 -17.102 43.943  1.00 30.80  ?  174 GLU   A CA  1 
ATOM   1411  C C   . GLU   A 1 174 ? -50.177 -16.305 42.826  1.00 31.64  ?  174 GLU   A C   1 
ATOM   1412  O O   . GLU   A 1 174 ? -50.764 -16.120 41.752  1.00 32.25  ?  174 GLU   A O   1 
ATOM   1413  C CB  . GLU   A 1 174 ? -51.522 -16.150 44.929  1.00 31.94  ?  174 GLU   A CB  1 
ATOM   1414  C CG  . GLU   A 1 174 ? -52.633 -16.776 45.763  1.00 34.47  ?  174 GLU   A CG  1 
ATOM   1415  C CD  . GLU   A 1 174 ? -53.027 -15.909 46.956  1.00 46.12  ?  174 GLU   A CD  1 
ATOM   1416  O OE1 . GLU   A 1 174 ? -52.353 -14.881 47.200  1.00 42.25  ?  174 GLU   A OE1 1 
ATOM   1417  O OE2 . GLU   A 1 174 ? -54.011 -16.257 47.653  1.00 46.84  ?  174 GLU   A OE2 1 
ATOM   1418  N N   . ASN   A 1 175 ? -48.963 -15.805 43.066  1.00 32.34  ?  175 ASN   A N   1 
ATOM   1419  C CA  . ASN   A 1 175 ? -48.277 -15.014 42.050  1.00 30.88  ?  175 ASN   A CA  1 
ATOM   1420  C C   . ASN   A 1 175 ? -47.786 -15.879 40.897  1.00 33.22  ?  175 ASN   A C   1 
ATOM   1421  O O   . ASN   A 1 175 ? -47.772 -15.422 39.749  1.00 36.67  ?  175 ASN   A O   1 
ATOM   1422  C CB  . ASN   A 1 175 ? -47.112 -14.243 42.675  1.00 32.96  ?  175 ASN   A CB  1 
ATOM   1423  C CG  . ASN   A 1 175 ? -47.539 -12.899 43.252  1.00 34.81  ?  175 ASN   A CG  1 
ATOM   1424  O OD1 . ASN   A 1 175 ? -47.571 -11.892 42.539  1.00 40.61  ?  175 ASN   A OD1 1 
ATOM   1425  N ND2 . ASN   A 1 175 ? -47.869 -12.876 44.547  1.00 29.61  ?  175 ASN   A ND2 1 
ATOM   1426  N N   . ILE   A 1 176 ? -47.374 -17.119 41.176  1.00 34.52  ?  176 ILE   A N   1 
ATOM   1427  C CA  . ILE   A 1 176 ? -46.950 -18.013 40.102  1.00 31.10  ?  176 ILE   A CA  1 
ATOM   1428  C C   . ILE   A 1 176 ? -48.126 -18.333 39.191  1.00 33.78  ?  176 ILE   A C   1 
ATOM   1429  O O   . ILE   A 1 176 ? -47.979 -18.410 37.967  1.00 38.89  ?  176 ILE   A O   1 
ATOM   1430  C CB  . ILE   A 1 176 ? -46.310 -19.289 40.681  1.00 29.68  ?  176 ILE   A CB  1 
ATOM   1431  C CG1 . ILE   A 1 176 ? -44.982 -18.953 41.359  1.00 38.04  ?  176 ILE   A CG1 1 
ATOM   1432  C CG2 . ILE   A 1 176 ? -46.093 -20.327 39.593  1.00 29.40  ?  176 ILE   A CG2 1 
ATOM   1433  C CD1 . ILE   A 1 176 ? -44.419 -20.062 42.246  1.00 37.97  ?  176 ILE   A CD1 1 
ATOM   1434  N N   . ALA   A 1 177 ? -49.316 -18.498 39.769  1.00 37.39  ?  177 ALA   A N   1 
ATOM   1435  C CA  . ALA   A 1 177 ? -50.491 -18.791 38.958  1.00 36.20  ?  177 ALA   A CA  1 
ATOM   1436  C C   . ALA   A 1 177 ? -50.957 -17.560 38.195  1.00 33.41  ?  177 ALA   A C   1 
ATOM   1437  O O   . ALA   A 1 177 ? -51.361 -17.662 37.030  1.00 38.77  ?  177 ALA   A O   1 
ATOM   1438  C CB  . ALA   A 1 177 ? -51.613 -19.333 39.839  1.00 32.84  ?  177 ALA   A CB  1 
ATOM   1439  N N   . GLN   A 1 178 ? -50.893 -16.385 38.827  1.00 32.92  ?  178 GLN   A N   1 
ATOM   1440  C CA  . GLN   A 1 178 ? -51.430 -15.179 38.204  1.00 36.15  ?  178 GLN   A CA  1 
ATOM   1441  C C   . GLN   A 1 178 ? -50.564 -14.725 37.038  1.00 36.13  ?  178 GLN   A C   1 
ATOM   1442  O O   . GLN   A 1 178 ? -51.074 -14.415 35.955  1.00 33.50  ?  178 GLN   A O   1 
ATOM   1443  C CB  . GLN   A 1 178 ? -51.553 -14.064 39.239  1.00 41.01  ?  178 GLN   A CB  1 
ATOM   1444  C CG  . GLN   A 1 178 ? -51.864 -12.707 38.630  1.00 45.29  ?  178 GLN   A CG  1 
ATOM   1445  C CD  . GLN   A 1 178 ? -51.601 -11.560 39.593  1.00 57.26  ?  178 GLN   A CD  1 
ATOM   1446  O OE1 . GLN   A 1 178 ? -51.339 -11.771 40.785  1.00 54.27  ?  178 GLN   A OE1 1 
ATOM   1447  N NE2 . GLN   A 1 178 ? -51.664 -10.333 39.077  1.00 55.33  ?  178 GLN   A NE2 1 
ATOM   1448  N N   . HIS   A 1 179 ? -49.251 -14.677 37.241  1.00 38.52  ?  179 HIS   A N   1 
ATOM   1449  C CA  . HIS   A 1 179 ? -48.329 -14.238 36.203  1.00 33.64  ?  179 HIS   A CA  1 
ATOM   1450  C C   . HIS   A 1 179 ? -47.866 -15.378 35.307  1.00 35.04  ?  179 HIS   A C   1 
ATOM   1451  O O   . HIS   A 1 179 ? -47.520 -15.141 34.145  1.00 36.28  ?  179 HIS   A O   1 
ATOM   1452  C CB  . HIS   A 1 179 ? -47.117 -13.555 36.841  1.00 31.61  ?  179 HIS   A CB  1 
ATOM   1453  C CG  . HIS   A 1 179 ? -47.456 -12.304 37.592  1.00 36.39  ?  179 HIS   A CG  1 
ATOM   1454  N ND1 . HIS   A 1 179 ? -47.576 -11.074 36.978  1.00 36.41  ?  179 HIS   A ND1 1 
ATOM   1455  C CD2 . HIS   A 1 179 ? -47.700 -12.092 38.907  1.00 35.34  ?  179 HIS   A CD2 1 
ATOM   1456  C CE1 . HIS   A 1 179 ? -47.877 -10.158 37.883  1.00 38.42  ?  179 HIS   A CE1 1 
ATOM   1457  N NE2 . HIS   A 1 179 ? -47.959 -10.750 39.061  1.00 37.19  ?  179 HIS   A NE2 1 
ATOM   1458  N N   . GLY   A 1 180 ? -47.860 -16.607 35.813  1.00 37.54  ?  180 GLY   A N   1 
ATOM   1459  C CA  . GLY   A 1 180 ? -47.396 -17.731 35.030  1.00 30.05  ?  180 GLY   A CA  1 
ATOM   1460  C C   . GLY   A 1 180 ? -45.911 -17.935 35.201  1.00 34.16  ?  180 GLY   A C   1 
ATOM   1461  O O   . GLY   A 1 180 ? -45.150 -16.964 35.280  1.00 33.58  ?  180 GLY   A O   1 
ATOM   1462  N N   . ALA   A 1 181 ? -45.485 -19.197 35.266  1.00 33.82  ?  181 ALA   A N   1 
ATOM   1463  C CA  . ALA   A 1 181 ? -44.075 -19.482 35.499  1.00 34.60  ?  181 ALA   A CA  1 
ATOM   1464  C C   . ALA   A 1 181 ? -43.195 -18.939 34.381  1.00 34.45  ?  181 ALA   A C   1 
ATOM   1465  O O   . ALA   A 1 181 ? -42.056 -18.528 34.631  1.00 36.55  ?  181 ALA   A O   1 
ATOM   1466  C CB  . ALA   A 1 181 ? -43.867 -20.987 35.663  1.00 35.78  ?  181 ALA   A CB  1 
ATOM   1467  N N   . ASP   A 1 182 ? -43.701 -18.916 33.148  1.00 34.46  ?  182 ASP   A N   1 
ATOM   1468  C CA  . ASP   A 1 182 ? -42.901 -18.442 32.026  1.00 34.77  ?  182 ASP   A CA  1 
ATOM   1469  C C   . ASP   A 1 182 ? -42.610 -16.952 32.089  1.00 34.92  ?  182 ASP   A C   1 
ATOM   1470  O O   . ASP   A 1 182 ? -41.736 -16.484 31.355  1.00 33.69  ?  182 ASP   A O   1 
ATOM   1471  C CB  . ASP   A 1 182 ? -43.600 -18.771 30.715  1.00 38.25  ?  182 ASP   A CB  1 
ATOM   1472  C CG  . ASP   A 1 182 ? -43.773 -20.254 30.520  1.00 49.86  ?  182 ASP   A CG  1 
ATOM   1473  O OD1 . ASP   A 1 182 ? -42.890 -21.009 30.985  1.00 48.12  ?  182 ASP   A OD1 1 
ATOM   1474  O OD2 . ASP   A 1 182 ? -44.787 -20.663 29.915  1.00 57.31  ?  182 ASP   A OD2 1 
ATOM   1475  N N   . ASN   A 1 183 ? -43.315 -16.201 32.931  1.00 33.08  ?  183 ASN   A N   1 
ATOM   1476  C CA  . ASN   A 1 183 ? -43.061 -14.779 33.093  1.00 29.25  ?  183 ASN   A CA  1 
ATOM   1477  C C   . ASN   A 1 183 ? -42.224 -14.460 34.316  1.00 26.15  ?  183 ASN   A C   1 
ATOM   1478  O O   . ASN   A 1 183 ? -41.798 -13.314 34.470  1.00 30.55  ?  183 ASN   A O   1 
ATOM   1479  C CB  . ASN   A 1 183 ? -44.376 -14.007 33.191  1.00 30.31  ?  183 ASN   A CB  1 
ATOM   1480  C CG  . ASN   A 1 183 ? -44.962 -13.689 31.842  1.00 36.64  ?  183 ASN   A CG  1 
ATOM   1481  O OD1 . ASN   A 1 183 ? -44.321 -13.047 31.004  1.00 32.44  ?  183 ASN   A OD1 1 
ATOM   1482  N ND2 . ASN   A 1 183 ? -46.185 -14.150 31.614  1.00 37.40  ?  183 ASN   A ND2 1 
ATOM   1483  N N   . ILE   A 1 184 ? -41.991 -15.426 35.194  1.00 27.23  ?  184 ILE   A N   1 
ATOM   1484  C CA  . ILE   A 1 184 ? -41.210 -15.194 36.402  1.00 28.71  ?  184 ILE   A CA  1 
ATOM   1485  C C   . ILE   A 1 184 ? -39.750 -15.403 36.024  1.00 27.30  ?  184 ILE   A C   1 
ATOM   1486  O O   . ILE   A 1 184 ? -39.301 -16.535 35.829  1.00 30.51  ?  184 ILE   A O   1 
ATOM   1487  C CB  . ILE   A 1 184 ? -41.653 -16.104 37.548  1.00 24.10  ?  184 ILE   A CB  1 
ATOM   1488  C CG1 . ILE   A 1 184 ? -43.163 -15.957 37.749  1.00 25.12  ?  184 ILE   A CG1 1 
ATOM   1489  C CG2 . ILE   A 1 184 ? -40.894 -15.762 38.817  1.00 23.09  ?  184 ILE   A CG2 1 
ATOM   1490  C CD1 . ILE   A 1 184 ? -43.722 -16.855 38.791  1.00 33.56  ?  184 ILE   A CD1 1 
ATOM   1491  N N   . VAL   A 1 185 ? -39.010 -14.297 35.895  1.00 26.69  ?  185 VAL   A N   1 
ATOM   1492  C CA  . VAL   A 1 185 ? -37.612 -14.393 35.488  1.00 27.09  ?  185 VAL   A CA  1 
ATOM   1493  C C   . VAL   A 1 185 ? -36.799 -15.122 36.547  1.00 29.09  ?  185 VAL   A C   1 
ATOM   1494  O O   . VAL   A 1 185 ? -35.958 -15.972 36.228  1.00 26.60  ?  185 VAL   A O   1 
ATOM   1495  C CB  . VAL   A 1 185 ? -37.041 -12.995 35.186  1.00 26.36  ?  185 VAL   A CB  1 
ATOM   1496  C CG1 . VAL   A 1 185 ? -35.564 -13.087 34.897  1.00 29.46  ?  185 VAL   A CG1 1 
ATOM   1497  C CG2 . VAL   A 1 185 ? -37.766 -12.380 33.991  1.00 29.56  ?  185 VAL   A CG2 1 
ATOM   1498  N N   . ALA   A 1 186 ? -37.052 -14.825 37.821  1.00 23.48  ?  186 ALA   A N   1 
ATOM   1499  C CA  . ALA   A 1 186 ? -36.356 -15.491 38.908  1.00 23.35  ?  186 ALA   A CA  1 
ATOM   1500  C C   . ALA   A 1 186 ? -37.063 -15.177 40.213  1.00 23.11  ?  186 ALA   A C   1 
ATOM   1501  O O   . ALA   A 1 186 ? -37.818 -14.206 40.320  1.00 25.07  ?  186 ALA   A O   1 
ATOM   1502  C CB  . ALA   A 1 186 ? -34.887 -15.064 38.993  1.00 25.58  ?  186 ALA   A CB  1 
ATOM   1503  N N   . ILE   A 1 187 ? -36.821 -16.028 41.199  1.00 22.90  ?  187 ILE   A N   1 
ATOM   1504  C CA  . ILE   A 1 187 ? -37.148 -15.740 42.585  1.00 20.52  ?  187 ILE   A CA  1 
ATOM   1505  C C   . ILE   A 1 187 ? -35.866 -15.315 43.284  1.00 22.28  ?  187 ILE   A C   1 
ATOM   1506  O O   . ILE   A 1 187 ? -34.828 -15.976 43.156  1.00 23.62  ?  187 ILE   A O   1 
ATOM   1507  C CB  . ILE   A 1 187 ? -37.795 -16.953 43.270  1.00 24.16  ?  187 ILE   A CB  1 
ATOM   1508  C CG1 . ILE   A 1 187 ? -39.204 -17.167 42.716  1.00 28.43  ?  187 ILE   A CG1 1 
ATOM   1509  C CG2 . ILE   A 1 187 ? -37.859 -16.752 44.772  1.00 24.04  ?  187 ILE   A CG2 1 
ATOM   1510  C CD1 . ILE   A 1 187 ? -39.696 -18.584 42.840  1.00 28.38  ?  187 ILE   A CD1 1 
ATOM   1511  N N   . VAL   A 1 188 ? -35.925 -14.193 43.992  1.00 22.81  ?  188 VAL   A N   1 
ATOM   1512  C CA  . VAL   A 1 188 ? -34.797 -13.672 44.751  1.00 19.46  ?  188 VAL   A CA  1 
ATOM   1513  C C   . VAL   A 1 188 ? -35.089 -13.903 46.225  1.00 19.35  ?  188 VAL   A C   1 
ATOM   1514  O O   . VAL   A 1 188 ? -36.084 -13.395 46.754  1.00 22.85  ?  188 VAL   A O   1 
ATOM   1515  C CB  . VAL   A 1 188 ? -34.557 -12.181 44.462  1.00 20.80  ?  188 VAL   A CB  1 
ATOM   1516  C CG1 . VAL   A 1 188 ? -33.299 -11.692 45.194  1.00 23.12  ?  188 VAL   A CG1 1 
ATOM   1517  C CG2 . VAL   A 1 188 ? -34.472 -11.932 42.958  1.00 22.80  ?  188 VAL   A CG2 1 
ATOM   1518  N N   . SER   A 1 189 ? -34.240 -14.676 46.883  1.00 19.08  ?  189 SER   A N   1 
ATOM   1519  C CA  . SER   A 1 189 ? -34.365 -14.948 48.310  1.00 19.03  ?  189 SER   A CA  1 
ATOM   1520  C C   . SER   A 1 189 ? -33.338 -14.084 49.032  1.00 19.59  ?  189 SER   A C   1 
ATOM   1521  O O   . SER   A 1 189 ? -32.148 -14.398 49.040  1.00 22.65  ?  189 SER   A O   1 
ATOM   1522  C CB  . SER   A 1 189 ? -34.159 -16.432 48.598  1.00 21.75  ?  189 SER   A CB  1 
ATOM   1523  O OG  . SER   A 1 189 ? -35.021 -17.233 47.800  1.00 24.07  ?  189 SER   A OG  1 
ATOM   1524  N N   . THR   A 1 190 ? -33.808 -13.000 49.649  1.00 22.13  ?  190 THR   A N   1 
ATOM   1525  C CA  . THR   A 1 190 ? -32.954 -12.012 50.309  1.00 18.50  ?  190 THR   A CA  1 
ATOM   1526  C C   . THR   A 1 190 ? -32.716 -12.428 51.756  1.00 17.56  ?  190 THR   A C   1 
ATOM   1527  O O   . THR   A 1 190 ? -33.671 -12.528 52.530  1.00 20.07  ?  190 THR   A O   1 
ATOM   1528  C CB  . THR   A 1 190 ? -33.626 -10.638 50.260  1.00 17.60  ?  190 THR   A CB  1 
ATOM   1529  O OG1 . THR   A 1 190 ? -33.965 -10.311 48.901  1.00 21.02  ?  190 THR   A OG1 1 
ATOM   1530  C CG2 . THR   A 1 190 ? -32.715 -9.575  50.818  1.00 23.36  ?  190 THR   A CG2 1 
ATOM   1531  N N   . VAL   A 1 191 ? -31.456 -12.661 52.129  1.00 19.01  ?  191 VAL   A N   1 
ATOM   1532  C CA  . VAL   A 1 191 ? -31.113 -13.154 53.465  1.00 17.78  ?  191 VAL   A CA  1 
ATOM   1533  C C   . VAL   A 1 191 ? -29.954 -12.334 54.026  1.00 18.28  ?  191 VAL   A C   1 
ATOM   1534  O O   . VAL   A 1 191 ? -28.913 -12.208 53.373  1.00 17.37  ?  191 VAL   A O   1 
ATOM   1535  C CB  . VAL   A 1 191 ? -30.758 -14.655 53.447  1.00 20.07  ?  191 VAL   A CB  1 
ATOM   1536  C CG1 . VAL   A 1 191 ? -31.995 -15.480 53.107  1.00 16.64  ?  191 VAL   A CG1 1 
ATOM   1537  C CG2 . VAL   A 1 191 ? -29.641 -14.955 52.436  1.00 17.43  ?  191 VAL   A CG2 1 
ATOM   1538  N N   . THR   A 1 192 ? -30.137 -11.739 55.211  1.00 17.90  ?  192 THR   A N   1 
ATOM   1539  C CA  . THR   A 1 192 ? -31.427 -11.551 55.863  1.00 17.88  ?  192 THR   A CA  1 
ATOM   1540  C C   . THR   A 1 192 ? -32.287 -10.603 55.023  1.00 21.83  ?  192 THR   A C   1 
ATOM   1541  O O   . THR   A 1 192 ? -31.791 -9.974  54.093  1.00 18.04  ?  192 THR   A O   1 
ATOM   1542  C CB  . THR   A 1 192 ? -31.274 -10.946 57.279  1.00 20.29  ?  192 THR   A CB  1 
ATOM   1543  O OG1 . THR   A 1 192 ? -30.624 -9.670  57.178  1.00 20.79  ?  192 THR   A OG1 1 
ATOM   1544  C CG2 . THR   A 1 192 ? -30.452 -11.861 58.202  1.00 18.06  ?  192 THR   A CG2 1 
ATOM   1545  N N   . CYS   A 1 193 ? -33.573 -10.499 55.341  1.00 22.80  ?  193 CYS   A N   1 
ATOM   1546  C CA  . CYS   A 1 193 ? -34.461 -9.625  54.579  1.00 23.06  ?  193 CYS   A CA  1 
ATOM   1547  C C   . CYS   A 1 193 ? -34.264 -8.199  55.074  1.00 22.71  ?  193 CYS   A C   1 
ATOM   1548  O O   . CYS   A 1 193 ? -34.832 -7.796  56.090  1.00 25.60  ?  193 CYS   A O   1 
ATOM   1549  C CB  . CYS   A 1 193 ? -35.910 -10.072 54.719  1.00 21.35  ?  193 CYS   A CB  1 
ATOM   1550  S SG  . CYS   A 1 193 ? -37.059 -9.118  53.707  1.00 24.86  ?  193 CYS   A SG  1 
ATOM   1551  N N   . ASN   A 1 194 ? -33.458 -7.428  54.344  1.00 26.38  ?  194 ASN   A N   1 
ATOM   1552  C CA  . ASN   A 1 194 ? -33.114 -6.071  54.767  1.00 24.14  ?  194 ASN   A CA  1 
ATOM   1553  C C   . ASN   A 1 194 ? -34.358 -5.220  54.985  1.00 27.99  ?  194 ASN   A C   1 
ATOM   1554  O O   . ASN   A 1 194 ? -34.518 -4.586  56.034  1.00 26.77  ?  194 ASN   A O   1 
ATOM   1555  C CB  . ASN   A 1 194 ? -32.202 -5.428  53.719  1.00 24.86  ?  194 ASN   A CB  1 
ATOM   1556  C CG  . ASN   A 1 194 ? -31.533 -4.160  54.217  1.00 27.84  ?  194 ASN   A CG  1 
ATOM   1557  O OD1 . ASN   A 1 194 ? -31.687 -3.767  55.378  1.00 26.33  ?  194 ASN   A OD1 1 
ATOM   1558  N ND2 . ASN   A 1 194 ? -30.758 -3.526  53.345  1.00 24.51  ?  194 ASN   A ND2 1 
ATOM   1559  N N   . SER   A 1 195 ? -35.266 -5.207  54.008  1.00 25.80  ?  195 SER   A N   1 
ATOM   1560  C CA  . SER   A 1 195 ? -36.386 -4.277  54.060  1.00 23.80  ?  195 SER   A CA  1 
ATOM   1561  C C   . SER   A 1 195 ? -37.375 -4.621  55.167  1.00 29.61  ?  195 SER   A C   1 
ATOM   1562  O O   . SER   A 1 195 ? -38.074 -3.732  55.664  1.00 33.56  ?  195 SER   A O   1 
ATOM   1563  C CB  . SER   A 1 195 ? -37.078 -4.249  52.708  1.00 23.62  ?  195 SER   A CB  1 
ATOM   1564  O OG  . SER   A 1 195 ? -36.114 -4.129  51.681  1.00 32.09  ?  195 SER   A OG  1 
ATOM   1565  N N   . ALA   A 1 196 ? -37.452 -5.888  55.570  1.00 26.63  ?  196 ALA   A N   1 
ATOM   1566  C CA  . ALA   A 1 196 ? -38.293 -6.271  56.697  1.00 28.49  ?  196 ALA   A CA  1 
ATOM   1567  C C   . ALA   A 1 196 ? -37.633 -6.002  58.046  1.00 27.07  ?  196 ALA   A C   1 
ATOM   1568  O O   . ALA   A 1 196 ? -38.264 -6.224  59.084  1.00 25.58  ?  196 ALA   A O   1 
ATOM   1569  C CB  . ALA   A 1 196 ? -38.671 -7.753  56.592  1.00 24.43  ?  196 ALA   A CB  1 
ATOM   1570  N N   . GLY   A 1 197 ? -36.388 -5.531  58.057  1.00 27.57  ?  197 GLY   A N   1 
ATOM   1571  C CA  . GLY   A 1 197 ? -35.706 -5.202  59.291  1.00 26.37  ?  197 GLY   A CA  1 
ATOM   1572  C C   . GLY   A 1 197 ? -34.490 -6.058  59.572  1.00 25.59  ?  197 GLY   A C   1 
ATOM   1573  O O   . GLY   A 1 197 ? -34.125 -6.257  60.735  1.00 24.33  ?  197 GLY   A O   1 
ATOM   1574  N N   . GLY   A 1 198 ? -33.840 -6.559  58.523  1.00 21.78  ?  198 GLY   A N   1 
ATOM   1575  C CA  . GLY   A 1 198 ? -32.769 -7.517  58.726  1.00 20.69  ?  198 GLY   A CA  1 
ATOM   1576  C C   . GLY   A 1 198 ? -33.250 -8.809  59.344  1.00 19.39  ?  198 GLY   A C   1 
ATOM   1577  O O   . GLY   A 1 198 ? -32.515 -9.445  60.115  1.00 16.43  ?  198 GLY   A O   1 
ATOM   1578  N N   . GLN   A 1 199 ? -34.453 -9.215  59.018  1.00 17.20  ?  199 GLN   A N   1 
ATOM   1579  C CA  . GLN   A 1 199 ? -35.137 -10.307 59.694  1.00 20.44  ?  199 GLN   A CA  1 
ATOM   1580  C C   . GLN   A 1 199 ? -34.846 -11.624 58.980  1.00 23.34  ?  199 GLN   A C   1 
ATOM   1581  O O   . GLN   A 1 199 ? -34.896 -11.677 57.748  1.00 20.53  ?  199 GLN   A O   1 
ATOM   1582  C CB  . GLN   A 1 199 ? -36.634 -10.053 59.742  1.00 22.46  ?  199 GLN   A CB  1 
ATOM   1583  C CG  . GLN   A 1 199 ? -37.024 -8.833  60.559  1.00 19.85  ?  199 GLN   A CG  1 
ATOM   1584  C CD  . GLN   A 1 199 ? -36.707 -8.989  62.032  1.00 21.26  ?  199 GLN   A CD  1 
ATOM   1585  O OE1 . GLN   A 1 199 ? -36.989 -10.025 62.631  1.00 25.41  ?  199 GLN   A OE1 1 
ATOM   1586  N NE2 . GLN   A 1 199 ? -36.116 -7.959  62.627  1.00 20.16  ?  199 GLN   A NE2 1 
ATOM   1587  N N   . PRO   A 1 200 ? -34.547 -12.693 59.712  1.00 19.86  ?  200 PRO   A N   1 
ATOM   1588  C CA  . PRO   A 1 200 ? -34.071 -13.914 59.059  1.00 19.75  ?  200 PRO   A CA  1 
ATOM   1589  C C   . PRO   A 1 200 ? -35.157 -14.648 58.286  1.00 20.08  ?  200 PRO   A C   1 
ATOM   1590  O O   . PRO   A 1 200 ? -36.352 -14.535 58.565  1.00 21.92  ?  200 PRO   A O   1 
ATOM   1591  C CB  . PRO   A 1 200 ? -33.556 -14.760 60.228  1.00 23.74  ?  200 PRO   A CB  1 
ATOM   1592  C CG  . PRO   A 1 200 ? -34.319 -14.266 61.420  1.00 19.61  ?  200 PRO   A CG  1 
ATOM   1593  C CD  . PRO   A 1 200 ? -34.514 -12.798 61.184  1.00 16.87  ?  200 PRO   A CD  1 
ATOM   1594  N N   . VAL   A 1 201 ? -34.708 -15.407 57.285  1.00 20.60  ?  201 VAL   A N   1 
ATOM   1595  C CA  . VAL   A 1 201 ? -35.523 -16.402 56.593  1.00 24.24  ?  201 VAL   A CA  1 
ATOM   1596  C C   . VAL   A 1 201 ? -35.156 -17.777 57.141  1.00 24.07  ?  201 VAL   A C   1 
ATOM   1597  O O   . VAL   A 1 201 ? -33.966 -18.097 57.280  1.00 24.78  ?  201 VAL   A O   1 
ATOM   1598  C CB  . VAL   A 1 201 ? -35.292 -16.351 55.071  1.00 22.54  ?  201 VAL   A CB  1 
ATOM   1599  C CG1 . VAL   A 1 201 ? -36.341 -17.192 54.350  1.00 23.95  ?  201 VAL   A CG1 1 
ATOM   1600  C CG2 . VAL   A 1 201 ? -35.302 -14.912 54.569  1.00 19.09  ?  201 VAL   A CG2 1 
ATOM   1601  N N   . SER   A 1 202 ? -36.162 -18.601 57.425  1.00 23.10  ?  202 SER   A N   1 
ATOM   1602  C CA  . SER   A 1 202 ? -35.907 -19.931 57.967  1.00 22.33  ?  202 SER   A CA  1 
ATOM   1603  C C   . SER   A 1 202 ? -35.402 -20.880 56.885  1.00 20.84  ?  202 SER   A C   1 
ATOM   1604  O O   . SER   A 1 202 ? -35.669 -20.703 55.695  1.00 23.41  ?  202 SER   A O   1 
ATOM   1605  C CB  . SER   A 1 202 ? -37.165 -20.514 58.615  1.00 26.06  ?  202 SER   A CB  1 
ATOM   1606  O OG  . SER   A 1 202 ? -38.071 -21.043 57.659  1.00 22.82  ?  202 SER   A OG  1 
ATOM   1607  N N   . MET   A 1 203 ? -34.659 -21.901 57.320  1.00 23.16  ?  203 MET   A N   1 
ATOM   1608  C CA  . MET   A 1 203 ? -34.162 -22.910 56.390  1.00 22.28  ?  203 MET   A CA  1 
ATOM   1609  C C   . MET   A 1 203 ? -35.306 -23.603 55.668  1.00 27.45  ?  203 MET   A C   1 
ATOM   1610  O O   . MET   A 1 203 ? -35.235 -23.838 54.454  1.00 23.46  ?  203 MET   A O   1 
ATOM   1611  C CB  . MET   A 1 203 ? -33.317 -23.940 57.133  1.00 20.48  ?  203 MET   A CB  1 
ATOM   1612  C CG  . MET   A 1 203 ? -32.695 -24.966 56.222  1.00 23.81  ?  203 MET   A CG  1 
ATOM   1613  S SD  . MET   A 1 203 ? -31.385 -24.251 55.222  1.00 22.33  ?  203 MET   A SD  1 
ATOM   1614  C CE  . MET   A 1 203 ? -30.123 -23.966 56.455  1.00 17.28  ?  203 MET   A CE  1 
ATOM   1615  N N   . SER   A 1 204 ? -36.374 -23.939 56.399  1.00 25.61  ?  204 SER   A N   1 
ATOM   1616  C CA  . SER   A 1 204 ? -37.499 -24.617 55.770  1.00 24.59  ?  204 SER   A CA  1 
ATOM   1617  C C   . SER   A 1 204 ? -38.270 -23.688 54.839  1.00 25.76  ?  204 SER   A C   1 
ATOM   1618  O O   . SER   A 1 204 ? -38.861 -24.155 53.861  1.00 27.60  ?  204 SER   A O   1 
ATOM   1619  C CB  . SER   A 1 204 ? -38.415 -25.224 56.835  1.00 27.64  ?  204 SER   A CB  1 
ATOM   1620  O OG  . SER   A 1 204 ? -39.067 -24.238 57.610  1.00 32.31  ?  204 SER   A OG  1 
ATOM   1621  N N   . ASN   A 1 205 ? -38.266 -22.377 55.098  1.00 30.11  ?  205 ASN   A N   1 
ATOM   1622  C CA  . ASN   A 1 205 ? -38.870 -21.451 54.141  1.00 25.69  ?  205 ASN   A CA  1 
ATOM   1623  C C   . ASN   A 1 205 ? -38.052 -21.393 52.857  1.00 24.31  ?  205 ASN   A C   1 
ATOM   1624  O O   . ASN   A 1 205 ? -38.595 -21.568 51.760  1.00 24.71  ?  205 ASN   A O   1 
ATOM   1625  C CB  . ASN   A 1 205 ? -39.024 -20.057 54.755  1.00 24.04  ?  205 ASN   A CB  1 
ATOM   1626  C CG  . ASN   A 1 205 ? -39.921 -19.136 53.914  1.00 29.86  ?  205 ASN   A CG  1 
ATOM   1627  O OD1 . ASN   A 1 205 ? -39.462 -18.142 53.338  1.00 25.41  ?  205 ASN   A OD1 1 
ATOM   1628  N ND2 . ASN   A 1 205 ? -41.207 -19.473 53.843  1.00 25.84  ?  205 ASN   A ND2 1 
ATOM   1629  N N   . LEU   A 1 206 ? -36.734 -21.166 52.975  1.00 24.59  ?  206 LEU   A N   1 
ATOM   1630  C CA  . LEU   A 1 206 ? -35.867 -21.183 51.793  1.00 27.85  ?  206 LEU   A CA  1 
ATOM   1631  C C   . LEU   A 1 206 ? -35.994 -22.501 51.033  1.00 26.30  ?  206 LEU   A C   1 
ATOM   1632  O O   . LEU   A 1 206 ? -35.967 -22.520 49.797  1.00 23.23  ?  206 LEU   A O   1 
ATOM   1633  C CB  . LEU   A 1 206 ? -34.408 -20.943 52.194  1.00 23.36  ?  206 LEU   A CB  1 
ATOM   1634  C CG  . LEU   A 1 206 ? -34.013 -19.611 52.845  1.00 24.14  ?  206 LEU   A CG  1 
ATOM   1635  C CD1 . LEU   A 1 206 ? -32.648 -19.714 53.512  1.00 22.18  ?  206 LEU   A CD1 1 
ATOM   1636  C CD2 . LEU   A 1 206 ? -34.021 -18.473 51.834  1.00 23.59  ?  206 LEU   A CD2 1 
ATOM   1637  N N   . LYS   A 1 207 ? -36.139 -23.612 51.760  1.00 25.75  ?  207 LYS   A N   1 
ATOM   1638  C CA  . LYS   A 1 207 ? -36.295 -24.917 51.126  1.00 25.88  ?  207 LYS   A CA  1 
ATOM   1639  C C   . LYS   A 1 207 ? -37.632 -25.024 50.403  1.00 29.05  ?  207 LYS   A C   1 
ATOM   1640  O O   . LYS   A 1 207 ? -37.689 -25.483 49.256  1.00 30.76  ?  207 LYS   A O   1 
ATOM   1641  C CB  . LYS   A 1 207 ? -36.162 -26.024 52.173  1.00 28.27  ?  207 LYS   A CB  1 
ATOM   1642  C CG  . LYS   A 1 207 ? -36.339 -27.431 51.617  1.00 33.22  ?  207 LYS   A CG  1 
ATOM   1643  C CD  . LYS   A 1 207 ? -36.212 -28.502 52.703  1.00 31.56  ?  207 LYS   A CD  1 
ATOM   1644  C CE  . LYS   A 1 207 ? -36.290 -29.898 52.096  1.00 37.66  ?  207 LYS   A CE  1 
ATOM   1645  N NZ  . LYS   A 1 207 ? -36.480 -30.957 53.129  1.00 47.96  ?  207 LYS   A NZ  1 
ATOM   1646  N N   . GLU   A 1 208 ? -38.725 -24.616 51.059  1.00 26.29  ?  208 GLU   A N   1 
ATOM   1647  C CA  . GLU   A 1 208 ? -40.036 -24.712 50.419  1.00 30.07  ?  208 GLU   A CA  1 
ATOM   1648  C C   . GLU   A 1 208 ? -40.114 -23.811 49.192  1.00 29.22  ?  208 GLU   A C   1 
ATOM   1649  O O   . GLU   A 1 208 ? -40.727 -24.177 48.183  1.00 34.12  ?  208 GLU   A O   1 
ATOM   1650  C CB  . GLU   A 1 208 ? -41.148 -24.368 51.413  1.00 29.93  ?  208 GLU   A CB  1 
ATOM   1651  C CG  . GLU   A 1 208 ? -42.542 -24.500 50.821  1.00 32.99  ?  208 GLU   A CG  1 
ATOM   1652  C CD  . GLU   A 1 208 ? -43.660 -24.359 51.851  1.00 44.83  ?  208 GLU   A CD  1 
ATOM   1653  O OE1 . GLU   A 1 208 ? -43.410 -23.851 52.967  1.00 45.19  ?  208 GLU   A OE1 1 
ATOM   1654  O OE2 . GLU   A 1 208 ? -44.802 -24.760 51.535  1.00 48.25  ?  208 GLU   A OE2 1 
ATOM   1655  N N   . VAL   A 1 209 ? -39.488 -22.633 49.257  1.00 28.47  ?  209 VAL   A N   1 
ATOM   1656  C CA  . VAL   A 1 209 ? -39.460 -21.741 48.103  1.00 27.35  ?  209 VAL   A CA  1 
ATOM   1657  C C   . VAL   A 1 209 ? -38.677 -22.367 46.954  1.00 30.79  ?  209 VAL   A C   1 
ATOM   1658  O O   . VAL   A 1 209 ? -39.101 -22.314 45.792  1.00 31.68  ?  209 VAL   A O   1 
ATOM   1659  C CB  . VAL   A 1 209 ? -38.878 -20.374 48.506  1.00 28.05  ?  209 VAL   A CB  1 
ATOM   1660  C CG1 . VAL   A 1 209 ? -38.420 -19.609 47.264  1.00 27.82  ?  209 VAL   A CG1 1 
ATOM   1661  C CG2 . VAL   A 1 209 ? -39.904 -19.576 49.282  1.00 23.65  ?  209 VAL   A CG2 1 
ATOM   1662  N N   . TYR   A 1 210 ? -37.525 -22.974 47.254  1.00 28.71  ?  210 TYR   A N   1 
ATOM   1663  C CA  . TYR   A 1 210 ? -36.721 -23.574 46.196  1.00 25.03  ?  210 TYR   A CA  1 
ATOM   1664  C C   . TYR   A 1 210 ? -37.421 -24.762 45.556  1.00 31.03  ?  210 TYR   A C   1 
ATOM   1665  O O   . TYR   A 1 210 ? -37.250 -25.006 44.358  1.00 31.60  ?  210 TYR   A O   1 
ATOM   1666  C CB  . TYR   A 1 210 ? -35.363 -24.013 46.733  1.00 26.37  ?  210 TYR   A CB  1 
ATOM   1667  C CG  . TYR   A 1 210 ? -34.442 -24.496 45.636  1.00 31.43  ?  210 TYR   A CG  1 
ATOM   1668  C CD1 . TYR   A 1 210 ? -33.881 -23.600 44.736  1.00 27.65  ?  210 TYR   A CD1 1 
ATOM   1669  C CD2 . TYR   A 1 210 ? -34.145 -25.847 45.490  1.00 30.79  ?  210 TYR   A CD2 1 
ATOM   1670  C CE1 . TYR   A 1 210 ? -33.042 -24.033 43.725  1.00 28.08  ?  210 TYR   A CE1 1 
ATOM   1671  C CE2 . TYR   A 1 210 ? -33.306 -26.289 44.480  1.00 28.05  ?  210 TYR   A CE2 1 
ATOM   1672  C CZ  . TYR   A 1 210 ? -32.759 -25.378 43.601  1.00 28.35  ?  210 TYR   A CZ  1 
ATOM   1673  O OH  . TYR   A 1 210 ? -31.926 -25.809 42.594  1.00 31.30  ?  210 TYR   A OH  1 
ATOM   1674  N N   . GLU   A 1 211 ? -38.206 -25.513 46.325  1.00 32.81  ?  211 GLU   A N   1 
ATOM   1675  C CA  . GLU   A 1 211 ? -38.876 -26.674 45.753  1.00 33.49  ?  211 GLU   A CA  1 
ATOM   1676  C C   . GLU   A 1 211 ? -40.051 -26.254 44.879  1.00 29.61  ?  211 GLU   A C   1 
ATOM   1677  O O   . GLU   A 1 211 ? -40.288 -26.850 43.822  1.00 33.93  ?  211 GLU   A O   1 
ATOM   1678  C CB  . GLU   A 1 211 ? -39.313 -27.623 46.872  1.00 34.26  ?  211 GLU   A CB  1 
ATOM   1679  C CG  . GLU   A 1 211 ? -38.115 -28.279 47.564  1.00 39.04  ?  211 GLU   A CG  1 
ATOM   1680  C CD  . GLU   A 1 211 ? -38.465 -29.020 48.846  1.00 43.08  ?  211 GLU   A CD  1 
ATOM   1681  O OE1 . GLU   A 1 211 ? -39.469 -28.665 49.508  1.00 41.88  ?  211 GLU   A OE1 1 
ATOM   1682  O OE2 . GLU   A 1 211 ? -37.718 -29.961 49.192  1.00 44.38  ?  211 GLU   A OE2 1 
ATOM   1683  N N   . ILE   A 1 212 ? -40.784 -25.220 45.300  1.00 31.99  ?  212 ILE   A N   1 
ATOM   1684  C CA  . ILE   A 1 212 ? -41.860 -24.667 44.482  1.00 28.63  ?  212 ILE   A CA  1 
ATOM   1685  C C   . ILE   A 1 212 ? -41.308 -24.131 43.170  1.00 35.16  ?  212 ILE   A C   1 
ATOM   1686  O O   . ILE   A 1 212 ? -41.892 -24.335 42.100  1.00 39.57  ?  212 ILE   A O   1 
ATOM   1687  C CB  . ILE   A 1 212 ? -42.607 -23.571 45.262  1.00 29.90  ?  212 ILE   A CB  1 
ATOM   1688  C CG1 . ILE   A 1 212 ? -43.371 -24.175 46.444  1.00 28.62  ?  212 ILE   A CG1 1 
ATOM   1689  C CG2 . ILE   A 1 212 ? -43.533 -22.806 44.333  1.00 34.43  ?  212 ILE   A CG2 1 
ATOM   1690  C CD1 . ILE   A 1 212 ? -43.965 -23.147 47.394  1.00 25.92  ?  212 ILE   A CD1 1 
ATOM   1691  N N   . ALA   A 1 213 ? -40.174 -23.438 43.233  1.00 31.75  ?  213 ALA   A N   1 
ATOM   1692  C CA  . ALA   A 1 213 ? -39.571 -22.890 42.025  1.00 32.18  ?  213 ALA   A CA  1 
ATOM   1693  C C   . ALA   A 1 213 ? -39.073 -23.992 41.102  1.00 30.09  ?  213 ALA   A C   1 
ATOM   1694  O O   . ALA   A 1 213 ? -39.195 -23.887 39.876  1.00 33.68  ?  213 ALA   A O   1 
ATOM   1695  C CB  . ALA   A 1 213 ? -38.429 -21.951 42.401  1.00 31.41  ?  213 ALA   A CB  1 
ATOM   1696  N N   . LYS   A 1 214 ? -38.511 -25.060 41.667  1.00 32.19  ?  214 LYS   A N   1 
ATOM   1697  C CA  . LYS   A 1 214 ? -37.958 -26.112 40.821  1.00 35.34  ?  214 LYS   A CA  1 
ATOM   1698  C C   . LYS   A 1 214 ? -39.052 -26.840 40.053  1.00 34.07  ?  214 LYS   A C   1 
ATOM   1699  O O   . LYS   A 1 214 ? -38.915 -27.068 38.847  1.00 38.85  ?  214 LYS   A O   1 
ATOM   1700  C CB  . LYS   A 1 214 ? -37.134 -27.089 41.654  1.00 32.81  ?  214 LYS   A CB  1 
ATOM   1701  C CG  . LYS   A 1 214 ? -35.775 -26.543 42.064  1.00 33.06  ?  214 LYS   A CG  1 
ATOM   1702  C CD  . LYS   A 1 214 ? -35.010 -25.970 40.878  1.00 40.51  ?  214 LYS   A CD  1 
ATOM   1703  C CE  . LYS   A 1 214 ? -34.919 -24.442 40.929  1.00 32.37  ?  214 LYS   A CE  1 
ATOM   1704  N NZ  . LYS   A 1 214 ? -34.179 -23.896 39.765  1.00 30.29  ?  214 LYS   A NZ  1 
ATOM   1705  N N   . GLN   A 1 215 ? -40.148 -27.202 40.723  1.00 35.11  ?  215 GLN   A N   1 
ATOM   1706  C CA  . GLN   A 1 215 ? -41.216 -27.900 40.018  1.00 37.16  ?  215 GLN   A CA  1 
ATOM   1707  C C   . GLN   A 1 215 ? -41.827 -27.044 38.916  1.00 37.58  ?  215 GLN   A C   1 
ATOM   1708  O O   . GLN   A 1 215 ? -42.397 -27.593 37.968  1.00 38.35  ?  215 GLN   A O   1 
ATOM   1709  C CB  . GLN   A 1 215 ? -42.293 -28.371 41.003  1.00 41.79  ?  215 GLN   A CB  1 
ATOM   1710  C CG  . GLN   A 1 215 ? -43.046 -27.271 41.738  1.00 41.29  ?  215 GLN   A CG  1 
ATOM   1711  C CD  . GLN   A 1 215 ? -44.003 -27.825 42.784  1.00 50.66  ?  215 GLN   A CD  1 
ATOM   1712  O OE1 . GLN   A 1 215 ? -43.742 -28.869 43.396  1.00 46.54  ?  215 GLN   A OE1 1 
ATOM   1713  N NE2 . GLN   A 1 215 ? -45.122 -27.128 42.992  1.00 45.87  ?  215 GLN   A NE2 1 
ATOM   1714  N N   . HIS   A 1 216 ? -41.694 -25.717 39.002  1.00 37.80  ?  216 HIS   A N   1 
ATOM   1715  C CA  . HIS   A 1 216 ? -42.115 -24.814 37.938  1.00 36.73  ?  216 HIS   A CA  1 
ATOM   1716  C C   . HIS   A 1 216 ? -40.985 -24.408 37.000  1.00 38.46  ?  216 HIS   A C   1 
ATOM   1717  O O   . HIS   A 1 216 ? -41.251 -23.725 36.003  1.00 36.63  ?  216 HIS   A O   1 
ATOM   1718  C CB  . HIS   A 1 216 ? -42.745 -23.552 38.530  1.00 33.68  ?  216 HIS   A CB  1 
ATOM   1719  C CG  . HIS   A 1 216 ? -44.102 -23.777 39.108  1.00 37.59  ?  216 HIS   A CG  1 
ATOM   1720  N ND1 . HIS   A 1 216 ? -44.303 -24.078 40.438  1.00 41.02  ?  216 HIS   A ND1 1 
ATOM   1721  C CD2 . HIS   A 1 216 ? -45.327 -23.763 38.534  1.00 36.22  ?  216 HIS   A CD2 1 
ATOM   1722  C CE1 . HIS   A 1 216 ? -45.595 -24.231 40.661  1.00 34.90  ?  216 HIS   A CE1 1 
ATOM   1723  N NE2 . HIS   A 1 216 ? -46.238 -24.045 39.523  1.00 43.97  ?  216 HIS   A NE2 1 
ATOM   1724  N N   . GLY   A 1 217 ? -39.746 -24.801 37.286  1.00 36.09  ?  217 GLY   A N   1 
ATOM   1725  C CA  . GLY   A 1 217 ? -38.626 -24.441 36.433  1.00 36.03  ?  217 GLY   A CA  1 
ATOM   1726  C C   . GLY   A 1 217 ? -38.214 -22.988 36.536  1.00 33.59  ?  217 GLY   A C   1 
ATOM   1727  O O   . GLY   A 1 217 ? -37.887 -22.367 35.518  1.00 35.77  ?  217 GLY   A O   1 
ATOM   1728  N N   . ILE   A 1 218 ? -38.217 -22.429 37.741  1.00 36.10  ?  218 ILE   A N   1 
ATOM   1729  C CA  . ILE   A 1 218 ? -37.900 -21.025 37.966  1.00 31.12  ?  218 ILE   A CA  1 
ATOM   1730  C C   . ILE   A 1 218 ? -36.529 -20.932 38.623  1.00 26.91  ?  218 ILE   A C   1 
ATOM   1731  O O   . ILE   A 1 218 ? -36.239 -21.655 39.583  1.00 26.53  ?  218 ILE   A O   1 
ATOM   1732  C CB  . ILE   A 1 218 ? -38.984 -20.345 38.820  1.00 30.23  ?  218 ILE   A CB  1 
ATOM   1733  C CG1 . ILE   A 1 218 ? -40.330 -20.396 38.093  1.00 30.88  ?  218 ILE   A CG1 1 
ATOM   1734  C CG2 . ILE   A 1 218 ? -38.597 -18.913 39.135  1.00 29.56  ?  218 ILE   A CG2 1 
ATOM   1735  C CD1 . ILE   A 1 218 ? -41.496 -19.947 38.937  1.00 30.47  ?  218 ILE   A CD1 1 
ATOM   1736  N N   . PHE   A 1 219 ? -35.684 -20.056 38.088  1.00 29.42  ?  219 PHE   A N   1 
ATOM   1737  C CA  . PHE   A 1 219 ? -34.347 -19.829 38.622  1.00 22.89  ?  219 PHE   A CA  1 
ATOM   1738  C C   . PHE   A 1 219 ? -34.438 -19.059 39.937  1.00 25.08  ?  219 PHE   A C   1 
ATOM   1739  O O   . PHE   A 1 219 ? -35.274 -18.167 40.089  1.00 26.76  ?  219 PHE   A O   1 
ATOM   1740  C CB  . PHE   A 1 219 ? -33.529 -19.053 37.585  1.00 24.45  ?  219 PHE   A CB  1 
ATOM   1741  C CG  . PHE   A 1 219 ? -32.043 -19.044 37.829  1.00 25.69  ?  219 PHE   A CG  1 
ATOM   1742  C CD1 . PHE   A 1 219 ? -31.231 -20.016 37.268  1.00 27.88  ?  219 PHE   A CD1 1 
ATOM   1743  C CD2 . PHE   A 1 219 ? -31.454 -18.033 38.575  1.00 24.83  ?  219 PHE   A CD2 1 
ATOM   1744  C CE1 . PHE   A 1 219 ? -29.865 -19.997 37.463  1.00 26.18  ?  219 PHE   A CE1 1 
ATOM   1745  C CE2 . PHE   A 1 219 ? -30.094 -18.012 38.782  1.00 23.98  ?  219 PHE   A CE2 1 
ATOM   1746  C CZ  . PHE   A 1 219 ? -29.294 -18.993 38.219  1.00 24.53  ?  219 PHE   A CZ  1 
ATOM   1747  N N   . VAL   A 1 220 ? -33.587 -19.412 40.898  1.00 23.75  ?  220 VAL   A N   1 
ATOM   1748  C CA  . VAL   A 1 220 ? -33.616 -18.820 42.236  1.00 22.40  ?  220 VAL   A CA  1 
ATOM   1749  C C   . VAL   A 1 220 ? -32.270 -18.156 42.509  1.00 22.26  ?  220 VAL   A C   1 
ATOM   1750  O O   . VAL   A 1 220 ? -31.222 -18.809 42.429  1.00 21.94  ?  220 VAL   A O   1 
ATOM   1751  C CB  . VAL   A 1 220 ? -33.934 -19.869 43.315  1.00 25.08  ?  220 VAL   A CB  1 
ATOM   1752  C CG1 . VAL   A 1 220 ? -33.860 -19.248 44.711  1.00 23.61  ?  220 VAL   A CG1 1 
ATOM   1753  C CG2 . VAL   A 1 220 ? -35.297 -20.481 43.073  1.00 22.51  ?  220 VAL   A CG2 1 
ATOM   1754  N N   . VAL   A 1 221 ? -32.294 -16.867 42.842  1.00 24.11  ?  221 VAL   A N   1 
ATOM   1755  C CA  . VAL   A 1 221 ? -31.088 -16.118 43.186  1.00 18.95  ?  221 VAL   A CA  1 
ATOM   1756  C C   . VAL   A 1 221 ? -31.128 -15.780 44.667  1.00 19.76  ?  221 VAL   A C   1 
ATOM   1757  O O   . VAL   A 1 221 ? -32.106 -15.204 45.153  1.00 21.15  ?  221 VAL   A O   1 
ATOM   1758  C CB  . VAL   A 1 221 ? -30.944 -14.835 42.356  1.00 19.90  ?  221 VAL   A CB  1 
ATOM   1759  C CG1 . VAL   A 1 221 ? -29.682 -14.075 42.785  1.00 17.57  ?  221 VAL   A CG1 1 
ATOM   1760  C CG2 . VAL   A 1 221 ? -30.892 -15.164 40.876  1.00 23.67  ?  221 VAL   A CG2 1 
ATOM   1761  N N   . MET   A 1 222 ? -30.065 -16.124 45.379  1.00 20.54  ?  222 MET   A N   1 
ATOM   1762  C CA  . MET   A 1 222 ? -29.936 -15.788 46.788  1.00 21.60  ?  222 MET   A CA  1 
ATOM   1763  C C   . MET   A 1 222 ? -29.216 -14.454 46.892  1.00 20.80  ?  222 MET   A C   1 
ATOM   1764  O O   . MET   A 1 222 ? -28.005 -14.377 46.679  1.00 20.20  ?  222 MET   A O   1 
ATOM   1765  C CB  . MET   A 1 222 ? -29.174 -16.875 47.539  1.00 22.91  ?  222 MET   A CB  1 
ATOM   1766  C CG  . MET   A 1 222 ? -29.211 -16.707 49.039  1.00 20.89  ?  222 MET   A CG  1 
ATOM   1767  S SD  . MET   A 1 222 ? -30.587 -17.618 49.717  1.00 27.52  ?  222 MET   A SD  1 
ATOM   1768  C CE  . MET   A 1 222 ? -29.848 -19.242 49.876  1.00 21.90  ?  222 MET   A CE  1 
ATOM   1769  N N   . ASP   A 1 223 ? -29.956 -13.400 47.209  1.00 23.14  ?  223 ASP   A N   1 
ATOM   1770  C CA  . ASP   A 1 223 ? -29.318 -12.143 47.577  1.00 22.10  ?  223 ASP   A CA  1 
ATOM   1771  C C   . ASP   A 1 223 ? -28.661 -12.341 48.938  1.00 21.41  ?  223 ASP   A C   1 
ATOM   1772  O O   . ASP   A 1 223 ? -29.350 -12.539 49.945  1.00 20.87  ?  223 ASP   A O   1 
ATOM   1773  C CB  . ASP   A 1 223 ? -30.348 -11.017 47.591  1.00 24.58  ?  223 ASP   A CB  1 
ATOM   1774  C CG  . ASP   A 1 223 ? -29.726 -9.651  47.840  1.00 25.90  ?  223 ASP   A CG  1 
ATOM   1775  O OD1 . ASP   A 1 223 ? -28.805 -9.547  48.682  1.00 27.08  ?  223 ASP   A OD1 1 
ATOM   1776  O OD2 . ASP   A 1 223 ? -30.164 -8.679  47.187  1.00 23.81  ?  223 ASP   A OD2 1 
ATOM   1777  N N   . SER   A 1 224 ? -27.329 -12.273 48.971  1.00 19.04  ?  224 SER   A N   1 
ATOM   1778  C CA  . SER   A 1 224 ? -26.535 -12.820 50.066  1.00 21.09  ?  224 SER   A CA  1 
ATOM   1779  C C   . SER   A 1 224 ? -25.751 -11.765 50.840  1.00 21.06  ?  224 SER   A C   1 
ATOM   1780  O O   . SER   A 1 224 ? -24.770 -12.107 51.506  1.00 22.27  ?  224 SER   A O   1 
ATOM   1781  C CB  . SER   A 1 224 ? -25.564 -13.867 49.521  1.00 18.88  ?  224 SER   A CB  1 
ATOM   1782  O OG  . SER   A 1 224 ? -26.250 -14.925 48.883  1.00 20.83  ?  224 SER   A OG  1 
ATOM   1783  N N   . ALA   A 1 225 ? -26.140 -10.489 50.769  1.00 20.08  ?  225 ALA   A N   1 
ATOM   1784  C CA  . ALA   A 1 225 ? -25.388 -9.462  51.490  1.00 18.96  ?  225 ALA   A CA  1 
ATOM   1785  C C   . ALA   A 1 225 ? -25.213 -9.819  52.967  1.00 18.89  ?  225 ALA   A C   1 
ATOM   1786  O O   . ALA   A 1 225 ? -24.135 -9.622  53.543  1.00 18.01  ?  225 ALA   A O   1 
ATOM   1787  C CB  . ALA   A 1 225 ? -26.080 -8.106  51.351  1.00 16.63  ?  225 ALA   A CB  1 
ATOM   1788  N N   . ARG   A 1 226 ? -26.250 -10.356 53.598  1.00 18.18  ?  226 ARG   A N   1 
ATOM   1789  C CA  . ARG   A 1 226 ? -26.195 -10.649 55.020  1.00 13.58  ?  226 ARG   A CA  1 
ATOM   1790  C C   . ARG   A 1 226 ? -26.494 -12.118 55.282  1.00 16.44  ?  226 ARG   A C   1 
ATOM   1791  O O   . ARG   A 1 226 ? -27.219 -12.477 56.215  1.00 16.65  ?  226 ARG   A O   1 
ATOM   1792  C CB  . ARG   A 1 226 ? -27.131 -9.719  55.777  1.00 14.87  ?  226 ARG   A CB  1 
ATOM   1793  C CG  . ARG   A 1 226 ? -26.746 -8.274  55.536  1.00 16.29  ?  226 ARG   A CG  1 
ATOM   1794  C CD  . ARG   A 1 226 ? -27.619 -7.304  56.285  1.00 19.05  ?  226 ARG   A CD  1 
ATOM   1795  N NE  . ARG   A 1 226 ? -27.295 -5.930  55.919  1.00 19.15  ?  226 ARG   A NE  1 
ATOM   1796  C CZ  . ARG   A 1 226 ? -27.764 -5.315  54.840  1.00 23.06  ?  226 ARG   A CZ  1 
ATOM   1797  N NH1 . ARG   A 1 226 ? -28.561 -5.936  53.981  1.00 19.60  ?  226 ARG   A NH1 1 
ATOM   1798  N NH2 . ARG   A 1 226 ? -27.424 -4.046  54.616  1.00 18.15  ?  226 ARG   A NH2 1 
ATOM   1799  N N   . PHE   A 1 227 ? -25.904 -12.989 54.464  1.00 15.03  ?  227 PHE   A N   1 
ATOM   1800  C CA  . PHE   A 1 227 ? -26.156 -14.420 54.591  1.00 18.66  ?  227 PHE   A CA  1 
ATOM   1801  C C   . PHE   A 1 227 ? -25.632 -14.996 55.906  1.00 16.62  ?  227 PHE   A C   1 
ATOM   1802  O O   . PHE   A 1 227 ? -26.220 -15.946 56.429  1.00 19.82  ?  227 PHE   A O   1 
ATOM   1803  C CB  . PHE   A 1 227 ? -25.545 -15.162 53.398  1.00 19.30  ?  227 PHE   A CB  1 
ATOM   1804  C CG  . PHE   A 1 227 ? -24.029 -15.204 53.395  1.00 17.34  ?  227 PHE   A CG  1 
ATOM   1805  C CD1 . PHE   A 1 227 ? -23.286 -14.070 53.122  1.00 18.78  ?  227 PHE   A CD1 1 
ATOM   1806  C CD2 . PHE   A 1 227 ? -23.355 -16.389 53.638  1.00 19.15  ?  227 PHE   A CD2 1 
ATOM   1807  C CE1 . PHE   A 1 227 ? -21.904 -14.106 53.109  1.00 19.99  ?  227 PHE   A CE1 1 
ATOM   1808  C CE2 . PHE   A 1 227 ? -21.967 -16.435 53.625  1.00 21.62  ?  227 PHE   A CE2 1 
ATOM   1809  C CZ  . PHE   A 1 227 ? -21.241 -15.289 53.360  1.00 18.68  ?  227 PHE   A CZ  1 
ATOM   1810  N N   . CYS   A 1 228 ? -24.528 -14.464 56.447  1.00 19.88  ?  228 CYS   A N   1 
ATOM   1811  C CA  . CYS   A 1 228 ? -23.964 -15.025 57.678  1.00 16.78  ?  228 CYS   A CA  1 
ATOM   1812  C C   . CYS   A 1 228 ? -24.819 -14.687 58.882  1.00 17.48  ?  228 CYS   A C   1 
ATOM   1813  O O   . CYS   A 1 228 ? -24.929 -15.486 59.818  1.00 22.17  ?  228 CYS   A O   1 
ATOM   1814  C CB  . CYS   A 1 228 ? -22.548 -14.511 57.913  1.00 15.74  ?  228 CYS   A CB  1 
ATOM   1815  S SG  . CYS   A 1 228 ? -21.375 -15.078 56.734  1.00 20.57  ?  228 CYS   A SG  1 
ATOM   1816  N N   . GLU   A 1 229 ? -25.396 -13.491 58.898  1.00 17.70  ?  229 GLU   A N   1 
ATOM   1817  C CA  . GLU   A 1 229 ? -26.360 -13.168 59.935  1.00 17.46  ?  229 GLU   A CA  1 
ATOM   1818  C C   . GLU   A 1 229 ? -27.575 -14.082 59.845  1.00 20.81  ?  229 GLU   A C   1 
ATOM   1819  O O   . GLU   A 1 229 ? -28.055 -14.588 60.869  1.00 20.93  ?  229 GLU   A O   1 
ATOM   1820  C CB  . GLU   A 1 229 ? -26.726 -11.688 59.830  1.00 18.27  ?  229 GLU   A CB  1 
ATOM   1821  C CG  . GLU   A 1 229 ? -25.469 -10.835 60.072  1.00 20.93  ?  229 GLU   A CG  1 
ATOM   1822  C CD  . GLU   A 1 229 ? -25.665 -9.350  59.865  1.00 20.23  ?  229 GLU   A CD  1 
ATOM   1823  O OE1 . GLU   A 1 229 ? -26.773 -8.925  59.481  1.00 22.19  ?  229 GLU   A OE1 1 
ATOM   1824  O OE2 . GLU   A 1 229 ? -24.687 -8.605  60.092  1.00 22.59  ?  229 GLU   A OE2 1 
ATOM   1825  N N   . ASN   A 1 230 ? -28.050 -14.358 58.625  1.00 19.20  ?  230 ASN   A N   1 
ATOM   1826  C CA  . ASN   A 1 230 ? -29.173 -15.277 58.467  1.00 17.77  ?  230 ASN   A CA  1 
ATOM   1827  C C   . ASN   A 1 230 ? -28.827 -16.661 58.991  1.00 18.47  ?  230 ASN   A C   1 
ATOM   1828  O O   . ASN   A 1 230 ? -29.646 -17.308 59.655  1.00 22.75  ?  230 ASN   A O   1 
ATOM   1829  C CB  . ASN   A 1 230 ? -29.595 -15.367 57.005  1.00 12.78  ?  230 ASN   A CB  1 
ATOM   1830  C CG  . ASN   A 1 230 ? -31.034 -15.793 56.859  1.00 19.00  ?  230 ASN   A CG  1 
ATOM   1831  O OD1 . ASN   A 1 230 ? -31.936 -14.958 56.843  1.00 22.75  ?  230 ASN   A OD1 1 
ATOM   1832  N ND2 . ASN   A 1 230 ? -31.264 -17.097 56.783  1.00 20.39  ?  230 ASN   A ND2 1 
ATOM   1833  N N   . ALA   A 1 231 ? -27.618 -17.132 58.693  1.00 18.53  ?  231 ALA   A N   1 
ATOM   1834  C CA  . ALA   A 1 231 ? -27.176 -18.425 59.194  1.00 18.66  ?  231 ALA   A CA  1 
ATOM   1835  C C   . ALA   A 1 231 ? -27.178 -18.450 60.715  1.00 20.83  ?  231 ALA   A C   1 
ATOM   1836  O O   . ALA   A 1 231 ? -27.632 -19.427 61.327  1.00 22.23  ?  231 ALA   A O   1 
ATOM   1837  C CB  . ALA   A 1 231 ? -25.780 -18.742 58.654  1.00 15.58  ?  231 ALA   A CB  1 
ATOM   1838  N N   . TYR   A 1 232 ? -26.675 -17.384 61.342  1.00 19.95  ?  232 TYR   A N   1 
ATOM   1839  C CA  . TYR   A 1 232 ? -26.663 -17.317 62.801  1.00 18.78  ?  232 TYR   A CA  1 
ATOM   1840  C C   . TYR   A 1 232 ? -28.064 -17.497 63.366  1.00 22.11  ?  232 TYR   A C   1 
ATOM   1841  O O   . TYR   A 1 232 ? -28.274 -18.271 64.309  1.00 22.83  ?  232 TYR   A O   1 
ATOM   1842  C CB  . TYR   A 1 232 ? -26.071 -15.987 63.265  1.00 18.61  ?  232 TYR   A CB  1 
ATOM   1843  C CG  . TYR   A 1 232 ? -25.983 -15.880 64.764  1.00 21.20  ?  232 TYR   A CG  1 
ATOM   1844  C CD1 . TYR   A 1 232 ? -24.876 -16.369 65.446  1.00 19.91  ?  232 TYR   A CD1 1 
ATOM   1845  C CD2 . TYR   A 1 232 ? -27.020 -15.312 65.508  1.00 21.82  ?  232 TYR   A CD2 1 
ATOM   1846  C CE1 . TYR   A 1 232 ? -24.786 -16.285 66.824  1.00 20.22  ?  232 TYR   A CE1 1 
ATOM   1847  C CE2 . TYR   A 1 232 ? -26.942 -15.226 66.890  1.00 27.65  ?  232 TYR   A CE2 1 
ATOM   1848  C CZ  . TYR   A 1 232 ? -25.814 -15.713 67.541  1.00 26.90  ?  232 TYR   A CZ  1 
ATOM   1849  O OH  . TYR   A 1 232 ? -25.716 -15.636 68.912  1.00 26.43  ?  232 TYR   A OH  1 
ATOM   1850  N N   . PHE   A 1 233 ? -29.042 -16.788 62.800  1.00 21.58  ?  233 PHE   A N   1 
ATOM   1851  C CA  . PHE   A 1 233 ? -30.406 -16.905 63.302  1.00 22.30  ?  233 PHE   A CA  1 
ATOM   1852  C C   . PHE   A 1 233 ? -30.973 -18.300 63.086  1.00 19.49  ?  233 PHE   A C   1 
ATOM   1853  O O   . PHE   A 1 233 ? -31.737 -18.780 63.924  1.00 21.42  ?  233 PHE   A O   1 
ATOM   1854  C CB  . PHE   A 1 233 ? -31.309 -15.855 62.658  1.00 18.65  ?  233 PHE   A CB  1 
ATOM   1855  C CG  . PHE   A 1 233 ? -31.050 -14.462 63.149  1.00 20.42  ?  233 PHE   A CG  1 
ATOM   1856  C CD1 . PHE   A 1 233 ? -31.170 -14.157 64.497  1.00 23.54  ?  233 PHE   A CD1 1 
ATOM   1857  C CD2 . PHE   A 1 233 ? -30.673 -13.460 62.269  1.00 19.11  ?  233 PHE   A CD2 1 
ATOM   1858  C CE1 . PHE   A 1 233 ? -30.926 -12.874 64.959  1.00 23.64  ?  233 PHE   A CE1 1 
ATOM   1859  C CE2 . PHE   A 1 233 ? -30.430 -12.175 62.721  1.00 19.76  ?  233 PHE   A CE2 1 
ATOM   1860  C CZ  . PHE   A 1 233 ? -30.552 -11.881 64.064  1.00 20.16  ?  233 PHE   A CZ  1 
ATOM   1861  N N   . ILE   A 1 234 ? -30.616 -18.971 61.987  1.00 18.09  ?  234 ILE   A N   1 
ATOM   1862  C CA  . ILE   A 1 234 ? -31.103 -20.336 61.795  1.00 19.65  ?  234 ILE   A CA  1 
ATOM   1863  C C   . ILE   A 1 234 ? -30.560 -21.250 62.892  1.00 22.40  ?  234 ILE   A C   1 
ATOM   1864  O O   . ILE   A 1 234 ? -31.289 -22.074 63.452  1.00 23.08  ?  234 ILE   A O   1 
ATOM   1865  C CB  . ILE   A 1 234 ? -30.751 -20.853 60.387  1.00 22.70  ?  234 ILE   A CB  1 
ATOM   1866  C CG1 . ILE   A 1 234 ? -31.596 -20.146 59.322  1.00 18.05  ?  234 ILE   A CG1 1 
ATOM   1867  C CG2 . ILE   A 1 234 ? -30.969 -22.354 60.303  1.00 20.74  ?  234 ILE   A CG2 1 
ATOM   1868  C CD1 . ILE   A 1 234 ? -31.166 -20.456 57.900  1.00 17.67  ?  234 ILE   A CD1 1 
ATOM   1869  N N   . LYS   A 1 235 ? -29.282 -21.098 63.241  1.00 20.49  ?  235 LYS   A N   1 
ATOM   1870  C CA  . LYS   A 1 235 ? -28.728 -21.887 64.341  1.00 21.52  ?  235 LYS   A CA  1 
ATOM   1871  C C   . LYS   A 1 235 ? -29.315 -21.467 65.686  1.00 26.24  ?  235 LYS   A C   1 
ATOM   1872  O O   . LYS   A 1 235 ? -29.494 -22.307 66.576  1.00 22.23  ?  235 LYS   A O   1 
ATOM   1873  C CB  . LYS   A 1 235 ? -27.205 -21.758 64.349  1.00 21.20  ?  235 LYS   A CB  1 
ATOM   1874  C CG  . LYS   A 1 235 ? -26.512 -22.493 65.467  1.00 25.04  ?  235 LYS   A CG  1 
ATOM   1875  C CD  . LYS   A 1 235 ? -25.020 -22.287 65.404  1.00 23.40  ?  235 LYS   A CD  1 
ATOM   1876  C CE  . LYS   A 1 235 ? -24.363 -22.804 66.670  1.00 27.14  ?  235 LYS   A CE  1 
ATOM   1877  N NZ  . LYS   A 1 235 ? -24.650 -24.235 66.877  1.00 31.50  ?  235 LYS   A NZ  1 
ATOM   1878  N N   . ALA   A 1 236 ? -29.645 -20.182 65.841  1.00 22.41  ?  236 ALA   A N   1 
ATOM   1879  C CA  . ALA   A 1 236 ? -30.208 -19.705 67.094  1.00 20.75  ?  236 ALA   A CA  1 
ATOM   1880  C C   . ALA   A 1 236 ? -31.623 -20.228 67.309  1.00 23.58  ?  236 ALA   A C   1 
ATOM   1881  O O   . ALA   A 1 236 ? -31.986 -20.604 68.429  1.00 27.33  ?  236 ALA   A O   1 
ATOM   1882  C CB  . ALA   A 1 236 ? -30.193 -18.176 67.117  1.00 21.80  ?  236 ALA   A CB  1 
ATOM   1883  N N   . ARG   A 1 237 ? -32.434 -20.278 66.256  1.00 21.78  ?  237 ARG   A N   1 
ATOM   1884  C CA  . ARG   A 1 237 ? -33.868 -20.465 66.418  1.00 24.66  ?  237 ARG   A CA  1 
ATOM   1885  C C   . ARG   A 1 237 ? -34.423 -21.750 65.816  1.00 27.96  ?  237 ARG   A C   1 
ATOM   1886  O O   . ARG   A 1 237 ? -35.603 -22.047 66.032  1.00 29.03  ?  237 ARG   A O   1 
ATOM   1887  C CB  . ARG   A 1 237 ? -34.616 -19.265 65.817  1.00 19.08  ?  237 ARG   A CB  1 
ATOM   1888  C CG  . ARG   A 1 237 ? -34.018 -17.934 66.242  1.00 19.96  ?  237 ARG   A CG  1 
ATOM   1889  C CD  . ARG   A 1 237 ? -34.806 -16.744 65.716  1.00 22.37  ?  237 ARG   A CD  1 
ATOM   1890  N NE  . ARG   A 1 237 ? -34.315 -15.484 66.265  1.00 21.65  ?  237 ARG   A NE  1 
ATOM   1891  C CZ  . ARG   A 1 237 ? -34.624 -14.288 65.781  1.00 21.33  ?  237 ARG   A CZ  1 
ATOM   1892  N NH1 . ARG   A 1 237 ? -35.353 -14.154 64.684  1.00 21.58  ?  237 ARG   A NH1 1 
ATOM   1893  N NH2 . ARG   A 1 237 ? -34.201 -13.201 66.419  1.00 20.08  ?  237 ARG   A NH2 1 
ATOM   1894  N N   . ASP   A 1 238 ? -33.628 -22.520 65.083  1.00 24.34  ?  238 ASP   A N   1 
ATOM   1895  C CA  . ASP   A 1 238 ? -34.125 -23.739 64.454  1.00 24.08  ?  238 ASP   A CA  1 
ATOM   1896  C C   . ASP   A 1 238 ? -33.536 -24.952 65.158  1.00 27.38  ?  238 ASP   A C   1 
ATOM   1897  O O   . ASP   A 1 238 ? -32.341 -25.238 64.982  1.00 26.79  ?  238 ASP   A O   1 
ATOM   1898  C CB  . ASP   A 1 238 ? -33.765 -23.761 62.967  1.00 25.97  ?  238 ASP   A CB  1 
ATOM   1899  C CG  . ASP   A 1 238 ? -34.464 -24.877 62.206  1.00 29.48  ?  238 ASP   A CG  1 
ATOM   1900  O OD1 . ASP   A 1 238 ? -34.857 -25.891 62.831  1.00 30.24  ?  238 ASP   A OD1 1 
ATOM   1901  O OD2 . ASP   A 1 238 ? -34.613 -24.738 60.971  1.00 25.45  ?  238 ASP   A OD2 1 
ATOM   1902  N N   . PRO   A 1 239 ? -34.328 -25.707 65.928  1.00 29.14  ?  239 PRO   A N   1 
ATOM   1903  C CA  . PRO   A 1 239 ? -33.776 -26.875 66.638  1.00 29.63  ?  239 PRO   A CA  1 
ATOM   1904  C C   . PRO   A 1 239 ? -33.083 -27.879 65.731  1.00 30.68  ?  239 PRO   A C   1 
ATOM   1905  O O   . PRO   A 1 239 ? -32.241 -28.647 66.215  1.00 27.36  ?  239 PRO   A O   1 
ATOM   1906  C CB  . PRO   A 1 239 ? -35.011 -27.495 67.314  1.00 29.48  ?  239 PRO   A CB  1 
ATOM   1907  C CG  . PRO   A 1 239 ? -36.185 -26.922 66.613  1.00 28.93  ?  239 PRO   A CG  1 
ATOM   1908  C CD  . PRO   A 1 239 ? -35.774 -25.556 66.152  1.00 29.23  ?  239 PRO   A CD  1 
ATOM   1909  N N   . LYS   A 1 240 ? -33.412 -27.901 64.435  1.00 28.10  ?  240 LYS   A N   1 
ATOM   1910  C CA  . LYS   A 1 240 ? -32.709 -28.776 63.505  1.00 25.16  ?  240 LYS   A CA  1 
ATOM   1911  C C   . LYS   A 1 240 ? -31.244 -28.387 63.376  1.00 27.24  ?  240 LYS   A C   1 
ATOM   1912  O O   . LYS   A 1 240 ? -30.396 -29.241 63.085  1.00 29.93  ?  240 LYS   A O   1 
ATOM   1913  C CB  . LYS   A 1 240 ? -33.404 -28.735 62.140  1.00 29.31  ?  240 LYS   A CB  1 
ATOM   1914  C CG  . LYS   A 1 240 ? -32.776 -29.611 61.062  1.00 32.75  ?  240 LYS   A CG  1 
ATOM   1915  C CD  . LYS   A 1 240 ? -33.599 -29.579 59.769  1.00 37.36  ?  240 LYS   A CD  1 
ATOM   1916  C CE  . LYS   A 1 240 ? -35.043 -30.006 60.020  1.00 40.51  ?  240 LYS   A CE  1 
ATOM   1917  N NZ  . LYS   A 1 240 ? -35.858 -30.149 58.769  1.00 43.39  ?  240 LYS   A NZ  1 
ATOM   1918  N N   . TYR   A 1 241 ? -30.921 -27.111 63.597  1.00 23.00  ?  241 TYR   A N   1 
ATOM   1919  C CA  . TYR   A 1 241 ? -29.577 -26.597 63.366  1.00 22.77  ?  241 TYR   A CA  1 
ATOM   1920  C C   . TYR   A 1 241 ? -28.924 -26.074 64.633  1.00 24.77  ?  241 TYR   A C   1 
ATOM   1921  O O   . TYR   A 1 241 ? -27.828 -25.509 64.560  1.00 27.45  ?  241 TYR   A O   1 
ATOM   1922  C CB  . TYR   A 1 241 ? -29.610 -25.498 62.301  1.00 23.69  ?  241 TYR   A CB  1 
ATOM   1923  C CG  . TYR   A 1 241 ? -29.885 -26.042 60.929  1.00 24.42  ?  241 TYR   A CG  1 
ATOM   1924  C CD1 . TYR   A 1 241 ? -28.879 -26.652 60.197  1.00 24.08  ?  241 TYR   A CD1 1 
ATOM   1925  C CD2 . TYR   A 1 241 ? -31.158 -25.977 60.373  1.00 28.25  ?  241 TYR   A CD2 1 
ATOM   1926  C CE1 . TYR   A 1 241 ? -29.122 -27.166 58.942  1.00 28.29  ?  241 TYR   A CE1 1 
ATOM   1927  C CE2 . TYR   A 1 241 ? -31.410 -26.492 59.121  1.00 26.32  ?  241 TYR   A CE2 1 
ATOM   1928  C CZ  . TYR   A 1 241 ? -30.389 -27.088 58.412  1.00 29.11  ?  241 TYR   A CZ  1 
ATOM   1929  O OH  . TYR   A 1 241 ? -30.631 -27.600 57.161  1.00 29.84  ?  241 TYR   A OH  1 
ATOM   1930  N N   . LYS   A 1 242 ? -29.564 -26.261 65.790  1.00 25.67  ?  242 LYS   A N   1 
ATOM   1931  C CA  . LYS   A 1 242 ? -29.077 -25.671 67.032  1.00 27.72  ?  242 LYS   A CA  1 
ATOM   1932  C C   . LYS   A 1 242 ? -27.680 -26.163 67.383  1.00 28.32  ?  242 LYS   A C   1 
ATOM   1933  O O   . LYS   A 1 242 ? -26.925 -25.459 68.065  1.00 27.73  ?  242 LYS   A O   1 
ATOM   1934  C CB  . LYS   A 1 242 ? -30.055 -25.979 68.168  1.00 28.14  ?  242 LYS   A CB  1 
ATOM   1935  C CG  . LYS   A 1 242 ? -29.669 -25.369 69.506  1.00 35.14  ?  242 LYS   A CG  1 
ATOM   1936  C CD  . LYS   A 1 242 ? -30.709 -25.652 70.580  1.00 40.89  ?  242 LYS   A CD  1 
ATOM   1937  C CE  . LYS   A 1 242 ? -30.393 -24.867 71.842  1.00 39.29  ?  242 LYS   A CE  1 
ATOM   1938  N NZ  . LYS   A 1 242 ? -28.942 -24.972 72.179  1.00 42.43  ?  242 LYS   A NZ  1 
ATOM   1939  N N   . ASN   A 1 243 ? -27.307 -27.350 66.911  1.00 26.04  ?  243 ASN   A N   1 
ATOM   1940  C CA  . ASN   A 1 243 ? -26.006 -27.925 67.208  1.00 26.64  ?  243 ASN   A CA  1 
ATOM   1941  C C   . ASN   A 1 243 ? -25.132 -28.067 65.968  1.00 29.98  ?  243 ASN   A C   1 
ATOM   1942  O O   . ASN   A 1 243 ? -24.116 -28.766 66.018  1.00 33.28  ?  243 ASN   A O   1 
ATOM   1943  C CB  . ASN   A 1 243 ? -26.186 -29.271 67.913  1.00 28.14  ?  243 ASN   A CB  1 
ATOM   1944  C CG  . ASN   A 1 243 ? -26.923 -29.136 69.252  1.00 30.42  ?  243 ASN   A CG  1 
ATOM   1945  O OD1 . ASN   A 1 243 ? -26.317 -28.830 70.284  1.00 30.79  ?  243 ASN   A OD1 1 
ATOM   1946  N ND2 . ASN   A 1 243 ? -28.236 -29.361 69.234  1.00 27.91  ?  243 ASN   A ND2 1 
ATOM   1947  N N   . ALA   A 1 244 ? -25.492 -27.419 64.863  1.00 26.68  ?  244 ALA   A N   1 
ATOM   1948  C CA  . ALA   A 1 244 ? -24.641 -27.358 63.684  1.00 24.88  ?  244 ALA   A CA  1 
ATOM   1949  C C   . ALA   A 1 244 ? -23.664 -26.187 63.795  1.00 25.39  ?  244 ALA   A C   1 
ATOM   1950  O O   . ALA   A 1 244 ? -23.809 -25.306 64.643  1.00 26.24  ?  244 ALA   A O   1 
ATOM   1951  C CB  . ALA   A 1 244 ? -25.492 -27.225 62.420  1.00 22.83  ?  244 ALA   A CB  1 
ATOM   1952  N N   . THR   A 1 245 ? -22.650 -26.189 62.929  1.00 25.37  ?  245 THR   A N   1 
ATOM   1953  C CA  . THR   A 1 245 ? -21.762 -25.040 62.797  1.00 23.37  ?  245 THR   A CA  1 
ATOM   1954  C C   . THR   A 1 245 ? -22.400 -23.986 61.891  1.00 25.31  ?  245 THR   A C   1 
ATOM   1955  O O   . THR   A 1 245 ? -23.360 -24.254 61.166  1.00 27.54  ?  245 THR   A O   1 
ATOM   1956  C CB  . THR   A 1 245 ? -20.403 -25.451 62.222  1.00 23.62  ?  245 THR   A CB  1 
ATOM   1957  O OG1 . THR   A 1 245 ? -20.558 -25.883 60.864  1.00 22.55  ?  245 THR   A OG1 1 
ATOM   1958  C CG2 . THR   A 1 245 ? -19.790 -26.579 63.030  1.00 24.69  ?  245 THR   A CG2 1 
ATOM   1959  N N   . ILE   A 1 246 ? -21.865 -22.765 61.947  1.00 20.53  ?  246 ILE   A N   1 
ATOM   1960  C CA  . ILE   A 1 246 ? -22.358 -21.718 61.055  1.00 22.91  ?  246 ILE   A CA  1 
ATOM   1961  C C   . ILE   A 1 246 ? -22.142 -22.119 59.601  1.00 22.43  ?  246 ILE   A C   1 
ATOM   1962  O O   . ILE   A 1 246 ? -23.027 -21.943 58.753  1.00 21.31  ?  246 ILE   A O   1 
ATOM   1963  C CB  . ILE   A 1 246 ? -21.684 -20.370 61.367  1.00 19.74  ?  246 ILE   A CB  1 
ATOM   1964  C CG1 . ILE   A 1 246 ? -22.144 -19.839 62.722  1.00 21.06  ?  246 ILE   A CG1 1 
ATOM   1965  C CG2 . ILE   A 1 246 ? -21.984 -19.370 60.260  1.00 19.12  ?  246 ILE   A CG2 1 
ATOM   1966  C CD1 . ILE   A 1 246 ? -23.601 -19.435 62.755  1.00 19.29  ?  246 ILE   A CD1 1 
ATOM   1967  N N   . LYS   A 1 247 ? -20.968 -22.683 59.293  1.00 19.08  ?  247 LYS   A N   1 
ATOM   1968  C CA  . LYS   A 1 247 ? -20.673 -23.062 57.915  1.00 23.87  ?  247 LYS   A CA  1 
ATOM   1969  C C   . LYS   A 1 247 ? -21.564 -24.196 57.435  1.00 20.99  ?  247 LYS   A C   1 
ATOM   1970  O O   . LYS   A 1 247 ? -21.895 -24.256 56.246  1.00 19.72  ?  247 LYS   A O   1 
ATOM   1971  C CB  . LYS   A 1 247 ? -19.206 -23.451 57.773  1.00 25.17  ?  247 LYS   A CB  1 
ATOM   1972  C CG  . LYS   A 1 247 ? -18.259 -22.273 57.817  1.00 22.26  ?  247 LYS   A CG  1 
ATOM   1973  C CD  . LYS   A 1 247 ? -16.846 -22.714 57.511  1.00 25.50  ?  247 LYS   A CD  1 
ATOM   1974  C CE  . LYS   A 1 247 ? -15.884 -21.559 57.580  1.00 23.43  ?  247 LYS   A CE  1 
ATOM   1975  N NZ  . LYS   A 1 247 ? -14.509 -22.025 57.297  1.00 25.49  ?  247 LYS   A NZ  1 
ATOM   1976  N N   . GLU   A 1 248 ? -21.961 -25.096 58.335  1.00 24.28  ?  248 GLU   A N   1 
ATOM   1977  C CA  . GLU   A 1 248 ? -22.914 -26.140 57.972  1.00 23.11  ?  248 GLU   A CA  1 
ATOM   1978  C C   . GLU   A 1 248 ? -24.279 -25.546 57.652  1.00 24.45  ?  248 GLU   A C   1 
ATOM   1979  O O   . GLU   A 1 248 ? -24.933 -25.961 56.684  1.00 23.25  ?  248 GLU   A O   1 
ATOM   1980  C CB  . GLU   A 1 248 ? -23.003 -27.174 59.099  1.00 23.29  ?  248 GLU   A CB  1 
ATOM   1981  C CG  . GLU   A 1 248 ? -21.826 -28.161 59.091  1.00 27.53  ?  248 GLU   A CG  1 
ATOM   1982  C CD  . GLU   A 1 248 ? -21.688 -28.968 60.380  1.00 29.18  ?  248 GLU   A CD  1 
ATOM   1983  O OE1 . GLU   A 1 248 ? -22.497 -28.774 61.309  1.00 25.33  ?  248 GLU   A OE1 1 
ATOM   1984  O OE2 . GLU   A 1 248 ? -20.756 -29.797 60.464  1.00 32.87  ?  248 GLU   A OE2 1 
ATOM   1985  N N   . VAL   A 1 249 ? -24.712 -24.552 58.434  1.00 23.73  ?  249 VAL   A N   1 
ATOM   1986  C CA  . VAL   A 1 249 ? -25.960 -23.852 58.132  1.00 20.96  ?  249 VAL   A CA  1 
ATOM   1987  C C   . VAL   A 1 249 ? -25.872 -23.173 56.768  1.00 20.15  ?  249 VAL   A C   1 
ATOM   1988  O O   . VAL   A 1 249 ? -26.776 -23.303 55.933  1.00 20.50  ?  249 VAL   A O   1 
ATOM   1989  C CB  . VAL   A 1 249 ? -26.294 -22.841 59.243  1.00 16.74  ?  249 VAL   A CB  1 
ATOM   1990  C CG1 . VAL   A 1 249 ? -27.472 -21.988 58.831  1.00 18.54  ?  249 VAL   A CG1 1 
ATOM   1991  C CG2 . VAL   A 1 249 ? -26.598 -23.560 60.560  1.00 19.95  ?  249 VAL   A CG2 1 
ATOM   1992  N N   . ILE   A 1 250 ? -24.784 -22.434 56.527  1.00 21.23  ?  250 ILE   A N   1 
ATOM   1993  C CA  . ILE   A 1 250 ? -24.600 -21.748 55.245  1.00 19.55  ?  250 ILE   A CA  1 
ATOM   1994  C C   . ILE   A 1 250 ? -24.684 -22.742 54.098  1.00 22.46  ?  250 ILE   A C   1 
ATOM   1995  O O   . ILE   A 1 250 ? -25.400 -22.531 53.111  1.00 22.02  ?  250 ILE   A O   1 
ATOM   1996  C CB  . ILE   A 1 250 ? -23.254 -21.003 55.223  1.00 20.46  ?  250 ILE   A CB  1 
ATOM   1997  C CG1 . ILE   A 1 250 ? -23.300 -19.762 56.113  1.00 20.35  ?  250 ILE   A CG1 1 
ATOM   1998  C CG2 . ILE   A 1 250 ? -22.879 -20.635 53.803  1.00 20.62  ?  250 ILE   A CG2 1 
ATOM   1999  C CD1 . ILE   A 1 250 ? -21.923 -19.179 56.399  1.00 21.41  ?  250 ILE   A CD1 1 
ATOM   2000  N N   . PHE   A 1 251 ? -23.944 -23.843 54.216  1.00 22.11  ?  251 PHE   A N   1 
ATOM   2001  C CA  . PHE   A 1 251 ? -23.934 -24.861 53.177  1.00 20.83  ?  251 PHE   A CA  1 
ATOM   2002  C C   . PHE   A 1 251 ? -25.349 -25.315 52.838  1.00 24.34  ?  251 PHE   A C   1 
ATOM   2003  O O   . PHE   A 1 251 ? -25.727 -25.388 51.663  1.00 24.92  ?  251 PHE   A O   1 
ATOM   2004  C CB  . PHE   A 1 251 ? -23.073 -26.030 53.642  1.00 21.03  ?  251 PHE   A CB  1 
ATOM   2005  C CG  . PHE   A 1 251 ? -22.606 -26.905 52.542  1.00 21.14  ?  251 PHE   A CG  1 
ATOM   2006  C CD1 . PHE   A 1 251 ? -21.525 -26.536 51.766  1.00 20.52  ?  251 PHE   A CD1 1 
ATOM   2007  C CD2 . PHE   A 1 251 ? -23.243 -28.108 52.283  1.00 23.90  ?  251 PHE   A CD2 1 
ATOM   2008  C CE1 . PHE   A 1 251 ? -21.084 -27.349 50.748  1.00 25.83  ?  251 PHE   A CE1 1 
ATOM   2009  C CE2 . PHE   A 1 251 ? -22.810 -28.926 51.270  1.00 23.62  ?  251 PHE   A CE2 1 
ATOM   2010  C CZ  . PHE   A 1 251 ? -21.730 -28.546 50.496  1.00 28.35  ?  251 PHE   A CZ  1 
ATOM   2011  N N   . ASP   A 1 252 ? -26.156 -25.601 53.867  1.00 23.84  ?  252 ASP   A N   1 
ATOM   2012  C CA  . ASP   A 1 252 ? -27.523 -26.061 53.640  1.00 21.83  ?  252 ASP   A CA  1 
ATOM   2013  C C   . ASP   A 1 252 ? -28.375 -24.976 52.992  1.00 22.77  ?  252 ASP   A C   1 
ATOM   2014  O O   . ASP   A 1 252 ? -29.173 -25.267 52.092  1.00 24.39  ?  252 ASP   A O   1 
ATOM   2015  C CB  . ASP   A 1 252 ? -28.148 -26.530 54.956  1.00 22.91  ?  252 ASP   A CB  1 
ATOM   2016  C CG  . ASP   A 1 252 ? -27.833 -27.992 55.271  1.00 28.70  ?  252 ASP   A CG  1 
ATOM   2017  O OD1 . ASP   A 1 252 ? -26.936 -28.571 54.616  1.00 28.14  ?  252 ASP   A OD1 1 
ATOM   2018  O OD2 . ASP   A 1 252 ? -28.486 -28.566 56.172  1.00 28.59  ?  252 ASP   A OD2 1 
ATOM   2019  N N   . MET   A 1 253 ? -28.208 -23.721 53.426  1.00 22.41  ?  253 MET   A N   1 
ATOM   2020  C CA  . MET   A 1 253 ? -28.942 -22.602 52.831  1.00 22.01  ?  253 MET   A CA  1 
ATOM   2021  C C   . MET   A 1 253 ? -28.802 -22.581 51.315  1.00 24.50  ?  253 MET   A C   1 
ATOM   2022  O O   . MET   A 1 253 ? -29.791 -22.429 50.588  1.00 23.57  ?  253 MET   A O   1 
ATOM   2023  C CB  . MET   A 1 253 ? -28.447 -21.273 53.407  1.00 21.98  ?  253 MET   A CB  1 
ATOM   2024  C CG  . MET   A 1 253 ? -28.829 -21.004 54.854  1.00 22.47  ?  253 MET   A CG  1 
ATOM   2025  S SD  . MET   A 1 253 ? -28.147 -19.436 55.443  1.00 24.97  ?  253 MET   A SD  1 
ATOM   2026  C CE  . MET   A 1 253 ? -28.603 -18.340 54.097  1.00 22.99  ?  253 MET   A CE  1 
ATOM   2027  N N   . TYR   A 1 254 ? -27.577 -22.737 50.820  1.00 22.25  ?  254 TYR   A N   1 
ATOM   2028  C CA  . TYR   A 1 254 ? -27.298 -22.552 49.402  1.00 21.68  ?  254 TYR   A CA  1 
ATOM   2029  C C   . TYR   A 1 254 ? -27.595 -23.782 48.566  1.00 24.58  ?  254 TYR   A C   1 
ATOM   2030  O O   . TYR   A 1 254 ? -27.359 -23.756 47.354  1.00 23.73  ?  254 TYR   A O   1 
ATOM   2031  C CB  . TYR   A 1 254 ? -25.854 -22.081 49.223  1.00 21.36  ?  254 TYR   A CB  1 
ATOM   2032  C CG  . TYR   A 1 254 ? -25.794 -20.629 49.608  1.00 22.14  ?  254 TYR   A CG  1 
ATOM   2033  C CD1 . TYR   A 1 254 ? -25.679 -20.252 50.936  1.00 20.80  ?  254 TYR   A CD1 1 
ATOM   2034  C CD2 . TYR   A 1 254 ? -25.968 -19.636 48.656  1.00 21.00  ?  254 TYR   A CD2 1 
ATOM   2035  C CE1 . TYR   A 1 254 ? -25.688 -18.927 51.304  1.00 21.37  ?  254 TYR   A CE1 1 
ATOM   2036  C CE2 . TYR   A 1 254 ? -25.975 -18.311 49.014  1.00 20.61  ?  254 TYR   A CE2 1 
ATOM   2037  C CZ  . TYR   A 1 254 ? -25.833 -17.964 50.334  1.00 22.11  ?  254 TYR   A CZ  1 
ATOM   2038  O OH  . TYR   A 1 254 ? -25.841 -16.643 50.682  1.00 22.35  ?  254 TYR   A OH  1 
ATOM   2039  N N   . LYS   A 1 255 ? -28.136 -24.839 49.175  1.00 22.22  ?  255 LYS   A N   1 
ATOM   2040  C CA  . LYS   A 1 255 ? -28.781 -25.885 48.397  1.00 26.83  ?  255 LYS   A CA  1 
ATOM   2041  C C   . LYS   A 1 255 ? -30.124 -25.433 47.847  1.00 25.24  ?  255 LYS   A C   1 
ATOM   2042  O O   . LYS   A 1 255 ? -30.704 -26.137 47.014  1.00 25.78  ?  255 LYS   A O   1 
ATOM   2043  C CB  . LYS   A 1 255 ? -28.979 -27.136 49.253  1.00 25.59  ?  255 LYS   A CB  1 
ATOM   2044  C CG  . LYS   A 1 255 ? -27.688 -27.757 49.767  1.00 27.51  ?  255 LYS   A CG  1 
ATOM   2045  C CD  . LYS   A 1 255 ? -27.987 -28.900 50.725  1.00 26.14  ?  255 LYS   A CD  1 
ATOM   2046  C CE  . LYS   A 1 255 ? -26.731 -29.358 51.442  1.00 25.81  ?  255 LYS   A CE  1 
ATOM   2047  N NZ  . LYS   A 1 255 ? -27.058 -30.419 52.441  1.00 34.59  ?  255 LYS   A NZ  1 
ATOM   2048  N N   . TYR   A 1 256 ? -30.617 -24.278 48.289  1.00 23.25  ?  256 TYR   A N   1 
ATOM   2049  C CA  . TYR   A 1 256 ? -31.949 -23.787 47.975  1.00 24.64  ?  256 TYR   A CA  1 
ATOM   2050  C C   . TYR   A 1 256 ? -31.866 -22.504 47.166  1.00 24.62  ?  256 TYR   A C   1 
ATOM   2051  O O   . TYR   A 1 256 ? -32.677 -21.588 47.314  1.00 25.06  ?  256 TYR   A O   1 
ATOM   2052  C CB  . TYR   A 1 256 ? -32.757 -23.610 49.257  1.00 26.75  ?  256 TYR   A CB  1 
ATOM   2053  C CG  . TYR   A 1 256 ? -32.752 -24.884 50.069  1.00 27.20  ?  256 TYR   A CG  1 
ATOM   2054  C CD1 . TYR   A 1 256 ? -33.109 -26.094 49.487  1.00 25.62  ?  256 TYR   A CD1 1 
ATOM   2055  C CD2 . TYR   A 1 256 ? -32.333 -24.892 51.390  1.00 25.57  ?  256 TYR   A CD2 1 
ATOM   2056  C CE1 . TYR   A 1 256 ? -33.080 -27.267 50.211  1.00 27.72  ?  256 TYR   A CE1 1 
ATOM   2057  C CE2 . TYR   A 1 256 ? -32.301 -26.063 52.120  1.00 29.76  ?  256 TYR   A CE2 1 
ATOM   2058  C CZ  . TYR   A 1 256 ? -32.678 -27.246 51.524  1.00 30.21  ?  256 TYR   A CZ  1 
ATOM   2059  O OH  . TYR   A 1 256 ? -32.647 -28.416 52.244  1.00 32.90  ?  256 TYR   A OH  1 
ATOM   2060  N N   . ALA   A 1 257 ? -30.865 -22.440 46.296  1.00 24.07  ?  257 ALA   A N   1 
ATOM   2061  C CA  . ALA   A 1 257 ? -30.761 -21.408 45.279  1.00 23.73  ?  257 ALA   A CA  1 
ATOM   2062  C C   . ALA   A 1 257 ? -29.932 -21.969 44.133  1.00 23.66  ?  257 ALA   A C   1 
ATOM   2063  O O   . ALA   A 1 257 ? -29.262 -22.996 44.272  1.00 25.68  ?  257 ALA   A O   1 
ATOM   2064  C CB  . ALA   A 1 257 ? -30.144 -20.119 45.838  1.00 20.68  ?  257 ALA   A CB  1 
ATOM   2065  N N   . ASP   A 1 258 ? -30.002 -21.299 42.983  1.00 22.56  ?  258 ASP   A N   1 
ATOM   2066  C CA  . ASP   A 1 258 ? -29.205 -21.663 41.824  1.00 19.76  ?  258 ASP   A CA  1 
ATOM   2067  C C   . ASP   A 1 258 ? -28.030 -20.730 41.602  1.00 22.44  ?  258 ASP   A C   1 
ATOM   2068  O O   . ASP   A 1 258 ? -27.163 -21.041 40.780  1.00 21.73  ?  258 ASP   A O   1 
ATOM   2069  C CB  . ASP   A 1 258 ? -30.069 -21.670 40.566  1.00 21.89  ?  258 ASP   A CB  1 
ATOM   2070  C CG  . ASP   A 1 258 ? -31.248 -22.591 40.689  1.00 24.79  ?  258 ASP   A CG  1 
ATOM   2071  O OD1 . ASP   A 1 258 ? -31.026 -23.800 40.932  1.00 28.35  ?  258 ASP   A OD1 1 
ATOM   2072  O OD2 . ASP   A 1 258 ? -32.395 -22.099 40.581  1.00 23.59  ?  258 ASP   A OD2 1 
ATOM   2073  N N   . ALA   A 1 259 ? -27.989 -19.605 42.310  1.00 19.82  ?  259 ALA   A N   1 
ATOM   2074  C CA  . ALA   A 1 259 ? -26.956 -18.590 42.159  1.00 18.50  ?  259 ALA   A CA  1 
ATOM   2075  C C   . ALA   A 1 259 ? -27.110 -17.601 43.304  1.00 20.19  ?  259 ALA   A C   1 
ATOM   2076  O O   . ALA   A 1 259 ? -28.114 -17.603 44.021  1.00 21.63  ?  259 ALA   A O   1 
ATOM   2077  C CB  . ALA   A 1 259 ? -27.053 -17.876 40.811  1.00 18.84  ?  259 ALA   A CB  1 
ATOM   2078  N N   . LEU   A 1 260 ? -26.105 -16.747 43.467  1.00 19.13  ?  260 LEU   A N   1 
ATOM   2079  C CA  . LEU   A 1 260 ? -26.180 -15.710 44.481  1.00 20.72  ?  260 LEU   A CA  1 
ATOM   2080  C C   . LEU   A 1 260 ? -25.623 -14.409 43.929  1.00 20.00  ?  260 LEU   A C   1 
ATOM   2081  O O   . LEU   A 1 260 ? -24.713 -14.400 43.096  1.00 18.62  ?  260 LEU   A O   1 
ATOM   2082  C CB  . LEU   A 1 260 ? -25.433 -16.101 45.770  1.00 19.70  ?  260 LEU   A CB  1 
ATOM   2083  C CG  . LEU   A 1 260 ? -23.927 -16.347 45.702  1.00 17.00  ?  260 LEU   A CG  1 
ATOM   2084  C CD1 . LEU   A 1 260 ? -23.124 -15.077 45.940  1.00 16.13  ?  260 LEU   A CD1 1 
ATOM   2085  C CD2 . LEU   A 1 260 ? -23.543 -17.417 46.699  1.00 17.53  ?  260 LEU   A CD2 1 
ATOM   2086  N N   . THR   A 1 261 ? -26.213 -13.312 44.383  1.00 21.68  ?  261 THR   A N   1 
ATOM   2087  C CA  . THR   A 1 261 ? -25.633 -11.988 44.263  1.00 18.04  ?  261 THR   A CA  1 
ATOM   2088  C C   . THR   A 1 261 ? -25.291 -11.532 45.670  1.00 17.25  ?  261 THR   A C   1 
ATOM   2089  O O   . THR   A 1 261 ? -26.059 -11.765 46.608  1.00 22.59  ?  261 THR   A O   1 
ATOM   2090  C CB  . THR   A 1 261 ? -26.596 -11.000 43.586  1.00 18.74  ?  261 THR   A CB  1 
ATOM   2091  O OG1 . THR   A 1 261 ? -27.853 -11.000 44.274  1.00 26.74  ?  261 THR   A OG1 1 
ATOM   2092  C CG2 . THR   A 1 261 ? -26.828 -11.381 42.134  1.00 19.55  ?  261 THR   A CG2 1 
ATOM   2093  N N   . MET   A 1 262 ? -24.132 -10.906 45.827  1.00 18.06  ?  262 MET   A N   1 
ATOM   2094  C CA  . MET   A 1 262 ? -23.644 -10.573 47.154  1.00 17.06  ?  262 MET   A CA  1 
ATOM   2095  C C   . MET   A 1 262 ? -22.966 -9.218  47.146  1.00 16.46  ?  262 MET   A C   1 
ATOM   2096  O O   . MET   A 1 262 ? -22.066 -8.981  46.340  1.00 17.44  ?  262 MET   A O   1 
ATOM   2097  C CB  . MET   A 1 262 ? -22.655 -11.621 47.653  1.00 17.47  ?  262 MET   A CB  1 
ATOM   2098  C CG  . MET   A 1 262 ? -22.162 -11.319 49.046  1.00 20.77  ?  262 MET   A CG  1 
ATOM   2099  S SD  . MET   A 1 262 ? -20.953 -12.518 49.588  1.00 25.39  ?  262 MET   A SD  1 
ATOM   2100  C CE  . MET   A 1 262 ? -21.937 -14.007 49.639  1.00 23.41  ?  262 MET   A CE  1 
ATOM   2101  N N   . SER   A 1 263 ? -23.384 -8.338  48.048  1.00 18.31  ?  263 SER   A N   1 
ATOM   2102  C CA  . SER   A 1 263 ? -22.570 -7.183  48.400  1.00 14.95  ?  263 SER   A CA  1 
ATOM   2103  C C   . SER   A 1 263 ? -21.613 -7.633  49.489  1.00 12.42  ?  263 SER   A C   1 
ATOM   2104  O O   . SER   A 1 263 ? -22.030 -7.883  50.624  1.00 14.44  ?  263 SER   A O   1 
ATOM   2105  C CB  . SER   A 1 263 ? -23.413 -6.009  48.885  1.00 16.99  ?  263 SER   A CB  1 
ATOM   2106  O OG  . SER   A 1 263 ? -22.545 -4.971  49.325  1.00 18.31  ?  263 SER   A OG  1 
ATOM   2107  N N   . ALA   A 1 264 ? -20.334 -7.749  49.152  1.00 14.95  ?  264 ALA   A N   1 
ATOM   2108  C CA  . ALA   A 1 264 ? -19.379 -8.152  50.173  1.00 15.62  ?  264 ALA   A CA  1 
ATOM   2109  C C   . ALA   A 1 264 ? -19.055 -7.015  51.118  1.00 14.73  ?  264 ALA   A C   1 
ATOM   2110  O O   . ALA   A 1 264 ? -18.190 -7.178  51.982  1.00 19.28  ?  264 ALA   A O   1 
ATOM   2111  C CB  . ALA   A 1 264 ? -18.090 -8.695  49.539  1.00 13.90  ?  264 ALA   A CB  1 
ATOM   2112  N N   . LYS   A 1 265 ? -19.720 -5.872  50.970  1.00 13.55  ?  265 LYS   A N   1 
ATOM   2113  C CA  . LYS   A 1 265 ? -19.542 -4.754  51.885  1.00 14.53  ?  265 LYS   A CA  1 
ATOM   2114  C C   . LYS   A 1 265 ? -20.330 -4.928  53.173  1.00 14.06  ?  265 LYS   A C   1 
ATOM   2115  O O   . LYS   A 1 265 ? -20.271 -4.050  54.044  1.00 14.92  ?  265 LYS   A O   1 
ATOM   2116  C CB  . LYS   A 1 265 ? -19.941 -3.452  51.187  1.00 13.13  ?  265 LYS   A CB  1 
ATOM   2117  C CG  . LYS   A 1 265 ? -19.492 -3.403  49.734  1.00 14.49  ?  265 LYS   A CG  1 
ATOM   2118  C CD  . LYS   A 1 265 ? -19.156 -2.012  49.288  1.00 12.42  ?  265 LYS   A CD  1 
ATOM   2119  C CE  . LYS   A 1 265 ? -20.210 -1.029  49.619  1.00 16.71  ?  265 LYS   A CE  1 
ATOM   2120  N NZ  . LYS   A 1 265 ? -20.106 0.176   48.734  1.00 19.11  ?  265 LYS   A NZ  1 
ATOM   2121  N N   . LYS   A 1 266 ? -21.054 -6.047  53.309  1.00 14.58  ?  266 LYS   A N   1 
ATOM   2122  C CA  . LYS   A 1 266 ? -21.847 -6.335  54.491  1.00 15.28  ?  266 LYS   A CA  1 
ATOM   2123  C C   . LYS   A 1 266 ? -21.154 -7.463  55.234  1.00 14.51  ?  266 LYS   A C   1 
ATOM   2124  O O   . LYS   A 1 266 ? -20.092 -7.235  55.837  1.00 18.82  ?  266 LYS   A O   1 
ATOM   2125  C CB  . LYS   A 1 266 ? -23.300 -6.644  54.109  1.00 14.88  ?  266 LYS   A CB  1 
ATOM   2126  C CG  . LYS   A 1 266 ? -24.171 -5.427  53.829  1.00 15.78  ?  266 LYS   A CG  1 
ATOM   2127  C CD  . LYS   A 1 266 ? -23.681 -4.639  52.614  1.00 15.13  ?  266 LYS   A CD  1 
ATOM   2128  C CE  . LYS   A 1 266 ? -24.808 -3.960  51.932  1.00 20.08  ?  266 LYS   A CE  1 
ATOM   2129  N NZ  . LYS   A 1 266 ? -24.249 -3.141  50.834  1.00 22.93  ?  266 LYS   A NZ  1 
ATOM   2130  N N   . ASP   A 1 267 ? -21.682 -8.693  55.207  1.00 17.56  ?  267 ASP   A N   1 
ATOM   2131  C CA  . ASP   A 1 267 ? -21.167 -9.730  56.093  1.00 19.22  ?  267 ASP   A CA  1 
ATOM   2132  C C   . ASP   A 1 267 ? -19.707 -10.132 55.864  1.00 18.00  ?  267 ASP   A C   1 
ATOM   2133  O O   . ASP   A 1 267 ? -19.066 -10.547 56.848  1.00 21.34  ?  267 ASP   A O   1 
ATOM   2134  C CB  . ASP   A 1 267 ? -22.061 -10.973 56.020  1.00 18.74  ?  267 ASP   A CB  1 
ATOM   2135  C CG  . ASP   A 1 267 ? -23.309 -10.840 56.859  1.00 20.64  ?  267 ASP   A CG  1 
ATOM   2136  O OD1 . ASP   A 1 267 ? -23.574 -9.707  57.335  1.00 21.45  ?  267 ASP   A OD1 1 
ATOM   2137  O OD2 . ASP   A 1 267 ? -24.027 -11.851 57.046  1.00 20.10  ?  267 ASP   A OD2 1 
ATOM   2138  N N   . PRO   A 1 268 ? -19.133 -10.071 54.647  1.00 14.30  ?  268 PRO   A N   1 
ATOM   2139  C CA  . PRO   A 1 268 ? -17.701 -10.385 54.510  1.00 13.44  ?  268 PRO   A CA  1 
ATOM   2140  C C   . PRO   A 1 268 ? -16.776 -9.293  55.038  1.00 14.56  ?  268 PRO   A C   1 
ATOM   2141  O O   . PRO   A 1 268 ? -15.559 -9.370  54.844  1.00 15.89  ?  268 PRO   A O   1 
ATOM   2142  C CB  . PRO   A 1 268 ? -17.531 -10.579 52.997  1.00 18.44  ?  268 PRO   A CB  1 
ATOM   2143  C CG  . PRO   A 1 268 ? -18.903 -10.951 52.519  1.00 13.46  ?  268 PRO   A CG  1 
ATOM   2144  C CD  . PRO   A 1 268 ? -19.817 -10.109 53.339  1.00 15.27  ?  268 PRO   A CD  1 
ATOM   2145  N N   . LEU   A 1 269 ? -17.332 -8.261  55.677  1.00 14.26  ?  269 LEU   A N   1 
ATOM   2146  C CA  . LEU   A 1 269 ? -16.547 -7.329  56.490  1.00 12.67  ?  269 LEU   A CA  1 
ATOM   2147  C C   . LEU   A 1 269 ? -15.623 -6.462  55.644  1.00 14.12  ?  269 LEU   A C   1 
ATOM   2148  O O   . LEU   A 1 269 ? -14.481 -6.218  56.026  1.00 13.38  ?  269 LEU   A O   1 
ATOM   2149  C CB  . LEU   A 1 269 ? -15.734 -8.073  57.561  1.00 12.76  ?  269 LEU   A CB  1 
ATOM   2150  C CG  . LEU   A 1 269 ? -16.499 -8.806  58.676  1.00 12.69  ?  269 LEU   A CG  1 
ATOM   2151  C CD1 . LEU   A 1 269 ? -15.679 -9.928  59.305  1.00 14.34  ?  269 LEU   A CD1 1 
ATOM   2152  C CD2 . LEU   A 1 269 ? -16.923 -7.822  59.724  1.00 13.09  ?  269 LEU   A CD2 1 
ATOM   2153  N N   . LEU   A 1 270 ? -16.104 -5.980  54.500  1.00 11.38  ?  270 LEU   A N   1 
ATOM   2154  C CA  . LEU   A 1 270 ? -15.247 -5.226  53.589  1.00 15.17  ?  270 LEU   A CA  1 
ATOM   2155  C C   . LEU   A 1 270 ? -15.724 -3.787  53.444  1.00 12.25  ?  270 LEU   A C   1 
ATOM   2156  O O   . LEU   A 1 270 ? -16.815 -3.416  53.878  1.00 14.28  ?  270 LEU   A O   1 
ATOM   2157  C CB  . LEU   A 1 270 ? -15.197 -5.866  52.200  1.00 12.17  ?  270 LEU   A CB  1 
ATOM   2158  C CG  . LEU   A 1 270 ? -14.849 -7.340  52.080  1.00 16.82  ?  270 LEU   A CG  1 
ATOM   2159  C CD1 . LEU   A 1 270 ? -14.796 -7.733  50.607  1.00 14.34  ?  270 LEU   A CD1 1 
ATOM   2160  C CD2 . LEU   A 1 270 ? -13.519 -7.619  52.781  1.00 13.82  ?  270 LEU   A CD2 1 
ATOM   2161  N N   . ASN   A 1 271 ? -14.872 -2.982  52.814  1.00 12.13  ?  271 ASN   A N   1 
ATOM   2162  C CA  . ASN   A 1 271 ? -15.164 -1.598  52.472  1.00 13.20  ?  271 ASN   A CA  1 
ATOM   2163  C C   . ASN   A 1 271 ? -15.613 -1.430  51.027  1.00 12.26  ?  271 ASN   A C   1 
ATOM   2164  O O   . ASN   A 1 271 ? -16.130 -0.362  50.665  1.00 16.43  ?  271 ASN   A O   1 
ATOM   2165  C CB  . ASN   A 1 271 ? -13.924 -0.736  52.712  1.00 11.43  ?  271 ASN   A CB  1 
ATOM   2166  C CG  . ASN   A 1 271 ? -13.421 -0.834  54.124  1.00 12.59  ?  271 ASN   A CG  1 
ATOM   2167  O OD1 . ASN   A 1 271 ? -12.251 -1.135  54.357  1.00 12.14  ?  271 ASN   A OD1 1 
ATOM   2168  N ND2 . ASN   A 1 271 ? -14.302 -0.576  55.083  1.00 13.60  ?  271 ASN   A ND2 1 
ATOM   2169  N N   . ILE   A 1 272 ? -15.401 -2.452  50.200  1.00 13.29  ?  272 ILE   A N   1 
ATOM   2170  C CA  . ILE   A 1 272 ? -15.793 -2.448  48.794  1.00 13.45  ?  272 ILE   A CA  1 
ATOM   2171  C C   . ILE   A 1 272 ? -15.793 -3.911  48.373  1.00 14.95  ?  272 ILE   A C   1 
ATOM   2172  O O   . ILE   A 1 272 ? -15.150 -4.755  49.013  1.00 16.54  ?  272 ILE   A O   1 
ATOM   2173  C CB  . ILE   A 1 272 ? -14.825 -1.603  47.926  1.00 10.72  ?  272 ILE   A CB  1 
ATOM   2174  C CG1 . ILE   A 1 272 ? -15.399 -1.337  46.535  1.00 13.61  ?  272 ILE   A CG1 1 
ATOM   2175  C CG2 . ILE   A 1 272 ? -13.488 -2.318  47.768  1.00 13.19  ?  272 ILE   A CG2 1 
ATOM   2176  C CD1 . ILE   A 1 272 ? -16.680 -0.509  46.537  1.00 14.91  ?  272 ILE   A CD1 1 
ATOM   2177  N N   . GLY   A 1 273 ? -16.539 -4.228  47.322  1.00 14.79  ?  273 GLY   A N   1 
ATOM   2178  C CA  . GLY   A 1 273 ? -16.529 -5.581  46.797  1.00 13.28  ?  273 GLY   A CA  1 
ATOM   2179  C C   . GLY   A 1 273 ? -17.894 -6.215  46.683  1.00 11.66  ?  273 GLY   A C   1 
ATOM   2180  O O   . GLY   A 1 273 ? -18.805 -5.934  47.464  1.00 14.95  ?  273 GLY   A O   1 
ATOM   2181  N N   . GLY   A 1 274 ? -18.034 -7.096  45.692  1.00 16.36  ?  274 GLY   A N   1 
ATOM   2182  C CA  . GLY   A 1 274 ? -19.273 -7.792  45.424  1.00 16.60  ?  274 GLY   A CA  1 
ATOM   2183  C C   . GLY   A 1 274 ? -18.940 -9.099  44.744  1.00 15.96  ?  274 GLY   A C   1 
ATOM   2184  O O   . GLY   A 1 274 ? -17.783 -9.386  44.442  1.00 15.54  ?  274 GLY   A O   1 
ATOM   2185  N N   . LEU   A 1 275 ? -19.967 -9.901  44.507  1.00 13.70  ?  275 LEU   A N   1 
ATOM   2186  C CA  . LEU   A 1 275 ? -19.699 -11.238 44.006  1.00 18.24  ?  275 LEU   A CA  1 
ATOM   2187  C C   . LEU   A 1 275 ? -20.951 -11.787 43.353  1.00 16.45  ?  275 LEU   A C   1 
ATOM   2188  O O   . LEU   A 1 275 ? -22.059 -11.579 43.851  1.00 16.39  ?  275 LEU   A O   1 
ATOM   2189  C CB  . LEU   A 1 275 ? -19.243 -12.170 45.135  1.00 22.35  ?  275 LEU   A CB  1 
ATOM   2190  C CG  . LEU   A 1 275 ? -18.959 -13.647 44.845  1.00 16.01  ?  275 LEU   A CG  1 
ATOM   2191  C CD1 . LEU   A 1 275 ? -17.702 -13.798 43.991  1.00 17.22  ?  275 LEU   A CD1 1 
ATOM   2192  C CD2 . LEU   A 1 275 ? -18.826 -14.399 46.163  1.00 17.38  ?  275 LEU   A CD2 1 
ATOM   2193  N N   . VAL   A 1 276 ? -20.756 -12.467 42.231  1.00 16.18  ?  276 VAL   A N   1 
ATOM   2194  C CA  . VAL   A 1 276 ? -21.749 -13.348 41.637  1.00 16.68  ?  276 VAL   A CA  1 
ATOM   2195  C C   . VAL   A 1 276 ? -21.191 -14.757 41.753  1.00 17.21  ?  276 VAL   A C   1 
ATOM   2196  O O   . VAL   A 1 276 ? -20.002 -14.976 41.503  1.00 19.61  ?  276 VAL   A O   1 
ATOM   2197  C CB  . VAL   A 1 276 ? -22.035 -12.980 40.167  1.00 18.24  ?  276 VAL   A CB  1 
ATOM   2198  C CG1 . VAL   A 1 276 ? -23.062 -13.917 39.562  1.00 16.62  ?  276 VAL   A CG1 1 
ATOM   2199  C CG2 . VAL   A 1 276 ? -22.518 -11.546 40.049  1.00 20.98  ?  276 VAL   A CG2 1 
ATOM   2200  N N   . ALA   A 1 277 ? -22.027 -15.703 42.166  1.00 18.17  ?  277 ALA   A N   1 
ATOM   2201  C CA  . ALA   A 1 277 ? -21.628 -17.104 42.161  1.00 19.61  ?  277 ALA   A CA  1 
ATOM   2202  C C   . ALA   A 1 277 ? -22.774 -17.932 41.606  1.00 19.12  ?  277 ALA   A C   1 
ATOM   2203  O O   . ALA   A 1 277 ? -23.942 -17.662 41.898  1.00 19.76  ?  277 ALA   A O   1 
ATOM   2204  C CB  . ALA   A 1 277 ? -21.230 -17.591 43.560  1.00 15.49  ?  277 ALA   A CB  1 
ATOM   2205  N N   . ILE   A 1 278 ? -22.447 -18.926 40.790  1.00 20.54  ?  278 ILE   A N   1 
ATOM   2206  C CA  . ILE   A 1 278 ? -23.456 -19.738 40.122  1.00 20.76  ?  278 ILE   A CA  1 
ATOM   2207  C C   . ILE   A 1 278 ? -23.189 -21.201 40.457  1.00 25.25  ?  278 ILE   A C   1 
ATOM   2208  O O   . ILE   A 1 278 ? -22.039 -21.649 40.430  1.00 24.65  ?  278 ILE   A O   1 
ATOM   2209  C CB  . ILE   A 1 278 ? -23.466 -19.483 38.603  1.00 23.84  ?  278 ILE   A CB  1 
ATOM   2210  C CG1 . ILE   A 1 278 ? -24.047 -18.095 38.335  1.00 23.78  ?  278 ILE   A CG1 1 
ATOM   2211  C CG2 . ILE   A 1 278 ? -24.292 -20.530 37.872  1.00 22.79  ?  278 ILE   A CG2 1 
ATOM   2212  C CD1 . ILE   A 1 278 ? -23.506 -17.432 37.108  1.00 27.43  ?  278 ILE   A CD1 1 
ATOM   2213  N N   . ARG   A 1 279 ? -24.245 -21.930 40.817  1.00 23.85  ?  279 ARG   A N   1 
ATOM   2214  C CA  . ARG   A 1 279 ? -24.074 -23.292 41.307  1.00 23.50  ?  279 ARG   A CA  1 
ATOM   2215  C C   . ARG   A 1 279 ? -23.482 -24.192 40.229  1.00 28.28  ?  279 ARG   A C   1 
ATOM   2216  O O   . ARG   A 1 279 ? -22.370 -24.709 40.376  1.00 31.42  ?  279 ARG   A O   1 
ATOM   2217  C CB  . ARG   A 1 279 ? -25.417 -23.829 41.796  1.00 29.06  ?  279 ARG   A CB  1 
ATOM   2218  C CG  . ARG   A 1 279 ? -25.348 -25.020 42.718  1.00 28.20  ?  279 ARG   A CG  1 
ATOM   2219  C CD  . ARG   A 1 279 ? -26.764 -25.391 43.140  1.00 32.84  ?  279 ARG   A CD  1 
ATOM   2220  N NE  . ARG   A 1 279 ? -26.800 -26.467 44.119  1.00 39.65  ?  279 ARG   A NE  1 
ATOM   2221  C CZ  . ARG   A 1 279 ? -27.915 -27.027 44.570  1.00 47.71  ?  279 ARG   A CZ  1 
ATOM   2222  N NH1 . ARG   A 1 279 ? -29.108 -26.638 44.141  1.00 38.12  ?  279 ARG   A NH1 1 
ATOM   2223  N NH2 . ARG   A 1 279 ? -27.833 -28.005 45.473  1.00 39.57  ?  279 ARG   A NH2 1 
ATOM   2224  N N   . ASP   A 1 280 ? -24.205 -24.379 39.125  1.00 28.82  ?  280 ASP   A N   1 
ATOM   2225  C CA  . ASP   A 1 280 ? -23.720 -25.277 38.084  1.00 31.89  ?  280 ASP   A CA  1 
ATOM   2226  C C   . ASP   A 1 280 ? -24.213 -24.952 36.681  1.00 32.19  ?  280 ASP   A C   1 
ATOM   2227  O O   . ASP   A 1 280 ? -23.914 -25.722 35.764  1.00 34.28  ?  280 ASP   A O   1 
ATOM   2228  C CB  . ASP   A 1 280 ? -24.098 -26.725 38.440  1.00 35.17  ?  280 ASP   A CB  1 
ATOM   2229  C CG  . ASP   A 1 280 ? -25.570 -26.881 38.756  1.00 37.74  ?  280 ASP   A CG  1 
ATOM   2230  O OD1 . ASP   A 1 280 ? -26.366 -26.001 38.361  1.00 40.97  ?  280 ASP   A OD1 1 
ATOM   2231  O OD2 . ASP   A 1 280 ? -25.932 -27.878 39.416  1.00 41.57  ?  280 ASP   A OD2 1 
ATOM   2232  N N   . ASN   A 1 281 ? -24.953 -23.864 36.469  1.00 33.48  ?  281 ASN   A N   1 
ATOM   2233  C CA  . ASN   A 1 281 ? -25.463 -23.522 35.139  1.00 32.17  ?  281 ASN   A CA  1 
ATOM   2234  C C   . ASN   A 1 281 ? -24.360 -22.792 34.384  1.00 29.77  ?  281 ASN   A C   1 
ATOM   2235  O O   . ASN   A 1 281 ? -24.152 -21.594 34.574  1.00 34.41  ?  281 ASN   A O   1 
ATOM   2236  C CB  . ASN   A 1 281 ? -26.725 -22.672 35.251  1.00 30.64  ?  281 ASN   A CB  1 
ATOM   2237  C CG  . ASN   A 1 281 ? -27.476 -22.535 33.929  1.00 33.14  ?  281 ASN   A CG  1 
ATOM   2238  O OD1 . ASN   A 1 281 ? -26.881 -22.367 32.866  1.00 33.99  ?  281 ASN   A OD1 1 
ATOM   2239  N ND2 . ASN   A 1 281 ? -28.800 -22.596 33.999  1.00 35.94  ?  281 ASN   A ND2 1 
ATOM   2240  N N   . GLU   A 1 282 ? -23.648 -23.514 33.515  1.00 32.97  ?  282 GLU   A N   1 
ATOM   2241  C CA  . GLU   A 1 282 ? -22.517 -22.911 32.818  1.00 31.38  ?  282 GLU   A CA  1 
ATOM   2242  C C   . GLU   A 1 282 ? -22.966 -21.910 31.759  1.00 33.37  ?  282 GLU   A C   1 
ATOM   2243  O O   . GLU   A 1 282 ? -22.229 -20.965 31.452  1.00 33.94  ?  282 GLU   A O   1 
ATOM   2244  C CB  . GLU   A 1 282 ? -21.650 -23.998 32.181  1.00 42.63  ?  282 GLU   A CB  1 
ATOM   2245  C CG  . GLU   A 1 282 ? -20.251 -23.533 31.791  1.00 46.10  ?  282 GLU   A CG  1 
ATOM   2246  C CD  . GLU   A 1 282 ? -19.448 -24.602 31.064  1.00 56.13  ?  282 GLU   A CD  1 
ATOM   2247  O OE1 . GLU   A 1 282 ? -20.012 -25.274 30.172  1.00 64.72  ?  282 GLU   A OE1 1 
ATOM   2248  O OE2 . GLU   A 1 282 ? -18.251 -24.770 31.390  1.00 53.20  ?  282 GLU   A OE2 1 
ATOM   2249  N N   . GLU   A 1 283 ? -24.161 -22.093 31.191  1.00 32.72  ?  283 GLU   A N   1 
ATOM   2250  C CA  . GLU   A 1 283 ? -24.624 -21.170 30.160  1.00 27.82  ?  283 GLU   A CA  1 
ATOM   2251  C C   . GLU   A 1 283 ? -24.909 -19.793 30.743  1.00 28.44  ?  283 GLU   A C   1 
ATOM   2252  O O   . GLU   A 1 283 ? -24.529 -18.772 30.156  1.00 27.85  ?  283 GLU   A O   1 
ATOM   2253  C CB  . GLU   A 1 283 ? -25.867 -21.722 29.460  1.00 33.03  ?  283 GLU   A CB  1 
ATOM   2254  C CG  . GLU   A 1 283 ? -26.319 -20.843 28.295  1.00 35.86  ?  283 GLU   A CG  1 
ATOM   2255  C CD  . GLU   A 1 283 ? -27.542 -21.367 27.575  1.00 44.88  ?  283 GLU   A CD  1 
ATOM   2256  O OE1 . GLU   A 1 283 ? -28.097 -22.400 28.005  1.00 46.37  ?  283 GLU   A OE1 1 
ATOM   2257  O OE2 . GLU   A 1 283 ? -27.949 -20.737 26.574  1.00 49.11  ?  283 GLU   A OE2 1 
ATOM   2258  N N   . ILE   A 1 284 ? -25.579 -19.739 31.894  1.00 27.34  ?  284 ILE   A N   1 
ATOM   2259  C CA  . ILE   A 1 284 ? -25.826 -18.445 32.511  1.00 27.39  ?  284 ILE   A CA  1 
ATOM   2260  C C   . ILE   A 1 284 ? -24.515 -17.842 33.011  1.00 30.04  ?  284 ILE   A C   1 
ATOM   2261  O O   . ILE   A 1 284 ? -24.313 -16.621 32.942  1.00 26.86  ?  284 ILE   A O   1 
ATOM   2262  C CB  . ILE   A 1 284 ? -26.890 -18.601 33.615  1.00 31.12  ?  284 ILE   A CB  1 
ATOM   2263  C CG1 . ILE   A 1 284 ? -28.281 -18.714 32.978  1.00 30.90  ?  284 ILE   A CG1 1 
ATOM   2264  C CG2 . ILE   A 1 284 ? -26.847 -17.446 34.600  1.00 28.13  ?  284 ILE   A CG2 1 
ATOM   2265  C CD1 . ILE   A 1 284 ? -29.392 -19.001 33.970  1.00 31.63  ?  284 ILE   A CD1 1 
ATOM   2266  N N   . PHE   A 1 285 ? -23.585 -18.684 33.468  1.00 27.48  ?  285 PHE   A N   1 
ATOM   2267  C CA  . PHE   A 1 285 ? -22.256 -18.204 33.841  1.00 26.90  ?  285 PHE   A CA  1 
ATOM   2268  C C   . PHE   A 1 285 ? -21.537 -17.558 32.660  1.00 25.66  ?  285 PHE   A C   1 
ATOM   2269  O O   . PHE   A 1 285 ? -20.935 -16.487 32.801  1.00 23.46  ?  285 PHE   A O   1 
ATOM   2270  C CB  . PHE   A 1 285 ? -21.436 -19.359 34.400  1.00 27.21  ?  285 PHE   A CB  1 
ATOM   2271  C CG  . PHE   A 1 285 ? -19.985 -19.037 34.603  1.00 29.69  ?  285 PHE   A CG  1 
ATOM   2272  C CD1 . PHE   A 1 285 ? -19.595 -18.075 35.521  1.00 25.21  ?  285 PHE   A CD1 1 
ATOM   2273  C CD2 . PHE   A 1 285 ? -19.008 -19.720 33.895  1.00 27.15  ?  285 PHE   A CD2 1 
ATOM   2274  C CE1 . PHE   A 1 285 ? -18.251 -17.789 35.723  1.00 21.82  ?  285 PHE   A CE1 1 
ATOM   2275  C CE2 . PHE   A 1 285 ? -17.669 -19.445 34.091  1.00 26.93  ?  285 PHE   A CE2 1 
ATOM   2276  C CZ  . PHE   A 1 285 ? -17.290 -18.479 35.010  1.00 25.34  ?  285 PHE   A CZ  1 
ATOM   2277  N N   . THR   A 1 286 ? -21.579 -18.197 31.488  1.00 23.78  ?  286 THR   A N   1 
ATOM   2278  C CA  . THR   A 1 286 ? -20.946 -17.612 30.309  1.00 29.95  ?  286 THR   A CA  1 
ATOM   2279  C C   . THR   A 1 286 ? -21.625 -16.306 29.906  1.00 25.95  ?  286 THR   A C   1 
ATOM   2280  O O   . THR   A 1 286 ? -20.951 -15.334 29.542  1.00 23.21  ?  286 THR   A O   1 
ATOM   2281  C CB  . THR   A 1 286 ? -20.968 -18.609 29.149  1.00 27.51  ?  286 THR   A CB  1 
ATOM   2282  O OG1 . THR   A 1 286 ? -20.311 -19.816 29.550  1.00 27.52  ?  286 THR   A OG1 1 
ATOM   2283  C CG2 . THR   A 1 286 ? -20.252 -18.044 27.936  1.00 24.06  ?  286 THR   A CG2 1 
ATOM   2284  N N   . LEU   A 1 287 ? -22.959 -16.266 29.943  1.00 23.75  ?  287 LEU   A N   1 
ATOM   2285  C CA  . LEU   A 1 287 ? -23.653 -15.032 29.591  1.00 24.23  ?  287 LEU   A CA  1 
ATOM   2286  C C   . LEU   A 1 287 ? -23.342 -13.927 30.593  1.00 24.24  ?  287 LEU   A C   1 
ATOM   2287  O O   . LEU   A 1 287 ? -23.121 -12.773 30.205  1.00 26.11  ?  287 LEU   A O   1 
ATOM   2288  C CB  . LEU   A 1 287 ? -25.158 -15.278 29.499  1.00 28.05  ?  287 LEU   A CB  1 
ATOM   2289  C CG  . LEU   A 1 287 ? -25.639 -16.181 28.359  1.00 26.15  ?  287 LEU   A CG  1 
ATOM   2290  C CD1 . LEU   A 1 287 ? -27.119 -16.538 28.533  1.00 26.98  ?  287 LEU   A CD1 1 
ATOM   2291  C CD2 . LEU   A 1 287 ? -25.400 -15.521 27.002  1.00 23.64  ?  287 LEU   A CD2 1 
ATOM   2292  N N   . ALA   A 1 288 ? -23.289 -14.263 31.881  1.00 20.83  ?  288 ALA   A N   1 
ATOM   2293  C CA  . ALA   A 1 288 ? -22.980 -13.251 32.883  1.00 23.70  ?  288 ALA   A CA  1 
ATOM   2294  C C   . ALA   A 1 288 ? -21.565 -12.707 32.702  1.00 22.93  ?  288 ALA   A C   1 
ATOM   2295  O O   . ALA   A 1 288 ? -21.331 -11.503 32.867  1.00 24.78  ?  288 ALA   A O   1 
ATOM   2296  C CB  . ALA   A 1 288 ? -23.170 -13.829 34.285  1.00 23.24  ?  288 ALA   A CB  1 
ATOM   2297  N N   . ARG   A 1 289 ? -20.606 -13.575 32.359  1.00 22.63  ?  289 ARG   A N   1 
ATOM   2298  C CA  . ARG   A 1 289 ? -19.248 -13.101 32.088  1.00 23.77  ?  289 ARG   A CA  1 
ATOM   2299  C C   . ARG   A 1 289 ? -19.225 -12.133 30.915  1.00 24.36  ?  289 ARG   A C   1 
ATOM   2300  O O   . ARG   A 1 289 ? -18.512 -11.123 30.948  1.00 25.02  ?  289 ARG   A O   1 
ATOM   2301  C CB  . ARG   A 1 289 ? -18.318 -14.276 31.800  1.00 22.38  ?  289 ARG   A CB  1 
ATOM   2302  C CG  . ARG   A 1 289 ? -17.761 -14.969 33.020  1.00 23.10  ?  289 ARG   A CG  1 
ATOM   2303  C CD  . ARG   A 1 289 ? -16.708 -15.984 32.580  1.00 25.89  ?  289 ARG   A CD  1 
ATOM   2304  N NE  . ARG   A 1 289 ? -15.733 -16.266 33.629  1.00 24.55  ?  289 ARG   A NE  1 
ATOM   2305  C CZ  . ARG   A 1 289 ? -14.640 -16.991 33.442  1.00 23.28  ?  289 ARG   A CZ  1 
ATOM   2306  N NH1 . ARG   A 1 289 ? -14.355 -17.512 32.261  1.00 24.94  ?  289 ARG   A NH1 1 
ATOM   2307  N NH2 . ARG   A 1 289 ? -13.814 -17.196 34.464  1.00 23.66  ?  289 ARG   A NH2 1 
ATOM   2308  N N   . GLN   A 1 290 ? -19.988 -12.433 29.859  1.00 23.88  ?  290 GLN   A N   1 
ATOM   2309  C CA  . GLN   A 1 290 ? -20.032 -11.549 28.700  1.00 22.58  ?  290 GLN   A CA  1 
ATOM   2310  C C   . GLN   A 1 290 ? -20.557 -10.168 29.066  1.00 22.93  ?  290 GLN   A C   1 
ATOM   2311  O O   . GLN   A 1 290 ? -20.132 -9.169  28.482  1.00 20.26  ?  290 GLN   A O   1 
ATOM   2312  C CB  . GLN   A 1 290 ? -20.890 -12.179 27.597  1.00 27.28  ?  290 GLN   A CB  1 
ATOM   2313  C CG  . GLN   A 1 290 ? -20.311 -13.483 27.062  1.00 27.44  ?  290 GLN   A CG  1 
ATOM   2314  C CD  . GLN   A 1 290 ? -21.202 -14.168 26.046  1.00 30.30  ?  290 GLN   A CD  1 
ATOM   2315  O OE1 . GLN   A 1 290 ? -22.383 -13.839 25.901  1.00 32.81  ?  290 GLN   A OE1 1 
ATOM   2316  N NE2 . GLN   A 1 290 ? -20.637 -15.133 25.334  1.00 30.37  ?  290 GLN   A NE2 1 
ATOM   2317  N N   . ARG   A 1 291 ? -21.476 -10.084 30.026  1.00 23.23  ?  291 ARG   A N   1 
ATOM   2318  C CA  . ARG   A 1 291 ? -21.935 -8.772  30.459  1.00 19.83  ?  291 ARG   A CA  1 
ATOM   2319  C C   . ARG   A 1 291 ? -20.963 -8.133  31.437  1.00 21.63  ?  291 ARG   A C   1 
ATOM   2320  O O   . ARG   A 1 291 ? -20.822 -6.903  31.458  1.00 25.82  ?  291 ARG   A O   1 
ATOM   2321  C CB  . ARG   A 1 291 ? -23.327 -8.871  31.085  1.00 26.36  ?  291 ARG   A CB  1 
ATOM   2322  C CG  . ARG   A 1 291 ? -23.868 -7.520  31.508  1.00 27.47  ?  291 ARG   A CG  1 
ATOM   2323  C CD  . ARG   A 1 291 ? -25.342 -7.545  31.761  1.00 25.44  ?  291 ARG   A CD  1 
ATOM   2324  N NE  . ARG   A 1 291 ? -25.788 -6.243  32.224  1.00 22.46  ?  291 ARG   A NE  1 
ATOM   2325  C CZ  . ARG   A 1 291 ? -26.165 -5.260  31.422  1.00 28.46  ?  291 ARG   A CZ  1 
ATOM   2326  N NH1 . ARG   A 1 291 ? -26.166 -5.406  30.105  1.00 26.65  ?  291 ARG   A NH1 1 
ATOM   2327  N NH2 . ARG   A 1 291 ? -26.558 -4.105  31.952  1.00 22.18  ?  291 ARG   A NH2 1 
ATOM   2328  N N   . CYS   A 1 292 ? -20.278 -8.948  32.238  1.00 23.00  ?  292 CYS   A N   1 
ATOM   2329  C CA  . CYS   A 1 292 ? -19.310 -8.420  33.194  1.00 22.09  ?  292 CYS   A CA  1 
ATOM   2330  C C   . CYS   A 1 292 ? -18.242 -7.574  32.508  1.00 21.96  ?  292 CYS   A C   1 
ATOM   2331  O O   . CYS   A 1 292 ? -17.832 -6.532  33.034  1.00 24.53  ?  292 CYS   A O   1 
ATOM   2332  C CB  . CYS   A 1 292 ? -18.661 -9.573  33.960  1.00 22.31  ?  292 CYS   A CB  1 
ATOM   2333  S SG  . CYS   A 1 292 ? -17.384 -9.063  35.139  1.00 23.99  ?  292 CYS   A SG  1 
ATOM   2334  N N   . VAL   A 1 293 ? -17.788 -8.001  31.327  1.00 25.21  ?  293 VAL   A N   1 
ATOM   2335  C CA  . VAL   A 1 293 ? -16.627 -7.364  30.698  1.00 24.98  ?  293 VAL   A CA  1 
ATOM   2336  C C   . VAL   A 1 293 ? -16.857 -5.887  30.384  1.00 22.88  ?  293 VAL   A C   1 
ATOM   2337  O O   . VAL   A 1 293 ? -15.999 -5.063  30.744  1.00 22.25  ?  293 VAL   A O   1 
ATOM   2338  C CB  . VAL   A 1 293 ? -16.189 -8.173  29.466  1.00 26.34  ?  293 VAL   A CB  1 
ATOM   2339  C CG1 . VAL   A 1 293 ? -15.186 -7.384  28.641  1.00 29.11  ?  293 VAL   A CG1 1 
ATOM   2340  C CG2 . VAL   A 1 293 ? -15.608 -9.513  29.910  1.00 23.34  ?  293 VAL   A CG2 1 
ATOM   2341  N N   . PRO   A 1 294 ? -17.949 -5.482  29.718  1.00 24.49  ?  294 PRO   A N   1 
ATOM   2342  C CA  . PRO   A 1 294 ? -18.135 -4.049  29.443  1.00 19.89  ?  294 PRO   A CA  1 
ATOM   2343  C C   . PRO   A 1 294 ? -18.588 -3.232  30.646  1.00 23.16  ?  294 PRO   A C   1 
ATOM   2344  O O   . PRO   A 1 294 ? -18.319 -2.028  30.703  1.00 24.32  ?  294 PRO   A O   1 
ATOM   2345  C CB  . PRO   A 1 294 ? -19.210 -4.048  28.351  1.00 27.55  ?  294 PRO   A CB  1 
ATOM   2346  C CG  . PRO   A 1 294 ? -19.967 -5.294  28.582  1.00 23.18  ?  294 PRO   A CG  1 
ATOM   2347  C CD  . PRO   A 1 294 ? -18.940 -6.295  28.987  1.00 22.05  ?  294 PRO   A CD  1 
ATOM   2348  N N   . MET   A 1 295 ? -19.276 -3.865  31.602  1.00 23.99  ?  295 MET   A N   1 
ATOM   2349  C CA  . MET   A 1 295 ? -19.890 -3.172  32.734  1.00 23.69  ?  295 MET   A CA  1 
ATOM   2350  C C   . MET   A 1 295 ? -18.968 -3.026  33.939  1.00 21.71  ?  295 MET   A C   1 
ATOM   2351  O O   . MET   A 1 295 ? -18.956 -1.969  34.577  1.00 22.27  ?  295 MET   A O   1 
ATOM   2352  C CB  . MET   A 1 295 ? -21.162 -3.903  33.173  1.00 20.20  ?  295 MET   A CB  1 
ATOM   2353  C CG  . MET   A 1 295 ? -22.300 -3.839  32.159  1.00 24.88  ?  295 MET   A CG  1 
ATOM   2354  S SD  . MET   A 1 295 ? -22.772 -2.137  31.779  1.00 31.85  ?  295 MET   A SD  1 
ATOM   2355  C CE  . MET   A 1 295 ? -23.572 -2.365  30.203  1.00 28.59  ?  295 MET   A CE  1 
ATOM   2356  N N   . GLU   A 1 296 ? -18.222 -4.073  34.291  1.00 23.02  ?  296 GLU   A N   1 
ATOM   2357  C CA  . GLU   A 1 296 ? -17.441 -4.098  35.524  1.00 21.50  ?  296 GLU   A CA  1 
ATOM   2358  C C   . GLU   A 1 296 ? -15.949 -4.215  35.265  1.00 18.74  ?  296 GLU   A C   1 
ATOM   2359  O O   . GLU   A 1 296 ? -15.162 -3.465  35.853  1.00 23.89  ?  296 GLU   A O   1 
ATOM   2360  C CB  . GLU   A 1 296 ? -17.903 -5.260  36.430  1.00 18.03  ?  296 GLU   A CB  1 
ATOM   2361  C CG  . GLU   A 1 296 ? -19.370 -5.204  36.850  1.00 22.60  ?  296 GLU   A CG  1 
ATOM   2362  C CD  . GLU   A 1 296 ? -19.656 -4.086  37.847  1.00 26.62  ?  296 GLU   A CD  1 
ATOM   2363  O OE1 . GLU   A 1 296 ? -18.890 -3.954  38.822  1.00 28.15  ?  296 GLU   A OE1 1 
ATOM   2364  O OE2 . GLU   A 1 296 ? -20.631 -3.325  37.644  1.00 31.49  ?  296 GLU   A OE2 1 
ATOM   2365  N N   . GLY   A 1 297 ? -15.538 -5.135  34.405  1.00 19.67  ?  297 GLY   A N   1 
ATOM   2366  C CA  . GLY   A 1 297 ? -14.131 -5.353  34.144  1.00 18.89  ?  297 GLY   A CA  1 
ATOM   2367  C C   . GLY   A 1 297 ? -13.923 -6.759  33.618  1.00 18.91  ?  297 GLY   A C   1 
ATOM   2368  O O   . GLY   A 1 297 ? -14.879 -7.474  33.321  1.00 22.53  ?  297 GLY   A O   1 
ATOM   2369  N N   . PHE   A 1 298 ? -12.649 -7.142  33.516  1.00 17.13  ?  298 PHE   A N   1 
ATOM   2370  C CA  . PHE   A 1 298 ? -12.339 -8.492  33.065  1.00 19.20  ?  298 PHE   A CA  1 
ATOM   2371  C C   . PHE   A 1 298 ? -12.736 -9.505  34.131  1.00 21.45  ?  298 PHE   A C   1 
ATOM   2372  O O   . PHE   A 1 298 ? -12.718 -9.223  35.335  1.00 20.77  ?  298 PHE   A O   1 
ATOM   2373  C CB  . PHE   A 1 298 ? -10.860 -8.646  32.724  1.00 23.00  ?  298 PHE   A CB  1 
ATOM   2374  C CG  . PHE   A 1 298 ? -10.502 -10.016 32.222  1.00 21.92  ?  298 PHE   A CG  1 
ATOM   2375  C CD1 . PHE   A 1 298 ? -10.956 -10.454 30.989  1.00 22.20  ?  298 PHE   A CD1 1 
ATOM   2376  C CD2 . PHE   A 1 298 ? -9.727  -10.872 32.988  1.00 19.66  ?  298 PHE   A CD2 1 
ATOM   2377  C CE1 . PHE   A 1 298 ? -10.638 -11.719 30.521  1.00 25.55  ?  298 PHE   A CE1 1 
ATOM   2378  C CE2 . PHE   A 1 298 ? -9.402  -12.142 32.525  1.00 20.22  ?  298 PHE   A CE2 1 
ATOM   2379  C CZ  . PHE   A 1 298 ? -9.857  -12.564 31.289  1.00 19.68  ?  298 PHE   A CZ  1 
ATOM   2380  N N   . VAL   A 1 299 ? -13.091 -10.707 33.674  1.00 21.40  ?  299 VAL   A N   1 
ATOM   2381  C CA  . VAL   A 1 299 ? -13.819 -11.635 34.534  1.00 18.99  ?  299 VAL   A CA  1 
ATOM   2382  C C   . VAL   A 1 299 ? -13.022 -12.142 35.722  1.00 19.52  ?  299 VAL   A C   1 
ATOM   2383  O O   . VAL   A 1 299 ? -13.620 -12.762 36.612  1.00 22.76  ?  299 VAL   A O   1 
ATOM   2384  C CB  . VAL   A 1 299 ? -14.328 -12.827 33.704  1.00 21.33  ?  299 VAL   A CB  1 
ATOM   2385  C CG1 . VAL   A 1 299 ? -15.241 -12.320 32.602  1.00 20.19  ?  299 VAL   A CG1 1 
ATOM   2386  C CG2 . VAL   A 1 299 ? -13.146 -13.601 33.118  1.00 19.13  ?  299 VAL   A CG2 1 
ATOM   2387  N N   . THR   A 1 300 ? -11.706 -11.909 35.788  1.00 18.53  ?  300 THR   A N   1 
ATOM   2388  C CA  . THR   A 1 300 ? -10.938 -12.362 36.946  1.00 20.17  ?  300 THR   A CA  1 
ATOM   2389  C C   . THR   A 1 300 ? -10.639 -11.236 37.937  1.00 19.59  ?  300 THR   A C   1 
ATOM   2390  O O   . THR   A 1 300 ? -9.886  -11.452 38.890  1.00 19.31  ?  300 THR   A O   1 
ATOM   2391  C CB  . THR   A 1 300 ? -9.634  -13.074 36.528  1.00 18.34  ?  300 THR   A CB  1 
ATOM   2392  O OG1 . THR   A 1 300 ? -8.763  -12.184 35.821  1.00 17.70  ?  300 THR   A OG1 1 
ATOM   2393  C CG2 . THR   A 1 300 ? -9.928  -14.296 35.644  1.00 15.44  ?  300 THR   A CG2 1 
ATOM   2394  N N   . TYR   A 1 301 ? -11.232 -10.049 37.757  1.00 18.77  ?  301 TYR   A N   1 
ATOM   2395  C CA  . TYR   A 1 301 ? -11.240 -9.057  38.833  1.00 16.96  ?  301 TYR   A CA  1 
ATOM   2396  C C   . TYR   A 1 301 ? -12.553 -8.296  38.967  1.00 19.35  ?  301 TYR   A C   1 
ATOM   2397  O O   . TYR   A 1 301 ? -12.848 -7.824  40.071  1.00 17.18  ?  301 TYR   A O   1 
ATOM   2398  C CB  . TYR   A 1 301 ? -10.084 -8.047  38.677  1.00 18.35  ?  301 TYR   A CB  1 
ATOM   2399  C CG  . TYR   A 1 301 ? -10.214 -7.103  37.506  1.00 14.50  ?  301 TYR   A CG  1 
ATOM   2400  C CD1 . TYR   A 1 301 ? -10.938 -5.919  37.611  1.00 18.24  ?  301 TYR   A CD1 1 
ATOM   2401  C CD2 . TYR   A 1 301 ? -9.598  -7.386  36.303  1.00 16.67  ?  301 TYR   A CD2 1 
ATOM   2402  C CE1 . TYR   A 1 301 ? -11.065 -5.054  36.527  1.00 15.69  ?  301 TYR   A CE1 1 
ATOM   2403  C CE2 . TYR   A 1 301 ? -9.706  -6.528  35.222  1.00 17.05  ?  301 TYR   A CE2 1 
ATOM   2404  C CZ  . TYR   A 1 301 ? -10.438 -5.367  35.338  1.00 19.09  ?  301 TYR   A CZ  1 
ATOM   2405  O OH  . TYR   A 1 301 ? -10.544 -4.521  34.247  1.00 20.26  ?  301 TYR   A OH  1 
ATOM   2406  N N   . GLY   A 1 302 ? -13.334 -8.141  37.902  1.00 17.58  ?  302 GLY   A N   1 
ATOM   2407  C CA  . GLY   A 1 302 ? -14.678 -7.597  37.993  1.00 17.91  ?  302 GLY   A CA  1 
ATOM   2408  C C   . GLY   A 1 302 ? -14.791 -6.228  38.629  1.00 16.58  ?  302 GLY   A C   1 
ATOM   2409  O O   . GLY   A 1 302 ? -15.714 -5.985  39.416  1.00 19.32  ?  302 GLY   A O   1 
ATOM   2410  N N   . GLY   A 1 303 ? -13.896 -5.314  38.283  1.00 16.10  ?  303 GLY   A N   1 
ATOM   2411  C CA  . GLY   A 1 303 ? -13.968 -3.981  38.838  1.00 17.66  ?  303 GLY   A CA  1 
ATOM   2412  C C   . GLY   A 1 303 ? -13.417 -3.849  40.236  1.00 17.32  ?  303 GLY   A C   1 
ATOM   2413  O O   . GLY   A 1 303 ? -13.692 -2.841  40.897  1.00 17.34  ?  303 GLY   A O   1 
ATOM   2414  N N   . LEU   A 1 304 ? -12.666 -4.843  40.712  1.00 16.54  ?  304 LEU   A N   1 
ATOM   2415  C CA  . LEU   A 1 304 ? -12.010 -4.815  42.015  1.00 17.16  ?  304 LEU   A CA  1 
ATOM   2416  C C   . LEU   A 1 304 ? -10.505 -4.897  41.838  1.00 15.81  ?  304 LEU   A C   1 
ATOM   2417  O O   . LEU   A 1 304 ? -10.020 -5.610  40.961  1.00 15.84  ?  304 LEU   A O   1 
ATOM   2418  C CB  . LEU   A 1 304 ? -12.450 -5.986  42.888  1.00 15.89  ?  304 LEU   A CB  1 
ATOM   2419  C CG  . LEU   A 1 304 ? -13.860 -5.906  43.447  1.00 15.73  ?  304 LEU   A CG  1 
ATOM   2420  C CD1 . LEU   A 1 304 ? -14.168 -7.198  44.166  1.00 16.58  ?  304 LEU   A CD1 1 
ATOM   2421  C CD2 . LEU   A 1 304 ? -13.939 -4.720  44.388  1.00 17.56  ?  304 LEU   A CD2 1 
ATOM   2422  N N   . ALA   A 1 305 ? -9.768  -4.184  42.689  1.00 17.76  ?  305 ALA   A N   1 
ATOM   2423  C CA  . ALA   A 1 305 ? -8.334  -4.397  42.767  1.00 16.07  ?  305 ALA   A CA  1 
ATOM   2424  C C   . ALA   A 1 305 ? -8.054  -5.790  43.319  1.00 15.45  ?  305 ALA   A C   1 
ATOM   2425  O O   . ALA   A 1 305 ? -8.886  -6.392  44.011  1.00 14.04  ?  305 ALA   A O   1 
ATOM   2426  C CB  . ALA   A 1 305 ? -7.677  -3.340  43.656  1.00 16.27  ?  305 ALA   A CB  1 
ATOM   2427  N N   . GLY   A 1 306 ? -6.865  -6.306  43.001  1.00 17.68  ?  306 GLY   A N   1 
ATOM   2428  C CA  . GLY   A 1 306 ? -6.493  -7.617  43.503  1.00 17.00  ?  306 GLY   A CA  1 
ATOM   2429  C C   . GLY   A 1 306 ? -6.513  -7.680  45.016  1.00 15.97  ?  306 GLY   A C   1 
ATOM   2430  O O   . GLY   A 1 306 ? -6.923  -8.689  45.598  1.00 18.91  ?  306 GLY   A O   1 
ATOM   2431  N N   . ARG   A 1 307 ? -6.097  -6.593  45.674  1.00 14.83  ?  307 ARG   A N   1 
ATOM   2432  C CA  . ARG   A 1 307 ? -6.097  -6.553  47.135  1.00 13.14  ?  307 ARG   A CA  1 
ATOM   2433  C C   . ARG   A 1 307 ? -7.503  -6.664  47.714  1.00 15.25  ?  307 ARG   A C   1 
ATOM   2434  O O   . ARG   A 1 307 ? -7.682  -7.189  48.822  1.00 13.00  ?  307 ARG   A O   1 
ATOM   2435  C CB  . ARG   A 1 307 ? -5.431  -5.269  47.625  1.00 13.19  ?  307 ARG   A CB  1 
ATOM   2436  C CG  . ARG   A 1 307 ? -5.961  -4.009  46.984  1.00 14.77  ?  307 ARG   A CG  1 
ATOM   2437  C CD  . ARG   A 1 307 ? -5.458  -2.763  47.702  1.00 14.51  ?  307 ARG   A CD  1 
ATOM   2438  N NE  . ARG   A 1 307 ? -6.008  -1.563  47.083  1.00 17.25  ?  307 ARG   A NE  1 
ATOM   2439  C CZ  . ARG   A 1 307 ? -5.383  -0.841  46.163  1.00 18.15  ?  307 ARG   A CZ  1 
ATOM   2440  N NH1 . ARG   A 1 307 ? -4.148  -1.131  45.780  1.00 14.43  ?  307 ARG   A NH1 1 
ATOM   2441  N NH2 . ARG   A 1 307 ? -6.014  0.197   45.611  1.00 15.85  ?  307 ARG   A NH2 1 
ATOM   2442  N N   . ASP   A 1 308 ? -8.513  -6.187  46.988  1.00 16.67  ?  308 ASP   A N   1 
ATOM   2443  C CA  . ASP   A 1 308 ? -9.869  -6.289  47.503  1.00 14.60  ?  308 ASP   A CA  1 
ATOM   2444  C C   . ASP   A 1 308 ? -10.428 -7.693  47.356  1.00 13.96  ?  308 ASP   A C   1 
ATOM   2445  O O   . ASP   A 1 308 ? -11.146 -8.158  48.244  1.00 15.07  ?  308 ASP   A O   1 
ATOM   2446  C CB  . ASP   A 1 308 ? -10.745 -5.239  46.833  1.00 15.37  ?  308 ASP   A CB  1 
ATOM   2447  C CG  . ASP   A 1 308 ? -10.482 -3.851  47.396  1.00 20.24  ?  308 ASP   A CG  1 
ATOM   2448  O OD1 . ASP   A 1 308 ? -10.573 -3.706  48.646  1.00 20.33  ?  308 ASP   A OD1 1 
ATOM   2449  O OD2 . ASP   A 1 308 ? -10.156 -2.925  46.619  1.00 18.10  ?  308 ASP   A OD2 1 
ATOM   2450  N N   . MET   A 1 309 ? -10.074 -8.406  46.290  1.00 16.01  ?  309 MET   A N   1 
ATOM   2451  C CA  . MET   A 1 309 ? -10.383 -9.833  46.261  1.00 15.25  ?  309 MET   A CA  1 
ATOM   2452  C C   . MET   A 1 309 ? -9.654  -10.560 47.379  1.00 13.91  ?  309 MET   A C   1 
ATOM   2453  O O   . MET   A 1 309 ? -10.198 -11.488 47.988  1.00 11.26  ?  309 MET   A O   1 
ATOM   2454  C CB  . MET   A 1 309 ? -10.021 -10.435 44.903  1.00 13.48  ?  309 MET   A CB  1 
ATOM   2455  C CG  . MET   A 1 309 ? -11.044 -10.149 43.819  1.00 16.16  ?  309 MET   A CG  1 
ATOM   2456  S SD  . MET   A 1 309 ? -10.625 -10.914 42.249  1.00 20.15  ?  309 MET   A SD  1 
ATOM   2457  C CE  . MET   A 1 309 ? -9.056  -10.144 41.845  1.00 16.94  ?  309 MET   A CE  1 
ATOM   2458  N N   . ALA   A 1 310 ? -8.416  -10.145 47.661  1.00 14.33  ?  310 ALA   A N   1 
ATOM   2459  C CA  . ALA   A 1 310 ? -7.652  -10.739 48.751  1.00 12.28  ?  310 ALA   A CA  1 
ATOM   2460  C C   . ALA   A 1 310 ? -8.330  -10.491 50.090  1.00 15.37  ?  310 ALA   A C   1 
ATOM   2461  O O   . ALA   A 1 310 ? -8.441  -11.404 50.923  1.00 16.82  ?  310 ALA   A O   1 
ATOM   2462  C CB  . ALA   A 1 310 ? -6.230  -10.172 48.751  1.00 11.85  ?  310 ALA   A CB  1 
ATOM   2463  N N   . ALA   A 1 311 ? -8.798  -9.259  50.316  1.00 14.35  ?  311 ALA   A N   1 
ATOM   2464  C CA  . ALA   A 1 311 ? -9.538  -8.966  51.535  1.00 13.19  ?  311 ALA   A CA  1 
ATOM   2465  C C   . ALA   A 1 311 ? -10.825 -9.774  51.602  1.00 14.60  ?  311 ALA   A C   1 
ATOM   2466  O O   . ALA   A 1 311 ? -11.235 -10.198 52.691  1.00 13.37  ?  311 ALA   A O   1 
ATOM   2467  C CB  . ALA   A 1 311 ? -9.837  -7.468  51.620  1.00 11.80  ?  311 ALA   A CB  1 
ATOM   2468  N N   . MET   A 1 312 ? -11.453 -10.022 50.447  1.00 12.86  ?  312 MET   A N   1 
ATOM   2469  C CA  . MET   A 1 312 ? -12.740 -10.713 50.420  1.00 11.67  ?  312 MET   A CA  1 
ATOM   2470  C C   . MET   A 1 312 ? -12.598 -12.179 50.804  1.00 14.83  ?  312 MET   A C   1 
ATOM   2471  O O   . MET   A 1 312 ? -13.461 -12.723 51.502  1.00 16.10  ?  312 MET   A O   1 
ATOM   2472  C CB  . MET   A 1 312 ? -13.376 -10.589 49.035  1.00 14.29  ?  312 MET   A CB  1 
ATOM   2473  C CG  . MET   A 1 312 ? -14.807 -11.082 48.980  1.00 15.47  ?  312 MET   A CG  1 
ATOM   2474  S SD  . MET   A 1 312 ? -15.572 -10.976 47.347  1.00 17.72  ?  312 MET   A SD  1 
ATOM   2475  C CE  . MET   A 1 312 ? -15.156 -9.298  46.866  1.00 15.78  ?  312 MET   A CE  1 
ATOM   2476  N N   . VAL   A 1 313 ? -11.519 -12.835 50.358  1.00 14.28  ?  313 VAL   A N   1 
ATOM   2477  C CA  . VAL   A 1 313 ? -11.290 -14.230 50.735  1.00 13.45  ?  313 VAL   A CA  1 
ATOM   2478  C C   . VAL   A 1 313 ? -11.131 -14.359 52.242  1.00 14.52  ?  313 VAL   A C   1 
ATOM   2479  O O   . VAL   A 1 313 ? -11.686 -15.273 52.864  1.00 17.11  ?  313 VAL   A O   1 
ATOM   2480  C CB  . VAL   A 1 313 ? -10.064 -14.795 49.999  1.00 15.29  ?  313 VAL   A CB  1 
ATOM   2481  C CG1 . VAL   A 1 313 ? -9.626  -16.114 50.631  1.00 15.90  ?  313 VAL   A CG1 1 
ATOM   2482  C CG2 . VAL   A 1 313 ? -10.379 -14.984 48.538  1.00 16.29  ?  313 VAL   A CG2 1 
ATOM   2483  N N   . GLN   A 1 314 ? -10.365 -13.456 52.854  1.00 13.02  ?  314 GLN   A N   1 
ATOM   2484  C CA  . GLN   A 1 314 ? -10.220 -13.485 54.304  1.00 15.15  ?  314 GLN   A CA  1 
ATOM   2485  C C   . GLN   A 1 314 ? -11.518 -13.097 54.999  1.00 16.10  ?  314 GLN   A C   1 
ATOM   2486  O O   . GLN   A 1 314 ? -11.923 -13.744 55.971  1.00 15.30  ?  314 GLN   A O   1 
ATOM   2487  C CB  . GLN   A 1 314 ? -9.077  -12.567 54.734  1.00 15.26  ?  314 GLN   A CB  1 
ATOM   2488  C CG  . GLN   A 1 314 ? -8.838  -12.518 56.235  1.00 17.11  ?  314 GLN   A CG  1 
ATOM   2489  C CD  . GLN   A 1 314 ? -8.437  -13.861 56.841  1.00 18.81  ?  314 GLN   A CD  1 
ATOM   2490  O OE1 . GLN   A 1 314 ? -7.925  -14.752 56.158  1.00 17.04  ?  314 GLN   A OE1 1 
ATOM   2491  N NE2 . GLN   A 1 314 ? -8.667  -14.001 58.137  1.00 21.31  ?  314 GLN   A NE2 1 
ATOM   2492  N N   . GLY   A 1 315 ? -12.186 -12.049 54.511  1.00 14.07  ?  315 GLY   A N   1 
ATOM   2493  C CA  . GLY   A 1 315 ? -13.396 -11.587 55.162  1.00 13.04  ?  315 GLY   A CA  1 
ATOM   2494  C C   . GLY   A 1 315 ? -14.541 -12.575 55.080  1.00 15.71  ?  315 GLY   A C   1 
ATOM   2495  O O   . GLY   A 1 315 ? -15.390 -12.616 55.973  1.00 16.23  ?  315 GLY   A O   1 
ATOM   2496  N N   . LEU   A 1 316 ? -14.600 -13.370 54.004  1.00 16.38  ?  316 LEU   A N   1 
ATOM   2497  C CA  . LEU   A 1 316 ? -15.634 -14.398 53.919  1.00 17.53  ?  316 LEU   A CA  1 
ATOM   2498  C C   . LEU   A 1 316 ? -15.477 -15.415 55.037  1.00 19.18  ?  316 LEU   A C   1 
ATOM   2499  O O   . LEU   A 1 316 ? -16.474 -15.935 55.548  1.00 20.11  ?  316 LEU   A O   1 
ATOM   2500  C CB  . LEU   A 1 316 ? -15.598 -15.087 52.547  1.00 16.33  ?  316 LEU   A CB  1 
ATOM   2501  C CG  . LEU   A 1 316 ? -16.279 -14.340 51.389  1.00 16.30  ?  316 LEU   A CG  1 
ATOM   2502  C CD1 . LEU   A 1 316 ? -15.924 -14.928 50.041  1.00 12.68  ?  316 LEU   A CD1 1 
ATOM   2503  C CD2 . LEU   A 1 316 ? -17.794 -14.310 51.560  1.00 14.38  ?  316 LEU   A CD2 1 
ATOM   2504  N N   . GLU   A 1 317 ? -14.238 -15.676 55.457  1.00 16.65  ?  317 GLU   A N   1 
ATOM   2505  C CA  . GLU   A 1 317 ? -13.993 -16.598 56.561  1.00 17.75  ?  317 GLU   A CA  1 
ATOM   2506  C C   . GLU   A 1 317 ? -14.363 -15.971 57.900  1.00 20.07  ?  317 GLU   A C   1 
ATOM   2507  O O   . GLU   A 1 317 ? -15.133 -16.546 58.679  1.00 20.04  ?  317 GLU   A O   1 
ATOM   2508  C CB  . GLU   A 1 317 ? -12.525 -17.020 56.555  1.00 21.45  ?  317 GLU   A CB  1 
ATOM   2509  C CG  . GLU   A 1 317 ? -12.110 -17.832 57.765  1.00 26.77  ?  317 GLU   A CG  1 
ATOM   2510  C CD  . GLU   A 1 317 ? -12.768 -19.198 57.800  1.00 31.95  ?  317 GLU   A CD  1 
ATOM   2511  O OE1 . GLU   A 1 317 ? -13.231 -19.672 56.731  1.00 28.12  ?  317 GLU   A OE1 1 
ATOM   2512  O OE2 . GLU   A 1 317 ? -12.819 -19.796 58.901  1.00 35.35  ?  317 GLU   A OE2 1 
ATOM   2513  N N   . GLU   A 1 318 ? -13.819 -14.786 58.183  1.00 18.86  ?  318 GLU   A N   1 
ATOM   2514  C CA  . GLU   A 1 318 ? -14.074 -14.132 59.461  1.00 19.54  ?  318 GLU   A CA  1 
ATOM   2515  C C   . GLU   A 1 318 ? -15.556 -13.855 59.659  1.00 19.28  ?  318 GLU   A C   1 
ATOM   2516  O O   . GLU   A 1 318 ? -16.062 -13.929 60.785  1.00 18.81  ?  318 GLU   A O   1 
ATOM   2517  C CB  . GLU   A 1 318 ? -13.274 -12.836 59.538  1.00 18.04  ?  318 GLU   A CB  1 
ATOM   2518  C CG  . GLU   A 1 318 ? -11.794 -13.056 59.383  1.00 15.07  ?  318 GLU   A CG  1 
ATOM   2519  C CD  . GLU   A 1 318 ? -11.005 -11.786 59.575  1.00 17.66  ?  318 GLU   A CD  1 
ATOM   2520  O OE1 . GLU   A 1 318 ? -11.587 -10.803 60.075  1.00 18.26  ?  318 GLU   A OE1 1 
ATOM   2521  O OE2 . GLU   A 1 318 ? -9.810  -11.765 59.215  1.00 16.65  ?  318 GLU   A OE2 1 
ATOM   2522  N N   . GLY   A 1 319 ? -16.264 -13.534 58.573  1.00 18.27  ?  319 GLY   A N   1 
ATOM   2523  C CA  . GLY   A 1 319 ? -17.683 -13.236 58.642  1.00 16.54  ?  319 GLY   A CA  1 
ATOM   2524  C C   . GLY   A 1 319 ? -18.543 -14.403 59.076  1.00 16.66  ?  319 GLY   A C   1 
ATOM   2525  O O   . GLY   A 1 319 ? -19.664 -14.189 59.549  1.00 16.69  ?  319 GLY   A O   1 
ATOM   2526  N N   . THR   A 1 320 ? -18.049 -15.633 58.933  1.00 16.92  ?  320 THR   A N   1 
ATOM   2527  C CA  . THR   A 1 320 ? -18.795 -16.798 59.395  1.00 18.02  ?  320 THR   A CA  1 
ATOM   2528  C C   . THR   A 1 320 ? -18.540 -17.152 60.855  1.00 15.15  ?  320 THR   A C   1 
ATOM   2529  O O   . THR   A 1 320 ? -19.216 -18.040 61.372  1.00 19.26  ?  320 THR   A O   1 
ATOM   2530  C CB  . THR   A 1 320 ? -18.472 -18.041 58.545  1.00 21.33  ?  320 THR   A CB  1 
ATOM   2531  O OG1 . THR   A 1 320 ? -17.142 -18.500 58.841  1.00 21.46  ?  320 THR   A OG1 1 
ATOM   2532  C CG2 . THR   A 1 320 ? -18.600 -17.745 57.055  1.00 16.16  ?  320 THR   A CG2 1 
ATOM   2533  N N   . GLU   A 1 321 ? -17.602 -16.499 61.535  1.00 17.43  ?  321 GLU   A N   1 
ATOM   2534  C CA  . GLU   A 1 321 ? -17.215 -16.932 62.876  1.00 15.80  ?  321 GLU   A CA  1 
ATOM   2535  C C   . GLU   A 1 321 ? -18.337 -16.668 63.873  1.00 21.18  ?  321 GLU   A C   1 
ATOM   2536  O O   . GLU   A 1 321 ? -18.789 -15.528 64.036  1.00 20.63  ?  321 GLU   A O   1 
ATOM   2537  C CB  . GLU   A 1 321 ? -15.930 -16.235 63.310  1.00 17.59  ?  321 GLU   A CB  1 
ATOM   2538  C CG  . GLU   A 1 321 ? -14.732 -16.617 62.445  1.00 24.47  ?  321 GLU   A CG  1 
ATOM   2539  C CD  . GLU   A 1 321 ? -13.441 -15.922 62.854  1.00 29.14  ?  321 GLU   A CD  1 
ATOM   2540  O OE1 . GLU   A 1 321 ? -13.478 -15.056 63.756  1.00 31.45  ?  321 GLU   A OE1 1 
ATOM   2541  O OE2 . GLU   A 1 321 ? -12.385 -16.248 62.266  1.00 34.73  ?  321 GLU   A OE2 1 
ATOM   2542  N N   . GLU   A 1 322 ? -18.787 -17.731 64.542  1.00 18.79  ?  322 GLU   A N   1 
ATOM   2543  C CA  . GLU   A 1 322 ? -19.959 -17.619 65.404  1.00 20.12  ?  322 GLU   A CA  1 
ATOM   2544  C C   . GLU   A 1 322 ? -19.696 -16.710 66.598  1.00 18.07  ?  322 GLU   A C   1 
ATOM   2545  O O   . GLU   A 1 322 ? -20.569 -15.927 66.994  1.00 18.62  ?  322 GLU   A O   1 
ATOM   2546  C CB  . GLU   A 1 322 ? -20.389 -19.000 65.879  1.00 18.86  ?  322 GLU   A CB  1 
ATOM   2547  C CG  . GLU   A 1 322 ? -21.665 -18.977 66.663  1.00 23.69  ?  322 GLU   A CG  1 
ATOM   2548  C CD  . GLU   A 1 322 ? -22.072 -20.348 67.124  1.00 29.24  ?  322 GLU   A CD  1 
ATOM   2549  O OE1 . GLU   A 1 322 ? -21.654 -21.329 66.471  1.00 26.62  ?  322 GLU   A OE1 1 
ATOM   2550  O OE2 . GLU   A 1 322 ? -22.798 -20.438 68.141  1.00 32.70  ?  322 GLU   A OE2 1 
ATOM   2551  N N   . GLU   A 1 323 ? -18.504 -16.794 67.186  1.00 17.46  ?  323 GLU   A N   1 
ATOM   2552  C CA  . GLU   A 1 323 ? -18.170 -15.892 68.280  1.00 20.62  ?  323 GLU   A CA  1 
ATOM   2553  C C   . GLU   A 1 323 ? -18.206 -14.434 67.817  1.00 17.80  ?  323 GLU   A C   1 
ATOM   2554  O O   . GLU   A 1 323 ? -18.639 -13.547 68.559  1.00 18.09  ?  323 GLU   A O   1 
ATOM   2555  C CB  . GLU   A 1 323 ? -16.805 -16.281 68.856  1.00 25.59  ?  323 GLU   A CB  1 
ATOM   2556  C CG  . GLU   A 1 323 ? -16.450 -15.628 70.188  1.00 27.19  ?  323 GLU   A CG  1 
ATOM   2557  C CD  . GLU   A 1 323 ? -17.182 -16.212 71.397  1.00 47.29  ?  323 GLU   A CD  1 
ATOM   2558  O OE1 . GLU   A 1 323 ? -18.290 -16.792 71.251  1.00 47.73  ?  323 GLU   A OE1 1 
ATOM   2559  O OE2 . GLU   A 1 323 ? -16.634 -16.082 72.516  1.00 48.40  ?  323 GLU   A OE2 1 
ATOM   2560  N N   . TYR   A 1 324 ? -17.801 -14.171 66.575  1.00 18.02  ?  324 TYR   A N   1 
ATOM   2561  C CA  . TYR   A 1 324 ? -17.968 -12.831 66.023  1.00 18.32  ?  324 TYR   A CA  1 
ATOM   2562  C C   . TYR   A 1 324 ? -19.444 -12.491 65.824  1.00 18.27  ?  324 TYR   A C   1 
ATOM   2563  O O   . TYR   A 1 324 ? -19.898 -11.409 66.220  1.00 18.00  ?  324 TYR   A O   1 
ATOM   2564  C CB  . TYR   A 1 324 ? -17.207 -12.689 64.702  1.00 19.60  ?  324 TYR   A CB  1 
ATOM   2565  C CG  . TYR   A 1 324 ? -17.828 -11.629 63.834  1.00 17.47  ?  324 TYR   A CG  1 
ATOM   2566  C CD1 . TYR   A 1 324 ? -17.692 -10.278 64.152  1.00 15.15  ?  324 TYR   A CD1 1 
ATOM   2567  C CD2 . TYR   A 1 324 ? -18.588 -11.975 62.726  1.00 15.96  ?  324 TYR   A CD2 1 
ATOM   2568  C CE1 . TYR   A 1 324 ? -18.280 -9.305  63.378  1.00 14.99  ?  324 TYR   A CE1 1 
ATOM   2569  C CE2 . TYR   A 1 324 ? -19.189 -11.012 61.949  1.00 14.86  ?  324 TYR   A CE2 1 
ATOM   2570  C CZ  . TYR   A 1 324 ? -19.032 -9.679  62.280  1.00 16.41  ?  324 TYR   A CZ  1 
ATOM   2571  O OH  . TYR   A 1 324 ? -19.628 -8.719  61.505  1.00 19.48  ?  324 TYR   A OH  1 
ATOM   2572  N N   . LEU   A 1 325 ? -20.207 -13.398 65.199  1.00 16.05  ?  325 LEU   A N   1 
ATOM   2573  C CA  . LEU   A 1 325 ? -21.616 -13.117 64.920  1.00 16.12  ?  325 LEU   A CA  1 
ATOM   2574  C C   . LEU   A 1 325 ? -22.421 -12.947 66.204  1.00 19.80  ?  325 LEU   A C   1 
ATOM   2575  O O   . LEU   A 1 325 ? -23.337 -12.115 66.266  1.00 19.88  ?  325 LEU   A O   1 
ATOM   2576  C CB  . LEU   A 1 325 ? -22.219 -14.228 64.058  1.00 14.75  ?  325 LEU   A CB  1 
ATOM   2577  C CG  . LEU   A 1 325 ? -21.702 -14.335 62.622  1.00 13.24  ?  325 LEU   A CG  1 
ATOM   2578  C CD1 . LEU   A 1 325 ? -22.034 -15.695 62.024  1.00 15.69  ?  325 LEU   A CD1 1 
ATOM   2579  C CD2 . LEU   A 1 325 ? -22.293 -13.224 61.775  1.00 15.74  ?  325 LEU   A CD2 1 
ATOM   2580  N N   . HIS   A 1 326 ? -22.112 -13.742 67.233  1.00 18.75  ?  326 HIS   A N   1 
ATOM   2581  C CA  . HIS   A 1 326 ? -22.786 -13.591 68.518  1.00 17.98  ?  326 HIS   A CA  1 
ATOM   2582  C C   . HIS   A 1 326 ? -22.607 -12.176 69.059  1.00 19.55  ?  326 HIS   A C   1 
ATOM   2583  O O   . HIS   A 1 326 ? -23.575 -11.537 69.495  1.00 16.97  ?  326 HIS   A O   1 
ATOM   2584  C CB  . HIS   A 1 326 ? -22.243 -14.631 69.498  1.00 17.29  ?  326 HIS   A CB  1 
ATOM   2585  C CG  . HIS   A 1 326 ? -22.810 -14.531 70.879  1.00 24.98  ?  326 HIS   A CG  1 
ATOM   2586  N ND1 . HIS   A 1 326 ? -24.110 -14.883 71.178  1.00 27.45  ?  326 HIS   A ND1 1 
ATOM   2587  C CD2 . HIS   A 1 326 ? -22.248 -14.135 72.046  1.00 22.67  ?  326 HIS   A CD2 1 
ATOM   2588  C CE1 . HIS   A 1 326 ? -24.326 -14.700 72.469  1.00 27.31  ?  326 HIS   A CE1 1 
ATOM   2589  N NE2 . HIS   A 1 326 ? -23.213 -14.245 73.017  1.00 21.42  ?  326 HIS   A NE2 1 
ATOM   2590  N N   . TYR   A 1 327 ? -21.369 -11.666 69.022  1.00 19.30  ?  327 TYR   A N   1 
ATOM   2591  C CA  A TYR   A 1 327 ? -21.100 -10.311 69.496  0.57 19.09  ?  327 TYR   A CA  1 
ATOM   2592  C CA  B TYR   A 1 327 ? -21.100 -10.311 69.495  0.43 19.10  ?  327 TYR   A CA  1 
ATOM   2593  C C   . TYR   A 1 327 ? -21.788 -9.276  68.619  1.00 17.56  ?  327 TYR   A C   1 
ATOM   2594  O O   . TYR   A 1 327 ? -22.420 -8.342  69.126  1.00 18.93  ?  327 TYR   A O   1 
ATOM   2595  C CB  A TYR   A 1 327 ? -19.591 -10.045 69.532  0.57 19.79  ?  327 TYR   A CB  1 
ATOM   2596  C CB  B TYR   A 1 327 ? -19.593 -10.049 69.528  0.43 21.27  ?  327 TYR   A CB  1 
ATOM   2597  C CG  A TYR   A 1 327 ? -19.215 -8.644  69.065  0.57 20.12  ?  327 TYR   A CG  1 
ATOM   2598  C CG  B TYR   A 1 327 ? -19.235 -8.572  69.571  0.43 20.05  ?  327 TYR   A CG  1 
ATOM   2599  C CD1 A TYR   A 1 327 ? -19.340 -7.544  69.910  0.57 19.20  ?  327 TYR   A CD1 1 
ATOM   2600  C CD1 B TYR   A 1 327 ? -19.231 -7.875  70.770  0.43 19.82  ?  327 TYR   A CD1 1 
ATOM   2601  C CD2 A TYR   A 1 327 ? -18.744 -8.423  67.776  0.57 18.46  ?  327 TYR   A CD2 1 
ATOM   2602  C CD2 B TYR   A 1 327 ? -18.906 -7.876  68.412  0.43 18.68  ?  327 TYR   A CD2 1 
ATOM   2603  C CE1 A TYR   A 1 327 ? -19.011 -6.272  69.479  0.57 18.07  ?  327 TYR   A CE1 1 
ATOM   2604  C CE1 B TYR   A 1 327 ? -18.913 -6.535  70.817  0.43 19.21  ?  327 TYR   A CE1 1 
ATOM   2605  C CE2 A TYR   A 1 327 ? -18.415 -7.156  67.341  0.57 17.66  ?  327 TYR   A CE2 1 
ATOM   2606  C CE2 B TYR   A 1 327 ? -18.590 -6.534  68.450  0.43 17.28  ?  327 TYR   A CE2 1 
ATOM   2607  C CZ  A TYR   A 1 327 ? -18.551 -6.083  68.192  0.57 17.05  ?  327 TYR   A CZ  1 
ATOM   2608  C CZ  B TYR   A 1 327 ? -18.594 -5.868  69.657  0.43 18.50  ?  327 TYR   A CZ  1 
ATOM   2609  O OH  A TYR   A 1 327 ? -18.213 -4.818  67.743  0.57 16.37  ?  327 TYR   A OH  1 
ATOM   2610  O OH  B TYR   A 1 327 ? -18.273 -4.527  69.707  0.43 19.18  ?  327 TYR   A OH  1 
ATOM   2611  N N   . ARG   A 1 328 ? -21.650 -9.412  67.300  1.00 17.21  ?  328 ARG   A N   1 
ATOM   2612  C CA  . ARG   A 1 328 ? -22.200 -8.429  66.376  1.00 15.68  ?  328 ARG   A CA  1 
ATOM   2613  C C   . ARG   A 1 328 ? -23.708 -8.326  66.542  1.00 16.61  ?  328 ARG   A C   1 
ATOM   2614  O O   . ARG   A 1 328 ? -24.259 -7.240  66.777  1.00 13.22  ?  328 ARG   A O   1 
ATOM   2615  C CB  . ARG   A 1 328 ? -21.826 -8.818  64.941  1.00 14.84  ?  328 ARG   A CB  1 
ATOM   2616  C CG  . ARG   A 1 328 ? -22.090 -7.760  63.889  1.00 17.65  ?  328 ARG   A CG  1 
ATOM   2617  C CD  . ARG   A 1 328 ? -23.556 -7.723  63.457  1.00 14.33  ?  328 ARG   A CD  1 
ATOM   2618  N NE  . ARG   A 1 328 ? -23.741 -7.012  62.200  1.00 17.23  ?  328 ARG   A NE  1 
ATOM   2619  C CZ  . ARG   A 1 328 ? -23.705 -5.694  62.064  1.00 16.80  ?  328 ARG   A CZ  1 
ATOM   2620  N NH1 . ARG   A 1 328 ? -23.414 -4.900  63.083  1.00 16.44  ?  328 ARG   A NH1 1 
ATOM   2621  N NH2 . ARG   A 1 328 ? -23.987 -5.156  60.881  1.00 16.65  ?  328 ARG   A NH2 1 
ATOM   2622  N N   . ILE   A 1 329 ? -24.394 -9.459  66.412  1.00 16.09  ?  329 ILE   A N   1 
ATOM   2623  C CA  . ILE   A 1 329 ? -25.843 -9.457  66.529  1.00 16.80  ?  329 ILE   A CA  1 
ATOM   2624  C C   . ILE   A 1 329 ? -26.265 -9.110  67.949  1.00 19.56  ?  329 ILE   A C   1 
ATOM   2625  O O   . ILE   A 1 329 ? -27.293 -8.448  68.154  1.00 19.75  ?  329 ILE   A O   1 
ATOM   2626  C CB  . ILE   A 1 329 ? -26.379 -10.817 66.049  1.00 17.93  ?  329 ILE   A CB  1 
ATOM   2627  C CG1 . ILE   A 1 329 ? -25.932 -11.013 64.588  1.00 17.27  ?  329 ILE   A CG1 1 
ATOM   2628  C CG2 . ILE   A 1 329 ? -27.898 -10.890 66.221  1.00 21.02  ?  329 ILE   A CG2 1 
ATOM   2629  C CD1 . ILE   A 1 329 ? -26.362 -12.293 63.938  1.00 18.87  ?  329 ILE   A CD1 1 
ATOM   2630  N N   . GLY   A 1 330 ? -25.464 -9.500  68.948  1.00 19.29  ?  330 GLY   A N   1 
ATOM   2631  C CA  . GLY   A 1 330 ? -25.764 -9.123  70.320  1.00 16.12  ?  330 GLY   A CA  1 
ATOM   2632  C C   . GLY   A 1 330 ? -25.681 -7.628  70.568  1.00 17.48  ?  330 GLY   A C   1 
ATOM   2633  O O   . GLY   A 1 330 ? -26.438 -7.086  71.381  1.00 18.90  ?  330 GLY   A O   1 
ATOM   2634  N N   . GLN   A 1 331 ? -24.761 -6.941  69.888  1.00 18.24  ?  331 GLN   A N   1 
ATOM   2635  C CA  . GLN   A 1 331 ? -24.682 -5.494  70.052  1.00 16.58  ?  331 GLN   A CA  1 
ATOM   2636  C C   . GLN   A 1 331 ? -25.917 -4.821  69.479  1.00 17.22  ?  331 GLN   A C   1 
ATOM   2637  O O   . GLN   A 1 331 ? -26.451 -3.878  70.072  1.00 19.50  ?  331 GLN   A O   1 
ATOM   2638  C CB  . GLN   A 1 331 ? -23.420 -4.952  69.385  1.00 16.82  ?  331 GLN   A CB  1 
ATOM   2639  C CG  . GLN   A 1 331 ? -23.400 -3.432  69.345  1.00 19.43  ?  331 GLN   A CG  1 
ATOM   2640  C CD  . GLN   A 1 331 ? -22.142 -2.871  68.736  1.00 19.80  ?  331 GLN   A CD  1 
ATOM   2641  O OE1 . GLN   A 1 331 ? -21.926 -2.964  67.526  1.00 18.65  ?  331 GLN   A OE1 1 
ATOM   2642  N NE2 . GLN   A 1 331 ? -21.299 -2.280  69.571  1.00 16.42  ?  331 GLN   A NE2 1 
ATOM   2643  N N   . VAL   A 1 332 ? -26.374 -5.294  68.318  1.00 15.40  ?  332 VAL   A N   1 
ATOM   2644  C CA  . VAL   A 1 332 ? -27.627 -4.821  67.737  1.00 18.19  ?  332 VAL   A CA  1 
ATOM   2645  C C   . VAL   A 1 332 ? -28.774 -5.021  68.713  1.00 18.33  ?  332 VAL   A C   1 
ATOM   2646  O O   . VAL   A 1 332 ? -29.586 -4.114  68.945  1.00 18.38  ?  332 VAL   A O   1 
ATOM   2647  C CB  . VAL   A 1 332 ? -27.900 -5.551  66.412  1.00 15.52  ?  332 VAL   A CB  1 
ATOM   2648  C CG1 . VAL   A 1 332 ? -29.261 -5.133  65.851  1.00 17.37  ?  332 VAL   A CG1 1 
ATOM   2649  C CG2 . VAL   A 1 332 ? -26.763 -5.302  65.421  1.00 15.38  ?  332 VAL   A CG2 1 
ATOM   2650  N N   . LYS   A 1 333 ? -28.871 -6.230  69.279  1.00 20.64  ?  333 LYS   A N   1 
ATOM   2651  C CA  . LYS   A 1 333 ? -29.928 -6.549  70.233  1.00 18.87  ?  333 LYS   A CA  1 
ATOM   2652  C C   . LYS   A 1 333 ? -29.846 -5.673  71.474  1.00 18.36  ?  333 LYS   A C   1 
ATOM   2653  O O   . LYS   A 1 333 ? -30.876 -5.359  72.081  1.00 21.10  ?  333 LYS   A O   1 
ATOM   2654  C CB  . LYS   A 1 333 ? -29.835 -8.025  70.620  1.00 21.79  ?  333 LYS   A CB  1 
ATOM   2655  C CG  . LYS   A 1 333 ? -30.887 -8.492  71.609  1.00 22.56  ?  333 LYS   A CG  1 
ATOM   2656  C CD  . LYS   A 1 333 ? -30.828 -9.994  71.798  1.00 25.41  ?  333 LYS   A CD  1 
ATOM   2657  C CE  . LYS   A 1 333 ? -32.058 -10.520 72.546  1.00 29.42  ?  333 LYS   A CE  1 
ATOM   2658  N NZ  . LYS   A 1 333 ? -32.180 -9.953  73.903  1.00 26.04  ?  333 LYS   A NZ  1 
ATOM   2659  N N   . TYR   A 1 334 ? -28.631 -5.269  71.859  1.00 21.74  ?  334 TYR   A N   1 
ATOM   2660  C CA  . TYR   A 1 334 ? -28.445 -4.438  73.048  1.00 20.71  ?  334 TYR   A CA  1 
ATOM   2661  C C   . TYR   A 1 334 ? -28.976 -3.028  72.818  1.00 19.76  ?  334 TYR   A C   1 
ATOM   2662  O O   . TYR   A 1 334 ? -29.682 -2.473  73.668  1.00 19.83  ?  334 TYR   A O   1 
ATOM   2663  C CB  . TYR   A 1 334 ? -26.964 -4.407  73.440  1.00 20.20  ?  334 TYR   A CB  1 
ATOM   2664  C CG  . TYR   A 1 334 ? -26.638 -3.363  74.481  1.00 19.66  ?  334 TYR   A CG  1 
ATOM   2665  C CD1 . TYR   A 1 334 ? -26.980 -3.553  75.810  1.00 22.14  ?  334 TYR   A CD1 1 
ATOM   2666  C CD2 . TYR   A 1 334 ? -25.980 -2.191  74.137  1.00 22.83  ?  334 TYR   A CD2 1 
ATOM   2667  C CE1 . TYR   A 1 334 ? -26.695 -2.593  76.770  1.00 24.11  ?  334 TYR   A CE1 1 
ATOM   2668  C CE2 . TYR   A 1 334 ? -25.684 -1.224  75.097  1.00 21.15  ?  334 TYR   A CE2 1 
ATOM   2669  C CZ  . TYR   A 1 334 ? -26.043 -1.434  76.403  1.00 24.21  ?  334 TYR   A CZ  1 
ATOM   2670  O OH  . TYR   A 1 334 ? -25.759 -0.482  77.353  1.00 26.25  ?  334 TYR   A OH  1 
ATOM   2671  N N   . LEU   A 1 335 ? -28.661 -2.432  71.667  1.00 16.51  ?  335 LEU   A N   1 
ATOM   2672  C CA  . LEU   A 1 335 ? -29.242 -1.130  71.358  1.00 17.71  ?  335 LEU   A CA  1 
ATOM   2673  C C   . LEU   A 1 335 ? -30.762 -1.224  71.259  1.00 20.84  ?  335 LEU   A C   1 
ATOM   2674  O O   . LEU   A 1 335 ? -31.481 -0.326  71.721  1.00 21.70  ?  335 LEU   A O   1 
ATOM   2675  C CB  . LEU   A 1 335 ? -28.632 -0.577  70.071  1.00 18.11  ?  335 LEU   A CB  1 
ATOM   2676  C CG  . LEU   A 1 335 ? -29.215 0.718   69.503  1.00 19.95  ?  335 LEU   A CG  1 
ATOM   2677  C CD1 . LEU   A 1 335 ? -29.223 1.831   70.541  1.00 21.94  ?  335 LEU   A CD1 1 
ATOM   2678  C CD2 . LEU   A 1 335 ? -28.439 1.144   68.264  1.00 24.69  ?  335 LEU   A CD2 1 
ATOM   2679  N N   . GLY   A 1 336 ? -31.272 -2.314  70.679  1.00 22.37  ?  336 GLY   A N   1 
ATOM   2680  C CA  . GLY   A 1 336 ? -32.717 -2.490  70.602  1.00 21.19  ?  336 GLY   A CA  1 
ATOM   2681  C C   . GLY   A 1 336 ? -33.367 -2.640  71.966  1.00 24.55  ?  336 GLY   A C   1 
ATOM   2682  O O   . GLY   A 1 336 ? -34.403 -2.025  72.243  1.00 24.66  ?  336 GLY   A O   1 
ATOM   2683  N N   . ASP   A 1 337 ? -32.770 -3.456  72.837  1.00 22.46  ?  337 ASP   A N   1 
ATOM   2684  C CA  . ASP   A 1 337 ? -33.324 -3.633  74.175  1.00 23.91  ?  337 ASP   A CA  1 
ATOM   2685  C C   . ASP   A 1 337 ? -33.255 -2.343  74.979  1.00 25.93  ?  337 ASP   A C   1 
ATOM   2686  O O   . ASP   A 1 337 ? -34.151 -2.056  75.780  1.00 29.50  ?  337 ASP   A O   1 
ATOM   2687  C CB  . ASP   A 1 337 ? -32.586 -4.750  74.916  1.00 29.98  ?  337 ASP   A CB  1 
ATOM   2688  C CG  . ASP   A 1 337 ? -32.932 -6.133  74.391  1.00 27.52  ?  337 ASP   A CG  1 
ATOM   2689  O OD1 . ASP   A 1 337 ? -34.064 -6.334  73.893  1.00 31.69  ?  337 ASP   A OD1 1 
ATOM   2690  O OD2 . ASP   A 1 337 ? -32.067 -7.023  74.492  1.00 28.27  ?  337 ASP   A OD2 1 
ATOM   2691  N N   . ARG   A 1 338 ? -32.191 -1.561  74.797  1.00 24.69  ?  338 ARG   A N   1 
ATOM   2692  C CA  . ARG   A 1 338 ? -32.116 -0.267  75.468  1.00 27.73  ?  338 ARG   A CA  1 
ATOM   2693  C C   . ARG   A 1 338 ? -33.293 0.611   75.075  1.00 23.42  ?  338 ARG   A C   1 
ATOM   2694  O O   . ARG   A 1 338 ? -33.943 1.213   75.934  1.00 29.69  ?  338 ARG   A O   1 
ATOM   2695  C CB  . ARG   A 1 338 ? -30.787 0.417   75.141  1.00 21.53  ?  338 ARG   A CB  1 
ATOM   2696  C CG  . ARG   A 1 338 ? -29.622 -0.086  75.980  1.00 24.61  ?  338 ARG   A CG  1 
ATOM   2697  C CD  . ARG   A 1 338 ? -29.647 0.532   77.387  1.00 28.35  ?  338 ARG   A CD  1 
ATOM   2698  N NE  . ARG   A 1 338 ? -28.866 1.764   77.420  1.00 35.99  ?  338 ARG   A NE  1 
ATOM   2699  C CZ  . ARG   A 1 338 ? -29.372 2.986   77.529  1.00 27.93  ?  338 ARG   A CZ  1 
ATOM   2700  N NH1 . ARG   A 1 338 ? -30.661 3.184   77.734  1.00 32.64  ?  338 ARG   A NH1 1 
ATOM   2701  N NH2 . ARG   A 1 338 ? -28.559 4.035   77.422  1.00 30.57  ?  338 ARG   A NH2 1 
ATOM   2702  N N   . LEU   A 1 339 ? -33.604 0.665   73.775  1.00 23.28  ?  339 LEU   A N   1 
ATOM   2703  C CA  . LEU   A 1 339 ? -34.717 1.483   73.300  1.00 25.86  ?  339 LEU   A CA  1 
ATOM   2704  C C   . LEU   A 1 339 ? -36.063 0.868   73.667  1.00 30.76  ?  339 LEU   A C   1 
ATOM   2705  O O   . LEU   A 1 339 ? -37.012 1.586   74.007  1.00 28.42  ?  339 LEU   A O   1 
ATOM   2706  C CB  . LEU   A 1 339 ? -34.610 1.673   71.788  1.00 24.27  ?  339 LEU   A CB  1 
ATOM   2707  C CG  . LEU   A 1 339 ? -33.356 2.415   71.320  1.00 25.86  ?  339 LEU   A CG  1 
ATOM   2708  C CD1 . LEU   A 1 339 ? -33.182 2.267   69.813  1.00 25.95  ?  339 LEU   A CD1 1 
ATOM   2709  C CD2 . LEU   A 1 339 ? -33.426 3.874   71.696  1.00 23.02  ?  339 LEU   A CD2 1 
ATOM   2710  N N   . ARG   A 1 340 ? -36.169 -0.458  73.599  1.00 29.82  ?  340 ARG   A N   1 
ATOM   2711  C CA  . ARG   A 1 340 ? -37.418 -1.123  73.954  1.00 27.97  ?  340 ARG   A CA  1 
ATOM   2712  C C   . ARG   A 1 340 ? -37.747 -0.933  75.434  1.00 30.25  ?  340 ARG   A C   1 
ATOM   2713  O O   . ARG   A 1 340 ? -38.911 -0.719  75.796  1.00 30.56  ?  340 ARG   A O   1 
ATOM   2714  C CB  . ARG   A 1 340 ? -37.311 -2.603  73.587  1.00 27.77  ?  340 ARG   A CB  1 
ATOM   2715  C CG  . ARG   A 1 340 ? -38.558 -3.431  73.806  1.00 28.63  ?  340 ARG   A CG  1 
ATOM   2716  C CD  . ARG   A 1 340 ? -38.474 -4.693  72.956  1.00 32.89  ?  340 ARG   A CD  1 
ATOM   2717  N NE  . ARG   A 1 340 ? -39.670 -5.518  73.064  1.00 31.72  ?  340 ARG   A NE  1 
ATOM   2718  C CZ  . ARG   A 1 340 ? -39.827 -6.484  73.957  1.00 34.83  ?  340 ARG   A CZ  1 
ATOM   2719  N NH1 . ARG   A 1 340 ? -38.891 -6.753  74.854  1.00 33.75  ?  340 ARG   A NH1 1 
ATOM   2720  N NH2 . ARG   A 1 340 ? -40.949 -7.199  73.951  1.00 37.01  ?  340 ARG   A NH2 1 
ATOM   2721  N N   . GLU   A 1 341 ? -36.733 -0.988  76.304  1.00 27.54  ?  341 GLU   A N   1 
ATOM   2722  C CA  . GLU   A 1 341 ? -36.953 -0.781  77.731  1.00 28.55  ?  341 GLU   A CA  1 
ATOM   2723  C C   . GLU   A 1 341 ? -37.416 0.633   78.051  1.00 34.51  ?  341 GLU   A C   1 
ATOM   2724  O O   . GLU   A 1 341 ? -38.059 0.836   79.086  1.00 37.03  ?  341 GLU   A O   1 
ATOM   2725  C CB  . GLU   A 1 341 ? -35.680 -1.085  78.523  1.00 32.72  ?  341 GLU   A CB  1 
ATOM   2726  C CG  . GLU   A 1 341 ? -35.356 -2.565  78.662  1.00 34.21  ?  341 GLU   A CG  1 
ATOM   2727  C CD  . GLU   A 1 341 ? -33.878 -2.820  78.923  1.00 36.86  ?  341 GLU   A CD  1 
ATOM   2728  O OE1 . GLU   A 1 341 ? -33.184 -1.903  79.425  1.00 41.29  ?  341 GLU   A OE1 1 
ATOM   2729  O OE2 . GLU   A 1 341 ? -33.403 -3.936  78.610  1.00 34.96  ?  341 GLU   A OE2 1 
ATOM   2730  N N   . ALA   A 1 342 ? -37.104 1.611   77.202  1.00 29.84  ?  342 ALA   A N   1 
ATOM   2731  C CA  . ALA   A 1 342 ? -37.531 2.985   77.422  1.00 28.98  ?  342 ALA   A CA  1 
ATOM   2732  C C   . ALA   A 1 342 ? -38.823 3.323   76.692  1.00 36.01  ?  342 ALA   A C   1 
ATOM   2733  O O   . ALA   A 1 342 ? -39.226 4.493   76.673  1.00 40.73  ?  342 ALA   A O   1 
ATOM   2734  C CB  . ALA   A 1 342 ? -36.428 3.961   77.010  1.00 27.74  ?  342 ALA   A CB  1 
ATOM   2735  N N   . GLY   A 1 343 ? -39.485 2.332   76.103  1.00 33.08  ?  343 GLY   A N   1 
ATOM   2736  C CA  . GLY   A 1 343 ? -40.775 2.557   75.486  1.00 29.62  ?  343 GLY   A CA  1 
ATOM   2737  C C   . GLY   A 1 343 ? -40.744 2.969   74.032  1.00 34.16  ?  343 GLY   A C   1 
ATOM   2738  O O   . GLY   A 1 343 ? -41.792 3.349   73.494  1.00 34.78  ?  343 GLY   A O   1 
ATOM   2739  N N   . ILE   A 1 344 ? -39.588 2.905   73.378  1.00 28.44  ?  344 ILE   A N   1 
ATOM   2740  C CA  . ILE   A 1 344 ? -39.470 3.233   71.960  1.00 31.76  ?  344 ILE   A CA  1 
ATOM   2741  C C   . ILE   A 1 344 ? -39.862 2.017   71.126  1.00 35.04  ?  344 ILE   A C   1 
ATOM   2742  O O   . ILE   A 1 344 ? -39.287 0.932   71.304  1.00 29.75  ?  344 ILE   A O   1 
ATOM   2743  C CB  . ILE   A 1 344 ? -38.050 3.704   71.614  1.00 32.70  ?  344 ILE   A CB  1 
ATOM   2744  C CG1 . ILE   A 1 344 ? -37.639 4.867   72.519  1.00 30.42  ?  344 ILE   A CG1 1 
ATOM   2745  C CG2 . ILE   A 1 344 ? -37.954 4.098   70.144  1.00 28.56  ?  344 ILE   A CG2 1 
ATOM   2746  C CD1 . ILE   A 1 344 ? -38.440 6.120   72.301  1.00 37.71  ?  344 ILE   A CD1 1 
ATOM   2747  N N   . PRO   A 1 345 ? -40.827 2.149   70.214  1.00 31.84  ?  345 PRO   A N   1 
ATOM   2748  C CA  . PRO   A 1 345 ? -41.250 0.996   69.401  1.00 38.24  ?  345 PRO   A CA  1 
ATOM   2749  C C   . PRO   A 1 345 ? -40.235 0.656   68.314  1.00 34.14  ?  345 PRO   A C   1 
ATOM   2750  O O   . PRO   A 1 345 ? -39.792 1.521   67.554  1.00 29.64  ?  345 PRO   A O   1 
ATOM   2751  C CB  . PRO   A 1 345 ? -42.582 1.460   68.798  1.00 34.25  ?  345 PRO   A CB  1 
ATOM   2752  C CG  . PRO   A 1 345 ? -42.466 2.961   68.767  1.00 36.82  ?  345 PRO   A CG  1 
ATOM   2753  C CD  . PRO   A 1 345 ? -41.685 3.328   70.000  1.00 34.93  ?  345 PRO   A CD  1 
ATOM   2754  N N   . ILE   A 1 346 ? -39.877 -0.626  68.241  1.00 29.64  ?  346 ILE   A N   1 
ATOM   2755  C CA  . ILE   A 1 346 ? -38.929 -1.132  67.260  1.00 30.89  ?  346 ILE   A CA  1 
ATOM   2756  C C   . ILE   A 1 346 ? -39.476 -2.433  66.687  1.00 25.50  ?  346 ILE   A C   1 
ATOM   2757  O O   . ILE   A 1 346 ? -40.405 -3.033  67.223  1.00 25.43  ?  346 ILE   A O   1 
ATOM   2758  C CB  . ILE   A 1 346 ? -37.526 -1.369  67.861  1.00 29.56  ?  346 ILE   A CB  1 
ATOM   2759  C CG1 . ILE   A 1 346 ? -37.603 -2.386  69.000  1.00 27.75  ?  346 ILE   A CG1 1 
ATOM   2760  C CG2 . ILE   A 1 346 ? -36.899 -0.061  68.330  1.00 27.55  ?  346 ILE   A CG2 1 
ATOM   2761  C CD1 . ILE   A 1 346 ? -36.251 -2.762  69.573  1.00 27.56  ?  346 ILE   A CD1 1 
ATOM   2762  N N   . GLN   A 1 347 ? -38.884 -2.867  65.581  1.00 25.38  ?  347 GLN   A N   1 
ATOM   2763  C CA  . GLN   A 1 347 ? -39.183 -4.187  65.040  1.00 29.38  ?  347 GLN   A CA  1 
ATOM   2764  C C   . GLN   A 1 347 ? -38.592 -5.249  65.963  1.00 29.44  ?  347 GLN   A C   1 
ATOM   2765  O O   . GLN   A 1 347 ? -37.368 -5.356  66.102  1.00 29.28  ?  347 GLN   A O   1 
ATOM   2766  C CB  . GLN   A 1 347 ? -38.628 -4.319  63.625  1.00 27.55  ?  347 GLN   A CB  1 
ATOM   2767  C CG  . GLN   A 1 347 ? -38.786 -5.712  63.038  1.00 29.41  ?  347 GLN   A CG  1 
ATOM   2768  C CD  . GLN   A 1 347 ? -40.173 -5.963  62.481  1.00 34.01  ?  347 GLN   A CD  1 
ATOM   2769  O OE1 . GLN   A 1 347 ? -41.082 -6.377  63.203  1.00 32.83  ?  347 GLN   A OE1 1 
ATOM   2770  N NE2 . GLN   A 1 347 ? -40.341 -5.717  61.183  1.00 35.62  ?  347 GLN   A NE2 1 
ATOM   2771  N N   . TYR   A 1 348 ? -39.452 -6.041  66.585  1.00 24.20  ?  348 TYR   A N   1 
ATOM   2772  C CA  . TYR   A 1 348 ? -39.009 -7.027  67.553  1.00 28.18  ?  348 TYR   A CA  1 
ATOM   2773  C C   . TYR   A 1 348 ? -39.286 -8.432  67.035  1.00 28.00  ?  348 TYR   A C   1 
ATOM   2774  O O   . TYR   A 1 348 ? -40.427 -8.733  66.660  1.00 26.74  ?  348 TYR   A O   1 
ATOM   2775  C CB  . TYR   A 1 348 ? -39.724 -6.807  68.898  1.00 28.22  ?  348 TYR   A CB  1 
ATOM   2776  C CG  . TYR   A 1 348 ? -39.167 -7.631  70.036  1.00 28.39  ?  348 TYR   A CG  1 
ATOM   2777  C CD1 . TYR   A 1 348 ? -37.859 -7.457  70.466  1.00 32.10  ?  348 TYR   A CD1 1 
ATOM   2778  C CD2 . TYR   A 1 348 ? -39.946 -8.578  70.677  1.00 34.88  ?  348 TYR   A CD2 1 
ATOM   2779  C CE1 . TYR   A 1 348 ? -37.340 -8.210  71.498  1.00 34.01  ?  348 TYR   A CE1 1 
ATOM   2780  C CE2 . TYR   A 1 348 ? -39.435 -9.339  71.719  1.00 35.32  ?  348 TYR   A CE2 1 
ATOM   2781  C CZ  . TYR   A 1 348 ? -38.134 -9.149  72.123  1.00 36.62  ?  348 TYR   A CZ  1 
ATOM   2782  O OH  . TYR   A 1 348 ? -37.622 -9.897  73.158  1.00 41.17  ?  348 TYR   A OH  1 
ATOM   2783  N N   . PRO   A 1 349 ? -38.292 -9.330  67.027  1.00 27.07  ?  349 PRO   A N   1 
ATOM   2784  C CA  . PRO   A 1 349 ? -36.919 -9.186  67.545  1.00 27.50  ?  349 PRO   A CA  1 
ATOM   2785  C C   . PRO   A 1 349 ? -36.032 -8.327  66.656  1.00 21.02  ?  349 PRO   A C   1 
ATOM   2786  O O   . PRO   A 1 349 ? -36.330 -8.167  65.472  1.00 21.12  ?  349 PRO   A O   1 
ATOM   2787  C CB  . PRO   A 1 349 ? -36.428 -10.640 67.590  1.00 26.79  ?  349 PRO   A CB  1 
ATOM   2788  C CG  . PRO   A 1 349 ? -37.114 -11.274 66.418  1.00 24.88  ?  349 PRO   A CG  1 
ATOM   2789  C CD  . PRO   A 1 349 ? -38.505 -10.663 66.431  1.00 25.15  ?  349 PRO   A CD  1 
ATOM   2790  N N   . THR   A 1 350 ? -34.945 -7.761  67.184  1.00 20.31  ?  350 THR   A N   1 
ATOM   2791  C CA  . THR   A 1 350 ? -34.017 -7.028  66.330  1.00 24.53  ?  350 THR   A CA  1 
ATOM   2792  C C   . THR   A 1 350 ? -33.361 -7.985  65.352  1.00 22.71  ?  350 THR   A C   1 
ATOM   2793  O O   . THR   A 1 350 ? -33.164 -9.165  65.650  1.00 24.04  ?  350 THR   A O   1 
ATOM   2794  C CB  . THR   A 1 350 ? -32.939 -6.313  67.154  1.00 21.60  ?  350 THR   A CB  1 
ATOM   2795  O OG1 . THR   A 1 350 ? -32.299 -7.252  68.029  1.00 24.49  ?  350 THR   A OG1 1 
ATOM   2796  C CG2 . THR   A 1 350 ? -33.555 -5.190  67.981  1.00 22.90  ?  350 THR   A CG2 1 
ATOM   2797  N N   . GLY   A 1 351 ? -33.049 -7.471  64.167  1.00 18.42  ?  351 GLY   A N   1 
ATOM   2798  C CA  . GLY   A 1 351 ? -32.393 -8.242  63.136  1.00 22.47  ?  351 GLY   A CA  1 
ATOM   2799  C C   . GLY   A 1 351 ? -30.891 -8.268  63.308  1.00 20.11  ?  351 GLY   A C   1 
ATOM   2800  O O   . GLY   A 1 351 ? -30.347 -7.948  64.367  1.00 23.33  ?  351 GLY   A O   1 
ATOM   2801  N N   . GLY   A 1 352 ? -30.203 -8.642  62.232  1.00 19.68  ?  352 GLY   A N   1 
ATOM   2802  C CA  . GLY   A 1 352 ? -28.773 -8.857  62.338  1.00 18.88  ?  352 GLY   A CA  1 
ATOM   2803  C C   . GLY   A 1 352 ? -27.922 -7.604  62.328  1.00 21.79  ?  352 GLY   A C   1 
ATOM   2804  O O   . GLY   A 1 352 ? -26.888 -7.556  63.005  1.00 19.91  ?  352 GLY   A O   1 
ATOM   2805  N N   . HIS   A 1 353 ? -28.323 -6.575  61.573  1.00 19.20  ?  353 HIS   A N   1 
ATOM   2806  C CA  . HIS   A 1 353 ? -27.416 -5.471  61.279  1.00 17.76  ?  353 HIS   A CA  1 
ATOM   2807  C C   . HIS   A 1 353 ? -27.879 -4.101  61.756  1.00 19.06  ?  353 HIS   A C   1 
ATOM   2808  O O   . HIS   A 1 353 ? -27.107 -3.141  61.630  1.00 22.59  ?  353 HIS   A O   1 
ATOM   2809  C CB  . HIS   A 1 353 ? -27.156 -5.383  59.772  1.00 15.95  ?  353 HIS   A CB  1 
ATOM   2810  C CG  . HIS   A 1 353 ? -28.349 -4.946  58.978  1.00 17.92  ?  353 HIS   A CG  1 
ATOM   2811  N ND1 . HIS   A 1 353 ? -29.537 -5.645  58.972  1.00 17.24  ?  353 HIS   A ND1 1 
ATOM   2812  C CD2 . HIS   A 1 353 ? -28.536 -3.880  58.163  1.00 19.26  ?  353 HIS   A CD2 1 
ATOM   2813  C CE1 . HIS   A 1 353 ? -30.405 -5.030  58.188  1.00 18.31  ?  353 HIS   A CE1 1 
ATOM   2814  N NE2 . HIS   A 1 353 ? -29.821 -3.958  57.682  1.00 22.39  ?  353 HIS   A NE2 1 
ATOM   2815  N N   . ALA   A 1 354 ? -29.088 -3.970  62.293  1.00 20.59  ?  354 ALA   A N   1 
ATOM   2816  C CA  . ALA   A 1 354 ? -29.627 -2.650  62.602  1.00 18.18  ?  354 ALA   A CA  1 
ATOM   2817  C C   . ALA   A 1 354 ? -30.833 -2.795  63.511  1.00 23.07  ?  354 ALA   A C   1 
ATOM   2818  O O   . ALA   A 1 354 ? -31.475 -3.851  63.554  1.00 22.10  ?  354 ALA   A O   1 
ATOM   2819  C CB  . ALA   A 1 354 ? -30.025 -1.895  61.327  1.00 18.88  ?  354 ALA   A CB  1 
ATOM   2820  N N   . VAL   A 1 355 ? -31.132 -1.714  64.240  1.00 20.55  ?  355 VAL   A N   1 
ATOM   2821  C CA  . VAL   A 1 355 ? -32.402 -1.555  64.942  1.00 23.80  ?  355 VAL   A CA  1 
ATOM   2822  C C   . VAL   A 1 355 ? -33.296 -0.676  64.076  1.00 24.55  ?  355 VAL   A C   1 
ATOM   2823  O O   . VAL   A 1 355 ? -32.861 0.378   63.594  1.00 23.06  ?  355 VAL   A O   1 
ATOM   2824  C CB  . VAL   A 1 355 ? -32.208 -0.940  66.339  1.00 23.89  ?  355 VAL   A CB  1 
ATOM   2825  C CG1 . VAL   A 1 355 ? -33.549 -0.784  67.047  1.00 20.80  ?  355 VAL   A CG1 1 
ATOM   2826  C CG2 . VAL   A 1 355 ? -31.260 -1.789  67.184  1.00 20.51  ?  355 VAL   A CG2 1 
ATOM   2827  N N   . PHE   A 1 356 ? -34.528 -1.122  63.847  1.00 19.28  ?  356 PHE   A N   1 
ATOM   2828  C CA  . PHE   A 1 356 ? -35.491 -0.397  63.022  1.00 29.94  ?  356 PHE   A CA  1 
ATOM   2829  C C   . PHE   A 1 356 ? -36.546 0.195   63.951  1.00 29.16  ?  356 PHE   A C   1 
ATOM   2830  O O   . PHE   A 1 356 ? -37.349 -0.540  64.535  1.00 30.27  ?  356 PHE   A O   1 
ATOM   2831  C CB  . PHE   A 1 356 ? -36.134 -1.308  61.975  1.00 32.63  ?  356 PHE   A CB  1 
ATOM   2832  C CG  . PHE   A 1 356 ? -35.207 -1.732  60.854  1.00 27.84  ?  356 PHE   A CG  1 
ATOM   2833  C CD1 . PHE   A 1 356 ? -34.119 -2.561  61.100  1.00 26.95  ?  356 PHE   A CD1 1 
ATOM   2834  C CD2 . PHE   A 1 356 ? -35.458 -1.343  59.549  1.00 30.93  ?  356 PHE   A CD2 1 
ATOM   2835  C CE1 . PHE   A 1 356 ? -33.280 -2.964  60.070  1.00 23.84  ?  356 PHE   A CE1 1 
ATOM   2836  C CE2 . PHE   A 1 356 ? -34.626 -1.745  58.512  1.00 29.96  ?  356 PHE   A CE2 1 
ATOM   2837  C CZ  . PHE   A 1 356 ? -33.536 -2.561  58.774  1.00 25.24  ?  356 PHE   A CZ  1 
ATOM   2838  N N   . VAL   A 1 357 ? -36.543 1.519   64.082  1.00 26.09  ?  357 VAL   A N   1 
ATOM   2839  C CA  . VAL   A 1 357 ? -37.463 2.226   64.967  1.00 25.52  ?  357 VAL   A CA  1 
ATOM   2840  C C   . VAL   A 1 357 ? -38.770 2.469   64.223  1.00 35.76  ?  357 VAL   A C   1 
ATOM   2841  O O   . VAL   A 1 357 ? -38.778 3.074   63.146  1.00 35.15  ?  357 VAL   A O   1 
ATOM   2842  C CB  . VAL   A 1 357 ? -36.847 3.545   65.451  1.00 28.69  ?  357 VAL   A CB  1 
ATOM   2843  C CG1 . VAL   A 1 357 ? -37.847 4.343   66.268  1.00 33.96  ?  357 VAL   A CG1 1 
ATOM   2844  C CG2 . VAL   A 1 357 ? -35.583 3.266   66.259  1.00 24.57  ?  357 VAL   A CG2 1 
ATOM   2845  N N   . ASP   A 1 358 ? -39.877 2.003   64.796  1.00 33.76  ?  358 ASP   A N   1 
ATOM   2846  C CA  . ASP   A 1 358 ? -41.188 2.128   64.163  1.00 39.87  ?  358 ASP   A CA  1 
ATOM   2847  C C   . ASP   A 1 358 ? -41.706 3.540   64.422  1.00 42.47  ?  358 ASP   A C   1 
ATOM   2848  O O   . ASP   A 1 358 ? -42.280 3.827   65.475  1.00 40.91  ?  358 ASP   A O   1 
ATOM   2849  C CB  . ASP   A 1 358 ? -42.140 1.061   64.693  1.00 40.38  ?  358 ASP   A CB  1 
ATOM   2850  C CG  . ASP   A 1 358 ? -43.384 0.898   63.834  1.00 43.12  ?  358 ASP   A CG  1 
ATOM   2851  O OD1 . ASP   A 1 358 ? -43.613 1.730   62.929  1.00 51.14  ?  358 ASP   A OD1 1 
ATOM   2852  O OD2 . ASP   A 1 358 ? -44.138 -0.072  64.067  1.00 48.98  ?  358 ASP   A OD2 1 
ATOM   2853  N N   . CYS   A 1 359 ? -41.493 4.431   63.454  1.00 39.52  ?  359 CYS   A N   1 
ATOM   2854  C CA  . CYS   A 1 359 ? -41.874 5.824   63.614  1.00 45.24  ?  359 CYS   A CA  1 
ATOM   2855  C C   . CYS   A 1 359 ? -43.355 6.061   63.365  1.00 51.89  ?  359 CYS   A C   1 
ATOM   2856  O O   . CYS   A 1 359 ? -43.874 7.108   63.768  1.00 50.91  ?  359 CYS   A O   1 
ATOM   2857  C CB  . CYS   A 1 359 ? -41.044 6.698   62.675  1.00 45.63  ?  359 CYS   A CB  1 
ATOM   2858  S SG  . CYS   A 1 359 ? -39.284 6.626   63.027  1.00 37.62  ?  359 CYS   A SG  1 
ATOM   2859  N N   . LYS   A 1 360 ? -44.038 5.120   62.703  1.00 48.71  ?  360 LYS   A N   1 
ATOM   2860  C CA  . LYS   A 1 360 ? -45.484 5.217   62.542  1.00 53.76  ?  360 LYS   A CA  1 
ATOM   2861  C C   . LYS   A 1 360 ? -46.178 5.433   63.882  1.00 52.84  ?  360 LYS   A C   1 
ATOM   2862  O O   . LYS   A 1 360 ? -47.183 6.149   63.956  1.00 56.43  ?  360 LYS   A O   1 
ATOM   2863  C CB  . LYS   A 1 360 ? -46.011 3.955   61.852  1.00 54.66  ?  360 LYS   A CB  1 
ATOM   2864  C CG  . LYS   A 1 360 ? -47.519 3.902   61.669  1.00 56.62  ?  360 LYS   A CG  1 
ATOM   2865  C CD  . LYS   A 1 360 ? -48.042 5.108   60.904  1.00 60.20  ?  360 LYS   A CD  1 
ATOM   2866  C CE  . LYS   A 1 360 ? -49.523 4.950   60.577  1.00 60.74  ?  360 LYS   A CE  1 
ATOM   2867  N NZ  . LYS   A 1 360 ? -50.328 4.575   61.778  1.00 61.82  ?  360 LYS   A NZ  1 
ATOM   2868  N N   . LYS   A 1 361 ? -45.643 4.852   64.955  1.00 53.01  ?  361 LYS   A N   1 
ATOM   2869  C CA  . LYS   A 1 361 ? -46.193 5.069   66.286  1.00 54.33  ?  361 LYS   A CA  1 
ATOM   2870  C C   . LYS   A 1 361 ? -45.550 6.247   67.009  1.00 51.22  ?  361 LYS   A C   1 
ATOM   2871  O O   . LYS   A 1 361 ? -46.216 6.898   67.824  1.00 47.64  ?  361 LYS   A O   1 
ATOM   2872  C CB  . LYS   A 1 361 ? -46.035 3.802   67.130  1.00 57.99  ?  361 LYS   A CB  1 
ATOM   2873  C CG  . LYS   A 1 361 ? -46.550 2.540   66.453  1.00 58.93  ?  361 LYS   A CG  1 
ATOM   2874  C CD  . LYS   A 1 361 ? -46.560 1.364   67.417  1.00 63.26  ?  361 LYS   A CD  1 
ATOM   2875  C CE  . LYS   A 1 361 ? -47.484 1.629   68.600  1.00 68.76  ?  361 LYS   A CE  1 
ATOM   2876  N NZ  . LYS   A 1 361 ? -47.462 0.524   69.598  1.00 68.07  ?  361 LYS   A NZ  1 
ATOM   2877  N N   . LEU   A 1 362 ? -44.275 6.539   66.727  1.00 50.52  ?  362 LEU   A N   1 
ATOM   2878  C CA  . LEU   A 1 362 ? -43.585 7.624   67.421  1.00 50.53  ?  362 LEU   A CA  1 
ATOM   2879  C C   . LEU   A 1 362 ? -44.158 8.986   67.053  1.00 51.38  ?  362 LEU   A C   1 
ATOM   2880  O O   . LEU   A 1 362 ? -44.298 9.864   67.915  1.00 47.53  ?  362 LEU   A O   1 
ATOM   2881  C CB  . LEU   A 1 362 ? -42.091 7.595   67.102  1.00 47.17  ?  362 LEU   A CB  1 
ATOM   2882  C CG  . LEU   A 1 362 ? -41.171 6.778   68.002  1.00 46.40  ?  362 LEU   A CG  1 
ATOM   2883  C CD1 . LEU   A 1 362 ? -39.729 7.190   67.757  1.00 46.32  ?  362 LEU   A CD1 1 
ATOM   2884  C CD2 . LEU   A 1 362 ? -41.549 6.950   69.459  1.00 38.76  ?  362 LEU   A CD2 1 
ATOM   2885  N N   . VAL   A 1 363 ? -44.466 9.191   65.778  1.00 53.40  ?  363 VAL   A N   1 
ATOM   2886  C CA  . VAL   A 1 363 ? -44.956 10.478  65.300  1.00 51.78  ?  363 VAL   A CA  1 
ATOM   2887  C C   . VAL   A 1 363 ? -46.244 10.248  64.513  1.00 58.40  ?  363 VAL   A C   1 
ATOM   2888  O O   . VAL   A 1 363 ? -46.277 10.473  63.294  1.00 55.67  ?  363 VAL   A O   1 
ATOM   2889  C CB  . VAL   A 1 363 ? -43.884 11.193  64.462  1.00 48.62  ?  363 VAL   A CB  1 
ATOM   2890  C CG1 . VAL   A 1 363 ? -42.845 11.820  65.368  1.00 49.63  ?  363 VAL   A CG1 1 
ATOM   2891  C CG2 . VAL   A 1 363 ? -43.207 10.213  63.532  1.00 49.57  ?  363 VAL   A CG2 1 
ATOM   2892  N N   . PRO   A 1 364 ? -47.329 9.812   65.163  1.00 57.38  ?  364 PRO   A N   1 
ATOM   2893  C CA  . PRO   A 1 364 ? -48.553 9.490   64.413  1.00 57.44  ?  364 PRO   A CA  1 
ATOM   2894  C C   . PRO   A 1 364 ? -49.253 10.705  63.827  1.00 58.12  ?  364 PRO   A C   1 
ATOM   2895  O O   . PRO   A 1 364 ? -50.152 10.531  62.991  1.00 59.26  ?  364 PRO   A O   1 
ATOM   2896  C CB  . PRO   A 1 364 ? -49.430 8.794   65.462  1.00 53.85  ?  364 PRO   A CB  1 
ATOM   2897  C CG  . PRO   A 1 364 ? -49.008 9.414   66.750  1.00 54.14  ?  364 PRO   A CG  1 
ATOM   2898  C CD  . PRO   A 1 364 ? -47.521 9.658   66.617  1.00 59.26  ?  364 PRO   A CD  1 
ATOM   2899  N N   . GLN   A 1 365 ? -48.878 11.923  64.228  1.00 54.49  ?  365 GLN   A N   1 
ATOM   2900  C CA  . GLN   A 1 365 ? -49.525 13.104  63.670  1.00 52.41  ?  365 GLN   A CA  1 
ATOM   2901  C C   . GLN   A 1 365 ? -49.080 13.384  62.242  1.00 61.72  ?  365 GLN   A C   1 
ATOM   2902  O O   . GLN   A 1 365 ? -49.806 14.056  61.501  1.00 67.18  ?  365 GLN   A O   1 
ATOM   2903  C CB  . GLN   A 1 365 ? -49.260 14.328  64.553  1.00 56.13  ?  365 GLN   A CB  1 
ATOM   2904  C CG  . GLN   A 1 365 ? -47.860 14.918  64.455  1.00 56.69  ?  365 GLN   A CG  1 
ATOM   2905  C CD  . GLN   A 1 365 ? -46.824 14.124  65.229  1.00 63.60  ?  365 GLN   A CD  1 
ATOM   2906  O OE1 . GLN   A 1 365 ? -47.157 13.187  65.961  1.00 60.34  ?  365 GLN   A OE1 1 
ATOM   2907  N NE2 . GLN   A 1 365 ? -45.554 14.496  65.070  1.00 57.01  ?  365 GLN   A NE2 1 
ATOM   2908  N N   . ILE   A 1 366 ? -47.922 12.877  61.836  1.00 61.80  ?  366 ILE   A N   1 
ATOM   2909  C CA  . ILE   A 1 366 ? -47.365 13.126  60.508  1.00 62.19  ?  366 ILE   A CA  1 
ATOM   2910  C C   . ILE   A 1 366 ? -47.723 11.944  59.613  1.00 62.75  ?  366 ILE   A C   1 
ATOM   2911  O O   . ILE   A 1 366 ? -47.295 10.815  59.901  1.00 56.50  ?  366 ILE   A O   1 
ATOM   2912  C CB  . ILE   A 1 366 ? -45.846 13.328  60.565  1.00 56.88  ?  366 ILE   A CB  1 
ATOM   2913  C CG1 . ILE   A 1 366 ? -45.505 14.534  61.439  1.00 51.72  ?  366 ILE   A CG1 1 
ATOM   2914  C CG2 . ILE   A 1 366 ? -45.287 13.489  59.164  1.00 58.88  ?  366 ILE   A CG2 1 
ATOM   2915  C CD1 . ILE   A 1 366 ? -44.045 14.626  61.782  1.00 56.41  ?  366 ILE   A CD1 1 
ATOM   2916  N N   . PRO   A 1 367 ? -48.486 12.146  58.540  1.00 63.43  ?  367 PRO   A N   1 
ATOM   2917  C CA  . PRO   A 1 367 ? -48.859 11.022  57.673  1.00 60.86  ?  367 PRO   A CA  1 
ATOM   2918  C C   . PRO   A 1 367 ? -47.674 10.548  56.844  1.00 60.95  ?  367 PRO   A C   1 
ATOM   2919  O O   . PRO   A 1 367 ? -46.647 11.220  56.720  1.00 60.99  ?  367 PRO   A O   1 
ATOM   2920  C CB  . PRO   A 1 367 ? -49.971 11.599  56.795  1.00 57.65  ?  367 PRO   A CB  1 
ATOM   2921  C CG  . PRO   A 1 367 ? -49.690 13.067  56.761  1.00 64.90  ?  367 PRO   A CG  1 
ATOM   2922  C CD  . PRO   A 1 367 ? -49.090 13.416  58.099  1.00 62.79  ?  367 PRO   A CD  1 
ATOM   2923  N N   . GLY   A 1 368 ? -47.843 9.356   56.260  1.00 63.48  ?  368 GLY   A N   1 
ATOM   2924  C CA  . GLY   A 1 368 ? -46.737 8.691   55.588  1.00 59.25  ?  368 GLY   A CA  1 
ATOM   2925  C C   . GLY   A 1 368 ? -46.200 9.446   54.388  1.00 65.62  ?  368 GLY   A C   1 
ATOM   2926  O O   . GLY   A 1 368 ? -45.006 9.361   54.084  1.00 57.11  ?  368 GLY   A O   1 
ATOM   2927  N N   . ASP   A 1 369 ? -47.067 10.191  53.689  1.00 61.27  ?  369 ASP   A N   1 
ATOM   2928  C CA  . ASP   A 1 369 ? -46.630 10.972  52.534  1.00 60.87  ?  369 ASP   A CA  1 
ATOM   2929  C C   . ASP   A 1 369 ? -45.739 12.145  52.929  1.00 60.84  ?  369 ASP   A C   1 
ATOM   2930  O O   . ASP   A 1 369 ? -45.026 12.685  52.073  1.00 56.61  ?  369 ASP   A O   1 
ATOM   2931  C CB  . ASP   A 1 369 ? -47.845 11.475  51.744  1.00 63.35  ?  369 ASP   A CB  1 
ATOM   2932  C CG  . ASP   A 1 369 ? -48.850 12.217  52.612  1.00 63.61  ?  369 ASP   A CG  1 
ATOM   2933  O OD1 . ASP   A 1 369 ? -48.839 12.012  53.843  1.00 65.03  ?  369 ASP   A OD1 1 
ATOM   2934  O OD2 . ASP   A 1 369 ? -49.661 12.997  52.062  1.00 67.17  ?  369 ASP   A OD2 1 
ATOM   2935  N N   . GLN   A 1 370 ? -45.763 12.548  54.200  1.00 59.78  ?  370 GLN   A N   1 
ATOM   2936  C CA  . GLN   A 1 370 ? -44.878 13.580  54.719  1.00 59.31  ?  370 GLN   A CA  1 
ATOM   2937  C C   . GLN   A 1 370 ? -43.660 12.995  55.431  1.00 56.66  ?  370 GLN   A C   1 
ATOM   2938  O O   . GLN   A 1 370 ? -42.927 13.733  56.101  1.00 54.79  ?  370 GLN   A O   1 
ATOM   2939  C CB  . GLN   A 1 370 ? -45.656 14.513  55.648  1.00 58.43  ?  370 GLN   A CB  1 
ATOM   2940  C CG  . GLN   A 1 370 ? -46.933 15.044  55.007  1.00 61.41  ?  370 GLN   A CG  1 
ATOM   2941  C CD  . GLN   A 1 370 ? -47.507 16.242  55.733  1.00 62.87  ?  370 GLN   A CD  1 
ATOM   2942  O OE1 . GLN   A 1 370 ? -47.037 16.619  56.810  1.00 67.34  ?  370 GLN   A OE1 1 
ATOM   2943  N NE2 . GLN   A 1 370 ? -48.525 16.855  55.142  1.00 59.75  ?  370 GLN   A NE2 1 
ATOM   2944  N N   . PHE   A 1 371 ? -43.431 11.685  55.291  1.00 49.54  ?  371 PHE   A N   1 
ATOM   2945  C CA  . PHE   A 1 371 ? -42.244 10.985  55.770  1.00 54.29  ?  371 PHE   A CA  1 
ATOM   2946  C C   . PHE   A 1 371 ? -42.065 11.174  57.274  1.00 53.01  ?  371 PHE   A C   1 
ATOM   2947  O O   . PHE   A 1 371 ? -41.247 11.997  57.714  1.00 47.90  ?  371 PHE   A O   1 
ATOM   2948  C CB  . PHE   A 1 371 ? -41.008 11.456  54.997  1.00 52.21  ?  371 PHE   A CB  1 
ATOM   2949  C CG  . PHE   A 1 371 ? -41.231 11.551  53.512  1.00 54.02  ?  371 PHE   A CG  1 
ATOM   2950  C CD1 . PHE   A 1 371 ? -41.535 10.418  52.771  1.00 53.06  ?  371 PHE   A CD1 1 
ATOM   2951  C CD2 . PHE   A 1 371 ? -41.148 12.774  52.858  1.00 55.31  ?  371 PHE   A CD2 1 
ATOM   2952  C CE1 . PHE   A 1 371 ? -41.755 10.499  51.404  1.00 57.88  ?  371 PHE   A CE1 1 
ATOM   2953  C CE2 . PHE   A 1 371 ? -41.361 12.863  51.489  1.00 52.22  ?  371 PHE   A CE2 1 
ATOM   2954  C CZ  . PHE   A 1 371 ? -41.665 11.724  50.762  1.00 55.81  ?  371 PHE   A CZ  1 
ATOM   2955  N N   . PRO   A 1 372 ? -42.817 10.428  58.091  1.00 47.64  ?  372 PRO   A N   1 
ATOM   2956  C CA  . PRO   A 1 372 ? -42.648 10.556  59.548  1.00 43.59  ?  372 PRO   A CA  1 
ATOM   2957  C C   . PRO   A 1 372 ? -41.284 10.097  60.029  1.00 42.93  ?  372 PRO   A C   1 
ATOM   2958  O O   . PRO   A 1 372 ? -40.679 10.756  60.884  1.00 43.83  ?  372 PRO   A O   1 
ATOM   2959  C CB  . PRO   A 1 372 ? -43.776 9.676   60.100  1.00 51.01  ?  372 PRO   A CB  1 
ATOM   2960  C CG  . PRO   A 1 372 ? -44.018 8.663   59.020  1.00 50.67  ?  372 PRO   A CG  1 
ATOM   2961  C CD  . PRO   A 1 372 ? -43.796 9.390   57.728  1.00 48.79  ?  372 PRO   A CD  1 
ATOM   2962  N N   . ALA   A 1 373 ? -40.772 8.989   59.489  1.00 40.27  ?  373 ALA   A N   1 
ATOM   2963  C CA  . ALA   A 1 373 ? -39.468 8.500   59.919  1.00 39.09  ?  373 ALA   A CA  1 
ATOM   2964  C C   . ALA   A 1 373 ? -38.351 9.471   59.554  1.00 39.75  ?  373 ALA   A C   1 
ATOM   2965  O O   . ALA   A 1 373 ? -37.386 9.615   60.313  1.00 40.38  ?  373 ALA   A O   1 
ATOM   2966  C CB  . ALA   A 1 373 ? -39.206 7.121   59.317  1.00 39.98  ?  373 ALA   A CB  1 
ATOM   2967  N N   . GLN   A 1 374 ? -38.461 10.154  58.413  1.00 38.76  ?  374 GLN   A N   1 
ATOM   2968  C CA  . GLN   A 1 374 ? -37.425 11.113  58.048  1.00 37.17  ?  374 GLN   A CA  1 
ATOM   2969  C C   . GLN   A 1 374 ? -37.463 12.341  58.945  1.00 38.77  ?  374 GLN   A C   1 
ATOM   2970  O O   . GLN   A 1 374 ? -36.431 13.000  59.141  1.00 38.45  ?  374 GLN   A O   1 
ATOM   2971  C CB  . GLN   A 1 374 ? -37.559 11.528  56.586  1.00 37.46  ?  374 GLN   A CB  1 
ATOM   2972  C CG  . GLN   A 1 374 ? -36.344 12.299  56.088  1.00 40.49  ?  374 GLN   A CG  1 
ATOM   2973  C CD  . GLN   A 1 374 ? -35.060 11.508  56.240  1.00 37.93  ?  374 GLN   A CD  1 
ATOM   2974  O OE1 . GLN   A 1 374 ? -34.924 10.424  55.673  1.00 39.26  ?  374 GLN   A OE1 1 
ATOM   2975  N NE2 . GLN   A 1 374 ? -34.112 12.040  57.013  1.00 33.35  ?  374 GLN   A NE2 1 
ATOM   2976  N N   . ALA   A 1 375 ? -38.632 12.663  59.497  1.00 35.82  ?  375 ALA   A N   1 
ATOM   2977  C CA  . ALA   A 1 375 ? -38.719 13.755  60.457  1.00 37.72  ?  375 ALA   A CA  1 
ATOM   2978  C C   . ALA   A 1 375 ? -38.071 13.376  61.778  1.00 35.05  ?  375 ALA   A C   1 
ATOM   2979  O O   . ALA   A 1 375 ? -37.477 14.229  62.447  1.00 37.30  ?  375 ALA   A O   1 
ATOM   2980  C CB  . ALA   A 1 375 ? -40.181 14.148  60.672  1.00 39.83  ?  375 ALA   A CB  1 
ATOM   2981  N N   . VAL   A 1 376 ? -38.171 12.105  62.167  1.00 37.64  ?  376 VAL   A N   1 
ATOM   2982  C CA  . VAL   A 1 376 ? -37.504 11.648  63.380  1.00 34.47  ?  376 VAL   A CA  1 
ATOM   2983  C C   . VAL   A 1 376 ? -35.998 11.597  63.166  1.00 31.24  ?  376 VAL   A C   1 
ATOM   2984  O O   . VAL   A 1 376 ? -35.220 11.913  64.072  1.00 28.69  ?  376 VAL   A O   1 
ATOM   2985  C CB  . VAL   A 1 376 ? -38.070 10.283  63.815  1.00 37.44  ?  376 VAL   A CB  1 
ATOM   2986  C CG1 . VAL   A 1 376 ? -37.335 9.750   65.042  1.00 39.31  ?  376 VAL   A CG1 1 
ATOM   2987  C CG2 . VAL   A 1 376 ? -39.566 10.395  64.093  1.00 35.10  ?  376 VAL   A CG2 1 
ATOM   2988  N N   . ILE   A 1 377 ? -35.562 11.224  61.960  1.00 31.56  ?  377 ILE   A N   1 
ATOM   2989  C CA  . ILE   A 1 377 ? -34.129 11.098  61.687  1.00 29.65  ?  377 ILE   A CA  1 
ATOM   2990  C C   . ILE   A 1 377 ? -33.439 12.452  61.776  1.00 31.68  ?  377 ILE   A C   1 
ATOM   2991  O O   . ILE   A 1 377 ? -32.376 12.583  62.395  1.00 30.34  ?  377 ILE   A O   1 
ATOM   2992  C CB  . ILE   A 1 377 ? -33.893 10.450  60.315  1.00 31.99  ?  377 ILE   A CB  1 
ATOM   2993  C CG1 . ILE   A 1 377 ? -34.167 8.954   60.392  1.00 31.12  ?  377 ILE   A CG1 1 
ATOM   2994  C CG2 . ILE   A 1 377 ? -32.475 10.731  59.836  1.00 29.74  ?  377 ILE   A CG2 1 
ATOM   2995  C CD1 . ILE   A 1 377 ? -34.613 8.356   59.101  1.00 33.52  ?  377 ILE   A CD1 1 
ATOM   2996  N N   . ASN   A 1 378 ? -34.015 13.472  61.131  1.00 30.71  ?  378 ASN   A N   1 
ATOM   2997  C CA  . ASN   A 1 378 ? -33.421 14.804  61.176  1.00 31.95  ?  378 ASN   A CA  1 
ATOM   2998  C C   . ASN   A 1 378 ? -33.445 15.370  62.588  1.00 32.64  ?  378 ASN   A C   1 
ATOM   2999  O O   . ASN   A 1 378 ? -32.538 16.116  62.978  1.00 34.59  ?  378 ASN   A O   1 
ATOM   3000  C CB  . ASN   A 1 378 ? -34.151 15.733  60.205  1.00 31.95  ?  378 ASN   A CB  1 
ATOM   3001  C CG  . ASN   A 1 378 ? -34.112 15.222  58.774  1.00 37.36  ?  378 ASN   A CG  1 
ATOM   3002  O OD1 . ASN   A 1 378 ? -33.383 14.278  58.466  1.00 37.86  ?  378 ASN   A OD1 1 
ATOM   3003  N ND2 . ASN   A 1 378 ? -34.889 15.843  57.893  1.00 36.07  ?  378 ASN   A ND2 1 
ATOM   3004  N N   . ALA   A 1 379 ? -34.462 15.014  63.373  1.00 30.78  ?  379 ALA   A N   1 
ATOM   3005  C CA  . ALA   A 1 379 ? -34.492 15.434  64.768  1.00 34.68  ?  379 ALA   A CA  1 
ATOM   3006  C C   . ALA   A 1 379 ? -33.394 14.744  65.566  1.00 30.78  ?  379 ALA   A C   1 
ATOM   3007  O O   . ALA   A 1 379 ? -32.728 15.379  66.392  1.00 31.49  ?  379 ALA   A O   1 
ATOM   3008  C CB  . ALA   A 1 379 ? -35.873 15.155  65.366  1.00 30.64  ?  379 ALA   A CB  1 
ATOM   3009  N N   . LEU   A 1 380 ? -33.176 13.449  65.320  1.00 31.75  ?  380 LEU   A N   1 
ATOM   3010  C CA  . LEU   A 1 380 ? -32.082 12.740  65.979  1.00 30.37  ?  380 LEU   A CA  1 
ATOM   3011  C C   . LEU   A 1 380 ? -30.724 13.314  65.603  1.00 28.95  ?  380 LEU   A C   1 
ATOM   3012  O O   . LEU   A 1 380 ? -29.797 13.298  66.422  1.00 27.96  ?  380 LEU   A O   1 
ATOM   3013  C CB  . LEU   A 1 380 ? -32.135 11.254  65.632  1.00 25.99  ?  380 LEU   A CB  1 
ATOM   3014  C CG  . LEU   A 1 380 ? -31.007 10.391  66.198  1.00 31.94  ?  380 LEU   A CG  1 
ATOM   3015  C CD1 . LEU   A 1 380 ? -31.011 10.428  67.723  1.00 33.74  ?  380 LEU   A CD1 1 
ATOM   3016  C CD2 . LEU   A 1 380 ? -31.106 8.957   65.690  1.00 30.35  ?  380 LEU   A CD2 1 
ATOM   3017  N N   . TYR   A 1 381 ? -30.576 13.824  64.377  1.00 32.20  ?  381 TYR   A N   1 
ATOM   3018  C CA  . TYR   A 1 381 ? -29.283 14.363  63.962  1.00 30.93  ?  381 TYR   A CA  1 
ATOM   3019  C C   . TYR   A 1 381 ? -28.999 15.693  64.641  1.00 31.36  ?  381 TYR   A C   1 
ATOM   3020  O O   . TYR   A 1 381 ? -27.954 15.865  65.274  1.00 32.62  ?  381 TYR   A O   1 
ATOM   3021  C CB  . TYR   A 1 381 ? -29.216 14.538  62.448  1.00 25.59  ?  381 TYR   A CB  1 
ATOM   3022  C CG  . TYR   A 1 381 ? -28.001 15.337  62.037  1.00 35.31  ?  381 TYR   A CG  1 
ATOM   3023  C CD1 . TYR   A 1 381 ? -26.725 14.787  62.114  1.00 30.32  ?  381 TYR   A CD1 1 
ATOM   3024  C CD2 . TYR   A 1 381 ? -28.123 16.649  61.588  1.00 38.21  ?  381 TYR   A CD2 1 
ATOM   3025  C CE1 . TYR   A 1 381 ? -25.608 15.520  61.752  1.00 33.58  ?  381 TYR   A CE1 1 
ATOM   3026  C CE2 . TYR   A 1 381 ? -27.009 17.388  61.218  1.00 34.66  ?  381 TYR   A CE2 1 
ATOM   3027  C CZ  . TYR   A 1 381 ? -25.756 16.817  61.302  1.00 33.30  ?  381 TYR   A CZ  1 
ATOM   3028  O OH  . TYR   A 1 381 ? -24.648 17.549  60.938  1.00 35.75  ?  381 TYR   A OH  1 
ATOM   3029  N N   . LEU   A 1 382 ? -29.913 16.657  64.494  1.00 34.13  ?  382 LEU   A N   1 
ATOM   3030  C CA  . LEU   A 1 382 ? -29.733 17.955  65.138  1.00 35.45  ?  382 LEU   A CA  1 
ATOM   3031  C C   . LEU   A 1 382 ? -29.529 17.804  66.638  1.00 40.13  ?  382 LEU   A C   1 
ATOM   3032  O O   . LEU   A 1 382 ? -28.752 18.550  67.247  1.00 43.64  ?  382 LEU   A O   1 
ATOM   3033  C CB  . LEU   A 1 382 ? -30.937 18.853  64.862  1.00 34.78  ?  382 LEU   A CB  1 
ATOM   3034  C CG  . LEU   A 1 382 ? -31.167 19.208  63.400  1.00 36.81  ?  382 LEU   A CG  1 
ATOM   3035  C CD1 . LEU   A 1 382 ? -32.417 20.054  63.261  1.00 41.35  ?  382 LEU   A CD1 1 
ATOM   3036  C CD2 . LEU   A 1 382 ? -29.950 19.923  62.835  1.00 37.60  ?  382 LEU   A CD2 1 
ATOM   3037  N N   . GLU   A 1 383 ? -30.204 16.827  67.246  1.00 38.26  ?  383 GLU   A N   1 
ATOM   3038  C CA  . GLU   A 1 383 ? -30.112 16.643  68.689  1.00 37.09  ?  383 GLU   A CA  1 
ATOM   3039  C C   . GLU   A 1 383 ? -28.764 16.075  69.113  1.00 35.04  ?  383 GLU   A C   1 
ATOM   3040  O O   . GLU   A 1 383 ? -28.292 16.376  70.214  1.00 37.82  ?  383 GLU   A O   1 
ATOM   3041  C CB  . GLU   A 1 383 ? -31.246 15.733  69.164  1.00 37.90  ?  383 GLU   A CB  1 
ATOM   3042  C CG  . GLU   A 1 383 ? -31.217 15.405  70.648  1.00 42.51  ?  383 GLU   A CG  1 
ATOM   3043  C CD  . GLU   A 1 383 ? -31.555 16.600  71.521  1.00 53.63  ?  383 GLU   A CD  1 
ATOM   3044  O OE1 . GLU   A 1 383 ? -32.194 17.558  71.016  1.00 52.88  ?  383 GLU   A OE1 1 
ATOM   3045  O OE2 . GLU   A 1 383 ? -31.180 16.578  72.715  1.00 54.08  ?  383 GLU   A OE2 1 
ATOM   3046  N N   . SER   A 1 384 ? -28.119 15.269  68.265  1.00 36.23  ?  384 SER   A N   1 
ATOM   3047  C CA  . SER   A 1 384 ? -26.984 14.486  68.740  1.00 31.22  ?  384 SER   A CA  1 
ATOM   3048  C C   . SER   A 1 384 ? -25.847 14.293  67.752  1.00 34.62  ?  384 SER   A C   1 
ATOM   3049  O O   . SER   A 1 384 ? -24.782 13.829  68.177  1.00 36.87  ?  384 SER   A O   1 
ATOM   3050  C CB  . SER   A 1 384 ? -27.462 13.099  69.183  1.00 33.76  ?  384 SER   A CB  1 
ATOM   3051  O OG  . SER   A 1 384 ? -28.032 12.412  68.083  1.00 33.44  ?  384 SER   A OG  1 
ATOM   3052  N N   . GLY   A 1 385 ? -26.016 14.597  66.467  1.00 35.85  ?  385 GLY   A N   1 
ATOM   3053  C CA  . GLY   A 1 385 ? -24.972 14.318  65.499  1.00 34.72  ?  385 GLY   A CA  1 
ATOM   3054  C C   . GLY   A 1 385 ? -24.906 12.885  65.013  1.00 28.89  ?  385 GLY   A C   1 
ATOM   3055  O O   . GLY   A 1 385 ? -23.997 12.550  64.246  1.00 27.25  ?  385 GLY   A O   1 
ATOM   3056  N N   . VAL   A 1 386 ? -25.822 12.030  65.446  1.00 27.43  ?  386 VAL   A N   1 
ATOM   3057  C CA  . VAL   A 1 386 ? -25.954 10.680  64.910  1.00 27.77  ?  386 VAL   A CA  1 
ATOM   3058  C C   . VAL   A 1 386 ? -26.789 10.744  63.638  1.00 26.29  ?  386 VAL   A C   1 
ATOM   3059  O O   . VAL   A 1 386 ? -27.884 11.318  63.634  1.00 30.15  ?  386 VAL   A O   1 
ATOM   3060  C CB  . VAL   A 1 386 ? -26.597 9.752   65.958  1.00 29.03  ?  386 VAL   A CB  1 
ATOM   3061  C CG1 . VAL   A 1 386 ? -27.078 8.446   65.324  1.00 20.24  ?  386 VAL   A CG1 1 
ATOM   3062  C CG2 . VAL   A 1 386 ? -25.616 9.479   67.090  1.00 27.45  ?  386 VAL   A CG2 1 
ATOM   3063  N N   . ARG   A 1 387 ? -26.282 10.163  62.551  1.00 26.50  ?  387 ARG   A N   1 
ATOM   3064  C CA  . ARG   A 1 387 ? -26.995 10.143  61.276  1.00 23.76  ?  387 ARG   A CA  1 
ATOM   3065  C C   . ARG   A 1 387 ? -27.554 8.750   61.017  1.00 23.13  ?  387 ARG   A C   1 
ATOM   3066  O O   . ARG   A 1 387 ? -26.792 7.780   60.933  1.00 23.76  ?  387 ARG   A O   1 
ATOM   3067  C CB  . ARG   A 1 387 ? -26.087 10.559  60.121  1.00 21.62  ?  387 ARG   A CB  1 
ATOM   3068  C CG  . ARG   A 1 387 ? -26.696 10.236  58.762  1.00 23.84  ?  387 ARG   A CG  1 
ATOM   3069  C CD  . ARG   A 1 387 ? -25.950 10.891  57.612  1.00 29.06  ?  387 ARG   A CD  1 
ATOM   3070  N NE  . ARG   A 1 387 ? -24.569 10.436  57.476  1.00 21.46  ?  387 ARG   A NE  1 
ATOM   3071  C CZ  . ARG   A 1 387 ? -23.757 10.817  56.500  1.00 22.74  ?  387 ARG   A CZ  1 
ATOM   3072  N NH1 . ARG   A 1 387 ? -24.156 11.657  55.558  1.00 25.14  ?  387 ARG   A NH1 1 
ATOM   3073  N NH2 . ARG   A 1 387 ? -22.515 10.343  56.467  1.00 19.82  ?  387 ARG   A NH2 1 
ATOM   3074  N N   . ALA   A 1 388 ? -28.875 8.659   60.878  1.00 25.66  ?  388 ALA   A N   1 
ATOM   3075  C CA  . ALA   A 1 388 ? -29.574 7.429   60.534  1.00 24.91  ?  388 ALA   A CA  1 
ATOM   3076  C C   . ALA   A 1 388 ? -30.213 7.569   59.147  1.00 27.19  ?  388 ALA   A C   1 
ATOM   3077  O O   . ALA   A 1 388 ? -30.072 8.595   58.475  1.00 25.70  ?  388 ALA   A O   1 
ATOM   3078  C CB  . ALA   A 1 388 ? -30.607 7.089   61.609  1.00 20.85  ?  388 ALA   A CB  1 
ATOM   3079  N N   . VAL   A 1 389 ? -30.926 6.521   58.712  1.00 27.13  ?  389 VAL   A N   1 
ATOM   3080  C CA  . VAL   A 1 389 ? -31.498 6.468   57.371  1.00 26.08  ?  389 VAL   A CA  1 
ATOM   3081  C C   . VAL   A 1 389 ? -32.943 5.993   57.452  1.00 30.64  ?  389 VAL   A C   1 
ATOM   3082  O O   . VAL   A 1 389 ? -33.343 5.307   58.394  1.00 27.90  ?  389 VAL   A O   1 
ATOM   3083  C CB  . VAL   A 1 389 ? -30.690 5.558   56.426  1.00 28.06  ?  389 VAL   A CB  1 
ATOM   3084  C CG1 . VAL   A 1 389 ? -30.941 4.088   56.746  1.00 25.29  ?  389 VAL   A CG1 1 
ATOM   3085  C CG2 . VAL   A 1 389 ? -31.015 5.870   54.972  1.00 30.83  ?  389 VAL   A CG2 1 
ATOM   3086  N N   . GLU   A 1 390 ? -33.724 6.362   56.435  1.00 37.60  ?  390 GLU   A N   1 
ATOM   3087  C CA  A GLU   A 1 390 ? -35.156 6.085   56.391  0.68 35.87  ?  390 GLU   A CA  1 
ATOM   3088  C CA  B GLU   A 1 390 ? -35.156 6.086   56.387  0.32 35.88  ?  390 GLU   A CA  1 
ATOM   3089  C C   . GLU   A 1 390 ? -35.425 4.837   55.559  1.00 34.17  ?  390 GLU   A C   1 
ATOM   3090  O O   . GLU   A 1 390 ? -34.943 4.720   54.428  1.00 40.80  ?  390 GLU   A O   1 
ATOM   3091  C CB  A GLU   A 1 390 ? -35.918 7.281   55.815  0.68 37.87  ?  390 GLU   A CB  1 
ATOM   3092  C CB  B GLU   A 1 390 ? -35.917 7.275   55.795  0.32 37.89  ?  390 GLU   A CB  1 
ATOM   3093  C CG  A GLU   A 1 390 ? -37.412 7.288   56.112  0.68 40.93  ?  390 GLU   A CG  1 
ATOM   3094  C CG  B GLU   A 1 390 ? -37.304 7.479   56.378  0.32 40.45  ?  390 GLU   A CG  1 
ATOM   3095  C CD  A GLU   A 1 390 ? -38.253 6.803   54.946  0.68 45.16  ?  390 GLU   A CD  1 
ATOM   3096  C CD  B GLU   A 1 390 ? -38.364 7.730   55.321  0.32 43.52  ?  390 GLU   A CD  1 
ATOM   3097  O OE1 A GLU   A 1 390 ? -37.668 6.312   53.957  0.68 42.70  ?  390 GLU   A OE1 1 
ATOM   3098  O OE1 B GLU   A 1 390 ? -38.590 6.833   54.481  0.32 45.00  ?  390 GLU   A OE1 1 
ATOM   3099  O OE2 A GLU   A 1 390 ? -39.499 6.915   55.021  0.68 45.45  ?  390 GLU   A OE2 1 
ATOM   3100  O OE2 B GLU   A 1 390 ? -38.972 8.822   55.329  0.32 42.30  ?  390 GLU   A OE2 1 
ATOM   3101  N N   . ILE   A 1 391 ? -36.191 3.906   56.124  1.00 37.48  ?  391 ILE   A N   1 
ATOM   3102  C CA  . ILE   A 1 391 ? -36.599 2.703   55.409  1.00 40.84  ?  391 ILE   A CA  1 
ATOM   3103  C C   . ILE   A 1 391 ? -38.118 2.674   55.413  1.00 44.03  ?  391 ILE   A C   1 
ATOM   3104  O O   . ILE   A 1 391 ? -38.739 1.830   56.070  1.00 41.83  ?  391 ILE   A O   1 
ATOM   3105  C CB  . ILE   A 1 391 ? -36.012 1.423   56.033  1.00 40.70  ?  391 ILE   A CB  1 
ATOM   3106  C CG1 . ILE   A 1 391 ? -34.516 1.584   56.286  1.00 32.70  ?  391 ILE   A CG1 1 
ATOM   3107  C CG2 . ILE   A 1 391 ? -36.253 0.216   55.123  1.00 37.07  ?  391 ILE   A CG2 1 
ATOM   3108  C CD1 . ILE   A 1 391 ? -33.696 1.693   55.042  1.00 33.09  ?  391 ILE   A CD1 1 
ATOM   3109  N N   . GLY   A 1 392 ? -38.727 3.612   54.695  1.00 48.50  ?  392 GLY   A N   1 
ATOM   3110  C CA  . GLY   A 1 392 ? -40.168 3.701   54.661  1.00 48.93  ?  392 GLY   A CA  1 
ATOM   3111  C C   . GLY   A 1 392 ? -40.690 4.290   53.372  1.00 51.98  ?  392 GLY   A C   1 
ATOM   3112  O O   . GLY   A 1 392 ? -40.405 3.777   52.285  1.00 49.55  ?  392 GLY   A O   1 
ATOM   3113  N N   . SER   A 1 393 ? -41.447 5.384   53.490  1.00 60.68  ?  393 SER   A N   1 
ATOM   3114  C CA  . SER   A 1 393 ? -42.117 5.970   52.332  1.00 61.33  ?  393 SER   A CA  1 
ATOM   3115  C C   . SER   A 1 393 ? -41.128 6.658   51.400  1.00 61.60  ?  393 SER   A C   1 
ATOM   3116  O O   . SER   A 1 393 ? -41.233 6.538   50.173  1.00 68.76  ?  393 SER   A O   1 
ATOM   3117  C CB  . SER   A 1 393 ? -43.181 6.959   52.803  1.00 59.96  ?  393 SER   A CB  1 
ATOM   3118  O OG  . SER   A 1 393 ? -42.650 7.814   53.801  1.00 66.14  ?  393 SER   A OG  1 
ATOM   3119  N N   . PHE   A 1 394 ? -40.176 7.397   51.970  1.00 56.62  ?  394 PHE   A N   1 
ATOM   3120  C CA  . PHE   A 1 394 ? -39.174 8.091   51.170  1.00 47.72  ?  394 PHE   A CA  1 
ATOM   3121  C C   . PHE   A 1 394 ? -38.414 7.114   50.278  1.00 49.54  ?  394 PHE   A C   1 
ATOM   3122  O O   . PHE   A 1 394 ? -38.303 7.320   49.064  1.00 50.07  ?  394 PHE   A O   1 
ATOM   3123  C CB  . PHE   A 1 394 ? -38.232 8.841   52.111  1.00 48.07  ?  394 PHE   A CB  1 
ATOM   3124  C CG  . PHE   A 1 394 ? -37.417 9.905   51.453  1.00 52.70  ?  394 PHE   A CG  1 
ATOM   3125  C CD1 . PHE   A 1 394 ? -37.795 10.436  50.235  1.00 48.23  ?  394 PHE   A CD1 1 
ATOM   3126  C CD2 . PHE   A 1 394 ? -36.255 10.371  52.058  1.00 50.49  ?  394 PHE   A CD2 1 
ATOM   3127  C CE1 . PHE   A 1 394 ? -37.031 11.418  49.631  1.00 52.35  ?  394 PHE   A CE1 1 
ATOM   3128  C CE2 . PHE   A 1 394 ? -35.488 11.352  51.458  1.00 46.18  ?  394 PHE   A CE2 1 
ATOM   3129  C CZ  . PHE   A 1 394 ? -35.879 11.878  50.244  1.00 48.35  ?  394 PHE   A CZ  1 
ATOM   3130  N N   . LEU   A 1 395 ? -37.917 6.021   50.862  1.00 45.66  ?  395 LEU   A N   1 
ATOM   3131  C CA  . LEU   A 1 395 ? -37.113 5.048   50.129  1.00 46.38  ?  395 LEU   A CA  1 
ATOM   3132  C C   . LEU   A 1 395 ? -37.931 4.202   49.158  1.00 61.04  ?  395 LEU   A C   1 
ATOM   3133  O O   . LEU   A 1 395 ? -37.351 3.610   48.239  1.00 63.78  ?  395 LEU   A O   1 
ATOM   3134  C CB  . LEU   A 1 395 ? -36.386 4.134   51.120  1.00 47.04  ?  395 LEU   A CB  1 
ATOM   3135  C CG  . LEU   A 1 395 ? -35.377 3.106   50.604  1.00 45.92  ?  395 LEU   A CG  1 
ATOM   3136  C CD1 . LEU   A 1 395 ? -34.216 3.013   51.567  1.00 42.70  ?  395 LEU   A CD1 1 
ATOM   3137  C CD2 . LEU   A 1 395 ? -36.012 1.739   50.430  1.00 45.36  ?  395 LEU   A CD2 1 
ATOM   3138  N N   . LEU   A 1 396 ? -39.256 4.131   49.330  1.00 60.95  ?  396 LEU   A N   1 
ATOM   3139  C CA  . LEU   A 1 396 ? -40.056 3.180   48.559  1.00 58.22  ?  396 LEU   A CA  1 
ATOM   3140  C C   . LEU   A 1 396 ? -40.249 3.616   47.111  1.00 61.10  ?  396 LEU   A C   1 
ATOM   3141  O O   . LEU   A 1 396 ? -40.417 2.763   46.231  1.00 58.15  ?  396 LEU   A O   1 
ATOM   3142  C CB  . LEU   A 1 396 ? -41.416 2.970   49.229  1.00 60.43  ?  396 LEU   A CB  1 
ATOM   3143  C CG  . LEU   A 1 396 ? -42.118 1.643   48.922  1.00 59.67  ?  396 LEU   A CG  1 
ATOM   3144  C CD1 . LEU   A 1 396 ? -41.192 0.456   49.192  1.00 49.15  ?  396 LEU   A CD1 1 
ATOM   3145  C CD2 . LEU   A 1 396 ? -43.404 1.515   49.728  1.00 59.75  ?  396 LEU   A CD2 1 
ATOM   3146  N N   . GLY   A 1 397 ? -40.231 4.918   46.843  1.00 71.90  ?  397 GLY   A N   1 
ATOM   3147  C CA  . GLY   A 1 397 ? -40.335 5.416   45.482  1.00 77.97  ?  397 GLY   A CA  1 
ATOM   3148  C C   . GLY   A 1 397 ? -41.674 5.155   44.817  1.00 76.79  ?  397 GLY   A C   1 
ATOM   3149  O O   . GLY   A 1 397 ? -42.723 5.470   45.375  1.00 80.50  ?  397 GLY   A O   1 
ATOM   3150  N N   . GLN   A 1 405 ? -47.928 8.030   45.333  1.00 80.55  ?  405 GLN   A N   1 
ATOM   3151  C CA  . GLN   A 1 405 ? -46.829 7.444   46.095  1.00 80.51  ?  405 GLN   A CA  1 
ATOM   3152  C C   . GLN   A 1 405 ? -47.125 6.001   46.501  1.00 79.76  ?  405 GLN   A C   1 
ATOM   3153  O O   . GLN   A 1 405 ? -48.214 5.693   46.985  1.00 88.26  ?  405 GLN   A O   1 
ATOM   3154  C CB  . GLN   A 1 405 ? -46.535 8.285   47.337  1.00 78.88  ?  405 GLN   A CB  1 
ATOM   3155  C CG  . GLN   A 1 405 ? -45.346 7.795   48.150  1.00 83.64  ?  405 GLN   A CG  1 
ATOM   3156  C CD  . GLN   A 1 405 ? -44.853 8.832   49.140  1.00 78.16  ?  405 GLN   A CD  1 
ATOM   3157  O OE1 . GLN   A 1 405 ? -44.575 8.519   50.298  1.00 76.92  ?  405 GLN   A OE1 1 
ATOM   3158  N NE2 . GLN   A 1 405 ? -44.736 10.076  48.685  1.00 77.76  ?  405 GLN   A NE2 1 
ATOM   3159  N N   . LYS   A 1 406 ? -46.140 5.125   46.303  1.00 80.12  ?  406 LYS   A N   1 
ATOM   3160  C CA  . LYS   A 1 406 ? -46.307 3.706   46.598  1.00 76.20  ?  406 LYS   A CA  1 
ATOM   3161  C C   . LYS   A 1 406 ? -46.591 3.492   48.084  1.00 76.23  ?  406 LYS   A C   1 
ATOM   3162  O O   . LYS   A 1 406 ? -45.925 4.072   48.947  1.00 79.46  ?  406 LYS   A O   1 
ATOM   3163  C CB  . LYS   A 1 406 ? -45.051 2.945   46.170  1.00 63.19  ?  406 LYS   A CB  1 
ATOM   3164  C CG  . LYS   A 1 406 ? -45.213 1.442   46.099  1.00 64.26  ?  406 LYS   A CG  1 
ATOM   3165  C CD  . LYS   A 1 406 ? -43.901 0.768   45.723  1.00 57.85  ?  406 LYS   A CD  1 
ATOM   3166  C CE  . LYS   A 1 406 ? -43.417 1.206   44.352  1.00 52.94  ?  406 LYS   A CE  1 
ATOM   3167  N NZ  . LYS   A 1 406 ? -42.097 0.592   44.007  1.00 51.68  ?  406 LYS   A NZ  1 
ATOM   3168  N N   . HIS   A 1 407 ? -47.584 2.651   48.381  1.00 70.77  ?  407 HIS   A N   1 
ATOM   3169  C CA  . HIS   A 1 407 ? -48.059 2.500   49.753  1.00 71.50  ?  407 HIS   A CA  1 
ATOM   3170  C C   . HIS   A 1 407 ? -47.072 1.695   50.593  1.00 68.61  ?  407 HIS   A C   1 
ATOM   3171  O O   . HIS   A 1 407 ? -46.631 0.613   50.191  1.00 64.04  ?  407 HIS   A O   1 
ATOM   3172  C CB  . HIS   A 1 407 ? -49.428 1.826   49.768  1.00 75.81  ?  407 HIS   A CB  1 
ATOM   3173  C CG  . HIS   A 1 407 ? -50.083 1.826   51.114  1.00 76.34  ?  407 HIS   A CG  1 
ATOM   3174  N ND1 . HIS   A 1 407 ? -50.837 2.885   51.573  1.00 79.76  ?  407 HIS   A ND1 1 
ATOM   3175  C CD2 . HIS   A 1 407 ? -50.091 0.901   52.103  1.00 73.65  ?  407 HIS   A CD2 1 
ATOM   3176  C CE1 . HIS   A 1 407 ? -51.285 2.610   52.785  1.00 83.66  ?  407 HIS   A CE1 1 
ATOM   3177  N NE2 . HIS   A 1 407 ? -50.847 1.412   53.130  1.00 81.81  ?  407 HIS   A NE2 1 
ATOM   3178  N N   . ALA   A 1 408 ? -46.745 2.218   51.773  1.00 70.70  ?  408 ALA   A N   1 
ATOM   3179  C CA  . ALA   A 1 408 ? -45.767 1.610   52.664  1.00 63.48  ?  408 ALA   A CA  1 
ATOM   3180  C C   . ALA   A 1 408 ? -46.463 0.893   53.812  1.00 59.38  ?  408 ALA   A C   1 
ATOM   3181  O O   . ALA   A 1 408 ? -47.397 1.426   54.419  1.00 59.45  ?  408 ALA   A O   1 
ATOM   3182  C CB  . ALA   A 1 408 ? -44.807 2.662   53.223  1.00 56.52  ?  408 ALA   A CB  1 
ATOM   3183  N N   . ASP   A 1 409 ? -46.000 -0.318  54.106  1.00 54.01  ?  409 ASP   A N   1 
ATOM   3184  C CA  . ASP   A 1 409 ? -46.501 -1.084  55.237  1.00 53.68  ?  409 ASP   A CA  1 
ATOM   3185  C C   . ASP   A 1 409 ? -45.663 -0.896  56.492  1.00 51.14  ?  409 ASP   A C   1 
ATOM   3186  O O   . ASP   A 1 409 ? -46.063 -1.363  57.564  1.00 55.06  ?  409 ASP   A O   1 
ATOM   3187  C CB  . ASP   A 1 409 ? -46.562 -2.571  54.878  1.00 48.95  ?  409 ASP   A CB  1 
ATOM   3188  C CG  . ASP   A 1 409 ? -47.716 -2.898  53.951  1.00 54.33  ?  409 ASP   A CG  1 
ATOM   3189  O OD1 . ASP   A 1 409 ? -48.875 -2.601  54.316  1.00 60.38  ?  409 ASP   A OD1 1 
ATOM   3190  O OD2 . ASP   A 1 409 ? -47.465 -3.439  52.853  1.00 58.69  ?  409 ASP   A OD2 1 
ATOM   3191  N N   . MET   A 1 410 ? -44.517 -0.231  56.382  1.00 51.81  ?  410 MET   A N   1 
ATOM   3192  C CA  . MET   A 1 410 ? -43.607 -0.032  57.502  1.00 49.36  ?  410 MET   A CA  1 
ATOM   3193  C C   . MET   A 1 410 ? -42.936 1.326   57.331  1.00 49.86  ?  410 MET   A C   1 
ATOM   3194  O O   . MET   A 1 410 ? -42.442 1.637   56.243  1.00 53.74  ?  410 MET   A O   1 
ATOM   3195  C CB  . MET   A 1 410 ? -42.560 -1.158  57.563  1.00 51.05  ?  410 MET   A CB  1 
ATOM   3196  C CG  . MET   A 1 410 ? -43.137 -2.584  57.669  1.00 50.85  ?  410 MET   A CG  1 
ATOM   3197  S SD  . MET   A 1 410 ? -42.038 -3.914  57.089  1.00 53.66  ?  410 MET   A SD  1 
ATOM   3198  C CE  . MET   A 1 410 ? -41.798 -3.444  55.370  1.00 39.47  ?  410 MET   A CE  1 
ATOM   3199  N N   . GLU   A 1 411 ? -42.928 2.131   58.393  1.00 47.71  ?  411 GLU   A N   1 
ATOM   3200  C CA  . GLU   A 1 411 ? -42.271 3.441   58.408  1.00 42.82  ?  411 GLU   A CA  1 
ATOM   3201  C C   . GLU   A 1 411 ? -41.139 3.397   59.433  1.00 44.33  ?  411 GLU   A C   1 
ATOM   3202  O O   . GLU   A 1 411 ? -41.336 3.736   60.603  1.00 44.08  ?  411 GLU   A O   1 
ATOM   3203  C CB  . GLU   A 1 411 ? -43.262 4.552   58.731  1.00 46.83  ?  411 GLU   A CB  1 
ATOM   3204  C CG  . GLU   A 1 411 ? -44.319 4.764   57.672  1.00 53.19  ?  411 GLU   A CG  1 
ATOM   3205  C CD  . GLU   A 1 411 ? -43.754 5.365   56.402  1.00 59.22  ?  411 GLU   A CD  1 
ATOM   3206  O OE1 . GLU   A 1 411 ? -42.656 5.969   56.462  1.00 56.70  ?  411 GLU   A OE1 1 
ATOM   3207  O OE2 . GLU   A 1 411 ? -44.410 5.232   55.344  1.00 59.24  ?  411 GLU   A OE2 1 
ATOM   3208  N N   . PHE   A 1 412 ? -39.949 3.005   58.981  1.00 42.01  ?  412 PHE   A N   1 
ATOM   3209  C CA  . PHE   A 1 412 ? -38.816 2.730   59.855  1.00 38.53  ?  412 PHE   A CA  1 
ATOM   3210  C C   . PHE   A 1 412 ? -37.769 3.835   59.778  1.00 34.24  ?  412 PHE   A C   1 
ATOM   3211  O O   . PHE   A 1 412 ? -37.456 4.340   58.694  1.00 32.90  ?  412 PHE   A O   1 
ATOM   3212  C CB  . PHE   A 1 412 ? -38.142 1.404   59.483  1.00 38.11  ?  412 PHE   A CB  1 
ATOM   3213  C CG  . PHE   A 1 412 ? -38.939 0.182   59.835  1.00 39.17  ?  412 PHE   A CG  1 
ATOM   3214  C CD1 . PHE   A 1 412 ? -39.781 0.177   60.932  1.00 38.18  ?  412 PHE   A CD1 1 
ATOM   3215  C CD2 . PHE   A 1 412 ? -38.826 -0.973  59.069  1.00 38.02  ?  412 PHE   A CD2 1 
ATOM   3216  C CE1 . PHE   A 1 412 ? -40.510 -0.959  61.257  1.00 43.30  ?  412 PHE   A CE1 1 
ATOM   3217  C CE2 . PHE   A 1 412 ? -39.546 -2.111  59.390  1.00 41.34  ?  412 PHE   A CE2 1 
ATOM   3218  C CZ  . PHE   A 1 412 ? -40.391 -2.106  60.483  1.00 38.86  ?  412 PHE   A CZ  1 
ATOM   3219  N N   . MET   A 1 413 ? -37.217 4.190   60.935  1.00 33.51  ?  413 MET   A N   1 
ATOM   3220  C CA  . MET   A 1 413 ? -35.902 4.808   61.018  1.00 30.37  ?  413 MET   A CA  1 
ATOM   3221  C C   . MET   A 1 413 ? -34.901 3.707   61.341  1.00 27.44  ?  413 MET   A C   1 
ATOM   3222  O O   . MET   A 1 413 ? -35.039 3.018   62.360  1.00 26.96  ?  413 MET   A O   1 
ATOM   3223  C CB  . MET   A 1 413 ? -35.838 5.902   62.084  1.00 30.43  ?  413 MET   A CB  1 
ATOM   3224  C CG  . MET   A 1 413 ? -34.395 6.225   62.476  1.00 29.07  ?  413 MET   A CG  1 
ATOM   3225  S SD  . MET   A 1 413 ? -34.170 7.528   63.706  1.00 32.52  ?  413 MET   A SD  1 
ATOM   3226  C CE  . MET   A 1 413 ? -34.886 6.776   65.169  1.00 31.09  ?  413 MET   A CE  1 
ATOM   3227  N N   . ARG   A 1 414 ? -33.903 3.542   60.480  1.00 25.75  ?  414 ARG   A N   1 
ATOM   3228  C CA  . ARG   A 1 414 ? -32.930 2.469   60.609  1.00 26.08  ?  414 ARG   A CA  1 
ATOM   3229  C C   . ARG   A 1 414 ? -31.666 2.994   61.282  1.00 22.46  ?  414 ARG   A C   1 
ATOM   3230  O O   . ARG   A 1 414 ? -30.994 3.887   60.753  1.00 21.29  ?  414 ARG   A O   1 
ATOM   3231  C CB  . ARG   A 1 414 ? -32.599 1.862   59.246  1.00 24.11  ?  414 ARG   A CB  1 
ATOM   3232  C CG  . ARG   A 1 414 ? -31.807 0.568   59.351  1.00 25.28  ?  414 ARG   A CG  1 
ATOM   3233  C CD  . ARG   A 1 414 ? -31.432 -0.004  57.992  1.00 23.09  ?  414 ARG   A CD  1 
ATOM   3234  N NE  . ARG   A 1 414 ? -30.375 0.750   57.331  1.00 27.61  ?  414 ARG   A NE  1 
ATOM   3235  C CZ  . ARG   A 1 414 ? -29.829 0.408   56.169  1.00 30.58  ?  414 ARG   A CZ  1 
ATOM   3236  N NH1 . ARG   A 1 414 ? -30.224 -0.671  55.511  1.00 27.98  ?  414 ARG   A NH1 1 
ATOM   3237  N NH2 . ARG   A 1 414 ? -28.865 1.167   55.654  1.00 25.97  ?  414 ARG   A NH2 1 
ATOM   3238  N N   . LEU   A 1 415 ? -31.348 2.438   62.444  1.00 21.55  ?  415 LEU   A N   1 
ATOM   3239  C CA  . LEU   A 1 415 ? -30.070 2.686   63.106  1.00 19.70  ?  415 LEU   A CA  1 
ATOM   3240  C C   . LEU   A 1 415 ? -29.145 1.549   62.684  1.00 20.95  ?  415 LEU   A C   1 
ATOM   3241  O O   . LEU   A 1 415 ? -29.133 0.478   63.288  1.00 20.06  ?  415 LEU   A O   1 
ATOM   3242  C CB  . LEU   A 1 415 ? -30.255 2.756   64.617  1.00 18.30  ?  415 LEU   A CB  1 
ATOM   3243  C CG  . LEU   A 1 415 ? -31.430 3.603   65.111  1.00 19.03  ?  415 LEU   A CG  1 
ATOM   3244  C CD1 . LEU   A 1 415 ? -31.730 3.339   66.583  1.00 19.73  ?  415 LEU   A CD1 1 
ATOM   3245  C CD2 . LEU   A 1 415 ? -31.155 5.075   64.887  1.00 25.21  ?  415 LEU   A CD2 1 
ATOM   3246  N N   . THR   A 1 416 ? -28.381 1.777   61.611  1.00 19.93  ?  416 THR   A N   1 
ATOM   3247  C CA  . THR   A 1 416 ? -27.594 0.727   60.971  1.00 17.31  ?  416 THR   A CA  1 
ATOM   3248  C C   . THR   A 1 416 ? -26.202 0.663   61.580  1.00 15.90  ?  416 THR   A C   1 
ATOM   3249  O O   . THR   A 1 416 ? -25.496 1.673   61.630  1.00 17.33  ?  416 THR   A O   1 
ATOM   3250  C CB  . THR   A 1 416 ? -27.484 0.969   59.468  1.00 18.44  ?  416 THR   A CB  1 
ATOM   3251  O OG1 . THR   A 1 416 ? -28.585 1.774   59.025  1.00 20.33  ?  416 THR   A OG1 1 
ATOM   3252  C CG2 . THR   A 1 416 ? -27.502 -0.356  58.726  1.00 17.14  ?  416 THR   A CG2 1 
ATOM   3253  N N   . ILE   A 1 417 ? -25.794 -0.532  61.999  1.00 18.72  ?  417 ILE   A N   1 
ATOM   3254  C CA  . ILE   A 1 417 ? -24.602 -0.725  62.825  1.00 19.32  ?  417 ILE   A CA  1 
ATOM   3255  C C   . ILE   A 1 417 ? -23.500 -1.342  61.976  1.00 16.20  ?  417 ILE   A C   1 
ATOM   3256  O O   . ILE   A 1 417 ? -23.616 -2.490  61.532  1.00 19.27  ?  417 ILE   A O   1 
ATOM   3257  C CB  . ILE   A 1 417 ? -24.901 -1.609  64.040  1.00 16.01  ?  417 ILE   A CB  1 
ATOM   3258  C CG1 . ILE   A 1 417 ? -26.051 -1.024  64.845  1.00 21.66  ?  417 ILE   A CG1 1 
ATOM   3259  C CG2 . ILE   A 1 417 ? -23.640 -1.785  64.900  1.00 18.95  ?  417 ILE   A CG2 1 
ATOM   3260  C CD1 . ILE   A 1 417 ? -25.821 0.403   65.272  1.00 21.72  ?  417 ILE   A CD1 1 
ATOM   3261  N N   . ALA   A 1 418 ? -22.419 -0.594  61.772  1.00 17.27  ?  418 ALA   A N   1 
ATOM   3262  C CA  . ALA   A 1 418 ? -21.254 -1.123  61.084  1.00 16.78  ?  418 ALA   A CA  1 
ATOM   3263  C C   . ALA   A 1 418 ? -20.604 -2.224  61.913  1.00 18.48  ?  418 ALA   A C   1 
ATOM   3264  O O   . ALA   A 1 418 ? -20.707 -2.247  63.142  1.00 19.36  ?  418 ALA   A O   1 
ATOM   3265  C CB  . ALA   A 1 418 ? -20.238 -0.011  60.823  1.00 15.46  ?  418 ALA   A CB  1 
ATOM   3266  N N   . ARG   A 1 419 ? -19.907 -3.132  61.231  1.00 15.37  ?  419 ARG   A N   1 
ATOM   3267  C CA  . ARG   A 1 419 ? -19.315 -4.288  61.897  1.00 15.06  ?  419 ARG   A CA  1 
ATOM   3268  C C   . ARG   A 1 419 ? -17.955 -3.947  62.496  1.00 14.90  ?  419 ARG   A C   1 
ATOM   3269  O O   . ARG   A 1 419 ? -17.039 -3.509  61.782  1.00 14.58  ?  419 ARG   A O   1 
ATOM   3270  C CB  . ARG   A 1 419 ? -19.184 -5.442  60.917  1.00 14.40  ?  419 ARG   A CB  1 
ATOM   3271  C CG  . ARG   A 1 419 ? -20.525 -5.969  60.472  1.00 14.00  ?  419 ARG   A CG  1 
ATOM   3272  C CD  . ARG   A 1 419 ? -20.390 -6.828  59.228  1.00 15.46  ?  419 ARG   A CD  1 
ATOM   3273  N NE  . ARG   A 1 419 ? -21.715 -7.126  58.704  1.00 17.16  ?  419 ARG   A NE  1 
ATOM   3274  C CZ  . ARG   A 1 419 ? -22.448 -6.250  58.036  1.00 16.41  ?  419 ARG   A CZ  1 
ATOM   3275  N NH1 . ARG   A 1 419 ? -21.979 -5.048  57.742  1.00 15.27  ?  419 ARG   A NH1 1 
ATOM   3276  N NH2 . ARG   A 1 419 ? -23.688 -6.580  57.676  1.00 16.69  ?  419 ARG   A NH2 1 
ATOM   3277  N N   . ARG   A 1 420 ? -17.841 -4.143  63.817  1.00 15.52  ?  420 ARG   A N   1 
ATOM   3278  C CA  . ARG   A 1 420 ? -16.589 -4.039  64.574  1.00 15.56  ?  420 ARG   A CA  1 
ATOM   3279  C C   . ARG   A 1 420 ? -16.057 -2.608  64.654  1.00 13.93  ?  420 ARG   A C   1 
ATOM   3280  O O   . ARG   A 1 420 ? -14.848 -2.407  64.789  1.00 17.06  ?  420 ARG   A O   1 
ATOM   3281  C CB  . ARG   A 1 420 ? -15.513 -4.975  64.005  1.00 15.03  ?  420 ARG   A CB  1 
ATOM   3282  C CG  . ARG   A 1 420 ? -15.969 -6.428  63.842  1.00 12.33  ?  420 ARG   A CG  1 
ATOM   3283  C CD  . ARG   A 1 420 ? -14.799 -7.374  63.637  1.00 12.32  ?  420 ARG   A CD  1 
ATOM   3284  N NE  . ARG   A 1 420 ? -14.118 -7.140  62.373  1.00 11.02  ?  420 ARG   A NE  1 
ATOM   3285  C CZ  . ARG   A 1 420 ? -13.500 -8.081  61.675  1.00 12.56  ?  420 ARG   A CZ  1 
ATOM   3286  N NH1 . ARG   A 1 420 ? -13.428 -9.330  62.109  1.00 15.05  ?  420 ARG   A NH1 1 
ATOM   3287  N NH2 . ARG   A 1 420 ? -12.960 -7.770  60.502  1.00 11.34  ?  420 ARG   A NH2 1 
ATOM   3288  N N   . VAL   A 1 421 ? -16.938 -1.606  64.619  1.00 14.99  ?  421 VAL   A N   1 
ATOM   3289  C CA  . VAL   A 1 421 ? -16.539 -0.202  64.549  1.00 12.44  ?  421 VAL   A CA  1 
ATOM   3290  C C   . VAL   A 1 421 ? -16.859 0.550   65.840  1.00 15.28  ?  421 VAL   A C   1 
ATOM   3291  O O   . VAL   A 1 421 ? -16.038 1.324   66.334  1.00 15.37  ?  421 VAL   A O   1 
ATOM   3292  C CB  . VAL   A 1 421 ? -17.190 0.493   63.335  1.00 17.46  ?  421 VAL   A CB  1 
ATOM   3293  C CG1 . VAL   A 1 421 ? -16.975 1.992   63.407  1.00 13.56  ?  421 VAL   A CG1 1 
ATOM   3294  C CG2 . VAL   A 1 421 ? -16.625 -0.079  62.045  1.00 12.89  ?  421 VAL   A CG2 1 
ATOM   3295  N N   . TYR   A 1 422 ? -18.067 0.379   66.371  1.00 14.51  ?  422 TYR   A N   1 
ATOM   3296  C CA  . TYR   A 1 422 ? -18.518 1.132   67.533  1.00 17.61  ?  422 TYR   A CA  1 
ATOM   3297  C C   . TYR   A 1 422 ? -18.669 0.207   68.734  1.00 17.85  ?  422 TYR   A C   1 
ATOM   3298  O O   . TYR   A 1 422 ? -18.997 -0.974  68.588  1.00 18.79  ?  422 TYR   A O   1 
ATOM   3299  C CB  . TYR   A 1 422 ? -19.850 1.844   67.246  1.00 16.11  ?  422 TYR   A CB  1 
ATOM   3300  C CG  . TYR   A 1 422 ? -19.769 2.857   66.124  1.00 15.19  ?  422 TYR   A CG  1 
ATOM   3301  C CD1 . TYR   A 1 422 ? -19.209 4.106   66.335  1.00 14.78  ?  422 TYR   A CD1 1 
ATOM   3302  C CD2 . TYR   A 1 422 ? -20.249 2.560   64.851  1.00 20.84  ?  422 TYR   A CD2 1 
ATOM   3303  C CE1 . TYR   A 1 422 ? -19.120 5.030   65.318  1.00 15.22  ?  422 TYR   A CE1 1 
ATOM   3304  C CE2 . TYR   A 1 422 ? -20.181 3.491   63.822  1.00 18.79  ?  422 TYR   A CE2 1 
ATOM   3305  C CZ  . TYR   A 1 422 ? -19.605 4.722   64.067  1.00 21.50  ?  422 TYR   A CZ  1 
ATOM   3306  O OH  . TYR   A 1 422 ? -19.508 5.657   63.060  1.00 23.29  ?  422 TYR   A OH  1 
ATOM   3307  N N   . THR   A 1 423 ? -18.421 0.752   69.925  1.00 17.01  ?  423 THR   A N   1 
ATOM   3308  C CA  . THR   A 1 423 ? -18.528 -0.009  71.160  1.00 18.95  ?  423 THR   A CA  1 
ATOM   3309  C C   . THR   A 1 423 ? -19.939 0.103   71.716  1.00 17.61  ?  423 THR   A C   1 
ATOM   3310  O O   . THR   A 1 423 ? -20.751 0.918   71.270  1.00 17.97  ?  423 THR   A O   1 
ATOM   3311  C CB  . THR   A 1 423 ? -17.511 0.473   72.211  1.00 21.80  ?  423 THR   A CB  1 
ATOM   3312  O OG1 . THR   A 1 423 ? -17.902 1.751   72.729  1.00 19.13  ?  423 THR   A OG1 1 
ATOM   3313  C CG2 . THR   A 1 423 ? -16.117 0.595   71.618  1.00 19.45  ?  423 THR   A CG2 1 
ATOM   3314  N N   . ASN   A 1 424 ? -20.235 -0.726  72.715  1.00 17.44  ?  424 ASN   A N   1 
ATOM   3315  C CA  . ASN   A 1 424 ? -21.534 -0.607  73.358  1.00 20.09  ?  424 ASN   A CA  1 
ATOM   3316  C C   . ASN   A 1 424 ? -21.684 0.737   74.053  1.00 18.65  ?  424 ASN   A C   1 
ATOM   3317  O O   . ASN   A 1 424 ? -22.810 1.172   74.312  1.00 23.25  ?  424 ASN   A O   1 
ATOM   3318  C CB  . ASN   A 1 424 ? -21.747 -1.761  74.339  1.00 23.56  ?  424 ASN   A CB  1 
ATOM   3319  C CG  . ASN   A 1 424 ? -21.960 -3.094  73.632  1.00 22.44  ?  424 ASN   A CG  1 
ATOM   3320  O OD1 . ASN   A 1 424 ? -22.614 -3.156  72.593  1.00 22.75  ?  424 ASN   A OD1 1 
ATOM   3321  N ND2 . ASN   A 1 424 ? -21.403 -4.160  74.190  1.00 23.75  ?  424 ASN   A ND2 1 
ATOM   3322  N N   . ASP   A 1 425 ? -20.574 1.419   74.334  1.00 19.99  ?  425 ASP   A N   1 
ATOM   3323  C CA  . ASP   A 1 425 ? -20.669 2.772   74.867  1.00 20.27  ?  425 ASP   A CA  1 
ATOM   3324  C C   . ASP   A 1 425 ? -21.119 3.762   73.798  1.00 21.68  ?  425 ASP   A C   1 
ATOM   3325  O O   . ASP   A 1 425 ? -21.828 4.725   74.111  1.00 22.80  ?  425 ASP   A O   1 
ATOM   3326  C CB  . ASP   A 1 425 ? -19.337 3.175   75.487  1.00 23.38  ?  425 ASP   A CB  1 
ATOM   3327  C CG  . ASP   A 1 425 ? -19.052 2.408   76.769  1.00 27.01  ?  425 ASP   A CG  1 
ATOM   3328  O OD1 . ASP   A 1 425 ? -20.032 2.015   77.447  1.00 27.21  ?  425 ASP   A OD1 1 
ATOM   3329  O OD2 . ASP   A 1 425 ? -17.865 2.187   77.091  1.00 26.95  ?  425 ASP   A OD2 1 
ATOM   3330  N N   . HIS   A 1 426 ? -20.737 3.542   72.538  1.00 20.63  ?  426 HIS   A N   1 
ATOM   3331  C CA  . HIS   A 1 426 ? -21.368 4.285   71.451  1.00 17.28  ?  426 HIS   A CA  1 
ATOM   3332  C C   . HIS   A 1 426 ? -22.857 3.964   71.370  1.00 17.36  ?  426 HIS   A C   1 
ATOM   3333  O O   . HIS   A 1 426 ? -23.675 4.851   71.110  1.00 19.58  ?  426 HIS   A O   1 
ATOM   3334  C CB  . HIS   A 1 426 ? -20.685 3.976   70.120  1.00 14.57  ?  426 HIS   A CB  1 
ATOM   3335  C CG  . HIS   A 1 426 ? -19.262 4.435   70.044  1.00 15.60  ?  426 HIS   A CG  1 
ATOM   3336  N ND1 . HIS   A 1 426 ? -18.220 3.578   69.758  1.00 14.69  ?  426 HIS   A ND1 1 
ATOM   3337  C CD2 . HIS   A 1 426 ? -18.708 5.661   70.199  1.00 16.33  ?  426 HIS   A CD2 1 
ATOM   3338  C CE1 . HIS   A 1 426 ? -17.085 4.254   69.753  1.00 16.21  ?  426 HIS   A CE1 1 
ATOM   3339  N NE2 . HIS   A 1 426 ? -17.352 5.519   70.027  1.00 15.90  ?  426 HIS   A NE2 1 
ATOM   3340  N N   . MET   A 1 427 ? -23.226 2.696   71.592  1.00 16.00  ?  427 MET   A N   1 
ATOM   3341  C CA  . MET   A 1 427 ? -24.635 2.315   71.561  1.00 18.58  ?  427 MET   A CA  1 
ATOM   3342  C C   . MET   A 1 427 ? -25.426 3.047   72.635  1.00 23.88  ?  427 MET   A C   1 
ATOM   3343  O O   . MET   A 1 427 ? -26.576 3.442   72.403  1.00 25.75  ?  427 MET   A O   1 
ATOM   3344  C CB  . MET   A 1 427 ? -24.792 0.800   71.734  1.00 15.80  ?  427 MET   A CB  1 
ATOM   3345  C CG  . MET   A 1 427 ? -24.160 -0.058  70.629  1.00 17.29  ?  427 MET   A CG  1 
ATOM   3346  S SD  . MET   A 1 427 ? -24.721 0.334   68.954  1.00 18.52  ?  427 MET   A SD  1 
ATOM   3347  C CE  . MET   A 1 427 ? -23.161 0.813   68.229  1.00 15.78  ?  427 MET   A CE  1 
ATOM   3348  N N   . ASP   A 1 428 ? -24.837 3.218   73.826  1.00 22.66  ?  428 ASP   A N   1 
ATOM   3349  C CA  . ASP   A 1 428 ? -25.523 3.944   74.897  1.00 25.06  ?  428 ASP   A CA  1 
ATOM   3350  C C   . ASP   A 1 428 ? -25.739 5.403   74.520  1.00 24.92  ?  428 ASP   A C   1 
ATOM   3351  O O   . ASP   A 1 428 ? -26.776 5.991   74.852  1.00 24.18  ?  428 ASP   A O   1 
ATOM   3352  C CB  . ASP   A 1 428 ? -24.727 3.858   76.202  1.00 20.50  ?  428 ASP   A CB  1 
ATOM   3353  C CG  . ASP   A 1 428 ? -24.849 2.509   76.885  1.00 21.66  ?  428 ASP   A CG  1 
ATOM   3354  O OD1 . ASP   A 1 428 ? -25.879 1.821   76.714  1.00 21.49  ?  428 ASP   A OD1 1 
ATOM   3355  O OD2 . ASP   A 1 428 ? -23.908 2.143   77.612  1.00 21.19  ?  428 ASP   A OD2 1 
ATOM   3356  N N   . TYR   A 1 429 ? -24.760 6.009   73.843  1.00 22.68  ?  429 TYR   A N   1 
ATOM   3357  C CA  . TYR   A 1 429 ? -24.925 7.378   73.370  1.00 23.67  ?  429 TYR   A CA  1 
ATOM   3358  C C   . TYR   A 1 429 ? -26.101 7.468   72.407  1.00 26.08  ?  429 TYR   A C   1 
ATOM   3359  O O   . TYR   A 1 429 ? -26.942 8.370   72.509  1.00 27.51  ?  429 TYR   A O   1 
ATOM   3360  C CB  . TYR   A 1 429 ? -23.630 7.867   72.703  1.00 24.62  ?  429 TYR   A CB  1 
ATOM   3361  C CG  . TYR   A 1 429 ? -23.728 9.266   72.125  1.00 22.75  ?  429 TYR   A CG  1 
ATOM   3362  C CD1 . TYR   A 1 429 ? -24.248 9.481   70.849  1.00 27.49  ?  429 TYR   A CD1 1 
ATOM   3363  C CD2 . TYR   A 1 429 ? -23.308 10.370  72.852  1.00 21.99  ?  429 TYR   A CD2 1 
ATOM   3364  C CE1 . TYR   A 1 429 ? -24.356 10.754  70.320  1.00 27.32  ?  429 TYR   A CE1 1 
ATOM   3365  C CE2 . TYR   A 1 429 ? -23.401 11.649  72.326  1.00 29.45  ?  429 TYR   A CE2 1 
ATOM   3366  C CZ  . TYR   A 1 429 ? -23.925 11.835  71.059  1.00 29.67  ?  429 TYR   A CZ  1 
ATOM   3367  O OH  . TYR   A 1 429 ? -24.024 13.104  70.531  1.00 30.73  ?  429 TYR   A OH  1 
ATOM   3368  N N   . ILE   A 1 430 ? -26.173 6.532   71.460  1.00 23.08  ?  430 ILE   A N   1 
ATOM   3369  C CA  . ILE   A 1 430 ? -27.263 6.528   70.491  1.00 23.43  ?  430 ILE   A CA  1 
ATOM   3370  C C   . ILE   A 1 430 ? -28.599 6.385   71.202  1.00 27.63  ?  430 ILE   A C   1 
ATOM   3371  O O   . ILE   A 1 430 ? -29.538 7.150   70.955  1.00 27.38  ?  430 ILE   A O   1 
ATOM   3372  C CB  . ILE   A 1 430 ? -27.053 5.406   69.461  1.00 25.53  ?  430 ILE   A CB  1 
ATOM   3373  C CG1 . ILE   A 1 430 ? -25.762 5.650   68.676  1.00 20.51  ?  430 ILE   A CG1 1 
ATOM   3374  C CG2 . ILE   A 1 430 ? -28.274 5.283   68.545  1.00 26.43  ?  430 ILE   A CG2 1 
ATOM   3375  C CD1 . ILE   A 1 430 ? -25.171 4.393   68.049  1.00 20.47  ?  430 ILE   A CD1 1 
ATOM   3376  N N   . ALA   A 1 431 ? -28.698 5.407   72.107  1.00 22.55  ?  431 ALA   A N   1 
ATOM   3377  C CA  . ALA   A 1 431 ? -29.963 5.153   72.789  1.00 26.66  ?  431 ALA   A CA  1 
ATOM   3378  C C   . ALA   A 1 431 ? -30.402 6.364   73.608  1.00 31.81  ?  431 ALA   A C   1 
ATOM   3379  O O   . ALA   A 1 431 ? -31.560 6.794   73.532  1.00 29.81  ?  431 ALA   A O   1 
ATOM   3380  C CB  . ALA   A 1 431 ? -29.839 3.914   73.682  1.00 28.45  ?  431 ALA   A CB  1 
ATOM   3381  N N   . ASP   A 1 432 ? -29.487 6.931   74.398  1.00 29.77  ?  432 ASP   A N   1 
ATOM   3382  C CA  . ASP   A 1 432 ? -29.857 8.065   75.238  1.00 32.22  ?  432 ASP   A CA  1 
ATOM   3383  C C   . ASP   A 1 432 ? -30.229 9.277   74.397  1.00 30.24  ?  432 ASP   A C   1 
ATOM   3384  O O   . ASP   A 1 432 ? -31.117 10.049  74.779  1.00 37.04  ?  432 ASP   A O   1 
ATOM   3385  C CB  . ASP   A 1 432 ? -28.719 8.395   76.205  1.00 34.78  ?  432 ASP   A CB  1 
ATOM   3386  C CG  . ASP   A 1 432 ? -28.407 7.245   77.141  1.00 28.14  ?  432 ASP   A CG  1 
ATOM   3387  O OD1 . ASP   A 1 432 ? -29.355 6.525   77.513  1.00 34.18  ?  432 ASP   A OD1 1 
ATOM   3388  O OD2 . ASP   A 1 432 ? -27.226 7.050   77.494  1.00 35.15  ?  432 ASP   A OD2 1 
ATOM   3389  N N   . ALA   A 1 433 ? -29.582 9.449   73.246  1.00 26.58  ?  433 ALA   A N   1 
ATOM   3390  C CA  . ALA   A 1 433 ? -29.974 10.514  72.329  1.00 30.66  ?  433 ALA   A CA  1 
ATOM   3391  C C   . ALA   A 1 433 ? -31.419 10.342  71.882  1.00 35.38  ?  433 ALA   A C   1 
ATOM   3392  O O   . ALA   A 1 433 ? -32.219 11.282  71.944  1.00 40.00  ?  433 ALA   A O   1 
ATOM   3393  C CB  . ALA   A 1 433 ? -29.038 10.532  71.120  1.00 30.48  ?  433 ALA   A CB  1 
ATOM   3394  N N   . LEU   A 1 434 ? -31.772 9.139   71.425  1.00 29.51  ?  434 LEU   A N   1 
ATOM   3395  C CA  . LEU   A 1 434 ? -33.117 8.912   70.915  1.00 32.84  ?  434 LEU   A CA  1 
ATOM   3396  C C   . LEU   A 1 434 ? -34.146 8.941   72.039  1.00 41.21  ?  434 LEU   A C   1 
ATOM   3397  O O   . LEU   A 1 434 ? -35.230 9.520   71.881  1.00 41.41  ?  434 LEU   A O   1 
ATOM   3398  C CB  . LEU   A 1 434 ? -33.170 7.586   70.165  1.00 30.26  ?  434 LEU   A CB  1 
ATOM   3399  C CG  . LEU   A 1 434 ? -34.517 7.278   69.523  1.00 35.21  ?  434 LEU   A CG  1 
ATOM   3400  C CD1 . LEU   A 1 434 ? -34.929 8.408   68.585  1.00 36.40  ?  434 LEU   A CD1 1 
ATOM   3401  C CD2 . LEU   A 1 434 ? -34.463 5.947   68.794  1.00 33.13  ?  434 LEU   A CD2 1 
ATOM   3402  N N   . ILE   A 1 435 ? -33.824 8.326   73.181  1.00 37.37  ?  435 ILE   A N   1 
ATOM   3403  C CA  . ILE   A 1 435 ? -34.726 8.360   74.328  1.00 39.47  ?  435 ILE   A CA  1 
ATOM   3404  C C   . ILE   A 1 435 ? -35.015 9.796   74.741  1.00 48.31  ?  435 ILE   A C   1 
ATOM   3405  O O   . ILE   A 1 435 ? -36.146 10.135  75.108  1.00 50.41  ?  435 ILE   A O   1 
ATOM   3406  C CB  . ILE   A 1 435 ? -34.138 7.554   75.499  1.00 36.94  ?  435 ILE   A CB  1 
ATOM   3407  C CG1 . ILE   A 1 435 ? -34.063 6.068   75.146  1.00 35.03  ?  435 ILE   A CG1 1 
ATOM   3408  C CG2 . ILE   A 1 435 ? -34.984 7.752   76.740  1.00 43.72  ?  435 ILE   A CG2 1 
ATOM   3409  C CD1 . ILE   A 1 435 ? -33.200 5.263   76.092  1.00 29.90  ?  435 ILE   A CD1 1 
ATOM   3410  N N   . GLY   A 1 436 ? -34.003 10.664  74.682  1.00 44.47  ?  436 GLY   A N   1 
ATOM   3411  C CA  . GLY   A 1 436 ? -34.147 12.044  75.105  1.00 46.39  ?  436 GLY   A CA  1 
ATOM   3412  C C   . GLY   A 1 436 ? -35.025 12.907  74.227  1.00 51.45  ?  436 GLY   A C   1 
ATOM   3413  O O   . GLY   A 1 436 ? -35.190 14.094  74.521  1.00 58.97  ?  436 GLY   A O   1 
ATOM   3414  N N   . LEU   A 1 437 ? -35.587 12.354  73.154  1.00 48.90  ?  437 LEU   A N   1 
ATOM   3415  C CA  . LEU   A 1 437 ? -36.496 13.083  72.278  1.00 56.17  ?  437 LEU   A CA  1 
ATOM   3416  C C   . LEU   A 1 437 ? -37.948 12.659  72.471  1.00 56.89  ?  437 LEU   A C   1 
ATOM   3417  O O   . LEU   A 1 437 ? -38.793 12.963  71.624  1.00 58.40  ?  437 LEU   A O   1 
ATOM   3418  C CB  . LEU   A 1 437 ? -36.083 12.899  70.816  1.00 49.73  ?  437 LEU   A CB  1 
ATOM   3419  C CG  . LEU   A 1 437 ? -34.759 13.529  70.378  1.00 46.18  ?  437 LEU   A CG  1 
ATOM   3420  C CD1 . LEU   A 1 437 ? -34.514 13.300  68.893  1.00 37.62  ?  437 LEU   A CD1 1 
ATOM   3421  C CD2 . LEU   A 1 437 ? -34.769 15.009  70.698  1.00 50.83  ?  437 LEU   A CD2 1 
ATOM   3422  N N   . LYS   A 1 438 ? -38.254 11.965  73.571  1.00 56.15  ?  438 LYS   A N   1 
ATOM   3423  C CA  . LYS   A 1 438 ? -39.579 11.371  73.726  1.00 61.89  ?  438 LYS   A CA  1 
ATOM   3424  C C   . LYS   A 1 438 ? -40.669 12.428  73.806  1.00 69.65  ?  438 LYS   A C   1 
ATOM   3425  O O   . LYS   A 1 438 ? -41.790 12.196  73.339  1.00 71.49  ?  438 LYS   A O   1 
ATOM   3426  C CB  . LYS   A 1 438 ? -39.610 10.467  74.959  1.00 62.56  ?  438 LYS   A CB  1 
ATOM   3427  C CG  . LYS   A 1 438 ? -39.159 9.033   74.676  1.00 60.34  ?  438 LYS   A CG  1 
ATOM   3428  C CD  . LYS   A 1 438 ? -38.947 8.224   75.958  1.00 61.24  ?  438 LYS   A CD  1 
ATOM   3429  C CE  . LYS   A 1 438 ? -40.202 8.189   76.822  1.00 70.66  ?  438 LYS   A CE  1 
ATOM   3430  N NZ  . LYS   A 1 438 ? -41.374 7.610   76.105  1.00 71.51  ?  438 LYS   A NZ  1 
ATOM   3431  N N   . GLU   A 1 439 ? -40.364 13.592  74.372  1.00 88.40  ?  439 GLU   A N   1 
ATOM   3432  C CA  . GLU   A 1 439 ? -41.350 14.655  74.504  1.00 90.23  ?  439 GLU   A CA  1 
ATOM   3433  C C   . GLU   A 1 439 ? -41.457 15.530  73.262  1.00 90.59  ?  439 GLU   A C   1 
ATOM   3434  O O   . GLU   A 1 439 ? -42.401 16.320  73.161  1.00 92.08  ?  439 GLU   A O   1 
ATOM   3435  C CB  . GLU   A 1 439 ? -41.022 15.535  75.718  1.00 91.27  ?  439 GLU   A CB  1 
ATOM   3436  C CG  . GLU   A 1 439 ? -39.842 16.483  75.517  1.00 91.15  ?  439 GLU   A CG  1 
ATOM   3437  C CD  . GLU   A 1 439 ? -38.497 15.772  75.477  1.00 95.88  ?  439 GLU   A CD  1 
ATOM   3438  O OE1 . GLU   A 1 439 ? -38.439 14.569  75.818  1.00 96.75  ?  439 GLU   A OE1 1 
ATOM   3439  O OE2 . GLU   A 1 439 ? -37.494 16.419  75.102  1.00 94.08  ?  439 GLU   A OE2 1 
ATOM   3440  N N   . LYS   A 1 440 ? -40.529 15.409  72.317  1.00 71.00  ?  440 LYS   A N   1 
ATOM   3441  C CA  . LYS   A 1 440 ? -40.512 16.264  71.139  1.00 67.01  ?  440 LYS   A CA  1 
ATOM   3442  C C   . LYS   A 1 440 ? -41.060 15.579  69.894  1.00 68.10  ?  440 LYS   A C   1 
ATOM   3443  O O   . LYS   A 1 440 ? -41.154 16.222  68.843  1.00 65.41  ?  440 LYS   A O   1 
ATOM   3444  C CB  . LYS   A 1 440 ? -39.089 16.762  70.881  1.00 64.67  ?  440 LYS   A CB  1 
ATOM   3445  C CG  . LYS   A 1 440 ? -38.488 17.495  72.066  1.00 64.23  ?  440 LYS   A CG  1 
ATOM   3446  C CD  . LYS   A 1 440 ? -37.111 18.037  71.742  1.00 60.80  ?  440 LYS   A CD  1 
ATOM   3447  C CE  . LYS   A 1 440 ? -36.489 18.706  72.955  1.00 64.61  ?  440 LYS   A CE  1 
ATOM   3448  N NZ  . LYS   A 1 440 ? -35.123 19.225  72.666  1.00 58.07  ?  440 LYS   A NZ  1 
ATOM   3449  N N   . PHE   A 1 441 ? -41.440 14.302  69.993  1.00 61.20  ?  441 PHE   A N   1 
ATOM   3450  C CA  . PHE   A 1 441 ? -41.956 13.576  68.835  1.00 57.44  ?  441 PHE   A CA  1 
ATOM   3451  C C   . PHE   A 1 441 ? -43.241 14.207  68.304  1.00 66.05  ?  441 PHE   A C   1 
ATOM   3452  O O   . PHE   A 1 441 ? -43.401 14.389  67.091  1.00 61.21  ?  441 PHE   A O   1 
ATOM   3453  C CB  . PHE   A 1 441 ? -42.181 12.110  69.207  1.00 50.60  ?  441 PHE   A CB  1 
ATOM   3454  C CG  . PHE   A 1 441 ? -40.909 11.353  69.467  1.00 57.09  ?  441 PHE   A CG  1 
ATOM   3455  C CD1 . PHE   A 1 441 ? -39.753 11.645  68.754  1.00 54.65  ?  441 PHE   A CD1 1 
ATOM   3456  C CD2 . PHE   A 1 441 ? -40.861 10.353  70.428  1.00 54.73  ?  441 PHE   A CD2 1 
ATOM   3457  C CE1 . PHE   A 1 441 ? -38.573 10.949  68.989  1.00 49.68  ?  441 PHE   A CE1 1 
ATOM   3458  C CE2 . PHE   A 1 441 ? -39.683 9.655   70.667  1.00 51.53  ?  441 PHE   A CE2 1 
ATOM   3459  C CZ  . PHE   A 1 441 ? -38.541 9.954   69.947  1.00 49.53  ?  441 PHE   A CZ  1 
ATOM   3460  N N   . ALA   A 1 442 ? -44.175 14.544  69.200  1.00 70.80  ?  442 ALA   A N   1 
ATOM   3461  C CA  . ALA   A 1 442 ? -45.410 15.194  68.773  1.00 65.40  ?  442 ALA   A CA  1 
ATOM   3462  C C   . ALA   A 1 442 ? -45.124 16.529  68.097  1.00 70.30  ?  442 ALA   A C   1 
ATOM   3463  O O   . ALA   A 1 442 ? -45.761 16.878  67.097  1.00 70.98  ?  442 ALA   A O   1 
ATOM   3464  C CB  . ALA   A 1 442 ? -46.342 15.385  69.968  1.00 63.65  ?  442 ALA   A CB  1 
ATOM   3465  N N   . THR   A 1 443 ? -44.156 17.282  68.622  1.00 80.01  ?  443 THR   A N   1 
ATOM   3466  C CA  . THR   A 1 443 ? -43.773 18.578  68.064  1.00 83.87  ?  443 THR   A CA  1 
ATOM   3467  C C   . THR   A 1 443 ? -42.767 18.395  66.924  1.00 85.43  ?  443 THR   A C   1 
ATOM   3468  O O   . THR   A 1 443 ? -41.636 18.879  66.959  1.00 87.16  ?  443 THR   A O   1 
ATOM   3469  C CB  . THR   A 1 443 ? -43.202 19.468  69.160  1.00 87.16  ?  443 THR   A CB  1 
ATOM   3470  O OG1 . THR   A 1 443 ? -43.945 19.267  70.368  1.00 88.78  ?  443 THR   A OG1 1 
ATOM   3471  C CG2 . THR   A 1 443 ? -43.284 20.935  68.754  1.00 89.90  ?  443 THR   A CG2 1 
ATOM   3472  N N   . LEU   A 1 444 ? -43.201 17.665  65.899  1.00 72.82  ?  444 LEU   A N   1 
ATOM   3473  C CA  . LEU   A 1 444 ? -42.373 17.413  64.729  1.00 71.42  ?  444 LEU   A CA  1 
ATOM   3474  C C   . LEU   A 1 444 ? -43.220 17.592  63.482  1.00 67.43  ?  444 LEU   A C   1 
ATOM   3475  O O   . LEU   A 1 444 ? -44.418 17.300  63.484  1.00 67.36  ?  444 LEU   A O   1 
ATOM   3476  C CB  . LEU   A 1 444 ? -41.752 16.006  64.747  1.00 63.19  ?  444 LEU   A CB  1 
ATOM   3477  C CG  . LEU   A 1 444 ? -40.531 15.797  65.644  1.00 55.96  ?  444 LEU   A CG  1 
ATOM   3478  C CD1 . LEU   A 1 444 ? -40.010 14.377  65.512  1.00 54.19  ?  444 LEU   A CD1 1 
ATOM   3479  C CD2 . LEU   A 1 444 ? -39.440 16.795  65.305  1.00 53.18  ?  444 LEU   A CD2 1 
ATOM   3480  N N   . LYS   A 1 445 ? -42.584 18.066  62.414  1.00 67.04  ?  445 LYS   A N   1 
ATOM   3481  C CA  . LYS   A 1 445 ? -43.272 18.404  61.179  1.00 64.77  ?  445 LYS   A CA  1 
ATOM   3482  C C   . LYS   A 1 445 ? -42.821 17.506  60.037  1.00 62.51  ?  445 LYS   A C   1 
ATOM   3483  O O   . LYS   A 1 445 ? -41.659 17.092  59.967  1.00 57.99  ?  445 LYS   A O   1 
ATOM   3484  C CB  . LYS   A 1 445 ? -43.034 19.873  60.797  1.00 70.10  ?  445 LYS   A CB  1 
ATOM   3485  C CG  . LYS   A 1 445 ? -43.777 20.874  61.674  1.00 72.57  ?  445 LYS   A CG  1 
ATOM   3486  C CD  . LYS   A 1 445 ? -45.259 20.541  61.761  1.00 61.36  ?  445 LYS   A CD  1 
ATOM   3487  C CE  . LYS   A 1 445 ? -45.919 20.548  60.394  1.00 59.63  ?  445 LYS   A CE  1 
ATOM   3488  N NZ  . LYS   A 1 445 ? -47.356 20.186  60.501  1.00 80.33  ?  445 LYS   A NZ  1 
ATOM   3489  N N   . GLY   A 1 446 ? -43.758 17.221  59.134  1.00 61.77  ?  446 GLY   A N   1 
ATOM   3490  C CA  . GLY   A 1 446 ? -43.472 16.467  57.928  1.00 59.99  ?  446 GLY   A CA  1 
ATOM   3491  C C   . GLY   A 1 446 ? -42.506 17.186  57.008  1.00 60.75  ?  446 GLY   A C   1 
ATOM   3492  O O   . GLY   A 1 446 ? -42.004 18.264  57.335  1.00 61.96  ?  446 GLY   A O   1 
ATOM   3493  N N   . LEU   A 1 447 ? -42.234 16.595  55.847  1.00 57.00  ?  447 LEU   A N   1 
ATOM   3494  C CA  . LEU   A 1 447 ? -41.274 17.155  54.915  1.00 61.64  ?  447 LEU   A CA  1 
ATOM   3495  C C   . LEU   A 1 447 ? -41.867 17.154  53.512  1.00 62.93  ?  447 LEU   A C   1 
ATOM   3496  O O   . LEU   A 1 447 ? -42.749 16.350  53.192  1.00 59.51  ?  447 LEU   A O   1 
ATOM   3497  C CB  . LEU   A 1 447 ? -39.947 16.372  54.967  1.00 56.89  ?  447 LEU   A CB  1 
ATOM   3498  C CG  . LEU   A 1 447 ? -39.153 16.542  56.274  1.00 54.96  ?  447 LEU   A CG  1 
ATOM   3499  C CD1 . LEU   A 1 447 ? -38.436 15.261  56.675  1.00 49.90  ?  447 LEU   A CD1 1 
ATOM   3500  C CD2 . LEU   A 1 447 ? -38.153 17.690  56.173  1.00 55.78  ?  447 LEU   A CD2 1 
ATOM   3501  N N   . GLU   A 1 448 ? -41.382 18.074  52.676  1.00 60.91  ?  448 GLU   A N   1 
ATOM   3502  C CA  . GLU   A 1 448 ? -41.932 18.288  51.344  1.00 59.61  ?  448 GLU   A CA  1 
ATOM   3503  C C   . GLU   A 1 448 ? -40.797 18.448  50.344  1.00 64.36  ?  448 GLU   A C   1 
ATOM   3504  O O   . GLU   A 1 448 ? -39.778 19.074  50.648  1.00 66.28  ?  448 GLU   A O   1 
ATOM   3505  C CB  . GLU   A 1 448 ? -42.842 19.525  51.319  1.00 68.04  ?  448 GLU   A CB  1 
ATOM   3506  C CG  . GLU   A 1 448 ? -43.481 19.832  49.974  1.00 64.21  ?  448 GLU   A CG  1 
ATOM   3507  C CD  . GLU   A 1 448 ? -44.261 21.129  50.005  1.00 66.94  ?  448 GLU   A CD  1 
ATOM   3508  O OE1 . GLU   A 1 448 ? -44.188 21.830  51.038  1.00 64.77  ?  448 GLU   A OE1 1 
ATOM   3509  O OE2 . GLU   A 1 448 ? -44.943 21.448  49.005  1.00 63.23  ?  448 GLU   A OE2 1 
ATOM   3510  N N   . PHE   A 1 449 ? -40.981 17.883  49.152  1.00 63.24  ?  449 PHE   A N   1 
ATOM   3511  C CA  . PHE   A 1 449 ? -39.930 17.894  48.145  1.00 59.87  ?  449 PHE   A CA  1 
ATOM   3512  C C   . PHE   A 1 449 ? -39.704 19.295  47.600  1.00 62.43  ?  449 PHE   A C   1 
ATOM   3513  O O   . PHE   A 1 449 ? -40.646 20.068  47.411  1.00 66.25  ?  449 PHE   A O   1 
ATOM   3514  C CB  . PHE   A 1 449 ? -40.276 16.952  46.990  1.00 59.10  ?  449 PHE   A CB  1 
ATOM   3515  C CG  . PHE   A 1 449 ? -40.140 15.499  47.328  1.00 58.10  ?  449 PHE   A CG  1 
ATOM   3516  C CD1 . PHE   A 1 449 ? -38.887 14.924  47.475  1.00 58.82  ?  449 PHE   A CD1 1 
ATOM   3517  C CD2 . PHE   A 1 449 ? -41.261 14.700  47.486  1.00 57.26  ?  449 PHE   A CD2 1 
ATOM   3518  C CE1 . PHE   A 1 449 ? -38.756 13.579  47.786  1.00 55.39  ?  449 PHE   A CE1 1 
ATOM   3519  C CE2 . PHE   A 1 449 ? -41.136 13.351  47.798  1.00 59.84  ?  449 PHE   A CE2 1 
ATOM   3520  C CZ  . PHE   A 1 449 ? -39.880 12.791  47.950  1.00 51.37  ?  449 PHE   A CZ  1 
ATOM   3521  N N   . GLU   A 1 450 ? -38.435 19.618  47.355  1.00 71.04  ?  450 GLU   A N   1 
ATOM   3522  C CA  . GLU   A 1 450 ? -38.061 20.731  46.501  1.00 76.72  ?  450 GLU   A CA  1 
ATOM   3523  C C   . GLU   A 1 450 ? -37.246 20.283  45.298  1.00 74.14  ?  450 GLU   A C   1 
ATOM   3524  O O   . GLU   A 1 450 ? -37.033 21.085  44.380  1.00 76.68  ?  450 GLU   A O   1 
ATOM   3525  C CB  . GLU   A 1 450 ? -37.277 21.790  47.295  1.00 76.06  ?  450 GLU   A CB  1 
ATOM   3526  C CG  . GLU   A 1 450 ? -35.814 21.462  47.523  1.00 76.13  ?  450 GLU   A CG  1 
ATOM   3527  C CD  . GLU   A 1 450 ? -35.127 22.484  48.410  1.00 82.05  ?  450 GLU   A CD  1 
ATOM   3528  O OE1 . GLU   A 1 450 ? -35.840 23.198  49.147  1.00 89.77  ?  450 GLU   A OE1 1 
ATOM   3529  O OE2 . GLU   A 1 450 ? -33.880 22.581  48.367  1.00 75.92  ?  450 GLU   A OE2 1 
ATOM   3530  N N   . TYR   A 1 451 ? -36.794 19.030  45.277  1.00 63.54  ?  451 TYR   A N   1 
ATOM   3531  C CA  . TYR   A 1 451 ? -36.164 18.424  44.105  1.00 65.08  ?  451 TYR   A CA  1 
ATOM   3532  C C   . TYR   A 1 451 ? -36.294 16.917  44.242  1.00 61.46  ?  451 TYR   A C   1 
ATOM   3533  O O   . TYR   A 1 451 ? -35.779 16.345  45.209  1.00 63.33  ?  451 TYR   A O   1 
ATOM   3534  C CB  . TYR   A 1 451 ? -34.690 18.814  43.982  1.00 62.51  ?  451 TYR   A CB  1 
ATOM   3535  C CG  . TYR   A 1 451 ? -33.884 17.768  43.235  1.00 60.60  ?  451 TYR   A CG  1 
ATOM   3536  C CD1 . TYR   A 1 451 ? -33.985 17.641  41.855  1.00 67.36  ?  451 TYR   A CD1 1 
ATOM   3537  C CD2 . TYR   A 1 451 ? -33.042 16.893  43.911  1.00 59.31  ?  451 TYR   A CD2 1 
ATOM   3538  C CE1 . TYR   A 1 451 ? -33.262 16.681  41.165  1.00 63.09  ?  451 TYR   A CE1 1 
ATOM   3539  C CE2 . TYR   A 1 451 ? -32.317 15.930  43.229  1.00 61.89  ?  451 TYR   A CE2 1 
ATOM   3540  C CZ  . TYR   A 1 451 ? -32.431 15.829  41.855  1.00 62.50  ?  451 TYR   A CZ  1 
ATOM   3541  O OH  . TYR   A 1 451 ? -31.710 14.873  41.170  1.00 58.36  ?  451 TYR   A OH  1 
ATOM   3542  N N   . GLU   A 1 452 ? -36.957 16.270  43.286  1.00 60.11  ?  452 GLU   A N   1 
ATOM   3543  C CA  . GLU   A 1 452 ? -37.165 14.829  43.361  1.00 63.09  ?  452 GLU   A CA  1 
ATOM   3544  C C   . GLU   A 1 452 ? -36.611 14.129  42.127  1.00 63.30  ?  452 GLU   A C   1 
ATOM   3545  O O   . GLU   A 1 452 ? -37.083 14.387  41.005  1.00 59.89  ?  452 GLU   A O   1 
ATOM   3546  C CB  . GLU   A 1 452 ? -38.648 14.492  43.540  1.00 63.85  ?  452 GLU   A CB  1 
ATOM   3547  C CG  . GLU   A 1 452 ? -38.899 13.000  43.711  1.00 55.75  ?  452 GLU   A CG  1 
ATOM   3548  C CD  . GLU   A 1 452 ? -40.363 12.666  43.874  1.00 59.22  ?  452 GLU   A CD  1 
ATOM   3549  O OE1 . GLU   A 1 452 ? -41.173 13.603  44.072  1.00 60.79  ?  452 GLU   A OE1 1 
ATOM   3550  O OE2 . GLU   A 1 452 ? -40.700 11.463  43.808  1.00 57.71  ?  452 GLU   A OE2 1 
ATOM   3551  N N   . PRO   A 1 453 ? -35.627 13.248  42.285  1.00 62.45  ?  453 PRO   A N   1 
ATOM   3552  C CA  . PRO   A 1 453 ? -35.146 12.435  41.164  1.00 62.11  ?  453 PRO   A CA  1 
ATOM   3553  C C   . PRO   A 1 453 ? -36.178 11.404  40.744  1.00 64.28  ?  453 PRO   A C   1 
ATOM   3554  O O   . PRO   A 1 453 ? -37.014 10.979  41.558  1.00 62.21  ?  453 PRO   A O   1 
ATOM   3555  C CB  . PRO   A 1 453 ? -33.893 11.753  41.737  1.00 60.93  ?  453 PRO   A CB  1 
ATOM   3556  C CG  . PRO   A 1 453 ? -33.517 12.559  42.926  1.00 61.07  ?  453 PRO   A CG  1 
ATOM   3557  C CD  . PRO   A 1 453 ? -34.797 13.080  43.485  1.00 58.54  ?  453 PRO   A CD  1 
ATOM   3558  N N   . PRO   A 1 454 ? -36.142 10.965  39.481  1.00 67.67  ?  454 PRO   A N   1 
ATOM   3559  C CA  . PRO   A 1 454 ? -37.084 9.919   39.054  1.00 62.11  ?  454 PRO   A CA  1 
ATOM   3560  C C   . PRO   A 1 454 ? -36.783 8.553   39.648  1.00 70.18  ?  454 PRO   A C   1 
ATOM   3561  O O   . PRO   A 1 454 ? -37.714 7.821   40.011  1.00 74.30  ?  454 PRO   A O   1 
ATOM   3562  C CB  . PRO   A 1 454 ? -36.929 9.916   37.523  1.00 61.30  ?  454 PRO   A CB  1 
ATOM   3563  C CG  . PRO   A 1 454 ? -36.266 11.226  37.188  1.00 60.40  ?  454 PRO   A CG  1 
ATOM   3564  C CD  . PRO   A 1 454 ? -35.376 11.514  38.351  1.00 65.39  ?  454 PRO   A CD  1 
ATOM   3565  N N   . VAL   A 1 455 ? -35.507 8.187   39.759  1.00 70.75  ?  455 VAL   A N   1 
ATOM   3566  C CA  . VAL   A 1 455 ? -35.084 6.856   40.183  1.00 69.16  ?  455 VAL   A CA  1 
ATOM   3567  C C   . VAL   A 1 455 ? -34.335 6.995   41.502  1.00 71.16  ?  455 VAL   A C   1 
ATOM   3568  O O   . VAL   A 1 455 ? -33.354 7.746   41.587  1.00 79.59  ?  455 VAL   A O   1 
ATOM   3569  C CB  . VAL   A 1 455 ? -34.201 6.178   39.119  1.00 70.89  ?  455 VAL   A CB  1 
ATOM   3570  C CG1 . VAL   A 1 455 ? -33.689 4.820   39.609  1.00 64.41  ?  455 VAL   A CG1 1 
ATOM   3571  C CG2 . VAL   A 1 455 ? -34.960 6.035   37.809  1.00 67.13  ?  455 VAL   A CG2 1 
ATOM   3572  N N   . LEU   A 1 456 ? -34.787 6.266   42.521  1.00 66.06  ?  456 LEU   A N   1 
ATOM   3573  C CA  . LEU   A 1 456 ? -34.154 6.254   43.842  1.00 59.41  ?  456 LEU   A CA  1 
ATOM   3574  C C   . LEU   A 1 456 ? -33.974 7.680   44.371  1.00 60.71  ?  456 LEU   A C   1 
ATOM   3575  O O   . LEU   A 1 456 ? -32.863 8.148   44.638  1.00 57.69  ?  456 LEU   A O   1 
ATOM   3576  C CB  . LEU   A 1 456 ? -32.823 5.492   43.799  1.00 52.42  ?  456 LEU   A CB  1 
ATOM   3577  C CG  . LEU   A 1 456 ? -32.920 3.980   43.544  1.00 52.23  ?  456 LEU   A CG  1 
ATOM   3578  C CD1 . LEU   A 1 456 ? -31.566 3.378   43.189  1.00 42.09  ?  456 LEU   A CD1 1 
ATOM   3579  C CD2 . LEU   A 1 456 ? -33.522 3.259   44.748  1.00 44.79  ?  456 LEU   A CD2 1 
ATOM   3580  N N   . ARG   A 1 457 ? -35.115 8.362   44.522  1.00 61.63  ?  457 ARG   A N   1 
ATOM   3581  C CA  . ARG   A 1 457 ? -35.130 9.772   44.910  1.00 56.47  ?  457 ARG   A CA  1 
ATOM   3582  C C   . ARG   A 1 457 ? -34.424 10.010  46.240  1.00 54.48  ?  457 ARG   A C   1 
ATOM   3583  O O   . ARG   A 1 457 ? -33.770 11.043  46.421  1.00 53.68  ?  457 ARG   A O   1 
ATOM   3584  C CB  . ARG   A 1 457 ? -36.573 10.264  45.000  1.00 57.56  ?  457 ARG   A CB  1 
ATOM   3585  C CG  . ARG   A 1 457 ? -37.414 9.457   45.988  1.00 53.91  ?  457 ARG   A CG  1 
ATOM   3586  C CD  . ARG   A 1 457 ? -38.874 9.862   45.987  1.00 56.87  ?  457 ARG   A CD  1 
ATOM   3587  N NE  . ARG   A 1 457 ? -39.658 8.989   46.851  1.00 56.32  ?  457 ARG   A NE  1 
ATOM   3588  C CZ  . ARG   A 1 457 ? -40.980 8.914   46.838  1.00 52.94  ?  457 ARG   A CZ  1 
ATOM   3589  N NH1 . ARG   A 1 457 ? -41.705 9.666   46.028  1.00 54.96  ?  457 ARG   A NH1 1 
ATOM   3590  N NH2 . ARG   A 1 457 ? -41.589 8.053   47.648  1.00 58.58  ?  457 ARG   A NH2 1 
ATOM   3591  N N   . HIS   A 1 458 ? -34.541 9.064   47.179  1.00 45.80  ?  458 HIS   A N   1 
ATOM   3592  C CA  . HIS   A 1 458 ? -34.112 9.292   48.556  1.00 45.82  ?  458 HIS   A CA  1 
ATOM   3593  C C   . HIS   A 1 458 ? -32.619 9.576   48.675  1.00 45.19  ?  458 HIS   A C   1 
ATOM   3594  O O   . HIS   A 1 458 ? -32.192 10.181  49.665  1.00 43.79  ?  458 HIS   A O   1 
ATOM   3595  C CB  . HIS   A 1 458 ? -34.488 8.086   49.417  1.00 47.37  ?  458 HIS   A CB  1 
ATOM   3596  C CG  . HIS   A 1 458 ? -33.888 6.797   48.944  1.00 54.25  ?  458 HIS   A CG  1 
ATOM   3597  N ND1 . HIS   A 1 458 ? -32.917 6.123   49.656  1.00 48.37  ?  458 HIS   A ND1 1 
ATOM   3598  C CD2 . HIS   A 1 458 ? -34.114 6.064   47.826  1.00 49.67  ?  458 HIS   A CD2 1 
ATOM   3599  C CE1 . HIS   A 1 458 ? -32.573 5.030   48.997  1.00 48.93  ?  458 HIS   A CE1 1 
ATOM   3600  N NE2 . HIS   A 1 458 ? -33.283 4.971   47.883  1.00 46.65  ?  458 HIS   A NE2 1 
ATOM   3601  N N   . PHE   A 1 459 ? -31.819 9.178   47.683  1.00 46.44  ?  459 PHE   A N   1 
ATOM   3602  C CA  . PHE   A 1 459 ? -30.376 9.370   47.777  1.00 41.98  ?  459 PHE   A CA  1 
ATOM   3603  C C   . PHE   A 1 459 ? -29.986 10.835  47.617  1.00 45.50  ?  459 PHE   A C   1 
ATOM   3604  O O   . PHE   A 1 459 ? -29.055 11.307  48.280  1.00 40.72  ?  459 PHE   A O   1 
ATOM   3605  C CB  . PHE   A 1 459 ? -29.665 8.524   46.725  1.00 41.85  ?  459 PHE   A CB  1 
ATOM   3606  C CG  . PHE   A 1 459 ? -29.660 7.062   47.028  1.00 38.59  ?  459 PHE   A CG  1 
ATOM   3607  C CD1 . PHE   A 1 459 ? -28.907 6.564   48.073  1.00 37.90  ?  459 PHE   A CD1 1 
ATOM   3608  C CD2 . PHE   A 1 459 ? -30.395 6.181   46.257  1.00 46.00  ?  459 PHE   A CD2 1 
ATOM   3609  C CE1 . PHE   A 1 459 ? -28.894 5.209   48.356  1.00 41.69  ?  459 PHE   A CE1 1 
ATOM   3610  C CE2 . PHE   A 1 459 ? -30.381 4.819   46.530  1.00 46.52  ?  459 PHE   A CE2 1 
ATOM   3611  C CZ  . PHE   A 1 459 ? -29.633 4.335   47.579  1.00 40.89  ?  459 PHE   A CZ  1 
ATOM   3612  N N   . THR   A 1 460 ? -30.666 11.567  46.728  1.00 43.66  ?  460 THR   A N   1 
ATOM   3613  C CA  . THR   A 1 460 ? -30.229 12.912  46.367  1.00 48.30  ?  460 THR   A CA  1 
ATOM   3614  C C   . THR   A 1 460 ? -31.343 13.952  46.426  1.00 45.02  ?  460 THR   A C   1 
ATOM   3615  O O   . THR   A 1 460 ? -31.121 15.094  46.011  1.00 44.31  ?  460 THR   A O   1 
ATOM   3616  C CB  . THR   A 1 460 ? -29.603 12.917  44.964  1.00 48.92  ?  460 THR   A CB  1 
ATOM   3617  O OG1 . THR   A 1 460 ? -30.545 12.416  44.008  1.00 46.43  ?  460 THR   A OG1 1 
ATOM   3618  C CG2 . THR   A 1 460 ? -28.341 12.052  44.931  1.00 44.87  ?  460 THR   A CG2 1 
ATOM   3619  N N   . ALA   A 1 461 ? -32.519 13.599  46.937  1.00 49.23  ?  461 ALA   A N   1 
ATOM   3620  C CA  . ALA   A 1 461 ? -33.635 14.536  46.984  1.00 52.23  ?  461 ALA   A CA  1 
ATOM   3621  C C   . ALA   A 1 461 ? -33.376 15.650  47.993  1.00 50.16  ?  461 ALA   A C   1 
ATOM   3622  O O   . ALA   A 1 461 ? -32.791 15.427  49.055  1.00 48.97  ?  461 ALA   A O   1 
ATOM   3623  C CB  . ALA   A 1 461 ? -34.929 13.802  47.342  1.00 48.77  ?  461 ALA   A CB  1 
ATOM   3624  N N   . ARG   A 1 462 ? -33.815 16.859  47.660  1.00 51.57  ?  462 ARG   A N   1 
ATOM   3625  C CA  . ARG   A 1 462 ? -33.721 17.994  48.565  1.00 53.84  ?  462 ARG   A CA  1 
ATOM   3626  C C   . ARG   A 1 462 ? -35.105 18.307  49.110  1.00 59.56  ?  462 ARG   A C   1 
ATOM   3627  O O   . ARG   A 1 462 ? -36.066 18.420  48.342  1.00 63.11  ?  462 ARG   A O   1 
ATOM   3628  C CB  . ARG   A 1 462 ? -33.125 19.214  47.866  1.00 56.85  ?  462 ARG   A CB  1 
ATOM   3629  C CG  . ARG   A 1 462 ? -31.649 19.069  47.537  1.00 60.30  ?  462 ARG   A CG  1 
ATOM   3630  C CD  . ARG   A 1 462 ? -31.045 20.405  47.142  1.00 56.91  ?  462 ARG   A CD  1 
ATOM   3631  N NE  . ARG   A 1 462 ? -31.047 21.352  48.251  1.00 52.90  ?  462 ARG   A NE  1 
ATOM   3632  C CZ  . ARG   A 1 462 ? -30.079 21.445  49.153  1.00 51.75  ?  462 ARG   A CZ  1 
ATOM   3633  N NH1 . ARG   A 1 462 ? -29.019 20.655  49.113  1.00 47.92  ?  462 ARG   A NH1 1 
ATOM   3634  N NH2 . ARG   A 1 462 ? -30.177 22.356  50.119  1.00 53.95  ?  462 ARG   A NH2 1 
ATOM   3635  N N   . LEU   A 1 463 ? -35.201 18.439  50.430  1.00 60.46  ?  463 LEU   A N   1 
ATOM   3636  C CA  . LEU   A 1 463 ? -36.470 18.536  51.137  1.00 60.37  ?  463 LEU   A CA  1 
ATOM   3637  C C   . LEU   A 1 463 ? -36.521 19.811  51.968  1.00 64.46  ?  463 LEU   A C   1 
ATOM   3638  O O   . LEU   A 1 463 ? -35.508 20.480  52.195  1.00 58.56  ?  463 LEU   A O   1 
ATOM   3639  C CB  . LEU   A 1 463 ? -36.687 17.315  52.043  1.00 56.96  ?  463 LEU   A CB  1 
ATOM   3640  C CG  . LEU   A 1 463 ? -36.930 15.975  51.352  1.00 52.08  ?  463 LEU   A CG  1 
ATOM   3641  C CD1 . LEU   A 1 463 ? -36.688 14.818  52.306  1.00 49.57  ?  463 LEU   A CD1 1 
ATOM   3642  C CD2 . LEU   A 1 463 ? -38.351 15.941  50.816  1.00 60.57  ?  463 LEU   A CD2 1 
ATOM   3643  N N   . LYS   A 1 464 ? -37.731 20.130  52.429  1.00 74.68  ?  464 LYS   A N   1 
ATOM   3644  C CA  . LYS   A 1 464 ? -38.003 21.278  53.279  1.00 75.82  ?  464 LYS   A CA  1 
ATOM   3645  C C   . LYS   A 1 464 ? -39.096 20.907  54.271  1.00 75.98  ?  464 LYS   A C   1 
ATOM   3646  O O   . LYS   A 1 464 ? -40.071 20.238  53.895  1.00 75.63  ?  464 LYS   A O   1 
ATOM   3647  C CB  . LYS   A 1 464 ? -38.437 22.507  52.467  1.00 77.40  ?  464 LYS   A CB  1 
ATOM   3648  C CG  . LYS   A 1 464 ? -37.293 23.452  52.144  1.00 82.28  ?  464 LYS   A CG  1 
ATOM   3649  C CD  . LYS   A 1 464 ? -37.774 24.713  51.447  1.00 85.32  ?  464 LYS   A CD  1 
ATOM   3650  C CE  . LYS   A 1 464 ? -36.680 25.773  51.435  1.00 80.62  ?  464 LYS   A CE  1 
ATOM   3651  N NZ  . LYS   A 1 464 ? -35.428 25.311  50.768  1.00 79.84  ?  464 LYS   A NZ  1 
ATOM   3652  N N   . PRO   A 1 465 ? -38.963 21.319  55.533  1.00 67.21  ?  465 PRO   A N   1 
ATOM   3653  C CA  . PRO   A 1 465 ? -39.995 21.000  56.526  1.00 64.01  ?  465 PRO   A CA  1 
ATOM   3654  C C   . PRO   A 1 465 ? -41.346 21.583  56.132  1.00 66.80  ?  465 PRO   A C   1 
ATOM   3655  O O   . PRO   A 1 465 ? -41.455 22.454  55.265  1.00 73.10  ?  465 PRO   A O   1 
ATOM   3656  C CB  . PRO   A 1 465 ? -39.465 21.644  57.814  1.00 63.64  ?  465 PRO   A CB  1 
ATOM   3657  C CG  . PRO   A 1 465 ? -37.998 21.811  57.590  1.00 53.04  ?  465 PRO   A CG  1 
ATOM   3658  C CD  . PRO   A 1 465 ? -37.842 22.072  56.123  1.00 60.71  ?  465 PRO   A CD  1 
ATOM   3659  N N   . ILE   A 1 466 ? -42.388 21.081  56.785  1.00 68.62  ?  466 ILE   A N   1 
ATOM   3660  C CA  . ILE   A 1 466 ? -43.745 21.561  56.537  1.00 67.83  ?  466 ILE   A CA  1 
ATOM   3661  C C   . ILE   A 1 466 ? -44.241 22.387  57.721  1.00 63.95  ?  466 ILE   A C   1 
ATOM   3662  O O   . ILE   A 1 466 ? -44.749 23.498  57.547  1.00 61.13  ?  466 ILE   A O   1 
ATOM   3663  C CB  . ILE   A 1 466 ? -44.701 20.388  56.241  1.00 61.23  ?  466 ILE   A CB  1 
ATOM   3664  C CG1 . ILE   A 1 466 ? -44.338 19.729  54.909  1.00 59.25  ?  466 ILE   A CG1 1 
ATOM   3665  C CG2 . ILE   A 1 466 ? -46.146 20.858  56.232  1.00 66.10  ?  466 ILE   A CG2 1 
ATOM   3666  C CD1 . ILE   A 1 466 ? -45.033 18.410  54.675  1.00 60.61  ?  466 ILE   A CD1 1 
ATOM   3667  N N   . ALA   B 1 2   ? 19.723  3.337   21.737  1.00 28.99  ?  2   ALA   B N   1 
ATOM   3668  C CA  . ALA   B 1 2   ? 18.737  3.261   22.806  1.00 25.56  ?  2   ALA   B CA  1 
ATOM   3669  C C   . ALA   B 1 2   ? 19.289  3.887   24.079  1.00 28.79  ?  2   ALA   B C   1 
ATOM   3670  O O   . ALA   B 1 2   ? 20.302  3.427   24.598  1.00 35.48  ?  2   ALA   B O   1 
ATOM   3671  C CB  . ALA   B 1 2   ? 18.342  1.820   23.054  1.00 22.37  ?  2   ALA   B CB  1 
ATOM   3672  N N   . LYS   B 1 3   ? 18.626  4.926   24.588  1.00 25.86  ?  3   LYS   B N   1 
ATOM   3673  C CA  . LYS   B 1 3   ? 19.083  5.642   25.777  1.00 27.18  ?  3   LYS   B CA  1 
ATOM   3674  C C   . LYS   B 1 3   ? 18.282  5.208   26.999  1.00 28.78  ?  3   LYS   B C   1 
ATOM   3675  O O   . LYS   B 1 3   ? 17.061  5.394   27.044  1.00 25.18  ?  3   LYS   B O   1 
ATOM   3676  C CB  . LYS   B 1 3   ? 18.960  7.158   25.600  1.00 30.03  ?  3   LYS   B CB  1 
ATOM   3677  C CG  . LYS   B 1 3   ? 19.435  7.944   26.836  1.00 38.96  ?  3   LYS   B CG  1 
ATOM   3678  C CD  . LYS   B 1 3   ? 19.175  9.451   26.730  1.00 40.06  ?  3   LYS   B CD  1 
ATOM   3679  C CE  . LYS   B 1 3   ? 17.687  9.762   26.841  1.00 41.45  ?  3   LYS   B CE  1 
ATOM   3680  N NZ  . LYS   B 1 3   ? 17.365  11.225  26.911  1.00 39.10  ?  3   LYS   B NZ  1 
ATOM   3681  N N   . ARG   B 1 4   ? 18.973  4.646   27.988  1.00 24.38  ?  4   ARG   B N   1 
ATOM   3682  C CA  A ARG   B 1 4   ? 18.359  4.341   29.271  0.53 25.07  ?  4   ARG   B CA  1 
ATOM   3683  C CA  B ARG   B 1 4   ? 18.359  4.343   29.271  0.47 25.07  ?  4   ARG   B CA  1 
ATOM   3684  C C   . ARG   B 1 4   ? 18.240  5.612   30.105  1.00 23.93  ?  4   ARG   B C   1 
ATOM   3685  O O   . ARG   B 1 4   ? 19.157  6.435   30.142  1.00 25.78  ?  4   ARG   B O   1 
ATOM   3686  C CB  A ARG   B 1 4   ? 19.183  3.288   30.019  0.53 25.05  ?  4   ARG   B CB  1 
ATOM   3687  C CB  B ARG   B 1 4   ? 19.181  3.294   30.025  0.47 25.06  ?  4   ARG   B CB  1 
ATOM   3688  C CG  A ARG   B 1 4   ? 19.307  1.964   29.279  0.53 23.98  ?  4   ARG   B CG  1 
ATOM   3689  C CG  B ARG   B 1 4   ? 19.221  1.933   29.354  0.47 23.98  ?  4   ARG   B CG  1 
ATOM   3690  C CD  A ARG   B 1 4   ? 20.342  1.030   29.890  0.53 23.00  ?  4   ARG   B CD  1 
ATOM   3691  C CD  B ARG   B 1 4   ? 19.800  0.863   30.264  0.47 23.70  ?  4   ARG   B CD  1 
ATOM   3692  N NE  A ARG   B 1 4   ? 19.896  0.440   31.147  0.53 25.50  ?  4   ARG   B NE  1 
ATOM   3693  N NE  B ARG   B 1 4   ? 21.243  0.719   30.119  0.47 25.35  ?  4   ARG   B NE  1 
ATOM   3694  C CZ  A ARG   B 1 4   ? 19.437  -0.797  31.283  0.53 21.79  ?  4   ARG   B CZ  1 
ATOM   3695  C CZ  B ARG   B 1 4   ? 21.843  -0.328  29.567  0.47 26.40  ?  4   ARG   B CZ  1 
ATOM   3696  N NH1 A ARG   B 1 4   ? 19.342  -1.619  30.252  0.53 21.58  ?  4   ARG   B NH1 1 
ATOM   3697  N NH1 B ARG   B 1 4   ? 21.151  -1.356  29.102  0.47 24.83  ?  4   ARG   B NH1 1 
ATOM   3698  N NH2 A ARG   B 1 4   ? 19.072  -1.223  32.487  0.53 20.98  ?  4   ARG   B NH2 1 
ATOM   3699  N NH2 B ARG   B 1 4   ? 23.170  -0.347  29.486  0.47 22.16  ?  4   ARG   B NH2 1 
ATOM   3700  N N   . ILE   B 1 5   ? 17.103  5.767   30.781  1.00 25.29  ?  5   ILE   B N   1 
ATOM   3701  C CA  . ILE   B 1 5   ? 16.827  6.935   31.612  1.00 23.26  ?  5   ILE   B CA  1 
ATOM   3702  C C   . ILE   B 1 5   ? 16.571  6.479   33.046  1.00 23.04  ?  5   ILE   B C   1 
ATOM   3703  O O   . ILE   B 1 5   ? 15.768  5.568   33.283  1.00 21.94  ?  5   ILE   B O   1 
ATOM   3704  C CB  . ILE   B 1 5   ? 15.640  7.744   31.063  1.00 22.82  ?  5   ILE   B CB  1 
ATOM   3705  C CG1 . ILE   B 1 5   ? 16.006  8.336   29.701  1.00 27.70  ?  5   ILE   B CG1 1 
ATOM   3706  C CG2 . ILE   B 1 5   ? 15.226  8.845   32.037  1.00 21.96  ?  5   ILE   B CG2 1 
ATOM   3707  C CD1 . ILE   B 1 5   ? 14.932  9.236   29.109  1.00 27.74  ?  5   ILE   B CD1 1 
ATOM   3708  N N   . VAL   B 1 6   ? 17.235  7.137   33.998  1.00 21.83  ?  6   VAL   B N   1 
ATOM   3709  C CA  . VAL   B 1 6   ? 17.213  6.721   35.393  1.00 21.36  ?  6   VAL   B CA  1 
ATOM   3710  C C   . VAL   B 1 6   ? 15.858  7.029   36.028  1.00 23.63  ?  6   VAL   B C   1 
ATOM   3711  O O   . VAL   B 1 6   ? 15.169  7.995   35.663  1.00 24.60  ?  6   VAL   B O   1 
ATOM   3712  C CB  . VAL   B 1 6   ? 18.359  7.412   36.157  1.00 22.77  ?  6   VAL   B CB  1 
ATOM   3713  C CG1 . VAL   B 1 6   ? 18.119  8.911   36.250  1.00 22.24  ?  6   VAL   B CG1 1 
ATOM   3714  C CG2 . VAL   B 1 6   ? 18.532  6.814   37.535  1.00 23.25  ?  6   VAL   B CG2 1 
ATOM   3715  N N   . GLU   B 1 7   ? 15.466  6.181   36.978  1.00 22.71  ?  7   GLU   B N   1 
ATOM   3716  C CA  . GLU   B 1 7   ? 14.252  6.398   37.756  1.00 22.32  ?  7   GLU   B CA  1 
ATOM   3717  C C   . GLU   B 1 7   ? 14.370  7.666   38.598  1.00 21.63  ?  7   GLU   B C   1 
ATOM   3718  O O   . GLU   B 1 7   ? 15.394  7.864   39.268  1.00 26.15  ?  7   GLU   B O   1 
ATOM   3719  C CB  . GLU   B 1 7   ? 14.004  5.212   38.680  1.00 21.80  ?  7   GLU   B CB  1 
ATOM   3720  C CG  . GLU   B 1 7   ? 13.526  3.962   38.001  1.00 20.77  ?  7   GLU   B CG  1 
ATOM   3721  C CD  . GLU   B 1 7   ? 14.618  3.174   37.316  1.00 25.64  ?  7   GLU   B CD  1 
ATOM   3722  O OE1 . GLU   B 1 7   ? 15.807  3.594   37.333  1.00 23.76  ?  7   GLU   B OE1 1 
ATOM   3723  O OE2 . GLU   B 1 7   ? 14.270  2.109   36.758  1.00 27.38  ?  7   GLU   B OE2 1 
ATOM   3724  N N   . PRO   B 1 8   ? 13.353  8.538   38.601  1.00 24.45  ?  8   PRO   B N   1 
ATOM   3725  C CA  . PRO   B 1 8   ? 13.352  9.686   39.521  1.00 22.20  ?  8   PRO   B CA  1 
ATOM   3726  C C   . PRO   B 1 8   ? 12.688  9.333   40.843  1.00 22.45  ?  8   PRO   B C   1 
ATOM   3727  O O   . PRO   B 1 8   ? 11.879  10.096  41.383  1.00 21.54  ?  8   PRO   B O   1 
ATOM   3728  C CB  . PRO   B 1 8   ? 12.561  10.747  38.749  1.00 22.39  ?  8   PRO   B CB  1 
ATOM   3729  C CG  . PRO   B 1 8   ? 11.596  9.946   37.937  1.00 21.09  ?  8   PRO   B CG  1 
ATOM   3730  C CD  . PRO   B 1 8   ? 12.235  8.602   37.642  1.00 22.68  ?  8   PRO   B CD  1 
ATOM   3731  N N   . PHE   B 1 9   ? 13.039  8.155   41.353  1.00 23.47  ?  9   PHE   B N   1 
ATOM   3732  C CA  . PHE   B 1 9   ? 12.550  7.597   42.605  1.00 21.99  ?  9   PHE   B CA  1 
ATOM   3733  C C   . PHE   B 1 9   ? 13.462  6.422   42.934  1.00 24.35  ?  9   PHE   B C   1 
ATOM   3734  O O   . PHE   B 1 9   ? 14.298  6.023   42.120  1.00 22.25  ?  9   PHE   B O   1 
ATOM   3735  C CB  . PHE   B 1 9   ? 11.084  7.156   42.507  1.00 22.76  ?  9   PHE   B CB  1 
ATOM   3736  C CG  . PHE   B 1 9   ? 10.809  6.217   41.364  1.00 21.64  ?  9   PHE   B CG  1 
ATOM   3737  C CD1 . PHE   B 1 9   ? 11.135  4.866   41.453  1.00 16.82  ?  9   PHE   B CD1 1 
ATOM   3738  C CD2 . PHE   B 1 9   ? 10.223  6.679   40.199  1.00 18.32  ?  9   PHE   B CD2 1 
ATOM   3739  C CE1 . PHE   B 1 9   ? 10.889  4.006   40.393  1.00 17.07  ?  9   PHE   B CE1 1 
ATOM   3740  C CE2 . PHE   B 1 9   ? 9.976   5.816   39.141  1.00 19.55  ?  9   PHE   B CE2 1 
ATOM   3741  C CZ  . PHE   B 1 9   ? 10.306  4.483   39.243  1.00 13.18  ?  9   PHE   B CZ  1 
ATOM   3742  N N   . ARG   B 1 10  ? 13.293  5.863   44.126  1.00 17.77  ?  10  ARG   B N   1 
ATOM   3743  C CA  . ARG   B 1 10  ? 13.936  4.602   44.453  1.00 19.21  ?  10  ARG   B CA  1 
ATOM   3744  C C   . ARG   B 1 10  ? 12.878  3.623   44.934  1.00 14.55  ?  10  ARG   B C   1 
ATOM   3745  O O   . ARG   B 1 10  ? 11.723  3.984   45.167  1.00 15.76  ?  10  ARG   B O   1 
ATOM   3746  C CB  . ARG   B 1 10  ? 15.056  4.776   45.493  1.00 20.16  ?  10  ARG   B CB  1 
ATOM   3747  C CG  . ARG   B 1 10  ? 14.585  5.279   46.829  1.00 22.91  ?  10  ARG   B CG  1 
ATOM   3748  C CD  . ARG   B 1 10  ? 15.762  5.630   47.717  1.00 22.70  ?  10  ARG   B CD  1 
ATOM   3749  N NE  . ARG   B 1 10  ? 15.308  6.303   48.927  1.00 24.53  ?  10  ARG   B NE  1 
ATOM   3750  C CZ  . ARG   B 1 10  ? 15.994  7.243   49.561  1.00 30.47  ?  10  ARG   B CZ  1 
ATOM   3751  N NH1 . ARG   B 1 10  ? 17.195  7.620   49.149  1.00 31.33  ?  10  ARG   B NH1 1 
ATOM   3752  N NH2 . ARG   B 1 10  ? 15.456  7.828   50.629  1.00 28.56  ?  10  ARG   B NH2 1 
ATOM   3753  N N   . ILE   B 1 11  ? 13.278  2.369   45.075  1.00 15.44  ?  11  ILE   B N   1 
ATOM   3754  C CA  . ILE   B 1 11  ? 12.339  1.296   45.379  1.00 13.87  ?  11  ILE   B CA  1 
ATOM   3755  C C   . ILE   B 1 11  ? 12.113  1.229   46.884  1.00 15.52  ?  11  ILE   B C   1 
ATOM   3756  O O   . ILE   B 1 11  ? 13.065  1.245   47.669  1.00 14.98  ?  11  ILE   B O   1 
ATOM   3757  C CB  . ILE   B 1 11  ? 12.859  -0.044  44.836  1.00 17.87  ?  11  ILE   B CB  1 
ATOM   3758  C CG1 . ILE   B 1 11  ? 12.984  0.028   43.306  1.00 16.00  ?  11  ILE   B CG1 1 
ATOM   3759  C CG2 . ILE   B 1 11  ? 11.969  -1.200  45.309  1.00 13.86  ?  11  ILE   B CG2 1 
ATOM   3760  C CD1 . ILE   B 1 11  ? 13.932  -1.000  42.709  1.00 18.96  ?  11  ILE   B CD1 1 
ATOM   3761  N N   . LYS   B 1 12  ? 10.849  1.159   47.291  1.00 18.28  ?  12  LYS   B N   1 
ATOM   3762  C CA  . LYS   B 1 12  ? 10.510  0.990   48.696  1.00 15.83  ?  12  LYS   B CA  1 
ATOM   3763  C C   . LYS   B 1 12  ? 9.952   -0.387  49.018  1.00 17.33  ?  12  LYS   B C   1 
ATOM   3764  O O   . LYS   B 1 12  ? 10.146  -0.865  50.134  1.00 20.15  ?  12  LYS   B O   1 
ATOM   3765  C CB  . LYS   B 1 12  ? 9.490   2.050   49.133  1.00 17.98  ?  12  LYS   B CB  1 
ATOM   3766  C CG  . LYS   B 1 12  ? 9.583   2.403   50.618  1.00 21.69  ?  12  LYS   B CG  1 
ATOM   3767  C CD  . LYS   B 1 12  ? 8.478   3.361   51.041  1.00 21.59  ?  12  LYS   B CD  1 
ATOM   3768  C CE  . LYS   B 1 12  ? 8.607   3.742   52.519  1.00 26.35  ?  12  LYS   B CE  1 
ATOM   3769  N NZ  . LYS   B 1 12  ? 9.386   5.008   52.711  1.00 24.84  ?  12  LYS   B NZ  1 
ATOM   3770  N N   . MET   B 1 13  ? 9.261   -1.035  48.077  1.00 14.17  ?  13  MET   B N   1 
ATOM   3771  C CA  . MET   B 1 13  ? 8.717   -2.365  48.312  1.00 14.16  ?  13  MET   B CA  1 
ATOM   3772  C C   . MET   B 1 13  ? 8.783   -3.178  47.029  1.00 14.86  ?  13  MET   B C   1 
ATOM   3773  O O   . MET   B 1 13  ? 8.543   -2.651  45.938  1.00 14.10  ?  13  MET   B O   1 
ATOM   3774  C CB  . MET   B 1 13  ? 7.267   -2.305  48.816  1.00 13.49  ?  13  MET   B CB  1 
ATOM   3775  C CG  . MET   B 1 13  ? 6.773   -3.627  49.421  1.00 16.41  ?  13  MET   B CG  1 
ATOM   3776  S SD  . MET   B 1 13  ? 4.981   -3.677  49.676  1.00 27.04  ?  13  MET   B SD  1 
ATOM   3777  C CE  . MET   B 1 13  ? 4.814   -2.403  50.898  1.00 20.10  ?  13  MET   B CE  1 
ATOM   3778  N N   . VAL   B 1 14  ? 9.101   -4.464  47.170  1.00 14.41  ?  14  VAL   B N   1 
ATOM   3779  C CA  . VAL   B 1 14  ? 9.290   -5.355  46.037  1.00 15.62  ?  14  VAL   B CA  1 
ATOM   3780  C C   . VAL   B 1 14  ? 8.236   -6.453  46.061  1.00 19.33  ?  14  VAL   B C   1 
ATOM   3781  O O   . VAL   B 1 14  ? 7.624   -6.754  47.091  1.00 17.13  ?  14  VAL   B O   1 
ATOM   3782  C CB  . VAL   B 1 14  ? 10.700  -5.978  46.019  1.00 18.17  ?  14  VAL   B CB  1 
ATOM   3783  C CG1 . VAL   B 1 14  ? 11.722  -4.930  45.662  1.00 17.36  ?  14  VAL   B CG1 1 
ATOM   3784  C CG2 . VAL   B 1 14  ? 11.016  -6.584  47.374  1.00 16.54  ?  14  VAL   B CG2 1 
ATOM   3785  N N   . GLU   B 1 15  ? 8.056   -7.070  44.898  1.00 17.04  ?  15  GLU   B N   1 
ATOM   3786  C CA  . GLU   B 1 15  ? 7.182   -8.219  44.704  1.00 16.34  ?  15  GLU   B CA  1 
ATOM   3787  C C   . GLU   B 1 15  ? 7.958   -9.241  43.877  1.00 17.40  ?  15  GLU   B C   1 
ATOM   3788  O O   . GLU   B 1 15  ? 8.425   -8.925  42.780  1.00 18.64  ?  15  GLU   B O   1 
ATOM   3789  C CB  . GLU   B 1 15  ? 5.892   -7.775  44.002  1.00 19.87  ?  15  GLU   B CB  1 
ATOM   3790  C CG  . GLU   B 1 15  ? 4.954   -8.870  43.575  1.00 27.90  ?  15  GLU   B CG  1 
ATOM   3791  C CD  . GLU   B 1 15  ? 3.784   -8.350  42.735  1.00 33.53  ?  15  GLU   B CD  1 
ATOM   3792  O OE1 . GLU   B 1 15  ? 3.924   -7.301  42.056  1.00 25.62  ?  15  GLU   B OE1 1 
ATOM   3793  O OE2 . GLU   B 1 15  ? 2.718   -9.006  42.751  1.00 39.42  ?  15  GLU   B OE2 1 
ATOM   3794  N N   . LYS   B 1 16  ? 8.121   -10.455 44.405  1.00 21.22  ?  16  LYS   B N   1 
ATOM   3795  C CA  . LYS   B 1 16  ? 8.876   -11.480 43.688  1.00 23.55  ?  16  LYS   B CA  1 
ATOM   3796  C C   . LYS   B 1 16  ? 8.200   -11.851 42.371  1.00 24.16  ?  16  LYS   B C   1 
ATOM   3797  O O   . LYS   B 1 16  ? 6.972   -11.854 42.261  1.00 27.87  ?  16  LYS   B O   1 
ATOM   3798  C CB  . LYS   B 1 16  ? 9.029   -12.726 44.560  1.00 26.22  ?  16  LYS   B CB  1 
ATOM   3799  C CG  . LYS   B 1 16  ? 9.868   -13.837 43.936  1.00 34.02  ?  16  LYS   B CG  1 
ATOM   3800  C CD  . LYS   B 1 16  ? 10.191  -14.931 44.958  1.00 41.04  ?  16  LYS   B CD  1 
ATOM   3801  C CE  . LYS   B 1 16  ? 11.066  -16.030 44.352  1.00 48.41  ?  16  LYS   B CE  1 
ATOM   3802  N NZ  . LYS   B 1 16  ? 11.416  -17.111 45.330  1.00 48.05  ?  16  LYS   B NZ  1 
ATOM   3803  N N   . ILE   B 1 17  ? 9.010   -12.150 41.357  1.00 23.66  ?  17  ILE   B N   1 
ATOM   3804  C CA  . ILE   B 1 17  ? 8.525   -12.747 40.120  1.00 25.21  ?  17  ILE   B CA  1 
ATOM   3805  C C   . ILE   B 1 17  ? 9.443   -13.906 39.769  1.00 26.61  ?  17  ILE   B C   1 
ATOM   3806  O O   . ILE   B 1 17  ? 10.566  -14.006 40.260  1.00 32.49  ?  17  ILE   B O   1 
ATOM   3807  C CB  . ILE   B 1 17  ? 8.447   -11.746 38.948  1.00 29.98  ?  17  ILE   B CB  1 
ATOM   3808  C CG1 . ILE   B 1 17  ? 9.826   -11.160 38.634  1.00 26.54  ?  17  ILE   B CG1 1 
ATOM   3809  C CG2 . ILE   B 1 17  ? 7.420   -10.656 39.255  1.00 28.80  ?  17  ILE   B CG2 1 
ATOM   3810  C CD1 . ILE   B 1 17  ? 9.801   -10.144 37.503  1.00 23.14  ?  17  ILE   B CD1 1 
ATOM   3811  N N   . ARG   B 1 18  ? 8.944   -14.804 38.925  1.00 27.69  ?  18  ARG   B N   1 
ATOM   3812  C CA  . ARG   B 1 18  ? 9.683   -16.013 38.595  1.00 30.65  ?  18  ARG   B CA  1 
ATOM   3813  C C   . ARG   B 1 18  ? 9.488   -16.334 37.127  1.00 32.23  ?  18  ARG   B C   1 
ATOM   3814  O O   . ARG   B 1 18  ? 8.439   -16.047 36.543  1.00 29.41  ?  18  ARG   B O   1 
ATOM   3815  C CB  . ARG   B 1 18  ? 9.247   -17.217 39.448  1.00 31.54  ?  18  ARG   B CB  1 
ATOM   3816  C CG  . ARG   B 1 18  ? 7.771   -17.586 39.299  1.00 40.05  ?  18  ARG   B CG  1 
ATOM   3817  C CD  . ARG   B 1 18  ? 7.395   -18.842 40.097  1.00 44.52  ?  18  ARG   B CD  1 
ATOM   3818  N NE  . ARG   B 1 18  ? 7.978   -20.055 39.533  1.00 39.25  ?  18  ARG   B NE  1 
ATOM   3819  C CZ  . ARG   B 1 18  ? 7.395   -20.807 38.609  1.00 39.94  ?  18  ARG   B CZ  1 
ATOM   3820  N NH1 . ARG   B 1 18  ? 6.200   -20.506 38.124  1.00 43.54  ?  18  ARG   B NH1 1 
ATOM   3821  N NH2 . ARG   B 1 18  ? 8.030   -21.885 38.154  1.00 42.46  ?  18  ARG   B NH2 1 
ATOM   3822  N N   . VAL   B 1 19  ? 10.519  -16.925 36.532  1.00 32.59  ?  19  VAL   B N   1 
ATOM   3823  C CA  . VAL   B 1 19  ? 10.438  -17.464 35.180  1.00 33.76  ?  19  VAL   B CA  1 
ATOM   3824  C C   . VAL   B 1 19  ? 9.971   -18.913 35.294  1.00 35.86  ?  19  VAL   B C   1 
ATOM   3825  O O   . VAL   B 1 19  ? 10.714  -19.746 35.839  1.00 32.32  ?  19  VAL   B O   1 
ATOM   3826  C CB  . VAL   B 1 19  ? 11.783  -17.371 34.449  1.00 28.17  ?  19  VAL   B CB  1 
ATOM   3827  C CG1 . VAL   B 1 19  ? 11.661  -17.977 33.064  1.00 25.57  ?  19  VAL   B CG1 1 
ATOM   3828  C CG2 . VAL   B 1 19  ? 12.241  -15.927 34.364  1.00 28.19  ?  19  VAL   B CG2 1 
ATOM   3829  N N   . PRO   B 1 20  ? 8.764   -19.245 34.846  1.00 37.02  ?  20  PRO   B N   1 
ATOM   3830  C CA  . PRO   B 1 20  ? 8.396   -20.659 34.749  1.00 41.69  ?  20  PRO   B CA  1 
ATOM   3831  C C   . PRO   B 1 20  ? 9.319   -21.361 33.764  1.00 43.33  ?  20  PRO   B C   1 
ATOM   3832  O O   . PRO   B 1 20  ? 9.770   -20.773 32.778  1.00 42.28  ?  20  PRO   B O   1 
ATOM   3833  C CB  . PRO   B 1 20  ? 6.948   -20.621 34.243  1.00 35.06  ?  20  PRO   B CB  1 
ATOM   3834  C CG  . PRO   B 1 20  ? 6.469   -19.235 34.548  1.00 33.16  ?  20  PRO   B CG  1 
ATOM   3835  C CD  . PRO   B 1 20  ? 7.676   -18.358 34.407  1.00 32.77  ?  20  PRO   B CD  1 
ATOM   3836  N N   . SER   B 1 21  ? 9.616   -22.624 34.051  1.00 44.38  ?  21  SER   B N   1 
ATOM   3837  C CA  . SER   B 1 21  ? 10.453  -23.397 33.146  1.00 48.07  ?  21  SER   B CA  1 
ATOM   3838  C C   . SER   B 1 21  ? 9.772   -23.516 31.791  1.00 45.96  ?  21  SER   B C   1 
ATOM   3839  O O   . SER   B 1 21  ? 8.546   -23.423 31.682  1.00 46.73  ?  21  SER   B O   1 
ATOM   3840  C CB  . SER   B 1 21  ? 10.735  -24.786 33.720  1.00 47.84  ?  21  SER   B CB  1 
ATOM   3841  O OG  . SER   B 1 21  ? 9.573   -25.597 33.691  1.00 48.15  ?  21  SER   B OG  1 
ATOM   3842  N N   . ARG   B 1 22  ? 10.592  -23.705 30.752  1.00 43.98  ?  22  ARG   B N   1 
ATOM   3843  C CA  . ARG   B 1 22  ? 10.071  -23.840 29.395  1.00 44.77  ?  22  ARG   B CA  1 
ATOM   3844  C C   . ARG   B 1 22  ? 8.899   -24.808 29.350  1.00 44.60  ?  22  ARG   B C   1 
ATOM   3845  O O   . ARG   B 1 22  ? 7.882   -24.540 28.700  1.00 44.97  ?  22  ARG   B O   1 
ATOM   3846  C CB  . ARG   B 1 22  ? 11.191  -24.300 28.460  1.00 44.88  ?  22  ARG   B CB  1 
ATOM   3847  C CG  . ARG   B 1 22  ? 10.747  -24.686 27.057  1.00 49.02  ?  22  ARG   B CG  1 
ATOM   3848  C CD  . ARG   B 1 22  ? 9.961   -23.570 26.401  1.00 46.54  ?  22  ARG   B CD  1 
ATOM   3849  N NE  . ARG   B 1 22  ? 9.622   -23.866 25.013  1.00 47.80  ?  22  ARG   B NE  1 
ATOM   3850  C CZ  . ARG   B 1 22  ? 10.184  -23.279 23.967  1.00 43.89  ?  22  ARG   B CZ  1 
ATOM   3851  N NH1 . ARG   B 1 22  ? 11.136  -22.372 24.116  1.00 47.11  ?  22  ARG   B NH1 1 
ATOM   3852  N NH2 . ARG   B 1 22  ? 9.775   -23.602 22.743  1.00 46.07  ?  22  ARG   B NH2 1 
ATOM   3853  N N   . GLU   B 1 23  ? 9.014   -25.923 30.069  1.00 43.95  ?  23  GLU   B N   1 
ATOM   3854  C CA  . GLU   B 1 23  ? 7.954   -26.923 30.075  1.00 46.09  ?  23  GLU   B CA  1 
ATOM   3855  C C   . GLU   B 1 23  ? 6.706   -26.404 30.781  1.00 44.96  ?  23  GLU   B C   1 
ATOM   3856  O O   . GLU   B 1 23  ? 5.583   -26.638 30.318  1.00 43.40  ?  23  GLU   B O   1 
ATOM   3857  C CB  . GLU   B 1 23  ? 8.465   -28.209 30.728  1.00 45.67  ?  23  GLU   B CB  1 
ATOM   3858  C CG  . GLU   B 1 23  ? 9.539   -28.943 29.903  1.00 48.92  ?  23  GLU   B CG  1 
ATOM   3859  C CD  . GLU   B 1 23  ? 10.925  -28.306 29.989  1.00 45.96  ?  23  GLU   B CD  1 
ATOM   3860  O OE1 . GLU   B 1 23  ? 11.139  -27.450 30.876  1.00 54.54  ?  23  GLU   B OE1 1 
ATOM   3861  O OE2 . GLU   B 1 23  ? 11.803  -28.665 29.171  1.00 44.02  ?  23  GLU   B OE2 1 
ATOM   3862  N N   . GLU   B 1 24  ? 6.881   -25.690 31.899  1.00 47.45  ?  24  GLU   B N   1 
ATOM   3863  C CA  . GLU   B 1 24  ? 5.738   -25.089 32.584  1.00 42.76  ?  24  GLU   B CA  1 
ATOM   3864  C C   . GLU   B 1 24  ? 4.958   -24.167 31.656  1.00 42.59  ?  24  GLU   B C   1 
ATOM   3865  O O   . GLU   B 1 24  ? 3.720   -24.160 31.664  1.00 42.39  ?  24  GLU   B O   1 
ATOM   3866  C CB  . GLU   B 1 24  ? 6.202   -24.311 33.812  1.00 41.10  ?  24  GLU   B CB  1 
ATOM   3867  C CG  . GLU   B 1 24  ? 6.737   -25.159 34.942  1.00 42.95  ?  24  GLU   B CG  1 
ATOM   3868  C CD  . GLU   B 1 24  ? 6.930   -24.350 36.204  1.00 45.36  ?  24  GLU   B CD  1 
ATOM   3869  O OE1 . GLU   B 1 24  ? 5.979   -23.643 36.600  1.00 48.70  ?  24  GLU   B OE1 1 
ATOM   3870  O OE2 . GLU   B 1 24  ? 8.033   -24.403 36.791  1.00 49.91  ?  24  GLU   B OE2 1 
ATOM   3871  N N   . ARG   B 1 25  ? 5.668   -23.374 30.853  1.00 40.96  ?  25  ARG   B N   1 
ATOM   3872  C CA  . ARG   B 1 25  ? 4.995   -22.486 29.914  1.00 41.52  ?  25  ARG   B CA  1 
ATOM   3873  C C   . ARG   B 1 25  ? 4.326   -23.275 28.797  1.00 44.96  ?  25  ARG   B C   1 
ATOM   3874  O O   . ARG   B 1 25  ? 3.239   -22.906 28.333  1.00 43.70  ?  25  ARG   B O   1 
ATOM   3875  C CB  . ARG   B 1 25  ? 5.998   -21.481 29.352  1.00 42.99  ?  25  ARG   B CB  1 
ATOM   3876  C CG  . ARG   B 1 25  ? 6.871   -20.848 30.425  1.00 40.69  ?  25  ARG   B CG  1 
ATOM   3877  C CD  . ARG   B 1 25  ? 7.669   -19.682 29.881  1.00 38.80  ?  25  ARG   B CD  1 
ATOM   3878  N NE  . ARG   B 1 25  ? 8.691   -20.088 28.926  1.00 38.46  ?  25  ARG   B NE  1 
ATOM   3879  C CZ  . ARG   B 1 25  ? 9.979   -20.204 29.217  1.00 39.50  ?  25  ARG   B CZ  1 
ATOM   3880  N NH1 . ARG   B 1 25  ? 10.435  -19.975 30.439  1.00 34.21  ?  25  ARG   B NH1 1 
ATOM   3881  N NH2 . ARG   B 1 25  ? 10.834  -20.546 28.253  1.00 43.83  ?  25  ARG   B NH2 1 
ATOM   3882  N N   . GLU   B 1 26  ? 4.956   -24.369 28.358  1.00 45.69  ?  26  GLU   B N   1 
ATOM   3883  C CA  . GLU   B 1 26  ? 4.347   -25.212 27.335  1.00 44.00  ?  26  GLU   B CA  1 
ATOM   3884  C C   . GLU   B 1 26  ? 3.049   -25.839 27.834  1.00 45.35  ?  26  GLU   B C   1 
ATOM   3885  O O   . GLU   B 1 26  ? 2.063   -25.917 27.091  1.00 45.58  ?  26  GLU   B O   1 
ATOM   3886  C CB  . GLU   B 1 26  ? 5.330   -26.298 26.890  1.00 44.30  ?  26  GLU   B CB  1 
ATOM   3887  C CG  . GLU   B 1 26  ? 6.400   -25.832 25.906  1.00 45.26  ?  26  GLU   B CG  1 
ATOM   3888  C CD  . GLU   B 1 26  ? 5.860   -25.630 24.501  1.00 49.69  ?  26  GLU   B CD  1 
ATOM   3889  O OE1 . GLU   B 1 26  ? 4.645   -25.830 24.290  1.00 55.21  ?  26  GLU   B OE1 1 
ATOM   3890  O OE2 . GLU   B 1 26  ? 6.653   -25.276 23.600  1.00 57.87  ?  26  GLU   B OE2 1 
ATOM   3891  N N   . ALA   B 1 27  ? 3.029   -26.290 29.091  1.00 41.13  ?  27  ALA   B N   1 
ATOM   3892  C CA  . ALA   B 1 27  ? 1.816   -26.890 29.638  1.00 44.53  ?  27  ALA   B CA  1 
ATOM   3893  C C   . ALA   B 1 27  ? 0.748   -25.834 29.880  1.00 46.75  ?  27  ALA   B C   1 
ATOM   3894  O O   . ALA   B 1 27  ? -0.411  -26.006 29.483  1.00 47.07  ?  27  ALA   B O   1 
ATOM   3895  C CB  . ALA   B 1 27  ? 2.132   -27.640 30.933  1.00 39.89  ?  27  ALA   B CB  1 
ATOM   3896  N N   . ALA   B 1 28  ? 1.129   -24.725 30.520  1.00 42.02  ?  28  ALA   B N   1 
ATOM   3897  C CA  . ALA   B 1 28  ? 0.154   -23.696 30.867  1.00 44.90  ?  28  ALA   B CA  1 
ATOM   3898  C C   . ALA   B 1 28  ? -0.502  -23.103 29.626  1.00 41.04  ?  28  ALA   B C   1 
ATOM   3899  O O   . ALA   B 1 28  ? -1.719  -22.885 29.607  1.00 42.11  ?  28  ALA   B O   1 
ATOM   3900  C CB  . ALA   B 1 28  ? 0.819   -22.601 31.705  1.00 41.03  ?  28  ALA   B CB  1 
ATOM   3901  N N   . LEU   B 1 29  ? 0.281   -22.834 28.578  1.00 37.69  ?  29  LEU   B N   1 
ATOM   3902  C CA  . LEU   B 1 29  ? -0.311  -22.243 27.381  1.00 43.59  ?  29  LEU   B CA  1 
ATOM   3903  C C   . LEU   B 1 29  ? -1.280  -23.205 26.705  1.00 47.09  ?  29  LEU   B C   1 
ATOM   3904  O O   . LEU   B 1 29  ? -2.277  -22.769 26.115  1.00 43.11  ?  29  LEU   B O   1 
ATOM   3905  C CB  . LEU   B 1 29  ? 0.783   -21.805 26.403  1.00 43.91  ?  29  LEU   B CB  1 
ATOM   3906  C CG  . LEU   B 1 29  ? 0.315   -20.999 25.182  1.00 40.98  ?  29  LEU   B CG  1 
ATOM   3907  C CD1 . LEU   B 1 29  ? -0.560  -19.833 25.608  1.00 40.55  ?  29  LEU   B CD1 1 
ATOM   3908  C CD2 . LEU   B 1 29  ? 1.500   -20.489 24.373  1.00 38.60  ?  29  LEU   B CD2 1 
ATOM   3909  N N   . LYS   B 1 30  ? -1.006  -24.510 26.785  1.00 49.35  ?  30  LYS   B N   1 
ATOM   3910  C CA  . LYS   B 1 30  ? -1.946  -25.494 26.263  1.00 47.23  ?  30  LYS   B CA  1 
ATOM   3911  C C   . LYS   B 1 30  ? -3.202  -25.566 27.126  1.00 45.18  ?  30  LYS   B C   1 
ATOM   3912  O O   . LYS   B 1 30  ? -4.319  -25.607 26.598  1.00 46.25  ?  30  LYS   B O   1 
ATOM   3913  C CB  . LYS   B 1 30  ? -1.268  -26.859 26.161  1.00 50.96  ?  30  LYS   B CB  1 
ATOM   3914  C CG  . LYS   B 1 30  ? -0.161  -26.928 25.113  1.00 60.65  ?  30  LYS   B CG  1 
ATOM   3915  C CD  . LYS   B 1 30  ? 0.489   -28.312 25.091  1.00 74.66  ?  30  LYS   B CD  1 
ATOM   3916  C CE  . LYS   B 1 30  ? 1.509   -28.448 23.961  1.00 74.88  ?  30  LYS   B CE  1 
ATOM   3917  N NZ  . LYS   B 1 30  ? 2.110   -29.816 23.907  1.00 63.78  ?  30  LYS   B NZ  1 
ATOM   3918  N N   . GLU   B 1 31  ? -3.044  -25.575 28.456  1.00 39.71  ?  31  GLU   B N   1 
ATOM   3919  C CA  . GLU   B 1 31  ? -4.216  -25.522 29.326  1.00 43.21  ?  31  GLU   B CA  1 
ATOM   3920  C C   . GLU   B 1 31  ? -5.038  -24.265 29.063  1.00 46.53  ?  31  GLU   B C   1 
ATOM   3921  O O   . GLU   B 1 31  ? -6.274  -24.310 29.061  1.00 48.21  ?  31  GLU   B O   1 
ATOM   3922  C CB  . GLU   B 1 31  ? -3.805  -25.587 30.798  1.00 46.18  ?  31  GLU   B CB  1 
ATOM   3923  C CG  . GLU   B 1 31  ? -4.898  -25.075 31.736  1.00 50.85  ?  31  GLU   B CG  1 
ATOM   3924  C CD  . GLU   B 1 31  ? -4.709  -25.489 33.182  1.00 59.71  ?  31  GLU   B CD  1 
ATOM   3925  O OE1 . GLU   B 1 31  ? -3.820  -26.325 33.459  1.00 64.48  ?  31  GLU   B OE1 1 
ATOM   3926  O OE2 . GLU   B 1 31  ? -5.460  -24.978 34.044  1.00 61.62  ?  31  GLU   B OE2 1 
ATOM   3927  N N   . ALA   B 1 32  ? -4.367  -23.135 28.829  1.00 45.92  ?  32  ALA   B N   1 
ATOM   3928  C CA  . ALA   B 1 32  ? -5.048  -21.890 28.500  1.00 39.11  ?  32  ALA   B CA  1 
ATOM   3929  C C   . ALA   B 1 32  ? -5.595  -21.876 27.082  1.00 45.12  ?  32  ALA   B C   1 
ATOM   3930  O O   . ALA   B 1 32  ? -6.138  -20.848 26.658  1.00 45.31  ?  32  ALA   B O   1 
ATOM   3931  C CB  . ALA   B 1 32  ? -4.100  -20.706 28.700  1.00 35.77  ?  32  ALA   B CB  1 
ATOM   3932  N N   . GLY   B 1 33  ? -5.469  -22.974 26.344  1.00 47.31  ?  33  GLY   B N   1 
ATOM   3933  C CA  . GLY   B 1 33  ? -5.982  -23.008 24.988  1.00 50.71  ?  33  GLY   B CA  1 
ATOM   3934  C C   . GLY   B 1 33  ? -5.323  -22.000 24.078  1.00 45.14  ?  33  GLY   B C   1 
ATOM   3935  O O   . GLY   B 1 33  ? -6.007  -21.348 23.279  1.00 46.45  ?  33  GLY   B O   1 
ATOM   3936  N N   . TYR   B 1 34  ? -4.004  -21.837 24.203  1.00 40.22  ?  34  TYR   B N   1 
ATOM   3937  C CA  . TYR   B 1 34  ? -3.228  -20.937 23.344  1.00 47.29  ?  34  TYR   B CA  1 
ATOM   3938  C C   . TYR   B 1 34  ? -3.792  -19.512 23.352  1.00 43.47  ?  34  TYR   B C   1 
ATOM   3939  O O   . TYR   B 1 34  ? -3.697  -18.777 22.364  1.00 41.98  ?  34  TYR   B O   1 
ATOM   3940  C CB  . TYR   B 1 34  ? -3.127  -21.498 21.918  1.00 46.72  ?  34  TYR   B CB  1 
ATOM   3941  C CG  . TYR   B 1 34  ? -2.331  -22.786 21.860  1.00 48.81  ?  34  TYR   B CG  1 
ATOM   3942  C CD1 . TYR   B 1 34  ? -2.912  -24.003 22.208  1.00 53.23  ?  34  TYR   B CD1 1 
ATOM   3943  C CD2 . TYR   B 1 34  ? -0.994  -22.786 21.485  1.00 48.95  ?  34  TYR   B CD2 1 
ATOM   3944  C CE1 . TYR   B 1 34  ? -2.187  -25.186 22.174  1.00 57.92  ?  34  TYR   B CE1 1 
ATOM   3945  C CE2 . TYR   B 1 34  ? -0.257  -23.965 21.446  1.00 58.84  ?  34  TYR   B CE2 1 
ATOM   3946  C CZ  . TYR   B 1 34  ? -0.859  -25.164 21.794  1.00 65.01  ?  34  TYR   B CZ  1 
ATOM   3947  O OH  . TYR   B 1 34  ? -0.137  -26.342 21.758  1.00 58.94  ?  34  TYR   B OH  1 
ATOM   3948  N N   . ASN   B 1 35  ? -4.376  -19.113 24.477  1.00 38.99  ?  35  ASN   B N   1 
ATOM   3949  C CA  . ASN   B 1 35  ? -4.830  -17.740 24.685  1.00 36.16  ?  35  ASN   B CA  1 
ATOM   3950  C C   . ASN   B 1 35  ? -4.257  -17.237 26.002  1.00 34.82  ?  35  ASN   B C   1 
ATOM   3951  O O   . ASN   B 1 35  ? -4.745  -17.640 27.078  1.00 32.74  ?  35  ASN   B O   1 
ATOM   3952  C CB  . ASN   B 1 35  ? -6.353  -17.654 24.678  1.00 33.73  ?  35  ASN   B CB  1 
ATOM   3953  C CG  . ASN   B 1 35  ? -6.854  -16.236 24.859  1.00 36.83  ?  35  ASN   B CG  1 
ATOM   3954  O OD1 . ASN   B 1 35  ? -6.073  -15.281 24.868  1.00 38.70  ?  35  ASN   B OD1 1 
ATOM   3955  N ND2 . ASN   B 1 35  ? -8.165  -16.088 25.000  1.00 38.96  ?  35  ASN   B ND2 1 
ATOM   3956  N N   . PRO   B 1 36  ? -3.242  -16.370 25.977  1.00 32.67  ?  36  PRO   B N   1 
ATOM   3957  C CA  . PRO   B 1 36  ? -2.628  -15.919 27.238  1.00 30.30  ?  36  PRO   B CA  1 
ATOM   3958  C C   . PRO   B 1 36  ? -3.582  -15.208 28.188  1.00 26.82  ?  36  PRO   B C   1 
ATOM   3959  O O   . PRO   B 1 36  ? -3.273  -15.113 29.383  1.00 26.39  ?  36  PRO   B O   1 
ATOM   3960  C CB  . PRO   B 1 36  ? -1.498  -14.986 26.772  1.00 26.54  ?  36  PRO   B CB  1 
ATOM   3961  C CG  . PRO   B 1 36  ? -1.744  -14.742 25.313  1.00 32.45  ?  36  PRO   B CG  1 
ATOM   3962  C CD  . PRO   B 1 36  ? -2.477  -15.932 24.801  1.00 33.22  ?  36  PRO   B CD  1 
ATOM   3963  N N   . PHE   B 1 37  ? -4.726  -14.712 27.709  1.00 29.85  ?  37  PHE   B N   1 
ATOM   3964  C CA  . PHE   B 1 37  ? -5.709  -14.108 28.606  1.00 29.31  ?  37  PHE   B CA  1 
ATOM   3965  C C   . PHE   B 1 37  ? -6.257  -15.113 29.613  1.00 27.58  ?  37  PHE   B C   1 
ATOM   3966  O O   . PHE   B 1 37  ? -6.788  -14.709 30.653  1.00 27.61  ?  37  PHE   B O   1 
ATOM   3967  C CB  . PHE   B 1 37  ? -6.864  -13.506 27.799  1.00 27.93  ?  37  PHE   B CB  1 
ATOM   3968  C CG  . PHE   B 1 37  ? -6.845  -12.000 27.716  1.00 27.88  ?  37  PHE   B CG  1 
ATOM   3969  C CD1 . PHE   B 1 37  ? -7.168  -11.227 28.819  1.00 27.80  ?  37  PHE   B CD1 1 
ATOM   3970  C CD2 . PHE   B 1 37  ? -6.542  -11.360 26.525  1.00 33.68  ?  37  PHE   B CD2 1 
ATOM   3971  C CE1 . PHE   B 1 37  ? -7.166  -9.844  28.737  1.00 27.62  ?  37  PHE   B CE1 1 
ATOM   3972  C CE2 . PHE   B 1 37  ? -6.544  -9.977  26.439  1.00 30.32  ?  37  PHE   B CE2 1 
ATOM   3973  C CZ  . PHE   B 1 37  ? -6.850  -9.222  27.550  1.00 28.83  ?  37  PHE   B CZ  1 
ATOM   3974  N N   . LEU   B 1 38  ? -6.131  -16.408 29.327  1.00 32.32  ?  38  LEU   B N   1 
ATOM   3975  C CA  . LEU   B 1 38  ? -6.583  -17.479 30.204  1.00 31.74  ?  38  LEU   B CA  1 
ATOM   3976  C C   . LEU   B 1 38  ? -5.467  -18.062 31.062  1.00 27.47  ?  38  LEU   B C   1 
ATOM   3977  O O   . LEU   B 1 38  ? -5.728  -18.966 31.864  1.00 31.59  ?  38  LEU   B O   1 
ATOM   3978  C CB  . LEU   B 1 38  ? -7.226  -18.590 29.371  1.00 31.91  ?  38  LEU   B CB  1 
ATOM   3979  C CG  . LEU   B 1 38  ? -8.379  -18.096 28.503  1.00 35.73  ?  38  LEU   B CG  1 
ATOM   3980  C CD1 . LEU   B 1 38  ? -9.022  -19.264 27.771  1.00 38.28  ?  38  LEU   B CD1 1 
ATOM   3981  C CD2 . LEU   B 1 38  ? -9.403  -17.325 29.352  1.00 33.27  ?  38  LEU   B CD2 1 
ATOM   3982  N N   . LEU   B 1 39  ? -4.237  -17.579 30.913  1.00 25.91  ?  39  LEU   B N   1 
ATOM   3983  C CA  . LEU   B 1 39  ? -3.156  -18.027 31.780  1.00 25.11  ?  39  LEU   B CA  1 
ATOM   3984  C C   . LEU   B 1 39  ? -3.302  -17.390 33.160  1.00 25.59  ?  39  LEU   B C   1 
ATOM   3985  O O   . LEU   B 1 39  ? -3.677  -16.216 33.266  1.00 23.94  ?  39  LEU   B O   1 
ATOM   3986  C CB  . LEU   B 1 39  ? -1.792  -17.655 31.188  1.00 24.15  ?  39  LEU   B CB  1 
ATOM   3987  C CG  . LEU   B 1 39  ? -1.285  -18.323 29.908  1.00 30.82  ?  39  LEU   B CG  1 
ATOM   3988  C CD1 . LEU   B 1 39  ? -0.104  -17.553 29.368  1.00 31.78  ?  39  LEU   B CD1 1 
ATOM   3989  C CD2 . LEU   B 1 39  ? -0.882  -19.753 30.178  1.00 31.03  ?  39  LEU   B CD2 1 
ATOM   3990  N N   . PRO   B 1 40  ? -3.012  -18.122 34.230  1.00 23.68  ?  40  PRO   B N   1 
ATOM   3991  C CA  . PRO   B 1 40  ? -2.944  -17.492 35.549  1.00 25.42  ?  40  PRO   B CA  1 
ATOM   3992  C C   . PRO   B 1 40  ? -1.691  -16.642 35.663  1.00 21.04  ?  40  PRO   B C   1 
ATOM   3993  O O   . PRO   B 1 40  ? -0.700  -16.859 34.963  1.00 21.76  ?  40  PRO   B O   1 
ATOM   3994  C CB  . PRO   B 1 40  ? -2.897  -18.679 36.511  1.00 22.60  ?  40  PRO   B CB  1 
ATOM   3995  C CG  . PRO   B 1 40  ? -2.259  -19.760 35.710  1.00 23.94  ?  40  PRO   B CG  1 
ATOM   3996  C CD  . PRO   B 1 40  ? -2.713  -19.561 34.288  1.00 23.29  ?  40  PRO   B CD  1 
ATOM   3997  N N   . SER   B 1 41  ? -1.746  -15.658 36.568  1.00 19.91  ?  41  SER   B N   1 
ATOM   3998  C CA  . SER   B 1 41  ? -0.592  -14.789 36.787  1.00 23.14  ?  41  SER   B CA  1 
ATOM   3999  C C   . SER   B 1 41  ? 0.637   -15.579 37.214  1.00 25.21  ?  41  SER   B C   1 
ATOM   4000  O O   . SER   B 1 41  ? 1.769   -15.141 36.979  1.00 25.70  ?  41  SER   B O   1 
ATOM   4001  C CB  . SER   B 1 41  ? -0.907  -13.734 37.844  1.00 19.64  ?  41  SER   B CB  1 
ATOM   4002  O OG  . SER   B 1 41  ? -0.827  -14.286 39.151  1.00 21.77  ?  41  SER   B OG  1 
ATOM   4003  N N   . SER   B 1 42  ? 0.440   -16.735 37.849  1.00 23.52  ?  42  SER   B N   1 
ATOM   4004  C CA  . SER   B 1 42  ? 1.579   -17.540 38.265  1.00 25.29  ?  42  SER   B CA  1 
ATOM   4005  C C   . SER   B 1 42  ? 2.328   -18.133 37.083  1.00 22.35  ?  42  SER   B C   1 
ATOM   4006  O O   . SER   B 1 42  ? 3.476   -18.553 37.245  1.00 30.78  ?  42  SER   B O   1 
ATOM   4007  C CB  . SER   B 1 42  ? 1.119   -18.655 39.207  1.00 23.96  ?  42  SER   B CB  1 
ATOM   4008  O OG  . SER   B 1 42  ? 0.270   -19.561 38.529  1.00 26.98  ?  42  SER   B OG  1 
ATOM   4009  N N   . ALA   B 1 43  ? 1.716   -18.181 35.904  1.00 23.75  ?  43  ALA   B N   1 
ATOM   4010  C CA  . ALA   B 1 43  ? 2.372   -18.720 34.720  1.00 24.73  ?  43  ALA   B CA  1 
ATOM   4011  C C   . ALA   B 1 43  ? 3.176   -17.673 33.974  1.00 29.30  ?  43  ALA   B C   1 
ATOM   4012  O O   . ALA   B 1 43  ? 3.804   -17.993 32.958  1.00 24.47  ?  43  ALA   B O   1 
ATOM   4013  C CB  . ALA   B 1 43  ? 1.345   -19.328 33.766  1.00 25.68  ?  43  ALA   B CB  1 
ATOM   4014  N N   . VAL   B 1 44  ? 3.163   -16.434 34.445  1.00 25.12  ?  44  VAL   B N   1 
ATOM   4015  C CA  . VAL   B 1 44  ? 3.707   -15.308 33.706  1.00 25.93  ?  44  VAL   B CA  1 
ATOM   4016  C C   . VAL   B 1 44  ? 4.907   -14.770 34.461  1.00 27.17  ?  44  VAL   B C   1 
ATOM   4017  O O   . VAL   B 1 44  ? 4.889   -14.672 35.693  1.00 26.59  ?  44  VAL   B O   1 
ATOM   4018  C CB  . VAL   B 1 44  ? 2.651   -14.208 33.491  1.00 23.89  ?  44  VAL   B CB  1 
ATOM   4019  C CG1 . VAL   B 1 44  ? 3.229   -13.077 32.643  1.00 23.40  ?  44  VAL   B CG1 1 
ATOM   4020  C CG2 . VAL   B 1 44  ? 1.403   -14.797 32.832  1.00 24.95  ?  44  VAL   B CG2 1 
ATOM   4021  N N   . TYR   B 1 45  ? 5.952   -14.434 33.713  1.00 26.46  ?  45  TYR   B N   1 
ATOM   4022  C CA  . TYR   B 1 45  ? 7.137   -13.811 34.271  1.00 24.81  ?  45  TYR   B CA  1 
ATOM   4023  C C   . TYR   B 1 45  ? 6.941   -12.301 34.269  1.00 26.19  ?  45  TYR   B C   1 
ATOM   4024  O O   . TYR   B 1 45  ? 6.491   -11.721 35.263  1.00 31.98  ?  45  TYR   B O   1 
ATOM   4025  C CB  . TYR   B 1 45  ? 8.359   -14.240 33.458  1.00 27.33  ?  45  TYR   B CB  1 
ATOM   4026  C CG  . TYR   B 1 45  ? 9.639   -13.530 33.805  1.00 32.65  ?  45  TYR   B CG  1 
ATOM   4027  C CD1 . TYR   B 1 45  ? 9.974   -13.264 35.122  1.00 25.22  ?  45  TYR   B CD1 1 
ATOM   4028  C CD2 . TYR   B 1 45  ? 10.525  -13.139 32.807  1.00 26.83  ?  45  TYR   B CD2 1 
ATOM   4029  C CE1 . TYR   B 1 45  ? 11.152  -12.622 35.435  1.00 28.50  ?  45  TYR   B CE1 1 
ATOM   4030  C CE2 . TYR   B 1 45  ? 11.707  -12.495 33.117  1.00 31.37  ?  45  TYR   B CE2 1 
ATOM   4031  C CZ  . TYR   B 1 45  ? 12.011  -12.237 34.432  1.00 26.60  ?  45  TYR   B CZ  1 
ATOM   4032  O OH  . TYR   B 1 45  ? 13.185  -11.592 34.743  1.00 33.04  ?  45  TYR   B OH  1 
ATOM   4033  N N   . ILE   B 1 46  ? 7.255   -11.662 33.152  1.00 24.73  ?  46  ILE   B N   1 
ATOM   4034  C CA  . ILE   B 1 46  ? 6.976   -10.244 32.952  1.00 25.51  ?  46  ILE   B CA  1 
ATOM   4035  C C   . ILE   B 1 46  ? 5.615   -10.132 32.271  1.00 18.83  ?  46  ILE   B C   1 
ATOM   4036  O O   . ILE   B 1 46  ? 5.401   -10.723 31.209  1.00 18.39  ?  46  ILE   B O   1 
ATOM   4037  C CB  . ILE   B 1 46  ? 8.085   -9.585  32.117  1.00 20.06  ?  46  ILE   B CB  1 
ATOM   4038  C CG1 . ILE   B 1 46  ? 9.410   -9.616  32.896  1.00 22.87  ?  46  ILE   B CG1 1 
ATOM   4039  C CG2 . ILE   B 1 46  ? 7.712   -8.167  31.724  1.00 13.86  ?  46  ILE   B CG2 1 
ATOM   4040  C CD1 . ILE   B 1 46  ? 10.606  -9.202  32.079  1.00 20.24  ?  46  ILE   B CD1 1 
ATOM   4041  N N   . ASP   B 1 47  ? 4.686   -9.400  32.892  1.00 16.33  ?  47  ASP   B N   1 
ATOM   4042  C CA  . ASP   B 1 47  ? 3.313   -9.286  32.400  1.00 19.20  ?  47  ASP   B CA  1 
ATOM   4043  C C   . ASP   B 1 47  ? 3.165   -7.970  31.637  1.00 19.14  ?  47  ASP   B C   1 
ATOM   4044  O O   . ASP   B 1 47  ? 3.245   -6.886  32.229  1.00 17.27  ?  47  ASP   B O   1 
ATOM   4045  C CB  . ASP   B 1 47  ? 2.317   -9.371  33.557  1.00 18.60  ?  47  ASP   B CB  1 
ATOM   4046  C CG  . ASP   B 1 47  ? 0.931   -9.839  33.118  1.00 20.76  ?  47  ASP   B CG  1 
ATOM   4047  O OD1 . ASP   B 1 47  ? 0.712   -10.009 31.897  1.00 18.96  ?  47  ASP   B OD1 1 
ATOM   4048  O OD2 . ASP   B 1 47  ? 0.067   -10.051 34.006  1.00 17.49  ?  47  ASP   B OD2 1 
ATOM   4049  N N   . LEU   B 1 48  ? 2.958   -8.071  30.320  1.00 17.67  ?  48  LEU   B N   1 
ATOM   4050  C CA  . LEU   B 1 48  ? 2.771   -6.918  29.442  1.00 16.19  ?  48  LEU   B CA  1 
ATOM   4051  C C   . LEU   B 1 48  ? 1.387   -6.921  28.806  1.00 19.39  ?  48  LEU   B C   1 
ATOM   4052  O O   . LEU   B 1 48  ? 1.184   -6.311  27.743  1.00 16.88  ?  48  LEU   B O   1 
ATOM   4053  C CB  . LEU   B 1 48  ? 3.842   -6.887  28.353  1.00 16.02  ?  48  LEU   B CB  1 
ATOM   4054  C CG  . LEU   B 1 48  ? 5.298   -6.978  28.794  1.00 15.19  ?  48  LEU   B CG  1 
ATOM   4055  C CD1 . LEU   B 1 48  ? 6.193   -6.790  27.603  1.00 13.49  ?  48  LEU   B CD1 1 
ATOM   4056  C CD2 . LEU   B 1 48  ? 5.614   -5.955  29.879  1.00 12.25  ?  48  LEU   B CD2 1 
ATOM   4057  N N   . LEU   B 1 49  ? 0.442   -7.633  29.425  1.00 15.85  ?  49  LEU   B N   1 
ATOM   4058  C CA  . LEU   B 1 49  ? -0.920  -7.690  28.911  1.00 18.46  ?  49  LEU   B CA  1 
ATOM   4059  C C   . LEU   B 1 49  ? -1.550  -6.303  28.865  1.00 16.68  ?  49  LEU   B C   1 
ATOM   4060  O O   . LEU   B 1 49  ? -2.218  -5.948  27.889  1.00 18.39  ?  49  LEU   B O   1 
ATOM   4061  C CB  . LEU   B 1 49  ? -1.751  -8.636  29.778  1.00 14.43  ?  49  LEU   B CB  1 
ATOM   4062  C CG  . LEU   B 1 49  ? -3.044  -9.165  29.162  1.00 22.93  ?  49  LEU   B CG  1 
ATOM   4063  C CD1 . LEU   B 1 49  ? -2.749  -10.125 28.016  1.00 24.61  ?  49  LEU   B CD1 1 
ATOM   4064  C CD2 . LEU   B 1 49  ? -3.892  -9.829  30.216  1.00 22.33  ?  49  LEU   B CD2 1 
ATOM   4065  N N   . THR   B 1 50  ? -1.337  -5.502  29.904  1.00 16.93  ?  50  THR   B N   1 
ATOM   4066  C CA  . THR   B 1 50  ? -1.926  -4.178  29.979  1.00 18.20  ?  50  THR   B CA  1 
ATOM   4067  C C   . THR   B 1 50  ? -1.065  -3.274  30.842  1.00 17.70  ?  50  THR   B C   1 
ATOM   4068  O O   . THR   B 1 50  ? -0.213  -3.731  31.611  1.00 19.34  ?  50  THR   B O   1 
ATOM   4069  C CB  . THR   B 1 50  ? -3.331  -4.212  30.574  1.00 16.87  ?  50  THR   B CB  1 
ATOM   4070  O OG1 . THR   B 1 50  ? -3.875  -2.891  30.519  1.00 26.79  ?  50  THR   B OG1 1 
ATOM   4071  C CG2 . THR   B 1 50  ? -3.260  -4.615  32.020  1.00 14.69  ?  50  THR   B CG2 1 
ATOM   4072  N N   . ASP   B 1 51  ? -1.323  -1.973  30.725  1.00 16.11  ?  51  ASP   B N   1 
ATOM   4073  C CA  . ASP   B 1 51  ? -0.835  -0.996  31.686  1.00 15.31  ?  51  ASP   B CA  1 
ATOM   4074  C C   . ASP   B 1 51  ? -1.942  -0.509  32.617  1.00 17.76  ?  51  ASP   B C   1 
ATOM   4075  O O   . ASP   B 1 51  ? -1.823  0.572   33.200  1.00 18.13  ?  51  ASP   B O   1 
ATOM   4076  C CB  . ASP   B 1 51  ? -0.212  0.192   30.959  1.00 17.77  ?  51  ASP   B CB  1 
ATOM   4077  C CG  . ASP   B 1 51  ? -1.238  1.001   30.223  1.00 17.09  ?  51  ASP   B CG  1 
ATOM   4078  O OD1 . ASP   B 1 51  ? -2.166  0.388   29.659  1.00 20.31  ?  51  ASP   B OD1 1 
ATOM   4079  O OD2 . ASP   B 1 51  ? -1.140  2.244   30.218  1.00 18.49  ?  51  ASP   B OD2 1 
ATOM   4080  N N   . SER   B 1 52  ? -3.010  -1.286  32.775  1.00 20.49  ?  52  SER   B N   1 
ATOM   4081  C CA  . SER   B 1 52  ? -4.208  -0.850  33.486  1.00 18.38  ?  52  SER   B CA  1 
ATOM   4082  C C   . SER   B 1 52  ? -4.267  -1.526  34.847  1.00 16.41  ?  52  SER   B C   1 
ATOM   4083  O O   . SER   B 1 52  ? -4.425  -2.747  34.931  1.00 18.86  ?  52  SER   B O   1 
ATOM   4084  C CB  . SER   B 1 52  ? -5.460  -1.169  32.672  1.00 16.68  ?  52  SER   B CB  1 
ATOM   4085  O OG  . SER   B 1 52  ? -6.625  -0.741  33.348  1.00 20.02  ?  52  SER   B OG  1 
ATOM   4086  N N   . GLY   B 1 53  ? -4.156  -0.734  35.911  1.00 14.73  ?  53  GLY   B N   1 
ATOM   4087  C CA  . GLY   B 1 53  ? -4.350  -1.239  37.245  1.00 14.91  ?  53  GLY   B CA  1 
ATOM   4088  C C   . GLY   B 1 53  ? -3.180  -1.982  37.835  1.00 16.98  ?  53  GLY   B C   1 
ATOM   4089  O O   . GLY   B 1 53  ? -3.263  -2.404  38.992  1.00 16.87  ?  53  GLY   B O   1 
ATOM   4090  N N   . THR   B 1 54  ? -2.091  -2.148  37.091  1.00 17.48  ?  54  THR   B N   1 
ATOM   4091  C CA  . THR   B 1 54  ? -0.916  -2.876  37.548  1.00 16.80  ?  54  THR   B CA  1 
ATOM   4092  C C   . THR   B 1 54  ? 0.209   -1.949  37.988  1.00 16.85  ?  54  THR   B C   1 
ATOM   4093  O O   . THR   B 1 54  ? 1.335   -2.409  38.193  1.00 19.42  ?  54  THR   B O   1 
ATOM   4094  C CB  . THR   B 1 54  ? -0.420  -3.799  36.434  1.00 13.65  ?  54  THR   B CB  1 
ATOM   4095  O OG1 . THR   B 1 54  ? -0.120  -3.006  35.287  1.00 15.37  ?  54  THR   B OG1 1 
ATOM   4096  C CG2 . THR   B 1 54  ? -1.505  -4.801  36.044  1.00 14.92  ?  54  THR   B CG2 1 
ATOM   4097  N N   . ASN   B 1 55  ? -0.065  -0.657  38.134  1.00 13.86  ?  55  ASN   B N   1 
ATOM   4098  C CA  . ASN   B 1 55  ? 0.987   0.296   38.439  1.00 14.04  ?  55  ASN   B CA  1 
ATOM   4099  C C   . ASN   B 1 55  ? 1.479   0.136   39.873  1.00 12.40  ?  55  ASN   B C   1 
ATOM   4100  O O   . ASN   B 1 55  ? 0.795   -0.406  40.745  1.00 15.54  ?  55  ASN   B O   1 
ATOM   4101  C CB  . ASN   B 1 55  ? 0.487   1.721   38.216  1.00 12.39  ?  55  ASN   B CB  1 
ATOM   4102  C CG  . ASN   B 1 55  ? -0.190  1.882   36.886  1.00 16.40  ?  55  ASN   B CG  1 
ATOM   4103  O OD1 . ASN   B 1 55  ? 0.467   1.973   35.857  1.00 16.73  ?  55  ASN   B OD1 1 
ATOM   4104  N ND2 . ASN   B 1 55  ? -1.516  1.897   36.891  1.00 14.80  ?  55  ASN   B ND2 1 
ATOM   4105  N N   . ALA   B 1 56  ? 2.691   0.630   40.110  1.00 12.18  ?  56  ALA   B N   1 
ATOM   4106  C CA  . ALA   B 1 56  ? 3.259   0.693   41.447  1.00 14.03  ?  56  ALA   B CA  1 
ATOM   4107  C C   . ALA   B 1 56  ? 2.967   2.061   42.048  1.00 12.81  ?  56  ALA   B C   1 
ATOM   4108  O O   . ALA   B 1 56  ? 3.281   3.092   41.442  1.00 14.61  ?  56  ALA   B O   1 
ATOM   4109  C CB  . ALA   B 1 56  ? 4.767   0.436   41.416  1.00 12.16  ?  56  ALA   B CB  1 
ATOM   4110  N N   . MET   B 1 57  ? 2.360   2.065   43.230  1.00 14.42  ?  57  MET   B N   1 
ATOM   4111  C CA  . MET   B 1 57  ? 2.007   3.292   43.923  1.00 13.70  ?  57  MET   B CA  1 
ATOM   4112  C C   . MET   B 1 57  ? 3.174   3.782   44.773  1.00 14.37  ?  57  MET   B C   1 
ATOM   4113  O O   . MET   B 1 57  ? 4.130   3.050   45.034  1.00 14.23  ?  57  MET   B O   1 
ATOM   4114  C CB  . MET   B 1 57  ? 0.761   3.076   44.788  1.00 16.54  ?  57  MET   B CB  1 
ATOM   4115  C CG  . MET   B 1 57  ? -0.534  2.863   43.987  1.00 13.08  ?  57  MET   B CG  1 
ATOM   4116  S SD  . MET   B 1 57  ? -1.997  2.984   45.045  1.00 17.14  ?  57  MET   B SD  1 
ATOM   4117  C CE  . MET   B 1 57  ? -1.786  1.516   46.042  1.00 16.92  ?  57  MET   B CE  1 
ATOM   4118  N N   . SER   B 1 58  ? 3.098   5.048   45.186  1.00 14.17  ?  58  SER   B N   1 
ATOM   4119  C CA  . SER   B 1 58  ? 4.120   5.639   46.039  1.00 15.88  ?  58  SER   B CA  1 
ATOM   4120  C C   . SER   B 1 58  ? 3.770   5.440   47.512  1.00 15.60  ?  58  SER   B C   1 
ATOM   4121  O O   . SER   B 1 58  ? 2.658   5.047   47.871  1.00 15.31  ?  58  SER   B O   1 
ATOM   4122  C CB  . SER   B 1 58  ? 4.275   7.131   45.750  1.00 14.04  ?  58  SER   B CB  1 
ATOM   4123  O OG  . SER   B 1 58  ? 3.182   7.844   46.302  1.00 17.74  ?  58  SER   B OG  1 
ATOM   4124  N N   . ASP   B 1 59  ? 4.717   5.780   48.368  1.00 16.08  ?  59  ASP   B N   1 
ATOM   4125  C CA  . ASP   B 1 59  ? 4.435   5.703   49.815  1.00 17.11  ?  59  ASP   B CA  1 
ATOM   4126  C C   . ASP   B 1 59  ? 3.358   6.726   50.185  1.00 14.52  ?  59  ASP   B C   1 
ATOM   4127  O O   . ASP   B 1 59  ? 2.514   6.417   51.017  1.00 15.01  ?  59  ASP   B O   1 
ATOM   4128  C CB  . ASP   B 1 59  ? 5.703   5.904   50.614  1.00 16.01  ?  59  ASP   B CB  1 
ATOM   4129  C CG  . ASP   B 1 59  ? 6.536   7.104   50.209  1.00 18.72  ?  59  ASP   B CG  1 
ATOM   4130  O OD1 . ASP   B 1 59  ? 6.158   7.782   49.238  1.00 24.72  ?  59  ASP   B OD1 1 
ATOM   4131  O OD2 . ASP   B 1 59  ? 7.551   7.329   50.869  1.00 18.57  ?  59  ASP   B OD2 1 
ATOM   4132  N N   . HIS   B 1 60  ? 3.402   7.896   49.549  1.00 14.54  ?  60  HIS   B N   1 
ATOM   4133  C CA  . HIS   B 1 60  ? 2.365   8.892   49.816  1.00 14.26  ?  60  HIS   B CA  1 
ATOM   4134  C C   . HIS   B 1 60  ? 0.993   8.387   49.420  1.00 16.57  ?  60  HIS   B C   1 
ATOM   4135  O O   . HIS   B 1 60  ? -0.005  8.702   50.081  1.00 15.48  ?  60  HIS   B O   1 
ATOM   4136  C CB  . HIS   B 1 60  ? 2.674   10.195  49.086  1.00 18.58  ?  60  HIS   B CB  1 
ATOM   4137  C CG  . HIS   B 1 60  ? 3.905   10.864  49.596  1.00 24.16  ?  60  HIS   B CG  1 
ATOM   4138  N ND1 . HIS   B 1 60  ? 3.997   11.357  50.877  1.00 24.06  ?  60  HIS   B ND1 1 
ATOM   4139  C CD2 . HIS   B 1 60  ? 5.110   11.077  49.021  1.00 29.80  ?  60  HIS   B CD2 1 
ATOM   4140  C CE1 . HIS   B 1 60  ? 5.205   11.853  51.070  1.00 26.67  ?  60  HIS   B CE1 1 
ATOM   4141  N NE2 . HIS   B 1 60  ? 5.899   11.701  49.956  1.00 30.04  ?  60  HIS   B NE2 1 
ATOM   4142  N N   . GLN   B 1 61  ? 0.912   7.637   48.322  1.00 13.20  ?  61  GLN   B N   1 
ATOM   4143  C CA  . GLN   B 1 61  ? -0.366  7.059   47.929  1.00 15.15  ?  61  GLN   B CA  1 
ATOM   4144  C C   . GLN   B 1 61  ? -0.864  6.077   48.979  1.00 15.49  ?  61  GLN   B C   1 
ATOM   4145  O O   . GLN   B 1 61  ? -2.028  6.129   49.390  1.00 14.58  ?  61  GLN   B O   1 
ATOM   4146  C CB  . GLN   B 1 61  ? -0.237  6.379   46.571  1.00 13.18  ?  61  GLN   B CB  1 
ATOM   4147  C CG  . GLN   B 1 61  ? -0.488  7.319   45.399  1.00 11.84  ?  61  GLN   B CG  1 
ATOM   4148  C CD  . GLN   B 1 61  ? -0.215  6.654   44.072  1.00 13.07  ?  61  GLN   B CD  1 
ATOM   4149  O OE1 . GLN   B 1 61  ? 0.876   6.162   43.837  1.00 15.52  ?  61  GLN   B OE1 1 
ATOM   4150  N NE2 . GLN   B 1 61  ? -1.207  6.639   43.198  1.00 12.98  ?  61  GLN   B NE2 1 
ATOM   4151  N N   . TRP   B 1 62  ? 0.010   5.177   49.436  1.00 14.74  ?  62  TRP   B N   1 
ATOM   4152  C CA  . TRP   B 1 62  ? -0.410  4.207   50.438  1.00 18.07  ?  62  TRP   B CA  1 
ATOM   4153  C C   . TRP   B 1 62  ? -0.783  4.894   51.741  1.00 16.84  ?  62  TRP   B C   1 
ATOM   4154  O O   . TRP   B 1 62  ? -1.800  4.554   52.349  1.00 18.33  ?  62  TRP   B O   1 
ATOM   4155  C CB  . TRP   B 1 62  ? 0.680   3.163   50.660  1.00 18.92  ?  62  TRP   B CB  1 
ATOM   4156  C CG  . TRP   B 1 62  ? 0.598   2.036   49.684  1.00 23.86  ?  62  TRP   B CG  1 
ATOM   4157  C CD1 . TRP   B 1 62  ? 1.237   1.941   48.478  1.00 23.17  ?  62  TRP   B CD1 1 
ATOM   4158  C CD2 . TRP   B 1 62  ? -0.190  0.846   49.816  1.00 27.67  ?  62  TRP   B CD2 1 
ATOM   4159  N NE1 . TRP   B 1 62  ? 0.909   0.753   47.860  1.00 26.86  ?  62  TRP   B NE1 1 
ATOM   4160  C CE2 . TRP   B 1 62  ? 0.034   0.065   48.660  1.00 28.27  ?  62  TRP   B CE2 1 
ATOM   4161  C CE3 . TRP   B 1 62  ? -1.060  0.363   50.803  1.00 28.51  ?  62  TRP   B CE3 1 
ATOM   4162  C CZ2 . TRP   B 1 62  ? -0.583  -1.173  48.465  1.00 31.33  ?  62  TRP   B CZ2 1 
ATOM   4163  C CZ3 . TRP   B 1 62  ? -1.672  -0.872  50.608  1.00 28.89  ?  62  TRP   B CZ3 1 
ATOM   4164  C CH2 . TRP   B 1 62  ? -1.430  -1.623  49.447  1.00 25.46  ?  62  TRP   B CH2 1 
ATOM   4165  N N   . ALA   B 1 63  ? 0.014   5.867   52.183  1.00 16.89  ?  63  ALA   B N   1 
ATOM   4166  C CA  . ALA   B 1 63  ? -0.357  6.609   53.384  1.00 18.15  ?  63  ALA   B CA  1 
ATOM   4167  C C   . ALA   B 1 63  ? -1.743  7.216   53.233  1.00 16.28  ?  63  ALA   B C   1 
ATOM   4168  O O   . ALA   B 1 63  ? -2.560  7.151   54.156  1.00 16.27  ?  63  ALA   B O   1 
ATOM   4169  C CB  . ALA   B 1 63  ? 0.672   7.698   53.685  1.00 15.70  ?  63  ALA   B CB  1 
ATOM   4170  N N   . ALA   B 1 64  ? -2.031  7.792   52.064  1.00 16.90  ?  64  ALA   B N   1 
ATOM   4171  C CA  . ALA   B 1 64  ? -3.347  8.380   51.833  1.00 20.77  ?  64  ALA   B CA  1 
ATOM   4172  C C   . ALA   B 1 64  ? -4.451  7.338   51.987  1.00 18.20  ?  64  ALA   B C   1 
ATOM   4173  O O   . ALA   B 1 64  ? -5.514  7.627   52.551  1.00 16.52  ?  64  ALA   B O   1 
ATOM   4174  C CB  . ALA   B 1 64  ? -3.394  9.025   50.449  1.00 14.71  ?  64  ALA   B CB  1 
ATOM   4175  N N   . MET   B 1 65  ? -4.212  6.115   51.504  1.00 15.25  ?  65  MET   B N   1 
ATOM   4176  C CA  . MET   B 1 65  ? -5.218  5.066   51.638  1.00 15.22  ?  65  MET   B CA  1 
ATOM   4177  C C   . MET   B 1 65  ? -5.458  4.717   53.098  1.00 16.62  ?  65  MET   B C   1 
ATOM   4178  O O   . MET   B 1 65  ? -6.596  4.448   53.502  1.00 13.52  ?  65  MET   B O   1 
ATOM   4179  C CB  . MET   B 1 65  ? -4.782  3.821   50.878  1.00 13.18  ?  65  MET   B CB  1 
ATOM   4180  C CG  . MET   B 1 65  ? -4.718  3.983   49.392  1.00 18.24  ?  65  MET   B CG  1 
ATOM   4181  S SD  . MET   B 1 65  ? -4.075  2.472   48.666  1.00 26.84  ?  65  MET   B SD  1 
ATOM   4182  C CE  . MET   B 1 65  ? -5.465  1.392   48.782  1.00 10.48  ?  65  MET   B CE  1 
ATOM   4183  N N   . ILE   B 1 66  ? -4.395  4.709   53.904  1.00 16.37  ?  66  ILE   B N   1 
ATOM   4184  C CA  . ILE   B 1 66  ? -4.517  4.315   55.305  1.00 12.86  ?  66  ILE   B CA  1 
ATOM   4185  C C   . ILE   B 1 66  ? -5.409  5.277   56.074  1.00 15.55  ?  66  ILE   B C   1 
ATOM   4186  O O   . ILE   B 1 66  ? -6.128  4.868   56.992  1.00 15.44  ?  66  ILE   B O   1 
ATOM   4187  C CB  . ILE   B 1 66  ? -3.126  4.211   55.949  1.00 16.08  ?  66  ILE   B CB  1 
ATOM   4188  C CG1 . ILE   B 1 66  ? -2.263  3.248   55.140  1.00 24.63  ?  66  ILE   B CG1 1 
ATOM   4189  C CG2 . ILE   B 1 66  ? -3.236  3.754   57.383  1.00 18.07  ?  66  ILE   B CG2 1 
ATOM   4190  C CD1 . ILE   B 1 66  ? -2.850  1.862   54.967  1.00 23.58  ?  66  ILE   B CD1 1 
ATOM   4191  N N   . THR   B 1 67  ? -5.384  6.562   55.730  1.00 15.57  ?  67  THR   B N   1 
ATOM   4192  C CA  . THR   B 1 67  ? -6.253  7.520   56.396  1.00 18.74  ?  67  THR   B CA  1 
ATOM   4193  C C   . THR   B 1 67  ? -7.518  7.794   55.593  1.00 17.28  ?  67  THR   B C   1 
ATOM   4194  O O   . THR   B 1 67  ? -8.213  8.782   55.861  1.00 17.02  ?  67  THR   B O   1 
ATOM   4195  C CB  . THR   B 1 67  ? -5.491  8.813   56.679  1.00 14.84  ?  67  THR   B CB  1 
ATOM   4196  O OG1 . THR   B 1 67  ? -4.908  9.284   55.462  1.00 18.30  ?  67  THR   B OG1 1 
ATOM   4197  C CG2 . THR   B 1 67  ? -4.373  8.558   57.669  1.00 16.66  ?  67  THR   B CG2 1 
ATOM   4198  N N   . GLY   B 1 68  ? -7.844  6.916   54.644  1.00 16.53  ?  68  GLY   B N   1 
ATOM   4199  C CA  . GLY   B 1 68  ? -9.006  7.132   53.795  1.00 14.21  ?  68  GLY   B CA  1 
ATOM   4200  C C   . GLY   B 1 68  ? -10.312 7.030   54.567  1.00 16.16  ?  68  GLY   B C   1 
ATOM   4201  O O   . GLY   B 1 68  ? -10.467 6.207   55.470  1.00 18.16  ?  68  GLY   B O   1 
ATOM   4202  N N   . ASP   B 1 69  ? -11.267 7.872   54.185  1.00 16.38  ?  69  ASP   B N   1 
ATOM   4203  C CA  . ASP   B 1 69  ? -12.561 7.988   54.853  1.00 17.48  ?  69  ASP   B CA  1 
ATOM   4204  C C   . ASP   B 1 69  ? -13.562 7.078   54.144  1.00 17.76  ?  69  ASP   B C   1 
ATOM   4205  O O   . ASP   B 1 69  ? -13.973 7.361   53.014  1.00 16.57  ?  69  ASP   B O   1 
ATOM   4206  C CB  . ASP   B 1 69  ? -13.011 9.451   54.834  1.00 18.68  ?  69  ASP   B CB  1 
ATOM   4207  C CG  . ASP   B 1 69  ? -14.365 9.683   55.506  1.00 20.22  ?  69  ASP   B CG  1 
ATOM   4208  O OD1 . ASP   B 1 69  ? -14.931 8.753   56.125  1.00 23.65  ?  69  ASP   B OD1 1 
ATOM   4209  O OD2 . ASP   B 1 69  ? -14.866 10.829  55.422  1.00 18.46  ?  69  ASP   B OD2 1 
ATOM   4210  N N   . GLU   B 1 70  ? -13.972 5.999   54.813  1.00 16.69  ?  70  GLU   B N   1 
ATOM   4211  C CA  . GLU   B 1 70  ? -14.806 4.975   54.194  1.00 19.46  ?  70  GLU   B CA  1 
ATOM   4212  C C   . GLU   B 1 70  ? -16.304 5.260   54.295  1.00 20.65  ?  70  GLU   B C   1 
ATOM   4213  O O   . GLU   B 1 70  ? -17.108 4.380   53.955  1.00 22.07  ?  70  GLU   B O   1 
ATOM   4214  C CB  . GLU   B 1 70  ? -14.500 3.598   54.806  1.00 18.39  ?  70  GLU   B CB  1 
ATOM   4215  C CG  . GLU   B 1 70  ? -13.118 3.047   54.473  1.00 15.55  ?  70  GLU   B CG  1 
ATOM   4216  C CD  . GLU   B 1 70  ? -12.868 2.952   52.975  1.00 19.18  ?  70  GLU   B CD  1 
ATOM   4217  O OE1 . GLU   B 1 70  ? -13.847 2.735   52.226  1.00 15.69  ?  70  GLU   B OE1 1 
ATOM   4218  O OE2 . GLU   B 1 70  ? -11.696 3.105   52.546  1.00 17.26  ?  70  GLU   B OE2 1 
ATOM   4219  N N   . ALA   B 1 71  ? -16.690 6.463   54.723  1.00 17.31  ?  71  ALA   B N   1 
ATOM   4220  C CA  . ALA   B 1 71  ? -18.097 6.805   54.895  1.00 22.42  ?  71  ALA   B CA  1 
ATOM   4221  C C   . ALA   B 1 71  ? -18.887 6.577   53.612  1.00 21.63  ?  71  ALA   B C   1 
ATOM   4222  O O   . ALA   B 1 71  ? -18.392 6.803   52.506  1.00 23.74  ?  71  ALA   B O   1 
ATOM   4223  C CB  . ALA   B 1 71  ? -18.237 8.268   55.336  1.00 22.35  ?  71  ALA   B CB  1 
ATOM   4224  N N   . TYR   B 1 72  ? -20.137 6.139   53.771  1.00 18.02  ?  72  TYR   B N   1 
ATOM   4225  C CA  . TYR   B 1 72  ? -20.987 5.888   52.615  1.00 20.36  ?  72  TYR   B CA  1 
ATOM   4226  C C   . TYR   B 1 72  ? -21.327 7.178   51.883  1.00 19.38  ?  72  TYR   B C   1 
ATOM   4227  O O   . TYR   B 1 72  ? -21.331 7.211   50.651  1.00 26.26  ?  72  TYR   B O   1 
ATOM   4228  C CB  . TYR   B 1 72  ? -22.267 5.173   53.050  1.00 22.17  ?  72  TYR   B CB  1 
ATOM   4229  C CG  . TYR   B 1 72  ? -23.074 4.628   51.888  1.00 22.69  ?  72  TYR   B CG  1 
ATOM   4230  C CD1 . TYR   B 1 72  ? -22.807 3.367   51.358  1.00 23.57  ?  72  TYR   B CD1 1 
ATOM   4231  C CD2 . TYR   B 1 72  ? -24.086 5.376   51.308  1.00 24.42  ?  72  TYR   B CD2 1 
ATOM   4232  C CE1 . TYR   B 1 72  ? -23.536 2.869   50.291  1.00 26.11  ?  72  TYR   B CE1 1 
ATOM   4233  C CE2 . TYR   B 1 72  ? -24.817 4.882   50.237  1.00 29.82  ?  72  TYR   B CE2 1 
ATOM   4234  C CZ  . TYR   B 1 72  ? -24.534 3.631   49.732  1.00 25.19  ?  72  TYR   B CZ  1 
ATOM   4235  O OH  . TYR   B 1 72  ? -25.266 3.150   48.671  1.00 33.51  ?  72  TYR   B OH  1 
ATOM   4236  N N   . ALA   B 1 73  ? -21.619 8.250   52.618  1.00 20.05  ?  73  ALA   B N   1 
ATOM   4237  C CA  . ALA   B 1 73  ? -22.047 9.512   52.028  1.00 21.56  ?  73  ALA   B CA  1 
ATOM   4238  C C   . ALA   B 1 73  ? -21.146 10.633  52.517  1.00 21.31  ?  73  ALA   B C   1 
ATOM   4239  O O   . ALA   B 1 73  ? -20.996 10.828  53.725  1.00 25.13  ?  73  ALA   B O   1 
ATOM   4240  C CB  . ALA   B 1 73  ? -23.499 9.828   52.388  1.00 20.28  ?  73  ALA   B CB  1 
ATOM   4241  N N   . GLY   B 1 74  ? -20.560 11.375  51.586  1.00 19.63  ?  74  GLY   B N   1 
ATOM   4242  C CA  . GLY   B 1 74  ? -19.838 12.573  51.964  1.00 23.40  ?  74  GLY   B CA  1 
ATOM   4243  C C   . GLY   B 1 74  ? -18.444 12.332  52.481  1.00 24.65  ?  74  GLY   B C   1 
ATOM   4244  O O   . GLY   B 1 74  ? -17.967 13.097  53.331  1.00 23.73  ?  74  GLY   B O   1 
ATOM   4245  N N   . SER   B 1 75  ? -17.787 11.269  52.009  1.00 22.37  ?  75  SER   B N   1 
ATOM   4246  C CA  . SER   B 1 75  ? -16.410 10.982  52.383  1.00 19.68  ?  75  SER   B CA  1 
ATOM   4247  C C   . SER   B 1 75  ? -15.537 12.218  52.210  1.00 21.27  ?  75  SER   B C   1 
ATOM   4248  O O   . SER   B 1 75  ? -15.711 12.993  51.268  1.00 21.70  ?  75  SER   B O   1 
ATOM   4249  C CB  . SER   B 1 75  ? -15.865 9.833   51.529  1.00 19.82  ?  75  SER   B CB  1 
ATOM   4250  O OG  . SER   B 1 75  ? -14.456 9.704   51.669  1.00 19.41  ?  75  SER   B OG  1 
ATOM   4251  N N   . ARG   B 1 76  ? -14.611 12.409  53.153  1.00 22.05  ?  76  ARG   B N   1 
ATOM   4252  C CA  . ARG   B 1 76  ? -13.659 13.512  53.059  1.00 21.33  ?  76  ARG   B CA  1 
ATOM   4253  C C   . ARG   B 1 76  ? -12.877 13.459  51.754  1.00 21.22  ?  76  ARG   B C   1 
ATOM   4254  O O   . ARG   B 1 76  ? -12.534 14.506  51.190  1.00 21.52  ?  76  ARG   B O   1 
ATOM   4255  C CB  . ARG   B 1 76  ? -12.711 13.476  54.265  1.00 21.98  ?  76  ARG   B CB  1 
ATOM   4256  C CG  . ARG   B 1 76  ? -11.666 14.580  54.294  1.00 25.91  ?  76  ARG   B CG  1 
ATOM   4257  C CD  . ARG   B 1 76  ? -10.592 14.327  55.364  1.00 26.84  ?  76  ARG   B CD  1 
ATOM   4258  N NE  . ARG   B 1 76  ? -9.596  13.359  54.913  1.00 30.53  ?  76  ARG   B NE  1 
ATOM   4259  C CZ  . ARG   B 1 76  ? -9.524  12.099  55.327  1.00 29.95  ?  76  ARG   B CZ  1 
ATOM   4260  N NH1 . ARG   B 1 76  ? -10.335 11.631  56.268  1.00 26.80  ?  76  ARG   B NH1 1 
ATOM   4261  N NH2 . ARG   B 1 76  ? -8.618  11.286  54.781  1.00 23.34  ?  76  ARG   B NH2 1 
ATOM   4262  N N   . ASN   B 1 77  ? -12.615 12.252  51.244  1.00 19.36  ?  77  ASN   B N   1 
ATOM   4263  C CA  . ASN   B 1 77  ? -11.841 12.075  50.025  1.00 20.04  ?  77  ASN   B CA  1 
ATOM   4264  C C   . ASN   B 1 77  ? -12.639 12.350  48.755  1.00 20.43  ?  77  ASN   B C   1 
ATOM   4265  O O   . ASN   B 1 77  ? -12.034 12.607  47.710  1.00 22.48  ?  77  ASN   B O   1 
ATOM   4266  C CB  . ASN   B 1 77  ? -11.260 10.662  49.996  1.00 17.25  ?  77  ASN   B CB  1 
ATOM   4267  C CG  . ASN   B 1 77  ? -10.520 10.325  51.274  1.00 18.97  ?  77  ASN   B CG  1 
ATOM   4268  O OD1 . ASN   B 1 77  ? -11.030 9.600   52.126  1.00 20.08  ?  77  ASN   B OD1 1 
ATOM   4269  N ND2 . ASN   B 1 77  ? -9.325  10.881  51.431  1.00 16.94  ?  77  ASN   B ND2 1 
ATOM   4270  N N   . TYR   B 1 78  ? -13.971 12.310  48.802  1.00 19.62  ?  78  TYR   B N   1 
ATOM   4271  C CA  . TYR   B 1 78  ? -14.736 12.793  47.657  1.00 20.21  ?  78  TYR   B CA  1 
ATOM   4272  C C   . TYR   B 1 78  ? -14.522 14.288  47.462  1.00 19.89  ?  78  TYR   B C   1 
ATOM   4273  O O   . TYR   B 1 78  ? -14.279 14.753  46.342  1.00 23.34  ?  78  TYR   B O   1 
ATOM   4274  C CB  . TYR   B 1 78  ? -16.225 12.476  47.828  1.00 20.56  ?  78  TYR   B CB  1 
ATOM   4275  C CG  . TYR   B 1 78  ? -17.148 13.325  46.961  1.00 20.47  ?  78  TYR   B CG  1 
ATOM   4276  C CD1 . TYR   B 1 78  ? -17.419 12.981  45.641  1.00 21.43  ?  78  TYR   B CD1 1 
ATOM   4277  C CD2 . TYR   B 1 78  ? -17.749 14.468  47.468  1.00 18.69  ?  78  TYR   B CD2 1 
ATOM   4278  C CE1 . TYR   B 1 78  ? -18.255 13.760  44.855  1.00 19.11  ?  78  TYR   B CE1 1 
ATOM   4279  C CE2 . TYR   B 1 78  ? -18.578 15.248  46.688  1.00 19.72  ?  78  TYR   B CE2 1 
ATOM   4280  C CZ  . TYR   B 1 78  ? -18.826 14.890  45.386  1.00 19.60  ?  78  TYR   B CZ  1 
ATOM   4281  O OH  . TYR   B 1 78  ? -19.657 15.671  44.615  1.00 23.64  ?  78  TYR   B OH  1 
ATOM   4282  N N   . TYR   B 1 79  ? -14.599 15.059  48.546  1.00 19.93  ?  79  TYR   B N   1 
ATOM   4283  C CA  . TYR   B 1 79  ? -14.403 16.499  48.432  1.00 20.62  ?  79  TYR   B CA  1 
ATOM   4284  C C   . TYR   B 1 79  ? -12.973 16.831  48.017  1.00 25.83  ?  79  TYR   B C   1 
ATOM   4285  O O   . TYR   B 1 79  ? -12.753 17.801  47.278  1.00 22.80  ?  79  TYR   B O   1 
ATOM   4286  C CB  . TYR   B 1 79  ? -14.784 17.177  49.752  1.00 20.42  ?  79  TYR   B CB  1 
ATOM   4287  C CG  . TYR   B 1 79  ? -16.227 16.911  50.144  1.00 24.78  ?  79  TYR   B CG  1 
ATOM   4288  C CD1 . TYR   B 1 79  ? -17.263 17.688  49.634  1.00 22.67  ?  79  TYR   B CD1 1 
ATOM   4289  C CD2 . TYR   B 1 79  ? -16.557 15.864  50.997  1.00 24.58  ?  79  TYR   B CD2 1 
ATOM   4290  C CE1 . TYR   B 1 79  ? -18.586 17.437  49.973  1.00 22.95  ?  79  TYR   B CE1 1 
ATOM   4291  C CE2 . TYR   B 1 79  ? -17.886 15.602  51.344  1.00 26.45  ?  79  TYR   B CE2 1 
ATOM   4292  C CZ  . TYR   B 1 79  ? -18.893 16.393  50.824  1.00 26.55  ?  79  TYR   B CZ  1 
ATOM   4293  O OH  . TYR   B 1 79  ? -20.208 16.146  51.158  1.00 27.15  ?  79  TYR   B OH  1 
ATOM   4294  N N   . ASP   B 1 80  ? -11.995 16.031  48.462  1.00 23.48  ?  80  ASP   B N   1 
ATOM   4295  C CA  . ASP   B 1 80  ? -10.622 16.209  48.002  1.00 17.82  ?  80  ASP   B CA  1 
ATOM   4296  C C   . ASP   B 1 80  ? -10.509 15.930  46.516  1.00 16.49  ?  80  ASP   B C   1 
ATOM   4297  O O   . ASP   B 1 80  ? -9.806  16.642  45.794  1.00 20.00  ?  80  ASP   B O   1 
ATOM   4298  C CB  . ASP   B 1 80  ? -9.683  15.279  48.762  1.00 19.88  ?  80  ASP   B CB  1 
ATOM   4299  C CG  . ASP   B 1 80  ? -9.427  15.729  50.168  1.00 27.98  ?  80  ASP   B CG  1 
ATOM   4300  O OD1 . ASP   B 1 80  ? -9.884  16.836  50.526  1.00 32.95  ?  80  ASP   B OD1 1 
ATOM   4301  O OD2 . ASP   B 1 80  ? -8.763  14.972  50.913  1.00 28.96  ?  80  ASP   B OD2 1 
ATOM   4302  N N   . LEU   B 1 81  ? -11.170 14.871  46.052  1.00 18.74  ?  81  LEU   B N   1 
ATOM   4303  C CA  . LEU   B 1 81  ? -11.153 14.526  44.637  1.00 18.37  ?  81  LEU   B CA  1 
ATOM   4304  C C   . LEU   B 1 81  ? -11.884 15.571  43.797  1.00 20.45  ?  81  LEU   B C   1 
ATOM   4305  O O   . LEU   B 1 81  ? -11.473 15.871  42.668  1.00 20.69  ?  81  LEU   B O   1 
ATOM   4306  C CB  . LEU   B 1 81  ? -11.774 13.144  44.456  1.00 18.02  ?  81  LEU   B CB  1 
ATOM   4307  C CG  . LEU   B 1 81  ? -11.819 12.595  43.034  1.00 16.15  ?  81  LEU   B CG  1 
ATOM   4308  C CD1 . LEU   B 1 81  ? -10.416 12.502  42.486  1.00 13.92  ?  81  LEU   B CD1 1 
ATOM   4309  C CD2 . LEU   B 1 81  ? -12.486 11.239  43.036  1.00 17.59  ?  81  LEU   B CD2 1 
ATOM   4310  N N   . LYS   B 1 82  ? -12.976 16.129  44.322  1.00 18.43  ?  82  LYS   B N   1 
ATOM   4311  C CA  . LYS   B 1 82  ? -13.683 17.173  43.591  1.00 21.36  ?  82  LYS   B CA  1 
ATOM   4312  C C   . LYS   B 1 82  ? -12.811 18.409  43.437  1.00 24.82  ?  82  LYS   B C   1 
ATOM   4313  O O   . LYS   B 1 82  ? -12.776 19.023  42.365  1.00 25.48  ?  82  LYS   B O   1 
ATOM   4314  C CB  . LYS   B 1 82  ? -14.993 17.510  44.305  1.00 24.89  ?  82  LYS   B CB  1 
ATOM   4315  C CG  . LYS   B 1 82  ? -15.884 18.534  43.602  1.00 24.08  ?  82  LYS   B CG  1 
ATOM   4316  C CD  . LYS   B 1 82  ? -17.217 18.653  44.333  1.00 26.40  ?  82  LYS   B CD  1 
ATOM   4317  C CE  . LYS   B 1 82  ? -18.082 19.752  43.759  1.00 26.04  ?  82  LYS   B CE  1 
ATOM   4318  N NZ  . LYS   B 1 82  ? -17.412 21.071  43.844  1.00 27.09  ?  82  LYS   B NZ  1 
ATOM   4319  N N   . ASP   B 1 83  ? -12.080 18.777  44.495  1.00 21.26  ?  83  ASP   B N   1 
ATOM   4320  C CA  . ASP   B 1 83  ? -11.182 19.924  44.413  1.00 22.01  ?  83  ASP   B CA  1 
ATOM   4321  C C   . ASP   B 1 83  ? -10.012 19.666  43.472  1.00 22.45  ?  83  ASP   B C   1 
ATOM   4322  O O   . ASP   B 1 83  ? -9.554  20.589  42.789  1.00 25.97  ?  83  ASP   B O   1 
ATOM   4323  C CB  . ASP   B 1 83  ? -10.670 20.289  45.807  1.00 23.06  ?  83  ASP   B CB  1 
ATOM   4324  C CG  . ASP   B 1 83  ? -11.775 20.794  46.717  1.00 31.30  ?  83  ASP   B CG  1 
ATOM   4325  O OD1 . ASP   B 1 83  ? -12.836 21.209  46.201  1.00 32.85  ?  83  ASP   B OD1 1 
ATOM   4326  O OD2 . ASP   B 1 83  ? -11.582 20.785  47.951  1.00 38.46  ?  83  ASP   B OD2 1 
ATOM   4327  N N   . LYS   B 1 84  ? -9.521  18.428  43.412  1.00 21.90  ?  84  LYS   B N   1 
ATOM   4328  C CA  . LYS   B 1 84  ? -8.405  18.123  42.522  1.00 24.02  ?  84  LYS   B CA  1 
ATOM   4329  C C   . LYS   B 1 84  ? -8.812  18.243  41.055  1.00 23.30  ?  84  LYS   B C   1 
ATOM   4330  O O   . LYS   B 1 84  ? -8.034  18.738  40.231  1.00 22.89  ?  84  LYS   B O   1 
ATOM   4331  C CB  . LYS   B 1 84  ? -7.863  16.725  42.825  1.00 19.57  ?  84  LYS   B CB  1 
ATOM   4332  C CG  . LYS   B 1 84  ? -6.513  16.437  42.189  1.00 19.63  ?  84  LYS   B CG  1 
ATOM   4333  C CD  . LYS   B 1 84  ? -5.440  17.357  42.749  1.00 23.26  ?  84  LYS   B CD  1 
ATOM   4334  C CE  . LYS   B 1 84  ? -4.099  17.060  42.123  1.00 28.03  ?  84  LYS   B CE  1 
ATOM   4335  N NZ  . LYS   B 1 84  ? -3.056  18.020  42.567  1.00 28.35  ?  84  LYS   B NZ  1 
ATOM   4336  N N   . ALA   B 1 85  ? -10.027 17.805  40.710  1.00 22.62  ?  85  ALA   B N   1 
ATOM   4337  C CA  . ALA   B 1 85  ? -10.485 17.899  39.326  1.00 24.60  ?  85  ALA   B CA  1 
ATOM   4338  C C   . ALA   B 1 85  ? -10.751 19.340  38.912  1.00 26.47  ?  85  ALA   B C   1 
ATOM   4339  O O   . ALA   B 1 85  ? -10.624 19.677  37.729  1.00 26.64  ?  85  ALA   B O   1 
ATOM   4340  C CB  . ALA   B 1 85  ? -11.744 17.061  39.130  1.00 21.11  ?  85  ALA   B CB  1 
ATOM   4341  N N   . LYS   B 1 86  ? -11.134 20.195  39.862  1.00 23.70  ?  86  LYS   B N   1 
ATOM   4342  C CA  . LYS   B 1 86  ? -11.238 21.624  39.593  1.00 23.06  ?  86  LYS   B CA  1 
ATOM   4343  C C   . LYS   B 1 86  ? -9.864  22.244  39.371  1.00 26.67  ?  86  LYS   B C   1 
ATOM   4344  O O   . LYS   B 1 86  ? -9.676  23.043  38.447  1.00 28.35  ?  86  LYS   B O   1 
ATOM   4345  C CB  . LYS   B 1 86  ? -11.955 22.309  40.753  1.00 29.89  ?  86  LYS   B CB  1 
ATOM   4346  C CG  . LYS   B 1 86  ? -12.085 23.810  40.613  1.00 35.86  ?  86  LYS   B CG  1 
ATOM   4347  C CD  . LYS   B 1 86  ? -12.873 24.183  39.375  1.00 29.19  ?  86  LYS   B CD  1 
ATOM   4348  C CE  . LYS   B 1 86  ? -13.066 25.676  39.302  1.00 29.84  ?  86  LYS   B CE  1 
ATOM   4349  N NZ  . LYS   B 1 86  ? -13.614 26.066  37.980  1.00 37.53  ?  86  LYS   B NZ  1 
ATOM   4350  N N   . GLU   B 1 87  ? -8.892  21.886  40.213  1.00 24.67  ?  87  GLU   B N   1 
ATOM   4351  C CA  . GLU   B 1 87  ? -7.538  22.404  40.059  1.00 25.54  ?  87  GLU   B CA  1 
ATOM   4352  C C   . GLU   B 1 87  ? -6.914  21.945  38.748  1.00 24.29  ?  87  GLU   B C   1 
ATOM   4353  O O   . GLU   B 1 87  ? -6.288  22.740  38.038  1.00 27.13  ?  87  GLU   B O   1 
ATOM   4354  C CB  . GLU   B 1 87  ? -6.680  21.965  41.247  1.00 27.44  ?  87  GLU   B CB  1 
ATOM   4355  C CG  . GLU   B 1 87  ? -5.188  21.905  40.945  1.00 35.63  ?  87  GLU   B CG  1 
ATOM   4356  C CD  . GLU   B 1 87  ? -4.402  21.117  41.994  1.00 41.39  ?  87  GLU   B CD  1 
ATOM   4357  O OE1 . GLU   B 1 87  ? -4.921  20.923  43.121  1.00 43.05  ?  87  GLU   B OE1 1 
ATOM   4358  O OE2 . GLU   B 1 87  ? -3.263  20.695  41.685  1.00 40.11  ?  87  GLU   B OE2 1 
ATOM   4359  N N   . LEU   B 1 88  ? -7.086  20.672  38.397  1.00 24.68  ?  88  LEU   B N   1 
ATOM   4360  C CA  . LEU   B 1 88  ? -6.414  20.142  37.216  1.00 24.46  ?  88  LEU   B CA  1 
ATOM   4361  C C   . LEU   B 1 88  ? -7.104  20.569  35.927  1.00 25.22  ?  88  LEU   B C   1 
ATOM   4362  O O   . LEU   B 1 88  ? -6.446  21.026  34.987  1.00 22.76  ?  88  LEU   B O   1 
ATOM   4363  C CB  . LEU   B 1 88  ? -6.339  18.618  37.287  1.00 23.87  ?  88  LEU   B CB  1 
ATOM   4364  C CG  . LEU   B 1 88  ? -5.275  18.018  38.202  1.00 26.86  ?  88  LEU   B CG  1 
ATOM   4365  C CD1 . LEU   B 1 88  ? -5.163  16.513  37.933  1.00 21.92  ?  88  LEU   B CD1 1 
ATOM   4366  C CD2 . LEU   B 1 88  ? -3.937  18.726  37.994  1.00 27.68  ?  88  LEU   B CD2 1 
ATOM   4367  N N   . PHE   B 1 89  ? -8.426  20.425  35.859  1.00 25.66  ?  89  PHE   B N   1 
ATOM   4368  C CA  . PHE   B 1 89  ? -9.137  20.567  34.596  1.00 28.20  ?  89  PHE   B CA  1 
ATOM   4369  C C   . PHE   B 1 89  ? -10.013 21.808  34.510  1.00 28.60  ?  89  PHE   B C   1 
ATOM   4370  O O   . PHE   B 1 89  ? -10.479 22.134  33.412  1.00 25.93  ?  89  PHE   B O   1 
ATOM   4371  C CB  . PHE   B 1 89  ? -10.005 19.326  34.345  1.00 26.92  ?  89  PHE   B CB  1 
ATOM   4372  C CG  . PHE   B 1 89  ? -9.302  18.030  34.620  1.00 23.21  ?  89  PHE   B CG  1 
ATOM   4373  C CD1 . PHE   B 1 89  ? -8.229  17.630  33.844  1.00 24.66  ?  89  PHE   B CD1 1 
ATOM   4374  C CD2 . PHE   B 1 89  ? -9.725  17.204  35.645  1.00 25.88  ?  89  PHE   B CD2 1 
ATOM   4375  C CE1 . PHE   B 1 89  ? -7.581  16.430  34.095  1.00 24.11  ?  89  PHE   B CE1 1 
ATOM   4376  C CE2 . PHE   B 1 89  ? -9.080  16.002  35.903  1.00 21.93  ?  89  PHE   B CE2 1 
ATOM   4377  C CZ  . PHE   B 1 89  ? -8.011  15.615  35.127  1.00 22.81  ?  89  PHE   B CZ  1 
ATOM   4378  N N   . ASN   B 1 90  ? -10.236 22.507  35.627  1.00 29.03  ?  90  ASN   B N   1 
ATOM   4379  C CA  . ASN   B 1 90  ? -11.183 23.619  35.728  1.00 27.26  ?  90  ASN   B CA  1 
ATOM   4380  C C   . ASN   B 1 90  ? -12.625 23.150  35.575  1.00 29.59  ?  90  ASN   B C   1 
ATOM   4381  O O   . ASN   B 1 90  ? -13.496 23.918  35.157  1.00 30.97  ?  90  ASN   B O   1 
ATOM   4382  C CB  . ASN   B 1 90  ? -10.882 24.735  34.724  1.00 26.73  ?  90  ASN   B CB  1 
ATOM   4383  C CG  . ASN   B 1 90  ? -11.475 26.061  35.150  1.00 35.29  ?  90  ASN   B CG  1 
ATOM   4384  O OD1 . ASN   B 1 90  ? -11.525 26.376  36.345  1.00 34.44  ?  90  ASN   B OD1 1 
ATOM   4385  N ND2 . ASN   B 1 90  ? -11.944 26.839  34.182  1.00 38.25  ?  90  ASN   B ND2 1 
ATOM   4386  N N   . TYR   B 1 91  ? -12.891 21.894  35.925  1.00 32.07  ?  91  TYR   B N   1 
ATOM   4387  C CA  . TYR   B 1 91  ? -14.229 21.325  35.853  1.00 28.64  ?  91  TYR   B CA  1 
ATOM   4388  C C   . TYR   B 1 91  ? -14.875 21.366  37.231  1.00 29.83  ?  91  TYR   B C   1 
ATOM   4389  O O   . TYR   B 1 91  ? -14.208 21.146  38.248  1.00 26.59  ?  91  TYR   B O   1 
ATOM   4390  C CB  . TYR   B 1 91  ? -14.192 19.891  35.317  1.00 21.86  ?  91  TYR   B CB  1 
ATOM   4391  C CG  . TYR   B 1 91  ? -13.860 19.803  33.838  1.00 26.62  ?  91  TYR   B CG  1 
ATOM   4392  C CD1 . TYR   B 1 91  ? -13.380 20.911  33.142  1.00 25.87  ?  91  TYR   B CD1 1 
ATOM   4393  C CD2 . TYR   B 1 91  ? -14.034 18.617  33.134  1.00 26.51  ?  91  TYR   B CD2 1 
ATOM   4394  C CE1 . TYR   B 1 91  ? -13.077 20.842  31.799  1.00 26.52  ?  91  TYR   B CE1 1 
ATOM   4395  C CE2 . TYR   B 1 91  ? -13.729 18.538  31.778  1.00 25.07  ?  91  TYR   B CE2 1 
ATOM   4396  C CZ  . TYR   B 1 91  ? -13.259 19.658  31.120  1.00 26.17  ?  91  TYR   B CZ  1 
ATOM   4397  O OH  . TYR   B 1 91  ? -12.953 19.595  29.780  1.00 24.16  ?  91  TYR   B OH  1 
ATOM   4398  N N   . ASP   B 1 92  ? -16.176 21.662  37.261  1.00 31.67  ?  92  ASP   B N   1 
ATOM   4399  C CA  . ASP   B 1 92  ? -16.864 21.942  38.512  1.00 27.01  ?  92  ASP   B CA  1 
ATOM   4400  C C   . ASP   B 1 92  ? -17.605 20.743  39.094  1.00 29.85  ?  92  ASP   B C   1 
ATOM   4401  O O   . ASP   B 1 92  ? -18.077 20.825  40.233  1.00 26.20  ?  92  ASP   B O   1 
ATOM   4402  C CB  . ASP   B 1 92  ? -17.846 23.101  38.317  1.00 29.04  ?  92  ASP   B CB  1 
ATOM   4403  C CG  . ASP   B 1 92  ? -17.143 24.433  38.136  1.00 37.11  ?  92  ASP   B CG  1 
ATOM   4404  O OD1 . ASP   B 1 92  ? -16.045 24.611  38.713  1.00 33.68  ?  92  ASP   B OD1 1 
ATOM   4405  O OD2 . ASP   B 1 92  ? -17.684 25.307  37.421  1.00 35.46  ?  92  ASP   B OD2 1 
ATOM   4406  N N   . TYR   B 1 93  ? -17.721 19.641  38.361  1.00 25.80  ?  93  TYR   B N   1 
ATOM   4407  C CA  . TYR   B 1 93  ? -18.529 18.514  38.802  1.00 29.01  ?  93  TYR   B CA  1 
ATOM   4408  C C   . TYR   B 1 93  ? -17.750 17.220  38.632  1.00 28.43  ?  93  TYR   B C   1 
ATOM   4409  O O   . TYR   B 1 93  ? -17.052 17.033  37.631  1.00 26.39  ?  93  TYR   B O   1 
ATOM   4410  C CB  . TYR   B 1 93  ? -19.840 18.422  38.017  1.00 29.04  ?  93  TYR   B CB  1 
ATOM   4411  C CG  . TYR   B 1 93  ? -20.743 19.637  38.115  1.00 29.59  ?  93  TYR   B CG  1 
ATOM   4412  C CD1 . TYR   B 1 93  ? -21.379 19.962  39.307  1.00 29.29  ?  93  TYR   B CD1 1 
ATOM   4413  C CD2 . TYR   B 1 93  ? -20.983 20.437  37.007  1.00 30.27  ?  93  TYR   B CD2 1 
ATOM   4414  C CE1 . TYR   B 1 93  ? -22.215 21.063  39.397  1.00 32.71  ?  93  TYR   B CE1 1 
ATOM   4415  C CE2 . TYR   B 1 93  ? -21.818 21.539  37.087  1.00 33.98  ?  93  TYR   B CE2 1 
ATOM   4416  C CZ  . TYR   B 1 93  ? -22.432 21.848  38.285  1.00 33.73  ?  93  TYR   B CZ  1 
ATOM   4417  O OH  . TYR   B 1 93  ? -23.264 22.946  38.379  1.00 38.91  ?  93  TYR   B OH  1 
ATOM   4418  N N   . ILE   B 1 94  ? -17.872 16.324  39.608  1.00 23.88  ?  94  ILE   B N   1 
ATOM   4419  C CA  . ILE   B 1 94  ? -17.223 15.023  39.539  1.00 23.28  ?  94  ILE   B CA  1 
ATOM   4420  C C   . ILE   B 1 94  ? -18.188 13.939  39.990  1.00 20.70  ?  94  ILE   B C   1 
ATOM   4421  O O   . ILE   B 1 94  ? -19.039 14.152  40.861  1.00 23.45  ?  94  ILE   B O   1 
ATOM   4422  C CB  . ILE   B 1 94  ? -15.942 14.960  40.388  1.00 22.28  ?  94  ILE   B CB  1 
ATOM   4423  C CG1 . ILE   B 1 94  ? -16.285 15.049  41.877  1.00 23.34  ?  94  ILE   B CG1 1 
ATOM   4424  C CG2 . ILE   B 1 94  ? -14.988 16.059  39.976  1.00 25.82  ?  94  ILE   B CG2 1 
ATOM   4425  C CD1 . ILE   B 1 94  ? -15.433 14.155  42.748  1.00 21.33  ?  94  ILE   B CD1 1 
ATOM   4426  N N   . ILE   B 1 95  ? -18.046 12.768  39.382  1.00 18.17  ?  95  ILE   B N   1 
ATOM   4427  C CA  . ILE   B 1 95  ? -18.712 11.548  39.822  1.00 18.62  ?  95  ILE   B CA  1 
ATOM   4428  C C   . ILE   B 1 95  ? -17.673 10.437  39.786  1.00 20.55  ?  95  ILE   B C   1 
ATOM   4429  O O   . ILE   B 1 95  ? -17.283 10.009  38.691  1.00 19.52  ?  95  ILE   B O   1 
ATOM   4430  C CB  . ILE   B 1 95  ? -19.902 11.182  38.923  1.00 21.37  ?  95  ILE   B CB  1 
ATOM   4431  C CG1 . ILE   B 1 95  ? -20.871 12.350  38.767  1.00 23.27  ?  95  ILE   B CG1 1 
ATOM   4432  C CG2 . ILE   B 1 95  ? -20.609 9.957   39.464  1.00 19.80  ?  95  ILE   B CG2 1 
ATOM   4433  C CD1 . ILE   B 1 95  ? -22.006 12.040  37.828  1.00 23.94  ?  95  ILE   B CD1 1 
ATOM   4434  N N   . PRO   B 1 96  ? -17.197 9.932   40.921  1.00 20.80  ?  96  PRO   B N   1 
ATOM   4435  C CA  . PRO   B 1 96  ? -16.295 8.777   40.866  1.00 22.89  ?  96  PRO   B CA  1 
ATOM   4436  C C   . PRO   B 1 96  ? -16.982 7.583   40.217  1.00 17.82  ?  96  PRO   B C   1 
ATOM   4437  O O   . PRO   B 1 96  ? -18.206 7.447   40.236  1.00 19.04  ?  96  PRO   B O   1 
ATOM   4438  C CB  . PRO   B 1 96  ? -15.954 8.507   42.340  1.00 18.31  ?  96  PRO   B CB  1 
ATOM   4439  C CG  . PRO   B 1 96  ? -17.011 9.187   43.118  1.00 18.58  ?  96  PRO   B CG  1 
ATOM   4440  C CD  . PRO   B 1 96  ? -17.480 10.357  42.301  1.00 18.52  ?  96  PRO   B CD  1 
ATOM   4441  N N   . ALA   B 1 97  ? -16.174 6.735   39.602  1.00 15.68  ?  97  ALA   B N   1 
ATOM   4442  C CA  . ALA   B 1 97  ? -16.614 5.451   39.093  1.00 17.71  ?  97  ALA   B CA  1 
ATOM   4443  C C   . ALA   B 1 97  ? -15.595 4.409   39.531  1.00 16.14  ?  97  ALA   B C   1 
ATOM   4444  O O   . ALA   B 1 97  ? -14.465 4.740   39.895  1.00 17.02  ?  97  ALA   B O   1 
ATOM   4445  C CB  . ALA   B 1 97  ? -16.769 5.471   37.568  1.00 15.44  ?  97  ALA   B CB  1 
ATOM   4446  N N   . HIS   B 1 98  ? -16.003 3.139   39.517  1.00 17.39  ?  98  HIS   B N   1 
ATOM   4447  C CA  . HIS   B 1 98  ? -15.077 2.107   39.959  1.00 17.19  ?  98  HIS   B CA  1 
ATOM   4448  C C   . HIS   B 1 98  ? -13.932 1.913   38.976  1.00 16.76  ?  98  HIS   B C   1 
ATOM   4449  O O   . HIS   B 1 98  ? -12.868 1.443   39.382  1.00 19.23  ?  98  HIS   B O   1 
ATOM   4450  C CB  . HIS   B 1 98  ? -15.816 0.792   40.221  1.00 20.42  ?  98  HIS   B CB  1 
ATOM   4451  C CG  . HIS   B 1 98  ? -16.185 0.028   38.988  1.00 21.34  ?  98  HIS   B CG  1 
ATOM   4452  N ND1 . HIS   B 1 98  ? -17.347 0.264   38.286  1.00 21.07  ?  98  HIS   B ND1 1 
ATOM   4453  C CD2 . HIS   B 1 98  ? -15.568 -0.999  38.358  1.00 17.42  ?  98  HIS   B CD2 1 
ATOM   4454  C CE1 . HIS   B 1 98  ? -17.419 -0.569  37.263  1.00 21.12  ?  98  HIS   B CE1 1 
ATOM   4455  N NE2 . HIS   B 1 98  ? -16.352 -1.348  37.286  1.00 20.05  ?  98  HIS   B NE2 1 
ATOM   4456  N N   . GLN   B 1 99  ? -14.119 2.275   37.708  1.00 17.82  ?  99  GLN   B N   1 
ATOM   4457  C CA  . GLN   B 1 99  ? -13.031 2.378   36.734  1.00 16.23  ?  99  GLN   B CA  1 
ATOM   4458  C C   . GLN   B 1 99  ? -13.609 2.972   35.453  1.00 14.95  ?  99  GLN   B C   1 
ATOM   4459  O O   . GLN   B 1 99  ? -14.768 3.398   35.415  1.00 14.08  ?  99  GLN   B O   1 
ATOM   4460  C CB  . GLN   B 1 99  ? -12.339 1.033   36.491  1.00 16.56  ?  99  GLN   B CB  1 
ATOM   4461  C CG  . GLN   B 1 99  ? -13.206 -0.032  35.879  1.00 17.35  ?  99  GLN   B CG  1 
ATOM   4462  C CD  . GLN   B 1 99  ? -12.476 -1.352  35.785  1.00 17.39  ?  99  GLN   B CD  1 
ATOM   4463  O OE1 . GLN   B 1 99  ? -12.053 -1.906  36.796  1.00 19.59  ?  99  GLN   B OE1 1 
ATOM   4464  N NE2 . GLN   B 1 99  ? -12.309 -1.859  34.567  1.00 17.17  ?  99  GLN   B NE2 1 
ATOM   4465  N N   . GLY   B 1 100 ? -12.797 2.981   34.395  1.00 22.26  ?  100 GLY   B N   1 
ATOM   4466  C CA  . GLY   B 1 100 ? -13.098 3.807   33.235  1.00 22.56  ?  100 GLY   B CA  1 
ATOM   4467  C C   . GLY   B 1 100 ? -14.367 3.419   32.498  1.00 22.70  ?  100 GLY   B C   1 
ATOM   4468  O O   . GLY   B 1 100 ? -15.119 4.289   32.050  1.00 23.01  ?  100 GLY   B O   1 
ATOM   4469  N N   . ARG   B 1 101 ? -14.605 2.115   32.323  1.00 22.62  ?  101 ARG   B N   1 
ATOM   4470  C CA  . ARG   B 1 101 ? -15.818 1.690   31.630  1.00 22.88  ?  101 ARG   B CA  1 
ATOM   4471  C C   . ARG   B 1 101 ? -17.061 1.852   32.497  1.00 23.01  ?  101 ARG   B C   1 
ATOM   4472  O O   . ARG   B 1 101 ? -18.176 1.825   31.972  1.00 23.39  ?  101 ARG   B O   1 
ATOM   4473  C CB  . ARG   B 1 101 ? -15.685 0.241   31.153  1.00 22.96  ?  101 ARG   B CB  1 
ATOM   4474  C CG  . ARG   B 1 101 ? -15.671 -0.791  32.265  1.00 22.85  ?  101 ARG   B CG  1 
ATOM   4475  C CD  . ARG   B 1 101 ? -15.111 -2.117  31.744  1.00 24.45  ?  101 ARG   B CD  1 
ATOM   4476  N NE  . ARG   B 1 101 ? -13.660 -2.073  31.594  1.00 24.21  ?  101 ARG   B NE  1 
ATOM   4477  C CZ  . ARG   B 1 101 ? -12.905 -3.091  31.201  1.00 23.31  ?  101 ARG   B CZ  1 
ATOM   4478  N NH1 . ARG   B 1 101 ? -13.438 -4.226  30.781  1.00 23.75  ?  101 ARG   B NH1 1 
ATOM   4479  N NH2 . ARG   B 1 101 ? -11.578 -2.971  31.246  1.00 23.35  ?  101 ARG   B NH2 1 
ATOM   4480  N N   . GLY   B 1 102 ? -16.896 2.010   33.812  1.00 22.84  ?  102 GLY   B N   1 
ATOM   4481  C CA  . GLY   B 1 102 ? -18.012 2.437   34.639  1.00 23.15  ?  102 GLY   B CA  1 
ATOM   4482  C C   . GLY   B 1 102 ? -18.311 3.910   34.453  1.00 23.46  ?  102 GLY   B C   1 
ATOM   4483  O O   . GLY   B 1 102 ? -19.474 4.323   34.458  1.00 24.00  ?  102 GLY   B O   1 
ATOM   4484  N N   . ALA   B 1 103 ? -17.266 4.722   34.273  1.00 23.29  ?  103 ALA   B N   1 
ATOM   4485  C CA  . ALA   B 1 103 ? -17.463 6.119   33.905  1.00 23.75  ?  103 ALA   B CA  1 
ATOM   4486  C C   . ALA   B 1 103 ? -18.157 6.239   32.555  1.00 27.33  ?  103 ALA   B C   1 
ATOM   4487  O O   . ALA   B 1 103 ? -18.968 7.150   32.344  1.00 27.20  ?  103 ALA   B O   1 
ATOM   4488  C CB  . ALA   B 1 103 ? -16.123 6.853   33.880  1.00 23.65  ?  103 ALA   B CB  1 
ATOM   4489  N N   . GLU   B 1 104 ? -17.847 5.331   31.622  1.00 23.88  ?  104 GLU   B N   1 
ATOM   4490  C CA  . GLU   B 1 104 ? -18.535 5.342   30.336  1.00 24.79  ?  104 GLU   B CA  1 
ATOM   4491  C C   . GLU   B 1 104 ? -19.991 4.930   30.488  1.00 24.67  ?  104 GLU   B C   1 
ATOM   4492  O O   . GLU   B 1 104 ? -20.868 5.471   29.804  1.00 27.07  ?  104 GLU   B O   1 
ATOM   4493  C CB  . GLU   B 1 104 ? -17.807 4.432   29.345  1.00 24.78  ?  104 GLU   B CB  1 
ATOM   4494  C CG  . GLU   B 1 104 ? -16.428 4.964   28.991  1.00 27.52  ?  104 GLU   B CG  1 
ATOM   4495  C CD  . GLU   B 1 104 ? -15.507 3.932   28.349  1.00 29.58  ?  104 GLU   B CD  1 
ATOM   4496  O OE1 . GLU   B 1 104 ? -15.820 2.720   28.386  1.00 26.99  ?  104 GLU   B OE1 1 
ATOM   4497  O OE2 . GLU   B 1 104 ? -14.453 4.344   27.819  1.00 31.85  ?  104 GLU   B OE2 1 
ATOM   4498  N N   . ASN   B 1 105 ? -20.268 3.978   31.382  1.00 24.47  ?  105 ASN   B N   1 
ATOM   4499  C CA  . ASN   B 1 105 ? -21.639 3.528   31.585  1.00 25.02  ?  105 ASN   B CA  1 
ATOM   4500  C C   . ASN   B 1 105 ? -22.481 4.603   32.258  1.00 26.85  ?  105 ASN   B C   1 
ATOM   4501  O O   . ASN   B 1 105 ? -23.685 4.698   31.998  1.00 28.44  ?  105 ASN   B O   1 
ATOM   4502  C CB  . ASN   B 1 105 ? -21.643 2.243   32.413  1.00 24.82  ?  105 ASN   B CB  1 
ATOM   4503  C CG  . ASN   B 1 105 ? -23.022 1.617   32.518  1.00 30.45  ?  105 ASN   B CG  1 
ATOM   4504  O OD1 . ASN   B 1 105 ? -23.844 1.751   31.615  1.00 32.45  ?  105 ASN   B OD1 1 
ATOM   4505  N ND2 . ASN   B 1 105 ? -23.281 0.931   33.626  1.00 26.69  ?  105 ASN   B ND2 1 
ATOM   4506  N N   . ILE   B 1 106 ? -21.868 5.414   33.124  1.00 26.33  ?  106 ILE   B N   1 
ATOM   4507  C CA  . ILE   B 1 106 ? -22.577 6.529   33.746  1.00 26.21  ?  106 ILE   B CA  1 
ATOM   4508  C C   . ILE   B 1 106 ? -22.995 7.555   32.695  1.00 29.16  ?  106 ILE   B C   1 
ATOM   4509  O O   . ILE   B 1 106 ? -24.168 7.936   32.604  1.00 32.54  ?  106 ILE   B O   1 
ATOM   4510  C CB  . ILE   B 1 106 ? -21.706 7.175   34.840  1.00 25.95  ?  106 ILE   B CB  1 
ATOM   4511  C CG1 . ILE   B 1 106 ? -21.594 6.256   36.053  1.00 25.88  ?  106 ILE   B CG1 1 
ATOM   4512  C CG2 . ILE   B 1 106 ? -22.289 8.513   35.268  1.00 29.30  ?  106 ILE   B CG2 1 
ATOM   4513  C CD1 . ILE   B 1 106 ? -20.823 6.870   37.209  1.00 25.76  ?  106 ILE   B CD1 1 
ATOM   4514  N N   . LEU   B 1 107 ? -22.042 8.005   31.874  1.00 26.53  ?  107 LEU   B N   1 
ATOM   4515  C CA  . LEU   B 1 107 ? -22.209 9.213   31.071  1.00 27.25  ?  107 LEU   B CA  1 
ATOM   4516  C C   . LEU   B 1 107 ? -22.775 8.966   29.672  1.00 27.98  ?  107 LEU   B C   1 
ATOM   4517  O O   . LEU   B 1 107 ? -23.579 9.772   29.196  1.00 30.64  ?  107 LEU   B O   1 
ATOM   4518  C CB  . LEU   B 1 107 ? -20.867 9.947   30.955  1.00 26.98  ?  107 LEU   B CB  1 
ATOM   4519  C CG  . LEU   B 1 107 ? -20.855 11.284  30.211  1.00 27.86  ?  107 LEU   B CG  1 
ATOM   4520  C CD1 . LEU   B 1 107 ? -21.609 12.334  30.994  1.00 28.83  ?  107 LEU   B CD1 1 
ATOM   4521  C CD2 . LEU   B 1 107 ? -19.435 11.746  29.943  1.00 27.64  ?  107 LEU   B CD2 1 
ATOM   4522  N N   . PHE   B 1 108 ? -22.371 7.900   28.974  1.00 27.25  ?  108 PHE   B N   1 
ATOM   4523  C CA  . PHE   B 1 108 ? -22.778 7.796   27.571  1.00 27.38  ?  108 PHE   B CA  1 
ATOM   4524  C C   . PHE   B 1 108 ? -24.283 7.582   27.415  1.00 28.32  ?  108 PHE   B C   1 
ATOM   4525  O O   . PHE   B 1 108 ? -24.878 8.185   26.516  1.00 28.95  ?  108 PHE   B O   1 
ATOM   4526  C CB  . PHE   B 1 108 ? -22.022 6.684   26.838  1.00 26.74  ?  108 PHE   B CB  1 
ATOM   4527  C CG  . PHE   B 1 108 ? -20.565 6.992   26.591  1.00 29.69  ?  108 PHE   B CG  1 
ATOM   4528  C CD1 . PHE   B 1 108 ? -19.999 8.181   27.031  1.00 26.80  ?  108 PHE   B CD1 1 
ATOM   4529  C CD2 . PHE   B 1 108 ? -19.763 6.090   25.916  1.00 30.06  ?  108 PHE   B CD2 1 
ATOM   4530  C CE1 . PHE   B 1 108 ? -18.664 8.455   26.816  1.00 29.61  ?  108 PHE   B CE1 1 
ATOM   4531  C CE2 . PHE   B 1 108 ? -18.419 6.362   25.696  1.00 31.34  ?  108 PHE   B CE2 1 
ATOM   4532  C CZ  . PHE   B 1 108 ? -17.870 7.545   26.145  1.00 28.23  ?  108 PHE   B CZ  1 
ATOM   4533  N N   . PRO   B 1 109 ? -24.938 6.744   28.234  1.00 28.54  ?  109 PRO   B N   1 
ATOM   4534  C CA  . PRO   B 1 109 ? -26.408 6.670   28.144  1.00 29.14  ?  109 PRO   B CA  1 
ATOM   4535  C C   . PRO   B 1 109 ? -27.086 7.986   28.470  1.00 30.14  ?  109 PRO   B C   1 
ATOM   4536  O O   . PRO   B 1 109 ? -28.113 8.325   27.870  1.00 31.19  ?  109 PRO   B O   1 
ATOM   4537  C CB  . PRO   B 1 109 ? -26.766 5.579   29.162  1.00 29.78  ?  109 PRO   B CB  1 
ATOM   4538  C CG  . PRO   B 1 109 ? -25.540 4.741   29.249  1.00 27.84  ?  109 PRO   B CG  1 
ATOM   4539  C CD  . PRO   B 1 109 ? -24.401 5.696   29.119  1.00 29.44  ?  109 PRO   B CD  1 
ATOM   4540  N N   . VAL   B 1 110 ? -26.532 8.739   29.418  1.00 30.16  ?  110 VAL   B N   1 
ATOM   4541  C CA  . VAL   B 1 110 ? -27.069 10.056  29.734  1.00 31.33  ?  110 VAL   B CA  1 
ATOM   4542  C C   . VAL   B 1 110 ? -26.901 10.999  28.545  1.00 31.58  ?  110 VAL   B C   1 
ATOM   4543  O O   . VAL   B 1 110 ? -27.802 11.780  28.227  1.00 32.84  ?  110 VAL   B O   1 
ATOM   4544  C CB  . VAL   B 1 110 ? -26.396 10.594  31.013  1.00 30.80  ?  110 VAL   B CB  1 
ATOM   4545  C CG1 . VAL   B 1 110 ? -26.612 12.079  31.152  1.00 32.54  ?  110 VAL   B CG1 1 
ATOM   4546  C CG2 . VAL   B 1 110 ? -26.934 9.860   32.241  1.00 30.83  ?  110 VAL   B CG2 1 
ATOM   4547  N N   . LEU   B 1 111 ? -25.763 10.921  27.849  1.00 30.77  ?  111 LEU   B N   1 
ATOM   4548  C CA  . LEU   B 1 111 ? -25.551 11.782  26.685  1.00 31.36  ?  111 LEU   B CA  1 
ATOM   4549  C C   . LEU   B 1 111 ? -26.527 11.461  25.556  1.00 32.03  ?  111 LEU   B C   1 
ATOM   4550  O O   . LEU   B 1 111 ? -27.009 12.373  24.873  1.00 34.18  ?  111 LEU   B O   1 
ATOM   4551  C CB  . LEU   B 1 111 ? -24.111 11.664  26.193  1.00 30.48  ?  111 LEU   B CB  1 
ATOM   4552  C CG  . LEU   B 1 111 ? -23.073 12.183  27.187  1.00 30.05  ?  111 LEU   B CG  1 
ATOM   4553  C CD1 . LEU   B 1 111 ? -21.672 12.002  26.632  1.00 29.38  ?  111 LEU   B CD1 1 
ATOM   4554  C CD2 . LEU   B 1 111 ? -23.347 13.637  27.537  1.00 31.21  ?  111 LEU   B CD2 1 
ATOM   4555  N N   . LEU   B 1 112 ? -26.822 10.176  25.328  1.00 31.50  ?  112 LEU   B N   1 
ATOM   4556  C CA  . LEU   B 1 112 ? -27.790 9.823   24.292  1.00 32.24  ?  112 LEU   B CA  1 
ATOM   4557  C C   . LEU   B 1 112 ? -29.189 10.294  24.664  1.00 33.56  ?  112 LEU   B C   1 
ATOM   4558  O O   . LEU   B 1 112 ? -29.911 10.835  23.821  1.00 34.67  ?  112 LEU   B O   1 
ATOM   4559  C CB  . LEU   B 1 112 ? -27.783 8.315   24.047  1.00 31.53  ?  112 LEU   B CB  1 
ATOM   4560  C CG  . LEU   B 1 112 ? -28.977 7.773   23.254  1.00 34.21  ?  112 LEU   B CG  1 
ATOM   4561  C CD1 . LEU   B 1 112 ? -29.006 8.336   21.845  1.00 39.08  ?  112 LEU   B CD1 1 
ATOM   4562  C CD2 . LEU   B 1 112 ? -28.969 6.259   23.211  1.00 33.58  ?  112 LEU   B CD2 1 
ATOM   4563  N N   . LYS   B 1 113 ? -29.584 10.094  25.924  1.00 33.83  ?  113 LYS   B N   1 
ATOM   4564  C CA  . LYS   B 1 113 ? -30.879 10.576  26.394  1.00 37.30  ?  113 LYS   B CA  1 
ATOM   4565  C C   . LYS   B 1 113 ? -30.992 12.087  26.243  1.00 36.14  ?  113 LYS   B C   1 
ATOM   4566  O O   . LYS   B 1 113 ? -32.055 12.607  25.886  1.00 37.62  ?  113 LYS   B O   1 
ATOM   4567  C CB  . LYS   B 1 113 ? -31.080 10.167  27.856  1.00 34.90  ?  113 LYS   B CB  1 
ATOM   4568  C CG  . LYS   B 1 113 ? -32.469 10.396  28.406  1.00 39.14  ?  113 LYS   B CG  1 
ATOM   4569  C CD  . LYS   B 1 113 ? -33.462 9.390   27.833  1.00 44.80  ?  113 LYS   B CD  1 
ATOM   4570  C CE  . LYS   B 1 113 ? -34.742 9.337   28.663  1.00 51.08  ?  113 LYS   B CE  1 
ATOM   4571  N NZ  . LYS   B 1 113 ? -35.428 10.657  28.725  1.00 52.28  ?  113 LYS   B NZ  1 
ATOM   4572  N N   . TYR   B 1 114 ? -29.907 12.807  26.514  1.00 35.58  ?  114 TYR   B N   1 
ATOM   4573  C CA  . TYR   B 1 114 ? -29.946 14.263  26.460  1.00 36.76  ?  114 TYR   B CA  1 
ATOM   4574  C C   . TYR   B 1 114 ? -30.137 14.751  25.030  1.00 40.04  ?  114 TYR   B C   1 
ATOM   4575  O O   . TYR   B 1 114 ? -30.971 15.623  24.769  1.00 47.41  ?  114 TYR   B O   1 
ATOM   4576  C CB  . TYR   B 1 114 ? -28.665 14.829  27.074  1.00 37.19  ?  114 TYR   B CB  1 
ATOM   4577  C CG  . TYR   B 1 114 ? -28.593 16.339  27.172  1.00 46.05  ?  114 TYR   B CG  1 
ATOM   4578  C CD1 . TYR   B 1 114 ? -29.169 17.015  28.241  1.00 49.80  ?  114 TYR   B CD1 1 
ATOM   4579  C CD2 . TYR   B 1 114 ? -27.912 17.084  26.217  1.00 47.10  ?  114 TYR   B CD2 1 
ATOM   4580  C CE1 . TYR   B 1 114 ? -29.085 18.394  28.343  1.00 52.95  ?  114 TYR   B CE1 1 
ATOM   4581  C CE2 . TYR   B 1 114 ? -27.826 18.461  26.310  1.00 48.38  ?  114 TYR   B CE2 1 
ATOM   4582  C CZ  . TYR   B 1 114 ? -28.413 19.110  27.374  1.00 55.18  ?  114 TYR   B CZ  1 
ATOM   4583  O OH  . TYR   B 1 114 ? -28.330 20.481  27.471  1.00 63.85  ?  114 TYR   B OH  1 
ATOM   4584  N N   . LYS   B 1 115 ? -29.383 14.184  24.083  1.00 36.66  ?  115 LYS   B N   1 
ATOM   4585  C CA  . LYS   B 1 115 ? -29.526 14.581  22.687  1.00 41.76  ?  115 LYS   B CA  1 
ATOM   4586  C C   . LYS   B 1 115 ? -30.874 14.157  22.115  1.00 51.37  ?  115 LYS   B C   1 
ATOM   4587  O O   . LYS   B 1 115 ? -31.369 14.790  21.178  1.00 52.92  ?  115 LYS   B O   1 
ATOM   4588  C CB  . LYS   B 1 115 ? -28.388 13.990  21.854  1.00 36.14  ?  115 LYS   B CB  1 
ATOM   4589  C CG  . LYS   B 1 115 ? -28.099 14.731  20.548  1.00 41.14  ?  115 LYS   B CG  1 
ATOM   4590  C CD  . LYS   B 1 115 ? -27.473 16.108  20.805  1.00 43.99  ?  115 LYS   B CD  1 
ATOM   4591  C CE  . LYS   B 1 115 ? -27.167 16.869  19.509  1.00 41.28  ?  115 LYS   B CE  1 
ATOM   4592  N NZ  . LYS   B 1 115 ? -26.096 16.230  18.702  1.00 37.71  ?  115 LYS   B NZ  1 
ATOM   4593  N N   . GLN   B 1 116 ? -31.484 13.102  22.666  1.00 47.18  ?  116 GLN   B N   1 
ATOM   4594  C CA  . GLN   B 1 116 ? -32.740 12.586  22.129  1.00 50.00  ?  116 GLN   B CA  1 
ATOM   4595  C C   . GLN   B 1 116 ? -33.925 13.503  22.400  1.00 55.44  ?  116 GLN   B C   1 
ATOM   4596  O O   . GLN   B 1 116 ? -34.972 13.333  21.769  1.00 65.57  ?  116 GLN   B O   1 
ATOM   4597  C CB  . GLN   B 1 116 ? -33.036 11.200  22.702  1.00 44.70  ?  116 GLN   B CB  1 
ATOM   4598  C CG  . GLN   B 1 116 ? -32.507 10.049  21.868  1.00 40.30  ?  116 GLN   B CG  1 
ATOM   4599  C CD  . GLN   B 1 116 ? -32.668 8.709   22.565  1.00 40.59  ?  116 GLN   B CD  1 
ATOM   4600  O OE1 . GLN   B 1 116 ? -32.989 8.647   23.752  1.00 42.83  ?  116 GLN   B OE1 1 
ATOM   4601  N NE2 . GLN   B 1 116 ? -32.440 7.630   21.830  1.00 40.91  ?  116 GLN   B NE2 1 
ATOM   4602  N N   . LYS   B 1 117 ? -33.803 14.451  23.324  1.00 52.76  ?  117 LYS   B N   1 
ATOM   4603  C CA  . LYS   B 1 117 ? -34.895 15.388  23.538  1.00 68.29  ?  117 LYS   B CA  1 
ATOM   4604  C C   . LYS   B 1 117 ? -35.135 16.200  22.268  1.00 77.94  ?  117 LYS   B C   1 
ATOM   4605  O O   . LYS   B 1 117 ? -34.221 16.435  21.471  1.00 75.15  ?  117 LYS   B O   1 
ATOM   4606  C CB  . LYS   B 1 117 ? -34.597 16.307  24.725  1.00 68.29  ?  117 LYS   B CB  1 
ATOM   4607  C CG  . LYS   B 1 117 ? -33.537 17.371  24.468  1.00 71.49  ?  117 LYS   B CG  1 
ATOM   4608  C CD  . LYS   B 1 117 ? -33.175 18.109  25.755  1.00 62.79  ?  117 LYS   B CD  1 
ATOM   4609  C CE  . LYS   B 1 117 ? -32.105 19.169  25.513  1.00 57.40  ?  117 LYS   B CE  1 
ATOM   4610  N NZ  . LYS   B 1 117 ? -31.733 19.887  26.768  1.00 58.63  ?  117 LYS   B NZ  1 
ATOM   4611  N N   . GLU   B 1 118 ? -36.390 16.607  22.072  1.00 94.54  ?  118 GLU   B N   1 
ATOM   4612  C CA  . GLU   B 1 118 ? -36.820 17.290  20.849  1.00 95.98  ?  118 GLU   B CA  1 
ATOM   4613  C C   . GLU   B 1 118 ? -36.587 16.433  19.607  1.00 95.06  ?  118 GLU   B C   1 
ATOM   4614  O O   . GLU   B 1 118 ? -36.305 16.954  18.525  1.00 98.03  ?  118 GLU   B O   1 
ATOM   4615  C CB  . GLU   B 1 118 ? -36.142 18.656  20.695  1.00 99.66  ?  118 GLU   B CB  1 
ATOM   4616  C CG  . GLU   B 1 118 ? -36.731 19.751  21.576  1.00 104.32 ?  118 GLU   B CG  1 
ATOM   4617  C CD  . GLU   B 1 118 ? -35.998 21.073  21.436  1.00 106.77 ?  118 GLU   B CD  1 
ATOM   4618  O OE1 . GLU   B 1 118 ? -34.751 21.077  21.540  1.00 98.80  ?  118 GLU   B OE1 1 
ATOM   4619  O OE2 . GLU   B 1 118 ? -36.669 22.106  21.213  1.00 102.23 ?  118 GLU   B OE2 1 
ATOM   4620  N N   . GLY   B 1 119 ? -36.693 15.114  19.756  1.00 78.09  ?  119 GLY   B N   1 
ATOM   4621  C CA  . GLY   B 1 119 ? -36.737 14.219  18.614  1.00 70.76  ?  119 GLY   B CA  1 
ATOM   4622  C C   . GLY   B 1 119 ? -35.450 14.064  17.839  1.00 72.58  ?  119 GLY   B C   1 
ATOM   4623  O O   . GLY   B 1 119 ? -35.445 13.376  16.813  1.00 62.09  ?  119 GLY   B O   1 
ATOM   4624  N N   . LYS   B 1 120 ? -34.358 14.677  18.290  1.00 80.58  ?  120 LYS   B N   1 
ATOM   4625  C CA  . LYS   B 1 120 ? -33.072 14.522  17.628  1.00 73.13  ?  120 LYS   B CA  1 
ATOM   4626  C C   . LYS   B 1 120 ? -32.504 13.127  17.896  1.00 68.73  ?  120 LYS   B C   1 
ATOM   4627  O O   . LYS   B 1 120 ? -33.086 12.310  18.619  1.00 69.87  ?  120 LYS   B O   1 
ATOM   4628  C CB  . LYS   B 1 120 ? -32.102 15.603  18.099  1.00 71.46  ?  120 LYS   B CB  1 
ATOM   4629  C CG  . LYS   B 1 120 ? -32.635 17.022  17.964  1.00 79.95  ?  120 LYS   B CG  1 
ATOM   4630  C CD  . LYS   B 1 120 ? -31.628 18.044  18.478  1.00 80.94  ?  120 LYS   B CD  1 
ATOM   4631  C CE  . LYS   B 1 120 ? -31.293 17.813  19.946  1.00 73.58  ?  120 LYS   B CE  1 
ATOM   4632  N NZ  . LYS   B 1 120 ? -32.481 17.978  20.828  1.00 78.71  ?  120 LYS   B NZ  1 
ATOM   4633  N N   . ALA   B 1 121 ? -31.344 12.855  17.295  1.00 54.22  ?  121 ALA   B N   1 
ATOM   4634  C CA  . ALA   B 1 121 ? -30.619 11.599  17.497  1.00 46.76  ?  121 ALA   B CA  1 
ATOM   4635  C C   . ALA   B 1 121 ? -31.434 10.396  17.023  1.00 45.45  ?  121 ALA   B C   1 
ATOM   4636  O O   . ALA   B 1 121 ? -31.453 9.343   17.666  1.00 36.93  ?  121 ALA   B O   1 
ATOM   4637  C CB  . ALA   B 1 121 ? -30.196 11.430  18.960  1.00 47.78  ?  121 ALA   B CB  1 
ATOM   4638  N N   . LYS   B 1 122 ? -32.098 10.549  15.873  1.00 41.37  ?  122 LYS   B N   1 
ATOM   4639  C CA  . LYS   B 1 122 ? -32.901 9.461   15.324  1.00 39.27  ?  122 LYS   B CA  1 
ATOM   4640  C C   . LYS   B 1 122 ? -32.028 8.302   14.866  1.00 38.09  ?  122 LYS   B C   1 
ATOM   4641  O O   . LYS   B 1 122 ? -32.417 7.136   14.995  1.00 37.88  ?  122 LYS   B O   1 
ATOM   4642  C CB  . LYS   B 1 122 ? -33.761 9.976   14.172  1.00 40.82  ?  122 LYS   B CB  1 
ATOM   4643  C CG  . LYS   B 1 122 ? -34.832 10.976  14.595  1.00 49.63  ?  122 LYS   B CG  1 
ATOM   4644  C CD  . LYS   B 1 122 ? -35.844 11.237  13.477  1.00 51.01  ?  122 LYS   B CD  1 
ATOM   4645  C CE  . LYS   B 1 122 ? -35.256 12.085  12.363  1.00 49.08  ?  122 LYS   B CE  1 
ATOM   4646  N NZ  . LYS   B 1 122 ? -34.989 13.479  12.818  1.00 55.27  ?  122 LYS   B NZ  1 
ATOM   4647  N N   . ASN   B 1 123 ? -30.850 8.602   14.320  1.00 39.64  ?  123 ASN   B N   1 
ATOM   4648  C CA  . ASN   B 1 123 ? -29.841 7.599   13.973  1.00 36.50  ?  123 ASN   B CA  1 
ATOM   4649  C C   . ASN   B 1 123 ? -28.541 8.029   14.632  1.00 37.25  ?  123 ASN   B C   1 
ATOM   4650  O O   . ASN   B 1 123 ? -27.618 8.508   13.962  1.00 35.47  ?  123 ASN   B O   1 
ATOM   4651  C CB  . ASN   B 1 123 ? -29.679 7.459   12.460  1.00 38.44  ?  123 ASN   B CB  1 
ATOM   4652  C CG  . ASN   B 1 123 ? -30.935 6.945   11.793  1.00 41.61  ?  123 ASN   B CG  1 
ATOM   4653  O OD1 . ASN   B 1 123 ? -31.141 5.735   11.687  1.00 42.09  ?  123 ASN   B OD1 1 
ATOM   4654  N ND2 . ASN   B 1 123 ? -31.786 7.863   11.342  1.00 39.52  ?  123 ASN   B ND2 1 
ATOM   4655  N N   . PRO   B 1 124 ? -28.430 7.852   15.946  1.00 34.65  ?  124 PRO   B N   1 
ATOM   4656  C CA  . PRO   B 1 124 ? -27.330 8.468   16.690  1.00 36.33  ?  124 PRO   B CA  1 
ATOM   4657  C C   . PRO   B 1 124 ? -25.985 7.802   16.435  1.00 38.24  ?  124 PRO   B C   1 
ATOM   4658  O O   . PRO   B 1 124 ? -25.887 6.587   16.230  1.00 34.67  ?  124 PRO   B O   1 
ATOM   4659  C CB  . PRO   B 1 124 ? -27.758 8.286   18.151  1.00 36.38  ?  124 PRO   B CB  1 
ATOM   4660  C CG  . PRO   B 1 124 ? -28.620 7.072   18.137  1.00 37.16  ?  124 PRO   B CG  1 
ATOM   4661  C CD  . PRO   B 1 124 ? -29.364 7.132   16.828  1.00 38.21  ?  124 PRO   B CD  1 
ATOM   4662  N N   . VAL   B 1 125 ? -24.930 8.621   16.480  1.00 32.77  ?  125 VAL   B N   1 
ATOM   4663  C CA  . VAL   B 1 125 ? -23.560 8.137   16.377  1.00 34.02  ?  125 VAL   B CA  1 
ATOM   4664  C C   . VAL   B 1 125 ? -22.694 8.871   17.393  1.00 32.12  ?  125 VAL   B C   1 
ATOM   4665  O O   . VAL   B 1 125 ? -23.035 9.957   17.872  1.00 31.95  ?  125 VAL   B O   1 
ATOM   4666  C CB  . VAL   B 1 125 ? -22.972 8.314   14.956  1.00 36.07  ?  125 VAL   B CB  1 
ATOM   4667  C CG1 . VAL   B 1 125 ? -23.740 7.474   13.934  1.00 33.44  ?  125 VAL   B CG1 1 
ATOM   4668  C CG2 . VAL   B 1 125 ? -22.982 9.774   14.563  1.00 37.45  ?  125 VAL   B CG2 1 
ATOM   4669  N N   . PHE   B 1 126 ? -21.569 8.246   17.728  1.00 32.23  ?  126 PHE   B N   1 
ATOM   4670  C CA  . PHE   B 1 126 ? -20.470 8.873   18.448  1.00 31.80  ?  126 PHE   B CA  1 
ATOM   4671  C C   . PHE   B 1 126 ? -19.271 8.952   17.512  1.00 30.67  ?  126 PHE   B C   1 
ATOM   4672  O O   . PHE   B 1 126 ? -18.990 7.999   16.775  1.00 32.25  ?  126 PHE   B O   1 
ATOM   4673  C CB  . PHE   B 1 126 ? -20.079 8.075   19.694  1.00 33.03  ?  126 PHE   B CB  1 
ATOM   4674  C CG  . PHE   B 1 126 ? -21.002 8.253   20.874  1.00 36.03  ?  126 PHE   B CG  1 
ATOM   4675  C CD1 . PHE   B 1 126 ? -22.316 7.821   20.826  1.00 33.98  ?  126 PHE   B CD1 1 
ATOM   4676  C CD2 . PHE   B 1 126 ? -20.527 8.801   22.054  1.00 32.94  ?  126 PHE   B CD2 1 
ATOM   4677  C CE1 . PHE   B 1 126 ? -23.149 7.969   21.926  1.00 31.02  ?  126 PHE   B CE1 1 
ATOM   4678  C CE2 . PHE   B 1 126 ? -21.354 8.948   23.153  1.00 33.70  ?  126 PHE   B CE2 1 
ATOM   4679  C CZ  . PHE   B 1 126 ? -22.662 8.533   23.092  1.00 28.85  ?  126 PHE   B CZ  1 
ATOM   4680  N N   . ILE   B 1 127 ? -18.563 10.078  17.536  1.00 31.17  ?  127 ILE   B N   1 
ATOM   4681  C CA  . ILE   B 1 127 ? -17.399 10.289  16.682  1.00 31.76  ?  127 ILE   B CA  1 
ATOM   4682  C C   . ILE   B 1 127 ? -16.184 10.490  17.571  1.00 31.96  ?  127 ILE   B C   1 
ATOM   4683  O O   . ILE   B 1 127 ? -16.228 11.279  18.518  1.00 35.19  ?  127 ILE   B O   1 
ATOM   4684  C CB  . ILE   B 1 127 ? -17.594 11.492  15.740  1.00 33.11  ?  127 ILE   B CB  1 
ATOM   4685  C CG1 . ILE   B 1 127 ? -18.717 11.216  14.747  1.00 33.64  ?  127 ILE   B CG1 1 
ATOM   4686  C CG2 . ILE   B 1 127 ? -16.316 11.798  14.982  1.00 33.89  ?  127 ILE   B CG2 1 
ATOM   4687  C CD1 . ILE   B 1 127 ? -18.992 12.377  13.844  1.00 35.06  ?  127 ILE   B CD1 1 
ATOM   4688  N N   . SER   B 1 128 ? -15.108 9.770   17.275  1.00 31.21  ?  128 SER   B N   1 
ATOM   4689  C CA  . SER   B 1 128 ? -13.871 9.868   18.031  1.00 30.95  ?  128 SER   B CA  1 
ATOM   4690  C C   . SER   B 1 128 ? -12.703 9.804   17.066  1.00 31.84  ?  128 SER   B C   1 
ATOM   4691  O O   . SER   B 1 128 ? -12.846 9.365   15.926  1.00 32.39  ?  128 SER   B O   1 
ATOM   4692  C CB  . SER   B 1 128 ? -13.748 8.738   19.057  1.00 29.74  ?  128 SER   B CB  1 
ATOM   4693  O OG  . SER   B 1 128 ? -12.522 8.826   19.764  1.00 29.58  ?  128 SER   B OG  1 
ATOM   4694  N N   . ASN   B 1 129 ? -11.530 10.229  17.534  1.00 32.09  ?  129 ASN   B N   1 
ATOM   4695  C CA  . ASN   B 1 129 ? -10.319 9.876   16.803  1.00 32.88  ?  129 ASN   B CA  1 
ATOM   4696  C C   . ASN   B 1 129 ? -10.147 8.361   16.770  1.00 32.23  ?  129 ASN   B C   1 
ATOM   4697  O O   . ASN   B 1 129 ? -9.838  7.788   15.720  1.00 32.94  ?  129 ASN   B O   1 
ATOM   4698  C CB  . ASN   B 1 129 ? -9.088  10.584  17.388  1.00 33.39  ?  129 ASN   B CB  1 
ATOM   4699  C CG  . ASN   B 1 129 ? -8.936  10.404  18.891  1.00 32.25  ?  129 ASN   B CG  1 
ATOM   4700  O OD1 . ASN   B 1 129 ? -9.904  10.189  19.618  1.00 31.21  ?  129 ASN   B OD1 1 
ATOM   4701  N ND2 . ASN   B 1 129 ? -7.708  10.523  19.366  1.00 32.59  ?  129 ASN   B ND2 1 
ATOM   4702  N N   . PHE   B 1 130 ? -10.380 7.693   17.900  1.00 31.01  ?  130 PHE   B N   1 
ATOM   4703  C CA  . PHE   B 1 130 ? -10.566 6.241   17.900  1.00 32.46  ?  130 PHE   B CA  1 
ATOM   4704  C C   . PHE   B 1 130 ? -11.193 5.812   19.220  1.00 30.16  ?  130 PHE   B C   1 
ATOM   4705  O O   . PHE   B 1 130 ? -10.559 5.929   20.274  1.00 30.56  ?  130 PHE   B O   1 
ATOM   4706  C CB  . PHE   B 1 130 ? -9.249  5.513   17.664  1.00 33.46  ?  130 PHE   B CB  1 
ATOM   4707  C CG  . PHE   B 1 130 ? -9.386  4.309   16.783  1.00 31.38  ?  130 PHE   B CG  1 
ATOM   4708  C CD1 . PHE   B 1 130 ? -10.109 3.203   17.208  1.00 35.96  ?  130 PHE   B CD1 1 
ATOM   4709  C CD2 . PHE   B 1 130 ? -8.816  4.287   15.526  1.00 34.02  ?  130 PHE   B CD2 1 
ATOM   4710  C CE1 . PHE   B 1 130 ? -10.247 2.092   16.394  1.00 36.81  ?  130 PHE   B CE1 1 
ATOM   4711  C CE2 . PHE   B 1 130 ? -8.949  3.183   14.708  1.00 36.03  ?  130 PHE   B CE2 1 
ATOM   4712  C CZ  . PHE   B 1 130 ? -9.667  2.082   15.143  1.00 36.20  ?  130 PHE   B CZ  1 
ATOM   4713  N N   . HIS   B 1 131 ? -12.424 5.310   19.159  1.00 29.95  ?  131 HIS   B N   1 
ATOM   4714  C CA  . HIS   B 1 131 ? -13.044 4.694   20.326  1.00 28.02  ?  131 HIS   B CA  1 
ATOM   4715  C C   . HIS   B 1 131 ? -12.248 3.474   20.763  1.00 27.37  ?  131 HIS   B C   1 
ATOM   4716  O O   . HIS   B 1 131 ? -11.963 2.590   19.953  1.00 29.23  ?  131 HIS   B O   1 
ATOM   4717  C CB  . HIS   B 1 131 ? -14.474 4.250   20.016  1.00 27.55  ?  131 HIS   B CB  1 
ATOM   4718  C CG  . HIS   B 1 131 ? -15.436 5.368   19.768  1.00 29.44  ?  131 HIS   B CG  1 
ATOM   4719  N ND1 . HIS   B 1 131 ? -15.679 5.878   18.511  1.00 31.95  ?  131 HIS   B ND1 1 
ATOM   4720  C CD2 . HIS   B 1 131 ? -16.249 6.045   20.614  1.00 32.78  ?  131 HIS   B CD2 1 
ATOM   4721  C CE1 . HIS   B 1 131 ? -16.588 6.833   18.596  1.00 33.76  ?  131 HIS   B CE1 1 
ATOM   4722  N NE2 . HIS   B 1 131 ? -16.955 6.951   19.860  1.00 30.25  ?  131 HIS   B NE2 1 
ATOM   4723  N N   A PHE   B 1 132 ? -11.899 3.400   22.046  0.47 28.46  ?  132 PHE   B N   1 
ATOM   4724  N N   B PHE   B 1 132 ? -11.889 3.441   22.044  0.53 28.46  ?  132 PHE   B N   1 
ATOM   4725  C CA  A PHE   B 1 132 ? -11.288 2.158   22.496  0.47 27.81  ?  132 PHE   B CA  1 
ATOM   4726  C CA  B PHE   B 1 132 ? -11.316 2.244   22.625  0.53 27.80  ?  132 PHE   B CA  1 
ATOM   4727  C C   A PHE   B 1 132 ? -12.376 1.124   22.802  0.47 27.77  ?  132 PHE   B C   1 
ATOM   4728  C C   B PHE   B 1 132 ? -12.388 1.153   22.718  0.53 27.76  ?  132 PHE   B C   1 
ATOM   4729  O O   A PHE   B 1 132 ? -13.572 1.430   22.812  0.47 28.96  ?  132 PHE   B O   1 
ATOM   4730  O O   B PHE   B 1 132 ? -13.583 1.398   22.528  0.53 29.15  ?  132 PHE   B O   1 
ATOM   4731  C CB  A PHE   B 1 132 ? -10.382 2.394   23.702  0.47 28.64  ?  132 PHE   B CB  1 
ATOM   4732  C CB  B PHE   B 1 132 ? -10.715 2.561   23.994  0.53 28.98  ?  132 PHE   B CB  1 
ATOM   4733  C CG  A PHE   B 1 132 ? -9.370  1.298   23.912  0.47 29.87  ?  132 PHE   B CG  1 
ATOM   4734  C CG  B PHE   B 1 132 ? -10.054 1.387   24.650  0.53 30.51  ?  132 PHE   B CG  1 
ATOM   4735  C CD1 A PHE   B 1 132 ? -8.467  0.974   22.913  0.47 28.07  ?  132 PHE   B CD1 1 
ATOM   4736  C CD1 B PHE   B 1 132 ? -8.849  0.896   24.168  0.53 29.39  ?  132 PHE   B CD1 1 
ATOM   4737  C CD2 A PHE   B 1 132 ? -9.331  0.585   25.100  0.47 30.60  ?  132 PHE   B CD2 1 
ATOM   4738  C CD2 B PHE   B 1 132 ? -10.646 0.763   25.733  0.53 29.71  ?  132 PHE   B CD2 1 
ATOM   4739  C CE1 A PHE   B 1 132 ? -7.542  -0.035  23.087  0.47 28.55  ?  132 PHE   B CE1 1 
ATOM   4740  C CE1 B PHE   B 1 132 ? -8.248  -0.193  24.765  0.53 32.15  ?  132 PHE   B CE1 1 
ATOM   4741  C CE2 A PHE   B 1 132 ? -8.404  -0.427  25.286  0.47 32.75  ?  132 PHE   B CE2 1 
ATOM   4742  C CE2 B PHE   B 1 132 ? -10.052 -0.326  26.331  0.53 30.99  ?  132 PHE   B CE2 1 
ATOM   4743  C CZ  A PHE   B 1 132 ? -7.508  -0.738  24.279  0.47 32.83  ?  132 PHE   B CZ  1 
ATOM   4744  C CZ  B PHE   B 1 132 ? -8.847  -0.801  25.851  0.53 34.20  ?  132 PHE   B CZ  1 
ATOM   4745  N N   A ASP   B 1 133 ? -11.948 -0.117  23.060  0.47 27.44  ?  133 ASP   B N   1 
ATOM   4746  N N   B ASP   B 1 133 ? -11.940 -0.069  23.009  0.53 27.42  ?  133 ASP   B N   1 
ATOM   4747  C CA  A ASP   B 1 133 ? -12.861 -1.254  22.934  0.47 28.96  ?  133 ASP   B CA  1 
ATOM   4748  C CA  B ASP   B 1 133 ? -12.820 -1.234  22.956  0.53 28.96  ?  133 ASP   B CA  1 
ATOM   4749  C C   A ASP   B 1 133 ? -14.047 -1.158  23.893  0.47 28.13  ?  133 ASP   B C   1 
ATOM   4750  C C   B ASP   B 1 133 ? -14.034 -1.074  23.869  0.53 28.12  ?  133 ASP   B C   1 
ATOM   4751  O O   A ASP   B 1 133 ? -15.190 -1.410  23.492  0.47 27.54  ?  133 ASP   B O   1 
ATOM   4752  O O   B ASP   B 1 133 ? -15.178 -1.204  23.418  0.53 27.46  ?  133 ASP   B O   1 
ATOM   4753  C CB  A ASP   B 1 133 ? -12.103 -2.575  23.113  0.47 30.63  ?  133 ASP   B CB  1 
ATOM   4754  C CB  B ASP   B 1 133 ? -12.022 -2.487  23.311  0.53 30.54  ?  133 ASP   B CB  1 
ATOM   4755  C CG  A ASP   B 1 133 ? -11.476 -2.733  24.489  0.47 32.34  ?  133 ASP   B CG  1 
ATOM   4756  C CG  B ASP   B 1 133 ? -10.880 -2.732  22.345  0.53 30.08  ?  133 ASP   B CG  1 
ATOM   4757  O OD1 A ASP   B 1 133 ? -11.486 -1.772  25.289  0.47 32.13  ?  133 ASP   B OD1 1 
ATOM   4758  O OD1 B ASP   B 1 133 ? -11.091 -2.568  21.126  0.53 31.91  ?  133 ASP   B OD1 1 
ATOM   4759  O OD2 A ASP   B 1 133 ? -10.964 -3.840  24.767  0.47 34.09  ?  133 ASP   B OD2 1 
ATOM   4760  O OD2 B ASP   B 1 133 ? -9.771  -3.076  22.802  0.53 37.75  ?  133 ASP   B OD2 1 
ATOM   4761  N N   . THR   B 1 134 ? -13.813 -0.792  25.159  1.00 26.11  ?  134 THR   B N   1 
ATOM   4762  C CA  . THR   B 1 134 ? -14.954 -0.627  26.064  1.00 24.52  ?  134 THR   B CA  1 
ATOM   4763  C C   . THR   B 1 134 ? -15.773 0.600   25.695  1.00 26.61  ?  134 THR   B C   1 
ATOM   4764  O O   . THR   B 1 134 ? -17.001 0.590   25.844  1.00 26.19  ?  134 THR   B O   1 
ATOM   4765  C CB  . THR   B 1 134 ? -14.524 -0.517  27.532  1.00 24.48  ?  134 THR   B CB  1 
ATOM   4766  O OG1 . THR   B 1 134 ? -13.968 0.781   27.779  1.00 25.01  ?  134 THR   B OG1 1 
ATOM   4767  C CG2 . THR   B 1 134 ? -13.508 -1.591  27.895  1.00 27.44  ?  134 THR   B CG2 1 
ATOM   4768  N N   . THR   B 1 135 ? -15.113 1.653   25.201  1.00 27.34  ?  135 THR   B N   1 
ATOM   4769  C CA  . THR   B 1 135 ? -15.813 2.875   24.820  1.00 26.98  ?  135 THR   B CA  1 
ATOM   4770  C C   . THR   B 1 135 ? -16.767 2.623   23.658  1.00 27.49  ?  135 THR   B C   1 
ATOM   4771  O O   . THR   B 1 135 ? -17.925 3.060   23.680  1.00 30.60  ?  135 THR   B O   1 
ATOM   4772  C CB  . THR   B 1 135 ? -14.799 3.958   24.450  1.00 27.73  ?  135 THR   B CB  1 
ATOM   4773  O OG1 . THR   B 1 135 ? -13.687 3.902   25.350  1.00 27.87  ?  135 THR   B OG1 1 
ATOM   4774  C CG2 . THR   B 1 135 ? -15.438 5.337   24.519  1.00 27.18  ?  135 THR   B CG2 1 
ATOM   4775  N N   . ALA   B 1 136 ? -16.294 1.920   22.627  1.00 27.11  ?  136 ALA   B N   1 
ATOM   4776  C CA  . ALA   B 1 136 ? -17.163 1.579   21.504  1.00 27.29  ?  136 ALA   B CA  1 
ATOM   4777  C C   . ALA   B 1 136 ? -18.262 0.604   21.917  1.00 28.85  ?  136 ALA   B C   1 
ATOM   4778  O O   . ALA   B 1 136 ? -19.388 0.694   21.414  1.00 27.20  ?  136 ALA   B O   1 
ATOM   4779  C CB  . ALA   B 1 136 ? -16.335 1.004   20.355  1.00 26.95  ?  136 ALA   B CB  1 
ATOM   4780  N N   . ALA   B 1 137 ? -17.960 -0.320  22.833  1.00 29.33  ?  137 ALA   B N   1 
ATOM   4781  C CA  . ALA   B 1 137 ? -18.971 -1.265  23.299  1.00 29.58  ?  137 ALA   B CA  1 
ATOM   4782  C C   . ALA   B 1 137 ? -20.137 -0.546  23.961  1.00 28.08  ?  137 ALA   B C   1 
ATOM   4783  O O   . ALA   B 1 137 ? -21.301 -0.904  23.743  1.00 29.19  ?  137 ALA   B O   1 
ATOM   4784  C CB  . ALA   B 1 137 ? -18.349 -2.269  24.268  1.00 25.71  ?  137 ALA   B CB  1 
ATOM   4785  N N   . HIS   B 1 138 ? -19.845 0.469   24.779  1.00 31.80  ?  138 HIS   B N   1 
ATOM   4786  C CA  . HIS   B 1 138 ? -20.917 1.232   25.411  1.00 26.84  ?  138 HIS   B CA  1 
ATOM   4787  C C   . HIS   B 1 138 ? -21.668 2.074   24.388  1.00 31.97  ?  138 HIS   B C   1 
ATOM   4788  O O   . HIS   B 1 138 ? -22.898 2.187   24.456  1.00 30.76  ?  138 HIS   B O   1 
ATOM   4789  C CB  . HIS   B 1 138 ? -20.355 2.105   26.529  1.00 29.27  ?  138 HIS   B CB  1 
ATOM   4790  C CG  . HIS   B 1 138 ? -20.064 1.348   27.785  1.00 27.06  ?  138 HIS   B CG  1 
ATOM   4791  N ND1 . HIS   B 1 138 ? -21.059 0.903   28.630  1.00 29.38  ?  138 HIS   B ND1 1 
ATOM   4792  C CD2 . HIS   B 1 138 ? -18.895 0.939   28.331  1.00 25.32  ?  138 HIS   B CD2 1 
ATOM   4793  C CE1 . HIS   B 1 138 ? -20.514 0.263   29.649  1.00 24.57  ?  138 HIS   B CE1 1 
ATOM   4794  N NE2 . HIS   B 1 138 ? -19.202 0.271   29.493  1.00 24.52  ?  138 HIS   B NE2 1 
ATOM   4795  N N   . VAL   B 1 139 ? -20.959 2.669   23.430  1.00 27.41  ?  139 VAL   B N   1 
ATOM   4796  C CA  . VAL   B 1 139 ? -21.655 3.348   22.339  1.00 31.43  ?  139 VAL   B CA  1 
ATOM   4797  C C   . VAL   B 1 139 ? -22.614 2.385   21.649  1.00 27.68  ?  139 VAL   B C   1 
ATOM   4798  O O   . VAL   B 1 139 ? -23.800 2.684   21.467  1.00 28.98  ?  139 VAL   B O   1 
ATOM   4799  C CB  . VAL   B 1 139 ? -20.651 3.953   21.347  1.00 30.25  ?  139 VAL   B CB  1 
ATOM   4800  C CG1 . VAL   B 1 139 ? -21.378 4.435   20.092  1.00 29.43  ?  139 VAL   B CG1 1 
ATOM   4801  C CG2 . VAL   B 1 139 ? -19.894 5.093   22.001  1.00 33.16  ?  139 VAL   B CG2 1 
ATOM   4802  N N   . GLU   B 1 140 ? -22.123 1.198   21.288  1.00 30.12  ?  140 GLU   B N   1 
ATOM   4803  C CA  . GLU   B 1 140 ? -22.948 0.250   20.547  1.00 29.44  ?  140 GLU   B CA  1 
ATOM   4804  C C   . GLU   B 1 140 ? -24.036 -0.366  21.420  1.00 31.91  ?  140 GLU   B C   1 
ATOM   4805  O O   . GLU   B 1 140 ? -25.138 -0.639  20.928  1.00 33.80  ?  140 GLU   B O   1 
ATOM   4806  C CB  . GLU   B 1 140 ? -22.060 -0.828  19.929  1.00 31.99  ?  140 GLU   B CB  1 
ATOM   4807  C CG  . GLU   B 1 140 ? -21.244 -0.303  18.745  1.00 31.18  ?  140 GLU   B CG  1 
ATOM   4808  C CD  . GLU   B 1 140 ? -20.035 -1.163  18.398  1.00 40.32  ?  140 GLU   B CD  1 
ATOM   4809  O OE1 . GLU   B 1 140 ? -19.820 -2.200  19.066  1.00 43.47  ?  140 GLU   B OE1 1 
ATOM   4810  O OE2 . GLU   B 1 140 ? -19.294 -0.791  17.455  1.00 38.22  ?  140 GLU   B OE2 1 
ATOM   4811  N N   . LEU   B 1 141 ? -23.764 -0.570  22.709  1.00 30.13  ?  141 LEU   B N   1 
ATOM   4812  C CA  . LEU   B 1 141 ? -24.789 -1.103  23.598  1.00 29.57  ?  141 LEU   B CA  1 
ATOM   4813  C C   . LEU   B 1 141 ? -25.995 -0.178  23.671  1.00 29.84  ?  141 LEU   B C   1 
ATOM   4814  O O   . LEU   B 1 141 ? -27.136 -0.639  23.769  1.00 35.45  ?  141 LEU   B O   1 
ATOM   4815  C CB  . LEU   B 1 141 ? -24.204 -1.330  24.990  1.00 38.39  ?  141 LEU   B CB  1 
ATOM   4816  C CG  . LEU   B 1 141 ? -23.783 -2.768  25.272  1.00 32.28  ?  141 LEU   B CG  1 
ATOM   4817  C CD1 . LEU   B 1 141 ? -22.900 -2.844  26.519  1.00 33.43  ?  141 LEU   B CD1 1 
ATOM   4818  C CD2 . LEU   B 1 141 ? -25.041 -3.596  25.426  1.00 30.04  ?  141 LEU   B CD2 1 
ATOM   4819  N N   . ASN   B 1 142 ? -25.766 1.131   23.616  1.00 32.44  ?  142 ASN   B N   1 
ATOM   4820  C CA  . ASN   B 1 142 ? -26.851 2.099   23.634  1.00 33.64  ?  142 ASN   B CA  1 
ATOM   4821  C C   . ASN   B 1 142 ? -27.413 2.380   22.242  1.00 35.95  ?  142 ASN   B C   1 
ATOM   4822  O O   . ASN   B 1 142 ? -28.060 3.416   22.040  1.00 40.35  ?  142 ASN   B O   1 
ATOM   4823  C CB  . ASN   B 1 142 ? -26.382 3.394   24.296  1.00 33.36  ?  142 ASN   B CB  1 
ATOM   4824  C CG  . ASN   B 1 142 ? -26.162 3.232   25.778  1.00 29.96  ?  142 ASN   B CG  1 
ATOM   4825  O OD1 . ASN   B 1 142 ? -27.071 3.443   26.573  1.00 32.70  ?  142 ASN   B OD1 1 
ATOM   4826  N ND2 . ASN   B 1 142 ? -24.956 2.833   26.160  1.00 34.07  ?  142 ASN   B ND2 1 
ATOM   4827  N N   . GLY   B 1 143 ? -27.185 1.486   21.284  1.00 32.73  ?  143 GLY   B N   1 
ATOM   4828  C CA  . GLY   B 1 143 ? -27.815 1.625   19.984  1.00 37.18  ?  143 GLY   B CA  1 
ATOM   4829  C C   . GLY   B 1 143 ? -27.260 2.735   19.125  1.00 37.51  ?  143 GLY   B C   1 
ATOM   4830  O O   . GLY   B 1 143 ? -27.991 3.296   18.302  1.00 36.15  ?  143 GLY   B O   1 
ATOM   4831  N N   . CYS   B 1 144 ? -25.983 3.069   19.288  1.00 33.99  ?  144 CYS   B N   1 
ATOM   4832  C CA  . CYS   B 1 144 ? -25.326 4.053   18.443  1.00 34.57  ?  144 CYS   B CA  1 
ATOM   4833  C C   . CYS   B 1 144 ? -24.180 3.394   17.686  1.00 36.01  ?  144 CYS   B C   1 
ATOM   4834  O O   . CYS   B 1 144 ? -23.736 2.290   18.017  1.00 38.90  ?  144 CYS   B O   1 
ATOM   4835  C CB  . CYS   B 1 144 ? -24.791 5.235   19.266  1.00 36.20  ?  144 CYS   B CB  1 
ATOM   4836  S SG  . CYS   B 1 144 ? -25.976 5.953   20.427  1.00 38.98  ?  144 CYS   B SG  1 
ATOM   4837  N N   . LYS   B 1 145 ? -23.699 4.085   16.663  1.00 35.33  ?  145 LYS   B N   1 
ATOM   4838  C CA  . LYS   B 1 145 ? -22.551 3.635   15.894  1.00 34.32  ?  145 LYS   B CA  1 
ATOM   4839  C C   . LYS   B 1 145 ? -21.313 4.397   16.355  1.00 34.90  ?  145 LYS   B C   1 
ATOM   4840  O O   . LYS   B 1 145 ? -21.377 5.600   16.626  1.00 36.48  ?  145 LYS   B O   1 
ATOM   4841  C CB  . LYS   B 1 145 ? -22.800 3.839   14.395  1.00 35.63  ?  145 LYS   B CB  1 
ATOM   4842  C CG  . LYS   B 1 145 ? -21.706 3.286   13.490  1.00 47.27  ?  145 LYS   B CG  1 
ATOM   4843  C CD  . LYS   B 1 145 ? -21.989 3.591   12.018  1.00 44.04  ?  145 LYS   B CD  1 
ATOM   4844  C CE  . LYS   B 1 145 ? -20.823 3.168   11.124  1.00 50.84  ?  145 LYS   B CE  1 
ATOM   4845  N NZ  . LYS   B 1 145 ? -20.862 3.846   9.787   1.00 54.32  ?  145 LYS   B NZ  1 
ATOM   4846  N N   . ALA   B 1 146 ? -20.191 3.691   16.465  1.00 33.93  ?  146 ALA   B N   1 
ATOM   4847  C CA  . ALA   B 1 146 ? -18.928 4.281   16.913  1.00 33.20  ?  146 ALA   B CA  1 
ATOM   4848  C C   . ALA   B 1 146 ? -18.074 4.591   15.687  1.00 34.60  ?  146 ALA   B C   1 
ATOM   4849  O O   . ALA   B 1 146 ? -17.469 3.692   15.097  1.00 36.85  ?  146 ALA   B O   1 
ATOM   4850  C CB  . ALA   B 1 146 ? -18.205 3.345   17.874  1.00 30.08  ?  146 ALA   B CB  1 
ATOM   4851  N N   . ILE   B 1 147 ? -18.023 5.871   15.309  1.00 37.52  ?  147 ILE   B N   1 
ATOM   4852  C CA  . ILE   B 1 147 ? -17.256 6.327   14.151  1.00 33.36  ?  147 ILE   B CA  1 
ATOM   4853  C C   . ILE   B 1 147 ? -15.841 6.674   14.597  1.00 32.59  ?  147 ILE   B C   1 
ATOM   4854  O O   . ILE   B 1 147 ? -15.655 7.404   15.579  1.00 31.90  ?  147 ILE   B O   1 
ATOM   4855  C CB  . ILE   B 1 147 ? -17.926 7.545   13.497  1.00 34.78  ?  147 ILE   B CB  1 
ATOM   4856  C CG1 . ILE   B 1 147 ? -19.430 7.327   13.334  1.00 35.75  ?  147 ILE   B CG1 1 
ATOM   4857  C CG2 . ILE   B 1 147 ? -17.262 7.856   12.158  1.00 35.44  ?  147 ILE   B CG2 1 
ATOM   4858  C CD1 . ILE   B 1 147 ? -19.789 6.383   12.237  1.00 37.86  ?  147 ILE   B CD1 1 
ATOM   4859  N N   . ASN   B 1 148 ? -14.843 6.173   13.862  1.00 32.54  ?  148 ASN   B N   1 
ATOM   4860  C CA  . ASN   B 1 148 ? -13.428 6.395   14.156  1.00 31.09  ?  148 ASN   B CA  1 
ATOM   4861  C C   . ASN   B 1 148 ? -12.767 7.073   12.966  1.00 34.27  ?  148 ASN   B C   1 
ATOM   4862  O O   . ASN   B 1 148 ? -12.736 6.503   11.871  1.00 32.31  ?  148 ASN   B O   1 
ATOM   4863  C CB  . ASN   B 1 148 ? -12.717 5.077   14.455  1.00 30.78  ?  148 ASN   B CB  1 
ATOM   4864  C CG  . ASN   B 1 148 ? -13.267 4.386   15.679  1.00 33.87  ?  148 ASN   B CG  1 
ATOM   4865  O OD1 . ASN   B 1 148 ? -13.624 5.039   16.660  1.00 38.06  ?  148 ASN   B OD1 1 
ATOM   4866  N ND2 . ASN   B 1 148 ? -13.337 3.057   15.635  1.00 28.61  ?  148 ASN   B ND2 1 
ATOM   4867  N N   . ILE   B 1 149 ? -12.215 8.269   13.182  1.00 31.89  ?  149 ILE   B N   1 
ATOM   4868  C CA  . ILE   B 1 149 ? -11.636 9.055   12.093  1.00 32.65  ?  149 ILE   B CA  1 
ATOM   4869  C C   . ILE   B 1 149 ? -10.202 9.478   12.406  1.00 31.81  ?  149 ILE   B C   1 
ATOM   4870  O O   . ILE   B 1 149 ? -9.831  10.642  12.213  1.00 32.27  ?  149 ILE   B O   1 
ATOM   4871  C CB  . ILE   B 1 149 ? -12.507 10.286  11.792  1.00 33.93  ?  149 ILE   B CB  1 
ATOM   4872  C CG1 . ILE   B 1 149 ? -12.745 11.101  13.063  1.00 33.60  ?  149 ILE   B CG1 1 
ATOM   4873  C CG2 . ILE   B 1 149 ? -13.840 9.870   11.181  1.00 34.95  ?  149 ILE   B CG2 1 
ATOM   4874  C CD1 . ILE   B 1 149 ? -13.477 12.394  12.819  1.00 34.83  ?  149 ILE   B CD1 1 
ATOM   4875  N N   . VAL   B 1 150 ? -9.377  8.536   12.877  1.00 30.60  ?  150 VAL   B N   1 
ATOM   4876  C CA  . VAL   B 1 150 ? -7.988  8.858   13.182  1.00 30.33  ?  150 VAL   B CA  1 
ATOM   4877  C C   . VAL   B 1 150 ? -7.265  9.299   11.907  1.00 30.44  ?  150 VAL   B C   1 
ATOM   4878  O O   . VAL   B 1 150 ? -7.584  8.865   10.794  1.00 31.17  ?  150 VAL   B O   1 
ATOM   4879  C CB  . VAL   B 1 150 ? -7.276  7.661   13.839  1.00 30.27  ?  150 VAL   B CB  1 
ATOM   4880  C CG1 . VAL   B 1 150 ? -7.017  6.552   12.821  1.00 32.90  ?  150 VAL   B CG1 1 
ATOM   4881  C CG2 . VAL   B 1 150 ? -5.972  8.095   14.526  1.00 27.47  ?  150 VAL   B CG2 1 
ATOM   4882  N N   . THR   B 1 151 ? -6.297  10.194  12.074  1.00 31.24  ?  151 THR   B N   1 
ATOM   4883  C CA  . THR   B 1 151 ? -5.465  10.629  10.961  1.00 31.11  ?  151 THR   B CA  1 
ATOM   4884  C C   . THR   B 1 151 ? -4.900  9.434   10.201  1.00 32.00  ?  151 THR   B C   1 
ATOM   4885  O O   . THR   B 1 151 ? -4.453  8.450   10.796  1.00 29.32  ?  151 THR   B O   1 
ATOM   4886  C CB  . THR   B 1 151 ? -4.320  11.503  11.475  1.00 31.44  ?  151 THR   B CB  1 
ATOM   4887  O OG1 . THR   B 1 151 ? -3.335  11.646  10.446  1.00 31.97  ?  151 THR   B OG1 1 
ATOM   4888  C CG2 . THR   B 1 151 ? -3.673  10.867  12.693  1.00 28.73  ?  151 THR   B CG2 1 
ATOM   4889  N N   . GLU   B 1 152 ? -4.917  9.535   8.869   1.00 35.12  ?  152 GLU   B N   1 
ATOM   4890  C CA  . GLU   B 1 152 ? -4.348  8.480   8.036   1.00 38.03  ?  152 GLU   B CA  1 
ATOM   4891  C C   . GLU   B 1 152 ? -2.882  8.214   8.372   1.00 36.69  ?  152 GLU   B C   1 
ATOM   4892  O O   . GLU   B 1 152 ? -2.389  7.098   8.152   1.00 32.31  ?  152 GLU   B O   1 
ATOM   4893  C CB  . GLU   B 1 152 ? -4.498  8.845   6.557   1.00 38.37  ?  152 GLU   B CB  1 
ATOM   4894  C CG  . GLU   B 1 152 ? -5.931  9.159   6.122   1.00 50.35  ?  152 GLU   B CG  1 
ATOM   4895  C CD  . GLU   B 1 152 ? -6.864  7.951   6.165   1.00 50.39  ?  152 GLU   B CD  1 
ATOM   4896  O OE1 . GLU   B 1 152 ? -7.333  7.593   7.267   1.00 50.99  ?  152 GLU   B OE1 1 
ATOM   4897  O OE2 . GLU   B 1 152 ? -7.137  7.364   5.093   1.00 53.97  ?  152 GLU   B OE2 1 
ATOM   4898  N N   . LYS   B 1 153 ? -2.176  9.207   8.926   1.00 34.54  ?  153 LYS   B N   1 
ATOM   4899  C CA  . LYS   B 1 153 ? -0.785  9.004   9.319   1.00 32.99  ?  153 LYS   B CA  1 
ATOM   4900  C C   . LYS   B 1 153 ? -0.616  7.829   10.271  1.00 30.55  ?  153 LYS   B C   1 
ATOM   4901  O O   . LYS   B 1 153 ? 0.479   7.261   10.342  1.00 31.28  ?  153 LYS   B O   1 
ATOM   4902  C CB  . LYS   B 1 153 ? -0.221  10.271  9.966   1.00 29.15  ?  153 LYS   B CB  1 
ATOM   4903  C CG  . LYS   B 1 153 ? -0.387  11.533  9.126   1.00 31.44  ?  153 LYS   B CG  1 
ATOM   4904  C CD  . LYS   B 1 153 ? 0.318   11.407  7.796   1.00 40.22  ?  153 LYS   B CD  1 
ATOM   4905  C CE  . LYS   B 1 153 ? 0.278   12.722  7.014   1.00 47.03  ?  153 LYS   B CE  1 
ATOM   4906  N NZ  . LYS   B 1 153 ? 0.911   13.844  7.773   1.00 44.74  ?  153 LYS   B NZ  1 
ATOM   4907  N N   . ALA   B 1 154 ? -1.668  7.448   11.003  1.00 32.24  ?  154 ALA   B N   1 
ATOM   4908  C CA  . ALA   B 1 154 ? -1.516  6.380   11.988  1.00 32.14  ?  154 ALA   B CA  1 
ATOM   4909  C C   . ALA   B 1 154 ? -1.344  5.017   11.326  1.00 34.82  ?  154 ALA   B C   1 
ATOM   4910  O O   . ALA   B 1 154 ? -0.724  4.122   11.914  1.00 33.83  ?  154 ALA   B O   1 
ATOM   4911  C CB  . ALA   B 1 154 ? -2.710  6.363   12.945  1.00 30.29  ?  154 ALA   B CB  1 
ATOM   4912  N N   . PHE   B 1 155 ? -1.863  4.845   10.109  1.00 30.87  ?  155 PHE   B N   1 
ATOM   4913  C CA  . PHE   B 1 155 ? -1.754  3.573   9.403   1.00 38.05  ?  155 PHE   B CA  1 
ATOM   4914  C C   . PHE   B 1 155 ? -0.373  3.333   8.812   1.00 37.91  ?  155 PHE   B C   1 
ATOM   4915  O O   . PHE   B 1 155 ? -0.073  2.204   8.412   1.00 43.60  ?  155 PHE   B O   1 
ATOM   4916  C CB  . PHE   B 1 155 ? -2.793  3.504   8.286   1.00 43.73  ?  155 PHE   B CB  1 
ATOM   4917  C CG  . PHE   B 1 155 ? -4.191  3.794   8.744   1.00 42.00  ?  155 PHE   B CG  1 
ATOM   4918  C CD1 . PHE   B 1 155 ? -4.947  2.816   9.362   1.00 52.14  ?  155 PHE   B CD1 1 
ATOM   4919  C CD2 . PHE   B 1 155 ? -4.749  5.044   8.551   1.00 43.95  ?  155 PHE   B CD2 1 
ATOM   4920  C CE1 . PHE   B 1 155 ? -6.236  3.080   9.783   1.00 46.02  ?  155 PHE   B CE1 1 
ATOM   4921  C CE2 . PHE   B 1 155 ? -6.036  5.316   8.969   1.00 45.93  ?  155 PHE   B CE2 1 
ATOM   4922  C CZ  . PHE   B 1 155 ? -6.779  4.334   9.587   1.00 48.20  ?  155 PHE   B CZ  1 
ATOM   4923  N N   . ASP   B 1 156 ? 0.465   4.360   8.746   1.00 37.12  ?  156 ASP   B N   1 
ATOM   4924  C CA  . ASP   B 1 156 ? 1.814   4.249   8.199   1.00 36.45  ?  156 ASP   B CA  1 
ATOM   4925  C C   . ASP   B 1 156 ? 2.761   4.038   9.380   1.00 31.20  ?  156 ASP   B C   1 
ATOM   4926  O O   . ASP   B 1 156 ? 3.396   4.967   9.886   1.00 31.80  ?  156 ASP   B O   1 
ATOM   4927  C CB  . ASP   B 1 156 ? 2.148   5.503   7.398   1.00 31.17  ?  156 ASP   B CB  1 
ATOM   4928  C CG  . ASP   B 1 156 ? 3.266   5.288   6.410   1.00 42.76  ?  156 ASP   B CG  1 
ATOM   4929  O OD1 . ASP   B 1 156 ? 4.156   4.443   6.670   1.00 46.19  ?  156 ASP   B OD1 1 
ATOM   4930  O OD2 . ASP   B 1 156 ? 3.262   5.981   5.371   1.00 50.81  ?  156 ASP   B OD2 1 
ATOM   4931  N N   . SER   B 1 157 ? 2.851   2.784   9.825   1.00 29.31  ?  157 SER   B N   1 
ATOM   4932  C CA  . SER   B 1 157 ? 3.451   2.525   11.132  1.00 36.35  ?  157 SER   B CA  1 
ATOM   4933  C C   . SER   B 1 157 ? 4.935   2.871   11.145  1.00 34.15  ?  157 SER   B C   1 
ATOM   4934  O O   . SER   B 1 157 ? 5.457   3.356   12.155  1.00 29.42  ?  157 SER   B O   1 
ATOM   4935  C CB  . SER   B 1 157 ? 3.229   1.067   11.544  1.00 33.18  ?  157 SER   B CB  1 
ATOM   4936  O OG  . SER   B 1 157 ? 3.901   0.181   10.669  1.00 43.92  ?  157 SER   B OG  1 
ATOM   4937  N N   . GLU   B 1 158 ? 5.630   2.651   10.036  1.00 34.76  ?  158 GLU   B N   1 
ATOM   4938  C CA  . GLU   B 1 158 ? 7.057   2.920   10.024  1.00 27.88  ?  158 GLU   B CA  1 
ATOM   4939  C C   . GLU   B 1 158 ? 7.380   4.381   9.726   1.00 33.03  ?  158 GLU   B C   1 
ATOM   4940  O O   . GLU   B 1 158 ? 8.532   4.789   9.904   1.00 27.60  ?  158 GLU   B O   1 
ATOM   4941  C CB  . GLU   B 1 158 ? 7.751   2.001   9.015   1.00 33.33  ?  158 GLU   B CB  1 
ATOM   4942  C CG  . GLU   B 1 158 ? 7.370   2.251   7.562   1.00 42.24  ?  158 GLU   B CG  1 
ATOM   4943  C CD  . GLU   B 1 158 ? 6.257   1.334   7.039   1.00 49.21  ?  158 GLU   B CD  1 
ATOM   4944  O OE1 . GLU   B 1 158 ? 5.265   1.080   7.761   1.00 40.38  ?  158 GLU   B OE1 1 
ATOM   4945  O OE2 . GLU   B 1 158 ? 6.378   0.870   5.882   1.00 51.01  ?  158 GLU   B OE2 1 
ATOM   4946  N N   . THR   B 1 159 ? 6.405   5.184   9.306   1.00 27.13  ?  159 THR   B N   1 
ATOM   4947  C CA  . THR   B 1 159 ? 6.644   6.590   8.998   1.00 28.93  ?  159 THR   B CA  1 
ATOM   4948  C C   . THR   B 1 159 ? 6.359   7.454   10.220  1.00 30.51  ?  159 THR   B C   1 
ATOM   4949  O O   . THR   B 1 159 ? 5.223   7.503   10.695  1.00 33.03  ?  159 THR   B O   1 
ATOM   4950  C CB  . THR   B 1 159 ? 5.776   7.044   7.831   1.00 26.60  ?  159 THR   B CB  1 
ATOM   4951  O OG1 . THR   B 1 159 ? 6.200   6.380   6.636   1.00 27.29  ?  159 THR   B OG1 1 
ATOM   4952  C CG2 . THR   B 1 159 ? 5.890   8.547   7.649   1.00 28.43  ?  159 THR   B CG2 1 
ATOM   4953  N N   . TYR   B 1 160 ? 7.381   8.153   10.709  1.00 28.61  ?  160 TYR   B N   1 
ATOM   4954  C CA  . TYR   B 1 160 ? 7.221   9.003   11.882  1.00 29.00  ?  160 TYR   B CA  1 
ATOM   4955  C C   . TYR   B 1 160 ? 6.216   10.120  11.608  1.00 32.17  ?  160 TYR   B C   1 
ATOM   4956  O O   . TYR   B 1 160 ? 6.152   10.661  10.498  1.00 28.64  ?  160 TYR   B O   1 
ATOM   4957  C CB  . TYR   B 1 160 ? 8.579   9.604   12.285  1.00 24.36  ?  160 TYR   B CB  1 
ATOM   4958  C CG  . TYR   B 1 160 ? 8.508   10.619  13.411  1.00 23.81  ?  160 TYR   B CG  1 
ATOM   4959  C CD1 . TYR   B 1 160 ? 8.139   11.936  13.168  1.00 24.73  ?  160 TYR   B CD1 1 
ATOM   4960  C CD2 . TYR   B 1 160 ? 8.814   10.262  14.712  1.00 24.69  ?  160 TYR   B CD2 1 
ATOM   4961  C CE1 . TYR   B 1 160 ? 8.048   12.858  14.190  1.00 23.28  ?  160 TYR   B CE1 1 
ATOM   4962  C CE2 . TYR   B 1 160 ? 8.735   11.181  15.744  1.00 25.03  ?  160 TYR   B CE2 1 
ATOM   4963  C CZ  . TYR   B 1 160 ? 8.353   12.484  15.469  1.00 26.50  ?  160 TYR   B CZ  1 
ATOM   4964  O OH  . TYR   B 1 160 ? 8.269   13.419  16.483  1.00 30.74  ?  160 TYR   B OH  1 
ATOM   4965  N N   . ASP   B 1 161 ? 5.437   10.470  12.638  1.00 25.04  ?  161 ASP   B N   1 
ATOM   4966  C CA  . ASP   B 1 161 ? 4.685   11.721  12.659  1.00 25.22  ?  161 ASP   B CA  1 
ATOM   4967  C C   . ASP   B 1 161 ? 4.513   12.185  14.101  1.00 24.54  ?  161 ASP   B C   1 
ATOM   4968  O O   . ASP   B 1 161 ? 4.492   11.375  15.030  1.00 23.60  ?  161 ASP   B O   1 
ATOM   4969  C CB  . ASP   B 1 161 ? 3.312   11.603  11.987  1.00 26.14  ?  161 ASP   B CB  1 
ATOM   4970  C CG  . ASP   B 1 161 ? 2.678   12.963  11.730  1.00 29.30  ?  161 ASP   B CG  1 
ATOM   4971  O OD1 . ASP   B 1 161 ? 3.099   13.645  10.778  1.00 29.53  ?  161 ASP   B OD1 1 
ATOM   4972  O OD2 . ASP   B 1 161 ? 1.770   13.367  12.486  1.00 29.25  ?  161 ASP   B OD2 1 
ATOM   4973  N N   . ASP   B 1 162 ? 4.375   13.503  14.273  1.00 25.10  ?  162 ASP   B N   1 
ATOM   4974  C CA  . ASP   B 1 162 ? 4.291   14.088  15.611  1.00 24.61  ?  162 ASP   B CA  1 
ATOM   4975  C C   . ASP   B 1 162 ? 2.987   13.749  16.319  1.00 24.60  ?  162 ASP   B C   1 
ATOM   4976  O O   . ASP   B 1 162 ? 2.966   13.642  17.551  1.00 28.12  ?  162 ASP   B O   1 
ATOM   4977  C CB  . ASP   B 1 162 ? 4.424   15.610  15.545  1.00 26.80  ?  162 ASP   B CB  1 
ATOM   4978  C CG  . ASP   B 1 162 ? 5.870   16.078  15.486  1.00 28.12  ?  162 ASP   B CG  1 
ATOM   4979  O OD1 . ASP   B 1 162 ? 6.735   15.460  16.144  1.00 26.24  ?  162 ASP   B OD1 1 
ATOM   4980  O OD2 . ASP   B 1 162 ? 6.130   17.078  14.782  1.00 31.27  ?  162 ASP   B OD2 1 
ATOM   4981  N N   . TRP   B 1 163 ? 1.887   13.611  15.578  1.00 25.49  ?  163 TRP   B N   1 
ATOM   4982  C CA  . TRP   B 1 163 ? 0.563   13.518  16.171  1.00 25.70  ?  163 TRP   B CA  1 
ATOM   4983  C C   . TRP   B 1 163 ? -0.222  12.404  15.480  1.00 25.96  ?  163 TRP   B C   1 
ATOM   4984  O O   . TRP   B 1 163 ? -1.229  12.633  14.820  1.00 26.97  ?  163 TRP   B O   1 
ATOM   4985  C CB  . TRP   B 1 163 ? -0.177  14.854  16.073  1.00 26.77  ?  163 TRP   B CB  1 
ATOM   4986  C CG  . TRP   B 1 163 ? 0.685   16.048  16.370  1.00 26.78  ?  163 TRP   B CG  1 
ATOM   4987  C CD1 . TRP   B 1 163 ? 1.135   16.977  15.477  1.00 27.58  ?  163 TRP   B CD1 1 
ATOM   4988  C CD2 . TRP   B 1 163 ? 1.209   16.436  17.644  1.00 25.97  ?  163 TRP   B CD2 1 
ATOM   4989  N NE1 . TRP   B 1 163 ? 1.896   17.921  16.114  1.00 27.33  ?  163 TRP   B NE1 1 
ATOM   4990  C CE2 . TRP   B 1 163 ? 1.957   17.617  17.446  1.00 26.35  ?  163 TRP   B CE2 1 
ATOM   4991  C CE3 . TRP   B 1 163 ? 1.115   15.904  18.935  1.00 24.98  ?  163 TRP   B CE3 1 
ATOM   4992  C CZ2 . TRP   B 1 163 ? 2.611   18.271  18.491  1.00 28.79  ?  163 TRP   B CZ2 1 
ATOM   4993  C CZ3 . TRP   B 1 163 ? 1.761   16.557  19.972  1.00 24.56  ?  163 TRP   B CZ3 1 
ATOM   4994  C CH2 . TRP   B 1 163 ? 2.497   17.728  19.744  1.00 28.43  ?  163 TRP   B CH2 1 
ATOM   4995  N N   . LYS   B 1 164 ? 0.233   11.164  15.649  1.00 25.06  ?  164 LYS   B N   1 
ATOM   4996  C CA  . LYS   B 1 164 ? -0.476  10.064  15.008  1.00 25.30  ?  164 LYS   B CA  1 
ATOM   4997  C C   . LYS   B 1 164 ? -1.832  9.783   15.639  1.00 25.42  ?  164 LYS   B C   1 
ATOM   4998  O O   . LYS   B 1 164 ? -2.567  8.939   15.116  1.00 25.74  ?  164 LYS   B O   1 
ATOM   4999  C CB  . LYS   B 1 164 ? 0.378   8.799   15.024  1.00 24.32  ?  164 LYS   B CB  1 
ATOM   5000  C CG  . LYS   B 1 164 ? 1.399   8.749   13.908  1.00 24.54  ?  164 LYS   B CG  1 
ATOM   5001  C CD  . LYS   B 1 164 ? 2.120   7.418   13.882  1.00 24.01  ?  164 LYS   B CD  1 
ATOM   5002  C CE  . LYS   B 1 164 ? 2.874   7.237   12.575  1.00 28.05  ?  164 LYS   B CE  1 
ATOM   5003  N NZ  . LYS   B 1 164 ? 3.683   5.987   12.522  1.00 23.30  ?  164 LYS   B NZ  1 
ATOM   5004  N N   . GLY   B 1 165 ? -2.190  10.461  16.726  1.00 25.22  ?  165 GLY   B N   1 
ATOM   5005  C CA  . GLY   B 1 165 ? -3.506  10.324  17.311  1.00 25.44  ?  165 GLY   B CA  1 
ATOM   5006  C C   . GLY   B 1 165 ? -4.519  11.362  16.877  1.00 26.71  ?  165 GLY   B C   1 
ATOM   5007  O O   . GLY   B 1 165 ? -5.661  11.315  17.341  1.00 26.99  ?  165 GLY   B O   1 
ATOM   5008  N N   . ASP   B 1 166 ? -4.144  12.288  15.995  1.00 27.52  ?  166 ASP   B N   1 
ATOM   5009  C CA  . ASP   B 1 166 ? -5.028  13.388  15.627  1.00 28.75  ?  166 ASP   B CA  1 
ATOM   5010  C C   . ASP   B 1 166 ? -6.346  12.887  15.046  1.00 29.57  ?  166 ASP   B C   1 
ATOM   5011  O O   . ASP   B 1 166 ? -6.416  11.816  14.435  1.00 29.48  ?  166 ASP   B O   1 
ATOM   5012  C CB  . ASP   B 1 166 ? -4.349  14.299  14.604  1.00 29.50  ?  166 ASP   B CB  1 
ATOM   5013  C CG  . ASP   B 1 166 ? -3.494  15.357  15.249  1.00 29.19  ?  166 ASP   B CG  1 
ATOM   5014  O OD1 . ASP   B 1 166 ? -3.493  15.422  16.499  1.00 30.19  ?  166 ASP   B OD1 1 
ATOM   5015  O OD2 . ASP   B 1 166 ? -2.820  16.121  14.515  1.00 30.67  ?  166 ASP   B OD2 1 
ATOM   5016  N N   . PHE   B 1 167 ? -7.402  13.680  15.259  1.00 30.40  ?  167 PHE   B N   1 
ATOM   5017  C CA  . PHE   B 1 167 ? -8.597  13.591  14.428  1.00 31.55  ?  167 PHE   B CA  1 
ATOM   5018  C C   . PHE   B 1 167 ? -8.247  13.916  12.982  1.00 32.45  ?  167 PHE   B C   1 
ATOM   5019  O O   . PHE   B 1 167 ? -7.369  14.735  12.704  1.00 32.56  ?  167 PHE   B O   1 
ATOM   5020  C CB  . PHE   B 1 167 ? -9.665  14.586  14.889  1.00 32.35  ?  167 PHE   B CB  1 
ATOM   5021  C CG  . PHE   B 1 167 ? -10.434 14.160  16.101  1.00 31.79  ?  167 PHE   B CG  1 
ATOM   5022  C CD1 . PHE   B 1 167 ? -9.858  14.214  17.360  1.00 30.70  ?  167 PHE   B CD1 1 
ATOM   5023  C CD2 . PHE   B 1 167 ? -11.747 13.738  15.986  1.00 32.40  ?  167 PHE   B CD2 1 
ATOM   5024  C CE1 . PHE   B 1 167 ? -10.575 13.832  18.485  1.00 30.19  ?  167 PHE   B CE1 1 
ATOM   5025  C CE2 . PHE   B 1 167 ? -12.470 13.354  17.107  1.00 31.91  ?  167 PHE   B CE2 1 
ATOM   5026  C CZ  . PHE   B 1 167 ? -11.885 13.406  18.353  1.00 30.80  ?  167 PHE   B CZ  1 
ATOM   5027  N N   . ASP   B 1 168 ? -8.964  13.292  12.054  1.00 35.03  ?  168 ASP   B N   1 
ATOM   5028  C CA  . ASP   B 1 168 ? -8.976  13.738  10.665  1.00 34.31  ?  168 ASP   B CA  1 
ATOM   5029  C C   . ASP   B 1 168 ? -10.062 14.802  10.545  1.00 35.55  ?  168 ASP   B C   1 
ATOM   5030  O O   . ASP   B 1 168 ? -11.253 14.487  10.584  1.00 36.06  ?  168 ASP   B O   1 
ATOM   5031  C CB  . ASP   B 1 168 ? -9.222  12.567  9.719   1.00 34.52  ?  168 ASP   B CB  1 
ATOM   5032  C CG  . ASP   B 1 168 ? -8.933  12.915  8.265   1.00 42.33  ?  168 ASP   B CG  1 
ATOM   5033  O OD1 . ASP   B 1 168 ? -9.238  14.054  7.842   1.00 36.54  ?  168 ASP   B OD1 1 
ATOM   5034  O OD2 . ASP   B 1 168 ? -8.388  12.045  7.548   1.00 43.99  ?  168 ASP   B OD2 1 
ATOM   5035  N N   . ILE   B 1 169 ? -9.650  16.067  10.428  1.00 36.03  ?  169 ILE   B N   1 
ATOM   5036  C CA  . ILE   B 1 169 ? -10.615 17.166  10.425  1.00 37.18  ?  169 ILE   B CA  1 
ATOM   5037  C C   . ILE   B 1 169 ? -11.530 17.076  9.208   1.00 38.49  ?  169 ILE   B C   1 
ATOM   5038  O O   . ILE   B 1 169 ? -12.739 17.320  9.304   1.00 39.29  ?  169 ILE   B O   1 
ATOM   5039  C CB  . ILE   B 1 169 ? -9.886  18.523  10.480  1.00 39.65  ?  169 ILE   B CB  1 
ATOM   5040  C CG1 . ILE   B 1 169 ? -8.969  18.589  11.699  1.00 36.14  ?  169 ILE   B CG1 1 
ATOM   5041  C CG2 . ILE   B 1 169 ? -10.891 19.667  10.522  1.00 38.63  ?  169 ILE   B CG2 1 
ATOM   5042  C CD1 . ILE   B 1 169 ? -9.707  18.433  13.021  1.00 35.63  ?  169 ILE   B CD1 1 
ATOM   5043  N N   . LYS   B 1 170 ? -10.966 16.734  8.045   1.00 40.00  ?  170 LYS   B N   1 
ATOM   5044  C CA  . LYS   B 1 170 ? -11.769 16.603  6.831   1.00 40.62  ?  170 LYS   B CA  1 
ATOM   5045  C C   . LYS   B 1 170 ? -12.870 15.566  7.015   1.00 40.03  ?  170 LYS   B C   1 
ATOM   5046  O O   . LYS   B 1 170 ? -14.048 15.848  6.772   1.00 41.08  ?  170 LYS   B O   1 
ATOM   5047  C CB  . LYS   B 1 170 ? -10.866 16.243  5.647   1.00 42.14  ?  170 LYS   B CB  1 
ATOM   5048  C CG  . LYS   B 1 170 ? -11.558 16.223  4.283   1.00 41.48  ?  170 LYS   B CG  1 
ATOM   5049  C CD  . LYS   B 1 170 ? -10.553 15.927  3.166   1.00 44.49  ?  170 LYS   B CD  1 
ATOM   5050  C CE  . LYS   B 1 170 ? -11.226 15.843  1.802   1.00 51.54  ?  170 LYS   B CE  1 
ATOM   5051  N NZ  . LYS   B 1 170 ? -12.258 14.765  1.744   1.00 48.57  ?  170 LYS   B NZ  1 
ATOM   5052  N N   . LYS   B 1 171 ? -12.506 14.362  7.474   1.00 39.49  ?  171 LYS   B N   1 
ATOM   5053  C CA  . LYS   B 1 171 ? -13.515 13.336  7.737   1.00 39.46  ?  171 LYS   B CA  1 
ATOM   5054  C C   . LYS   B 1 171 ? -14.477 13.754  8.840   1.00 38.84  ?  171 LYS   B C   1 
ATOM   5055  O O   . LYS   B 1 171 ? -15.625 13.298  8.860   1.00 39.32  ?  171 LYS   B O   1 
ATOM   5056  C CB  . LYS   B 1 171 ? -12.851 12.010  8.115   1.00 37.50  ?  171 LYS   B CB  1 
ATOM   5057  C CG  . LYS   B 1 171 ? -12.061 11.338  7.006   1.00 39.65  ?  171 LYS   B CG  1 
ATOM   5058  C CD  . LYS   B 1 171 ? -11.408 10.061  7.534   1.00 41.36  ?  171 LYS   B CD  1 
ATOM   5059  C CE  . LYS   B 1 171 ? -10.611 9.335   6.459   1.00 46.60  ?  171 LYS   B CE  1 
ATOM   5060  N NZ  . LYS   B 1 171 ? -10.220 7.970   6.918   1.00 49.14  ?  171 LYS   B NZ  1 
ATOM   5061  N N   . LEU   B 1 172 ? -14.032 14.594  9.779   1.00 38.34  ?  172 LEU   B N   1 
ATOM   5062  C CA  . LEU   B 1 172 ? -14.940 15.066  10.822  1.00 38.44  ?  172 LEU   B CA  1 
ATOM   5063  C C   . LEU   B 1 172 ? -16.045 15.928  10.226  1.00 39.99  ?  172 LEU   B C   1 
ATOM   5064  O O   . LEU   B 1 172 ? -17.234 15.712  10.492  1.00 40.45  ?  172 LEU   B O   1 
ATOM   5065  C CB  . LEU   B 1 172 ? -14.170 15.842  11.895  1.00 37.64  ?  172 LEU   B CB  1 
ATOM   5066  C CG  . LEU   B 1 172 ? -15.029 16.477  13.001  1.00 42.10  ?  172 LEU   B CG  1 
ATOM   5067  C CD1 . LEU   B 1 172 ? -15.756 15.412  13.827  1.00 37.11  ?  172 LEU   B CD1 1 
ATOM   5068  C CD2 . LEU   B 1 172 ? -14.211 17.392  13.909  1.00 37.17  ?  172 LEU   B CD2 1 
ATOM   5069  N N   . LYS   B 1 173 ? -15.668 16.911  9.408   1.00 40.83  ?  173 LYS   B N   1 
ATOM   5070  C CA  . LYS   B 1 173 ? -16.668 17.747  8.758   1.00 42.37  ?  173 LYS   B CA  1 
ATOM   5071  C C   . LYS   B 1 173 ? -17.566 16.915  7.850   1.00 43.14  ?  173 LYS   B C   1 
ATOM   5072  O O   . LYS   B 1 173 ? -18.785 17.117  7.816   1.00 44.08  ?  173 LYS   B O   1 
ATOM   5073  C CB  . LYS   B 1 173 ? -15.977 18.866  7.978   1.00 43.07  ?  173 LYS   B CB  1 
ATOM   5074  C CG  . LYS   B 1 173 ? -15.174 19.818  8.854   1.00 42.49  ?  173 LYS   B CG  1 
ATOM   5075  C CD  . LYS   B 1 173 ? -14.576 20.947  8.022   1.00 48.29  ?  173 LYS   B CD  1 
ATOM   5076  C CE  . LYS   B 1 173 ? -13.794 21.936  8.880   1.00 46.00  ?  173 LYS   B CE  1 
ATOM   5077  N NZ  . LYS   B 1 173 ? -13.220 23.046  8.061   1.00 52.26  ?  173 LYS   B NZ  1 
ATOM   5078  N N   . GLU   B 1 174 ? -16.983 15.963  7.120   1.00 42.77  ?  174 GLU   B N   1 
ATOM   5079  C CA  . GLU   B 1 174 ? -17.789 15.105  6.259   1.00 43.46  ?  174 GLU   B CA  1 
ATOM   5080  C C   . GLU   B 1 174 ? -18.783 14.293  7.073   1.00 43.12  ?  174 GLU   B C   1 
ATOM   5081  O O   . GLU   B 1 174 ? -19.923 14.089  6.645   1.00 44.08  ?  174 GLU   B O   1 
ATOM   5082  C CB  . GLU   B 1 174 ? -16.891 14.182  5.437   1.00 43.00  ?  174 GLU   B CB  1 
ATOM   5083  C CG  . GLU   B 1 174 ? -16.162 14.876  4.302   1.00 46.57  ?  174 GLU   B CG  1 
ATOM   5084  C CD  . GLU   B 1 174 ? -15.002 14.055  3.775   1.00 56.99  ?  174 GLU   B CD  1 
ATOM   5085  O OE1 . GLU   B 1 174 ? -14.689 13.008  4.388   1.00 56.98  ?  174 GLU   B OE1 1 
ATOM   5086  O OE2 . GLU   B 1 174 ? -14.402 14.459  2.752   1.00 63.85  ?  174 GLU   B OE2 1 
ATOM   5087  N N   . ASN   B 1 175 ? -18.372 13.827  8.258   1.00 41.77  ?  175 ASN   B N   1 
ATOM   5088  C CA  . ASN   B 1 175 ? -19.284 13.041  9.084   1.00 42.54  ?  175 ASN   B CA  1 
ATOM   5089  C C   . ASN   B 1 175 ? -20.365 13.906  9.714   1.00 42.11  ?  175 ASN   B C   1 
ATOM   5090  O O   . ASN   B 1 175 ? -21.502 13.451  9.867   1.00 42.53  ?  175 ASN   B O   1 
ATOM   5091  C CB  . ASN   B 1 175 ? -18.513 12.277  10.158  1.00 39.75  ?  175 ASN   B CB  1 
ATOM   5092  C CG  . ASN   B 1 175 ? -17.981 10.962  9.648   1.00 39.12  ?  175 ASN   B CG  1 
ATOM   5093  O OD1 . ASN   B 1 175 ? -18.737 10.007  9.463   1.00 39.28  ?  175 ASN   B OD1 1 
ATOM   5094  N ND2 . ASN   B 1 175 ? -16.677 10.903  9.399   1.00 39.94  ?  175 ASN   B ND2 1 
ATOM   5095  N N   . ILE   B 1 176 ? -20.042 15.148  10.079  1.00 42.28  ?  176 ILE   B N   1 
ATOM   5096  C CA  . ILE   B 1 176 ? -21.087 16.066  10.521  1.00 43.17  ?  176 ILE   B CA  1 
ATOM   5097  C C   . ILE   B 1 176 ? -22.064 16.332  9.384   1.00 44.78  ?  176 ILE   B C   1 
ATOM   5098  O O   . ILE   B 1 176 ? -23.251 16.589  9.616   1.00 45.58  ?  176 ILE   B O   1 
ATOM   5099  C CB  . ILE   B 1 176 ? -20.454 17.367  11.057  1.00 43.09  ?  176 ILE   B CB  1 
ATOM   5100  C CG1 . ILE   B 1 176 ? -19.547 17.059  12.253  1.00 41.50  ?  176 ILE   B CG1 1 
ATOM   5101  C CG2 . ILE   B 1 176 ? -21.528 18.392  11.437  1.00 44.13  ?  176 ILE   B CG2 1 
ATOM   5102  C CD1 . ILE   B 1 176 ? -18.909 18.275  12.863  1.00 41.35  ?  176 ILE   B CD1 1 
ATOM   5103  N N   . ALA   B 1 177 ? -21.590 16.254  8.140   1.00 45.28  ?  177 ALA   B N   1 
ATOM   5104  C CA  . ALA   B 1 177 ? -22.443 16.503  6.984   1.00 46.83  ?  177 ALA   B CA  1 
ATOM   5105  C C   . ALA   B 1 177 ? -23.326 15.298  6.675   1.00 47.03  ?  177 ALA   B C   1 
ATOM   5106  O O   . ALA   B 1 177 ? -24.533 15.443  6.459   1.00 49.28  ?  177 ALA   B O   1 
ATOM   5107  C CB  . ALA   B 1 177 ? -21.582 16.863  5.775   1.00 47.30  ?  177 ALA   B CB  1 
ATOM   5108  N N   . GLN   B 1 178 ? -22.742 14.098  6.667   1.00 46.00  ?  178 GLN   B N   1 
ATOM   5109  C CA  . GLN   B 1 178 ? -23.476 12.910  6.243   1.00 46.22  ?  178 GLN   B CA  1 
ATOM   5110  C C   . GLN   B 1 178 ? -24.443 12.414  7.308   1.00 45.87  ?  178 GLN   B C   1 
ATOM   5111  O O   . GLN   B 1 178 ? -25.442 11.765  6.976   1.00 46.50  ?  178 GLN   B O   1 
ATOM   5112  C CB  . GLN   B 1 178 ? -22.497 11.797  5.867   1.00 45.26  ?  178 GLN   B CB  1 
ATOM   5113  C CG  . GLN   B 1 178 ? -21.574 12.146  4.698   1.00 48.37  ?  178 GLN   B CG  1 
ATOM   5114  C CD  . GLN   B 1 178 ? -22.282 12.108  3.361   1.00 47.13  ?  178 GLN   B CD  1 
ATOM   5115  O OE1 . GLN   B 1 178 ? -23.412 11.627  3.257   1.00 48.33  ?  178 GLN   B OE1 1 
ATOM   5116  N NE2 . GLN   B 1 178 ? -21.621 12.615  2.325   1.00 52.85  ?  178 GLN   B NE2 1 
ATOM   5117  N N   . HIS   B 1 179 ? -24.168 12.696  8.581   1.00 44.90  ?  179 HIS   B N   1 
ATOM   5118  C CA  . HIS   B 1 179 ? -25.040 12.267  9.664   1.00 44.51  ?  179 HIS   B CA  1 
ATOM   5119  C C   . HIS   B 1 179 ? -25.903 13.388  10.219  1.00 45.31  ?  179 HIS   B C   1 
ATOM   5120  O O   . HIS   B 1 179 ? -27.024 13.124  10.666  1.00 45.65  ?  179 HIS   B O   1 
ATOM   5121  C CB  . HIS   B 1 179 ? -24.210 11.657  10.798  1.00 43.83  ?  179 HIS   B CB  1 
ATOM   5122  C CG  . HIS   B 1 179 ? -23.469 10.421  10.398  1.00 41.97  ?  179 HIS   B CG  1 
ATOM   5123  N ND1 . HIS   B 1 179 ? -24.078 9.187   10.306  1.00 41.85  ?  179 HIS   B ND1 1 
ATOM   5124  C CD2 . HIS   B 1 179 ? -22.175 10.229  10.053  1.00 41.24  ?  179 HIS   B CD2 1 
ATOM   5125  C CE1 . HIS   B 1 179 ? -23.188 8.287   9.927   1.00 43.44  ?  179 HIS   B CE1 1 
ATOM   5126  N NE2 . HIS   B 1 179 ? -22.025 8.893   9.769   1.00 41.87  ?  179 HIS   B NE2 1 
ATOM   5127  N N   . GLY   B 1 180 ? -25.424 14.628  10.184  1.00 45.65  ?  180 GLY   B N   1 
ATOM   5128  C CA  . GLY   B 1 180 ? -26.165 15.732  10.764  1.00 46.37  ?  180 GLY   B CA  1 
ATOM   5129  C C   . GLY   B 1 180 ? -25.806 15.946  12.220  1.00 45.21  ?  180 GLY   B C   1 
ATOM   5130  O O   . GLY   B 1 180 ? -25.651 14.980  12.973  1.00 44.14  ?  180 GLY   B O   1 
ATOM   5131  N N   . ALA   B 1 181 ? -25.664 17.208  12.631  1.00 45.54  ?  181 ALA   B N   1 
ATOM   5132  C CA  . ALA   B 1 181 ? -25.287 17.504  14.008  1.00 44.50  ?  181 ALA   B CA  1 
ATOM   5133  C C   . ALA   B 1 181 ? -26.337 17.040  15.005  1.00 44.31  ?  181 ALA   B C   1 
ATOM   5134  O O   . ALA   B 1 181 ? -26.031 16.914  16.196  1.00 43.22  ?  181 ALA   B O   1 
ATOM   5135  C CB  . ALA   B 1 181 ? -25.036 19.002  14.179  1.00 45.08  ?  181 ALA   B CB  1 
ATOM   5136  N N   . ASP   B 1 182 ? -27.568 16.789  14.551  1.00 45.35  ?  182 ASP   B N   1 
ATOM   5137  C CA  . ASP   B 1 182 ? -28.592 16.249  15.433  1.00 45.19  ?  182 ASP   B CA  1 
ATOM   5138  C C   . ASP   B 1 182 ? -28.366 14.776  15.748  1.00 43.98  ?  182 ASP   B C   1 
ATOM   5139  O O   . ASP   B 1 182 ? -28.870 14.291  16.765  1.00 49.52  ?  182 ASP   B O   1 
ATOM   5140  C CB  . ASP   B 1 182 ? -29.981 16.444  14.818  1.00 46.75  ?  182 ASP   B CB  1 
ATOM   5141  C CG  . ASP   B 1 182 ? -30.442 17.885  14.878  1.00 52.41  ?  182 ASP   B CG  1 
ATOM   5142  O OD1 . ASP   B 1 182 ? -29.661 18.732  15.361  1.00 56.94  ?  182 ASP   B OD1 1 
ATOM   5143  O OD2 . ASP   B 1 182 ? -31.579 18.175  14.443  1.00 60.39  ?  182 ASP   B OD2 1 
ATOM   5144  N N   . ASN   B 1 183 ? -27.629 14.054  14.907  1.00 43.62  ?  183 ASN   B N   1 
ATOM   5145  C CA  . ASN   B 1 183 ? -27.369 12.642  15.145  1.00 42.51  ?  183 ASN   B CA  1 
ATOM   5146  C C   . ASN   B 1 183 ? -26.039 12.379  15.835  1.00 40.95  ?  183 ASN   B C   1 
ATOM   5147  O O   . ASN   B 1 183 ? -25.758 11.222  16.170  1.00 39.92  ?  183 ASN   B O   1 
ATOM   5148  C CB  . ASN   B 1 183 ? -27.407 11.857  13.830  1.00 43.03  ?  183 ASN   B CB  1 
ATOM   5149  C CG  . ASN   B 1 183 ? -28.812 11.645  13.322  1.00 44.29  ?  183 ASN   B CG  1 
ATOM   5150  O OD1 . ASN   B 1 183 ? -29.595 10.897  13.912  1.00 44.05  ?  183 ASN   B OD1 1 
ATOM   5151  N ND2 . ASN   B 1 183 ? -29.139 12.295  12.214  1.00 45.65  ?  183 ASN   B ND2 1 
ATOM   5152  N N   A ILE   B 1 184 ? -25.219 13.409  16.043  0.46 40.79  ?  184 ILE   B N   1 
ATOM   5153  N N   B ILE   B 1 184 ? -25.220 13.405  16.056  0.54 40.78  ?  184 ILE   B N   1 
ATOM   5154  C CA  A ILE   B 1 184 ? -23.935 13.271  16.727  0.46 39.37  ?  184 ILE   B CA  1 
ATOM   5155  C CA  B ILE   B 1 184 ? -23.931 13.240  16.721  0.54 39.36  ?  184 ILE   B CA  1 
ATOM   5156  C C   A ILE   B 1 184 ? -24.208 13.428  18.220  0.46 38.65  ?  184 ILE   B C   1 
ATOM   5157  C C   B ILE   B 1 184 ? -24.170 13.423  18.217  0.54 38.62  ?  184 ILE   B C   1 
ATOM   5158  O O   A ILE   B 1 184 ? -24.383 14.542  18.717  0.46 39.06  ?  184 ILE   B O   1 
ATOM   5159  O O   B ILE   B 1 184 ? -24.290 14.546  18.709  0.54 39.00  ?  184 ILE   B O   1 
ATOM   5160  C CB  A ILE   B 1 184 ? -22.909 14.295  16.236  0.46 39.56  ?  184 ILE   B CB  1 
ATOM   5161  C CB  B ILE   B 1 184 ? -22.886 14.219  16.189  0.54 39.53  ?  184 ILE   B CB  1 
ATOM   5162  C CG1 A ILE   B 1 184 ? -22.972 14.459  14.717  0.46 40.71  ?  184 ILE   B CG1 1 
ATOM   5163  C CG1 B ILE   B 1 184 ? -22.731 14.050  14.681  0.54 40.35  ?  184 ILE   B CG1 1 
ATOM   5164  C CG2 A ILE   B 1 184 ? -21.506 13.883  16.661  0.46 38.11  ?  184 ILE   B CG2 1 
ATOM   5165  C CG2 B ILE   B 1 184 ? -21.549 13.993  16.876  0.54 38.06  ?  184 ILE   B CG2 1 
ATOM   5166  C CD1 A ILE   B 1 184 ? -22.559 13.237  13.952  0.46 40.29  ?  184 ILE   B CD1 1 
ATOM   5167  C CD1 B ILE   B 1 184 ? -21.752 15.001  14.087  0.54 40.60  ?  184 ILE   B CD1 1 
ATOM   5168  N N   . VAL   B 1 185 ? -24.251 12.308  18.943  1.00 37.60  ?  185 VAL   B N   1 
ATOM   5169  C CA  . VAL   B 1 185 ? -24.499 12.386  20.380  1.00 36.87  ?  185 VAL   B CA  1 
ATOM   5170  C C   . VAL   B 1 185 ? -23.339 13.080  21.078  1.00 36.02  ?  185 VAL   B C   1 
ATOM   5171  O O   . VAL   B 1 185 ? -23.538 13.924  21.959  1.00 36.06  ?  185 VAL   B O   1 
ATOM   5172  C CB  . VAL   B 1 185 ? -24.754 10.989  20.970  1.00 35.91  ?  185 VAL   B CB  1 
ATOM   5173  C CG1 . VAL   B 1 185 ? -25.021 11.101  22.464  1.00 35.18  ?  185 VAL   B CG1 1 
ATOM   5174  C CG2 . VAL   B 1 185 ? -25.919 10.334  20.283  1.00 36.80  ?  185 VAL   B CG2 1 
ATOM   5175  N N   . ALA   B 1 186 ? -22.114 12.750  20.686  1.00 35.27  ?  186 ALA   B N   1 
ATOM   5176  C CA  . ALA   B 1 186 ? -20.941 13.376  21.273  1.00 34.48  ?  186 ALA   B CA  1 
ATOM   5177  C C   . ALA   B 1 186 ? -19.735 13.062  20.409  1.00 34.08  ?  186 ALA   B C   1 
ATOM   5178  O O   . ALA   B 1 186 ? -19.736 12.115  19.618  1.00 34.08  ?  186 ALA   B O   1 
ATOM   5179  C CB  . ALA   B 1 186 ? -20.694 12.905  22.715  1.00 33.15  ?  186 ALA   B CB  1 
ATOM   5180  N N   . ILE   B 1 187 ? -18.708 13.884  20.570  1.00 33.77  ?  187 ILE   B N   1 
ATOM   5181  C CA  . ILE   B 1 187 ? -17.378 13.610  20.050  1.00 33.12  ?  187 ILE   B CA  1 
ATOM   5182  C C   . ILE   B 1 187 ? -16.515 13.203  21.234  1.00 31.63  ?  187 ILE   B C   1 
ATOM   5183  O O   . ILE   B 1 187 ? -16.569 13.839  22.293  1.00 31.35  ?  187 ILE   B O   1 
ATOM   5184  C CB  . ILE   B 1 187 ? -16.803 14.826  19.306  1.00 33.90  ?  187 ILE   B CB  1 
ATOM   5185  C CG1 . ILE   B 1 187 ? -17.624 15.077  18.037  1.00 35.35  ?  187 ILE   B CG1 1 
ATOM   5186  C CG2 . ILE   B 1 187 ? -15.324 14.633  18.974  1.00 33.09  ?  187 ILE   B CG2 1 
ATOM   5187  C CD1 . ILE   B 1 187 ? -17.400 16.426  17.436  1.00 36.34  ?  187 ILE   B CD1 1 
ATOM   5188  N N   . VAL   B 1 188 ? -15.768 12.115  21.074  1.00 30.70  ?  188 VAL   B N   1 
ATOM   5189  C CA  . VAL   B 1 188 ? -14.946 11.557  22.136  1.00 29.25  ?  188 VAL   B CA  1 
ATOM   5190  C C   . VAL   B 1 188 ? -13.490 11.738  21.727  1.00 28.75  ?  188 VAL   B C   1 
ATOM   5191  O O   . VAL   B 1 188 ? -12.998 11.050  20.826  1.00 29.11  ?  188 VAL   B O   1 
ATOM   5192  C CB  . VAL   B 1 188 ? -15.283 10.083  22.405  1.00 29.96  ?  188 VAL   B CB  1 
ATOM   5193  C CG1 . VAL   B 1 188 ? -14.394 9.517   23.508  1.00 30.38  ?  188 VAL   B CG1 1 
ATOM   5194  C CG2 . VAL   B 1 188 ? -16.744 9.938   22.789  1.00 29.42  ?  188 VAL   B CG2 1 
ATOM   5195  N N   . SER   B 1 189 ? -12.798 12.677  22.370  1.00 28.45  ?  189 SER   B N   1 
ATOM   5196  C CA  . SER   B 1 189 ? -11.374 12.891  22.129  1.00 27.90  ?  189 SER   B CA  1 
ATOM   5197  C C   . SER   B 1 189 ? -10.596 11.960  23.045  1.00 26.43  ?  189 SER   B C   1 
ATOM   5198  O O   . SER   B 1 189 ? -10.629 12.122  24.267  1.00 25.80  ?  189 SER   B O   1 
ATOM   5199  C CB  . SER   B 1 189 ? -10.994 14.345  22.384  1.00 28.31  ?  189 SER   B CB  1 
ATOM   5200  O OG  . SER   B 1 189 ? -11.625 15.217  21.465  1.00 29.70  ?  189 SER   B OG  1 
ATOM   5201  N N   . THR   B 1 190 ? -9.893  10.988  22.464  1.00 25.90  ?  190 THR   B N   1 
ATOM   5202  C CA  . THR   B 1 190 ? -9.144  9.995   23.234  1.00 24.53  ?  190 THR   B CA  1 
ATOM   5203  C C   . THR   B 1 190 ? -7.679  10.411  23.317  1.00 23.92  ?  190 THR   B C   1 
ATOM   5204  O O   . THR   B 1 190 ? -6.987  10.439  22.298  1.00 24.19  ?  190 THR   B O   1 
ATOM   5205  C CB  . THR   B 1 190 ? -9.262  8.613   22.597  1.00 24.31  ?  190 THR   B CB  1 
ATOM   5206  O OG1 . THR   B 1 190 ? -10.645 8.297   22.371  1.00 25.04  ?  190 THR   B OG1 1 
ATOM   5207  C CG2 . THR   B 1 190 ? -8.653  7.568   23.497  1.00 22.94  ?  190 THR   B CG2 1 
ATOM   5208  N N   . VAL   B 1 191 ? -7.204  10.713  24.525  1.00 23.11  ?  191 VAL   B N   1 
ATOM   5209  C CA  . VAL   B 1 191 ? -5.846  11.222  24.732  1.00 22.56  ?  191 VAL   B CA  1 
ATOM   5210  C C   . VAL   B 1 191 ? -5.145  10.372  25.791  1.00 24.79  ?  191 VAL   B C   1 
ATOM   5211  O O   . VAL   B 1 191 ? -5.668  10.211  26.899  1.00 20.86  ?  191 VAL   B O   1 
ATOM   5212  C CB  . VAL   B 1 191 ? -5.851  12.707  25.140  1.00 23.09  ?  191 VAL   B CB  1 
ATOM   5213  C CG1 . VAL   B 1 191 ? -6.363  13.559  23.996  1.00 24.46  ?  191 VAL   B CG1 1 
ATOM   5214  C CG2 . VAL   B 1 191 ? -6.712  12.938  26.406  1.00 22.93  ?  191 VAL   B CG2 1 
ATOM   5215  N N   . THR   B 1 192 ? -3.986  9.788   25.445  1.00 20.84  ?  192 THR   B N   1 
ATOM   5216  C CA  . THR   B 1 192 ? -3.520  9.639   24.063  1.00 21.80  ?  192 THR   B CA  1 
ATOM   5217  C C   . THR   B 1 192 ? -4.438  8.682   23.327  1.00 21.44  ?  192 THR   B C   1 
ATOM   5218  O O   . THR   B 1 192 ? -5.265  8.028   23.942  1.00 21.88  ?  192 THR   B O   1 
ATOM   5219  C CB  . THR   B 1 192 ? -2.091  9.061   23.978  1.00 22.19  ?  192 THR   B CB  1 
ATOM   5220  O OG1 . THR   B 1 192 ? -2.046  7.835   24.718  1.00 19.09  ?  192 THR   B OG1 1 
ATOM   5221  C CG2 . THR   B 1 192 ? -1.044  10.036  24.523  1.00 22.60  ?  192 THR   B CG2 1 
ATOM   5222  N N   . CYS   B 1 193 ? -4.284  8.571   22.014  1.00 22.34  ?  193 CYS   B N   1 
ATOM   5223  C CA  . CYS   B 1 193 ? -5.135  7.669   21.245  1.00 22.58  ?  193 CYS   B CA  1 
ATOM   5224  C C   . CYS   B 1 193 ? -4.609  6.248   21.415  1.00 21.57  ?  193 CYS   B C   1 
ATOM   5225  O O   . CYS   B 1 193 ? -3.672  5.836   20.731  1.00 22.85  ?  193 CYS   B O   1 
ATOM   5226  C CB  . CYS   B 1 193 ? -5.172  8.081   19.782  1.00 23.69  ?  193 CYS   B CB  1 
ATOM   5227  S SG  . CYS   B 1 193 ? -6.351  7.120   18.834  1.00 24.45  ?  193 CYS   B SG  1 
ATOM   5228  N N   . ASN   B 1 194 ? -5.208  5.496   22.343  1.00 21.11  ?  194 ASN   B N   1 
ATOM   5229  C CA  . ASN   B 1 194 ? -4.727  4.152   22.662  1.00 22.29  ?  194 ASN   B CA  1 
ATOM   5230  C C   . ASN   B 1 194 ? -4.675  3.276   21.413  1.00 21.88  ?  194 ASN   B C   1 
ATOM   5231  O O   . ASN   B 1 194 ? -3.617  2.756   21.042  1.00 26.89  ?  194 ASN   B O   1 
ATOM   5232  C CB  . ASN   B 1 194 ? -5.628  3.524   23.728  1.00 22.60  ?  194 ASN   B CB  1 
ATOM   5233  C CG  . ASN   B 1 194 ? -5.021  2.273   24.370  1.00 27.49  ?  194 ASN   B CG  1 
ATOM   5234  O OD1 . ASN   B 1 194 ? -3.908  1.853   24.050  1.00 27.97  ?  194 ASN   B OD1 1 
ATOM   5235  N ND2 . ASN   B 1 194 ? -5.763  1.680   25.297  1.00 30.17  ?  194 ASN   B ND2 1 
ATOM   5236  N N   . SER   B 1 195 ? -5.816  3.124   20.743  1.00 22.96  ?  195 SER   B N   1 
ATOM   5237  C CA  . SER   B 1 195 ? -5.916  2.261   19.570  1.00 27.59  ?  195 SER   B CA  1 
ATOM   5238  C C   . SER   B 1 195 ? -4.888  2.623   18.501  1.00 32.71  ?  195 SER   B C   1 
ATOM   5239  O O   . SER   B 1 195 ? -4.335  1.737   17.836  1.00 33.54  ?  195 SER   B O   1 
ATOM   5240  C CB  . SER   B 1 195 ? -7.329  2.354   19.007  1.00 32.05  ?  195 SER   B CB  1 
ATOM   5241  O OG  . SER   B 1 195 ? -8.239  2.659   20.049  1.00 35.12  ?  195 SER   B OG  1 
ATOM   5242  N N   . ALA   B 1 196 ? -4.619  3.918   18.311  1.00 33.55  ?  196 ALA   B N   1 
ATOM   5243  C CA  . ALA   B 1 196 ? -3.604  4.322   17.340  1.00 23.59  ?  196 ALA   B CA  1 
ATOM   5244  C C   . ALA   B 1 196 ? -2.183  4.027   17.800  1.00 28.39  ?  196 ALA   B C   1 
ATOM   5245  O O   . ALA   B 1 196 ? -1.240  4.305   17.048  1.00 27.46  ?  196 ALA   B O   1 
ATOM   5246  C CB  . ALA   B 1 196 ? -3.735  5.811   17.024  1.00 25.85  ?  196 ALA   B CB  1 
ATOM   5247  N N   . GLY   B 1 197 ? -1.995  3.487   19.001  1.00 27.82  ?  197 GLY   B N   1 
ATOM   5248  C CA  . GLY   B 1 197 ? -0.664  3.178   19.481  1.00 24.33  ?  197 GLY   B CA  1 
ATOM   5249  C C   . GLY   B 1 197 ? -0.216  4.035   20.647  1.00 21.20  ?  197 GLY   B C   1 
ATOM   5250  O O   . GLY   B 1 197 ? 0.984   4.233   20.861  1.00 22.16  ?  197 GLY   B O   1 
ATOM   5251  N N   . GLY   B 1 198 ? -1.171  4.544   21.414  1.00 20.75  ?  198 GLY   B N   1 
ATOM   5252  C CA  . GLY   B 1 198 ? -0.836  5.455   22.489  1.00 20.43  ?  198 GLY   B CA  1 
ATOM   5253  C C   . GLY   B 1 198 ? -0.242  6.751   21.993  1.00 22.59  ?  198 GLY   B C   1 
ATOM   5254  O O   . GLY   B 1 198 ? 0.578   7.361   22.691  1.00 21.62  ?  198 GLY   B O   1 
ATOM   5255  N N   . GLN   B 1 199 ? -0.631  7.186   20.792  1.00 20.49  ?  199 GLN   B N   1 
ATOM   5256  C CA  . GLN   B 1 199 ? -0.120  8.292   19.993  1.00 21.24  ?  199 GLN   B CA  1 
ATOM   5257  C C   . GLN   B 1 199 ? -0.825  9.590   20.358  1.00 21.93  ?  199 GLN   B C   1 
ATOM   5258  O O   . GLN   B 1 199 ? -2.055  9.627   20.441  1.00 22.48  ?  199 GLN   B O   1 
ATOM   5259  C CB  . GLN   B 1 199 ? -0.305  8.017   18.503  1.00 22.12  ?  199 GLN   B CB  1 
ATOM   5260  C CG  . GLN   B 1 199 ? 0.497   6.843   17.989  1.00 22.49  ?  199 GLN   B CG  1 
ATOM   5261  C CD  . GLN   B 1 199 ? 1.984   7.005   18.236  1.00 21.47  ?  199 GLN   B CD  1 
ATOM   5262  O OE1 . GLN   B 1 199 ? 2.530   8.103   18.113  1.00 21.98  ?  199 GLN   B OE1 1 
ATOM   5263  N NE2 . GLN   B 1 199 ? 2.646   5.912   18.602  1.00 20.13  ?  199 GLN   B NE2 1 
ATOM   5264  N N   . PRO   B 1 200 ? -0.052  10.652  20.552  1.00 21.96  ?  200 PRO   B N   1 
ATOM   5265  C CA  . PRO   B 1 200 ? -0.623  11.890  21.085  1.00 22.93  ?  200 PRO   B CA  1 
ATOM   5266  C C   . PRO   B 1 200 ? -1.506  12.609  20.074  1.00 23.87  ?  200 PRO   B C   1 
ATOM   5267  O O   . PRO   B 1 200 ? -1.396  12.439  18.857  1.00 24.83  ?  200 PRO   B O   1 
ATOM   5268  C CB  . PRO   B 1 200 ? 0.615   12.725  21.432  1.00 22.34  ?  200 PRO   B CB  1 
ATOM   5269  C CG  . PRO   B 1 200 ? 1.665   12.245  20.478  1.00 21.99  ?  200 PRO   B CG  1 
ATOM   5270  C CD  . PRO   B 1 200 ? 1.394   10.775  20.273  1.00 21.53  ?  200 PRO   B CD  1 
ATOM   5271  N N   . VAL   B 1 201 ? -2.415  13.416  20.617  1.00 24.89  ?  201 VAL   B N   1 
ATOM   5272  C CA  . VAL   B 1 201 ? -3.249  14.335  19.852  1.00 25.73  ?  201 VAL   B CA  1 
ATOM   5273  C C   . VAL   B 1 201 ? -2.754  15.741  20.147  1.00 26.04  ?  201 VAL   B C   1 
ATOM   5274  O O   . VAL   B 1 201 ? -2.588  16.108  21.318  1.00 30.15  ?  201 VAL   B O   1 
ATOM   5275  C CB  . VAL   B 1 201 ? -4.733  14.188  20.224  1.00 26.18  ?  201 VAL   B CB  1 
ATOM   5276  C CG1 . VAL   B 1 201 ? -5.602  15.069  19.336  1.00 27.62  ?  201 VAL   B CG1 1 
ATOM   5277  C CG2 . VAL   B 1 201 ? -5.154  12.727  20.159  1.00 25.68  ?  201 VAL   B CG2 1 
ATOM   5278  N N   . SER   B 1 202 ? -2.503  16.519  19.100  1.00 26.95  ?  202 SER   B N   1 
ATOM   5279  C CA  . SER   B 1 202 ? -1.933  17.844  19.293  1.00 27.27  ?  202 SER   B CA  1 
ATOM   5280  C C   . SER   B 1 202 ? -2.944  18.779  19.953  1.00 28.78  ?  202 SER   B C   1 
ATOM   5281  O O   . SER   B 1 202 ? -4.156  18.547  19.928  1.00 28.41  ?  202 SER   B O   1 
ATOM   5282  C CB  . SER   B 1 202 ? -1.480  18.434  17.961  1.00 28.15  ?  202 SER   B CB  1 
ATOM   5283  O OG  . SER   B 1 202 ? -2.594  18.877  17.210  1.00 29.40  ?  202 SER   B OG  1 
ATOM   5284  N N   . MET   B 1 203 ? -2.424  19.858  20.548  1.00 27.91  ?  203 MET   B N   1 
ATOM   5285  C CA  . MET   B 1 203 ? -3.302  20.861  21.146  1.00 28.59  ?  203 MET   B CA  1 
ATOM   5286  C C   . MET   B 1 203 ? -4.137  21.575  20.088  1.00 30.30  ?  203 MET   B C   1 
ATOM   5287  O O   . MET   B 1 203 ? -5.303  21.903  20.331  1.00 33.41  ?  203 MET   B O   1 
ATOM   5288  C CB  . MET   B 1 203 ? -2.489  21.878  21.949  1.00 29.03  ?  203 MET   B CB  1 
ATOM   5289  C CG  . MET   B 1 203 ? -3.345  22.840  22.759  1.00 28.90  ?  203 MET   B CG  1 
ATOM   5290  S SD  . MET   B 1 203 ? -4.050  22.023  24.198  1.00 31.80  ?  203 MET   B SD  1 
ATOM   5291  C CE  . MET   B 1 203 ? -2.584  21.797  25.190  1.00 28.83  ?  203 MET   B CE  1 
ATOM   5292  N N   . SER   B 1 204 ? -3.565  21.831  18.910  1.00 30.57  ?  204 SER   B N   1 
ATOM   5293  C CA  . SER   B 1 204 ? -4.339  22.511  17.875  1.00 31.98  ?  204 SER   B CA  1 
ATOM   5294  C C   . SER   B 1 204 ? -5.387  21.590  17.262  1.00 32.36  ?  204 SER   B C   1 
ATOM   5295  O O   . SER   B 1 204 ? -6.433  22.063  16.809  1.00 33.48  ?  204 SER   B O   1 
ATOM   5296  C CB  . SER   B 1 204 ? -3.411  23.068  16.794  1.00 32.45  ?  204 SER   B CB  1 
ATOM   5297  O OG  . SER   B 1 204 ? -2.588  22.054  16.244  1.00 37.79  ?  204 SER   B OG  1 
ATOM   5298  N N   . ASN   B 1 205 ? -5.130  20.281  17.240  1.00 31.49  ?  205 ASN   B N   1 
ATOM   5299  C CA  . ASN   B 1 205 ? -6.151  19.337  16.791  1.00 31.77  ?  205 ASN   B CA  1 
ATOM   5300  C C   . ASN   B 1 205 ? -7.289  19.235  17.805  1.00 31.72  ?  205 ASN   B C   1 
ATOM   5301  O O   . ASN   B 1 205 ? -8.465  19.197  17.421  1.00 32.59  ?  205 ASN   B O   1 
ATOM   5302  C CB  . ASN   B 1 205 ? -5.517  17.968  16.540  1.00 30.83  ?  205 ASN   B CB  1 
ATOM   5303  C CG  . ASN   B 1 205 ? -6.480  16.977  15.911  1.00 31.20  ?  205 ASN   B CG  1 
ATOM   5304  O OD1 . ASN   B 1 205 ? -7.033  16.106  16.588  1.00 30.61  ?  205 ASN   B OD1 1 
ATOM   5305  N ND2 . ASN   B 1 205 ? -6.680  17.102  14.605  1.00 34.66  ?  205 ASN   B ND2 1 
ATOM   5306  N N   . LEU   B 1 206 ? -6.961  19.201  19.103  1.00 30.75  ?  206 LEU   B N   1 
ATOM   5307  C CA  . LEU   B 1 206 ? -7.995  19.249  20.135  1.00 30.73  ?  206 LEU   B CA  1 
ATOM   5308  C C   . LEU   B 1 206 ? -8.802  20.538  20.048  1.00 31.98  ?  206 LEU   B C   1 
ATOM   5309  O O   . LEU   B 1 206 ? -10.030 20.522  20.192  1.00 32.58  ?  206 LEU   B O   1 
ATOM   5310  C CB  . LEU   B 1 206 ? -7.369  19.125  21.524  1.00 29.50  ?  206 LEU   B CB  1 
ATOM   5311  C CG  . LEU   B 1 206 ? -6.826  17.778  21.989  1.00 28.17  ?  206 LEU   B CG  1 
ATOM   5312  C CD1 . LEU   B 1 206 ? -6.182  17.936  23.359  1.00 27.14  ?  206 LEU   B CD1 1 
ATOM   5313  C CD2 . LEU   B 1 206 ? -7.915  16.708  22.023  1.00 28.14  ?  206 LEU   B CD2 1 
ATOM   5314  N N   . LYS   B 1 207 ? -8.124  21.664  19.825  1.00 32.40  ?  207 LYS   B N   1 
ATOM   5315  C CA  . LYS   B 1 207 ? -8.800  22.956  19.798  1.00 33.57  ?  207 LYS   B CA  1 
ATOM   5316  C C   . LYS   B 1 207 ? -9.721  23.079  18.594  1.00 34.88  ?  207 LYS   B C   1 
ATOM   5317  O O   . LYS   B 1 207 ? -10.838 23.590  18.714  1.00 35.77  ?  207 LYS   B O   1 
ATOM   5318  C CB  . LYS   B 1 207 ? -7.765  24.082  19.799  1.00 33.68  ?  207 LYS   B CB  1 
ATOM   5319  C CG  . LYS   B 1 207 ? -8.343  25.483  19.637  1.00 34.97  ?  207 LYS   B CG  1 
ATOM   5320  C CD  . LYS   B 1 207 ? -7.268  26.534  19.869  1.00 41.17  ?  207 LYS   B CD  1 
ATOM   5321  C CE  . LYS   B 1 207 ? -7.828  27.946  19.826  1.00 38.63  ?  207 LYS   B CE  1 
ATOM   5322  N NZ  . LYS   B 1 207 ? -8.462  28.254  18.519  1.00 47.22  ?  207 LYS   B NZ  1 
ATOM   5323  N N   . GLU   B 1 208 ? -9.274  22.618  17.423  1.00 35.04  ?  208 GLU   B N   1 
ATOM   5324  C CA  . GLU   B 1 208 ? -10.106 22.733  16.229  1.00 36.31  ?  208 GLU   B CA  1 
ATOM   5325  C C   . GLU   B 1 208 ? -11.335 21.835  16.316  1.00 36.45  ?  208 GLU   B C   1 
ATOM   5326  O O   . GLU   B 1 208 ? -12.434 22.247  15.929  1.00 37.59  ?  208 GLU   B O   1 
ATOM   5327  C CB  . GLU   B 1 208 ? -9.293  22.410  14.978  1.00 36.42  ?  208 GLU   B CB  1 
ATOM   5328  C CG  . GLU   B 1 208 ? -10.055 22.672  13.699  1.00 37.81  ?  208 GLU   B CG  1 
ATOM   5329  C CD  . GLU   B 1 208 ? -9.170  22.677  12.476  1.00 42.20  ?  208 GLU   B CD  1 
ATOM   5330  O OE1 . GLU   B 1 208 ? -7.991  22.269  12.581  1.00 44.61  ?  208 GLU   B OE1 1 
ATOM   5331  O OE2 . GLU   B 1 208 ? -9.658  23.102  11.408  1.00 42.69  ?  208 GLU   B OE2 1 
ATOM   5332  N N   . VAL   B 1 209 ? -11.173 20.610  16.823  1.00 35.32  ?  209 VAL   B N   1 
ATOM   5333  C CA  . VAL   B 1 209 ? -12.313 19.707  16.966  1.00 35.38  ?  209 VAL   B CA  1 
ATOM   5334  C C   . VAL   B 1 209 ? -13.361 20.306  17.896  1.00 35.79  ?  209 VAL   B C   1 
ATOM   5335  O O   . VAL   B 1 209 ? -14.563 20.250  17.616  1.00 36.66  ?  209 VAL   B O   1 
ATOM   5336  C CB  . VAL   B 1 209 ? -11.845 18.326  17.463  1.00 34.01  ?  209 VAL   B CB  1 
ATOM   5337  C CG1 . VAL   B 1 209 ? -13.036 17.481  17.883  1.00 33.98  ?  209 VAL   B CG1 1 
ATOM   5338  C CG2 . VAL   B 1 209 ? -11.042 17.617  16.386  1.00 33.81  ?  209 VAL   B CG2 1 
ATOM   5339  N N   . TYR   B 1 210 ? -12.927 20.883  19.016  1.00 35.19  ?  210 TYR   B N   1 
ATOM   5340  C CA  . TYR   B 1 210 ? -13.878 21.469  19.956  1.00 35.55  ?  210 TYR   B CA  1 
ATOM   5341  C C   . TYR   B 1 210 ? -14.591 22.668  19.349  1.00 38.25  ?  210 TYR   B C   1 
ATOM   5342  O O   . TYR   B 1 210 ? -15.798 22.846  19.548  1.00 43.48  ?  210 TYR   B O   1 
ATOM   5343  C CB  . TYR   B 1 210 ? -13.164 21.873  21.240  1.00 34.60  ?  210 TYR   B CB  1 
ATOM   5344  C CG  . TYR   B 1 210 ? -14.074 22.381  22.331  1.00 34.83  ?  210 TYR   B CG  1 
ATOM   5345  C CD1 . TYR   B 1 210 ? -14.926 21.521  23.002  1.00 34.42  ?  210 TYR   B CD1 1 
ATOM   5346  C CD2 . TYR   B 1 210 ? -14.063 23.718  22.709  1.00 35.45  ?  210 TYR   B CD2 1 
ATOM   5347  C CE1 . TYR   B 1 210 ? -15.751 21.976  24.004  1.00 35.35  ?  210 TYR   B CE1 1 
ATOM   5348  C CE2 . TYR   B 1 210 ? -14.884 24.181  23.716  1.00 35.67  ?  210 TYR   B CE2 1 
ATOM   5349  C CZ  . TYR   B 1 210 ? -15.726 23.306  24.359  1.00 35.26  ?  210 TYR   B CZ  1 
ATOM   5350  O OH  . TYR   B 1 210 ? -16.546 23.751  25.370  1.00 37.36  ?  210 TYR   B OH  1 
ATOM   5351  N N   . GLU   B 1 211 ? -13.861 23.506  18.612  1.00 38.83  ?  211 GLU   B N   1 
ATOM   5352  C CA  . GLU   B 1 211 ? -14.482 24.658  17.969  1.00 39.09  ?  211 GLU   B CA  1 
ATOM   5353  C C   . GLU   B 1 211 ? -15.485 24.223  16.913  1.00 40.08  ?  211 GLU   B C   1 
ATOM   5354  O O   . GLU   B 1 211 ? -16.565 24.812  16.793  1.00 41.22  ?  211 GLU   B O   1 
ATOM   5355  C CB  . GLU   B 1 211 ? -13.406 25.553  17.360  1.00 39.35  ?  211 GLU   B CB  1 
ATOM   5356  C CG  . GLU   B 1 211 ? -12.677 26.368  18.400  1.00 38.81  ?  211 GLU   B CG  1 
ATOM   5357  C CD  . GLU   B 1 211 ? -11.365 26.924  17.901  1.00 42.13  ?  211 GLU   B CD  1 
ATOM   5358  O OE1 . GLU   B 1 211 ? -11.043 26.743  16.707  1.00 39.27  ?  211 GLU   B OE1 1 
ATOM   5359  O OE2 . GLU   B 1 211 ? -10.650 27.541  18.716  1.00 46.00  ?  211 GLU   B OE2 1 
ATOM   5360  N N   . ILE   B 1 212 ? -15.144 23.193  16.140  1.00 39.71  ?  212 ILE   B N   1 
ATOM   5361  C CA  . ILE   B 1 212 ? -16.084 22.656  15.166  1.00 40.59  ?  212 ILE   B CA  1 
ATOM   5362  C C   . ILE   B 1 212 ? -17.330 22.144  15.870  1.00 40.74  ?  212 ILE   B C   1 
ATOM   5363  O O   . ILE   B 1 212 ? -18.460 22.464  15.484  1.00 42.98  ?  212 ILE   B O   1 
ATOM   5364  C CB  . ILE   B 1 212 ? -15.407 21.561  14.324  1.00 40.03  ?  212 ILE   B CB  1 
ATOM   5365  C CG1 . ILE   B 1 212 ? -14.384 22.200  13.378  1.00 40.37  ?  212 ILE   B CG1 1 
ATOM   5366  C CG2 . ILE   B 1 212 ? -16.433 20.763  13.551  1.00 40.71  ?  212 ILE   B CG2 1 
ATOM   5367  C CD1 . ILE   B 1 212 ? -13.516 21.211  12.619  1.00 39.74  ?  212 ILE   B CD1 1 
ATOM   5368  N N   . ALA   B 1 213 ? -17.142 21.367  16.940  1.00 39.37  ?  213 ALA   B N   1 
ATOM   5369  C CA  . ALA   B 1 213 ? -18.286 20.804  17.642  1.00 39.32  ?  213 ALA   B CA  1 
ATOM   5370  C C   . ALA   B 1 213 ? -19.080 21.885  18.359  1.00 40.68  ?  213 ALA   B C   1 
ATOM   5371  O O   . ALA   B 1 213 ? -20.309 21.804  18.444  1.00 43.94  ?  213 ALA   B O   1 
ATOM   5372  C CB  . ALA   B 1 213 ? -17.822 19.740  18.635  1.00 37.77  ?  213 ALA   B CB  1 
ATOM   5373  N N   . LYS   B 1 214 ? -18.395 22.905  18.883  1.00 45.42  ?  214 LYS   B N   1 
ATOM   5374  C CA  . LYS   B 1 214 ? -19.075 23.909  19.693  1.00 46.01  ?  214 LYS   B CA  1 
ATOM   5375  C C   . LYS   B 1 214 ? -20.057 24.722  18.858  1.00 50.34  ?  214 LYS   B C   1 
ATOM   5376  O O   . LYS   B 1 214 ? -21.198 24.952  19.275  1.00 53.45  ?  214 LYS   B O   1 
ATOM   5377  C CB  . LYS   B 1 214 ? -18.054 24.819  20.375  1.00 45.52  ?  214 LYS   B CB  1 
ATOM   5378  C CG  . LYS   B 1 214 ? -17.937 24.582  21.877  1.00 47.93  ?  214 LYS   B CG  1 
ATOM   5379  C CD  . LYS   B 1 214 ? -19.299 24.721  22.551  1.00 49.30  ?  214 LYS   B CD  1 
ATOM   5380  C CE  . LYS   B 1 214 ? -19.219 24.531  24.056  1.00 51.00  ?  214 LYS   B CE  1 
ATOM   5381  N NZ  . LYS   B 1 214 ? -20.575 24.540  24.697  1.00 55.71  ?  214 LYS   B NZ  1 
ATOM   5382  N N   . GLN   B 1 215 ? -19.640 25.155  17.669  1.00 52.44  ?  215 GLN   B N   1 
ATOM   5383  C CA  . GLN   B 1 215 ? -20.555 25.908  16.824  1.00 54.06  ?  215 GLN   B CA  1 
ATOM   5384  C C   . GLN   B 1 215 ? -21.683 25.049  16.267  1.00 54.87  ?  215 GLN   B C   1 
ATOM   5385  O O   . GLN   B 1 215 ? -22.659 25.606  15.754  1.00 56.50  ?  215 GLN   B O   1 
ATOM   5386  C CB  . GLN   B 1 215 ? -19.793 26.575  15.679  1.00 54.69  ?  215 GLN   B CB  1 
ATOM   5387  C CG  . GLN   B 1 215 ? -19.206 25.605  14.678  1.00 54.30  ?  215 GLN   B CG  1 
ATOM   5388  C CD  . GLN   B 1 215 ? -18.551 26.306  13.510  1.00 57.12  ?  215 GLN   B CD  1 
ATOM   5389  O OE1 . GLN   B 1 215 ? -18.296 25.698  12.470  1.00 63.47  ?  215 GLN   B OE1 1 
ATOM   5390  N NE2 . GLN   B 1 215 ? -18.272 27.596  13.674  1.00 57.54  ?  215 GLN   B NE2 1 
ATOM   5391  N N   . HIS   B 1 216 ? -21.591 23.721  16.366  1.00 48.54  ?  216 HIS   B N   1 
ATOM   5392  C CA  . HIS   B 1 216 ? -22.661 22.834  15.923  1.00 45.99  ?  216 HIS   B CA  1 
ATOM   5393  C C   . HIS   B 1 216 ? -23.468 22.243  17.074  1.00 44.05  ?  216 HIS   B C   1 
ATOM   5394  O O   . HIS   B 1 216 ? -24.312 21.375  16.836  1.00 44.25  ?  216 HIS   B O   1 
ATOM   5395  C CB  . HIS   B 1 216 ? -22.093 21.707  15.062  1.00 44.06  ?  216 HIS   B CB  1 
ATOM   5396  C CG  . HIS   B 1 216 ? -21.574 22.166  13.737  1.00 50.67  ?  216 HIS   B CG  1 
ATOM   5397  N ND1 . HIS   B 1 216 ? -20.297 22.657  13.568  1.00 49.86  ?  216 HIS   B ND1 1 
ATOM   5398  C CD2 . HIS   B 1 216 ? -22.162 22.217  12.518  1.00 47.66  ?  216 HIS   B CD2 1 
ATOM   5399  C CE1 . HIS   B 1 216 ? -20.118 22.985  12.300  1.00 49.84  ?  216 HIS   B CE1 1 
ATOM   5400  N NE2 . HIS   B 1 216 ? -21.236 22.730  11.642  1.00 55.25  ?  216 HIS   B NE2 1 
ATOM   5401  N N   . GLY   B 1 217 ? -23.232 22.688  18.306  1.00 43.38  ?  217 GLY   B N   1 
ATOM   5402  C CA  . GLY   B 1 217 ? -23.972 22.192  19.455  1.00 42.86  ?  217 GLY   B CA  1 
ATOM   5403  C C   . GLY   B 1 217 ? -23.681 20.753  19.830  1.00 43.32  ?  217 GLY   B C   1 
ATOM   5404  O O   . GLY   B 1 217 ? -24.598 20.022  20.226  1.00 45.08  ?  217 GLY   B O   1 
ATOM   5405  N N   . ILE   B 1 218 ? -22.426 20.324  19.725  1.00 40.47  ?  218 ILE   B N   1 
ATOM   5406  C CA  . ILE   B 1 218 ? -22.053 18.931  19.946  1.00 39.50  ?  218 ILE   B CA  1 
ATOM   5407  C C   . ILE   B 1 218 ? -21.221 18.831  21.222  1.00 37.83  ?  218 ILE   B C   1 
ATOM   5408  O O   . ILE   B 1 218 ? -20.164 19.467  21.345  1.00 41.61  ?  218 ILE   B O   1 
ATOM   5409  C CB  . ILE   B 1 218 ? -21.295 18.352  18.745  1.00 39.14  ?  218 ILE   B CB  1 
ATOM   5410  C CG1 . ILE   B 1 218 ? -22.171 18.400  17.490  1.00 40.56  ?  218 ILE   B CG1 1 
ATOM   5411  C CG2 . ILE   B 1 218 ? -20.835 16.921  19.044  1.00 37.81  ?  218 ILE   B CG2 1 
ATOM   5412  C CD1 . ILE   B 1 218 ? -21.440 17.991  16.237  1.00 40.64  ?  218 ILE   B CD1 1 
ATOM   5413  N N   . PHE   B 1 219 ? -21.694 18.014  22.157  1.00 37.08  ?  219 PHE   B N   1 
ATOM   5414  C CA  . PHE   B 1 219 ? -21.000 17.771  23.415  1.00 35.71  ?  219 PHE   B CA  1 
ATOM   5415  C C   . PHE   B 1 219 ? -19.713 16.981  23.175  1.00 34.56  ?  219 PHE   B C   1 
ATOM   5416  O O   . PHE   B 1 219 ? -19.697 16.010  22.415  1.00 34.45  ?  219 PHE   B O   1 
ATOM   5417  C CB  . PHE   B 1 219 ? -21.945 17.012  24.350  1.00 35.31  ?  219 PHE   B CB  1 
ATOM   5418  C CG  . PHE   B 1 219 ? -21.518 16.987  25.789  1.00 34.16  ?  219 PHE   B CG  1 
ATOM   5419  C CD1 . PHE   B 1 219 ? -20.728 15.959  26.272  1.00 32.76  ?  219 PHE   B CD1 1 
ATOM   5420  C CD2 . PHE   B 1 219 ? -21.948 17.966  26.668  1.00 34.52  ?  219 PHE   B CD2 1 
ATOM   5421  C CE1 . PHE   B 1 219 ? -20.350 15.923  27.603  1.00 31.72  ?  219 PHE   B CE1 1 
ATOM   5422  C CE2 . PHE   B 1 219 ? -21.573 17.936  27.999  1.00 33.49  ?  219 PHE   B CE2 1 
ATOM   5423  C CZ  . PHE   B 1 219 ? -20.777 16.915  28.465  1.00 32.09  ?  219 PHE   B CZ  1 
ATOM   5424  N N   . VAL   B 1 220 ? -18.625 17.398  23.823  1.00 33.72  ?  220 VAL   B N   1 
ATOM   5425  C CA  . VAL   B 1 220 ? -17.311 16.780  23.643  1.00 32.65  ?  220 VAL   B CA  1 
ATOM   5426  C C   . VAL   B 1 220 ? -16.875 16.142  24.956  1.00 31.23  ?  220 VAL   B C   1 
ATOM   5427  O O   . VAL   B 1 220 ? -16.791 16.824  25.986  1.00 30.98  ?  220 VAL   B O   1 
ATOM   5428  C CB  . VAL   B 1 220 ? -16.258 17.795  23.168  1.00 32.88  ?  220 VAL   B CB  1 
ATOM   5429  C CG1 . VAL   B 1 220 ? -14.928 17.094  22.914  1.00 31.82  ?  220 VAL   B CG1 1 
ATOM   5430  C CG2 . VAL   B 1 220 ? -16.739 18.542  21.928  1.00 34.36  ?  220 VAL   B CG2 1 
ATOM   5431  N N   . VAL   B 1 221 ? -16.564 14.844  24.906  1.00 31.98  ?  221 VAL   B N   1 
ATOM   5432  C CA  . VAL   B 1 221 ? -16.063 14.072  26.044  1.00 28.92  ?  221 VAL   B CA  1 
ATOM   5433  C C   . VAL   B 1 221 ? -14.607 13.711  25.778  1.00 28.02  ?  221 VAL   B C   1 
ATOM   5434  O O   . VAL   B 1 221 ? -14.292 13.083  24.760  1.00 28.09  ?  221 VAL   B O   1 
ATOM   5435  C CB  . VAL   B 1 221 ? -16.897 12.803  26.279  1.00 28.57  ?  221 VAL   B CB  1 
ATOM   5436  C CG1 . VAL   B 1 221 ? -16.250 11.939  27.344  1.00 27.08  ?  221 VAL   B CG1 1 
ATOM   5437  C CG2 . VAL   B 1 221 ? -18.306 13.161  26.691  1.00 29.38  ?  221 VAL   B CG2 1 
ATOM   5438  N N   . MET   B 1 222 ? -13.720 14.100  26.689  1.00 27.19  ?  222 MET   B N   1 
ATOM   5439  C CA  . MET   B 1 222 ? -12.305 13.742  26.609  1.00 26.24  ?  222 MET   B CA  1 
ATOM   5440  C C   . MET   B 1 222 ? -12.088 12.409  27.319  1.00 24.98  ?  222 MET   B C   1 
ATOM   5441  O O   . MET   B 1 222 ? -12.134 12.346  28.551  1.00 27.96  ?  222 MET   B O   1 
ATOM   5442  C CB  . MET   B 1 222 ? -11.443 14.833  27.243  1.00 26.01  ?  222 MET   B CB  1 
ATOM   5443  C CG  . MET   B 1 222 ? -9.939  14.677  27.008  1.00 25.53  ?  222 MET   B CG  1 
ATOM   5444  S SD  . MET   B 1 222 ? -9.303  15.774  25.711  1.00 28.90  ?  222 MET   B SD  1 
ATOM   5445  C CE  . MET   B 1 222 ? -9.882  17.363  26.287  1.00 27.38  ?  222 MET   B CE  1 
ATOM   5446  N N   . ASP   B 1 223 ? -11.848 11.343  26.553  1.00 24.92  ?  223 ASP   B N   1 
ATOM   5447  C CA  . ASP   B 1 223 ? -11.466 10.061  27.150  1.00 25.49  ?  223 ASP   B CA  1 
ATOM   5448  C C   . ASP   B 1 223 ? -10.047 10.175  27.693  1.00 22.97  ?  223 ASP   B C   1 
ATOM   5449  O O   . ASP   B 1 223 ? -9.078  10.131  26.931  1.00 23.69  ?  223 ASP   B O   1 
ATOM   5450  C CB  . ASP   B 1 223 ? -11.573 8.941   26.120  1.00 25.01  ?  223 ASP   B CB  1 
ATOM   5451  C CG  . ASP   B 1 223 ? -11.270 7.561   26.709  1.00 26.16  ?  223 ASP   B CG  1 
ATOM   5452  O OD1 . ASP   B 1 223 ? -10.333 7.412   27.531  1.00 25.43  ?  223 ASP   B OD1 1 
ATOM   5453  O OD2 . ASP   B 1 223 ? -11.982 6.613   26.334  1.00 24.23  ?  223 ASP   B OD2 1 
ATOM   5454  N N   . SER   B 1 224 ? -9.913  10.263  29.015  1.00 21.69  ?  224 SER   B N   1 
ATOM   5455  C CA  . SER   B 1 224 ? -8.733  10.842  29.641  1.00 22.59  ?  224 SER   B CA  1 
ATOM   5456  C C   . SER   B 1 224 ? -7.835  9.820   30.330  1.00 20.71  ?  224 SER   B C   1 
ATOM   5457  O O   . SER   B 1 224 ? -7.089  10.179  31.242  1.00 24.69  ?  224 SER   B O   1 
ATOM   5458  C CB  . SER   B 1 224 ? -9.163  11.914  30.638  1.00 25.48  ?  224 SER   B CB  1 
ATOM   5459  O OG  . SER   B 1 224 ? -9.734  13.016  29.953  1.00 28.89  ?  224 SER   B OG  1 
ATOM   5460  N N   . ALA   B 1 225 ? -7.868  8.556   29.893  1.00 22.44  ?  225 ALA   B N   1 
ATOM   5461  C CA  . ALA   B 1 225 ? -7.083  7.521   30.567  1.00 20.70  ?  225 ALA   B CA  1 
ATOM   5462  C C   . ALA   B 1 225 ? -5.599  7.863   30.588  1.00 20.56  ?  225 ALA   B C   1 
ATOM   5463  O O   . ALA   B 1 225 ? -4.915  7.643   31.598  1.00 21.44  ?  225 ALA   B O   1 
ATOM   5464  C CB  . ALA   B 1 225 ? -7.299  6.167   29.891  1.00 23.24  ?  225 ALA   B CB  1 
ATOM   5465  N N   . ARG   B 1 226 ? -5.076  8.396   29.487  1.00 19.87  ?  226 ARG   B N   1 
ATOM   5466  C CA  . ARG   B 1 226 ? -3.648  8.682   29.433  1.00 19.87  ?  226 ARG   B CA  1 
ATOM   5467  C C   . ARG   B 1 226 ? -3.405  10.149  29.101  1.00 18.36  ?  226 ARG   B C   1 
ATOM   5468  O O   . ARG   B 1 226 ? -2.578  10.478  28.245  1.00 19.63  ?  226 ARG   B O   1 
ATOM   5469  C CB  . ARG   B 1 226 ? -2.963  7.735   28.443  1.00 19.05  ?  226 ARG   B CB  1 
ATOM   5470  C CG  . ARG   B 1 226 ? -3.142  6.264   28.858  1.00 21.23  ?  226 ARG   B CG  1 
ATOM   5471  C CD  . ARG   B 1 226 ? -2.517  5.261   27.887  1.00 23.30  ?  226 ARG   B CD  1 
ATOM   5472  N NE  . ARG   B 1 226 ? -2.794  3.874   28.263  1.00 19.04  ?  226 ARG   B NE  1 
ATOM   5473  C CZ  . ARG   B 1 226 ? -3.909  3.220   27.955  1.00 22.61  ?  226 ARG   B CZ  1 
ATOM   5474  N NH1 . ARG   B 1 226 ? -4.890  3.804   27.282  1.00 22.12  ?  226 ARG   B NH1 1 
ATOM   5475  N NH2 . ARG   B 1 226 ? -4.051  1.952   28.343  1.00 17.31  ?  226 ARG   B NH2 1 
ATOM   5476  N N   . PHE   B 1 227 ? -4.097  11.043  29.812  1.00 18.76  ?  227 PHE   B N   1 
ATOM   5477  C CA  . PHE   B 1 227 ? -4.024  12.465  29.485  1.00 21.93  ?  227 PHE   B CA  1 
ATOM   5478  C C   . PHE   B 1 227 ? -2.682  13.078  29.863  1.00 21.96  ?  227 PHE   B C   1 
ATOM   5479  O O   . PHE   B 1 227 ? -2.238  14.030  29.212  1.00 21.54  ?  227 PHE   B O   1 
ATOM   5480  C CB  . PHE   B 1 227 ? -5.155  13.227  30.171  1.00 20.49  ?  227 PHE   B CB  1 
ATOM   5481  C CG  . PHE   B 1 227 ? -4.976  13.375  31.654  1.00 20.38  ?  227 PHE   B CG  1 
ATOM   5482  C CD1 . PHE   B 1 227 ? -5.232  12.308  32.509  1.00 24.09  ?  227 PHE   B CD1 1 
ATOM   5483  C CD2 . PHE   B 1 227 ? -4.564  14.582  32.200  1.00 19.66  ?  227 PHE   B CD2 1 
ATOM   5484  C CE1 . PHE   B 1 227 ? -5.071  12.440  33.889  1.00 27.13  ?  227 PHE   B CE1 1 
ATOM   5485  C CE2 . PHE   B 1 227 ? -4.401  14.723  33.571  1.00 21.78  ?  227 PHE   B CE2 1 
ATOM   5486  C CZ  . PHE   B 1 227 ? -4.658  13.650  34.422  1.00 25.67  ?  227 PHE   B CZ  1 
ATOM   5487  N N   . CYS   B 1 228 ? -2.032  12.571  30.914  1.00 19.82  ?  228 CYS   B N   1 
ATOM   5488  C CA  . CYS   B 1 228 ? -0.726  13.101  31.285  1.00 20.08  ?  228 CYS   B CA  1 
ATOM   5489  C C   . CYS   B 1 228 ? 0.326   12.739  30.248  1.00 20.63  ?  228 CYS   B C   1 
ATOM   5490  O O   . CYS   B 1 228 ? 1.210   13.551  29.947  1.00 18.28  ?  228 CYS   B O   1 
ATOM   5491  C CB  . CYS   B 1 228 ? -0.310  12.584  32.660  1.00 20.36  ?  228 CYS   B CB  1 
ATOM   5492  S SG  . CYS   B 1 228 ? -1.319  13.187  34.020  1.00 25.56  ?  228 CYS   B SG  1 
ATOM   5493  N N   . GLU   B 1 229 ? 0.259   11.524  29.699  1.00 18.43  ?  229 GLU   B N   1 
ATOM   5494  C CA  . GLU   B 1 229 ? 1.199   11.167  28.643  1.00 19.29  ?  229 GLU   B CA  1 
ATOM   5495  C C   . GLU   B 1 229 ? 0.948   11.991  27.385  1.00 22.59  ?  229 GLU   B C   1 
ATOM   5496  O O   . GLU   B 1 229 ? 1.900   12.405  26.709  1.00 21.42  ?  229 GLU   B O   1 
ATOM   5497  C CB  . GLU   B 1 229 ? 1.127   9.672   28.354  1.00 20.37  ?  229 GLU   B CB  1 
ATOM   5498  C CG  . GLU   B 1 229 ? 1.757   8.858   29.468  1.00 22.10  ?  229 GLU   B CG  1 
ATOM   5499  C CD  . GLU   B 1 229 ? 1.301   7.415   29.502  1.00 20.16  ?  229 GLU   B CD  1 
ATOM   5500  O OE1 . GLU   B 1 229 ? 0.688   6.961   28.515  1.00 23.36  ?  229 GLU   B OE1 1 
ATOM   5501  O OE2 . GLU   B 1 229 ? 1.565   6.735   30.525  1.00 20.69  ?  229 GLU   B OE2 1 
ATOM   5502  N N   . ASN   B 1 230 ? -0.320  12.259  27.062  1.00 19.62  ?  230 ASN   B N   1 
ATOM   5503  C CA  . ASN   B 1 230 ? -0.606  13.190  25.976  1.00 20.36  ?  230 ASN   B CA  1 
ATOM   5504  C C   . ASN   B 1 230 ? 0.006   14.550  26.264  1.00 20.70  ?  230 ASN   B C   1 
ATOM   5505  O O   . ASN   B 1 230 ? 0.662   15.139  25.400  1.00 22.31  ?  230 ASN   B O   1 
ATOM   5506  C CB  . ASN   B 1 230 ? -2.111  13.326  25.752  1.00 21.25  ?  230 ASN   B CB  1 
ATOM   5507  C CG  . ASN   B 1 230 ? -2.446  13.816  24.343  1.00 25.35  ?  230 ASN   B CG  1 
ATOM   5508  O OD1 . ASN   B 1 230 ? -2.447  13.030  23.393  1.00 24.29  ?  230 ASN   B OD1 1 
ATOM   5509  N ND2 . ASN   B 1 230 ? -2.718  15.114  24.202  1.00 23.36  ?  230 ASN   B ND2 1 
ATOM   5510  N N   . ALA   B 1 231 ? -0.183  15.052  27.488  1.00 21.59  ?  231 ALA   B N   1 
ATOM   5511  C CA  . ALA   B 1 231 ? 0.314   16.379  27.839  1.00 24.43  ?  231 ALA   B CA  1 
ATOM   5512  C C   . ALA   B 1 231 ? 1.823   16.471  27.674  1.00 25.53  ?  231 ALA   B C   1 
ATOM   5513  O O   . ALA   B 1 231 ? 2.342   17.500  27.217  1.00 24.82  ?  231 ALA   B O   1 
ATOM   5514  C CB  . ALA   B 1 231 ? -0.082  16.731  29.272  1.00 20.30  ?  231 ALA   B CB  1 
ATOM   5515  N N   . TYR   B 1 232 ? 2.547   15.412  28.048  1.00 20.00  ?  232 TYR   B N   1 
ATOM   5516  C CA  . TYR   B 1 232 ? 4.000   15.426  27.902  1.00 18.52  ?  232 TYR   B CA  1 
ATOM   5517  C C   . TYR   B 1 232 ? 4.401   15.563  26.440  1.00 21.86  ?  232 TYR   B C   1 
ATOM   5518  O O   . TYR   B 1 232 ? 5.332   16.310  26.108  1.00 23.89  ?  232 TYR   B O   1 
ATOM   5519  C CB  . TYR   B 1 232 ? 4.597   14.155  28.506  1.00 21.38  ?  232 TYR   B CB  1 
ATOM   5520  C CG  . TYR   B 1 232 ? 6.092   14.017  28.299  1.00 21.49  ?  232 TYR   B CG  1 
ATOM   5521  C CD1 . TYR   B 1 232 ? 6.607   13.505  27.111  1.00 25.43  ?  232 TYR   B CD1 1 
ATOM   5522  C CD2 . TYR   B 1 232 ? 6.984   14.393  29.283  1.00 18.48  ?  232 TYR   B CD2 1 
ATOM   5523  C CE1 . TYR   B 1 232 ? 7.962   13.388  26.911  1.00 24.13  ?  232 TYR   B CE1 1 
ATOM   5524  C CE2 . TYR   B 1 232 ? 8.354   14.264  29.091  1.00 20.14  ?  232 TYR   B CE2 1 
ATOM   5525  C CZ  . TYR   B 1 232 ? 8.828   13.759  27.903  1.00 21.72  ?  232 TYR   B CZ  1 
ATOM   5526  O OH  . TYR   B 1 232 ? 10.178  13.631  27.680  1.00 23.89  ?  232 TYR   B OH  1 
ATOM   5527  N N   . PHE   B 1 233 ? 3.713   14.840  25.550  1.00 22.75  ?  233 PHE   B N   1 
ATOM   5528  C CA  . PHE   B 1 233 ? 4.044   14.894  24.131  1.00 24.43  ?  233 PHE   B CA  1 
ATOM   5529  C C   . PHE   B 1 233 ? 3.767   16.271  23.550  1.00 23.33  ?  233 PHE   B C   1 
ATOM   5530  O O   . PHE   B 1 233 ? 4.513   16.742  22.688  1.00 23.80  ?  233 PHE   B O   1 
ATOM   5531  C CB  . PHE   B 1 233 ? 3.263   13.829  23.359  1.00 20.43  ?  233 PHE   B CB  1 
ATOM   5532  C CG  . PHE   B 1 233 ? 3.812   12.438  23.512  1.00 19.41  ?  233 PHE   B CG  1 
ATOM   5533  C CD1 . PHE   B 1 233 ? 5.128   12.161  23.189  1.00 21.04  ?  233 PHE   B CD1 1 
ATOM   5534  C CD2 . PHE   B 1 233 ? 3.004   11.403  23.952  1.00 20.00  ?  233 PHE   B CD2 1 
ATOM   5535  C CE1 . PHE   B 1 233 ? 5.639   10.879  23.326  1.00 22.96  ?  233 PHE   B CE1 1 
ATOM   5536  C CE2 . PHE   B 1 233 ? 3.500   10.121  24.084  1.00 18.36  ?  233 PHE   B CE2 1 
ATOM   5537  C CZ  . PHE   B 1 233 ? 4.825   9.859   23.776  1.00 19.02  ?  233 PHE   B CZ  1 
ATOM   5538  N N   . ILE   B 1 234 ? 2.690   16.924  23.992  1.00 22.27  ?  234 ILE   B N   1 
ATOM   5539  C CA  . ILE   B 1 234 ? 2.416   18.288  23.544  1.00 25.91  ?  234 ILE   B CA  1 
ATOM   5540  C C   . ILE   B 1 234 ? 3.553   19.221  23.956  1.00 27.47  ?  234 ILE   B C   1 
ATOM   5541  O O   . ILE   B 1 234 ? 4.059   20.006  23.147  1.00 24.36  ?  234 ILE   B O   1 
ATOM   5542  C CB  . ILE   B 1 234 ? 1.060   18.772  24.085  1.00 27.37  ?  234 ILE   B CB  1 
ATOM   5543  C CG1 . ILE   B 1 234 ? -0.088  18.064  23.356  1.00 24.59  ?  234 ILE   B CG1 1 
ATOM   5544  C CG2 . ILE   B 1 234 ? 0.939   20.281  23.925  1.00 26.69  ?  234 ILE   B CG2 1 
ATOM   5545  C CD1 . ILE   B 1 234 ? -1.460  18.400  23.915  1.00 24.73  ?  234 ILE   B CD1 1 
ATOM   5546  N N   . LYS   B 1 235 ? 3.986   19.142  25.218  1.00 25.77  ?  235 LYS   B N   1 
ATOM   5547  C CA  . LYS   B 1 235 ? 5.152   19.922  25.618  1.00 29.32  ?  235 LYS   B CA  1 
ATOM   5548  C C   . LYS   B 1 235 ? 6.399   19.499  24.845  1.00 28.78  ?  235 LYS   B C   1 
ATOM   5549  O O   . LYS   B 1 235 ? 7.236   20.345  24.503  1.00 29.22  ?  235 LYS   B O   1 
ATOM   5550  C CB  . LYS   B 1 235 ? 5.387   19.808  27.127  1.00 23.18  ?  235 LYS   B CB  1 
ATOM   5551  C CG  . LYS   B 1 235 ? 6.588   20.600  27.608  1.00 23.84  ?  235 LYS   B CG  1 
ATOM   5552  C CD  . LYS   B 1 235 ? 6.674   20.660  29.113  1.00 24.77  ?  235 LYS   B CD  1 
ATOM   5553  C CE  . LYS   B 1 235 ? 7.994   21.283  29.530  1.00 24.90  ?  235 LYS   B CE  1 
ATOM   5554  N NZ  . LYS   B 1 235 ? 8.017   21.600  30.981  1.00 30.85  ?  235 LYS   B NZ  1 
ATOM   5555  N N   . ALA   B 1 236 ? 6.521   18.211  24.517  1.00 27.52  ?  236 ALA   B N   1 
ATOM   5556  C CA  . ALA   B 1 236 ? 7.726   17.732  23.848  1.00 27.25  ?  236 ALA   B CA  1 
ATOM   5557  C C   . ALA   B 1 236 ? 7.783   18.098  22.366  1.00 26.35  ?  236 ALA   B C   1 
ATOM   5558  O O   . ALA   B 1 236 ? 8.883   18.247  21.822  1.00 26.80  ?  236 ALA   B O   1 
ATOM   5559  C CB  . ALA   B 1 236 ? 7.842   16.217  24.012  1.00 25.03  ?  236 ALA   B CB  1 
ATOM   5560  N N   . ARG   B 1 237 ? 6.635   18.241  21.690  1.00 23.38  ?  237 ARG   B N   1 
ATOM   5561  C CA  . ARG   B 1 237 ? 6.613   18.398  20.239  1.00 24.53  ?  237 ARG   B CA  1 
ATOM   5562  C C   . ARG   B 1 237 ? 5.937   19.667  19.732  1.00 26.19  ?  237 ARG   B C   1 
ATOM   5563  O O   . ARG   B 1 237 ? 6.211   20.074  18.597  1.00 32.78  ?  237 ARG   B O   1 
ATOM   5564  C CB  . ARG   B 1 237 ? 5.921   17.195  19.581  1.00 29.68  ?  237 ARG   B CB  1 
ATOM   5565  C CG  . ARG   B 1 237 ? 6.525   15.858  19.963  1.00 28.47  ?  237 ARG   B CG  1 
ATOM   5566  C CD  . ARG   B 1 237 ? 5.804   14.692  19.296  1.00 26.44  ?  237 ARG   B CD  1 
ATOM   5567  N NE  . ARG   B 1 237 ? 6.353   13.425  19.762  1.00 23.11  ?  237 ARG   B NE  1 
ATOM   5568  C CZ  . ARG   B 1 237 ? 5.780   12.247  19.578  1.00 20.74  ?  237 ARG   B CZ  1 
ATOM   5569  N NH1 . ARG   B 1 237 ? 4.619   12.135  18.959  1.00 23.03  ?  237 ARG   B NH1 1 
ATOM   5570  N NH2 . ARG   B 1 237 ? 6.385   11.154  20.031  1.00 21.87  ?  237 ARG   B NH2 1 
ATOM   5571  N N   . ASP   B 1 238 ? 5.058   20.289  20.510  1.00 27.56  ?  238 ASP   B N   1 
ATOM   5572  C CA  . ASP   B 1 238 ? 4.434   21.539  20.094  1.00 30.94  ?  238 ASP   B CA  1 
ATOM   5573  C C   . ASP   B 1 238 ? 5.266   22.689  20.639  1.00 33.37  ?  238 ASP   B C   1 
ATOM   5574  O O   . ASP   B 1 238 ? 5.263   22.916  21.861  1.00 31.36  ?  238 ASP   B O   1 
ATOM   5575  C CB  . ASP   B 1 238 ? 3.001   21.629  20.600  1.00 27.23  ?  238 ASP   B CB  1 
ATOM   5576  C CG  . ASP   B 1 238 ? 2.282   22.891  20.130  1.00 33.63  ?  238 ASP   B CG  1 
ATOM   5577  O OD1 . ASP   B 1 238 ? 2.944   23.812  19.602  1.00 35.63  ?  238 ASP   B OD1 1 
ATOM   5578  O OD2 . ASP   B 1 238 ? 1.041   22.961  20.287  1.00 29.13  ?  238 ASP   B OD2 1 
ATOM   5579  N N   . PRO   B 1 239 ? 5.968   23.446  19.791  1.00 30.16  ?  239 PRO   B N   1 
ATOM   5580  C CA  . PRO   B 1 239 ? 6.831   24.524  20.300  1.00 32.82  ?  239 PRO   B CA  1 
ATOM   5581  C C   . PRO   B 1 239 ? 6.098   25.554  21.139  1.00 32.71  ?  239 PRO   B C   1 
ATOM   5582  O O   . PRO   B 1 239 ? 6.739   26.237  21.948  1.00 35.41  ?  239 PRO   B O   1 
ATOM   5583  C CB  . PRO   B 1 239 ? 7.407   25.148  19.019  1.00 29.11  ?  239 PRO   B CB  1 
ATOM   5584  C CG  . PRO   B 1 239 ? 6.476   24.742  17.936  1.00 30.12  ?  239 PRO   B CG  1 
ATOM   5585  C CD  . PRO   B 1 239 ? 5.972   23.382  18.323  1.00 34.00  ?  239 PRO   B CD  1 
ATOM   5586  N N   . LYS   B 1 240 ? 4.777   25.675  20.984  1.00 35.59  ?  240 LYS   B N   1 
ATOM   5587  C CA  . LYS   B 1 240 ? 4.013   26.622  21.789  1.00 28.81  ?  240 LYS   B CA  1 
ATOM   5588  C C   . LYS   B 1 240 ? 4.179   26.353  23.281  1.00 30.84  ?  240 LYS   B C   1 
ATOM   5589  O O   . LYS   B 1 240 ? 4.255   27.289  24.082  1.00 31.81  ?  240 LYS   B O   1 
ATOM   5590  C CB  . LYS   B 1 240 ? 2.537   26.565  21.392  1.00 32.60  ?  240 LYS   B CB  1 
ATOM   5591  C CG  . LYS   B 1 240 ? 1.668   27.651  22.023  1.00 36.80  ?  240 LYS   B CG  1 
ATOM   5592  C CD  . LYS   B 1 240 ? 0.214   27.513  21.595  1.00 36.26  ?  240 LYS   B CD  1 
ATOM   5593  C CE  . LYS   B 1 240 ? -0.602  28.764  21.930  1.00 39.98  ?  240 LYS   B CE  1 
ATOM   5594  N NZ  . LYS   B 1 240 ? -0.688  29.021  23.397  1.00 46.85  ?  240 LYS   B NZ  1 
ATOM   5595  N N   . TYR   B 1 241 ? 4.242   25.082  23.678  1.00 31.94  ?  241 TYR   B N   1 
ATOM   5596  C CA  . TYR   B 1 241 ? 4.273   24.724  25.091  1.00 33.37  ?  241 TYR   B CA  1 
ATOM   5597  C C   . TYR   B 1 241 ? 5.650   24.260  25.543  1.00 35.04  ?  241 TYR   B C   1 
ATOM   5598  O O   . TYR   B 1 241 ? 5.765   23.569  26.560  1.00 30.16  ?  241 TYR   B O   1 
ATOM   5599  C CB  . TYR   B 1 241 ? 3.224   23.652  25.390  1.00 30.10  ?  241 TYR   B CB  1 
ATOM   5600  C CG  . TYR   B 1 241 ? 1.812   24.133  25.175  1.00 28.79  ?  241 TYR   B CG  1 
ATOM   5601  C CD1 . TYR   B 1 241 ? 1.226   24.085  23.918  1.00 29.17  ?  241 TYR   B CD1 1 
ATOM   5602  C CD2 . TYR   B 1 241 ? 1.071   24.653  26.224  1.00 30.52  ?  241 TYR   B CD2 1 
ATOM   5603  C CE1 . TYR   B 1 241 ? -0.059  24.532  23.715  1.00 29.15  ?  241 TYR   B CE1 1 
ATOM   5604  C CE2 . TYR   B 1 241 ? -0.215  25.102  26.031  1.00 27.02  ?  241 TYR   B CE2 1 
ATOM   5605  C CZ  . TYR   B 1 241 ? -0.777  25.037  24.774  1.00 32.54  ?  241 TYR   B CZ  1 
ATOM   5606  O OH  . TYR   B 1 241 ? -2.067  25.486  24.575  1.00 34.78  ?  241 TYR   B OH  1 
ATOM   5607  N N   . LYS   B 1 242 ? 6.699   24.632  24.806  1.00 36.52  ?  242 LYS   B N   1 
ATOM   5608  C CA  . LYS   B 1 242 ? 8.044   24.227  25.192  1.00 32.33  ?  242 LYS   B CA  1 
ATOM   5609  C C   . LYS   B 1 242 ? 8.413   24.770  26.564  1.00 29.52  ?  242 LYS   B C   1 
ATOM   5610  O O   . LYS   B 1 242 ? 9.167   24.131  27.302  1.00 31.19  ?  242 LYS   B O   1 
ATOM   5611  C CB  . LYS   B 1 242 ? 9.044   24.690  24.133  1.00 38.40  ?  242 LYS   B CB  1 
ATOM   5612  C CG  . LYS   B 1 242 ? 10.435  24.099  24.287  1.00 47.35  ?  242 LYS   B CG  1 
ATOM   5613  C CD  . LYS   B 1 242 ? 11.287  24.383  23.060  1.00 52.37  ?  242 LYS   B CD  1 
ATOM   5614  C CE  . LYS   B 1 242 ? 11.335  25.867  22.772  1.00 49.29  ?  242 LYS   B CE  1 
ATOM   5615  N NZ  . LYS   B 1 242 ? 11.865  26.596  23.958  1.00 51.80  ?  242 LYS   B NZ  1 
ATOM   5616  N N   . ASN   B 1 243 ? 7.866   25.922  26.938  1.00 35.66  ?  243 ASN   B N   1 
ATOM   5617  C CA  . ASN   B 1 243 ? 8.176   26.577  28.202  1.00 36.88  ?  243 ASN   B CA  1 
ATOM   5618  C C   . ASN   B 1 243 ? 7.063   26.432  29.233  1.00 35.42  ?  243 ASN   B C   1 
ATOM   5619  O O   . ASN   B 1 243 ? 7.119   27.075  30.288  1.00 35.43  ?  243 ASN   B O   1 
ATOM   5620  C CB  . ASN   B 1 243 ? 8.473   28.061  27.957  1.00 39.49  ?  243 ASN   B CB  1 
ATOM   5621  C CG  . ASN   B 1 243 ? 9.782   28.277  27.221  1.00 36.36  ?  243 ASN   B CG  1 
ATOM   5622  O OD1 . ASN   B 1 243 ? 10.770  27.594  27.487  1.00 38.74  ?  243 ASN   B OD1 1 
ATOM   5623  N ND2 . ASN   B 1 243 ? 9.795   29.220  26.287  1.00 36.75  ?  243 ASN   B ND2 1 
ATOM   5624  N N   . ALA   B 1 244 ? 6.057   25.613  28.957  1.00 31.23  ?  244 ALA   B N   1 
ATOM   5625  C CA  . ALA   B 1 244 ? 4.937   25.448  29.867  1.00 28.18  ?  244 ALA   B CA  1 
ATOM   5626  C C   . ALA   B 1 244 ? 5.179   24.274  30.798  1.00 30.52  ?  244 ALA   B C   1 
ATOM   5627  O O   . ALA   B 1 244 ? 5.912   23.339  30.468  1.00 35.90  ?  244 ALA   B O   1 
ATOM   5628  C CB  . ALA   B 1 244 ? 3.644   25.221  29.088  1.00 30.07  ?  244 ALA   B CB  1 
ATOM   5629  N N   . THR   B 1 245 ? 4.551   24.320  31.966  1.00 29.49  ?  245 THR   B N   1 
ATOM   5630  C CA  . THR   B 1 245 ? 4.553   23.138  32.812  1.00 29.30  ?  245 THR   B CA  1 
ATOM   5631  C C   . THR   B 1 245 ? 3.501   22.150  32.317  1.00 26.92  ?  245 THR   B C   1 
ATOM   5632  O O   . THR   B 1 245 ? 2.605   22.493  31.543  1.00 25.36  ?  245 THR   B O   1 
ATOM   5633  C CB  . THR   B 1 245 ? 4.296   23.502  34.274  1.00 27.95  ?  245 THR   B CB  1 
ATOM   5634  O OG1 . THR   B 1 245 ? 2.964   24.006  34.425  1.00 23.68  ?  245 THR   B OG1 1 
ATOM   5635  C CG2 . THR   B 1 245 ? 5.281   24.565  34.737  1.00 30.01  ?  245 THR   B CG2 1 
ATOM   5636  N N   . ILE   B 1 246 ? 3.632   20.901  32.766  1.00 28.21  ?  246 ILE   B N   1 
ATOM   5637  C CA  . ILE   B 1 246 ? 2.696   19.858  32.351  1.00 26.81  ?  246 ILE   B CA  1 
ATOM   5638  C C   . ILE   B 1 246 ? 1.277   20.201  32.793  1.00 24.71  ?  246 ILE   B C   1 
ATOM   5639  O O   . ILE   B 1 246 ? 0.312   19.986  32.051  1.00 29.35  ?  246 ILE   B O   1 
ATOM   5640  C CB  . ILE   B 1 246 ? 3.151   18.490  32.897  1.00 24.56  ?  246 ILE   B CB  1 
ATOM   5641  C CG1 . ILE   B 1 246 ? 4.471   18.079  32.243  1.00 22.44  ?  246 ILE   B CG1 1 
ATOM   5642  C CG2 . ILE   B 1 246 ? 2.075   17.432  32.679  1.00 20.25  ?  246 ILE   B CG2 1 
ATOM   5643  C CD1 . ILE   B 1 246 ? 4.353   17.832  30.749  1.00 21.75  ?  246 ILE   B CD1 1 
ATOM   5644  N N   . LYS   B 1 247 ? 1.124   20.751  34.001  1.00 23.92  ?  247 LYS   B N   1 
ATOM   5645  C CA  . LYS   B 1 247 ? -0.206  21.140  34.462  1.00 27.11  ?  247 LYS   B CA  1 
ATOM   5646  C C   . LYS   B 1 247 ? -0.797  22.253  33.599  1.00 25.79  ?  247 LYS   B C   1 
ATOM   5647  O O   . LYS   B 1 247 ? -2.007  22.279  33.354  1.00 30.18  ?  247 LYS   B O   1 
ATOM   5648  C CB  . LYS   B 1 247 ? -0.156  21.565  35.927  1.00 27.93  ?  247 LYS   B CB  1 
ATOM   5649  C CG  . LYS   B 1 247 ? -0.020  20.408  36.911  1.00 27.08  ?  247 LYS   B CG  1 
ATOM   5650  C CD  . LYS   B 1 247 ? -0.146  20.909  38.337  1.00 28.56  ?  247 LYS   B CD  1 
ATOM   5651  C CE  . LYS   B 1 247 ? -0.007  19.789  39.334  1.00 28.24  ?  247 LYS   B CE  1 
ATOM   5652  N NZ  . LYS   B 1 247 ? -0.391  20.231  40.702  1.00 26.73  ?  247 LYS   B NZ  1 
ATOM   5653  N N   . GLU   B 1 248 ? 0.032   23.187  33.137  1.00 26.27  ?  248 GLU   B N   1 
ATOM   5654  C CA  . GLU   B 1 248 ? -0.481  24.219  32.242  1.00 27.33  ?  248 GLU   B CA  1 
ATOM   5655  C C   . GLU   B 1 248 ? -0.927  23.620  30.914  1.00 29.82  ?  248 GLU   B C   1 
ATOM   5656  O O   . GLU   B 1 248 ? -1.910  24.078  30.321  1.00 32.93  ?  248 GLU   B O   1 
ATOM   5657  C CB  . GLU   B 1 248 ? 0.579   25.302  32.023  1.00 30.96  ?  248 GLU   B CB  1 
ATOM   5658  C CG  . GLU   B 1 248 ? 0.722   26.266  33.199  1.00 37.55  ?  248 GLU   B CG  1 
ATOM   5659  C CD  . GLU   B 1 248 ? 2.019   27.067  33.178  1.00 33.83  ?  248 GLU   B CD  1 
ATOM   5660  O OE1 . GLU   B 1 248 ? 2.772   26.982  32.183  1.00 32.70  ?  248 GLU   B OE1 1 
ATOM   5661  O OE2 . GLU   B 1 248 ? 2.286   27.777  34.175  1.00 38.39  ?  248 GLU   B OE2 1 
ATOM   5662  N N   . VAL   B 1 249 ? -0.221  22.596  30.431  1.00 29.65  ?  249 VAL   B N   1 
ATOM   5663  C CA  . VAL   B 1 249 ? -0.650  21.920  29.210  1.00 27.49  ?  249 VAL   B CA  1 
ATOM   5664  C C   . VAL   B 1 249 ? -1.983  21.220  29.441  1.00 28.62  ?  249 VAL   B C   1 
ATOM   5665  O O   . VAL   B 1 249 ? -2.919  21.360  28.647  1.00 25.04  ?  249 VAL   B O   1 
ATOM   5666  C CB  . VAL   B 1 249 ? 0.435   20.939  28.734  1.00 28.10  ?  249 VAL   B CB  1 
ATOM   5667  C CG1 . VAL   B 1 249 ? -0.080  20.093  27.573  1.00 24.38  ?  249 VAL   B CG1 1 
ATOM   5668  C CG2 . VAL   B 1 249 ? 1.698   21.701  28.335  1.00 28.26  ?  249 VAL   B CG2 1 
ATOM   5669  N N   . ILE   B 1 250 ? -2.091  20.467  30.542  1.00 23.44  ?  250 ILE   B N   1 
ATOM   5670  C CA  . ILE   B 1 250 ? -3.343  19.792  30.878  1.00 22.81  ?  250 ILE   B CA  1 
ATOM   5671  C C   . ILE   B 1 250 ? -4.477  20.800  30.972  1.00 25.01  ?  250 ILE   B C   1 
ATOM   5672  O O   . ILE   B 1 250 ? -5.550  20.611  30.386  1.00 24.64  ?  250 ILE   B O   1 
ATOM   5673  C CB  . ILE   B 1 250 ? -3.188  19.002  32.190  1.00 27.24  ?  250 ILE   B CB  1 
ATOM   5674  C CG1 . ILE   B 1 250 ? -2.387  17.723  31.954  1.00 23.24  ?  250 ILE   B CG1 1 
ATOM   5675  C CG2 . ILE   B 1 250 ? -4.548  18.682  32.800  1.00 22.39  ?  250 ILE   B CG2 1 
ATOM   5676  C CD1 . ILE   B 1 250 ? -1.883  17.101  33.222  1.00 26.14  ?  250 ILE   B CD1 1 
ATOM   5677  N N   . PHE   B 1 251 ? -4.245  21.896  31.703  1.00 29.68  ?  251 PHE   B N   1 
ATOM   5678  C CA  . PHE   B 1 251 ? -5.270  22.920  31.887  1.00 28.13  ?  251 PHE   B CA  1 
ATOM   5679  C C   . PHE   B 1 251 ? -5.786  23.439  30.552  1.00 29.67  ?  251 PHE   B C   1 
ATOM   5680  O O   . PHE   B 1 251 ? -6.982  23.726  30.411  1.00 27.55  ?  251 PHE   B O   1 
ATOM   5681  C CB  . PHE   B 1 251 ? -4.702  24.059  32.729  1.00 28.35  ?  251 PHE   B CB  1 
ATOM   5682  C CG  . PHE   B 1 251 ? -5.739  24.994  33.282  1.00 32.36  ?  251 PHE   B CG  1 
ATOM   5683  C CD1 . PHE   B 1 251 ? -6.388  24.703  34.478  1.00 32.50  ?  251 PHE   B CD1 1 
ATOM   5684  C CD2 . PHE   B 1 251 ? -6.044  26.180  32.627  1.00 30.05  ?  251 PHE   B CD2 1 
ATOM   5685  C CE1 . PHE   B 1 251 ? -7.332  25.574  35.000  1.00 30.77  ?  251 PHE   B CE1 1 
ATOM   5686  C CE2 . PHE   B 1 251 ? -6.988  27.051  33.141  1.00 33.16  ?  251 PHE   B CE2 1 
ATOM   5687  C CZ  . PHE   B 1 251 ? -7.632  26.748  34.329  1.00 31.49  ?  251 PHE   B CZ  1 
ATOM   5688  N N   . ASP   B 1 252 ? -4.902  23.555  29.557  1.00 27.44  ?  252 ASP   B N   1 
ATOM   5689  C CA  . ASP   B 1 252 ? -5.322  24.000  28.234  1.00 32.08  ?  252 ASP   B CA  1 
ATOM   5690  C C   . ASP   B 1 252 ? -6.056  22.901  27.482  1.00 27.82  ?  252 ASP   B C   1 
ATOM   5691  O O   . ASP   B 1 252 ? -7.031  23.180  26.780  1.00 28.87  ?  252 ASP   B O   1 
ATOM   5692  C CB  . ASP   B 1 252 ? -4.121  24.477  27.415  1.00 30.98  ?  252 ASP   B CB  1 
ATOM   5693  C CG  . ASP   B 1 252 ? -3.747  25.911  27.714  1.00 32.97  ?  252 ASP   B CG  1 
ATOM   5694  O OD1 . ASP   B 1 252 ? -3.905  26.323  28.881  1.00 32.42  ?  252 ASP   B OD1 1 
ATOM   5695  O OD2 . ASP   B 1 252 ? -3.319  26.630  26.780  1.00 35.21  ?  252 ASP   B OD2 1 
ATOM   5696  N N   . MET   B 1 253 ? -5.598  21.654  27.613  1.00 26.73  ?  253 MET   B N   1 
ATOM   5697  C CA  . MET   B 1 253 ? -6.250  20.549  26.916  1.00 26.76  ?  253 MET   B CA  1 
ATOM   5698  C C   . MET   B 1 253 ? -7.747  20.530  27.186  1.00 27.39  ?  253 MET   B C   1 
ATOM   5699  O O   . MET   B 1 253 ? -8.544  20.264  26.281  1.00 28.14  ?  253 MET   B O   1 
ATOM   5700  C CB  . MET   B 1 253 ? -5.626  19.214  27.333  1.00 26.82  ?  253 MET   B CB  1 
ATOM   5701  C CG  . MET   B 1 253 ? -4.304  18.882  26.659  1.00 24.91  ?  253 MET   B CG  1 
ATOM   5702  S SD  . MET   B 1 253 ? -3.513  17.449  27.420  1.00 25.27  ?  253 MET   B SD  1 
ATOM   5703  C CE  . MET   B 1 253 ? -4.780  16.214  27.182  1.00 23.33  ?  253 MET   B CE  1 
ATOM   5704  N N   . TYR   B 1 254 ? -8.147  20.830  28.421  1.00 27.13  ?  254 TYR   B N   1 
ATOM   5705  C CA  . TYR   B 1 254 ? -9.526  20.657  28.854  1.00 27.54  ?  254 TYR   B CA  1 
ATOM   5706  C C   . TYR   B 1 254 ? -10.363 21.924  28.716  1.00 30.59  ?  254 TYR   B C   1 
ATOM   5707  O O   . TYR   B 1 254 ? -11.523 21.933  29.143  1.00 35.92  ?  254 TYR   B O   1 
ATOM   5708  C CB  . TYR   B 1 254 ? -9.548  20.123  30.286  1.00 28.19  ?  254 TYR   B CB  1 
ATOM   5709  C CG  . TYR   B 1 254 ? -9.104  18.676  30.320  1.00 27.86  ?  254 TYR   B CG  1 
ATOM   5710  C CD1 . TYR   B 1 254 ? -7.758  18.341  30.245  1.00 25.63  ?  254 TYR   B CD1 1 
ATOM   5711  C CD2 . TYR   B 1 254 ? -10.032 17.647  30.376  1.00 25.17  ?  254 TYR   B CD2 1 
ATOM   5712  C CE1 . TYR   B 1 254 ? -7.348  17.033  30.249  1.00 23.46  ?  254 TYR   B CE1 1 
ATOM   5713  C CE2 . TYR   B 1 254 ? -9.629  16.337  30.376  1.00 24.18  ?  254 TYR   B CE2 1 
ATOM   5714  C CZ  . TYR   B 1 254 ? -8.289  16.035  30.316  1.00 24.23  ?  254 TYR   B CZ  1 
ATOM   5715  O OH  . TYR   B 1 254 ? -7.887  14.721  30.318  1.00 24.11  ?  254 TYR   B OH  1 
ATOM   5716  N N   . LYS   B 1 255 ? -9.804  22.988  28.125  1.00 29.71  ?  255 LYS   B N   1 
ATOM   5717  C CA  . LYS   B 1 255 ? -10.627 24.027  27.519  1.00 31.00  ?  255 LYS   B CA  1 
ATOM   5718  C C   . LYS   B 1 255 ? -11.373 23.503  26.302  1.00 31.73  ?  255 LYS   B C   1 
ATOM   5719  O O   . LYS   B 1 255 ? -12.322 24.146  25.844  1.00 33.88  ?  255 LYS   B O   1 
ATOM   5720  C CB  . LYS   B 1 255 ? -9.768  25.217  27.075  1.00 31.52  ?  255 LYS   B CB  1 
ATOM   5721  C CG  . LYS   B 1 255 ? -9.023  25.969  28.170  1.00 32.66  ?  255 LYS   B CG  1 
ATOM   5722  C CD  . LYS   B 1 255 ? -7.984  26.910  27.552  1.00 31.41  ?  255 LYS   B CD  1 
ATOM   5723  C CE  . LYS   B 1 255 ? -7.548  28.010  28.510  1.00 31.52  ?  255 LYS   B CE  1 
ATOM   5724  N NZ  . LYS   B 1 255 ? -7.319  27.481  29.878  1.00 39.69  ?  255 LYS   B NZ  1 
ATOM   5725  N N   . TYR   B 1 256 ? -10.951 22.363  25.760  1.00 31.06  ?  256 TYR   B N   1 
ATOM   5726  C CA  . TYR   B 1 256 ? -11.474 21.827  24.511  1.00 31.71  ?  256 TYR   B CA  1 
ATOM   5727  C C   . TYR   B 1 256 ? -12.239 20.530  24.739  1.00 31.23  ?  256 TYR   B C   1 
ATOM   5728  O O   . TYR   B 1 256 ? -12.163 19.588  23.944  1.00 31.06  ?  256 TYR   B O   1 
ATOM   5729  C CB  . TYR   B 1 256 ? -10.344 21.634  23.508  1.00 31.51  ?  256 TYR   B CB  1 
ATOM   5730  C CG  . TYR   B 1 256 ? -9.452  22.848  23.449  1.00 34.25  ?  256 TYR   B CG  1 
ATOM   5731  C CD1 . TYR   B 1 256 ? -9.971  24.090  23.092  1.00 36.82  ?  256 TYR   B CD1 1 
ATOM   5732  C CD2 . TYR   B 1 256 ? -8.105  22.763  23.766  1.00 30.82  ?  256 TYR   B CD2 1 
ATOM   5733  C CE1 . TYR   B 1 256 ? -9.168  25.214  23.049  1.00 33.35  ?  256 TYR   B CE1 1 
ATOM   5734  C CE2 . TYR   B 1 256 ? -7.300  23.877  23.727  1.00 32.89  ?  256 TYR   B CE2 1 
ATOM   5735  C CZ  . TYR   B 1 256 ? -7.837  25.100  23.367  1.00 32.36  ?  256 TYR   B CZ  1 
ATOM   5736  O OH  . TYR   B 1 256 ? -7.036  26.213  23.325  1.00 36.99  ?  256 TYR   B OH  1 
ATOM   5737  N N   . ALA   B 1 257 ? -12.984 20.486  25.840  1.00 32.92  ?  257 ALA   B N   1 
ATOM   5738  C CA  . ALA   B 1 257 ? -13.958 19.441  26.116  1.00 30.79  ?  257 ALA   B CA  1 
ATOM   5739  C C   . ALA   B 1 257 ? -14.986 20.006  27.083  1.00 31.20  ?  257 ALA   B C   1 
ATOM   5740  O O   . ALA   B 1 257 ? -14.747 21.019  27.746  1.00 31.33  ?  257 ALA   B O   1 
ATOM   5741  C CB  . ALA   B 1 257 ? -13.303 18.184  26.695  1.00 31.79  ?  257 ALA   B CB  1 
ATOM   5742  N N   . ASP   B 1 258 ? -16.142 19.343  27.142  1.00 31.45  ?  258 ASP   B N   1 
ATOM   5743  C CA  . ASP   B 1 258 ? -17.182 19.687  28.102  1.00 31.76  ?  258 ASP   B CA  1 
ATOM   5744  C C   . ASP   B 1 258 ? -17.266 18.702  29.254  1.00 30.56  ?  258 ASP   B C   1 
ATOM   5745  O O   . ASP   B 1 258 ? -17.911 19.005  30.265  1.00 30.59  ?  258 ASP   B O   1 
ATOM   5746  C CB  . ASP   B 1 258 ? -18.547 19.748  27.415  1.00 33.03  ?  258 ASP   B CB  1 
ATOM   5747  C CG  . ASP   B 1 258 ? -18.536 20.620  26.186  1.00 34.26  ?  258 ASP   B CG  1 
ATOM   5748  O OD1 . ASP   B 1 258 ? -18.122 21.794  26.300  1.00 34.68  ?  258 ASP   B OD1 1 
ATOM   5749  O OD2 . ASP   B 1 258 ? -18.923 20.123  25.104  1.00 34.82  ?  258 ASP   B OD2 1 
ATOM   5750  N N   . ALA   B 1 259 ? -16.652 17.531  29.109  1.00 29.55  ?  259 ALA   B N   1 
ATOM   5751  C CA  . ALA   B 1 259 ? -16.644 16.521  30.155  1.00 28.36  ?  259 ALA   B CA  1 
ATOM   5752  C C   . ALA   B 1 259 ? -15.461 15.602  29.908  1.00 27.25  ?  259 ALA   B C   1 
ATOM   5753  O O   . ALA   B 1 259 ? -14.811 15.661  28.861  1.00 27.49  ?  259 ALA   B O   1 
ATOM   5754  C CB  . ALA   B 1 259 ? -17.955 15.729  30.187  1.00 28.65  ?  259 ALA   B CB  1 
ATOM   5755  N N   . LEU   B 1 260 ? -15.178 14.751  30.893  1.00 26.04  ?  260 LEU   B N   1 
ATOM   5756  C CA  . LEU   B 1 260 ? -14.205 13.693  30.698  1.00 24.98  ?  260 LEU   B CA  1 
ATOM   5757  C C   . LEU   B 1 260 ? -14.737 12.413  31.314  1.00 24.21  ?  260 LEU   B C   1 
ATOM   5758  O O   . LEU   B 1 260 ? -15.593 12.433  32.207  1.00 27.06  ?  260 LEU   B O   1 
ATOM   5759  C CB  . LEU   B 1 260 ? -12.823 14.049  31.290  1.00 24.09  ?  260 LEU   B CB  1 
ATOM   5760  C CG  . LEU   B 1 260 ? -12.660 14.305  32.796  1.00 26.54  ?  260 LEU   B CG  1 
ATOM   5761  C CD1 . LEU   B 1 260 ? -12.393 13.028  33.575  1.00 22.04  ?  260 LEU   B CD1 1 
ATOM   5762  C CD2 . LEU   B 1 260 ? -11.546 15.313  33.052  1.00 24.92  ?  260 LEU   B CD2 1 
ATOM   5763  N N   . THR   B 1 261 ? -14.247 11.300  30.786  1.00 23.85  ?  261 THR   B N   1 
ATOM   5764  C CA  . THR   B 1 261 ? -14.337 9.991   31.412  1.00 22.60  ?  261 THR   B CA  1 
ATOM   5765  C C   . THR   B 1 261 ? -12.913 9.489   31.525  1.00 22.29  ?  261 THR   B C   1 
ATOM   5766  O O   . THR   B 1 261 ? -12.140 9.596   30.567  1.00 23.83  ?  261 THR   B O   1 
ATOM   5767  C CB  . THR   B 1 261 ? -15.173 9.007   30.590  1.00 23.01  ?  261 THR   B CB  1 
ATOM   5768  O OG1 . THR   B 1 261 ? -14.582 8.850   29.293  1.00 24.41  ?  261 THR   B OG1 1 
ATOM   5769  C CG2 . THR   B 1 261 ? -16.596 9.508   30.434  1.00 24.66  ?  261 THR   B CG2 1 
ATOM   5770  N N   . MET   B 1 262 ? -12.558 8.964   32.689  1.00 20.36  ?  262 MET   B N   1 
ATOM   5771  C CA  . MET   B 1 262 ? -11.180 8.612   32.962  1.00 21.23  ?  262 MET   B CA  1 
ATOM   5772  C C   . MET   B 1 262 ? -11.120 7.227   33.575  1.00 19.21  ?  262 MET   B C   1 
ATOM   5773  O O   . MET   B 1 262 ? -11.864 6.930   34.515  1.00 19.04  ?  262 MET   B O   1 
ATOM   5774  C CB  . MET   B 1 262 ? -10.541 9.632   33.907  1.00 20.94  ?  262 MET   B CB  1 
ATOM   5775  C CG  . MET   B 1 262 ? -9.058  9.400   34.126  1.00 25.00  ?  262 MET   B CG  1 
ATOM   5776  S SD  . MET   B 1 262 ? -8.392  10.541  35.337  1.00 32.03  ?  262 MET   B SD  1 
ATOM   5777  C CE  . MET   B 1 262 ? -8.650  12.103  34.497  1.00 26.09  ?  262 MET   B CE  1 
ATOM   5778  N N   . SER   B 1 263 ? -10.253 6.380   33.031  1.00 18.02  ?  263 SER   B N   1 
ATOM   5779  C CA  . SER   B 1 263 ? -9.744  5.242   33.785  1.00 19.19  ?  263 SER   B CA  1 
ATOM   5780  C C   . SER   B 1 263 ? -8.563  5.729   34.608  1.00 21.87  ?  263 SER   B C   1 
ATOM   5781  O O   . SER   B 1 263 ? -7.496  6.030   34.059  1.00 19.71  ?  263 SER   B O   1 
ATOM   5782  C CB  . SER   B 1 263 ? -9.320  4.095   32.873  1.00 21.16  ?  263 SER   B CB  1 
ATOM   5783  O OG  . SER   B 1 263 ? -8.932  2.977   33.663  1.00 16.14  ?  263 SER   B OG  1 
ATOM   5784  N N   . ALA   B 1 264 ? -8.749  5.820   35.921  1.00 19.09  ?  264 ALA   B N   1 
ATOM   5785  C CA  . ALA   B 1 264 ? -7.643  6.211   36.776  1.00 18.07  ?  264 ALA   B CA  1 
ATOM   5786  C C   . ALA   B 1 264 ? -6.652  5.075   36.992  1.00 17.18  ?  264 ALA   B C   1 
ATOM   5787  O O   . ALA   B 1 264 ? -5.666  5.262   37.705  1.00 16.67  ?  264 ALA   B O   1 
ATOM   5788  C CB  . ALA   B 1 264 ? -8.174  6.732   38.112  1.00 18.11  ?  264 ALA   B CB  1 
ATOM   5789  N N   . LYS   B 1 265 ? -6.882  3.909   36.387  1.00 18.30  ?  265 LYS   B N   1 
ATOM   5790  C CA  . LYS   B 1 265 ? -5.940  2.802   36.465  1.00 14.49  ?  265 LYS   B CA  1 
ATOM   5791  C C   . LYS   B 1 265 ? -4.754  2.989   35.534  1.00 14.94  ?  265 LYS   B C   1 
ATOM   5792  O O   . LYS   B 1 265 ? -3.866  2.130   35.511  1.00 14.81  ?  265 LYS   B O   1 
ATOM   5793  C CB  . LYS   B 1 265 ? -6.648  1.480   36.148  1.00 15.43  ?  265 LYS   B CB  1 
ATOM   5794  C CG  . LYS   B 1 265 ? -7.868  1.207   37.003  1.00 15.57  ?  265 LYS   B CG  1 
ATOM   5795  C CD  . LYS   B 1 265 ? -8.733  0.085   36.424  1.00 19.23  ?  265 LYS   B CD  1 
ATOM   5796  C CE  . LYS   B 1 265 ? -8.142  -1.310  36.646  1.00 14.78  ?  265 LYS   B CE  1 
ATOM   5797  N NZ  . LYS   B 1 265 ? -9.091  -2.377  36.177  1.00 16.18  ?  265 LYS   B NZ  1 
ATOM   5798  N N   . LYS   B 1 266 ? -4.720  4.086   34.769  1.00 16.19  ?  266 LYS   B N   1 
ATOM   5799  C CA  . LYS   B 1 266 ? -3.595  4.392   33.892  1.00 14.85  ?  266 LYS   B CA  1 
ATOM   5800  C C   . LYS   B 1 266 ? -2.792  5.552   34.476  1.00 18.00  ?  266 LYS   B C   1 
ATOM   5801  O O   . LYS   B 1 266 ? -2.094  5.375   35.480  1.00 18.86  ?  266 LYS   B O   1 
ATOM   5802  C CB  . LYS   B 1 266 ? -4.064  4.714   32.468  1.00 20.45  ?  266 LYS   B CB  1 
ATOM   5803  C CG  . LYS   B 1 266 ? -4.474  3.492   31.621  1.00 20.40  ?  266 LYS   B CG  1 
ATOM   5804  C CD  . LYS   B 1 266 ? -5.593  2.696   32.278  1.00 18.88  ?  266 LYS   B CD  1 
ATOM   5805  C CE  . LYS   B 1 266 ? -6.431  1.936   31.300  1.00 22.07  ?  266 LYS   B CE  1 
ATOM   5806  N NZ  . LYS   B 1 266 ? -7.059  2.843   30.310  1.00 29.28  ?  266 LYS   B NZ  1 
ATOM   5807  N N   . ASP   B 1 267 ? -2.901  6.745   33.882  1.00 21.84  ?  267 ASP   B N   1 
ATOM   5808  C CA  . ASP   B 1 267 ? -2.000  7.839   34.253  1.00 22.06  ?  267 ASP   B CA  1 
ATOM   5809  C C   . ASP   B 1 267 ? -2.061  8.274   35.727  1.00 21.28  ?  267 ASP   B C   1 
ATOM   5810  O O   . ASP   B 1 267 ? -1.023  8.747   36.229  1.00 24.72  ?  267 ASP   B O   1 
ATOM   5811  C CB  . ASP   B 1 267 ? -2.240  9.045   33.330  1.00 18.04  ?  267 ASP   B CB  1 
ATOM   5812  C CG  . ASP   B 1 267 ? -1.473  8.934   32.014  1.00 24.30  ?  267 ASP   B CG  1 
ATOM   5813  O OD1 . ASP   B 1 267 ? -0.950  7.835   31.712  1.00 26.09  ?  267 ASP   B OD1 1 
ATOM   5814  O OD2 . ASP   B 1 267 ? -1.392  9.942   31.274  1.00 22.20  ?  267 ASP   B OD2 1 
ATOM   5815  N N   . PRO   B 1 268 ? -3.179  8.161   36.456  1.00 17.84  ?  268 PRO   B N   1 
ATOM   5816  C CA  . PRO   B 1 268 ? -3.160  8.412   37.908  1.00 17.41  ?  268 PRO   B CA  1 
ATOM   5817  C C   . PRO   B 1 268 ? -2.514  7.321   38.750  1.00 20.02  ?  268 PRO   B C   1 
ATOM   5818  O O   . PRO   B 1 268 ? -2.585  7.400   39.983  1.00 20.72  ?  268 PRO   B O   1 
ATOM   5819  C CB  . PRO   B 1 268 ? -4.653  8.538   38.250  1.00 19.90  ?  268 PRO   B CB  1 
ATOM   5820  C CG  . PRO   B 1 268 ? -5.294  8.956   36.973  1.00 19.64  ?  268 PRO   B CG  1 
ATOM   5821  C CD  . PRO   B 1 268 ? -4.556  8.196   35.929  1.00 17.12  ?  268 PRO   B CD  1 
ATOM   5822  N N   . LEU   B 1 269 ? -1.904  6.302   38.147  1.00 17.27  ?  269 LEU   B N   1 
ATOM   5823  C CA  . LEU   B 1 269 ? -1.027  5.397   38.887  1.00 13.14  ?  269 LEU   B CA  1 
ATOM   5824  C C   . LEU   B 1 269 ? -1.787  4.621   39.961  1.00 18.31  ?  269 LEU   B C   1 
ATOM   5825  O O   . LEU   B 1 269 ? -1.309  4.462   41.090  1.00 16.22  ?  269 LEU   B O   1 
ATOM   5826  C CB  . LEU   B 1 269 ? 0.143   6.162   39.510  1.00 18.74  ?  269 LEU   B CB  1 
ATOM   5827  C CG  . LEU   B 1 269 ? 1.051   6.906   38.530  1.00 15.93  ?  269 LEU   B CG  1 
ATOM   5828  C CD1 . LEU   B 1 269 ? 1.656   8.146   39.177  1.00 17.37  ?  269 LEU   B CD1 1 
ATOM   5829  C CD2 . LEU   B 1 269 ? 2.140   5.974   38.073  1.00 15.80  ?  269 LEU   B CD2 1 
ATOM   5830  N N   . LEU   B 1 270 ? -2.969  4.119   39.614  1.00 15.63  ?  270 LEU   B N   1 
ATOM   5831  C CA  . LEU   B 1 270 ? -3.799  3.375   40.554  1.00 15.74  ?  270 LEU   B CA  1 
ATOM   5832  C C   . LEU   B 1 270 ? -3.915  1.912   40.143  1.00 16.82  ?  270 LEU   B C   1 
ATOM   5833  O O   . LEU   B 1 270 ? -3.546  1.514   39.032  1.00 19.08  ?  270 LEU   B O   1 
ATOM   5834  C CB  . LEU   B 1 270 ? -5.192  4.001   40.660  1.00 17.78  ?  270 LEU   B CB  1 
ATOM   5835  C CG  . LEU   B 1 270 ? -5.221  5.454   41.135  1.00 18.24  ?  270 LEU   B CG  1 
ATOM   5836  C CD1 . LEU   B 1 270 ? -6.651  5.948   41.235  1.00 17.59  ?  270 LEU   B CD1 1 
ATOM   5837  C CD2 . LEU   B 1 270 ? -4.490  5.580   42.478  1.00 17.47  ?  270 LEU   B CD2 1 
ATOM   5838  N N   . ASN   B 1 271 ? -4.415  1.111   41.083  1.00 16.15  ?  271 ASN   B N   1 
ATOM   5839  C CA  . ASN   B 1 271 ? -4.775  -0.280  40.842  1.00 17.19  ?  271 ASN   B CA  1 
ATOM   5840  C C   . ASN   B 1 271 ? -6.256  -0.460  40.537  1.00 16.94  ?  271 ASN   B C   1 
ATOM   5841  O O   . ASN   B 1 271 ? -6.648  -1.516  40.019  1.00 16.27  ?  271 ASN   B O   1 
ATOM   5842  C CB  . ASN   B 1 271 ? -4.399  -1.136  42.055  1.00 13.93  ?  271 ASN   B CB  1 
ATOM   5843  C CG  . ASN   B 1 271 ? -2.913  -1.078  42.363  1.00 15.36  ?  271 ASN   B CG  1 
ATOM   5844  O OD1 . ASN   B 1 271 ? -2.508  -0.804  43.491  1.00 18.09  ?  271 ASN   B OD1 1 
ATOM   5845  N ND2 . ASN   B 1 271 ? -2.093  -1.316  41.351  1.00 17.04  ?  271 ASN   B ND2 1 
ATOM   5846  N N   . ILE   B 1 272 ? -7.069  0.551   40.847  1.00 13.73  ?  272 ILE   B N   1 
ATOM   5847  C CA  . ILE   B 1 272 ? -8.500  0.547   40.570  1.00 15.71  ?  272 ILE   B CA  1 
ATOM   5848  C C   . ILE   B 1 272 ? -8.932  2.010   40.570  1.00 17.15  ?  272 ILE   B C   1 
ATOM   5849  O O   . ILE   B 1 272 ? -8.262  2.872   41.149  1.00 18.51  ?  272 ILE   B O   1 
ATOM   5850  C CB  . ILE   B 1 272 ? -9.280  -0.294  41.619  1.00 15.79  ?  272 ILE   B CB  1 
ATOM   5851  C CG1 . ILE   B 1 272 ? -10.687 -0.620  41.122  1.00 15.03  ?  272 ILE   B CG1 1 
ATOM   5852  C CG2 . ILE   B 1 272 ? -9.319  0.401   42.997  1.00 13.81  ?  272 ILE   B CG2 1 
ATOM   5853  C CD1 . ILE   B 1 272 ? -10.710 -1.239  39.735  1.00 19.75  ?  272 ILE   B CD1 1 
ATOM   5854  N N   . GLY   B 1 273 ? -10.025 2.308   39.886  1.00 16.44  ?  273 GLY   B N   1 
ATOM   5855  C CA  . GLY   B 1 273 ? -10.606 3.634   39.987  1.00 16.81  ?  273 GLY   B CA  1 
ATOM   5856  C C   . GLY   B 1 273 ? -10.894 4.285   38.657  1.00 16.18  ?  273 GLY   B C   1 
ATOM   5857  O O   . GLY   B 1 273 ? -10.246 4.007   37.646  1.00 15.81  ?  273 GLY   B O   1 
ATOM   5858  N N   . GLY   B 1 274 ? -11.890 5.167   38.655  1.00 18.78  ?  274 GLY   B N   1 
ATOM   5859  C CA  . GLY   B 1 274 ? -12.306 5.876   37.460  1.00 16.12  ?  274 GLY   B CA  1 
ATOM   5860  C C   . GLY   B 1 274 ? -12.988 7.159   37.870  1.00 16.86  ?  274 GLY   B C   1 
ATOM   5861  O O   . GLY   B 1 274 ? -13.213 7.411   39.055  1.00 20.84  ?  274 GLY   B O   1 
ATOM   5862  N N   . LEU   B 1 275 ? -13.332 7.971   36.873  1.00 21.35  ?  275 LEU   B N   1 
ATOM   5863  C CA  . LEU   B 1 275 ? -13.821 9.311   37.171  1.00 18.84  ?  275 LEU   B CA  1 
ATOM   5864  C C   . LEU   B 1 275 ? -14.588 9.892   35.995  1.00 21.68  ?  275 LEU   B C   1 
ATOM   5865  O O   . LEU   B 1 275 ? -14.089 9.912   34.862  1.00 21.22  ?  275 LEU   B O   1 
ATOM   5866  C CB  . LEU   B 1 275 ? -12.663 10.239  37.535  1.00 18.56  ?  275 LEU   B CB  1 
ATOM   5867  C CG  . LEU   B 1 275 ? -13.106 11.657  37.881  1.00 21.91  ?  275 LEU   B CG  1 
ATOM   5868  C CD1 . LEU   B 1 275 ? -13.885 11.677  39.208  1.00 19.21  ?  275 LEU   B CD1 1 
ATOM   5869  C CD2 . LEU   B 1 275 ? -11.891 12.585  37.910  1.00 22.33  ?  275 LEU   B CD2 1 
ATOM   5870  N N   . VAL   B 1 276 ? -15.789 10.386  36.277  1.00 23.87  ?  276 VAL   B N   1 
ATOM   5871  C CA  . VAL   B 1 276 ? -16.492 11.314  35.397  1.00 24.68  ?  276 VAL   B CA  1 
ATOM   5872  C C   . VAL   B 1 276 ? -16.291 12.721  35.947  1.00 22.80  ?  276 VAL   B C   1 
ATOM   5873  O O   . VAL   B 1 276 ? -16.489 12.960  37.142  1.00 22.44  ?  276 VAL   B O   1 
ATOM   5874  C CB  . VAL   B 1 276 ? -17.990 10.978  35.307  1.00 23.11  ?  276 VAL   B CB  1 
ATOM   5875  C CG1 . VAL   B 1 276 ? -18.672 11.898  34.324  1.00 24.57  ?  276 VAL   B CG1 1 
ATOM   5876  C CG2 . VAL   B 1 276 ? -18.191 9.528   34.937  1.00 22.60  ?  276 VAL   B CG2 1 
ATOM   5877  N N   . ALA   B 1 277 ? -15.888 13.648  35.094  1.00 23.56  ?  277 ALA   B N   1 
ATOM   5878  C CA  . ALA   B 1 277 ? -15.877 15.054  35.465  1.00 24.21  ?  277 ALA   B CA  1 
ATOM   5879  C C   . ALA   B 1 277 ? -16.582 15.841  34.375  1.00 25.66  ?  277 ALA   B C   1 
ATOM   5880  O O   . ALA   B 1 277 ? -16.473 15.511  33.191  1.00 26.65  ?  277 ALA   B O   1 
ATOM   5881  C CB  . ALA   B 1 277 ? -14.454 15.580  35.687  1.00 23.61  ?  277 ALA   B CB  1 
ATOM   5882  N N   . ILE   B 1 278 ? -17.340 16.857  34.780  1.00 27.76  ?  278 ILE   B N   1 
ATOM   5883  C CA  . ILE   B 1 278 ? -18.155 17.645  33.865  1.00 27.97  ?  278 ILE   B CA  1 
ATOM   5884  C C   . ILE   B 1 278 ? -17.864 19.120  34.099  1.00 28.62  ?  278 ILE   B C   1 
ATOM   5885  O O   . ILE   B 1 278 ? -17.874 19.586  35.243  1.00 34.24  ?  278 ILE   B O   1 
ATOM   5886  C CB  . ILE   B 1 278 ? -19.652 17.346  34.048  1.00 32.25  ?  278 ILE   B CB  1 
ATOM   5887  C CG1 . ILE   B 1 278 ? -19.950 15.917  33.598  1.00 28.13  ?  278 ILE   B CG1 1 
ATOM   5888  C CG2 . ILE   B 1 278 ? -20.493 18.352  33.282  1.00 33.73  ?  278 ILE   B CG2 1 
ATOM   5889  C CD1 . ILE   B 1 278 ? -21.227 15.377  34.161  1.00 28.29  ?  278 ILE   B CD1 1 
ATOM   5890  N N   . ARG   B 1 279 ? -17.608 19.851  33.018  1.00 29.49  ?  279 ARG   B N   1 
ATOM   5891  C CA  . ARG   B 1 279 ? -17.164 21.235  33.111  1.00 31.72  ?  279 ARG   B CA  1 
ATOM   5892  C C   . ARG   B 1 279 ? -18.195 22.129  33.790  1.00 35.33  ?  279 ARG   B C   1 
ATOM   5893  O O   . ARG   B 1 279 ? -17.939 22.633  34.889  1.00 35.85  ?  279 ARG   B O   1 
ATOM   5894  C CB  . ARG   B 1 279 ? -16.835 21.767  31.724  1.00 30.94  ?  279 ARG   B CB  1 
ATOM   5895  C CG  . ARG   B 1 279 ? -16.066 23.061  31.706  1.00 33.68  ?  279 ARG   B CG  1 
ATOM   5896  C CD  . ARG   B 1 279 ? -15.631 23.316  30.280  1.00 34.45  ?  279 ARG   B CD  1 
ATOM   5897  N NE  . ARG   B 1 279 ? -14.927 24.575  30.091  1.00 40.44  ?  279 ARG   B NE  1 
ATOM   5898  C CZ  . ARG   B 1 279 ? -14.605 25.059  28.900  1.00 46.06  ?  279 ARG   B CZ  1 
ATOM   5899  N NH1 . ARG   B 1 279 ? -14.924 24.416  27.786  1.00 43.52  ?  279 ARG   B NH1 1 
ATOM   5900  N NH2 . ARG   B 1 279 ? -13.952 26.218  28.821  1.00 48.03  ?  279 ARG   B NH2 1 
ATOM   5901  N N   . ASP   B 1 280 ? -19.359 22.336  33.163  1.00 33.20  ?  280 ASP   B N   1 
ATOM   5902  C CA  . ASP   B 1 280 ? -20.346 23.224  33.771  1.00 37.72  ?  280 ASP   B CA  1 
ATOM   5903  C C   . ASP   B 1 280 ? -21.794 22.800  33.528  1.00 37.98  ?  280 ASP   B C   1 
ATOM   5904  O O   . ASP   B 1 280 ? -22.713 23.377  34.121  1.00 36.77  ?  280 ASP   B O   1 
ATOM   5905  C CB  . ASP   B 1 280 ? -20.129 24.668  33.287  1.00 37.59  ?  280 ASP   B CB  1 
ATOM   5906  C CG  . ASP   B 1 280 ? -19.948 24.771  31.782  1.00 47.31  ?  280 ASP   B CG  1 
ATOM   5907  O OD1 . ASP   B 1 280 ? -20.445 23.889  31.050  1.00 55.05  ?  280 ASP   B OD1 1 
ATOM   5908  O OD2 . ASP   B 1 280 ? -19.296 25.738  31.328  1.00 46.47  ?  280 ASP   B OD2 1 
ATOM   5909  N N   . ASN   B 1 281 ? -22.022 21.788  32.688  1.00 36.32  ?  281 ASN   B N   1 
ATOM   5910  C CA  . ASN   B 1 281 ? -23.395 21.376  32.404  1.00 42.45  ?  281 ASN   B CA  1 
ATOM   5911  C C   . ASN   B 1 281 ? -24.029 20.660  33.591  1.00 36.42  ?  281 ASN   B C   1 
ATOM   5912  O O   . ASN   B 1 281 ? -23.894 19.438  33.730  1.00 35.04  ?  281 ASN   B O   1 
ATOM   5913  C CB  . ASN   B 1 281 ? -23.449 20.478  31.169  1.00 40.05  ?  281 ASN   B CB  1 
ATOM   5914  C CG  . ASN   B 1 281 ? -24.833 20.421  30.560  1.00 41.13  ?  281 ASN   B CG  1 
ATOM   5915  O OD1 . ASN   B 1 281 ? -25.823 20.151  31.247  1.00 35.90  ?  281 ASN   B OD1 1 
ATOM   5916  N ND2 . ASN   B 1 281 ? -24.912 20.675  29.262  1.00 40.64  ?  281 ASN   B ND2 1 
ATOM   5917  N N   . GLU   B 1 282 ? -24.744 21.408  34.439  1.00 36.69  ?  282 GLU   B N   1 
ATOM   5918  C CA  . GLU   B 1 282 ? -25.293 20.816  35.655  1.00 34.66  ?  282 GLU   B CA  1 
ATOM   5919  C C   . GLU   B 1 282 ? -26.426 19.841  35.357  1.00 35.48  ?  282 GLU   B C   1 
ATOM   5920  O O   . GLU   B 1 282 ? -26.664 18.912  36.140  1.00 35.93  ?  282 GLU   B O   1 
ATOM   5921  C CB  . GLU   B 1 282 ? -25.782 21.900  36.616  1.00 37.53  ?  282 GLU   B CB  1 
ATOM   5922  C CG  . GLU   B 1 282 ? -26.110 21.344  38.004  1.00 44.34  ?  282 GLU   B CG  1 
ATOM   5923  C CD  . GLU   B 1 282 ? -26.627 22.385  38.974  1.00 47.11  ?  282 GLU   B CD  1 
ATOM   5924  O OE1 . GLU   B 1 282 ? -27.364 23.292  38.538  1.00 55.25  ?  282 GLU   B OE1 1 
ATOM   5925  O OE2 . GLU   B 1 282 ? -26.297 22.287  40.177  1.00 43.48  ?  282 GLU   B OE2 1 
ATOM   5926  N N   . GLU   B 1 283 ? -27.136 20.030  34.244  1.00 36.18  ?  283 GLU   B N   1 
ATOM   5927  C CA  . GLU   B 1 283 ? -28.185 19.084  33.882  1.00 35.97  ?  283 GLU   B CA  1 
ATOM   5928  C C   . GLU   B 1 283 ? -27.599 17.727  33.511  1.00 34.29  ?  283 GLU   B C   1 
ATOM   5929  O O   . GLU   B 1 283 ? -28.113 16.686  33.936  1.00 34.76  ?  283 GLU   B O   1 
ATOM   5930  C CB  . GLU   B 1 283 ? -29.023 19.631  32.728  1.00 38.16  ?  283 GLU   B CB  1 
ATOM   5931  C CG  . GLU   B 1 283 ? -30.168 18.711  32.358  1.00 44.31  ?  283 GLU   B CG  1 
ATOM   5932  C CD  . GLU   B 1 283 ? -30.950 19.193  31.154  1.00 52.75  ?  283 GLU   B CD  1 
ATOM   5933  O OE1 . GLU   B 1 283 ? -30.699 20.328  30.687  1.00 52.78  ?  283 GLU   B OE1 1 
ATOM   5934  O OE2 . GLU   B 1 283 ? -31.817 18.429  30.675  1.00 56.77  ?  283 GLU   B OE2 1 
ATOM   5935  N N   . ILE   B 1 284 ? -26.535 17.716  32.706  1.00 34.00  ?  284 ILE   B N   1 
ATOM   5936  C CA  . ILE   B 1 284 ? -25.856 16.458  32.409  1.00 34.25  ?  284 ILE   B CA  1 
ATOM   5937  C C   . ILE   B 1 284 ? -25.346 15.826  33.694  1.00 31.47  ?  284 ILE   B C   1 
ATOM   5938  O O   . ILE   B 1 284 ? -25.461 14.611  33.896  1.00 30.68  ?  284 ILE   B O   1 
ATOM   5939  C CB  . ILE   B 1 284 ? -24.713 16.683  31.400  1.00 36.53  ?  284 ILE   B CB  1 
ATOM   5940  C CG1 . ILE   B 1 284 ? -25.257 17.235  30.082  1.00 40.28  ?  284 ILE   B CG1 1 
ATOM   5941  C CG2 . ILE   B 1 284 ? -23.961 15.380  31.150  1.00 31.69  ?  284 ILE   B CG2 1 
ATOM   5942  C CD1 . ILE   B 1 284 ? -26.020 16.228  29.290  1.00 38.91  ?  284 ILE   B CD1 1 
ATOM   5943  N N   . PHE   B 1 285 ? -24.801 16.646  34.594  1.00 31.14  ?  285 PHE   B N   1 
ATOM   5944  C CA  . PHE   B 1 285 ? -24.274 16.130  35.854  1.00 29.92  ?  285 PHE   B CA  1 
ATOM   5945  C C   . PHE   B 1 285 ? -25.376 15.514  36.707  1.00 29.69  ?  285 PHE   B C   1 
ATOM   5946  O O   . PHE   B 1 285 ? -25.188 14.443  37.295  1.00 28.58  ?  285 PHE   B O   1 
ATOM   5947  C CB  . PHE   B 1 285 ? -23.557 17.251  36.606  1.00 31.09  ?  285 PHE   B CB  1 
ATOM   5948  C CG  . PHE   B 1 285 ? -23.263 16.939  38.046  1.00 34.78  ?  285 PHE   B CG  1 
ATOM   5949  C CD1 . PHE   B 1 285 ? -22.316 15.989  38.388  1.00 29.10  ?  285 PHE   B CD1 1 
ATOM   5950  C CD2 . PHE   B 1 285 ? -23.918 17.620  39.060  1.00 31.47  ?  285 PHE   B CD2 1 
ATOM   5951  C CE1 . PHE   B 1 285 ? -22.036 15.713  39.717  1.00 29.53  ?  285 PHE   B CE1 1 
ATOM   5952  C CE2 . PHE   B 1 285 ? -23.642 17.347  40.393  1.00 33.16  ?  285 PHE   B CE2 1 
ATOM   5953  C CZ  . PHE   B 1 285 ? -22.698 16.395  40.720  1.00 30.93  ?  285 PHE   B CZ  1 
ATOM   5954  N N   . THR   B 1 286 ? -26.538 16.169  36.779  1.00 33.49  ?  286 THR   B N   1 
ATOM   5955  C CA  . THR   B 1 286 ? -27.648 15.615  37.550  1.00 30.82  ?  286 THR   B CA  1 
ATOM   5956  C C   . THR   B 1 286 ? -28.123 14.293  36.963  1.00 32.68  ?  286 THR   B C   1 
ATOM   5957  O O   . THR   B 1 286 ? -28.360 13.328  37.698  1.00 32.91  ?  286 THR   B O   1 
ATOM   5958  C CB  . THR   B 1 286 ? -28.800 16.614  37.608  1.00 33.79  ?  286 THR   B CB  1 
ATOM   5959  O OG1 . THR   B 1 286 ? -28.366 17.796  38.288  1.00 38.38  ?  286 THR   B OG1 1 
ATOM   5960  C CG2 . THR   B 1 286 ? -29.974 16.021  38.355  1.00 32.29  ?  286 THR   B CG2 1 
ATOM   5961  N N   . LEU   B 1 287 ? -28.264 14.228  35.637  1.00 32.31  ?  287 LEU   B N   1 
ATOM   5962  C CA  . LEU   B 1 287 ? -28.672 12.983  34.995  1.00 34.20  ?  287 LEU   B CA  1 
ATOM   5963  C C   . LEU   B 1 287 ? -27.632 11.882  35.188  1.00 32.32  ?  287 LEU   B C   1 
ATOM   5964  O O   . LEU   B 1 287 ? -27.986 10.724  35.454  1.00 30.08  ?  287 LEU   B O   1 
ATOM   5965  C CB  . LEU   B 1 287 ? -28.931 13.234  33.510  1.00 34.59  ?  287 LEU   B CB  1 
ATOM   5966  C CG  . LEU   B 1 287 ? -30.185 14.047  33.193  1.00 33.95  ?  287 LEU   B CG  1 
ATOM   5967  C CD1 . LEU   B 1 287 ? -30.234 14.368  31.711  1.00 39.00  ?  287 LEU   B CD1 1 
ATOM   5968  C CD2 . LEU   B 1 287 ? -31.415 13.281  33.613  1.00 34.12  ?  287 LEU   B CD2 1 
ATOM   5969  N N   . ALA   B 1 288 ? -26.342 12.222  35.062  1.00 29.18  ?  288 ALA   B N   1 
ATOM   5970  C CA  . ALA   B 1 288 ? -25.288 11.239  35.298  1.00 27.78  ?  288 ALA   B CA  1 
ATOM   5971  C C   . ALA   B 1 288 ? -25.272 10.771  36.747  1.00 30.46  ?  288 ALA   B C   1 
ATOM   5972  O O   . ALA   B 1 288 ? -24.963 9.603   37.019  1.00 27.69  ?  288 ALA   B O   1 
ATOM   5973  C CB  . ALA   B 1 288 ? -23.925 11.818  34.918  1.00 27.45  ?  288 ALA   B CB  1 
ATOM   5974  N N   . ARG   B 1 289 ? -25.592 11.663  37.688  1.00 27.81  ?  289 ARG   B N   1 
ATOM   5975  C CA  . ARG   B 1 289 ? -25.700 11.248  39.082  1.00 28.09  ?  289 ARG   B CA  1 
ATOM   5976  C C   . ARG   B 1 289 ? -26.840 10.260  39.271  1.00 27.65  ?  289 ARG   B C   1 
ATOM   5977  O O   . ARG   B 1 289 ? -26.727 9.314   40.061  1.00 28.16  ?  289 ARG   B O   1 
ATOM   5978  C CB  . ARG   B 1 289 ? -25.904 12.460  39.984  1.00 29.04  ?  289 ARG   B CB  1 
ATOM   5979  C CG  . ARG   B 1 289 ? -24.652 12.937  40.682  1.00 28.17  ?  289 ARG   B CG  1 
ATOM   5980  C CD  . ARG   B 1 289 ? -25.031 13.864  41.818  1.00 36.66  ?  289 ARG   B CD  1 
ATOM   5981  N NE  . ARG   B 1 289 ? -23.895 14.208  42.665  1.00 36.00  ?  289 ARG   B NE  1 
ATOM   5982  C CZ  . ARG   B 1 289 ? -23.976 15.002  43.723  1.00 32.01  ?  289 ARG   B CZ  1 
ATOM   5983  N NH1 . ARG   B 1 289 ? -25.125 15.552  44.085  1.00 28.89  ?  289 ARG   B NH1 1 
ATOM   5984  N NH2 . ARG   B 1 289 ? -22.878 15.256  44.431  1.00 29.24  ?  289 ARG   B NH2 1 
ATOM   5985  N N   . GLN   B 1 290 ? -27.950 10.462  38.551  1.00 28.61  ?  290 GLN   B N   1 
ATOM   5986  C CA  . GLN   B 1 290 ? -29.099 9.577   38.693  1.00 30.20  ?  290 GLN   B CA  1 
ATOM   5987  C C   . GLN   B 1 290 ? -28.817 8.192   38.124  1.00 28.71  ?  290 GLN   B C   1 
ATOM   5988  O O   . GLN   B 1 290 ? -29.362 7.202   38.621  1.00 27.30  ?  290 GLN   B O   1 
ATOM   5989  C CB  . GLN   B 1 290 ? -30.328 10.204  38.030  1.00 34.10  ?  290 GLN   B CB  1 
ATOM   5990  C CG  . GLN   B 1 290 ? -30.893 11.405  38.799  1.00 38.73  ?  290 GLN   B CG  1 
ATOM   5991  C CD  . GLN   B 1 290 ? -31.866 12.244  37.973  1.00 49.88  ?  290 GLN   B CD  1 
ATOM   5992  O OE1 . GLN   B 1 290 ? -32.151 11.932  36.812  1.00 45.08  ?  290 GLN   B OE1 1 
ATOM   5993  N NE2 . GLN   B 1 290 ? -32.380 13.317  38.574  1.00 46.66  ?  290 GLN   B NE2 1 
ATOM   5994  N N   . ARG   B 1 291 ? -27.968 8.095   37.098  1.00 28.15  ?  291 ARG   B N   1 
ATOM   5995  C CA  . ARG   B 1 291 ? -27.560 6.781   36.613  1.00 27.03  ?  291 ARG   B CA  1 
ATOM   5996  C C   . ARG   B 1 291 ? -26.461 6.167   37.474  1.00 28.80  ?  291 ARG   B C   1 
ATOM   5997  O O   . ARG   B 1 291 ? -26.397 4.940   37.612  1.00 28.81  ?  291 ARG   B O   1 
ATOM   5998  C CB  . ARG   B 1 291 ? -27.093 6.867   35.155  1.00 29.86  ?  291 ARG   B CB  1 
ATOM   5999  C CG  . ARG   B 1 291 ? -26.776 5.498   34.575  1.00 30.25  ?  291 ARG   B CG  1 
ATOM   6000  C CD  . ARG   B 1 291 ? -26.653 5.481   33.074  1.00 28.28  ?  291 ARG   B CD  1 
ATOM   6001  N NE  . ARG   B 1 291 ? -26.322 4.137   32.617  1.00 26.95  ?  291 ARG   B NE  1 
ATOM   6002  C CZ  . ARG   B 1 291 ? -27.216 3.193   32.353  1.00 32.31  ?  291 ARG   B CZ  1 
ATOM   6003  N NH1 . ARG   B 1 291 ? -28.516 3.419   32.460  1.00 27.32  ?  291 ARG   B NH1 1 
ATOM   6004  N NH2 . ARG   B 1 291 ? -26.794 1.992   31.967  1.00 33.63  ?  291 ARG   B NH2 1 
ATOM   6005  N N   . CYS   B 1 292 ? -25.594 6.994   38.062  1.00 28.25  ?  292 CYS   B N   1 
ATOM   6006  C CA  . CYS   B 1 292 ? -24.525 6.470   38.907  1.00 26.16  ?  292 CYS   B CA  1 
ATOM   6007  C C   . CYS   B 1 292 ? -25.070 5.611   40.046  1.00 26.88  ?  292 CYS   B C   1 
ATOM   6008  O O   . CYS   B 1 292 ? -24.466 4.591   40.399  1.00 25.05  ?  292 CYS   B O   1 
ATOM   6009  C CB  . CYS   B 1 292 ? -23.684 7.622   39.458  1.00 23.04  ?  292 CYS   B CB  1 
ATOM   6010  S SG  . CYS   B 1 292 ? -22.393 7.126   40.655  1.00 24.88  ?  292 CYS   B SG  1 
ATOM   6011  N N   . VAL   B 1 293 ? -26.223 5.978   40.607  1.00 28.36  ?  293 VAL   B N   1 
ATOM   6012  C CA  . VAL   B 1 293 ? -26.714 5.341   41.833  1.00 25.16  ?  293 VAL   B CA  1 
ATOM   6013  C C   . VAL   B 1 293 ? -27.087 3.873   41.622  1.00 25.31  ?  293 VAL   B C   1 
ATOM   6014  O O   . VAL   B 1 293 ? -26.679 3.030   42.435  1.00 21.36  ?  293 VAL   B O   1 
ATOM   6015  C CB  . VAL   B 1 293 ? -27.892 6.131   42.428  1.00 25.97  ?  293 VAL   B CB  1 
ATOM   6016  C CG1 . VAL   B 1 293 ? -28.585 5.315   43.497  1.00 28.79  ?  293 VAL   B CG1 1 
ATOM   6017  C CG2 . VAL   B 1 293 ? -27.396 7.448   43.002  1.00 29.92  ?  293 VAL   B CG2 1 
ATOM   6018  N N   . PRO   B 1 294 ? -27.853 3.500   40.583  1.00 24.51  ?  294 PRO   B N   1 
ATOM   6019  C CA  . PRO   B 1 294 ? -28.114 2.066   40.375  1.00 23.44  ?  294 PRO   B CA  1 
ATOM   6020  C C   . PRO   B 1 294 ? -26.893 1.290   39.932  1.00 24.27  ?  294 PRO   B C   1 
ATOM   6021  O O   . PRO   B 1 294 ? -26.749 0.120   40.308  1.00 28.44  ?  294 PRO   B O   1 
ATOM   6022  C CB  . PRO   B 1 294 ? -29.192 2.047   39.280  1.00 24.39  ?  294 PRO   B CB  1 
ATOM   6023  C CG  . PRO   B 1 294 ? -29.716 3.409   39.210  1.00 27.69  ?  294 PRO   B CG  1 
ATOM   6024  C CD  . PRO   B 1 294 ? -28.615 4.316   39.622  1.00 27.18  ?  294 PRO   B CD  1 
ATOM   6025  N N   . MET   B 1 295 ? -26.004 1.908   39.153  1.00 22.89  ?  295 MET   B N   1 
ATOM   6026  C CA  . MET   B 1 295 ? -24.977 1.186   38.411  1.00 23.61  ?  295 MET   B CA  1 
ATOM   6027  C C   . MET   B 1 295 ? -23.666 1.054   39.170  1.00 25.64  ?  295 MET   B C   1 
ATOM   6028  O O   . MET   B 1 295 ? -23.033 -0.008  39.132  1.00 23.12  ?  295 MET   B O   1 
ATOM   6029  C CB  . MET   B 1 295 ? -24.716 1.890   37.075  1.00 25.11  ?  295 MET   B CB  1 
ATOM   6030  C CG  . MET   B 1 295 ? -25.897 1.858   36.128  1.00 30.14  ?  295 MET   B CG  1 
ATOM   6031  S SD  . MET   B 1 295 ? -26.294 0.177   35.624  1.00 31.69  ?  295 MET   B SD  1 
ATOM   6032  C CE  . MET   B 1 295 ? -27.811 0.460   34.738  1.00 30.31  ?  295 MET   B CE  1 
ATOM   6033  N N   . GLU   B 1 296 ? -23.237 2.122   39.840  1.00 24.42  ?  296 GLU   B N   1 
ATOM   6034  C CA  . GLU   B 1 296 ? -21.935 2.174   40.485  1.00 22.29  ?  296 GLU   B CA  1 
ATOM   6035  C C   . GLU   B 1 296 ? -22.049 2.247   42.002  1.00 24.87  ?  296 GLU   B C   1 
ATOM   6036  O O   . GLU   B 1 296 ? -21.491 1.403   42.712  1.00 23.76  ?  296 GLU   B O   1 
ATOM   6037  C CB  . GLU   B 1 296 ? -21.151 3.373   39.939  1.00 21.00  ?  296 GLU   B CB  1 
ATOM   6038  C CG  . GLU   B 1 296 ? -20.842 3.237   38.456  1.00 21.97  ?  296 GLU   B CG  1 
ATOM   6039  C CD  . GLU   B 1 296 ? -19.757 2.193   38.190  1.00 24.45  ?  296 GLU   B CD  1 
ATOM   6040  O OE1 . GLU   B 1 296 ? -18.784 2.141   38.966  1.00 27.19  ?  296 GLU   B OE1 1 
ATOM   6041  O OE2 . GLU   B 1 296 ? -19.871 1.429   37.206  1.00 29.34  ?  296 GLU   B OE2 1 
ATOM   6042  N N   . GLY   B 1 297 ? -22.775 3.230   42.510  1.00 20.84  ?  297 GLY   B N   1 
ATOM   6043  C CA  . GLY   B 1 297 ? -22.923 3.411   43.937  1.00 24.34  ?  297 GLY   B CA  1 
ATOM   6044  C C   . GLY   B 1 297 ? -23.404 4.821   44.211  1.00 24.59  ?  297 GLY   B C   1 
ATOM   6045  O O   . GLY   B 1 297 ? -23.767 5.562   43.296  1.00 26.77  ?  297 GLY   B O   1 
ATOM   6046  N N   . PHE   B 1 298 ? -23.394 5.177   45.489  1.00 26.00  ?  298 PHE   B N   1 
ATOM   6047  C CA  . PHE   B 1 298 ? -23.754 6.538   45.842  1.00 23.96  ?  298 PHE   B CA  1 
ATOM   6048  C C   . PHE   B 1 298 ? -22.774 7.512   45.201  1.00 25.73  ?  298 PHE   B C   1 
ATOM   6049  O O   . PHE   B 1 298 ? -21.623 7.175   44.905  1.00 25.70  ?  298 PHE   B O   1 
ATOM   6050  C CB  . PHE   B 1 298 ? -23.786 6.722   47.358  1.00 24.13  ?  298 PHE   B CB  1 
ATOM   6051  C CG  . PHE   B 1 298 ? -24.369 8.025   47.781  1.00 20.37  ?  298 PHE   B CG  1 
ATOM   6052  C CD1 . PHE   B 1 298 ? -25.650 8.379   47.388  1.00 26.78  ?  298 PHE   B CD1 1 
ATOM   6053  C CD2 . PHE   B 1 298 ? -23.638 8.907   48.552  1.00 21.31  ?  298 PHE   B CD2 1 
ATOM   6054  C CE1 . PHE   B 1 298 ? -26.200 9.584   47.766  1.00 26.22  ?  298 PHE   B CE1 1 
ATOM   6055  C CE2 . PHE   B 1 298 ? -24.183 10.113  48.942  1.00 26.77  ?  298 PHE   B CE2 1 
ATOM   6056  C CZ  . PHE   B 1 298 ? -25.464 10.455  48.541  1.00 30.61  ?  298 PHE   B CZ  1 
ATOM   6057  N N   . VAL   B 1 299 ? -23.248 8.736   44.971  1.00 24.39  ?  299 VAL   B N   1 
ATOM   6058  C CA  . VAL   B 1 299 ? -22.521 9.674   44.129  1.00 21.28  ?  299 VAL   B CA  1 
ATOM   6059  C C   . VAL   B 1 299 ? -21.263 10.231  44.774  1.00 24.20  ?  299 VAL   B C   1 
ATOM   6060  O O   . VAL   B 1 299 ? -20.489 10.913  44.091  1.00 23.99  ?  299 VAL   B O   1 
ATOM   6061  C CB  . VAL   B 1 299 ? -23.483 10.806  43.733  1.00 29.10  ?  299 VAL   B CB  1 
ATOM   6062  C CG1 . VAL   B 1 299 ? -24.728 10.215  43.078  1.00 27.93  ?  299 VAL   B CG1 1 
ATOM   6063  C CG2 . VAL   B 1 299 ? -23.872 11.609  44.965  1.00 27.16  ?  299 VAL   B CG2 1 
ATOM   6064  N N   . THR   B 1 300 ? -21.025 9.971   46.062  1.00 20.95  ?  300 THR   B N   1 
ATOM   6065  C CA  . THR   B 1 300 ? -19.806 10.440  46.712  1.00 21.60  ?  300 THR   B CA  1 
ATOM   6066  C C   . THR   B 1 300 ? -18.765 9.342   46.901  1.00 24.78  ?  300 THR   B C   1 
ATOM   6067  O O   . THR   B 1 300 ? -17.709 9.600   47.496  1.00 22.89  ?  300 THR   B O   1 
ATOM   6068  C CB  . THR   B 1 300 ? -20.128 11.090  48.059  1.00 18.28  ?  300 THR   B CB  1 
ATOM   6069  O OG1 . THR   B 1 300 ? -20.758 10.134  48.919  1.00 20.35  ?  300 THR   B OG1 1 
ATOM   6070  C CG2 . THR   B 1 300 ? -21.057 12.280  47.853  1.00 20.72  ?  300 THR   B CG2 1 
ATOM   6071  N N   . TYR   B 1 301 ? -19.028 8.127   46.419  1.00 21.71  ?  301 TYR   B N   1 
ATOM   6072  C CA  . TYR   B 1 301 ? -17.976 7.132   46.269  1.00 21.57  ?  301 TYR   B CA  1 
ATOM   6073  C C   . TYR   B 1 301 ? -18.040 6.382   44.945  1.00 19.87  ?  301 TYR   B C   1 
ATOM   6074  O O   . TYR   B 1 301 ? -16.998 5.904   44.486  1.00 20.98  ?  301 TYR   B O   1 
ATOM   6075  C CB  . TYR   B 1 301 ? -17.984 6.130   47.443  1.00 18.53  ?  301 TYR   B CB  1 
ATOM   6076  C CG  . TYR   B 1 301 ? -19.134 5.145   47.447  1.00 23.46  ?  301 TYR   B CG  1 
ATOM   6077  C CD1 . TYR   B 1 301 ? -19.036 3.925   46.783  1.00 22.72  ?  301 TYR   B CD1 1 
ATOM   6078  C CD2 . TYR   B 1 301 ? -20.309 5.420   48.132  1.00 22.30  ?  301 TYR   B CD2 1 
ATOM   6079  C CE1 . TYR   B 1 301 ? -20.084 3.021   46.781  1.00 18.84  ?  301 TYR   B CE1 1 
ATOM   6080  C CE2 . TYR   B 1 301 ? -21.354 4.515   48.141  1.00 23.67  ?  301 TYR   B CE2 1 
ATOM   6081  C CZ  . TYR   B 1 301 ? -21.237 3.322   47.455  1.00 21.00  ?  301 TYR   B CZ  1 
ATOM   6082  O OH  . TYR   B 1 301 ? -22.277 2.420   47.453  1.00 23.41  ?  301 TYR   B OH  1 
ATOM   6083  N N   . GLY   B 1 302 ? -19.206 6.272   44.314  1.00 21.36  ?  302 GLY   B N   1 
ATOM   6084  C CA  . GLY   B 1 302 ? -19.263 5.777   42.943  1.00 19.22  ?  302 GLY   B CA  1 
ATOM   6085  C C   . GLY   B 1 302 ? -18.622 4.426   42.729  1.00 15.99  ?  302 GLY   B C   1 
ATOM   6086  O O   . GLY   B 1 302 ? -18.012 4.186   41.681  1.00 20.51  ?  302 GLY   B O   1 
ATOM   6087  N N   . GLY   B 1 303 ? -18.757 3.529   43.693  1.00 18.38  ?  303 GLY   B N   1 
ATOM   6088  C CA  . GLY   B 1 303 ? -18.175 2.211   43.569  1.00 19.77  ?  303 GLY   B CA  1 
ATOM   6089  C C   . GLY   B 1 303 ? -16.720 2.107   43.958  1.00 18.71  ?  303 GLY   B C   1 
ATOM   6090  O O   . GLY   B 1 303 ? -16.079 1.094   43.638  1.00 18.63  ?  303 GLY   B O   1 
ATOM   6091  N N   . LEU   B 1 304 ? -16.169 3.116   44.629  1.00 18.05  ?  304 LEU   B N   1 
ATOM   6092  C CA  . LEU   B 1 304 ? -14.801 3.072   45.125  1.00 19.00  ?  304 LEU   B CA  1 
ATOM   6093  C C   . LEU   B 1 304 ? -14.802 3.105   46.647  1.00 19.16  ?  304 LEU   B C   1 
ATOM   6094  O O   . LEU   B 1 304 ? -15.578 3.842   47.259  1.00 15.29  ?  304 LEU   B O   1 
ATOM   6095  C CB  . LEU   B 1 304 ? -13.975 4.249   44.579  1.00 23.60  ?  304 LEU   B CB  1 
ATOM   6096  C CG  . LEU   B 1 304 ? -13.554 4.244   43.105  1.00 19.60  ?  304 LEU   B CG  1 
ATOM   6097  C CD1 . LEU   B 1 304 ? -12.884 5.550   42.753  1.00 17.64  ?  304 LEU   B CD1 1 
ATOM   6098  C CD2 . LEU   B 1 304 ? -12.606 3.100   42.842  1.00 17.65  ?  304 LEU   B CD2 1 
ATOM   6099  N N   . ALA   B 1 305 ? -13.945 2.291   47.258  1.00 19.65  ?  305 ALA   B N   1 
ATOM   6100  C CA  . ALA   B 1 305 ? -13.641 2.482   48.667  1.00 17.25  ?  305 ALA   B CA  1 
ATOM   6101  C C   . ALA   B 1 305 ? -13.027 3.862   48.873  1.00 15.57  ?  305 ALA   B C   1 
ATOM   6102  O O   . ALA   B 1 305 ? -12.339 4.389   48.001  1.00 13.37  ?  305 ALA   B O   1 
ATOM   6103  C CB  . ALA   B 1 305 ? -12.680 1.399   49.157  1.00 17.67  ?  305 ALA   B CB  1 
ATOM   6104  N N   . GLY   B 1 306 ? -13.301 4.467   50.030  1.00 15.60  ?  306 GLY   B N   1 
ATOM   6105  C CA  . GLY   B 1 306 ? -12.726 5.778   50.313  1.00 15.81  ?  306 GLY   B CA  1 
ATOM   6106  C C   . GLY   B 1 306 ? -11.216 5.826   50.144  1.00 16.08  ?  306 GLY   B C   1 
ATOM   6107  O O   . GLY   B 1 306 ? -10.661 6.834   49.693  1.00 15.22  ?  306 GLY   B O   1 
ATOM   6108  N N   . ARG   B 1 307 ? -10.526 4.733   50.491  1.00 16.13  ?  307 ARG   B N   1 
ATOM   6109  C CA  . ARG   B 1 307 ? -9.074  4.720   50.349  1.00 13.45  ?  307 ARG   B CA  1 
ATOM   6110  C C   . ARG   B 1 307 ? -8.648  4.861   48.892  1.00 14.70  ?  307 ARG   B C   1 
ATOM   6111  O O   . ARG   B 1 307 ? -7.589  5.429   48.603  1.00 12.86  ?  307 ARG   B O   1 
ATOM   6112  C CB  . ARG   B 1 307 ? -8.492  3.446   50.966  1.00 14.19  ?  307 ARG   B CB  1 
ATOM   6113  C CG  . ARG   B 1 307 ? -9.132  2.152   50.498  1.00 14.90  ?  307 ARG   B CG  1 
ATOM   6114  C CD  . ARG   B 1 307 ? -8.304  0.929   50.911  1.00 15.58  ?  307 ARG   B CD  1 
ATOM   6115  N NE  . ARG   B 1 307 ? -8.974  -0.309  50.531  1.00 17.05  ?  307 ARG   B NE  1 
ATOM   6116  C CZ  . ARG   B 1 307 ? -9.873  -0.925  51.288  1.00 19.04  ?  307 ARG   B CZ  1 
ATOM   6117  N NH1 . ARG   B 1 307 ? -10.198 -0.465  52.485  1.00 14.90  ?  307 ARG   B NH1 1 
ATOM   6118  N NH2 . ARG   B 1 307 ? -10.469 -2.024  50.829  1.00 17.21  ?  307 ARG   B NH2 1 
ATOM   6119  N N   . ASP   B 1 308 ? -9.461  4.386   47.955  1.00 16.46  ?  308 ASP   B N   1 
ATOM   6120  C CA  . ASP   B 1 308 ? -9.039  4.489   46.564  1.00 15.50  ?  308 ASP   B CA  1 
ATOM   6121  C C   . ASP   B 1 308 ? -9.246  5.899   46.026  1.00 16.26  ?  308 ASP   B C   1 
ATOM   6122  O O   . ASP   B 1 308 ? -8.405  6.403   45.273  1.00 16.40  ?  308 ASP   B O   1 
ATOM   6123  C CB  . ASP   B 1 308 ? -9.759  3.438   45.727  1.00 13.53  ?  308 ASP   B CB  1 
ATOM   6124  C CG  . ASP   B 1 308 ? -9.276  2.033   46.051  1.00 16.65  ?  308 ASP   B CG  1 
ATOM   6125  O OD1 . ASP   B 1 308 ? -8.055  1.764   45.934  1.00 18.17  ?  308 ASP   B OD1 1 
ATOM   6126  O OD2 . ASP   B 1 308 ? -10.111 1.198   46.446  1.00 21.33  ?  308 ASP   B OD2 1 
ATOM   6127  N N   . MET   B 1 309 ? -10.329 6.570   46.432  1.00 16.67  ?  309 MET   B N   1 
ATOM   6128  C CA  . MET   B 1 309 ? -10.447 7.998   46.137  1.00 14.29  ?  309 MET   B CA  1 
ATOM   6129  C C   . MET   B 1 309 ? -9.284  8.775   46.739  1.00 14.52  ?  309 MET   B C   1 
ATOM   6130  O O   . MET   B 1 309 ? -8.785  9.730   46.133  1.00 12.90  ?  309 MET   B O   1 
ATOM   6131  C CB  . MET   B 1 309 ? -11.772 8.546   46.666  1.00 18.93  ?  309 MET   B CB  1 
ATOM   6132  C CG  . MET   B 1 309 ? -13.001 8.130   45.878  1.00 17.61  ?  309 MET   B CG  1 
ATOM   6133  S SD  . MET   B 1 309 ? -14.442 9.041   46.439  1.00 25.11  ?  309 MET   B SD  1 
ATOM   6134  C CE  . MET   B 1 309 ? -14.893 8.116   47.901  1.00 15.57  ?  309 MET   B CE  1 
ATOM   6135  N N   . ALA   B 1 310 ? -8.844  8.386   47.942  1.00 16.34  ?  310 ALA   B N   1 
ATOM   6136  C CA  . ALA   B 1 310 ? -7.681  9.021   48.555  1.00 16.19  ?  310 ALA   B CA  1 
ATOM   6137  C C   . ALA   B 1 310 ? -6.429  8.787   47.724  1.00 17.85  ?  310 ALA   B C   1 
ATOM   6138  O O   . ALA   B 1 310 ? -5.632  9.711   47.509  1.00 16.24  ?  310 ALA   B O   1 
ATOM   6139  C CB  . ALA   B 1 310 ? -7.479  8.491   49.977  1.00 18.21  ?  310 ALA   B CB  1 
ATOM   6140  N N   . ALA   B 1 311 ? -6.230  7.545   47.261  1.00 13.77  ?  311 ALA   B N   1 
ATOM   6141  C CA  . ALA   B 1 311 ? -5.086  7.245   46.411  1.00 13.47  ?  311 ALA   B CA  1 
ATOM   6142  C C   . ALA   B 1 311 ? -5.178  7.971   45.076  1.00 12.99  ?  311 ALA   B C   1 
ATOM   6143  O O   . ALA   B 1 311 ? -4.147  8.342   44.503  1.00 14.98  ?  311 ALA   B O   1 
ATOM   6144  C CB  . ALA   B 1 311 ? -4.980  5.734   46.194  1.00 12.10  ?  311 ALA   B CB  1 
ATOM   6145  N N   . MET   B 1 312 ? -6.397  8.188   44.575  1.00 14.79  ?  312 MET   B N   1 
ATOM   6146  C CA  . MET   B 1 312 ? -6.578  8.870   43.295  1.00 17.25  ?  312 MET   B CA  1 
ATOM   6147  C C   . MET   B 1 312 ? -6.165  10.327  43.380  1.00 13.80  ?  312 MET   B C   1 
ATOM   6148  O O   . MET   B 1 312 ? -5.573  10.863  42.442  1.00 17.06  ?  312 MET   B O   1 
ATOM   6149  C CB  . MET   B 1 312 ? -8.036  8.773   42.838  1.00 15.74  ?  312 MET   B CB  1 
ATOM   6150  C CG  . MET   B 1 312 ? -8.280  9.316   41.411  1.00 16.01  ?  312 MET   B CG  1 
ATOM   6151  S SD  . MET   B 1 312 ? -9.980  9.121   40.805  1.00 21.95  ?  312 MET   B SD  1 
ATOM   6152  C CE  . MET   B 1 312 ? -10.235 7.368   41.044  1.00 19.18  ?  312 MET   B CE  1 
ATOM   6153  N N   . VAL   B 1 313 ? -6.500  10.992  44.484  1.00 16.80  ?  313 VAL   B N   1 
ATOM   6154  C CA  . VAL   B 1 313 ? -6.148  12.400  44.630  1.00 17.30  ?  313 VAL   B CA  1 
ATOM   6155  C C   . VAL   B 1 313 ? -4.639  12.571  44.613  1.00 18.24  ?  313 VAL   B C   1 
ATOM   6156  O O   . VAL   B 1 313 ? -4.115  13.528  44.028  1.00 19.96  ?  313 VAL   B O   1 
ATOM   6157  C CB  . VAL   B 1 313 ? -6.770  12.970  45.915  1.00 18.88  ?  313 VAL   B CB  1 
ATOM   6158  C CG1 . VAL   B 1 313 ? -6.350  14.413  46.108  1.00 20.59  ?  313 VAL   B CG1 1 
ATOM   6159  C CG2 . VAL   B 1 313 ? -8.266  12.850  45.857  1.00 16.92  ?  313 VAL   B CG2 1 
ATOM   6160  N N   . GLN   B 1 314 ? -3.914  11.645  45.249  1.00 18.00  ?  314 GLN   B N   1 
ATOM   6161  C CA  . GLN   B 1 314 ? -2.460  11.726  45.278  1.00 17.80  ?  314 GLN   B CA  1 
ATOM   6162  C C   . GLN   B 1 314 ? -1.856  11.266  43.958  1.00 18.23  ?  314 GLN   B C   1 
ATOM   6163  O O   . GLN   B 1 314 ? -0.924  11.899  43.442  1.00 20.09  ?  314 GLN   B O   1 
ATOM   6164  C CB  . GLN   B 1 314 ? -1.909  10.901  46.444  1.00 17.05  ?  314 GLN   B CB  1 
ATOM   6165  C CG  . GLN   B 1 314 ? -0.388  10.859  46.523  1.00 17.60  ?  314 GLN   B CG  1 
ATOM   6166  C CD  . GLN   B 1 314 ? 0.229   12.211  46.865  1.00 20.09  ?  314 GLN   B CD  1 
ATOM   6167  O OE1 . GLN   B 1 314 ? -0.398  13.037  47.523  1.00 26.33  ?  314 GLN   B OE1 1 
ATOM   6168  N NE2 . GLN   B 1 314 ? 1.461   12.440  46.415  1.00 17.08  ?  314 GLN   B NE2 1 
ATOM   6169  N N   . GLY   B 1 315 ? -2.382  10.177  43.389  1.00 20.25  ?  315 GLY   B N   1 
ATOM   6170  C CA  . GLY   B 1 315 ? -1.872  9.702   42.109  1.00 18.95  ?  315 GLY   B CA  1 
ATOM   6171  C C   . GLY   B 1 315 ? -2.123  10.671  40.969  1.00 21.27  ?  315 GLY   B C   1 
ATOM   6172  O O   . GLY   B 1 315 ? -1.308  10.781  40.048  1.00 21.23  ?  315 GLY   B O   1 
ATOM   6173  N N   . LEU   B 1 316 ? -3.259  11.374  41.000  1.00 18.95  ?  316 LEU   B N   1 
ATOM   6174  C CA  . LEU   B 1 316 ? -3.516  12.409  40.000  1.00 20.03  ?  316 LEU   B CA  1 
ATOM   6175  C C   . LEU   B 1 316 ? -2.405  13.446  39.989  1.00 20.58  ?  316 LEU   B C   1 
ATOM   6176  O O   . LEU   B 1 316 ? -1.989  13.916  38.920  1.00 19.91  ?  316 LEU   B O   1 
ATOM   6177  C CB  . LEU   B 1 316 ? -4.863  13.084  40.258  1.00 18.01  ?  316 LEU   B CB  1 
ATOM   6178  C CG  . LEU   B 1 316 ? -6.088  12.409  39.650  1.00 16.96  ?  316 LEU   B CG  1 
ATOM   6179  C CD1 . LEU   B 1 316 ? -7.369  12.969  40.253  1.00 16.17  ?  316 LEU   B CD1 1 
ATOM   6180  C CD2 . LEU   B 1 316 ? -6.085  12.578  38.136  1.00 17.75  ?  316 LEU   B CD2 1 
ATOM   6181  N N   . GLU   B 1 317 ? -1.906  13.804  41.173  1.00 23.08  ?  317 GLU   B N   1 
ATOM   6182  C CA  . GLU   B 1 317 ? -0.809  14.763  41.272  1.00 24.61  ?  317 GLU   B CA  1 
ATOM   6183  C C   . GLU   B 1 317 ? 0.501   14.162  40.775  1.00 19.29  ?  317 GLU   B C   1 
ATOM   6184  O O   . GLU   B 1 317 ? 1.218   14.782  39.980  1.00 23.81  ?  317 GLU   B O   1 
ATOM   6185  C CB  . GLU   B 1 317 ? -0.664  15.244  42.719  1.00 22.11  ?  317 GLU   B CB  1 
ATOM   6186  C CG  . GLU   B 1 317 ? 0.532   16.163  42.947  1.00 26.80  ?  317 GLU   B CG  1 
ATOM   6187  C CD  . GLU   B 1 317 ? 0.396   17.501  42.235  1.00 27.37  ?  317 GLU   B CD  1 
ATOM   6188  O OE1 . GLU   B 1 317 ? -0.723  17.848  41.791  1.00 28.23  ?  317 GLU   B OE1 1 
ATOM   6189  O OE2 . GLU   B 1 317 ? 1.418   18.210  42.122  1.00 31.34  ?  317 GLU   B OE2 1 
ATOM   6190  N N   . GLU   B 1 318 ? 0.824   12.949  41.226  1.00 18.90  ?  318 GLU   B N   1 
ATOM   6191  C CA  . GLU   B 1 318 ? 2.099   12.335  40.861  1.00 19.36  ?  318 GLU   B CA  1 
ATOM   6192  C C   . GLU   B 1 318 ? 2.192   12.070  39.367  1.00 20.42  ?  318 GLU   B C   1 
ATOM   6193  O O   . GLU   B 1 318 ? 3.282   12.148  38.786  1.00 18.68  ?  318 GLU   B O   1 
ATOM   6194  C CB  . GLU   B 1 318 ? 2.296   11.032  41.635  1.00 17.53  ?  318 GLU   B CB  1 
ATOM   6195  C CG  . GLU   B 1 318 ? 2.401   11.208  43.128  1.00 19.08  ?  318 GLU   B CG  1 
ATOM   6196  C CD  . GLU   B 1 318 ? 2.738   9.909   43.841  1.00 24.22  ?  318 GLU   B CD  1 
ATOM   6197  O OE1 . GLU   B 1 318 ? 2.987   8.894   43.146  1.00 21.86  ?  318 GLU   B OE1 1 
ATOM   6198  O OE2 . GLU   B 1 318 ? 2.759   9.904   45.091  1.00 17.33  ?  318 GLU   B OE2 1 
ATOM   6199  N N   . GLY   B 1 319 ? 1.072   11.753  38.728  1.00 17.72  ?  319 GLY   B N   1 
ATOM   6200  C CA  . GLY   B 1 319 ? 1.111   11.440  37.317  1.00 19.77  ?  319 GLY   B CA  1 
ATOM   6201  C C   . GLY   B 1 319 ? 1.333   12.632  36.420  1.00 19.81  ?  319 GLY   B C   1 
ATOM   6202  O O   . GLY   B 1 319 ? 1.579   12.445  35.224  1.00 24.19  ?  319 GLY   B O   1 
ATOM   6203  N N   . THR   B 1 320 ? 1.236   13.843  36.958  1.00 18.94  ?  320 THR   B N   1 
ATOM   6204  C CA  . THR   B 1 320 ? 1.516   15.046  36.188  1.00 21.34  ?  320 THR   B CA  1 
ATOM   6205  C C   . THR   B 1 320 ? 2.975   15.470  36.269  1.00 21.28  ?  320 THR   B C   1 
ATOM   6206  O O   . THR   B 1 320 ? 3.378   16.381  35.538  1.00 21.99  ?  320 THR   B O   1 
ATOM   6207  C CB  . THR   B 1 320 ? 0.645   16.214  36.670  1.00 23.02  ?  320 THR   B CB  1 
ATOM   6208  O OG1 . THR   B 1 320 ? 0.984   16.524  38.028  1.00 23.08  ?  320 THR   B OG1 1 
ATOM   6209  C CG2 . THR   B 1 320 ? -0.846  15.875  36.581  1.00 18.95  ?  320 THR   B CG2 1 
ATOM   6210  N N   . GLU   B 1 321 ? 3.765   14.857  37.147  1.00 20.42  ?  321 GLU   B N   1 
ATOM   6211  C CA  . GLU   B 1 321 ? 5.127   15.319  37.380  1.00 19.35  ?  321 GLU   B CA  1 
ATOM   6212  C C   . GLU   B 1 321 ? 5.990   14.989  36.170  1.00 20.80  ?  321 GLU   B C   1 
ATOM   6213  O O   . GLU   B 1 321 ? 6.132   13.820  35.794  1.00 25.15  ?  321 GLU   B O   1 
ATOM   6214  C CB  . GLU   B 1 321 ? 5.682   14.697  38.661  1.00 19.88  ?  321 GLU   B CB  1 
ATOM   6215  C CG  . GLU   B 1 321 ? 4.901   15.125  39.911  1.00 21.67  ?  321 GLU   B CG  1 
ATOM   6216  C CD  . GLU   B 1 321 ? 5.388   14.470  41.208  1.00 33.41  ?  321 GLU   B CD  1 
ATOM   6217  O OE1 . GLU   B 1 321 ? 6.378   13.700  41.174  1.00 29.93  ?  321 GLU   B OE1 1 
ATOM   6218  O OE2 . GLU   B 1 321 ? 4.769   14.732  42.270  1.00 31.40  ?  321 GLU   B OE2 1 
ATOM   6219  N N   . GLU   B 1 322 ? 6.564   16.029  35.558  1.00 21.74  ?  322 GLU   B N   1 
ATOM   6220  C CA  . GLU   B 1 322 ? 7.250   15.873  34.277  1.00 21.04  ?  322 GLU   B CA  1 
ATOM   6221  C C   . GLU   B 1 322 ? 8.450   14.940  34.378  1.00 22.14  ?  322 GLU   B C   1 
ATOM   6222  O O   . GLU   B 1 322 ? 8.715   14.160  33.454  1.00 21.37  ?  322 GLU   B O   1 
ATOM   6223  C CB  . GLU   B 1 322 ? 7.691   17.238  33.768  1.00 17.73  ?  322 GLU   B CB  1 
ATOM   6224  C CG  . GLU   B 1 322 ? 8.471   17.198  32.491  1.00 23.98  ?  322 GLU   B CG  1 
ATOM   6225  C CD  . GLU   B 1 322 ? 8.709   18.588  31.950  1.00 26.94  ?  322 GLU   B CD  1 
ATOM   6226  O OE1 . GLU   B 1 322 ? 8.022   19.527  32.413  1.00 29.20  ?  322 GLU   B OE1 1 
ATOM   6227  O OE2 . GLU   B 1 322 ? 9.582   18.744  31.075  1.00 35.43  ?  322 GLU   B OE2 1 
ATOM   6228  N N   . GLU   B 1 323 ? 9.201   15.019  35.481  1.00 18.28  ?  323 GLU   B N   1 
ATOM   6229  C CA  A GLU   B 1 323 ? 10.369  14.159  35.614  0.57 20.51  ?  323 GLU   B CA  1 
ATOM   6230  C CA  B GLU   B 1 323 ? 10.368  14.158  35.657  0.43 20.53  ?  323 GLU   B CA  1 
ATOM   6231  C C   . GLU   B 1 323 ? 9.972   12.687  35.678  1.00 22.16  ?  323 GLU   B C   1 
ATOM   6232  O O   . GLU   B 1 323 ? 10.720  11.827  35.196  1.00 21.02  ?  323 GLU   B O   1 
ATOM   6233  C CB  A GLU   B 1 323 ? 11.200  14.573  36.833  0.57 21.14  ?  323 GLU   B CB  1 
ATOM   6234  C CB  B GLU   B 1 323 ? 11.107  14.542  36.946  0.43 21.19  ?  323 GLU   B CB  1 
ATOM   6235  C CG  A GLU   B 1 323 ? 10.501  14.450  38.180  0.57 23.83  ?  323 GLU   B CG  1 
ATOM   6236  C CG  B GLU   B 1 323 ? 12.531  14.016  37.055  0.43 22.79  ?  323 GLU   B CG  1 
ATOM   6237  C CD  A GLU   B 1 323 ? 9.638   15.657  38.553  0.57 24.86  ?  323 GLU   B CD  1 
ATOM   6238  C CD  B GLU   B 1 323 ? 13.185  14.313  38.405  0.43 27.83  ?  323 GLU   B CD  1 
ATOM   6239  O OE1 A GLU   B 1 323 ? 9.339   16.501  37.676  0.57 17.49  ?  323 GLU   B OE1 1 
ATOM   6240  O OE1 B GLU   B 1 323 ? 12.462  14.599  39.389  0.43 26.37  ?  323 GLU   B OE1 1 
ATOM   6241  O OE2 A GLU   B 1 323 ? 9.259   15.752  39.743  0.57 26.49  ?  323 GLU   B OE2 1 
ATOM   6242  O OE2 B GLU   B 1 323 ? 14.433  14.253  38.485  0.43 30.27  ?  323 GLU   B OE2 1 
ATOM   6243  N N   . TYR   B 1 324 ? 8.796   12.372  36.235  1.00 16.89  ?  324 TYR   B N   1 
ATOM   6244  C CA  . TYR   B 1 324 ? 8.310   10.999  36.158  1.00 15.91  ?  324 TYR   B CA  1 
ATOM   6245  C C   . TYR   B 1 324 ? 7.890   10.645  34.732  1.00 20.96  ?  324 TYR   B C   1 
ATOM   6246  O O   . TYR   B 1 324 ? 8.225   9.563   34.232  1.00 20.43  ?  324 TYR   B O   1 
ATOM   6247  C CB  . TYR   B 1 324 ? 7.139   10.780  37.129  1.00 21.37  ?  324 TYR   B CB  1 
ATOM   6248  C CG  . TYR   B 1 324 ? 6.156   9.757   36.592  1.00 19.40  ?  324 TYR   B CG  1 
ATOM   6249  C CD1 . TYR   B 1 324 ? 6.451   8.397   36.619  1.00 16.18  ?  324 TYR   B CD1 1 
ATOM   6250  C CD2 . TYR   B 1 324 ? 4.954   10.153  36.023  1.00 20.28  ?  324 TYR   B CD2 1 
ATOM   6251  C CE1 . TYR   B 1 324 ? 5.580   7.468   36.095  1.00 15.34  ?  324 TYR   B CE1 1 
ATOM   6252  C CE2 . TYR   B 1 324 ? 4.078   9.228   35.497  1.00 18.31  ?  324 TYR   B CE2 1 
ATOM   6253  C CZ  . TYR   B 1 324 ? 4.400   7.887   35.540  1.00 17.13  ?  324 TYR   B CZ  1 
ATOM   6254  O OH  . TYR   B 1 324 ? 3.530   6.964   35.016  1.00 21.25  ?  324 TYR   B OH  1 
ATOM   6255  N N   . LEU   B 1 325 ? 7.150   11.539  34.060  1.00 18.06  ?  325 LEU   B N   1 
ATOM   6256  C CA  . LEU   B 1 325 ? 6.673   11.242  32.710  1.00 18.81  ?  325 LEU   B CA  1 
ATOM   6257  C C   . LEU   B 1 325 ? 7.834   11.041  31.745  1.00 19.30  ?  325 LEU   B C   1 
ATOM   6258  O O   . LEU   B 1 325 ? 7.797   10.144  30.893  1.00 17.69  ?  325 LEU   B O   1 
ATOM   6259  C CB  . LEU   B 1 325 ? 5.759   12.361  32.212  1.00 18.92  ?  325 LEU   B CB  1 
ATOM   6260  C CG  . LEU   B 1 325 ? 4.354   12.434  32.807  1.00 16.69  ?  325 LEU   B CG  1 
ATOM   6261  C CD1 . LEU   B 1 325 ? 3.746   13.794  32.510  1.00 18.73  ?  325 LEU   B CD1 1 
ATOM   6262  C CD2 . LEU   B 1 325 ? 3.489   11.333  32.225  1.00 19.75  ?  325 LEU   B CD2 1 
ATOM   6263  N N   . HIS   B 1 326 ? 8.872   11.874  31.862  1.00 19.25  ?  326 HIS   B N   1 
ATOM   6264  C CA  . HIS   B 1 326 ? 10.065  11.721  31.036  1.00 17.65  ?  326 HIS   B CA  1 
ATOM   6265  C C   . HIS   B 1 326 ? 10.656  10.318  31.171  1.00 20.84  ?  326 HIS   B C   1 
ATOM   6266  O O   . HIS   B 1 326 ? 10.943  9.657   30.166  1.00 18.77  ?  326 HIS   B O   1 
ATOM   6267  C CB  . HIS   B 1 326 ? 11.086  12.789  31.429  1.00 17.92  ?  326 HIS   B CB  1 
ATOM   6268  C CG  . HIS   B 1 326 ? 12.340  12.763  30.610  1.00 21.98  ?  326 HIS   B CG  1 
ATOM   6269  N ND1 . HIS   B 1 326 ? 12.352  13.028  29.259  1.00 22.90  ?  326 HIS   B ND1 1 
ATOM   6270  C CD2 . HIS   B 1 326 ? 13.625  12.516  30.957  1.00 20.80  ?  326 HIS   B CD2 1 
ATOM   6271  C CE1 . HIS   B 1 326 ? 13.590  12.939  28.806  1.00 26.83  ?  326 HIS   B CE1 1 
ATOM   6272  N NE2 . HIS   B 1 326 ? 14.381  12.631  29.816  1.00 22.06  ?  326 HIS   B NE2 1 
ATOM   6273  N N   . TYR   B 1 327 ? 10.835  9.841   32.408  1.00 18.24  ?  327 TYR   B N   1 
ATOM   6274  C CA  A TYR   B 1 327 ? 11.364  8.493   32.604  0.65 18.15  ?  327 TYR   B CA  1 
ATOM   6275  C CA  B TYR   B 1 327 ? 11.358  8.493   32.619  0.35 17.92  ?  327 TYR   B CA  1 
ATOM   6276  C C   . TYR   B 1 327 ? 10.402  7.436   32.078  1.00 16.52  ?  327 TYR   B C   1 
ATOM   6277  O O   . TYR   B 1 327 ? 10.825  6.478   31.429  1.00 17.88  ?  327 TYR   B O   1 
ATOM   6278  C CB  A TYR   B 1 327 ? 11.665  8.247   34.085  0.65 20.67  ?  327 TYR   B CB  1 
ATOM   6279  C CB  B TYR   B 1 327 ? 11.621  8.251   34.108  0.35 20.58  ?  327 TYR   B CB  1 
ATOM   6280  C CG  A TYR   B 1 327 ? 11.249  6.872   34.577  0.65 20.42  ?  327 TYR   B CG  1 
ATOM   6281  C CG  B TYR   B 1 327 ? 11.741  6.780   34.451  0.35 20.43  ?  327 TYR   B CG  1 
ATOM   6282  C CD1 A TYR   B 1 327 ? 12.082  5.767   34.421  0.65 20.19  ?  327 TYR   B CD1 1 
ATOM   6283  C CD1 B TYR   B 1 327 ? 12.951  6.117   34.328  0.35 20.60  ?  327 TYR   B CD1 1 
ATOM   6284  C CD2 A TYR   B 1 327 ? 10.020  6.680   35.199  0.65 19.60  ?  327 TYR   B CD2 1 
ATOM   6285  C CD2 B TYR   B 1 327 ? 10.635  6.051   34.883  0.35 20.18  ?  327 TYR   B CD2 1 
ATOM   6286  C CE1 A TYR   B 1 327 ? 11.693  4.508   34.865  0.65 20.19  ?  327 TYR   B CE1 1 
ATOM   6287  C CE1 B TYR   B 1 327 ? 13.062  4.771   34.622  0.35 20.32  ?  327 TYR   B CE1 1 
ATOM   6288  C CE2 A TYR   B 1 327 ? 9.627   5.430   35.644  0.65 19.16  ?  327 TYR   B CE2 1 
ATOM   6289  C CE2 B TYR   B 1 327 ? 10.737  4.706   35.179  0.35 19.55  ?  327 TYR   B CE2 1 
ATOM   6290  C CZ  A TYR   B 1 327 ? 10.463  4.349   35.480  0.65 19.12  ?  327 TYR   B CZ  1 
ATOM   6291  C CZ  B TYR   B 1 327 ? 11.953  4.072   35.047  0.35 20.37  ?  327 TYR   B CZ  1 
ATOM   6292  O OH  A TYR   B 1 327 ? 10.056  3.112   35.938  0.65 16.34  ?  327 TYR   B OH  1 
ATOM   6293  O OH  B TYR   B 1 327 ? 12.059  2.734   35.349  0.35 21.21  ?  327 TYR   B OH  1 
ATOM   6294  N N   . ARG   B 1 328 ? 9.104   7.577   32.371  1.00 19.91  ?  328 ARG   B N   1 
ATOM   6295  C CA  . ARG   B 1 328 ? 8.134   6.563   31.965  1.00 16.58  ?  328 ARG   B CA  1 
ATOM   6296  C C   . ARG   B 1 328 ? 8.091   6.433   30.452  1.00 18.03  ?  328 ARG   B C   1 
ATOM   6297  O O   . ARG   B 1 328 ? 8.212   5.329   29.906  1.00 18.67  ?  328 ARG   B O   1 
ATOM   6298  C CB  . ARG   B 1 328 ? 6.745   6.909   32.516  1.00 19.81  ?  328 ARG   B CB  1 
ATOM   6299  C CG  . ARG   B 1 328 ? 5.679   5.795   32.403  1.00 17.07  ?  328 ARG   B CG  1 
ATOM   6300  C CD  . ARG   B 1 328 ? 5.162   5.598   30.971  1.00 14.90  ?  328 ARG   B CD  1 
ATOM   6301  N NE  . ARG   B 1 328 ? 3.819   5.037   30.907  1.00 18.65  ?  328 ARG   B NE  1 
ATOM   6302  C CZ  . ARG   B 1 328 ? 3.537   3.744   30.981  1.00 15.75  ?  328 ARG   B CZ  1 
ATOM   6303  N NH1 . ARG   B 1 328 ? 4.473   2.841   31.222  1.00 14.20  ?  328 ARG   B NH1 1 
ATOM   6304  N NH2 . ARG   B 1 328 ? 2.288   3.344   30.783  1.00 16.31  ?  328 ARG   B NH2 1 
ATOM   6305  N N   . ILE   B 1 329 ? 7.886   7.552   29.758  1.00 16.86  ?  329 ILE   B N   1 
ATOM   6306  C CA  . ILE   B 1 329 ? 7.789   7.515   28.305  1.00 14.59  ?  329 ILE   B CA  1 
ATOM   6307  C C   . ILE   B 1 329 ? 9.133   7.153   27.699  1.00 17.70  ?  329 ILE   B C   1 
ATOM   6308  O O   . ILE   B 1 329 ? 9.195   6.473   26.666  1.00 15.14  ?  329 ILE   B O   1 
ATOM   6309  C CB  . ILE   B 1 329 ? 7.259   8.870   27.803  1.00 17.45  ?  329 ILE   B CB  1 
ATOM   6310  C CG1 . ILE   B 1 329 ? 5.822   9.072   28.298  1.00 17.82  ?  329 ILE   B CG1 1 
ATOM   6311  C CG2 . ILE   B 1 329 ? 7.391   8.998   26.285  1.00 20.69  ?  329 ILE   B CG2 1 
ATOM   6312  C CD1 . ILE   B 1 329 ? 5.278   10.464  28.048  1.00 22.75  ?  329 ILE   B CD1 1 
ATOM   6313  N N   . GLY   B 1 330 ? 10.228  7.579   28.337  1.00 17.13  ?  330 GLY   B N   1 
ATOM   6314  C CA  . GLY   B 1 330 ? 11.547  7.218   27.848  1.00 15.99  ?  330 GLY   B CA  1 
ATOM   6315  C C   . GLY   B 1 330 ? 11.843  5.738   27.980  1.00 17.03  ?  330 GLY   B C   1 
ATOM   6316  O O   . GLY   B 1 330 ? 12.518  5.157   27.120  1.00 18.25  ?  330 GLY   B O   1 
ATOM   6317  N N   . GLN   B 1 331 ? 11.355  5.106   29.049  1.00 15.32  ?  331 GLN   B N   1 
ATOM   6318  C CA  . GLN   B 1 331 ? 11.472  3.656   29.149  1.00 13.28  ?  331 GLN   B CA  1 
ATOM   6319  C C   . GLN   B 1 331 ? 10.772  2.970   27.981  1.00 15.29  ?  331 GLN   B C   1 
ATOM   6320  O O   . GLN   B 1 331 ? 11.324  2.051   27.368  1.00 16.32  ?  331 GLN   B O   1 
ATOM   6321  C CB  . GLN   B 1 331 ? 10.906  3.161   30.475  1.00 15.58  ?  331 GLN   B CB  1 
ATOM   6322  C CG  . GLN   B 1 331 ? 10.958  1.648   30.590  1.00 17.41  ?  331 GLN   B CG  1 
ATOM   6323  C CD  . GLN   B 1 331 ? 10.477  1.144   31.926  1.00 18.26  ?  331 GLN   B CD  1 
ATOM   6324  O OE1 . GLN   B 1 331 ? 9.296   1.277   32.263  1.00 18.10  ?  331 GLN   B OE1 1 
ATOM   6325  N NE2 . GLN   B 1 331 ? 11.389  0.558   32.705  1.00 16.98  ?  331 GLN   B NE2 1 
ATOM   6326  N N   . VAL   B 1 332 ? 9.546   3.398   27.664  1.00 15.74  ?  332 VAL   B N   1 
ATOM   6327  C CA  . VAL   B 1 332 ? 8.841   2.846   26.504  1.00 14.59  ?  332 VAL   B CA  1 
ATOM   6328  C C   . VAL   B 1 332 ? 9.657   3.073   25.238  1.00 15.93  ?  332 VAL   B C   1 
ATOM   6329  O O   . VAL   B 1 332 ? 9.780   2.182   24.384  1.00 17.55  ?  332 VAL   B O   1 
ATOM   6330  C CB  . VAL   B 1 332 ? 7.430   3.461   26.382  1.00 12.47  ?  332 VAL   B CB  1 
ATOM   6331  C CG1 . VAL   B 1 332 ? 6.762   3.033   25.065  1.00 13.19  ?  332 VAL   B CG1 1 
ATOM   6332  C CG2 . VAL   B 1 332 ? 6.549   3.080   27.582  1.00 13.13  ?  332 VAL   B CG2 1 
ATOM   6333  N N   . LYS   B 1 333 ? 10.217  4.276   25.090  1.00 17.19  ?  333 LYS   B N   1 
ATOM   6334  C CA  . LYS   B 1 333 ? 11.033  4.581   23.920  1.00 15.31  ?  333 LYS   B CA  1 
ATOM   6335  C C   . LYS   B 1 333 ? 12.261  3.683   23.860  1.00 15.81  ?  333 LYS   B C   1 
ATOM   6336  O O   . LYS   B 1 333 ? 12.678  3.260   22.779  1.00 20.43  ?  333 LYS   B O   1 
ATOM   6337  C CB  . LYS   B 1 333 ? 11.449  6.049   23.949  1.00 16.87  ?  333 LYS   B CB  1 
ATOM   6338  C CG  . LYS   B 1 333 ? 12.171  6.482   22.702  1.00 18.08  ?  333 LYS   B CG  1 
ATOM   6339  C CD  . LYS   B 1 333 ? 12.608  7.930   22.763  1.00 17.55  ?  333 LYS   B CD  1 
ATOM   6340  C CE  . LYS   B 1 333 ? 13.036  8.405   21.372  1.00 24.52  ?  333 LYS   B CE  1 
ATOM   6341  N NZ  . LYS   B 1 333 ? 14.260  7.682   20.897  1.00 18.86  ?  333 LYS   B NZ  1 
ATOM   6342  N N   . TYR   B 1 334 ? 12.839  3.366   25.017  1.00 19.01  ?  334 TYR   B N   1 
ATOM   6343  C CA  . TYR   B 1 334 ? 14.023  2.513   25.063  1.00 19.29  ?  334 TYR   B CA  1 
ATOM   6344  C C   . TYR   B 1 334 ? 13.727  1.118   24.517  1.00 18.91  ?  334 TYR   B C   1 
ATOM   6345  O O   . TYR   B 1 334 ? 14.478  0.592   23.688  1.00 19.36  ?  334 TYR   B O   1 
ATOM   6346  C CB  . TYR   B 1 334 ? 14.541  2.442   26.498  1.00 17.73  ?  334 TYR   B CB  1 
ATOM   6347  C CG  . TYR   B 1 334 ? 15.667  1.470   26.684  1.00 21.11  ?  334 TYR   B CG  1 
ATOM   6348  C CD1 . TYR   B 1 334 ? 16.956  1.789   26.272  1.00 23.17  ?  334 TYR   B CD1 1 
ATOM   6349  C CD2 . TYR   B 1 334 ? 15.449  0.230   27.272  1.00 23.24  ?  334 TYR   B CD2 1 
ATOM   6350  C CE1 . TYR   B 1 334 ? 18.000  0.892   26.428  1.00 21.06  ?  334 TYR   B CE1 1 
ATOM   6351  C CE2 . TYR   B 1 334 ? 16.491  -0.675  27.441  1.00 21.67  ?  334 TYR   B CE2 1 
ATOM   6352  C CZ  . TYR   B 1 334 ? 17.764  -0.332  27.017  1.00 23.24  ?  334 TYR   B CZ  1 
ATOM   6353  O OH  . TYR   B 1 334 ? 18.802  -1.214  27.184  1.00 22.75  ?  334 TYR   B OH  1 
ATOM   6354  N N   . LEU   B 1 335 ? 12.636  0.497   24.978  1.00 16.23  ?  335 LEU   B N   1 
ATOM   6355  C CA  . LEU   B 1 335 ? 12.234  -0.798  24.430  1.00 14.72  ?  335 LEU   B CA  1 
ATOM   6356  C C   . LEU   B 1 335 ? 12.023  -0.713  22.928  1.00 18.07  ?  335 LEU   B C   1 
ATOM   6357  O O   . LEU   B 1 335 ? 12.437  -1.610  22.181  1.00 19.90  ?  335 LEU   B O   1 
ATOM   6358  C CB  . LEU   B 1 335 ? 10.956  -1.289  25.110  1.00 16.82  ?  335 LEU   B CB  1 
ATOM   6359  C CG  . LEU   B 1 335 ? 10.371  -2.602  24.587  1.00 18.28  ?  335 LEU   B CG  1 
ATOM   6360  C CD1 . LEU   B 1 335 ? 11.396  -3.733  24.678  1.00 16.21  ?  335 LEU   B CD1 1 
ATOM   6361  C CD2 . LEU   B 1 335 ? 9.116   -2.955  25.378  1.00 15.14  ?  335 LEU   B CD2 1 
ATOM   6362  N N   . GLY   B 1 336 ? 11.377  0.358   22.467  1.00 18.79  ?  336 GLY   B N   1 
ATOM   6363  C CA  . GLY   B 1 336 ? 11.138  0.504   21.042  1.00 16.12  ?  336 GLY   B CA  1 
ATOM   6364  C C   . GLY   B 1 336 ? 12.424  0.657   20.260  1.00 20.86  ?  336 GLY   B C   1 
ATOM   6365  O O   . GLY   B 1 336 ? 12.585  0.060   19.195  1.00 21.38  ?  336 GLY   B O   1 
ATOM   6366  N N   . ASP   B 1 337 ? 13.367  1.444   20.791  1.00 20.54  ?  337 ASP   B N   1 
ATOM   6367  C CA  . ASP   B 1 337 ? 14.650  1.641   20.122  1.00 20.18  ?  337 ASP   B CA  1 
ATOM   6368  C C   . ASP   B 1 337 ? 15.471  0.355   20.089  1.00 22.52  ?  337 ASP   B C   1 
ATOM   6369  O O   . ASP   B 1 337 ? 16.107  0.051   19.074  1.00 21.61  ?  337 ASP   B O   1 
ATOM   6370  C CB  . ASP   B 1 337 ? 15.432  2.766   20.805  1.00 17.87  ?  337 ASP   B CB  1 
ATOM   6371  C CG  . ASP   B 1 337 ? 14.872  4.145   20.484  1.00 20.62  ?  337 ASP   B CG  1 
ATOM   6372  O OD1 . ASP   B 1 337 ? 14.115  4.267   19.504  1.00 24.21  ?  337 ASP   B OD1 1 
ATOM   6373  O OD2 . ASP   B 1 337 ? 15.194  5.113   21.201  1.00 21.89  ?  337 ASP   B OD2 1 
ATOM   6374  N N   . ARG   B 1 338 ? 15.478  -0.409  21.189  1.00 22.02  ?  338 ARG   B N   1 
ATOM   6375  C CA  . ARG   B 1 338 ? 16.154  -1.705  21.187  1.00 21.17  ?  338 ARG   B CA  1 
ATOM   6376  C C   . ARG   B 1 338 ? 15.587  -2.612  20.101  1.00 21.36  ?  338 ARG   B C   1 
ATOM   6377  O O   . ARG   B 1 338 ? 16.331  -3.354  19.449  1.00 22.06  ?  338 ARG   B O   1 
ATOM   6378  C CB  . ARG   B 1 338 ? 16.032  -2.384  22.558  1.00 20.49  ?  338 ARG   B CB  1 
ATOM   6379  C CG  . ARG   B 1 338 ? 16.851  -1.788  23.715  1.00 21.86  ?  338 ARG   B CG  1 
ATOM   6380  C CD  . ARG   B 1 338 ? 18.319  -2.250  23.774  1.00 20.90  ?  338 ARG   B CD  1 
ATOM   6381  N NE  . ARG   B 1 338 ? 18.573  -3.512  23.085  1.00 23.91  ?  338 ARG   B NE  1 
ATOM   6382  C CZ  . ARG   B 1 338 ? 18.464  -4.715  23.635  1.00 23.08  ?  338 ARG   B CZ  1 
ATOM   6383  N NH1 . ARG   B 1 338 ? 18.105  -4.869  24.896  1.00 26.11  ?  338 ARG   B NH1 1 
ATOM   6384  N NH2 . ARG   B 1 338 ? 18.718  -5.792  22.897  1.00 26.32  ?  338 ARG   B NH2 1 
ATOM   6385  N N   . LEU   B 1 339 ? 14.272  -2.555  19.878  1.00 20.10  ?  339 LEU   B N   1 
ATOM   6386  C CA  . LEU   B 1 339 ? 13.664  -3.380  18.835  1.00 24.98  ?  339 LEU   B CA  1 
ATOM   6387  C C   . LEU   B 1 339 ? 13.964  -2.841  17.440  1.00 23.73  ?  339 LEU   B C   1 
ATOM   6388  O O   . LEU   B 1 339 ? 14.245  -3.615  16.516  1.00 22.14  ?  339 LEU   B O   1 
ATOM   6389  C CB  . LEU   B 1 339 ? 12.154  -3.475  19.053  1.00 23.64  ?  339 LEU   B CB  1 
ATOM   6390  C CG  . LEU   B 1 339 ? 11.706  -4.208  20.312  1.00 21.84  ?  339 LEU   B CG  1 
ATOM   6391  C CD1 . LEU   B 1 339 ? 10.183  -4.135  20.438  1.00 19.15  ?  339 LEU   B CD1 1 
ATOM   6392  C CD2 . LEU   B 1 339 ? 12.197  -5.654  20.284  1.00 18.77  ?  339 LEU   B CD2 1 
ATOM   6393  N N   . ARG   B 1 340 ? 13.891  -1.520  17.260  1.00 21.09  ?  340 ARG   B N   1 
ATOM   6394  C CA  . ARG   B 1 340 ? 14.187  -0.944  15.954  1.00 24.63  ?  340 ARG   B CA  1 
ATOM   6395  C C   . ARG   B 1 340 ? 15.632  -1.200  15.557  1.00 26.68  ?  340 ARG   B C   1 
ATOM   6396  O O   . ARG   B 1 340 ? 15.920  -1.501  14.390  1.00 25.65  ?  340 ARG   B O   1 
ATOM   6397  C CB  . ARG   B 1 340 ? 13.892  0.555   15.960  1.00 24.18  ?  340 ARG   B CB  1 
ATOM   6398  C CG  . ARG   B 1 340 ? 12.417  0.889   15.991  1.00 29.77  ?  340 ARG   B CG  1 
ATOM   6399  C CD  . ARG   B 1 340 ? 12.207  2.390   16.011  1.00 29.09  ?  340 ARG   B CD  1 
ATOM   6400  N NE  . ARG   B 1 340 ? 12.988  3.050   14.977  1.00 32.54  ?  340 ARG   B NE  1 
ATOM   6401  C CZ  . ARG   B 1 340 ? 12.598  3.182   13.718  1.00 35.24  ?  340 ARG   B CZ  1 
ATOM   6402  N NH1 . ARG   B 1 340 ? 11.454  2.672   13.295  1.00 38.87  ?  340 ARG   B NH1 1 
ATOM   6403  N NH2 . ARG   B 1 340 ? 13.374  3.845   12.864  1.00 37.34  ?  340 ARG   B NH2 1 
ATOM   6404  N N   . GLU   B 1 341 ? 16.558  -1.085  16.514  1.00 25.58  ?  341 GLU   B N   1 
ATOM   6405  C CA  . GLU   B 1 341 ? 17.965  -1.328  16.211  1.00 26.31  ?  341 GLU   B CA  1 
ATOM   6406  C C   . GLU   B 1 341 ? 18.197  -2.759  15.749  1.00 30.64  ?  341 GLU   B C   1 
ATOM   6407  O O   . GLU   B 1 341 ? 19.154  -3.022  15.016  1.00 31.23  ?  341 GLU   B O   1 
ATOM   6408  C CB  . GLU   B 1 341 ? 18.833  -1.002  17.427  1.00 23.66  ?  341 GLU   B CB  1 
ATOM   6409  C CG  . GLU   B 1 341 ? 18.925  0.488   17.714  1.00 29.80  ?  341 GLU   B CG  1 
ATOM   6410  C CD  . GLU   B 1 341 ? 19.480  0.797   19.097  1.00 35.15  ?  341 GLU   B CD  1 
ATOM   6411  O OE1 . GLU   B 1 341 ? 20.233  -0.039  19.644  1.00 37.57  ?  341 GLU   B OE1 1 
ATOM   6412  O OE2 . GLU   B 1 341 ? 19.154  1.877   19.642  1.00 30.09  ?  341 GLU   B OE2 1 
ATOM   6413  N N   . ALA   B 1 342 ? 17.331  -3.689  16.145  1.00 23.99  ?  342 ALA   B N   1 
ATOM   6414  C CA  . ALA   B 1 342 ? 17.418  -5.069  15.689  1.00 26.41  ?  342 ALA   B CA  1 
ATOM   6415  C C   . ALA   B 1 342 ? 16.542  -5.347  14.471  1.00 29.47  ?  342 ALA   B C   1 
ATOM   6416  O O   . ALA   B 1 342 ? 16.360  -6.516  14.108  1.00 27.60  ?  342 ALA   B O   1 
ATOM   6417  C CB  . ALA   B 1 342 ? 17.047  -6.022  16.826  1.00 28.36  ?  342 ALA   B CB  1 
ATOM   6418  N N   . GLY   B 1 343 ? 15.995  -4.310  13.837  1.00 26.55  ?  343 GLY   B N   1 
ATOM   6419  C CA  . GLY   B 1 343 ? 15.201  -4.482  12.635  1.00 24.78  ?  343 GLY   B CA  1 
ATOM   6420  C C   . GLY   B 1 343 ? 13.764  -4.905  12.856  1.00 27.46  ?  343 GLY   B C   1 
ATOM   6421  O O   . GLY   B 1 343 ? 13.099  -5.297  11.891  1.00 30.34  ?  343 GLY   B O   1 
ATOM   6422  N N   . ILE   B 1 344 ? 13.260  -4.838  14.084  1.00 26.34  ?  344 ILE   B N   1 
ATOM   6423  C CA  . ILE   B 1 344 ? 11.883  -5.226  14.391  1.00 24.37  ?  344 ILE   B CA  1 
ATOM   6424  C C   . ILE   B 1 344 ? 10.946  -4.069  14.060  1.00 26.61  ?  344 ILE   B C   1 
ATOM   6425  O O   . ILE   B 1 344 ? 11.124  -2.963  14.591  1.00 28.68  ?  344 ILE   B O   1 
ATOM   6426  C CB  . ILE   B 1 344 ? 11.733  -5.639  15.863  1.00 30.90  ?  344 ILE   B CB  1 
ATOM   6427  C CG1 . ILE   B 1 344 ? 12.719  -6.756  16.222  1.00 31.78  ?  344 ILE   B CG1 1 
ATOM   6428  C CG2 . ILE   B 1 344 ? 10.303  -6.092  16.151  1.00 23.79  ?  344 ILE   B CG2 1 
ATOM   6429  C CD1 . ILE   B 1 344 ? 12.426  -8.066  15.522  1.00 32.18  ?  344 ILE   B CD1 1 
ATOM   6430  N N   . PRO   B 1 345 ? 9.931   -4.276  13.218  1.00 27.45  ?  345 PRO   B N   1 
ATOM   6431  C CA  . PRO   B 1 345 ? 9.021   -3.173  12.855  1.00 28.74  ?  345 PRO   B CA  1 
ATOM   6432  C C   . PRO   B 1 345 ? 8.074   -2.823  13.997  1.00 26.85  ?  345 PRO   B C   1 
ATOM   6433  O O   . PRO   B 1 345 ? 7.440   -3.701  14.588  1.00 26.33  ?  345 PRO   B O   1 
ATOM   6434  C CB  . PRO   B 1 345 ? 8.249   -3.729  11.651  1.00 30.79  ?  345 PRO   B CB  1 
ATOM   6435  C CG  . PRO   B 1 345 ? 8.965   -4.985  11.246  1.00 32.80  ?  345 PRO   B CG  1 
ATOM   6436  C CD  . PRO   B 1 345 ? 9.629   -5.508  12.475  1.00 31.65  ?  345 PRO   B CD  1 
ATOM   6437  N N   . ILE   B 1 346 ? 7.967   -1.524  14.297  1.00 22.00  ?  346 ILE   B N   1 
ATOM   6438  C CA  . ILE   B 1 346 ? 7.106   -1.035  15.373  1.00 27.10  ?  346 ILE   B CA  1 
ATOM   6439  C C   . ILE   B 1 346 ? 6.400   0.242   14.929  1.00 28.00  ?  346 ILE   B C   1 
ATOM   6440  O O   . ILE   B 1 346 ? 6.800   0.905   13.968  1.00 23.57  ?  346 ILE   B O   1 
ATOM   6441  C CB  . ILE   B 1 346 ? 7.875   -0.751  16.689  1.00 26.14  ?  346 ILE   B CB  1 
ATOM   6442  C CG1 . ILE   B 1 346 ? 8.755   0.492   16.538  1.00 22.52  ?  346 ILE   B CG1 1 
ATOM   6443  C CG2 . ILE   B 1 346 ? 8.706   -1.955  17.128  1.00 21.42  ?  346 ILE   B CG2 1 
ATOM   6444  C CD1 . ILE   B 1 346 ? 9.332   0.976   17.863  1.00 21.02  ?  346 ILE   B CD1 1 
ATOM   6445  N N   . GLN   B 1 347 ? 5.336   0.589   15.656  1.00 26.09  ?  347 GLN   B N   1 
ATOM   6446  C CA  . GLN   B 1 347 ? 4.692   1.883   15.455  1.00 26.14  ?  347 GLN   B CA  1 
ATOM   6447  C C   . GLN   B 1 347 ? 5.659   2.979   15.885  1.00 26.64  ?  347 GLN   B C   1 
ATOM   6448  O O   . GLN   B 1 347 ? 6.035   3.063   17.060  1.00 23.44  ?  347 GLN   B O   1 
ATOM   6449  C CB  . GLN   B 1 347 ? 3.381   1.970   16.239  1.00 25.37  ?  347 GLN   B CB  1 
ATOM   6450  C CG  . GLN   B 1 347 ? 2.684   3.339   16.181  1.00 27.52  ?  347 GLN   B CG  1 
ATOM   6451  C CD  . GLN   B 1 347 ? 2.088   3.671   14.806  1.00 35.23  ?  347 GLN   B CD  1 
ATOM   6452  O OE1 . GLN   B 1 347 ? 2.780   4.162   13.907  1.00 32.88  ?  347 GLN   B OE1 1 
ATOM   6453  N NE2 . GLN   B 1 347 ? 0.795   3.416   14.649  1.00 34.74  ?  347 GLN   B NE2 1 
ATOM   6454  N N   . TYR   B 1 348 ? 6.076   3.804   14.931  1.00 20.57  ?  348 TYR   B N   1 
ATOM   6455  C CA  . TYR   B 1 348 ? 7.125   4.779   15.142  1.00 22.58  ?  348 TYR   B CA  1 
ATOM   6456  C C   . TYR   B 1 348 ? 6.575   6.185   14.935  1.00 24.88  ?  348 TYR   B C   1 
ATOM   6457  O O   . TYR   B 1 348 ? 5.972   6.454   13.888  1.00 28.40  ?  348 TYR   B O   1 
ATOM   6458  C CB  . TYR   B 1 348 ? 8.281   4.510   14.167  1.00 23.27  ?  348 TYR   B CB  1 
ATOM   6459  C CG  . TYR   B 1 348 ? 9.472   5.422   14.314  1.00 28.91  ?  348 TYR   B CG  1 
ATOM   6460  C CD1 . TYR   B 1 348 ? 10.248  5.408   15.466  1.00 30.22  ?  348 TYR   B CD1 1 
ATOM   6461  C CD2 . TYR   B 1 348 ? 9.843   6.273   13.284  1.00 30.92  ?  348 TYR   B CD2 1 
ATOM   6462  C CE1 . TYR   B 1 348 ? 11.345  6.235   15.595  1.00 29.75  ?  348 TYR   B CE1 1 
ATOM   6463  C CE2 . TYR   B 1 348 ? 10.939  7.101   13.403  1.00 29.10  ?  348 TYR   B CE2 1 
ATOM   6464  C CZ  . TYR   B 1 348 ? 11.687  7.077   14.559  1.00 30.34  ?  348 TYR   B CZ  1 
ATOM   6465  O OH  . TYR   B 1 348 ? 12.778  7.907   14.678  1.00 38.31  ?  348 TYR   B OH  1 
ATOM   6466  N N   . PRO   B 1 349 ? 6.742   7.104   15.896  1.00 23.83  ?  349 PRO   B N   1 
ATOM   6467  C CA  . PRO   B 1 349 ? 7.408   6.971   17.196  1.00 20.69  ?  349 PRO   B CA  1 
ATOM   6468  C C   . PRO   B 1 349 ? 6.585   6.174   18.203  1.00 21.70  ?  349 PRO   B C   1 
ATOM   6469  O O   . PRO   B 1 349 ? 5.363   6.049   18.055  1.00 21.68  ?  349 PRO   B O   1 
ATOM   6470  C CB  . PRO   B 1 349 ? 7.549   8.427   17.641  1.00 19.66  ?  349 PRO   B CB  1 
ATOM   6471  C CG  . PRO   B 1 349 ? 6.283   9.041   17.140  1.00 18.70  ?  349 PRO   B CG  1 
ATOM   6472  C CD  . PRO   B 1 349 ? 6.109   8.429   15.765  1.00 22.93  ?  349 PRO   B CD  1 
ATOM   6473  N N   . THR   B 1 350 ? 7.247   5.625   19.221  1.00 22.01  ?  350 THR   B N   1 
ATOM   6474  C CA  . THR   B 1 350 ? 6.544   4.963   20.312  1.00 18.18  ?  350 THR   B CA  1 
ATOM   6475  C C   . THR   B 1 350 ? 5.677   5.969   21.051  1.00 20.77  ?  350 THR   B C   1 
ATOM   6476  O O   . THR   B 1 350 ? 6.047   7.136   21.208  1.00 21.96  ?  350 THR   B O   1 
ATOM   6477  C CB  . THR   B 1 350 ? 7.536   4.327   21.281  1.00 19.07  ?  350 THR   B CB  1 
ATOM   6478  O OG1 . THR   B 1 350 ? 8.439   5.335   21.769  1.00 20.04  ?  350 THR   B OG1 1 
ATOM   6479  C CG2 . THR   B 1 350 ? 8.334   3.213   20.593  1.00 19.73  ?  350 THR   B CG2 1 
ATOM   6480  N N   . GLY   B 1 351 ? 4.514   5.517   21.501  1.00 17.26  ?  351 GLY   B N   1 
ATOM   6481  C CA  . GLY   B 1 351 ? 3.609   6.363   22.245  1.00 19.57  ?  351 GLY   B CA  1 
ATOM   6482  C C   . GLY   B 1 351 ? 3.975   6.402   23.713  1.00 19.39  ?  351 GLY   B C   1 
ATOM   6483  O O   . GLY   B 1 351 ? 5.109   6.122   24.112  1.00 18.94  ?  351 GLY   B O   1 
ATOM   6484  N N   . GLY   B 1 352 ? 2.982   6.732   24.539  1.00 15.78  ?  352 GLY   B N   1 
ATOM   6485  C CA  . GLY   B 1 352 ? 3.263   6.963   25.944  1.00 15.49  ?  352 GLY   B CA  1 
ATOM   6486  C C   . GLY   B 1 352 ? 3.428   5.710   26.776  1.00 19.73  ?  352 GLY   B C   1 
ATOM   6487  O O   . GLY   B 1 352 ? 4.211   5.704   27.734  1.00 19.93  ?  352 GLY   B O   1 
ATOM   6488  N N   . HIS   B 1 353 ? 2.716   4.630   26.429  1.00 15.23  ?  353 HIS   B N   1 
ATOM   6489  C CA  . HIS   B 1 353 ? 2.481   3.560   27.389  1.00 14.66  ?  353 HIS   B CA  1 
ATOM   6490  C C   . HIS   B 1 353 ? 2.828   2.159   26.905  1.00 15.51  ?  353 HIS   B C   1 
ATOM   6491  O O   . HIS   B 1 353 ? 2.757   1.219   27.705  1.00 13.99  ?  353 HIS   B O   1 
ATOM   6492  C CB  . HIS   B 1 353 ? 1.008   3.578   27.831  1.00 18.22  ?  353 HIS   B CB  1 
ATOM   6493  C CG  . HIS   B 1 353 ? 0.045   3.119   26.778  1.00 16.09  ?  353 HIS   B CG  1 
ATOM   6494  N ND1 . HIS   B 1 353 ? -0.074  3.735   25.551  1.00 19.39  ?  353 HIS   B ND1 1 
ATOM   6495  C CD2 . HIS   B 1 353 ? -0.865  2.113   26.784  1.00 23.11  ?  353 HIS   B CD2 1 
ATOM   6496  C CE1 . HIS   B 1 353 ? -1.014  3.126   24.846  1.00 22.50  ?  353 HIS   B CE1 1 
ATOM   6497  N NE2 . HIS   B 1 353 ? -1.513  2.141   25.572  1.00 19.09  ?  353 HIS   B NE2 1 
ATOM   6498  N N   . ALA   B 1 354 ? 3.217   1.989   25.645  1.00 15.84  ?  354 ALA   B N   1 
ATOM   6499  C CA  . ALA   B 1 354 ? 3.362   0.659   25.069  1.00 19.19  ?  354 ALA   B CA  1 
ATOM   6500  C C   . ALA   B 1 354 ? 4.128   0.759   23.765  1.00 19.19  ?  354 ALA   B C   1 
ATOM   6501  O O   . ALA   B 1 354 ? 4.066   1.778   23.073  1.00 21.80  ?  354 ALA   B O   1 
ATOM   6502  C CB  . ALA   B 1 354 ? 1.998   0.005   24.807  1.00 20.46  ?  354 ALA   B CB  1 
ATOM   6503  N N   . VAL   B 1 355 ? 4.837   -0.317  23.433  1.00 19.44  ?  355 VAL   B N   1 
ATOM   6504  C CA  . VAL   B 1 355 ? 5.439   -0.494  22.116  1.00 19.01  ?  355 VAL   B CA  1 
ATOM   6505  C C   . VAL   B 1 355 ? 4.543   -1.429  21.321  1.00 18.39  ?  355 VAL   B C   1 
ATOM   6506  O O   . VAL   B 1 355 ? 4.138   -2.483  21.823  1.00 17.44  ?  355 VAL   B O   1 
ATOM   6507  C CB  . VAL   B 1 355 ? 6.870   -1.050  22.221  1.00 15.64  ?  355 VAL   B CB  1 
ATOM   6508  C CG1 . VAL   B 1 355 ? 7.462   -1.290  20.832  1.00 20.26  ?  355 VAL   B CG1 1 
ATOM   6509  C CG2 . VAL   B 1 355 ? 7.742   -0.106  23.038  1.00 15.65  ?  355 VAL   B CG2 1 
ATOM   6510  N N   . PHE   B 1 356 ? 4.212   -1.037  20.094  1.00 17.23  ?  356 PHE   B N   1 
ATOM   6511  C CA  . PHE   B 1 356 ? 3.332   -1.807  19.224  1.00 21.47  ?  356 PHE   B CA  1 
ATOM   6512  C C   . PHE   B 1 356 ? 4.161   -2.397  18.091  1.00 25.78  ?  356 PHE   B C   1 
ATOM   6513  O O   . PHE   B 1 356 ? 4.698   -1.657  17.256  1.00 21.84  ?  356 PHE   B O   1 
ATOM   6514  C CB  . PHE   B 1 356 ? 2.201   -0.937  18.667  1.00 25.25  ?  356 PHE   B CB  1 
ATOM   6515  C CG  . PHE   B 1 356 ? 1.152   -0.555  19.681  1.00 23.99  ?  356 PHE   B CG  1 
ATOM   6516  C CD1 . PHE   B 1 356 ? 1.376   0.473   20.578  1.00 24.97  ?  356 PHE   B CD1 1 
ATOM   6517  C CD2 . PHE   B 1 356 ? -0.066  -1.201  19.712  1.00 23.42  ?  356 PHE   B CD2 1 
ATOM   6518  C CE1 . PHE   B 1 356 ? 0.416   0.833   21.501  1.00 26.78  ?  356 PHE   B CE1 1 
ATOM   6519  C CE2 . PHE   B 1 356 ? -1.037  -0.840  20.625  1.00 26.35  ?  356 PHE   B CE2 1 
ATOM   6520  C CZ  . PHE   B 1 356 ? -0.799  0.181   21.524  1.00 25.42  ?  356 PHE   B CZ  1 
ATOM   6521  N N   . VAL   B 1 357 ? 4.252   -3.725  18.050  1.00 21.99  ?  357 VAL   B N   1 
ATOM   6522  C CA  . VAL   B 1 357 ? 5.069   -4.423  17.065  1.00 26.07  ?  357 VAL   B CA  1 
ATOM   6523  C C   . VAL   B 1 357 ? 4.191   -4.840  15.897  1.00 30.97  ?  357 VAL   B C   1 
ATOM   6524  O O   . VAL   B 1 357 ? 3.168   -5.506  16.087  1.00 28.13  ?  357 VAL   B O   1 
ATOM   6525  C CB  . VAL   B 1 357 ? 5.763   -5.642  17.690  1.00 26.93  ?  357 VAL   B CB  1 
ATOM   6526  C CG1 . VAL   B 1 357 ? 6.575   -6.373  16.638  1.00 26.89  ?  357 VAL   B CG1 1 
ATOM   6527  C CG2 . VAL   B 1 357 ? 6.634   -5.205  18.864  1.00 19.76  ?  357 VAL   B CG2 1 
ATOM   6528  N N   . ASP   B 1 358 ? 4.595   -4.461  14.687  1.00 31.45  ?  358 ASP   B N   1 
ATOM   6529  C CA  . ASP   B 1 358 ? 3.836   -4.787  13.483  1.00 39.60  ?  358 ASP   B CA  1 
ATOM   6530  C C   . ASP   B 1 358 ? 4.160   -6.220  13.079  1.00 38.59  ?  358 ASP   B C   1 
ATOM   6531  O O   . ASP   B 1 358 ? 5.251   -6.499  12.570  1.00 40.21  ?  358 ASP   B O   1 
ATOM   6532  C CB  . ASP   B 1 358 ? 4.170   -3.803  12.365  1.00 44.68  ?  358 ASP   B CB  1 
ATOM   6533  C CG  . ASP   B 1 358 ? 3.098   -3.749  11.293  1.00 55.38  ?  358 ASP   B CG  1 
ATOM   6534  O OD1 . ASP   B 1 358 ? 2.447   -4.789  11.046  1.00 58.91  ?  358 ASP   B OD1 1 
ATOM   6535  O OD2 . ASP   B 1 358 ? 2.907   -2.664  10.701  1.00 48.86  ?  358 ASP   B OD2 1 
ATOM   6536  N N   . CYS   B 1 359 ? 3.213   -7.130  13.302  1.00 38.93  ?  359 CYS   B N   1 
ATOM   6537  C CA  . CYS   B 1 359 ? 3.455   -8.551  13.090  1.00 47.58  ?  359 CYS   B CA  1 
ATOM   6538  C C   . CYS   B 1 359 ? 3.154   -9.014  11.673  1.00 51.23  ?  359 CYS   B C   1 
ATOM   6539  O O   . CYS   B 1 359 ? 3.498   -10.150 11.326  1.00 52.30  ?  359 CYS   B O   1 
ATOM   6540  C CB  . CYS   B 1 359 ? 2.635   -9.377  14.080  1.00 45.84  ?  359 CYS   B CB  1 
ATOM   6541  S SG  . CYS   B 1 359 ? 3.125   -9.090  15.784  1.00 38.29  ?  359 CYS   B SG  1 
ATOM   6542  N N   . LYS   B 1 360 ? 2.519   -8.173  10.856  1.00 56.51  ?  360 LYS   B N   1 
ATOM   6543  C CA  . LYS   B 1 360 ? 2.351   -8.505  9.447   1.00 61.94  ?  360 LYS   B CA  1 
ATOM   6544  C C   . LYS   B 1 360 ? 3.699   -8.769  8.786   1.00 61.21  ?  360 LYS   B C   1 
ATOM   6545  O O   . LYS   B 1 360 ? 3.846   -9.721  8.009   1.00 63.26  ?  360 LYS   B O   1 
ATOM   6546  C CB  . LYS   B 1 360 ? 1.615   -7.370  8.738   1.00 63.50  ?  360 LYS   B CB  1 
ATOM   6547  C CG  . LYS   B 1 360 ? 0.476   -6.794  9.563   1.00 64.96  ?  360 LYS   B CG  1 
ATOM   6548  C CD  . LYS   B 1 360 ? -0.010  -5.450  9.030   1.00 77.53  ?  360 LYS   B CD  1 
ATOM   6549  C CE  . LYS   B 1 360 ? -0.674  -5.577  7.667   1.00 76.20  ?  360 LYS   B CE  1 
ATOM   6550  N NZ  . LYS   B 1 360 ? -1.326  -4.298  7.265   1.00 79.79  ?  360 LYS   B NZ  1 
ATOM   6551  N N   . LYS   B 1 361 ? 4.700   -7.950  9.106   1.00 56.67  ?  361 LYS   B N   1 
ATOM   6552  C CA  . LYS   B 1 361 ? 6.020   -8.051  8.500   1.00 52.61  ?  361 LYS   B CA  1 
ATOM   6553  C C   . LYS   B 1 361 ? 6.920   -9.059  9.201   1.00 53.84  ?  361 LYS   B C   1 
ATOM   6554  O O   . LYS   B 1 361 ? 7.966   -9.425  8.649   1.00 52.54  ?  361 LYS   B O   1 
ATOM   6555  C CB  . LYS   B 1 361 ? 6.681   -6.667  8.488   1.00 45.33  ?  361 LYS   B CB  1 
ATOM   6556  C CG  . LYS   B 1 361 ? 5.699   -5.546  8.140   1.00 49.78  ?  361 LYS   B CG  1 
ATOM   6557  C CD  . LYS   B 1 361 ? 6.291   -4.158  8.347   1.00 54.42  ?  361 LYS   B CD  1 
ATOM   6558  C CE  . LYS   B 1 361 ? 7.345   -3.832  7.300   1.00 54.75  ?  361 LYS   B CE  1 
ATOM   6559  N NZ  . LYS   B 1 361 ? 7.924   -2.476  7.515   1.00 55.76  ?  361 LYS   B NZ  1 
ATOM   6560  N N   . LEU   B 1 362 ? 6.534   -9.525  10.391  1.00 47.05  ?  362 LEU   B N   1 
ATOM   6561  C CA  . LEU   B 1 362 ? 7.349   -10.490 11.119  1.00 49.68  ?  362 LEU   B CA  1 
ATOM   6562  C C   . LEU   B 1 362 ? 7.093   -11.917 10.657  1.00 52.12  ?  362 LEU   B C   1 
ATOM   6563  O O   . LEU   B 1 362 ? 8.027   -12.722 10.570  1.00 54.72  ?  362 LEU   B O   1 
ATOM   6564  C CB  . LEU   B 1 362 ? 7.078   -10.387 12.618  1.00 48.94  ?  362 LEU   B CB  1 
ATOM   6565  C CG  . LEU   B 1 362 ? 7.805   -9.308  13.408  1.00 44.48  ?  362 LEU   B CG  1 
ATOM   6566  C CD1 . LEU   B 1 362 ? 7.574   -9.533  14.887  1.00 32.69  ?  362 LEU   B CD1 1 
ATOM   6567  C CD2 . LEU   B 1 362 ? 9.292   -9.326  13.069  1.00 43.40  ?  362 LEU   B CD2 1 
ATOM   6568  N N   . VAL   B 1 363 ? 5.835   -12.259 10.397  1.00 52.63  ?  363 VAL   B N   1 
ATOM   6569  C CA  . VAL   B 1 363 ? 5.471   -13.631 10.053  1.00 54.07  ?  363 VAL   B CA  1 
ATOM   6570  C C   . VAL   B 1 363 ? 4.669   -13.613 8.758   1.00 56.56  ?  363 VAL   B C   1 
ATOM   6571  O O   . VAL   B 1 363 ? 3.444   -13.814 8.775   1.00 58.07  ?  363 VAL   B O   1 
ATOM   6572  C CB  . VAL   B 1 363 ? 4.699   -14.308 11.196  1.00 50.11  ?  363 VAL   B CB  1 
ATOM   6573  C CG1 . VAL   B 1 363 ? 5.674   -14.873 12.212  1.00 48.20  ?  363 VAL   B CG1 1 
ATOM   6574  C CG2 . VAL   B 1 363 ? 3.756   -13.315 11.867  1.00 49.07  ?  363 VAL   B CG2 1 
ATOM   6575  N N   . PRO   B 1 364 ? 5.319   -13.383 7.615   1.00 60.88  ?  364 PRO   B N   1 
ATOM   6576  C CA  . PRO   B 1 364 ? 4.572   -13.343 6.349   1.00 58.29  ?  364 PRO   B CA  1 
ATOM   6577  C C   . PRO   B 1 364 ? 3.865   -14.651 6.030   1.00 58.35  ?  364 PRO   B C   1 
ATOM   6578  O O   . PRO   B 1 364 ? 2.791   -14.635 5.414   1.00 51.79  ?  364 PRO   B O   1 
ATOM   6579  C CB  . PRO   B 1 364 ? 5.658   -13.010 5.316   1.00 47.44  ?  364 PRO   B CB  1 
ATOM   6580  C CG  . PRO   B 1 364 ? 6.943   -13.467 5.948   1.00 46.75  ?  364 PRO   B CG  1 
ATOM   6581  C CD  . PRO   B 1 364 ? 6.774   -13.236 7.419   1.00 55.92  ?  364 PRO   B CD  1 
ATOM   6582  N N   . GLN   B 1 365 ? 4.421   -15.784 6.461   1.00 54.82  ?  365 GLN   B N   1 
ATOM   6583  C CA  . GLN   B 1 365 ? 3.849   -17.085 6.136   1.00 59.80  ?  365 GLN   B CA  1 
ATOM   6584  C C   . GLN   B 1 365 ? 2.553   -17.379 6.892   1.00 66.48  ?  365 GLN   B C   1 
ATOM   6585  O O   . GLN   B 1 365 ? 1.986   -18.465 6.710   1.00 68.83  ?  365 GLN   B O   1 
ATOM   6586  C CB  . GLN   B 1 365 ? 4.879   -18.187 6.407   1.00 63.66  ?  365 GLN   B CB  1 
ATOM   6587  C CG  . GLN   B 1 365 ? 5.179   -18.449 7.882   1.00 63.52  ?  365 GLN   B CG  1 
ATOM   6588  C CD  . GLN   B 1 365 ? 6.177   -17.472 8.478   1.00 57.65  ?  365 GLN   B CD  1 
ATOM   6589  O OE1 . GLN   B 1 365 ? 6.795   -16.681 7.768   1.00 61.19  ?  365 GLN   B OE1 1 
ATOM   6590  N NE2 . GLN   B 1 365 ? 6.339   -17.529 9.791   1.00 57.91  ?  365 GLN   B NE2 1 
ATOM   6591  N N   . ILE   B 1 366 ? 2.066   -16.456 7.714   1.00 66.97  ?  366 ILE   B N   1 
ATOM   6592  C CA  . ILE   B 1 366 ? 0.859   -16.649 8.508   1.00 63.26  ?  366 ILE   B CA  1 
ATOM   6593  C C   . ILE   B 1 366 ? -0.176  -15.621 8.060   1.00 63.38  ?  366 ILE   B C   1 
ATOM   6594  O O   . ILE   B 1 366 ? 0.049   -14.415 8.203   1.00 64.22  ?  366 ILE   B O   1 
ATOM   6595  C CB  . ILE   B 1 366 ? 1.143   -16.527 10.015  1.00 61.35  ?  366 ILE   B CB  1 
ATOM   6596  C CG1 . ILE   B 1 366 ? 2.173   -17.580 10.436  1.00 56.47  ?  366 ILE   B CG1 1 
ATOM   6597  C CG2 . ILE   B 1 366 ? -0.138  -16.672 10.823  1.00 63.13  ?  366 ILE   B CG2 1 
ATOM   6598  C CD1 . ILE   B 1 366 ? 2.469   -17.603 11.911  1.00 56.76  ?  366 ILE   B CD1 1 
ATOM   6599  N N   . PRO   B 1 367 ? -1.314  -16.040 7.507   1.00 64.60  ?  367 PRO   B N   1 
ATOM   6600  C CA  . PRO   B 1 367 ? -2.328  -15.075 7.060   1.00 64.76  ?  367 PRO   B CA  1 
ATOM   6601  C C   . PRO   B 1 367 ? -3.073  -14.463 8.237   1.00 64.47  ?  367 PRO   B C   1 
ATOM   6602  O O   . PRO   B 1 367 ? -2.959  -14.899 9.383   1.00 64.83  ?  367 PRO   B O   1 
ATOM   6603  C CB  . PRO   B 1 367 ? -3.263  -15.920 6.192   1.00 66.69  ?  367 PRO   B CB  1 
ATOM   6604  C CG  . PRO   B 1 367 ? -3.145  -17.297 6.768   1.00 68.46  ?  367 PRO   B CG  1 
ATOM   6605  C CD  . PRO   B 1 367 ? -1.707  -17.430 7.218   1.00 66.89  ?  367 PRO   B CD  1 
ATOM   6606  N N   . GLY   B 1 368 ? -3.868  -13.435 7.924   1.00 67.02  ?  368 GLY   B N   1 
ATOM   6607  C CA  . GLY   B 1 368 ? -4.597  -12.726 8.965   1.00 62.34  ?  368 GLY   B CA  1 
ATOM   6608  C C   . GLY   B 1 368 ? -5.615  -13.582 9.696   1.00 69.58  ?  368 GLY   B C   1 
ATOM   6609  O O   . GLY   B 1 368 ? -5.832  -13.405 10.898  1.00 66.25  ?  368 GLY   B O   1 
ATOM   6610  N N   . ASP   B 1 369 ? -6.256  -14.518 8.989   1.00 74.81  ?  369 ASP   B N   1 
ATOM   6611  C CA  . ASP   B 1 369 ? -7.247  -15.374 9.633   1.00 71.99  ?  369 ASP   B CA  1 
ATOM   6612  C C   . ASP   B 1 369 ? -6.603  -16.363 10.597  1.00 71.24  ?  369 ASP   B C   1 
ATOM   6613  O O   . ASP   B 1 369 ? -7.258  -16.822 11.540  1.00 75.50  ?  369 ASP   B O   1 
ATOM   6614  C CB  . ASP   B 1 369 ? -8.065  -16.118 8.577   1.00 74.59  ?  369 ASP   B CB  1 
ATOM   6615  C CG  . ASP   B 1 369 ? -7.202  -16.965 7.659   1.00 80.49  ?  369 ASP   B CG  1 
ATOM   6616  O OD1 . ASP   B 1 369 ? -6.759  -18.051 8.088   1.00 78.09  ?  369 ASP   B OD1 1 
ATOM   6617  O OD2 . ASP   B 1 369 ? -6.963  -16.542 6.508   1.00 88.27  ?  369 ASP   B OD2 1 
ATOM   6618  N N   . GLN   B 1 370 ? -5.334  -16.710 10.377  1.00 68.61  ?  370 GLN   B N   1 
ATOM   6619  C CA  . GLN   B 1 370 ? -4.588  -17.588 11.269  1.00 70.19  ?  370 GLN   B CA  1 
ATOM   6620  C C   . GLN   B 1 370 ? -3.860  -16.823 12.371  1.00 66.71  ?  370 GLN   B C   1 
ATOM   6621  O O   . GLN   B 1 370 ? -2.942  -17.374 12.989  1.00 62.21  ?  370 GLN   B O   1 
ATOM   6622  C CB  . GLN   B 1 370 ? -3.591  -18.434 10.472  1.00 71.92  ?  370 GLN   B CB  1 
ATOM   6623  C CG  . GLN   B 1 370 ? -4.227  -19.473 9.561   1.00 70.48  ?  370 GLN   B CG  1 
ATOM   6624  C CD  . GLN   B 1 370 ? -3.194  -20.302 8.820   1.00 71.90  ?  370 GLN   B CD  1 
ATOM   6625  O OE1 . GLN   B 1 370 ? -1.992  -20.053 8.923   1.00 73.94  ?  370 GLN   B OE1 1 
ATOM   6626  N NE2 . GLN   B 1 370 ? -3.658  -21.296 8.070   1.00 72.25  ?  370 GLN   B NE2 1 
ATOM   6627  N N   . PHE   B 1 371 ? -4.238  -15.561 12.608  1.00 62.84  ?  371 PHE   B N   1 
ATOM   6628  C CA  . PHE   B 1 371 ? -3.771  -14.730 13.714  1.00 63.58  ?  371 PHE   B CA  1 
ATOM   6629  C C   . PHE   B 1 371 ? -2.251  -14.613 13.738  1.00 59.49  ?  371 PHE   B C   1 
ATOM   6630  O O   . PHE   B 1 371 ? -1.592  -15.278 14.549  1.00 61.45  ?  371 PHE   B O   1 
ATOM   6631  C CB  . PHE   B 1 371 ? -4.279  -15.294 15.043  1.00 63.08  ?  371 PHE   B CB  1 
ATOM   6632  C CG  . PHE   B 1 371 ? -5.699  -15.773 14.985  1.00 63.50  ?  371 PHE   B CG  1 
ATOM   6633  C CD1 . PHE   B 1 371 ? -6.746  -14.867 14.995  1.00 61.96  ?  371 PHE   B CD1 1 
ATOM   6634  C CD2 . PHE   B 1 371 ? -5.987  -17.129 14.905  1.00 67.75  ?  371 PHE   B CD2 1 
ATOM   6635  C CE1 . PHE   B 1 371 ? -8.055  -15.302 14.935  1.00 64.30  ?  371 PHE   B CE1 1 
ATOM   6636  C CE2 . PHE   B 1 371 ? -7.295  -17.571 14.838  1.00 64.00  ?  371 PHE   B CE2 1 
ATOM   6637  C CZ  . PHE   B 1 371 ? -8.329  -16.655 14.853  1.00 62.23  ?  371 PHE   B CZ  1 
ATOM   6638  N N   . PRO   B 1 372 ? -1.656  -13.781 12.878  1.00 59.10  ?  372 PRO   B N   1 
ATOM   6639  C CA  . PRO   B 1 372 ? -0.195  -13.612 12.942  1.00 57.64  ?  372 PRO   B CA  1 
ATOM   6640  C C   . PRO   B 1 372 ? 0.273   -13.035 14.267  1.00 47.83  ?  372 PRO   B C   1 
ATOM   6641  O O   . PRO   B 1 372 ? 1.242   -13.540 14.850  1.00 43.33  ?  372 PRO   B O   1 
ATOM   6642  C CB  . PRO   B 1 372 ? 0.103   -12.668 11.766  1.00 50.54  ?  372 PRO   B CB  1 
ATOM   6643  C CG  . PRO   B 1 372 ? -1.086  -12.770 10.870  1.00 61.02  ?  372 PRO   B CG  1 
ATOM   6644  C CD  . PRO   B 1 372 ? -2.255  -13.013 11.776  1.00 63.18  ?  372 PRO   B CD  1 
ATOM   6645  N N   . ALA   B 1 373 ? -0.403  -11.996 14.767  1.00 43.35  ?  373 ALA   B N   1 
ATOM   6646  C CA  . ALA   B 1 373 ? 0.023   -11.361 16.011  1.00 47.66  ?  373 ALA   B CA  1 
ATOM   6647  C C   . ALA   B 1 373 ? -0.046  -12.330 17.185  1.00 43.36  ?  373 ALA   B C   1 
ATOM   6648  O O   . ALA   B 1 373 ? 0.856   -12.353 18.030  1.00 40.48  ?  373 ALA   B O   1 
ATOM   6649  C CB  . ALA   B 1 373 ? -0.827  -10.123 16.291  1.00 47.04  ?  373 ALA   B CB  1 
ATOM   6650  N N   . GLN   B 1 374 ? -1.107  -13.136 17.261  1.00 42.77  ?  374 GLN   B N   1 
ATOM   6651  C CA  . GLN   B 1 374 ? -1.208  -14.086 18.362  1.00 39.47  ?  374 GLN   B CA  1 
ATOM   6652  C C   . GLN   B 1 374 ? -0.095  -15.118 18.291  1.00 38.58  ?  374 GLN   B C   1 
ATOM   6653  O O   . GLN   B 1 374 ? 0.434   -15.539 19.325  1.00 36.27  ?  374 GLN   B O   1 
ATOM   6654  C CB  . GLN   B 1 374 ? -2.575  -14.769 18.361  1.00 48.49  ?  374 GLN   B CB  1 
ATOM   6655  C CG  . GLN   B 1 374 ? -2.948  -15.383 19.703  1.00 37.03  ?  374 GLN   B CG  1 
ATOM   6656  C CD  . GLN   B 1 374 ? -2.772  -14.400 20.844  1.00 39.31  ?  374 GLN   B CD  1 
ATOM   6657  O OE1 . GLN   B 1 374 ? -3.464  -13.383 20.916  1.00 40.24  ?  374 GLN   B OE1 1 
ATOM   6658  N NE2 . GLN   B 1 374 ? -1.828  -14.691 21.738  1.00 33.18  ?  374 GLN   B NE2 1 
ATOM   6659  N N   . ALA   B 1 375 ? 0.292   -15.518 17.080  1.00 39.31  ?  375 ALA   B N   1 
ATOM   6660  C CA  . ALA   B 1 375 ? 1.356   -16.507 16.939  1.00 43.04  ?  375 ALA   B CA  1 
ATOM   6661  C C   . ALA   B 1 375 ? 2.682   -15.962 17.450  1.00 36.38  ?  375 ALA   B C   1 
ATOM   6662  O O   . ALA   B 1 375 ? 3.441   -16.671 18.124  1.00 36.93  ?  375 ALA   B O   1 
ATOM   6663  C CB  . ALA   B 1 375 ? 1.475   -16.941 15.478  1.00 46.41  ?  375 ALA   B CB  1 
ATOM   6664  N N   . VAL   B 1 376 ? 2.983   -14.702 17.135  1.00 37.45  ?  376 VAL   B N   1 
ATOM   6665  C CA  . VAL   B 1 376 ? 4.174   -14.069 17.694  1.00 37.04  ?  376 VAL   B CA  1 
ATOM   6666  C C   . VAL   B 1 376 ? 4.070   -13.998 19.214  1.00 32.92  ?  376 VAL   B C   1 
ATOM   6667  O O   . VAL   B 1 376 ? 5.021   -14.331 19.935  1.00 33.77  ?  376 VAL   B O   1 
ATOM   6668  C CB  . VAL   B 1 376 ? 4.375   -12.677 17.069  1.00 32.29  ?  376 VAL   B CB  1 
ATOM   6669  C CG1 . VAL   B 1 376 ? 5.577   -12.002 17.682  1.00 38.47  ?  376 VAL   B CG1 1 
ATOM   6670  C CG2 . VAL   B 1 376 ? 4.532   -12.792 15.553  1.00 35.94  ?  376 VAL   B CG2 1 
ATOM   6671  N N   . ILE   B 1 377 ? 2.902   -13.588 19.720  1.00 34.32  ?  377 ILE   B N   1 
ATOM   6672  C CA  . ILE   B 1 377 ? 2.684   -13.482 21.162  1.00 33.98  ?  377 ILE   B CA  1 
ATOM   6673  C C   . ILE   B 1 377 ? 2.870   -14.831 21.836  1.00 30.48  ?  377 ILE   B C   1 
ATOM   6674  O O   . ILE   B 1 377 ? 3.494   -14.930 22.898  1.00 29.48  ?  377 ILE   B O   1 
ATOM   6675  C CB  . ILE   B 1 377 ? 1.286   -12.908 21.444  1.00 32.47  ?  377 ILE   B CB  1 
ATOM   6676  C CG1 . ILE   B 1 377 ? 1.217   -11.450 21.018  1.00 28.58  ?  377 ILE   B CG1 1 
ATOM   6677  C CG2 . ILE   B 1 377 ? 0.929   -13.038 22.915  1.00 28.05  ?  377 ILE   B CG2 1 
ATOM   6678  C CD1 . ILE   B 1 377 ? -0.183  -10.950 20.941  1.00 31.29  ?  377 ILE   B CD1 1 
ATOM   6679  N N   . ASN   B 1 378 ? 2.325   -15.890 21.239  1.00 34.42  ?  378 ASN   B N   1 
ATOM   6680  C CA  . ASN   B 1 378 ? 2.440   -17.202 21.863  1.00 31.65  ?  378 ASN   B CA  1 
ATOM   6681  C C   . ASN   B 1 378 ? 3.882   -17.689 21.849  1.00 33.18  ?  378 ASN   B C   1 
ATOM   6682  O O   . ASN   B 1 378 ? 4.364   -18.243 22.845  1.00 34.49  ?  378 ASN   B O   1 
ATOM   6683  C CB  . ASN   B 1 378 ? 1.506   -18.193 21.172  1.00 35.73  ?  378 ASN   B CB  1 
ATOM   6684  C CG  . ASN   B 1 378 ? 0.053   -17.965 21.536  1.00 39.13  ?  378 ASN   B CG  1 
ATOM   6685  O OD1 . ASN   B 1 378 ? -0.276  -17.033 22.275  1.00 37.16  ?  378 ASN   B OD1 1 
ATOM   6686  N ND2 . ASN   B 1 378 ? -0.824  -18.813 21.027  1.00 39.79  ?  378 ASN   B ND2 1 
ATOM   6687  N N   . ALA   B 1 379 ? 4.594   -17.466 20.744  1.00 33.91  ?  379 ALA   B N   1 
ATOM   6688  C CA  . ALA   B 1 379 ? 5.999   -17.853 20.692  1.00 32.64  ?  379 ALA   B CA  1 
ATOM   6689  C C   . ALA   B 1 379 ? 6.821   -17.037 21.678  1.00 33.76  ?  379 ALA   B C   1 
ATOM   6690  O O   . ALA   B 1 379 ? 7.691   -17.580 22.369  1.00 38.48  ?  379 ALA   B O   1 
ATOM   6691  C CB  . ALA   B 1 379 ? 6.540   -17.694 19.271  1.00 32.99  ?  379 ALA   B CB  1 
ATOM   6692  N N   . LEU   B 1 380 ? 6.548   -15.733 21.767  1.00 31.60  ?  380 LEU   B N   1 
ATOM   6693  C CA  . LEU   B 1 380 ? 7.230   -14.898 22.752  1.00 30.60  ?  380 LEU   B CA  1 
ATOM   6694  C C   . LEU   B 1 380 ? 7.000   -15.412 24.171  1.00 33.51  ?  380 LEU   B C   1 
ATOM   6695  O O   . LEU   B 1 380 ? 7.924   -15.418 24.997  1.00 27.85  ?  380 LEU   B O   1 
ATOM   6696  C CB  . LEU   B 1 380 ? 6.758   -13.451 22.621  1.00 30.43  ?  380 LEU   B CB  1 
ATOM   6697  C CG  . LEU   B 1 380 ? 7.345   -12.475 23.639  1.00 27.77  ?  380 LEU   B CG  1 
ATOM   6698  C CD1 . LEU   B 1 380 ? 8.833   -12.340 23.409  1.00 28.62  ?  380 LEU   B CD1 1 
ATOM   6699  C CD2 . LEU   B 1 380 ? 6.646   -11.118 23.561  1.00 24.67  ?  380 LEU   B CD2 1 
ATOM   6700  N N   . TYR   B 1 381 ? 5.779   -15.857 24.475  1.00 30.16  ?  381 TYR   B N   1 
ATOM   6701  C CA  . TYR   B 1 381 ? 5.517   -16.385 25.808  1.00 29.85  ?  381 TYR   B CA  1 
ATOM   6702  C C   . TYR   B 1 381 ? 6.243   -17.703 26.026  1.00 34.05  ?  381 TYR   B C   1 
ATOM   6703  O O   . TYR   B 1 381 ? 6.884   -17.903 27.063  1.00 35.87  ?  381 TYR   B O   1 
ATOM   6704  C CB  . TYR   B 1 381 ? 4.020   -16.573 26.045  1.00 26.38  ?  381 TYR   B CB  1 
ATOM   6705  C CG  . TYR   B 1 381 ? 3.770   -17.329 27.335  1.00 31.89  ?  381 TYR   B CG  1 
ATOM   6706  C CD1 . TYR   B 1 381 ? 3.908   -16.698 28.564  1.00 28.27  ?  381 TYR   B CD1 1 
ATOM   6707  C CD2 . TYR   B 1 381 ? 3.445   -18.682 27.324  1.00 30.58  ?  381 TYR   B CD2 1 
ATOM   6708  C CE1 . TYR   B 1 381 ? 3.702   -17.384 29.749  1.00 31.90  ?  381 TYR   B CE1 1 
ATOM   6709  C CE2 . TYR   B 1 381 ? 3.241   -19.377 28.499  1.00 33.70  ?  381 TYR   B CE2 1 
ATOM   6710  C CZ  . TYR   B 1 381 ? 3.372   -18.725 29.709  1.00 35.76  ?  381 TYR   B CZ  1 
ATOM   6711  O OH  . TYR   B 1 381 ? 3.170   -19.413 30.884  1.00 40.25  ?  381 TYR   B OH  1 
ATOM   6712  N N   . LEU   B 1 382 ? 6.136   -18.629 25.068  1.00 34.94  ?  382 LEU   B N   1 
ATOM   6713  C CA  . LEU   B 1 382 ? 6.804   -19.917 25.224  1.00 34.03  ?  382 LEU   B CA  1 
ATOM   6714  C C   . LEU   B 1 382 ? 8.311   -19.749 25.352  1.00 40.68  ?  382 LEU   B C   1 
ATOM   6715  O O   . LEU   B 1 382 ? 8.960   -20.509 26.079  1.00 42.84  ?  382 LEU   B O   1 
ATOM   6716  C CB  . LEU   B 1 382 ? 6.476   -20.833 24.045  1.00 42.47  ?  382 LEU   B CB  1 
ATOM   6717  C CG  . LEU   B 1 382 ? 5.034   -21.321 23.887  1.00 37.82  ?  382 LEU   B CG  1 
ATOM   6718  C CD1 . LEU   B 1 382 ? 4.852   -21.999 22.548  1.00 43.12  ?  382 LEU   B CD1 1 
ATOM   6719  C CD2 . LEU   B 1 382 ? 4.655   -22.265 25.016  1.00 41.39  ?  382 LEU   B CD2 1 
ATOM   6720  N N   . GLU   B 1 383 ? 8.879   -18.743 24.681  1.00 40.42  ?  383 GLU   B N   1 
ATOM   6721  C CA  . GLU   B 1 383 ? 10.327  -18.577 24.681  1.00 39.43  ?  383 GLU   B CA  1 
ATOM   6722  C C   . GLU   B 1 383 ? 10.838  -17.879 25.932  1.00 35.80  ?  383 GLU   B C   1 
ATOM   6723  O O   . GLU   B 1 383 ? 11.992  -18.089 26.318  1.00 38.20  ?  383 GLU   B O   1 
ATOM   6724  C CB  . GLU   B 1 383 ? 10.772  -17.796 23.442  1.00 40.98  ?  383 GLU   B CB  1 
ATOM   6725  C CG  . GLU   B 1 383 ? 12.260  -17.942 23.103  1.00 46.90  ?  383 GLU   B CG  1 
ATOM   6726  C CD  . GLU   B 1 383 ? 12.580  -19.235 22.356  1.00 51.06  ?  383 GLU   B CD  1 
ATOM   6727  O OE1 . GLU   B 1 383 ? 11.785  -20.205 22.426  1.00 44.90  ?  383 GLU   B OE1 1 
ATOM   6728  O OE2 . GLU   B 1 383 ? 13.632  -19.276 21.684  1.00 52.48  ?  383 GLU   B OE2 1 
ATOM   6729  N N   . SER   B 1 384 ? 10.014  -17.058 26.582  1.00 37.34  ?  384 SER   B N   1 
ATOM   6730  C CA  . SER   B 1 384 ? 10.532  -16.212 27.652  1.00 33.75  ?  384 SER   B CA  1 
ATOM   6731  C C   . SER   B 1 384 ? 9.620   -16.044 28.851  1.00 30.88  ?  384 SER   B C   1 
ATOM   6732  O O   . SER   B 1 384 ? 10.081  -15.502 29.860  1.00 30.16  ?  384 SER   B O   1 
ATOM   6733  C CB  . SER   B 1 384 ? 10.847  -14.815 27.110  1.00 32.31  ?  384 SER   B CB  1 
ATOM   6734  O OG  . SER   B 1 384 ? 9.642   -14.125 26.818  1.00 31.47  ?  384 SER   B OG  1 
ATOM   6735  N N   . GLY   B 1 385 ? 8.356   -16.452 28.787  1.00 30.72  ?  385 GLY   B N   1 
ATOM   6736  C CA  . GLY   B 1 385 ? 7.443   -16.189 29.879  1.00 30.55  ?  385 GLY   B CA  1 
ATOM   6737  C C   . GLY   B 1 385 ? 6.895   -14.782 29.919  1.00 28.85  ?  385 GLY   B C   1 
ATOM   6738  O O   . GLY   B 1 385 ? 6.249   -14.413 30.908  1.00 27.60  ?  385 GLY   B O   1 
ATOM   6739  N N   . VAL   B 1 386 ? 7.152   -13.983 28.889  1.00 25.90  ?  386 VAL   B N   1 
ATOM   6740  C CA  . VAL   B 1 386 ? 6.535   -12.670 28.747  1.00 24.03  ?  386 VAL   B CA  1 
ATOM   6741  C C   . VAL   B 1 386 ? 5.140   -12.854 28.164  1.00 25.00  ?  386 VAL   B C   1 
ATOM   6742  O O   . VAL   B 1 386 ? 4.954   -13.607 27.201  1.00 25.30  ?  386 VAL   B O   1 
ATOM   6743  C CB  . VAL   B 1 386 ? 7.397   -11.760 27.855  1.00 24.53  ?  386 VAL   B CB  1 
ATOM   6744  C CG1 . VAL   B 1 386 ? 6.694   -10.434 27.593  1.00 20.76  ?  386 VAL   B CG1 1 
ATOM   6745  C CG2 . VAL   B 1 386 ? 8.766   -11.534 28.484  1.00 26.05  ?  386 VAL   B CG2 1 
ATOM   6746  N N   . ARG   B 1 387 ? 4.154   -12.180 28.753  1.00 24.70  ?  387 ARG   B N   1 
ATOM   6747  C CA  . ARG   B 1 387 ? 2.788   -12.181 28.244  1.00 22.35  ?  387 ARG   B CA  1 
ATOM   6748  C C   . ARG   B 1 387 ? 2.479   -10.822 27.629  1.00 19.49  ?  387 ARG   B C   1 
ATOM   6749  O O   . ARG   B 1 387 ? 2.502   -9.803  28.327  1.00 18.99  ?  387 ARG   B O   1 
ATOM   6750  C CB  . ARG   B 1 387 ? 1.774   -12.504 29.343  1.00 18.87  ?  387 ARG   B CB  1 
ATOM   6751  C CG  . ARG   B 1 387 ? 0.348   -12.148 28.935  1.00 18.22  ?  387 ARG   B CG  1 
ATOM   6752  C CD  . ARG   B 1 387 ? -0.684  -12.848 29.793  1.00 22.43  ?  387 ARG   B CD  1 
ATOM   6753  N NE  . ARG   B 1 387 ? -0.776  -12.302 31.144  1.00 16.28  ?  387 ARG   B NE  1 
ATOM   6754  C CZ  . ARG   B 1 387 ? -1.556  -12.803 32.090  1.00 21.91  ?  387 ARG   B CZ  1 
ATOM   6755  N NH1 . ARG   B 1 387 ? -2.321  -13.863 31.868  1.00 20.54  ?  387 ARG   B NH1 1 
ATOM   6756  N NH2 . ARG   B 1 387 ? -1.573  -12.227 33.291  1.00 21.11  ?  387 ARG   B NH2 1 
ATOM   6757  N N   . ALA   B 1 388 ? 2.172   -10.821 26.338  1.00 18.86  ?  388 ALA   B N   1 
ATOM   6758  C CA  . ALA   B 1 388 ? 1.719   -9.659  25.588  1.00 18.59  ?  388 ALA   B CA  1 
ATOM   6759  C C   . ALA   B 1 388 ? 0.267   -9.862  25.156  1.00 23.30  ?  388 ALA   B C   1 
ATOM   6760  O O   . ALA   B 1 388 ? -0.362  -10.881 25.451  1.00 21.70  ?  388 ALA   B O   1 
ATOM   6761  C CB  . ALA   B 1 388 ? 2.627   -9.411  24.386  1.00 21.07  ?  388 ALA   B CB  1 
ATOM   6762  N N   . VAL   B 1 389 ? -0.267  -8.876  24.443  1.00 21.79  ?  389 VAL   B N   1 
ATOM   6763  C CA  . VAL   B 1 389 ? -1.667  -8.869  24.041  1.00 26.95  ?  389 VAL   B CA  1 
ATOM   6764  C C   . VAL   B 1 389 ? -1.736  -8.480  22.569  1.00 25.59  ?  389 VAL   B C   1 
ATOM   6765  O O   . VAL   B 1 389 ? -0.881  -7.746  22.062  1.00 22.32  ?  389 VAL   B O   1 
ATOM   6766  C CB  . VAL   B 1 389 ? -2.496  -7.907  24.925  1.00 21.75  ?  389 VAL   B CB  1 
ATOM   6767  C CG1 . VAL   B 1 389 ? -2.129  -6.442  24.634  1.00 21.00  ?  389 VAL   B CG1 1 
ATOM   6768  C CG2 . VAL   B 1 389 ? -3.976  -8.159  24.767  1.00 24.46  ?  389 VAL   B CG2 1 
ATOM   6769  N N   . GLU   B 1 390 ? -2.742  -9.000  21.871  1.00 31.45  ?  390 GLU   B N   1 
ATOM   6770  C CA  . GLU   B 1 390 ? -2.894  -8.753  20.444  1.00 34.15  ?  390 GLU   B CA  1 
ATOM   6771  C C   . GLU   B 1 390 ? -3.838  -7.590  20.178  1.00 33.74  ?  390 GLU   B C   1 
ATOM   6772  O O   . GLU   B 1 390 ? -4.897  -7.476  20.799  1.00 34.40  ?  390 GLU   B O   1 
ATOM   6773  C CB  . GLU   B 1 390 ? -3.417  -9.987  19.705  1.00 36.09  ?  390 GLU   B CB  1 
ATOM   6774  C CG  . GLU   B 1 390 ? -3.812  -9.666  18.268  1.00 43.83  ?  390 GLU   B CG  1 
ATOM   6775  C CD  . GLU   B 1 390 ? -4.252  -10.877 17.479  1.00 50.88  ?  390 GLU   B CD  1 
ATOM   6776  O OE1 . GLU   B 1 390 ? -3.998  -12.008 17.939  1.00 56.63  ?  390 GLU   B OE1 1 
ATOM   6777  O OE2 . GLU   B 1 390 ? -4.849  -10.700 16.396  1.00 54.41  ?  390 GLU   B OE2 1 
ATOM   6778  N N   . ILE   B 1 391 ? -3.436  -6.731  19.249  1.00 34.17  ?  391 ILE   B N   1 
ATOM   6779  C CA  . ILE   B 1 391 ? -4.310  -5.730  18.659  1.00 43.02  ?  391 ILE   B CA  1 
ATOM   6780  C C   . ILE   B 1 391 ? -4.387  -6.047  17.169  1.00 47.24  ?  391 ILE   B C   1 
ATOM   6781  O O   . ILE   B 1 391 ? -3.738  -5.383  16.351  1.00 50.64  ?  391 ILE   B O   1 
ATOM   6782  C CB  . ILE   B 1 391 ? -3.788  -4.302  18.914  1.00 40.85  ?  391 ILE   B CB  1 
ATOM   6783  C CG1 . ILE   B 1 391 ? -3.414  -4.112  20.389  1.00 34.04  ?  391 ILE   B CG1 1 
ATOM   6784  C CG2 . ILE   B 1 391 ? -4.807  -3.265  18.476  1.00 44.43  ?  391 ILE   B CG2 1 
ATOM   6785  C CD1 . ILE   B 1 391 ? -4.532  -4.400  21.378  1.00 34.71  ?  391 ILE   B CD1 1 
ATOM   6786  N N   . GLY   B 1 392 ? -5.151  -7.077  16.812  1.00 45.80  ?  392 GLY   B N   1 
ATOM   6787  C CA  . GLY   B 1 392 ? -5.189  -7.565  15.446  1.00 52.87  ?  392 GLY   B CA  1 
ATOM   6788  C C   . GLY   B 1 392 ? -6.469  -8.303  15.090  1.00 54.43  ?  392 GLY   B C   1 
ATOM   6789  O O   . GLY   B 1 392 ? -7.553  -7.967  15.572  1.00 54.53  ?  392 GLY   B O   1 
ATOM   6790  N N   . SER   B 1 393 ? -6.330  -9.321  14.228  1.00 61.33  ?  393 SER   B N   1 
ATOM   6791  C CA  . SER   B 1 393 ? -7.480  -10.072 13.721  1.00 58.55  ?  393 SER   B CA  1 
ATOM   6792  C C   . SER   B 1 393 ? -8.137  -10.942 14.785  1.00 55.94  ?  393 SER   B C   1 
ATOM   6793  O O   . SER   B 1 393 ? -9.312  -11.290 14.639  1.00 53.81  ?  393 SER   B O   1 
ATOM   6794  C CB  . SER   B 1 393 ? -7.066  -10.961 12.544  1.00 56.52  ?  393 SER   B CB  1 
ATOM   6795  O OG  . SER   B 1 393 ? -6.697  -10.200 11.406  1.00 57.62  ?  393 SER   B OG  1 
ATOM   6796  N N   . PHE   B 1 394 ? -7.408  -11.325 15.832  1.00 47.80  ?  394 PHE   B N   1 
ATOM   6797  C CA  . PHE   B 1 394 ? -8.025  -12.099 16.903  1.00 53.39  ?  394 PHE   B CA  1 
ATOM   6798  C C   . PHE   B 1 394 ? -8.917  -11.220 17.769  1.00 53.36  ?  394 PHE   B C   1 
ATOM   6799  O O   . PHE   B 1 394 ? -10.018 -11.635 18.146  1.00 56.16  ?  394 PHE   B O   1 
ATOM   6800  C CB  . PHE   B 1 394 ? -6.949  -12.782 17.743  1.00 54.73  ?  394 PHE   B CB  1 
ATOM   6801  C CG  . PHE   B 1 394 ? -7.484  -13.671 18.830  1.00 57.60  ?  394 PHE   B CG  1 
ATOM   6802  C CD1 . PHE   B 1 394 ? -8.381  -14.686 18.539  1.00 57.64  ?  394 PHE   B CD1 1 
ATOM   6803  C CD2 . PHE   B 1 394 ? -7.062  -13.510 20.142  1.00 47.62  ?  394 PHE   B CD2 1 
ATOM   6804  C CE1 . PHE   B 1 394 ? -8.865  -15.514 19.544  1.00 53.91  ?  394 PHE   B CE1 1 
ATOM   6805  C CE2 . PHE   B 1 394 ? -7.537  -14.333 21.147  1.00 48.53  ?  394 PHE   B CE2 1 
ATOM   6806  C CZ  . PHE   B 1 394 ? -8.442  -15.335 20.848  1.00 50.20  ?  394 PHE   B CZ  1 
ATOM   6807  N N   . LEU   B 1 395 ? -8.467  -10.002 18.094  1.00 50.78  ?  395 LEU   B N   1 
ATOM   6808  C CA  . LEU   B 1 395 ? -9.339  -9.081  18.817  1.00 49.54  ?  395 LEU   B CA  1 
ATOM   6809  C C   . LEU   B 1 395 ? -10.522 -8.661  17.964  1.00 60.15  ?  395 LEU   B C   1 
ATOM   6810  O O   . LEU   B 1 395 ? -11.621 -8.458  18.492  1.00 58.81  ?  395 LEU   B O   1 
ATOM   6811  C CB  . LEU   B 1 395 ? -8.568  -7.840  19.278  1.00 51.98  ?  395 LEU   B CB  1 
ATOM   6812  C CG  . LEU   B 1 395 ? -9.312  -6.823  20.165  1.00 49.75  ?  395 LEU   B CG  1 
ATOM   6813  C CD1 . LEU   B 1 395 ? -8.352  -6.126  21.114  1.00 53.85  ?  395 LEU   B CD1 1 
ATOM   6814  C CD2 . LEU   B 1 395 ? -10.079 -5.772  19.359  1.00 54.98  ?  395 LEU   B CD2 1 
ATOM   6815  N N   . LEU   B 1 396 ? -10.314 -8.521  16.652  1.00 80.48  ?  396 LEU   B N   1 
ATOM   6816  C CA  . LEU   B 1 396 ? -11.353 -7.980  15.783  1.00 79.67  ?  396 LEU   B CA  1 
ATOM   6817  C C   . LEU   B 1 396 ? -12.599 -8.861  15.794  1.00 81.40  ?  396 LEU   B C   1 
ATOM   6818  O O   . LEU   B 1 396 ? -13.715 -8.374  16.010  1.00 89.37  ?  396 LEU   B O   1 
ATOM   6819  C CB  . LEU   B 1 396 ? -10.804 -7.814  14.365  1.00 80.82  ?  396 LEU   B CB  1 
ATOM   6820  C CG  . LEU   B 1 396 ? -11.669 -6.996  13.406  1.00 87.33  ?  396 LEU   B CG  1 
ATOM   6821  C CD1 . LEU   B 1 396 ? -12.016 -5.657  14.029  1.00 88.60  ?  396 LEU   B CD1 1 
ATOM   6822  C CD2 . LEU   B 1 396 ? -10.957 -6.795  12.084  1.00 86.87  ?  396 LEU   B CD2 1 
ATOM   6823  N N   . GLY   B 1 397 ? -12.426 -10.160 15.580  1.00 69.36  ?  397 GLY   B N   1 
ATOM   6824  C CA  . GLY   B 1 397 ? -13.532 -11.099 15.600  1.00 64.47  ?  397 GLY   B CA  1 
ATOM   6825  C C   . GLY   B 1 397 ? -14.030 -11.447 14.211  1.00 69.67  ?  397 GLY   B C   1 
ATOM   6826  O O   . GLY   B 1 397 ? -13.416 -11.138 13.184  1.00 66.16  ?  397 GLY   B O   1 
ATOM   6827  N N   . ARG   B 1 398 ? -15.180 -12.118 14.192  1.00 65.55  ?  398 ARG   B N   1 
ATOM   6828  C CA  . ARG   B 1 398 ? -15.823 -12.515 12.947  1.00 72.39  ?  398 ARG   B CA  1 
ATOM   6829  C C   . ARG   B 1 398 ? -16.845 -11.472 12.517  1.00 79.64  ?  398 ARG   B C   1 
ATOM   6830  O O   . ARG   B 1 398 ? -17.527 -10.867 13.350  1.00 74.05  ?  398 ARG   B O   1 
ATOM   6831  C CB  . ARG   B 1 398 ? -16.502 -13.880 13.087  1.00 69.58  ?  398 ARG   B CB  1 
ATOM   6832  C CG  . ARG   B 1 398 ? -15.530 -15.049 13.128  1.00 68.66  ?  398 ARG   B CG  1 
ATOM   6833  C CD  . ARG   B 1 398 ? -16.241 -16.389 12.978  1.00 67.28  ?  398 ARG   B CD  1 
ATOM   6834  N NE  . ARG   B 1 398 ? -15.356 -17.506 13.293  1.00 66.96  ?  398 ARG   B NE  1 
ATOM   6835  C CZ  . ARG   B 1 398 ? -14.655 -18.192 12.399  1.00 68.35  ?  398 ARG   B CZ  1 
ATOM   6836  N NH1 . ARG   B 1 398 ? -14.730 -17.923 11.106  1.00 68.90  ?  398 ARG   B NH1 1 
ATOM   6837  N NH2 . ARG   B 1 398 ? -13.859 -19.175 12.815  1.00 66.81  ?  398 ARG   B NH2 1 
ATOM   6838  N N   . ASP   B 1 399 ? -16.936 -11.265 11.207  1.00 90.15  ?  399 ASP   B N   1 
ATOM   6839  C CA  . ASP   B 1 399 ? -17.905 -10.332 10.654  1.00 91.91  ?  399 ASP   B CA  1 
ATOM   6840  C C   . ASP   B 1 399 ? -19.322 -10.835 10.924  1.00 95.75  ?  399 ASP   B C   1 
ATOM   6841  O O   . ASP   B 1 399 ? -19.640 -11.985 10.587  1.00 96.66  ?  399 ASP   B O   1 
ATOM   6842  C CB  . ASP   B 1 399 ? -17.679 -10.172 9.152   1.00 91.89  ?  399 ASP   B CB  1 
ATOM   6843  C CG  . ASP   B 1 399 ? -18.684 -9.246  8.505   1.00 96.77  ?  399 ASP   B CG  1 
ATOM   6844  O OD1 . ASP   B 1 399 ? -19.096 -8.265  9.156   1.00 97.36  ?  399 ASP   B OD1 1 
ATOM   6845  O OD2 . ASP   B 1 399 ? -19.071 -9.507  7.345   1.00 97.13  ?  399 ASP   B OD2 1 
ATOM   6846  N N   . PRO   B 1 400 ? -20.191 -10.023 11.532  1.00 89.32  ?  400 PRO   B N   1 
ATOM   6847  C CA  . PRO   B 1 400 ? -21.567 -10.483 11.787  1.00 89.01  ?  400 PRO   B CA  1 
ATOM   6848  C C   . PRO   B 1 400 ? -22.357 -10.758 10.521  1.00 93.23  ?  400 PRO   B C   1 
ATOM   6849  O O   . PRO   B 1 400 ? -23.353 -11.491 10.573  1.00 89.98  ?  400 PRO   B O   1 
ATOM   6850  C CB  . PRO   B 1 400 ? -22.183 -9.323  12.584  1.00 85.82  ?  400 PRO   B CB  1 
ATOM   6851  C CG  . PRO   B 1 400 ? -21.020 -8.562  13.130  1.00 85.62  ?  400 PRO   B CG  1 
ATOM   6852  C CD  . PRO   B 1 400 ? -19.938 -8.693  12.108  1.00 90.54  ?  400 PRO   B CD  1 
ATOM   6853  N N   . ALA   B 1 401 ? -21.943 -10.202 9.387   1.00 88.49  ?  401 ALA   B N   1 
ATOM   6854  C CA  . ALA   B 1 401 ? -22.691 -10.326 8.148   1.00 83.80  ?  401 ALA   B CA  1 
ATOM   6855  C C   . ALA   B 1 401 ? -22.220 -11.477 7.269   1.00 86.25  ?  401 ALA   B C   1 
ATOM   6856  O O   . ALA   B 1 401 ? -22.903 -11.807 6.292   1.00 78.34  ?  401 ALA   B O   1 
ATOM   6857  C CB  . ALA   B 1 401 ? -22.609 -9.016  7.368   1.00 81.29  ?  401 ALA   B CB  1 
ATOM   6858  N N   . THR   B 1 402 ? -21.075 -12.088 7.580   1.00 93.56  ?  402 THR   B N   1 
ATOM   6859  C CA  . THR   B 1 402 ? -20.589 -13.246 6.837   1.00 94.08  ?  402 THR   B CA  1 
ATOM   6860  C C   . THR   B 1 402 ? -20.267 -14.453 7.704   1.00 97.94  ?  402 THR   B C   1 
ATOM   6861  O O   . THR   B 1 402 ? -20.194 -15.565 7.165   1.00 96.15  ?  402 THR   B O   1 
ATOM   6862  C CB  . THR   B 1 402 ? -19.332 -12.890 6.028   1.00 93.25  ?  402 THR   B CB  1 
ATOM   6863  O OG1 . THR   B 1 402 ? -18.321 -12.378 6.904   1.00 94.58  ?  402 THR   B OG1 1 
ATOM   6864  C CG2 . THR   B 1 402 ? -19.649 -11.853 4.975   1.00 94.21  ?  402 THR   B CG2 1 
ATOM   6865  N N   . GLY   B 1 403 ? -20.070 -14.284 9.009   1.00 91.15  ?  403 GLY   B N   1 
ATOM   6866  C CA  . GLY   B 1 403 ? -19.664 -15.397 9.842   1.00 92.80  ?  403 GLY   B CA  1 
ATOM   6867  C C   . GLY   B 1 403 ? -18.246 -15.863 9.613   1.00 90.80  ?  403 GLY   B C   1 
ATOM   6868  O O   . GLY   B 1 403 ? -17.891 -16.967 10.036  1.00 88.81  ?  403 GLY   B O   1 
ATOM   6869  N N   . GLU   B 1 404 ? -17.426 -15.057 8.946   1.00 87.62  ?  404 GLU   B N   1 
ATOM   6870  C CA  . GLU   B 1 404 ? -16.026 -15.361 8.681   1.00 84.60  ?  404 GLU   B CA  1 
ATOM   6871  C C   . GLU   B 1 404 ? -15.141 -14.278 9.294   1.00 79.62  ?  404 GLU   B C   1 
ATOM   6872  O O   . GLU   B 1 404 ? -15.621 -13.338 9.933   1.00 78.72  ?  404 GLU   B O   1 
ATOM   6873  C CB  . GLU   B 1 404 ? -15.768 -15.495 7.176   1.00 88.60  ?  404 GLU   B CB  1 
ATOM   6874  C CG  . GLU   B 1 404 ? -16.161 -16.845 6.580   1.00 90.75  ?  404 GLU   B CG  1 
ATOM   6875  C CD  . GLU   B 1 404 ? -15.113 -17.928 6.806   1.00 91.14  ?  404 GLU   B CD  1 
ATOM   6876  O OE1 . GLU   B 1 404 ? -14.587 -18.044 7.936   1.00 80.76  ?  404 GLU   B OE1 1 
ATOM   6877  O OE2 . GLU   B 1 404 ? -14.813 -18.664 5.842   1.00 92.73  ?  404 GLU   B OE2 1 
ATOM   6878  N N   . GLN   B 1 405 ? -13.833 -14.421 9.086   1.00 77.68  ?  405 GLN   B N   1 
ATOM   6879  C CA  . GLN   B 1 405 ? -12.873 -13.498 9.676   1.00 72.83  ?  405 GLN   B CA  1 
ATOM   6880  C C   . GLN   B 1 405 ? -13.078 -12.083 9.147   1.00 73.72  ?  405 GLN   B C   1 
ATOM   6881  O O   . GLN   B 1 405 ? -13.122 -11.855 7.933   1.00 69.73  ?  405 GLN   B O   1 
ATOM   6882  C CB  . GLN   B 1 405 ? -11.443 -13.971 9.391   1.00 73.34  ?  405 GLN   B CB  1 
ATOM   6883  C CG  . GLN   B 1 405 ? -10.350 -13.049 9.928   1.00 61.61  ?  405 GLN   B CG  1 
ATOM   6884  C CD  . GLN   B 1 405 ? -10.369 -12.936 11.443  1.00 64.77  ?  405 GLN   B CD  1 
ATOM   6885  O OE1 . GLN   B 1 405 ? -10.549 -13.932 12.149  1.00 60.65  ?  405 GLN   B OE1 1 
ATOM   6886  N NE2 . GLN   B 1 405 ? -10.192 -11.719 11.951  1.00 57.09  ?  405 GLN   B NE2 1 
ATOM   6887  N N   . LYS   B 1 406 ? -13.212 -11.135 10.071  1.00 69.62  ?  406 LYS   B N   1 
ATOM   6888  C CA  . LYS   B 1 406 ? -13.251 -9.722  9.722   1.00 73.48  ?  406 LYS   B CA  1 
ATOM   6889  C C   . LYS   B 1 406 ? -11.839 -9.254  9.373   1.00 77.96  ?  406 LYS   B C   1 
ATOM   6890  O O   . LYS   B 1 406 ? -10.933 -9.318  10.211  1.00 72.77  ?  406 LYS   B O   1 
ATOM   6891  C CB  . LYS   B 1 406 ? -13.828 -8.927  10.892  1.00 75.44  ?  406 LYS   B CB  1 
ATOM   6892  C CG  . LYS   B 1 406 ? -14.392 -7.563  10.546  1.00 84.21  ?  406 LYS   B CG  1 
ATOM   6893  C CD  . LYS   B 1 406 ? -15.158 -6.997  11.735  1.00 82.74  ?  406 LYS   B CD  1 
ATOM   6894  C CE  . LYS   B 1 406 ? -15.512 -5.533  11.530  1.00 80.84  ?  406 LYS   B CE  1 
ATOM   6895  N NZ  . LYS   B 1 406 ? -14.295 -4.681  11.422  1.00 74.10  ?  406 LYS   B NZ  1 
ATOM   6896  N N   . HIS   B 1 407 ? -11.646 -8.805  8.131   1.00 83.59  ?  407 HIS   B N   1 
ATOM   6897  C CA  . HIS   B 1 407 ? -10.318 -8.434  7.651   1.00 82.63  ?  407 HIS   B CA  1 
ATOM   6898  C C   . HIS   B 1 407 ? -9.756  -7.262  8.448   1.00 82.26  ?  407 HIS   B C   1 
ATOM   6899  O O   . HIS   B 1 407 ? -10.334 -6.170  8.458   1.00 83.43  ?  407 HIS   B O   1 
ATOM   6900  C CB  . HIS   B 1 407 ? -10.377 -8.083  6.163   1.00 83.92  ?  407 HIS   B CB  1 
ATOM   6901  C CG  . HIS   B 1 407 ? -9.113  -7.478  5.634   1.00 89.92  ?  407 HIS   B CG  1 
ATOM   6902  N ND1 . HIS   B 1 407 ? -8.022  -8.236  5.263   1.00 92.52  ?  407 HIS   B ND1 1 
ATOM   6903  C CD2 . HIS   B 1 407 ? -8.762  -6.187  5.420   1.00 87.40  ?  407 HIS   B CD2 1 
ATOM   6904  C CE1 . HIS   B 1 407 ? -7.057  -7.439  4.840   1.00 88.69  ?  407 HIS   B CE1 1 
ATOM   6905  N NE2 . HIS   B 1 407 ? -7.479  -6.190  4.926   1.00 85.19  ?  407 HIS   B NE2 1 
ATOM   6906  N N   . ALA   B 1 408 ? -8.622  -7.488  9.109   1.00 77.18  ?  408 ALA   B N   1 
ATOM   6907  C CA  . ALA   B 1 408 ? -7.949  -6.446  9.873   1.00 79.19  ?  408 ALA   B CA  1 
ATOM   6908  C C   . ALA   B 1 408 ? -6.945  -5.706  9.000   1.00 75.91  ?  408 ALA   B C   1 
ATOM   6909  O O   . ALA   B 1 408 ? -6.226  -6.315  8.202   1.00 74.77  ?  408 ALA   B O   1 
ATOM   6910  C CB  . ALA   B 1 408 ? -7.236  -7.035  11.093  1.00 70.64  ?  408 ALA   B CB  1 
ATOM   6911  N N   . ASP   B 1 409 ? -6.898  -4.385  9.160   1.00 70.97  ?  409 ASP   B N   1 
ATOM   6912  C CA  . ASP   B 1 409 ? -5.948  -3.553  8.436   1.00 72.67  ?  409 ASP   B CA  1 
ATOM   6913  C C   . ASP   B 1 409 ? -4.591  -3.459  9.131   1.00 72.67  ?  409 ASP   B C   1 
ATOM   6914  O O   . ASP   B 1 409 ? -3.693  -2.780  8.622   1.00 72.48  ?  409 ASP   B O   1 
ATOM   6915  C CB  . ASP   B 1 409 ? -6.533  -2.150  8.219   1.00 67.80  ?  409 ASP   B CB  1 
ATOM   6916  C CG  . ASP   B 1 409 ? -7.065  -1.533  9.498   1.00 65.64  ?  409 ASP   B CG  1 
ATOM   6917  O OD1 . ASP   B 1 409 ? -7.978  -2.126  10.111  1.00 70.01  ?  409 ASP   B OD1 1 
ATOM   6918  O OD2 . ASP   B 1 409 ? -6.562  -0.458  9.893   1.00 57.27  ?  409 ASP   B OD2 1 
ATOM   6919  N N   . MET   B 1 410 ? -4.419  -4.128  10.270  1.00 73.17  ?  410 MET   B N   1 
ATOM   6920  C CA  . MET   B 1 410 ? -3.140  -4.177  10.967  1.00 69.88  ?  410 MET   B CA  1 
ATOM   6921  C C   . MET   B 1 410 ? -3.112  -5.440  11.819  1.00 67.82  ?  410 MET   B C   1 
ATOM   6922  O O   . MET   B 1 410 ? -4.096  -6.178  11.909  1.00 71.93  ?  410 MET   B O   1 
ATOM   6923  C CB  . MET   B 1 410 ? -2.913  -2.921  11.817  1.00 69.56  ?  410 MET   B CB  1 
ATOM   6924  C CG  . MET   B 1 410 ? -1.442  -2.562  12.006  1.00 68.41  ?  410 MET   B CG  1 
ATOM   6925  S SD  . MET   B 1 410 ? -0.647  -2.055  10.468  1.00 73.31  ?  410 MET   B SD  1 
ATOM   6926  C CE  . MET   B 1 410 ? -1.511  -0.518  10.138  1.00 64.53  ?  410 MET   B CE  1 
ATOM   6927  N N   . GLU   B 1 411 ? -1.963  -5.684  12.446  1.00 56.05  ?  411 GLU   B N   1 
ATOM   6928  C CA  . GLU   B 1 411 ? -1.759  -6.931  13.184  1.00 54.75  ?  411 GLU   B CA  1 
ATOM   6929  C C   . GLU   B 1 411 ? -0.653  -6.664  14.209  1.00 48.55  ?  411 GLU   B C   1 
ATOM   6930  O O   . GLU   B 1 411 ? 0.490   -7.099  14.048  1.00 46.11  ?  411 GLU   B O   1 
ATOM   6931  C CB  . GLU   B 1 411 ? -1.407  -8.088  12.245  1.00 53.98  ?  411 GLU   B CB  1 
ATOM   6932  C CG  . GLU   B 1 411 ? -1.583  -9.489  12.827  1.00 61.68  ?  411 GLU   B CG  1 
ATOM   6933  C CD  . GLU   B 1 411 ? -3.047  -9.932  12.933  1.00 62.46  ?  411 GLU   B CD  1 
ATOM   6934  O OE1 . GLU   B 1 411 ? -3.866  -9.491  12.095  1.00 63.16  ?  411 GLU   B OE1 1 
ATOM   6935  O OE2 . GLU   B 1 411 ? -3.375  -10.729 13.849  1.00 58.93  ?  411 GLU   B OE2 1 
ATOM   6936  N N   . PHE   B 1 412 ? -1.020  -5.945  15.269  1.00 44.43  ?  412 PHE   B N   1 
ATOM   6937  C CA  . PHE   B 1 412 ? -0.084  -5.498  16.294  1.00 37.54  ?  412 PHE   B CA  1 
ATOM   6938  C C   . PHE   B 1 412 ? 0.045   -6.519  17.415  1.00 37.18  ?  412 PHE   B C   1 
ATOM   6939  O O   . PHE   B 1 412 ? -0.931  -7.172  17.799  1.00 39.21  ?  412 PHE   B O   1 
ATOM   6940  C CB  . PHE   B 1 412 ? -0.535  -4.172  16.910  1.00 37.15  ?  412 PHE   B CB  1 
ATOM   6941  C CG  . PHE   B 1 412 ? -0.239  -2.968  16.072  1.00 41.92  ?  412 PHE   B CG  1 
ATOM   6942  C CD1 . PHE   B 1 412 ? 0.864   -2.938  15.239  1.00 37.72  ?  412 PHE   B CD1 1 
ATOM   6943  C CD2 . PHE   B 1 412 ? -1.065  -1.847  16.136  1.00 42.55  ?  412 PHE   B CD2 1 
ATOM   6944  C CE1 . PHE   B 1 412 ? 1.139   -1.812  14.467  1.00 47.99  ?  412 PHE   B CE1 1 
ATOM   6945  C CE2 . PHE   B 1 412 ? -0.795  -0.723  15.375  1.00 46.49  ?  412 PHE   B CE2 1 
ATOM   6946  C CZ  . PHE   B 1 412 ? 0.310   -0.705  14.537  1.00 47.47  ?  412 PHE   B CZ  1 
ATOM   6947  N N   . MET   B 1 413 ? 1.258   -6.649  17.934  1.00 29.74  ?  413 MET   B N   1 
ATOM   6948  C CA  . MET   B 1 413 ? 1.485   -7.152  19.280  1.00 25.92  ?  413 MET   B CA  1 
ATOM   6949  C C   . MET   B 1 413 ? 1.794   -5.954  20.167  1.00 24.07  ?  413 MET   B C   1 
ATOM   6950  O O   . MET   B 1 413 ? 2.634   -5.121  19.812  1.00 23.54  ?  413 MET   B O   1 
ATOM   6951  C CB  . MET   B 1 413 ? 2.632   -8.159  19.320  1.00 24.90  ?  413 MET   B CB  1 
ATOM   6952  C CG  . MET   B 1 413 ? 3.144   -8.404  20.719  1.00 23.63  ?  413 MET   B CG  1 
ATOM   6953  S SD  . MET   B 1 413 ? 4.412   -9.685  20.847  1.00 34.12  ?  413 MET   B SD  1 
ATOM   6954  C CE  . MET   B 1 413 ? 5.740   -8.972  19.876  1.00 34.01  ?  413 MET   B CE  1 
ATOM   6955  N N   . ARG   B 1 414 ? 1.089   -5.839  21.287  1.00 23.41  ?  414 ARG   B N   1 
ATOM   6956  C CA  . ARG   B 1 414 ? 1.238   -4.690  22.167  1.00 22.28  ?  414 ARG   B CA  1 
ATOM   6957  C C   . ARG   B 1 414 ? 2.039   -5.098  23.396  1.00 21.03  ?  414 ARG   B C   1 
ATOM   6958  O O   . ARG   B 1 414 ? 1.622   -5.979  24.157  1.00 22.78  ?  414 ARG   B O   1 
ATOM   6959  C CB  . ARG   B 1 414 ? -0.113  -4.111  22.578  1.00 22.71  ?  414 ARG   B CB  1 
ATOM   6960  C CG  . ARG   B 1 414 ? 0.026   -2.842  23.417  1.00 21.67  ?  414 ARG   B CG  1 
ATOM   6961  C CD  . ARG   B 1 414 ? -1.321  -2.281  23.849  1.00 23.14  ?  414 ARG   B CD  1 
ATOM   6962  N NE  . ARG   B 1 414 ? -1.874  -2.971  25.004  1.00 22.33  ?  414 ARG   B NE  1 
ATOM   6963  C CZ  . ARG   B 1 414 ? -3.052  -2.693  25.545  1.00 30.23  ?  414 ARG   B CZ  1 
ATOM   6964  N NH1 . ARG   B 1 414 ? -3.861  -1.788  25.015  1.00 32.46  ?  414 ARG   B NH1 1 
ATOM   6965  N NH2 . ARG   B 1 414 ? -3.430  -3.341  26.642  1.00 27.55  ?  414 ARG   B NH2 1 
ATOM   6966  N N   . LEU   B 1 415 ? 3.184   -4.459  23.585  1.00 19.97  ?  415 LEU   B N   1 
ATOM   6967  C CA  . LEU   B 1 415 ? 4.001   -4.651  24.778  1.00 18.71  ?  415 LEU   B CA  1 
ATOM   6968  C C   . LEU   B 1 415 ? 3.645   -3.488  25.698  1.00 18.18  ?  415 LEU   B C   1 
ATOM   6969  O O   . LEU   B 1 415 ? 4.212   -2.399  25.597  1.00 19.86  ?  415 LEU   B O   1 
ATOM   6970  C CB  . LEU   B 1 415 ? 5.482   -4.697  24.416  1.00 18.14  ?  415 LEU   B CB  1 
ATOM   6971  C CG  . LEU   B 1 415 ? 5.849   -5.600  23.224  1.00 19.14  ?  415 LEU   B CG  1 
ATOM   6972  C CD1 . LEU   B 1 415 ? 7.234   -5.279  22.662  1.00 18.89  ?  415 LEU   B CD1 1 
ATOM   6973  C CD2 . LEU   B 1 415 ? 5.764   -7.072  23.603  1.00 19.89  ?  415 LEU   B CD2 1 
ATOM   6974  N N   . THR   B 1 416 ? 2.663   -3.715  26.573  1.00 19.13  ?  416 THR   B N   1 
ATOM   6975  C CA  . THR   B 1 416 ? 2.124   -2.669  27.434  1.00 18.09  ?  416 THR   B CA  1 
ATOM   6976  C C   . THR   B 1 416 ? 2.904   -2.618  28.740  1.00 16.94  ?  416 THR   B C   1 
ATOM   6977  O O   . THR   B 1 416 ? 3.081   -3.643  29.410  1.00 18.29  ?  416 THR   B O   1 
ATOM   6978  C CB  . THR   B 1 416 ? 0.639   -2.897  27.722  1.00 18.47  ?  416 THR   B CB  1 
ATOM   6979  O OG1 . THR   B 1 416 ? 0.070   -3.760  26.727  1.00 21.59  ?  416 THR   B OG1 1 
ATOM   6980  C CG2 . THR   B 1 416 ? -0.104  -1.570  27.696  1.00 20.97  ?  416 THR   B CG2 1 
ATOM   6981  N N   . ILE   B 1 417 ? 3.338   -1.418  29.118  1.00 18.40  ?  417 ILE   B N   1 
ATOM   6982  C CA  . ILE   B 1 417 ? 4.306   -1.212  30.190  1.00 14.57  ?  417 ILE   B CA  1 
ATOM   6983  C C   . ILE   B 1 417 ? 3.598   -0.569  31.373  1.00 15.33  ?  417 ILE   B C   1 
ATOM   6984  O O   . ILE   B 1 417 ? 3.084   0.552   31.265  1.00 17.36  ?  417 ILE   B O   1 
ATOM   6985  C CB  . ILE   B 1 417 ? 5.477   -0.340  29.716  1.00 14.35  ?  417 ILE   B CB  1 
ATOM   6986  C CG1 . ILE   B 1 417 ? 6.055   -0.877  28.398  1.00 15.56  ?  417 ILE   B CG1 1 
ATOM   6987  C CG2 . ILE   B 1 417 ? 6.540   -0.237  30.796  1.00 15.96  ?  417 ILE   B CG2 1 
ATOM   6988  C CD1 . ILE   B 1 417 ? 6.727   -2.225  28.509  1.00 17.33  ?  417 ILE   B CD1 1 
ATOM   6989  N N   . ALA   B 1 418 ? 3.559   -1.278  32.498  1.00 16.65  ?  418 ALA   B N   1 
ATOM   6990  C CA  . ALA   B 1 418 ? 2.991   -0.718  33.715  1.00 14.87  ?  418 ALA   B CA  1 
ATOM   6991  C C   . ALA   B 1 418 ? 3.906   0.377   34.252  1.00 15.19  ?  418 ALA   B C   1 
ATOM   6992  O O   . ALA   B 1 418 ? 5.111   0.395   33.985  1.00 19.09  ?  418 ALA   B O   1 
ATOM   6993  C CB  . ALA   B 1 418 ? 2.801   -1.808  34.768  1.00 16.37  ?  418 ALA   B CB  1 
ATOM   6994  N N   . ARG   B 1 419 ? 3.323   1.304   35.003  1.00 19.34  ?  419 ARG   B N   1 
ATOM   6995  C CA  . ARG   B 1 419 ? 4.040   2.498   35.446  1.00 16.37  ?  419 ARG   B CA  1 
ATOM   6996  C C   . ARG   B 1 419 ? 4.815   2.219   36.727  1.00 14.64  ?  419 ARG   B C   1 
ATOM   6997  O O   . ARG   B 1 419 ? 4.226   1.857   37.752  1.00 14.81  ?  419 ARG   B O   1 
ATOM   6998  C CB  . ARG   B 1 419 ? 3.065   3.657   35.649  1.00 17.58  ?  419 ARG   B CB  1 
ATOM   6999  C CG  . ARG   B 1 419 ? 2.417   4.108   34.374  1.00 14.25  ?  419 ARG   B CG  1 
ATOM   7000  C CD  . ARG   B 1 419 ? 1.130   4.856   34.611  1.00 15.76  ?  419 ARG   B CD  1 
ATOM   7001  N NE  . ARG   B 1 419 ? 0.473   5.154   33.345  1.00 19.50  ?  419 ARG   B NE  1 
ATOM   7002  C CZ  . ARG   B 1 419 ? -0.250  4.283   32.657  1.00 17.89  ?  419 ARG   B CZ  1 
ATOM   7003  N NH1 . ARG   B 1 419 ? -0.468  3.059   33.108  1.00 18.42  ?  419 ARG   B NH1 1 
ATOM   7004  N NH2 . ARG   B 1 419 ? -0.758  4.644   31.486  1.00 20.67  ?  419 ARG   B NH2 1 
ATOM   7005  N N   . ARG   B 1 420 ? 6.140   2.390   36.654  1.00 14.57  ?  420 ARG   B N   1 
ATOM   7006  C CA  . ARG   B 1 420 ? 7.057   2.316   37.793  1.00 12.69  ?  420 ARG   B CA  1 
ATOM   7007  C C   . ARG   B 1 420 ? 7.206   0.899   38.339  1.00 15.63  ?  420 ARG   B C   1 
ATOM   7008  O O   . ARG   B 1 420 ? 7.568   0.720   39.498  1.00 14.82  ?  420 ARG   B O   1 
ATOM   7009  C CB  . ARG   B 1 420 ? 6.637   3.269   38.921  1.00 12.89  ?  420 ARG   B CB  1 
ATOM   7010  C CG  . ARG   B 1 420 ? 6.297   4.682   38.463  1.00 14.53  ?  420 ARG   B CG  1 
ATOM   7011  C CD  . ARG   B 1 420 ? 6.187   5.628   39.648  1.00 10.83  ?  420 ARG   B CD  1 
ATOM   7012  N NE  . ARG   B 1 420 ? 4.977   5.432   40.439  1.00 15.51  ?  420 ARG   B NE  1 
ATOM   7013  C CZ  . ARG   B 1 420 ? 4.459   6.365   41.229  1.00 15.62  ?  420 ARG   B CZ  1 
ATOM   7014  N NH1 . ARG   B 1 420 ? 5.020   7.560   41.344  1.00 17.79  ?  420 ARG   B NH1 1 
ATOM   7015  N NH2 . ARG   B 1 420 ? 3.348   6.099   41.911  1.00 13.71  ?  420 ARG   B NH2 1 
ATOM   7016  N N   . VAL   B 1 421 ? 6.946   -0.111  37.515  1.00 16.87  ?  421 VAL   B N   1 
ATOM   7017  C CA  . VAL   B 1 421 ? 6.971   -1.504  37.942  1.00 12.78  ?  421 VAL   B CA  1 
ATOM   7018  C C   . VAL   B 1 421 ? 8.242   -2.211  37.493  1.00 15.44  ?  421 VAL   B C   1 
ATOM   7019  O O   . VAL   B 1 421 ? 8.832   -2.976  38.260  1.00 16.51  ?  421 VAL   B O   1 
ATOM   7020  C CB  . VAL   B 1 421 ? 5.726   -2.241  37.401  1.00 16.23  ?  421 VAL   B CB  1 
ATOM   7021  C CG1 . VAL   B 1 421 ? 5.827   -3.743  37.690  1.00 13.74  ?  421 VAL   B CG1 1 
ATOM   7022  C CG2 . VAL   B 1 421 ? 4.453   -1.643  37.972  1.00 15.20  ?  421 VAL   B CG2 1 
ATOM   7023  N N   . TYR   B 1 422 ? 8.647   -1.985  36.243  1.00 13.20  ?  422 TYR   B N   1 
ATOM   7024  C CA  . TYR   B 1 422 ? 9.720   -2.727  35.598  1.00 17.56  ?  422 TYR   B CA  1 
ATOM   7025  C C   . TYR   B 1 422 ? 10.905  -1.812  35.321  1.00 15.33  ?  422 TYR   B C   1 
ATOM   7026  O O   . TYR   B 1 422 ? 10.737  -0.623  35.032  1.00 17.45  ?  422 TYR   B O   1 
ATOM   7027  C CB  . TYR   B 1 422 ? 9.233   -3.371  34.286  1.00 16.69  ?  422 TYR   B CB  1 
ATOM   7028  C CG  . TYR   B 1 422 ? 8.163   -4.433  34.499  1.00 18.62  ?  422 TYR   B CG  1 
ATOM   7029  C CD1 . TYR   B 1 422 ? 8.473   -5.638  35.135  1.00 15.00  ?  422 TYR   B CD1 1 
ATOM   7030  C CD2 . TYR   B 1 422 ? 6.852   -4.235  34.071  1.00 12.58  ?  422 TYR   B CD2 1 
ATOM   7031  C CE1 . TYR   B 1 422 ? 7.503   -6.614  35.349  1.00 15.55  ?  422 TYR   B CE1 1 
ATOM   7032  C CE2 . TYR   B 1 422 ? 5.871   -5.206  34.281  1.00 14.60  ?  422 TYR   B CE2 1 
ATOM   7033  C CZ  . TYR   B 1 422 ? 6.214   -6.401  34.919  1.00 17.87  ?  422 TYR   B CZ  1 
ATOM   7034  O OH  . TYR   B 1 422 ? 5.263   -7.383  35.142  1.00 20.17  ?  422 TYR   B OH  1 
ATOM   7035  N N   . THR   B 1 423 ? 12.106  -2.371  35.418  1.00 15.10  ?  423 THR   B N   1 
ATOM   7036  C CA  . THR   B 1 423 ? 13.306  -1.589  35.173  1.00 19.40  ?  423 THR   B CA  1 
ATOM   7037  C C   . THR   B 1 423 ? 13.727  -1.714  33.710  1.00 20.37  ?  423 THR   B C   1 
ATOM   7038  O O   . THR   B 1 423 ? 13.169  -2.491  32.934  1.00 17.90  ?  423 THR   B O   1 
ATOM   7039  C CB  . THR   B 1 423 ? 14.451  -2.027  36.094  1.00 21.25  ?  423 THR   B CB  1 
ATOM   7040  O OG1 . THR   B 1 423 ? 14.968  -3.286  35.653  1.00 19.92  ?  423 THR   B OG1 1 
ATOM   7041  C CG2 . THR   B 1 423 ? 13.973  -2.159  37.547  1.00 14.94  ?  423 THR   B CG2 1 
ATOM   7042  N N   . ASN   B 1 424 ? 14.732  -0.926  33.329  1.00 17.57  ?  424 ASN   B N   1 
ATOM   7043  C CA  . ASN   B 1 424 ? 15.235  -1.030  31.968  1.00 21.67  ?  424 ASN   B CA  1 
ATOM   7044  C C   . ASN   B 1 424 ? 15.915  -2.369  31.732  1.00 20.36  ?  424 ASN   B C   1 
ATOM   7045  O O   . ASN   B 1 424 ? 15.969  -2.835  30.592  1.00 18.45  ?  424 ASN   B O   1 
ATOM   7046  C CB  . ASN   B 1 424 ? 16.175  0.138   31.668  1.00 20.61  ?  424 ASN   B CB  1 
ATOM   7047  C CG  . ASN   B 1 424 ? 15.428  1.471   31.551  1.00 24.08  ?  424 ASN   B CG  1 
ATOM   7048  O OD1 . ASN   B 1 424 ? 14.262  1.506   31.167  1.00 20.96  ?  424 ASN   B OD1 1 
ATOM   7049  N ND2 . ASN   B 1 424 ? 16.101  2.568   31.886  1.00 24.84  ?  424 ASN   B ND2 1 
ATOM   7050  N N   . ASP   B 1 425 ? 16.407  -3.018  32.786  1.00 19.74  ?  425 ASP   B N   1 
ATOM   7051  C CA  . ASP   B 1 425 ? 16.898  -4.376  32.614  1.00 19.25  ?  425 ASP   B CA  1 
ATOM   7052  C C   . ASP   B 1 425 ? 15.756  -5.340  32.320  1.00 20.63  ?  425 ASP   B C   1 
ATOM   7053  O O   . ASP   B 1 425 ? 15.954  -6.328  31.602  1.00 19.32  ?  425 ASP   B O   1 
ATOM   7054  C CB  . ASP   B 1 425 ? 17.683  -4.805  33.850  1.00 25.53  ?  425 ASP   B CB  1 
ATOM   7055  C CG  . ASP   B 1 425 ? 18.982  -4.024  34.010  1.00 22.51  ?  425 ASP   B CG  1 
ATOM   7056  O OD1 . ASP   B 1 425 ? 19.512  -3.551  32.983  1.00 25.17  ?  425 ASP   B OD1 1 
ATOM   7057  O OD2 . ASP   B 1 425 ? 19.471  -3.884  35.149  1.00 23.80  ?  425 ASP   B OD2 1 
ATOM   7058  N N   . HIS   B 1 426 ? 14.558  -5.072  32.850  1.00 18.38  ?  426 HIS   B N   1 
ATOM   7059  C CA  . HIS   B 1 426 ? 13.392  -5.845  32.433  1.00 16.56  ?  426 HIS   B CA  1 
ATOM   7060  C C   . HIS   B 1 426 ? 13.080  -5.592  30.965  1.00 17.55  ?  426 HIS   B C   1 
ATOM   7061  O O   . HIS   B 1 426 ? 12.643  -6.499  30.250  1.00 16.53  ?  426 HIS   B O   1 
ATOM   7062  C CB  . HIS   B 1 426 ? 12.179  -5.501  33.294  1.00 17.97  ?  426 HIS   B CB  1 
ATOM   7063  C CG  . HIS   B 1 426 ? 12.270  -6.012  34.698  1.00 17.39  ?  426 HIS   B CG  1 
ATOM   7064  N ND1 . HIS   B 1 426 ? 12.174  -5.185  35.797  1.00 15.11  ?  426 HIS   B ND1 1 
ATOM   7065  C CD2 . HIS   B 1 426 ? 12.433  -7.266  35.186  1.00 17.16  ?  426 HIS   B CD2 1 
ATOM   7066  C CE1 . HIS   B 1 426 ? 12.285  -5.904  36.900  1.00 16.68  ?  426 HIS   B CE1 1 
ATOM   7067  N NE2 . HIS   B 1 426 ? 12.441  -7.170  36.558  1.00 16.66  ?  426 HIS   B NE2 1 
ATOM   7068  N N   . MET   B 1 427 ? 13.308  -4.362  30.495  1.00 18.37  ?  427 MET   B N   1 
ATOM   7069  C CA  . MET   B 1 427 ? 13.069  -4.060  29.089  1.00 20.26  ?  427 MET   B CA  1 
ATOM   7070  C C   . MET   B 1 427 ? 14.039  -4.821  28.198  1.00 19.69  ?  427 MET   B C   1 
ATOM   7071  O O   . MET   B 1 427 ? 13.651  -5.328  27.138  1.00 18.82  ?  427 MET   B O   1 
ATOM   7072  C CB  . MET   B 1 427 ? 13.182  -2.553  28.832  1.00 18.32  ?  427 MET   B CB  1 
ATOM   7073  C CG  . MET   B 1 427 ? 12.214  -1.683  29.623  1.00 17.19  ?  427 MET   B CG  1 
ATOM   7074  S SD  . MET   B 1 427 ? 10.463  -1.990  29.315  1.00 19.81  ?  427 MET   B SD  1 
ATOM   7075  C CE  . MET   B 1 427 ? 9.918   -2.376  30.977  1.00 16.66  ?  427 MET   B CE  1 
ATOM   7076  N N   . ASP   B 1 428 ? 15.304  -4.910  28.609  1.00 19.48  ?  428 ASP   B N   1 
ATOM   7077  C CA  . ASP   B 1 428 ? 16.269  -5.685  27.844  1.00 21.07  ?  428 ASP   B CA  1 
ATOM   7078  C C   . ASP   B 1 428 ? 15.839  -7.140  27.739  1.00 17.51  ?  428 ASP   B C   1 
ATOM   7079  O O   . ASP   B 1 428 ? 15.934  -7.740  26.667  1.00 21.74  ?  428 ASP   B O   1 
ATOM   7080  C CB  . ASP   B 1 428 ? 17.657  -5.579  28.478  1.00 21.10  ?  428 ASP   B CB  1 
ATOM   7081  C CG  . ASP   B 1 428 ? 18.302  -4.224  28.252  1.00 21.85  ?  428 ASP   B CG  1 
ATOM   7082  O OD1 . ASP   B 1 428 ? 17.888  -3.528  27.303  1.00 21.17  ?  428 ASP   B OD1 1 
ATOM   7083  O OD2 . ASP   B 1 428 ? 19.225  -3.862  29.021  1.00 20.70  ?  428 ASP   B OD2 1 
ATOM   7084  N N   . TYR   B 1 429 ? 15.366  -7.726  28.840  1.00 21.07  ?  429 TYR   B N   1 
ATOM   7085  C CA  . TYR   B 1 429 ? 14.882  -9.100  28.779  1.00 20.48  ?  429 TYR   B CA  1 
ATOM   7086  C C   . TYR   B 1 429 ? 13.789  -9.243  27.730  1.00 22.30  ?  429 TYR   B C   1 
ATOM   7087  O O   . TYR   B 1 429 ? 13.779  -10.214 26.961  1.00 21.78  ?  429 TYR   B O   1 
ATOM   7088  C CB  . TYR   B 1 429 ? 14.372  -9.548  30.151  1.00 19.15  ?  429 TYR   B CB  1 
ATOM   7089  C CG  . TYR   B 1 429 ? 13.893  -10.992 30.170  1.00 24.72  ?  429 TYR   B CG  1 
ATOM   7090  C CD1 . TYR   B 1 429 ? 12.612  -11.336 29.744  1.00 23.70  ?  429 TYR   B CD1 1 
ATOM   7091  C CD2 . TYR   B 1 429 ? 14.722  -12.008 30.611  1.00 26.56  ?  429 TYR   B CD2 1 
ATOM   7092  C CE1 . TYR   B 1 429 ? 12.177  -12.654 29.751  1.00 30.41  ?  429 TYR   B CE1 1 
ATOM   7093  C CE2 . TYR   B 1 429 ? 14.295  -13.327 30.631  1.00 29.71  ?  429 TYR   B CE2 1 
ATOM   7094  C CZ  . TYR   B 1 429 ? 13.026  -13.648 30.201  1.00 34.27  ?  429 TYR   B CZ  1 
ATOM   7095  O OH  . TYR   B 1 429 ? 12.612  -14.969 30.227  1.00 32.50  ?  429 TYR   B OH  1 
ATOM   7096  N N   . ILE   B 1 430 ? 12.865  -8.277  27.681  1.00 20.97  ?  430 ILE   B N   1 
ATOM   7097  C CA  . ILE   B 1 430 ? 11.757  -8.326  26.732  1.00 17.91  ?  430 ILE   B CA  1 
ATOM   7098  C C   . ILE   B 1 430 ? 12.271  -8.227  25.304  1.00 19.37  ?  430 ILE   B C   1 
ATOM   7099  O O   . ILE   B 1 430 ? 11.931  -9.052  24.452  1.00 20.33  ?  430 ILE   B O   1 
ATOM   7100  C CB  . ILE   B 1 430 ? 10.743  -7.211  27.046  1.00 15.12  ?  430 ILE   B CB  1 
ATOM   7101  C CG1 . ILE   B 1 430 ? 10.137  -7.441  28.438  1.00 16.82  ?  430 ILE   B CG1 1 
ATOM   7102  C CG2 . ILE   B 1 430 ? 9.674   -7.143  25.979  1.00 16.55  ?  430 ILE   B CG2 1 
ATOM   7103  C CD1 . ILE   B 1 430 ? 9.670   -6.180  29.136  1.00 17.00  ?  430 ILE   B CD1 1 
ATOM   7104  N N   . ALA   B 1 431 ? 13.081  -7.202  25.018  1.00 21.29  ?  431 ALA   B N   1 
ATOM   7105  C CA  . ALA   B 1 431 ? 13.608  -7.014  23.669  1.00 24.86  ?  431 ALA   B CA  1 
ATOM   7106  C C   . ALA   B 1 431 ? 14.423  -8.220  23.222  1.00 20.63  ?  431 ALA   B C   1 
ATOM   7107  O O   . ALA   B 1 431 ? 14.210  -8.758  22.132  1.00 24.18  ?  431 ALA   B O   1 
ATOM   7108  C CB  . ALA   B 1 431 ? 14.455  -5.740  23.607  1.00 19.57  ?  431 ALA   B CB  1 
ATOM   7109  N N   . ASP   B 1 432 ? 15.359  -8.663  24.060  1.00 25.42  ?  432 ASP   B N   1 
ATOM   7110  C CA  . ASP   B 1 432 ? 16.198  -9.801  23.701  1.00 26.14  ?  432 ASP   B CA  1 
ATOM   7111  C C   . ASP   B 1 432 ? 15.366  -11.038 23.414  1.00 26.42  ?  432 ASP   B C   1 
ATOM   7112  O O   . ASP   B 1 432 ? 15.681  -11.811 22.503  1.00 29.91  ?  432 ASP   B O   1 
ATOM   7113  C CB  . ASP   B 1 432 ? 17.194  -10.079 24.821  1.00 30.03  ?  432 ASP   B CB  1 
ATOM   7114  C CG  . ASP   B 1 432 ? 18.223  -9.000  24.930  1.00 28.83  ?  432 ASP   B CG  1 
ATOM   7115  O OD1 . ASP   B 1 432 ? 18.445  -8.326  23.905  1.00 34.43  ?  432 ASP   B OD1 1 
ATOM   7116  O OD2 . ASP   B 1 432 ? 18.792  -8.815  26.023  1.00 34.81  ?  432 ASP   B OD2 1 
ATOM   7117  N N   . ALA   B 1 433 ? 14.294  -11.236 24.177  1.00 25.96  ?  433 ALA   B N   1 
ATOM   7118  C CA  . ALA   B 1 433 ? 13.433  -12.389 23.957  1.00 28.27  ?  433 ALA   B CA  1 
ATOM   7119  C C   . ALA   B 1 433 ? 12.822  -12.360 22.564  1.00 27.78  ?  433 ALA   B C   1 
ATOM   7120  O O   . ALA   B 1 433 ? 12.807  -13.376 21.859  1.00 32.93  ?  433 ALA   B O   1 
ATOM   7121  C CB  . ALA   B 1 433 ? 12.345  -12.436 25.030  1.00 26.56  ?  433 ALA   B CB  1 
ATOM   7122  N N   . LEU   B 1 434 ? 12.315  -11.199 22.142  1.00 27.87  ?  434 LEU   B N   1 
ATOM   7123  C CA  . LEU   B 1 434 ? 11.700  -11.113 20.823  1.00 28.66  ?  434 LEU   B CA  1 
ATOM   7124  C C   . LEU   B 1 434 ? 12.752  -11.147 19.723  1.00 32.90  ?  434 LEU   B C   1 
ATOM   7125  O O   . LEU   B 1 434 ? 12.531  -11.746 18.664  1.00 34.98  ?  434 LEU   B O   1 
ATOM   7126  C CB  . LEU   B 1 434 ? 10.844  -9.849  20.716  1.00 28.38  ?  434 LEU   B CB  1 
ATOM   7127  C CG  . LEU   B 1 434 ? 9.989   -9.742  19.449  1.00 31.91  ?  434 LEU   B CG  1 
ATOM   7128  C CD1 . LEU   B 1 434 ? 8.942   -10.854 19.403  1.00 35.01  ?  434 LEU   B CD1 1 
ATOM   7129  C CD2 . LEU   B 1 434 ? 9.341   -8.366  19.309  1.00 24.41  ?  434 LEU   B CD2 1 
ATOM   7130  N N   . ILE   B 1 435 ? 13.897  -10.501 19.949  1.00 31.92  ?  435 ILE   B N   1 
ATOM   7131  C CA  . ILE   B 1 435 ? 14.979  -10.533 18.964  1.00 33.79  ?  435 ILE   B CA  1 
ATOM   7132  C C   . ILE   B 1 435 ? 15.433  -11.970 18.725  1.00 38.92  ?  435 ILE   B C   1 
ATOM   7133  O O   . ILE   B 1 435 ? 15.586  -12.413 17.579  1.00 34.83  ?  435 ILE   B O   1 
ATOM   7134  C CB  . ILE   B 1 435 ? 16.144  -9.640  19.424  1.00 29.08  ?  435 ILE   B CB  1 
ATOM   7135  C CG1 . ILE   B 1 435 ? 15.723  -8.168  19.390  1.00 26.26  ?  435 ILE   B CG1 1 
ATOM   7136  C CG2 . ILE   B 1 435 ? 17.379  -9.875  18.561  1.00 31.04  ?  435 ILE   B CG2 1 
ATOM   7137  C CD1 . ILE   B 1 435 ? 16.641  -7.262  20.190  1.00 29.54  ?  435 ILE   B CD1 1 
ATOM   7138  N N   . GLY   B 1 436 ? 15.616  -12.729 19.806  1.00 37.07  ?  436 GLY   B N   1 
ATOM   7139  C CA  . GLY   B 1 436 ? 16.093  -14.098 19.736  1.00 38.40  ?  436 GLY   B CA  1 
ATOM   7140  C C   . GLY   B 1 436 ? 15.182  -15.051 18.990  1.00 38.80  ?  436 GLY   B C   1 
ATOM   7141  O O   . GLY   B 1 436 ? 15.530  -16.216 18.789  1.00 51.28  ?  436 GLY   B O   1 
ATOM   7142  N N   . LEU   B 1 437 ? 14.013  -14.572 18.574  1.00 43.35  ?  437 LEU   B N   1 
ATOM   7143  C CA  . LEU   B 1 437 ? 13.081  -15.351 17.773  1.00 38.91  ?  437 LEU   B CA  1 
ATOM   7144  C C   . LEU   B 1 437 ? 13.112  -14.977 16.299  1.00 45.64  ?  437 LEU   B C   1 
ATOM   7145  O O   . LEU   B 1 437 ? 12.260  -15.448 15.540  1.00 48.90  ?  437 LEU   B O   1 
ATOM   7146  C CB  . LEU   B 1 437 ? 11.656  -15.182 18.301  1.00 41.02  ?  437 LEU   B CB  1 
ATOM   7147  C CG  . LEU   B 1 437 ? 11.325  -15.792 19.658  1.00 40.32  ?  437 LEU   B CG  1 
ATOM   7148  C CD1 . LEU   B 1 437 ? 9.851   -15.624 19.924  1.00 39.84  ?  437 LEU   B CD1 1 
ATOM   7149  C CD2 . LEU   B 1 437 ? 11.706  -17.256 19.663  1.00 48.64  ?  437 LEU   B CD2 1 
ATOM   7150  N N   . LYS   B 1 438 ? 14.059  -14.134 15.877  1.00 44.94  ?  438 LYS   B N   1 
ATOM   7151  C CA  . LYS   B 1 438 ? 14.024  -13.613 14.513  1.00 50.30  ?  438 LYS   B CA  1 
ATOM   7152  C C   . LYS   B 1 438 ? 14.134  -14.734 13.489  1.00 54.70  ?  438 LYS   B C   1 
ATOM   7153  O O   . LYS   B 1 438 ? 13.285  -14.864 12.600  1.00 53.61  ?  438 LYS   B O   1 
ATOM   7154  C CB  . LYS   B 1 438 ? 15.131  -12.578 14.315  1.00 46.36  ?  438 LYS   B CB  1 
ATOM   7155  C CG  . LYS   B 1 438 ? 14.736  -11.193 14.793  1.00 43.77  ?  438 LYS   B CG  1 
ATOM   7156  C CD  . LYS   B 1 438 ? 15.914  -10.240 14.817  1.00 42.36  ?  438 LYS   B CD  1 
ATOM   7157  C CE  . LYS   B 1 438 ? 16.298  -9.781  13.430  1.00 42.43  ?  438 LYS   B CE  1 
ATOM   7158  N NZ  . LYS   B 1 438 ? 17.447  -8.841  13.519  1.00 41.55  ?  438 LYS   B NZ  1 
ATOM   7159  N N   . GLU   B 1 439 ? 15.172  -15.564 13.606  1.00 68.10  ?  439 GLU   B N   1 
ATOM   7160  C CA  . GLU   B 1 439 ? 15.317  -16.699 12.703  1.00 62.27  ?  439 GLU   B CA  1 
ATOM   7161  C C   . GLU   B 1 439 ? 14.179  -17.698 12.862  1.00 60.95  ?  439 GLU   B C   1 
ATOM   7162  O O   . GLU   B 1 439 ? 13.880  -18.437 11.919  1.00 61.05  ?  439 GLU   B O   1 
ATOM   7163  C CB  . GLU   B 1 439 ? 16.664  -17.391 12.937  1.00 67.18  ?  439 GLU   B CB  1 
ATOM   7164  C CG  . GLU   B 1 439 ? 17.892  -16.509 12.681  1.00 73.34  ?  439 GLU   B CG  1 
ATOM   7165  C CD  . GLU   B 1 439 ? 18.346  -15.735 13.916  1.00 73.20  ?  439 GLU   B CD  1 
ATOM   7166  O OE1 . GLU   B 1 439 ? 17.960  -16.120 15.042  1.00 78.11  ?  439 GLU   B OE1 1 
ATOM   7167  O OE2 . GLU   B 1 439 ? 19.092  -14.741 13.760  1.00 68.90  ?  439 GLU   B OE2 1 
ATOM   7168  N N   . LYS   B 1 440 ? 13.530  -17.726 14.027  1.00 57.39  ?  440 LYS   B N   1 
ATOM   7169  C CA  . LYS   B 1 440 ? 12.443  -18.663 14.275  1.00 56.11  ?  440 LYS   B CA  1 
ATOM   7170  C C   . LYS   B 1 440 ? 11.099  -18.169 13.753  1.00 55.65  ?  440 LYS   B C   1 
ATOM   7171  O O   . LYS   B 1 440 ? 10.160  -18.967 13.668  1.00 61.29  ?  440 LYS   B O   1 
ATOM   7172  C CB  . LYS   B 1 440 ? 12.347  -18.959 15.777  1.00 53.29  ?  440 LYS   B CB  1 
ATOM   7173  C CG  . LYS   B 1 440 ? 11.617  -20.254 16.132  1.00 57.39  ?  440 LYS   B CG  1 
ATOM   7174  C CD  . LYS   B 1 440 ? 11.594  -20.482 17.642  1.00 57.78  ?  440 LYS   B CD  1 
ATOM   7175  C CE  . LYS   B 1 440 ? 10.772  -21.716 18.027  1.00 53.14  ?  440 LYS   B CE  1 
ATOM   7176  N NZ  . LYS   B 1 440 ? 10.730  -21.916 19.511  1.00 56.24  ?  440 LYS   B NZ  1 
ATOM   7177  N N   . PHE   B 1 441 ? 10.985  -16.885 13.392  1.00 56.70  ?  441 PHE   B N   1 
ATOM   7178  C CA  . PHE   B 1 441 ? 9.706   -16.356 12.924  1.00 52.12  ?  441 PHE   B CA  1 
ATOM   7179  C C   . PHE   B 1 441 ? 9.225   -17.088 11.680  1.00 62.17  ?  441 PHE   B C   1 
ATOM   7180  O O   . PHE   B 1 441 ? 8.027   -17.356 11.535  1.00 63.38  ?  441 PHE   B O   1 
ATOM   7181  C CB  . PHE   B 1 441 ? 9.818   -14.853 12.641  1.00 48.65  ?  441 PHE   B CB  1 
ATOM   7182  C CG  . PHE   B 1 441 ? 9.876   -13.999 13.881  1.00 51.47  ?  441 PHE   B CG  1 
ATOM   7183  C CD1 . PHE   B 1 441 ? 9.299   -14.428 15.064  1.00 45.38  ?  441 PHE   B CD1 1 
ATOM   7184  C CD2 . PHE   B 1 441 ? 10.507  -12.765 13.860  1.00 48.24  ?  441 PHE   B CD2 1 
ATOM   7185  C CE1 . PHE   B 1 441 ? 9.352   -13.642 16.207  1.00 43.94  ?  441 PHE   B CE1 1 
ATOM   7186  C CE2 . PHE   B 1 441 ? 10.564  -11.977 14.999  1.00 47.39  ?  441 PHE   B CE2 1 
ATOM   7187  C CZ  . PHE   B 1 441 ? 9.986   -12.418 16.175  1.00 40.82  ?  441 PHE   B CZ  1 
ATOM   7188  N N   . ALA   B 1 442 ? 10.149  -17.422 10.773  1.00 62.41  ?  442 ALA   B N   1 
ATOM   7189  C CA  . ALA   B 1 442 ? 9.764   -18.028 9.502   1.00 61.03  ?  442 ALA   B CA  1 
ATOM   7190  C C   . ALA   B 1 442 ? 9.094   -19.381 9.705   1.00 64.14  ?  442 ALA   B C   1 
ATOM   7191  O O   . ALA   B 1 442 ? 8.157   -19.735 8.978   1.00 66.63  ?  442 ALA   B O   1 
ATOM   7192  C CB  . ALA   B 1 442 ? 10.991  -18.163 8.601   1.00 57.82  ?  442 ALA   B CB  1 
ATOM   7193  N N   . THR   B 1 443 ? 9.554   -20.150 10.690  1.00 64.93  ?  443 THR   B N   1 
ATOM   7194  C CA  . THR   B 1 443 ? 9.014   -21.475 10.962  1.00 63.49  ?  443 THR   B CA  1 
ATOM   7195  C C   . THR   B 1 443 ? 7.846   -21.453 11.944  1.00 65.45  ?  443 THR   B C   1 
ATOM   7196  O O   . THR   B 1 443 ? 7.407   -22.518 12.389  1.00 67.02  ?  443 THR   B O   1 
ATOM   7197  C CB  . THR   B 1 443 ? 10.120  -22.404 11.481  1.00 65.77  ?  443 THR   B CB  1 
ATOM   7198  O OG1 . THR   B 1 443 ? 10.979  -21.686 12.378  1.00 63.97  ?  443 THR   B OG1 1 
ATOM   7199  C CG2 . THR   B 1 443 ? 10.939  -22.965 10.322  1.00 57.63  ?  443 THR   B CG2 1 
ATOM   7200  N N   . LEU   B 1 444 ? 7.331   -20.274 12.287  1.00 66.58  ?  444 LEU   B N   1 
ATOM   7201  C CA  . LEU   B 1 444 ? 6.142   -20.190 13.123  1.00 68.79  ?  444 LEU   B CA  1 
ATOM   7202  C C   . LEU   B 1 444 ? 4.899   -20.546 12.319  1.00 63.94  ?  444 LEU   B C   1 
ATOM   7203  O O   . LEU   B 1 444 ? 4.774   -20.189 11.144  1.00 60.31  ?  444 LEU   B O   1 
ATOM   7204  C CB  . LEU   B 1 444 ? 5.994   -18.791 13.723  1.00 64.08  ?  444 LEU   B CB  1 
ATOM   7205  C CG  . LEU   B 1 444 ? 7.100   -18.340 14.677  1.00 56.40  ?  444 LEU   B CG  1 
ATOM   7206  C CD1 . LEU   B 1 444 ? 6.656   -17.129 15.488  1.00 51.08  ?  444 LEU   B CD1 1 
ATOM   7207  C CD2 . LEU   B 1 444 ? 7.522   -19.485 15.583  1.00 55.33  ?  444 LEU   B CD2 1 
ATOM   7208  N N   . LYS   B 1 445 ? 3.974   -21.245 12.967  1.00 64.49  ?  445 LYS   B N   1 
ATOM   7209  C CA  . LYS   B 1 445 ? 2.750   -21.717 12.340  1.00 71.94  ?  445 LYS   B CA  1 
ATOM   7210  C C   . LYS   B 1 445 ? 1.551   -20.940 12.868  1.00 67.28  ?  445 LYS   B C   1 
ATOM   7211  O O   . LYS   B 1 445 ? 1.537   -20.491 14.017  1.00 67.63  ?  445 LYS   B O   1 
ATOM   7212  C CB  . LYS   B 1 445 ? 2.560   -23.216 12.595  1.00 74.42  ?  445 LYS   B CB  1 
ATOM   7213  C CG  . LYS   B 1 445 ? 3.677   -24.072 12.022  1.00 81.46  ?  445 LYS   B CG  1 
ATOM   7214  C CD  . LYS   B 1 445 ? 3.561   -25.515 12.478  1.00 90.96  ?  445 LYS   B CD  1 
ATOM   7215  C CE  . LYS   B 1 445 ? 4.634   -26.377 11.832  1.00 92.71  ?  445 LYS   B CE  1 
ATOM   7216  N NZ  . LYS   B 1 445 ? 4.508   -26.397 10.347  1.00 93.58  ?  445 LYS   B NZ  1 
ATOM   7217  N N   . GLY   B 1 446 ? 0.539   -20.790 12.017  1.00 70.17  ?  446 GLY   B N   1 
ATOM   7218  C CA  . GLY   B 1 446 ? -0.687  -20.117 12.397  1.00 66.07  ?  446 GLY   B CA  1 
ATOM   7219  C C   . GLY   B 1 446 ? -1.427  -20.850 13.497  1.00 77.37  ?  446 GLY   B C   1 
ATOM   7220  O O   . GLY   B 1 446 ? -1.030  -21.945 13.899  1.00 76.57  ?  446 GLY   B O   1 
ATOM   7221  N N   . LEU   B 1 447 ? -2.509  -20.248 13.998  1.00 82.03  ?  447 LEU   B N   1 
ATOM   7222  C CA  . LEU   B 1 447 ? -3.286  -20.829 15.081  1.00 79.68  ?  447 LEU   B CA  1 
ATOM   7223  C C   . LEU   B 1 447 ? -4.696  -21.138 14.599  1.00 77.30  ?  447 LEU   B C   1 
ATOM   7224  O O   . LEU   B 1 447 ? -5.213  -20.500 13.675  1.00 72.60  ?  447 LEU   B O   1 
ATOM   7225  C CB  . LEU   B 1 447 ? -3.336  -19.886 16.293  1.00 75.48  ?  447 LEU   B CB  1 
ATOM   7226  C CG  . LEU   B 1 447 ? -1.977  -19.606 16.943  1.00 73.81  ?  447 LEU   B CG  1 
ATOM   7227  C CD1 . LEU   B 1 447 ? -2.068  -18.494 17.979  1.00 64.20  ?  447 LEU   B CD1 1 
ATOM   7228  C CD2 . LEU   B 1 447 ? -1.409  -20.880 17.559  1.00 73.99  ?  447 LEU   B CD2 1 
ATOM   7229  N N   . GLU   B 1 448 ? -5.319  -22.122 15.241  1.00 67.67  ?  448 GLU   B N   1 
ATOM   7230  C CA  . GLU   B 1 448 ? -6.630  -22.606 14.839  1.00 72.10  ?  448 GLU   B CA  1 
ATOM   7231  C C   . GLU   B 1 448 ? -7.513  -22.754 16.070  1.00 65.76  ?  448 GLU   B C   1 
ATOM   7232  O O   . GLU   B 1 448 ? -7.035  -23.075 17.160  1.00 61.29  ?  448 GLU   B O   1 
ATOM   7233  C CB  . GLU   B 1 448 ? -6.507  -23.942 14.092  1.00 71.78  ?  448 GLU   B CB  1 
ATOM   7234  C CG  . GLU   B 1 448 ? -7.748  -24.384 13.350  1.00 72.98  ?  448 GLU   B CG  1 
ATOM   7235  C CD  . GLU   B 1 448 ? -7.522  -25.679 12.600  1.00 81.79  ?  448 GLU   B CD  1 
ATOM   7236  O OE1 . GLU   B 1 448 ? -6.422  -26.259 12.742  1.00 79.21  ?  448 GLU   B OE1 1 
ATOM   7237  O OE2 . GLU   B 1 448 ? -8.437  -26.116 11.870  1.00 90.55  ?  448 GLU   B OE2 1 
ATOM   7238  N N   . PHE   B 1 449 ? -8.809  -22.515 15.886  1.00 63.78  ?  449 PHE   B N   1 
ATOM   7239  C CA  . PHE   B 1 449 ? -9.742  -22.572 17.002  1.00 63.07  ?  449 PHE   B CA  1 
ATOM   7240  C C   . PHE   B 1 449 ? -9.950  -24.001 17.489  1.00 68.43  ?  449 PHE   B C   1 
ATOM   7241  O O   . PHE   B 1 449 ? -10.025 -24.946 16.697  1.00 69.28  ?  449 PHE   B O   1 
ATOM   7242  C CB  . PHE   B 1 449 ? -11.093 -21.979 16.605  1.00 62.38  ?  449 PHE   B CB  1 
ATOM   7243  C CG  . PHE   B 1 449 ? -11.107 -20.487 16.546  1.00 56.65  ?  449 PHE   B CG  1 
ATOM   7244  C CD1 . PHE   B 1 449 ? -11.180 -19.742 17.706  1.00 59.98  ?  449 PHE   B CD1 1 
ATOM   7245  C CD2 . PHE   B 1 449 ? -11.062 -19.831 15.332  1.00 52.82  ?  449 PHE   B CD2 1 
ATOM   7246  C CE1 . PHE   B 1 449 ? -11.195 -18.364 17.658  1.00 62.53  ?  449 PHE   B CE1 1 
ATOM   7247  C CE2 . PHE   B 1 449 ? -11.083 -18.461 15.276  1.00 56.50  ?  449 PHE   B CE2 1 
ATOM   7248  C CZ  . PHE   B 1 449 ? -11.147 -17.724 16.440  1.00 62.22  ?  449 PHE   B CZ  1 
ATOM   7249  N N   . GLU   B 1 450 ? -10.042 -24.147 18.809  1.00 66.39  ?  450 GLU   B N   1 
ATOM   7250  C CA  . GLU   B 1 450 ? -10.576 -25.337 19.459  1.00 64.80  ?  450 GLU   B CA  1 
ATOM   7251  C C   . GLU   B 1 450 ? -11.901 -25.066 20.148  1.00 64.41  ?  450 GLU   B C   1 
ATOM   7252  O O   . GLU   B 1 450 ? -12.790 -25.919 20.129  1.00 76.56  ?  450 GLU   B O   1 
ATOM   7253  C CB  . GLU   B 1 450 ? -9.571  -25.885 20.479  1.00 66.47  ?  450 GLU   B CB  1 
ATOM   7254  C CG  . GLU   B 1 450 ? -9.784  -27.348 20.836  1.00 77.90  ?  450 GLU   B CG  1 
ATOM   7255  C CD  . GLU   B 1 450 ? -8.774  -27.856 21.850  1.00 88.62  ?  450 GLU   B CD  1 
ATOM   7256  O OE1 . GLU   B 1 450 ? -8.380  -27.073 22.741  1.00 87.65  ?  450 GLU   B OE1 1 
ATOM   7257  O OE2 . GLU   B 1 450 ? -8.370  -29.037 21.753  1.00 91.13  ?  450 GLU   B OE2 1 
ATOM   7258  N N   . TYR   B 1 451 ? -12.047 -23.889 20.755  1.00 59.74  ?  451 TYR   B N   1 
ATOM   7259  C CA  . TYR   B 1 451 ? -13.321 -23.389 21.260  1.00 65.59  ?  451 TYR   B CA  1 
ATOM   7260  C C   . TYR   B 1 451 ? -13.415 -21.911 20.913  1.00 62.05  ?  451 TYR   B C   1 
ATOM   7261  O O   . TYR   B 1 451 ? -12.465 -21.157 21.151  1.00 58.97  ?  451 TYR   B O   1 
ATOM   7262  C CB  . TYR   B 1 451 ? -13.460 -23.585 22.780  1.00 61.64  ?  451 TYR   B CB  1 
ATOM   7263  C CG  . TYR   B 1 451 ? -14.419 -22.604 23.435  1.00 66.64  ?  451 TYR   B CG  1 
ATOM   7264  C CD1 . TYR   B 1 451 ? -15.799 -22.769 23.335  1.00 71.28  ?  451 TYR   B CD1 1 
ATOM   7265  C CD2 . TYR   B 1 451 ? -13.944 -21.504 24.147  1.00 65.13  ?  451 TYR   B CD2 1 
ATOM   7266  C CE1 . TYR   B 1 451 ? -16.678 -21.866 23.926  1.00 70.04  ?  451 TYR   B CE1 1 
ATOM   7267  C CE2 . TYR   B 1 451 ? -14.814 -20.598 24.741  1.00 64.96  ?  451 TYR   B CE2 1 
ATOM   7268  C CZ  . TYR   B 1 451 ? -16.179 -20.783 24.629  1.00 71.68  ?  451 TYR   B CZ  1 
ATOM   7269  O OH  . TYR   B 1 451 ? -17.042 -19.883 25.221  1.00 65.87  ?  451 TYR   B OH  1 
ATOM   7270  N N   . GLU   B 1 452 ? -14.551 -21.494 20.359  1.00 56.93  ?  452 GLU   B N   1 
ATOM   7271  C CA  . GLU   B 1 452 ? -14.731 -20.108 19.943  1.00 60.22  ?  452 GLU   B CA  1 
ATOM   7272  C C   . GLU   B 1 452 ? -16.074 -19.586 20.435  1.00 61.51  ?  452 GLU   B C   1 
ATOM   7273  O O   . GLU   B 1 452 ? -17.129 -20.133 20.047  1.00 61.41  ?  452 GLU   B O   1 
ATOM   7274  C CB  . GLU   B 1 452 ? -14.623 -19.975 18.424  1.00 63.76  ?  452 GLU   B CB  1 
ATOM   7275  C CG  . GLU   B 1 452 ? -14.641 -18.535 17.949  1.00 60.97  ?  452 GLU   B CG  1 
ATOM   7276  C CD  . GLU   B 1 452 ? -14.508 -18.414 16.451  1.00 61.84  ?  452 GLU   B CD  1 
ATOM   7277  O OE1 . GLU   B 1 452 ? -14.771 -19.413 15.748  1.00 63.88  ?  452 GLU   B OE1 1 
ATOM   7278  O OE2 . GLU   B 1 452 ? -14.141 -17.316 15.980  1.00 63.92  ?  452 GLU   B OE2 1 
ATOM   7279  N N   . PRO   B 1 453 ? -16.094 -18.544 21.262  1.00 61.03  ?  453 PRO   B N   1 
ATOM   7280  C CA  . PRO   B 1 453 ? -17.360 -17.951 21.694  1.00 63.96  ?  453 PRO   B CA  1 
ATOM   7281  C C   . PRO   B 1 453 ? -17.843 -16.919 20.690  1.00 60.95  ?  453 PRO   B C   1 
ATOM   7282  O O   . PRO   B 1 453 ? -17.047 -16.397 19.893  1.00 57.67  ?  453 PRO   B O   1 
ATOM   7283  C CB  . PRO   B 1 453 ? -16.997 -17.300 23.035  1.00 63.66  ?  453 PRO   B CB  1 
ATOM   7284  C CG  . PRO   B 1 453 ? -15.581 -16.882 22.842  1.00 58.30  ?  453 PRO   B CG  1 
ATOM   7285  C CD  . PRO   B 1 453 ? -14.942 -17.911 21.923  1.00 56.98  ?  453 PRO   B CD  1 
ATOM   7286  N N   . PRO   B 1 454 ? -19.140 -16.595 20.700  1.00 59.91  ?  454 PRO   B N   1 
ATOM   7287  C CA  . PRO   B 1 454 ? -19.673 -15.721 19.641  1.00 56.87  ?  454 PRO   B CA  1 
ATOM   7288  C C   . PRO   B 1 454 ? -19.197 -14.282 19.731  1.00 58.54  ?  454 PRO   B C   1 
ATOM   7289  O O   . PRO   B 1 454 ? -18.942 -13.662 18.692  1.00 66.47  ?  454 PRO   B O   1 
ATOM   7290  C CB  . PRO   B 1 454 ? -21.195 -15.831 19.832  1.00 59.65  ?  454 PRO   B CB  1 
ATOM   7291  C CG  . PRO   B 1 454 ? -21.402 -17.089 20.619  1.00 58.37  ?  454 PRO   B CG  1 
ATOM   7292  C CD  . PRO   B 1 454 ? -20.215 -17.175 21.525  1.00 61.00  ?  454 PRO   B CD  1 
ATOM   7293  N N   . VAL   B 1 455 ? -19.072 -13.723 20.933  1.00 54.85  ?  455 VAL   B N   1 
ATOM   7294  C CA  . VAL   B 1 455 ? -18.747 -12.313 21.111  1.00 53.21  ?  455 VAL   B CA  1 
ATOM   7295  C C   . VAL   B 1 455 ? -17.497 -12.198 21.974  1.00 64.23  ?  455 VAL   B C   1 
ATOM   7296  O O   . VAL   B 1 455 ? -17.285 -13.008 22.885  1.00 59.62  ?  455 VAL   B O   1 
ATOM   7297  C CB  . VAL   B 1 455 ? -19.925 -11.538 21.745  1.00 59.54  ?  455 VAL   B CB  1 
ATOM   7298  C CG1 . VAL   B 1 455 ? -19.662 -10.036 21.737  1.00 59.46  ?  455 VAL   B CG1 1 
ATOM   7299  C CG2 . VAL   B 1 455 ? -21.230 -11.859 21.032  1.00 49.95  ?  455 VAL   B CG2 1 
ATOM   7300  N N   . LEU   B 1 456 ? -16.667 -11.192 21.674  1.00 67.34  ?  456 LEU   B N   1 
ATOM   7301  C CA  . LEU   B 1 456 ? -15.480 -10.861 22.467  1.00 60.72  ?  456 LEU   B CA  1 
ATOM   7302  C C   . LEU   B 1 456 ? -14.571 -12.074 22.638  1.00 58.68  ?  456 LEU   B C   1 
ATOM   7303  O O   . LEU   B 1 456 ? -14.087 -12.371 23.731  1.00 64.07  ?  456 LEU   B O   1 
ATOM   7304  C CB  . LEU   B 1 456 ? -15.875 -10.289 23.830  1.00 66.13  ?  456 LEU   B CB  1 
ATOM   7305  C CG  . LEU   B 1 456 ? -16.559 -8.923  23.859  1.00 64.31  ?  456 LEU   B CG  1 
ATOM   7306  C CD1 . LEU   B 1 456 ? -16.991 -8.587  25.275  1.00 57.55  ?  456 LEU   B CD1 1 
ATOM   7307  C CD2 . LEU   B 1 456 ? -15.623 -7.856  23.316  1.00 65.45  ?  456 LEU   B CD2 1 
ATOM   7308  N N   . ARG   B 1 457 ? -14.339 -12.784 21.533  1.00 52.39  ?  457 ARG   B N   1 
ATOM   7309  C CA  . ARG   B 1 457 ? -13.665 -14.074 21.621  1.00 51.62  ?  457 ARG   B CA  1 
ATOM   7310  C C   . ARG   B 1 457 ? -12.254 -13.948 22.184  1.00 52.09  ?  457 ARG   B C   1 
ATOM   7311  O O   . ARG   B 1 457 ? -11.739 -14.909 22.765  1.00 54.48  ?  457 ARG   B O   1 
ATOM   7312  C CB  . ARG   B 1 457 ? -13.633 -14.742 20.245  1.00 55.75  ?  457 ARG   B CB  1 
ATOM   7313  C CG  . ARG   B 1 457 ? -12.823 -13.969 19.232  1.00 55.22  ?  457 ARG   B CG  1 
ATOM   7314  C CD  . ARG   B 1 457 ? -12.880 -14.568 17.846  1.00 50.03  ?  457 ARG   B CD  1 
ATOM   7315  N NE  . ARG   B 1 457 ? -11.868 -13.934 17.012  1.00 54.24  ?  457 ARG   B NE  1 
ATOM   7316  C CZ  . ARG   B 1 457 ? -11.639 -14.232 15.742  1.00 61.47  ?  457 ARG   B CZ  1 
ATOM   7317  N NH1 . ARG   B 1 457 ? -12.368 -15.133 15.102  1.00 61.42  ?  457 ARG   B NH1 1 
ATOM   7318  N NH2 . ARG   B 1 457 ? -10.652 -13.611 15.099  1.00 55.10  ?  457 ARG   B NH2 1 
ATOM   7319  N N   . HIS   B 1 458 ? -11.627 -12.772 22.061  1.00 50.28  ?  458 HIS   B N   1 
ATOM   7320  C CA  . HIS   B 1 458 ? -10.224 -12.640 22.448  1.00 48.11  ?  458 HIS   B CA  1 
ATOM   7321  C C   . HIS   B 1 458 ? -10.006 -12.814 23.946  1.00 44.06  ?  458 HIS   B C   1 
ATOM   7322  O O   . HIS   B 1 458 ? -8.911  -13.209 24.356  1.00 44.24  ?  458 HIS   B O   1 
ATOM   7323  C CB  . HIS   B 1 458 ? -9.656  -11.290 21.994  1.00 48.23  ?  458 HIS   B CB  1 
ATOM   7324  C CG  . HIS   B 1 458 ? -10.384 -10.100 22.543  1.00 48.33  ?  458 HIS   B CG  1 
ATOM   7325  N ND1 . HIS   B 1 458 ? -11.664 -9.762  22.154  1.00 54.70  ?  458 HIS   B ND1 1 
ATOM   7326  C CD2 . HIS   B 1 458 ? -9.999  -9.151  23.431  1.00 52.85  ?  458 HIS   B CD2 1 
ATOM   7327  C CE1 . HIS   B 1 458 ? -12.040 -8.664  22.787  1.00 53.20  ?  458 HIS   B CE1 1 
ATOM   7328  N NE2 . HIS   B 1 458 ? -11.048 -8.273  23.568  1.00 54.06  ?  458 HIS   B NE2 1 
ATOM   7329  N N   . PHE   B 1 459 ? -11.023 -12.555 24.768  1.00 44.21  ?  459 PHE   B N   1 
ATOM   7330  C CA  . PHE   B 1 459 ? -10.854 -12.717 26.208  1.00 47.28  ?  459 PHE   B CA  1 
ATOM   7331  C C   . PHE   B 1 459 ? -10.821 -14.187 26.615  1.00 45.25  ?  459 PHE   B C   1 
ATOM   7332  O O   . PHE   B 1 459 ? -10.059 -14.568 27.514  1.00 44.47  ?  459 PHE   B O   1 
ATOM   7333  C CB  . PHE   B 1 459 ? -11.968 -11.987 26.953  1.00 42.09  ?  459 PHE   B CB  1 
ATOM   7334  C CG  . PHE   B 1 459 ? -11.821 -10.495 26.949  1.00 41.57  ?  459 PHE   B CG  1 
ATOM   7335  C CD1 . PHE   B 1 459 ? -10.750 -9.896  27.574  1.00 40.37  ?  459 PHE   B CD1 1 
ATOM   7336  C CD2 . PHE   B 1 459 ? -12.763 -9.693  26.330  1.00 49.65  ?  459 PHE   B CD2 1 
ATOM   7337  C CE1 . PHE   B 1 459 ? -10.613 -8.522  27.581  1.00 43.87  ?  459 PHE   B CE1 1 
ATOM   7338  C CE2 . PHE   B 1 459 ? -12.631 -8.319  26.333  1.00 45.86  ?  459 PHE   B CE2 1 
ATOM   7339  C CZ  . PHE   B 1 459 ? -11.557 -7.733  26.960  1.00 39.24  ?  459 PHE   B CZ  1 
ATOM   7340  N N   . THR   B 1 460 ? -11.631 -15.029 25.966  1.00 47.24  ?  460 THR   B N   1 
ATOM   7341  C CA  . THR   B 1 460 ? -11.871 -16.373 26.473  1.00 47.59  ?  460 THR   B CA  1 
ATOM   7342  C C   . THR   B 1 460 ? -11.854 -17.487 25.433  1.00 48.99  ?  460 THR   B C   1 
ATOM   7343  O O   . THR   B 1 460 ? -12.130 -18.633 25.799  1.00 51.21  ?  460 THR   B O   1 
ATOM   7344  C CB  . THR   B 1 460 ? -13.221 -16.412 27.206  1.00 51.27  ?  460 THR   B CB  1 
ATOM   7345  O OG1 . THR   B 1 460 ? -14.209 -15.766 26.396  1.00 51.44  ?  460 THR   B OG1 1 
ATOM   7346  C CG2 . THR   B 1 460 ? -13.126 -15.705 28.555  1.00 45.33  ?  460 THR   B CG2 1 
ATOM   7347  N N   . ALA   B 1 461 ? -11.553 -17.210 24.167  1.00 49.91  ?  461 ALA   B N   1 
ATOM   7348  C CA  . ALA   B 1 461 ? -11.525 -18.288 23.188  1.00 49.23  ?  461 ALA   B CA  1 
ATOM   7349  C C   . ALA   B 1 461 ? -10.320 -19.191 23.415  1.00 52.63  ?  461 ALA   B C   1 
ATOM   7350  O O   . ALA   B 1 461 ? -9.282  -18.762 23.925  1.00 51.65  ?  461 ALA   B O   1 
ATOM   7351  C CB  . ALA   B 1 461 ? -11.480 -17.741 21.759  1.00 57.48  ?  461 ALA   B CB  1 
ATOM   7352  N N   . ARG   B 1 462 ? -10.463 -20.453 23.022  1.00 49.52  ?  462 ARG   B N   1 
ATOM   7353  C CA  . ARG   B 1 462 ? -9.352  -21.393 23.023  1.00 55.67  ?  462 ARG   B CA  1 
ATOM   7354  C C   . ARG   B 1 462 ? -8.899  -21.642 21.589  1.00 54.54  ?  462 ARG   B C   1 
ATOM   7355  O O   . ARG   B 1 462 ? -9.689  -21.547 20.646  1.00 58.23  ?  462 ARG   B O   1 
ATOM   7356  C CB  . ARG   B 1 462 ? -9.735  -22.713 23.704  1.00 56.43  ?  462 ARG   B CB  1 
ATOM   7357  C CG  . ARG   B 1 462 ? -10.184 -22.557 25.155  1.00 53.47  ?  462 ARG   B CG  1 
ATOM   7358  C CD  . ARG   B 1 462 ? -10.461 -23.909 25.799  1.00 49.75  ?  462 ARG   B CD  1 
ATOM   7359  N NE  . ARG   B 1 462 ? -9.263  -24.738 25.855  1.00 49.72  ?  462 ARG   B NE  1 
ATOM   7360  C CZ  . ARG   B 1 462 ? -8.352  -24.673 26.817  1.00 51.20  ?  462 ARG   B CZ  1 
ATOM   7361  N NH1 . ARG   B 1 462 ? -8.472  -23.828 27.829  1.00 49.70  ?  462 ARG   B NH1 1 
ATOM   7362  N NH2 . ARG   B 1 462 ? -7.290  -25.472 26.761  1.00 53.25  ?  462 ARG   B NH2 1 
ATOM   7363  N N   . LEU   B 1 463 ? -7.613  -21.938 21.428  1.00 51.06  ?  463 LEU   B N   1 
ATOM   7364  C CA  . LEU   B 1 463 ? -7.014  -22.099 20.113  1.00 54.63  ?  463 LEU   B CA  1 
ATOM   7365  C C   . LEU   B 1 463 ? -6.084  -23.306 20.123  1.00 60.00  ?  463 LEU   B C   1 
ATOM   7366  O O   . LEU   B 1 463 ? -5.836  -23.920 21.164  1.00 61.07  ?  463 LEU   B O   1 
ATOM   7367  C CB  . LEU   B 1 463 ? -6.248  -20.838 19.684  1.00 59.14  ?  463 LEU   B CB  1 
ATOM   7368  C CG  . LEU   B 1 463 ? -7.006  -19.663 19.052  1.00 58.66  ?  463 LEU   B CG  1 
ATOM   7369  C CD1 . LEU   B 1 463 ? -7.802  -18.858 20.070  1.00 55.67  ?  463 LEU   B CD1 1 
ATOM   7370  C CD2 . LEU   B 1 463 ? -6.034  -18.762 18.313  1.00 63.45  ?  463 LEU   B CD2 1 
ATOM   7371  N N   . LYS   B 1 464 ? -5.566  -23.646 18.941  1.00 65.54  ?  464 LYS   B N   1 
ATOM   7372  C CA  . LYS   B 1 464 ? -4.581  -24.711 18.801  1.00 66.00  ?  464 LYS   B CA  1 
ATOM   7373  C C   . LYS   B 1 464 ? -3.775  -24.455 17.535  1.00 69.07  ?  464 LYS   B C   1 
ATOM   7374  O O   . LYS   B 1 464 ? -4.280  -23.814 16.607  1.00 64.77  ?  464 LYS   B O   1 
ATOM   7375  C CB  . LYS   B 1 464 ? -5.254  -26.093 18.752  1.00 63.61  ?  464 LYS   B CB  1 
ATOM   7376  C CG  . LYS   B 1 464 ? -6.273  -26.258 17.633  1.00 72.70  ?  464 LYS   B CG  1 
ATOM   7377  C CD  . LYS   B 1 464 ? -6.908  -27.644 17.641  1.00 66.56  ?  464 LYS   B CD  1 
ATOM   7378  C CE  . LYS   B 1 464 ? -7.804  -27.839 16.427  1.00 65.67  ?  464 LYS   B CE  1 
ATOM   7379  N NZ  . LYS   B 1 464 ? -8.346  -29.223 16.351  1.00 62.79  ?  464 LYS   B NZ  1 
ATOM   7380  N N   . PRO   B 1 465 ? -2.525  -24.911 17.475  1.00 75.68  ?  465 PRO   B N   1 
ATOM   7381  C CA  . PRO   B 1 465 ? -1.718  -24.696 16.271  1.00 80.09  ?  465 PRO   B CA  1 
ATOM   7382  C C   . PRO   B 1 465 ? -2.034  -25.706 15.178  1.00 77.99  ?  465 PRO   B C   1 
ATOM   7383  O O   . PRO   B 1 465 ? -2.453  -26.838 15.435  1.00 77.30  ?  465 PRO   B O   1 
ATOM   7384  C CB  . PRO   B 1 465 ? -0.280  -24.862 16.779  1.00 76.03  ?  465 PRO   B CB  1 
ATOM   7385  C CG  . PRO   B 1 465 ? -0.402  -25.807 17.914  1.00 72.22  ?  465 PRO   B CG  1 
ATOM   7386  C CD  . PRO   B 1 465 ? -1.738  -25.525 18.560  1.00 73.45  ?  465 PRO   B CD  1 
ATOM   7387  N N   . ILE   B 1 466 ? -1.819  -25.273 13.939  1.00 83.74  ?  466 ILE   B N   1 
ATOM   7388  C CA  . ILE   B 1 466 ? -2.166  -26.068 12.766  1.00 77.94  ?  466 ILE   B CA  1 
ATOM   7389  C C   . ILE   B 1 466 ? -1.052  -27.051 12.429  1.00 76.32  ?  466 ILE   B C   1 
ATOM   7390  O O   . ILE   B 1 466 ? 0.124   -26.774 12.660  1.00 77.28  ?  466 ILE   B O   1 
ATOM   7391  C CB  . ILE   B 1 466 ? -2.476  -25.158 11.565  1.00 69.66  ?  466 ILE   B CB  1 
ATOM   7392  C CG1 . ILE   B 1 466 ? -3.551  -24.136 11.941  1.00 68.58  ?  466 ILE   B CG1 1 
ATOM   7393  C CG2 . ILE   B 1 466 ? -2.919  -25.984 10.368  1.00 71.28  ?  466 ILE   B CG2 1 
ATOM   7394  C CD1 . ILE   B 1 466 ? -3.845  -23.126 10.861  1.00 67.26  ?  466 ILE   B CD1 1 
ATOM   7395  N N   . ALA   C 1 2   ? -19.762 2.999   89.269  1.00 35.07  ?  2   ALA   C N   1 
ATOM   7396  C CA  . ALA   C 1 2   ? -18.754 3.056   88.217  1.00 32.91  ?  2   ALA   C CA  1 
ATOM   7397  C C   . ALA   C 1 2   ? -19.366 3.638   86.955  1.00 36.36  ?  2   ALA   C C   1 
ATOM   7398  O O   . ALA   C 1 2   ? -20.459 3.236   86.554  1.00 36.02  ?  2   ALA   C O   1 
ATOM   7399  C CB  . ALA   C 1 2   ? -18.185 1.678   87.948  1.00 32.52  ?  2   ALA   C CB  1 
ATOM   7400  N N   . LYS   C 1 3   ? -18.669 4.577   86.321  1.00 31.38  ?  3   LYS   C N   1 
ATOM   7401  C CA  . LYS   C 1 3   ? -19.210 5.293   85.174  1.00 30.91  ?  3   LYS   C CA  1 
ATOM   7402  C C   . LYS   C 1 3   ? -18.383 5.000   83.933  1.00 32.70  ?  3   LYS   C C   1 
ATOM   7403  O O   . LYS   C 1 3   ? -17.156 5.141   83.947  1.00 29.57  ?  3   LYS   C O   1 
ATOM   7404  C CB  . LYS   C 1 3   ? -19.253 6.804   85.415  1.00 33.85  ?  3   LYS   C CB  1 
ATOM   7405  C CG  . LYS   C 1 3   ? -19.738 7.583   84.200  1.00 43.17  ?  3   LYS   C CG  1 
ATOM   7406  C CD  . LYS   C 1 3   ? -19.603 9.088   84.376  1.00 49.51  ?  3   LYS   C CD  1 
ATOM   7407  C CE  . LYS   C 1 3   ? -20.113 9.826   83.137  1.00 56.59  ?  3   LYS   C CE  1 
ATOM   7408  N NZ  . LYS   C 1 3   ? -21.577 9.617   82.896  1.00 52.04  ?  3   LYS   C NZ  1 
ATOM   7409  N N   . ARG   C 1 4   ? -19.063 4.604   82.866  1.00 29.35  ?  4   ARG   C N   1 
ATOM   7410  C CA  A ARG   C 1 4   ? -18.419 4.368   81.585  0.45 29.13  ?  4   ARG   C CA  1 
ATOM   7411  C CA  B ARG   C 1 4   ? -18.422 4.368   81.585  0.55 29.13  ?  4   ARG   C CA  1 
ATOM   7412  C C   . ARG   C 1 4   ? -18.293 5.677   80.817  1.00 29.57  ?  4   ARG   C C   1 
ATOM   7413  O O   . ARG   C 1 4   ? -19.219 6.496   80.801  1.00 29.10  ?  4   ARG   C O   1 
ATOM   7414  C CB  A ARG   C 1 4   ? -19.221 3.362   80.759  0.45 28.21  ?  4   ARG   C CB  1 
ATOM   7415  C CB  B ARG   C 1 4   ? -19.224 3.364   80.760  0.55 28.21  ?  4   ARG   C CB  1 
ATOM   7416  C CG  A ARG   C 1 4   ? -19.591 2.075   81.474  0.45 28.98  ?  4   ARG   C CG  1 
ATOM   7417  C CG  B ARG   C 1 4   ? -19.482 2.041   81.444  0.55 28.90  ?  4   ARG   C CG  1 
ATOM   7418  C CD  A ARG   C 1 4   ? -20.508 1.233   80.595  0.45 29.17  ?  4   ARG   C CD  1 
ATOM   7419  C CD  B ARG   C 1 4   ? -20.077 1.061   80.450  0.55 28.82  ?  4   ARG   C CD  1 
ATOM   7420  N NE  A ARG   C 1 4   ? -20.606 -0.148  81.048  0.45 29.73  ?  4   ARG   C NE  1 
ATOM   7421  N NE  B ARG   C 1 4   ? -19.630 -0.304  80.690  0.55 28.90  ?  4   ARG   C NE  1 
ATOM   7422  C CZ  A ARG   C 1 4   ? -21.659 -0.668  81.662  0.45 30.92  ?  4   ARG   C CZ  1 
ATOM   7423  C CZ  B ARG   C 1 4   ? -19.419 -1.198  79.736  0.55 28.39  ?  4   ARG   C CZ  1 
ATOM   7424  N NH1 A ARG   C 1 4   ? -22.745 0.051   81.902  0.45 31.69  ?  4   ARG   C NH1 1 
ATOM   7425  N NH1 B ARG   C 1 4   ? -19.559 -0.891  78.457  0.55 27.70  ?  4   ARG   C NH1 1 
ATOM   7426  N NH2 A ARG   C 1 4   ? -21.622 -1.942  82.045  0.45 31.42  ?  4   ARG   C NH2 1 
ATOM   7427  N NH2 B ARG   C 1 4   ? -19.056 -2.430  80.073  0.55 28.64  ?  4   ARG   C NH2 1 
ATOM   7428  N N   . ILE   C 1 5   ? -17.143 5.866   80.178  1.00 30.04  ?  5   ILE   C N   1 
ATOM   7429  C CA  . ILE   C 1 5   ? -16.883 7.009   79.309  1.00 26.27  ?  5   ILE   C CA  1 
ATOM   7430  C C   . ILE   C 1 5   ? -16.617 6.474   77.907  1.00 28.38  ?  5   ILE   C C   1 
ATOM   7431  O O   . ILE   C 1 5   ? -15.807 5.556   77.735  1.00 28.68  ?  5   ILE   C O   1 
ATOM   7432  C CB  . ILE   C 1 5   ? -15.700 7.862   79.811  1.00 28.01  ?  5   ILE   C CB  1 
ATOM   7433  C CG1 . ILE   C 1 5   ? -16.050 8.558   81.128  1.00 31.54  ?  5   ILE   C CG1 1 
ATOM   7434  C CG2 . ILE   C 1 5   ? -15.316 8.916   78.780  1.00 28.16  ?  5   ILE   C CG2 1 
ATOM   7435  C CD1 . ILE   C 1 5   ? -15.716 7.760   82.375  1.00 33.76  ?  5   ILE   C CD1 1 
ATOM   7436  N N   . VAL   C 1 6   ? -17.287 7.064   76.912  1.00 24.99  ?  6   VAL   C N   1 
ATOM   7437  C CA  . VAL   C 1 6   ? -17.266 6.551   75.545  1.00 24.75  ?  6   VAL   C CA  1 
ATOM   7438  C C   . VAL   C 1 6   ? -15.929 6.858   74.877  1.00 26.40  ?  6   VAL   C C   1 
ATOM   7439  O O   . VAL   C 1 6   ? -15.254 7.850   75.195  1.00 25.03  ?  6   VAL   C O   1 
ATOM   7440  C CB  . VAL   C 1 6   ? -18.440 7.153   74.749  1.00 28.61  ?  6   VAL   C CB  1 
ATOM   7441  C CG1 . VAL   C 1 6   ? -18.215 8.643   74.480  1.00 26.53  ?  6   VAL   C CG1 1 
ATOM   7442  C CG2 . VAL   C 1 6   ? -18.676 6.391   73.446  1.00 25.04  ?  6   VAL   C CG2 1 
ATOM   7443  N N   . GLU   C 1 7   ? -15.530 5.980   73.958  1.00 24.05  ?  7   GLU   C N   1 
ATOM   7444  C CA  . GLU   C 1 7   ? -14.320 6.195   73.179  1.00 24.14  ?  7   GLU   C CA  1 
ATOM   7445  C C   . GLU   C 1 7   ? -14.448 7.469   72.349  1.00 21.61  ?  7   GLU   C C   1 
ATOM   7446  O O   . GLU   C 1 7   ? -15.470 7.663   71.674  1.00 22.89  ?  7   GLU   C O   1 
ATOM   7447  C CB  . GLU   C 1 7   ? -14.062 5.006   72.253  1.00 23.01  ?  7   GLU   C CB  1 
ATOM   7448  C CG  . GLU   C 1 7   ? -13.572 3.762   72.946  1.00 21.05  ?  7   GLU   C CG  1 
ATOM   7449  C CD  . GLU   C 1 7   ? -14.669 2.972   73.633  1.00 24.35  ?  7   GLU   C CD  1 
ATOM   7450  O OE1 . GLU   C 1 7   ? -15.868 3.278   73.446  1.00 24.42  ?  7   GLU   C OE1 1 
ATOM   7451  O OE2 . GLU   C 1 7   ? -14.325 2.020   74.364  1.00 26.97  ?  7   GLU   C OE2 1 
ATOM   7452  N N   . PRO   C 1 8   ? -13.446 8.360   72.371  1.00 22.84  ?  8   PRO   C N   1 
ATOM   7453  C CA  . PRO   C 1 8   ? -13.463 9.525   71.476  1.00 22.49  ?  8   PRO   C CA  1 
ATOM   7454  C C   . PRO   C 1 8   ? -12.861 9.181   70.122  1.00 26.23  ?  8   PRO   C C   1 
ATOM   7455  O O   . PRO   C 1 8   ? -12.122 9.971   69.523  1.00 26.95  ?  8   PRO   C O   1 
ATOM   7456  C CB  . PRO   C 1 8   ? -12.620 10.554  72.236  1.00 21.42  ?  8   PRO   C CB  1 
ATOM   7457  C CG  . PRO   C 1 8   ? -11.603 9.704   72.965  1.00 23.89  ?  8   PRO   C CG  1 
ATOM   7458  C CD  . PRO   C 1 8   ? -12.309 8.402   73.312  1.00 25.48  ?  8   PRO   C CD  1 
ATOM   7459  N N   . PHE   C 1 9   ? -13.169 7.975   69.650  1.00 21.81  ?  9   PHE   C N   1 
ATOM   7460  C CA  . PHE   C 1 9   ? -12.683 7.443   68.384  1.00 21.41  ?  9   PHE   C CA  1 
ATOM   7461  C C   . PHE   C 1 9   ? -13.561 6.248   68.046  1.00 20.86  ?  9   PHE   C C   1 
ATOM   7462  O O   . PHE   C 1 9   ? -14.396 5.826   68.848  1.00 20.24  ?  9   PHE   C O   1 
ATOM   7463  C CB  . PHE   C 1 9   ? -11.196 7.045   68.456  1.00 20.40  ?  9   PHE   C CB  1 
ATOM   7464  C CG  . PHE   C 1 9   ? -10.859 6.148   69.623  1.00 18.55  ?  9   PHE   C CG  1 
ATOM   7465  C CD1 . PHE   C 1 9   ? -11.119 4.787   69.570  1.00 19.56  ?  9   PHE   C CD1 1 
ATOM   7466  C CD2 . PHE   C 1 9   ? -10.286 6.663   70.765  1.00 20.50  ?  9   PHE   C CD2 1 
ATOM   7467  C CE1 . PHE   C 1 9   ? -10.826 3.960   70.642  1.00 18.80  ?  9   PHE   C CE1 1 
ATOM   7468  C CE2 . PHE   C 1 9   ? -9.984  5.838   71.842  1.00 20.67  ?  9   PHE   C CE2 1 
ATOM   7469  C CZ  . PHE   C 1 9   ? -10.257 4.489   71.779  1.00 18.94  ?  9   PHE   C CZ  1 
ATOM   7470  N N   . ARG   C 1 10  ? -13.370 5.702   66.852  1.00 18.99  ?  10  ARG   C N   1 
ATOM   7471  C CA  . ARG   C 1 10  ? -13.992 4.437   66.508  1.00 19.18  ?  10  ARG   C CA  1 
ATOM   7472  C C   . ARG   C 1 10  ? -12.912 3.491   66.014  1.00 18.48  ?  10  ARG   C C   1 
ATOM   7473  O O   . ARG   C 1 10  ? -11.766 3.884   65.780  1.00 17.84  ?  10  ARG   C O   1 
ATOM   7474  C CB  . ARG   C 1 10  ? -15.105 4.600   65.464  1.00 21.94  ?  10  ARG   C CB  1 
ATOM   7475  C CG  . ARG   C 1 10  ? -14.640 5.099   64.124  1.00 19.28  ?  10  ARG   C CG  1 
ATOM   7476  C CD  . ARG   C 1 10  ? -15.817 5.574   63.310  1.00 21.65  ?  10  ARG   C CD  1 
ATOM   7477  N NE  . ARG   C 1 10  ? -15.356 6.177   62.068  1.00 27.27  ?  10  ARG   C NE  1 
ATOM   7478  C CZ  . ARG   C 1 10  ? -16.030 7.089   61.381  1.00 32.08  ?  10  ARG   C CZ  1 
ATOM   7479  N NH1 . ARG   C 1 10  ? -17.205 7.536   61.794  1.00 29.28  ?  10  ARG   C NH1 1 
ATOM   7480  N NH2 . ARG   C 1 10  ? -15.509 7.566   60.251  1.00 31.49  ?  10  ARG   C NH2 1 
ATOM   7481  N N   . ILE   C 1 11  ? -13.283 2.228   65.884  1.00 18.68  ?  11  ILE   C N   1 
ATOM   7482  C CA  . ILE   C 1 11  ? -12.323 1.180   65.575  1.00 18.18  ?  11  ILE   C CA  1 
ATOM   7483  C C   . ILE   C 1 11  ? -12.123 1.132   64.070  1.00 17.75  ?  11  ILE   C C   1 
ATOM   7484  O O   . ILE   C 1 11  ? -13.088 1.144   63.301  1.00 18.10  ?  11  ILE   C O   1 
ATOM   7485  C CB  . ILE   C 1 11  ? -12.808 -0.167  66.132  1.00 18.72  ?  11  ILE   C CB  1 
ATOM   7486  C CG1 . ILE   C 1 11  ? -12.930 -0.073  67.657  1.00 19.19  ?  11  ILE   C CG1 1 
ATOM   7487  C CG2 . ILE   C 1 11  ? -11.880 -1.295  65.720  1.00 18.32  ?  11  ILE   C CG2 1 
ATOM   7488  C CD1 . ILE   C 1 11  ? -13.748 -1.153  68.288  1.00 19.98  ?  11  ILE   C CD1 1 
ATOM   7489  N N   . LYS   C 1 12  ? -10.870 1.120   63.639  1.00 17.05  ?  12  LYS   C N   1 
ATOM   7490  C CA  . LYS   C 1 12  ? -10.577 1.006   62.217  1.00 16.67  ?  12  LYS   C CA  1 
ATOM   7491  C C   . LYS   C 1 12  ? -9.967  -0.332  61.844  1.00 17.07  ?  12  LYS   C C   1 
ATOM   7492  O O   . LYS   C 1 12  ? -10.109 -0.760  60.696  1.00 19.03  ?  12  LYS   C O   1 
ATOM   7493  C CB  . LYS   C 1 12  ? -9.629  2.128   61.774  1.00 18.05  ?  12  LYS   C CB  1 
ATOM   7494  C CG  . LYS   C 1 12  ? -9.673  2.444   60.285  1.00 16.84  ?  12  LYS   C CG  1 
ATOM   7495  C CD  . LYS   C 1 12  ? -8.487  3.291   59.886  1.00 19.63  ?  12  LYS   C CD  1 
ATOM   7496  C CE  . LYS   C 1 12  ? -8.552  3.661   58.407  1.00 22.68  ?  12  LYS   C CE  1 
ATOM   7497  N NZ  . LYS   C 1 12  ? -9.330  4.910   58.178  1.00 23.99  ?  12  LYS   C NZ  1 
ATOM   7498  N N   . MET   C 1 13  ? -9.279  -0.993  62.778  1.00 16.40  ?  13  MET   C N   1 
ATOM   7499  C CA  . MET   C 1 13  ? -8.709  -2.309  62.533  1.00 16.33  ?  13  MET   C CA  1 
ATOM   7500  C C   . MET   C 1 13  ? -8.745  -3.109  63.826  1.00 16.77  ?  13  MET   C C   1 
ATOM   7501  O O   . MET   C 1 13  ? -8.510  -2.561  64.909  1.00 16.78  ?  13  MET   C O   1 
ATOM   7502  C CB  . MET   C 1 13  ? -7.276  -2.212  62.008  1.00 15.61  ?  13  MET   C CB  1 
ATOM   7503  C CG  . MET   C 1 13  ? -6.727  -3.531  61.492  1.00 15.58  ?  13  MET   C CG  1 
ATOM   7504  S SD  . MET   C 1 13  ? -5.112  -3.381  60.727  1.00 25.38  ?  13  MET   C SD  1 
ATOM   7505  C CE  . MET   C 1 13  ? -4.078  -3.013  62.124  1.00 24.29  ?  13  MET   C CE  1 
ATOM   7506  N N   . VAL   C 1 14  ? -9.050  -4.400  63.710  1.00 17.20  ?  14  VAL   C N   1 
ATOM   7507  C CA  . VAL   C 1 14  ? -9.206  -5.264  64.873  1.00 18.75  ?  14  VAL   C CA  1 
ATOM   7508  C C   . VAL   C 1 14  ? -8.132  -6.341  64.855  1.00 17.95  ?  14  VAL   C C   1 
ATOM   7509  O O   . VAL   C 1 14  ? -7.627  -6.742  63.803  1.00 17.44  ?  14  VAL   C O   1 
ATOM   7510  C CB  . VAL   C 1 14  ? -10.602 -5.919  64.948  1.00 18.67  ?  14  VAL   C CB  1 
ATOM   7511  C CG1 . VAL   C 1 14  ? -11.674 -4.870  65.161  1.00 18.92  ?  14  VAL   C CG1 1 
ATOM   7512  C CG2 . VAL   C 1 14  ? -10.875 -6.733  63.688  1.00 18.79  ?  14  VAL   C CG2 1 
ATOM   7513  N N   . GLU   C 1 15  ? -7.802  -6.819  66.047  1.00 18.56  ?  15  GLU   C N   1 
ATOM   7514  C CA  . GLU   C 1 15  ? -6.943  -7.975  66.240  1.00 19.60  ?  15  GLU   C CA  1 
ATOM   7515  C C   . GLU   C 1 15  ? -7.769  -8.997  67.004  1.00 21.98  ?  15  GLU   C C   1 
ATOM   7516  O O   . GLU   C 1 15  ? -8.326  -8.681  68.060  1.00 21.82  ?  15  GLU   C O   1 
ATOM   7517  C CB  . GLU   C 1 15  ? -5.678  -7.573  67.001  1.00 22.12  ?  15  GLU   C CB  1 
ATOM   7518  C CG  . GLU   C 1 15  ? -4.765  -8.689  67.440  1.00 27.41  ?  15  GLU   C CG  1 
ATOM   7519  C CD  . GLU   C 1 15  ? -3.570  -8.158  68.225  1.00 33.39  ?  15  GLU   C CD  1 
ATOM   7520  O OE1 . GLU   C 1 15  ? -3.703  -7.097  68.883  1.00 27.83  ?  15  GLU   C OE1 1 
ATOM   7521  O OE2 . GLU   C 1 15  ? -2.494  -8.793  68.177  1.00 36.99  ?  15  GLU   C OE2 1 
ATOM   7522  N N   . LYS   C 1 16  ? -7.882  -10.202 66.463  1.00 23.06  ?  16  LYS   C N   1 
ATOM   7523  C CA  . LYS   C 1 16  ? -8.753  -11.196 67.069  1.00 25.61  ?  16  LYS   C CA  1 
ATOM   7524  C C   . LYS   C 1 16  ? -8.042  -11.886 68.231  1.00 30.47  ?  16  LYS   C C   1 
ATOM   7525  O O   . LYS   C 1 16  ? -6.841  -12.157 68.165  1.00 37.97  ?  16  LYS   C O   1 
ATOM   7526  C CB  . LYS   C 1 16  ? -9.217  -12.190 66.000  1.00 35.12  ?  16  LYS   C CB  1 
ATOM   7527  C CG  . LYS   C 1 16  ? -9.999  -11.476 64.854  1.00 36.00  ?  16  LYS   C CG  1 
ATOM   7528  C CD  . LYS   C 1 16  ? -10.590 -12.421 63.802  1.00 29.63  ?  16  LYS   C CD  1 
ATOM   7529  C CE  . LYS   C 1 16  ? -9.504  -13.112 62.996  1.00 30.18  ?  16  LYS   C CE  1 
ATOM   7530  N NZ  . LYS   C 1 16  ? -8.696  -12.169 62.166  1.00 28.45  ?  16  LYS   C NZ  1 
ATOM   7531  N N   . ILE   C 1 17  ? -8.778  -12.104 69.327  1.00 30.81  ?  17  ILE   C N   1 
ATOM   7532  C CA  . ILE   C 1 17  ? -8.251  -12.733 70.533  1.00 29.08  ?  17  ILE   C CA  1 
ATOM   7533  C C   . ILE   C 1 17  ? -9.281  -13.730 71.044  1.00 31.41  ?  17  ILE   C C   1 
ATOM   7534  O O   . ILE   C 1 17  ? -10.474 -13.619 70.767  1.00 34.87  ?  17  ILE   C O   1 
ATOM   7535  C CB  . ILE   C 1 17  ? -7.906  -11.715 71.644  1.00 29.62  ?  17  ILE   C CB  1 
ATOM   7536  C CG1 . ILE   C 1 17  ? -9.169  -10.987 72.113  1.00 34.04  ?  17  ILE   C CG1 1 
ATOM   7537  C CG2 . ILE   C 1 17  ? -6.832  -10.735 71.170  1.00 31.89  ?  17  ILE   C CG2 1 
ATOM   7538  C CD1 . ILE   C 1 17  ? -8.990  -10.172 73.383  1.00 33.64  ?  17  ILE   C CD1 1 
ATOM   7539  N N   . ARG   C 1 18  ? -8.806  -14.711 71.809  1.00 36.18  ?  18  ARG   C N   1 
ATOM   7540  C CA  . ARG   C 1 18  ? -9.621  -15.856 72.187  1.00 40.59  ?  18  ARG   C CA  1 
ATOM   7541  C C   . ARG   C 1 18  ? -9.381  -16.205 73.647  1.00 43.04  ?  18  ARG   C C   1 
ATOM   7542  O O   . ARG   C 1 18  ? -8.333  -15.900 74.221  1.00 42.94  ?  18  ARG   C O   1 
ATOM   7543  C CB  . ARG   C 1 18  ? -9.308  -17.081 71.313  1.00 41.13  ?  18  ARG   C CB  1 
ATOM   7544  C CG  . ARG   C 1 18  ? -7.862  -17.544 71.430  1.00 46.44  ?  18  ARG   C CG  1 
ATOM   7545  C CD  . ARG   C 1 18  ? -7.559  -18.770 70.577  1.00 50.76  ?  18  ARG   C CD  1 
ATOM   7546  N NE  . ARG   C 1 18  ? -8.032  -20.006 71.191  1.00 52.99  ?  18  ARG   C NE  1 
ATOM   7547  C CZ  . ARG   C 1 18  ? -7.361  -20.694 72.106  1.00 50.31  ?  18  ARG   C CZ  1 
ATOM   7548  N NH1 . ARG   C 1 18  ? -6.187  -20.282 72.558  1.00 50.53  ?  18  ARG   C NH1 1 
ATOM   7549  N NH2 . ARG   C 1 18  ? -7.884  -21.821 72.585  1.00 49.03  ?  18  ARG   C NH2 1 
ATOM   7550  N N   . VAL   C 1 19  ? -10.367 -16.863 74.244  1.00 43.67  ?  19  VAL   C N   1 
ATOM   7551  C CA  . VAL   C 1 19  ? -10.218 -17.462 75.566  1.00 44.27  ?  19  VAL   C CA  1 
ATOM   7552  C C   . VAL   C 1 19  ? -9.821  -18.922 75.366  1.00 43.15  ?  19  VAL   C C   1 
ATOM   7553  O O   . VAL   C 1 19  ? -10.596 -19.683 74.766  1.00 47.02  ?  19  VAL   C O   1 
ATOM   7554  C CB  . VAL   C 1 19  ? -11.506 -17.354 76.390  1.00 38.18  ?  19  VAL   C CB  1 
ATOM   7555  C CG1 . VAL   C 1 19  ? -11.240 -17.751 77.837  1.00 40.50  ?  19  VAL   C CG1 1 
ATOM   7556  C CG2 . VAL   C 1 19  ? -12.071 -15.952 76.319  1.00 42.49  ?  19  VAL   C CG2 1 
ATOM   7557  N N   . PRO   C 1 20  ? -8.636  -19.339 75.801  1.00 43.12  ?  20  PRO   C N   1 
ATOM   7558  C CA  . PRO   C 1 20  ? -8.318  -20.770 75.764  1.00 46.31  ?  20  PRO   C CA  1 
ATOM   7559  C C   . PRO   C 1 20  ? -9.249  -21.540 76.689  1.00 50.13  ?  20  PRO   C C   1 
ATOM   7560  O O   . PRO   C 1 20  ? -9.650  -21.048 77.748  1.00 48.84  ?  20  PRO   C O   1 
ATOM   7561  C CB  . PRO   C 1 20  ? -6.863  -20.824 76.243  1.00 46.09  ?  20  PRO   C CB  1 
ATOM   7562  C CG  . PRO   C 1 20  ? -6.331  -19.438 76.003  1.00 41.58  ?  20  PRO   C CG  1 
ATOM   7563  C CD  . PRO   C 1 20  ? -7.489  -18.524 76.233  1.00 40.88  ?  20  PRO   C CD  1 
ATOM   7564  N N   . SER   C 1 21  ? -9.613  -22.752 76.273  1.00 50.13  ?  21  SER   C N   1 
ATOM   7565  C CA  . SER   C 1 21  ? -10.496 -23.566 77.097  1.00 55.64  ?  21  SER   C CA  1 
ATOM   7566  C C   . SER   C 1 21  ? -9.859  -23.815 78.462  1.00 49.55  ?  21  SER   C C   1 
ATOM   7567  O O   . SER   C 1 21  ? -8.639  -23.726 78.632  1.00 45.98  ?  21  SER   C O   1 
ATOM   7568  C CB  . SER   C 1 21  ? -10.813 -24.894 76.404  1.00 52.57  ?  21  SER   C CB  1 
ATOM   7569  O OG  . SER   C 1 21  ? -9.650  -25.689 76.237  1.00 54.02  ?  21  SER   C OG  1 
ATOM   7570  N N   . ARG   C 1 22  ? -10.709 -24.105 79.451  1.00 52.20  ?  22  ARG   C N   1 
ATOM   7571  C CA  . ARG   C 1 22  ? -10.204 -24.393 80.791  1.00 51.95  ?  22  ARG   C CA  1 
ATOM   7572  C C   . ARG   C 1 22  ? -9.119  -25.461 80.735  1.00 54.41  ?  22  ARG   C C   1 
ATOM   7573  O O   . ARG   C 1 22  ? -8.013  -25.271 81.259  1.00 50.02  ?  22  ARG   C O   1 
ATOM   7574  C CB  . ARG   C 1 22  ? -11.352 -24.823 81.710  1.00 52.42  ?  22  ARG   C CB  1 
ATOM   7575  C CG  . ARG   C 1 22  ? -10.948 -24.984 83.178  1.00 54.38  ?  22  ARG   C CG  1 
ATOM   7576  C CD  . ARG   C 1 22  ? -10.159 -23.767 83.654  1.00 60.03  ?  22  ARG   C CD  1 
ATOM   7577  N NE  . ARG   C 1 22  ? -9.690  -23.876 85.032  1.00 57.24  ?  22  ARG   C NE  1 
ATOM   7578  C CZ  . ARG   C 1 22  ? -10.325 -23.372 86.081  1.00 57.25  ?  22  ARG   C CZ  1 
ATOM   7579  N NH1 . ARG   C 1 22  ? -11.489 -22.754 85.954  1.00 52.98  ?  22  ARG   C NH1 1 
ATOM   7580  N NH2 . ARG   C 1 22  ? -9.774  -23.483 87.289  1.00 57.36  ?  22  ARG   C NH2 1 
ATOM   7581  N N   . GLU   C 1 23  ? -9.415  -26.581 80.063  1.00 60.79  ?  23  GLU   C N   1 
ATOM   7582  C CA  . GLU   C 1 23  ? -8.406  -27.607 79.816  1.00 59.79  ?  23  GLU   C CA  1 
ATOM   7583  C C   . GLU   C 1 23  ? -7.143  -27.009 79.215  1.00 57.92  ?  23  GLU   C C   1 
ATOM   7584  O O   . GLU   C 1 23  ? -6.030  -27.338 79.641  1.00 59.47  ?  23  GLU   C O   1 
ATOM   7585  C CB  . GLU   C 1 23  ? -8.979  -28.689 78.897  1.00 60.06  ?  23  GLU   C CB  1 
ATOM   7586  C CG  . GLU   C 1 23  ? -8.024  -29.840 78.578  1.00 61.01  ?  23  GLU   C CG  1 
ATOM   7587  C CD  . GLU   C 1 23  ? -8.666  -30.900 77.689  1.00 61.73  ?  23  GLU   C CD  1 
ATOM   7588  O OE1 . GLU   C 1 23  ? -9.898  -30.839 77.498  1.00 62.09  ?  23  GLU   C OE1 1 
ATOM   7589  O OE2 . GLU   C 1 23  ? -7.945  -31.789 77.180  1.00 62.20  ?  23  GLU   C OE2 1 
ATOM   7590  N N   . GLU   C 1 24  ? -7.296  -26.115 78.229  1.00 54.88  ?  24  GLU   C N   1 
ATOM   7591  C CA  . GLU   C 1 24  ? -6.134  -25.476 77.613  1.00 52.89  ?  24  GLU   C CA  1 
ATOM   7592  C C   . GLU   C 1 24  ? -5.438  -24.528 78.584  1.00 49.29  ?  24  GLU   C C   1 
ATOM   7593  O O   . GLU   C 1 24  ? -4.204  -24.514 78.666  1.00 42.01  ?  24  GLU   C O   1 
ATOM   7594  C CB  . GLU   C 1 24  ? -6.550  -24.732 76.340  1.00 55.98  ?  24  GLU   C CB  1 
ATOM   7595  C CG  . GLU   C 1 24  ? -6.645  -25.610 75.087  1.00 53.84  ?  24  GLU   C CG  1 
ATOM   7596  C CD  . GLU   C 1 24  ? -7.196  -24.865 73.876  1.00 51.47  ?  24  GLU   C CD  1 
ATOM   7597  O OE1 . GLU   C 1 24  ? -7.841  -23.810 74.060  1.00 48.67  ?  24  GLU   C OE1 1 
ATOM   7598  O OE2 . GLU   C 1 24  ? -6.983  -25.335 72.737  1.00 49.93  ?  24  GLU   C OE2 1 
ATOM   7599  N N   . ARG   C 1 25  ? -6.211  -23.728 79.327  1.00 49.63  ?  25  ARG   C N   1 
ATOM   7600  C CA  . ARG   C 1 25  ? -5.611  -22.828 80.309  1.00 48.60  ?  25  ARG   C CA  1 
ATOM   7601  C C   . ARG   C 1 25  ? -4.911  -23.615 81.408  1.00 51.55  ?  25  ARG   C C   1 
ATOM   7602  O O   . ARG   C 1 25  ? -3.778  -23.295 81.789  1.00 48.10  ?  25  ARG   C O   1 
ATOM   7603  C CB  . ARG   C 1 25  ? -6.671  -21.898 80.903  1.00 46.95  ?  25  ARG   C CB  1 
ATOM   7604  C CG  . ARG   C 1 25  ? -7.318  -20.967 79.897  1.00 49.19  ?  25  ARG   C CG  1 
ATOM   7605  C CD  . ARG   C 1 25  ? -8.077  -19.821 80.563  1.00 44.38  ?  25  ARG   C CD  1 
ATOM   7606  N NE  . ARG   C 1 25  ? -9.155  -20.271 81.434  1.00 47.99  ?  25  ARG   C NE  1 
ATOM   7607  C CZ  . ARG   C 1 25  ? -10.365 -20.620 81.015  1.00 48.94  ?  25  ARG   C CZ  1 
ATOM   7608  N NH1 . ARG   C 1 25  ? -10.678 -20.623 79.729  1.00 41.56  ?  25  ARG   C NH1 1 
ATOM   7609  N NH2 . ARG   C 1 25  ? -11.284 -20.979 81.910  1.00 50.01  ?  25  ARG   C NH2 1 
ATOM   7610  N N   . GLU   C 1 26  ? -5.578  -24.650 81.932  1.00 49.40  ?  26  GLU   C N   1 
ATOM   7611  C CA  . GLU   C 1 26  ? -4.941  -25.540 82.897  1.00 51.41  ?  26  GLU   C CA  1 
ATOM   7612  C C   . GLU   C 1 26  ? -3.646  -26.116 82.337  1.00 49.74  ?  26  GLU   C C   1 
ATOM   7613  O O   . GLU   C 1 26  ? -2.603  -26.091 83.002  1.00 48.34  ?  26  GLU   C O   1 
ATOM   7614  C CB  . GLU   C 1 26  ? -5.898  -26.668 83.290  1.00 53.81  ?  26  GLU   C CB  1 
ATOM   7615  C CG  . GLU   C 1 26  ? -7.076  -26.250 84.160  1.00 54.98  ?  26  GLU   C CG  1 
ATOM   7616  C CD  . GLU   C 1 26  ? -8.059  -27.391 84.396  1.00 57.07  ?  26  GLU   C CD  1 
ATOM   7617  O OE1 . GLU   C 1 26  ? -7.829  -28.500 83.866  1.00 52.88  ?  26  GLU   C OE1 1 
ATOM   7618  O OE2 . GLU   C 1 26  ? -9.065  -27.178 85.108  1.00 56.87  ?  26  GLU   C OE2 1 
ATOM   7619  N N   . ALA   C 1 27  ? -3.693  -26.630 81.105  1.00 44.85  ?  27  ALA   C N   1 
ATOM   7620  C CA  . ALA   C 1 27  ? -2.509  -27.246 80.518  1.00 47.77  ?  27  ALA   C CA  1 
ATOM   7621  C C   . ALA   C 1 27  ? -1.419  -26.214 80.248  1.00 51.34  ?  27  ALA   C C   1 
ATOM   7622  O O   . ALA   C 1 27  ? -0.229  -26.495 80.442  1.00 48.02  ?  27  ALA   C O   1 
ATOM   7623  C CB  . ALA   C 1 27  ? -2.886  -27.984 79.234  1.00 44.69  ?  27  ALA   C CB  1 
ATOM   7624  N N   . ALA   C 1 28  ? -1.808  -25.011 79.813  1.00 46.89  ?  28  ALA   C N   1 
ATOM   7625  C CA  . ALA   C 1 28  ? -0.824  -23.984 79.484  1.00 48.04  ?  28  ALA   C CA  1 
ATOM   7626  C C   . ALA   C 1 28  ? -0.112  -23.479 80.731  1.00 44.48  ?  28  ALA   C C   1 
ATOM   7627  O O   . ALA   C 1 28  ? 1.116   -23.347 80.747  1.00 44.38  ?  28  ALA   C O   1 
ATOM   7628  C CB  . ALA   C 1 28  ? -1.498  -22.826 78.750  1.00 45.78  ?  28  ALA   C CB  1 
ATOM   7629  N N   . LEU   C 1 29  ? -0.870  -23.172 81.783  1.00 45.41  ?  29  LEU   C N   1 
ATOM   7630  C CA  . LEU   C 1 29  ? -0.250  -22.678 83.005  1.00 44.49  ?  29  LEU   C CA  1 
ATOM   7631  C C   . LEU   C 1 29  ? 0.709   -23.707 83.587  1.00 51.30  ?  29  LEU   C C   1 
ATOM   7632  O O   . LEU   C 1 29  ? 1.777   -23.351 84.102  1.00 50.12  ?  29  LEU   C O   1 
ATOM   7633  C CB  . LEU   C 1 29  ? -1.325  -22.308 84.022  1.00 45.77  ?  29  LEU   C CB  1 
ATOM   7634  C CG  . LEU   C 1 29  ? -0.756  -21.701 85.302  1.00 49.88  ?  29  LEU   C CG  1 
ATOM   7635  C CD1 . LEU   C 1 29  ? 0.052   -20.444 84.979  1.00 47.75  ?  29  LEU   C CD1 1 
ATOM   7636  C CD2 . LEU   C 1 29  ? -1.871  -21.409 86.301  1.00 51.43  ?  29  LEU   C CD2 1 
ATOM   7637  N N   . LYS   C 1 30  ? 0.345   -24.990 83.510  1.00 47.59  ?  30  LYS   C N   1 
ATOM   7638  C CA  . LYS   C 1 30  ? 1.236   -26.046 83.981  1.00 49.06  ?  30  LYS   C CA  1 
ATOM   7639  C C   . LYS   C 1 30  ? 2.485   -26.144 83.110  1.00 48.26  ?  30  LYS   C C   1 
ATOM   7640  O O   . LYS   C 1 30  ? 3.586   -26.390 83.619  1.00 46.04  ?  30  LYS   C O   1 
ATOM   7641  C CB  . LYS   C 1 30  ? 0.480   -27.374 84.025  1.00 49.17  ?  30  LYS   C CB  1 
ATOM   7642  C CG  . LYS   C 1 30  ? -0.614  -27.390 85.085  1.00 62.98  ?  30  LYS   C CG  1 
ATOM   7643  C CD  . LYS   C 1 30  ? -1.645  -28.499 84.882  1.00 70.96  ?  30  LYS   C CD  1 
ATOM   7644  C CE  . LYS   C 1 30  ? -2.790  -28.361 85.896  1.00 66.81  ?  30  LYS   C CE  1 
ATOM   7645  N NZ  . LYS   C 1 30  ? -3.834  -29.427 85.784  1.00 62.13  ?  30  LYS   C NZ  1 
ATOM   7646  N N   . GLU   C 1 31  ? 2.337   -25.947 81.797  1.00 46.21  ?  31  GLU   C N   1 
ATOM   7647  C CA  . GLU   C 1 31  ? 3.505   -25.880 80.923  1.00 50.75  ?  31  GLU   C CA  1 
ATOM   7648  C C   . GLU   C 1 31  ? 4.393   -24.692 81.285  1.00 54.50  ?  31  GLU   C C   1 
ATOM   7649  O O   . GLU   C 1 31  ? 5.626   -24.773 81.200  1.00 49.35  ?  31  GLU   C O   1 
ATOM   7650  C CB  . GLU   C 1 31  ? 3.054   -25.798 79.460  1.00 46.93  ?  31  GLU   C CB  1 
ATOM   7651  C CG  . GLU   C 1 31  ? 4.146   -25.399 78.468  1.00 48.92  ?  31  GLU   C CG  1 
ATOM   7652  C CD  . GLU   C 1 31  ? 5.312   -26.373 78.450  1.00 67.34  ?  31  GLU   C CD  1 
ATOM   7653  O OE1 . GLU   C 1 31  ? 5.068   -27.601 78.423  1.00 68.99  ?  31  GLU   C OE1 1 
ATOM   7654  O OE2 . GLU   C 1 31  ? 6.475   -25.911 78.473  1.00 70.22  ?  31  GLU   C OE2 1 
ATOM   7655  N N   . ALA   C 1 32  ? 3.782   -23.583 81.701  1.00 52.35  ?  32  ALA   C N   1 
ATOM   7656  C CA  . ALA   C 1 32  ? 4.509   -22.375 82.062  1.00 52.50  ?  32  ALA   C CA  1 
ATOM   7657  C C   . ALA   C 1 32  ? 5.130   -22.446 83.450  1.00 52.37  ?  32  ALA   C C   1 
ATOM   7658  O O   . ALA   C 1 32  ? 5.829   -21.505 83.847  1.00 54.23  ?  32  ALA   C O   1 
ATOM   7659  C CB  . ALA   C 1 32  ? 3.577   -21.161 81.978  1.00 48.10  ?  32  ALA   C CB  1 
ATOM   7660  N N   . GLY   C 1 33  ? 4.900   -23.524 84.193  1.00 46.85  ?  33  GLY   C N   1 
ATOM   7661  C CA  . GLY   C 1 33  ? 5.403   -23.593 85.548  1.00 52.77  ?  33  GLY   C CA  1 
ATOM   7662  C C   . GLY   C 1 33  ? 4.753   -22.612 86.498  1.00 60.09  ?  33  GLY   C C   1 
ATOM   7663  O O   . GLY   C 1 33  ? 5.397   -22.170 87.454  1.00 58.92  ?  33  GLY   C O   1 
ATOM   7664  N N   . TYR   C 1 34  ? 3.493   -22.247 86.249  1.00 54.78  ?  34  TYR   C N   1 
ATOM   7665  C CA  . TYR   C 1 34  ? 2.726   -21.372 87.141  1.00 53.54  ?  34  TYR   C CA  1 
ATOM   7666  C C   . TYR   C 1 34  ? 3.373   -19.992 87.278  1.00 53.76  ?  34  TYR   C C   1 
ATOM   7667  O O   . TYR   C 1 34  ? 3.355   -19.377 88.347  1.00 55.44  ?  34  TYR   C O   1 
ATOM   7668  C CB  . TYR   C 1 34  ? 2.517   -22.030 88.510  1.00 51.67  ?  34  TYR   C CB  1 
ATOM   7669  C CG  . TYR   C 1 34  ? 1.714   -23.314 88.429  1.00 59.08  ?  34  TYR   C CG  1 
ATOM   7670  C CD1 . TYR   C 1 34  ? 0.320   -23.285 88.374  1.00 54.97  ?  34  TYR   C CD1 1 
ATOM   7671  C CD2 . TYR   C 1 34  ? 2.344   -24.556 88.391  1.00 59.68  ?  34  TYR   C CD2 1 
ATOM   7672  C CE1 . TYR   C 1 34  ? -0.423  -24.452 88.289  1.00 48.66  ?  34  TYR   C CE1 1 
ATOM   7673  C CE2 . TYR   C 1 34  ? 1.605   -25.733 88.307  1.00 57.12  ?  34  TYR   C CE2 1 
ATOM   7674  C CZ  . TYR   C 1 34  ? 0.223   -25.671 88.259  1.00 57.46  ?  34  TYR   C CZ  1 
ATOM   7675  O OH  . TYR   C 1 34  ? -0.516  -26.827 88.178  1.00 62.33  ?  34  TYR   C OH  1 
ATOM   7676  N N   . ASN   C 1 35  ? 3.942   -19.497 86.184  1.00 52.24  ?  35  ASN   C N   1 
ATOM   7677  C CA  . ASN   C 1 35  ? 4.486   -18.139 86.121  1.00 55.55  ?  35  ASN   C CA  1 
ATOM   7678  C C   . ASN   C 1 35  ? 4.020   -17.479 84.826  1.00 57.21  ?  35  ASN   C C   1 
ATOM   7679  O O   . ASN   C 1 35  ? 4.551   -17.806 83.743  1.00 45.94  ?  35  ASN   C O   1 
ATOM   7680  C CB  . ASN   C 1 35  ? 6.009   -18.149 86.223  1.00 49.09  ?  35  ASN   C CB  1 
ATOM   7681  C CG  . ASN   C 1 35  ? 6.610   -16.758 86.141  1.00 45.28  ?  35  ASN   C CG  1 
ATOM   7682  O OD1 . ASN   C 1 35  ? 5.898   -15.755 86.168  1.00 47.25  ?  35  ASN   C OD1 1 
ATOM   7683  N ND2 . ASN   C 1 35  ? 7.931   -16.693 86.046  1.00 42.12  ?  35  ASN   C ND2 1 
ATOM   7684  N N   . PRO   C 1 36  ? 3.063   -16.544 84.892  1.00 52.94  ?  36  PRO   C N   1 
ATOM   7685  C CA  . PRO   C 1 36  ? 2.486   -15.970 83.661  1.00 47.15  ?  36  PRO   C CA  1 
ATOM   7686  C C   . PRO   C 1 36  ? 3.471   -15.221 82.775  1.00 44.45  ?  36  PRO   C C   1 
ATOM   7687  O O   . PRO   C 1 36  ? 3.149   -14.977 81.605  1.00 42.10  ?  36  PRO   C O   1 
ATOM   7688  C CB  . PRO   C 1 36  ? 1.400   -15.027 84.197  1.00 45.97  ?  36  PRO   C CB  1 
ATOM   7689  C CG  . PRO   C 1 36  ? 1.052   -15.589 85.550  1.00 46.21  ?  36  PRO   C CG  1 
ATOM   7690  C CD  . PRO   C 1 36  ? 2.341   -16.107 86.099  1.00 46.77  ?  36  PRO   C CD  1 
ATOM   7691  N N   . PHE   C 1 37  ? 4.644   -14.829 83.283  1.00 46.26  ?  37  PHE   C N   1 
ATOM   7692  C CA  . PHE   C 1 37  ? 5.640   -14.187 82.427  1.00 43.25  ?  37  PHE   C CA  1 
ATOM   7693  C C   . PHE   C 1 37  ? 6.254   -15.161 81.427  1.00 38.45  ?  37  PHE   C C   1 
ATOM   7694  O O   . PHE   C 1 37  ? 6.838   -14.722 80.434  1.00 37.18  ?  37  PHE   C O   1 
ATOM   7695  C CB  . PHE   C 1 37  ? 6.749   -13.557 83.271  1.00 42.71  ?  37  PHE   C CB  1 
ATOM   7696  C CG  . PHE   C 1 37  ? 6.853   -12.071 83.128  1.00 31.24  ?  37  PHE   C CG  1 
ATOM   7697  C CD1 . PHE   C 1 37  ? 7.186   -11.500 81.917  1.00 32.04  ?  37  PHE   C CD1 1 
ATOM   7698  C CD2 . PHE   C 1 37  ? 6.641   -11.244 84.216  1.00 36.82  ?  37  PHE   C CD2 1 
ATOM   7699  C CE1 . PHE   C 1 37  ? 7.288   -10.127 81.784  1.00 29.47  ?  37  PHE   C CE1 1 
ATOM   7700  C CE2 . PHE   C 1 37  ? 6.743   -9.870  84.090  1.00 36.74  ?  37  PHE   C CE2 1 
ATOM   7701  C CZ  . PHE   C 1 37  ? 7.059   -9.312  82.871  1.00 29.29  ?  37  PHE   C CZ  1 
ATOM   7702  N N   . LEU   C 1 38  ? 6.144   -16.464 81.684  1.00 45.68  ?  38  LEU   C N   1 
ATOM   7703  C CA  . LEU   C 1 38  ? 6.580   -17.528 80.787  1.00 43.22  ?  38  LEU   C CA  1 
ATOM   7704  C C   . LEU   C 1 38  ? 5.478   -17.994 79.855  1.00 35.18  ?  38  LEU   C C   1 
ATOM   7705  O O   . LEU   C 1 38  ? 5.724   -18.859 79.007  1.00 32.39  ?  38  LEU   C O   1 
ATOM   7706  C CB  . LEU   C 1 38  ? 7.079   -18.735 81.591  1.00 43.64  ?  38  LEU   C CB  1 
ATOM   7707  C CG  . LEU   C 1 38  ? 8.430   -18.625 82.285  1.00 45.67  ?  38  LEU   C CG  1 
ATOM   7708  C CD1 . LEU   C 1 38  ? 8.761   -19.939 82.980  1.00 44.67  ?  38  LEU   C CD1 1 
ATOM   7709  C CD2 . LEU   C 1 38  ? 9.511   -18.222 81.281  1.00 38.12  ?  38  LEU   C CD2 1 
ATOM   7710  N N   . LEU   C 1 39  ? 4.270   -17.481 80.020  1.00 31.39  ?  39  LEU   C N   1 
ATOM   7711  C CA  . LEU   C 1 39  ? 3.193   -17.858 79.130  1.00 34.67  ?  39  LEU   C CA  1 
ATOM   7712  C C   . LEU   C 1 39  ? 3.436   -17.254 77.752  1.00 32.31  ?  39  LEU   C C   1 
ATOM   7713  O O   . LEU   C 1 39  ? 3.861   -16.098 77.643  1.00 26.00  ?  39  LEU   C O   1 
ATOM   7714  C CB  . LEU   C 1 39  ? 1.846   -17.382 79.674  1.00 35.32  ?  39  LEU   C CB  1 
ATOM   7715  C CG  . LEU   C 1 39  ? 1.133   -18.233 80.721  1.00 37.20  ?  39  LEU   C CG  1 
ATOM   7716  C CD1 . LEU   C 1 39  ? -0.128  -17.537 81.144  1.00 38.53  ?  39  LEU   C CD1 1 
ATOM   7717  C CD2 . LEU   C 1 39  ? 0.811   -19.610 80.160  1.00 42.11  ?  39  LEU   C CD2 1 
ATOM   7718  N N   . PRO   C 1 40  ? 3.215   -18.015 76.686  1.00 32.62  ?  40  PRO   C N   1 
ATOM   7719  C CA  . PRO   C 1 40  ? 3.133   -17.405 75.360  1.00 27.13  ?  40  PRO   C CA  1 
ATOM   7720  C C   . PRO   C 1 40  ? 1.847   -16.602 75.246  1.00 28.60  ?  40  PRO   C C   1 
ATOM   7721  O O   . PRO   C 1 40  ? 0.858   -16.857 75.938  1.00 25.02  ?  40  PRO   C O   1 
ATOM   7722  C CB  . PRO   C 1 40  ? 3.129   -18.610 74.417  1.00 26.42  ?  40  PRO   C CB  1 
ATOM   7723  C CG  . PRO   C 1 40  ? 2.498   -19.699 75.235  1.00 26.05  ?  40  PRO   C CG  1 
ATOM   7724  C CD  . PRO   C 1 40  ? 2.981   -19.469 76.645  1.00 28.12  ?  40  PRO   C CD  1 
ATOM   7725  N N   . SER   C 1 41  ? 1.867   -15.610 74.354  1.00 27.38  ?  41  SER   C N   1 
ATOM   7726  C CA  . SER   C 1 41  ? 0.665   -14.810 74.152  1.00 24.55  ?  41  SER   C CA  1 
ATOM   7727  C C   . SER   C 1 41  ? -0.503  -15.648 73.646  1.00 27.80  ?  41  SER   C C   1 
ATOM   7728  O O   . SER   C 1 41  ? -1.658  -15.248 73.818  1.00 28.67  ?  41  SER   C O   1 
ATOM   7729  C CB  . SER   C 1 41  ? 0.937   -13.676 73.175  1.00 21.01  ?  41  SER   C CB  1 
ATOM   7730  O OG  . SER   C 1 41  ? 1.061   -14.192 71.867  1.00 30.03  ?  41  SER   C OG  1 
ATOM   7731  N N   . SER   C 1 42  ? -0.232  -16.792 73.014  1.00 27.16  ?  42  SER   C N   1 
ATOM   7732  C CA  . SER   C 1 42  ? -1.311  -17.673 72.584  1.00 24.98  ?  42  SER   C CA  1 
ATOM   7733  C C   . SER   C 1 42  ? -2.095  -18.233 73.761  1.00 31.33  ?  42  SER   C C   1 
ATOM   7734  O O   . SER   C 1 42  ? -3.221  -18.707 73.574  1.00 35.83  ?  42  SER   C O   1 
ATOM   7735  C CB  . SER   C 1 42  ? -0.748  -18.814 71.738  1.00 31.32  ?  42  SER   C CB  1 
ATOM   7736  O OG  . SER   C 1 42  ? 0.052   -19.691 72.523  1.00 36.34  ?  42  SER   C OG  1 
ATOM   7737  N N   . ALA   C 1 43  ? -1.536  -18.179 74.967  1.00 29.86  ?  43  ALA   C N   1 
ATOM   7738  C CA  . ALA   C 1 43  ? -2.196  -18.690 76.157  1.00 29.73  ?  43  ALA   C CA  1 
ATOM   7739  C C   . ALA   C 1 43  ? -3.000  -17.628 76.897  1.00 35.08  ?  43  ALA   C C   1 
ATOM   7740  O O   . ALA   C 1 43  ? -3.636  -17.950 77.907  1.00 37.62  ?  43  ALA   C O   1 
ATOM   7741  C CB  . ALA   C 1 43  ? -1.162  -19.300 77.106  1.00 30.05  ?  43  ALA   C CB  1 
ATOM   7742  N N   . VAL   C 1 44  ? -3.005  -16.387 76.413  1.00 32.18  ?  44  VAL   C N   1 
ATOM   7743  C CA  . VAL   C 1 44  ? -3.585  -15.250 77.116  1.00 29.42  ?  44  VAL   C CA  1 
ATOM   7744  C C   . VAL   C 1 44  ? -4.764  -14.720 76.311  1.00 32.64  ?  44  VAL   C C   1 
ATOM   7745  O O   . VAL   C 1 44  ? -4.722  -14.693 75.076  1.00 26.23  ?  44  VAL   C O   1 
ATOM   7746  C CB  . VAL   C 1 44  ? -2.530  -14.143 77.341  1.00 30.86  ?  44  VAL   C CB  1 
ATOM   7747  C CG1 . VAL   C 1 44  ? -3.117  -12.967 78.111  1.00 31.27  ?  44  VAL   C CG1 1 
ATOM   7748  C CG2 . VAL   C 1 44  ? -1.296  -14.711 78.053  1.00 24.82  ?  44  VAL   C CG2 1 
ATOM   7749  N N   . TYR   C 1 45  ? -5.813  -14.294 77.020  1.00 35.27  ?  45  TYR   C N   1 
ATOM   7750  C CA  . TYR   C 1 45  ? -6.988  -13.683 76.404  1.00 33.89  ?  45  TYR   C CA  1 
ATOM   7751  C C   . TYR   C 1 45  ? -6.883  -12.161 76.452  1.00 27.07  ?  45  TYR   C C   1 
ATOM   7752  O O   . TYR   C 1 45  ? -6.614  -11.518 75.433  1.00 34.31  ?  45  TYR   C O   1 
ATOM   7753  C CB  . TYR   C 1 45  ? -8.267  -14.170 77.094  1.00 33.16  ?  45  TYR   C CB  1 
ATOM   7754  C CG  . TYR   C 1 45  ? -9.515  -13.416 76.686  1.00 33.76  ?  45  TYR   C CG  1 
ATOM   7755  C CD1 . TYR   C 1 45  ? -9.884  -13.325 75.357  1.00 35.89  ?  45  TYR   C CD1 1 
ATOM   7756  C CD2 . TYR   C 1 45  ? -10.327 -12.802 77.637  1.00 40.82  ?  45  TYR   C CD2 1 
ATOM   7757  C CE1 . TYR   C 1 45  ? -11.020 -12.636 74.975  1.00 43.71  ?  45  TYR   C CE1 1 
ATOM   7758  C CE2 . TYR   C 1 45  ? -11.477 -12.110 77.264  1.00 38.33  ?  45  TYR   C CE2 1 
ATOM   7759  C CZ  . TYR   C 1 45  ? -11.813 -12.028 75.928  1.00 38.55  ?  45  TYR   C CZ  1 
ATOM   7760  O OH  . TYR   C 1 45  ? -12.942 -11.342 75.525  1.00 40.03  ?  45  TYR   C OH  1 
ATOM   7761  N N   . ILE   C 1 46  ? -7.101  -11.574 77.621  1.00 29.04  ?  46  ILE   C N   1 
ATOM   7762  C CA  . ILE   C 1 46  ? -6.834  -10.158 77.852  1.00 25.45  ?  46  ILE   C CA  1 
ATOM   7763  C C   . ILE   C 1 46  ? -5.497  -10.067 78.567  1.00 25.65  ?  46  ILE   C C   1 
ATOM   7764  O O   . ILE   C 1 46  ? -5.318  -10.664 79.633  1.00 27.50  ?  46  ILE   C O   1 
ATOM   7765  C CB  . ILE   C 1 46  ? -7.944  -9.494  78.681  1.00 28.70  ?  46  ILE   C CB  1 
ATOM   7766  C CG1 . ILE   C 1 46  ? -9.272  -9.508  77.926  1.00 24.99  ?  46  ILE   C CG1 1 
ATOM   7767  C CG2 . ILE   C 1 46  ? -7.556  -8.062  79.031  1.00 23.92  ?  46  ILE   C CG2 1 
ATOM   7768  C CD1 . ILE   C 1 46  ? -10.430 -8.953  78.737  1.00 27.83  ?  46  ILE   C CD1 1 
ATOM   7769  N N   . ASP   C 1 47  ? -4.559  -9.333  77.989  1.00 22.76  ?  47  ASP   C N   1 
ATOM   7770  C CA  . ASP   C 1 47  ? -3.211  -9.240  78.530  1.00 23.27  ?  47  ASP   C CA  1 
ATOM   7771  C C   . ASP   C 1 47  ? -3.078  -7.915  79.267  1.00 24.74  ?  47  ASP   C C   1 
ATOM   7772  O O   . ASP   C 1 47  ? -3.103  -6.844  78.647  1.00 24.02  ?  47  ASP   C O   1 
ATOM   7773  C CB  . ASP   C 1 47  ? -2.163  -9.366  77.430  1.00 21.96  ?  47  ASP   C CB  1 
ATOM   7774  C CG  . ASP   C 1 47  ? -0.839  -9.900  77.952  1.00 26.94  ?  47  ASP   C CG  1 
ATOM   7775  O OD1 . ASP   C 1 47  ? -0.612  -9.825  79.176  1.00 25.48  ?  47  ASP   C OD1 1 
ATOM   7776  O OD2 . ASP   C 1 47  ? -0.031  -10.399 77.143  1.00 24.17  ?  47  ASP   C OD2 1 
ATOM   7777  N N   . LEU   C 1 48  ? -2.935  -7.996  80.590  1.00 23.11  ?  48  LEU   C N   1 
ATOM   7778  C CA  . LEU   C 1 48  ? -2.732  -6.834  81.445  1.00 23.64  ?  48  LEU   C CA  1 
ATOM   7779  C C   . LEU   C 1 48  ? -1.346  -6.830  82.072  1.00 26.42  ?  48  LEU   C C   1 
ATOM   7780  O O   . LEU   C 1 48  ? -1.134  -6.195  83.110  1.00 26.04  ?  48  LEU   C O   1 
ATOM   7781  C CB  . LEU   C 1 48  ? -3.800  -6.785  82.529  1.00 24.12  ?  48  LEU   C CB  1 
ATOM   7782  C CG  . LEU   C 1 48  ? -5.225  -6.924  82.019  1.00 24.35  ?  48  LEU   C CG  1 
ATOM   7783  C CD1 . LEU   C 1 48  ? -6.161  -6.950  83.197  1.00 25.49  ?  48  LEU   C CD1 1 
ATOM   7784  C CD2 . LEU   C 1 48  ? -5.565  -5.778  81.072  1.00 23.43  ?  48  LEU   C CD2 1 
ATOM   7785  N N   . LEU   C 1 49  ? -0.406  -7.543  81.462  1.00 22.71  ?  49  LEU   C N   1 
ATOM   7786  C CA  . LEU   C 1 49  ? 0.958   -7.568  81.966  1.00 24.83  ?  49  LEU   C CA  1 
ATOM   7787  C C   . LEU   C 1 49  ? 1.549   -6.167  82.033  1.00 22.43  ?  49  LEU   C C   1 
ATOM   7788  O O   . LEU   C 1 49  ? 2.194   -5.804  83.020  1.00 23.26  ?  49  LEU   C O   1 
ATOM   7789  C CB  . LEU   C 1 49  ? 1.805   -8.464  81.073  1.00 23.19  ?  49  LEU   C CB  1 
ATOM   7790  C CG  . LEU   C 1 49  ? 3.141   -8.925  81.625  1.00 27.17  ?  49  LEU   C CG  1 
ATOM   7791  C CD1 . LEU   C 1 49  ? 2.902   -9.799  82.833  1.00 29.48  ?  49  LEU   C CD1 1 
ATOM   7792  C CD2 . LEU   C 1 49  ? 3.880   -9.679  80.559  1.00 24.26  ?  49  LEU   C CD2 1 
ATOM   7793  N N   . THR   C 1 50  ? 1.318   -5.357  81.004  1.00 22.42  ?  50  THR   C N   1 
ATOM   7794  C CA  . THR   C 1 50  ? 1.965   -4.062  80.898  1.00 23.15  ?  50  THR   C CA  1 
ATOM   7795  C C   . THR   C 1 50  ? 1.106   -3.125  80.070  1.00 20.38  ?  50  THR   C C   1 
ATOM   7796  O O   . THR   C 1 50  ? 0.227   -3.557  79.319  1.00 25.06  ?  50  THR   C O   1 
ATOM   7797  C CB  . THR   C 1 50  ? 3.348   -4.170  80.251  1.00 19.86  ?  50  THR   C CB  1 
ATOM   7798  O OG1 . THR   C 1 50  ? 3.978   -2.890  80.294  1.00 29.75  ?  50  THR   C OG1 1 
ATOM   7799  C CG2 . THR   C 1 50  ? 3.213   -4.563  78.810  1.00 19.67  ?  50  THR   C CG2 1 
ATOM   7800  N N   . ASP   C 1 51  ? 1.381   -1.828  80.209  1.00 19.63  ?  51  ASP   C N   1 
ATOM   7801  C CA  . ASP   C 1 51  ? 0.859   -0.811  79.305  1.00 19.03  ?  51  ASP   C CA  1 
ATOM   7802  C C   . ASP   C 1 51  ? 1.931   -0.311  78.348  1.00 20.83  ?  51  ASP   C C   1 
ATOM   7803  O O   . ASP   C 1 51  ? 1.777   0.760   77.746  1.00 19.52  ?  51  ASP   C O   1 
ATOM   7804  C CB  . ASP   C 1 51  ? 0.277   0.362   80.091  1.00 20.11  ?  51  ASP   C CB  1 
ATOM   7805  C CG  . ASP   C 1 51  ? 1.346   1.166   80.814  1.00 21.57  ?  51  ASP   C CG  1 
ATOM   7806  O OD1 . ASP   C 1 51  ? 2.272   0.542   81.371  1.00 24.48  ?  51  ASP   C OD1 1 
ATOM   7807  O OD2 . ASP   C 1 51  ? 1.258   2.415   80.829  1.00 19.39  ?  51  ASP   C OD2 1 
ATOM   7808  N N   . SER   C 1 52  ? 3.002   -1.076  78.186  1.00 19.86  ?  52  SER   C N   1 
ATOM   7809  C CA  . SER   C 1 52  ? 4.195   -0.649  77.467  1.00 19.80  ?  52  SER   C CA  1 
ATOM   7810  C C   . SER   C 1 52  ? 4.253   -1.365  76.128  1.00 18.86  ?  52  SER   C C   1 
ATOM   7811  O O   . SER   C 1 52  ? 4.446   -2.586  76.080  1.00 19.05  ?  52  SER   C O   1 
ATOM   7812  C CB  . SER   C 1 52  ? 5.440   -0.952  78.294  1.00 19.55  ?  52  SER   C CB  1 
ATOM   7813  O OG  . SER   C 1 52  ? 6.615   -0.523  77.636  1.00 21.81  ?  52  SER   C OG  1 
ATOM   7814  N N   . GLY   C 1 53  ? 4.105   -0.606  75.045  1.00 16.11  ?  53  GLY   C N   1 
ATOM   7815  C CA  . GLY   C 1 53  ? 4.308   -1.138  73.720  1.00 15.74  ?  53  GLY   C CA  1 
ATOM   7816  C C   . GLY   C 1 53  ? 3.138   -1.883  73.123  1.00 16.47  ?  53  GLY   C C   1 
ATOM   7817  O O   . GLY   C 1 53  ? 3.227   -2.313  71.967  1.00 16.51  ?  53  GLY   C O   1 
ATOM   7818  N N   . THR   C 1 54  ? 2.056   -2.058  73.867  1.00 16.57  ?  54  THR   C N   1 
ATOM   7819  C CA  . THR   C 1 54  ? 0.878   -2.775  73.406  1.00 20.53  ?  54  THR   C CA  1 
ATOM   7820  C C   . THR   C 1 54  ? -0.244  -1.836  72.978  1.00 19.14  ?  54  THR   C C   1 
ATOM   7821  O O   . THR   C 1 54  ? -1.382  -2.285  72.797  1.00 19.74  ?  54  THR   C O   1 
ATOM   7822  C CB  . THR   C 1 54  ? 0.378   -3.707  74.506  1.00 17.63  ?  54  THR   C CB  1 
ATOM   7823  O OG1 . THR   C 1 54  ? 0.170   -2.952  75.710  1.00 18.84  ?  54  THR   C OG1 1 
ATOM   7824  C CG2 . THR   C 1 54  ? 1.386   -4.804  74.776  1.00 17.67  ?  54  THR   C CG2 1 
ATOM   7825  N N   . ASN   C 1 55  ? 0.052   -0.552  72.802  1.00 16.00  ?  55  ASN   C N   1 
ATOM   7826  C CA  . ASN   C 1 55  ? -0.978  0.425   72.503  1.00 17.10  ?  55  ASN   C CA  1 
ATOM   7827  C C   . ASN   C 1 55  ? -1.485  0.270   71.073  1.00 18.16  ?  55  ASN   C C   1 
ATOM   7828  O O   . ASN   C 1 55  ? -0.780  -0.215  70.183  1.00 19.40  ?  55  ASN   C O   1 
ATOM   7829  C CB  . ASN   C 1 55  ? -0.431  1.834   72.723  1.00 17.95  ?  55  ASN   C CB  1 
ATOM   7830  C CG  . ASN   C 1 55  ? 0.234   1.988   74.083  1.00 22.64  ?  55  ASN   C CG  1 
ATOM   7831  O OD1 . ASN   C 1 55  ? -0.448  2.101   75.100  1.00 24.44  ?  55  ASN   C OD1 1 
ATOM   7832  N ND2 . ASN   C 1 55  ? 1.569   1.973   74.110  1.00 17.55  ?  55  ASN   C ND2 1 
ATOM   7833  N N   . ALA   C 1 56  ? -2.732  0.687   70.859  1.00 16.91  ?  56  ALA   C N   1 
ATOM   7834  C CA  . ALA   C 1 56  ? -3.296  0.767   69.520  1.00 17.02  ?  56  ALA   C CA  1 
ATOM   7835  C C   . ALA   C 1 56  ? -2.992  2.138   68.922  1.00 17.00  ?  56  ALA   C C   1 
ATOM   7836  O O   . ALA   C 1 56  ? -3.306  3.170   69.528  1.00 19.21  ?  56  ALA   C O   1 
ATOM   7837  C CB  . ALA   C 1 56  ? -4.804  0.520   69.555  1.00 16.13  ?  56  ALA   C CB  1 
ATOM   7838  N N   . MET   C 1 57  ? -2.391  2.145   67.737  1.00 14.98  ?  57  MET   C N   1 
ATOM   7839  C CA  . MET   C 1 57  ? -2.043  3.376   67.043  1.00 14.88  ?  57  MET   C CA  1 
ATOM   7840  C C   . MET   C 1 57  ? -3.188  3.859   66.161  1.00 16.34  ?  57  MET   C C   1 
ATOM   7841  O O   . MET   C 1 57  ? -4.124  3.121   65.846  1.00 19.02  ?  57  MET   C O   1 
ATOM   7842  C CB  . MET   C 1 57  ? -0.787  3.179   66.195  1.00 15.94  ?  57  MET   C CB  1 
ATOM   7843  C CG  . MET   C 1 57  ? 0.481   2.974   67.004  1.00 15.05  ?  57  MET   C CG  1 
ATOM   7844  S SD  . MET   C 1 57  ? 1.959   3.247   66.004  1.00 21.59  ?  57  MET   C SD  1 
ATOM   7845  C CE  . MET   C 1 57  ? 1.882   1.835   64.908  1.00 17.24  ?  57  MET   C CE  1 
ATOM   7846  N N   . SER   C 1 58  ? -3.111  5.124   65.770  1.00 16.29  ?  58  SER   C N   1 
ATOM   7847  C CA  . SER   C 1 58  ? -4.124  5.702   64.906  1.00 14.53  ?  58  SER   C CA  1 
ATOM   7848  C C   . SER   C 1 58  ? -3.786  5.448   63.439  1.00 15.39  ?  58  SER   C C   1 
ATOM   7849  O O   . SER   C 1 58  ? -2.699  4.975   63.094  1.00 14.98  ?  58  SER   C O   1 
ATOM   7850  C CB  . SER   C 1 58  ? -4.255  7.201   65.160  1.00 15.11  ?  58  SER   C CB  1 
ATOM   7851  O OG  . SER   C 1 58  ? -3.092  7.889   64.729  1.00 16.24  ?  58  SER   C OG  1 
ATOM   7852  N N   . ASP   C 1 59  ? -4.746  5.769   62.565  1.00 17.27  ?  59  ASP   C N   1 
ATOM   7853  C CA  . ASP   C 1 59  ? -4.483  5.704   61.130  1.00 15.42  ?  59  ASP   C CA  1 
ATOM   7854  C C   . ASP   C 1 59  ? -3.388  6.689   60.740  1.00 16.53  ?  59  ASP   C C   1 
ATOM   7855  O O   . ASP   C 1 59  ? -2.538  6.385   59.894  1.00 14.52  ?  59  ASP   C O   1 
ATOM   7856  C CB  . ASP   C 1 59  ? -5.765  5.967   60.331  1.00 14.72  ?  59  ASP   C CB  1 
ATOM   7857  C CG  . ASP   C 1 59  ? -6.561  7.170   60.839  1.00 20.36  ?  59  ASP   C CG  1 
ATOM   7858  O OD1 . ASP   C 1 59  ? -6.277  7.687   61.943  1.00 21.58  ?  59  ASP   C OD1 1 
ATOM   7859  O OD2 . ASP   C 1 59  ? -7.501  7.588   60.127  1.00 22.29  ?  59  ASP   C OD2 1 
ATOM   7860  N N   . HIS   C 1 60  ? -3.380  7.867   61.370  1.00 18.31  ?  60  HIS   C N   1 
ATOM   7861  C CA  . HIS   C 1 60  ? -2.343  8.852   61.090  1.00 16.11  ?  60  HIS   C CA  1 
ATOM   7862  C C   . HIS   C 1 60  ? -0.977  8.334   61.491  1.00 16.10  ?  60  HIS   C C   1 
ATOM   7863  O O   . HIS   C 1 60  ? 0.022   8.613   60.819  1.00 18.37  ?  60  HIS   C O   1 
ATOM   7864  C CB  . HIS   C 1 60  ? -2.640  10.156  61.819  1.00 17.63  ?  60  HIS   C CB  1 
ATOM   7865  C CG  . HIS   C 1 60  ? -3.923  10.794  61.398  1.00 23.40  ?  60  HIS   C CG  1 
ATOM   7866  N ND1 . HIS   C 1 60  ? -4.150  11.222  60.111  1.00 24.18  ?  60  HIS   C ND1 1 
ATOM   7867  C CD2 . HIS   C 1 60  ? -5.051  11.069  62.092  1.00 25.14  ?  60  HIS   C CD2 1 
ATOM   7868  C CE1 . HIS   C 1 60  ? -5.366  11.731  60.028  1.00 21.31  ?  60  HIS   C CE1 1 
ATOM   7869  N NE2 . HIS   C 1 60  ? -5.930  11.654  61.219  1.00 21.95  ?  60  HIS   C NE2 1 
ATOM   7870  N N   . GLN   C 1 61  ? -0.905  7.596   62.597  1.00 16.53  ?  61  GLN   C N   1 
ATOM   7871  C CA  . GLN   C 1 61  ? 0.382   7.053   63.007  1.00 16.26  ?  61  GLN   C CA  1 
ATOM   7872  C C   . GLN   C 1 61  ? 0.887   6.045   61.989  1.00 14.38  ?  61  GLN   C C   1 
ATOM   7873  O O   . GLN   C 1 61  ? 2.056   6.090   61.596  1.00 16.18  ?  61  GLN   C O   1 
ATOM   7874  C CB  . GLN   C 1 61  ? 0.274   6.432   64.393  1.00 14.70  ?  61  GLN   C CB  1 
ATOM   7875  C CG  . GLN   C 1 61  ? 0.298   7.465   65.510  1.00 18.88  ?  61  GLN   C CG  1 
ATOM   7876  C CD  . GLN   C 1 61  ? 0.096   6.854   66.876  1.00 15.68  ?  61  GLN   C CD  1 
ATOM   7877  O OE1 . GLN   C 1 61  ? -0.960  6.307   67.170  1.00 17.74  ?  61  GLN   C OE1 1 
ATOM   7878  N NE2 . GLN   C 1 61  ? 1.116   6.934   67.715  1.00 17.65  ?  61  GLN   C NE2 1 
ATOM   7879  N N   . TRP   C 1 62  ? 0.007   5.154   61.524  1.00 16.36  ?  62  TRP   C N   1 
ATOM   7880  C CA  . TRP   C 1 62  ? 0.399   4.179   60.509  1.00 16.89  ?  62  TRP   C CA  1 
ATOM   7881  C C   . TRP   C 1 62  ? 0.756   4.856   59.194  1.00 16.02  ?  62  TRP   C C   1 
ATOM   7882  O O   . TRP   C 1 62  ? 1.704   4.444   58.519  1.00 16.69  ?  62  TRP   C O   1 
ATOM   7883  C CB  . TRP   C 1 62  ? -0.722  3.162   60.308  1.00 16.31  ?  62  TRP   C CB  1 
ATOM   7884  C CG  . TRP   C 1 62  ? -0.714  2.100   61.351  1.00 20.33  ?  62  TRP   C CG  1 
ATOM   7885  C CD1 . TRP   C 1 62  ? -1.448  2.069   62.506  1.00 21.22  ?  62  TRP   C CD1 1 
ATOM   7886  C CD2 . TRP   C 1 62  ? 0.096   0.918   61.358  1.00 23.80  ?  62  TRP   C CD2 1 
ATOM   7887  N NE1 . TRP   C 1 62  ? -1.153  0.931   63.222  1.00 21.69  ?  62  TRP   C NE1 1 
ATOM   7888  C CE2 . TRP   C 1 62  ? -0.209  0.209   62.539  1.00 25.57  ?  62  TRP   C CE2 1 
ATOM   7889  C CE3 . TRP   C 1 62  ? 1.050   0.390   60.480  1.00 27.62  ?  62  TRP   C CE3 1 
ATOM   7890  C CZ2 . TRP   C 1 62  ? 0.404   -1.003  62.860  1.00 29.01  ?  62  TRP   C CZ2 1 
ATOM   7891  C CZ3 . TRP   C 1 62  ? 1.658   -0.813  60.800  1.00 28.98  ?  62  TRP   C CZ3 1 
ATOM   7892  C CH2 . TRP   C 1 62  ? 1.333   -1.497  61.978  1.00 27.84  ?  62  TRP   C CH2 1 
ATOM   7893  N N   . ALA   C 1 63  ? 0.009   5.893   58.812  1.00 15.02  ?  63  ALA   C N   1 
ATOM   7894  C CA  . ALA   C 1 63  ? 0.357   6.647   57.612  1.00 16.59  ?  63  ALA   C CA  1 
ATOM   7895  C C   . ALA   C 1 63  ? 1.713   7.327   57.767  1.00 16.33  ?  63  ALA   C C   1 
ATOM   7896  O O   . ALA   C 1 63  ? 2.521   7.338   56.832  1.00 17.12  ?  63  ALA   C O   1 
ATOM   7897  C CB  . ALA   C 1 63  ? -0.729  7.678   57.310  1.00 13.79  ?  63  ALA   C CB  1 
ATOM   7898  N N   . ALA   C 1 64  ? 1.975   7.907   58.941  1.00 15.89  ?  64  ALA   C N   1 
ATOM   7899  C CA  . ALA   C 1 64  ? 3.277   8.516   59.193  1.00 15.18  ?  64  ALA   C CA  1 
ATOM   7900  C C   . ALA   C 1 64  ? 4.396   7.497   59.035  1.00 15.12  ?  64  ALA   C C   1 
ATOM   7901  O O   . ALA   C 1 64  ? 5.463   7.812   58.496  1.00 17.58  ?  64  ALA   C O   1 
ATOM   7902  C CB  . ALA   C 1 64  ? 3.305   9.135   60.594  1.00 14.77  ?  64  ALA   C CB  1 
ATOM   7903  N N   . MET   C 1 65  ? 4.166   6.263   59.484  1.00 14.86  ?  65  MET   C N   1 
ATOM   7904  C CA  . MET   C 1 65  ? 5.173   5.221   59.324  1.00 13.94  ?  65  MET   C CA  1 
ATOM   7905  C C   . MET   C 1 65  ? 5.418   4.900   57.858  1.00 14.08  ?  65  MET   C C   1 
ATOM   7906  O O   . MET   C 1 65  ? 6.558   4.645   57.453  1.00 14.21  ?  65  MET   C O   1 
ATOM   7907  C CB  . MET   C 1 65  ? 4.740   3.962   60.065  1.00 12.83  ?  65  MET   C CB  1 
ATOM   7908  C CG  . MET   C 1 65  ? 4.751   4.102   61.563  1.00 18.21  ?  65  MET   C CG  1 
ATOM   7909  S SD  . MET   C 1 65  ? 4.304   2.565   62.368  1.00 25.75  ?  65  MET   C SD  1 
ATOM   7910  C CE  . MET   C 1 65  ? 5.796   1.646   62.225  1.00 16.80  ?  65  MET   C CE  1 
ATOM   7911  N N   . ILE   C 1 66  ? 4.359   4.889   57.046  1.00 16.97  ?  66  ILE   C N   1 
ATOM   7912  C CA  . ILE   C 1 66  ? 4.500   4.456   55.658  1.00 14.31  ?  66  ILE   C CA  1 
ATOM   7913  C C   . ILE   C 1 66  ? 5.393   5.406   54.874  1.00 16.96  ?  66  ILE   C C   1 
ATOM   7914  O O   . ILE   C 1 66  ? 6.141   4.980   53.990  1.00 14.67  ?  66  ILE   C O   1 
ATOM   7915  C CB  . ILE   C 1 66  ? 3.107   4.309   55.026  1.00 15.56  ?  66  ILE   C CB  1 
ATOM   7916  C CG1 . ILE   C 1 66  ? 2.443   3.069   55.606  1.00 20.77  ?  66  ILE   C CG1 1 
ATOM   7917  C CG2 . ILE   C 1 66  ? 3.191   4.206   53.532  1.00 20.94  ?  66  ILE   C CG2 1 
ATOM   7918  C CD1 . ILE   C 1 66  ? 1.027   2.927   55.218  1.00 23.14  ?  66  ILE   C CD1 1 
ATOM   7919  N N   . THR   C 1 67  ? 5.362   6.696   55.194  1.00 17.17  ?  67  THR   C N   1 
ATOM   7920  C CA  . THR   C 1 67  ? 6.225   7.664   54.539  1.00 16.93  ?  67  THR   C CA  1 
ATOM   7921  C C   . THR   C 1 67  ? 7.468   7.974   55.368  1.00 19.14  ?  67  THR   C C   1 
ATOM   7922  O O   . THR   C 1 67  ? 8.132   8.989   55.127  1.00 18.99  ?  67  THR   C O   1 
ATOM   7923  C CB  . THR   C 1 67  ? 5.426   8.928   54.240  1.00 16.99  ?  67  THR   C CB  1 
ATOM   7924  O OG1 . THR   C 1 67  ? 4.767   9.351   55.436  1.00 20.64  ?  67  THR   C OG1 1 
ATOM   7925  C CG2 . THR   C 1 67  ? 4.366   8.637   53.183  1.00 17.89  ?  67  THR   C CG2 1 
ATOM   7926  N N   . GLY   C 1 68  ? 7.799   7.109   56.324  1.00 17.17  ?  68  GLY   C N   1 
ATOM   7927  C CA  . GLY   C 1 68  ? 8.951   7.356   57.173  1.00 14.65  ?  68  GLY   C CA  1 
ATOM   7928  C C   . GLY   C 1 68  ? 10.248  7.325   56.384  1.00 16.60  ?  68  GLY   C C   1 
ATOM   7929  O O   . GLY   C 1 68  ? 10.411  6.547   55.442  1.00 18.87  ?  68  GLY   C O   1 
ATOM   7930  N N   . ASP   C 1 69  ? 11.169  8.198   56.770  1.00 17.38  ?  69  ASP   C N   1 
ATOM   7931  C CA  . ASP   C 1 69  ? 12.457  8.360   56.102  1.00 18.47  ?  69  ASP   C CA  1 
ATOM   7932  C C   . ASP   C 1 69  ? 13.469  7.466   56.815  1.00 18.52  ?  69  ASP   C C   1 
ATOM   7933  O O   . ASP   C 1 69  ? 13.862  7.748   57.954  1.00 17.98  ?  69  ASP   C O   1 
ATOM   7934  C CB  . ASP   C 1 69  ? 12.858  9.837   56.133  1.00 19.64  ?  69  ASP   C CB  1 
ATOM   7935  C CG  . ASP   C 1 69  ? 14.201  10.116  55.473  1.00 24.75  ?  69  ASP   C CG  1 
ATOM   7936  O OD1 . ASP   C 1 69  ? 14.805  9.183   54.900  1.00 25.92  ?  69  ASP   C OD1 1 
ATOM   7937  O OD2 . ASP   C 1 69  ? 14.655  11.286  55.537  1.00 20.67  ?  69  ASP   C OD2 1 
ATOM   7938  N N   . GLU   C 1 70  ? 13.891  6.387   56.150  1.00 18.79  ?  70  GLU   C N   1 
ATOM   7939  C CA  . GLU   C 1 70  ? 14.767  5.384   56.750  1.00 17.80  ?  70  GLU   C CA  1 
ATOM   7940  C C   . GLU   C 1 70  ? 16.250  5.734   56.646  1.00 22.01  ?  70  GLU   C C   1 
ATOM   7941  O O   . GLU   C 1 70  ? 17.096  4.894   56.998  1.00 18.83  ?  70  GLU   C O   1 
ATOM   7942  C CB  . GLU   C 1 70  ? 14.511  4.012   56.119  1.00 17.06  ?  70  GLU   C CB  1 
ATOM   7943  C CG  . GLU   C 1 70  ? 13.155  3.389   56.462  1.00 18.99  ?  70  GLU   C CG  1 
ATOM   7944  C CD  . GLU   C 1 70  ? 12.918  3.227   57.970  1.00 19.49  ?  70  GLU   C CD  1 
ATOM   7945  O OE1 . GLU   C 1 70  ? 13.896  3.199   58.749  1.00 16.98  ?  70  GLU   C OE1 1 
ATOM   7946  O OE2 . GLU   C 1 70  ? 11.740  3.120   58.379  1.00 19.60  ?  70  GLU   C OE2 1 
ATOM   7947  N N   . ALA   C 1 71  ? 16.573  6.962   56.232  1.00 19.88  ?  71  ALA   C N   1 
ATOM   7948  C CA  . ALA   C 1 71  ? 17.958  7.377   56.023  1.00 21.94  ?  71  ALA   C CA  1 
ATOM   7949  C C   . ALA   C 1 71  ? 18.810  7.185   57.274  1.00 23.71  ?  71  ALA   C C   1 
ATOM   7950  O O   . ALA   C 1 71  ? 18.374  7.455   58.398  1.00 20.86  ?  71  ALA   C O   1 
ATOM   7951  C CB  . ALA   C 1 71  ? 18.004  8.842   55.590  1.00 21.14  ?  71  ALA   C CB  1 
ATOM   7952  N N   . TYR   C 1 72  ? 20.049  6.727   57.066  1.00 23.56  ?  72  TYR   C N   1 
ATOM   7953  C CA  . TYR   C 1 72  ? 20.936  6.467   58.194  1.00 23.14  ?  72  TYR   C CA  1 
ATOM   7954  C C   . TYR   C 1 72  ? 21.279  7.752   58.927  1.00 21.87  ?  72  TYR   C C   1 
ATOM   7955  O O   . TYR   C 1 72  ? 21.310  7.780   60.162  1.00 23.08  ?  72  TYR   C O   1 
ATOM   7956  C CB  . TYR   C 1 72  ? 22.223  5.782   57.726  1.00 22.37  ?  72  TYR   C CB  1 
ATOM   7957  C CG  . TYR   C 1 72  ? 23.007  5.203   58.884  1.00 22.22  ?  72  TYR   C CG  1 
ATOM   7958  C CD1 . TYR   C 1 72  ? 22.666  3.966   59.414  1.00 26.72  ?  72  TYR   C CD1 1 
ATOM   7959  C CD2 . TYR   C 1 72  ? 24.051  5.904   59.476  1.00 20.03  ?  72  TYR   C CD2 1 
ATOM   7960  C CE1 . TYR   C 1 72  ? 23.350  3.427   60.486  1.00 25.18  ?  72  TYR   C CE1 1 
ATOM   7961  C CE2 . TYR   C 1 72  ? 24.750  5.375   60.554  1.00 23.12  ?  72  TYR   C CE2 1 
ATOM   7962  C CZ  . TYR   C 1 72  ? 24.389  4.132   61.054  1.00 28.03  ?  72  TYR   C CZ  1 
ATOM   7963  O OH  . TYR   C 1 72  ? 25.056  3.575   62.118  1.00 32.43  ?  72  TYR   C OH  1 
ATOM   7964  N N   . ALA   C 1 73  ? 21.540  8.822   58.184  1.00 20.43  ?  73  ALA   C N   1 
ATOM   7965  C CA  . ALA   C 1 73  ? 21.924  10.100  58.754  1.00 23.17  ?  73  ALA   C CA  1 
ATOM   7966  C C   . ALA   C 1 73  ? 21.026  11.181  58.181  1.00 23.52  ?  73  ALA   C C   1 
ATOM   7967  O O   . ALA   C 1 73  ? 20.868  11.278  56.961  1.00 23.81  ?  73  ALA   C O   1 
ATOM   7968  C CB  . ALA   C 1 73  ? 23.390  10.417  58.459  1.00 23.66  ?  73  ALA   C CB  1 
ATOM   7969  N N   . GLY   C 1 74  ? 20.442  11.992  59.057  1.00 23.42  ?  74  GLY   C N   1 
ATOM   7970  C CA  . GLY   C 1 74  ? 19.688  13.142  58.603  1.00 25.16  ?  74  GLY   C CA  1 
ATOM   7971  C C   . GLY   C 1 74  ? 18.260  12.846  58.228  1.00 23.36  ?  74  GLY   C C   1 
ATOM   7972  O O   . GLY   C 1 74  ? 17.677  13.580  57.427  1.00 21.64  ?  74  GLY   C O   1 
ATOM   7973  N N   . SER   C 1 75  ? 17.680  11.782  58.780  1.00 24.29  ?  75  SER   C N   1 
ATOM   7974  C CA  . SER   C 1 75  ? 16.295  11.441  58.487  1.00 21.33  ?  75  SER   C CA  1 
ATOM   7975  C C   . SER   C 1 75  ? 15.386  12.638  58.706  1.00 20.94  ?  75  SER   C C   1 
ATOM   7976  O O   . SER   C 1 75  ? 15.507  13.364  59.697  1.00 23.33  ?  75  SER   C O   1 
ATOM   7977  C CB  . SER   C 1 75  ? 15.823  10.281  59.363  1.00 22.99  ?  75  SER   C CB  1 
ATOM   7978  O OG  . SER   C 1 75  ? 14.403  10.183  59.336  1.00 20.79  ?  75  SER   C OG  1 
ATOM   7979  N N   . ARG   C 1 76  ? 14.478  12.840  57.757  1.00 21.18  ?  76  ARG   C N   1 
ATOM   7980  C CA  A ARG   C 1 76  ? 13.498  13.916  57.854  0.43 23.44  ?  76  ARG   C CA  1 
ATOM   7981  C CA  B ARG   C 1 76  ? 13.526  13.938  57.874  0.57 23.45  ?  76  ARG   C CA  1 
ATOM   7982  C C   . ARG   C 1 76  ? 12.716  13.839  59.162  1.00 20.73  ?  76  ARG   C C   1 
ATOM   7983  O O   . ARG   C 1 76  ? 12.356  14.868  59.748  1.00 24.18  ?  76  ARG   C O   1 
ATOM   7984  C CB  A ARG   C 1 76  ? 12.569  13.839  56.636  0.43 22.24  ?  76  ARG   C CB  1 
ATOM   7985  C CB  B ARG   C 1 76  ? 12.610  13.963  56.645  0.57 22.21  ?  76  ARG   C CB  1 
ATOM   7986  C CG  A ARG   C 1 76  ? 11.353  14.738  56.650  0.43 25.07  ?  76  ARG   C CG  1 
ATOM   7987  C CG  B ARG   C 1 76  ? 11.126  13.881  56.955  0.57 24.01  ?  76  ARG   C CG  1 
ATOM   7988  C CD  A ARG   C 1 76  ? 10.578  14.621  55.325  0.43 26.20  ?  76  ARG   C CD  1 
ATOM   7989  C CD  B ARG   C 1 76  ? 10.289  13.878  55.679  0.57 26.16  ?  76  ARG   C CD  1 
ATOM   7990  N NE  A ARG   C 1 76  ? 10.075  13.273  55.066  0.43 26.43  ?  76  ARG   C NE  1 
ATOM   7991  N NE  B ARG   C 1 76  ? 10.561  12.711  54.849  0.57 27.32  ?  76  ARG   C NE  1 
ATOM   7992  C CZ  A ARG   C 1 76  ? 10.637  12.397  54.240  0.43 26.29  ?  76  ARG   C CZ  1 
ATOM   7993  C CZ  B ARG   C 1 76  ? 9.888   11.570  54.917  0.57 25.10  ?  76  ARG   C CZ  1 
ATOM   7994  N NH1 A ARG   C 1 76  ? 11.736  12.688  53.562  0.43 23.79  ?  76  ARG   C NH1 1 
ATOM   7995  N NH1 B ARG   C 1 76  ? 8.875   11.415  55.757  0.57 21.55  ?  76  ARG   C NH1 1 
ATOM   7996  N NH2 A ARG   C 1 76  ? 10.084  11.196  54.091  0.43 24.06  ?  76  ARG   C NH2 1 
ATOM   7997  N NH2 B ARG   C 1 76  ? 10.244  10.559  54.127  0.57 23.11  ?  76  ARG   C NH2 1 
ATOM   7998  N N   . ASN   C 1 77  ? 12.451  12.622  59.640  1.00 18.96  ?  77  ASN   C N   1 
ATOM   7999  C CA  . ASN   C 1 77  ? 11.665  12.446  60.856  1.00 21.60  ?  77  ASN   C CA  1 
ATOM   8000  C C   . ASN   C 1 77  ? 12.452  12.823  62.109  1.00 23.81  ?  77  ASN   C C   1 
ATOM   8001  O O   . ASN   C 1 77  ? 11.850  13.176  63.132  1.00 23.06  ?  77  ASN   C O   1 
ATOM   8002  C CB  . ASN   C 1 77  ? 11.168  11.001  60.934  1.00 20.65  ?  77  ASN   C CB  1 
ATOM   8003  C CG  . ASN   C 1 77  ? 10.457  10.561  59.659  1.00 18.59  ?  77  ASN   C CG  1 
ATOM   8004  O OD1 . ASN   C 1 77  ? 10.983  9.769   58.883  1.00 21.99  ?  77  ASN   C OD1 1 
ATOM   8005  N ND2 . ASN   C 1 77  ? 9.260   11.085  59.436  1.00 20.91  ?  77  ASN   C ND2 1 
ATOM   8006  N N   . TYR   C 1 78  ? 13.787  12.748  62.062  1.00 21.83  ?  78  TYR   C N   1 
ATOM   8007  C CA  . TYR   C 1 78  ? 14.583  13.238  63.181  1.00 21.34  ?  78  TYR   C CA  1 
ATOM   8008  C C   . TYR   C 1 78  ? 14.339  14.724  63.411  1.00 20.68  ?  78  TYR   C C   1 
ATOM   8009  O O   . TYR   C 1 78  ? 14.165  15.166  64.553  1.00 19.72  ?  78  TYR   C O   1 
ATOM   8010  C CB  . TYR   C 1 78  ? 16.071  12.977  62.940  1.00 22.66  ?  78  TYR   C CB  1 
ATOM   8011  C CG  . TYR   C 1 78  ? 16.966  13.768  63.872  1.00 23.10  ?  78  TYR   C CG  1 
ATOM   8012  C CD1 . TYR   C 1 78  ? 17.142  13.377  65.193  1.00 20.38  ?  78  TYR   C CD1 1 
ATOM   8013  C CD2 . TYR   C 1 78  ? 17.622  14.915  63.437  1.00 21.86  ?  78  TYR   C CD2 1 
ATOM   8014  C CE1 . TYR   C 1 78  ? 17.948  14.098  66.049  1.00 21.60  ?  78  TYR   C CE1 1 
ATOM   8015  C CE2 . TYR   C 1 78  ? 18.430  15.646  64.292  1.00 17.98  ?  78  TYR   C CE2 1 
ATOM   8016  C CZ  . TYR   C 1 78  ? 18.589  15.234  65.592  1.00 20.31  ?  78  TYR   C CZ  1 
ATOM   8017  O OH  . TYR   C 1 78  ? 19.396  15.951  66.455  1.00 25.51  ?  78  TYR   C OH  1 
ATOM   8018  N N   . TYR   C 1 79  ? 14.312  15.508  62.336  1.00 19.70  ?  79  TYR   C N   1 
ATOM   8019  C CA  . TYR   C 1 79  ? 14.092  16.943  62.480  1.00 24.11  ?  79  TYR   C CA  1 
ATOM   8020  C C   . TYR   C 1 79  ? 12.677  17.243  62.957  1.00 23.32  ?  79  TYR   C C   1 
ATOM   8021  O O   . TYR   C 1 79  ? 12.470  18.171  63.748  1.00 25.51  ?  79  TYR   C O   1 
ATOM   8022  C CB  . TYR   C 1 79  ? 14.392  17.643  61.156  1.00 20.50  ?  79  TYR   C CB  1 
ATOM   8023  C CG  . TYR   C 1 79  ? 15.825  17.442  60.733  1.00 22.52  ?  79  TYR   C CG  1 
ATOM   8024  C CD1 . TYR   C 1 79  ? 16.849  18.118  61.370  1.00 21.99  ?  79  TYR   C CD1 1 
ATOM   8025  C CD2 . TYR   C 1 79  ? 16.156  16.551  59.724  1.00 24.00  ?  79  TYR   C CD2 1 
ATOM   8026  C CE1 . TYR   C 1 79  ? 18.167  17.927  61.008  1.00 27.35  ?  79  TYR   C CE1 1 
ATOM   8027  C CE2 . TYR   C 1 79  ? 17.474  16.353  59.348  1.00 27.16  ?  79  TYR   C CE2 1 
ATOM   8028  C CZ  . TYR   C 1 79  ? 18.476  17.044  59.998  1.00 32.58  ?  79  TYR   C CZ  1 
ATOM   8029  O OH  . TYR   C 1 79  ? 19.792  16.861  59.643  1.00 38.67  ?  79  TYR   C OH  1 
ATOM   8030  N N   . ASP   C 1 80  ? 11.689  16.468  62.496  1.00 25.42  ?  80  ASP   C N   1 
ATOM   8031  C CA  . ASP   C 1 80  ? 10.327  16.630  63.002  1.00 21.56  ?  80  ASP   C CA  1 
ATOM   8032  C C   . ASP   C 1 80  ? 10.252  16.307  64.485  1.00 23.85  ?  80  ASP   C C   1 
ATOM   8033  O O   . ASP   C 1 80  ? 9.535   16.976  65.239  1.00 23.88  ?  80  ASP   C O   1 
ATOM   8034  C CB  . ASP   C 1 80  ? 9.357   15.734  62.237  1.00 22.24  ?  80  ASP   C CB  1 
ATOM   8035  C CG  . ASP   C 1 80  ? 9.209   16.129  60.792  1.00 24.43  ?  80  ASP   C CG  1 
ATOM   8036  O OD1 . ASP   C 1 80  ? 9.696   17.215  60.403  1.00 29.53  ?  80  ASP   C OD1 1 
ATOM   8037  O OD2 . ASP   C 1 80  ? 8.597   15.340  60.043  1.00 30.84  ?  80  ASP   C OD2 1 
ATOM   8038  N N   . LEU   C 1 81  ? 10.971  15.267  64.916  1.00 20.32  ?  81  LEU   C N   1 
ATOM   8039  C CA  . LEU   C 1 81  ? 10.993  14.914  66.328  1.00 20.47  ?  81  LEU   C CA  1 
ATOM   8040  C C   . LEU   C 1 81  ? 11.696  15.983  67.157  1.00 23.38  ?  81  LEU   C C   1 
ATOM   8041  O O   . LEU   C 1 81  ? 11.211  16.363  68.228  1.00 21.88  ?  81  LEU   C O   1 
ATOM   8042  C CB  . LEU   C 1 81  ? 11.671  13.558  66.508  1.00 22.27  ?  81  LEU   C CB  1 
ATOM   8043  C CG  . LEU   C 1 81  ? 11.672  13.013  67.932  1.00 24.25  ?  81  LEU   C CG  1 
ATOM   8044  C CD1 . LEU   C 1 81  ? 10.244  12.934  68.461  1.00 17.77  ?  81  LEU   C CD1 1 
ATOM   8045  C CD2 . LEU   C 1 81  ? 12.348  11.652  67.946  1.00 19.01  ?  81  LEU   C CD2 1 
ATOM   8046  N N   . LYS   C 1 82  ? 12.842  16.473  66.682  1.00 19.08  ?  82  LYS   C N   1 
ATOM   8047  C CA  . LYS   C 1 82  ? 13.522  17.572  67.361  1.00 21.84  ?  82  LYS   C CA  1 
ATOM   8048  C C   . LYS   C 1 82  ? 12.593  18.768  67.542  1.00 26.11  ?  82  LYS   C C   1 
ATOM   8049  O O   . LYS   C 1 82  ? 12.563  19.381  68.616  1.00 28.16  ?  82  LYS   C O   1 
ATOM   8050  C CB  . LYS   C 1 82  ? 14.773  17.973  66.573  1.00 21.77  ?  82  LYS   C CB  1 
ATOM   8051  C CG  . LYS   C 1 82  ? 15.579  19.121  67.183  1.00 22.53  ?  82  LYS   C CG  1 
ATOM   8052  C CD  . LYS   C 1 82  ? 16.855  19.359  66.384  1.00 25.60  ?  82  LYS   C CD  1 
ATOM   8053  C CE  . LYS   C 1 82  ? 17.782  20.355  67.069  1.00 24.35  ?  82  LYS   C CE  1 
ATOM   8054  N NZ  . LYS   C 1 82  ? 17.200  21.720  67.088  1.00 32.39  ?  82  LYS   C NZ  1 
ATOM   8055  N N   . ASP   C 1 83  ? 11.831  19.115  66.502  1.00 22.67  ?  83  ASP   C N   1 
ATOM   8056  C CA  . ASP   C 1 83  ? 10.883  20.222  66.602  1.00 22.89  ?  83  ASP   C CA  1 
ATOM   8057  C C   . ASP   C 1 83  ? 9.802   19.930  67.631  1.00 26.34  ?  83  ASP   C C   1 
ATOM   8058  O O   . ASP   C 1 83  ? 9.471   20.782  68.465  1.00 30.23  ?  83  ASP   C O   1 
ATOM   8059  C CB  . ASP   C 1 83  ? 10.242  20.489  65.247  1.00 21.05  ?  83  ASP   C CB  1 
ATOM   8060  C CG  . ASP   C 1 83  ? 11.239  20.922  64.207  1.00 28.41  ?  83  ASP   C CG  1 
ATOM   8061  O OD1 . ASP   C 1 83  ? 12.421  21.145  64.545  1.00 28.36  ?  83  ASP   C OD1 1 
ATOM   8062  O OD2 . ASP   C 1 83  ? 10.828  21.035  63.036  1.00 35.17  ?  83  ASP   C OD2 1 
ATOM   8063  N N   . LYS   C 1 84  ? 9.222   18.731  67.569  1.00 28.37  ?  84  LYS   C N   1 
ATOM   8064  C CA  . LYS   C 1 84  ? 8.148   18.376  68.487  1.00 26.61  ?  84  LYS   C CA  1 
ATOM   8065  C C   . LYS   C 1 84  ? 8.596   18.514  69.935  1.00 27.02  ?  84  LYS   C C   1 
ATOM   8066  O O   . LYS   C 1 84  ? 7.865   19.067  70.765  1.00 28.05  ?  84  LYS   C O   1 
ATOM   8067  C CB  . LYS   C 1 84  ? 7.667   16.955  68.199  1.00 23.84  ?  84  LYS   C CB  1 
ATOM   8068  C CG  . LYS   C 1 84  ? 6.309   16.634  68.784  1.00 22.60  ?  84  LYS   C CG  1 
ATOM   8069  C CD  . LYS   C 1 84  ? 5.237   17.537  68.193  1.00 22.56  ?  84  LYS   C CD  1 
ATOM   8070  C CE  . LYS   C 1 84  ? 3.885   17.242  68.809  1.00 24.54  ?  84  LYS   C CE  1 
ATOM   8071  N NZ  . LYS   C 1 84  ? 2.821   18.106  68.233  1.00 29.97  ?  84  LYS   C NZ  1 
ATOM   8072  N N   . ALA   C 1 85  ? 9.805   18.044  70.255  1.00 24.38  ?  85  ALA   C N   1 
ATOM   8073  C CA  . ALA   C 1 85  ? 10.298  18.160  71.626  1.00 26.32  ?  85  ALA   C CA  1 
ATOM   8074  C C   . ALA   C 1 85  ? 10.581  19.608  72.010  1.00 26.94  ?  85  ALA   C C   1 
ATOM   8075  O O   . ALA   C 1 85  ? 10.509  19.958  73.194  1.00 27.05  ?  85  ALA   C O   1 
ATOM   8076  C CB  . ALA   C 1 85  ? 11.552  17.311  71.816  1.00 23.77  ?  85  ALA   C CB  1 
ATOM   8077  N N   . LYS   C 1 86  ? 10.919  20.456  71.037  1.00 29.04  ?  86  LYS   C N   1 
ATOM   8078  C CA  . LYS   C 1 86  ? 11.001  21.887  71.311  1.00 29.91  ?  86  LYS   C CA  1 
ATOM   8079  C C   . LYS   C 1 86  ? 9.617   22.476  71.560  1.00 29.01  ?  86  LYS   C C   1 
ATOM   8080  O O   . LYS   C 1 86  ? 9.451   23.344  72.426  1.00 30.39  ?  86  LYS   C O   1 
ATOM   8081  C CB  . LYS   C 1 86  ? 11.686  22.607  70.151  1.00 30.08  ?  86  LYS   C CB  1 
ATOM   8082  C CG  . LYS   C 1 86  ? 11.791  24.108  70.339  1.00 26.50  ?  86  LYS   C CG  1 
ATOM   8083  C CD  . LYS   C 1 86  ? 12.748  24.460  71.463  1.00 29.25  ?  86  LYS   C CD  1 
ATOM   8084  C CE  . LYS   C 1 86  ? 12.734  25.955  71.737  1.00 31.26  ?  86  LYS   C CE  1 
ATOM   8085  N NZ  . LYS   C 1 86  ? 13.517  26.290  72.954  1.00 29.60  ?  86  LYS   C NZ  1 
ATOM   8086  N N   . GLU   C 1 87  ? 8.608   22.002  70.825  1.00 26.46  ?  87  GLU   C N   1 
ATOM   8087  C CA  . GLU   C 1 87  ? 7.248   22.498  71.017  1.00 23.54  ?  87  GLU   C CA  1 
ATOM   8088  C C   . GLU   C 1 87  ? 6.691   22.080  72.373  1.00 28.94  ?  87  GLU   C C   1 
ATOM   8089  O O   . GLU   C 1 87  ? 6.158   22.908  73.120  1.00 27.29  ?  87  GLU   C O   1 
ATOM   8090  C CB  . GLU   C 1 87  ? 6.340   21.991  69.899  1.00 27.19  ?  87  GLU   C CB  1 
ATOM   8091  C CG  . GLU   C 1 87  ? 4.864   22.256  70.167  1.00 31.84  ?  87  GLU   C CG  1 
ATOM   8092  C CD  . GLU   C 1 87  ? 3.936   21.464  69.263  1.00 36.39  ?  87  GLU   C CD  1 
ATOM   8093  O OE1 . GLU   C 1 87  ? 4.437   20.732  68.379  1.00 37.43  ?  87  GLU   C OE1 1 
ATOM   8094  O OE2 . GLU   C 1 87  ? 2.700   21.580  69.438  1.00 42.09  ?  87  GLU   C OE2 1 
ATOM   8095  N N   . LEU   C 1 88  ? 6.804   20.796  72.711  1.00 28.91  ?  88  LEU   C N   1 
ATOM   8096  C CA  . LEU   C 1 88  ? 6.116   20.278  73.887  1.00 28.62  ?  88  LEU   C CA  1 
ATOM   8097  C C   . LEU   C 1 88  ? 6.813   20.679  75.178  1.00 27.82  ?  88  LEU   C C   1 
ATOM   8098  O O   . LEU   C 1 88  ? 6.164   21.127  76.129  1.00 32.30  ?  88  LEU   C O   1 
ATOM   8099  C CB  . LEU   C 1 88  ? 6.006   18.759  73.803  1.00 28.54  ?  88  LEU   C CB  1 
ATOM   8100  C CG  . LEU   C 1 88  ? 5.023   18.189  72.789  1.00 22.92  ?  88  LEU   C CG  1 
ATOM   8101  C CD1 . LEU   C 1 88  ? 5.003   16.679  72.945  1.00 23.73  ?  88  LEU   C CD1 1 
ATOM   8102  C CD2 . LEU   C 1 88  ? 3.641   18.774  73.002  1.00 23.49  ?  88  LEU   C CD2 1 
ATOM   8103  N N   . PHE   C 1 89  ? 8.131   20.513  75.237  1.00 29.06  ?  89  PHE   C N   1 
ATOM   8104  C CA  . PHE   C 1 89  ? 8.871   20.702  76.470  1.00 27.92  ?  89  PHE   C CA  1 
ATOM   8105  C C   . PHE   C 1 89  ? 9.702   21.972  76.489  1.00 30.40  ?  89  PHE   C C   1 
ATOM   8106  O O   . PHE   C 1 89  ? 10.182  22.356  77.563  1.00 30.58  ?  89  PHE   C O   1 
ATOM   8107  C CB  . PHE   C 1 89  ? 9.791   19.501  76.715  1.00 27.32  ?  89  PHE   C CB  1 
ATOM   8108  C CG  . PHE   C 1 89  ? 9.186   18.185  76.319  1.00 26.64  ?  89  PHE   C CG  1 
ATOM   8109  C CD1 . PHE   C 1 89  ? 8.163   17.624  77.066  1.00 28.56  ?  89  PHE   C CD1 1 
ATOM   8110  C CD2 . PHE   C 1 89  ? 9.645   17.506  75.213  1.00 27.79  ?  89  PHE   C CD2 1 
ATOM   8111  C CE1 . PHE   C 1 89  ? 7.611   16.411  76.712  1.00 24.40  ?  89  PHE   C CE1 1 
ATOM   8112  C CE2 . PHE   C 1 89  ? 9.089   16.294  74.851  1.00 28.49  ?  89  PHE   C CE2 1 
ATOM   8113  C CZ  . PHE   C 1 89  ? 8.075   15.747  75.606  1.00 22.81  ?  89  PHE   C CZ  1 
ATOM   8114  N N   . ASN   C 1 90  ? 9.871   22.634  75.342  1.00 29.64  ?  90  ASN   C N   1 
ATOM   8115  C CA  . ASN   C 1 90  ? 10.793  23.757  75.187  1.00 29.00  ?  90  ASN   C CA  1 
ATOM   8116  C C   . ASN   C 1 90  ? 12.247  23.327  75.362  1.00 29.22  ?  90  ASN   C C   1 
ATOM   8117  O O   . ASN   C 1 90  ? 13.085  24.111  75.816  1.00 34.41  ?  90  ASN   C O   1 
ATOM   8118  C CB  . ASN   C 1 90  ? 10.457  24.906  76.146  1.00 31.38  ?  90  ASN   C CB  1 
ATOM   8119  C CG  . ASN   C 1 90  ? 11.075  26.212  75.718  1.00 31.29  ?  90  ASN   C CG  1 
ATOM   8120  O OD1 . ASN   C 1 90  ? 11.401  26.395  74.546  1.00 32.63  ?  90  ASN   C OD1 1 
ATOM   8121  N ND2 . ASN   C 1 90  ? 11.244  27.129  76.661  1.00 33.67  ?  90  ASN   C ND2 1 
ATOM   8122  N N   . TYR   C 1 91  ? 12.567  22.087  75.003  1.00 30.53  ?  91  TYR   C N   1 
ATOM   8123  C CA  . TYR   C 1 91  ? 13.924  21.569  75.108  1.00 26.92  ?  91  TYR   C CA  1 
ATOM   8124  C C   . TYR   C 1 91  ? 14.605  21.638  73.746  1.00 27.44  ?  91  TYR   C C   1 
ATOM   8125  O O   . TYR   C 1 91  ? 13.974  21.387  72.717  1.00 23.44  ?  91  TYR   C O   1 
ATOM   8126  C CB  . TYR   C 1 91  ? 13.923  20.132  75.630  1.00 23.13  ?  91  TYR   C CB  1 
ATOM   8127  C CG  . TYR   C 1 91  ? 13.639  20.014  77.108  1.00 26.31  ?  91  TYR   C CG  1 
ATOM   8128  C CD1 . TYR   C 1 91  ? 13.232  21.116  77.853  1.00 27.14  ?  91  TYR   C CD1 1 
ATOM   8129  C CD2 . TYR   C 1 91  ? 13.789  18.803  77.763  1.00 23.00  ?  91  TYR   C CD2 1 
ATOM   8130  C CE1 . TYR   C 1 91  ? 12.978  21.010  79.207  1.00 27.04  ?  91  TYR   C CE1 1 
ATOM   8131  C CE2 . TYR   C 1 91  ? 13.534  18.689  79.121  1.00 25.05  ?  91  TYR   C CE2 1 
ATOM   8132  C CZ  . TYR   C 1 91  ? 13.132  19.793  79.834  1.00 22.52  ?  91  TYR   C CZ  1 
ATOM   8133  O OH  . TYR   C 1 91  ? 12.884  19.682  81.179  1.00 27.38  ?  91  TYR   C OH  1 
ATOM   8134  N N   . ASP   C 1 92  ? 15.901  21.967  73.743  1.00 24.77  ?  92  ASP   C N   1 
ATOM   8135  C CA  . ASP   C 1 92  ? 16.596  22.305  72.504  1.00 24.28  ?  92  ASP   C CA  1 
ATOM   8136  C C   . ASP   C 1 92  ? 17.339  21.145  71.858  1.00 24.83  ?  92  ASP   C C   1 
ATOM   8137  O O   . ASP   C 1 92  ? 17.703  21.250  70.683  1.00 27.85  ?  92  ASP   C O   1 
ATOM   8138  C CB  . ASP   C 1 92  ? 17.600  23.434  72.750  1.00 29.90  ?  92  ASP   C CB  1 
ATOM   8139  C CG  . ASP   C 1 92  ? 16.933  24.769  72.918  1.00 33.18  ?  92  ASP   C CG  1 
ATOM   8140  O OD1 . ASP   C 1 92  ? 15.823  24.946  72.372  1.00 32.26  ?  92  ASP   C OD1 1 
ATOM   8141  O OD2 . ASP   C 1 92  ? 17.517  25.641  73.595  1.00 37.51  ?  92  ASP   C OD2 1 
ATOM   8142  N N   . TYR   C 1 93  ? 17.610  20.071  72.588  1.00 27.09  ?  93  TYR   C N   1 
ATOM   8143  C CA  . TYR   C 1 93  ? 18.390  18.960  72.065  1.00 25.80  ?  93  TYR   C CA  1 
ATOM   8144  C C   . TYR   C 1 93  ? 17.622  17.666  72.260  1.00 27.98  ?  93  TYR   C C   1 
ATOM   8145  O O   . TYR   C 1 93  ? 16.962  17.474  73.287  1.00 23.88  ?  93  TYR   C O   1 
ATOM   8146  C CB  . TYR   C 1 93  ? 19.748  18.847  72.757  1.00 24.29  ?  93  TYR   C CB  1 
ATOM   8147  C CG  . TYR   C 1 93  ? 20.569  20.113  72.705  1.00 30.26  ?  93  TYR   C CG  1 
ATOM   8148  C CD1 . TYR   C 1 93  ? 21.254  20.471  71.551  1.00 32.60  ?  93  TYR   C CD1 1 
ATOM   8149  C CD2 . TYR   C 1 93  ? 20.655  20.954  73.805  1.00 29.35  ?  93  TYR   C CD2 1 
ATOM   8150  C CE1 . TYR   C 1 93  ? 22.005  21.632  71.496  1.00 30.92  ?  93  TYR   C CE1 1 
ATOM   8151  C CE2 . TYR   C 1 93  ? 21.402  22.114  73.759  1.00 31.83  ?  93  TYR   C CE2 1 
ATOM   8152  C CZ  . TYR   C 1 93  ? 22.075  22.445  72.601  1.00 31.92  ?  93  TYR   C CZ  1 
ATOM   8153  O OH  . TYR   C 1 93  ? 22.822  23.596  72.547  1.00 35.60  ?  93  TYR   C OH  1 
ATOM   8154  N N   . ILE   C 1 94  ? 17.714  16.777  71.276  1.00 25.25  ?  94  ILE   C N   1 
ATOM   8155  C CA  . ILE   C 1 94  ? 17.137  15.446  71.394  1.00 24.32  ?  94  ILE   C CA  1 
ATOM   8156  C C   . ILE   C 1 94  ? 18.140  14.407  70.920  1.00 22.06  ?  94  ILE   C C   1 
ATOM   8157  O O   . ILE   C 1 94  ? 18.960  14.657  70.029  1.00 20.52  ?  94  ILE   C O   1 
ATOM   8158  C CB  . ILE   C 1 94  ? 15.825  15.300  70.604  1.00 20.93  ?  94  ILE   C CB  1 
ATOM   8159  C CG1 . ILE   C 1 94  ? 16.081  15.489  69.110  1.00 24.53  ?  94  ILE   C CG1 1 
ATOM   8160  C CG2 . ILE   C 1 94  ? 14.792  16.278  71.112  1.00 23.33  ?  94  ILE   C CG2 1 
ATOM   8161  C CD1 . ILE   C 1 94  ? 15.216  14.622  68.239  1.00 22.53  ?  94  ILE   C CD1 1 
ATOM   8162  N N   . ILE   C 1 95  ? 18.068  13.234  71.539  1.00 18.46  ?  95  ILE   C N   1 
ATOM   8163  C CA  . ILE   C 1 95  ? 18.704  12.014  71.052  1.00 18.09  ?  95  ILE   C CA  1 
ATOM   8164  C C   . ILE   C 1 95  ? 17.636  10.931  71.084  1.00 20.56  ?  95  ILE   C C   1 
ATOM   8165  O O   . ILE   C 1 95  ? 17.172  10.554  72.172  1.00 20.61  ?  95  ILE   C O   1 
ATOM   8166  C CB  . ILE   C 1 95  ? 19.910  11.596  71.904  1.00 23.41  ?  95  ILE   C CB  1 
ATOM   8167  C CG1 . ILE   C 1 95  ? 20.948  12.711  72.003  1.00 22.28  ?  95  ILE   C CG1 1 
ATOM   8168  C CG2 . ILE   C 1 95  ? 20.559  10.354  71.327  1.00 22.08  ?  95  ILE   C CG2 1 
ATOM   8169  C CD1 . ILE   C 1 95  ? 21.846  12.536  73.167  1.00 20.66  ?  95  ILE   C CD1 1 
ATOM   8170  N N   . PRO   C 1 96  ? 17.211  10.402  69.948  1.00 18.42  ?  96  PRO   C N   1 
ATOM   8171  C CA  . PRO   C 1 96  ? 16.277  9.277   69.986  1.00 18.20  ?  96  PRO   C CA  1 
ATOM   8172  C C   . PRO   C 1 96  ? 16.951  8.067   70.605  1.00 16.29  ?  96  PRO   C C   1 
ATOM   8173  O O   . PRO   C 1 96  ? 18.179  7.968   70.668  1.00 16.80  ?  96  PRO   C O   1 
ATOM   8174  C CB  . PRO   C 1 96  ? 15.924  9.040   68.511  1.00 19.68  ?  96  PRO   C CB  1 
ATOM   8175  C CG  . PRO   C 1 96  ? 17.025  9.690   67.744  1.00 18.09  ?  96  PRO   C CG  1 
ATOM   8176  C CD  . PRO   C 1 96  ? 17.540  10.821  68.576  1.00 19.08  ?  96  PRO   C CD  1 
ATOM   8177  N N   . ALA   C 1 97  ? 16.119  7.157   71.104  1.00 16.47  ?  97  ALA   C N   1 
ATOM   8178  C CA  . ALA   C 1 97  ? 16.583  5.914   71.702  1.00 16.49  ?  97  ALA   C CA  1 
ATOM   8179  C C   . ALA   C 1 97  ? 15.571  4.830   71.367  1.00 16.35  ?  97  ALA   C C   1 
ATOM   8180  O O   . ALA   C 1 97  ? 14.414  5.119   71.050  1.00 17.44  ?  97  ALA   C O   1 
ATOM   8181  C CB  . ALA   C 1 97  ? 16.771  6.050   73.219  1.00 14.47  ?  97  ALA   C CB  1 
ATOM   8182  N N   . HIS   C 1 98  ? 16.009  3.567   71.417  1.00 17.23  ?  98  HIS   C N   1 
ATOM   8183  C CA  . HIS   C 1 98  ? 15.110  2.517   70.954  1.00 15.78  ?  98  HIS   C CA  1 
ATOM   8184  C C   . HIS   C 1 98  ? 13.959  2.301   71.928  1.00 16.63  ?  98  HIS   C C   1 
ATOM   8185  O O   . HIS   C 1 98  ? 12.856  1.958   71.494  1.00 17.22  ?  98  HIS   C O   1 
ATOM   8186  C CB  . HIS   C 1 98  ? 15.882  1.222   70.671  1.00 15.70  ?  98  HIS   C CB  1 
ATOM   8187  C CG  . HIS   C 1 98  ? 16.203  0.409   71.884  1.00 17.25  ?  98  HIS   C CG  1 
ATOM   8188  N ND1 . HIS   C 1 98  ? 17.379  0.550   72.585  1.00 20.95  ?  98  HIS   C ND1 1 
ATOM   8189  C CD2 . HIS   C 1 98  ? 15.522  -0.592  72.490  1.00 18.19  ?  98  HIS   C CD2 1 
ATOM   8190  C CE1 . HIS   C 1 98  ? 17.394  -0.305  73.593  1.00 20.21  ?  98  HIS   C CE1 1 
ATOM   8191  N NE2 . HIS   C 1 98  ? 16.278  -1.010  73.557  1.00 18.91  ?  98  HIS   C NE2 1 
ATOM   8192  N N   . GLN   C 1 99  ? 14.170  2.535   73.222  1.00 16.42  ?  99  GLN   C N   1 
ATOM   8193  C CA  . GLN   C 1 99  ? 13.074  2.631   74.187  1.00 17.14  ?  99  GLN   C CA  1 
ATOM   8194  C C   . GLN   C 1 99  ? 13.617  3.247   75.474  1.00 16.64  ?  99  GLN   C C   1 
ATOM   8195  O O   . GLN   C 1 99  ? 14.760  3.717   75.528  1.00 15.31  ?  99  GLN   C O   1 
ATOM   8196  C CB  . GLN   C 1 99  ? 12.412  1.276   74.441  1.00 16.47  ?  99  GLN   C CB  1 
ATOM   8197  C CG  . GLN   C 1 99  ? 13.296  0.255   75.109  1.00 20.75  ?  99  GLN   C CG  1 
ATOM   8198  C CD  . GLN   C 1 99  ? 12.578  -1.066  75.252  1.00 22.22  ?  99  GLN   C CD  1 
ATOM   8199  O OE1 . GLN   C 1 99  ? 12.178  -1.670  74.254  1.00 21.20  ?  99  GLN   C OE1 1 
ATOM   8200  N NE2 . GLN   C 1 99  ? 12.376  -1.508  76.493  1.00 21.80  ?  99  GLN   C NE2 1 
ATOM   8201  N N   . GLY   C 1 100 ? 12.795  3.214   76.521  1.00 17.43  ?  100 GLY   C N   1 
ATOM   8202  C CA  . GLY   C 1 100 ? 13.069  4.012   77.706  1.00 13.79  ?  100 GLY   C CA  1 
ATOM   8203  C C   . GLY   C 1 100 ? 14.357  3.640   78.412  1.00 18.57  ?  100 GLY   C C   1 
ATOM   8204  O O   . GLY   C 1 100 ? 15.112  4.518   78.837  1.00 15.61  ?  100 GLY   C O   1 
ATOM   8205  N N   . ARG   C 1 101 ? 14.618  2.338   78.573  1.00 15.44  ?  101 ARG   C N   1 
ATOM   8206  C CA  . ARG   C 1 101 ? 15.830  1.939   79.277  1.00 18.52  ?  101 ARG   C CA  1 
ATOM   8207  C C   . ARG   C 1 101 ? 17.074  2.129   78.425  1.00 14.08  ?  101 ARG   C C   1 
ATOM   8208  O O   . ARG   C 1 101 ? 18.185  2.103   78.966  1.00 15.67  ?  101 ARG   C O   1 
ATOM   8209  C CB  . ARG   C 1 101 ? 15.735  0.486   79.745  1.00 16.63  ?  101 ARG   C CB  1 
ATOM   8210  C CG  . ARG   C 1 101 ? 15.716  -0.531  78.613  1.00 14.44  ?  101 ARG   C CG  1 
ATOM   8211  C CD  . ARG   C 1 101 ? 15.158  -1.845  79.119  1.00 16.28  ?  101 ARG   C CD  1 
ATOM   8212  N NE  . ARG   C 1 101 ? 13.715  -1.756  79.331  1.00 18.69  ?  101 ARG   C NE  1 
ATOM   8213  C CZ  . ARG   C 1 101 ? 12.963  -2.746  79.789  1.00 18.98  ?  101 ARG   C CZ  1 
ATOM   8214  N NH1 . ARG   C 1 101 ? 13.492  -3.896  80.169  1.00 18.73  ?  101 ARG   C NH1 1 
ATOM   8215  N NH2 . ARG   C 1 101 ? 11.645  -2.585  79.852  1.00 19.05  ?  101 ARG   C NH2 1 
ATOM   8216  N N   . GLY   C 1 102 ? 16.913  2.311   77.113  1.00 19.14  ?  102 GLY   C N   1 
ATOM   8217  C CA  . GLY   C 1 102 ? 18.021  2.773   76.298  1.00 14.54  ?  102 GLY   C CA  1 
ATOM   8218  C C   . GLY   C 1 102 ? 18.284  4.251   76.501  1.00 16.47  ?  102 GLY   C C   1 
ATOM   8219  O O   . GLY   C 1 102 ? 19.437  4.696   76.496  1.00 14.73  ?  102 GLY   C O   1 
ATOM   8220  N N   . ALA   C 1 103 ? 17.218  5.032   76.694  1.00 14.30  ?  103 ALA   C N   1 
ATOM   8221  C CA  . ALA   C 1 103 ? 17.376  6.434   77.063  1.00 16.39  ?  103 ALA   C CA  1 
ATOM   8222  C C   . ALA   C 1 103 ? 18.116  6.575   78.388  1.00 19.69  ?  103 ALA   C C   1 
ATOM   8223  O O   . ALA   C 1 103 ? 18.958  7.467   78.540  1.00 20.61  ?  103 ALA   C O   1 
ATOM   8224  C CB  . ALA   C 1 103 ? 16.011  7.118   77.142  1.00 16.90  ?  103 ALA   C CB  1 
ATOM   8225  N N   . GLU   C 1 104 ? 17.817  5.705   79.359  1.00 16.12  ?  104 GLU   C N   1 
ATOM   8226  C CA  . GLU   C 1 104 ? 18.530  5.744   80.633  1.00 16.97  ?  104 GLU   C CA  1 
ATOM   8227  C C   . GLU   C 1 104 ? 19.983  5.324   80.458  1.00 19.67  ?  104 GLU   C C   1 
ATOM   8228  O O   . GLU   C 1 104 ? 20.876  5.883   81.102  1.00 19.39  ?  104 GLU   C O   1 
ATOM   8229  C CB  . GLU   C 1 104 ? 17.819  4.855   81.661  1.00 18.70  ?  104 GLU   C CB  1 
ATOM   8230  C CG  . GLU   C 1 104 ? 16.389  5.323   81.970  1.00 21.20  ?  104 GLU   C CG  1 
ATOM   8231  C CD  . GLU   C 1 104 ? 15.490  4.246   82.592  1.00 23.14  ?  104 GLU   C CD  1 
ATOM   8232  O OE1 . GLU   C 1 104 ? 15.815  3.039   82.511  1.00 20.42  ?  104 GLU   C OE1 1 
ATOM   8233  O OE2 . GLU   C 1 104 ? 14.444  4.615   83.165  1.00 22.54  ?  104 GLU   C OE2 1 
ATOM   8234  N N   . ASN   C 1 105 ? 20.242  4.351   79.580  1.00 18.17  ?  105 ASN   C N   1 
ATOM   8235  C CA  . ASN   C 1 105 ? 21.608  3.885   79.385  1.00 17.39  ?  105 ASN   C CA  1 
ATOM   8236  C C   . ASN   C 1 105 ? 22.458  4.935   78.680  1.00 19.96  ?  105 ASN   C C   1 
ATOM   8237  O O   . ASN   C 1 105 ? 23.677  4.980   78.880  1.00 21.00  ?  105 ASN   C O   1 
ATOM   8238  C CB  . ASN   C 1 105 ? 21.607  2.574   78.602  1.00 17.50  ?  105 ASN   C CB  1 
ATOM   8239  C CG  . ASN   C 1 105 ? 22.978  1.931   78.539  1.00 20.45  ?  105 ASN   C CG  1 
ATOM   8240  O OD1 . ASN   C 1 105 ? 23.791  2.092   79.443  1.00 19.92  ?  105 ASN   C OD1 1 
ATOM   8241  N ND2 . ASN   C 1 105 ? 23.246  1.213   77.457  1.00 19.43  ?  105 ASN   C ND2 1 
ATOM   8242  N N   . ILE   C 1 106 ? 21.837  5.794   77.872  1.00 19.79  ?  106 ILE   C N   1 
ATOM   8243  C CA  . ILE   C 1 106 ? 22.558  6.916   77.275  1.00 20.82  ?  106 ILE   C CA  1 
ATOM   8244  C C   . ILE   C 1 106 ? 22.870  7.970   78.328  1.00 22.51  ?  106 ILE   C C   1 
ATOM   8245  O O   . ILE   C 1 106 ? 24.025  8.378   78.506  1.00 23.23  ?  106 ILE   C O   1 
ATOM   8246  C CB  . ILE   C 1 106 ? 21.741  7.521   76.122  1.00 21.77  ?  106 ILE   C CB  1 
ATOM   8247  C CG1 . ILE   C 1 106 ? 21.666  6.549   74.945  1.00 20.51  ?  106 ILE   C CG1 1 
ATOM   8248  C CG2 . ILE   C 1 106 ? 22.327  8.870   75.700  1.00 21.62  ?  106 ILE   C CG2 1 
ATOM   8249  C CD1 . ILE   C 1 106 ? 20.713  7.003   73.877  1.00 16.36  ?  106 ILE   C CD1 1 
ATOM   8250  N N   . LEU   C 1 107 ? 21.848  8.421   79.047  1.00 18.46  ?  107 LEU   C N   1 
ATOM   8251  C CA  . LEU   C 1 107 ? 21.980  9.620   79.865  1.00 21.12  ?  107 LEU   C CA  1 
ATOM   8252  C C   . LEU   C 1 107 ? 22.682  9.350   81.190  1.00 22.62  ?  107 LEU   C C   1 
ATOM   8253  O O   . LEU   C 1 107 ? 23.545  10.134  81.603  1.00 22.96  ?  107 LEU   C O   1 
ATOM   8254  C CB  . LEU   C 1 107 ? 20.600  10.227  80.120  1.00 22.44  ?  107 LEU   C CB  1 
ATOM   8255  C CG  . LEU   C 1 107 ? 20.595  11.580  80.828  1.00 25.42  ?  107 LEU   C CG  1 
ATOM   8256  C CD1 . LEU   C 1 107 ? 21.460  12.562  80.053  1.00 20.16  ?  107 LEU   C CD1 1 
ATOM   8257  C CD2 . LEU   C 1 107 ? 19.160  12.101  80.987  1.00 19.75  ?  107 LEU   C CD2 1 
ATOM   8258  N N   . PHE   C 1 108 ? 22.320  8.264   81.883  1.00 19.83  ?  108 PHE   C N   1 
ATOM   8259  C CA  . PHE   C 1 108 ? 22.734  8.142   83.280  1.00 23.54  ?  108 PHE   C CA  1 
ATOM   8260  C C   . PHE   C 1 108 ? 24.241  7.993   83.432  1.00 20.27  ?  108 PHE   C C   1 
ATOM   8261  O O   . PHE   C 1 108 ? 24.820  8.678   84.295  1.00 22.69  ?  108 PHE   C O   1 
ATOM   8262  C CB  . PHE   C 1 108 ? 21.973  7.001   83.964  1.00 21.56  ?  108 PHE   C CB  1 
ATOM   8263  C CG  . PHE   C 1 108 ? 20.524  7.320   84.262  1.00 26.36  ?  108 PHE   C CG  1 
ATOM   8264  C CD1 . PHE   C 1 108 ? 19.924  8.466   83.753  1.00 22.82  ?  108 PHE   C CD1 1 
ATOM   8265  C CD2 . PHE   C 1 108 ? 19.771  6.483   85.066  1.00 23.70  ?  108 PHE   C CD2 1 
ATOM   8266  C CE1 . PHE   C 1 108 ? 18.602  8.760   84.024  1.00 20.95  ?  108 PHE   C CE1 1 
ATOM   8267  C CE2 . PHE   C 1 108 ? 18.438  6.776   85.346  1.00 23.20  ?  108 PHE   C CE2 1 
ATOM   8268  C CZ  . PHE   C 1 108 ? 17.857  7.918   84.826  1.00 21.93  ?  108 PHE   C CZ  1 
ATOM   8269  N N   . PRO   C 1 109 ? 24.938  7.145   82.666  1.00 21.91  ?  109 PRO   C N   1 
ATOM   8270  C CA  . PRO   C 1 109 ? 26.403  7.099   82.812  1.00 22.00  ?  109 PRO   C CA  1 
ATOM   8271  C C   . PRO   C 1 109 ? 27.056  8.436   82.534  1.00 22.35  ?  109 PRO   C C   1 
ATOM   8272  O O   . PRO   C 1 109 ? 28.076  8.765   83.149  1.00 25.67  ?  109 PRO   C O   1 
ATOM   8273  C CB  . PRO   C 1 109 ? 26.821  6.040   81.782  1.00 22.09  ?  109 PRO   C CB  1 
ATOM   8274  C CG  . PRO   C 1 109 ? 25.618  5.186   81.633  1.00 20.35  ?  109 PRO   C CG  1 
ATOM   8275  C CD  . PRO   C 1 109 ? 24.467  6.125   81.713  1.00 19.73  ?  109 PRO   C CD  1 
ATOM   8276  N N   . VAL   C 1 110 ? 26.484  9.221   81.624  1.00 23.05  ?  110 VAL   C N   1 
ATOM   8277  C CA  . VAL   C 1 110 ? 27.032  10.535  81.311  1.00 23.04  ?  110 VAL   C CA  1 
ATOM   8278  C C   . VAL   C 1 110 ? 26.885  11.469  82.507  1.00 24.28  ?  110 VAL   C C   1 
ATOM   8279  O O   . VAL   C 1 110 ? 27.830  12.166  82.894  1.00 22.83  ?  110 VAL   C O   1 
ATOM   8280  C CB  . VAL   C 1 110 ? 26.343  11.103  80.057  1.00 20.36  ?  110 VAL   C CB  1 
ATOM   8281  C CG1 . VAL   C 1 110 ? 26.638  12.587  79.909  1.00 23.97  ?  110 VAL   C CG1 1 
ATOM   8282  C CG2 . VAL   C 1 110 ? 26.774  10.325  78.813  1.00 18.70  ?  110 VAL   C CG2 1 
ATOM   8283  N N   . LEU   C 1 111 ? 25.696  11.491  83.115  1.00 22.11  ?  111 LEU   C N   1 
ATOM   8284  C CA  . LEU   C 1 111 ? 25.490  12.334  84.285  1.00 24.20  ?  111 LEU   C CA  1 
ATOM   8285  C C   . LEU   C 1 111 ? 26.469  11.996  85.403  1.00 26.63  ?  111 LEU   C C   1 
ATOM   8286  O O   . LEU   C 1 111 ? 26.901  12.892  86.137  1.00 25.58  ?  111 LEU   C O   1 
ATOM   8287  C CB  . LEU   C 1 111 ? 24.051  12.202  84.780  1.00 25.24  ?  111 LEU   C CB  1 
ATOM   8288  C CG  . LEU   C 1 111 ? 22.971  12.669  83.806  1.00 20.56  ?  111 LEU   C CG  1 
ATOM   8289  C CD1 . LEU   C 1 111 ? 21.593  12.499  84.421  1.00 19.40  ?  111 LEU   C CD1 1 
ATOM   8290  C CD2 . LEU   C 1 111 ? 23.226  14.112  83.409  1.00 23.70  ?  111 LEU   C CD2 1 
ATOM   8291  N N   . LEU   C 1 112 ? 26.834  10.718  85.548  1.00 20.02  ?  112 LEU   C N   1 
ATOM   8292  C CA  . LEU   C 1 112 ? 27.794  10.350  86.583  1.00 24.11  ?  112 LEU   C CA  1 
ATOM   8293  C C   . LEU   C 1 112 ? 29.183  10.865  86.241  1.00 28.06  ?  112 LEU   C C   1 
ATOM   8294  O O   . LEU   C 1 112 ? 29.844  11.494  87.077  1.00 27.22  ?  112 LEU   C O   1 
ATOM   8295  C CB  . LEU   C 1 112 ? 27.818  8.836   86.782  1.00 21.54  ?  112 LEU   C CB  1 
ATOM   8296  C CG  . LEU   C 1 112 ? 28.897  8.343   87.746  1.00 24.41  ?  112 LEU   C CG  1 
ATOM   8297  C CD1 . LEU   C 1 112 ? 28.735  8.995   89.106  1.00 27.94  ?  112 LEU   C CD1 1 
ATOM   8298  C CD2 . LEU   C 1 112 ? 28.847  6.842   87.881  1.00 27.22  ?  112 LEU   C CD2 1 
ATOM   8299  N N   . LYS   C 1 113 ? 29.641  10.603  85.011  1.00 25.26  ?  113 LYS   C N   1 
ATOM   8300  C CA  . LYS   C 1 113 ? 30.938  11.102  84.561  1.00 27.54  ?  113 LYS   C CA  1 
ATOM   8301  C C   . LYS   C 1 113 ? 31.023  12.613  84.719  1.00 33.02  ?  113 LYS   C C   1 
ATOM   8302  O O   . LYS   C 1 113 ? 32.034  13.145  85.194  1.00 32.40  ?  113 LYS   C O   1 
ATOM   8303  C CB  . LYS   C 1 113 ? 31.162  10.698  83.101  1.00 27.65  ?  113 LYS   C CB  1 
ATOM   8304  C CG  . LYS   C 1 113 ? 32.501  11.110  82.512  1.00 34.08  ?  113 LYS   C CG  1 
ATOM   8305  C CD  . LYS   C 1 113 ? 33.617  10.238  83.056  1.00 38.77  ?  113 LYS   C CD  1 
ATOM   8306  C CE  . LYS   C 1 113 ? 34.918  10.437  82.297  1.00 44.09  ?  113 LYS   C CE  1 
ATOM   8307  N NZ  . LYS   C 1 113 ? 35.946  9.444   82.737  1.00 48.14  ?  113 LYS   C NZ  1 
ATOM   8308  N N   . TYR   C 1 114 ? 29.951  13.317  84.345  1.00 29.79  ?  114 TYR   C N   1 
ATOM   8309  C CA  . TYR   C 1 114 ? 29.918  14.767  84.469  1.00 30.13  ?  114 TYR   C CA  1 
ATOM   8310  C C   . TYR   C 1 114 ? 30.015  15.198  85.929  1.00 36.55  ?  114 TYR   C C   1 
ATOM   8311  O O   . TYR   C 1 114 ? 30.700  16.177  86.250  1.00 42.01  ?  114 TYR   C O   1 
ATOM   8312  C CB  . TYR   C 1 114 ? 28.643  15.296  83.812  1.00 27.16  ?  114 TYR   C CB  1 
ATOM   8313  C CG  . TYR   C 1 114 ? 28.500  16.797  83.790  1.00 33.53  ?  114 TYR   C CG  1 
ATOM   8314  C CD1 . TYR   C 1 114 ? 29.064  17.552  82.772  1.00 38.04  ?  114 TYR   C CD1 1 
ATOM   8315  C CD2 . TYR   C 1 114 ? 27.780  17.460  84.777  1.00 38.71  ?  114 TYR   C CD2 1 
ATOM   8316  C CE1 . TYR   C 1 114 ? 28.927  18.930  82.745  1.00 42.95  ?  114 TYR   C CE1 1 
ATOM   8317  C CE2 . TYR   C 1 114 ? 27.635  18.834  84.760  1.00 37.88  ?  114 TYR   C CE2 1 
ATOM   8318  C CZ  . TYR   C 1 114 ? 28.209  19.564  83.741  1.00 43.76  ?  114 TYR   C CZ  1 
ATOM   8319  O OH  . TYR   C 1 114 ? 28.067  20.934  83.719  1.00 50.97  ?  114 TYR   C OH  1 
ATOM   8320  N N   . LYS   C 1 115 ? 29.354  14.469  86.834  1.00 32.22  ?  115 LYS   C N   1 
ATOM   8321  C CA  . LYS   C 1 115 ? 29.430  14.817  88.250  1.00 31.96  ?  115 LYS   C CA  1 
ATOM   8322  C C   . LYS   C 1 115 ? 30.802  14.506  88.837  1.00 41.80  ?  115 LYS   C C   1 
ATOM   8323  O O   . LYS   C 1 115 ? 31.251  15.203  89.755  1.00 40.06  ?  115 LYS   C O   1 
ATOM   8324  C CB  . LYS   C 1 115 ? 28.348  14.077  89.033  1.00 30.19  ?  115 LYS   C CB  1 
ATOM   8325  C CG  . LYS   C 1 115 ? 28.113  14.614  90.429  1.00 33.31  ?  115 LYS   C CG  1 
ATOM   8326  C CD  . LYS   C 1 115 ? 27.332  15.922  90.396  1.00 32.35  ?  115 LYS   C CD  1 
ATOM   8327  C CE  . LYS   C 1 115 ? 26.912  16.354  91.795  1.00 34.60  ?  115 LYS   C CE  1 
ATOM   8328  N NZ  . LYS   C 1 115 ? 26.033  17.559  91.769  1.00 31.83  ?  115 LYS   C NZ  1 
ATOM   8329  N N   . GLN   C 1 116 ? 31.484  13.477  88.326  1.00 37.22  ?  116 GLN   C N   1 
ATOM   8330  C CA  . GLN   C 1 116 ? 32.771  13.072  88.886  1.00 42.71  ?  116 GLN   C CA  1 
ATOM   8331  C C   . GLN   C 1 116 ? 33.883  14.082  88.637  1.00 47.78  ?  116 GLN   C C   1 
ATOM   8332  O O   . GLN   C 1 116 ? 34.969  13.922  89.203  1.00 51.56  ?  116 GLN   C O   1 
ATOM   8333  C CB  . GLN   C 1 116 ? 33.182  11.709  88.326  1.00 37.34  ?  116 GLN   C CB  1 
ATOM   8334  C CG  . GLN   C 1 116 ? 32.431  10.542  88.954  1.00 32.34  ?  116 GLN   C CG  1 
ATOM   8335  C CD  . GLN   C 1 116 ? 32.639  9.238   88.205  1.00 33.01  ?  116 GLN   C CD  1 
ATOM   8336  O OE1 . GLN   C 1 116 ? 33.013  9.225   87.029  1.00 32.39  ?  116 GLN   C OE1 1 
ATOM   8337  N NE2 . GLN   C 1 116 ? 32.390  8.132   88.886  1.00 33.20  ?  116 GLN   C NE2 1 
ATOM   8338  N N   . LYS   C 1 117 ? 33.645  15.104  87.817  1.00 49.76  ?  117 LYS   C N   1 
ATOM   8339  C CA  . LYS   C 1 117 ? 34.663  16.117  87.566  1.00 59.98  ?  117 LYS   C CA  1 
ATOM   8340  C C   . LYS   C 1 117 ? 35.081  16.800  88.865  1.00 64.66  ?  117 LYS   C C   1 
ATOM   8341  O O   . LYS   C 1 117 ? 34.244  17.147  89.704  1.00 63.39  ?  117 LYS   C O   1 
ATOM   8342  C CB  . LYS   C 1 117 ? 34.142  17.146  86.560  1.00 57.93  ?  117 LYS   C CB  1 
ATOM   8343  C CG  . LYS   C 1 117 ? 34.040  16.600  85.140  1.00 57.96  ?  117 LYS   C CG  1 
ATOM   8344  C CD  . LYS   C 1 117 ? 32.982  17.319  84.304  1.00 57.06  ?  117 LYS   C CD  1 
ATOM   8345  C CE  . LYS   C 1 117 ? 33.298  18.800  84.119  1.00 66.11  ?  117 LYS   C CE  1 
ATOM   8346  N NZ  . LYS   C 1 117 ? 32.350  19.457  83.166  1.00 56.72  ?  117 LYS   C NZ  1 
ATOM   8347  N N   . GLU   C 1 118 ? 36.394  16.979  89.025  1.00 66.48  ?  118 GLU   C N   1 
ATOM   8348  C CA  . GLU   C 1 118 ? 36.992  17.529  90.245  1.00 67.57  ?  118 GLU   C CA  1 
ATOM   8349  C C   . GLU   C 1 118 ? 36.742  16.620  91.447  1.00 67.21  ?  118 GLU   C C   1 
ATOM   8350  O O   . GLU   C 1 118 ? 36.512  17.087  92.564  1.00 68.68  ?  118 GLU   C O   1 
ATOM   8351  C CB  . GLU   C 1 118 ? 36.505  18.953  90.532  1.00 75.81  ?  118 GLU   C CB  1 
ATOM   8352  C CG  . GLU   C 1 118 ? 37.227  20.038  89.748  1.00 81.11  ?  118 GLU   C CG  1 
ATOM   8353  C CD  . GLU   C 1 118 ? 36.431  20.519  88.552  1.00 86.58  ?  118 GLU   C CD  1 
ATOM   8354  O OE1 . GLU   C 1 118 ? 35.293  20.037  88.360  1.00 84.77  ?  118 GLU   C OE1 1 
ATOM   8355  O OE2 . GLU   C 1 118 ? 36.941  21.382  87.806  1.00 91.96  ?  118 GLU   C OE2 1 
ATOM   8356  N N   . GLY   C 1 119 ? 36.790  15.311  91.213  1.00 67.32  ?  119 GLY   C N   1 
ATOM   8357  C CA  . GLY   C 1 119 ? 36.778  14.350  92.300  1.00 63.23  ?  119 GLY   C CA  1 
ATOM   8358  C C   . GLY   C 1 119 ? 35.525  14.334  93.143  1.00 61.14  ?  119 GLY   C C   1 
ATOM   8359  O O   . GLY   C 1 119 ? 35.567  13.869  94.284  1.00 63.06  ?  119 GLY   C O   1 
ATOM   8360  N N   . LYS   C 1 120 ? 34.409  14.835  92.623  1.00 54.34  ?  120 LYS   C N   1 
ATOM   8361  C CA  . LYS   C 1 120 ? 33.143  14.735  93.332  1.00 46.40  ?  120 LYS   C CA  1 
ATOM   8362  C C   . LYS   C 1 120 ? 32.533  13.350  93.113  1.00 44.96  ?  120 LYS   C C   1 
ATOM   8363  O O   . LYS   C 1 120 ? 33.133  12.466  92.491  1.00 44.61  ?  120 LYS   C O   1 
ATOM   8364  C CB  . LYS   C 1 120 ? 32.188  15.835  92.875  1.00 49.78  ?  120 LYS   C CB  1 
ATOM   8365  C CG  . LYS   C 1 120 ? 32.776  17.238  92.941  1.00 58.02  ?  120 LYS   C CG  1 
ATOM   8366  C CD  . LYS   C 1 120 ? 31.738  18.298  92.577  1.00 54.39  ?  120 LYS   C CD  1 
ATOM   8367  C CE  . LYS   C 1 120 ? 31.182  18.103  91.169  1.00 49.19  ?  120 LYS   C CE  1 
ATOM   8368  N NZ  . LYS   C 1 120 ? 32.221  18.207  90.100  1.00 48.92  ?  120 LYS   C NZ  1 
ATOM   8369  N N   . ALA   C 1 121 ? 31.321  13.162  93.643  1.00 38.80  ?  121 ALA   C N   1 
ATOM   8370  C CA  . ALA   C 1 121 ? 30.547  11.930  93.467  1.00 33.66  ?  121 ALA   C CA  1 
ATOM   8371  C C   . ALA   C 1 121 ? 31.329  10.694  93.914  1.00 36.02  ?  121 ALA   C C   1 
ATOM   8372  O O   . ALA   C 1 121 ? 31.253  9.629   93.293  1.00 34.71  ?  121 ALA   C O   1 
ATOM   8373  C CB  . ALA   C 1 121 ? 30.070  11.777  92.020  1.00 36.20  ?  121 ALA   C CB  1 
ATOM   8374  N N   . LYS   C 1 122 ? 32.075  10.829  95.012  1.00 30.64  ?  122 LYS   C N   1 
ATOM   8375  C CA  . LYS   C 1 122 ? 32.880  9.712   95.494  1.00 31.54  ?  122 LYS   C CA  1 
ATOM   8376  C C   . LYS   C 1 122 ? 32.021  8.602   96.080  1.00 34.67  ?  122 LYS   C C   1 
ATOM   8377  O O   . LYS   C 1 122 ? 32.432  7.437   96.071  1.00 35.39  ?  122 LYS   C O   1 
ATOM   8378  C CB  . LYS   C 1 122 ? 33.904  10.198  96.520  1.00 34.82  ?  122 LYS   C CB  1 
ATOM   8379  C CG  . LYS   C 1 122 ? 35.259  10.520  95.885  1.00 45.47  ?  122 LYS   C CG  1 
ATOM   8380  C CD  . LYS   C 1 122 ? 35.676  9.388   94.924  1.00 46.87  ?  122 LYS   C CD  1 
ATOM   8381  C CE  . LYS   C 1 122 ? 36.640  9.844   93.826  1.00 44.53  ?  122 LYS   C CE  1 
ATOM   8382  N NZ  . LYS   C 1 122 ? 37.936  10.358  94.357  1.00 37.50  ?  122 LYS   C NZ  1 
ATOM   8383  N N   . ASN   C 1 123 ? 30.839  8.937   96.596  1.00 37.00  ?  123 ASN   C N   1 
ATOM   8384  C CA  . ASN   C 1 123 ? 29.841  7.955   97.019  1.00 31.07  ?  123 ASN   C CA  1 
ATOM   8385  C C   . ASN   C 1 123 ? 28.522  8.328   96.358  1.00 30.89  ?  123 ASN   C C   1 
ATOM   8386  O O   . ASN   C 1 123 ? 27.591  8.792   97.026  1.00 25.96  ?  123 ASN   C O   1 
ATOM   8387  C CB  . ASN   C 1 123 ? 29.708  7.912   98.542  1.00 30.84  ?  123 ASN   C CB  1 
ATOM   8388  C CG  . ASN   C 1 123 ? 30.994  7.504   99.220  1.00 33.89  ?  123 ASN   C CG  1 
ATOM   8389  O OD1 . ASN   C 1 123 ? 31.730  8.342   99.742  1.00 35.15  ?  123 ASN   C OD1 1 
ATOM   8390  N ND2 . ASN   C 1 123 ? 31.278  6.208   99.208  1.00 33.40  ?  123 ASN   C ND2 1 
ATOM   8391  N N   . PRO   C 1 124 ? 28.410  8.124   95.042  1.00 27.73  ?  124 PRO   C N   1 
ATOM   8392  C CA  . PRO   C 1 124 ? 27.338  8.773   94.279  1.00 27.05  ?  124 PRO   C CA  1 
ATOM   8393  C C   . PRO   C 1 124 ? 25.984  8.117   94.509  1.00 23.93  ?  124 PRO   C C   1 
ATOM   8394  O O   . PRO   C 1 124 ? 25.888  6.922   94.794  1.00 27.49  ?  124 PRO   C O   1 
ATOM   8395  C CB  . PRO   C 1 124 ? 27.795  8.603   92.824  1.00 27.39  ?  124 PRO   C CB  1 
ATOM   8396  C CG  . PRO   C 1 124 ? 28.588  7.331   92.840  1.00 26.55  ?  124 PRO   C CG  1 
ATOM   8397  C CD  . PRO   C 1 124 ? 29.278  7.290   94.186  1.00 28.19  ?  124 PRO   C CD  1 
ATOM   8398  N N   . VAL   C 1 125 ? 24.921  8.919   94.386  1.00 25.69  ?  125 VAL   C N   1 
ATOM   8399  C CA  . VAL   C 1 125 ? 23.555  8.430   94.541  1.00 24.51  ?  125 VAL   C CA  1 
ATOM   8400  C C   . VAL   C 1 125 ? 22.647  9.153   93.552  1.00 24.81  ?  125 VAL   C C   1 
ATOM   8401  O O   . VAL   C 1 125 ? 22.951  10.251  93.075  1.00 21.01  ?  125 VAL   C O   1 
ATOM   8402  C CB  . VAL   C 1 125 ? 22.998  8.596   95.983  1.00 25.75  ?  125 VAL   C CB  1 
ATOM   8403  C CG1 . VAL   C 1 125 ? 23.869  7.883   97.020  1.00 26.52  ?  125 VAL   C CG1 1 
ATOM   8404  C CG2 . VAL   C 1 125 ? 22.834  10.064  96.346  1.00 28.87  ?  125 VAL   C CG2 1 
ATOM   8405  N N   . PHE   C 1 126 ? 21.525  8.505   93.235  1.00 21.06  ?  126 PHE   C N   1 
ATOM   8406  C CA  . PHE   C 1 126 ? 20.399  9.126   92.545  1.00 23.71  ?  126 PHE   C CA  1 
ATOM   8407  C C   . PHE   C 1 126 ? 19.212  9.167   93.498  1.00 25.04  ?  126 PHE   C C   1 
ATOM   8408  O O   . PHE   C 1 126 ? 18.972  8.210   94.245  1.00 22.69  ?  126 PHE   C O   1 
ATOM   8409  C CB  . PHE   C 1 126 ? 19.989  8.363   91.278  1.00 20.85  ?  126 PHE   C CB  1 
ATOM   8410  C CG  . PHE   C 1 126 ? 20.930  8.531   90.104  1.00 25.86  ?  126 PHE   C CG  1 
ATOM   8411  C CD1 . PHE   C 1 126 ? 22.207  8.004   90.135  1.00 24.85  ?  126 PHE   C CD1 1 
ATOM   8412  C CD2 . PHE   C 1 126 ? 20.503  9.160   88.941  1.00 26.42  ?  126 PHE   C CD2 1 
ATOM   8413  C CE1 . PHE   C 1 126 ? 23.055  8.137   89.048  1.00 27.96  ?  126 PHE   C CE1 1 
ATOM   8414  C CE2 . PHE   C 1 126 ? 21.347  9.290   87.848  1.00 25.37  ?  126 PHE   C CE2 1 
ATOM   8415  C CZ  . PHE   C 1 126 ? 22.622  8.777   87.900  1.00 25.12  ?  126 PHE   C CZ  1 
ATOM   8416  N N   . ILE   C 1 127 ? 18.472  10.273  93.468  1.00 22.30  ?  127 ILE   C N   1 
ATOM   8417  C CA  . ILE   C 1 127 ? 17.319  10.488  94.336  1.00 24.82  ?  127 ILE   C CA  1 
ATOM   8418  C C   . ILE   C 1 127 ? 16.088  10.644  93.453  1.00 27.76  ?  127 ILE   C C   1 
ATOM   8419  O O   . ILE   C 1 127 ? 16.118  11.382  92.461  1.00 28.26  ?  127 ILE   C O   1 
ATOM   8420  C CB  . ILE   C 1 127 ? 17.515  11.721  95.240  1.00 26.86  ?  127 ILE   C CB  1 
ATOM   8421  C CG1 . ILE   C 1 127 ? 18.710  11.513  96.173  1.00 27.93  ?  127 ILE   C CG1 1 
ATOM   8422  C CG2 . ILE   C 1 127 ? 16.270  12.013  96.053  1.00 21.83  ?  127 ILE   C CG2 1 
ATOM   8423  C CD1 . ILE   C 1 127 ? 18.928  12.659  97.150  1.00 26.53  ?  127 ILE   C CD1 1 
ATOM   8424  N N   . SER   C 1 128 ? 15.014  9.940   93.802  1.00 24.73  ?  128 SER   C N   1 
ATOM   8425  C CA  . SER   C 1 128 ? 13.790  9.974   93.014  1.00 26.19  ?  128 SER   C CA  1 
ATOM   8426  C C   . SER   C 1 128 ? 12.606  9.956   93.957  1.00 23.06  ?  128 SER   C C   1 
ATOM   8427  O O   . SER   C 1 128 ? 12.707  9.487   95.093  1.00 24.30  ?  128 SER   C O   1 
ATOM   8428  C CB  . SER   C 1 128 ? 13.686  8.782   92.046  1.00 20.55  ?  128 SER   C CB  1 
ATOM   8429  O OG  . SER   C 1 128 ? 12.515  8.864   91.238  1.00 21.54  ?  128 SER   C OG  1 
ATOM   8430  N N   . ASN   C 1 129 ? 11.470  10.467  93.477  1.00 26.30  ?  129 ASN   C N   1 
ATOM   8431  C CA  . ASN   C 1 129 ? 10.225  10.167  94.170  1.00 25.48  ?  129 ASN   C CA  1 
ATOM   8432  C C   . ASN   C 1 129 ? 10.007  8.660   94.203  1.00 23.02  ?  129 ASN   C C   1 
ATOM   8433  O O   . ASN   C 1 129 ? 9.661   8.102   95.251  1.00 26.28  ?  129 ASN   C O   1 
ATOM   8434  C CB  . ASN   C 1 129 ? 9.041   10.919  93.540  1.00 22.06  ?  129 ASN   C CB  1 
ATOM   8435  C CG  . ASN   C 1 129 ? 8.888   10.682  92.048  1.00 24.11  ?  129 ASN   C CG  1 
ATOM   8436  O OD1 . ASN   C 1 129 ? 9.852   10.408  91.330  1.00 26.38  ?  129 ASN   C OD1 1 
ATOM   8437  N ND2 . ASN   C 1 129 ? 7.662   10.824  91.565  1.00 21.68  ?  129 ASN   C ND2 1 
ATOM   8438  N N   . PHE   C 1 130 ? 10.272  7.980   93.085  1.00 23.06  ?  130 PHE   C N   1 
ATOM   8439  C CA  . PHE   C 1 130 ? 10.459  6.532   93.069  1.00 25.56  ?  130 PHE   C CA  1 
ATOM   8440  C C   . PHE   C 1 130 ? 11.071  6.074   91.747  1.00 26.80  ?  130 PHE   C C   1 
ATOM   8441  O O   . PHE   C 1 130 ? 10.490  6.284   90.675  1.00 23.76  ?  130 PHE   C O   1 
ATOM   8442  C CB  . PHE   C 1 130 ? 9.139   5.799   93.324  1.00 25.07  ?  130 PHE   C CB  1 
ATOM   8443  C CG  . PHE   C 1 130 ? 9.297   4.527   94.113  1.00 25.69  ?  130 PHE   C CG  1 
ATOM   8444  C CD1 . PHE   C 1 130 ? 9.935   3.426   93.557  1.00 27.82  ?  130 PHE   C CD1 1 
ATOM   8445  C CD2 . PHE   C 1 130 ? 8.812   4.433   95.403  1.00 30.69  ?  130 PHE   C CD2 1 
ATOM   8446  C CE1 . PHE   C 1 130 ? 10.077  2.252   94.276  1.00 23.79  ?  130 PHE   C CE1 1 
ATOM   8447  C CE2 . PHE   C 1 130 ? 8.958   3.257   96.138  1.00 32.20  ?  130 PHE   C CE2 1 
ATOM   8448  C CZ  . PHE   C 1 130 ? 9.593   2.167   95.568  1.00 27.73  ?  130 PHE   C CZ  1 
ATOM   8449  N N   . HIS   C 1 131 ? 12.246  5.447   91.820  1.00 25.10  ?  131 HIS   C N   1 
ATOM   8450  C CA  . HIS   C 1 131 ? 12.909  4.903   90.639  1.00 25.89  ?  131 HIS   C CA  1 
ATOM   8451  C C   . HIS   C 1 131 ? 12.190  3.656   90.149  1.00 24.08  ?  131 HIS   C C   1 
ATOM   8452  O O   . HIS   C 1 131 ? 11.952  2.725   90.924  1.00 22.66  ?  131 HIS   C O   1 
ATOM   8453  C CB  . HIS   C 1 131 ? 14.360  4.516   90.952  1.00 23.58  ?  131 HIS   C CB  1 
ATOM   8454  C CG  . HIS   C 1 131 ? 15.298  5.670   91.129  1.00 25.95  ?  131 HIS   C CG  1 
ATOM   8455  N ND1 . HIS   C 1 131 ? 15.799  6.037   92.361  1.00 23.39  ?  131 HIS   C ND1 1 
ATOM   8456  C CD2 . HIS   C 1 131 ? 15.875  6.498   90.226  1.00 23.23  ?  131 HIS   C CD2 1 
ATOM   8457  C CE1 . HIS   C 1 131 ? 16.625  7.057   92.210  1.00 24.93  ?  131 HIS   C CE1 1 
ATOM   8458  N NE2 . HIS   C 1 131 ? 16.693  7.352   90.924  1.00 23.59  ?  131 HIS   C NE2 1 
ATOM   8459  N N   A PHE   C 1 132 ? 11.863  3.606   88.859  0.48 25.76  ?  132 PHE   C N   1 
ATOM   8460  N N   B PHE   C 1 132 ? 11.873  3.640   88.855  0.52 25.76  ?  132 PHE   C N   1 
ATOM   8461  C CA  A PHE   C 1 132 ? 11.281  2.364   88.375  0.48 25.36  ?  132 PHE   C CA  1 
ATOM   8462  C CA  B PHE   C 1 132 ? 11.348  2.455   88.205  0.52 25.32  ?  132 PHE   C CA  1 
ATOM   8463  C C   A PHE   C 1 132 ? 12.386  1.347   88.076  0.48 23.64  ?  132 PHE   C C   1 
ATOM   8464  C C   B PHE   C 1 132 ? 12.396  1.337   88.234  0.52 23.62  ?  132 PHE   C C   1 
ATOM   8465  O O   A PHE   C 1 132 ? 13.574  1.675   88.041  0.48 23.43  ?  132 PHE   C O   1 
ATOM   8466  O O   B PHE   C 1 132 ? 13.556  1.546   88.589  0.52 23.83  ?  132 PHE   C O   1 
ATOM   8467  C CB  A PHE   C 1 132 ? 10.397  2.606   87.154  0.48 25.41  ?  132 PHE   C CB  1 
ATOM   8468  C CB  B PHE   C 1 132 ? 10.926  2.793   86.774  0.52 24.92  ?  132 PHE   C CB  1 
ATOM   8469  C CG  A PHE   C 1 132 ? 9.424   1.488   86.898  0.48 26.92  ?  132 PHE   C CG  1 
ATOM   8470  C CG  B PHE   C 1 132 ? 10.288  1.650   86.049  0.52 27.44  ?  132 PHE   C CG  1 
ATOM   8471  C CD1 A PHE   C 1 132 ? 8.616   1.016   87.919  0.48 26.35  ?  132 PHE   C CD1 1 
ATOM   8472  C CD1 B PHE   C 1 132 ? 9.100   1.103   86.509  0.52 27.43  ?  132 PHE   C CD1 1 
ATOM   8473  C CD2 A PHE   C 1 132 ? 9.329   0.900   85.646  0.48 27.82  ?  132 PHE   C CD2 1 
ATOM   8474  C CD2 B PHE   C 1 132 ? 10.881  1.111   84.919  0.52 25.27  ?  132 PHE   C CD2 1 
ATOM   8475  C CE1 A PHE   C 1 132 ? 7.726   -0.017  87.704  0.48 26.83  ?  132 PHE   C CE1 1 
ATOM   8476  C CE1 B PHE   C 1 132 ? 8.517   0.045   85.852  0.52 29.03  ?  132 PHE   C CE1 1 
ATOM   8477  C CE2 A PHE   C 1 132 ? 8.440   -0.135  85.422  0.48 29.60  ?  132 PHE   C CE2 1 
ATOM   8478  C CE2 B PHE   C 1 132 ? 10.303  0.055   84.260  0.52 26.28  ?  132 PHE   C CE2 1 
ATOM   8479  C CZ  A PHE   C 1 132 ? 7.636   -0.594  86.453  0.48 29.56  ?  132 PHE   C CZ  1 
ATOM   8480  C CZ  B PHE   C 1 132 ? 9.119   -0.478  84.724  0.52 29.20  ?  132 PHE   C CZ  1 
ATOM   8481  N N   A ASP   C 1 133 ? 11.974  0.095   87.847  0.48 22.29  ?  133 ASP   C N   1 
ATOM   8482  N N   B ASP   C 1 133 ? 11.964  0.128   87.866  0.52 22.27  ?  133 ASP   C N   1 
ATOM   8483  C CA  A ASP   C 1 133 ? 12.899  -1.031  87.964  0.48 24.48  ?  133 ASP   C CA  1 
ATOM   8484  C CA  B ASP   C 1 133 ? 12.851  -1.030  87.933  0.52 24.47  ?  133 ASP   C CA  1 
ATOM   8485  C C   A ASP   C 1 133 ? 14.109  -0.879  87.043  0.48 24.36  ?  133 ASP   C C   1 
ATOM   8486  C C   B ASP   C 1 133 ? 14.086  -0.837  87.057  0.52 24.36  ?  133 ASP   C C   1 
ATOM   8487  O O   A ASP   C 1 133 ? 15.251  -1.071  87.478  0.48 22.81  ?  133 ASP   C O   1 
ATOM   8488  O O   B ASP   C 1 133 ? 15.221  -0.963  87.534  0.52 22.79  ?  133 ASP   C O   1 
ATOM   8489  C CB  A ASP   C 1 133 ? 12.165  -2.352  87.705  0.48 26.00  ?  133 ASP   C CB  1 
ATOM   8490  C CB  B ASP   C 1 133 ? 12.090  -2.297  87.537  0.52 26.09  ?  133 ASP   C CB  1 
ATOM   8491  C CG  A ASP   C 1 133 ? 11.664  -2.483  86.282  0.48 28.97  ?  133 ASP   C CG  1 
ATOM   8492  C CG  B ASP   C 1 133 ? 10.926  -2.592  88.466  0.52 29.14  ?  133 ASP   C CG  1 
ATOM   8493  O OD1 A ASP   C 1 133 ? 11.290  -1.454  85.679  0.48 25.81  ?  133 ASP   C OD1 1 
ATOM   8494  O OD1 B ASP   C 1 133 ? 9.931   -1.839  88.429  0.52 29.24  ?  133 ASP   C OD1 1 
ATOM   8495  O OD2 A ASP   C 1 133 ? 11.656  -3.622  85.766  0.48 31.57  ?  133 ASP   C OD2 1 
ATOM   8496  O OD2 B ASP   C 1 133 ? 11.005  -3.571  89.238  0.52 35.21  ?  133 ASP   C OD2 1 
ATOM   8497  N N   . THR   C 1 134 ? 13.888  -0.523  85.771  1.00 22.98  ?  134 THR   C N   1 
ATOM   8498  C CA  . THR   C 1 134 ? 15.033  -0.326  84.877  1.00 20.91  ?  134 THR   C CA  1 
ATOM   8499  C C   . THR   C 1 134 ? 15.812  0.928   85.240  1.00 22.56  ?  134 THR   C C   1 
ATOM   8500  O O   . THR   C 1 134 ? 17.042  0.956   85.096  1.00 20.72  ?  134 THR   C O   1 
ATOM   8501  C CB  . THR   C 1 134 ? 14.598  -0.234  83.411  1.00 19.37  ?  134 THR   C CB  1 
ATOM   8502  O OG1 . THR   C 1 134 ? 13.920  1.015   83.187  1.00 19.20  ?  134 THR   C OG1 1 
ATOM   8503  C CG2 . THR   C 1 134 ? 13.685  -1.396  83.045  1.00 20.90  ?  134 THR   C CG2 1 
ATOM   8504  N N   . THR   C 1 135 ? 15.115  1.970   85.702  1.00 24.15  ?  135 THR   C N   1 
ATOM   8505  C CA  . THR   C 1 135 ? 15.785  3.197   86.120  1.00 23.70  ?  135 THR   C CA  1 
ATOM   8506  C C   . THR   C 1 135 ? 16.765  2.925   87.257  1.00 22.85  ?  135 THR   C C   1 
ATOM   8507  O O   . THR   C 1 135 ? 17.939  3.306   87.184  1.00 24.24  ?  135 THR   C O   1 
ATOM   8508  C CB  . THR   C 1 135 ? 14.747  4.239   86.543  1.00 24.90  ?  135 THR   C CB  1 
ATOM   8509  O OG1 . THR   C 1 135 ? 13.672  4.271   85.590  1.00 23.55  ?  135 THR   C OG1 1 
ATOM   8510  C CG2 . THR   C 1 135 ? 15.387  5.609   86.640  1.00 23.16  ?  135 THR   C CG2 1 
ATOM   8511  N N   . ALA   C 1 136 ? 16.295  2.270   88.326  1.00 21.85  ?  136 ALA   C N   1 
ATOM   8512  C CA  . ALA   C 1 136 ? 17.170  1.944   89.449  1.00 23.50  ?  136 ALA   C CA  1 
ATOM   8513  C C   . ALA   C 1 136 ? 18.255  0.952   89.052  1.00 25.13  ?  136 ALA   C C   1 
ATOM   8514  O O   . ALA   C 1 136 ? 19.378  1.021   89.571  1.00 23.92  ?  136 ALA   C O   1 
ATOM   8515  C CB  . ALA   C 1 136 ? 16.357  1.383   90.615  1.00 24.07  ?  136 ALA   C CB  1 
ATOM   8516  N N   . ALA   C 1 137 ? 17.941  0.024   88.148  1.00 20.11  ?  137 ALA   C N   1 
ATOM   8517  C CA  . ALA   C 1 137 ? 18.940  -0.939  87.708  1.00 22.63  ?  137 ALA   C CA  1 
ATOM   8518  C C   . ALA   C 1 137 ? 20.128  -0.233  87.065  1.00 22.53  ?  137 ALA   C C   1 
ATOM   8519  O O   . ALA   C 1 137 ? 21.284  -0.573  87.337  1.00 20.77  ?  137 ALA   C O   1 
ATOM   8520  C CB  . ALA   C 1 137 ? 18.311  -1.938  86.740  1.00 23.00  ?  137 ALA   C CB  1 
ATOM   8521  N N   . HIS   C 1 138 ? 19.860  0.764   86.224  1.00 23.40  ?  138 HIS   C N   1 
ATOM   8522  C CA  . HIS   C 1 138 ? 20.947  1.500   85.590  1.00 22.19  ?  138 HIS   C CA  1 
ATOM   8523  C C   . HIS   C 1 138 ? 21.698  2.357   86.595  1.00 26.59  ?  138 HIS   C C   1 
ATOM   8524  O O   . HIS   C 1 138 ? 22.923  2.509   86.498  1.00 26.10  ?  138 HIS   C O   1 
ATOM   8525  C CB  . HIS   C 1 138 ? 20.395  2.353   84.455  1.00 23.08  ?  138 HIS   C CB  1 
ATOM   8526  C CG  . HIS   C 1 138 ? 20.189  1.586   83.192  1.00 21.46  ?  138 HIS   C CG  1 
ATOM   8527  N ND1 . HIS   C 1 138 ? 21.220  0.939   82.548  1.00 19.34  ?  138 HIS   C ND1 1 
ATOM   8528  C CD2 . HIS   C 1 138 ? 19.074  1.336   82.468  1.00 19.68  ?  138 HIS   C CD2 1 
ATOM   8529  C CE1 . HIS   C 1 138 ? 20.754  0.342   81.466  1.00 18.91  ?  138 HIS   C CE1 1 
ATOM   8530  N NE2 . HIS   C 1 138 ? 19.454  0.565   81.397  1.00 20.15  ?  138 HIS   C NE2 1 
ATOM   8531  N N   . VAL   C 1 139 ? 20.985  2.943   87.555  1.00 19.75  ?  139 VAL   C N   1 
ATOM   8532  C CA  . VAL   C 1 139 ? 21.662  3.617   88.656  1.00 24.41  ?  139 VAL   C CA  1 
ATOM   8533  C C   . VAL   C 1 139 ? 22.607  2.646   89.353  1.00 23.00  ?  139 VAL   C C   1 
ATOM   8534  O O   . VAL   C 1 139 ? 23.805  2.915   89.506  1.00 24.31  ?  139 VAL   C O   1 
ATOM   8535  C CB  . VAL   C 1 139 ? 20.632  4.224   89.624  1.00 24.28  ?  139 VAL   C CB  1 
ATOM   8536  C CG1 . VAL   C 1 139 ? 21.285  4.615   90.927  1.00 22.59  ?  139 VAL   C CG1 1 
ATOM   8537  C CG2 . VAL   C 1 139 ? 19.959  5.436   88.986  1.00 20.02  ?  139 VAL   C CG2 1 
ATOM   8538  N N   . GLU   C 1 140 ? 22.097  1.475   89.731  1.00 24.05  ?  140 GLU   C N   1 
ATOM   8539  C CA  . GLU   C 1 140 ? 22.932  0.503   90.430  1.00 25.13  ?  140 GLU   C CA  1 
ATOM   8540  C C   . GLU   C 1 140 ? 24.045  -0.028  89.529  1.00 29.33  ?  140 GLU   C C   1 
ATOM   8541  O O   . GLU   C 1 140 ? 25.184  -0.206  89.979  1.00 29.74  ?  140 GLU   C O   1 
ATOM   8542  C CB  . GLU   C 1 140 ? 22.056  -0.628  90.969  1.00 26.19  ?  140 GLU   C CB  1 
ATOM   8543  C CG  . GLU   C 1 140 ? 21.132  -0.155  92.091  1.00 25.79  ?  140 GLU   C CG  1 
ATOM   8544  C CD  . GLU   C 1 140 ? 20.014  -1.136  92.451  1.00 33.55  ?  140 GLU   C CD  1 
ATOM   8545  O OE1 . GLU   C 1 140 ? 19.800  -2.131  91.718  1.00 35.14  ?  140 GLU   C OE1 1 
ATOM   8546  O OE2 . GLU   C 1 140 ? 19.342  -0.898  93.481  1.00 35.25  ?  140 GLU   C OE2 1 
ATOM   8547  N N   . LEU   C 1 141 ? 23.738  -0.266  88.253  1.00 27.17  ?  141 LEU   C N   1 
ATOM   8548  C CA  . LEU   C 1 141 ? 24.748  -0.737  87.314  1.00 28.57  ?  141 LEU   C CA  1 
ATOM   8549  C C   . LEU   C 1 141 ? 25.943  0.208   87.259  1.00 26.65  ?  141 LEU   C C   1 
ATOM   8550  O O   . LEU   C 1 141 ? 27.085  -0.239  87.114  1.00 25.48  ?  141 LEU   C O   1 
ATOM   8551  C CB  . LEU   C 1 141 ? 24.107  -0.899  85.934  1.00 27.62  ?  141 LEU   C CB  1 
ATOM   8552  C CG  . LEU   C 1 141 ? 24.569  -1.976  84.957  1.00 30.58  ?  141 LEU   C CG  1 
ATOM   8553  C CD1 . LEU   C 1 141 ? 25.108  -3.186  85.686  1.00 29.26  ?  141 LEU   C CD1 1 
ATOM   8554  C CD2 . LEU   C 1 141 ? 23.390  -2.373  84.095  1.00 29.60  ?  141 LEU   C CD2 1 
ATOM   8555  N N   . ASN   C 1 142 ? 25.711  1.509   87.415  1.00 26.11  ?  142 ASN   C N   1 
ATOM   8556  C CA  . ASN   C 1 142 ? 26.775  2.498   87.342  1.00 27.77  ?  142 ASN   C CA  1 
ATOM   8557  C C   . ASN   C 1 142 ? 27.392  2.820   88.705  1.00 29.03  ?  142 ASN   C C   1 
ATOM   8558  O O   . ASN   C 1 142 ? 28.002  3.883   88.863  1.00 30.72  ?  142 ASN   C O   1 
ATOM   8559  C CB  . ASN   C 1 142 ? 26.256  3.772   86.674  1.00 25.52  ?  142 ASN   C CB  1 
ATOM   8560  C CG  . ASN   C 1 142 ? 26.134  3.630   85.169  1.00 27.00  ?  142 ASN   C CG  1 
ATOM   8561  O OD1 . ASN   C 1 142 ? 27.118  3.783   84.440  1.00 27.83  ?  142 ASN   C OD1 1 
ATOM   8562  N ND2 . ASN   C 1 142 ? 24.925  3.335   84.693  1.00 23.22  ?  142 ASN   C ND2 1 
ATOM   8563  N N   . GLY   C 1 143 ? 27.263  1.926   89.684  1.00 23.00  ?  143 GLY   C N   1 
ATOM   8564  C CA  . GLY   C 1 143 ? 27.939  2.118   90.953  1.00 25.96  ?  143 GLY   C CA  1 
ATOM   8565  C C   . GLY   C 1 143 ? 27.310  3.133   91.874  1.00 26.98  ?  143 GLY   C C   1 
ATOM   8566  O O   . GLY   C 1 143 ? 27.976  3.599   92.806  1.00 29.11  ?  143 GLY   C O   1 
ATOM   8567  N N   . CYS   C 1 144 ? 26.048  3.489   91.649  1.00 26.62  ?  144 CYS   C N   1 
ATOM   8568  C CA  . CYS   C 1 144 ? 25.330  4.462   92.460  1.00 23.26  ?  144 CYS   C CA  1 
ATOM   8569  C C   . CYS   C 1 144 ? 24.208  3.785   93.234  1.00 29.63  ?  144 CYS   C C   1 
ATOM   8570  O O   . CYS   C 1 144 ? 23.827  2.642   92.964  1.00 29.07  ?  144 CYS   C O   1 
ATOM   8571  C CB  . CYS   C 1 144 ? 24.751  5.585   91.592  1.00 24.91  ?  144 CYS   C CB  1 
ATOM   8572  S SG  . CYS   C 1 144 ? 25.924  6.397   90.491  1.00 27.63  ?  144 CYS   C SG  1 
ATOM   8573  N N   . LYS   C 1 145 ? 23.674  4.521   94.203  1.00 24.99  ?  145 LYS   C N   1 
ATOM   8574  C CA  . LYS   C 1 145 ? 22.539  4.087   95.002  1.00 28.81  ?  145 LYS   C CA  1 
ATOM   8575  C C   . LYS   C 1 145 ? 21.271  4.771   94.497  1.00 27.02  ?  145 LYS   C C   1 
ATOM   8576  O O   . LYS   C 1 145 ? 21.283  5.963   94.170  1.00 26.67  ?  145 LYS   C O   1 
ATOM   8577  C CB  . LYS   C 1 145 ? 22.775  4.409   96.485  1.00 29.32  ?  145 LYS   C CB  1 
ATOM   8578  C CG  . LYS   C 1 145 ? 21.661  3.956   97.431  1.00 35.16  ?  145 LYS   C CG  1 
ATOM   8579  C CD  . LYS   C 1 145 ? 21.941  4.341   98.893  1.00 39.58  ?  145 LYS   C CD  1 
ATOM   8580  C CE  . LYS   C 1 145 ? 22.810  3.306   99.623  1.00 48.77  ?  145 LYS   C CE  1 
ATOM   8581  N NZ  . LYS   C 1 145 ? 24.231  3.216   99.144  1.00 38.49  ?  145 LYS   C NZ  1 
ATOM   8582  N N   . ALA   C 1 146 ? 20.186  4.004   94.408  1.00 24.37  ?  146 ALA   C N   1 
ATOM   8583  C CA  . ALA   C 1 146 ? 18.888  4.515   93.976  1.00 23.43  ?  146 ALA   C CA  1 
ATOM   8584  C C   . ALA   C 1 146 ? 18.048  4.776   95.219  1.00 25.29  ?  146 ALA   C C   1 
ATOM   8585  O O   . ALA   C 1 146 ? 17.635  3.836   95.904  1.00 33.95  ?  146 ALA   C O   1 
ATOM   8586  C CB  . ALA   C 1 146 ? 18.193  3.529   93.040  1.00 21.46  ?  146 ALA   C CB  1 
ATOM   8587  N N   . ILE   C 1 147 ? 17.802  6.047   95.519  1.00 26.91  ?  147 ILE   C N   1 
ATOM   8588  C CA  . ILE   C 1 147 ? 17.101  6.452   96.734  1.00 26.85  ?  147 ILE   C CA  1 
ATOM   8589  C C   . ILE   C 1 147 ? 15.700  6.918   96.357  1.00 24.51  ?  147 ILE   C C   1 
ATOM   8590  O O   . ILE   C 1 147 ? 15.537  7.788   95.490  1.00 24.59  ?  147 ILE   C O   1 
ATOM   8591  C CB  . ILE   C 1 147 ? 17.875  7.551   97.477  1.00 26.87  ?  147 ILE   C CB  1 
ATOM   8592  C CG1 . ILE   C 1 147 ? 19.297  7.067   97.780  1.00 26.60  ?  147 ILE   C CG1 1 
ATOM   8593  C CG2 . ILE   C 1 147 ? 17.140  7.953   98.749  1.00 31.17  ?  147 ILE   C CG2 1 
ATOM   8594  C CD1 . ILE   C 1 147 ? 20.214  8.136   98.315  1.00 29.15  ?  147 ILE   C CD1 1 
ATOM   8595  N N   . ASN   C 1 148 ? 14.691  6.325   96.996  1.00 30.02  ?  148 ASN   C N   1 
ATOM   8596  C CA  . ASN   C 1 148 ? 13.285  6.619   96.737  1.00 25.70  ?  148 ASN   C CA  1 
ATOM   8597  C C   . ASN   C 1 148 ? 12.694  7.360   97.928  1.00 29.25  ?  148 ASN   C C   1 
ATOM   8598  O O   . ASN   C 1 148 ? 12.818  6.902   99.070  1.00 25.09  ?  148 ASN   C O   1 
ATOM   8599  C CB  . ASN   C 1 148 ? 12.496  5.333   96.487  1.00 24.79  ?  148 ASN   C CB  1 
ATOM   8600  C CG  . ASN   C 1 148 ? 13.036  4.544   95.324  1.00 26.74  ?  148 ASN   C CG  1 
ATOM   8601  O OD1 . ASN   C 1 148 ? 13.322  5.101   94.272  1.00 26.78  ?  148 ASN   C OD1 1 
ATOM   8602  N ND2 . ASN   C 1 148 ? 13.187  3.238   95.508  1.00 27.47  ?  148 ASN   C ND2 1 
ATOM   8603  N N   . ILE   C 1 149 ? 12.051  8.498   97.667  1.00 26.35  ?  149 ILE   C N   1 
ATOM   8604  C CA  . ILE   C 1 149 ? 11.503  9.305   98.750  1.00 27.46  ?  149 ILE   C CA  1 
ATOM   8605  C C   . ILE   C 1 149 ? 10.086  9.757   98.423  1.00 26.83  ?  149 ILE   C C   1 
ATOM   8606  O O   . ILE   C 1 149 ? 9.730   10.920  98.645  1.00 31.93  ?  149 ILE   C O   1 
ATOM   8607  C CB  . ILE   C 1 149 ? 12.410  10.512  99.063  1.00 25.10  ?  149 ILE   C CB  1 
ATOM   8608  C CG1 . ILE   C 1 149 ? 12.714  11.305  97.798  1.00 28.45  ?  149 ILE   C CG1 1 
ATOM   8609  C CG2 . ILE   C 1 149 ? 13.711  10.063  99.727  1.00 24.30  ?  149 ILE   C CG2 1 
ATOM   8610  C CD1 . ILE   C 1 149 ? 13.352  12.640  98.071  1.00 25.43  ?  149 ILE   C CD1 1 
ATOM   8611  N N   . VAL   C 1 150 ? 9.255   8.839   97.922  1.00 29.05  ?  150 VAL   C N   1 
ATOM   8612  C CA  . VAL   C 1 150 ? 7.855   9.168   97.686  1.00 28.60  ?  150 VAL   C CA  1 
ATOM   8613  C C   . VAL   C 1 150 ? 7.206   9.621   98.993  1.00 27.90  ?  150 VAL   C C   1 
ATOM   8614  O O   . VAL   C 1 150 ? 7.624   9.238   100.094 1.00 31.43  ?  150 VAL   C O   1 
ATOM   8615  C CB  . VAL   C 1 150 ? 7.091   7.975   97.084  1.00 26.66  ?  150 VAL   C CB  1 
ATOM   8616  C CG1 . VAL   C 1 150 ? 6.759   6.954   98.157  1.00 28.71  ?  150 VAL   C CG1 1 
ATOM   8617  C CG2 . VAL   C 1 150 ? 5.828   8.442   96.395  1.00 26.72  ?  150 VAL   C CG2 1 
ATOM   8618  N N   . THR   C 1 151 ? 6.187   10.464  98.867  1.00 31.98  ?  151 THR   C N   1 
ATOM   8619  C CA  . THR   C 1 151 ? 5.412   10.882  100.024 1.00 31.67  ?  151 THR   C CA  1 
ATOM   8620  C C   . THR   C 1 151 ? 4.836   9.673   100.751 1.00 31.94  ?  151 THR   C C   1 
ATOM   8621  O O   . THR   C 1 151 ? 4.457   8.675   100.131 1.00 32.63  ?  151 THR   C O   1 
ATOM   8622  C CB  . THR   C 1 151 ? 4.282   11.806  99.586  1.00 29.15  ?  151 THR   C CB  1 
ATOM   8623  O OG1 . THR   C 1 151 ? 3.451   12.101  100.713 1.00 36.90  ?  151 THR   C OG1 1 
ATOM   8624  C CG2 . THR   C 1 151 ? 3.457   11.135  98.512  1.00 32.17  ?  151 THR   C CG2 1 
ATOM   8625  N N   . GLU   C 1 152 ? 4.779   9.769   102.081 1.00 31.21  ?  152 GLU   C N   1 
ATOM   8626  C CA  . GLU   C 1 152 ? 4.164   8.729   102.898 1.00 35.28  ?  152 GLU   C CA  1 
ATOM   8627  C C   . GLU   C 1 152 ? 2.687   8.513   102.563 1.00 35.73  ?  152 GLU   C C   1 
ATOM   8628  O O   . GLU   C 1 152 ? 2.137   7.453   102.886 1.00 34.61  ?  152 GLU   C O   1 
ATOM   8629  C CB  . GLU   C 1 152 ? 4.308   9.083   104.378 1.00 36.78  ?  152 GLU   C CB  1 
ATOM   8630  C CG  . GLU   C 1 152 ? 3.598   10.392  104.757 1.00 46.46  ?  152 GLU   C CG  1 
ATOM   8631  C CD  . GLU   C 1 152 ? 3.537   10.644  106.260 1.00 57.18  ?  152 GLU   C CD  1 
ATOM   8632  O OE1 . GLU   C 1 152 ? 4.003   9.783   107.039 1.00 67.45  ?  152 GLU   C OE1 1 
ATOM   8633  O OE2 . GLU   C 1 152 ? 3.018   11.710  106.663 1.00 62.15  ?  152 GLU   C OE2 1 
ATOM   8634  N N   . LYS   C 1 153 ? 2.026   9.489   101.934 1.00 36.27  ?  153 LYS   C N   1 
ATOM   8635  C CA  . LYS   C 1 153 ? 0.629   9.299   101.555 1.00 34.51  ?  153 LYS   C CA  1 
ATOM   8636  C C   . LYS   C 1 153 ? 0.457   8.122   100.606 1.00 33.04  ?  153 LYS   C C   1 
ATOM   8637  O O   . LYS   C 1 153 ? -0.624  7.526   100.550 1.00 34.26  ?  153 LYS   C O   1 
ATOM   8638  C CB  . LYS   C 1 153 ? 0.075   10.566  100.903 1.00 35.61  ?  153 LYS   C CB  1 
ATOM   8639  C CG  . LYS   C 1 153 ? 0.189   11.819  101.754 1.00 38.39  ?  153 LYS   C CG  1 
ATOM   8640  C CD  . LYS   C 1 153 ? -0.605  11.692  103.035 1.00 46.56  ?  153 LYS   C CD  1 
ATOM   8641  C CE  . LYS   C 1 153 ? -0.729  13.039  103.741 1.00 56.48  ?  153 LYS   C CE  1 
ATOM   8642  N NZ  . LYS   C 1 153 ? -1.449  14.040  102.898 1.00 55.83  ?  153 LYS   C NZ  1 
ATOM   8643  N N   . ALA   C 1 154 ? 1.498   7.778   99.844  1.00 34.98  ?  154 ALA   C N   1 
ATOM   8644  C CA  . ALA   C 1 154 ? 1.384   6.695   98.874  1.00 33.70  ?  154 ALA   C CA  1 
ATOM   8645  C C   . ALA   C 1 154 ? 1.274   5.333   99.541  1.00 39.02  ?  154 ALA   C C   1 
ATOM   8646  O O   . ALA   C 1 154 ? 0.774   4.389   98.921  1.00 39.47  ?  154 ALA   C O   1 
ATOM   8647  C CB  . ALA   C 1 154 ? 2.580   6.703   97.923  1.00 29.42  ?  154 ALA   C CB  1 
ATOM   8648  N N   . PHE   C 1 155 ? 1.725   5.212   100.787 1.00 36.55  ?  155 PHE   C N   1 
ATOM   8649  C CA  . PHE   C 1 155 ? 1.690   3.943   101.497 1.00 38.30  ?  155 PHE   C CA  1 
ATOM   8650  C C   . PHE   C 1 155 ? 0.353   3.673   102.172 1.00 39.90  ?  155 PHE   C C   1 
ATOM   8651  O O   . PHE   C 1 155 ? 0.106   2.541   102.595 1.00 43.92  ?  155 PHE   C O   1 
ATOM   8652  C CB  . PHE   C 1 155 ? 2.820   3.910   102.523 1.00 40.02  ?  155 PHE   C CB  1 
ATOM   8653  C CG  . PHE   C 1 155 ? 4.190   4.008   101.906 1.00 43.89  ?  155 PHE   C CG  1 
ATOM   8654  C CD1 . PHE   C 1 155 ? 4.561   3.149   100.879 1.00 46.38  ?  155 PHE   C CD1 1 
ATOM   8655  C CD2 . PHE   C 1 155 ? 5.093   4.973   102.328 1.00 41.80  ?  155 PHE   C CD2 1 
ATOM   8656  C CE1 . PHE   C 1 155 ? 5.821   3.236   100.297 1.00 53.23  ?  155 PHE   C CE1 1 
ATOM   8657  C CE2 . PHE   C 1 155 ? 6.356   5.069   101.752 1.00 41.45  ?  155 PHE   C CE2 1 
ATOM   8658  C CZ  . PHE   C 1 155 ? 6.719   4.201   100.736 1.00 50.29  ?  155 PHE   C CZ  1 
ATOM   8659  N N   . ASP   C 1 156 ? -0.514  4.674   102.275 1.00 39.06  ?  156 ASP   C N   1 
ATOM   8660  C CA  . ASP   C 1 156 ? -1.849  4.499   102.841 1.00 34.75  ?  156 ASP   C CA  1 
ATOM   8661  C C   . ASP   C 1 156 ? -2.785  4.198   101.677 1.00 38.32  ?  156 ASP   C C   1 
ATOM   8662  O O   . ASP   C 1 156 ? -3.361  5.097   101.057 1.00 31.41  ?  156 ASP   C O   1 
ATOM   8663  C CB  . ASP   C 1 156 ? -2.263  5.737   103.621 1.00 34.81  ?  156 ASP   C CB  1 
ATOM   8664  C CG  . ASP   C 1 156 ? -3.423  5.474   104.549 1.00 49.12  ?  156 ASP   C CG  1 
ATOM   8665  O OD1 . ASP   C 1 156 ? -4.124  4.456   104.352 1.00 48.88  ?  156 ASP   C OD1 1 
ATOM   8666  O OD2 . ASP   C 1 156 ? -3.649  6.296   105.465 1.00 55.20  ?  156 ASP   C OD2 1 
ATOM   8667  N N   . SER   C 1 157 ? -2.945  2.904   101.389 1.00 34.87  ?  157 SER   C N   1 
ATOM   8668  C CA  . SER   C 1 157 ? -3.497  2.483   100.104 1.00 41.98  ?  157 SER   C CA  1 
ATOM   8669  C C   . SER   C 1 157 ? -4.937  2.947   99.916  1.00 40.29  ?  157 SER   C C   1 
ATOM   8670  O O   . SER   C 1 157 ? -5.314  3.403   98.830  1.00 36.89  ?  157 SER   C O   1 
ATOM   8671  C CB  . SER   C 1 157 ? -3.404  0.965   99.980  1.00 43.00  ?  157 SER   C CB  1 
ATOM   8672  O OG  . SER   C 1 157 ? -3.829  0.543   98.703  1.00 50.50  ?  157 SER   C OG  1 
ATOM   8673  N N   . GLU   C 1 158 ? -5.760  2.840   100.951 1.00 39.71  ?  158 GLU   C N   1 
ATOM   8674  C CA  . GLU   C 1 158 ? -7.166  3.177   100.804 1.00 41.05  ?  158 GLU   C CA  1 
ATOM   8675  C C   . GLU   C 1 158 ? -7.481  4.625   101.152 1.00 39.17  ?  158 GLU   C C   1 
ATOM   8676  O O   . GLU   C 1 158 ? -8.603  5.070   100.898 1.00 39.20  ?  158 GLU   C O   1 
ATOM   8677  C CB  . GLU   C 1 158 ? -8.023  2.237   101.660 1.00 50.31  ?  158 GLU   C CB  1 
ATOM   8678  C CG  . GLU   C 1 158 ? -7.816  0.761   101.325 1.00 54.24  ?  158 GLU   C CG  1 
ATOM   8679  C CD  . GLU   C 1 158 ? -9.110  -0.036  101.335 1.00 61.73  ?  158 GLU   C CD  1 
ATOM   8680  O OE1 . GLU   C 1 158 ? -10.149 0.498   100.879 1.00 55.87  ?  158 GLU   C OE1 1 
ATOM   8681  O OE2 . GLU   C 1 158 ? -9.084  -1.198  101.800 1.00 65.65  ?  158 GLU   C OE2 1 
ATOM   8682  N N   . THR   C 1 159 ? -6.537  5.374   101.710 1.00 36.15  ?  159 THR   C N   1 
ATOM   8683  C CA  . THR   C 1 159 ? -6.788  6.774   102.032 1.00 38.82  ?  159 THR   C CA  1 
ATOM   8684  C C   . THR   C 1 159 ? -6.551  7.623   100.791 1.00 38.09  ?  159 THR   C C   1 
ATOM   8685  O O   . THR   C 1 159 ? -5.435  7.656   100.266 1.00 39.89  ?  159 THR   C O   1 
ATOM   8686  C CB  . THR   C 1 159 ? -5.887  7.241   103.175 1.00 37.41  ?  159 THR   C CB  1 
ATOM   8687  O OG1 . THR   C 1 159 ? -6.219  6.526   104.369 1.00 34.48  ?  159 THR   C OG1 1 
ATOM   8688  C CG2 . THR   C 1 159 ? -6.061  8.733   103.427 1.00 35.09  ?  159 THR   C CG2 1 
ATOM   8689  N N   . TYR   C 1 160 ? -7.591  8.311   100.327 1.00 33.99  ?  160 TYR   C N   1 
ATOM   8690  C CA  . TYR   C 1 160 ? -7.451  9.143   99.140  1.00 37.78  ?  160 TYR   C CA  1 
ATOM   8691  C C   . TYR   C 1 160 ? -6.432  10.253  99.380  1.00 34.31  ?  160 TYR   C C   1 
ATOM   8692  O O   . TYR   C 1 160 ? -6.373  10.840  100.464 1.00 32.37  ?  160 TYR   C O   1 
ATOM   8693  C CB  . TYR   C 1 160 ? -8.806  9.747   98.747  1.00 33.29  ?  160 TYR   C CB  1 
ATOM   8694  C CG  . TYR   C 1 160 ? -8.736  10.687  97.555  1.00 33.54  ?  160 TYR   C CG  1 
ATOM   8695  C CD1 . TYR   C 1 160 ? -8.422  12.033  97.721  1.00 33.25  ?  160 TYR   C CD1 1 
ATOM   8696  C CD2 . TYR   C 1 160 ? -8.972  10.229  96.266  1.00 32.48  ?  160 TYR   C CD2 1 
ATOM   8697  C CE1 . TYR   C 1 160 ? -8.333  12.890  96.646  1.00 31.79  ?  160 TYR   C CE1 1 
ATOM   8698  C CE2 . TYR   C 1 160 ? -8.893  11.090  95.178  1.00 31.10  ?  160 TYR   C CE2 1 
ATOM   8699  C CZ  . TYR   C 1 160 ? -8.568  12.417  95.379  1.00 32.64  ?  160 TYR   C CZ  1 
ATOM   8700  O OH  . TYR   C 1 160 ? -8.489  13.283  94.314  1.00 35.13  ?  160 TYR   C OH  1 
ATOM   8701  N N   . ASP   C 1 161 ? -5.627  10.537  98.356  1.00 30.59  ?  161 ASP   C N   1 
ATOM   8702  C CA  . ASP   C 1 161 ? -4.831  11.755  98.313  1.00 31.16  ?  161 ASP   C CA  1 
ATOM   8703  C C   . ASP   C 1 161 ? -4.703  12.206  96.864  1.00 32.27  ?  161 ASP   C C   1 
ATOM   8704  O O   . ASP   C 1 161 ? -4.710  11.384  95.941  1.00 31.41  ?  161 ASP   C O   1 
ATOM   8705  C CB  . ASP   C 1 161 ? -3.446  11.559  98.943  1.00 32.65  ?  161 ASP   C CB  1 
ATOM   8706  C CG  . ASP   C 1 161 ? -2.737  12.876  99.216  1.00 36.12  ?  161 ASP   C CG  1 
ATOM   8707  O OD1 . ASP   C 1 161 ? -3.030  13.523  100.249 1.00 42.80  ?  161 ASP   C OD1 1 
ATOM   8708  O OD2 . ASP   C 1 161 ? -1.885  13.267  98.396  1.00 31.82  ?  161 ASP   C OD2 1 
ATOM   8709  N N   . ASP   C 1 162 ? -4.587  13.526  96.671  1.00 30.20  ?  162 ASP   C N   1 
ATOM   8710  C CA  . ASP   C 1 162 ? -4.508  14.074  95.317  1.00 31.29  ?  162 ASP   C CA  1 
ATOM   8711  C C   . ASP   C 1 162 ? -3.199  13.703  94.625  1.00 28.41  ?  162 ASP   C C   1 
ATOM   8712  O O   . ASP   C 1 162 ? -3.174  13.490  93.409  1.00 29.73  ?  162 ASP   C O   1 
ATOM   8713  C CB  . ASP   C 1 162 ? -4.666  15.600  95.343  1.00 32.84  ?  162 ASP   C CB  1 
ATOM   8714  C CG  . ASP   C 1 162 ? -6.128  16.060  95.377  1.00 37.87  ?  162 ASP   C CG  1 
ATOM   8715  O OD1 . ASP   C 1 162 ? -7.042  15.275  95.033  1.00 33.98  ?  162 ASP   C OD1 1 
ATOM   8716  O OD2 . ASP   C 1 162 ? -6.360  17.234  95.742  1.00 37.11  ?  162 ASP   C OD2 1 
ATOM   8717  N N   . TRP   C 1 163 ? -2.092  13.644  95.366  1.00 32.17  ?  163 TRP   C N   1 
ATOM   8718  C CA  . TRP   C 1 163 ? -0.765  13.575  94.758  1.00 27.31  ?  163 TRP   C CA  1 
ATOM   8719  C C   . TRP   C 1 163 ? 0.060   12.473  95.423  1.00 30.32  ?  163 TRP   C C   1 
ATOM   8720  O O   . TRP   C 1 163 ? 1.079   12.739  96.063  1.00 30.60  ?  163 TRP   C O   1 
ATOM   8721  C CB  . TRP   C 1 163 ? -0.066  14.929  94.844  1.00 27.61  ?  163 TRP   C CB  1 
ATOM   8722  C CG  . TRP   C 1 163 ? -0.960  16.084  94.500  1.00 29.67  ?  163 TRP   C CG  1 
ATOM   8723  C CD1 . TRP   C 1 163 ? -1.509  16.979  95.372  1.00 30.76  ?  163 TRP   C CD1 1 
ATOM   8724  C CD2 . TRP   C 1 163 ? -1.426  16.459  93.194  1.00 27.93  ?  163 TRP   C CD2 1 
ATOM   8725  N NE1 . TRP   C 1 163 ? -2.279  17.893  94.690  1.00 36.53  ?  163 TRP   C NE1 1 
ATOM   8726  C CE2 . TRP   C 1 163 ? -2.238  17.601  93.353  1.00 33.64  ?  163 TRP   C CE2 1 
ATOM   8727  C CE3 . TRP   C 1 163 ? -1.222  15.951  91.906  1.00 27.43  ?  163 TRP   C CE3 1 
ATOM   8728  C CZ2 . TRP   C 1 163 ? -2.855  18.236  92.274  1.00 35.55  ?  163 TRP   C CZ2 1 
ATOM   8729  C CZ3 . TRP   C 1 163 ? -1.828  16.588  90.835  1.00 31.46  ?  163 TRP   C CZ3 1 
ATOM   8730  C CH2 . TRP   C 1 163 ? -2.636  17.717  91.027  1.00 33.47  ?  163 TRP   C CH2 1 
ATOM   8731  N N   . LYS   C 1 164 ? -0.359  11.220  95.237  1.00 26.46  ?  164 LYS   C N   1 
ATOM   8732  C CA  . LYS   C 1 164 ? 0.381   10.136  95.874  1.00 26.64  ?  164 LYS   C CA  1 
ATOM   8733  C C   . LYS   C 1 164 ? 1.723   9.864   95.217  1.00 28.18  ?  164 LYS   C C   1 
ATOM   8734  O O   . LYS   C 1 164 ? 2.430   8.954   95.666  1.00 28.34  ?  164 LYS   C O   1 
ATOM   8735  C CB  . LYS   C 1 164 ? -0.452  8.856   95.894  1.00 28.34  ?  164 LYS   C CB  1 
ATOM   8736  C CG  . LYS   C 1 164 ? -1.537  8.844   96.957  1.00 29.81  ?  164 LYS   C CG  1 
ATOM   8737  C CD  . LYS   C 1 164 ? -2.240  7.497   97.017  1.00 29.11  ?  164 LYS   C CD  1 
ATOM   8738  C CE  . LYS   C 1 164 ? -3.121  7.402   98.244  1.00 31.76  ?  164 LYS   C CE  1 
ATOM   8739  N NZ  . LYS   C 1 164 ? -3.544  6.002   98.521  1.00 33.01  ?  164 LYS   C NZ  1 
ATOM   8740  N N   . GLY   C 1 165 ? 2.105   10.615  94.185  1.00 30.32  ?  165 GLY   C N   1 
ATOM   8741  C CA  . GLY   C 1 165 ? 3.437   10.521  93.627  1.00 25.96  ?  165 GLY   C CA  1 
ATOM   8742  C C   . GLY   C 1 165 ? 4.401   11.609  94.057  1.00 27.97  ?  165 GLY   C C   1 
ATOM   8743  O O   . GLY   C 1 165 ? 5.534   11.629  93.570  1.00 25.49  ?  165 GLY   C O   1 
ATOM   8744  N N   . ASP   C 1 166 ? 3.995   12.505  94.962  1.00 25.75  ?  166 ASP   C N   1 
ATOM   8745  C CA  . ASP   C 1 166 ? 4.839   13.623  95.380  1.00 28.50  ?  166 ASP   C CA  1 
ATOM   8746  C C   . ASP   C 1 166 ? 6.159   13.150  95.982  1.00 30.53  ?  166 ASP   C C   1 
ATOM   8747  O O   . ASP   C 1 166 ? 6.243   12.092  96.617  1.00 29.51  ?  166 ASP   C O   1 
ATOM   8748  C CB  . ASP   C 1 166 ? 4.113   14.496  96.415  1.00 26.55  ?  166 ASP   C CB  1 
ATOM   8749  C CG  . ASP   C 1 166 ? 3.216   15.557  95.779  1.00 30.72  ?  166 ASP   C CG  1 
ATOM   8750  O OD1 . ASP   C 1 166 ? 3.137   15.602  94.536  1.00 32.01  ?  166 ASP   C OD1 1 
ATOM   8751  O OD2 . ASP   C 1 166 ? 2.585   16.352  96.527  1.00 31.70  ?  166 ASP   C OD2 1 
ATOM   8752  N N   . PHE   C 1 167 ? 7.202   13.957  95.774  1.00 28.78  ?  167 PHE   C N   1 
ATOM   8753  C CA  . PHE   C 1 167 ? 8.405   13.861  96.589  1.00 26.36  ?  167 PHE   C CA  1 
ATOM   8754  C C   . PHE   C 1 167 ? 8.081   14.201  98.036  1.00 29.90  ?  167 PHE   C C   1 
ATOM   8755  O O   . PHE   C 1 167 ? 7.369   15.167  98.317  1.00 26.69  ?  167 PHE   C O   1 
ATOM   8756  C CB  . PHE   C 1 167 ? 9.472   14.843  96.106  1.00 26.14  ?  167 PHE   C CB  1 
ATOM   8757  C CG  . PHE   C 1 167 ? 10.272  14.375  94.935  1.00 27.24  ?  167 PHE   C CG  1 
ATOM   8758  C CD1 . PHE   C 1 167 ? 9.780   14.491  93.660  1.00 24.90  ?  167 PHE   C CD1 1 
ATOM   8759  C CD2 . PHE   C 1 167 ? 11.549  13.880  95.114  1.00 24.82  ?  167 PHE   C CD2 1 
ATOM   8760  C CE1 . PHE   C 1 167 ? 10.530  14.091  92.583  1.00 25.63  ?  167 PHE   C CE1 1 
ATOM   8761  C CE2 . PHE   C 1 167 ? 12.308  13.478  94.038  1.00 25.70  ?  167 PHE   C CE2 1 
ATOM   8762  C CZ  . PHE   C 1 167 ? 11.793  13.582  92.768  1.00 25.11  ?  167 PHE   C CZ  1 
ATOM   8763  N N   . ASP   C 1 168 ? 8.644   13.429  98.958  1.00 30.05  ?  168 ASP   C N   1 
ATOM   8764  C CA  . ASP   C 1 168 ? 8.685   13.828  100.365 1.00 31.41  ?  168 ASP   C CA  1 
ATOM   8765  C C   . ASP   C 1 168 ? 9.771   14.892  100.482 1.00 29.72  ?  168 ASP   C C   1 
ATOM   8766  O O   . ASP   C 1 168 ? 10.962  14.581  100.467 1.00 32.10  ?  168 ASP   C O   1 
ATOM   8767  C CB  . ASP   C 1 168 ? 8.966   12.619  101.250 1.00 32.65  ?  168 ASP   C CB  1 
ATOM   8768  C CG  . ASP   C 1 168 ? 8.835   12.918  102.738 1.00 36.12  ?  168 ASP   C CG  1 
ATOM   8769  O OD1 . ASP   C 1 168 ? 9.322   13.969  103.219 1.00 33.36  ?  168 ASP   C OD1 1 
ATOM   8770  O OD2 . ASP   C 1 168 ? 8.242   12.070  103.435 1.00 37.36  ?  168 ASP   C OD2 1 
ATOM   8771  N N   . ILE   C 1 169 ? 9.365   16.159  100.573 1.00 30.07  ?  169 ILE   C N   1 
ATOM   8772  C CA  . ILE   C 1 169 ? 10.341  17.246  100.600 1.00 31.26  ?  169 ILE   C CA  1 
ATOM   8773  C C   . ILE   C 1 169 ? 11.229  17.146  101.834 1.00 32.72  ?  169 ILE   C C   1 
ATOM   8774  O O   . ILE   C 1 169 ? 12.423  17.471  101.788 1.00 34.74  ?  169 ILE   C O   1 
ATOM   8775  C CB  . ILE   C 1 169 ? 9.624   18.606  100.532 1.00 36.85  ?  169 ILE   C CB  1 
ATOM   8776  C CG1 . ILE   C 1 169 ? 8.731   18.673  99.297  1.00 32.02  ?  169 ILE   C CG1 1 
ATOM   8777  C CG2 . ILE   C 1 169 ? 10.640  19.741  100.518 1.00 37.27  ?  169 ILE   C CG2 1 
ATOM   8778  C CD1 . ILE   C 1 169 ? 9.483   18.537  97.995  1.00 31.63  ?  169 ILE   C CD1 1 
ATOM   8779  N N   . LYS   C 1 170 ? 10.668  16.697  102.959 1.00 33.07  ?  170 LYS   C N   1 
ATOM   8780  C CA  . LYS   C 1 170 ? 11.474  16.577  104.168 1.00 35.26  ?  170 LYS   C CA  1 
ATOM   8781  C C   . LYS   C 1 170 ? 12.609  15.584  103.968 1.00 34.68  ?  170 LYS   C C   1 
ATOM   8782  O O   . LYS   C 1 170 ? 13.750  15.854  104.362 1.00 36.38  ?  170 LYS   C O   1 
ATOM   8783  C CB  . LYS   C 1 170 ? 10.602  16.174  105.359 1.00 37.93  ?  170 LYS   C CB  1 
ATOM   8784  C CG  . LYS   C 1 170 ? 11.359  16.126  106.696 1.00 42.24  ?  170 LYS   C CG  1 
ATOM   8785  C CD  . LYS   C 1 170 ? 10.420  15.771  107.844 1.00 46.78  ?  170 LYS   C CD  1 
ATOM   8786  C CE  . LYS   C 1 170 ? 11.140  15.767  109.195 1.00 54.07  ?  170 LYS   C CE  1 
ATOM   8787  N NZ  . LYS   C 1 170 ? 12.215  14.737  109.272 1.00 48.95  ?  170 LYS   C NZ  1 
ATOM   8788  N N   . LYS   C 1 171 ? 12.327  14.442  103.329 1.00 32.78  ?  171 LYS   C N   1 
ATOM   8789  C CA  . LYS   C 1 171 ? 13.384  13.475  103.048 1.00 31.70  ?  171 LYS   C CA  1 
ATOM   8790  C C   . LYS   C 1 171 ? 14.332  13.948  101.958 1.00 32.01  ?  171 LYS   C C   1 
ATOM   8791  O O   . LYS   C 1 171 ? 15.474  13.475  101.901 1.00 29.86  ?  171 LYS   C O   1 
ATOM   8792  C CB  . LYS   C 1 171 ? 12.792  12.129  102.632 1.00 34.68  ?  171 LYS   C CB  1 
ATOM   8793  C CG  . LYS   C 1 171 ? 12.058  11.376  103.725 1.00 37.29  ?  171 LYS   C CG  1 
ATOM   8794  C CD  . LYS   C 1 171 ? 11.581  10.038  103.181 1.00 36.21  ?  171 LYS   C CD  1 
ATOM   8795  C CE  . LYS   C 1 171 ? 10.861  9.220   104.236 1.00 38.84  ?  171 LYS   C CE  1 
ATOM   8796  N NZ  . LYS   C 1 171 ? 10.480  7.890   103.671 1.00 42.88  ?  171 LYS   C NZ  1 
ATOM   8797  N N   . LEU   C 1 172 ? 13.884  14.845  101.078 1.00 31.94  ?  172 LEU   C N   1 
ATOM   8798  C CA  . LEU   C 1 172 ? 14.770  15.329  100.023 1.00 30.29  ?  172 LEU   C CA  1 
ATOM   8799  C C   . LEU   C 1 172 ? 15.913  16.138  100.612 1.00 34.34  ?  172 LEU   C C   1 
ATOM   8800  O O   . LEU   C 1 172 ? 17.090  15.869  100.338 1.00 30.73  ?  172 LEU   C O   1 
ATOM   8801  C CB  . LEU   C 1 172 ? 13.986  16.163  99.012  1.00 28.18  ?  172 LEU   C CB  1 
ATOM   8802  C CG  . LEU   C 1 172 ? 14.805  16.778  97.875  1.00 29.53  ?  172 LEU   C CG  1 
ATOM   8803  C CD1 . LEU   C 1 172 ? 15.533  15.698  97.094  1.00 30.55  ?  172 LEU   C CD1 1 
ATOM   8804  C CD2 . LEU   C 1 172 ? 13.920  17.599  96.950  1.00 27.35  ?  172 LEU   C CD2 1 
ATOM   8805  N N   . LYS   C 1 173 ? 15.582  17.127  101.446 1.00 32.57  ?  173 LYS   C N   1 
ATOM   8806  C CA  . LYS   C 1 173 ? 16.618  17.917  102.094 1.00 32.75  ?  173 LYS   C CA  1 
ATOM   8807  C C   . LYS   C 1 173 ? 17.421  17.078  103.081 1.00 32.21  ?  173 LYS   C C   1 
ATOM   8808  O O   . LYS   C 1 173 ? 18.630  17.292  103.230 1.00 34.19  ?  173 LYS   C O   1 
ATOM   8809  C CB  . LYS   C 1 173 ? 15.983  19.125  102.784 1.00 38.87  ?  173 LYS   C CB  1 
ATOM   8810  C CG  . LYS   C 1 173 ? 15.199  20.036  101.838 1.00 32.03  ?  173 LYS   C CG  1 
ATOM   8811  C CD  . LYS   C 1 173 ? 14.510  21.178  102.586 1.00 39.40  ?  173 LYS   C CD  1 
ATOM   8812  C CE  . LYS   C 1 173 ? 13.835  22.149  101.618 1.00 41.93  ?  173 LYS   C CE  1 
ATOM   8813  N NZ  . LYS   C 1 173 ? 13.164  23.308  102.278 1.00 37.10  ?  173 LYS   C NZ  1 
ATOM   8814  N N   . GLU   C 1 174 ? 16.777  16.122  103.755 1.00 30.97  ?  174 GLU   C N   1 
ATOM   8815  C CA  . GLU   C 1 174 ? 17.506  15.219  104.643 1.00 34.98  ?  174 GLU   C CA  1 
ATOM   8816  C C   . GLU   C 1 174 ? 18.561  14.441  103.871 1.00 34.48  ?  174 GLU   C C   1 
ATOM   8817  O O   . GLU   C 1 174 ? 19.706  14.306  104.322 1.00 35.06  ?  174 GLU   C O   1 
ATOM   8818  C CB  . GLU   C 1 174 ? 16.540  14.255  105.339 1.00 33.57  ?  174 GLU   C CB  1 
ATOM   8819  C CG  . GLU   C 1 174 ? 15.885  14.799  106.603 1.00 40.65  ?  174 GLU   C CG  1 
ATOM   8820  C CD  . GLU   C 1 174 ? 14.747  13.915  107.109 1.00 46.06  ?  174 GLU   C CD  1 
ATOM   8821  O OE1 . GLU   C 1 174 ? 13.792  13.653  106.343 1.00 42.09  ?  174 GLU   C OE1 1 
ATOM   8822  O OE2 . GLU   C 1 174 ? 14.807  13.481  108.279 1.00 56.81  ?  174 GLU   C OE2 1 
ATOM   8823  N N   . ASN   C 1 175 ? 18.189  13.918  102.700 1.00 30.61  ?  175 ASN   C N   1 
ATOM   8824  C CA  . ASN   C 1 175 ? 19.149  13.169  101.898 1.00 32.77  ?  175 ASN   C CA  1 
ATOM   8825  C C   . ASN   C 1 175 ? 20.218  14.078  101.307 1.00 30.77  ?  175 ASN   C C   1 
ATOM   8826  O O   . ASN   C 1 175 ? 21.373  13.660  101.167 1.00 34.39  ?  175 ASN   C O   1 
ATOM   8827  C CB  . ASN   C 1 175 ? 18.431  12.390  100.795 1.00 30.96  ?  175 ASN   C CB  1 
ATOM   8828  C CG  . ASN   C 1 175 ? 17.991  11.017  101.252 1.00 27.68  ?  175 ASN   C CG  1 
ATOM   8829  O OD1 . ASN   C 1 175 ? 18.815  10.116  101.410 1.00 33.26  ?  175 ASN   C OD1 1 
ATOM   8830  N ND2 . ASN   C 1 175 ? 16.690  10.846  101.466 1.00 29.50  ?  175 ASN   C ND2 1 
ATOM   8831  N N   . ILE   C 1 176 ? 19.867  15.319  100.964 1.00 28.48  ?  176 ILE   C N   1 
ATOM   8832  C CA  . ILE   C 1 176 ? 20.901  16.257  100.539 1.00 32.58  ?  176 ILE   C CA  1 
ATOM   8833  C C   . ILE   C 1 176 ? 21.843  16.563  101.698 1.00 30.00  ?  176 ILE   C C   1 
ATOM   8834  O O   . ILE   C 1 176 ? 23.044  16.779  101.494 1.00 27.68  ?  176 ILE   C O   1 
ATOM   8835  C CB  . ILE   C 1 176 ? 20.264  17.535  99.960  1.00 30.31  ?  176 ILE   C CB  1 
ATOM   8836  C CG1 . ILE   C 1 176 ? 19.452  17.202  98.704  1.00 31.20  ?  176 ILE   C CG1 1 
ATOM   8837  C CG2 . ILE   C 1 176 ? 21.331  18.564  99.624  1.00 31.77  ?  176 ILE   C CG2 1 
ATOM   8838  C CD1 . ILE   C 1 176 ? 18.842  18.401  98.034  1.00 29.20  ?  176 ILE   C CD1 1 
ATOM   8839  N N   . ALA   C 1 177 ? 21.327  16.553  102.930 1.00 30.61  ?  177 ALA   C N   1 
ATOM   8840  C CA  . ALA   C 1 177 ? 22.168  16.813  104.095 1.00 34.91  ?  177 ALA   C CA  1 
ATOM   8841  C C   . ALA   C 1 177 ? 23.083  15.632  104.402 1.00 35.97  ?  177 ALA   C C   1 
ATOM   8842  O O   . ALA   C 1 177 ? 24.273  15.821  104.684 1.00 43.35  ?  177 ALA   C O   1 
ATOM   8843  C CB  . ALA   C 1 177 ? 21.296  17.141  105.306 1.00 32.27  ?  177 ALA   C CB  1 
ATOM   8844  N N   . GLN   C 1 178 ? 22.546  14.407  104.365 1.00 37.85  ?  178 GLN   C N   1 
ATOM   8845  C CA  . GLN   C 1 178 ? 23.340  13.233  104.730 1.00 34.46  ?  178 GLN   C CA  1 
ATOM   8846  C C   . GLN   C 1 178 ? 24.379  12.923  103.664 1.00 35.28  ?  178 GLN   C C   1 
ATOM   8847  O O   . GLN   C 1 178 ? 25.563  12.746  103.969 1.00 34.95  ?  178 GLN   C O   1 
ATOM   8848  C CB  . GLN   C 1 178 ? 22.432  12.019  104.947 1.00 37.78  ?  178 GLN   C CB  1 
ATOM   8849  C CG  . GLN   C 1 178 ? 21.355  12.191  106.018 1.00 45.87  ?  178 GLN   C CG  1 
ATOM   8850  C CD  . GLN   C 1 178 ? 21.862  11.912  107.422 1.00 53.65  ?  178 GLN   C CD  1 
ATOM   8851  O OE1 . GLN   C 1 178 ? 22.033  12.831  108.225 1.00 62.98  ?  178 GLN   C OE1 1 
ATOM   8852  N NE2 . GLN   C 1 178 ? 22.095  10.638  107.729 1.00 45.68  ?  178 GLN   C NE2 1 
ATOM   8853  N N   . HIS   C 1 179 ? 23.957  12.858  102.401 1.00 34.15  ?  179 HIS   C N   1 
ATOM   8854  C CA  . HIS   C 1 179 ? 24.872  12.469  101.337 1.00 31.93  ?  179 HIS   C CA  1 
ATOM   8855  C C   . HIS   C 1 179 ? 25.716  13.635  100.841 1.00 34.36  ?  179 HIS   C C   1 
ATOM   8856  O O   . HIS   C 1 179 ? 26.871  13.432  100.452 1.00 30.72  ?  179 HIS   C O   1 
ATOM   8857  C CB  . HIS   C 1 179 ? 24.089  11.851  100.178 1.00 31.42  ?  179 HIS   C CB  1 
ATOM   8858  C CG  . HIS   C 1 179 ? 23.350  10.606  100.555 1.00 29.23  ?  179 HIS   C CG  1 
ATOM   8859  N ND1 . HIS   C 1 179 ? 23.961  9.371   100.625 1.00 31.62  ?  179 HIS   C ND1 1 
ATOM   8860  C CD2 . HIS   C 1 179 ? 22.059  10.407  100.909 1.00 31.96  ?  179 HIS   C CD2 1 
ATOM   8861  C CE1 . HIS   C 1 179 ? 23.072  8.463   100.987 1.00 31.92  ?  179 HIS   C CE1 1 
ATOM   8862  N NE2 . HIS   C 1 179 ? 21.911  9.065   101.167 1.00 36.59  ?  179 HIS   C NE2 1 
ATOM   8863  N N   . GLY   C 1 180 ? 25.174  14.850  100.854 1.00 32.93  ?  180 GLY   C N   1 
ATOM   8864  C CA  . GLY   C 1 180 ? 25.866  15.971  100.248 1.00 30.05  ?  180 GLY   C CA  1 
ATOM   8865  C C   . GLY   C 1 180 ? 25.519  16.137  98.783  1.00 34.62  ?  180 GLY   C C   1 
ATOM   8866  O O   . GLY   C 1 180 ? 25.405  15.148  98.048  1.00 33.24  ?  180 GLY   C O   1 
ATOM   8867  N N   . ALA   C 1 181 ? 25.336  17.384  98.341  1.00 32.69  ?  181 ALA   C N   1 
ATOM   8868  C CA  . ALA   C 1 181 ? 25.020  17.626  96.940  1.00 31.17  ?  181 ALA   C CA  1 
ATOM   8869  C C   . ALA   C 1 181 ? 26.135  17.167  96.013  1.00 32.67  ?  181 ALA   C C   1 
ATOM   8870  O O   . ALA   C 1 181 ? 25.877  16.906  94.834  1.00 33.02  ?  181 ALA   C O   1 
ATOM   8871  C CB  . ALA   C 1 181 ? 24.729  19.108  96.715  1.00 37.48  ?  181 ALA   C CB  1 
ATOM   8872  N N   . ASP   C 1 182 ? 27.366  17.055  96.521  1.00 37.69  ?  182 ASP   C N   1 
ATOM   8873  C CA  . ASP   C 1 182 ? 28.469  16.565  95.701  1.00 35.96  ?  182 ASP   C CA  1 
ATOM   8874  C C   . ASP   C 1 182 ? 28.256  15.122  95.271  1.00 29.99  ?  182 ASP   C C   1 
ATOM   8875  O O   . ASP   C 1 182 ? 28.790  14.701  94.240  1.00 30.76  ?  182 ASP   C O   1 
ATOM   8876  C CB  . ASP   C 1 182 ? 29.790  16.687  96.462  1.00 38.97  ?  182 ASP   C CB  1 
ATOM   8877  C CG  . ASP   C 1 182 ? 30.369  18.087  96.414  1.00 43.81  ?  182 ASP   C CG  1 
ATOM   8878  O OD1 . ASP   C 1 182 ? 29.881  18.919  95.618  1.00 46.59  ?  182 ASP   C OD1 1 
ATOM   8879  O OD2 . ASP   C 1 182 ? 31.318  18.354  97.179  1.00 49.05  ?  182 ASP   C OD2 1 
ATOM   8880  N N   . ASN   C 1 183 ? 27.498  14.349  96.048  1.00 28.02  ?  183 ASN   C N   1 
ATOM   8881  C CA  . ASN   C 1 183 ? 27.268  12.939  95.764  1.00 30.34  ?  183 ASN   C CA  1 
ATOM   8882  C C   . ASN   C 1 183 ? 25.978  12.677  95.005  1.00 30.99  ?  183 ASN   C C   1 
ATOM   8883  O O   . ASN   C 1 183 ? 25.785  11.559  94.518  1.00 29.10  ?  183 ASN   C O   1 
ATOM   8884  C CB  . ASN   C 1 183 ? 27.239  12.123  97.058  1.00 26.79  ?  183 ASN   C CB  1 
ATOM   8885  C CG  . ASN   C 1 183 ? 28.609  11.905  97.633  1.00 27.39  ?  183 ASN   C CG  1 
ATOM   8886  O OD1 . ASN   C 1 183 ? 29.574  11.694  96.902  1.00 30.64  ?  183 ASN   C OD1 1 
ATOM   8887  N ND2 . ASN   C 1 183 ? 28.708  11.951  98.957  1.00 34.36  ?  183 ASN   C ND2 1 
ATOM   8888  N N   . ILE   C 1 184 ? 25.089  13.660  94.903  1.00 24.99  ?  184 ILE   C N   1 
ATOM   8889  C CA  . ILE   C 1 184 ? 23.812  13.469  94.230  1.00 29.01  ?  184 ILE   C CA  1 
ATOM   8890  C C   . ILE   C 1 184 ? 24.051  13.728  92.746  1.00 23.95  ?  184 ILE   C C   1 
ATOM   8891  O O   . ILE   C 1 184 ? 24.167  14.874  92.310  1.00 26.52  ?  184 ILE   C O   1 
ATOM   8892  C CB  . ILE   C 1 184 ? 22.724  14.369  94.817  1.00 24.27  ?  184 ILE   C CB  1 
ATOM   8893  C CG1 . ILE   C 1 184 ? 22.643  14.131  96.332  1.00 27.21  ?  184 ILE   C CG1 1 
ATOM   8894  C CG2 . ILE   C 1 184 ? 21.384  14.096  94.142  1.00 24.91  ?  184 ILE   C CG2 1 
ATOM   8895  C CD1 . ILE   C 1 184 ? 21.713  15.052  97.061  1.00 33.10  ?  184 ILE   C CD1 1 
ATOM   8896  N N   . VAL   C 1 185 ? 24.150  12.650  91.970  1.00 23.86  ?  185 VAL   C N   1 
ATOM   8897  C CA  . VAL   C 1 185 ? 24.372  12.786  90.532  1.00 27.03  ?  185 VAL   C CA  1 
ATOM   8898  C C   . VAL   C 1 185 ? 23.174  13.450  89.868  1.00 23.89  ?  185 VAL   C C   1 
ATOM   8899  O O   . VAL   C 1 185 ? 23.323  14.363  89.049  1.00 25.01  ?  185 VAL   C O   1 
ATOM   8900  C CB  . VAL   C 1 185 ? 24.675  11.415  89.900  1.00 23.03  ?  185 VAL   C CB  1 
ATOM   8901  C CG1 . VAL   C 1 185 ? 24.787  11.545  88.387  1.00 22.82  ?  185 VAL   C CG1 1 
ATOM   8902  C CG2 . VAL   C 1 185 ? 25.949  10.841  90.482  1.00 26.54  ?  185 VAL   C CG2 1 
ATOM   8903  N N   . ALA   C 1 186 ? 21.969  13.006  90.214  1.00 20.44  ?  186 ALA   C N   1 
ATOM   8904  C CA  . ALA   C 1 186 ? 20.763  13.546  89.613  1.00 22.69  ?  186 ALA   C CA  1 
ATOM   8905  C C   . ALA   C 1 186 ? 19.585  13.239  90.514  1.00 25.54  ?  186 ALA   C C   1 
ATOM   8906  O O   . ALA   C 1 186 ? 19.589  12.249  91.250  1.00 27.01  ?  186 ALA   C O   1 
ATOM   8907  C CB  . ALA   C 1 186 ? 20.506  12.971  88.213  1.00 18.35  ?  186 ALA   C CB  1 
ATOM   8908  N N   . ILE   C 1 187 ? 18.591  14.118  90.464  1.00 24.47  ?  187 ILE   C N   1 
ATOM   8909  C CA  . ILE   C 1 187 ? 17.260  13.845  90.987  1.00 24.29  ?  187 ILE   C CA  1 
ATOM   8910  C C   . ILE   C 1 187 ? 16.393  13.436  89.812  1.00 24.93  ?  187 ILE   C C   1 
ATOM   8911  O O   . ILE   C 1 187 ? 16.433  14.075  88.751  1.00 23.91  ?  187 ILE   C O   1 
ATOM   8912  C CB  . ILE   C 1 187 ? 16.680  15.071  91.709  1.00 27.16  ?  187 ILE   C CB  1 
ATOM   8913  C CG1 . ILE   C 1 187 ? 17.508  15.380  92.961  1.00 26.30  ?  187 ILE   C CG1 1 
ATOM   8914  C CG2 . ILE   C 1 187 ? 15.203  14.855  92.039  1.00 23.53  ?  187 ILE   C CG2 1 
ATOM   8915  C CD1 . ILE   C 1 187 ? 17.154  16.684  93.601  1.00 22.94  ?  187 ILE   C CD1 1 
ATOM   8916  N N   . VAL   C 1 188 ? 15.646  12.349  89.973  1.00 27.01  ?  188 VAL   C N   1 
ATOM   8917  C CA  . VAL   C 1 188 ? 14.811  11.814  88.901  1.00 24.66  ?  188 VAL   C CA  1 
ATOM   8918  C C   . VAL   C 1 188 ? 13.359  11.988  89.318  1.00 24.50  ?  188 VAL   C C   1 
ATOM   8919  O O   . VAL   C 1 188 ? 12.904  11.386  90.302  1.00 25.87  ?  188 VAL   C O   1 
ATOM   8920  C CB  . VAL   C 1 188 ? 15.135  10.346  88.590  1.00 24.82  ?  188 VAL   C CB  1 
ATOM   8921  C CG1 . VAL   C 1 188 ? 14.174  9.800   87.530  1.00 22.79  ?  188 VAL   C CG1 1 
ATOM   8922  C CG2 . VAL   C 1 188 ? 16.580  10.216  88.114  1.00 22.03  ?  188 VAL   C CG2 1 
ATOM   8923  N N   . SER   C 1 189 ? 12.633  12.822  88.580  1.00 22.11  ?  189 SER   C N   1 
ATOM   8924  C CA  . SER   C 1 189 ? 11.211  13.035  88.816  1.00 24.52  ?  189 SER   C CA  1 
ATOM   8925  C C   . SER   C 1 189 ? 10.433  12.102  87.899  1.00 20.45  ?  189 SER   C C   1 
ATOM   8926  O O   . SER   C 1 189 ? 10.400  12.309  86.685  1.00 26.73  ?  189 SER   C O   1 
ATOM   8927  C CB  . SER   C 1 189 ? 10.832  14.494  88.566  1.00 24.38  ?  189 SER   C CB  1 
ATOM   8928  O OG  . SER   C 1 189 ? 11.466  15.354  89.500  1.00 25.55  ?  189 SER   C OG  1 
ATOM   8929  N N   . THR   C 1 190 ? 9.801   11.080  88.477  1.00 23.01  ?  190 THR   C N   1 
ATOM   8930  C CA  . THR   C 1 190 ? 9.022   10.110  87.712  1.00 23.38  ?  190 THR   C CA  1 
ATOM   8931  C C   . THR   C 1 190 ? 7.566   10.568  87.640  1.00 24.60  ?  190 THR   C C   1 
ATOM   8932  O O   . THR   C 1 190 ? 6.893   10.656  88.672  1.00 23.76  ?  190 THR   C O   1 
ATOM   8933  C CB  . THR   C 1 190 ? 9.124   8.722   88.346  1.00 20.94  ?  190 THR   C CB  1 
ATOM   8934  O OG1 . THR   C 1 190 ? 10.502  8.412   88.607  1.00 23.10  ?  190 THR   C OG1 1 
ATOM   8935  C CG2 . THR   C 1 190 ? 8.559   7.664   87.415  1.00 22.25  ?  190 THR   C CG2 1 
ATOM   8936  N N   . VAL   C 1 191 ? 7.079   10.849  86.428  1.00 21.30  ?  191 VAL   C N   1 
ATOM   8937  C CA  . VAL   C 1 191 ? 5.744   11.414  86.221  1.00 21.78  ?  191 VAL   C CA  1 
ATOM   8938  C C   . VAL   C 1 191 ? 5.010   10.589  85.169  1.00 23.44  ?  191 VAL   C C   1 
ATOM   8939  O O   . VAL   C 1 191 ? 5.511   10.429  84.050  1.00 18.90  ?  191 VAL   C O   1 
ATOM   8940  C CB  . VAL   C 1 191 ? 5.808   12.896  85.804  1.00 25.45  ?  191 VAL   C CB  1 
ATOM   8941  C CG1 . VAL   C 1 191 ? 6.349   13.732  86.948  1.00 25.14  ?  191 VAL   C CG1 1 
ATOM   8942  C CG2 . VAL   C 1 191 ? 6.687   13.096  84.561  1.00 20.47  ?  191 VAL   C CG2 1 
ATOM   8943  N N   . THR   C 1 192 ? 3.848   10.019  85.530  1.00 25.35  ?  192 THR   C N   1 
ATOM   8944  C CA  . THR   C 1 192 ? 3.388   9.838   86.911  1.00 24.10  ?  192 THR   C CA  1 
ATOM   8945  C C   . THR   C 1 192 ? 4.360   8.924   87.636  1.00 20.00  ?  192 THR   C C   1 
ATOM   8946  O O   . THR   C 1 192 ? 5.266   8.384   87.019  1.00 21.41  ?  192 THR   C O   1 
ATOM   8947  C CB  . THR   C 1 192 ? 1.988   9.192   86.981  1.00 23.96  ?  192 THR   C CB  1 
ATOM   8948  O OG1 . THR   C 1 192 ? 2.017   7.942   86.278  1.00 21.51  ?  192 THR   C OG1 1 
ATOM   8949  C CG2 . THR   C 1 192 ? 0.911   10.096  86.366  1.00 23.64  ?  192 THR   C CG2 1 
ATOM   8950  N N   . CYS   C 1 193 ? 4.171   8.736   88.937  1.00 24.69  ?  193 CYS   C N   1 
ATOM   8951  C CA  . CYS   C 1 193 ? 5.068   7.876   89.706  1.00 20.63  ?  193 CYS   C CA  1 
ATOM   8952  C C   . CYS   C 1 193 ? 4.606   6.434   89.555  1.00 23.30  ?  193 CYS   C C   1 
ATOM   8953  O O   . CYS   C 1 193 ? 3.646   6.003   90.196  1.00 26.97  ?  193 CYS   C O   1 
ATOM   8954  C CB  . CYS   C 1 193 ? 5.104   8.294   91.165  1.00 20.54  ?  193 CYS   C CB  1 
ATOM   8955  S SG  . CYS   C 1 193 ? 6.226   7.271   92.111  1.00 28.22  ?  193 CYS   C SG  1 
ATOM   8956  N N   . ASN   C 1 194 ? 5.304   5.687   88.705  1.00 25.14  ?  194 ASN   C N   1 
ATOM   8957  C CA  . ASN   C 1 194 ? 4.855   4.356   88.313  1.00 26.22  ?  194 ASN   C CA  1 
ATOM   8958  C C   . ASN   C 1 194 ? 4.742   3.423   89.513  1.00 26.50  ?  194 ASN   C C   1 
ATOM   8959  O O   . ASN   C 1 194 ? 3.703   2.789   89.723  1.00 27.70  ?  194 ASN   C O   1 
ATOM   8960  C CB  . ASN   C 1 194 ? 5.823   3.786   87.276  1.00 25.62  ?  194 ASN   C CB  1 
ATOM   8961  C CG  . ASN   C 1 194 ? 5.266   2.572   86.563  1.00 28.51  ?  194 ASN   C CG  1 
ATOM   8962  O OD1 . ASN   C 1 194 ? 4.153   2.128   86.847  1.00 31.74  ?  194 ASN   C OD1 1 
ATOM   8963  N ND2 . ASN   C 1 194 ? 6.028   2.043   85.609  1.00 27.16  ?  194 ASN   C ND2 1 
ATOM   8964  N N   . SER   C 1 195 ? 5.810   3.323   90.311  1.00 26.98  ?  195 SER   C N   1 
ATOM   8965  C CA  . SER   C 1 195 ? 5.860   2.377   91.423  1.00 28.35  ?  195 SER   C CA  1 
ATOM   8966  C C   . SER   C 1 195 ? 4.933   2.743   92.575  1.00 29.13  ?  195 SER   C C   1 
ATOM   8967  O O   . SER   C 1 195 ? 4.716   1.910   93.461  1.00 30.87  ?  195 SER   C O   1 
ATOM   8968  C CB  . SER   C 1 195 ? 7.290   2.263   91.941  1.00 26.79  ?  195 SER   C CB  1 
ATOM   8969  O OG  . SER   C 1 195 ? 8.198   2.042   90.876  1.00 34.71  ?  195 SER   C OG  1 
ATOM   8970  N N   . ALA   C 1 196 ? 4.389   3.954   92.601  1.00 31.74  ?  196 ALA   C N   1 
ATOM   8971  C CA  . ALA   C 1 196 ? 3.423   4.332   93.619  1.00 28.78  ?  196 ALA   C CA  1 
ATOM   8972  C C   . ALA   C 1 196 ? 1.992   4.042   93.189  1.00 29.43  ?  196 ALA   C C   1 
ATOM   8973  O O   . ALA   C 1 196 ? 1.051   4.444   93.876  1.00 29.19  ?  196 ALA   C O   1 
ATOM   8974  C CB  . ALA   C 1 196 ? 3.583   5.813   93.975  1.00 23.55  ?  196 ALA   C CB  1 
ATOM   8975  N N   . GLY   C 1 197 ? 1.809   3.346   92.075  1.00 26.16  ?  197 GLY   C N   1 
ATOM   8976  C CA  . GLY   C 1 197 ? 0.496   3.097   91.535  1.00 28.70  ?  197 GLY   C CA  1 
ATOM   8977  C C   . GLY   C 1 197 ? 0.132   3.917   90.316  1.00 31.00  ?  197 GLY   C C   1 
ATOM   8978  O O   . GLY   C 1 197 ? -1.052  3.973   89.966  1.00 30.18  ?  197 GLY   C O   1 
ATOM   8979  N N   . GLY   C 1 198 ? 1.104   4.542   89.657  1.00 26.66  ?  198 GLY   C N   1 
ATOM   8980  C CA  . GLY   C 1 198 ? 0.799   5.460   88.573  1.00 24.74  ?  198 GLY   C CA  1 
ATOM   8981  C C   . GLY   C 1 198 ? 0.163   6.740   89.061  1.00 22.73  ?  198 GLY   C C   1 
ATOM   8982  O O   . GLY   C 1 198 ? -0.700  7.304   88.375  1.00 24.48  ?  198 GLY   C O   1 
ATOM   8983  N N   . GLN   C 1 199 ? 0.576   7.215   90.222  1.00 21.86  ?  199 GLN   C N   1 
ATOM   8984  C CA  . GLN   C 1 199 ? 0.009   8.330   90.962  1.00 27.74  ?  199 GLN   C CA  1 
ATOM   8985  C C   . GLN   C 1 199 ? 0.685   9.638   90.568  1.00 24.37  ?  199 GLN   C C   1 
ATOM   8986  O O   . GLN   C 1 199 ? 1.899   9.667   90.368  1.00 25.15  ?  199 GLN   C O   1 
ATOM   8987  C CB  . GLN   C 1 199 ? 0.159   8.096   92.456  1.00 25.80  ?  199 GLN   C CB  1 
ATOM   8988  C CG  . GLN   C 1 199 ? -0.619  6.882   92.929  1.00 30.36  ?  199 GLN   C CG  1 
ATOM   8989  C CD  . GLN   C 1 199 ? -2.102  7.002   92.626  1.00 24.58  ?  199 GLN   C CD  1 
ATOM   8990  O OE1 . GLN   C 1 199 ? -2.715  8.030   92.901  1.00 25.53  ?  199 GLN   C OE1 1 
ATOM   8991  N NE2 . GLN   C 1 199 ? -2.679  5.958   92.035  1.00 24.56  ?  199 GLN   C NE2 1 
ATOM   8992  N N   . PRO   C 1 200 ? -0.075  10.721  90.445  1.00 23.40  ?  200 PRO   C N   1 
ATOM   8993  C CA  . PRO   C 1 200 ? 0.480   11.957  89.884  1.00 25.71  ?  200 PRO   C CA  1 
ATOM   8994  C C   . PRO   C 1 200 ? 1.382   12.707  90.855  1.00 26.03  ?  200 PRO   C C   1 
ATOM   8995  O O   . PRO   C 1 200 ? 1.316   12.546  92.076  1.00 28.60  ?  200 PRO   C O   1 
ATOM   8996  C CB  . PRO   C 1 200 ? -0.764  12.786  89.558  1.00 24.06  ?  200 PRO   C CB  1 
ATOM   8997  C CG  . PRO   C 1 200 ? -1.793  12.302  90.534  1.00 24.88  ?  200 PRO   C CG  1 
ATOM   8998  C CD  . PRO   C 1 200 ? -1.521  10.826  90.690  1.00 24.69  ?  200 PRO   C CD  1 
ATOM   8999  N N   . VAL   C 1 201 ? 2.243   13.539  90.262  1.00 29.53  ?  201 VAL   C N   1 
ATOM   9000  C CA  . VAL   C 1 201 ? 3.106   14.483  90.969  1.00 26.43  ?  201 VAL   C CA  1 
ATOM   9001  C C   . VAL   C 1 201 ? 2.570   15.887  90.714  1.00 25.56  ?  201 VAL   C C   1 
ATOM   9002  O O   . VAL   C 1 201 ? 2.425   16.297  89.558  1.00 24.30  ?  201 VAL   C O   1 
ATOM   9003  C CB  . VAL   C 1 201 ? 4.573   14.371  90.507  1.00 27.55  ?  201 VAL   C CB  1 
ATOM   9004  C CG1 . VAL   C 1 201 ? 5.502   15.122  91.454  1.00 26.71  ?  201 VAL   C CG1 1 
ATOM   9005  C CG2 . VAL   C 1 201 ? 5.005   12.910  90.364  1.00 26.57  ?  201 VAL   C CG2 1 
ATOM   9006  N N   . SER   C 1 202 ? 2.298   16.631  91.785  1.00 26.85  ?  202 SER   C N   1 
ATOM   9007  C CA  . SER   C 1 202 ? 1.727   17.963  91.623  1.00 28.08  ?  202 SER   C CA  1 
ATOM   9008  C C   . SER   C 1 202 ? 2.727   18.905  90.957  1.00 28.49  ?  202 SER   C C   1 
ATOM   9009  O O   . SER   C 1 202 ? 3.941   18.695  91.002  1.00 29.74  ?  202 SER   C O   1 
ATOM   9010  C CB  . SER   C 1 202 ? 1.310   18.537  92.973  1.00 27.55  ?  202 SER   C CB  1 
ATOM   9011  O OG  . SER   C 1 202 ? 2.454   18.944  93.702  1.00 29.35  ?  202 SER   C OG  1 
ATOM   9012  N N   . MET   C 1 203 ? 2.202   19.964  90.330  1.00 26.39  ?  203 MET   C N   1 
ATOM   9013  C CA  . MET   C 1 203 ? 3.092   20.980  89.775  1.00 26.75  ?  203 MET   C CA  1 
ATOM   9014  C C   . MET   C 1 203 ? 3.927   21.631  90.870  1.00 31.55  ?  203 MET   C C   1 
ATOM   9015  O O   . MET   C 1 203 ? 5.124   21.884  90.681  1.00 34.44  ?  203 MET   C O   1 
ATOM   9016  C CB  . MET   C 1 203 ? 2.293   22.037  89.015  1.00 26.67  ?  203 MET   C CB  1 
ATOM   9017  C CG  . MET   C 1 203 ? 3.157   23.004  88.198  1.00 26.60  ?  203 MET   C CG  1 
ATOM   9018  S SD  . MET   C 1 203 ? 3.795   22.318  86.646  1.00 33.35  ?  203 MET   C SD  1 
ATOM   9019  C CE  . MET   C 1 203 ? 2.280   22.096  85.730  1.00 27.19  ?  203 MET   C CE  1 
ATOM   9020  N N   . SER   C 1 204 ? 3.316   21.890  92.032  1.00 29.67  ?  204 SER   C N   1 
ATOM   9021  C CA  . SER   C 1 204 ? 4.041   22.526  93.127  1.00 33.06  ?  204 SER   C CA  1 
ATOM   9022  C C   . SER   C 1 204 ? 5.156   21.632  93.651  1.00 29.95  ?  204 SER   C C   1 
ATOM   9023  O O   . SER   C 1 204 ? 6.246   22.115  93.980  1.00 34.88  ?  204 SER   C O   1 
ATOM   9024  C CB  . SER   C 1 204 ? 3.073   22.890  94.251  1.00 30.94  ?  204 SER   C CB  1 
ATOM   9025  O OG  . SER   C 1 204 ? 2.074   23.773  93.775  1.00 43.20  ?  204 SER   C OG  1 
ATOM   9026  N N   . ASN   C 1 205 ? 4.905   20.324  93.736  1.00 29.97  ?  205 ASN   C N   1 
ATOM   9027  C CA  . ASN   C 1 205 ? 5.956   19.395  94.142  1.00 31.51  ?  205 ASN   C CA  1 
ATOM   9028  C C   . ASN   C 1 205 ? 7.122   19.413  93.156  1.00 31.20  ?  205 ASN   C C   1 
ATOM   9029  O O   . ASN   C 1 205 ? 8.289   19.384  93.564  1.00 32.08  ?  205 ASN   C O   1 
ATOM   9030  C CB  . ASN   C 1 205 ? 5.379   17.986  94.273  1.00 32.25  ?  205 ASN   C CB  1 
ATOM   9031  C CG  . ASN   C 1 205 ? 6.288   17.048  95.038  1.00 29.99  ?  205 ASN   C CG  1 
ATOM   9032  O OD1 . ASN   C 1 205 ? 6.882   16.135  94.463  1.00 29.44  ?  205 ASN   C OD1 1 
ATOM   9033  N ND2 . ASN   C 1 205 ? 6.398   17.263  96.341  1.00 29.36  ?  205 ASN   C ND2 1 
ATOM   9034  N N   . LEU   C 1 206 ? 6.828   19.470  91.852  1.00 30.00  ?  206 LEU   C N   1 
ATOM   9035  C CA  . LEU   C 1 206 ? 7.892   19.543  90.853  1.00 29.96  ?  206 LEU   C CA  1 
ATOM   9036  C C   . LEU   C 1 206 ? 8.648   20.863  90.945  1.00 30.37  ?  206 LEU   C C   1 
ATOM   9037  O O   . LEU   C 1 206 ? 9.872   20.904  90.765  1.00 28.52  ?  206 LEU   C O   1 
ATOM   9038  C CB  . LEU   C 1 206 ? 7.306   19.374  89.453  1.00 29.63  ?  206 LEU   C CB  1 
ATOM   9039  C CG  . LEU   C 1 206 ? 6.549   18.093  89.118  1.00 28.24  ?  206 LEU   C CG  1 
ATOM   9040  C CD1 . LEU   C 1 206 ? 5.813   18.284  87.806  1.00 25.71  ?  206 LEU   C CD1 1 
ATOM   9041  C CD2 . LEU   C 1 206 ? 7.504   16.912  89.017  1.00 24.60  ?  206 LEU   C CD2 1 
ATOM   9042  N N   . LYS   C 1 207 ? 7.924   21.952  91.210  1.00 33.48  ?  207 LYS   C N   1 
ATOM   9043  C CA  . LYS   C 1 207 ? 8.540   23.268  91.341  1.00 32.02  ?  207 LYS   C CA  1 
ATOM   9044  C C   . LYS   C 1 207 ? 9.473   23.325  92.545  1.00 30.72  ?  207 LYS   C C   1 
ATOM   9045  O O   . LYS   C 1 207 ? 10.625  23.757  92.432  1.00 27.68  ?  207 LYS   C O   1 
ATOM   9046  C CB  . LYS   C 1 207 ? 7.442   24.328  91.454  1.00 36.89  ?  207 LYS   C CB  1 
ATOM   9047  C CG  . LYS   C 1 207 ? 7.928   25.761  91.436  1.00 39.49  ?  207 LYS   C CG  1 
ATOM   9048  C CD  . LYS   C 1 207 ? 6.783   26.721  91.701  1.00 40.85  ?  207 LYS   C CD  1 
ATOM   9049  C CE  . LYS   C 1 207 ? 7.159   28.130  91.297  1.00 44.92  ?  207 LYS   C CE  1 
ATOM   9050  N NZ  . LYS   C 1 207 ? 8.543   28.469  91.725  1.00 50.75  ?  207 LYS   C NZ  1 
ATOM   9051  N N   . GLU   C 1 208 ? 8.991   22.895  93.714  1.00 31.63  ?  208 GLU   C N   1 
ATOM   9052  C CA  . GLU   C 1 208 ? 9.818   22.960  94.915  1.00 31.02  ?  208 GLU   C CA  1 
ATOM   9053  C C   . GLU   C 1 208 ? 11.049  22.069  94.789  1.00 32.81  ?  208 GLU   C C   1 
ATOM   9054  O O   . GLU   C 1 208 ? 12.147  22.456  95.206  1.00 33.76  ?  208 GLU   C O   1 
ATOM   9055  C CB  . GLU   C 1 208 ? 8.995   22.578  96.147  1.00 31.07  ?  208 GLU   C CB  1 
ATOM   9056  C CG  . GLU   C 1 208 ? 9.749   22.754  97.457  1.00 35.12  ?  208 GLU   C CG  1 
ATOM   9057  C CD  . GLU   C 1 208 ? 8.863   22.605  98.686  1.00 41.46  ?  208 GLU   C CD  1 
ATOM   9058  O OE1 . GLU   C 1 208 ? 7.655   22.314  98.534  1.00 43.28  ?  208 GLU   C OE1 1 
ATOM   9059  O OE2 . GLU   C 1 208 ? 9.381   22.791  99.810  1.00 46.56  ?  208 GLU   C OE2 1 
ATOM   9060  N N   . VAL   C 1 209 ? 10.892  20.883  94.191  1.00 34.30  ?  209 VAL   C N   1 
ATOM   9061  C CA  . VAL   C 1 209 ? 12.024  19.973  94.008  1.00 29.06  ?  209 VAL   C CA  1 
ATOM   9062  C C   . VAL   C 1 209 ? 13.083  20.610  93.114  1.00 30.90  ?  209 VAL   C C   1 
ATOM   9063  O O   . VAL   C 1 209 ? 14.282  20.586  93.423  1.00 29.87  ?  209 VAL   C O   1 
ATOM   9064  C CB  . VAL   C 1 209 ? 11.540  18.626  93.437  1.00 31.08  ?  209 VAL   C CB  1 
ATOM   9065  C CG1 . VAL   C 1 209 ? 12.711  17.825  92.859  1.00 29.48  ?  209 VAL   C CG1 1 
ATOM   9066  C CG2 . VAL   C 1 209 ? 10.813  17.819  94.505  1.00 28.38  ?  209 VAL   C CG2 1 
ATOM   9067  N N   . TYR   C 1 210 ? 12.659  21.181  91.987  1.00 29.23  ?  210 TYR   C N   1 
ATOM   9068  C CA  . TYR   C 1 210 ? 13.624  21.779  91.070  1.00 30.11  ?  210 TYR   C CA  1 
ATOM   9069  C C   . TYR   C 1 210 ? 14.304  22.990  91.697  1.00 32.84  ?  210 TYR   C C   1 
ATOM   9070  O O   . TYR   C 1 210 ? 15.499  23.219  91.476  1.00 33.00  ?  210 TYR   C O   1 
ATOM   9071  C CB  . TYR   C 1 210 ? 12.937  22.155  89.757  1.00 29.72  ?  210 TYR   C CB  1 
ATOM   9072  C CG  . TYR   C 1 210 ? 13.894  22.609  88.673  1.00 31.69  ?  210 TYR   C CG  1 
ATOM   9073  C CD1 . TYR   C 1 210 ? 14.772  21.717  88.072  1.00 29.29  ?  210 TYR   C CD1 1 
ATOM   9074  C CD2 . TYR   C 1 210 ? 13.914  23.934  88.247  1.00 34.06  ?  210 TYR   C CD2 1 
ATOM   9075  C CE1 . TYR   C 1 210 ? 15.644  22.137  87.077  1.00 32.03  ?  210 TYR   C CE1 1 
ATOM   9076  C CE2 . TYR   C 1 210 ? 14.780  24.360  87.257  1.00 29.98  ?  210 TYR   C CE2 1 
ATOM   9077  C CZ  . TYR   C 1 210 ? 15.640  23.463  86.678  1.00 29.28  ?  210 TYR   C CZ  1 
ATOM   9078  O OH  . TYR   C 1 210 ? 16.499  23.896  85.698  1.00 27.10  ?  210 TYR   C OH  1 
ATOM   9079  N N   . GLU   C 1 211 ? 13.566  23.765  92.498  1.00 32.36  ?  211 GLU   C N   1 
ATOM   9080  C CA  . GLU   C 1 211 ? 14.181  24.877  93.217  1.00 32.16  ?  211 GLU   C CA  1 
ATOM   9081  C C   . GLU   C 1 211 ? 15.251  24.384  94.183  1.00 32.54  ?  211 GLU   C C   1 
ATOM   9082  O O   . GLU   C 1 211 ? 16.347  24.954  94.250  1.00 33.17  ?  211 GLU   C O   1 
ATOM   9083  C CB  . GLU   C 1 211 ? 13.114  25.669  93.967  1.00 32.35  ?  211 GLU   C CB  1 
ATOM   9084  C CG  . GLU   C 1 211 ? 12.153  26.441  93.074  1.00 36.21  ?  211 GLU   C CG  1 
ATOM   9085  C CD  . GLU   C 1 211 ? 11.006  27.061  93.861  1.00 36.11  ?  211 GLU   C CD  1 
ATOM   9086  O OE1 . GLU   C 1 211 ? 11.001  26.952  95.107  1.00 42.42  ?  211 GLU   C OE1 1 
ATOM   9087  O OE2 . GLU   C 1 211 ? 10.109  27.660  93.235  1.00 39.31  ?  211 GLU   C OE2 1 
ATOM   9088  N N   . ILE   C 1 212 ? 14.950  23.326  94.939  1.00 29.46  ?  212 ILE   C N   1 
ATOM   9089  C CA  . ILE   C 1 212 ? 15.914  22.782  95.893  1.00 32.69  ?  212 ILE   C CA  1 
ATOM   9090  C C   . ILE   C 1 212 ? 17.129  22.228  95.165  1.00 33.97  ?  212 ILE   C C   1 
ATOM   9091  O O   . ILE   C 1 212 ? 18.273  22.415  95.597  1.00 32.60  ?  212 ILE   C O   1 
ATOM   9092  C CB  . ILE   C 1 212 ? 15.243  21.705  96.765  1.00 32.99  ?  212 ILE   C CB  1 
ATOM   9093  C CG1 . ILE   C 1 212 ? 14.198  22.334  97.691  1.00 33.74  ?  212 ILE   C CG1 1 
ATOM   9094  C CG2 . ILE   C 1 212 ? 16.283  20.921  97.547  1.00 29.20  ?  212 ILE   C CG2 1 
ATOM   9095  C CD1 . ILE   C 1 212 ? 13.211  21.338  98.263  1.00 33.53  ?  212 ILE   C CD1 1 
ATOM   9096  N N   . ALA   C 1 213 ? 16.901  21.535  94.051  1.00 29.10  ?  213 ALA   C N   1 
ATOM   9097  C CA  . ALA   C 1 213 ? 18.009  20.967  93.297  1.00 29.13  ?  213 ALA   C CA  1 
ATOM   9098  C C   . ALA   C 1 213 ? 18.860  22.045  92.644  1.00 32.50  ?  213 ALA   C C   1 
ATOM   9099  O O   . ALA   C 1 213 ? 20.079  21.880  92.522  1.00 34.70  ?  213 ALA   C O   1 
ATOM   9100  C CB  . ALA   C 1 213 ? 17.479  20.003  92.244  1.00 27.77  ?  213 ALA   C CB  1 
ATOM   9101  N N   . LYS   C 1 214 ? 18.249  23.146  92.212  1.00 33.57  ?  214 LYS   C N   1 
ATOM   9102  C CA  . LYS   C 1 214 ? 19.041  24.202  91.597  1.00 33.66  ?  214 LYS   C CA  1 
ATOM   9103  C C   . LYS   C 1 214 ? 19.820  25.004  92.629  1.00 37.57  ?  214 LYS   C C   1 
ATOM   9104  O O   . LYS   C 1 214 ? 20.931  25.461  92.334  1.00 41.21  ?  214 LYS   C O   1 
ATOM   9105  C CB  . LYS   C 1 214 ? 18.148  25.115  90.764  1.00 31.59  ?  214 LYS   C CB  1 
ATOM   9106  C CG  . LYS   C 1 214 ? 17.815  24.510  89.420  1.00 35.05  ?  214 LYS   C CG  1 
ATOM   9107  C CD  . LYS   C 1 214 ? 19.085  24.320  88.601  1.00 42.21  ?  214 LYS   C CD  1 
ATOM   9108  C CE  . LYS   C 1 214 ? 18.974  23.153  87.619  1.00 38.12  ?  214 LYS   C CE  1 
ATOM   9109  N NZ  . LYS   C 1 214 ? 19.558  21.884  88.150  1.00 30.27  ?  214 LYS   C NZ  1 
ATOM   9110  N N   . GLN   C 1 215 ? 19.282  25.166  93.841  1.00 33.59  ?  215 GLN   C N   1 
ATOM   9111  C CA  . GLN   C 1 215 ? 20.040  25.852  94.878  1.00 37.35  ?  215 GLN   C CA  1 
ATOM   9112  C C   . GLN   C 1 215 ? 21.253  25.048  95.325  1.00 37.68  ?  215 GLN   C C   1 
ATOM   9113  O O   . GLN   C 1 215 ? 22.170  25.616  95.922  1.00 42.97  ?  215 GLN   C O   1 
ATOM   9114  C CB  . GLN   C 1 215 ? 19.140  26.176  96.077  1.00 43.44  ?  215 GLN   C CB  1 
ATOM   9115  C CG  . GLN   C 1 215 ? 19.069  25.097  97.153  1.00 39.60  ?  215 GLN   C CG  1 
ATOM   9116  C CD  . GLN   C 1 215 ? 17.963  25.349  98.175  1.00 46.40  ?  215 GLN   C CD  1 
ATOM   9117  O OE1 . GLN   C 1 215 ? 16.913  25.917  97.852  1.00 48.39  ?  215 GLN   C OE1 1 
ATOM   9118  N NE2 . GLN   C 1 215 ? 18.198  24.929  99.416  1.00 49.89  ?  215 GLN   C NE2 1 
ATOM   9119  N N   . HIS   C 1 216 ? 21.289  23.748  95.042  1.00 38.98  ?  216 HIS   C N   1 
ATOM   9120  C CA  . HIS   C 1 216 ? 22.460  22.928  95.312  1.00 33.26  ?  216 HIS   C CA  1 
ATOM   9121  C C   . HIS   C 1 216 ? 23.209  22.547  94.044  1.00 33.36  ?  216 HIS   C C   1 
ATOM   9122  O O   . HIS   C 1 216 ? 24.151  21.756  94.114  1.00 32.30  ?  216 HIS   C O   1 
ATOM   9123  C CB  . HIS   C 1 216 ? 22.072  21.655  96.066  1.00 34.59  ?  216 HIS   C CB  1 
ATOM   9124  C CG  . HIS   C 1 216 ? 21.577  21.893  97.457  1.00 34.36  ?  216 HIS   C CG  1 
ATOM   9125  N ND1 . HIS   C 1 216 ? 20.258  22.169  97.740  1.00 38.47  ?  216 HIS   C ND1 1 
ATOM   9126  C CD2 . HIS   C 1 216 ? 22.219  21.868  98.648  1.00 32.42  ?  216 HIS   C CD2 1 
ATOM   9127  C CE1 . HIS   C 1 216 ? 20.109  22.316  99.045  1.00 35.06  ?  216 HIS   C CE1 1 
ATOM   9128  N NE2 . HIS   C 1 216 ? 21.284  22.139  99.618  1.00 33.87  ?  216 HIS   C NE2 1 
ATOM   9129  N N   . GLY   C 1 217 ? 22.809  23.072  92.891  1.00 35.18  ?  217 GLY   C N   1 
ATOM   9130  C CA  . GLY   C 1 217 ? 23.464  22.708  91.645  1.00 32.70  ?  217 GLY   C CA  1 
ATOM   9131  C C   . GLY   C 1 217 ? 23.290  21.255  91.246  1.00 32.48  ?  217 GLY   C C   1 
ATOM   9132  O O   . GLY   C 1 217 ? 24.232  20.643  90.725  1.00 29.02  ?  217 GLY   C O   1 
ATOM   9133  N N   . ILE   C 1 218 ? 22.107  20.688  91.468  1.00 30.71  ?  218 ILE   C N   1 
ATOM   9134  C CA  . ILE   C 1 218 ? 21.854  19.270  91.222  1.00 33.82  ?  218 ILE   C CA  1 
ATOM   9135  C C   . ILE   C 1 218 ? 21.036  19.117  89.946  1.00 28.12  ?  218 ILE   C C   1 
ATOM   9136  O O   . ILE   C 1 218 ? 19.983  19.748  89.792  1.00 26.60  ?  218 ILE   C O   1 
ATOM   9137  C CB  . ILE   C 1 218 ? 21.139  18.618  92.417  1.00 29.80  ?  218 ILE   C CB  1 
ATOM   9138  C CG1 . ILE   C 1 218 ? 21.978  18.784  93.683  1.00 28.00  ?  218 ILE   C CG1 1 
ATOM   9139  C CG2 . ILE   C 1 218 ? 20.872  17.144  92.133  1.00 25.26  ?  218 ILE   C CG2 1 
ATOM   9140  C CD1 . ILE   C 1 218 ? 21.315  18.241  94.927  1.00 29.17  ?  218 ILE   C CD1 1 
ATOM   9141  N N   . PHE   C 1 219 ? 21.523  18.275  89.035  1.00 23.69  ?  219 PHE   C N   1 
ATOM   9142  C CA  . PHE   C 1 219 ? 20.827  18.010  87.782  1.00 23.26  ?  219 PHE   C CA  1 
ATOM   9143  C C   . PHE   C 1 219 ? 19.538  17.243  88.039  1.00 22.20  ?  219 PHE   C C   1 
ATOM   9144  O O   . PHE   C 1 219 ? 19.483  16.379  88.916  1.00 24.97  ?  219 PHE   C O   1 
ATOM   9145  C CB  . PHE   C 1 219 ? 21.736  17.210  86.850  1.00 22.44  ?  219 PHE   C CB  1 
ATOM   9146  C CG  . PHE   C 1 219 ? 21.385  17.329  85.400  1.00 26.39  ?  219 PHE   C CG  1 
ATOM   9147  C CD1 . PHE   C 1 219 ? 21.860  18.389  84.646  1.00 24.35  ?  219 PHE   C CD1 1 
ATOM   9148  C CD2 . PHE   C 1 219 ? 20.610  16.362  84.779  1.00 23.22  ?  219 PHE   C CD2 1 
ATOM   9149  C CE1 . PHE   C 1 219 ? 21.550  18.499  83.306  1.00 24.34  ?  219 PHE   C CE1 1 
ATOM   9150  C CE2 . PHE   C 1 219 ? 20.299  16.461  83.431  1.00 25.41  ?  219 PHE   C CE2 1 
ATOM   9151  C CZ  . PHE   C 1 219 ? 20.773  17.532  82.693  1.00 25.74  ?  219 PHE   C CZ  1 
ATOM   9152  N N   . VAL   C 1 220 ? 18.496  17.563  87.270  1.00 23.97  ?  220 VAL   C N   1 
ATOM   9153  C CA  . VAL   C 1 220 ? 17.165  16.984  87.445  1.00 23.75  ?  220 VAL   C CA  1 
ATOM   9154  C C   . VAL   C 1 220 ? 16.748  16.335  86.135  1.00 24.65  ?  220 VAL   C C   1 
ATOM   9155  O O   . VAL   C 1 220 ? 16.698  17.001  85.092  1.00 23.73  ?  220 VAL   C O   1 
ATOM   9156  C CB  . VAL   C 1 220 ? 16.128  18.032  87.882  1.00 24.09  ?  220 VAL   C CB  1 
ATOM   9157  C CG1 . VAL   C 1 220 ? 14.757  17.393  88.032  1.00 24.02  ?  220 VAL   C CG1 1 
ATOM   9158  C CG2 . VAL   C 1 220 ? 16.531  18.678  89.188  1.00 23.16  ?  220 VAL   C CG2 1 
ATOM   9159  N N   . VAL   C 1 221 ? 16.448  15.038  86.190  1.00 26.07  ?  221 VAL   C N   1 
ATOM   9160  C CA  . VAL   C 1 221 ? 15.953  14.276  85.048  1.00 23.58  ?  221 VAL   C CA  1 
ATOM   9161  C C   . VAL   C 1 221 ? 14.472  14.021  85.266  1.00 21.50  ?  221 VAL   C C   1 
ATOM   9162  O O   . VAL   C 1 221 ? 14.068  13.567  86.345  1.00 25.60  ?  221 VAL   C O   1 
ATOM   9163  C CB  . VAL   C 1 221 ? 16.704  12.948  84.876  1.00 21.87  ?  221 VAL   C CB  1 
ATOM   9164  C CG1 . VAL   C 1 221 ? 16.217  12.233  83.633  1.00 22.01  ?  221 VAL   C CG1 1 
ATOM   9165  C CG2 . VAL   C 1 221 ? 18.193  13.188  84.806  1.00 25.79  ?  221 VAL   C CG2 1 
ATOM   9166  N N   . MET   C 1 222 ? 13.665  14.331  84.259  1.00 23.73  ?  222 MET   C N   1 
ATOM   9167  C CA  . MET   C 1 222 ? 12.236  14.030  84.277  1.00 25.03  ?  222 MET   C CA  1 
ATOM   9168  C C   . MET   C 1 222 ? 12.036  12.700  83.562  1.00 23.22  ?  222 MET   C C   1 
ATOM   9169  O O   . MET   C 1 222 ? 12.103  12.631  82.334  1.00 25.17  ?  222 MET   C O   1 
ATOM   9170  C CB  . MET   C 1 222 ? 11.425  15.135  83.607  1.00 21.80  ?  222 MET   C CB  1 
ATOM   9171  C CG  . MET   C 1 222 ? 9.922   15.007  83.812  1.00 23.06  ?  222 MET   C CG  1 
ATOM   9172  S SD  . MET   C 1 222 ? 9.334   15.867  85.292  1.00 32.48  ?  222 MET   C SD  1 
ATOM   9173  C CE  . MET   C 1 222 ? 9.436   17.571  84.744  1.00 25.64  ?  222 MET   C CE  1 
ATOM   9174  N N   . ASP   C 1 223 ? 11.803  11.640  84.329  1.00 21.18  ?  223 ASP   C N   1 
ATOM   9175  C CA  . ASP   C 1 223 ? 11.346  10.382  83.748  1.00 23.02  ?  223 ASP   C CA  1 
ATOM   9176  C C   . ASP   C 1 223 ? 9.928   10.581  83.217  1.00 21.93  ?  223 ASP   C C   1 
ATOM   9177  O O   . ASP   C 1 223 ? 8.989   10.751  84.001  1.00 22.16  ?  223 ASP   C O   1 
ATOM   9178  C CB  . ASP   C 1 223 ? 11.409  9.282   84.806  1.00 24.89  ?  223 ASP   C CB  1 
ATOM   9179  C CG  . ASP   C 1 223 ? 11.159  7.900   84.237  1.00 24.74  ?  223 ASP   C CG  1 
ATOM   9180  O OD1 . ASP   C 1 223 ? 10.264  7.746   83.375  1.00 27.03  ?  223 ASP   C OD1 1 
ATOM   9181  O OD2 . ASP   C 1 223 ? 11.865  6.964   84.661  1.00 24.50  ?  223 ASP   C OD2 1 
ATOM   9182  N N   . SER   C 1 224 ? 9.759   10.540  81.890  1.00 20.64  ?  224 SER   C N   1 
ATOM   9183  C CA  . SER   C 1 224 ? 8.581   11.087  81.228  1.00 19.13  ?  224 SER   C CA  1 
ATOM   9184  C C   . SER   C 1 224 ? 7.713   10.039  80.534  1.00 23.20  ?  224 SER   C C   1 
ATOM   9185  O O   . SER   C 1 224 ? 6.963   10.386  79.616  1.00 24.20  ?  224 SER   C O   1 
ATOM   9186  C CB  . SER   C 1 224 ? 9.006   12.136  80.207  1.00 19.93  ?  224 SER   C CB  1 
ATOM   9187  O OG  . SER   C 1 224 ? 9.719   13.171  80.842  1.00 24.05  ?  224 SER   C OG  1 
ATOM   9188  N N   . ALA   C 1 225 ? 7.780   8.772   80.948  1.00 20.13  ?  225 ALA   C N   1 
ATOM   9189  C CA  . ALA   C 1 225 ? 7.006   7.744   80.254  1.00 22.59  ?  225 ALA   C CA  1 
ATOM   9190  C C   . ALA   C 1 225 ? 5.513   8.060   80.258  1.00 20.55  ?  225 ALA   C C   1 
ATOM   9191  O O   . ALA   C 1 225 ? 4.832   7.881   79.241  1.00 21.26  ?  225 ALA   C O   1 
ATOM   9192  C CB  . ALA   C 1 225 ? 7.259   6.375   80.881  1.00 25.57  ?  225 ALA   C CB  1 
ATOM   9193  N N   . ARG   C 1 226 ? 4.980   8.522   81.387  1.00 20.47  ?  226 ARG   C N   1 
ATOM   9194  C CA  . ARG   C 1 226 ? 3.550   8.784   81.452  1.00 19.85  ?  226 ARG   C CA  1 
ATOM   9195  C C   . ARG   C 1 226 ? 3.291   10.241  81.806  1.00 21.20  ?  226 ARG   C C   1 
ATOM   9196  O O   . ARG   C 1 226 ? 2.444   10.543  82.650  1.00 21.16  ?  226 ARG   C O   1 
ATOM   9197  C CB  . ARG   C 1 226 ? 2.888   7.833   82.449  1.00 20.25  ?  226 ARG   C CB  1 
ATOM   9198  C CG  . ARG   C 1 226 ? 3.205   6.379   82.127  1.00 23.37  ?  226 ARG   C CG  1 
ATOM   9199  C CD  . ARG   C 1 226 ? 2.488   5.381   83.023  1.00 25.74  ?  226 ARG   C CD  1 
ATOM   9200  N NE  . ARG   C 1 226 ? 2.822   4.013   82.637  1.00 20.96  ?  226 ARG   C NE  1 
ATOM   9201  C CZ  . ARG   C 1 226 ? 3.929   3.384   83.009  1.00 26.44  ?  226 ARG   C CZ  1 
ATOM   9202  N NH1 . ARG   C 1 226 ? 4.812   3.956   83.820  1.00 25.10  ?  226 ARG   C NH1 1 
ATOM   9203  N NH2 . ARG   C 1 226 ? 4.161   2.153   82.554  1.00 19.77  ?  226 ARG   C NH2 1 
ATOM   9204  N N   . PHE   C 1 227 ? 4.006   11.152  81.143  1.00 20.02  ?  227 PHE   C N   1 
ATOM   9205  C CA  . PHE   C 1 227 ? 3.918   12.564  81.500  1.00 22.09  ?  227 PHE   C CA  1 
ATOM   9206  C C   . PHE   C 1 227 ? 2.564   13.164  81.149  1.00 22.42  ?  227 PHE   C C   1 
ATOM   9207  O O   . PHE   C 1 227 ? 2.131   14.125  81.796  1.00 22.99  ?  227 PHE   C O   1 
ATOM   9208  C CB  . PHE   C 1 227 ? 5.032   13.346  80.812  1.00 21.06  ?  227 PHE   C CB  1 
ATOM   9209  C CG  . PHE   C 1 227 ? 4.839   13.512  79.325  1.00 22.42  ?  227 PHE   C CG  1 
ATOM   9210  C CD1 . PHE   C 1 227 ? 5.114   12.473  78.452  1.00 23.13  ?  227 PHE   C CD1 1 
ATOM   9211  C CD2 . PHE   C 1 227 ? 4.413   14.719  78.799  1.00 22.56  ?  227 PHE   C CD2 1 
ATOM   9212  C CE1 . PHE   C 1 227 ? 4.957   12.628  77.080  1.00 27.15  ?  227 PHE   C CE1 1 
ATOM   9213  C CE2 . PHE   C 1 227 ? 4.253   14.884  77.432  1.00 25.47  ?  227 PHE   C CE2 1 
ATOM   9214  C CZ  . PHE   C 1 227 ? 4.527   13.833  76.566  1.00 25.31  ?  227 PHE   C CZ  1 
ATOM   9215  N N   . CYS   C 1 228 ? 1.888   12.625  80.130  1.00 22.07  ?  228 CYS   C N   1 
ATOM   9216  C CA  . CYS   C 1 228 ? 0.590   13.158  79.729  1.00 23.29  ?  228 CYS   C CA  1 
ATOM   9217  C C   . CYS   C 1 228 ? -0.491  12.794  80.733  1.00 22.16  ?  228 CYS   C C   1 
ATOM   9218  O O   . CYS   C 1 228 ? -1.385  13.602  81.009  1.00 23.86  ?  228 CYS   C O   1 
ATOM   9219  C CB  . CYS   C 1 228 ? 0.214   12.646  78.345  1.00 19.89  ?  228 CYS   C CB  1 
ATOM   9220  S SG  . CYS   C 1 228 ? 1.216   13.313  77.005  1.00 26.67  ?  228 CYS   C SG  1 
ATOM   9221  N N   . GLU   C 1 229 ? -0.444  11.574  81.270  1.00 23.64  ?  229 GLU   C N   1 
ATOM   9222  C CA  . GLU   C 1 229 ? -1.365  11.224  82.344  1.00 24.26  ?  229 GLU   C CA  1 
ATOM   9223  C C   . GLU   C 1 229 ? -1.096  12.071  83.579  1.00 24.26  ?  229 GLU   C C   1 
ATOM   9224  O O   . GLU   C 1 229 ? -2.032  12.430  84.305  1.00 29.89  ?  229 GLU   C O   1 
ATOM   9225  C CB  . GLU   C 1 229 ? -1.266  9.726   82.651  1.00 23.13  ?  229 GLU   C CB  1 
ATOM   9226  C CG  . GLU   C 1 229 ? -1.789  8.864   81.501  1.00 26.64  ?  229 GLU   C CG  1 
ATOM   9227  C CD  . GLU   C 1 229 ? -1.449  7.373   81.598  1.00 25.18  ?  229 GLU   C CD  1 
ATOM   9228  O OE1 . GLU   C 1 229 ? -0.949  6.916   82.644  1.00 27.27  ?  229 GLU   C OE1 1 
ATOM   9229  O OE2 . GLU   C 1 229 ? -1.696  6.652   80.600  1.00 24.69  ?  229 GLU   C OE2 1 
ATOM   9230  N N   . ASN   C 1 230 ? 0.171   12.435  83.813  1.00 24.74  ?  230 ASN   C N   1 
ATOM   9231  C CA  . ASN   C 1 230 ? 0.481   13.349  84.905  1.00 22.17  ?  230 ASN   C CA  1 
ATOM   9232  C C   . ASN   C 1 230 ? -0.069  14.739  84.623  1.00 24.97  ?  230 ASN   C C   1 
ATOM   9233  O O   . ASN   C 1 230 ? -0.591  15.400  85.527  1.00 28.23  ?  230 ASN   C O   1 
ATOM   9234  C CB  . ASN   C 1 230 ? 1.987   13.409  85.139  1.00 21.66  ?  230 ASN   C CB  1 
ATOM   9235  C CG  . ASN   C 1 230 ? 2.332   13.787  86.564  1.00 28.62  ?  230 ASN   C CG  1 
ATOM   9236  O OD1 . ASN   C 1 230 ? 2.336   12.935  87.451  1.00 26.81  ?  230 ASN   C OD1 1 
ATOM   9237  N ND2 . ASN   C 1 230 ? 2.609   15.072  86.797  1.00 25.09  ?  230 ASN   C ND2 1 
ATOM   9238  N N   . ALA   C 1 231 ? 0.036   15.198  83.376  1.00 25.16  ?  231 ALA   C N   1 
ATOM   9239  C CA  . ALA   C 1 231 ? -0.509  16.505  83.023  1.00 24.86  ?  231 ALA   C CA  1 
ATOM   9240  C C   . ALA   C 1 231 ? -2.026  16.525  83.138  1.00 25.41  ?  231 ALA   C C   1 
ATOM   9241  O O   . ALA   C 1 231 ? -2.607  17.540  83.540  1.00 29.79  ?  231 ALA   C O   1 
ATOM   9242  C CB  . ALA   C 1 231 ? -0.072  16.900  81.611  1.00 25.09  ?  231 ALA   C CB  1 
ATOM   9243  N N   . TYR   C 1 232 ? -2.693  15.424  82.792  1.00 25.42  ?  232 TYR   C N   1 
ATOM   9244  C CA  . TYR   C 1 232 ? -4.142  15.377  82.958  1.00 24.49  ?  232 TYR   C CA  1 
ATOM   9245  C C   . TYR   C 1 232 ? -4.517  15.479  84.431  1.00 28.96  ?  232 TYR   C C   1 
ATOM   9246  O O   . TYR   C 1 232 ? -5.417  16.239  84.804  1.00 26.81  ?  232 TYR   C O   1 
ATOM   9247  C CB  . TYR   C 1 232 ? -4.716  14.097  82.350  1.00 22.78  ?  232 TYR   C CB  1 
ATOM   9248  C CG  . TYR   C 1 232 ? -6.212  13.942  82.573  1.00 28.39  ?  232 TYR   C CG  1 
ATOM   9249  C CD1 . TYR   C 1 232 ? -6.709  13.368  83.736  1.00 28.77  ?  232 TYR   C CD1 1 
ATOM   9250  C CD2 . TYR   C 1 232 ? -7.125  14.375  81.622  1.00 27.33  ?  232 TYR   C CD2 1 
ATOM   9251  C CE1 . TYR   C 1 232 ? -8.063  13.233  83.948  1.00 27.19  ?  232 TYR   C CE1 1 
ATOM   9252  C CE2 . TYR   C 1 232 ? -8.486  14.241  81.827  1.00 25.03  ?  232 TYR   C CE2 1 
ATOM   9253  C CZ  . TYR   C 1 232 ? -8.945  13.665  82.993  1.00 27.66  ?  232 TYR   C CZ  1 
ATOM   9254  O OH  . TYR   C 1 232 ? -10.297 13.519  83.217  1.00 32.93  ?  232 TYR   C OH  1 
ATOM   9255  N N   . PHE   C 1 233 ? -3.837  14.704  85.284  1.00 27.34  ?  233 PHE   C N   1 
ATOM   9256  C CA  . PHE   C 1 233 ? -4.112  14.748  86.714  1.00 28.69  ?  233 PHE   C CA  1 
ATOM   9257  C C   . PHE   C 1 233 ? -3.812  16.117  87.304  1.00 30.97  ?  233 PHE   C C   1 
ATOM   9258  O O   . PHE   C 1 233 ? -4.474  16.532  88.260  1.00 28.85  ?  233 PHE   C O   1 
ATOM   9259  C CB  . PHE   C 1 233 ? -3.294  13.685  87.449  1.00 26.41  ?  233 PHE   C CB  1 
ATOM   9260  C CG  . PHE   C 1 233 ? -3.860  12.295  87.350  1.00 29.21  ?  233 PHE   C CG  1 
ATOM   9261  C CD1 . PHE   C 1 233 ? -5.182  12.044  87.676  1.00 26.32  ?  233 PHE   C CD1 1 
ATOM   9262  C CD2 . PHE   C 1 233 ? -3.058  11.235  86.947  1.00 26.15  ?  233 PHE   C CD2 1 
ATOM   9263  C CE1 . PHE   C 1 233 ? -5.700  10.761  87.586  1.00 31.31  ?  233 PHE   C CE1 1 
ATOM   9264  C CE2 . PHE   C 1 233 ? -3.565  9.954   86.859  1.00 24.25  ?  233 PHE   C CE2 1 
ATOM   9265  C CZ  . PHE   C 1 233 ? -4.886  9.714   87.172  1.00 26.96  ?  233 PHE   C CZ  1 
ATOM   9266  N N   . ILE   C 1 234 ? -2.812  16.826  86.773  1.00 28.07  ?  234 ILE   C N   1 
ATOM   9267  C CA  . ILE   C 1 234 ? -2.559  18.181  87.253  1.00 30.20  ?  234 ILE   C CA  1 
ATOM   9268  C C   . ILE   C 1 234 ? -3.735  19.088  86.907  1.00 29.57  ?  234 ILE   C C   1 
ATOM   9269  O O   . ILE   C 1 234 ? -4.216  19.856  87.749  1.00 27.78  ?  234 ILE   C O   1 
ATOM   9270  C CB  . ILE   C 1 234 ? -1.227  18.718  86.692  1.00 27.38  ?  234 ILE   C CB  1 
ATOM   9271  C CG1 . ILE   C 1 234 ? -0.041  18.130  87.465  1.00 27.63  ?  234 ILE   C CG1 1 
ATOM   9272  C CG2 . ILE   C 1 234 ? -1.186  20.238  86.773  1.00 30.18  ?  234 ILE   C CG2 1 
ATOM   9273  C CD1 . ILE   C 1 234 ? 1.318   18.566  86.929  1.00 27.26  ?  234 ILE   C CD1 1 
ATOM   9274  N N   . LYS   C 1 235 ? -4.248  18.981  85.683  1.00 27.59  ?  235 LYS   C N   1 
ATOM   9275  C CA  . LYS   C 1 235 ? -5.388  19.808  85.294  1.00 30.59  ?  235 LYS   C CA  1 
ATOM   9276  C C   . LYS   C 1 235 ? -6.656  19.432  86.059  1.00 33.26  ?  235 LYS   C C   1 
ATOM   9277  O O   . LYS   C 1 235 ? -7.468  20.311  86.383  1.00 32.36  ?  235 LYS   C O   1 
ATOM   9278  C CB  . LYS   C 1 235 ? -5.624  19.708  83.786  1.00 28.58  ?  235 LYS   C CB  1 
ATOM   9279  C CG  . LYS   C 1 235 ? -6.780  20.564  83.312  1.00 33.06  ?  235 LYS   C CG  1 
ATOM   9280  C CD  . LYS   C 1 235 ? -6.954  20.549  81.816  1.00 29.11  ?  235 LYS   C CD  1 
ATOM   9281  C CE  . LYS   C 1 235 ? -8.209  21.326  81.439  1.00 31.56  ?  235 LYS   C CE  1 
ATOM   9282  N NZ  . LYS   C 1 235 ? -8.164  21.780  80.018  1.00 36.62  ?  235 LYS   C NZ  1 
ATOM   9283  N N   . ALA   C 1 236 ? -6.844  18.146  86.365  1.00 31.76  ?  236 ALA   C N   1 
ATOM   9284  C CA  . ALA   C 1 236 ? -8.037  17.740  87.102  1.00 30.09  ?  236 ALA   C CA  1 
ATOM   9285  C C   . ALA   C 1 236 ? -8.010  18.248  88.538  1.00 37.44  ?  236 ALA   C C   1 
ATOM   9286  O O   . ALA   C 1 236 ? -9.030  18.725  89.050  1.00 41.73  ?  236 ALA   C O   1 
ATOM   9287  C CB  . ALA   C 1 236 ? -8.184  16.218  87.081  1.00 27.74  ?  236 ALA   C CB  1 
ATOM   9288  N N   . ARG   C 1 237 ? -6.855  18.175  89.201  1.00 32.69  ?  237 ARG   C N   1 
ATOM   9289  C CA  . ARG   C 1 237 ? -6.800  18.345  90.644  1.00 29.85  ?  237 ARG   C CA  1 
ATOM   9290  C C   . ARG   C 1 237 ? -6.123  19.625  91.112  1.00 34.09  ?  237 ARG   C C   1 
ATOM   9291  O O   . ARG   C 1 237 ? -6.164  19.915  92.311  1.00 40.96  ?  237 ARG   C O   1 
ATOM   9292  C CB  . ARG   C 1 237 ? -6.089  17.142  91.281  1.00 33.09  ?  237 ARG   C CB  1 
ATOM   9293  C CG  . ARG   C 1 237 ? -6.720  15.823  90.903  1.00 34.79  ?  237 ARG   C CG  1 
ATOM   9294  C CD  . ARG   C 1 237 ? -5.982  14.639  91.494  1.00 30.66  ?  237 ARG   C CD  1 
ATOM   9295  N NE  . ARG   C 1 237 ? -6.641  13.396  91.110  1.00 33.35  ?  237 ARG   C NE  1 
ATOM   9296  C CZ  . ARG   C 1 237 ? -6.160  12.184  91.348  1.00 32.19  ?  237 ARG   C CZ  1 
ATOM   9297  N NH1 . ARG   C 1 237 ? -4.995  12.008  91.954  1.00 29.33  ?  237 ARG   C NH1 1 
ATOM   9298  N NH2 . ARG   C 1 237 ? -6.866  11.123  90.969  1.00 31.31  ?  237 ARG   C NH2 1 
ATOM   9299  N N   . ASP   C 1 238 ? -5.497  20.391  90.225  1.00 34.16  ?  238 ASP   C N   1 
ATOM   9300  C CA  . ASP   C 1 238 ? -4.866  21.639  90.644  1.00 36.21  ?  238 ASP   C CA  1 
ATOM   9301  C C   . ASP   C 1 238 ? -5.703  22.810  90.152  1.00 37.37  ?  238 ASP   C C   1 
ATOM   9302  O O   . ASP   C 1 238 ? -5.787  23.033  88.932  1.00 35.01  ?  238 ASP   C O   1 
ATOM   9303  C CB  . ASP   C 1 238 ? -3.433  21.740  90.115  1.00 33.02  ?  238 ASP   C CB  1 
ATOM   9304  C CG  . ASP   C 1 238 ? -2.670  22.928  90.694  1.00 38.09  ?  238 ASP   C CG  1 
ATOM   9305  O OD1 . ASP   C 1 238 ? -3.312  23.885  91.181  1.00 41.62  ?  238 ASP   C OD1 1 
ATOM   9306  O OD2 . ASP   C 1 238 ? -1.420  22.913  90.655  1.00 38.20  ?  238 ASP   C OD2 1 
ATOM   9307  N N   . PRO   C 1 239 ? -6.325  23.582  91.052  1.00 33.88  ?  239 PRO   C N   1 
ATOM   9308  C CA  . PRO   C 1 239 ? -7.148  24.722  90.607  1.00 41.02  ?  239 PRO   C CA  1 
ATOM   9309  C C   . PRO   C 1 239 ? -6.388  25.725  89.761  1.00 36.74  ?  239 PRO   C C   1 
ATOM   9310  O O   . PRO   C 1 239 ? -6.990  26.391  88.909  1.00 43.19  ?  239 PRO   C O   1 
ATOM   9311  C CB  . PRO   C 1 239 ? -7.618  25.351  91.927  1.00 40.08  ?  239 PRO   C CB  1 
ATOM   9312  C CG  . PRO   C 1 239 ? -7.495  24.258  92.939  1.00 43.53  ?  239 PRO   C CG  1 
ATOM   9313  C CD  . PRO   C 1 239 ? -6.336  23.415  92.514  1.00 33.98  ?  239 PRO   C CD  1 
ATOM   9314  N N   . LYS   C 1 240 ? -5.078  25.847  89.973  1.00 37.18  ?  240 LYS   C N   1 
ATOM   9315  C CA  . LYS   C 1 240 ? -4.268  26.775  89.193  1.00 36.27  ?  240 LYS   C CA  1 
ATOM   9316  C C   . LYS   C 1 240 ? -4.319  26.458  87.703  1.00 37.93  ?  240 LYS   C C   1 
ATOM   9317  O O   . LYS   C 1 240 ? -4.229  27.365  86.870  1.00 40.12  ?  240 LYS   C O   1 
ATOM   9318  C CB  . LYS   C 1 240 ? -2.830  26.739  89.720  1.00 35.44  ?  240 LYS   C CB  1 
ATOM   9319  C CG  . LYS   C 1 240 ? -1.779  27.355  88.817  1.00 40.26  ?  240 LYS   C CG  1 
ATOM   9320  C CD  . LYS   C 1 240 ? -1.888  28.862  88.785  1.00 49.95  ?  240 LYS   C CD  1 
ATOM   9321  C CE  . LYS   C 1 240 ? -0.595  29.472  88.283  1.00 50.00  ?  240 LYS   C CE  1 
ATOM   9322  N NZ  . LYS   C 1 240 ? 0.572   28.976  89.062  1.00 43.59  ?  240 LYS   C NZ  1 
ATOM   9323  N N   . TYR   C 1 241 ? -4.486  25.184  87.348  1.00 40.32  ?  241 TYR   C N   1 
ATOM   9324  C CA  . TYR   C 1 241 ? -4.491  24.743  85.958  1.00 35.74  ?  241 TYR   C CA  1 
ATOM   9325  C C   . TYR   C 1 241 ? -5.876  24.295  85.496  1.00 38.06  ?  241 TYR   C C   1 
ATOM   9326  O O   . TYR   C 1 241 ? -5.992  23.535  84.527  1.00 36.93  ?  241 TYR   C O   1 
ATOM   9327  C CB  . TYR   C 1 241 ? -3.458  23.631  85.771  1.00 37.23  ?  241 TYR   C CB  1 
ATOM   9328  C CG  . TYR   C 1 241 ? -2.051  24.148  85.934  1.00 32.54  ?  241 TYR   C CG  1 
ATOM   9329  C CD1 . TYR   C 1 241 ? -1.375  24.696  84.858  1.00 34.37  ?  241 TYR   C CD1 1 
ATOM   9330  C CD2 . TYR   C 1 241 ? -1.421  24.139  87.168  1.00 31.22  ?  241 TYR   C CD2 1 
ATOM   9331  C CE1 . TYR   C 1 241 ? -0.103  25.197  84.998  1.00 34.32  ?  241 TYR   C CE1 1 
ATOM   9332  C CE2 . TYR   C 1 241 ? -0.150  24.643  87.316  1.00 31.73  ?  241 TYR   C CE2 1 
ATOM   9333  C CZ  . TYR   C 1 241 ? 0.505   25.171  86.223  1.00 32.59  ?  241 TYR   C CZ  1 
ATOM   9334  O OH  . TYR   C 1 241 ? 1.782   25.672  86.341  1.00 35.61  ?  241 TYR   C OH  1 
ATOM   9335  N N   . LYS   C 1 242 ? -6.929  24.781  86.159  1.00 39.68  ?  242 LYS   C N   1 
ATOM   9336  C CA  . LYS   C 1 242 ? -8.287  24.345  85.849  1.00 38.09  ?  242 LYS   C CA  1 
ATOM   9337  C C   . LYS   C 1 242 ? -8.664  24.651  84.403  1.00 35.96  ?  242 LYS   C C   1 
ATOM   9338  O O   . LYS   C 1 242 ? -9.333  23.845  83.745  1.00 37.52  ?  242 LYS   C O   1 
ATOM   9339  C CB  . LYS   C 1 242 ? -9.267  25.007  86.819  1.00 39.53  ?  242 LYS   C CB  1 
ATOM   9340  C CG  . LYS   C 1 242 ? -10.732 24.732  86.548  1.00 43.68  ?  242 LYS   C CG  1 
ATOM   9341  C CD  . LYS   C 1 242 ? -11.612 25.533  87.492  1.00 45.48  ?  242 LYS   C CD  1 
ATOM   9342  C CE  . LYS   C 1 242 ? -13.078 25.325  87.167  1.00 54.68  ?  242 LYS   C CE  1 
ATOM   9343  N NZ  . LYS   C 1 242 ? -13.386 25.650  85.739  1.00 53.24  ?  242 LYS   C NZ  1 
ATOM   9344  N N   . ASN   C 1 243 ? -8.239  25.804  83.884  1.00 33.40  ?  243 ASN   C N   1 
ATOM   9345  C CA  . ASN   C 1 243 ? -8.598  26.227  82.536  1.00 36.88  ?  243 ASN   C CA  1 
ATOM   9346  C C   . ASN   C 1 243 ? -7.402  26.244  81.592  1.00 37.00  ?  243 ASN   C C   1 
ATOM   9347  O O   . ASN   C 1 243 ? -7.444  26.907  80.551  1.00 39.90  ?  243 ASN   C O   1 
ATOM   9348  C CB  . ASN   C 1 243 ? -9.273  27.598  82.574  1.00 50.06  ?  243 ASN   C CB  1 
ATOM   9349  C CG  . ASN   C 1 243 ? -10.769 27.504  82.819  1.00 48.01  ?  243 ASN   C CG  1 
ATOM   9350  O OD1 . ASN   C 1 243 ? -11.283 28.028  83.807  1.00 54.23  ?  243 ASN   C OD1 1 
ATOM   9351  N ND2 . ASN   C 1 243 ? -11.477 26.836  81.910  1.00 53.21  ?  243 ASN   C ND2 1 
ATOM   9352  N N   . ALA   C 1 244 ? -6.343  25.519  81.929  1.00 34.95  ?  244 ALA   C N   1 
ATOM   9353  C CA  . ALA   C 1 244 ? -5.186  25.380  81.062  1.00 33.89  ?  244 ALA   C CA  1 
ATOM   9354  C C   . ALA   C 1 244 ? -5.374  24.197  80.117  1.00 33.64  ?  244 ALA   C C   1 
ATOM   9355  O O   . ALA   C 1 244 ? -6.041  23.214  80.448  1.00 33.74  ?  244 ALA   C O   1 
ATOM   9356  C CB  . ALA   C 1 244 ? -3.914  25.190  81.895  1.00 30.44  ?  244 ALA   C CB  1 
ATOM   9357  N N   . THR   C 1 245 ? -4.790  24.303  78.927  1.00 31.10  ?  245 THR   C N   1 
ATOM   9358  C CA  . THR   C 1 245 ? -4.747  23.154  78.036  1.00 30.79  ?  245 THR   C CA  1 
ATOM   9359  C C   . THR   C 1 245 ? -3.741  22.130  78.556  1.00 28.85  ?  245 THR   C C   1 
ATOM   9360  O O   . THR   C 1 245 ? -2.863  22.441  79.365  1.00 32.67  ?  245 THR   C O   1 
ATOM   9361  C CB  . THR   C 1 245 ? -4.381  23.585  76.620  1.00 29.97  ?  245 THR   C CB  1 
ATOM   9362  O OG1 . THR   C 1 245 ? -3.006  23.974  76.580  1.00 29.32  ?  245 THR   C OG1 1 
ATOM   9363  C CG2 . THR   C 1 245 ? -5.232  24.767  76.200  1.00 29.67  ?  245 THR   C CG2 1 
ATOM   9364  N N   . ILE   C 1 246 ? -3.884  20.884  78.093  1.00 30.48  ?  246 ILE   C N   1 
ATOM   9365  C CA  . ILE   C 1 246 ? -2.944  19.840  78.500  1.00 27.19  ?  246 ILE   C CA  1 
ATOM   9366  C C   . ILE   C 1 246 ? -1.521  20.208  78.092  1.00 27.95  ?  246 ILE   C C   1 
ATOM   9367  O O   . ILE   C 1 246 ? -0.570  19.994  78.853  1.00 31.10  ?  246 ILE   C O   1 
ATOM   9368  C CB  . ILE   C 1 246 ? -3.362  18.474  77.924  1.00 26.42  ?  246 ILE   C CB  1 
ATOM   9369  C CG1 . ILE   C 1 246 ? -4.616  17.964  78.634  1.00 26.19  ?  246 ILE   C CG1 1 
ATOM   9370  C CG2 . ILE   C 1 246 ? -2.225  17.459  78.062  1.00 24.37  ?  246 ILE   C CG2 1 
ATOM   9371  C CD1 . ILE   C 1 246 ? -4.431  17.777  80.121  1.00 24.01  ?  246 ILE   C CD1 1 
ATOM   9372  N N   . LYS   C 1 247 ? -1.350  20.779  76.895  1.00 27.58  ?  247 LYS   C N   1 
ATOM   9373  C CA  . LYS   C 1 247 ? -0.016  21.188  76.463  1.00 27.20  ?  247 LYS   C CA  1 
ATOM   9374  C C   . LYS   C 1 247 ? 0.533   22.326  77.318  1.00 29.42  ?  247 LYS   C C   1 
ATOM   9375  O O   . LYS   C 1 247 ? 1.747   22.395  77.546  1.00 31.30  ?  247 LYS   C O   1 
ATOM   9376  C CB  . LYS   C 1 247 ? -0.036  21.602  74.996  1.00 24.03  ?  247 LYS   C CB  1 
ATOM   9377  C CG  . LYS   C 1 247 ? -0.107  20.445  74.018  1.00 25.53  ?  247 LYS   C CG  1 
ATOM   9378  C CD  . LYS   C 1 247 ? -0.204  20.957  72.596  1.00 26.99  ?  247 LYS   C CD  1 
ATOM   9379  C CE  . LYS   C 1 247 ? -0.253  19.820  71.596  1.00 34.33  ?  247 LYS   C CE  1 
ATOM   9380  N NZ  . LYS   C 1 247 ? -0.201  20.327  70.194  1.00 38.18  ?  247 LYS   C NZ  1 
ATOM   9381  N N   . GLU   C 1 248 ? -0.332  23.232  77.781  1.00 29.29  ?  248 GLU   C N   1 
ATOM   9382  C CA  . GLU   C 1 248 ? 0.115   24.279  78.697  1.00 30.04  ?  248 GLU   C CA  1 
ATOM   9383  C C   . GLU   C 1 248 ? 0.559   23.696  80.028  1.00 29.33  ?  248 GLU   C C   1 
ATOM   9384  O O   . GLU   C 1 248 ? 1.463   24.239  80.673  1.00 34.40  ?  248 GLU   C O   1 
ATOM   9385  C CB  . GLU   C 1 248 ? -1.000  25.303  78.924  1.00 28.10  ?  248 GLU   C CB  1 
ATOM   9386  C CG  . GLU   C 1 248 ? -1.247  26.235  77.751  1.00 33.60  ?  248 GLU   C CG  1 
ATOM   9387  C CD  . GLU   C 1 248 ? -2.510  27.061  77.910  1.00 39.29  ?  248 GLU   C CD  1 
ATOM   9388  O OE1 . GLU   C 1 248 ? -3.332  26.730  78.796  1.00 36.35  ?  248 GLU   C OE1 1 
ATOM   9389  O OE2 . GLU   C 1 248 ? -2.680  28.043  77.148  1.00 42.62  ?  248 GLU   C OE2 1 
ATOM   9390  N N   . VAL   C 1 249 ? -0.068  22.603  80.461  1.00 29.81  ?  249 VAL   C N   1 
ATOM   9391  C CA  . VAL   C 1 249 ? 0.353   21.964  81.700  1.00 29.16  ?  249 VAL   C CA  1 
ATOM   9392  C C   . VAL   C 1 249 ? 1.695   21.278  81.506  1.00 28.99  ?  249 VAL   C C   1 
ATOM   9393  O O   . VAL   C 1 249 ? 2.579   21.356  82.367  1.00 27.49  ?  249 VAL   C O   1 
ATOM   9394  C CB  . VAL   C 1 249 ? -0.724  20.979  82.179  1.00 26.53  ?  249 VAL   C CB  1 
ATOM   9395  C CG1 . VAL   C 1 249 ? -0.211  20.190  83.365  1.00 23.92  ?  249 VAL   C CG1 1 
ATOM   9396  C CG2 . VAL   C 1 249 ? -2.004  21.728  82.520  1.00 30.74  ?  249 VAL   C CG2 1 
ATOM   9397  N N   . ILE   C 1 250 ? 1.873   20.612  80.362  1.00 28.12  ?  250 ILE   C N   1 
ATOM   9398  C CA  . ILE   C 1 250 ? 3.153   19.977  80.050  1.00 26.77  ?  250 ILE   C CA  1 
ATOM   9399  C C   . ILE   C 1 250 ? 4.261   21.020  79.997  1.00 28.81  ?  250 ILE   C C   1 
ATOM   9400  O O   . ILE   C 1 250 ? 5.330   20.847  80.595  1.00 28.38  ?  250 ILE   C O   1 
ATOM   9401  C CB  . ILE   C 1 250 ? 3.052   19.204  78.724  1.00 23.66  ?  250 ILE   C CB  1 
ATOM   9402  C CG1 . ILE   C 1 250 ? 2.137   17.988  78.885  1.00 23.06  ?  250 ILE   C CG1 1 
ATOM   9403  C CG2 . ILE   C 1 250 ? 4.440   18.828  78.222  1.00 23.14  ?  250 ILE   C CG2 1 
ATOM   9404  C CD1 . ILE   C 1 250 ? 1.678   17.386  77.564  1.00 27.58  ?  250 ILE   C CD1 1 
ATOM   9405  N N   . PHE   C 1 251 ? 4.012   22.125  79.285  1.00 29.42  ?  251 PHE   C N   1 
ATOM   9406  C CA  . PHE   C 1 251 ? 5.027   23.158  79.111  1.00 27.92  ?  251 PHE   C CA  1 
ATOM   9407  C C   . PHE   C 1 251 ? 5.514   23.685  80.453  1.00 30.06  ?  251 PHE   C C   1 
ATOM   9408  O O   . PHE   C 1 251 ? 6.705   23.973  80.622  1.00 29.96  ?  251 PHE   C O   1 
ATOM   9409  C CB  . PHE   C 1 251 ? 4.462   24.287  78.247  1.00 31.15  ?  251 PHE   C CB  1 
ATOM   9410  C CG  . PHE   C 1 251 ? 5.499   25.255  77.739  1.00 32.15  ?  251 PHE   C CG  1 
ATOM   9411  C CD1 . PHE   C 1 251 ? 6.142   25.032  76.531  1.00 31.34  ?  251 PHE   C CD1 1 
ATOM   9412  C CD2 . PHE   C 1 251 ? 5.811   26.401  78.454  1.00 32.99  ?  251 PHE   C CD2 1 
ATOM   9413  C CE1 . PHE   C 1 251 ? 7.088   25.923  76.056  1.00 30.16  ?  251 PHE   C CE1 1 
ATOM   9414  C CE2 . PHE   C 1 251 ? 6.756   27.296  77.983  1.00 30.68  ?  251 PHE   C CE2 1 
ATOM   9415  C CZ  . PHE   C 1 251 ? 7.394   27.055  76.783  1.00 30.43  ?  251 PHE   C CZ  1 
ATOM   9416  N N   . ASP   C 1 252 ? 4.613   23.796  81.430  1.00 31.47  ?  252 ASP   C N   1 
ATOM   9417  C CA  . ASP   C 1 252 ? 5.034   24.231  82.755  1.00 28.27  ?  252 ASP   C CA  1 
ATOM   9418  C C   . ASP   C 1 252 ? 5.812   23.139  83.472  1.00 30.70  ?  252 ASP   C C   1 
ATOM   9419  O O   . ASP   C 1 252 ? 6.790   23.428  84.174  1.00 27.89  ?  252 ASP   C O   1 
ATOM   9420  C CB  . ASP   C 1 252 ? 3.824   24.654  83.585  1.00 30.87  ?  252 ASP   C CB  1 
ATOM   9421  C CG  . ASP   C 1 252 ? 3.418   26.085  83.326  1.00 32.90  ?  252 ASP   C CG  1 
ATOM   9422  O OD1 . ASP   C 1 252 ? 3.988   26.704  82.403  1.00 33.27  ?  252 ASP   C OD1 1 
ATOM   9423  O OD2 . ASP   C 1 252 ? 2.537   26.594  84.048  1.00 40.75  ?  252 ASP   C OD2 1 
ATOM   9424  N N   . MET   C 1 253 ? 5.392   21.879  83.303  1.00 31.27  ?  253 MET   C N   1 
ATOM   9425  C CA  . MET   C 1 253 ? 6.051   20.770  83.986  1.00 29.06  ?  253 MET   C CA  1 
ATOM   9426  C C   . MET   C 1 253 ? 7.542   20.761  83.702  1.00 27.87  ?  253 MET   C C   1 
ATOM   9427  O O   . MET   C 1 253 ? 8.355   20.568  84.612  1.00 28.85  ?  253 MET   C O   1 
ATOM   9428  C CB  . MET   C 1 253 ? 5.432   19.438  83.559  1.00 29.39  ?  253 MET   C CB  1 
ATOM   9429  C CG  . MET   C 1 253 ? 4.276   18.952  84.412  1.00 24.33  ?  253 MET   C CG  1 
ATOM   9430  S SD  . MET   C 1 253 ? 3.378   17.596  83.614  1.00 27.22  ?  253 MET   C SD  1 
ATOM   9431  C CE  . MET   C 1 253 ? 4.657   16.349  83.539  1.00 26.47  ?  253 MET   C CE  1 
ATOM   9432  N N   . TYR   C 1 254 ? 7.920   20.999  82.453  1.00 24.97  ?  254 TYR   C N   1 
ATOM   9433  C CA  . TYR   C 1 254 ? 9.301   20.842  82.026  1.00 27.58  ?  254 TYR   C CA  1 
ATOM   9434  C C   . TYR   C 1 254 ? 10.147  22.091  82.250  1.00 30.88  ?  254 TYR   C C   1 
ATOM   9435  O O   . TYR   C 1 254 ? 11.335  22.089  81.905  1.00 31.80  ?  254 TYR   C O   1 
ATOM   9436  C CB  . TYR   C 1 254 ? 9.318   20.376  80.569  1.00 25.94  ?  254 TYR   C CB  1 
ATOM   9437  C CG  . TYR   C 1 254 ? 8.885   18.931  80.539  1.00 27.77  ?  254 TYR   C CG  1 
ATOM   9438  C CD1 . TYR   C 1 254 ? 7.542   18.588  80.538  1.00 25.36  ?  254 TYR   C CD1 1 
ATOM   9439  C CD2 . TYR   C 1 254 ? 9.826   17.906  80.611  1.00 29.54  ?  254 TYR   C CD2 1 
ATOM   9440  C CE1 . TYR   C 1 254 ? 7.146   17.269  80.562  1.00 24.98  ?  254 TYR   C CE1 1 
ATOM   9441  C CE2 . TYR   C 1 254 ? 9.441   16.588  80.633  1.00 22.42  ?  254 TYR   C CE2 1 
ATOM   9442  C CZ  . TYR   C 1 254 ? 8.102   16.275  80.613  1.00 26.13  ?  254 TYR   C CZ  1 
ATOM   9443  O OH  . TYR   C 1 254 ? 7.720   14.957  80.637  1.00 25.72  ?  254 TYR   C OH  1 
ATOM   9444  N N   . LYS   C 1 255 ? 9.572   23.138  82.852  1.00 30.54  ?  255 LYS   C N   1 
ATOM   9445  C CA  . LYS   C 1 255 ? 10.364  24.188  83.478  1.00 29.41  ?  255 LYS   C CA  1 
ATOM   9446  C C   . LYS   C 1 255 ? 11.075  23.698  84.733  1.00 31.27  ?  255 LYS   C C   1 
ATOM   9447  O O   . LYS   C 1 255 ? 11.930  24.411  85.265  1.00 30.75  ?  255 LYS   C O   1 
ATOM   9448  C CB  . LYS   C 1 255 ? 9.480   25.383  83.856  1.00 31.97  ?  255 LYS   C CB  1 
ATOM   9449  C CG  . LYS   C 1 255 ? 8.599   25.943  82.749  1.00 30.47  ?  255 LYS   C CG  1 
ATOM   9450  C CD  . LYS   C 1 255 ? 7.775   27.113  83.286  1.00 29.58  ?  255 LYS   C CD  1 
ATOM   9451  C CE  . LYS   C 1 255 ? 6.934   27.798  82.207  1.00 29.65  ?  255 LYS   C CE  1 
ATOM   9452  N NZ  . LYS   C 1 255 ? 7.759   28.234  81.045  1.00 42.31  ?  255 LYS   C NZ  1 
ATOM   9453  N N   . TYR   C 1 256 ? 10.741  22.507  85.222  1.00 30.66  ?  256 TYR   C N   1 
ATOM   9454  C CA  . TYR   C 1 256 ? 11.244  22.011  86.494  1.00 30.43  ?  256 TYR   C CA  1 
ATOM   9455  C C   . TYR   C 1 256 ? 12.054  20.736  86.311  1.00 32.01  ?  256 TYR   C C   1 
ATOM   9456  O O   . TYR   C 1 256 ? 12.037  19.840  87.159  1.00 32.00  ?  256 TYR   C O   1 
ATOM   9457  C CB  . TYR   C 1 256 ? 10.091  21.805  87.470  1.00 33.15  ?  256 TYR   C CB  1 
ATOM   9458  C CG  . TYR   C 1 256 ? 9.188   23.016  87.523  1.00 34.78  ?  256 TYR   C CG  1 
ATOM   9459  C CD1 . TYR   C 1 256 ? 9.667   24.232  87.995  1.00 35.94  ?  256 TYR   C CD1 1 
ATOM   9460  C CD2 . TYR   C 1 256 ? 7.875   22.953  87.087  1.00 27.61  ?  256 TYR   C CD2 1 
ATOM   9461  C CE1 . TYR   C 1 256 ? 8.862   25.347  88.040  1.00 34.52  ?  256 TYR   C CE1 1 
ATOM   9462  C CE2 . TYR   C 1 256 ? 7.061   24.065  87.133  1.00 31.91  ?  256 TYR   C CE2 1 
ATOM   9463  C CZ  . TYR   C 1 256 ? 7.563   25.260  87.610  1.00 31.18  ?  256 TYR   C CZ  1 
ATOM   9464  O OH  . TYR   C 1 256 ? 6.769   26.379  87.661  1.00 38.41  ?  256 TYR   C OH  1 
ATOM   9465  N N   . ALA   C 1 257 ? 12.765  20.650  85.193  1.00 29.62  ?  257 ALA   C N   1 
ATOM   9466  C CA  . ALA   C 1 257 ? 13.752  19.611  84.976  1.00 27.07  ?  257 ALA   C CA  1 
ATOM   9467  C C   . ALA   C 1 257 ? 14.777  20.149  83.993  1.00 25.67  ?  257 ALA   C C   1 
ATOM   9468  O O   . ALA   C 1 257 ? 14.540  21.148  83.309  1.00 29.44  ?  257 ALA   C O   1 
ATOM   9469  C CB  . ALA   C 1 257 ? 13.112  18.319  84.464  1.00 26.67  ?  257 ALA   C CB  1 
ATOM   9470  N N   . ASP   C 1 258 ? 15.931  19.484  83.943  1.00 27.95  ?  258 ASP   C N   1 
ATOM   9471  C CA  . ASP   C 1 258 ? 17.023  19.870  83.055  1.00 26.92  ?  258 ASP   C CA  1 
ATOM   9472  C C   . ASP   C 1 258 ? 17.109  18.990  81.824  1.00 25.77  ?  258 ASP   C C   1 
ATOM   9473  O O   . ASP   C 1 258 ? 17.757  19.370  80.841  1.00 25.63  ?  258 ASP   C O   1 
ATOM   9474  C CB  . ASP   C 1 258 ? 18.356  19.813  83.809  1.00 26.22  ?  258 ASP   C CB  1 
ATOM   9475  C CG  . ASP   C 1 258 ? 18.391  20.756  85.003  1.00 26.60  ?  258 ASP   C CG  1 
ATOM   9476  O OD1 . ASP   C 1 258 ? 18.118  21.959  84.803  1.00 27.11  ?  258 ASP   C OD1 1 
ATOM   9477  O OD2 . ASP   C 1 258 ? 18.668  20.301  86.137  1.00 25.81  ?  258 ASP   C OD2 1 
ATOM   9478  N N   . ALA   C 1 259 ? 16.467  17.830  81.866  1.00 27.90  ?  259 ALA   C N   1 
ATOM   9479  C CA  . ALA   C 1 259 ? 16.524  16.849  80.797  1.00 21.33  ?  259 ALA   C CA  1 
ATOM   9480  C C   . ALA   C 1 259 ? 15.386  15.875  81.031  1.00 18.67  ?  259 ALA   C C   1 
ATOM   9481  O O   . ALA   C 1 259 ? 14.777  15.857  82.103  1.00 20.30  ?  259 ALA   C O   1 
ATOM   9482  C CB  . ALA   C 1 259 ? 17.874  16.132  80.778  1.00 20.20  ?  259 ALA   C CB  1 
ATOM   9483  N N   . LEU   C 1 260 ? 15.097  15.063  80.020  1.00 23.72  ?  260 LEU   C N   1 
ATOM   9484  C CA  . LEU   C 1 260 ? 14.104  14.016  80.187  1.00 22.71  ?  260 LEU   C CA  1 
ATOM   9485  C C   . LEU   C 1 260 ? 14.596  12.718  79.566  1.00 22.31  ?  260 LEU   C C   1 
ATOM   9486  O O   . LEU   C 1 260 ? 15.338  12.707  78.577  1.00 24.08  ?  260 LEU   C O   1 
ATOM   9487  C CB  . LEU   C 1 260 ? 12.734  14.404  79.591  1.00 21.75  ?  260 LEU   C CB  1 
ATOM   9488  C CG  . LEU   C 1 260 ? 12.559  14.660  78.094  1.00 23.00  ?  260 LEU   C CG  1 
ATOM   9489  C CD1 . LEU   C 1 260 ? 12.258  13.387  77.335  1.00 21.90  ?  260 LEU   C CD1 1 
ATOM   9490  C CD2 . LEU   C 1 260 ? 11.460  15.678  77.861  1.00 23.65  ?  260 LEU   C CD2 1 
ATOM   9491  N N   . THR   C 1 261 ? 14.191  11.625  80.191  1.00 21.49  ?  261 THR   C N   1 
ATOM   9492  C CA  . THR   C 1 261 ? 14.241  10.299  79.606  1.00 19.56  ?  261 THR   C CA  1 
ATOM   9493  C C   . THR   C 1 261 ? 12.802  9.845   79.454  1.00 20.42  ?  261 THR   C C   1 
ATOM   9494  O O   . THR   C 1 261 ? 12.021  9.919   80.408  1.00 19.95  ?  261 THR   C O   1 
ATOM   9495  C CB  . THR   C 1 261 ? 15.018  9.325   80.490  1.00 21.47  ?  261 THR   C CB  1 
ATOM   9496  O OG1 . THR   C 1 261 ? 14.449  9.325   81.807  1.00 22.46  ?  261 THR   C OG1 1 
ATOM   9497  C CG2 . THR   C 1 261 ? 16.481  9.728   80.568  1.00 23.01  ?  261 THR   C CG2 1 
ATOM   9498  N N   . MET   C 1 262 ? 12.446  9.405   78.257  1.00 19.41  ?  262 MET   C N   1 
ATOM   9499  C CA  . MET   C 1 262 ? 11.070  9.058   77.961  1.00 22.79  ?  262 MET   C CA  1 
ATOM   9500  C C   . MET   C 1 262 ? 11.016  7.692   77.311  1.00 20.52  ?  262 MET   C C   1 
ATOM   9501  O O   . MET   C 1 262 ? 11.686  7.456   76.302  1.00 21.33  ?  262 MET   C O   1 
ATOM   9502  C CB  . MET   C 1 262 ? 10.426  10.084  77.031  1.00 19.80  ?  262 MET   C CB  1 
ATOM   9503  C CG  . MET   C 1 262 ? 9.013   9.709   76.642  1.00 26.27  ?  262 MET   C CG  1 
ATOM   9504  S SD  . MET   C 1 262 ? 8.358   10.876  75.461  1.00 27.62  ?  262 MET   C SD  1 
ATOM   9505  C CE  . MET   C 1 262 ? 8.444   12.369  76.435  1.00 26.38  ?  262 MET   C CE  1 
ATOM   9506  N N   . SER   C 1 263 ? 10.220  6.800   77.881  1.00 19.33  ?  263 SER   C N   1 
ATOM   9507  C CA  . SER   C 1 263 ? 9.772   5.637   77.132  1.00 19.95  ?  263 SER   C CA  1 
ATOM   9508  C C   . SER   C 1 263 ? 8.582   6.073   76.295  1.00 19.24  ?  263 SER   C C   1 
ATOM   9509  O O   . SER   C 1 263 ? 7.510   6.368   76.837  1.00 19.41  ?  263 SER   C O   1 
ATOM   9510  C CB  . SER   C 1 263 ? 9.398   4.485   78.055  1.00 18.81  ?  263 SER   C CB  1 
ATOM   9511  O OG  . SER   C 1 263 ? 8.892   3.421   77.263  1.00 21.88  ?  263 SER   C OG  1 
ATOM   9512  N N   . ALA   C 1 264 ? 8.768   6.139   74.978  1.00 22.55  ?  264 ALA   C N   1 
ATOM   9513  C CA  . ALA   C 1 264 ? 7.670   6.525   74.107  1.00 19.71  ?  264 ALA   C CA  1 
ATOM   9514  C C   . ALA   C 1 264 ? 6.639   5.418   73.941  1.00 18.88  ?  264 ALA   C C   1 
ATOM   9515  O O   . ALA   C 1 264 ? 5.606   5.649   73.304  1.00 18.42  ?  264 ALA   C O   1 
ATOM   9516  C CB  . ALA   C 1 264 ? 8.209   6.958   72.745  1.00 20.34  ?  264 ALA   C CB  1 
ATOM   9517  N N   . LYS   C 1 265 ? 6.891   4.238   74.512  1.00 20.14  ?  265 LYS   C N   1 
ATOM   9518  C CA  . LYS   C 1 265 ? 5.987   3.095   74.447  1.00 15.55  ?  265 LYS   C CA  1 
ATOM   9519  C C   . LYS   C 1 265 ? 4.815   3.223   75.402  1.00 19.43  ?  265 LYS   C C   1 
ATOM   9520  O O   . LYS   C 1 265 ? 3.955   2.334   75.432  1.00 17.65  ?  265 LYS   C O   1 
ATOM   9521  C CB  . LYS   C 1 265 ? 6.752   1.806   74.756  1.00 19.86  ?  265 LYS   C CB  1 
ATOM   9522  C CG  . LYS   C 1 265 ? 7.966   1.580   73.871  1.00 16.91  ?  265 LYS   C CG  1 
ATOM   9523  C CD  . LYS   C 1 265 ? 8.814   0.430   74.392  1.00 18.08  ?  265 LYS   C CD  1 
ATOM   9524  C CE  . LYS   C 1 265 ? 8.066   -0.904  74.350  1.00 17.95  ?  265 LYS   C CE  1 
ATOM   9525  N NZ  . LYS   C 1 265 ? 8.951   -2.027  74.804  1.00 18.86  ?  265 LYS   C NZ  1 
ATOM   9526  N N   . LYS   C 1 266 ? 4.771   4.287   76.197  1.00 15.97  ?  266 LYS   C N   1 
ATOM   9527  C CA  . LYS   C 1 266 ? 3.633   4.505   77.071  1.00 18.47  ?  266 LYS   C CA  1 
ATOM   9528  C C   . LYS   C 1 266 ? 2.753   5.599   76.485  1.00 17.29  ?  266 LYS   C C   1 
ATOM   9529  O O   . LYS   C 1 266 ? 2.052   5.360   75.498  1.00 20.31  ?  266 LYS   C O   1 
ATOM   9530  C CB  . LYS   C 1 266 ? 4.096   4.843   78.490  1.00 20.54  ?  266 LYS   C CB  1 
ATOM   9531  C CG  . LYS   C 1 266 ? 4.663   3.646   79.244  1.00 19.46  ?  266 LYS   C CG  1 
ATOM   9532  C CD  . LYS   C 1 266 ? 6.123   3.431   78.926  1.00 23.95  ?  266 LYS   C CD  1 
ATOM   9533  C CE  . LYS   C 1 266 ? 6.622   2.075   79.372  1.00 26.00  ?  266 LYS   C CE  1 
ATOM   9534  N NZ  . LYS   C 1 266 ? 7.395   2.037   80.660  1.00 31.23  ?  266 LYS   C NZ  1 
ATOM   9535  N N   . ASP   C 1 267 ? 2.795   6.800   77.066  1.00 22.52  ?  267 ASP   C N   1 
ATOM   9536  C CA  . ASP   C 1 267 ? 1.839   7.836   76.677  1.00 23.12  ?  267 ASP   C CA  1 
ATOM   9537  C C   . ASP   C 1 267 ? 1.902   8.234   75.203  1.00 22.22  ?  267 ASP   C C   1 
ATOM   9538  O O   . ASP   C 1 267 ? 0.834   8.512   74.632  1.00 25.34  ?  267 ASP   C O   1 
ATOM   9539  C CB  . ASP   C 1 267 ? 2.013   9.065   77.580  1.00 24.46  ?  267 ASP   C CB  1 
ATOM   9540  C CG  . ASP   C 1 267 ? 1.309   8.910   78.932  1.00 26.26  ?  267 ASP   C CG  1 
ATOM   9541  O OD1 . ASP   C 1 267 ? 0.869   7.786   79.278  1.00 25.57  ?  267 ASP   C OD1 1 
ATOM   9542  O OD2 . ASP   C 1 267 ? 1.185   9.922   79.655  1.00 28.34  ?  267 ASP   C OD2 1 
ATOM   9543  N N   . PRO   C 1 268 ? 3.071   8.290   74.526  1.00 17.29  ?  268 PRO   C N   1 
ATOM   9544  C CA  . PRO   C 1 268 ? 3.063   8.650   73.096  1.00 16.67  ?  268 PRO   C CA  1 
ATOM   9545  C C   . PRO   C 1 268 ? 2.449   7.588   72.192  1.00 21.39  ?  268 PRO   C C   1 
ATOM   9546  O O   . PRO   C 1 268 ? 2.513   7.702   70.958  1.00 21.79  ?  268 PRO   C O   1 
ATOM   9547  C CB  . PRO   C 1 268 ? 4.550   8.860   72.781  1.00 20.17  ?  268 PRO   C CB  1 
ATOM   9548  C CG  . PRO   C 1 268 ? 5.151   9.209   74.079  1.00 17.48  ?  268 PRO   C CG  1 
ATOM   9549  C CD  . PRO   C 1 268 ? 4.434   8.348   75.073  1.00 19.20  ?  268 PRO   C CD  1 
ATOM   9550  N N   . LEU   C 1 269 ? 1.875   6.540   72.794  1.00 19.60  ?  269 LEU   C N   1 
ATOM   9551  C CA  . LEU   C 1 269 ? 0.976   5.617   72.093  1.00 18.78  ?  269 LEU   C CA  1 
ATOM   9552  C C   . LEU   C 1 269 ? 1.699   4.807   71.019  1.00 15.46  ?  269 LEU   C C   1 
ATOM   9553  O O   . LEU   C 1 269 ? 1.212   4.665   69.899  1.00 17.97  ?  269 LEU   C O   1 
ATOM   9554  C CB  . LEU   C 1 269 ? -0.206  6.374   71.483  1.00 20.03  ?  269 LEU   C CB  1 
ATOM   9555  C CG  . LEU   C 1 269 ? -1.157  7.067   72.445  1.00 17.17  ?  269 LEU   C CG  1 
ATOM   9556  C CD1 . LEU   C 1 269 ? -1.875  8.208   71.734  1.00 17.28  ?  269 LEU   C CD1 1 
ATOM   9557  C CD2 . LEU   C 1 269 ? -2.155  6.052   72.964  1.00 20.37  ?  269 LEU   C CD2 1 
ATOM   9558  N N   . LEU   C 1 270 ? 2.854   4.254   71.373  1.00 16.87  ?  270 LEU   C N   1 
ATOM   9559  C CA  . LEU   C 1 270 ? 3.692   3.531   70.422  1.00 17.35  ?  270 LEU   C CA  1 
ATOM   9560  C C   . LEU   C 1 270 ? 3.899   2.081   70.847  1.00 19.92  ?  270 LEU   C C   1 
ATOM   9561  O O   . LEU   C 1 270 ? 3.637   1.686   71.989  1.00 21.01  ?  270 LEU   C O   1 
ATOM   9562  C CB  . LEU   C 1 270 ? 5.064   4.195   70.269  1.00 17.95  ?  270 LEU   C CB  1 
ATOM   9563  C CG  . LEU   C 1 270 ? 5.124   5.660   69.848  1.00 17.14  ?  270 LEU   C CG  1 
ATOM   9564  C CD1 . LEU   C 1 270 ? 6.567   6.089   69.766  1.00 17.38  ?  270 LEU   C CD1 1 
ATOM   9565  C CD2 . LEU   C 1 270 ? 4.423   5.854   68.522  1.00 14.34  ?  270 LEU   C CD2 1 
ATOM   9566  N N   . ASN   C 1 271 ? 4.400   1.295   69.896  1.00 16.46  ?  271 ASN   C N   1 
ATOM   9567  C CA  . ASN   C 1 271 ? 4.797   -0.088  70.121  1.00 15.61  ?  271 ASN   C CA  1 
ATOM   9568  C C   . ASN   C 1 271 ? 6.286   -0.232  70.405  1.00 16.41  ?  271 ASN   C C   1 
ATOM   9569  O O   . ASN   C 1 271 ? 6.712   -1.283  70.901  1.00 15.60  ?  271 ASN   C O   1 
ATOM   9570  C CB  . ASN   C 1 271 ? 4.440   -0.942  68.898  1.00 14.01  ?  271 ASN   C CB  1 
ATOM   9571  C CG  . ASN   C 1 271 ? 2.964   -0.864  68.542  1.00 17.93  ?  271 ASN   C CG  1 
ATOM   9572  O OD1 . ASN   C 1 271 ? 2.602   -0.515  67.412  1.00 16.23  ?  271 ASN   C OD1 1 
ATOM   9573  N ND2 . ASN   C 1 271 ? 2.104   -1.204  69.498  1.00 15.02  ?  271 ASN   C ND2 1 
ATOM   9574  N N   . ILE   C 1 272 ? 7.076   0.790   70.077  1.00 14.35  ?  272 ILE   C N   1 
ATOM   9575  C CA  . ILE   C 1 272 ? 8.507   0.811   70.354  1.00 17.65  ?  272 ILE   C CA  1 
ATOM   9576  C C   . ILE   C 1 272 ? 8.925   2.274   70.334  1.00 15.71  ?  272 ILE   C C   1 
ATOM   9577  O O   . ILE   C 1 272 ? 8.241   3.121   69.753  1.00 18.56  ?  272 ILE   C O   1 
ATOM   9578  C CB  . ILE   C 1 272 ? 9.292   -0.036  69.316  1.00 16.20  ?  272 ILE   C CB  1 
ATOM   9579  C CG1 . ILE   C 1 272 ? 10.740  -0.247  69.755  1.00 12.46  ?  272 ILE   C CG1 1 
ATOM   9580  C CG2 . ILE   C 1 272 ? 9.204   0.591   67.924  1.00 13.26  ?  272 ILE   C CG2 1 
ATOM   9581  C CD1 . ILE   C 1 272 ? 10.879  -0.986  71.095  1.00 13.85  ?  272 ILE   C CD1 1 
ATOM   9582  N N   . GLY   C 1 273 ? 10.025  2.586   71.002  1.00 15.59  ?  273 GLY   C N   1 
ATOM   9583  C CA  . GLY   C 1 273 ? 10.575  3.924   70.903  1.00 15.86  ?  273 GLY   C CA  1 
ATOM   9584  C C   . GLY   C 1 273 ? 10.899  4.547   72.239  1.00 14.00  ?  273 GLY   C C   1 
ATOM   9585  O O   . GLY   C 1 273 ? 10.316  4.208   73.272  1.00 19.93  ?  273 GLY   C O   1 
ATOM   9586  N N   . GLY   C 1 274 ? 11.849  5.475   72.219  1.00 17.27  ?  274 GLY   C N   1 
ATOM   9587  C CA  . GLY   C 1 274 ? 12.309  6.170   73.407  1.00 14.70  ?  274 GLY   C CA  1 
ATOM   9588  C C   . GLY   C 1 274 ? 12.965  7.463   72.981  1.00 15.94  ?  274 GLY   C C   1 
ATOM   9589  O O   . GLY   C 1 274 ? 13.130  7.738   71.790  1.00 16.21  ?  274 GLY   C O   1 
ATOM   9590  N N   . LEU   C 1 275 ? 13.341  8.263   73.974  1.00 17.05  ?  275 LEU   C N   1 
ATOM   9591  C CA  . LEU   C 1 275 ? 13.788  9.615   73.687  1.00 16.76  ?  275 LEU   C CA  1 
ATOM   9592  C C   . LEU   C 1 275 ? 14.565  10.167  74.868  1.00 17.95  ?  275 LEU   C C   1 
ATOM   9593  O O   . LEU   C 1 275 ? 14.167  10.007  76.028  1.00 17.40  ?  275 LEU   C O   1 
ATOM   9594  C CB  . LEU   C 1 275 ? 12.606  10.535  73.367  1.00 15.62  ?  275 LEU   C CB  1 
ATOM   9595  C CG  . LEU   C 1 275 ? 12.972  11.971  72.999  1.00 17.80  ?  275 LEU   C CG  1 
ATOM   9596  C CD1 . LEU   C 1 275 ? 13.622  12.001  71.632  1.00 16.46  ?  275 LEU   C CD1 1 
ATOM   9597  C CD2 . LEU   C 1 275 ? 11.761  12.896  73.067  1.00 16.91  ?  275 LEU   C CD2 1 
ATOM   9598  N N   . VAL   C 1 276 ? 15.683  10.806  74.555  1.00 17.74  ?  276 VAL   C N   1 
ATOM   9599  C CA  . VAL   C 1 276 ? 16.396  11.679  75.474  1.00 20.38  ?  276 VAL   C CA  1 
ATOM   9600  C C   . VAL   C 1 276 ? 16.209  13.099  74.965  1.00 16.81  ?  276 VAL   C C   1 
ATOM   9601  O O   . VAL   C 1 276 ? 16.306  13.348  73.760  1.00 18.12  ?  276 VAL   C O   1 
ATOM   9602  C CB  . VAL   C 1 276 ? 17.888  11.312  75.562  1.00 23.04  ?  276 VAL   C CB  1 
ATOM   9603  C CG1 . VAL   C 1 276 ? 18.606  12.237  76.530  1.00 20.53  ?  276 VAL   C CG1 1 
ATOM   9604  C CG2 . VAL   C 1 276 ? 18.066  9.857   75.976  1.00 17.05  ?  276 VAL   C CG2 1 
ATOM   9605  N N   . ALA   C 1 277 ? 15.892  14.017  75.865  1.00 18.99  ?  277 ALA   C N   1 
ATOM   9606  C CA  . ALA   C 1 277 ? 15.811  15.422  75.499  1.00 22.48  ?  277 ALA   C CA  1 
ATOM   9607  C C   . ALA   C 1 277 ? 16.495  16.225  76.585  1.00 22.83  ?  277 ALA   C C   1 
ATOM   9608  O O   . ALA   C 1 277 ? 16.309  15.953  77.772  1.00 25.10  ?  277 ALA   C O   1 
ATOM   9609  C CB  . ALA   C 1 277 ? 14.365  15.893  75.310  1.00 21.33  ?  277 ALA   C CB  1 
ATOM   9610  N N   . ILE   C 1 278 ? 17.311  17.188  76.175  1.00 25.20  ?  278 ILE   C N   1 
ATOM   9611  C CA  A ILE   C 1 278 ? 18.094  18.015  77.087  0.49 24.40  ?  278 ILE   C CA  1 
ATOM   9612  C CA  B ILE   C 1 278 ? 18.079  18.011  77.096  0.51 24.40  ?  278 ILE   C CA  1 
ATOM   9613  C C   . ILE   C 1 278 ? 17.689  19.464  76.871  1.00 26.29  ?  278 ILE   C C   1 
ATOM   9614  O O   . ILE   C 1 278 ? 17.655  19.936  75.729  1.00 26.24  ?  278 ILE   C O   1 
ATOM   9615  C CB  A ILE   C 1 278 ? 19.608  17.828  76.872  0.49 25.74  ?  278 ILE   C CB  1 
ATOM   9616  C CB  B ILE   C 1 278 ? 19.589  17.782  76.918  0.51 25.74  ?  278 ILE   C CB  1 
ATOM   9617  C CG1 A ILE   C 1 278 ? 20.024  16.398  77.209  0.49 24.47  ?  278 ILE   C CG1 1 
ATOM   9618  C CG1 B ILE   C 1 278 ? 19.908  16.323  77.248  0.51 24.45  ?  278 ILE   C CG1 1 
ATOM   9619  C CG2 A ILE   C 1 278 ? 20.398  18.820  77.711  0.49 27.48  ?  278 ILE   C CG2 1 
ATOM   9620  C CG2 B ILE   C 1 278 ? 20.387  18.722  77.805  0.51 27.47  ?  278 ILE   C CG2 1 
ATOM   9621  C CD1 A ILE   C 1 278 ? 20.340  15.565  75.998  0.49 23.40  ?  278 ILE   C CD1 1 
ATOM   9622  C CD1 B ILE   C 1 278 ? 21.349  15.960  77.124  0.51 24.96  ?  278 ILE   C CD1 1 
ATOM   9623  N N   . ARG   C 1 279 ? 17.378  20.160  77.967  1.00 26.71  ?  279 ARG   C N   1 
ATOM   9624  C CA  . ARG   C 1 279 ? 16.858  21.520  77.889  1.00 26.66  ?  279 ARG   C CA  1 
ATOM   9625  C C   . ARG   C 1 279 ? 17.839  22.462  77.198  1.00 30.82  ?  279 ARG   C C   1 
ATOM   9626  O O   . ARG   C 1 279 ? 17.528  23.044  76.153  1.00 32.45  ?  279 ARG   C O   1 
ATOM   9627  C CB  . ARG   C 1 279 ? 16.531  22.011  79.292  1.00 25.69  ?  279 ARG   C CB  1 
ATOM   9628  C CG  . ARG   C 1 279 ? 15.811  23.322  79.345  1.00 31.18  ?  279 ARG   C CG  1 
ATOM   9629  C CD  . ARG   C 1 279 ? 15.376  23.537  80.770  1.00 31.74  ?  279 ARG   C CD  1 
ATOM   9630  N NE  . ARG   C 1 279 ? 14.665  24.790  80.963  1.00 35.98  ?  279 ARG   C NE  1 
ATOM   9631  C CZ  . ARG   C 1 279 ? 14.094  25.135  82.107  1.00 42.12  ?  279 ARG   C CZ  1 
ATOM   9632  N NH1 . ARG   C 1 279 ? 14.094  24.316  83.149  1.00 34.82  ?  279 ARG   C NH1 1 
ATOM   9633  N NH2 . ARG   C 1 279 ? 13.514  26.330  82.212  1.00 43.26  ?  279 ARG   C NH2 1 
ATOM   9634  N N   . ASP   C 1 280 ? 19.038  22.640  77.779  1.00 28.94  ?  280 ASP   C N   1 
ATOM   9635  C CA  . ASP   C 1 280 ? 20.004  23.550  77.172  1.00 32.53  ?  280 ASP   C CA  1 
ATOM   9636  C C   . ASP   C 1 280 ? 21.461  23.208  77.449  1.00 30.61  ?  280 ASP   C C   1 
ATOM   9637  O O   . ASP   C 1 280 ? 22.336  23.872  76.883  1.00 33.01  ?  280 ASP   C O   1 
ATOM   9638  C CB  . ASP   C 1 280 ? 19.710  25.004  77.614  1.00 33.65  ?  280 ASP   C CB  1 
ATOM   9639  C CG  . ASP   C 1 280 ? 19.580  25.158  79.119  1.00 35.54  ?  280 ASP   C CG  1 
ATOM   9640  O OD1 . ASP   C 1 280 ? 20.397  24.573  79.858  1.00 35.60  ?  280 ASP   C OD1 1 
ATOM   9641  O OD2 . ASP   C 1 280 ? 18.669  25.899  79.567  1.00 40.23  ?  280 ASP   C OD2 1 
ATOM   9642  N N   . ASN   C 1 281 ? 21.766  22.200  78.266  1.00 27.01  ?  281 ASN   C N   1 
ATOM   9643  C CA  . ASN   C 1 281 ? 23.162  21.853  78.549  1.00 31.61  ?  281 ASN   C CA  1 
ATOM   9644  C C   . ASN   C 1 281 ? 23.741  21.157  77.325  1.00 30.77  ?  281 ASN   C C   1 
ATOM   9645  O O   . ASN   C 1 281 ? 23.465  19.981  77.073  1.00 30.66  ?  281 ASN   C O   1 
ATOM   9646  C CB  . ASN   C 1 281 ? 23.267  20.976  79.794  1.00 32.30  ?  281 ASN   C CB  1 
ATOM   9647  C CG  . ASN   C 1 281 ? 24.705  20.837  80.321  1.00 29.44  ?  281 ASN   C CG  1 
ATOM   9648  O OD1 . ASN   C 1 281 ? 25.650  20.614  79.565  1.00 29.38  ?  281 ASN   C OD1 1 
ATOM   9649  N ND2 . ASN   C 1 281 ? 24.862  20.974  81.634  1.00 30.92  ?  281 ASN   C ND2 1 
ATOM   9650  N N   . GLU   C 1 282 ? 24.553  21.885  76.556  1.00 30.89  ?  282 GLU   C N   1 
ATOM   9651  C CA  . GLU   C 1 282 ? 25.080  21.340  75.313  1.00 31.21  ?  282 GLU   C CA  1 
ATOM   9652  C C   . GLU   C 1 282 ? 26.241  20.391  75.555  1.00 29.00  ?  282 GLU   C C   1 
ATOM   9653  O O   . GLU   C 1 282 ? 26.507  19.521  74.719  1.00 27.59  ?  282 GLU   C O   1 
ATOM   9654  C CB  . GLU   C 1 282 ? 25.510  22.471  74.384  1.00 31.92  ?  282 GLU   C CB  1 
ATOM   9655  C CG  . GLU   C 1 282 ? 25.772  22.023  72.964  1.00 37.88  ?  282 GLU   C CG  1 
ATOM   9656  C CD  . GLU   C 1 282 ? 26.256  23.151  72.081  1.00 41.36  ?  282 GLU   C CD  1 
ATOM   9657  O OE1 . GLU   C 1 282 ? 26.750  24.164  72.624  1.00 50.24  ?  282 GLU   C OE1 1 
ATOM   9658  O OE2 . GLU   C 1 282 ? 26.135  23.023  70.845  1.00 36.64  ?  282 GLU   C OE2 1 
ATOM   9659  N N   . GLU   C 1 283 ? 26.937  20.544  76.683  1.00 27.09  ?  283 GLU   C N   1 
ATOM   9660  C CA  . GLU   C 1 283 ? 28.015  19.625  77.019  1.00 30.34  ?  283 GLU   C CA  1 
ATOM   9661  C C   . GLU   C 1 283 ? 27.464  18.251  77.361  1.00 28.00  ?  283 GLU   C C   1 
ATOM   9662  O O   . GLU   C 1 283 ? 27.977  17.227  76.892  1.00 28.03  ?  283 GLU   C O   1 
ATOM   9663  C CB  . GLU   C 1 283 ? 28.835  20.175  78.187  1.00 32.07  ?  283 GLU   C CB  1 
ATOM   9664  C CG  . GLU   C 1 283 ? 29.930  19.225  78.649  1.00 32.94  ?  283 GLU   C CG  1 
ATOM   9665  C CD  . GLU   C 1 283 ? 30.708  19.756  79.839  1.00 40.39  ?  283 GLU   C CD  1 
ATOM   9666  O OE1 . GLU   C 1 283 ? 30.255  20.741  80.463  1.00 42.25  ?  283 GLU   C OE1 1 
ATOM   9667  O OE2 . GLU   C 1 283 ? 31.774  19.186  80.151  1.00 43.88  ?  283 GLU   C OE2 1 
ATOM   9668  N N   . ILE   C 1 284 ? 26.419  18.209  78.187  1.00 24.69  ?  284 ILE   C N   1 
ATOM   9669  C CA  . ILE   C 1 284 ? 25.796  16.931  78.505  1.00 28.40  ?  284 ILE   C CA  1 
ATOM   9670  C C   . ILE   C 1 284 ? 25.171  16.318  77.261  1.00 21.13  ?  284 ILE   C C   1 
ATOM   9671  O O   . ILE   C 1 284 ? 25.194  15.095  77.084  1.00 18.17  ?  284 ILE   C O   1 
ATOM   9672  C CB  . ILE   C 1 284 ? 24.783  17.118  79.647  1.00 27.38  ?  284 ILE   C CB  1 
ATOM   9673  C CG1 . ILE   C 1 284 ? 25.544  17.363  80.953  1.00 29.54  ?  284 ILE   C CG1 1 
ATOM   9674  C CG2 . ILE   C 1 284 ? 23.874  15.913  79.770  1.00 27.95  ?  284 ILE   C CG2 1 
ATOM   9675  C CD1 . ILE   C 1 284 ? 24.671  17.560  82.146  1.00 33.71  ?  284 ILE   C CD1 1 
ATOM   9676  N N   . PHE   C 1 285 ? 24.641  17.149  76.361  1.00 23.51  ?  285 PHE   C N   1 
ATOM   9677  C CA  . PHE   C 1 285 ? 24.108  16.637  75.101  1.00 24.86  ?  285 PHE   C CA  1 
ATOM   9678  C C   . PHE   C 1 285 ? 25.208  16.015  74.252  1.00 23.58  ?  285 PHE   C C   1 
ATOM   9679  O O   . PHE   C 1 285 ? 25.048  14.910  73.723  1.00 19.83  ?  285 PHE   C O   1 
ATOM   9680  C CB  . PHE   C 1 285 ? 23.406  17.766  74.346  1.00 29.76  ?  285 PHE   C CB  1 
ATOM   9681  C CG  . PHE   C 1 285 ? 23.100  17.453  72.905  1.00 27.20  ?  285 PHE   C CG  1 
ATOM   9682  C CD1 . PHE   C 1 285 ? 22.203  16.455  72.567  1.00 24.55  ?  285 PHE   C CD1 1 
ATOM   9683  C CD2 . PHE   C 1 285 ? 23.694  18.182  71.888  1.00 29.27  ?  285 PHE   C CD2 1 
ATOM   9684  C CE1 . PHE   C 1 285 ? 21.910  16.186  71.239  1.00 27.64  ?  285 PHE   C CE1 1 
ATOM   9685  C CE2 . PHE   C 1 285 ? 23.402  17.917  70.560  1.00 24.90  ?  285 PHE   C CE2 1 
ATOM   9686  C CZ  . PHE   C 1 285 ? 22.508  16.925  70.239  1.00 24.52  ?  285 PHE   C CZ  1 
ATOM   9687  N N   . THR   C 1 286 ? 26.343  16.714  74.123  1.00 27.44  ?  286 THR   C N   1 
ATOM   9688  C CA  . THR   C 1 286 ? 27.458  16.203  73.333  1.00 24.83  ?  286 THR   C CA  1 
ATOM   9689  C C   . THR   C 1 286 ? 27.967  14.886  73.891  1.00 25.04  ?  286 THR   C C   1 
ATOM   9690  O O   . THR   C 1 286 ? 28.252  13.948  73.135  1.00 22.09  ?  286 THR   C O   1 
ATOM   9691  C CB  . THR   C 1 286 ? 28.590  17.227  73.305  1.00 24.88  ?  286 THR   C CB  1 
ATOM   9692  O OG1 . THR   C 1 286 ? 28.109  18.449  72.737  1.00 29.36  ?  286 THR   C OG1 1 
ATOM   9693  C CG2 . THR   C 1 286 ? 29.735  16.713  72.469  1.00 26.54  ?  286 THR   C CG2 1 
ATOM   9694  N N   . LEU   C 1 287 ? 28.099  14.810  75.217  1.00 26.71  ?  287 LEU   C N   1 
ATOM   9695  C CA  . LEU   C 1 287 ? 28.561  13.592  75.867  1.00 24.93  ?  287 LEU   C CA  1 
ATOM   9696  C C   . LEU   C 1 287 ? 27.565  12.455  75.692  1.00 22.77  ?  287 LEU   C C   1 
ATOM   9697  O O   . LEU   C 1 287 ? 27.962  11.295  75.532  1.00 22.22  ?  287 LEU   C O   1 
ATOM   9698  C CB  . LEU   C 1 287 ? 28.805  13.861  77.353  1.00 25.61  ?  287 LEU   C CB  1 
ATOM   9699  C CG  . LEU   C 1 287 ? 29.984  14.773  77.684  1.00 25.08  ?  287 LEU   C CG  1 
ATOM   9700  C CD1 . LEU   C 1 287 ? 29.976  15.133  79.156  1.00 26.88  ?  287 LEU   C CD1 1 
ATOM   9701  C CD2 . LEU   C 1 287 ? 31.281  14.090  77.285  1.00 26.23  ?  287 LEU   C CD2 1 
ATOM   9702  N N   . ALA   C 1 288 ? 26.267  12.761  75.745  1.00 17.84  ?  288 ALA   C N   1 
ATOM   9703  C CA  . ALA   C 1 288 ? 25.276  11.709  75.563  1.00 23.60  ?  288 ALA   C CA  1 
ATOM   9704  C C   . ALA   C 1 288 ? 25.265  11.193  74.129  1.00 19.20  ?  288 ALA   C C   1 
ATOM   9705  O O   . ALA   C 1 288 ? 25.061  9.995   73.911  1.00 20.95  ?  288 ALA   C O   1 
ATOM   9706  C CB  . ALA   C 1 288 ? 23.889  12.204  75.978  1.00 19.20  ?  288 ALA   C CB  1 
ATOM   9707  N N   . ARG   C 1 289 ? 25.498  12.067  73.143  1.00 17.08  ?  289 ARG   C N   1 
ATOM   9708  C CA  . ARG   C 1 289 ? 25.622  11.602  71.763  1.00 19.82  ?  289 ARG   C CA  1 
ATOM   9709  C C   . ARG   C 1 289 ? 26.774  10.615  71.606  1.00 22.73  ?  289 ARG   C C   1 
ATOM   9710  O O   . ARG   C 1 289 ? 26.652  9.618   70.882  1.00 19.59  ?  289 ARG   C O   1 
ATOM   9711  C CB  . ARG   C 1 289 ? 25.811  12.787  70.816  1.00 20.57  ?  289 ARG   C CB  1 
ATOM   9712  C CG  . ARG   C 1 289 ? 24.521  13.513  70.429  1.00 18.88  ?  289 ARG   C CG  1 
ATOM   9713  C CD  . ARG   C 1 289 ? 24.808  14.527  69.321  1.00 25.27  ?  289 ARG   C CD  1 
ATOM   9714  N NE  . ARG   C 1 289 ? 23.662  14.738  68.442  1.00 25.25  ?  289 ARG   C NE  1 
ATOM   9715  C CZ  . ARG   C 1 289 ? 23.691  15.473  67.338  1.00 31.19  ?  289 ARG   C CZ  1 
ATOM   9716  N NH1 . ARG   C 1 289 ? 24.788  16.115  66.964  1.00 30.35  ?  289 ARG   C NH1 1 
ATOM   9717  N NH2 . ARG   C 1 289 ? 22.594  15.562  66.586  1.00 29.84  ?  289 ARG   C NH2 1 
ATOM   9718  N N   . GLN   C 1 290 ? 27.902  10.870  72.278  1.00 21.74  ?  290 GLN   C N   1 
ATOM   9719  C CA  . GLN   C 1 290 ? 29.048  9.976   72.155  1.00 24.04  ?  290 GLN   C CA  1 
ATOM   9720  C C   . GLN   C 1 290 ? 28.762  8.612   72.770  1.00 19.63  ?  290 GLN   C C   1 
ATOM   9721  O O   . GLN   C 1 290 ? 29.288  7.598   72.301  1.00 17.89  ?  290 GLN   C O   1 
ATOM   9722  C CB  . GLN   C 1 290 ? 30.284  10.616  72.791  1.00 26.03  ?  290 GLN   C CB  1 
ATOM   9723  C CG  . GLN   C 1 290 ? 30.719  11.911  72.098  1.00 31.66  ?  290 GLN   C CG  1 
ATOM   9724  C CD  . GLN   C 1 290 ? 31.776  12.702  72.868  1.00 34.22  ?  290 GLN   C CD  1 
ATOM   9725  O OE1 . GLN   C 1 290 ? 32.182  12.324  73.970  1.00 33.23  ?  290 GLN   C OE1 1 
ATOM   9726  N NE2 . GLN   C 1 290 ? 32.221  13.812  72.283  1.00 39.67  ?  290 GLN   C NE2 1 
ATOM   9727  N N   . ARG   C 1 291 ? 27.930  8.557   73.811  1.00 23.14  ?  291 ARG   C N   1 
ATOM   9728  C CA  . ARG   C 1 291 ? 27.507  7.257   74.321  1.00 21.30  ?  291 ARG   C CA  1 
ATOM   9729  C C   . ARG   C 1 291 ? 26.428  6.630   73.439  1.00 21.50  ?  291 ARG   C C   1 
ATOM   9730  O O   . ARG   C 1 291 ? 26.372  5.402   73.307  1.00 21.06  ?  291 ARG   C O   1 
ATOM   9731  C CB  . ARG   C 1 291 ? 27.026  7.386   75.773  1.00 18.23  ?  291 ARG   C CB  1 
ATOM   9732  C CG  . ARG   C 1 291 ? 26.518  6.070   76.351  1.00 21.39  ?  291 ARG   C CG  1 
ATOM   9733  C CD  . ARG   C 1 291 ? 26.701  5.944   77.852  1.00 19.58  ?  291 ARG   C CD  1 
ATOM   9734  N NE  . ARG   C 1 291 ? 26.228  4.641   78.311  1.00 22.24  ?  291 ARG   C NE  1 
ATOM   9735  C CZ  . ARG   C 1 291 ? 27.011  3.607   78.593  1.00 24.25  ?  291 ARG   C CZ  1 
ATOM   9736  N NH1 . ARG   C 1 291 ? 28.327  3.692   78.504  1.00 21.66  ?  291 ARG   C NH1 1 
ATOM   9737  N NH2 . ARG   C 1 291 ? 26.460  2.460   78.977  1.00 21.22  ?  291 ARG   C NH2 1 
ATOM   9738  N N   . CYS   C 1 292 ? 25.592  7.453   72.799  1.00 19.11  ?  292 CYS   C N   1 
ATOM   9739  C CA  . CYS   C 1 292 ? 24.531  6.925   71.951  1.00 18.29  ?  292 CYS   C CA  1 
ATOM   9740  C C   . CYS   C 1 292 ? 25.089  6.053   70.835  1.00 19.08  ?  292 CYS   C C   1 
ATOM   9741  O O   . CYS   C 1 292 ? 24.518  5.004   70.518  1.00 17.92  ?  292 CYS   C O   1 
ATOM   9742  C CB  . CYS   C 1 292 ? 23.712  8.072   71.364  1.00 17.80  ?  292 CYS   C CB  1 
ATOM   9743  S SG  . CYS   C 1 292 ? 22.395  7.537   70.226  1.00 20.46  ?  292 CYS   C SG  1 
ATOM   9744  N N   . VAL   C 1 293 ? 26.214  6.458   70.237  1.00 21.59  ?  293 VAL   C N   1 
ATOM   9745  C CA  . VAL   C 1 293 ? 26.689  5.786   69.022  1.00 21.32  ?  293 VAL   C CA  1 
ATOM   9746  C C   . VAL   C 1 293 ? 27.016  4.316   69.256  1.00 20.52  ?  293 VAL   C C   1 
ATOM   9747  O O   . VAL   C 1 293 ? 26.513  3.469   68.499  1.00 20.36  ?  293 VAL   C O   1 
ATOM   9748  C CB  . VAL   C 1 293 ? 27.863  6.568   68.406  1.00 21.16  ?  293 VAL   C CB  1 
ATOM   9749  C CG1 . VAL   C 1 293 ? 28.482  5.770   67.272  1.00 23.12  ?  293 VAL   C CG1 1 
ATOM   9750  C CG2 . VAL   C 1 293 ? 27.380  7.935   67.906  1.00 24.96  ?  293 VAL   C CG2 1 
ATOM   9751  N N   . PRO   C 1 294 ? 27.830  3.936   70.251  1.00 20.53  ?  294 PRO   C N   1 
ATOM   9752  C CA  . PRO   C 1 294 ? 28.119  2.501   70.416  1.00 19.14  ?  294 PRO   C CA  1 
ATOM   9753  C C   . PRO   C 1 294 ? 26.958  1.703   70.974  1.00 20.69  ?  294 PRO   C C   1 
ATOM   9754  O O   . PRO   C 1 294 ? 26.851  0.507   70.670  1.00 19.28  ?  294 PRO   C O   1 
ATOM   9755  C CB  . PRO   C 1 294 ? 29.318  2.487   71.376  1.00 21.25  ?  294 PRO   C CB  1 
ATOM   9756  C CG  . PRO   C 1 294 ? 29.241  3.769   72.100  1.00 19.84  ?  294 PRO   C CG  1 
ATOM   9757  C CD  . PRO   C 1 294 ? 28.690  4.760   71.124  1.00 19.98  ?  294 PRO   C CD  1 
ATOM   9758  N N   . MET   C 1 295 ? 26.080  2.325   71.771  1.00 20.72  ?  295 MET   C N   1 
ATOM   9759  C CA  . MET   C 1 295 ? 25.033  1.625   72.512  1.00 18.21  ?  295 MET   C CA  1 
ATOM   9760  C C   . MET   C 1 295 ? 23.721  1.487   71.740  1.00 19.40  ?  295 MET   C C   1 
ATOM   9761  O O   . MET   C 1 295 ? 23.091  0.423   71.782  1.00 19.32  ?  295 MET   C O   1 
ATOM   9762  C CB  . MET   C 1 295 ? 24.768  2.349   73.835  1.00 19.38  ?  295 MET   C CB  1 
ATOM   9763  C CG  . MET   C 1 295 ? 25.937  2.284   74.798  1.00 20.57  ?  295 MET   C CG  1 
ATOM   9764  S SD  . MET   C 1 295 ? 26.235  0.584   75.317  1.00 25.08  ?  295 MET   C SD  1 
ATOM   9765  C CE  . MET   C 1 295 ? 27.779  0.760   76.202  1.00 24.16  ?  295 MET   C CE  1 
ATOM   9766  N N   . GLU   C 1 296 ? 23.279  2.543   71.058  1.00 16.37  ?  296 GLU   C N   1 
ATOM   9767  C CA  . GLU   C 1 296 ? 21.977  2.566   70.405  1.00 15.96  ?  296 GLU   C CA  1 
ATOM   9768  C C   . GLU   C 1 296 ? 22.071  2.654   68.890  1.00 18.28  ?  296 GLU   C C   1 
ATOM   9769  O O   . GLU   C 1 296 ? 21.422  1.881   68.182  1.00 17.70  ?  296 GLU   C O   1 
ATOM   9770  C CB  . GLU   C 1 296 ? 21.145  3.743   70.937  1.00 19.58  ?  296 GLU   C CB  1 
ATOM   9771  C CG  . GLU   C 1 296 ? 20.820  3.656   72.413  1.00 17.01  ?  296 GLU   C CG  1 
ATOM   9772  C CD  . GLU   C 1 296 ? 19.661  2.712   72.708  1.00 19.83  ?  296 GLU   C CD  1 
ATOM   9773  O OE1 . GLU   C 1 296 ? 18.702  2.657   71.910  1.00 23.32  ?  296 GLU   C OE1 1 
ATOM   9774  O OE2 . GLU   C 1 296 ? 19.711  2.020   73.746  1.00 29.84  ?  296 GLU   C OE2 1 
ATOM   9775  N N   . GLY   C 1 297 ? 22.868  3.569   68.373  1.00 15.64  ?  297 GLY   C N   1 
ATOM   9776  C CA  . GLY   C 1 297 ? 22.973  3.774   66.945  1.00 16.50  ?  297 GLY   C CA  1 
ATOM   9777  C C   . GLY   C 1 297 ? 23.412  5.198   66.683  1.00 17.70  ?  297 GLY   C C   1 
ATOM   9778  O O   . GLY   C 1 297 ? 23.815  5.915   67.594  1.00 19.64  ?  297 GLY   C O   1 
ATOM   9779  N N   . PHE   C 1 298 ? 23.332  5.598   65.420  1.00 16.83  ?  298 PHE   C N   1 
ATOM   9780  C CA  . PHE   C 1 298 ? 23.732  6.955   65.085  1.00 19.17  ?  298 PHE   C CA  1 
ATOM   9781  C C   . PHE   C 1 298 ? 22.742  7.959   65.670  1.00 19.25  ?  298 PHE   C C   1 
ATOM   9782  O O   . PHE   C 1 298 ? 21.571  7.657   65.906  1.00 20.93  ?  298 PHE   C O   1 
ATOM   9783  C CB  . PHE   C 1 298 ? 23.855  7.135   63.570  1.00 21.91  ?  298 PHE   C CB  1 
ATOM   9784  C CG  . PHE   C 1 298 ? 24.367  8.476   63.178  1.00 24.35  ?  298 PHE   C CG  1 
ATOM   9785  C CD1 . PHE   C 1 298 ? 25.641  8.879   63.550  1.00 27.15  ?  298 PHE   C CD1 1 
ATOM   9786  C CD2 . PHE   C 1 298 ? 23.573  9.354   62.463  1.00 25.28  ?  298 PHE   C CD2 1 
ATOM   9787  C CE1 . PHE   C 1 298 ? 26.114  10.127  63.199  1.00 28.02  ?  298 PHE   C CE1 1 
ATOM   9788  C CE2 . PHE   C 1 298 ? 24.049  10.608  62.107  1.00 24.01  ?  298 PHE   C CE2 1 
ATOM   9789  C CZ  . PHE   C 1 298 ? 25.315  10.991  62.479  1.00 22.37  ?  298 PHE   C CZ  1 
ATOM   9790  N N   . VAL   C 1 299 ? 23.235  9.173   65.910  1.00 20.72  ?  299 VAL   C N   1 
ATOM   9791  C CA  . VAL   C 1 299 ? 22.528  10.128  66.748  1.00 21.21  ?  299 VAL   C CA  1 
ATOM   9792  C C   . VAL   C 1 299 ? 21.246  10.657  66.128  1.00 21.89  ?  299 VAL   C C   1 
ATOM   9793  O O   . VAL   C 1 299 ? 20.488  11.348  66.819  1.00 18.06  ?  299 VAL   C O   1 
ATOM   9794  C CB  . VAL   C 1 299 ? 23.477  11.290  67.085  1.00 21.90  ?  299 VAL   C CB  1 
ATOM   9795  C CG1 . VAL   C 1 299 ? 24.746  10.749  67.733  1.00 23.70  ?  299 VAL   C CG1 1 
ATOM   9796  C CG2 . VAL   C 1 299 ? 23.808  12.073  65.826  1.00 21.06  ?  299 VAL   C CG2 1 
ATOM   9797  N N   . THR   C 1 300 ? 20.979  10.366  64.852  1.00 20.36  ?  300 THR   C N   1 
ATOM   9798  C CA  . THR   C 1 300 ? 19.753  10.817  64.206  1.00 21.57  ?  300 THR   C CA  1 
ATOM   9799  C C   . THR   C 1 300 ? 18.731  9.701   64.019  1.00 20.49  ?  300 THR   C C   1 
ATOM   9800  O O   . THR   C 1 300 ? 17.702  9.926   63.376  1.00 20.68  ?  300 THR   C O   1 
ATOM   9801  C CB  . THR   C 1 300 ? 20.048  11.476  62.852  1.00 24.39  ?  300 THR   C CB  1 
ATOM   9802  O OG1 . THR   C 1 300 ? 20.612  10.516  61.945  1.00 21.43  ?  300 THR   C OG1 1 
ATOM   9803  C CG2 . THR   C 1 300 ? 20.998  12.664  63.027  1.00 23.78  ?  300 THR   C CG2 1 
ATOM   9804  N N   . TYR   C 1 301 ? 18.986  8.503   64.557  1.00 16.73  ?  301 TYR   C N   1 
ATOM   9805  C CA  . TYR   C 1 301 ? 17.916  7.515   64.690  1.00 18.10  ?  301 TYR   C CA  1 
ATOM   9806  C C   . TYR   C 1 301 ? 17.958  6.736   66.001  1.00 17.46  ?  301 TYR   C C   1 
ATOM   9807  O O   . TYR   C 1 301 ? 16.899  6.311   66.470  1.00 17.58  ?  301 TYR   C O   1 
ATOM   9808  C CB  . TYR   C 1 301 ? 17.918  6.532   63.499  1.00 19.58  ?  301 TYR   C CB  1 
ATOM   9809  C CG  . TYR   C 1 301 ? 19.087  5.589   63.464  1.00 18.12  ?  301 TYR   C CG  1 
ATOM   9810  C CD1 . TYR   C 1 301 ? 19.049  4.387   64.157  1.00 17.82  ?  301 TYR   C CD1 1 
ATOM   9811  C CD2 . TYR   C 1 301 ? 20.227  5.889   62.737  1.00 19.43  ?  301 TYR   C CD2 1 
ATOM   9812  C CE1 . TYR   C 1 301 ? 20.120  3.523   64.148  1.00 16.90  ?  301 TYR   C CE1 1 
ATOM   9813  C CE2 . TYR   C 1 301 ? 21.305  5.017   62.713  1.00 20.03  ?  301 TYR   C CE2 1 
ATOM   9814  C CZ  . TYR   C 1 301 ? 21.243  3.839   63.429  1.00 18.36  ?  301 TYR   C CZ  1 
ATOM   9815  O OH  . TYR   C 1 301 ? 22.300  2.959   63.427  1.00 20.53  ?  301 TYR   C OH  1 
ATOM   9816  N N   . GLY   C 1 302 ? 19.120  6.547   66.618  1.00 18.26  ?  302 GLY   C N   1 
ATOM   9817  C CA  . GLY   C 1 302 ? 19.199  6.026   67.976  1.00 18.33  ?  302 GLY   C CA  1 
ATOM   9818  C C   . GLY   C 1 302 ? 18.601  4.652   68.198  1.00 18.22  ?  302 GLY   C C   1 
ATOM   9819  O O   . GLY   C 1 302 ? 18.035  4.397   69.268  1.00 19.48  ?  302 GLY   C O   1 
ATOM   9820  N N   . GLY   C 1 303 ? 18.731  3.752   67.224  1.00 16.38  ?  303 GLY   C N   1 
ATOM   9821  C CA  . GLY   C 1 303 ? 18.202  2.410   67.356  1.00 16.56  ?  303 GLY   C CA  1 
ATOM   9822  C C   . GLY   C 1 303 ? 16.749  2.253   66.971  1.00 16.41  ?  303 GLY   C C   1 
ATOM   9823  O O   . GLY   C 1 303 ? 16.145  1.221   67.292  1.00 16.35  ?  303 GLY   C O   1 
ATOM   9824  N N   . LEU   C 1 304 ? 16.166  3.249   66.312  1.00 13.74  ?  304 LEU   C N   1 
ATOM   9825  C CA  . LEU   C 1 304 ? 14.797  3.211   65.831  1.00 16.71  ?  304 LEU   C CA  1 
ATOM   9826  C C   . LEU   C 1 304 ? 14.780  3.239   64.312  1.00 17.90  ?  304 LEU   C C   1 
ATOM   9827  O O   . LEU   C 1 304 ? 15.611  3.898   63.682  1.00 16.22  ?  304 LEU   C O   1 
ATOM   9828  C CB  . LEU   C 1 304 ? 13.994  4.409   66.348  1.00 19.20  ?  304 LEU   C CB  1 
ATOM   9829  C CG  . LEU   C 1 304 ? 13.620  4.453   67.824  1.00 18.07  ?  304 LEU   C CG  1 
ATOM   9830  C CD1 . LEU   C 1 304 ? 13.057  5.819   68.159  1.00 19.29  ?  304 LEU   C CD1 1 
ATOM   9831  C CD2 . LEU   C 1 304 ? 12.593  3.379   68.115  1.00 14.57  ?  304 LEU   C CD2 1 
ATOM   9832  N N   . ALA   C 1 305 ? 13.810  2.545   63.727  1.00 17.32  ?  305 ALA   C N   1 
ATOM   9833  C CA  . ALA   C 1 305 ? 13.529  2.775   62.325  1.00 16.60  ?  305 ALA   C CA  1 
ATOM   9834  C C   . ALA   C 1 305 ? 13.009  4.193   62.138  1.00 19.42  ?  305 ALA   C C   1 
ATOM   9835  O O   . ALA   C 1 305 ? 12.420  4.786   63.048  1.00 16.32  ?  305 ALA   C O   1 
ATOM   9836  C CB  . ALA   C 1 305 ? 12.507  1.770   61.805  1.00 19.00  ?  305 ALA   C CB  1 
ATOM   9837  N N   . GLY   C 1 306 ? 13.247  4.749   60.950  1.00 15.95  ?  306 GLY   C N   1 
ATOM   9838  C CA  . GLY   C 1 306 ? 12.690  6.058   60.650  1.00 15.18  ?  306 GLY   C CA  1 
ATOM   9839  C C   . GLY   C 1 306 ? 11.181  6.088   60.799  1.00 16.26  ?  306 GLY   C C   1 
ATOM   9840  O O   . GLY   C 1 306 ? 10.608  7.089   61.241  1.00 18.07  ?  306 GLY   C O   1 
ATOM   9841  N N   . ARG   C 1 307 ? 10.513  4.985   60.455  1.00 14.69  ?  307 ARG   C N   1 
ATOM   9842  C CA  . ARG   C 1 307 ? 9.059   4.973   60.548  1.00 13.79  ?  307 ARG   C CA  1 
ATOM   9843  C C   . ARG   C 1 307 ? 8.594   5.121   61.990  1.00 16.88  ?  307 ARG   C C   1 
ATOM   9844  O O   . ARG   C 1 307 ? 7.490   5.620   62.237  1.00 15.82  ?  307 ARG   C O   1 
ATOM   9845  C CB  . ARG   C 1 307 ? 8.493   3.695   59.932  1.00 12.70  ?  307 ARG   C CB  1 
ATOM   9846  C CG  . ARG   C 1 307 ? 9.135   2.433   60.445  1.00 13.49  ?  307 ARG   C CG  1 
ATOM   9847  C CD  . ARG   C 1 307 ? 8.414   1.206   59.906  1.00 14.37  ?  307 ARG   C CD  1 
ATOM   9848  N NE  . ARG   C 1 307 ? 9.092   -0.018  60.323  1.00 22.34  ?  307 ARG   C NE  1 
ATOM   9849  C CZ  . ARG   C 1 307 ? 9.984   -0.670  59.587  1.00 17.57  ?  307 ARG   C CZ  1 
ATOM   9850  N NH1 . ARG   C 1 307 ? 10.292  -0.277  58.362  1.00 14.58  ?  307 ARG   C NH1 1 
ATOM   9851  N NH2 . ARG   C 1 307 ? 10.588  -1.739  60.096  1.00 14.74  ?  307 ARG   C NH2 1 
ATOM   9852  N N   . ASP   C 1 308 ? 9.423   4.724   62.953  1.00 17.75  ?  308 ASP   C N   1 
ATOM   9853  C CA  . ASP   C 1 308 ? 9.016   4.834   64.347  1.00 15.04  ?  308 ASP   C CA  1 
ATOM   9854  C C   . ASP   C 1 308 ? 9.256   6.228   64.908  1.00 14.53  ?  308 ASP   C C   1 
ATOM   9855  O O   . ASP   C 1 308 ? 8.483   6.687   65.753  1.00 16.13  ?  308 ASP   C O   1 
ATOM   9856  C CB  . ASP   C 1 308 ? 9.718   3.764   65.169  1.00 16.01  ?  308 ASP   C CB  1 
ATOM   9857  C CG  . ASP   C 1 308 ? 9.153   2.394   64.892  1.00 17.93  ?  308 ASP   C CG  1 
ATOM   9858  O OD1 . ASP   C 1 308 ? 7.910   2.248   64.986  1.00 19.61  ?  308 ASP   C OD1 1 
ATOM   9859  O OD2 . ASP   C 1 308 ? 9.933   1.480   64.550  1.00 20.80  ?  308 ASP   C OD2 1 
ATOM   9860  N N   . MET   C 1 309 ? 10.287  6.929   64.438  1.00 15.04  ?  309 MET   C N   1 
ATOM   9861  C CA  . MET   C 1 309 ? 10.393  8.345   64.770  1.00 13.65  ?  309 MET   C CA  1 
ATOM   9862  C C   . MET   C 1 309 ? 9.213   9.116   64.199  1.00 13.92  ?  309 MET   C C   1 
ATOM   9863  O O   . MET   C 1 309 ? 8.684   10.029  64.845  1.00 15.45  ?  309 MET   C O   1 
ATOM   9864  C CB  . MET   C 1 309 ? 11.717  8.914   64.259  1.00 13.87  ?  309 MET   C CB  1 
ATOM   9865  C CG  . MET   C 1 309 ? 12.926  8.493   65.072  1.00 16.31  ?  309 MET   C CG  1 
ATOM   9866  S SD  . MET   C 1 309 ? 14.450  9.264   64.477  1.00 23.50  ?  309 MET   C SD  1 
ATOM   9867  C CE  . MET   C 1 309 ? 14.630  8.457   62.892  1.00 17.45  ?  309 MET   C CE  1 
ATOM   9868  N N   . ALA   C 1 310 ? 8.759   8.740   62.996  1.00 16.13  ?  310 ALA   C N   1 
ATOM   9869  C CA  . ALA   C 1 310 ? 7.579   9.373   62.420  1.00 17.17  ?  310 ALA   C CA  1 
ATOM   9870  C C   . ALA   C 1 310 ? 6.327   9.047   63.227  1.00 16.55  ?  310 ALA   C C   1 
ATOM   9871  O O   . ALA   C 1 310 ? 5.467   9.914   63.432  1.00 16.75  ?  310 ALA   C O   1 
ATOM   9872  C CB  . ALA   C 1 310 ? 7.406   8.929   60.966  1.00 17.18  ?  310 ALA   C CB  1 
ATOM   9873  N N   . ALA   C 1 311 ? 6.193   7.796   63.670  1.00 15.46  ?  311 ALA   C N   1 
ATOM   9874  C CA  . ALA   C 1 311 ? 5.062   7.448   64.518  1.00 16.31  ?  311 ALA   C CA  1 
ATOM   9875  C C   . ALA   C 1 311 ? 5.143   8.167   65.857  1.00 15.40  ?  311 ALA   C C   1 
ATOM   9876  O O   . ALA   C 1 311 ? 4.106   8.502   66.437  1.00 19.97  ?  311 ALA   C O   1 
ATOM   9877  C CB  . ALA   C 1 311 ? 5.000   5.935   64.724  1.00 13.56  ?  311 ALA   C CB  1 
ATOM   9878  N N   . MET   C 1 312 ? 6.361   8.431   66.347  1.00 13.75  ?  312 MET   C N   1 
ATOM   9879  C CA  . MET   C 1 312 ? 6.522   9.100   67.635  1.00 12.38  ?  312 MET   C CA  1 
ATOM   9880  C C   . MET   C 1 312 ? 6.123   10.562  67.543  1.00 15.24  ?  312 MET   C C   1 
ATOM   9881  O O   . MET   C 1 312 ? 5.512   11.100  68.470  1.00 18.06  ?  312 MET   C O   1 
ATOM   9882  C CB  . MET   C 1 312 ? 7.964   8.971   68.118  1.00 11.25  ?  312 MET   C CB  1 
ATOM   9883  C CG  . MET   C 1 312 ? 8.198   9.464   69.560  1.00 15.08  ?  312 MET   C CG  1 
ATOM   9884  S SD  . MET   C 1 312 ? 9.910   9.365   70.099  1.00 21.28  ?  312 MET   C SD  1 
ATOM   9885  C CE  . MET   C 1 312 ? 10.314  7.667   69.705  1.00 17.22  ?  312 MET   C CE  1 
ATOM   9886  N N   . VAL   C 1 313 ? 6.460   11.221  66.432  1.00 16.72  ?  313 VAL   C N   1 
ATOM   9887  C CA  . VAL   C 1 313 ? 6.059   12.611  66.234  1.00 18.05  ?  313 VAL   C CA  1 
ATOM   9888  C C   . VAL   C 1 313 ? 4.542   12.740  66.273  1.00 19.29  ?  313 VAL   C C   1 
ATOM   9889  O O   . VAL   C 1 313 ? 3.998   13.682  66.862  1.00 20.34  ?  313 VAL   C O   1 
ATOM   9890  C CB  . VAL   C 1 313 ? 6.637   13.145  64.911  1.00 19.88  ?  313 VAL   C CB  1 
ATOM   9891  C CG1 . VAL   C 1 313 ? 6.154   14.562  64.647  1.00 22.88  ?  313 VAL   C CG1 1 
ATOM   9892  C CG2 . VAL   C 1 313 ? 8.145   13.097  64.945  1.00 19.50  ?  313 VAL   C CG2 1 
ATOM   9893  N N   . GLN   C 1 314 ? 3.835   11.793  65.651  1.00 20.80  ?  314 GLN   C N   1 
ATOM   9894  C CA  . GLN   C 1 314 ? 2.376   11.834  65.649  1.00 22.98  ?  314 GLN   C CA  1 
ATOM   9895  C C   . GLN   C 1 314 ? 1.804   11.399  66.991  1.00 21.45  ?  314 GLN   C C   1 
ATOM   9896  O O   . GLN   C 1 314 ? 0.827   11.987  67.474  1.00 20.78  ?  314 GLN   C O   1 
ATOM   9897  C CB  . GLN   C 1 314 ? 1.825   10.946  64.535  1.00 16.76  ?  314 GLN   C CB  1 
ATOM   9898  C CG  . GLN   C 1 314 ? 0.318   10.888  64.521  1.00 18.29  ?  314 GLN   C CG  1 
ATOM   9899  C CD  . GLN   C 1 314 ? -0.296  12.190  64.067  1.00 22.14  ?  314 GLN   C CD  1 
ATOM   9900  O OE1 . GLN   C 1 314 ? 0.344   12.972  63.364  1.00 26.05  ?  314 GLN   C OE1 1 
ATOM   9901  N NE2 . GLN   C 1 314 ? -1.545  12.430  64.454  1.00 20.64  ?  314 GLN   C NE2 1 
ATOM   9902  N N   . GLY   C 1 315 ? 2.398   10.369  67.605  1.00 21.64  ?  315 GLY   C N   1 
ATOM   9903  C CA  . GLY   C 1 315 ? 1.905   9.900   68.889  1.00 18.19  ?  315 GLY   C CA  1 
ATOM   9904  C C   . GLY   C 1 315 ? 2.105   10.901  70.005  1.00 19.34  ?  315 GLY   C C   1 
ATOM   9905  O O   . GLY   C 1 315 ? 1.287   10.982  70.921  1.00 22.61  ?  315 GLY   C O   1 
ATOM   9906  N N   . LEU   C 1 316 ? 3.194   11.668  69.955  1.00 18.07  ?  316 LEU   C N   1 
ATOM   9907  C CA  . LEU   C 1 316 ? 3.403   12.708  70.954  1.00 19.01  ?  316 LEU   C CA  1 
ATOM   9908  C C   . LEU   C 1 316 ? 2.252   13.693  70.952  1.00 22.79  ?  316 LEU   C C   1 
ATOM   9909  O O   . LEU   C 1 316 ? 1.807   14.144  72.015  1.00 22.06  ?  316 LEU   C O   1 
ATOM   9910  C CB  . LEU   C 1 316 ? 4.728   13.425  70.699  1.00 19.62  ?  316 LEU   C CB  1 
ATOM   9911  C CG  . LEU   C 1 316 ? 5.947   12.708  71.268  1.00 18.86  ?  316 LEU   C CG  1 
ATOM   9912  C CD1 . LEU   C 1 316 ? 7.227   13.284  70.670  1.00 17.09  ?  316 LEU   C CD1 1 
ATOM   9913  C CD2 . LEU   C 1 316 ? 5.945   12.808  72.799  1.00 16.28  ?  316 LEU   C CD2 1 
ATOM   9914  N N   . GLU   C 1 317 ? 1.742   14.023  69.766  1.00 23.03  ?  317 GLU   C N   1 
ATOM   9915  C CA  . GLU   C 1 317 ? 0.586   14.902  69.670  1.00 24.44  ?  317 GLU   C CA  1 
ATOM   9916  C C   . GLU   C 1 317 ? -0.663  14.216  70.209  1.00 23.39  ?  317 GLU   C C   1 
ATOM   9917  O O   . GLU   C 1 317 ? -1.350  14.753  71.088  1.00 22.97  ?  317 GLU   C O   1 
ATOM   9918  C CB  . GLU   C 1 317 ? 0.386   15.342  68.215  1.00 23.24  ?  317 GLU   C CB  1 
ATOM   9919  C CG  . GLU   C 1 317 ? -0.818  16.252  67.989  1.00 23.78  ?  317 GLU   C CG  1 
ATOM   9920  C CD  . GLU   C 1 317 ? -0.702  17.578  68.737  1.00 30.71  ?  317 GLU   C CD  1 
ATOM   9921  O OE1 . GLU   C 1 317 ? 0.424   17.957  69.126  1.00 30.39  ?  317 GLU   C OE1 1 
ATOM   9922  O OE2 . GLU   C 1 317 ? -1.743  18.242  68.946  1.00 38.28  ?  317 GLU   C OE2 1 
ATOM   9923  N N   . GLU   C 1 318 ? -0.953  13.010  69.711  1.00 21.20  ?  318 GLU   C N   1 
ATOM   9924  C CA  . GLU   C 1 318 ? -2.181  12.318  70.089  1.00 20.38  ?  318 GLU   C CA  1 
ATOM   9925  C C   . GLU   C 1 318 ? -2.255  12.052  71.583  1.00 19.52  ?  318 GLU   C C   1 
ATOM   9926  O O   . GLU   C 1 318 ? -3.348  12.079  72.160  1.00 24.91  ?  318 GLU   C O   1 
ATOM   9927  C CB  . GLU   C 1 318 ? -2.297  11.008  69.320  1.00 18.09  ?  318 GLU   C CB  1 
ATOM   9928  C CG  . GLU   C 1 318 ? -2.367  11.184  67.822  1.00 21.00  ?  318 GLU   C CG  1 
ATOM   9929  C CD  . GLU   C 1 318 ? -2.844  9.928   67.135  1.00 21.90  ?  318 GLU   C CD  1 
ATOM   9930  O OE1 . GLU   C 1 318 ? -3.253  8.985   67.854  1.00 21.09  ?  318 GLU   C OE1 1 
ATOM   9931  O OE2 . GLU   C 1 318 ? -2.820  9.884   65.889  1.00 18.87  ?  318 GLU   C OE2 1 
ATOM   9932  N N   . GLY   C 1 319 ? -1.114  11.807  72.226  1.00 20.02  ?  319 GLY   C N   1 
ATOM   9933  C CA  . GLY   C 1 319 ? -1.089  11.506  73.643  1.00 18.42  ?  319 GLY   C CA  1 
ATOM   9934  C C   . GLY   C 1 319 ? -1.400  12.680  74.535  1.00 22.26  ?  319 GLY   C C   1 
ATOM   9935  O O   . GLY   C 1 319 ? -1.684  12.475  75.721  1.00 23.25  ?  319 GLY   C O   1 
ATOM   9936  N N   . THR   C 1 320 ? -1.362  13.899  74.002  1.00 23.54  ?  320 THR   C N   1 
ATOM   9937  C CA  . THR   C 1 320 ? -1.684  15.087  74.781  1.00 24.73  ?  320 THR   C CA  1 
ATOM   9938  C C   . THR   C 1 320 ? -3.153  15.472  74.705  1.00 24.23  ?  320 THR   C C   1 
ATOM   9939  O O   . THR   C 1 320 ? -3.579  16.360  75.449  1.00 23.77  ?  320 THR   C O   1 
ATOM   9940  C CB  . THR   C 1 320 ? -0.853  16.285  74.310  1.00 25.15  ?  320 THR   C CB  1 
ATOM   9941  O OG1 . THR   C 1 320 ? -1.293  16.666  72.999  1.00 24.11  ?  320 THR   C OG1 1 
ATOM   9942  C CG2 . THR   C 1 320 ? 0.647   15.947  74.283  1.00 23.33  ?  320 THR   C CG2 1 
ATOM   9943  N N   . GLU   C 1 321 ? -3.936  14.838  73.838  1.00 28.18  ?  321 GLU   C N   1 
ATOM   9944  C CA  . GLU   C 1 321 ? -5.313  15.268  73.610  1.00 23.10  ?  321 GLU   C CA  1 
ATOM   9945  C C   . GLU   C 1 321 ? -6.179  14.981  74.832  1.00 27.03  ?  321 GLU   C C   1 
ATOM   9946  O O   . GLU   C 1 321 ? -6.263  13.837  75.290  1.00 28.58  ?  321 GLU   C O   1 
ATOM   9947  C CB  . GLU   C 1 321 ? -5.858  14.584  72.365  1.00 23.86  ?  321 GLU   C CB  1 
ATOM   9948  C CG  . GLU   C 1 321 ? -4.939  14.821  71.191  1.00 24.69  ?  321 GLU   C CG  1 
ATOM   9949  C CD  . GLU   C 1 321 ? -5.576  14.514  69.864  1.00 31.37  ?  321 GLU   C CD  1 
ATOM   9950  O OE1 . GLU   C 1 321 ? -6.608  13.822  69.855  1.00 38.48  ?  321 GLU   C OE1 1 
ATOM   9951  O OE2 . GLU   C 1 321 ? -5.045  14.971  68.828  1.00 34.28  ?  321 GLU   C OE2 1 
ATOM   9952  N N   . GLU   C 1 322 ? -6.819  16.030  75.358  1.00 26.03  ?  322 GLU   C N   1 
ATOM   9953  C CA  . GLU   C 1 322 ? -7.502  15.926  76.643  1.00 29.20  ?  322 GLU   C CA  1 
ATOM   9954  C C   . GLU   C 1 322 ? -8.667  14.949  76.576  1.00 24.37  ?  322 GLU   C C   1 
ATOM   9955  O O   . GLU   C 1 322 ? -8.941  14.227  77.543  1.00 24.93  ?  322 GLU   C O   1 
ATOM   9956  C CB  . GLU   C 1 322 ? -7.982  17.309  77.090  1.00 25.00  ?  322 GLU   C CB  1 
ATOM   9957  C CG  . GLU   C 1 322 ? -8.819  17.304  78.354  1.00 30.91  ?  322 GLU   C CG  1 
ATOM   9958  C CD  . GLU   C 1 322 ? -8.981  18.692  78.956  1.00 35.54  ?  322 GLU   C CD  1 
ATOM   9959  O OE1 . GLU   C 1 322 ? -8.242  19.615  78.548  1.00 32.88  ?  322 GLU   C OE1 1 
ATOM   9960  O OE2 . GLU   C 1 322 ? -9.846  18.858  79.843  1.00 40.67  ?  322 GLU   C OE2 1 
ATOM   9961  N N   . GLU   C 1 323 ? -9.360  14.904  75.441  1.00 24.26  ?  323 GLU   C N   1 
ATOM   9962  C CA  . GLU   C 1 323 ? -10.524 14.037  75.353  1.00 26.40  ?  323 GLU   C CA  1 
ATOM   9963  C C   . GLU   C 1 323 ? -10.109 12.571  75.340  1.00 26.47  ?  323 GLU   C C   1 
ATOM   9964  O O   . GLU   C 1 323 ? -10.798 11.722  75.921  1.00 29.87  ?  323 GLU   C O   1 
ATOM   9965  C CB  . GLU   C 1 323 ? -11.363 14.401  74.125  1.00 27.10  ?  323 GLU   C CB  1 
ATOM   9966  C CG  . GLU   C 1 323 ? -10.642 14.287  72.791  1.00 36.50  ?  323 GLU   C CG  1 
ATOM   9967  C CD  . GLU   C 1 323 ? -9.815  15.522  72.424  1.00 47.49  ?  323 GLU   C CD  1 
ATOM   9968  O OE1 . GLU   C 1 323 ? -9.434  16.293  73.343  1.00 37.26  ?  323 GLU   C OE1 1 
ATOM   9969  O OE2 . GLU   C 1 323 ? -9.545  15.713  71.208  1.00 45.95  ?  323 GLU   C OE2 1 
ATOM   9970  N N   . TYR   C 1 324 ? -8.977  12.253  74.709  1.00 21.58  ?  324 TYR   C N   1 
ATOM   9971  C CA  . TYR   C 1 324 ? -8.449  10.898  74.806  1.00 22.22  ?  324 TYR   C CA  1 
ATOM   9972  C C   . TYR   C 1 324 ? -7.984  10.581  76.229  1.00 23.33  ?  324 TYR   C C   1 
ATOM   9973  O O   . TYR   C 1 324 ? -8.263  9.493   76.748  1.00 24.22  ?  324 TYR   C O   1 
ATOM   9974  C CB  . TYR   C 1 324 ? -7.309  10.692  73.800  1.00 24.33  ?  324 TYR   C CB  1 
ATOM   9975  C CG  . TYR   C 1 324 ? -6.291  9.711   74.325  1.00 22.33  ?  324 TYR   C CG  1 
ATOM   9976  C CD1 . TYR   C 1 324 ? -6.501  8.340   74.234  1.00 17.76  ?  324 TYR   C CD1 1 
ATOM   9977  C CD2 . TYR   C 1 324 ? -5.135  10.159  74.960  1.00 24.57  ?  324 TYR   C CD2 1 
ATOM   9978  C CE1 . TYR   C 1 324 ? -5.581  7.448   74.755  1.00 19.32  ?  324 TYR   C CE1 1 
ATOM   9979  C CE2 . TYR   C 1 324 ? -4.217  9.276   75.479  1.00 20.06  ?  324 TYR   C CE2 1 
ATOM   9980  C CZ  . TYR   C 1 324 ? -4.448  7.926   75.377  1.00 19.06  ?  324 TYR   C CZ  1 
ATOM   9981  O OH  . TYR   C 1 324 ? -3.518  7.062   75.899  1.00 23.60  ?  324 TYR   C OH  1 
ATOM   9982  N N   . LEU   C 1 325 ? -7.263  11.507  76.878  1.00 20.87  ?  325 LEU   C N   1 
ATOM   9983  C CA  . LEU   C 1 325 ? -6.769  11.244  78.229  1.00 22.70  ?  325 LEU   C CA  1 
ATOM   9984  C C   . LEU   C 1 325 ? -7.914  11.051  79.209  1.00 23.85  ?  325 LEU   C C   1 
ATOM   9985  O O   . LEU   C 1 325 ? -7.828  10.219  80.124  1.00 22.44  ?  325 LEU   C O   1 
ATOM   9986  C CB  . LEU   C 1 325 ? -5.865  12.385  78.695  1.00 22.24  ?  325 LEU   C CB  1 
ATOM   9987  C CG  . LEU   C 1 325 ? -4.481  12.432  78.045  1.00 21.93  ?  325 LEU   C CG  1 
ATOM   9988  C CD1 . LEU   C 1 325 ? -3.869  13.807  78.223  1.00 22.52  ?  325 LEU   C CD1 1 
ATOM   9989  C CD2 . LEU   C 1 325 ? -3.593  11.372  78.664  1.00 23.28  ?  325 LEU   C CD2 1 
ATOM   9990  N N   . HIS   C 1 326 ? -8.987  11.830  79.045  1.00 25.07  ?  326 HIS   C N   1 
ATOM   9991  C CA  . HIS   C 1 326 ? -10.156 11.701  79.908  1.00 25.32  ?  326 HIS   C CA  1 
ATOM   9992  C C   . HIS   C 1 326 ? -10.769 10.309  79.797  1.00 26.31  ?  326 HIS   C C   1 
ATOM   9993  O O   . HIS   C 1 326 ? -11.098 9.680   80.811  1.00 25.36  ?  326 HIS   C O   1 
ATOM   9994  C CB  . HIS   C 1 326 ? -11.170 12.783  79.545  1.00 24.26  ?  326 HIS   C CB  1 
ATOM   9995  C CG  . HIS   C 1 326 ? -12.463 12.676  80.289  1.00 25.27  ?  326 HIS   C CG  1 
ATOM   9996  N ND1 . HIS   C 1 326 ? -12.556 12.868  81.649  1.00 32.59  ?  326 HIS   C ND1 1 
ATOM   9997  C CD2 . HIS   C 1 326 ? -13.716 12.398  79.861  1.00 29.16  ?  326 HIS   C CD2 1 
ATOM   9998  C CE1 . HIS   C 1 326 ? -13.811 12.712  82.029  1.00 38.11  ?  326 HIS   C CE1 1 
ATOM   9999  N NE2 . HIS   C 1 326 ? -14.535 12.426  80.963  1.00 30.70  ?  326 HIS   C NE2 1 
ATOM   10000 N N   . TYR   C 1 327 ? -10.913 9.807   78.567  1.00 22.58  ?  327 TYR   C N   1 
ATOM   10001 C CA  A TYR   C 1 327 ? -11.435 8.459   78.362  0.61 23.05  ?  327 TYR   C CA  1 
ATOM   10002 C CA  B TYR   C 1 327 ? -11.436 8.460   78.363  0.39 23.07  ?  327 TYR   C CA  1 
ATOM   10003 C C   . TYR   C 1 327 ? -10.470 7.404   78.889  1.00 22.07  ?  327 TYR   C C   1 
ATOM   10004 O O   . TYR   C 1 327 ? -10.883 6.455   79.562  1.00 25.29  ?  327 TYR   C O   1 
ATOM   10005 C CB  A TYR   C 1 327 ? -11.717 8.226   76.873  0.61 24.73  ?  327 TYR   C CB  1 
ATOM   10006 C CB  B TYR   C 1 327 ? -11.722 8.227   76.876  0.39 24.72  ?  327 TYR   C CB  1 
ATOM   10007 C CG  A TYR   C 1 327 ? -11.254 6.871   76.363  0.61 24.01  ?  327 TYR   C CG  1 
ATOM   10008 C CG  B TYR   C 1 327 ? -11.780 6.762   76.497  0.39 24.05  ?  327 TYR   C CG  1 
ATOM   10009 C CD1 A TYR   C 1 327 ? -12.060 5.746   76.484  0.61 23.72  ?  327 TYR   C CD1 1 
ATOM   10010 C CD1 B TYR   C 1 327 ? -12.955 6.038   76.626  0.39 23.33  ?  327 TYR   C CD1 1 
ATOM   10011 C CD2 A TYR   C 1 327 ? -10.006 6.718   75.766  0.61 23.15  ?  327 TYR   C CD2 1 
ATOM   10012 C CD2 B TYR   C 1 327 ? -10.652 6.099   76.022  0.39 23.44  ?  327 TYR   C CD2 1 
ATOM   10013 C CE1 A TYR   C 1 327 ? -11.634 4.509   76.029  0.61 23.54  ?  327 TYR   C CE1 1 
ATOM   10014 C CE1 B TYR   C 1 327 ? -13.008 4.698   76.293  0.39 23.17  ?  327 TYR   C CE1 1 
ATOM   10015 C CE2 A TYR   C 1 327 ? -9.572  5.486   75.312  0.61 22.47  ?  327 TYR   C CE2 1 
ATOM   10016 C CE2 B TYR   C 1 327 ? -10.695 4.762   75.691  0.39 22.90  ?  327 TYR   C CE2 1 
ATOM   10017 C CZ  A TYR   C 1 327 ? -10.391 4.385   75.439  0.61 22.86  ?  327 TYR   C CZ  1 
ATOM   10018 C CZ  B TYR   C 1 327 ? -11.874 4.064   75.827  0.39 23.91  ?  327 TYR   C CZ  1 
ATOM   10019 O OH  A TYR   C 1 327 ? -9.958  3.158   74.974  0.61 20.20  ?  327 TYR   C OH  1 
ATOM   10020 O OH  B TYR   C 1 327 ? -11.920 2.729   75.489  0.39 23.59  ?  327 TYR   C OH  1 
ATOM   10021 N N   . ARG   C 1 328 ? -9.181  7.541   78.572  1.00 21.93  ?  328 ARG   C N   1 
ATOM   10022 C CA  . ARG   C 1 328 ? -8.207  6.525   78.962  1.00 21.33  ?  328 ARG   C CA  1 
ATOM   10023 C C   . ARG   C 1 328 ? -8.116  6.406   80.475  1.00 23.42  ?  328 ARG   C C   1 
ATOM   10024 O O   . ARG   C 1 328 ? -8.088  5.297   81.024  1.00 22.43  ?  328 ARG   C O   1 
ATOM   10025 C CB  . ARG   C 1 328 ? -6.841  6.861   78.354  1.00 19.84  ?  328 ARG   C CB  1 
ATOM   10026 C CG  . ARG   C 1 328 ? -5.748  5.798   78.525  1.00 21.41  ?  328 ARG   C CG  1 
ATOM   10027 C CD  . ARG   C 1 328 ? -5.131  5.808   79.945  1.00 19.45  ?  328 ARG   C CD  1 
ATOM   10028 N NE  . ARG   C 1 328 ? -3.812  5.189   80.006  1.00 20.86  ?  328 ARG   C NE  1 
ATOM   10029 C CZ  . ARG   C 1 328 ? -3.585  3.888   79.890  1.00 18.70  ?  328 ARG   C CZ  1 
ATOM   10030 N NH1 . ARG   C 1 328 ? -4.563  3.033   79.627  1.00 17.90  ?  328 ARG   C NH1 1 
ATOM   10031 N NH2 . ARG   C 1 328 ? -2.348  3.435   80.045  1.00 17.46  ?  328 ARG   C NH2 1 
ATOM   10032 N N   . ILE   C 1 329 ? -8.024  7.541   81.167  1.00 21.73  ?  329 ILE   C N   1 
ATOM   10033 C CA  . ILE   C 1 329 ? -7.855  7.493   82.609  1.00 22.02  ?  329 ILE   C CA  1 
ATOM   10034 C C   . ILE   C 1 329 ? -9.171  7.142   83.272  1.00 22.94  ?  329 ILE   C C   1 
ATOM   10035 O O   . ILE   C 1 329 ? -9.188  6.464   84.303  1.00 23.49  ?  329 ILE   C O   1 
ATOM   10036 C CB  . ILE   C 1 329 ? -7.279  8.824   83.120  1.00 23.38  ?  329 ILE   C CB  1 
ATOM   10037 C CG1 . ILE   C 1 329 ? -5.923  9.087   82.458  1.00 23.09  ?  329 ILE   C CG1 1 
ATOM   10038 C CG2 . ILE   C 1 329 ? -7.131  8.812   84.632  1.00 24.96  ?  329 ILE   C CG2 1 
ATOM   10039 C CD1 . ILE   C 1 329 ? -5.257  10.338  82.922  1.00 24.87  ?  329 ILE   C CD1 1 
ATOM   10040 N N   . GLY   C 1 330 ? -10.290 7.560   82.674  1.00 26.01  ?  330 GLY   C N   1 
ATOM   10041 C CA  . GLY   C 1 330 ? -11.592 7.164   83.180  1.00 25.04  ?  330 GLY   C CA  1 
ATOM   10042 C C   . GLY   C 1 330 ? -11.882 5.684   83.015  1.00 24.81  ?  330 GLY   C C   1 
ATOM   10043 O O   . GLY   C 1 330 ? -12.611 5.098   83.826  1.00 26.80  ?  330 GLY   C O   1 
ATOM   10044 N N   . GLN   C 1 331 ? -11.329 5.058   81.974  1.00 22.84  ?  331 GLN   C N   1 
ATOM   10045 C CA  . GLN   C 1 331 ? -11.462 3.611   81.852  1.00 22.42  ?  331 GLN   C CA  1 
ATOM   10046 C C   . GLN   C 1 331 ? -10.711 2.896   82.969  1.00 22.34  ?  331 GLN   C C   1 
ATOM   10047 O O   . GLN   C 1 331 ? -11.219 1.926   83.546  1.00 24.24  ?  331 GLN   C O   1 
ATOM   10048 C CB  . GLN   C 1 331 ? -10.963 3.137   80.490  1.00 22.85  ?  331 GLN   C CB  1 
ATOM   10049 C CG  . GLN   C 1 331 ? -11.029 1.623   80.347  1.00 23.32  ?  331 GLN   C CG  1 
ATOM   10050 C CD  . GLN   C 1 331 ? -10.567 1.139   79.000  1.00 22.90  ?  331 GLN   C CD  1 
ATOM   10051 O OE1 . GLN   C 1 331 ? -9.388  1.234   78.669  1.00 19.99  ?  331 GLN   C OE1 1 
ATOM   10052 N NE2 . GLN   C 1 331 ? -11.496 0.614   78.209  1.00 20.67  ?  331 GLN   C NE2 1 
ATOM   10053 N N   . VAL   C 1 332 ? -9.504  3.359   83.290  1.00 21.95  ?  332 VAL   C N   1 
ATOM   10054 C CA  . VAL   C 1 332 ? -8.797  2.822   84.450  1.00 22.36  ?  332 VAL   C CA  1 
ATOM   10055 C C   . VAL   C 1 332 ? -9.612  3.053   85.716  1.00 25.78  ?  332 VAL   C C   1 
ATOM   10056 O O   . VAL   C 1 332 ? -9.717  2.170   86.577  1.00 24.91  ?  332 VAL   C O   1 
ATOM   10057 C CB  . VAL   C 1 332 ? -7.394  3.445   84.566  1.00 21.88  ?  332 VAL   C CB  1 
ATOM   10058 C CG1 . VAL   C 1 332 ? -6.735  3.005   85.863  1.00 21.63  ?  332 VAL   C CG1 1 
ATOM   10059 C CG2 . VAL   C 1 332 ? -6.522  3.061   83.363  1.00 23.01  ?  332 VAL   C CG2 1 
ATOM   10060 N N   . LYS   C 1 333 ? -10.197 4.245   85.851  1.00 23.90  ?  333 LYS   C N   1 
ATOM   10061 C CA  . LYS   C 1 333 ? -11.031 4.525   87.009  1.00 25.05  ?  333 LYS   C CA  1 
ATOM   10062 C C   . LYS   C 1 333 ? -12.249 3.612   87.031  1.00 25.49  ?  333 LYS   C C   1 
ATOM   10063 O O   . LYS   C 1 333 ? -12.636 3.118   88.095  1.00 28.56  ?  333 LYS   C O   1 
ATOM   10064 C CB  . LYS   C 1 333 ? -11.450 5.995   87.011  1.00 25.73  ?  333 LYS   C CB  1 
ATOM   10065 C CG  . LYS   C 1 333 ? -11.935 6.492   88.362  1.00 30.67  ?  333 LYS   C CG  1 
ATOM   10066 C CD  . LYS   C 1 333 ? -12.475 7.919   88.282  1.00 33.00  ?  333 LYS   C CD  1 
ATOM   10067 C CE  . LYS   C 1 333 ? -13.063 8.368   89.621  1.00 37.65  ?  333 LYS   C CE  1 
ATOM   10068 N NZ  . LYS   C 1 333 ? -14.279 7.586   90.001  1.00 30.00  ?  333 LYS   C NZ  1 
ATOM   10069 N N   . TYR   C 1 334 ? -12.840 3.345   85.862  1.00 25.15  ?  334 TYR   C N   1 
ATOM   10070 C CA  . TYR   C 1 334 ? -14.021 2.484   85.795  1.00 25.57  ?  334 TYR   C CA  1 
ATOM   10071 C C   . TYR   C 1 334 ? -13.720 1.086   86.324  1.00 25.30  ?  334 TYR   C C   1 
ATOM   10072 O O   . TYR   C 1 334 ? -14.482 0.538   87.130  1.00 26.16  ?  334 TYR   C O   1 
ATOM   10073 C CB  . TYR   C 1 334 ? -14.545 2.417   84.359  1.00 25.13  ?  334 TYR   C CB  1 
ATOM   10074 C CG  . TYR   C 1 334 ? -15.678 1.432   84.163  1.00 25.46  ?  334 TYR   C CG  1 
ATOM   10075 C CD1 . TYR   C 1 334 ? -16.967 1.737   84.569  1.00 28.58  ?  334 TYR   C CD1 1 
ATOM   10076 C CD2 . TYR   C 1 334 ? -15.456 0.201   83.567  1.00 28.50  ?  334 TYR   C CD2 1 
ATOM   10077 C CE1 . TYR   C 1 334 ? -18.007 0.833   84.396  1.00 26.86  ?  334 TYR   C CE1 1 
ATOM   10078 C CE2 . TYR   C 1 334 ? -16.489 -0.707  83.387  1.00 25.05  ?  334 TYR   C CE2 1 
ATOM   10079 C CZ  . TYR   C 1 334 ? -17.755 -0.383  83.804  1.00 26.12  ?  334 TYR   C CZ  1 
ATOM   10080 O OH  . TYR   C 1 334 ? -18.775 -1.283  83.628  1.00 26.64  ?  334 TYR   C OH  1 
ATOM   10081 N N   . LEU   C 1 335 ? -12.603 0.495   85.893  1.00 24.26  ?  335 LEU   C N   1 
ATOM   10082 C CA  . LEU   C 1 335 ? -12.223 -0.812  86.420  1.00 23.99  ?  335 LEU   C CA  1 
ATOM   10083 C C   . LEU   C 1 335 ? -11.986 -0.748  87.927  1.00 25.64  ?  335 LEU   C C   1 
ATOM   10084 O O   . LEU   C 1 335 ? -12.396 -1.650  88.669  1.00 25.09  ?  335 LEU   C O   1 
ATOM   10085 C CB  . LEU   C 1 335 ? -10.981 -1.328  85.693  1.00 22.76  ?  335 LEU   C CB  1 
ATOM   10086 C CG  . LEU   C 1 335 ? -10.402 -2.627  86.252  1.00 22.41  ?  335 LEU   C CG  1 
ATOM   10087 C CD1 . LEU   C 1 335 ? -11.448 -3.735  86.239  1.00 25.02  ?  335 LEU   C CD1 1 
ATOM   10088 C CD2 . LEU   C 1 335 ? -9.163  -3.032  85.473  1.00 21.19  ?  335 LEU   C CD2 1 
ATOM   10089 N N   . GLY   C 1 336 ? -11.347 0.322   88.401  1.00 25.18  ?  336 GLY   C N   1 
ATOM   10090 C CA  . GLY   C 1 336 ? -11.120 0.460   89.829  1.00 25.98  ?  336 GLY   C CA  1 
ATOM   10091 C C   . GLY   C 1 336 ? -12.404 0.630   90.612  1.00 28.29  ?  336 GLY   C C   1 
ATOM   10092 O O   . GLY   C 1 336 ? -12.533 0.120   91.729  1.00 31.11  ?  336 GLY   C O   1 
ATOM   10093 N N   . ASP   C 1 337 ? -13.376 1.345   90.041  1.00 27.14  ?  337 ASP   C N   1 
ATOM   10094 C CA  . ASP   C 1 337 ? -14.658 1.511   90.714  1.00 30.87  ?  337 ASP   C CA  1 
ATOM   10095 C C   . ASP   C 1 337 ? -15.450 0.204   90.739  1.00 30.71  ?  337 ASP   C C   1 
ATOM   10096 O O   . ASP   C 1 337 ? -16.076 -0.125  91.755  1.00 30.37  ?  337 ASP   C O   1 
ATOM   10097 C CB  . ASP   C 1 337 ? -15.459 2.630   90.045  1.00 28.71  ?  337 ASP   C CB  1 
ATOM   10098 C CG  . ASP   C 1 337 ? -14.979 4.015   90.455  1.00 31.24  ?  337 ASP   C CG  1 
ATOM   10099 O OD1 . ASP   C 1 337 ? -14.397 4.143   91.553  1.00 35.56  ?  337 ASP   C OD1 1 
ATOM   10100 O OD2 . ASP   C 1 337 ? -15.189 4.981   89.690  1.00 29.28  ?  337 ASP   C OD2 1 
ATOM   10101 N N   . ARG   C 1 338 ? -15.425 -0.561  89.639  1.00 31.85  ?  338 ARG   C N   1 
ATOM   10102 C CA  . ARG   C 1 338 ? -16.091 -1.861  89.635  1.00 28.66  ?  338 ARG   C CA  1 
ATOM   10103 C C   . ARG   C 1 338 ? -15.561 -2.748  90.751  1.00 29.57  ?  338 ARG   C C   1 
ATOM   10104 O O   . ARG   C 1 338 ? -16.321 -3.493  91.378  1.00 30.55  ?  338 ARG   C O   1 
ATOM   10105 C CB  . ARG   C 1 338 ? -15.906 -2.560  88.287  1.00 27.25  ?  338 ARG   C CB  1 
ATOM   10106 C CG  . ARG   C 1 338 ? -16.633 -1.942  87.083  1.00 28.30  ?  338 ARG   C CG  1 
ATOM   10107 C CD  . ARG   C 1 338 ? -18.116 -2.285  87.045  1.00 29.09  ?  338 ARG   C CD  1 
ATOM   10108 N NE  . ARG   C 1 338 ? -18.435 -3.494  87.794  1.00 32.73  ?  338 ARG   C NE  1 
ATOM   10109 C CZ  . ARG   C 1 338 ? -18.381 -4.725  87.302  1.00 31.43  ?  338 ARG   C CZ  1 
ATOM   10110 N NH1 . ARG   C 1 338 ? -18.020 -4.956  86.053  1.00 26.64  ?  338 ARG   C NH1 1 
ATOM   10111 N NH2 . ARG   C 1 338 ? -18.694 -5.750  88.090  1.00 34.40  ?  338 ARG   C NH2 1 
ATOM   10112 N N   . LEU   C 1 339 ? -14.257 -2.678  91.017  1.00 29.14  ?  339 LEU   C N   1 
ATOM   10113 C CA  . LEU   C 1 339 ? -13.662 -3.523  92.045  1.00 31.25  ?  339 LEU   C CA  1 
ATOM   10114 C C   . LEU   C 1 339 ? -14.000 -3.017  93.443  1.00 32.90  ?  339 LEU   C C   1 
ATOM   10115 O O   . LEU   C 1 339 ? -14.419 -3.795  94.307  1.00 31.59  ?  339 LEU   C O   1 
ATOM   10116 C CB  . LEU   C 1 339 ? -12.143 -3.601  91.843  1.00 30.38  ?  339 LEU   C CB  1 
ATOM   10117 C CG  . LEU   C 1 339 ? -11.668 -4.252  90.540  1.00 30.91  ?  339 LEU   C CG  1 
ATOM   10118 C CD1 . LEU   C 1 339 ? -10.141 -4.354  90.492  1.00 27.03  ?  339 LEU   C CD1 1 
ATOM   10119 C CD2 . LEU   C 1 339 ? -12.315 -5.619  90.375  1.00 28.20  ?  339 LEU   C CD2 1 
ATOM   10120 N N   . ARG   C 1 340 ? -13.819 -1.716  93.686  1.00 29.50  ?  340 ARG   C N   1 
ATOM   10121 C CA  . ARG   C 1 340 ? -14.165 -1.158  94.988  1.00 31.36  ?  340 ARG   C CA  1 
ATOM   10122 C C   . ARG   C 1 340 ? -15.611 -1.470  95.352  1.00 34.06  ?  340 ARG   C C   1 
ATOM   10123 O O   . ARG   C 1 340 ? -15.902 -1.904  96.473  1.00 33.90  ?  340 ARG   C O   1 
ATOM   10124 C CB  . ARG   C 1 340 ? -13.920 0.348   94.994  1.00 31.13  ?  340 ARG   C CB  1 
ATOM   10125 C CG  . ARG   C 1 340 ? -12.463 0.727   95.017  1.00 34.85  ?  340 ARG   C CG  1 
ATOM   10126 C CD  . ARG   C 1 340 ? -12.301 2.231   95.019  1.00 37.71  ?  340 ARG   C CD  1 
ATOM   10127 N NE  . ARG   C 1 340 ? -13.166 2.868   96.004  1.00 38.44  ?  340 ARG   C NE  1 
ATOM   10128 C CZ  . ARG   C 1 340 ? -12.809 3.139   97.252  1.00 42.22  ?  340 ARG   C CZ  1 
ATOM   10129 N NH1 . ARG   C 1 340 ? -11.619 2.794   97.719  1.00 43.29  ?  340 ARG   C NH1 1 
ATOM   10130 N NH2 . ARG   C 1 340 ? -13.664 3.776   98.048  1.00 41.16  ?  340 ARG   C NH2 1 
ATOM   10131 N N   . GLU   C 1 341 ? -16.532 -1.273  94.406  1.00 31.72  ?  341 GLU   C N   1 
ATOM   10132 C CA  . GLU   C 1 341 ? -17.943 -1.511  94.692  1.00 33.81  ?  341 GLU   C CA  1 
ATOM   10133 C C   . GLU   C 1 341 ? -18.214 -2.964  95.054  1.00 39.05  ?  341 GLU   C C   1 
ATOM   10134 O O   . GLU   C 1 341 ? -19.237 -3.253  95.686  1.00 39.19  ?  341 GLU   C O   1 
ATOM   10135 C CB  . GLU   C 1 341 ? -18.807 -1.085  93.502  1.00 31.83  ?  341 GLU   C CB  1 
ATOM   10136 C CG  . GLU   C 1 341 ? -18.806 0.421   93.259  1.00 39.43  ?  341 GLU   C CG  1 
ATOM   10137 C CD  . GLU   C 1 341 ? -19.455 0.817   91.939  1.00 40.99  ?  341 GLU   C CD  1 
ATOM   10138 O OE1 . GLU   C 1 341 ? -20.460 0.188   91.546  1.00 45.89  ?  341 GLU   C OE1 1 
ATOM   10139 O OE2 . GLU   C 1 341 ? -18.956 1.759   91.289  1.00 36.56  ?  341 GLU   C OE2 1 
ATOM   10140 N N   . ALA   C 1 342 ? -17.319 -3.882  94.689  1.00 34.78  ?  342 ALA   C N   1 
ATOM   10141 C CA  . ALA   C 1 342 ? -17.442 -5.275  95.093  1.00 37.87  ?  342 ALA   C CA  1 
ATOM   10142 C C   . ALA   C 1 342 ? -16.591 -5.607  96.312  1.00 37.63  ?  342 ALA   C C   1 
ATOM   10143 O O   . ALA   C 1 342 ? -16.435 -6.785  96.644  1.00 37.19  ?  342 ALA   C O   1 
ATOM   10144 C CB  . ALA   C 1 342 ? -17.081 -6.200  93.934  1.00 36.09  ?  342 ALA   C CB  1 
ATOM   10145 N N   . GLY   C 1 343 ? -16.039 -4.599  96.982  1.00 35.01  ?  343 GLY   C N   1 
ATOM   10146 C CA  . GLY   C 1 343 ? -15.298 -4.835  98.202  1.00 37.03  ?  343 GLY   C CA  1 
ATOM   10147 C C   . GLY   C 1 343 ? -13.865 -5.263  98.007  1.00 42.05  ?  343 GLY   C C   1 
ATOM   10148 O O   . GLY   C 1 343 ? -13.258 -5.792  98.945  1.00 39.78  ?  343 GLY   C O   1 
ATOM   10149 N N   . ILE   C 1 344 ? -13.304 -5.058  96.820  1.00 39.32  ?  344 ILE   C N   1 
ATOM   10150 C CA  . ILE   C 1 344 ? -11.911 -5.394  96.542  1.00 37.03  ?  344 ILE   C CA  1 
ATOM   10151 C C   . ILE   C 1 344 ? -11.048 -4.198  96.933  1.00 38.13  ?  344 ILE   C C   1 
ATOM   10152 O O   . ILE   C 1 344 ? -11.275 -3.093  96.417  1.00 34.86  ?  344 ILE   C O   1 
ATOM   10153 C CB  . ILE   C 1 344 ? -11.694 -5.754  95.071  1.00 37.50  ?  344 ILE   C CB  1 
ATOM   10154 C CG1 . ILE   C 1 344 ? -12.677 -6.839  94.629  1.00 37.55  ?  344 ILE   C CG1 1 
ATOM   10155 C CG2 . ILE   C 1 344 ? -10.259 -6.192  94.859  1.00 31.57  ?  344 ILE   C CG2 1 
ATOM   10156 C CD1 . ILE   C 1 344 ? -12.595 -8.096  95.450  1.00 40.77  ?  344 ILE   C CD1 1 
ATOM   10157 N N   . PRO   C 1 345 ? -10.053 -4.372  97.801  1.00 35.82  ?  345 PRO   C N   1 
ATOM   10158 C CA  . PRO   C 1 345 ? -9.164  -3.254  98.131  1.00 39.35  ?  345 PRO   C CA  1 
ATOM   10159 C C   . PRO   C 1 345 ? -8.222  -2.946  96.977  1.00 40.25  ?  345 PRO   C C   1 
ATOM   10160 O O   . PRO   C 1 345 ? -7.672  -3.849  96.340  1.00 38.39  ?  345 PRO   C O   1 
ATOM   10161 C CB  . PRO   C 1 345 ? -8.400  -3.760  99.361  1.00 44.19  ?  345 PRO   C CB  1 
ATOM   10162 C CG  . PRO   C 1 345 ? -8.411  -5.240  99.215  1.00 44.17  ?  345 PRO   C CG  1 
ATOM   10163 C CD  . PRO   C 1 345 ? -9.723  -5.588  98.565  1.00 48.05  ?  345 PRO   C CD  1 
ATOM   10164 N N   . ILE   C 1 346 ? -8.063  -1.652  96.691  1.00 34.28  ?  346 ILE   C N   1 
ATOM   10165 C CA  . ILE   C 1 346 ? -7.187  -1.182  95.627  1.00 34.20  ?  346 ILE   C CA  1 
ATOM   10166 C C   . ILE   C 1 346 ? -6.528  0.108   96.088  1.00 32.83  ?  346 ILE   C C   1 
ATOM   10167 O O   . ILE   C 1 346 ? -7.016  0.794   96.988  1.00 33.69  ?  346 ILE   C O   1 
ATOM   10168 C CB  . ILE   C 1 346 ? -7.924  -0.932  94.278  1.00 34.68  ?  346 ILE   C CB  1 
ATOM   10169 C CG1 . ILE   C 1 346 ? -8.689  0.396   94.308  1.00 30.26  ?  346 ILE   C CG1 1 
ATOM   10170 C CG2 . ILE   C 1 346 ? -8.858  -2.093  93.906  1.00 32.02  ?  346 ILE   C CG2 1 
ATOM   10171 C CD1 . ILE   C 1 346 ? -9.413  0.706   93.019  1.00 32.33  ?  346 ILE   C CD1 1 
ATOM   10172 N N   . GLN   C 1 347 ? -5.399  0.430   95.462  1.00 30.72  ?  347 GLN   C N   1 
ATOM   10173 C CA  . GLN   C 1 347 ? -4.816  1.752   95.638  1.00 34.48  ?  347 GLN   C CA  1 
ATOM   10174 C C   . GLN   C 1 347 ? -5.819  2.803   95.187  1.00 33.34  ?  347 GLN   C C   1 
ATOM   10175 O O   . GLN   C 1 347 ? -6.217  2.838   94.019  1.00 36.56  ?  347 GLN   C O   1 
ATOM   10176 C CB  . GLN   C 1 347 ? -3.510  1.879   94.855  1.00 28.05  ?  347 GLN   C CB  1 
ATOM   10177 C CG  . GLN   C 1 347 ? -3.010  3.319   94.692  1.00 31.54  ?  347 GLN   C CG  1 
ATOM   10178 C CD  . GLN   C 1 347 ? -2.245  3.850   95.904  1.00 38.26  ?  347 GLN   C CD  1 
ATOM   10179 O OE1 . GLN   C 1 347 ? -2.717  3.781   97.037  1.00 38.98  ?  347 GLN   C OE1 1 
ATOM   10180 N NE2 . GLN   C 1 347 ? -1.055  4.397   95.659  1.00 37.55  ?  347 GLN   C NE2 1 
ATOM   10181 N N   . TYR   C 1 348 ? -6.243  3.646   96.118  1.00 27.29  ?  348 TYR   C N   1 
ATOM   10182 C CA  . TYR   C 1 348 ? -7.268  4.636   95.861  1.00 30.90  ?  348 TYR   C CA  1 
ATOM   10183 C C   . TYR   C 1 348 ? -6.686  6.029   96.065  1.00 32.58  ?  348 TYR   C C   1 
ATOM   10184 O O   . TYR   C 1 348 ? -5.998  6.259   97.069  1.00 35.32  ?  348 TYR   C O   1 
ATOM   10185 C CB  . TYR   C 1 348 ? -8.459  4.398   96.799  1.00 34.43  ?  348 TYR   C CB  1 
ATOM   10186 C CG  . TYR   C 1 348 ? -9.632  5.336   96.629  1.00 37.82  ?  348 TYR   C CG  1 
ATOM   10187 C CD1 . TYR   C 1 348 ? -10.334 5.400   95.432  1.00 34.81  ?  348 TYR   C CD1 1 
ATOM   10188 C CD2 . TYR   C 1 348 ? -10.061 6.129   97.689  1.00 36.43  ?  348 TYR   C CD2 1 
ATOM   10189 C CE1 . TYR   C 1 348 ? -11.417 6.255   95.288  1.00 38.39  ?  348 TYR   C CE1 1 
ATOM   10190 C CE2 . TYR   C 1 348 ? -11.131 6.976   97.559  1.00 35.98  ?  348 TYR   C CE2 1 
ATOM   10191 C CZ  . TYR   C 1 348 ? -11.809 7.035   96.362  1.00 38.65  ?  348 TYR   C CZ  1 
ATOM   10192 O OH  . TYR   C 1 348 ? -12.877 7.891   96.247  1.00 45.05  ?  348 TYR   C OH  1 
ATOM   10193 N N   . PRO   C 1 349 ? -6.883  6.969   95.127  1.00 30.23  ?  349 PRO   C N   1 
ATOM   10194 C CA  . PRO   C 1 349 ? -7.589  6.856   93.843  1.00 29.19  ?  349 PRO   C CA  1 
ATOM   10195 C C   . PRO   C 1 349 ? -6.789  6.056   92.826  1.00 29.06  ?  349 PRO   C C   1 
ATOM   10196 O O   . PRO   C 1 349 ? -5.606  5.790   93.054  1.00 27.73  ?  349 PRO   C O   1 
ATOM   10197 C CB  . PRO   C 1 349 ? -7.737  8.318   93.412  1.00 28.38  ?  349 PRO   C CB  1 
ATOM   10198 C CG  . PRO   C 1 349 ? -6.489  8.960   93.937  1.00 27.85  ?  349 PRO   C CG  1 
ATOM   10199 C CD  . PRO   C 1 349 ? -6.229  8.284   95.266  1.00 29.61  ?  349 PRO   C CD  1 
ATOM   10200 N N   . THR   C 1 350 ? -7.391  5.661   91.705  1.00 26.34  ?  350 THR   C N   1 
ATOM   10201 C CA  . THR   C 1 350 ? -6.646  4.942   90.681  1.00 25.65  ?  350 THR   C CA  1 
ATOM   10202 C C   . THR   C 1 350 ? -5.712  5.893   89.948  1.00 29.59  ?  350 THR   C C   1 
ATOM   10203 O O   . THR   C 1 350 ? -6.039  7.065   89.730  1.00 24.98  ?  350 THR   C O   1 
ATOM   10204 C CB  . THR   C 1 350 ? -7.589  4.274   89.672  1.00 24.73  ?  350 THR   C CB  1 
ATOM   10205 O OG1 . THR   C 1 350 ? -8.450  5.259   89.079  1.00 25.88  ?  350 THR   C OG1 1 
ATOM   10206 C CG2 . THR   C 1 350 ? -8.435  3.192   90.332  1.00 26.32  ?  350 THR   C CG2 1 
ATOM   10207 N N   . GLY   C 1 351 ? -4.544  5.376   89.567  1.00 23.30  ?  351 GLY   C N   1 
ATOM   10208 C CA  . GLY   C 1 351 ? -3.598  6.114   88.759  1.00 24.79  ?  351 GLY   C CA  1 
ATOM   10209 C C   . GLY   C 1 351 ? -4.015  6.168   87.301  1.00 26.77  ?  351 GLY   C C   1 
ATOM   10210 O O   . GLY   C 1 351 ? -5.135  5.824   86.921  1.00 29.41  ?  351 GLY   C O   1 
ATOM   10211 N N   . GLY   C 1 352 ? -3.082  6.608   86.466  1.00 22.54  ?  352 GLY   C N   1 
ATOM   10212 C CA  . GLY   C 1 352 ? -3.436  6.876   85.086  1.00 21.88  ?  352 GLY   C CA  1 
ATOM   10213 C C   . GLY   C 1 352 ? -3.387  5.711   84.125  1.00 25.34  ?  352 GLY   C C   1 
ATOM   10214 O O   . GLY   C 1 352 ? -3.837  5.860   82.980  1.00 26.34  ?  352 GLY   C O   1 
ATOM   10215 N N   . HIS   C 1 353 ? -2.862  4.550   84.536  1.00 20.72  ?  353 HIS   C N   1 
ATOM   10216 C CA  . HIS   C 1 353 ? -2.636  3.480   83.563  1.00 22.06  ?  353 HIS   C CA  1 
ATOM   10217 C C   . HIS   C 1 353 ? -2.926  2.082   84.081  1.00 23.93  ?  353 HIS   C C   1 
ATOM   10218 O O   . HIS   C 1 353 ? -2.883  1.143   83.283  1.00 19.64  ?  353 HIS   C O   1 
ATOM   10219 C CB  . HIS   C 1 353 ? -1.185  3.525   83.053  1.00 18.05  ?  353 HIS   C CB  1 
ATOM   10220 C CG  . HIS   C 1 353 ? -0.158  3.144   84.081  1.00 20.72  ?  353 HIS   C CG  1 
ATOM   10221 N ND1 . HIS   C 1 353 ? 0.013   3.837   85.260  1.00 19.51  ?  353 HIS   C ND1 1 
ATOM   10222 C CD2 . HIS   C 1 353 ? 0.766   2.151   84.093  1.00 20.91  ?  353 HIS   C CD2 1 
ATOM   10223 C CE1 . HIS   C 1 353 ? 0.988   3.281   85.959  1.00 22.72  ?  353 HIS   C CE1 1 
ATOM   10224 N NE2 . HIS   C 1 353 ? 1.467   2.260   85.270  1.00 19.75  ?  353 HIS   C NE2 1 
ATOM   10225 N N   . ALA   C 1 354 ? -3.229  1.906   85.364  1.00 23.97  ?  354 ALA   C N   1 
ATOM   10226 C CA  . ALA   C 1 354 ? -3.340  0.575   85.943  1.00 26.41  ?  354 ALA   C CA  1 
ATOM   10227 C C   . ALA   C 1 354 ? -4.101  0.628   87.262  1.00 24.64  ?  354 ALA   C C   1 
ATOM   10228 O O   . ALA   C 1 354 ? -4.107  1.647   87.957  1.00 29.43  ?  354 ALA   C O   1 
ATOM   10229 C CB  . ALA   C 1 354 ? -1.958  -0.049  86.172  1.00 24.05  ?  354 ALA   C CB  1 
ATOM   10230 N N   . VAL   C 1 355 ? -4.724  -0.498  87.602  1.00 22.17  ?  355 VAL   C N   1 
ATOM   10231 C CA  . VAL   C 1 355 ? -5.392  -0.704  88.881  1.00 25.03  ?  355 VAL   C CA  1 
ATOM   10232 C C   . VAL   C 1 355 ? -4.529  -1.654  89.697  1.00 27.25  ?  355 VAL   C C   1 
ATOM   10233 O O   . VAL   C 1 355 ? -4.084  -2.688  89.186  1.00 24.14  ?  355 VAL   C O   1 
ATOM   10234 C CB  . VAL   C 1 355 ? -6.813  -1.273  88.696  1.00 24.13  ?  355 VAL   C CB  1 
ATOM   10235 C CG1 . VAL   C 1 355 ? -7.430  -1.648  90.045  1.00 23.00  ?  355 VAL   C CG1 1 
ATOM   10236 C CG2 . VAL   C 1 355 ? -7.710  -0.287  87.934  1.00 22.34  ?  355 VAL   C CG2 1 
ATOM   10237 N N   . PHE   C 1 356 ? -4.282  -1.305  90.955  1.00 25.28  ?  356 PHE   C N   1 
ATOM   10238 C CA  . PHE   C 1 356 ? -3.440  -2.104  91.838  1.00 30.54  ?  356 PHE   C CA  1 
ATOM   10239 C C   . PHE   C 1 356 ? -4.309  -2.711  92.929  1.00 31.07  ?  356 PHE   C C   1 
ATOM   10240 O O   . PHE   C 1 356 ? -4.937  -1.982  93.701  1.00 32.12  ?  356 PHE   C O   1 
ATOM   10241 C CB  . PHE   C 1 356 ? -2.318  -1.257  92.438  1.00 35.40  ?  356 PHE   C CB  1 
ATOM   10242 C CG  . PHE   C 1 356 ? -1.307  -0.795  91.429  1.00 32.20  ?  356 PHE   C CG  1 
ATOM   10243 C CD1 . PHE   C 1 356 ? -1.602  0.238   90.555  1.00 31.37  ?  356 PHE   C CD1 1 
ATOM   10244 C CD2 . PHE   C 1 356 ? -0.061  -1.391  91.356  1.00 38.41  ?  356 PHE   C CD2 1 
ATOM   10245 C CE1 . PHE   C 1 356 ? -0.685  0.665   89.619  1.00 32.40  ?  356 PHE   C CE1 1 
ATOM   10246 C CE2 . PHE   C 1 356 ? 0.870   -0.965  90.425  1.00 34.50  ?  356 PHE   C CE2 1 
ATOM   10247 C CZ  . PHE   C 1 356 ? 0.561   0.068   89.555  1.00 35.83  ?  356 PHE   C CZ  1 
ATOM   10248 N N   . VAL   C 1 357 ? -4.344  -4.040  92.986  1.00 34.61  ?  357 VAL   C N   1 
ATOM   10249 C CA  . VAL   C 1 357 ? -5.164  -4.790  93.932  1.00 38.76  ?  357 VAL   C CA  1 
ATOM   10250 C C   . VAL   C 1 357 ? -4.282  -5.308  95.062  1.00 49.81  ?  357 VAL   C C   1 
ATOM   10251 O O   . VAL   C 1 357 ? -3.185  -5.826  94.815  1.00 51.52  ?  357 VAL   C O   1 
ATOM   10252 C CB  . VAL   C 1 357 ? -5.871  -5.962  93.223  1.00 36.83  ?  357 VAL   C CB  1 
ATOM   10253 C CG1 . VAL   C 1 357 ? -6.739  -6.730  94.200  1.00 35.86  ?  357 VAL   C CG1 1 
ATOM   10254 C CG2 . VAL   C 1 357 ? -6.669  -5.471  92.024  1.00 33.70  ?  357 VAL   C CG2 1 
ATOM   10255 N N   . ASP   C 1 358 ? -4.763  -5.190  96.302  1.00 46.47  ?  358 ASP   C N   1 
ATOM   10256 C CA  A ASP   C 1 358 ? -4.064  -5.739  97.461  0.61 54.78  ?  358 ASP   C CA  1 
ATOM   10257 C CA  B ASP   C 1 358 ? -4.070  -5.736  97.467  0.39 54.78  ?  358 ASP   C CA  1 
ATOM   10258 C C   . ASP   C 1 358 ? -4.544  -7.169  97.692  1.00 56.86  ?  358 ASP   C C   1 
ATOM   10259 O O   . ASP   C 1 358 ? -5.703  -7.397  98.059  1.00 56.62  ?  358 ASP   C O   1 
ATOM   10260 C CB  A ASP   C 1 358 ? -4.289  -4.877  98.699  0.61 54.38  ?  358 ASP   C CB  1 
ATOM   10261 C CB  B ASP   C 1 358 ? -4.326  -4.878  98.704  0.39 54.42  ?  358 ASP   C CB  1 
ATOM   10262 C CG  A ASP   C 1 358 ? -3.584  -5.430  99.922  0.61 60.19  ?  358 ASP   C CG  1 
ATOM   10263 C CG  B ASP   C 1 358 ? -3.734  -5.482  99.966  0.39 60.11  ?  358 ASP   C CG  1 
ATOM   10264 O OD1 A ASP   C 1 358 ? -2.365  -5.695  99.830  0.61 62.07  ?  358 ASP   C OD1 1 
ATOM   10265 O OD1 B ASP   C 1 358 ? -2.776  -6.277  99.852  0.39 61.79  ?  358 ASP   C OD1 1 
ATOM   10266 O OD2 A ASP   C 1 358 ? -4.242  -5.599  100.974 0.61 61.11  ?  358 ASP   C OD2 1 
ATOM   10267 O OD2 B ASP   C 1 358 ? -4.231  -5.172  101.072 0.39 60.74  ?  358 ASP   C OD2 1 
ATOM   10268 N N   . CYS   C 1 359 ? -3.648  -8.135  97.489  1.00 55.93  ?  359 CYS   C N   1 
ATOM   10269 C CA  . CYS   C 1 359 ? -4.009  -9.545  97.590  1.00 58.37  ?  359 CYS   C CA  1 
ATOM   10270 C C   . CYS   C 1 359 ? -3.845  -10.126 98.991  1.00 65.85  ?  359 CYS   C C   1 
ATOM   10271 O O   . CYS   C 1 359 ? -4.368  -11.216 99.247  1.00 61.05  ?  359 CYS   C O   1 
ATOM   10272 C CB  . CYS   C 1 359 ? -3.182  -10.380 96.604  1.00 58.47  ?  359 CYS   C CB  1 
ATOM   10273 S SG  . CYS   C 1 359 ? -3.542  -10.119 94.846  1.00 49.20  ?  359 CYS   C SG  1 
ATOM   10274 N N   . LYS   C 1 360 ? -3.134  -9.446  99.896  1.00 77.66  ?  360 LYS   C N   1 
ATOM   10275 C CA  . LYS   C 1 360 ? -2.987  -9.960  101.257 1.00 78.22  ?  360 LYS   C CA  1 
ATOM   10276 C C   . LYS   C 1 360 ? -4.328  -10.150 101.948 1.00 78.04  ?  360 LYS   C C   1 
ATOM   10277 O O   . LYS   C 1 360 ? -4.425  -10.954 102.882 1.00 79.87  ?  360 LYS   C O   1 
ATOM   10278 C CB  . LYS   C 1 360 ? -2.114  -9.028  102.101 1.00 79.29  ?  360 LYS   C CB  1 
ATOM   10279 C CG  . LYS   C 1 360 ? -0.621  -9.294  102.008 1.00 80.10  ?  360 LYS   C CG  1 
ATOM   10280 C CD  . LYS   C 1 360 ? 0.144   -8.419  102.989 1.00 82.15  ?  360 LYS   C CD  1 
ATOM   10281 C CE  . LYS   C 1 360 ? 1.647   -8.597  102.848 1.00 83.02  ?  360 LYS   C CE  1 
ATOM   10282 N NZ  . LYS   C 1 360 ? 2.400   -7.641  103.707 1.00 85.59  ?  360 LYS   C NZ  1 
ATOM   10283 N N   . LYS   C 1 361 ? -5.359  -9.430  101.513 1.00 64.12  ?  361 LYS   C N   1 
ATOM   10284 C CA  . LYS   C 1 361 ? -6.671  -9.536  102.129 1.00 66.82  ?  361 LYS   C CA  1 
ATOM   10285 C C   . LYS   C 1 361 ? -7.531  -10.613 101.484 1.00 64.24  ?  361 LYS   C C   1 
ATOM   10286 O O   . LYS   C 1 361 ? -8.398  -11.191 102.157 1.00 55.02  ?  361 LYS   C O   1 
ATOM   10287 C CB  . LYS   C 1 361 ? -7.376  -8.180  102.065 1.00 64.29  ?  361 LYS   C CB  1 
ATOM   10288 C CG  . LYS   C 1 361 ? -6.551  -7.053  102.670 1.00 59.96  ?  361 LYS   C CG  1 
ATOM   10289 C CD  . LYS   C 1 361 ? -7.215  -5.707  102.472 1.00 62.16  ?  361 LYS   C CD  1 
ATOM   10290 C CE  . LYS   C 1 361 ? -8.652  -5.719  102.969 1.00 64.92  ?  361 LYS   C CE  1 
ATOM   10291 N NZ  . LYS   C 1 361 ? -9.303  -4.388  102.809 1.00 65.02  ?  361 LYS   C NZ  1 
ATOM   10292 N N   . LEU   C 1 362 ? -7.296  -10.907 100.203 1.00 57.71  ?  362 LEU   C N   1 
ATOM   10293 C CA  . LEU   C 1 362 ? -8.058  -11.940 99.506  1.00 64.98  ?  362 LEU   C CA  1 
ATOM   10294 C C   . LEU   C 1 362 ? -7.586  -13.345 99.862  1.00 67.22  ?  362 LEU   C C   1 
ATOM   10295 O O   . LEU   C 1 362 ? -8.399  -14.274 99.921  1.00 65.56  ?  362 LEU   C O   1 
ATOM   10296 C CB  . LEU   C 1 362 ? -7.964  -11.730 97.992  1.00 61.74  ?  362 LEU   C CB  1 
ATOM   10297 C CG  . LEU   C 1 362 ? -8.484  -10.403 97.441  1.00 53.49  ?  362 LEU   C CG  1 
ATOM   10298 C CD1 . LEU   C 1 362 ? -8.249  -10.303 95.935  1.00 47.53  ?  362 LEU   C CD1 1 
ATOM   10299 C CD2 . LEU   C 1 362 ? -9.955  -10.246 97.766  1.00 44.71  ?  362 LEU   C CD2 1 
ATOM   10300 N N   . VAL   C 1 363 ? -6.292  -13.522 100.105 1.00 70.42  ?  363 VAL   C N   1 
ATOM   10301 C CA  . VAL   C 1 363 ? -5.742  -14.831 100.450 1.00 65.24  ?  363 VAL   C CA  1 
ATOM   10302 C C   . VAL   C 1 363 ? -4.955  -14.723 101.753 1.00 63.29  ?  363 VAL   C C   1 
ATOM   10303 O O   . VAL   C 1 363 ? -3.725  -14.886 101.752 1.00 64.53  ?  363 VAL   C O   1 
ATOM   10304 C CB  . VAL   C 1 363 ? -4.877  -15.379 99.304  1.00 62.86  ?  363 VAL   C CB  1 
ATOM   10305 C CG1 . VAL   C 1 363 ? -5.762  -15.905 98.200  1.00 68.73  ?  363 VAL   C CG1 1 
ATOM   10306 C CG2 . VAL   C 1 363 ? -3.989  -14.292 98.746  1.00 60.48  ?  363 VAL   C CG2 1 
ATOM   10307 N N   . PRO   C 1 364 ? -5.615  -14.462 102.887 1.00 64.29  ?  364 PRO   C N   1 
ATOM   10308 C CA  . PRO   C 1 364 ? -4.870  -14.351 104.151 1.00 66.86  ?  364 PRO   C CA  1 
ATOM   10309 C C   . PRO   C 1 364 ? -4.171  -15.637 104.547 1.00 70.10  ?  364 PRO   C C   1 
ATOM   10310 O O   . PRO   C 1 364 ? -3.135  -15.588 105.223 1.00 68.64  ?  364 PRO   C O   1 
ATOM   10311 C CB  . PRO   C 1 364 ? -5.956  -13.964 105.167 1.00 55.24  ?  364 PRO   C CB  1 
ATOM   10312 C CG  . PRO   C 1 364 ? -7.111  -13.468 104.342 1.00 63.86  ?  364 PRO   C CG  1 
ATOM   10313 C CD  . PRO   C 1 364 ? -7.060  -14.265 103.082 1.00 58.81  ?  364 PRO   C CD  1 
ATOM   10314 N N   . GLN   C 1 365 ? -4.704  -16.790 104.133 1.00 70.87  ?  365 GLN   C N   1 
ATOM   10315 C CA  . GLN   C 1 365 ? -4.117  -18.092 104.433 1.00 68.97  ?  365 GLN   C CA  1 
ATOM   10316 C C   . GLN   C 1 365 ? -2.787  -18.328 103.724 1.00 66.88  ?  365 GLN   C C   1 
ATOM   10317 O O   . GLN   C 1 365 ? -2.167  -19.375 103.948 1.00 75.52  ?  365 GLN   C O   1 
ATOM   10318 C CB  . GLN   C 1 365 ? -5.104  -19.210 104.068 1.00 66.97  ?  365 GLN   C CB  1 
ATOM   10319 C CG  . GLN   C 1 365 ? -5.129  -19.602 102.582 1.00 69.42  ?  365 GLN   C CG  1 
ATOM   10320 C CD  . GLN   C 1 365 ? -5.870  -18.606 101.705 1.00 64.77  ?  365 GLN   C CD  1 
ATOM   10321 O OE1 . GLN   C 1 365 ? -6.573  -17.725 102.199 1.00 61.52  ?  365 GLN   C OE1 1 
ATOM   10322 N NE2 . GLN   C 1 365 ? -5.712  -18.744 100.394 1.00 65.69  ?  365 GLN   C NE2 1 
ATOM   10323 N N   . ILE   C 1 366 ? -2.336  -17.405 102.886 1.00 72.40  ?  366 ILE   C N   1 
ATOM   10324 C CA  . ILE   C 1 366 ? -1.075  -17.518 102.159 1.00 72.46  ?  366 ILE   C CA  1 
ATOM   10325 C C   . ILE   C 1 366 ? -0.133  -16.440 102.688 1.00 75.90  ?  366 ILE   C C   1 
ATOM   10326 O O   . ILE   C 1 366 ? -0.422  -15.245 102.533 1.00 77.51  ?  366 ILE   C O   1 
ATOM   10327 C CB  . ILE   C 1 366 ? -1.278  -17.379 100.640 1.00 65.03  ?  366 ILE   C CB  1 
ATOM   10328 C CG1 . ILE   C 1 366 ? -2.433  -18.265 100.172 1.00 61.68  ?  366 ILE   C CG1 1 
ATOM   10329 C CG2 . ILE   C 1 366 ? -0.005  -17.746 99.888  1.00 68.73  ?  366 ILE   C CG2 1 
ATOM   10330 C CD1 . ILE   C 1 366 ? -2.625  -18.279 98.674  1.00 62.22  ?  366 ILE   C CD1 1 
ATOM   10331 N N   . PRO   C 1 367 ? 0.979   -16.800 103.322 1.00 81.51  ?  367 PRO   C N   1 
ATOM   10332 C CA  . PRO   C 1 367 ? 1.953   -15.786 103.743 1.00 83.47  ?  367 PRO   C CA  1 
ATOM   10333 C C   . PRO   C 1 367 ? 2.628   -15.149 102.536 1.00 79.47  ?  367 PRO   C C   1 
ATOM   10334 O O   . PRO   C 1 367 ? 2.514   -15.616 101.402 1.00 75.80  ?  367 PRO   C O   1 
ATOM   10335 C CB  . PRO   C 1 367 ? 2.948   -16.578 104.596 1.00 82.63  ?  367 PRO   C CB  1 
ATOM   10336 C CG  . PRO   C 1 367 ? 2.835   -17.987 104.091 1.00 81.16  ?  367 PRO   C CG  1 
ATOM   10337 C CD  . PRO   C 1 367 ? 1.395   -18.164 103.695 1.00 82.14  ?  367 PRO   C CD  1 
ATOM   10338 N N   . GLY   C 1 368 ? 3.351   -14.057 102.799 1.00 73.31  ?  368 GLY   C N   1 
ATOM   10339 C CA  . GLY   C 1 368 ? 3.988   -13.326 101.711 1.00 69.09  ?  368 GLY   C CA  1 
ATOM   10340 C C   . GLY   C 1 368 ? 5.091   -14.110 101.019 1.00 69.47  ?  368 GLY   C C   1 
ATOM   10341 O O   . GLY   C 1 368 ? 5.227   -14.057 99.794  1.00 65.94  ?  368 GLY   C O   1 
ATOM   10342 N N   . ASP   C 1 369 ? 5.891   -14.847 101.788 1.00 72.28  ?  369 ASP   C N   1 
ATOM   10343 C CA  . ASP   C 1 369 ? 6.996   -15.599 101.206 1.00 69.18  ?  369 ASP   C CA  1 
ATOM   10344 C C   . ASP   C 1 369 ? 6.531   -16.740 100.310 1.00 68.27  ?  369 ASP   C C   1 
ATOM   10345 O O   . ASP   C 1 369 ? 7.349   -17.287 99.564  1.00 70.45  ?  369 ASP   C O   1 
ATOM   10346 C CB  . ASP   C 1 369 ? 7.887   -16.146 102.317 1.00 70.33  ?  369 ASP   C CB  1 
ATOM   10347 C CG  . ASP   C 1 369 ? 7.157   -17.115 103.216 1.00 73.33  ?  369 ASP   C CG  1 
ATOM   10348 O OD1 . ASP   C 1 369 ? 5.909   -17.102 103.207 1.00 75.87  ?  369 ASP   C OD1 1 
ATOM   10349 O OD2 . ASP   C 1 369 ? 7.828   -17.887 103.932 1.00 83.25  ?  369 ASP   C OD2 1 
ATOM   10350 N N   . GLN   C 1 370 ? 5.255   -17.120 100.374 1.00 74.36  ?  370 GLN   C N   1 
ATOM   10351 C CA  . GLN   C 1 370 ? 4.690   -18.144 99.504  1.00 72.67  ?  370 GLN   C CA  1 
ATOM   10352 C C   . GLN   C 1 370 ? 3.806   -17.551 98.412  1.00 68.78  ?  370 GLN   C C   1 
ATOM   10353 O O   . GLN   C 1 370 ? 2.969   -18.261 97.844  1.00 61.17  ?  370 GLN   C O   1 
ATOM   10354 C CB  . GLN   C 1 370 ? 3.914   -19.174 100.327 1.00 73.91  ?  370 GLN   C CB  1 
ATOM   10355 C CG  . GLN   C 1 370 ? 4.810   -20.053 101.186 1.00 77.61  ?  370 GLN   C CG  1 
ATOM   10356 C CD  . GLN   C 1 370 ? 6.005   -20.593 100.410 1.00 79.76  ?  370 GLN   C CD  1 
ATOM   10357 O OE1 . GLN   C 1 370 ? 5.849   -21.307 99.419  1.00 76.53  ?  370 GLN   C OE1 1 
ATOM   10358 N NE2 . GLN   C 1 370 ? 7.206   -20.245 100.858 1.00 81.06  ?  370 GLN   C NE2 1 
ATOM   10359 N N   . PHE   C 1 371 ? 3.971   -16.260 98.123  1.00 66.01  ?  371 PHE   C N   1 
ATOM   10360 C CA  . PHE   C 1 371 ? 3.423   -15.599 96.945  1.00 66.87  ?  371 PHE   C CA  1 
ATOM   10361 C C   . PHE   C 1 371 ? 1.896   -15.608 96.949  1.00 62.57  ?  371 PHE   C C   1 
ATOM   10362 O O   . PHE   C 1 371 ? 1.274   -16.308 96.138  1.00 57.84  ?  371 PHE   C O   1 
ATOM   10363 C CB  . PHE   C 1 371 ? 3.979   -16.265 95.679  1.00 64.63  ?  371 PHE   C CB  1 
ATOM   10364 C CG  . PHE   C 1 371 ? 5.423   -16.678 95.804  1.00 62.36  ?  371 PHE   C CG  1 
ATOM   10365 C CD1 . PHE   C 1 371 ? 6.387   -15.766 96.211  1.00 60.75  ?  371 PHE   C CD1 1 
ATOM   10366 C CD2 . PHE   C 1 371 ? 5.810   -17.984 95.556  1.00 68.36  ?  371 PHE   C CD2 1 
ATOM   10367 C CE1 . PHE   C 1 371 ? 7.713   -16.146 96.346  1.00 61.01  ?  371 PHE   C CE1 1 
ATOM   10368 C CE2 . PHE   C 1 371 ? 7.138   -18.371 95.692  1.00 64.73  ?  371 PHE   C CE2 1 
ATOM   10369 C CZ  . PHE   C 1 371 ? 8.086   -17.449 96.089  1.00 57.91  ?  371 PHE   C CZ  1 
ATOM   10370 N N   . PRO   C 1 372 ? 1.254   -14.840 97.835  1.00 62.96  ?  372 PRO   C N   1 
ATOM   10371 C CA  . PRO   C 1 372 ? -0.215  -14.775 97.789  1.00 60.94  ?  372 PRO   C CA  1 
ATOM   10372 C C   . PRO   C 1 372 ? -0.735  -14.035 96.569  1.00 53.96  ?  372 PRO   C C   1 
ATOM   10373 O O   . PRO   C 1 372 ? -1.700  -14.493 95.943  1.00 50.48  ?  372 PRO   C O   1 
ATOM   10374 C CB  . PRO   C 1 372 ? -0.570  -14.056 99.098  1.00 59.30  ?  372 PRO   C CB  1 
ATOM   10375 C CG  . PRO   C 1 372 ? 0.604   -13.211 99.384  1.00 63.61  ?  372 PRO   C CG  1 
ATOM   10376 C CD  . PRO   C 1 372 ? 1.811   -13.966 98.882  1.00 61.59  ?  372 PRO   C CD  1 
ATOM   10377 N N   . ALA   C 1 373 ? -0.123  -12.900 96.214  1.00 47.91  ?  373 ALA   C N   1 
ATOM   10378 C CA  . ALA   C 1 373 ? -0.577  -12.152 95.047  1.00 52.43  ?  373 ALA   C CA  1 
ATOM   10379 C C   . ALA   C 1 373 ? -0.451  -12.983 93.778  1.00 53.11  ?  373 ALA   C C   1 
ATOM   10380 O O   . ALA   C 1 373 ? -1.364  -13.000 92.944  1.00 54.88  ?  373 ALA   C O   1 
ATOM   10381 C CB  . ALA   C 1 373 ? 0.206   -10.845 94.917  1.00 53.30  ?  373 ALA   C CB  1 
ATOM   10382 N N   . GLN   C 1 374 ? 0.674   -13.686 93.615  1.00 51.87  ?  374 GLN   C N   1 
ATOM   10383 C CA  . GLN   C 1 374 ? 0.847   -14.521 92.432  1.00 45.12  ?  374 GLN   C CA  1 
ATOM   10384 C C   . GLN   C 1 374 ? -0.154  -15.668 92.403  1.00 50.18  ?  374 GLN   C C   1 
ATOM   10385 O O   . GLN   C 1 374 ? -0.576  -16.092 91.321  1.00 50.78  ?  374 GLN   C O   1 
ATOM   10386 C CB  . GLN   C 1 374 ? 2.272   -15.067 92.371  1.00 52.98  ?  374 GLN   C CB  1 
ATOM   10387 C CG  . GLN   C 1 374 ? 2.573   -15.823 91.090  1.00 45.30  ?  374 GLN   C CG  1 
ATOM   10388 C CD  . GLN   C 1 374 ? 2.349   -14.969 89.864  1.00 49.97  ?  374 GLN   C CD  1 
ATOM   10389 O OE1 . GLN   C 1 374 ? 3.103   -14.028 89.599  1.00 46.52  ?  374 GLN   C OE1 1 
ATOM   10390 N NE2 . GLN   C 1 374 ? 1.300   -15.280 89.114  1.00 42.52  ?  374 GLN   C NE2 1 
ATOM   10391 N N   . ALA   C 1 375 ? -0.541  -16.185 93.574  1.00 50.08  ?  375 ALA   C N   1 
ATOM   10392 C CA  . ALA   C 1 375 ? -1.552  -17.234 93.613  1.00 45.94  ?  375 ALA   C CA  1 
ATOM   10393 C C   . ALA   C 1 375 ? -2.916  -16.702 93.199  1.00 51.24  ?  375 ALA   C C   1 
ATOM   10394 O O   . ALA   C 1 375 ? -3.730  -17.451 92.645  1.00 57.59  ?  375 ALA   C O   1 
ATOM   10395 C CB  . ALA   C 1 375 ? -1.620  -17.853 95.007  1.00 54.42  ?  375 ALA   C CB  1 
ATOM   10396 N N   . VAL   C 1 376 ? -3.185  -15.417 93.456  1.00 47.54  ?  376 VAL   C N   1 
ATOM   10397 C CA  . VAL   C 1 376 ? -4.401  -14.797 92.938  1.00 46.68  ?  376 VAL   C CA  1 
ATOM   10398 C C   . VAL   C 1 376 ? -4.311  -14.646 91.423  1.00 46.10  ?  376 VAL   C C   1 
ATOM   10399 O O   . VAL   C 1 376 ? -5.274  -14.926 90.696  1.00 47.28  ?  376 VAL   C O   1 
ATOM   10400 C CB  . VAL   C 1 376 ? -4.645  -13.446 93.636  1.00 47.05  ?  376 VAL   C CB  1 
ATOM   10401 C CG1 . VAL   C 1 376 ? -5.740  -12.668 92.940  1.00 48.14  ?  376 VAL   C CG1 1 
ATOM   10402 C CG2 . VAL   C 1 376 ? -5.008  -13.663 95.104  1.00 51.66  ?  376 VAL   C CG2 1 
ATOM   10403 N N   . ILE   C 1 377 ? -3.144  -14.232 90.924  1.00 45.89  ?  377 ILE   C N   1 
ATOM   10404 C CA  . ILE   C 1 377 ? -2.966  -14.014 89.488  1.00 44.16  ?  377 ILE   C CA  1 
ATOM   10405 C C   . ILE   C 1 377 ? -3.137  -15.318 88.719  1.00 44.64  ?  377 ILE   C C   1 
ATOM   10406 O O   . ILE   C 1 377 ? -3.770  -15.353 87.656  1.00 43.96  ?  377 ILE   C O   1 
ATOM   10407 C CB  . ILE   C 1 377 ? -1.594  -13.368 89.222  1.00 42.38  ?  377 ILE   C CB  1 
ATOM   10408 C CG1 . ILE   C 1 377 ? -1.553  -11.959 89.821  1.00 43.67  ?  377 ILE   C CG1 1 
ATOM   10409 C CG2 . ILE   C 1 377 ? -1.294  -13.324 87.735  1.00 40.17  ?  377 ILE   C CG2 1 
ATOM   10410 C CD1 . ILE   C 1 377 ? -0.271  -11.215 89.556  1.00 40.73  ?  377 ILE   C CD1 1 
ATOM   10411 N N   . ASN   C 1 378 ? -2.589  -16.415 89.248  1.00 41.25  ?  378 ASN   C N   1 
ATOM   10412 C CA  . ASN   C 1 378 ? -2.740  -17.704 88.582  1.00 41.55  ?  378 ASN   C CA  1 
ATOM   10413 C C   . ASN   C 1 378 ? -4.184  -18.191 88.628  1.00 49.65  ?  378 ASN   C C   1 
ATOM   10414 O O   . ASN   C 1 378 ? -4.683  -18.760 87.647  1.00 46.61  ?  378 ASN   C O   1 
ATOM   10415 C CB  . ASN   C 1 378 ? -1.800  -18.723 89.213  1.00 46.79  ?  378 ASN   C CB  1 
ATOM   10416 C CG  . ASN   C 1 378 ? -0.346  -18.396 88.953  1.00 55.78  ?  378 ASN   C CG  1 
ATOM   10417 O OD1 . ASN   C 1 378 ? -0.015  -17.278 88.548  1.00 55.81  ?  378 ASN   C OD1 1 
ATOM   10418 N ND2 . ASN   C 1 378 ? 0.533   -19.370 89.173  1.00 57.78  ?  378 ASN   C ND2 1 
ATOM   10419 N N   . ALA   C 1 379 ? -4.871  -17.981 89.759  1.00 49.72  ?  379 ALA   C N   1 
ATOM   10420 C CA  . ALA   C 1 379 ? -6.291  -18.311 89.834  1.00 49.61  ?  379 ALA   C CA  1 
ATOM   10421 C C   . ALA   C 1 379 ? -7.100  -17.435 88.887  1.00 47.48  ?  379 ALA   C C   1 
ATOM   10422 O O   . ALA   C 1 379 ? -7.942  -17.934 88.127  1.00 44.54  ?  379 ALA   C O   1 
ATOM   10423 C CB  . ALA   C 1 379 ? -6.793  -18.167 91.270  1.00 41.68  ?  379 ALA   C CB  1 
ATOM   10424 N N   . LEU   C 1 380 ? -6.851  -16.121 88.917  1.00 44.33  ?  380 LEU   C N   1 
ATOM   10425 C CA  . LEU   C 1 380 ? -7.461  -15.223 87.940  1.00 47.59  ?  380 LEU   C CA  1 
ATOM   10426 C C   . LEU   C 1 380 ? -7.219  -15.712 86.519  1.00 44.25  ?  380 LEU   C C   1 
ATOM   10427 O O   . LEU   C 1 380 ? -8.130  -15.687 85.681  1.00 38.76  ?  380 LEU   C O   1 
ATOM   10428 C CB  . LEU   C 1 380 ? -6.915  -13.803 88.112  1.00 45.26  ?  380 LEU   C CB  1 
ATOM   10429 C CG  . LEU   C 1 380 ? -7.413  -12.781 87.086  1.00 41.27  ?  380 LEU   C CG  1 
ATOM   10430 C CD1 . LEU   C 1 380 ? -8.916  -12.630 87.210  1.00 42.52  ?  380 LEU   C CD1 1 
ATOM   10431 C CD2 . LEU   C 1 380 ? -6.718  -11.434 87.245  1.00 37.50  ?  380 LEU   C CD2 1 
ATOM   10432 N N   . TYR   C 1 381 ? -5.998  -16.181 86.237  1.00 43.41  ?  381 TYR   C N   1 
ATOM   10433 C CA  . TYR   C 1 381 ? -5.691  -16.675 84.901  1.00 39.41  ?  381 TYR   C CA  1 
ATOM   10434 C C   . TYR   C 1 381 ? -6.495  -17.929 84.570  1.00 46.98  ?  381 TYR   C C   1 
ATOM   10435 O O   . TYR   C 1 381 ? -7.095  -18.026 83.490  1.00 44.36  ?  381 TYR   C O   1 
ATOM   10436 C CB  . TYR   C 1 381 ? -4.200  -16.960 84.759  1.00 40.40  ?  381 TYR   C CB  1 
ATOM   10437 C CG  . TYR   C 1 381 ? -3.923  -17.647 83.444  1.00 43.73  ?  381 TYR   C CG  1 
ATOM   10438 C CD1 . TYR   C 1 381 ? -3.903  -16.923 82.257  1.00 39.77  ?  381 TYR   C CD1 1 
ATOM   10439 C CD2 . TYR   C 1 381 ? -3.736  -19.023 83.379  1.00 43.22  ?  381 TYR   C CD2 1 
ATOM   10440 C CE1 . TYR   C 1 381 ? -3.674  -17.546 81.042  1.00 39.26  ?  381 TYR   C CE1 1 
ATOM   10441 C CE2 . TYR   C 1 381 ? -3.513  -19.658 82.168  1.00 44.55  ?  381 TYR   C CE2 1 
ATOM   10442 C CZ  . TYR   C 1 381 ? -3.481  -18.912 81.005  1.00 42.87  ?  381 TYR   C CZ  1 
ATOM   10443 O OH  . TYR   C 1 381 ? -3.258  -19.535 79.802  1.00 45.16  ?  381 TYR   C OH  1 
ATOM   10444 N N   . LEU   C 1 382 ? -6.501  -18.914 85.477  1.00 48.04  ?  382 LEU   C N   1 
ATOM   10445 C CA  . LEU   C 1 382 ? -7.227  -20.154 85.213  1.00 46.88  ?  382 LEU   C CA  1 
ATOM   10446 C C   . LEU   C 1 382 ? -8.719  -19.910 85.037  1.00 48.34  ?  382 LEU   C C   1 
ATOM   10447 O O   . LEU   C 1 382 ? -9.371  -20.588 84.234  1.00 46.03  ?  382 LEU   C O   1 
ATOM   10448 C CB  . LEU   C 1 382 ? -6.993  -21.156 86.341  1.00 52.63  ?  382 LEU   C CB  1 
ATOM   10449 C CG  . LEU   C 1 382 ? -5.612  -21.795 86.491  1.00 48.64  ?  382 LEU   C CG  1 
ATOM   10450 C CD1 . LEU   C 1 382 ? -5.667  -22.893 87.538  1.00 48.66  ?  382 LEU   C CD1 1 
ATOM   10451 C CD2 . LEU   C 1 382 ? -5.139  -22.352 85.167  1.00 50.90  ?  382 LEU   C CD2 1 
ATOM   10452 N N   . GLU   C 1 383 ? -9.277  -18.948 85.769  1.00 47.58  ?  383 GLU   C N   1 
ATOM   10453 C CA  . GLU   C 1 383 ? -10.705 -18.689 85.684  1.00 50.04  ?  383 GLU   C CA  1 
ATOM   10454 C C   . GLU   C 1 383 ? -11.072 -17.793 84.511  1.00 53.62  ?  383 GLU   C C   1 
ATOM   10455 O O   . GLU   C 1 383 ? -12.240 -17.784 84.103  1.00 57.52  ?  383 GLU   C O   1 
ATOM   10456 C CB  . GLU   C 1 383 ? -11.201 -18.056 86.990  1.00 55.13  ?  383 GLU   C CB  1 
ATOM   10457 C CG  . GLU   C 1 383 ? -12.702 -18.188 87.228  1.00 57.63  ?  383 GLU   C CG  1 
ATOM   10458 C CD  . GLU   C 1 383 ? -13.130 -19.628 87.461  1.00 63.21  ?  383 GLU   C CD  1 
ATOM   10459 O OE1 . GLU   C 1 383 ? -12.267 -20.452 87.831  1.00 65.96  ?  383 GLU   C OE1 1 
ATOM   10460 O OE2 . GLU   C 1 383 ? -14.325 -19.937 87.276  1.00 68.28  ?  383 GLU   C OE2 1 
ATOM   10461 N N   . SER   C 1 384 ? -10.113 -17.053 83.950  1.00 44.10  ?  384 SER   C N   1 
ATOM   10462 C CA  . SER   C 1 384 ? -10.445 -16.012 82.977  1.00 48.58  ?  384 SER   C CA  1 
ATOM   10463 C C   . SER   C 1 384 ? -9.529  -15.937 81.768  1.00 41.82  ?  384 SER   C C   1 
ATOM   10464 O O   . SER   C 1 384 ? -9.954  -15.391 80.744  1.00 42.76  ?  384 SER   C O   1 
ATOM   10465 C CB  . SER   C 1 384 ? -10.451 -14.638 83.654  1.00 41.81  ?  384 SER   C CB  1 
ATOM   10466 O OG  . SER   C 1 384 ? -9.172  -14.332 84.186  1.00 39.21  ?  384 SER   C OG  1 
ATOM   10467 N N   . GLY   C 1 385 ? -8.300  -16.439 81.831  1.00 42.02  ?  385 GLY   C N   1 
ATOM   10468 C CA  . GLY   C 1 385 ? -7.345  -16.196 80.773  1.00 37.68  ?  385 GLY   C CA  1 
ATOM   10469 C C   . GLY   C 1 385 ? -6.698  -14.829 80.810  1.00 38.17  ?  385 GLY   C C   1 
ATOM   10470 O O   . GLY   C 1 385 ? -5.848  -14.542 79.958  1.00 36.23  ?  385 GLY   C O   1 
ATOM   10471 N N   . VAL   C 1 386 ? -7.080  -13.980 81.761  1.00 37.30  ?  386 VAL   C N   1 
ATOM   10472 C CA  . VAL   C 1 386 ? -6.491  -12.657 81.929  1.00 32.42  ?  386 VAL   C CA  1 
ATOM   10473 C C   . VAL   C 1 386 ? -5.130  -12.807 82.593  1.00 34.64  ?  386 VAL   C C   1 
ATOM   10474 O O   . VAL   C 1 386 ? -4.989  -13.534 83.585  1.00 36.75  ?  386 VAL   C O   1 
ATOM   10475 C CB  . VAL   C 1 386 ? -7.415  -11.758 82.770  1.00 34.81  ?  386 VAL   C CB  1 
ATOM   10476 C CG1 . VAL   C 1 386 ? -6.731  -10.447 83.113  1.00 32.58  ?  386 VAL   C CG1 1 
ATOM   10477 C CG2 . VAL   C 1 386 ? -8.734  -11.510 82.044  1.00 33.94  ?  386 VAL   C CG2 1 
ATOM   10478 N N   . ARG   C 1 387 ? -4.130  -12.108 82.066  1.00 33.12  ?  387 ARG   C N   1 
ATOM   10479 C CA  . ARG   C 1 387 ? -2.777  -12.139 82.608  1.00 34.04  ?  387 ARG   C CA  1 
ATOM   10480 C C   . ARG   C 1 387 ? -2.475  -10.813 83.291  1.00 34.26  ?  387 ARG   C C   1 
ATOM   10481 O O   . ARG   C 1 387 ? -2.502  -9.759  82.648  1.00 33.42  ?  387 ARG   C O   1 
ATOM   10482 C CB  . ARG   C 1 387 ? -1.751  -12.423 81.513  1.00 33.71  ?  387 ARG   C CB  1 
ATOM   10483 C CG  . ARG   C 1 387 ? -0.312  -12.224 81.948  1.00 35.96  ?  387 ARG   C CG  1 
ATOM   10484 C CD  . ARG   C 1 387 ? 0.676   -13.000 81.060  1.00 36.72  ?  387 ARG   C CD  1 
ATOM   10485 N NE  . ARG   C 1 387 ? 0.857   -12.430 79.726  1.00 33.51  ?  387 ARG   C NE  1 
ATOM   10486 C CZ  . ARG   C 1 387 ? 1.708   -12.905 78.826  1.00 33.44  ?  387 ARG   C CZ  1 
ATOM   10487 N NH1 . ARG   C 1 387 ? 2.475   -13.954 79.085  1.00 34.42  ?  387 ARG   C NH1 1 
ATOM   10488 N NH2 . ARG   C 1 387 ? 1.792   -12.319 77.634  1.00 32.40  ?  387 ARG   C NH2 1 
ATOM   10489 N N   . ALA   C 1 388 ? -2.185  -10.871 84.586  1.00 35.43  ?  388 ALA   C N   1 
ATOM   10490 C CA  . ALA   C 1 388 ? -1.751  -9.721  85.364  1.00 35.91  ?  388 ALA   C CA  1 
ATOM   10491 C C   . ALA   C 1 388 ? -0.274  -9.874  85.714  1.00 37.09  ?  388 ALA   C C   1 
ATOM   10492 O O   . ALA   C 1 388 ? 0.365   -10.884 85.403  1.00 37.23  ?  388 ALA   C O   1 
ATOM   10493 C CB  . ALA   C 1 388 ? -2.603  -9.569  86.624  1.00 36.60  ?  388 ALA   C CB  1 
ATOM   10494 N N   . VAL   C 1 389 ? 0.276   -8.855  86.369  1.00 37.41  ?  389 VAL   C N   1 
ATOM   10495 C CA  . VAL   C 1 389 ? 1.676   -8.854  86.774  1.00 38.44  ?  389 VAL   C CA  1 
ATOM   10496 C C   . VAL   C 1 389 ? 1.736   -8.647  88.283  1.00 39.79  ?  389 VAL   C C   1 
ATOM   10497 O O   . VAL   C 1 389 ? 0.963   -7.864  88.846  1.00 39.72  ?  389 VAL   C O   1 
ATOM   10498 C CB  . VAL   C 1 389 ? 2.490   -7.787  86.004  1.00 37.85  ?  389 VAL   C CB  1 
ATOM   10499 C CG1 . VAL   C 1 389 ? 1.986   -6.386  86.285  1.00 37.47  ?  389 VAL   C CG1 1 
ATOM   10500 C CG2 . VAL   C 1 389 ? 3.968   -7.905  86.314  1.00 38.93  ?  389 VAL   C CG2 1 
ATOM   10501 N N   . GLU   C 1 390 ? 2.633   -9.383  88.940  1.00 41.09  ?  390 GLU   C N   1 
ATOM   10502 C CA  . GLU   C 1 390 ? 2.714   -9.403  90.396  1.00 45.47  ?  390 GLU   C CA  1 
ATOM   10503 C C   . GLU   C 1 390 ? 3.720   -8.367  90.873  1.00 43.27  ?  390 GLU   C C   1 
ATOM   10504 O O   . GLU   C 1 390 ? 4.878   -8.379  90.453  1.00 45.55  ?  390 GLU   C O   1 
ATOM   10505 C CB  . GLU   C 1 390 ? 3.108   -10.796 90.895  1.00 46.32  ?  390 GLU   C CB  1 
ATOM   10506 C CG  . GLU   C 1 390 ? 2.867   -11.042 92.391  1.00 45.09  ?  390 GLU   C CG  1 
ATOM   10507 C CD  . GLU   C 1 390 ? 4.104   -10.799 93.241  1.00 54.16  ?  390 GLU   C CD  1 
ATOM   10508 O OE1 . GLU   C 1 390 ? 5.146   -10.383 92.686  1.00 48.97  ?  390 GLU   C OE1 1 
ATOM   10509 O OE2 . GLU   C 1 390 ? 4.038   -11.033 94.468  1.00 53.07  ?  390 GLU   C OE2 1 
ATOM   10510 N N   . ILE   C 1 391 ? 3.271   -7.475  91.748  1.00 51.43  ?  391 ILE   C N   1 
ATOM   10511 C CA  . ILE   C 1 391 ? 4.158   -6.530  92.414  1.00 59.41  ?  391 ILE   C CA  1 
ATOM   10512 C C   . ILE   C 1 391 ? 4.228   -6.891  93.895  1.00 60.81  ?  391 ILE   C C   1 
ATOM   10513 O O   . ILE   C 1 391 ? 3.407   -6.431  94.699  1.00 60.30  ?  391 ILE   C O   1 
ATOM   10514 C CB  . ILE   C 1 391 ? 3.683   -5.079  92.211  1.00 57.96  ?  391 ILE   C CB  1 
ATOM   10515 C CG1 . ILE   C 1 391 ? 3.553   -4.764  90.718  1.00 42.12  ?  391 ILE   C CG1 1 
ATOM   10516 C CG2 . ILE   C 1 391 ? 4.613   -4.100  92.920  1.00 51.18  ?  391 ILE   C CG2 1 
ATOM   10517 C CD1 . ILE   C 1 391 ? 4.760   -5.140  89.893  1.00 42.79  ?  391 ILE   C CD1 1 
ATOM   10518 N N   . GLY   C 1 392 ? 5.197   -7.728  94.263  1.00 52.71  ?  392 GLY   C N   1 
ATOM   10519 C CA  . GLY   C 1 392 ? 5.300   -8.192  95.629  1.00 54.29  ?  392 GLY   C CA  1 
ATOM   10520 C C   . GLY   C 1 392 ? 6.508   -9.066  95.891  1.00 59.62  ?  392 GLY   C C   1 
ATOM   10521 O O   . GLY   C 1 392 ? 7.574   -8.859  95.299  1.00 56.41  ?  392 GLY   C O   1 
ATOM   10522 N N   . SER   C 1 393 ? 6.337   -10.056 96.779  1.00 62.07  ?  393 SER   C N   1 
ATOM   10523 C CA  . SER   C 1 393 ? 7.450   -10.899 97.214  1.00 55.23  ?  393 SER   C CA  1 
ATOM   10524 C C   . SER   C 1 393 ? 8.055   -11.699 96.065  1.00 52.59  ?  393 SER   C C   1 
ATOM   10525 O O   . SER   C 1 393 ? 9.241   -12.044 96.109  1.00 53.64  ?  393 SER   C O   1 
ATOM   10526 C CB  . SER   C 1 393 ? 6.983   -11.841 98.326  1.00 60.59  ?  393 SER   C CB  1 
ATOM   10527 O OG  . SER   C 1 393 ? 6.736   -11.142 99.538  1.00 55.43  ?  393 SER   C OG  1 
ATOM   10528 N N   . PHE   C 1 394 ? 7.264   -12.012 95.037  1.00 51.00  ?  394 PHE   C N   1 
ATOM   10529 C CA  . PHE   C 1 394 ? 7.814   -12.682 93.860  1.00 50.52  ?  394 PHE   C CA  1 
ATOM   10530 C C   . PHE   C 1 394 ? 8.652   -11.725 93.007  1.00 57.07  ?  394 PHE   C C   1 
ATOM   10531 O O   . PHE   C 1 394 ? 9.655   -12.144 92.415  1.00 54.76  ?  394 PHE   C O   1 
ATOM   10532 C CB  . PHE   C 1 394 ? 6.676   -13.306 93.038  1.00 48.93  ?  394 PHE   C CB  1 
ATOM   10533 C CG  . PHE   C 1 394 ? 7.127   -14.364 92.049  1.00 57.55  ?  394 PHE   C CG  1 
ATOM   10534 C CD1 . PHE   C 1 394 ? 7.964   -15.402 92.444  1.00 57.67  ?  394 PHE   C CD1 1 
ATOM   10535 C CD2 . PHE   C 1 394 ? 6.687   -14.335 90.735  1.00 50.04  ?  394 PHE   C CD2 1 
ATOM   10536 C CE1 . PHE   C 1 394 ? 8.372   -16.374 91.543  1.00 49.85  ?  394 PHE   C CE1 1 
ATOM   10537 C CE2 . PHE   C 1 394 ? 7.092   -15.305 89.832  1.00 58.79  ?  394 PHE   C CE2 1 
ATOM   10538 C CZ  . PHE   C 1 394 ? 7.936   -16.326 90.241  1.00 51.94  ?  394 PHE   C CZ  1 
ATOM   10539 N N   . LEU   C 1 395 ? 8.269   -10.443 92.939  1.00 51.74  ?  395 LEU   C N   1 
ATOM   10540 C CA  . LEU   C 1 395 ? 9.082   -9.452  92.238  1.00 51.90  ?  395 LEU   C CA  1 
ATOM   10541 C C   . LEU   C 1 395 ? 10.231  -8.948  93.104  1.00 56.12  ?  395 LEU   C C   1 
ATOM   10542 O O   . LEU   C 1 395 ? 11.318  -8.663  92.587  1.00 54.87  ?  395 LEU   C O   1 
ATOM   10543 C CB  . LEU   C 1 395 ? 8.219   -8.271  91.781  1.00 55.64  ?  395 LEU   C CB  1 
ATOM   10544 C CG  . LEU   C 1 395 ? 8.969   -7.086  91.144  1.00 57.03  ?  395 LEU   C CG  1 
ATOM   10545 C CD1 . LEU   C 1 395 ? 8.203   -6.505  89.965  1.00 62.36  ?  395 LEU   C CD1 1 
ATOM   10546 C CD2 . LEU   C 1 395 ? 9.269   -5.984  92.154  1.00 59.18  ?  395 LEU   C CD2 1 
ATOM   10547 N N   . LEU   C 1 396 ? 10.007  -8.812  94.412  1.00 65.19  ?  396 LEU   C N   1 
ATOM   10548 C CA  . LEU   C 1 396 ? 11.030  -8.252  95.289  1.00 66.13  ?  396 LEU   C CA  1 
ATOM   10549 C C   . LEU   C 1 396 ? 12.309  -9.091  95.254  1.00 66.85  ?  396 LEU   C C   1 
ATOM   10550 O O   . LEU   C 1 396 ? 13.386  -8.590  94.909  1.00 70.15  ?  396 LEU   C O   1 
ATOM   10551 C CB  . LEU   C 1 396 ? 10.479  -8.127  96.711  1.00 69.37  ?  396 LEU   C CB  1 
ATOM   10552 C CG  . LEU   C 1 396 ? 11.326  -7.334  97.711  1.00 75.85  ?  396 LEU   C CG  1 
ATOM   10553 C CD1 . LEU   C 1 396 ? 11.653  -5.953  97.160  1.00 75.15  ?  396 LEU   C CD1 1 
ATOM   10554 C CD2 . LEU   C 1 396 ? 10.605  -7.218  99.040  1.00 78.21  ?  396 LEU   C CD2 1 
ATOM   10555 N N   . GLY   C 1 397 ? 12.210  -10.370 95.595  1.00 59.40  ?  397 GLY   C N   1 
ATOM   10556 C CA  . GLY   C 1 397 ? 13.323  -11.295 95.478  1.00 55.94  ?  397 GLY   C CA  1 
ATOM   10557 C C   . GLY   C 1 397 ? 13.891  -11.698 96.830  1.00 66.02  ?  397 GLY   C C   1 
ATOM   10558 O O   . GLY   C 1 397 ? 13.359  -11.366 97.893  1.00 65.44  ?  397 GLY   C O   1 
ATOM   10559 N N   . ARG   C 1 398 ? 14.994  -12.444 96.769  1.00 61.94  ?  398 ARG   C N   1 
ATOM   10560 C CA  . ARG   C 1 398 ? 15.741  -12.839 97.967  1.00 67.57  ?  398 ARG   C CA  1 
ATOM   10561 C C   . ARG   C 1 398 ? 16.790  -11.792 98.316  1.00 63.55  ?  398 ARG   C C   1 
ATOM   10562 O O   . ARG   C 1 398 ? 17.357  -11.157 97.425  1.00 63.06  ?  398 ARG   C O   1 
ATOM   10563 C CB  . ARG   C 1 398 ? 16.414  -14.204 97.774  1.00 67.95  ?  398 ARG   C CB  1 
ATOM   10564 C CG  . ARG   C 1 398 ? 15.445  -15.378 97.756  1.00 70.48  ?  398 ARG   C CG  1 
ATOM   10565 C CD  . ARG   C 1 398 ? 16.157  -16.712 97.559  1.00 66.43  ?  398 ARG   C CD  1 
ATOM   10566 N NE  . ARG   C 1 398 ? 15.205  -17.810 97.432  1.00 74.00  ?  398 ARG   C NE  1 
ATOM   10567 C CZ  . ARG   C 1 398 ? 14.736  -18.521 98.450  1.00 78.75  ?  398 ARG   C CZ  1 
ATOM   10568 N NH1 . ARG   C 1 398 ? 15.132  -18.294 99.692  1.00 69.90  ?  398 ARG   C NH1 1 
ATOM   10569 N NH2 . ARG   C 1 398 ? 13.845  -19.483 98.216  1.00 80.64  ?  398 ARG   C NH2 1 
ATOM   10570 N N   . LYS   C 1 406 ? 13.420  -11.485 100.651 1.00 68.27  ?  406 LYS   C N   1 
ATOM   10571 C CA  . LYS   C 1 406 ? 13.164  -10.120 101.099 1.00 72.26  ?  406 LYS   C CA  1 
ATOM   10572 C C   . LYS   C 1 406 ? 11.697  -9.960  101.497 1.00 75.58  ?  406 LYS   C C   1 
ATOM   10573 O O   . LYS   C 1 406 ? 10.793  -10.346 100.751 1.00 72.09  ?  406 LYS   C O   1 
ATOM   10574 C CB  . LYS   C 1 406 ? 13.535  -9.113  100.003 1.00 72.66  ?  406 LYS   C CB  1 
ATOM   10575 C CG  . LYS   C 1 406 ? 13.784  -7.686  100.487 1.00 75.40  ?  406 LYS   C CG  1 
ATOM   10576 C CD  . LYS   C 1 406 ? 15.226  -7.483  100.942 1.00 74.43  ?  406 LYS   C CD  1 
ATOM   10577 C CE  . LYS   C 1 406 ? 15.565  -6.003  101.061 1.00 65.07  ?  406 LYS   C CE  1 
ATOM   10578 N NZ  . LYS   C 1 406 ? 15.363  -5.292  99.764  1.00 63.65  ?  406 LYS   C NZ  1 
ATOM   10579 N N   . HIS   C 1 407 ? 11.472  -9.396  102.682 1.00 74.10  ?  407 HIS   C N   1 
ATOM   10580 C CA  . HIS   C 1 407 ? 10.117  -9.171  103.172 1.00 81.05  ?  407 HIS   C CA  1 
ATOM   10581 C C   . HIS   C 1 407 ? 9.451   -8.041  102.392 1.00 80.59  ?  407 HIS   C C   1 
ATOM   10582 O O   . HIS   C 1 407 ? 9.916   -6.896  102.424 1.00 80.38  ?  407 HIS   C O   1 
ATOM   10583 C CB  . HIS   C 1 407 ? 10.149  -8.846  104.663 1.00 74.08  ?  407 HIS   C CB  1 
ATOM   10584 C CG  . HIS   C 1 407 ? 8.828   -8.404  105.211 1.00 82.86  ?  407 HIS   C CG  1 
ATOM   10585 N ND1 . HIS   C 1 407 ? 8.397   -7.096  105.152 1.00 85.89  ?  407 HIS   C ND1 1 
ATOM   10586 C CD2 . HIS   C 1 407 ? 7.843   -9.097  105.828 1.00 86.59  ?  407 HIS   C CD2 1 
ATOM   10587 C CE1 . HIS   C 1 407 ? 7.202   -7.003  105.708 1.00 89.44  ?  407 HIS   C CE1 1 
ATOM   10588 N NE2 . HIS   C 1 407 ? 6.844   -8.203  106.128 1.00 87.77  ?  407 HIS   C NE2 1 
ATOM   10589 N N   . ALA   C 1 408 ? 8.359   -8.356  101.700 1.00 78.92  ?  408 ALA   C N   1 
ATOM   10590 C CA  . ALA   C 1 408 ? 7.587   -7.353  100.978 1.00 82.66  ?  408 ALA   C CA  1 
ATOM   10591 C C   . ALA   C 1 408 ? 6.487   -6.800  101.878 1.00 90.95  ?  408 ALA   C C   1 
ATOM   10592 O O   . ALA   C 1 408 ? 5.744   -7.564  102.505 1.00 87.55  ?  408 ALA   C O   1 
ATOM   10593 C CB  . ALA   C 1 408 ? 6.987   -7.943  99.701  1.00 68.50  ?  408 ALA   C CB  1 
ATOM   10594 N N   . ASP   C 1 409 ? 6.394   -5.468  101.944 1.00 106.69 ?  409 ASP   C N   1 
ATOM   10595 C CA  . ASP   C 1 409 ? 5.362   -4.811  102.738 1.00 106.89 ?  409 ASP   C CA  1 
ATOM   10596 C C   . ASP   C 1 409 ? 3.985   -4.886  102.093 1.00 105.19 ?  409 ASP   C C   1 
ATOM   10597 O O   . ASP   C 1 409 ? 2.986   -4.625  102.772 1.00 105.92 ?  409 ASP   C O   1 
ATOM   10598 C CB  . ASP   C 1 409 ? 5.734   -3.346  102.978 1.00 108.07 ?  409 ASP   C CB  1 
ATOM   10599 C CG  . ASP   C 1 409 ? 6.822   -3.182  104.024 1.00 109.25 ?  409 ASP   C CG  1 
ATOM   10600 O OD1 . ASP   C 1 409 ? 7.291   -4.205  104.564 1.00 110.44 ?  409 ASP   C OD1 1 
ATOM   10601 O OD2 . ASP   C 1 409 ? 7.206   -2.027  104.309 1.00 109.74 ?  409 ASP   C OD2 1 
ATOM   10602 N N   . MET   C 1 410 ? 3.908   -5.233  100.811 1.00 88.26  ?  410 MET   C N   1 
ATOM   10603 C CA  . MET   C 1 410 ? 2.639   -5.296  100.105 1.00 78.45  ?  410 MET   C CA  1 
ATOM   10604 C C   . MET   C 1 410 ? 2.701   -6.414  99.077  1.00 69.23  ?  410 MET   C C   1 
ATOM   10605 O O   . MET   C 1 410 ? 3.754   -6.682  98.491  1.00 67.23  ?  410 MET   C O   1 
ATOM   10606 C CB  . MET   C 1 410 ? 2.311   -3.959  99.427  1.00 82.23  ?  410 MET   C CB  1 
ATOM   10607 C CG  . MET   C 1 410 ? 3.304   -3.551  98.342  1.00 80.88  ?  410 MET   C CG  1 
ATOM   10608 S SD  . MET   C 1 410 ? 3.581   -1.769  98.250  1.00 81.16  ?  410 MET   C SD  1 
ATOM   10609 C CE  . MET   C 1 410 ? 4.206   -1.429  99.898  1.00 73.07  ?  410 MET   C CE  1 
ATOM   10610 N N   . GLU   C 1 411 ? 1.545   -7.053  98.888  1.00 68.39  ?  411 GLU   C N   1 
ATOM   10611 C CA  . GLU   C 1 411 ? 1.382   -8.130  97.887  1.00 70.47  ?  411 GLU   C CA  1 
ATOM   10612 C C   . GLU   C 1 411 ? 0.361   -7.578  96.876  1.00 71.41  ?  411 GLU   C C   1 
ATOM   10613 O O   . GLU   C 1 411 ? -0.847  -7.830  97.060  1.00 59.43  ?  411 GLU   C O   1 
ATOM   10614 C CB  . GLU   C 1 411 ? 0.985   -9.422  98.593  1.00 59.31  ?  411 GLU   C CB  1 
ATOM   10615 C CG  . GLU   C 1 411 ? 2.011   -9.904  99.612  1.00 60.38  ?  411 GLU   C CG  1 
ATOM   10616 C CD  . GLU   C 1 411 ? 3.343   -10.375 99.066  1.00 59.28  ?  411 GLU   C CD  1 
ATOM   10617 O OE1 . GLU   C 1 411 ? 3.374   -10.948 97.966  1.00 54.60  ?  411 GLU   C OE1 1 
ATOM   10618 O OE2 . GLU   C 1 411 ? 4.353   -10.163 99.761  1.00 65.53  ?  411 GLU   C OE2 1 
ATOM   10619 N N   . PHE   C 1 412 ? 0.841   -6.854  95.860  1.00 84.03  ?  412 PHE   C N   1 
ATOM   10620 C CA  . PHE   C 1 412 ? -0.007  -6.167  94.898  1.00 81.52  ?  412 PHE   C CA  1 
ATOM   10621 C C   . PHE   C 1 412 ? -0.222  -7.008  93.647  1.00 79.90  ?  412 PHE   C C   1 
ATOM   10622 O O   . PHE   C 1 412 ? 0.550   -7.914  93.327  1.00 80.29  ?  412 PHE   C O   1 
ATOM   10623 C CB  . PHE   C 1 412 ? 0.598   -4.819  94.493  1.00 82.37  ?  412 PHE   C CB  1 
ATOM   10624 C CG  . PHE   C 1 412 ? 0.195   -3.678  95.377  1.00 87.03  ?  412 PHE   C CG  1 
ATOM   10625 C CD1 . PHE   C 1 412 ? -0.148  -3.894  96.701  1.00 82.38  ?  412 PHE   C CD1 1 
ATOM   10626 C CD2 . PHE   C 1 412 ? 0.146   -2.385  94.878  1.00 84.06  ?  412 PHE   C CD2 1 
ATOM   10627 C CE1 . PHE   C 1 412 ? -0.527  -2.842  97.516  1.00 82.93  ?  412 PHE   C CE1 1 
ATOM   10628 C CE2 . PHE   C 1 412 ? -0.234  -1.328  95.687  1.00 84.10  ?  412 PHE   C CE2 1 
ATOM   10629 C CZ  . PHE   C 1 412 ? -0.570  -1.557  97.007  1.00 88.57  ?  412 PHE   C CZ  1 
ATOM   10630 N N   . MET   C 1 413 ? -1.301  -6.685  92.941  1.00 54.79  ?  413 MET   C N   1 
ATOM   10631 C CA  . MET   C 1 413 ? -1.550  -7.174  91.592  1.00 39.56  ?  413 MET   C CA  1 
ATOM   10632 C C   . MET   C 1 413 ? -1.848  -5.967  90.722  1.00 35.90  ?  413 MET   C C   1 
ATOM   10633 O O   . MET   C 1 413 ? -2.773  -5.202  91.018  1.00 32.18  ?  413 MET   C O   1 
ATOM   10634 C CB  . MET   C 1 413 ? -2.713  -8.166  91.557  1.00 38.47  ?  413 MET   C CB  1 
ATOM   10635 C CG  . MET   C 1 413 ? -3.183  -8.495  90.158  1.00 33.07  ?  413 MET   C CG  1 
ATOM   10636 S SD  . MET   C 1 413 ? -4.421  -9.802  90.135  1.00 39.11  ?  413 MET   C SD  1 
ATOM   10637 C CE  . MET   C 1 413 ? -5.769  -9.030  91.026  1.00 41.18  ?  413 MET   C CE  1 
ATOM   10638 N N   . ARG   C 1 414 ? -1.056  -5.780  89.671  1.00 34.92  ?  414 ARG   C N   1 
ATOM   10639 C CA  . ARG   C 1 414 ? -1.217  -4.647  88.772  1.00 30.08  ?  414 ARG   C CA  1 
ATOM   10640 C C   . ARG   C 1 414 ? -1.998  -5.095  87.544  1.00 29.64  ?  414 ARG   C C   1 
ATOM   10641 O O   . ARG   C 1 414 ? -1.559  -5.986  86.810  1.00 28.87  ?  414 ARG   C O   1 
ATOM   10642 C CB  . ARG   C 1 414 ? 0.130   -4.051  88.359  1.00 29.76  ?  414 ARG   C CB  1 
ATOM   10643 C CG  . ARG   C 1 414 ? -0.015  -2.808  87.487  1.00 30.71  ?  414 ARG   C CG  1 
ATOM   10644 C CD  . ARG   C 1 414 ? 1.326   -2.216  87.075  1.00 28.14  ?  414 ARG   C CD  1 
ATOM   10645 N NE  . ARG   C 1 414 ? 1.965   -2.952  85.992  1.00 31.86  ?  414 ARG   C NE  1 
ATOM   10646 C CZ  . ARG   C 1 414 ? 2.933   -2.459  85.227  1.00 39.61  ?  414 ARG   C CZ  1 
ATOM   10647 N NH1 . ARG   C 1 414 ? 3.389   -1.225  85.395  1.00 37.33  ?  414 ARG   C NH1 1 
ATOM   10648 N NH2 . ARG   C 1 414 ? 3.452   -3.218  84.265  1.00 33.08  ?  414 ARG   C NH2 1 
ATOM   10649 N N   . LEU   C 1 415 ? -3.159  -4.488  87.338  1.00 28.26  ?  415 LEU   C N   1 
ATOM   10650 C CA  . LEU   C 1 415 ? -3.938  -4.674  86.122  1.00 27.17  ?  415 LEU   C CA  1 
ATOM   10651 C C   . LEU   C 1 415 ? -3.584  -3.482  85.239  1.00 26.00  ?  415 LEU   C C   1 
ATOM   10652 O O   . LEU   C 1 415 ? -4.146  -2.395  85.377  1.00 25.58  ?  415 LEU   C O   1 
ATOM   10653 C CB  . LEU   C 1 415 ? -5.426  -4.765  86.440  1.00 27.23  ?  415 LEU   C CB  1 
ATOM   10654 C CG  . LEU   C 1 415 ? -5.837  -5.771  87.528  1.00 28.57  ?  415 LEU   C CG  1 
ATOM   10655 C CD1 . LEU   C 1 415 ? -7.263  -5.501  88.037  1.00 28.66  ?  415 LEU   C CD1 1 
ATOM   10656 C CD2 . LEU   C 1 415 ? -5.701  -7.218  87.044  1.00 28.95  ?  415 LEU   C CD2 1 
ATOM   10657 N N   . THR   C 1 416 ? -2.609  -3.679  84.353  1.00 25.57  ?  416 THR   C N   1 
ATOM   10658 C CA  . THR   C 1 416 ? -2.105  -2.610  83.501  1.00 24.60  ?  416 THR   C CA  1 
ATOM   10659 C C   . THR   C 1 416 ? -2.899  -2.586  82.202  1.00 23.54  ?  416 THR   C C   1 
ATOM   10660 O O   . THR   C 1 416 ? -3.056  -3.617  81.544  1.00 23.54  ?  416 THR   C O   1 
ATOM   10661 C CB  . THR   C 1 416 ? -0.609  -2.788  83.203  1.00 26.26  ?  416 THR   C CB  1 
ATOM   10662 O OG1 . THR   C 1 416 ? -0.011  -3.665  84.168  1.00 27.84  ?  416 THR   C OG1 1 
ATOM   10663 C CG2 . THR   C 1 416 ? 0.120   -1.437  83.263  1.00 24.45  ?  416 THR   C CG2 1 
ATOM   10664 N N   . ILE   C 1 417 ? -3.382  -1.408  81.828  1.00 22.81  ?  417 ILE   C N   1 
ATOM   10665 C CA  . ILE   C 1 417 ? -4.314  -1.250  80.718  1.00 21.94  ?  417 ILE   C CA  1 
ATOM   10666 C C   . ILE   C 1 417 ? -3.578  -0.605  79.553  1.00 22.46  ?  417 ILE   C C   1 
ATOM   10667 O O   . ILE   C 1 417 ? -3.147  0.552   79.647  1.00 21.31  ?  417 ILE   C O   1 
ATOM   10668 C CB  . ILE   C 1 417 ? -5.533  -0.405  81.120  1.00 22.66  ?  417 ILE   C CB  1 
ATOM   10669 C CG1 . ILE   C 1 417 ? -6.127  -0.886  82.450  1.00 23.62  ?  417 ILE   C CG1 1 
ATOM   10670 C CG2 . ILE   C 1 417 ? -6.564  -0.398  80.004  1.00 21.05  ?  417 ILE   C CG2 1 
ATOM   10671 C CD1 . ILE   C 1 417 ? -6.455  -2.362  82.503  1.00 23.20  ?  417 ILE   C CD1 1 
ATOM   10672 N N   . ALA   C 1 418 ? -3.449  -1.340  78.452  1.00 21.27  ?  418 ALA   C N   1 
ATOM   10673 C CA  . ALA   C 1 418 ? -2.921  -0.752  77.228  1.00 20.21  ?  418 ALA   C CA  1 
ATOM   10674 C C   . ALA   C 1 418 ? -3.859  0.345   76.727  1.00 19.94  ?  418 ALA   C C   1 
ATOM   10675 O O   . ALA   C 1 418 ? -5.053  0.377   77.046  1.00 22.43  ?  418 ALA   C O   1 
ATOM   10676 C CB  . ALA   C 1 418 ? -2.739  -1.820  76.155  1.00 19.93  ?  418 ALA   C CB  1 
ATOM   10677 N N   . ARG   C 1 419 ? -3.307  1.268   75.945  1.00 20.77  ?  419 ARG   C N   1 
ATOM   10678 C CA  . ARG   C 1 419 ? -4.064  2.437   75.508  1.00 18.53  ?  419 ARG   C CA  1 
ATOM   10679 C C   . ARG   C 1 419 ? -4.826  2.133   74.230  1.00 19.18  ?  419 ARG   C C   1 
ATOM   10680 O O   . ARG   C 1 419 ? -4.238  1.695   73.237  1.00 17.89  ?  419 ARG   C O   1 
ATOM   10681 C CB  . ARG   C 1 419 ? -3.140  3.634   75.297  1.00 19.03  ?  419 ARG   C CB  1 
ATOM   10682 C CG  . ARG   C 1 419 ? -2.483  4.094   76.577  1.00 18.91  ?  419 ARG   C CG  1 
ATOM   10683 C CD  . ARG   C 1 419 ? -1.282  4.977   76.325  1.00 18.87  ?  419 ARG   C CD  1 
ATOM   10684 N NE  . ARG   C 1 419 ? -0.618  5.267   77.588  1.00 20.68  ?  419 ARG   C NE  1 
ATOM   10685 C CZ  . ARG   C 1 419 ? 0.185   4.419   78.215  1.00 20.06  ?  419 ARG   C CZ  1 
ATOM   10686 N NH1 . ARG   C 1 419 ? 0.480   3.237   77.697  1.00 19.96  ?  419 ARG   C NH1 1 
ATOM   10687 N NH2 . ARG   C 1 419 ? 0.691   4.757   79.400  1.00 22.29  ?  419 ARG   C NH2 1 
ATOM   10688 N N   . ARG   C 1 420 ? -6.140  2.369   74.270  1.00 17.98  ?  420 ARG   C N   1 
ATOM   10689 C CA  . ARG   C 1 420 ? -7.041  2.292   73.125  1.00 18.92  ?  420 ARG   C CA  1 
ATOM   10690 C C   . ARG   C 1 420 ? -7.198  0.873   72.593  1.00 18.60  ?  420 ARG   C C   1 
ATOM   10691 O O   . ARG   C 1 420 ? -7.600  0.685   71.450  1.00 19.05  ?  420 ARG   C O   1 
ATOM   10692 C CB  . ARG   C 1 420 ? -6.590  3.239   72.004  1.00 17.63  ?  420 ARG   C CB  1 
ATOM   10693 C CG  . ARG   C 1 420 ? -6.421  4.691   72.471  1.00 18.57  ?  420 ARG   C CG  1 
ATOM   10694 C CD  . ARG   C 1 420 ? -6.240  5.658   71.300  1.00 16.93  ?  420 ARG   C CD  1 
ATOM   10695 N NE  . ARG   C 1 420 ? -5.007  5.431   70.551  1.00 20.10  ?  420 ARG   C NE  1 
ATOM   10696 C CZ  . ARG   C 1 420 ? -4.453  6.320   69.734  1.00 19.45  ?  420 ARG   C CZ  1 
ATOM   10697 N NH1 . ARG   C 1 420 ? -4.979  7.523   69.561  1.00 16.72  ?  420 ARG   C NH1 1 
ATOM   10698 N NH2 . ARG   C 1 420 ? -3.332  6.000   69.087  1.00 16.61  ?  420 ARG   C NH2 1 
ATOM   10699 N N   . VAL   C 1 421 ? -6.929  -0.132  73.418  1.00 20.07  ?  421 VAL   C N   1 
ATOM   10700 C CA  . VAL   C 1 421 ? -6.943  -1.528  72.994  1.00 18.42  ?  421 VAL   C CA  1 
ATOM   10701 C C   . VAL   C 1 421 ? -8.200  -2.247  73.460  1.00 19.76  ?  421 VAL   C C   1 
ATOM   10702 O O   . VAL   C 1 421 ? -8.815  -2.997  72.702  1.00 19.57  ?  421 VAL   C O   1 
ATOM   10703 C CB  . VAL   C 1 421 ? -5.672  -2.232  73.513  1.00 18.80  ?  421 VAL   C CB  1 
ATOM   10704 C CG1 . VAL   C 1 421 ? -5.736  -3.728  73.247  1.00 21.01  ?  421 VAL   C CG1 1 
ATOM   10705 C CG2 . VAL   C 1 421 ? -4.458  -1.620  72.865  1.00 18.46  ?  421 VAL   C CG2 1 
ATOM   10706 N N   . TYR   C 1 422 ? -8.582  -2.049  74.717  1.00 19.12  ?  422 TYR   C N   1 
ATOM   10707 C CA  . TYR   C 1 422 ? -9.688  -2.775  75.319  1.00 19.88  ?  422 TYR   C CA  1 
ATOM   10708 C C   . TYR   C 1 422 ? -10.850 -1.835  75.592  1.00 20.28  ?  422 TYR   C C   1 
ATOM   10709 O O   . TYR   C 1 422 ? -10.663 -0.648  75.885  1.00 20.10  ?  422 TYR   C O   1 
ATOM   10710 C CB  . TYR   C 1 422 ? -9.248  -3.466  76.618  1.00 20.32  ?  422 TYR   C CB  1 
ATOM   10711 C CG  . TYR   C 1 422 ? -8.148  -4.479  76.388  1.00 23.34  ?  422 TYR   C CG  1 
ATOM   10712 C CD1 . TYR   C 1 422 ? -8.407  -5.682  75.737  1.00 20.86  ?  422 TYR   C CD1 1 
ATOM   10713 C CD2 . TYR   C 1 422 ? -6.845  -4.225  76.804  1.00 20.74  ?  422 TYR   C CD2 1 
ATOM   10714 C CE1 . TYR   C 1 422 ? -7.391  -6.605  75.514  1.00 21.20  ?  422 TYR   C CE1 1 
ATOM   10715 C CE2 . TYR   C 1 422 ? -5.836  -5.138  76.582  1.00 21.06  ?  422 TYR   C CE2 1 
ATOM   10716 C CZ  . TYR   C 1 422 ? -6.110  -6.330  75.939  1.00 21.29  ?  422 TYR   C CZ  1 
ATOM   10717 O OH  . TYR   C 1 422 ? -5.084  -7.239  75.716  1.00 21.67  ?  422 TYR   C OH  1 
ATOM   10718 N N   . THR   C 1 423 ? -12.054 -2.382  75.488  1.00 19.60  ?  423 THR   C N   1 
ATOM   10719 C CA  . THR   C 1 423 ? -13.263 -1.632  75.759  1.00 19.53  ?  423 THR   C CA  1 
ATOM   10720 C C   . THR   C 1 423 ? -13.640 -1.763  77.230  1.00 20.84  ?  423 THR   C C   1 
ATOM   10721 O O   . THR   C 1 423 ? -13.068 -2.558  77.978  1.00 20.66  ?  423 THR   C O   1 
ATOM   10722 C CB  . THR   C 1 423 ? -14.412 -2.134  74.888  1.00 21.63  ?  423 THR   C CB  1 
ATOM   10723 O OG1 . THR   C 1 423 ? -14.810 -3.427  75.355  1.00 20.56  ?  423 THR   C OG1 1 
ATOM   10724 C CG2 . THR   C 1 423 ? -13.987 -2.226  73.408  1.00 19.11  ?  423 THR   C CG2 1 
ATOM   10725 N N   . ASN   C 1 424 ? -14.636 -0.975  77.643  1.00 20.10  ?  424 ASN   C N   1 
ATOM   10726 C CA  . ASN   C 1 424 ? -15.141 -1.117  79.001  1.00 26.47  ?  424 ASN   C CA  1 
ATOM   10727 C C   . ASN   C 1 424 ? -15.793 -2.478  79.216  1.00 24.50  ?  424 ASN   C C   1 
ATOM   10728 O O   . ASN   C 1 424 ? -15.831 -2.970  80.348  1.00 23.12  ?  424 ASN   C O   1 
ATOM   10729 C CB  . ASN   C 1 424 ? -16.114 0.016   79.321  1.00 23.34  ?  424 ASN   C CB  1 
ATOM   10730 C CG  . ASN   C 1 424 ? -15.420 1.367   79.389  1.00 29.07  ?  424 ASN   C CG  1 
ATOM   10731 O OD1 . ASN   C 1 424 ? -14.320 1.484   79.941  1.00 27.53  ?  424 ASN   C OD1 1 
ATOM   10732 N ND2 . ASN   C 1 424 ? -16.050 2.391   78.812  1.00 29.86  ?  424 ASN   C ND2 1 
ATOM   10733 N N   . ASP   C 1 425 ? -16.279 -3.117  78.150  1.00 21.17  ?  425 ASP   C N   1 
ATOM   10734 C CA  . ASP   C 1 425 ? -16.759 -4.484  78.303  1.00 23.56  ?  425 ASP   C CA  1 
ATOM   10735 C C   . ASP   C 1 425 ? -15.619 -5.443  78.618  1.00 22.27  ?  425 ASP   C C   1 
ATOM   10736 O O   . ASP   C 1 425 ? -15.825 -6.422  79.346  1.00 23.08  ?  425 ASP   C O   1 
ATOM   10737 C CB  . ASP   C 1 425 ? -17.519 -4.929  77.055  1.00 21.63  ?  425 ASP   C CB  1 
ATOM   10738 C CG  . ASP   C 1 425 ? -18.876 -4.265  76.940  1.00 25.05  ?  425 ASP   C CG  1 
ATOM   10739 O OD1 . ASP   C 1 425 ? -19.437 -3.856  77.983  1.00 26.15  ?  425 ASP   C OD1 1 
ATOM   10740 O OD2 . ASP   C 1 425 ? -19.391 -4.154  75.808  1.00 27.50  ?  425 ASP   C OD2 1 
ATOM   10741 N N   . HIS   C 1 426 ? -14.417 -5.181  78.097  1.00 21.83  ?  426 HIS   C N   1 
ATOM   10742 C CA  . HIS   C 1 426 ? -13.256 -5.950  78.534  1.00 22.31  ?  426 HIS   C CA  1 
ATOM   10743 C C   . HIS   C 1 426 ? -12.959 -5.680  80.000  1.00 22.88  ?  426 HIS   C C   1 
ATOM   10744 O O   . HIS   C 1 426 ? -12.612 -6.598  80.747  1.00 23.72  ?  426 HIS   C O   1 
ATOM   10745 C CB  . HIS   C 1 426 ? -12.034 -5.624  77.672  1.00 21.72  ?  426 HIS   C CB  1 
ATOM   10746 C CG  . HIS   C 1 426 ? -12.092 -6.199  76.287  1.00 21.41  ?  426 HIS   C CG  1 
ATOM   10747 N ND1 . HIS   C 1 426 ? -11.963 -5.424  75.156  1.00 20.88  ?  426 HIS   C ND1 1 
ATOM   10748 C CD2 . HIS   C 1 426 ? -12.256 -7.472  75.853  1.00 21.87  ?  426 HIS   C CD2 1 
ATOM   10749 C CE1 . HIS   C 1 426 ? -12.049 -6.193  74.084  1.00 20.63  ?  426 HIS   C CE1 1 
ATOM   10750 N NE2 . HIS   C 1 426 ? -12.236 -7.439  74.480  1.00 21.37  ?  426 HIS   C NE2 1 
ATOM   10751 N N   . MET   C 1 427 ? -13.102 -4.423  80.429  1.00 23.34  ?  427 MET   C N   1 
ATOM   10752 C CA  . MET   C 1 427 ? -12.930 -4.096  81.842  1.00 23.90  ?  427 MET   C CA  1 
ATOM   10753 C C   . MET   C 1 427 ? -13.907 -4.876  82.704  1.00 24.04  ?  427 MET   C C   1 
ATOM   10754 O O   . MET   C 1 427 ? -13.543 -5.370  83.779  1.00 25.04  ?  427 MET   C O   1 
ATOM   10755 C CB  . MET   C 1 427 ? -13.115 -2.594  82.066  1.00 22.70  ?  427 MET   C CB  1 
ATOM   10756 C CG  . MET   C 1 427 ? -12.139 -1.703  81.311  1.00 21.95  ?  427 MET   C CG  1 
ATOM   10757 S SD  . MET   C 1 427 ? -10.404 -2.007  81.691  1.00 22.69  ?  427 MET   C SD  1 
ATOM   10758 C CE  . MET   C 1 427 ? -9.850  -2.760  80.156  1.00 21.73  ?  427 MET   C CE  1 
ATOM   10759 N N   . ASP   C 1 428 ? -15.158 -4.988  82.250  1.00 23.87  ?  428 ASP   C N   1 
ATOM   10760 C CA  . ASP   C 1 428 ? -16.157 -5.732  83.005  1.00 24.71  ?  428 ASP   C CA  1 
ATOM   10761 C C   . ASP   C 1 428 ? -15.757 -7.190  83.149  1.00 25.54  ?  428 ASP   C C   1 
ATOM   10762 O O   . ASP   C 1 428 ? -15.880 -7.772  84.236  1.00 27.22  ?  428 ASP   C O   1 
ATOM   10763 C CB  . ASP   C 1 428 ? -17.524 -5.620  82.329  1.00 26.74  ?  428 ASP   C CB  1 
ATOM   10764 C CG  . ASP   C 1 428 ? -18.234 -4.321  82.654  1.00 23.99  ?  428 ASP   C CG  1 
ATOM   10765 O OD1 . ASP   C 1 428 ? -17.866 -3.677  83.657  1.00 27.01  ?  428 ASP   C OD1 1 
ATOM   10766 O OD2 . ASP   C 1 428 ? -19.170 -3.951  81.913  1.00 23.97  ?  428 ASP   C OD2 1 
ATOM   10767 N N   . TYR   C 1 429 ? -15.296 -7.799  82.058  1.00 25.20  ?  429 TYR   C N   1 
ATOM   10768 C CA  . TYR   C 1 429 ? -14.832 -9.178  82.106  1.00 26.01  ?  429 TYR   C CA  1 
ATOM   10769 C C   . TYR   C 1 429 ? -13.733 -9.345  83.140  1.00 26.72  ?  429 TYR   C C   1 
ATOM   10770 O O   . TYR   C 1 429 ? -13.746 -10.296 83.927  1.00 28.14  ?  429 TYR   C O   1 
ATOM   10771 C CB  . TYR   C 1 429 ? -14.335 -9.602  80.728  1.00 25.45  ?  429 TYR   C CB  1 
ATOM   10772 C CG  . TYR   C 1 429 ? -13.818 -11.025 80.656  1.00 34.76  ?  429 TYR   C CG  1 
ATOM   10773 C CD1 . TYR   C 1 429 ? -12.525 -11.345 81.060  1.00 33.79  ?  429 TYR   C CD1 1 
ATOM   10774 C CD2 . TYR   C 1 429 ? -14.622 -12.047 80.164  1.00 35.56  ?  429 TYR   C CD2 1 
ATOM   10775 C CE1 . TYR   C 1 429 ? -12.054 -12.644 80.987  1.00 38.35  ?  429 TYR   C CE1 1 
ATOM   10776 C CE2 . TYR   C 1 429 ? -14.157 -13.343 80.080  1.00 36.91  ?  429 TYR   C CE2 1 
ATOM   10777 C CZ  . TYR   C 1 429 ? -12.874 -13.637 80.488  1.00 39.83  ?  429 TYR   C CZ  1 
ATOM   10778 O OH  . TYR   C 1 429 ? -12.418 -14.934 80.404  1.00 42.20  ?  429 TYR   C OH  1 
ATOM   10779 N N   . ILE   C 1 430 ? -12.761 -8.432  83.140  1.00 26.16  ?  430 ILE   C N   1 
ATOM   10780 C CA  . ILE   C 1 430 ? -11.677 -8.500  84.117  1.00 26.88  ?  430 ILE   C CA  1 
ATOM   10781 C C   . ILE   C 1 430 ? -12.234 -8.385  85.530  1.00 28.78  ?  430 ILE   C C   1 
ATOM   10782 O O   . ILE   C 1 430 ? -11.935 -9.210  86.401  1.00 31.71  ?  430 ILE   C O   1 
ATOM   10783 C CB  . ILE   C 1 430 ? -10.625 -7.412  83.835  1.00 26.10  ?  430 ILE   C CB  1 
ATOM   10784 C CG1 . ILE   C 1 430 ? -10.054 -7.565  82.422  1.00 25.26  ?  430 ILE   C CG1 1 
ATOM   10785 C CG2 . ILE   C 1 430 ? -9.520  -7.459  84.883  1.00 26.94  ?  430 ILE   C CG2 1 
ATOM   10786 C CD1 . ILE   C 1 430 ? -9.363  -6.318  81.916  1.00 24.32  ?  430 ILE   C CD1 1 
ATOM   10787 N N   . ALA   C 1 431 ? -13.066 -7.368  85.774  1.00 27.38  ?  431 ALA   C N   1 
ATOM   10788 C CA  . ALA   C 1 431 ? -13.629 -7.174  87.104  1.00 28.84  ?  431 ALA   C CA  1 
ATOM   10789 C C   . ALA   C 1 431 ? -14.428 -8.392  87.544  1.00 30.50  ?  431 ALA   C C   1 
ATOM   10790 O O   . ALA   C 1 431 ? -14.212 -8.926  88.638  1.00 35.23  ?  431 ALA   C O   1 
ATOM   10791 C CB  . ALA   C 1 431 ? -14.504 -5.921  87.130  1.00 27.58  ?  431 ALA   C CB  1 
ATOM   10792 N N   . ASP   C 1 432 ? -15.342 -8.859  86.688  1.00 29.37  ?  432 ASP   C N   1 
ATOM   10793 C CA  . ASP   C 1 432 ? -16.194 -9.987  87.042  1.00 29.93  ?  432 ASP   C CA  1 
ATOM   10794 C C   . ASP   C 1 432 ? -15.391 -11.248 87.317  1.00 37.06  ?  432 ASP   C C   1 
ATOM   10795 O O   . ASP   C 1 432 ? -15.778 -12.054 88.172  1.00 37.44  ?  432 ASP   C O   1 
ATOM   10796 C CB  . ASP   C 1 432 ? -17.205 -10.236 85.932  1.00 31.04  ?  432 ASP   C CB  1 
ATOM   10797 C CG  . ASP   C 1 432 ? -18.209 -9.124  85.826  1.00 35.76  ?  432 ASP   C CG  1 
ATOM   10798 O OD1 . ASP   C 1 432 ? -18.343 -8.370  86.811  1.00 40.83  ?  432 ASP   C OD1 1 
ATOM   10799 O OD2 . ASP   C 1 432 ? -18.865 -9.002  84.775  1.00 41.92  ?  432 ASP   C OD2 1 
ATOM   10800 N N   . ALA   C 1 433 ? -14.276 -11.438 86.614  1.00 33.48  ?  433 ALA   C N   1 
ATOM   10801 C CA  . ALA   C 1 433 ? -13.441 -12.604 86.872  1.00 33.53  ?  433 ALA   C CA  1 
ATOM   10802 C C   . ALA   C 1 433 ? -12.842 -12.549 88.271  1.00 36.08  ?  433 ALA   C C   1 
ATOM   10803 O O   . ALA   C 1 433 ? -12.935 -13.519 89.033  1.00 44.58  ?  433 ALA   C O   1 
ATOM   10804 C CB  . ALA   C 1 433 ? -12.346 -12.704 85.816  1.00 33.38  ?  433 ALA   C CB  1 
ATOM   10805 N N   . LEU   C 1 434 ? -12.232 -11.416 88.632  1.00 33.60  ?  434 LEU   C N   1 
ATOM   10806 C CA  . LEU   C 1 434 ? -11.635 -11.282 89.958  1.00 35.14  ?  434 LEU   C CA  1 
ATOM   10807 C C   . LEU   C 1 434 ? -12.694 -11.369 91.055  1.00 41.64  ?  434 LEU   C C   1 
ATOM   10808 O O   . LEU   C 1 434 ? -12.462 -11.971 92.109  1.00 45.77  ?  434 LEU   C O   1 
ATOM   10809 C CB  . LEU   C 1 434 ? -10.858 -9.964  90.049  1.00 33.83  ?  434 LEU   C CB  1 
ATOM   10810 C CG  . LEU   C 1 434 ? -10.114 -9.639  91.349  1.00 33.79  ?  434 LEU   C CG  1 
ATOM   10811 C CD1 . LEU   C 1 434 ? -9.069  -10.689 91.660  1.00 43.82  ?  434 LEU   C CD1 1 
ATOM   10812 C CD2 . LEU   C 1 434 ? -9.471  -8.263  91.287  1.00 32.93  ?  434 LEU   C CD2 1 
ATOM   10813 N N   . ILE   C 1 435 ? -13.869 -10.789 90.817  1.00 38.34  ?  435 ILE   C N   1 
ATOM   10814 C CA  . ILE   C 1 435 ? -14.930 -10.811 91.821  1.00 42.50  ?  435 ILE   C CA  1 
ATOM   10815 C C   . ILE   C 1 435 ? -15.435 -12.235 92.037  1.00 50.09  ?  435 ILE   C C   1 
ATOM   10816 O O   . ILE   C 1 435 ? -15.567 -12.699 93.177  1.00 50.67  ?  435 ILE   C O   1 
ATOM   10817 C CB  . ILE   C 1 435 ? -16.068 -9.859  91.406  1.00 38.27  ?  435 ILE   C CB  1 
ATOM   10818 C CG1 . ILE   C 1 435 ? -15.603 -8.404  91.508  1.00 35.14  ?  435 ILE   C CG1 1 
ATOM   10819 C CG2 . ILE   C 1 435 ? -17.317 -10.101 92.242  1.00 38.01  ?  435 ILE   C CG2 1 
ATOM   10820 C CD1 . ILE   C 1 435 ? -16.442 -7.438  90.687  1.00 35.20  ?  435 ILE   C CD1 1 
ATOM   10821 N N   . GLY   C 1 436 ? -15.706 -12.956 90.944  1.00 46.80  ?  436 GLY   C N   1 
ATOM   10822 C CA  . GLY   C 1 436 ? -16.261 -14.298 91.025  1.00 48.55  ?  436 GLY   C CA  1 
ATOM   10823 C C   . GLY   C 1 436 ? -15.451 -15.267 91.863  1.00 52.32  ?  436 GLY   C C   1 
ATOM   10824 O O   . GLY   C 1 436 ? -15.998 -16.272 92.330  1.00 61.34  ?  436 GLY   C O   1 
ATOM   10825 N N   . LEU   C 1 437 ? -14.163 -14.987 92.069  1.00 52.95  ?  437 LEU   C N   1 
ATOM   10826 C CA  . LEU   C 1 437 ? -13.293 -15.808 92.904  1.00 53.64  ?  437 LEU   C CA  1 
ATOM   10827 C C   . LEU   C 1 437 ? -13.410 -15.493 94.391  1.00 60.50  ?  437 LEU   C C   1 
ATOM   10828 O O   . LEU   C 1 437 ? -12.589 -15.989 95.170  1.00 62.86  ?  437 LEU   C O   1 
ATOM   10829 C CB  . LEU   C 1 437 ? -11.832 -15.632 92.480  1.00 51.57  ?  437 LEU   C CB  1 
ATOM   10830 C CG  . LEU   C 1 437 ? -11.416 -15.990 91.056  1.00 51.98  ?  437 LEU   C CG  1 
ATOM   10831 C CD1 . LEU   C 1 437 ? -9.955  -15.622 90.838  1.00 47.20  ?  437 LEU   C CD1 1 
ATOM   10832 C CD2 . LEU   C 1 437 ? -11.657 -17.468 90.772  1.00 55.72  ?  437 LEU   C CD2 1 
ATOM   10833 N N   . LYS   C 1 438 ? -14.392 -14.685 94.805  1.00 58.46  ?  438 LYS   C N   1 
ATOM   10834 C CA  . LYS   C 1 438 ? -14.426 -14.217 96.189  1.00 59.85  ?  438 LYS   C CA  1 
ATOM   10835 C C   . LYS   C 1 438 ? -14.567 -15.367 97.178  1.00 65.98  ?  438 LYS   C C   1 
ATOM   10836 O O   . LYS   C 1 438 ? -14.018 -15.300 98.284  1.00 69.10  ?  438 LYS   C O   1 
ATOM   10837 C CB  . LYS   C 1 438 ? -15.556 -13.203 96.377  1.00 57.39  ?  438 LYS   C CB  1 
ATOM   10838 C CG  . LYS   C 1 438 ? -15.090 -11.752 96.286  1.00 54.40  ?  438 LYS   C CG  1 
ATOM   10839 C CD  . LYS   C 1 438 ? -16.186 -10.818 95.773  1.00 54.65  ?  438 LYS   C CD  1 
ATOM   10840 C CE  . LYS   C 1 438 ? -17.323 -10.649 96.769  1.00 53.25  ?  438 LYS   C CE  1 
ATOM   10841 N NZ  . LYS   C 1 438 ? -18.387 -9.752  96.226  1.00 51.07  ?  438 LYS   C NZ  1 
ATOM   10842 N N   . GLU   C 1 439 ? -15.273 -16.432 96.796  1.00 68.91  ?  439 GLU   C N   1 
ATOM   10843 C CA  . GLU   C 1 439 ? -15.495 -17.568 97.681  1.00 69.33  ?  439 GLU   C CA  1 
ATOM   10844 C C   . GLU   C 1 439 ? -14.486 -18.692 97.486  1.00 69.25  ?  439 GLU   C C   1 
ATOM   10845 O O   . GLU   C 1 439 ? -14.433 -19.608 98.313  1.00 71.44  ?  439 GLU   C O   1 
ATOM   10846 C CB  . GLU   C 1 439 ? -16.917 -18.111 97.495  1.00 72.50  ?  439 GLU   C CB  1 
ATOM   10847 C CG  . GLU   C 1 439 ? -17.999 -17.147 97.962  1.00 75.98  ?  439 GLU   C CG  1 
ATOM   10848 C CD  . GLU   C 1 439 ? -17.845 -16.759 99.428  1.00 85.25  ?  439 GLU   C CD  1 
ATOM   10849 O OE1 . GLU   C 1 439 ? -17.795 -17.666 100.290 1.00 87.43  ?  439 GLU   C OE1 1 
ATOM   10850 O OE2 . GLU   C 1 439 ? -17.765 -15.546 99.719  1.00 80.92  ?  439 GLU   C OE2 1 
ATOM   10851 N N   . LYS   C 1 440 ? -13.693 -18.652 96.420  1.00 68.44  ?  440 LYS   C N   1 
ATOM   10852 C CA  . LYS   C 1 440 ? -12.596 -19.592 96.245  1.00 66.92  ?  440 LYS   C CA  1 
ATOM   10853 C C   . LYS   C 1 440 ? -11.260 -19.020 96.694  1.00 66.49  ?  440 LYS   C C   1 
ATOM   10854 O O   . LYS   C 1 440 ? -10.264 -19.750 96.702  1.00 74.30  ?  440 LYS   C O   1 
ATOM   10855 C CB  . LYS   C 1 440 ? -12.499 -20.034 94.780  1.00 68.40  ?  440 LYS   C CB  1 
ATOM   10856 C CG  . LYS   C 1 440 ? -13.740 -20.750 94.271  1.00 76.01  ?  440 LYS   C CG  1 
ATOM   10857 C CD  . LYS   C 1 440 ? -13.700 -20.928 92.757  1.00 79.45  ?  440 LYS   C CD  1 
ATOM   10858 C CE  . LYS   C 1 440 ? -14.987 -21.564 92.245  1.00 87.47  ?  440 LYS   C CE  1 
ATOM   10859 N NZ  . LYS   C 1 440 ? -15.004 -21.673 90.758  1.00 90.68  ?  440 LYS   C NZ  1 
ATOM   10860 N N   . PHE   C 1 441 ? -11.219 -17.737 97.067  1.00 68.12  ?  441 PHE   C N   1 
ATOM   10861 C CA  . PHE   C 1 441 ? -9.963  -17.112 97.472  1.00 65.22  ?  441 PHE   C CA  1 
ATOM   10862 C C   . PHE   C 1 441 ? -9.357  -17.818 98.678  1.00 71.82  ?  441 PHE   C C   1 
ATOM   10863 O O   . PHE   C 1 441 ? -8.131  -17.927 98.791  1.00 71.67  ?  441 PHE   C O   1 
ATOM   10864 C CB  . PHE   C 1 441 ? -10.191 -15.632 97.784  1.00 61.39  ?  441 PHE   C CB  1 
ATOM   10865 C CG  . PHE   C 1 441 ? -10.170 -14.734 96.575  1.00 61.13  ?  441 PHE   C CG  1 
ATOM   10866 C CD1 . PHE   C 1 441 ? -9.378  -15.032 95.478  1.00 62.13  ?  441 PHE   C CD1 1 
ATOM   10867 C CD2 . PHE   C 1 441 ? -10.936 -13.579 96.544  1.00 58.56  ?  441 PHE   C CD2 1 
ATOM   10868 C CE1 . PHE   C 1 441 ? -9.354  -14.196 94.369  1.00 59.48  ?  441 PHE   C CE1 1 
ATOM   10869 C CE2 . PHE   C 1 441 ? -10.915 -12.740 95.435  1.00 59.76  ?  441 PHE   C CE2 1 
ATOM   10870 C CZ  . PHE   C 1 441 ? -10.126 -13.052 94.349  1.00 54.92  ?  441 PHE   C CZ  1 
ATOM   10871 N N   . ALA   C 1 442 ? -10.202 -18.310 99.588  1.00 76.74  ?  442 ALA   C N   1 
ATOM   10872 C CA  . ALA   C 1 442 ? -9.715  -18.932 100.812 1.00 76.24  ?  442 ALA   C CA  1 
ATOM   10873 C C   . ALA   C 1 442 ? -9.360  -20.406 100.638 1.00 79.18  ?  442 ALA   C C   1 
ATOM   10874 O O   . ALA   C 1 442 ? -8.677  -20.967 101.501 1.00 80.29  ?  442 ALA   C O   1 
ATOM   10875 C CB  . ALA   C 1 442 ? -10.755 -18.780 101.925 1.00 77.65  ?  442 ALA   C CB  1 
ATOM   10876 N N   . THR   C 1 443 ? -9.798  -21.045 99.554  1.00 78.38  ?  443 THR   C N   1 
ATOM   10877 C CA  . THR   C 1 443 ? -9.532  -22.461 99.329  1.00 73.07  ?  443 THR   C CA  1 
ATOM   10878 C C   . THR   C 1 443 ? -8.342  -22.709 98.408  1.00 72.70  ?  443 THR   C C   1 
ATOM   10879 O O   . THR   C 1 443 ? -8.047  -23.868 98.101  1.00 73.37  ?  443 THR   C O   1 
ATOM   10880 C CB  . THR   C 1 443 ? -10.774 -23.156 98.752  1.00 73.41  ?  443 THR   C CB  1 
ATOM   10881 O OG1 . THR   C 1 443 ? -10.991 -22.718 97.405  1.00 78.00  ?  443 THR   C OG1 1 
ATOM   10882 C CG2 . THR   C 1 443 ? -12.010 -22.847 99.593  1.00 75.38  ?  443 THR   C CG2 1 
ATOM   10883 N N   . LEU   C 1 444 ? -7.655  -21.667 97.958  1.00 74.42  ?  444 LEU   C N   1 
ATOM   10884 C CA  . LEU   C 1 444 ? -6.521  -21.840 97.063  1.00 73.31  ?  444 LEU   C CA  1 
ATOM   10885 C C   . LEU   C 1 444 ? -5.213  -21.693 97.831  1.00 73.36  ?  444 LEU   C C   1 
ATOM   10886 O O   . LEU   C 1 444 ? -5.123  -20.944 98.808  1.00 71.14  ?  444 LEU   C O   1 
ATOM   10887 C CB  . LEU   C 1 444 ? -6.581  -20.848 95.899  1.00 72.53  ?  444 LEU   C CB  1 
ATOM   10888 C CG  . LEU   C 1 444 ? -6.632  -19.343 96.163  1.00 70.76  ?  444 LEU   C CG  1 
ATOM   10889 C CD1 . LEU   C 1 444 ? -5.232  -18.745 96.183  1.00 67.83  ?  444 LEU   C CD1 1 
ATOM   10890 C CD2 . LEU   C 1 444 ? -7.491  -18.669 95.106  1.00 59.15  ?  444 LEU   C CD2 1 
ATOM   10891 N N   . LYS   C 1 445 ? -4.200  -22.421 97.375  1.00 69.74  ?  445 LYS   C N   1 
ATOM   10892 C CA  . LYS   C 1 445 ? -2.943  -22.575 98.089  1.00 72.98  ?  445 LYS   C CA  1 
ATOM   10893 C C   . LYS   C 1 445 ? -1.839  -21.766 97.416  1.00 74.25  ?  445 LYS   C C   1 
ATOM   10894 O O   . LYS   C 1 445 ? -1.899  -21.454 96.221  1.00 72.07  ?  445 LYS   C O   1 
ATOM   10895 C CB  . LYS   C 1 445 ? -2.549  -24.059 98.166  1.00 79.77  ?  445 LYS   C CB  1 
ATOM   10896 C CG  . LYS   C 1 445 ? -1.414  -24.380 99.134  1.00 82.49  ?  445 LYS   C CG  1 
ATOM   10897 C CD  . LYS   C 1 445 ? -1.715  -23.873 100.537 1.00 77.26  ?  445 LYS   C CD  1 
ATOM   10898 C CE  . LYS   C 1 445 ? -0.527  -24.077 101.459 1.00 79.72  ?  445 LYS   C CE  1 
ATOM   10899 N NZ  . LYS   C 1 445 ? -0.771  -23.497 102.807 1.00 82.48  ?  445 LYS   C NZ  1 
ATOM   10900 N N   . GLY   C 1 446 ? -0.828  -21.419 98.206  1.00 70.77  ?  446 GLY   C N   1 
ATOM   10901 C CA  . GLY   C 1 446 ? 0.320   -20.705 97.696  1.00 72.62  ?  446 GLY   C CA  1 
ATOM   10902 C C   . GLY   C 1 446 ? 1.214   -21.595 96.853  1.00 73.15  ?  446 GLY   C C   1 
ATOM   10903 O O   . GLY   C 1 446 ? 1.011   -22.802 96.714  1.00 68.05  ?  446 GLY   C O   1 
ATOM   10904 N N   . LEU   C 1 447 ? 2.240   -20.969 96.283  1.00 68.78  ?  447 LEU   C N   1 
ATOM   10905 C CA  . LEU   C 1 447 ? 3.180   -21.625 95.388  1.00 69.11  ?  447 LEU   C CA  1 
ATOM   10906 C C   . LEU   C 1 447 ? 4.563   -21.695 96.021  1.00 70.78  ?  447 LEU   C C   1 
ATOM   10907 O O   . LEU   C 1 447 ? 4.938   -20.843 96.832  1.00 70.32  ?  447 LEU   C O   1 
ATOM   10908 C CB  . LEU   C 1 447 ? 3.270   -20.884 94.048  1.00 70.52  ?  447 LEU   C CB  1 
ATOM   10909 C CG  . LEU   C 1 447 ? 2.006   -20.824 93.184  1.00 72.73  ?  447 LEU   C CG  1 
ATOM   10910 C CD1 . LEU   C 1 447 ? 2.064   -19.648 92.219  1.00 61.85  ?  447 LEU   C CD1 1 
ATOM   10911 C CD2 . LEU   C 1 447 ? 1.818   -22.128 92.422  1.00 68.31  ?  447 LEU   C CD2 1 
ATOM   10912 N N   . GLU   C 1 448 ? 5.315   -22.722 95.646  1.00 75.17  ?  448 GLU   C N   1 
ATOM   10913 C CA  . GLU   C 1 448 ? 6.728   -22.851 95.978  1.00 72.30  ?  448 GLU   C CA  1 
ATOM   10914 C C   . GLU   C 1 448 ? 7.519   -23.002 94.683  1.00 63.56  ?  448 GLU   C C   1 
ATOM   10915 O O   . GLU   C 1 448 ? 6.965   -22.938 93.584  1.00 60.22  ?  448 GLU   C O   1 
ATOM   10916 C CB  . GLU   C 1 448 ? 6.970   -24.023 96.937  1.00 62.46  ?  448 GLU   C CB  1 
ATOM   10917 C CG  . GLU   C 1 448 ? 6.506   -25.383 96.435  1.00 65.30  ?  448 GLU   C CG  1 
ATOM   10918 C CD  . GLU   C 1 448 ? 6.646   -26.470 97.493  1.00 75.81  ?  448 GLU   C CD  1 
ATOM   10919 O OE1 . GLU   C 1 448 ? 7.178   -26.174 98.584  1.00 78.67  ?  448 GLU   C OE1 1 
ATOM   10920 O OE2 . GLU   C 1 448 ? 6.218   -27.619 97.241  1.00 77.73  ?  448 GLU   C OE2 1 
ATOM   10921 N N   . PHE   C 1 449 ? 8.826   -23.206 94.814  1.00 59.58  ?  449 PHE   C N   1 
ATOM   10922 C CA  . PHE   C 1 449 ? 9.718   -23.195 93.663  1.00 62.25  ?  449 PHE   C CA  1 
ATOM   10923 C C   . PHE   C 1 449 ? 9.972   -24.605 93.143  1.00 65.52  ?  449 PHE   C C   1 
ATOM   10924 O O   . PHE   C 1 449 ? 10.288  -25.520 93.915  1.00 61.27  ?  449 PHE   C O   1 
ATOM   10925 C CB  . PHE   C 1 449 ? 11.053  -22.531 94.009  1.00 61.22  ?  449 PHE   C CB  1 
ATOM   10926 C CG  . PHE   C 1 449 ? 10.986  -21.034 94.104  1.00 56.38  ?  449 PHE   C CG  1 
ATOM   10927 C CD1 . PHE   C 1 449 ? 10.942  -20.259 92.962  1.00 60.28  ?  449 PHE   C CD1 1 
ATOM   10928 C CD2 . PHE   C 1 449 ? 10.986  -20.403 95.336  1.00 58.83  ?  449 PHE   C CD2 1 
ATOM   10929 C CE1 . PHE   C 1 449 ? 10.882  -18.883 93.048  1.00 61.88  ?  449 PHE   C CE1 1 
ATOM   10930 C CE2 . PHE   C 1 449 ? 10.931  -19.033 95.428  1.00 53.23  ?  449 PHE   C CE2 1 
ATOM   10931 C CZ  . PHE   C 1 449 ? 10.878  -18.272 94.287  1.00 58.36  ?  449 PHE   C CZ  1 
ATOM   10932 N N   . GLU   C 1 450 ? 9.819   -24.770 91.830  1.00 68.34  ?  450 GLU   C N   1 
ATOM   10933 C CA  . GLU   C 1 450 ? 10.415  -25.880 91.099  1.00 67.39  ?  450 GLU   C CA  1 
ATOM   10934 C C   . GLU   C 1 450 ? 11.738  -25.474 90.461  1.00 67.97  ?  450 GLU   C C   1 
ATOM   10935 O O   . GLU   C 1 450 ? 12.648  -26.304 90.341  1.00 72.13  ?  450 GLU   C O   1 
ATOM   10936 C CB  . GLU   C 1 450 ? 9.440   -26.391 90.029  1.00 67.32  ?  450 GLU   C CB  1 
ATOM   10937 C CG  . GLU   C 1 450 ? 10.059  -27.272 88.951  1.00 68.51  ?  450 GLU   C CG  1 
ATOM   10938 C CD  . GLU   C 1 450 ? 9.164   -27.419 87.725  1.00 73.71  ?  450 GLU   C CD  1 
ATOM   10939 O OE1 . GLU   C 1 450 ? 7.927   -27.292 87.866  1.00 75.73  ?  450 GLU   C OE1 1 
ATOM   10940 O OE2 . GLU   C 1 450 ? 9.700   -27.655 86.617  1.00 67.46  ?  450 GLU   C OE2 1 
ATOM   10941 N N   . TYR   C 1 451 ? 11.869  -24.200 90.086  1.00 62.91  ?  451 TYR   C N   1 
ATOM   10942 C CA  . TYR   C 1 451 ? 13.071  -23.664 89.461  1.00 60.06  ?  451 TYR   C CA  1 
ATOM   10943 C C   . TYR   C 1 451 ? 13.172  -22.186 89.810  1.00 61.31  ?  451 TYR   C C   1 
ATOM   10944 O O   . TYR   C 1 451 ? 12.201  -21.446 89.633  1.00 62.99  ?  451 TYR   C O   1 
ATOM   10945 C CB  . TYR   C 1 451 ? 13.025  -23.864 87.942  1.00 57.37  ?  451 TYR   C CB  1 
ATOM   10946 C CG  . TYR   C 1 451 ? 14.053  -23.078 87.157  1.00 60.56  ?  451 TYR   C CG  1 
ATOM   10947 C CD1 . TYR   C 1 451 ? 15.400  -23.423 87.188  1.00 64.54  ?  451 TYR   C CD1 1 
ATOM   10948 C CD2 . TYR   C 1 451 ? 13.673  -22.001 86.363  1.00 65.88  ?  451 TYR   C CD2 1 
ATOM   10949 C CE1 . TYR   C 1 451 ? 16.344  -22.706 86.462  1.00 64.28  ?  451 TYR   C CE1 1 
ATOM   10950 C CE2 . TYR   C 1 451 ? 14.607  -21.280 85.632  1.00 64.40  ?  451 TYR   C CE2 1 
ATOM   10951 C CZ  . TYR   C 1 451 ? 15.940  -21.637 85.685  1.00 66.65  ?  451 TYR   C CZ  1 
ATOM   10952 O OH  . TYR   C 1 451 ? 16.867  -20.920 84.960  1.00 69.97  ?  451 TYR   C OH  1 
ATOM   10953 N N   . GLU   C 1 452 ? 14.334  -21.757 90.316  1.00 57.29  ?  452 GLU   C N   1 
ATOM   10954 C CA  . GLU   C 1 452 ? 14.500  -20.345 90.646  1.00 52.58  ?  452 GLU   C CA  1 
ATOM   10955 C C   . GLU   C 1 452 ? 15.853  -19.816 90.186  1.00 51.71  ?  452 GLU   C C   1 
ATOM   10956 O O   . GLU   C 1 452 ? 16.896  -20.329 90.609  1.00 54.98  ?  452 GLU   C O   1 
ATOM   10957 C CB  . GLU   C 1 452 ? 14.335  -20.119 92.147  1.00 49.87  ?  452 GLU   C CB  1 
ATOM   10958 C CG  . GLU   C 1 452 ? 14.427  -18.655 92.553  1.00 52.40  ?  452 GLU   C CG  1 
ATOM   10959 C CD  . GLU   C 1 452 ? 14.207  -18.443 94.040  1.00 59.32  ?  452 GLU   C CD  1 
ATOM   10960 O OE1 . GLU   C 1 452 ? 13.950  -19.439 94.749  1.00 56.81  ?  452 GLU   C OE1 1 
ATOM   10961 O OE2 . GLU   C 1 452 ? 14.291  -17.282 94.498  1.00 55.59  ?  452 GLU   C OE2 1 
ATOM   10962 N N   . PRO   C 1 453 ? 15.877  -18.802 89.326  1.00 49.44  ?  453 PRO   C N   1 
ATOM   10963 C CA  . PRO   C 1 453 ? 17.151  -18.212 88.899  1.00 59.90  ?  453 PRO   C CA  1 
ATOM   10964 C C   . PRO   C 1 453 ? 17.677  -17.239 89.940  1.00 65.28  ?  453 PRO   C C   1 
ATOM   10965 O O   . PRO   C 1 453 ? 16.941  -16.837 90.855  1.00 48.24  ?  453 PRO   C O   1 
ATOM   10966 C CB  . PRO   C 1 453 ? 16.788  -17.493 87.587  1.00 61.26  ?  453 PRO   C CB  1 
ATOM   10967 C CG  . PRO   C 1 453 ? 15.441  -18.036 87.190  1.00 55.08  ?  453 PRO   C CG  1 
ATOM   10968 C CD  . PRO   C 1 453 ? 14.761  -18.344 88.488  1.00 55.88  ?  453 PRO   C CD  1 
ATOM   10969 N N   . PRO   C 1 454 ? 18.951  -16.836 89.837  1.00 80.28  ?  454 PRO   C N   1 
ATOM   10970 C CA  . PRO   C 1 454 ? 19.529  -15.993 90.899  1.00 77.67  ?  454 PRO   C CA  1 
ATOM   10971 C C   . PRO   C 1 454 ? 19.028  -14.557 90.900  1.00 76.29  ?  454 PRO   C C   1 
ATOM   10972 O O   . PRO   C 1 454 ? 18.888  -13.969 91.980  1.00 81.02  ?  454 PRO   C O   1 
ATOM   10973 C CB  . PRO   C 1 454 ? 21.040  -16.064 90.621  1.00 77.41  ?  454 PRO   C CB  1 
ATOM   10974 C CG  . PRO   C 1 454 ? 21.224  -17.273 89.764  1.00 79.59  ?  454 PRO   C CG  1 
ATOM   10975 C CD  . PRO   C 1 454 ? 19.988  -17.349 88.926  1.00 77.72  ?  454 PRO   C CD  1 
ATOM   10976 N N   . VAL   C 1 455 ? 18.774  -13.960 89.736  1.00 57.95  ?  455 VAL   C N   1 
ATOM   10977 C CA  . VAL   C 1 455 ? 18.363  -12.561 89.653  1.00 55.60  ?  455 VAL   C CA  1 
ATOM   10978 C C   . VAL   C 1 455 ? 17.166  -12.438 88.718  1.00 50.19  ?  455 VAL   C C   1 
ATOM   10979 O O   . VAL   C 1 455 ? 17.084  -13.139 87.702  1.00 53.20  ?  455 VAL   C O   1 
ATOM   10980 C CB  . VAL   C 1 455 ? 19.513  -11.641 89.182  1.00 53.54  ?  455 VAL   C CB  1 
ATOM   10981 C CG1 . VAL   C 1 455 ? 20.588  -11.510 90.257  1.00 48.26  ?  455 VAL   C CG1 1 
ATOM   10982 C CG2 . VAL   C 1 455 ? 20.106  -12.150 87.876  1.00 50.72  ?  455 VAL   C CG2 1 
ATOM   10983 N N   . LEU   C 1 456 ? 16.247  -11.532 89.068  1.00 51.22  ?  456 LEU   C N   1 
ATOM   10984 C CA  . LEU   C 1 456 ? 15.015  -11.256 88.322  1.00 49.86  ?  456 LEU   C CA  1 
ATOM   10985 C C   . LEU   C 1 456 ? 14.258  -12.551 88.017  1.00 48.08  ?  456 LEU   C C   1 
ATOM   10986 O O   . LEU   C 1 456 ? 13.940  -12.877 86.873  1.00 49.99  ?  456 LEU   C O   1 
ATOM   10987 C CB  . LEU   C 1 456 ? 15.313  -10.458 87.044  1.00 52.12  ?  456 LEU   C CB  1 
ATOM   10988 C CG  . LEU   C 1 456 ? 15.659  -8.966  87.198  1.00 51.15  ?  456 LEU   C CG  1 
ATOM   10989 C CD1 . LEU   C 1 456 ? 17.092  -8.746  87.657  1.00 49.32  ?  456 LEU   C CD1 1 
ATOM   10990 C CD2 . LEU   C 1 456 ? 15.413  -8.208  85.912  1.00 47.26  ?  456 LEU   C CD2 1 
ATOM   10991 N N   . ARG   C 1 457 ? 13.959  -13.287 89.087  1.00 52.57  ?  457 ARG   C N   1 
ATOM   10992 C CA  . ARG   C 1 457 ? 13.391  -14.625 88.964  1.00 48.92  ?  457 ARG   C CA  1 
ATOM   10993 C C   . ARG   C 1 457 ? 11.964  -14.615 88.437  1.00 49.79  ?  457 ARG   C C   1 
ATOM   10994 O O   . ARG   C 1 457 ? 11.529  -15.619 87.864  1.00 51.12  ?  457 ARG   C O   1 
ATOM   10995 C CB  . ARG   C 1 457 ? 13.426  -15.324 90.320  1.00 49.06  ?  457 ARG   C CB  1 
ATOM   10996 C CG  . ARG   C 1 457 ? 12.592  -14.615 91.370  1.00 46.96  ?  457 ARG   C CG  1 
ATOM   10997 C CD  . ARG   C 1 457 ? 12.832  -15.162 92.760  1.00 45.50  ?  457 ARG   C CD  1 
ATOM   10998 N NE  . ARG   C 1 457 ? 11.920  -14.551 93.715  1.00 46.22  ?  457 ARG   C NE  1 
ATOM   10999 C CZ  . ARG   C 1 457 ? 11.966  -14.739 95.025  1.00 55.60  ?  457 ARG   C CZ  1 
ATOM   11000 N NH1 . ARG   C 1 457 ? 12.889  -15.511 95.580  1.00 51.77  ?  457 ARG   C NH1 1 
ATOM   11001 N NH2 . ARG   C 1 457 ? 11.061  -14.141 95.798  1.00 55.69  ?  457 ARG   C NH2 1 
ATOM   11002 N N   . HIS   C 1 458 ? 11.236  -13.505 88.613  1.00 58.16  ?  458 HIS   C N   1 
ATOM   11003 C CA  . HIS   C 1 458 ? 9.815   -13.442 88.265  1.00 58.34  ?  458 HIS   C CA  1 
ATOM   11004 C C   . HIS   C 1 458 ? 9.565   -13.635 86.773  1.00 50.39  ?  458 HIS   C C   1 
ATOM   11005 O O   . HIS   C 1 458 ? 8.432   -13.934 86.375  1.00 45.74  ?  458 HIS   C O   1 
ATOM   11006 C CB  . HIS   C 1 458 ? 9.216   -12.108 88.741  1.00 56.75  ?  458 HIS   C CB  1 
ATOM   11007 C CG  . HIS   C 1 458 ? 9.924   -10.890 88.219  1.00 58.61  ?  458 HIS   C CG  1 
ATOM   11008 N ND1 . HIS   C 1 458 ? 11.246  -10.613 88.499  1.00 57.72  ?  458 HIS   C ND1 1 
ATOM   11009 C CD2 . HIS   C 1 458 ? 9.482   -9.861  87.456  1.00 53.56  ?  458 HIS   C CD2 1 
ATOM   11010 C CE1 . HIS   C 1 458 ? 11.590  -9.476  87.922  1.00 53.65  ?  458 HIS   C CE1 1 
ATOM   11011 N NE2 . HIS   C 1 458 ? 10.537  -8.998  87.285  1.00 53.79  ?  458 HIS   C NE2 1 
ATOM   11012 N N   . PHE   C 1 459 ? 10.599  -13.487 85.946  1.00 45.81  ?  459 PHE   C N   1 
ATOM   11013 C CA  . PHE   C 1 459 ? 10.471  -13.706 84.510  1.00 45.02  ?  459 PHE   C CA  1 
ATOM   11014 C C   . PHE   C 1 459 ? 10.459  -15.192 84.149  1.00 50.71  ?  459 PHE   C C   1 
ATOM   11015 O O   . PHE   C 1 459 ? 9.748   -15.601 83.221  1.00 42.46  ?  459 PHE   C O   1 
ATOM   11016 C CB  . PHE   C 1 459 ? 11.620  -13.013 83.784  1.00 39.78  ?  459 PHE   C CB  1 
ATOM   11017 C CG  . PHE   C 1 459 ? 11.587  -11.516 83.863  1.00 38.14  ?  459 PHE   C CG  1 
ATOM   11018 C CD1 . PHE   C 1 459 ? 10.404  -10.818 83.722  1.00 41.43  ?  459 PHE   C CD1 1 
ATOM   11019 C CD2 . PHE   C 1 459 ? 12.756  -10.803 84.052  1.00 45.76  ?  459 PHE   C CD2 1 
ATOM   11020 C CE1 . PHE   C 1 459 ? 10.387  -9.430  83.773  1.00 39.59  ?  459 PHE   C CE1 1 
ATOM   11021 C CE2 . PHE   C 1 459 ? 12.744  -9.421  84.106  1.00 42.60  ?  459 PHE   C CE2 1 
ATOM   11022 C CZ  . PHE   C 1 459 ? 11.561  -8.738  83.969  1.00 39.98  ?  459 PHE   C CZ  1 
ATOM   11023 N N   . THR   C 1 460 ? 11.253  -16.011 84.863  1.00 50.63  ?  460 THR   C N   1 
ATOM   11024 C CA  . THR   C 1 460 ? 11.537  -17.377 84.435  1.00 46.56  ?  460 THR   C CA  1 
ATOM   11025 C C   . THR   C 1 460 ? 11.511  -18.420 85.548  1.00 51.75  ?  460 THR   C C   1 
ATOM   11026 O O   . THR   C 1 460 ? 11.771  -19.595 85.263  1.00 52.10  ?  460 THR   C O   1 
ATOM   11027 C CB  . THR   C 1 460 ? 12.914  -17.442 83.747  1.00 45.12  ?  460 THR   C CB  1 
ATOM   11028 O OG1 . THR   C 1 460 ? 13.885  -16.786 84.570  1.00 42.40  ?  460 THR   C OG1 1 
ATOM   11029 C CG2 . THR   C 1 460 ? 12.876  -16.773 82.381  1.00 38.42  ?  460 THR   C CG2 1 
ATOM   11030 N N   . ALA   C 1 461 ? 11.232  -18.048 86.794  1.00 49.07  ?  461 ALA   C N   1 
ATOM   11031 C CA  . ALA   C 1 461 ? 11.135  -19.057 87.839  1.00 50.97  ?  461 ALA   C CA  1 
ATOM   11032 C C   . ALA   C 1 461 ? 9.906   -19.926 87.610  1.00 58.53  ?  461 ALA   C C   1 
ATOM   11033 O O   . ALA   C 1 461 ? 8.822   -19.432 87.283  1.00 56.41  ?  461 ALA   C O   1 
ATOM   11034 C CB  . ALA   C 1 461 ? 11.069  -18.413 89.224  1.00 50.84  ?  461 ALA   C CB  1 
ATOM   11035 N N   . ARG   C 1 462 ? 10.080  -21.232 87.772  1.00 61.02  ?  462 ARG   C N   1 
ATOM   11036 C CA  . ARG   C 1 462 ? 8.997   -22.191 87.602  1.00 60.21  ?  462 ARG   C CA  1 
ATOM   11037 C C   . ARG   C 1 462 ? 8.473   -22.587 88.976  1.00 60.04  ?  462 ARG   C C   1 
ATOM   11038 O O   . ARG   C 1 462 ? 9.205   -23.164 89.786  1.00 61.25  ?  462 ARG   C O   1 
ATOM   11039 C CB  . ARG   C 1 462 ? 9.471   -23.410 86.811  1.00 60.39  ?  462 ARG   C CB  1 
ATOM   11040 C CG  . ARG   C 1 462 ? 9.922   -23.069 85.389  1.00 51.65  ?  462 ARG   C CG  1 
ATOM   11041 C CD  . ARG   C 1 462 ? 10.134  -24.320 84.568  1.00 51.86  ?  462 ARG   C CD  1 
ATOM   11042 N NE  . ARG   C 1 462 ? 8.951   -25.171 84.582  1.00 51.01  ?  462 ARG   C NE  1 
ATOM   11043 C CZ  . ARG   C 1 462 ? 7.948   -25.071 83.721  1.00 53.78  ?  462 ARG   C CZ  1 
ATOM   11044 N NH1 . ARG   C 1 462 ? 7.963   -24.178 82.742  1.00 52.28  ?  462 ARG   C NH1 1 
ATOM   11045 N NH2 . ARG   C 1 462 ? 6.904   -25.885 83.845  1.00 54.31  ?  462 ARG   C NH2 1 
ATOM   11046 N N   . LEU   C 1 463 ? 7.215   -22.262 89.239  1.00 62.24  ?  463 LEU   C N   1 
ATOM   11047 C CA  . LEU   C 1 463 ? 6.606   -22.483 90.538  1.00 61.94  ?  463 LEU   C CA  1 
ATOM   11048 C C   . LEU   C 1 463 ? 5.740   -23.738 90.523  1.00 62.99  ?  463 LEU   C C   1 
ATOM   11049 O O   . LEU   C 1 463 ? 5.529   -24.378 89.491  1.00 59.40  ?  463 LEU   C O   1 
ATOM   11050 C CB  . LEU   C 1 463 ? 5.776   -21.266 90.952  1.00 65.74  ?  463 LEU   C CB  1 
ATOM   11051 C CG  . LEU   C 1 463 ? 6.512   -19.926 90.912  1.00 61.65  ?  463 LEU   C CG  1 
ATOM   11052 C CD1 . LEU   C 1 463 ? 5.595   -18.799 91.376  1.00 64.47  ?  463 LEU   C CD1 1 
ATOM   11053 C CD2 . LEU   C 1 463 ? 7.773   -19.991 91.752  1.00 52.90  ?  463 LEU   C CD2 1 
ATOM   11054 N N   . LYS   C 1 464 ? 5.231   -24.085 91.706  1.00 70.49  ?  464 LYS   C N   1 
ATOM   11055 C CA  . LYS   C 1 464 ? 4.421   -25.281 91.849  1.00 70.92  ?  464 LYS   C CA  1 
ATOM   11056 C C   . LYS   C 1 464 ? 3.520   -25.093 93.054  1.00 70.53  ?  464 LYS   C C   1 
ATOM   11057 O O   . LYS   C 1 464 ? 3.967   -24.518 94.055  1.00 72.68  ?  464 LYS   C O   1 
ATOM   11058 C CB  . LYS   C 1 464 ? 5.301   -26.527 92.015  1.00 71.55  ?  464 LYS   C CB  1 
ATOM   11059 C CG  . LYS   C 1 464 ? 4.546   -27.846 91.982  1.00 80.63  ?  464 LYS   C CG  1 
ATOM   11060 C CD  . LYS   C 1 464 ? 5.477   -29.029 92.213  1.00 85.21  ?  464 LYS   C CD  1 
ATOM   11061 C CE  . LYS   C 1 464 ? 4.707   -30.344 92.195  1.00 93.04  ?  464 LYS   C CE  1 
ATOM   11062 N NZ  . LYS   C 1 464 ? 5.563   -31.513 92.543  1.00 94.01  ?  464 LYS   C NZ  1 
ATOM   11063 N N   . PRO   C 1 465 ? 2.256   -25.513 92.989  1.00 71.91  ?  465 PRO   C N   1 
ATOM   11064 C CA  . PRO   C 1 465 ? 1.401   -25.467 94.181  1.00 78.38  ?  465 PRO   C CA  1 
ATOM   11065 C C   . PRO   C 1 465 ? 1.918   -26.377 95.289  1.00 76.39  ?  465 PRO   C C   1 
ATOM   11066 O O   . PRO   C 1 465 ? 2.760   -27.254 95.078  1.00 70.77  ?  465 PRO   C O   1 
ATOM   11067 C CB  . PRO   C 1 465 ? 0.039   -25.940 93.657  1.00 71.49  ?  465 PRO   C CB  1 
ATOM   11068 C CG  . PRO   C 1 465 ? 0.061   -25.576 92.205  1.00 66.65  ?  465 PRO   C CG  1 
ATOM   11069 C CD  . PRO   C 1 465 ? 1.484   -25.791 91.766  1.00 65.91  ?  465 PRO   C CD  1 
ATOM   11070 N N   . ILE   C 1 466 ? 1.396   -26.149 96.492  1.00 73.31  ?  466 ILE   C N   1 
ATOM   11071 C CA  . ILE   C 1 466 ? 1.824   -26.901 97.667  1.00 83.84  ?  466 ILE   C CA  1 
ATOM   11072 C C   . ILE   C 1 466 ? 0.712   -27.837 98.132  1.00 87.90  ?  466 ILE   C C   1 
ATOM   11073 O O   . ILE   C 1 466 ? -0.195  -27.431 98.858  1.00 91.57  ?  466 ILE   C O   1 
ATOM   11074 C CB  . ILE   C 1 466 ? 2.260   -25.957 98.809  1.00 82.51  ?  466 ILE   C CB  1 
ATOM   11075 C CG1 . ILE   C 1 466 ? 3.239   -24.899 98.292  1.00 80.77  ?  466 ILE   C CG1 1 
ATOM   11076 C CG2 . ILE   C 1 466 ? 2.903   -26.748 99.936  1.00 83.63  ?  466 ILE   C CG2 1 
ATOM   11077 C CD1 . ILE   C 1 466 ? 3.729   -23.938 99.360  1.00 75.24  ?  466 ILE   C CD1 1 
ATOM   11078 N N   . ALA   D 1 2   ? 31.014  -4.469  31.569  1.00 34.85  ?  2   ALA   D N   1 
ATOM   11079 C CA  . ALA   D 1 2   ? 30.191  -4.716  32.756  1.00 32.83  ?  2   ALA   D CA  1 
ATOM   11080 C C   . ALA   D 1 2   ? 28.887  -5.412  32.366  1.00 31.02  ?  2   ALA   D C   1 
ATOM   11081 O O   . ALA   D 1 2   ? 28.411  -5.261  31.242  1.00 30.36  ?  2   ALA   D O   1 
ATOM   11082 C CB  . ALA   D 1 2   ? 29.910  -3.413  33.490  1.00 28.63  ?  2   ALA   D CB  1 
ATOM   11083 N N   . LYS   D 1 3   ? 28.320  -6.187  33.287  1.00 25.08  ?  3   LYS   D N   1 
ATOM   11084 C CA  . LYS   D 1 3   ? 27.140  -6.997  33.004  1.00 27.84  ?  3   LYS   D CA  1 
ATOM   11085 C C   . LYS   D 1 3   ? 25.999  -6.591  33.923  1.00 30.11  ?  3   LYS   D C   1 
ATOM   11086 O O   . LYS   D 1 3   ? 26.108  -6.716  35.149  1.00 29.78  ?  3   LYS   D O   1 
ATOM   11087 C CB  . LYS   D 1 3   ? 27.431  -8.490  33.177  1.00 29.46  ?  3   LYS   D CB  1 
ATOM   11088 C CG  . LYS   D 1 3   ? 26.260  -9.368  32.759  1.00 33.33  ?  3   LYS   D CG  1 
ATOM   11089 C CD  . LYS   D 1 3   ? 26.642  -10.829 32.658  1.00 36.14  ?  3   LYS   D CD  1 
ATOM   11090 C CE  . LYS   D 1 3   ? 26.527  -11.523 33.998  1.00 40.83  ?  3   LYS   D CE  1 
ATOM   11091 N NZ  . LYS   D 1 3   ? 26.631  -13.005 33.853  1.00 50.94  ?  3   LYS   D NZ  1 
ATOM   11092 N N   . ARG   D 1 4   ? 24.901  -6.131  33.334  1.00 26.19  ?  4   ARG   D N   1 
ATOM   11093 C CA  A ARG   D 1 4   ? 23.707  -5.815  34.102  0.52 25.48  ?  4   ARG   D CA  1 
ATOM   11094 C CA  B ARG   D 1 4   ? 23.710  -5.822  34.109  0.48 25.48  ?  4   ARG   D CA  1 
ATOM   11095 C C   . ARG   D 1 4   ? 22.904  -7.091  34.344  1.00 26.57  ?  4   ARG   D C   1 
ATOM   11096 O O   . ARG   D 1 4   ? 22.656  -7.862  33.413  1.00 25.96  ?  4   ARG   D O   1 
ATOM   11097 C CB  A ARG   D 1 4   ? 22.855  -4.783  33.362  0.52 27.49  ?  4   ARG   D CB  1 
ATOM   11098 C CB  B ARG   D 1 4   ? 22.866  -4.778  33.387  0.48 27.47  ?  4   ARG   D CB  1 
ATOM   11099 C CG  A ARG   D 1 4   ? 23.619  -3.623  32.716  0.52 25.33  ?  4   ARG   D CG  1 
ATOM   11100 C CG  B ARG   D 1 4   ? 23.426  -3.381  33.484  0.48 25.88  ?  4   ARG   D CG  1 
ATOM   11101 C CD  A ARG   D 1 4   ? 22.638  -2.753  31.927  0.52 26.06  ?  4   ARG   D CD  1 
ATOM   11102 C CD  B ARG   D 1 4   ? 22.774  -2.470  32.470  0.48 26.18  ?  4   ARG   D CD  1 
ATOM   11103 N NE  A ARG   D 1 4   ? 23.262  -1.724  31.100  0.52 27.45  ?  4   ARG   D NE  1 
ATOM   11104 N NE  B ARG   D 1 4   ? 22.855  -1.072  32.870  0.48 26.25  ?  4   ARG   D NE  1 
ATOM   11105 C CZ  A ARG   D 1 4   ? 23.376  -0.449  31.446  0.52 25.90  ?  4   ARG   D CZ  1 
ATOM   11106 C CZ  B ARG   D 1 4   ? 21.825  -0.357  33.301  0.48 23.49  ?  4   ARG   D CZ  1 
ATOM   11107 N NH1 A ARG   D 1 4   ? 22.952  -0.012  32.621  0.52 26.49  ?  4   ARG   D NH1 1 
ATOM   11108 N NH1 B ARG   D 1 4   ? 20.609  -0.870  33.374  0.48 24.03  ?  4   ARG   D NH1 1 
ATOM   11109 N NH2 A ARG   D 1 4   ? 23.931  0.410   30.594  0.52 25.50  ?  4   ARG   D NH2 1 
ATOM   11110 N NH2 B ARG   D 1 4   ? 22.020  0.907   33.660  0.48 23.84  ?  4   ARG   D NH2 1 
ATOM   11111 N N   . ILE   D 1 5   ? 22.499  -7.314  35.592  1.00 28.64  ?  5   ILE   D N   1 
ATOM   11112 C CA  . ILE   D 1 5   ? 21.698  -8.477  35.970  1.00 26.36  ?  5   ILE   D CA  1 
ATOM   11113 C C   . ILE   D 1 5   ? 20.319  -7.998  36.408  1.00 24.51  ?  5   ILE   D C   1 
ATOM   11114 O O   . ILE   D 1 5   ? 20.202  -7.129  37.280  1.00 25.84  ?  5   ILE   D O   1 
ATOM   11115 C CB  . ILE   D 1 5   ? 22.389  -9.301  37.072  1.00 28.22  ?  5   ILE   D CB  1 
ATOM   11116 C CG1 . ILE   D 1 5   ? 23.718  -9.854  36.541  1.00 29.22  ?  5   ILE   D CG1 1 
ATOM   11117 C CG2 . ILE   D 1 5   ? 21.486  -10.435 37.527  1.00 22.10  ?  5   ILE   D CG2 1 
ATOM   11118 C CD1 . ILE   D 1 5   ? 24.643  -10.386 37.614  1.00 25.50  ?  5   ILE   D CD1 1 
ATOM   11119 N N   . VAL   D 1 6   ? 19.277  -8.573  35.803  1.00 23.16  ?  6   VAL   D N   1 
ATOM   11120 C CA  . VAL   D 1 6   ? 17.911  -8.093  35.990  1.00 27.74  ?  6   VAL   D CA  1 
ATOM   11121 C C   . VAL   D 1 6   ? 17.415  -8.435  37.394  1.00 23.02  ?  6   VAL   D C   1 
ATOM   11122 O O   . VAL   D 1 6   ? 17.869  -9.396  38.027  1.00 21.48  ?  6   VAL   D O   1 
ATOM   11123 C CB  . VAL   D 1 6   ? 16.990  -8.677  34.896  1.00 26.81  ?  6   VAL   D CB  1 
ATOM   11124 C CG1 . VAL   D 1 6   ? 16.842  -10.190 35.044  1.00 22.45  ?  6   VAL   D CG1 1 
ATOM   11125 C CG2 . VAL   D 1 6   ? 15.627  -8.005  34.910  1.00 21.47  ?  6   VAL   D CG2 1 
ATOM   11126 N N   . GLU   D 1 7   ? 16.496  -7.615  37.896  1.00 23.65  ?  7   GLU   D N   1 
ATOM   11127 C CA  . GLU   D 1 7   ? 15.917  -7.831  39.217  1.00 23.20  ?  7   GLU   D CA  1 
ATOM   11128 C C   . GLU   D 1 7   ? 15.088  -9.111  39.227  1.00 23.06  ?  7   GLU   D C   1 
ATOM   11129 O O   . GLU   D 1 7   ? 14.262  -9.313  38.333  1.00 25.99  ?  7   GLU   D O   1 
ATOM   11130 C CB  . GLU   D 1 7   ? 15.030  -6.648  39.598  1.00 24.16  ?  7   GLU   D CB  1 
ATOM   11131 C CG  . GLU   D 1 7   ? 15.760  -5.352  39.912  1.00 19.13  ?  7   GLU   D CG  1 
ATOM   11132 C CD  . GLU   D 1 7   ? 16.381  -4.665  38.694  1.00 24.48  ?  7   GLU   D CD  1 
ATOM   11133 O OE1 . GLU   D 1 7   ? 16.098  -5.050  37.534  1.00 25.25  ?  7   GLU   D OE1 1 
ATOM   11134 O OE2 . GLU   D 1 7   ? 17.161  -3.715  38.911  1.00 26.40  ?  7   GLU   D OE2 1 
ATOM   11135 N N   . PRO   D 1 8   ? 15.263  -9.992  40.213  1.00 18.62  ?  8   PRO   D N   1 
ATOM   11136 C CA  . PRO   D 1 8   ? 14.351  -11.137 40.325  1.00 18.89  ?  8   PRO   D CA  1 
ATOM   11137 C C   . PRO   D 1 8   ? 13.076  -10.765 41.077  1.00 17.18  ?  8   PRO   D C   1 
ATOM   11138 O O   . PRO   D 1 8   ? 12.558  -11.531 41.897  1.00 18.58  ?  8   PRO   D O   1 
ATOM   11139 C CB  . PRO   D 1 8   ? 15.190  -12.165 41.081  1.00 18.07  ?  8   PRO   D CB  1 
ATOM   11140 C CG  . PRO   D 1 8   ? 16.025  -11.307 41.999  1.00 18.97  ?  8   PRO   D CG  1 
ATOM   11141 C CD  . PRO   D 1 8   ? 16.353  -10.059 41.200  1.00 20.38  ?  8   PRO   D CD  1 
ATOM   11142 N N   . PHE   D 1 9   ? 12.570  -9.570  40.797  1.00 17.79  ?  9   PHE   D N   1 
ATOM   11143 C CA  . PHE   D 1 9   ? 11.381  -9.022  41.433  1.00 16.67  ?  9   PHE   D CA  1 
ATOM   11144 C C   . PHE   D 1 9   ? 10.915  -7.864  40.570  1.00 16.92  ?  9   PHE   D C   1 
ATOM   11145 O O   . PHE   D 1 9   ? 11.548  -7.520  39.568  1.00 20.69  ?  9   PHE   D O   1 
ATOM   11146 C CB  . PHE   D 1 9   ? 11.660  -8.568  42.874  1.00 15.16  ?  9   PHE   D CB  1 
ATOM   11147 C CG  . PHE   D 1 9   ? 12.830  -7.620  43.002  1.00 18.80  ?  9   PHE   D CG  1 
ATOM   11148 C CD1 . PHE   D 1 9   ? 12.697  -6.273  42.683  1.00 19.23  ?  9   PHE   D CD1 1 
ATOM   11149 C CD2 . PHE   D 1 9   ? 14.065  -8.079  43.440  1.00 18.10  ?  9   PHE   D CD2 1 
ATOM   11150 C CE1 . PHE   D 1 9   ? 13.777  -5.405  42.797  1.00 18.58  ?  9   PHE   D CE1 1 
ATOM   11151 C CE2 . PHE   D 1 9   ? 15.144  -7.212  43.555  1.00 18.41  ?  9   PHE   D CE2 1 
ATOM   11152 C CZ  . PHE   D 1 9   ? 14.994  -5.874  43.229  1.00 17.46  ?  9   PHE   D CZ  1 
ATOM   11153 N N   . ARG   D 1 10  ? 9.804   -7.259  40.960  1.00 17.58  ?  10  ARG   D N   1 
ATOM   11154 C CA  . ARG   D 1 10  ? 9.359   -6.037  40.315  1.00 15.69  ?  10  ARG   D CA  1 
ATOM   11155 C C   . ARG   D 1 10  ? 8.951   -5.062  41.408  1.00 18.22  ?  10  ARG   D C   1 
ATOM   11156 O O   . ARG   D 1 10  ? 8.849   -5.419  42.586  1.00 13.92  ?  10  ARG   D O   1 
ATOM   11157 C CB  . ARG   D 1 10  ? 8.225   -6.289  39.302  1.00 17.53  ?  10  ARG   D CB  1 
ATOM   11158 C CG  . ARG   D 1 10  ? 6.939   -6.846  39.865  1.00 16.24  ?  10  ARG   D CG  1 
ATOM   11159 C CD  . ARG   D 1 10  ? 6.016   -7.334  38.753  1.00 20.38  ?  10  ARG   D CD  1 
ATOM   11160 N NE  . ARG   D 1 10  ? 4.749   -7.815  39.296  1.00 22.37  ?  10  ARG   D NE  1 
ATOM   11161 C CZ  . ARG   D 1 10  ? 3.988   -8.739  38.726  1.00 24.77  ?  10  ARG   D CZ  1 
ATOM   11162 N NH1 . ARG   D 1 10  ? 4.347   -9.335  37.599  1.00 25.95  ?  10  ARG   D NH1 1 
ATOM   11163 N NH2 . ARG   D 1 10  ? 2.836   -9.075  39.302  1.00 27.21  ?  10  ARG   D NH2 1 
ATOM   11164 N N   . ILE   D 1 11  ? 8.757   -3.812  41.012  1.00 16.92  ?  11  ILE   D N   1 
ATOM   11165 C CA  . ILE   D 1 11  ? 8.564   -2.744  41.982  1.00 15.00  ?  11  ILE   D CA  1 
ATOM   11166 C C   . ILE   D 1 11  ? 7.100   -2.731  42.391  1.00 14.73  ?  11  ILE   D C   1 
ATOM   11167 O O   . ILE   D 1 11  ? 6.206   -2.808  41.542  1.00 16.64  ?  11  ILE   D O   1 
ATOM   11168 C CB  . ILE   D 1 11  ? 9.005   -1.395  41.389  1.00 18.37  ?  11  ILE   D CB  1 
ATOM   11169 C CG1 . ILE   D 1 11  ? 10.474  -1.468  40.943  1.00 16.15  ?  11  ILE   D CG1 1 
ATOM   11170 C CG2 . ILE   D 1 11  ? 8.772   -0.259  42.378  1.00 15.97  ?  11  ILE   D CG2 1 
ATOM   11171 C CD1 . ILE   D 1 11  ? 10.931  -0.287  40.122  1.00 17.07  ?  11  ILE   D CD1 1 
ATOM   11172 N N   . LYS   D 1 12  ? 6.844   -2.679  43.691  1.00 17.42  ?  12  LYS   D N   1 
ATOM   11173 C CA  . LYS   D 1 12  ? 5.473   -2.543  44.156  1.00 20.05  ?  12  LYS   D CA  1 
ATOM   11174 C C   . LYS   D 1 12  ? 5.205   -1.205  44.820  1.00 18.47  ?  12  LYS   D C   1 
ATOM   11175 O O   . LYS   D 1 12  ? 4.064   -0.752  44.816  1.00 17.42  ?  12  LYS   D O   1 
ATOM   11176 C CB  . LYS   D 1 12  ? 5.113   -3.676  45.129  1.00 20.12  ?  12  LYS   D CB  1 
ATOM   11177 C CG  . LYS   D 1 12  ? 3.602   -3.929  45.236  1.00 22.95  ?  12  LYS   D CG  1 
ATOM   11178 C CD  . LYS   D 1 12  ? 3.285   -5.213  45.993  1.00 26.45  ?  12  LYS   D CD  1 
ATOM   11179 C CE  . LYS   D 1 12  ? 1.770   -5.467  46.076  1.00 30.02  ?  12  LYS   D CE  1 
ATOM   11180 N NZ  . LYS   D 1 12  ? 1.474   -6.880  46.474  1.00 23.24  ?  12  LYS   D NZ  1 
ATOM   11181 N N   . MET   D 1 13  ? 6.227   -0.558  45.377  1.00 15.85  ?  13  MET   D N   1 
ATOM   11182 C CA  . MET   D 1 13  ? 6.053   0.767   45.950  1.00 15.10  ?  13  MET   D CA  1 
ATOM   11183 C C   . MET   D 1 13  ? 7.320   1.573   45.708  1.00 15.70  ?  13  MET   D C   1 
ATOM   11184 O O   . MET   D 1 13  ? 8.428   1.042   45.796  1.00 17.51  ?  13  MET   D O   1 
ATOM   11185 C CB  . MET   D 1 13  ? 5.723   0.696   47.446  1.00 14.84  ?  13  MET   D CB  1 
ATOM   11186 C CG  . MET   D 1 13  ? 5.331   2.033   48.074  1.00 15.17  ?  13  MET   D CG  1 
ATOM   11187 S SD  . MET   D 1 13  ? 5.084   1.926   49.860  1.00 30.96  ?  13  MET   D SD  1 
ATOM   11188 C CE  . MET   D 1 13  ? 3.844   0.658   49.897  1.00 17.58  ?  13  MET   D CE  1 
ATOM   11189 N N   . VAL   D 1 14  ? 7.143   2.852   45.392  1.00 16.51  ?  14  VAL   D N   1 
ATOM   11190 C CA  . VAL   D 1 14  ? 8.244   3.742   45.075  1.00 17.27  ?  14  VAL   D CA  1 
ATOM   11191 C C   . VAL   D 1 14  ? 8.311   4.836   46.126  1.00 17.97  ?  14  VAL   D C   1 
ATOM   11192 O O   . VAL   D 1 14  ? 7.340   5.129   46.832  1.00 17.59  ?  14  VAL   D O   1 
ATOM   11193 C CB  . VAL   D 1 14  ? 8.113   4.355   43.664  1.00 18.09  ?  14  VAL   D CB  1 
ATOM   11194 C CG1 . VAL   D 1 14  ? 8.077   3.266   42.629  1.00 18.15  ?  14  VAL   D CG1 1 
ATOM   11195 C CG2 . VAL   D 1 14  ? 6.851   5.182   43.563  1.00 18.57  ?  14  VAL   D CG2 1 
ATOM   11196 N N   . GLU   D 1 15  ? 9.487   5.442   46.220  1.00 18.24  ?  15  GLU   D N   1 
ATOM   11197 C CA  . GLU   D 1 15  ? 9.740   6.570   47.099  1.00 20.98  ?  15  GLU   D CA  1 
ATOM   11198 C C   . GLU   D 1 15  ? 10.455  7.622   46.266  1.00 22.40  ?  15  GLU   D C   1 
ATOM   11199 O O   . GLU   D 1 15  ? 11.449  7.317   45.604  1.00 22.95  ?  15  GLU   D O   1 
ATOM   11200 C CB  . GLU   D 1 15  ? 10.572  6.136   48.320  1.00 19.18  ?  15  GLU   D CB  1 
ATOM   11201 C CG  . GLU   D 1 15  ? 11.018  7.247   49.237  1.00 26.64  ?  15  GLU   D CG  1 
ATOM   11202 C CD  . GLU   D 1 15  ? 11.951  6.757   50.339  1.00 32.75  ?  15  GLU   D CD  1 
ATOM   11203 O OE1 . GLU   D 1 15  ? 12.836  5.923   50.043  1.00 28.36  ?  15  GLU   D OE1 1 
ATOM   11204 O OE2 . GLU   D 1 15  ? 11.799  7.201   51.503  1.00 41.86  ?  15  GLU   D OE2 1 
ATOM   11205 N N   . LYS   D 1 16  ? 9.929   8.841   46.262  1.00 25.49  ?  16  LYS   D N   1 
ATOM   11206 C CA  . LYS   D 1 16  ? 10.491  9.888   45.420  1.00 26.73  ?  16  LYS   D CA  1 
ATOM   11207 C C   . LYS   D 1 16  ? 11.886  10.274  45.902  1.00 28.22  ?  16  LYS   D C   1 
ATOM   11208 O O   . LYS   D 1 16  ? 12.160  10.305  47.106  1.00 27.93  ?  16  LYS   D O   1 
ATOM   11209 C CB  . LYS   D 1 16  ? 9.570   11.110  45.423  1.00 31.88  ?  16  LYS   D CB  1 
ATOM   11210 C CG  . LYS   D 1 16  ? 10.066  12.312  44.630  1.00 30.20  ?  16  LYS   D CG  1 
ATOM   11211 C CD  . LYS   D 1 16  ? 9.001   13.407  44.626  1.00 33.84  ?  16  LYS   D CD  1 
ATOM   11212 C CE  . LYS   D 1 16  ? 9.365   14.536  43.678  1.00 41.16  ?  16  LYS   D CE  1 
ATOM   11213 N NZ  . LYS   D 1 16  ? 8.223   15.466  43.484  1.00 46.37  ?  16  LYS   D NZ  1 
ATOM   11214 N N   . ILE   D 1 17  ? 12.782  10.544  44.956  1.00 28.49  ?  17  ILE   D N   1 
ATOM   11215 C CA  . ILE   D 1 17  ? 14.075  11.131  45.274  1.00 27.04  ?  17  ILE   D CA  1 
ATOM   11216 C C   . ILE   D 1 17  ? 14.333  12.257  44.291  1.00 31.03  ?  17  ILE   D C   1 
ATOM   11217 O O   . ILE   D 1 17  ? 13.823  12.255  43.167  1.00 36.56  ?  17  ILE   D O   1 
ATOM   11218 C CB  . ILE   D 1 17  ? 15.238  10.108  45.255  1.00 30.07  ?  17  ILE   D CB  1 
ATOM   11219 C CG1 . ILE   D 1 17  ? 15.432  9.504   43.865  1.00 32.75  ?  17  ILE   D CG1 1 
ATOM   11220 C CG2 . ILE   D 1 17  ? 15.028  9.029   46.326  1.00 32.21  ?  17  ILE   D CG2 1 
ATOM   11221 C CD1 . ILE   D 1 17  ? 16.634  8.568   43.773  1.00 30.31  ?  17  ILE   D CD1 1 
ATOM   11222 N N   . ARG   D 1 18  ? 15.128  13.227  44.726  1.00 36.04  ?  18  ARG   D N   1 
ATOM   11223 C CA  . ARG   D 1 18  ? 15.396  14.427  43.952  1.00 39.45  ?  18  ARG   D CA  1 
ATOM   11224 C C   . ARG   D 1 18  ? 16.867  14.783  44.106  1.00 39.74  ?  18  ARG   D C   1 
ATOM   11225 O O   . ARG   D 1 18  ? 17.469  14.543  45.154  1.00 39.05  ?  18  ARG   D O   1 
ATOM   11226 C CB  . ARG   D 1 18  ? 14.503  15.591  44.417  1.00 42.98  ?  18  ARG   D CB  1 
ATOM   11227 C CG  . ARG   D 1 18  ? 14.578  16.839  43.558  1.00 49.48  ?  18  ARG   D CG  1 
ATOM   11228 C CD  . ARG   D 1 18  ? 14.121  18.067  44.335  1.00 52.05  ?  18  ARG   D CD  1 
ATOM   11229 N NE  . ARG   D 1 18  ? 14.875  18.221  45.574  1.00 54.38  ?  18  ARG   D NE  1 
ATOM   11230 C CZ  . ARG   D 1 18  ? 15.306  19.380  46.055  1.00 62.40  ?  18  ARG   D CZ  1 
ATOM   11231 N NH1 . ARG   D 1 18  ? 15.089  20.520  45.415  1.00 63.97  ?  18  ARG   D NH1 1 
ATOM   11232 N NH2 . ARG   D 1 18  ? 15.981  19.395  47.202  1.00 62.01  ?  18  ARG   D NH2 1 
ATOM   11233 N N   . VAL   D 1 19  ? 17.450  15.341  43.054  1.00 40.87  ?  19  VAL   D N   1 
ATOM   11234 C CA  . VAL   D 1 19  ? 18.816  15.851  43.104  1.00 45.48  ?  19  VAL   D CA  1 
ATOM   11235 C C   . VAL   D 1 19  ? 18.738  17.365  43.267  1.00 50.00  ?  19  VAL   D C   1 
ATOM   11236 O O   . VAL   D 1 19  ? 18.187  18.043  42.387  1.00 48.90  ?  19  VAL   D O   1 
ATOM   11237 C CB  . VAL   D 1 19  ? 19.630  15.447  41.863  1.00 43.10  ?  19  VAL   D CB  1 
ATOM   11238 C CG1 . VAL   D 1 19  ? 18.799  15.578  40.603  1.00 45.09  ?  19  VAL   D CG1 1 
ATOM   11239 C CG2 . VAL   D 1 19  ? 20.924  16.261  41.773  1.00 43.77  ?  19  VAL   D CG2 1 
ATOM   11240 N N   . PRO   D 1 20  ? 19.209  17.921  44.380  1.00 51.63  ?  20  PRO   D N   1 
ATOM   11241 C CA  . PRO   D 1 20  ? 19.166  19.376  44.550  1.00 56.28  ?  20  PRO   D CA  1 
ATOM   11242 C C   . PRO   D 1 20  ? 20.091  20.075  43.570  1.00 60.39  ?  20  PRO   D C   1 
ATOM   11243 O O   . PRO   D 1 20  ? 21.172  19.577  43.243  1.00 58.45  ?  20  PRO   D O   1 
ATOM   11244 C CB  . PRO   D 1 20  ? 19.628  19.580  45.998  1.00 55.13  ?  20  PRO   D CB  1 
ATOM   11245 C CG  . PRO   D 1 20  ? 20.379  18.327  46.341  1.00 49.49  ?  20  PRO   D CG  1 
ATOM   11246 C CD  . PRO   D 1 20  ? 19.705  17.232  45.584  1.00 43.87  ?  20  PRO   D CD  1 
ATOM   11247 N N   . SER   D 1 21  ? 19.647  21.238  43.098  1.00 63.16  ?  21  SER   D N   1 
ATOM   11248 C CA  . SER   D 1 21  ? 20.483  22.074  42.249  1.00 67.56  ?  21  SER   D CA  1 
ATOM   11249 C C   . SER   D 1 21  ? 21.789  22.395  42.963  1.00 67.15  ?  21  SER   D C   1 
ATOM   11250 O O   . SER   D 1 21  ? 21.844  22.458  44.194  1.00 62.96  ?  21  SER   D O   1 
ATOM   11251 C CB  . SER   D 1 21  ? 19.746  23.363  41.892  1.00 71.64  ?  21  SER   D CB  1 
ATOM   11252 O OG  . SER   D 1 21  ? 18.409  23.083  41.512  1.00 71.99  ?  21  SER   D OG  1 
ATOM   11253 N N   . ARG   D 1 22  ? 22.856  22.588  42.178  1.00 72.10  ?  22  ARG   D N   1 
ATOM   11254 C CA  . ARG   D 1 22  ? 24.168  22.786  42.788  1.00 70.11  ?  22  ARG   D CA  1 
ATOM   11255 C C   . ARG   D 1 22  ? 24.190  24.019  43.676  1.00 72.09  ?  22  ARG   D C   1 
ATOM   11256 O O   . ARG   D 1 22  ? 24.903  24.043  44.684  1.00 68.53  ?  22  ARG   D O   1 
ATOM   11257 C CB  . ARG   D 1 22  ? 25.264  22.887  41.728  1.00 75.44  ?  22  ARG   D CB  1 
ATOM   11258 C CG  . ARG   D 1 22  ? 26.657  22.813  42.352  1.00 72.52  ?  22  ARG   D CG  1 
ATOM   11259 C CD  . ARG   D 1 22  ? 27.777  23.091  41.373  1.00 74.55  ?  22  ARG   D CD  1 
ATOM   11260 N NE  . ARG   D 1 22  ? 29.064  23.128  42.059  1.00 78.15  ?  22  ARG   D NE  1 
ATOM   11261 C CZ  . ARG   D 1 22  ? 29.904  22.104  42.135  1.00 82.62  ?  22  ARG   D CZ  1 
ATOM   11262 N NH1 . ARG   D 1 22  ? 29.639  20.947  41.551  1.00 82.65  ?  22  ARG   D NH1 1 
ATOM   11263 N NH2 . ARG   D 1 22  ? 31.042  22.246  42.811  1.00 83.46  ?  22  ARG   D NH2 1 
ATOM   11264 N N   . GLU   D 1 23  ? 23.419  25.048  43.323  1.00 92.94  ?  23  GLU   D N   1 
ATOM   11265 C CA  . GLU   D 1 23  ? 23.244  26.175  44.231  1.00 94.30  ?  23  GLU   D CA  1 
ATOM   11266 C C   . GLU   D 1 23  ? 22.696  25.700  45.571  1.00 93.48  ?  23  GLU   D C   1 
ATOM   11267 O O   . GLU   D 1 23  ? 23.262  26.000  46.629  1.00 96.03  ?  23  GLU   D O   1 
ATOM   11268 C CB  . GLU   D 1 23  ? 22.324  27.222  43.602  1.00 95.58  ?  23  GLU   D CB  1 
ATOM   11269 C CG  . GLU   D 1 23  ? 22.885  27.885  42.347  1.00 97.15  ?  23  GLU   D CG  1 
ATOM   11270 C CD  . GLU   D 1 23  ? 22.744  27.023  41.102  1.00 96.30  ?  23  GLU   D CD  1 
ATOM   11271 O OE1 . GLU   D 1 23  ? 22.130  25.938  41.189  1.00 94.23  ?  23  GLU   D OE1 1 
ATOM   11272 O OE2 . GLU   D 1 23  ? 23.248  27.436  40.034  1.00 97.36  ?  23  GLU   D OE2 1 
ATOM   11273 N N   . GLU   D 1 24  ? 21.599  24.937  45.544  1.00 73.19  ?  24  GLU   D N   1 
ATOM   11274 C CA  . GLU   D 1 24  ? 21.091  24.328  46.769  1.00 67.55  ?  24  GLU   D CA  1 
ATOM   11275 C C   . GLU   D 1 24  ? 22.073  23.303  47.318  1.00 65.82  ?  24  GLU   D C   1 
ATOM   11276 O O   . GLU   D 1 24  ? 22.293  23.229  48.533  1.00 63.74  ?  24  GLU   D O   1 
ATOM   11277 C CB  . GLU   D 1 24  ? 19.739  23.665  46.509  1.00 66.30  ?  24  GLU   D CB  1 
ATOM   11278 C CG  . GLU   D 1 24  ? 18.704  24.555  45.851  1.00 70.76  ?  24  GLU   D CG  1 
ATOM   11279 C CD  . GLU   D 1 24  ? 17.460  23.786  45.443  1.00 66.10  ?  24  GLU   D CD  1 
ATOM   11280 O OE1 . GLU   D 1 24  ? 17.529  22.540  45.357  1.00 62.59  ?  24  GLU   D OE1 1 
ATOM   11281 O OE2 . GLU   D 1 24  ? 16.415  24.428  45.206  1.00 63.97  ?  24  GLU   D OE2 1 
ATOM   11282 N N   . ARG   D 1 25  ? 22.672  22.506  46.431  1.00 67.75  ?  25  ARG   D N   1 
ATOM   11283 C CA  . ARG   D 1 25  ? 23.558  21.426  46.855  1.00 62.98  ?  25  ARG   D CA  1 
ATOM   11284 C C   . ARG   D 1 25  ? 24.806  21.965  47.548  1.00 68.14  ?  25  ARG   D C   1 
ATOM   11285 O O   . ARG   D 1 25  ? 25.278  21.383  48.532  1.00 57.13  ?  25  ARG   D O   1 
ATOM   11286 C CB  . ARG   D 1 25  ? 23.925  20.576  45.639  1.00 58.94  ?  25  ARG   D CB  1 
ATOM   11287 C CG  . ARG   D 1 25  ? 24.397  19.177  45.952  1.00 62.77  ?  25  ARG   D CG  1 
ATOM   11288 C CD  . ARG   D 1 25  ? 24.158  18.245  44.767  1.00 59.64  ?  25  ARG   D CD  1 
ATOM   11289 N NE  . ARG   D 1 25  ? 25.004  18.559  43.621  1.00 65.19  ?  25  ARG   D NE  1 
ATOM   11290 C CZ  . ARG   D 1 25  ? 24.567  19.098  42.491  1.00 61.83  ?  25  ARG   D CZ  1 
ATOM   11291 N NH1 . ARG   D 1 25  ? 23.291  19.396  42.315  1.00 64.55  ?  25  ARG   D NH1 1 
ATOM   11292 N NH2 . ARG   D 1 25  ? 25.432  19.337  41.510  1.00 60.76  ?  25  ARG   D NH2 1 
ATOM   11293 N N   . GLU   D 1 26  ? 25.349  23.081  47.054  1.00 68.99  ?  26  GLU   D N   1 
ATOM   11294 C CA  . GLU   D 1 26  ? 26.566  23.640  47.630  1.00 67.81  ?  26  GLU   D CA  1 
ATOM   11295 C C   . GLU   D 1 26  ? 26.282  24.457  48.883  1.00 64.88  ?  26  GLU   D C   1 
ATOM   11296 O O   . GLU   D 1 26  ? 27.105  24.472  49.807  1.00 65.33  ?  26  GLU   D O   1 
ATOM   11297 C CB  . GLU   D 1 26  ? 27.282  24.499  46.593  1.00 74.62  ?  26  GLU   D CB  1 
ATOM   11298 C CG  . GLU   D 1 26  ? 28.727  24.792  46.904  1.00 82.90  ?  26  GLU   D CG  1 
ATOM   11299 C CD  . GLU   D 1 26  ? 29.365  25.646  45.829  1.00 93.17  ?  26  GLU   D CD  1 
ATOM   11300 O OE1 . GLU   D 1 26  ? 28.698  25.892  44.799  1.00 87.59  ?  26  GLU   D OE1 1 
ATOM   11301 O OE2 . GLU   D 1 26  ? 30.525  26.073  46.014  1.00 102.44 ?  26  GLU   D OE2 1 
ATOM   11302 N N   . ALA   D 1 27  ? 25.138  25.144  48.929  1.00 65.60  ?  27  ALA   D N   1 
ATOM   11303 C CA  . ALA   D 1 27  ? 24.737  25.821  50.158  1.00 67.37  ?  27  ALA   D CA  1 
ATOM   11304 C C   . ALA   D 1 27  ? 24.518  24.818  51.282  1.00 63.21  ?  27  ALA   D C   1 
ATOM   11305 O O   . ALA   D 1 27  ? 24.868  25.080  52.438  1.00 61.66  ?  27  ALA   D O   1 
ATOM   11306 C CB  . ALA   D 1 27  ? 23.473  26.646  49.918  1.00 62.45  ?  27  ALA   D CB  1 
ATOM   11307 N N   . ALA   D 1 28  ? 23.948  23.656  50.955  1.00 63.96  ?  28  ALA   D N   1 
ATOM   11308 C CA  . ALA   D 1 28  ? 23.742  22.615  51.954  1.00 62.06  ?  28  ALA   D CA  1 
ATOM   11309 C C   . ALA   D 1 28  ? 25.063  22.042  52.453  1.00 63.37  ?  28  ALA   D C   1 
ATOM   11310 O O   . ALA   D 1 28  ? 25.162  21.650  53.621  1.00 62.37  ?  28  ALA   D O   1 
ATOM   11311 C CB  . ALA   D 1 28  ? 22.867  21.505  51.377  1.00 57.03  ?  28  ALA   D CB  1 
ATOM   11312 N N   . LEU   D 1 29  ? 26.082  21.977  51.593  1.00 61.87  ?  29  LEU   D N   1 
ATOM   11313 C CA  . LEU   D 1 29  ? 27.375  21.478  52.047  1.00 63.15  ?  29  LEU   D CA  1 
ATOM   11314 C C   . LEU   D 1 29  ? 28.079  22.494  52.935  1.00 66.66  ?  29  LEU   D C   1 
ATOM   11315 O O   . LEU   D 1 29  ? 28.782  22.107  53.877  1.00 64.56  ?  29  LEU   D O   1 
ATOM   11316 C CB  . LEU   D 1 29  ? 28.254  21.106  50.853  1.00 61.35  ?  29  LEU   D CB  1 
ATOM   11317 C CG  . LEU   D 1 29  ? 29.591  20.431  51.183  1.00 59.89  ?  29  LEU   D CG  1 
ATOM   11318 C CD1 . LEU   D 1 29  ? 29.400  19.271  52.146  1.00 48.81  ?  29  LEU   D CD1 1 
ATOM   11319 C CD2 . LEU   D 1 29  ? 30.270  19.957  49.909  1.00 60.36  ?  29  LEU   D CD2 1 
ATOM   11320 N N   . LYS   D 1 30  ? 27.901  23.789  52.656  1.00 63.76  ?  30  LYS   D N   1 
ATOM   11321 C CA  . LYS   D 1 30  ? 28.446  24.815  53.541  1.00 67.48  ?  30  LYS   D CA  1 
ATOM   11322 C C   . LYS   D 1 30  ? 27.921  24.643  54.961  1.00 66.25  ?  30  LYS   D C   1 
ATOM   11323 O O   . LYS   D 1 30  ? 28.700  24.507  55.912  1.00 69.39  ?  30  LYS   D O   1 
ATOM   11324 C CB  . LYS   D 1 30  ? 28.115  26.212  53.005  1.00 69.60  ?  30  LYS   D CB  1 
ATOM   11325 C CG  . LYS   D 1 30  ? 28.917  26.618  51.768  1.00 75.14  ?  30  LYS   D CG  1 
ATOM   11326 C CD  . LYS   D 1 30  ? 28.599  28.040  51.319  1.00 74.11  ?  30  LYS   D CD  1 
ATOM   11327 C CE  . LYS   D 1 30  ? 29.369  28.401  50.054  1.00 81.71  ?  30  LYS   D CE  1 
ATOM   11328 N NZ  . LYS   D 1 30  ? 29.153  29.816  49.636  1.00 82.29  ?  30  LYS   D NZ  1 
ATOM   11329 N N   . GLU   D 1 31  ? 26.594  24.620  55.121  1.00 64.20  ?  31  GLU   D N   1 
ATOM   11330 C CA  . GLU   D 1 31  ? 26.019  24.457  56.452  1.00 63.26  ?  31  GLU   D CA  1 
ATOM   11331 C C   . GLU   D 1 31  ? 26.373  23.105  57.052  1.00 59.12  ?  31  GLU   D C   1 
ATOM   11332 O O   . GLU   D 1 31  ? 26.456  22.973  58.279  1.00 56.81  ?  31  GLU   D O   1 
ATOM   11333 C CB  . GLU   D 1 31  ? 24.503  24.637  56.397  1.00 58.40  ?  31  GLU   D CB  1 
ATOM   11334 C CG  . GLU   D 1 31  ? 23.853  24.743  57.763  1.00 58.60  ?  31  GLU   D CG  1 
ATOM   11335 C CD  . GLU   D 1 31  ? 22.487  25.395  57.705  1.00 72.84  ?  31  GLU   D CD  1 
ATOM   11336 O OE1 . GLU   D 1 31  ? 21.950  25.549  56.587  1.00 74.56  ?  31  GLU   D OE1 1 
ATOM   11337 O OE2 . GLU   D 1 31  ? 21.956  25.763  58.776  1.00 73.56  ?  31  GLU   D OE2 1 
ATOM   11338 N N   . ALA   D 1 32  ? 26.593  22.093  56.208  1.00 61.67  ?  32  ALA   D N   1 
ATOM   11339 C CA  . ALA   D 1 32  ? 26.998  20.775  56.678  1.00 61.39  ?  32  ALA   D CA  1 
ATOM   11340 C C   . ALA   D 1 32  ? 28.423  20.755  57.205  1.00 66.43  ?  32  ALA   D C   1 
ATOM   11341 O O   . ALA   D 1 32  ? 28.804  19.787  57.878  1.00 66.27  ?  32  ALA   D O   1 
ATOM   11342 C CB  . ALA   D 1 32  ? 26.857  19.744  55.559  1.00 50.22  ?  32  ALA   D CB  1 
ATOM   11343 N N   . GLY   D 1 33  ? 29.211  21.789  56.922  1.00 66.94  ?  33  GLY   D N   1 
ATOM   11344 C CA  . GLY   D 1 33  ? 30.596  21.799  57.344  1.00 67.37  ?  33  GLY   D CA  1 
ATOM   11345 C C   . GLY   D 1 33  ? 31.438  20.733  56.685  1.00 68.44  ?  33  GLY   D C   1 
ATOM   11346 O O   . GLY   D 1 33  ? 32.348  20.192  57.320  1.00 73.09  ?  33  GLY   D O   1 
ATOM   11347 N N   . TYR   D 1 34  ? 31.135  20.396  55.430  1.00 62.78  ?  34  TYR   D N   1 
ATOM   11348 C CA  . TYR   D 1 34  ? 31.973  19.505  54.628  1.00 62.58  ?  34  TYR   D CA  1 
ATOM   11349 C C   . TYR   D 1 34  ? 32.161  18.151  55.311  1.00 64.20  ?  34  TYR   D C   1 
ATOM   11350 O O   . TYR   D 1 34  ? 33.237  17.555  55.275  1.00 67.51  ?  34  TYR   D O   1 
ATOM   11351 C CB  . TYR   D 1 34  ? 33.316  20.171  54.312  1.00 67.18  ?  34  TYR   D CB  1 
ATOM   11352 C CG  . TYR   D 1 34  ? 33.144  21.519  53.641  1.00 68.67  ?  34  TYR   D CG  1 
ATOM   11353 C CD1 . TYR   D 1 34  ? 33.047  21.623  52.258  1.00 67.25  ?  34  TYR   D CD1 1 
ATOM   11354 C CD2 . TYR   D 1 34  ? 33.047  22.686  54.391  1.00 69.94  ?  34  TYR   D CD2 1 
ATOM   11355 C CE1 . TYR   D 1 34  ? 32.871  22.851  51.640  1.00 60.18  ?  34  TYR   D CE1 1 
ATOM   11356 C CE2 . TYR   D 1 34  ? 32.869  23.916  53.785  1.00 68.13  ?  34  TYR   D CE2 1 
ATOM   11357 C CZ  . TYR   D 1 34  ? 32.782  23.993  52.410  1.00 65.64  ?  34  TYR   D CZ  1 
ATOM   11358 O OH  . TYR   D 1 34  ? 32.608  25.216  51.805  1.00 71.42  ?  34  TYR   D OH  1 
ATOM   11359 N N   . ASN   D 1 35  ? 31.101  17.670  55.950  1.00 61.72  ?  35  ASN   D N   1 
ATOM   11360 C CA  . ASN   D 1 35  ? 31.056  16.319  56.508  1.00 57.97  ?  35  ASN   D CA  1 
ATOM   11361 C C   . ASN   D 1 35  ? 29.730  15.692  56.098  1.00 55.88  ?  35  ASN   D C   1 
ATOM   11362 O O   . ASN   D 1 35  ? 28.664  16.136  56.576  1.00 53.54  ?  35  ASN   D O   1 
ATOM   11363 C CB  . ASN   D 1 35  ? 31.219  16.340  58.026  1.00 56.49  ?  35  ASN   D CB  1 
ATOM   11364 C CG  . ASN   D 1 35  ? 31.251  14.947  58.628  1.00 58.04  ?  35  ASN   D CG  1 
ATOM   11365 O OD1 . ASN   D 1 35  ? 31.448  13.955  57.923  1.00 58.66  ?  35  ASN   D OD1 1 
ATOM   11366 N ND2 . ASN   D 1 35  ? 31.051  14.866  59.938  1.00 59.77  ?  35  ASN   D ND2 1 
ATOM   11367 N N   . PRO   D 1 36  ? 29.732  14.683  55.223  1.00 59.24  ?  36  PRO   D N   1 
ATOM   11368 C CA  . PRO   D 1 36  ? 28.451  14.157  54.724  1.00 50.80  ?  36  PRO   D CA  1 
ATOM   11369 C C   . PRO   D 1 36  ? 27.569  13.572  55.814  1.00 45.17  ?  36  PRO   D C   1 
ATOM   11370 O O   . PRO   D 1 36  ? 26.340  13.588  55.672  1.00 45.48  ?  36  PRO   D O   1 
ATOM   11371 C CB  . PRO   D 1 36  ? 28.883  13.092  53.702  1.00 44.57  ?  36  PRO   D CB  1 
ATOM   11372 C CG  . PRO   D 1 36  ? 30.298  13.431  53.348  1.00 41.12  ?  36  PRO   D CG  1 
ATOM   11373 C CD  . PRO   D 1 36  ? 30.885  14.008  54.604  1.00 54.06  ?  36  PRO   D CD  1 
ATOM   11374 N N   . PHE   D 1 37  ? 28.152  13.064  56.903  1.00 47.80  ?  37  PHE   D N   1 
ATOM   11375 C CA  . PHE   D 1 37  ? 27.348  12.513  57.988  1.00 44.53  ?  37  PHE   D CA  1 
ATOM   11376 C C   . PHE   D 1 37  ? 26.430  13.556  58.611  1.00 41.70  ?  37  PHE   D C   1 
ATOM   11377 O O   . PHE   D 1 37  ? 25.419  13.188  59.215  1.00 39.77  ?  37  PHE   D O   1 
ATOM   11378 C CB  . PHE   D 1 37  ? 28.248  11.915  59.076  1.00 46.37  ?  37  PHE   D CB  1 
ATOM   11379 C CG  . PHE   D 1 37  ? 28.300  10.412  59.074  1.00 39.46  ?  37  PHE   D CG  1 
ATOM   11380 C CD1 . PHE   D 1 37  ? 27.270  9.667   59.633  1.00 41.81  ?  37  PHE   D CD1 1 
ATOM   11381 C CD2 . PHE   D 1 37  ? 29.387  9.742   58.528  1.00 42.67  ?  37  PHE   D CD2 1 
ATOM   11382 C CE1 . PHE   D 1 37  ? 27.312  8.274   59.635  1.00 41.86  ?  37  PHE   D CE1 1 
ATOM   11383 C CE2 . PHE   D 1 37  ? 29.445  8.354   58.529  1.00 43.63  ?  37  PHE   D CE2 1 
ATOM   11384 C CZ  . PHE   D 1 37  ? 28.405  7.617   59.082  1.00 45.32  ?  37  PHE   D CZ  1 
ATOM   11385 N N   . LEU   D 1 38  ? 26.758  14.841  58.484  1.00 47.19  ?  38  LEU   D N   1 
ATOM   11386 C CA  . LEU   D 1 38  ? 25.954  15.913  59.055  1.00 46.77  ?  38  LEU   D CA  1 
ATOM   11387 C C   . LEU   D 1 38  ? 24.972  16.514  58.058  1.00 45.49  ?  38  LEU   D C   1 
ATOM   11388 O O   . LEU   D 1 38  ? 24.309  17.505  58.385  1.00 40.55  ?  38  LEU   D O   1 
ATOM   11389 C CB  . LEU   D 1 38  ? 26.858  17.020  59.613  1.00 53.67  ?  38  LEU   D CB  1 
ATOM   11390 C CG  . LEU   D 1 38  ? 27.730  16.676  60.821  1.00 55.58  ?  38  LEU   D CG  1 
ATOM   11391 C CD1 . LEU   D 1 38  ? 28.569  17.880  61.234  1.00 59.98  ?  38  LEU   D CD1 1 
ATOM   11392 C CD2 . LEU   D 1 38  ? 26.882  16.187  61.979  1.00 54.38  ?  38  LEU   D CD2 1 
ATOM   11393 N N   . LEU   D 1 39  ? 24.876  15.951  56.848  1.00 40.53  ?  39  LEU   D N   1 
ATOM   11394 C CA  . LEU   D 1 39  ? 23.895  16.375  55.860  1.00 35.94  ?  39  LEU   D CA  1 
ATOM   11395 C C   . LEU   D 1 39  ? 22.535  15.746  56.162  1.00 38.08  ?  39  LEU   D C   1 
ATOM   11396 O O   . LEU   D 1 39  ? 22.458  14.569  56.531  1.00 33.66  ?  39  LEU   D O   1 
ATOM   11397 C CB  . LEU   D 1 39  ? 24.336  15.970  54.455  1.00 39.37  ?  39  LEU   D CB  1 
ATOM   11398 C CG  . LEU   D 1 39  ? 25.399  16.786  53.721  1.00 49.40  ?  39  LEU   D CG  1 
ATOM   11399 C CD1 . LEU   D 1 39  ? 26.024  15.937  52.629  1.00 45.07  ?  39  LEU   D CD1 1 
ATOM   11400 C CD2 . LEU   D 1 39  ? 24.793  18.054  53.126  1.00 48.95  ?  39  LEU   D CD2 1 
ATOM   11401 N N   . PRO   D 1 40  ? 21.450  16.498  56.014  1.00 37.50  ?  40  PRO   D N   1 
ATOM   11402 C CA  . PRO   D 1 40  ? 20.123  15.885  56.080  1.00 34.09  ?  40  PRO   D CA  1 
ATOM   11403 C C   . PRO   D 1 40  ? 19.821  15.153  54.783  1.00 30.85  ?  40  PRO   D C   1 
ATOM   11404 O O   . PRO   D 1 40  ? 20.362  15.469  53.722  1.00 33.04  ?  40  PRO   D O   1 
ATOM   11405 C CB  . PRO   D 1 40  ? 19.190  17.084  56.285  1.00 30.53  ?  40  PRO   D CB  1 
ATOM   11406 C CG  . PRO   D 1 40  ? 19.891  18.195  55.593  1.00 34.15  ?  40  PRO   D CG  1 
ATOM   11407 C CD  . PRO   D 1 40  ? 21.380  17.941  55.732  1.00 35.33  ?  40  PRO   D CD  1 
ATOM   11408 N N   . SER   D 1 41  ? 18.955  14.143  54.882  1.00 27.30  ?  41  SER   D N   1 
ATOM   11409 C CA  . SER   D 1 41  ? 18.655  13.332  53.706  1.00 29.91  ?  41  SER   D CA  1 
ATOM   11410 C C   . SER   D 1 41  ? 17.999  14.152  52.603  1.00 31.31  ?  41  SER   D C   1 
ATOM   11411 O O   . SER   D 1 41  ? 18.093  13.791  51.425  1.00 32.78  ?  41  SER   D O   1 
ATOM   11412 C CB  . SER   D 1 41  ? 17.757  12.163  54.090  1.00 24.88  ?  41  SER   D CB  1 
ATOM   11413 O OG  . SER   D 1 41  ? 16.506  12.638  54.534  1.00 24.82  ?  41  SER   D OG  1 
ATOM   11414 N N   . SER   D 1 42  ? 17.331  15.253  52.961  1.00 32.35  ?  42  SER   D N   1 
ATOM   11415 C CA  . SER   D 1 42  ? 16.729  16.132  51.965  1.00 31.68  ?  42  SER   D CA  1 
ATOM   11416 C C   . SER   D 1 42  ? 17.755  16.707  50.998  1.00 35.59  ?  42  SER   D C   1 
ATOM   11417 O O   . SER   D 1 42  ? 17.383  17.177  49.916  1.00 41.83  ?  42  SER   D O   1 
ATOM   11418 C CB  . SER   D 1 42  ? 15.998  17.271  52.666  1.00 29.57  ?  42  SER   D CB  1 
ATOM   11419 O OG  . SER   D 1 42  ? 16.919  18.019  53.443  1.00 32.71  ?  42  SER   D OG  1 
ATOM   11420 N N   . ALA   D 1 43  ? 19.033  16.698  51.366  1.00 33.48  ?  43  ALA   D N   1 
ATOM   11421 C CA  . ALA   D 1 43  ? 20.086  17.245  50.530  1.00 35.43  ?  43  ALA   D CA  1 
ATOM   11422 C C   . ALA   D 1 43  ? 20.817  16.180  49.725  1.00 38.31  ?  43  ALA   D C   1 
ATOM   11423 O O   . ALA   D 1 43  ? 21.769  16.511  49.013  1.00 38.00  ?  43  ALA   D O   1 
ATOM   11424 C CB  . ALA   D 1 43  ? 21.086  18.018  51.391  1.00 42.05  ?  43  ALA   D CB  1 
ATOM   11425 N N   . VAL   D 1 44  ? 20.393  14.921  49.805  1.00 35.72  ?  44  VAL   D N   1 
ATOM   11426 C CA  . VAL   D 1 44  ? 21.082  13.813  49.154  1.00 37.51  ?  44  VAL   D CA  1 
ATOM   11427 C C   . VAL   D 1 44  ? 20.193  13.259  48.052  1.00 33.95  ?  44  VAL   D C   1 
ATOM   11428 O O   . VAL   D 1 44  ? 18.988  13.065  48.254  1.00 34.35  ?  44  VAL   D O   1 
ATOM   11429 C CB  . VAL   D 1 44  ? 21.462  12.716  50.163  1.00 31.57  ?  44  VAL   D CB  1 
ATOM   11430 C CG1 . VAL   D 1 44  ? 21.987  11.490  49.440  1.00 29.66  ?  44  VAL   D CG1 1 
ATOM   11431 C CG2 . VAL   D 1 44  ? 22.511  13.251  51.145  1.00 36.03  ?  44  VAL   D CG2 1 
ATOM   11432 N N   . TYR   D 1 45  ? 20.787  13.023  46.881  1.00 33.41  ?  45  TYR   D N   1 
ATOM   11433 C CA  . TYR   D 1 45  ? 20.088  12.352  45.794  1.00 31.82  ?  45  TYR   D CA  1 
ATOM   11434 C C   . TYR   D 1 45  ? 20.100  10.848  46.036  1.00 31.36  ?  45  TYR   D C   1 
ATOM   11435 O O   . TYR   D 1 45  ? 19.154  10.298  46.609  1.00 36.13  ?  45  TYR   D O   1 
ATOM   11436 C CB  . TYR   D 1 45  ? 20.727  12.698  44.447  1.00 34.94  ?  45  TYR   D CB  1 
ATOM   11437 C CG  . TYR   D 1 45  ? 20.107  11.973  43.273  1.00 36.89  ?  45  TYR   D CG  1 
ATOM   11438 C CD1 . TYR   D 1 45  ? 18.729  11.884  43.139  1.00 32.69  ?  45  TYR   D CD1 1 
ATOM   11439 C CD2 . TYR   D 1 45  ? 20.902  11.393  42.286  1.00 37.76  ?  45  TYR   D CD2 1 
ATOM   11440 C CE1 . TYR   D 1 45  ? 18.155  11.223  42.067  1.00 38.66  ?  45  TYR   D CE1 1 
ATOM   11441 C CE2 . TYR   D 1 45  ? 20.334  10.726  41.207  1.00 32.97  ?  45  TYR   D CE2 1 
ATOM   11442 C CZ  . TYR   D 1 45  ? 18.960  10.644  41.105  1.00 39.12  ?  45  TYR   D CZ  1 
ATOM   11443 O OH  . TYR   D 1 45  ? 18.378  9.984   40.040  1.00 39.92  ?  45  TYR   D OH  1 
ATOM   11444 N N   . ILE   D 1 46  ? 21.166  10.179  45.612  1.00 32.17  ?  46  ILE   D N   1 
ATOM   11445 C CA  . ILE   D 1 46  ? 21.377  8.770   45.917  1.00 24.50  ?  46  ILE   D CA  1 
ATOM   11446 C C   . ILE   D 1 46  ? 22.259  8.688   47.151  1.00 26.64  ?  46  ILE   D C   1 
ATOM   11447 O O   . ILE   D 1 46  ? 23.310  9.333   47.216  1.00 26.62  ?  46  ILE   D O   1 
ATOM   11448 C CB  . ILE   D 1 46  ? 22.011  8.036   44.724  1.00 30.36  ?  46  ILE   D CB  1 
ATOM   11449 C CG1 . ILE   D 1 46  ? 21.041  8.022   43.542  1.00 24.85  ?  46  ILE   D CG1 1 
ATOM   11450 C CG2 . ILE   D 1 46  ? 22.382  6.614   45.109  1.00 26.79  ?  46  ILE   D CG2 1 
ATOM   11451 C CD1 . ILE   D 1 46  ? 21.608  7.406   42.276  1.00 28.02  ?  46  ILE   D CD1 1 
ATOM   11452 N N   . ASP   D 1 47  ? 21.826  7.911   48.138  1.00 28.20  ?  47  ASP   D N   1 
ATOM   11453 C CA  . ASP   D 1 47  ? 22.493  7.843   49.432  1.00 28.96  ?  47  ASP   D CA  1 
ATOM   11454 C C   . ASP   D 1 47  ? 23.287  6.545   49.501  1.00 26.67  ?  47  ASP   D C   1 
ATOM   11455 O O   . ASP   D 1 47  ? 22.710  5.458   49.622  1.00 24.88  ?  47  ASP   D O   1 
ATOM   11456 C CB  . ASP   D 1 47  ? 21.479  7.933   50.568  1.00 23.58  ?  47  ASP   D CB  1 
ATOM   11457 C CG  . ASP   D 1 47  ? 22.091  8.447   51.869  1.00 27.66  ?  47  ASP   D CG  1 
ATOM   11458 O OD1 . ASP   D 1 47  ? 23.331  8.570   51.954  1.00 27.70  ?  47  ASP   D OD1 1 
ATOM   11459 O OD2 . ASP   D 1 47  ? 21.325  8.741   52.809  1.00 26.96  ?  47  ASP   D OD2 1 
ATOM   11460 N N   . LEU   D 1 48  ? 24.611  6.665   49.421  1.00 24.04  ?  48  LEU   D N   1 
ATOM   11461 C CA  . LEU   D 1 48  ? 25.519  5.531   49.519  1.00 29.13  ?  48  LEU   D CA  1 
ATOM   11462 C C   . LEU   D 1 48  ? 26.254  5.497   50.856  1.00 30.62  ?  48  LEU   D C   1 
ATOM   11463 O O   . LEU   D 1 48  ? 27.307  4.858   50.969  1.00 31.13  ?  48  LEU   D O   1 
ATOM   11464 C CB  . LEU   D 1 48  ? 26.518  5.568   48.365  1.00 24.83  ?  48  LEU   D CB  1 
ATOM   11465 C CG  . LEU   D 1 48  ? 25.888  5.603   46.973  1.00 24.32  ?  48  LEU   D CG  1 
ATOM   11466 C CD1 . LEU   D 1 48  ? 26.950  5.514   45.903  1.00 25.06  ?  48  LEU   D CD1 1 
ATOM   11467 C CD2 . LEU   D 1 48  ? 24.875  4.480   46.815  1.00 26.16  ?  48  LEU   D CD2 1 
ATOM   11468 N N   . LEU   D 1 49  ? 25.722  6.176   51.873  1.00 26.27  ?  49  LEU   D N   1 
ATOM   11469 C CA  . LEU   D 1 49  ? 26.415  6.254   53.152  1.00 27.36  ?  49  LEU   D CA  1 
ATOM   11470 C C   . LEU   D 1 49  ? 26.551  4.880   53.800  1.00 27.14  ?  49  LEU   D C   1 
ATOM   11471 O O   . LEU   D 1 49  ? 27.571  4.596   54.437  1.00 28.63  ?  49  LEU   D O   1 
ATOM   11472 C CB  . LEU   D 1 49  ? 25.683  7.230   54.079  1.00 26.69  ?  49  LEU   D CB  1 
ATOM   11473 C CG  . LEU   D 1 49  ? 26.316  7.574   55.433  1.00 30.96  ?  49  LEU   D CG  1 
ATOM   11474 C CD1 . LEU   D 1 49  ? 27.673  8.210   55.251  1.00 40.34  ?  49  LEU   D CD1 1 
ATOM   11475 C CD2 . LEU   D 1 49  ? 25.422  8.499   56.229  1.00 29.18  ?  49  LEU   D CD2 1 
ATOM   11476 N N   . THR   D 1 50  ? 25.557  4.011   53.626  1.00 24.78  ?  50  THR   D N   1 
ATOM   11477 C CA  . THR   D 1 50  ? 25.551  2.708   54.276  1.00 21.82  ?  50  THR   D CA  1 
ATOM   11478 C C   . THR   D 1 50  ? 24.578  1.784   53.554  1.00 23.29  ?  50  THR   D C   1 
ATOM   11479 O O   . THR   D 1 50  ? 23.685  2.231   52.824  1.00 26.00  ?  50  THR   D O   1 
ATOM   11480 C CB  . THR   D 1 50  ? 25.163  2.829   55.753  1.00 26.81  ?  50  THR   D CB  1 
ATOM   11481 O OG1 . THR   D 1 50  ? 25.343  1.567   56.398  1.00 29.64  ?  50  THR   D OG1 1 
ATOM   11482 C CG2 . THR   D 1 50  ? 23.711  3.224   55.872  1.00 22.16  ?  50  THR   D CG2 1 
ATOM   11483 N N   . ASP   D 1 51  ? 24.768  0.480   53.765  1.00 23.03  ?  51  ASP   D N   1 
ATOM   11484 C CA  . ASP   D 1 51  ? 23.778  -0.532  53.410  1.00 19.07  ?  51  ASP   D CA  1 
ATOM   11485 C C   . ASP   D 1 51  ? 22.970  -0.970  54.623  1.00 21.94  ?  51  ASP   D C   1 
ATOM   11486 O O   . ASP   D 1 51  ? 22.330  -2.027  54.594  1.00 20.57  ?  51  ASP   D O   1 
ATOM   11487 C CB  . ASP   D 1 51  ? 24.451  -1.745  52.759  1.00 20.43  ?  51  ASP   D CB  1 
ATOM   11488 C CG  . ASP   D 1 51  ? 25.358  -2.496  53.715  1.00 20.08  ?  51  ASP   D CG  1 
ATOM   11489 O OD1 . ASP   D 1 51  ? 26.039  -1.847  54.527  1.00 24.21  ?  51  ASP   D OD1 1 
ATOM   11490 O OD2 . ASP   D 1 51  ? 25.390  -3.738  53.667  1.00 20.07  ?  51  ASP   D OD2 1 
ATOM   11491 N N   . SER   D 1 52  ? 22.978  -0.173  55.683  1.00 21.38  ?  52  SER   D N   1 
ATOM   11492 C CA  . SER   D 1 52  ? 22.409  -0.565  56.965  1.00 19.34  ?  52  SER   D CA  1 
ATOM   11493 C C   . SER   D 1 52  ? 21.048  0.094   57.148  1.00 20.87  ?  52  SER   D C   1 
ATOM   11494 O O   . SER   D 1 52  ? 20.960  1.316   57.309  1.00 23.18  ?  52  SER   D O   1 
ATOM   11495 C CB  . SER   D 1 52  ? 23.350  -0.181  58.100  1.00 21.87  ?  52  SER   D CB  1 
ATOM   11496 O OG  . SER   D 1 52  ? 22.866  -0.660  59.334  1.00 25.24  ?  52  SER   D OG  1 
ATOM   11497 N N   . GLY   D 1 53  ? 19.994  -0.719  57.166  1.00 18.57  ?  53  GLY   D N   1 
ATOM   11498 C CA  . GLY   D 1 53  ? 18.687  -0.234  57.564  1.00 18.53  ?  53  GLY   D CA  1 
ATOM   11499 C C   . GLY   D 1 53  ? 17.965  0.586   56.525  1.00 19.08  ?  53  GLY   D C   1 
ATOM   11500 O O   . GLY   D 1 53  ? 16.907  1.153   56.825  1.00 18.66  ?  53  GLY   D O   1 
ATOM   11501 N N   . THR   D 1 54  ? 18.499  0.659   55.311  1.00 17.76  ?  54  THR   D N   1 
ATOM   11502 C CA  . THR   D 1 54  ? 17.907  1.407   54.212  1.00 20.40  ?  54  THR   D CA  1 
ATOM   11503 C C   . THR   D 1 54  ? 17.343  0.494   53.130  1.00 19.08  ?  54  THR   D C   1 
ATOM   11504 O O   . THR   D 1 54  ? 16.961  0.975   52.059  1.00 21.71  ?  54  THR   D O   1 
ATOM   11505 C CB  . THR   D 1 54  ? 18.951  2.344   53.611  1.00 24.43  ?  54  THR   D CB  1 
ATOM   11506 O OG1 . THR   D 1 54  ? 20.112  1.581   53.242  1.00 23.97  ?  54  THR   D OG1 1 
ATOM   11507 C CG2 . THR   D 1 54  ? 19.360  3.396   54.632  1.00 22.27  ?  54  THR   D CG2 1 
ATOM   11508 N N   . ASN   D 1 55  ? 17.272  -0.807  53.390  1.00 17.46  ?  55  ASN   D N   1 
ATOM   11509 C CA  . ASN   D 1 55  ? 16.842  -1.764  52.387  1.00 17.88  ?  55  ASN   D CA  1 
ATOM   11510 C C   . ASN   D 1 55  ? 15.344  -1.640  52.118  1.00 20.00  ?  55  ASN   D C   1 
ATOM   11511 O O   . ASN   D 1 55  ? 14.574  -1.124  52.936  1.00 19.59  ?  55  ASN   D O   1 
ATOM   11512 C CB  . ASN   D 1 55  ? 17.170  -3.180  52.852  1.00 18.74  ?  55  ASN   D CB  1 
ATOM   11513 C CG  . ASN   D 1 55  ? 18.577  -3.300  53.386  1.00 19.07  ?  55  ASN   D CG  1 
ATOM   11514 O OD1 . ASN   D 1 55  ? 19.549  -3.228  52.631  1.00 17.54  ?  55  ASN   D OD1 1 
ATOM   11515 N ND2 . ASN   D 1 55  ? 18.700  -3.484  54.699  1.00 15.98  ?  55  ASN   D ND2 1 
ATOM   11516 N N   . ALA   D 1 56  ? 14.933  -2.125  50.947  1.00 18.72  ?  56  ALA   D N   1 
ATOM   11517 C CA  . ALA   D 1 56  ? 13.526  -2.198  50.582  1.00 14.22  ?  56  ALA   D CA  1 
ATOM   11518 C C   . ALA   D 1 56  ? 12.992  -3.574  50.941  1.00 15.51  ?  56  ALA   D C   1 
ATOM   11519 O O   . ALA   D 1 56  ? 13.547  -4.589  50.512  1.00 18.25  ?  56  ALA   D O   1 
ATOM   11520 C CB  . ALA   D 1 56  ? 13.331  -1.938  49.091  1.00 14.36  ?  56  ALA   D CB  1 
ATOM   11521 N N   . MET   D 1 57  ? 11.910  -3.605  51.707  1.00 16.52  ?  57  MET   D N   1 
ATOM   11522 C CA  . MET   D 1 57  ? 11.303  -4.860  52.118  1.00 14.26  ?  57  MET   D CA  1 
ATOM   11523 C C   . MET   D 1 57  ? 10.317  -5.357  51.062  1.00 12.99  ?  57  MET   D C   1 
ATOM   11524 O O   . MET   D 1 57  ? 9.948   -4.642  50.127  1.00 15.46  ?  57  MET   D O   1 
ATOM   11525 C CB  . MET   D 1 57  ? 10.610  -4.697  53.466  1.00 16.16  ?  57  MET   D CB  1 
ATOM   11526 C CG  . MET   D 1 57  ? 11.561  -4.434  54.620  1.00 15.96  ?  57  MET   D CG  1 
ATOM   11527 S SD  . MET   D 1 57  ? 10.689  -4.499  56.195  1.00 18.35  ?  57  MET   D SD  1 
ATOM   11528 C CE  . MET   D 1 57  ? 9.501   -3.187  55.945  1.00 19.36  ?  57  MET   D CE  1 
ATOM   11529 N N   . SER   D 1 58  ? 9.884   -6.605  51.219  1.00 11.67  ?  58  SER   D N   1 
ATOM   11530 C CA  . SER   D 1 58  ? 8.925   -7.192  50.295  1.00 13.25  ?  58  SER   D CA  1 
ATOM   11531 C C   . SER   D 1 58  ? 7.499   -6.954  50.789  1.00 16.13  ?  58  SER   D C   1 
ATOM   11532 O O   . SER   D 1 58  ? 7.269   -6.543  51.931  1.00 16.38  ?  58  SER   D O   1 
ATOM   11533 C CB  . SER   D 1 58  ? 9.181   -8.690  50.135  1.00 13.16  ?  58  SER   D CB  1 
ATOM   11534 O OG  . SER   D 1 58  ? 8.928   -9.359  51.372  1.00 14.72  ?  58  SER   D OG  1 
ATOM   11535 N N   . ASP   D 1 59  ? 6.525   -7.219  49.909  1.00 14.44  ?  59  ASP   D N   1 
ATOM   11536 C CA  . ASP   D 1 59  ? 5.137   -7.192  50.358  1.00 12.30  ?  59  ASP   D CA  1 
ATOM   11537 C C   . ASP   D 1 59  ? 4.903   -8.228  51.454  1.00 15.75  ?  59  ASP   D C   1 
ATOM   11538 O O   . ASP   D 1 59  ? 4.192   -7.957  52.430  1.00 16.46  ?  59  ASP   D O   1 
ATOM   11539 C CB  . ASP   D 1 59  ? 4.182   -7.392  49.181  1.00 17.28  ?  59  ASP   D CB  1 
ATOM   11540 C CG  . ASP   D 1 59  ? 4.496   -8.627  48.352  1.00 18.05  ?  59  ASP   D CG  1 
ATOM   11541 O OD1 . ASP   D 1 59  ? 5.475   -9.348  48.659  1.00 21.84  ?  59  ASP   D OD1 1 
ATOM   11542 O OD2 . ASP   D 1 59  ? 3.738   -8.874  47.392  1.00 25.72  ?  59  ASP   D OD2 1 
ATOM   11543 N N   . HIS   D 1 60  ? 5.537   -9.401  51.341  1.00 15.91  ?  60  HIS   D N   1 
ATOM   11544 C CA  . HIS   D 1 60  ? 5.418   -10.408 52.394  1.00 15.62  ?  60  HIS   D CA  1 
ATOM   11545 C C   . HIS   D 1 60  ? 5.963   -9.910  53.720  1.00 17.91  ?  60  HIS   D C   1 
ATOM   11546 O O   . HIS   D 1 60  ? 5.437   -10.273 54.779  1.00 17.05  ?  60  HIS   D O   1 
ATOM   11547 C CB  . HIS   D 1 60  ? 6.125   -11.694 51.983  1.00 16.44  ?  60  HIS   D CB  1 
ATOM   11548 C CG  . HIS   D 1 60  ? 5.378   -12.459 50.945  1.00 20.71  ?  60  HIS   D CG  1 
ATOM   11549 N ND1 . HIS   D 1 60  ? 5.687   -12.393 49.604  1.00 30.45  ?  60  HIS   D ND1 1 
ATOM   11550 C CD2 . HIS   D 1 60  ? 4.292   -13.260 51.042  1.00 20.30  ?  60  HIS   D CD2 1 
ATOM   11551 C CE1 . HIS   D 1 60  ? 4.842   -13.145 48.921  1.00 26.20  ?  60  HIS   D CE1 1 
ATOM   11552 N NE2 . HIS   D 1 60  ? 3.981   -13.676 49.769  1.00 26.43  ?  60  HIS   D NE2 1 
ATOM   11553 N N   . GLN   D 1 61  ? 7.004   -9.078  53.688  1.00 16.56  ?  61  GLN   D N   1 
ATOM   11554 C CA  . GLN   D 1 61  ? 7.547   -8.549  54.933  1.00 16.32  ?  61  GLN   D CA  1 
ATOM   11555 C C   . GLN   D 1 61  ? 6.602   -7.535  55.565  1.00 19.25  ?  61  GLN   D C   1 
ATOM   11556 O O   . GLN   D 1 61  ? 6.368   -7.571  56.783  1.00 19.26  ?  61  GLN   D O   1 
ATOM   11557 C CB  . GLN   D 1 61  ? 8.917   -7.933  54.682  1.00 16.81  ?  61  GLN   D CB  1 
ATOM   11558 C CG  . GLN   D 1 61  ? 10.031  -8.952  54.658  1.00 20.73  ?  61  GLN   D CG  1 
ATOM   11559 C CD  . GLN   D 1 61  ? 11.366  -8.325  54.341  1.00 17.70  ?  61  GLN   D CD  1 
ATOM   11560 O OE1 . GLN   D 1 61  ? 11.551  -7.793  53.256  1.00 17.24  ?  61  GLN   D OE1 1 
ATOM   11561 N NE2 . GLN   D 1 61  ? 12.294  -8.364  55.292  1.00 18.01  ?  61  GLN   D NE2 1 
ATOM   11562 N N   . TRP   D 1 62  ? 6.047   -6.626  54.759  1.00 16.56  ?  62  TRP   D N   1 
ATOM   11563 C CA  . TRP   D 1 62  ? 5.047   -5.701  55.281  1.00 19.10  ?  62  TRP   D CA  1 
ATOM   11564 C C   . TRP   D 1 62  ? 3.819   -6.446  55.787  1.00 16.09  ?  62  TRP   D C   1 
ATOM   11565 O O   . TRP   D 1 62  ? 3.279   -6.110  56.846  1.00 14.91  ?  62  TRP   D O   1 
ATOM   11566 C CB  . TRP   D 1 62  ? 4.656   -4.682  54.217  1.00 15.05  ?  62  TRP   D CB  1 
ATOM   11567 C CG  . TRP   D 1 62  ? 5.660   -3.596  54.071  1.00 23.04  ?  62  TRP   D CG  1 
ATOM   11568 C CD1 . TRP   D 1 62  ? 6.734   -3.580  53.223  1.00 22.51  ?  62  TRP   D CD1 1 
ATOM   11569 C CD2 . TRP   D 1 62  ? 5.704   -2.362  54.800  1.00 27.59  ?  62  TRP   D CD2 1 
ATOM   11570 N NE1 . TRP   D 1 62  ? 7.431   -2.405  53.370  1.00 28.04  ?  62  TRP   D NE1 1 
ATOM   11571 C CE2 . TRP   D 1 62  ? 6.823   -1.642  54.333  1.00 30.95  ?  62  TRP   D CE2 1 
ATOM   11572 C CE3 . TRP   D 1 62  ? 4.902   -1.793  55.800  1.00 31.21  ?  62  TRP   D CE3 1 
ATOM   11573 C CZ2 . TRP   D 1 62  ? 7.169   -0.381  54.839  1.00 36.66  ?  62  TRP   D CZ2 1 
ATOM   11574 C CZ3 . TRP   D 1 62  ? 5.248   -0.535  56.303  1.00 32.94  ?  62  TRP   D CZ3 1 
ATOM   11575 C CH2 . TRP   D 1 62  ? 6.369   0.153   55.819  1.00 32.07  ?  62  TRP   D CH2 1 
ATOM   11576 N N   . ALA   D 1 63  ? 3.377   -7.475  55.058  1.00 15.85  ?  63  ALA   D N   1 
ATOM   11577 C CA  . ALA   D 1 63  ? 2.255   -8.279  55.536  1.00 16.70  ?  63  ALA   D CA  1 
ATOM   11578 C C   . ALA   D 1 63  ? 2.567   -8.914  56.887  1.00 15.88  ?  63  ALA   D C   1 
ATOM   11579 O O   . ALA   D 1 63  ? 1.686   -9.013  57.752  1.00 18.65  ?  63  ALA   D O   1 
ATOM   11580 C CB  . ALA   D 1 63  ? 1.892   -9.343  54.503  1.00 13.27  ?  63  ALA   D CB  1 
ATOM   11581 N N   . ALA   D 1 64  ? 3.819   -9.332  57.097  1.00 18.45  ?  64  ALA   D N   1 
ATOM   11582 C CA  . ALA   D 1 64  ? 4.199   -9.888  58.392  1.00 18.61  ?  64  ALA   D CA  1 
ATOM   11583 C C   . ALA   D 1 64  ? 4.172   -8.819  59.471  1.00 17.61  ?  64  ALA   D C   1 
ATOM   11584 O O   . ALA   D 1 64  ? 3.748   -9.082  60.606  1.00 19.25  ?  64  ALA   D O   1 
ATOM   11585 C CB  . ALA   D 1 64  ? 5.579   -10.534 58.310  1.00 15.90  ?  64  ALA   D CB  1 
ATOM   11586 N N   A MET   D 1 65  ? 4.623   -7.604  59.139  0.54 15.00  ?  65  MET   D N   1 
ATOM   11587 N N   B MET   D 1 65  ? 4.619   -7.606  59.140  0.46 14.02  ?  65  MET   D N   1 
ATOM   11588 C CA  A MET   D 1 65  ? 4.598   -6.512  60.108  0.54 17.13  ?  65  MET   D CA  1 
ATOM   11589 C CA  B MET   D 1 65  ? 4.591   -6.519  60.113  0.46 18.16  ?  65  MET   D CA  1 
ATOM   11590 C C   A MET   D 1 65  ? 3.173   -6.195  60.547  0.54 17.73  ?  65  MET   D C   1 
ATOM   11591 C C   B MET   D 1 65  ? 3.168   -6.205  60.552  0.46 18.21  ?  65  MET   D C   1 
ATOM   11592 O O   A MET   D 1 65  ? 2.926   -5.922  61.728  0.54 18.54  ?  65  MET   D O   1 
ATOM   11593 O O   B MET   D 1 65  ? 2.916   -5.943  61.734  0.46 17.98  ?  65  MET   D O   1 
ATOM   11594 C CB  A MET   D 1 65  ? 5.262   -5.264  59.519  0.54 18.02  ?  65  MET   D CB  1 
ATOM   11595 C CB  B MET   D 1 65  ? 5.248   -5.277  59.520  0.46 18.51  ?  65  MET   D CB  1 
ATOM   11596 C CG  A MET   D 1 65  ? 6.781   -5.357  59.376  0.54 18.28  ?  65  MET   D CG  1 
ATOM   11597 C CG  B MET   D 1 65  ? 6.712   -5.462  59.198  0.46 18.29  ?  65  MET   D CG  1 
ATOM   11598 S SD  A MET   D 1 65  ? 7.642   -3.800  59.711  0.54 17.17  ?  65  MET   D SD  1 
ATOM   11599 S SD  B MET   D 1 65  ? 7.383   -4.020  58.371  0.46 16.83  ?  65  MET   D SD  1 
ATOM   11600 C CE  A MET   D 1 65  ? 6.871   -2.708  58.526  0.54 20.19  ?  65  MET   D CE  1 
ATOM   11601 C CE  B MET   D 1 65  ? 7.117   -2.757  59.606  0.46 18.79  ?  65  MET   D CE  1 
ATOM   11602 N N   . ILE   D 1 66  ? 2.223   -6.237  59.611  1.00 19.20  ?  66  ILE   D N   1 
ATOM   11603 C CA  . ILE   D 1 66  ? 0.849   -5.855  59.912  1.00 20.39  ?  66  ILE   D CA  1 
ATOM   11604 C C   . ILE   D 1 66  ? 0.185   -6.847  60.855  1.00 16.72  ?  66  ILE   D C   1 
ATOM   11605 O O   . ILE   D 1 66  ? -0.641  -6.456  61.691  1.00 18.95  ?  66  ILE   D O   1 
ATOM   11606 C CB  . ILE   D 1 66  ? 0.069   -5.689  58.595  1.00 19.19  ?  66  ILE   D CB  1 
ATOM   11607 C CG1 . ILE   D 1 66  ? 0.460   -4.370  57.941  1.00 24.95  ?  66  ILE   D CG1 1 
ATOM   11608 C CG2 . ILE   D 1 66  ? -1.427  -5.699  58.828  1.00 17.52  ?  66  ILE   D CG2 1 
ATOM   11609 C CD1 . ILE   D 1 66  ? -0.052  -3.150  58.696  1.00 32.86  ?  66  ILE   D CD1 1 
ATOM   11610 N N   . THR   D 1 67  ? 0.533   -8.130  60.768  1.00 15.58  ?  67  THR   D N   1 
ATOM   11611 C CA  . THR   D 1 67  ? -0.014  -9.108  61.697  1.00 17.76  ?  67  THR   D CA  1 
ATOM   11612 C C   . THR   D 1 67  ? 0.940   -9.417  62.851  1.00 17.33  ?  67  THR   D C   1 
ATOM   11613 O O   . THR   D 1 67  ? 0.728   -10.397 63.576  1.00 18.48  ?  67  THR   D O   1 
ATOM   11614 C CB  . THR   D 1 67  ? -0.417  -10.387 60.954  1.00 18.29  ?  67  THR   D CB  1 
ATOM   11615 O OG1 . THR   D 1 67  ? 0.678   -10.868 60.165  1.00 21.41  ?  67  THR   D OG1 1 
ATOM   11616 C CG2 . THR   D 1 67  ? -1.600  -10.113 60.032  1.00 17.91  ?  67  THR   D CG2 1 
ATOM   11617 N N   . GLY   D 1 68  ? 1.952   -8.576  63.069  1.00 17.24  ?  68  GLY   D N   1 
ATOM   11618 C CA  . GLY   D 1 68  ? 2.917   -8.832  64.129  1.00 14.76  ?  68  GLY   D CA  1 
ATOM   11619 C C   . GLY   D 1 68  ? 2.294   -8.734  65.514  1.00 18.29  ?  68  GLY   D C   1 
ATOM   11620 O O   . GLY   D 1 68  ? 1.440   -7.889  65.780  1.00 20.55  ?  68  GLY   D O   1 
ATOM   11621 N N   . ASP   D 1 69  ? 2.746   -9.606  66.408  1.00 15.60  ?  69  ASP   D N   1 
ATOM   11622 C CA  . ASP   D 1 69  ? 2.222   -9.700  67.768  1.00 13.75  ?  69  ASP   D CA  1 
ATOM   11623 C C   . ASP   D 1 69  ? 3.048   -8.795  68.683  1.00 19.13  ?  69  ASP   D C   1 
ATOM   11624 O O   . ASP   D 1 69  ? 4.223   -9.072  68.960  1.00 18.10  ?  69  ASP   D O   1 
ATOM   11625 C CB  . ASP   D 1 69  ? 2.260   -11.156 68.220  1.00 18.96  ?  69  ASP   D CB  1 
ATOM   11626 C CG  . ASP   D 1 69  ? 1.720   -11.366 69.620  1.00 22.94  ?  69  ASP   D CG  1 
ATOM   11627 O OD1 . ASP   D 1 69  ? 1.213   -10.404 70.242  1.00 19.64  ?  69  ASP   D OD1 1 
ATOM   11628 O OD2 . ASP   D 1 69  ? 1.823   -12.519 70.103  1.00 21.24  ?  69  ASP   D OD2 1 
ATOM   11629 N N   . GLU   D 1 70  ? 2.425   -7.732  69.179  1.00 20.92  ?  70  GLU   D N   1 
ATOM   11630 C CA  . GLU   D 1 70  ? 3.095   -6.725  69.988  1.00 20.01  ?  70  GLU   D CA  1 
ATOM   11631 C C   . GLU   D 1 70  ? 3.132   -7.070  71.478  1.00 19.03  ?  70  GLU   D C   1 
ATOM   11632 O O   . GLU   D 1 70  ? 3.535   -6.220  72.286  1.00 18.45  ?  70  GLU   D O   1 
ATOM   11633 C CB  . GLU   D 1 70  ? 2.429   -5.357  69.765  1.00 18.99  ?  70  GLU   D CB  1 
ATOM   11634 C CG  . GLU   D 1 70  ? 2.608   -4.813  68.333  1.00 16.11  ?  70  GLU   D CG  1 
ATOM   11635 C CD  . GLU   D 1 70  ? 4.076   -4.530  67.989  1.00 19.42  ?  70  GLU   D CD  1 
ATOM   11636 O OE1 . GLU   D 1 70  ? 4.907   -4.412  68.922  1.00 16.64  ?  70  GLU   D OE1 1 
ATOM   11637 O OE2 . GLU   D 1 70  ? 4.406   -4.427  66.785  1.00 18.39  ?  70  GLU   D OE2 1 
ATOM   11638 N N   . ALA   D 1 71  ? 2.771   -8.303  71.847  1.00 21.11  ?  71  ALA   D N   1 
ATOM   11639 C CA  . ALA   D 1 71  ? 2.738   -8.717  73.249  1.00 21.60  ?  71  ALA   D CA  1 
ATOM   11640 C C   . ALA   D 1 71  ? 4.083   -8.501  73.929  1.00 20.28  ?  71  ALA   D C   1 
ATOM   11641 O O   . ALA   D 1 71  ? 5.142   -8.778  73.357  1.00 21.70  ?  71  ALA   D O   1 
ATOM   11642 C CB  . ALA   D 1 71  ? 2.339   -10.192 73.358  1.00 19.98  ?  71  ALA   D CB  1 
ATOM   11643 N N   . TYR   D 1 72  ? 4.039   -8.019  75.176  1.00 19.85  ?  72  TYR   D N   1 
ATOM   11644 C CA  . TYR   D 1 72  ? 5.283   -7.721  75.872  1.00 20.15  ?  72  TYR   D CA  1 
ATOM   11645 C C   . TYR   D 1 72  ? 6.070   -8.989  76.164  1.00 22.82  ?  72  TYR   D C   1 
ATOM   11646 O O   . TYR   D 1 72  ? 7.307   -8.964  76.150  1.00 24.59  ?  72  TYR   D O   1 
ATOM   11647 C CB  . TYR   D 1 72  ? 4.999   -6.958  77.166  1.00 22.18  ?  72  TYR   D CB  1 
ATOM   11648 C CG  . TYR   D 1 72  ? 6.223   -6.342  77.798  1.00 19.58  ?  72  TYR   D CG  1 
ATOM   11649 C CD1 . TYR   D 1 72  ? 6.637   -5.058  77.459  1.00 22.03  ?  72  TYR   D CD1 1 
ATOM   11650 C CD2 . TYR   D 1 72  ? 6.976   -7.048  78.728  1.00 22.12  ?  72  TYR   D CD2 1 
ATOM   11651 C CE1 . TYR   D 1 72  ? 7.771   -4.491  78.038  1.00 18.96  ?  72  TYR   D CE1 1 
ATOM   11652 C CE2 . TYR   D 1 72  ? 8.108   -6.490  79.309  1.00 24.36  ?  72  TYR   D CE2 1 
ATOM   11653 C CZ  . TYR   D 1 72  ? 8.502   -5.213  78.954  1.00 23.79  ?  72  TYR   D CZ  1 
ATOM   11654 O OH  . TYR   D 1 72  ? 9.627   -4.672  79.536  1.00 35.10  ?  72  TYR   D OH  1 
ATOM   11655 N N   . ALA   D 1 73  ? 5.377   -10.100 76.416  1.00 20.47  ?  73  ALA   D N   1 
ATOM   11656 C CA  . ALA   D 1 73  ? 6.014   -11.366 76.761  1.00 21.92  ?  73  ALA   D CA  1 
ATOM   11657 C C   . ALA   D 1 73  ? 5.385   -12.488 75.950  1.00 19.84  ?  73  ALA   D C   1 
ATOM   11658 O O   . ALA   D 1 73  ? 4.157   -12.610 75.903  1.00 24.33  ?  73  ALA   D O   1 
ATOM   11659 C CB  . ALA   D 1 73  ? 5.881   -11.664 78.255  1.00 19.80  ?  73  ALA   D CB  1 
ATOM   11660 N N   . GLY   D 1 74  ? 6.221   -13.308 75.321  1.00 17.81  ?  74  GLY   D N   1 
ATOM   11661 C CA  . GLY   D 1 74  ? 5.712   -14.458 74.598  1.00 22.04  ?  74  GLY   D CA  1 
ATOM   11662 C C   . GLY   D 1 74  ? 5.101   -14.161 73.251  1.00 20.27  ?  74  GLY   D C   1 
ATOM   11663 O O   . GLY   D 1 74  ? 4.201   -14.892 72.813  1.00 22.01  ?  74  GLY   D O   1 
ATOM   11664 N N   . SER   D 1 75  ? 5.562   -13.109 72.574  1.00 19.81  ?  75  SER   D N   1 
ATOM   11665 C CA  . SER   D 1 75  ? 5.041   -12.774 71.256  1.00 19.53  ?  75  SER   D CA  1 
ATOM   11666 C C   . SER   D 1 75  ? 5.133   -13.966 70.316  1.00 19.41  ?  75  SER   D C   1 
ATOM   11667 O O   . SER   D 1 75  ? 6.105   -14.729 70.343  1.00 20.94  ?  75  SER   D O   1 
ATOM   11668 C CB  . SER   D 1 75  ? 5.809   -11.591 70.660  1.00 20.01  ?  75  SER   D CB  1 
ATOM   11669 O OG  . SER   D 1 75  ? 5.569   -11.493 69.262  1.00 20.14  ?  75  SER   D OG  1 
ATOM   11670 N N   . ARG   D 1 76  ? 4.100   -14.128 69.491  1.00 17.37  ?  76  ARG   D N   1 
ATOM   11671 C CA  A ARG   D 1 76  ? 4.092   -15.200 68.501  0.55 20.23  ?  76  ARG   D CA  1 
ATOM   11672 C CA  B ARG   D 1 76  ? 4.104   -15.212 68.515  0.45 20.23  ?  76  ARG   D CA  1 
ATOM   11673 C C   . ARG   D 1 76  ? 5.341   -15.153 67.630  1.00 18.36  ?  76  ARG   D C   1 
ATOM   11674 O O   . ARG   D 1 76  ? 5.891   -16.196 67.253  1.00 18.14  ?  76  ARG   D O   1 
ATOM   11675 C CB  A ARG   D 1 76  ? 2.828   -15.097 67.638  0.55 22.16  ?  76  ARG   D CB  1 
ATOM   11676 C CB  B ARG   D 1 76  ? 2.835   -15.161 67.666  0.45 22.16  ?  76  ARG   D CB  1 
ATOM   11677 C CG  A ARG   D 1 76  ? 2.577   -16.288 66.720  0.55 22.44  ?  76  ARG   D CG  1 
ATOM   11678 C CG  B ARG   D 1 76  ? 1.562   -15.409 68.448  0.45 23.46  ?  76  ARG   D CG  1 
ATOM   11679 C CD  A ARG   D 1 76  ? 1.390   -16.040 65.793  0.55 22.06  ?  76  ARG   D CD  1 
ATOM   11680 C CD  B ARG   D 1 76  ? 0.382   -15.562 67.517  0.45 23.59  ?  76  ARG   D CD  1 
ATOM   11681 N NE  A ARG   D 1 76  ? 1.718   -15.079 64.747  0.55 22.11  ?  76  ARG   D NE  1 
ATOM   11682 N NE  B ARG   D 1 76  ? 0.297   -14.442 66.590  0.45 24.95  ?  76  ARG   D NE  1 
ATOM   11683 C CZ  A ARG   D 1 76  ? 1.331   -13.811 64.741  0.55 21.46  ?  76  ARG   D CZ  1 
ATOM   11684 C CZ  B ARG   D 1 76  ? -0.397  -13.336 66.817  0.45 23.71  ?  76  ARG   D CZ  1 
ATOM   11685 N NH1 A ARG   D 1 76  ? 0.540   -13.326 65.683  0.55 22.50  ?  76  ARG   D NH1 1 
ATOM   11686 N NH1 B ARG   D 1 76  ? -1.097  -13.176 67.927  0.45 20.54  ?  76  ARG   D NH1 1 
ATOM   11687 N NH2 A ARG   D 1 76  ? 1.748   -13.009 63.764  0.55 19.70  ?  76  ARG   D NH2 1 
ATOM   11688 N NH2 B ARG   D 1 76  ? -0.391  -12.368 65.904  0.45 23.42  ?  76  ARG   D NH2 1 
ATOM   11689 N N   . ASN   D 1 77  ? 5.807   -13.943 67.306  1.00 18.64  ?  77  ASN   D N   1 
ATOM   11690 C CA  . ASN   D 1 77  ? 6.939   -13.763 66.407  1.00 16.72  ?  77  ASN   D CA  1 
ATOM   11691 C C   . ASN   D 1 77  ? 8.276   -14.054 67.066  1.00 18.31  ?  77  ASN   D C   1 
ATOM   11692 O O   . ASN   D 1 77  ? 9.239   -14.362 66.354  1.00 17.47  ?  77  ASN   D O   1 
ATOM   11693 C CB  . ASN   D 1 77  ? 6.920   -12.343 65.849  1.00 17.47  ?  77  ASN   D CB  1 
ATOM   11694 C CG  . ASN   D 1 77  ? 5.545   -11.952 65.319  1.00 17.67  ?  77  ASN   D CG  1 
ATOM   11695 O OD1 . ASN   D 1 77  ? 4.822   -11.162 65.939  1.00 16.42  ?  77  ASN   D OD1 1 
ATOM   11696 N ND2 . ASN   D 1 77  ? 5.168   -12.524 64.174  1.00 14.85  ?  77  ASN   D ND2 1 
ATOM   11697 N N   . TYR   D 1 78  ? 8.366   -13.972 68.400  1.00 12.77  ?  78  TYR   D N   1 
ATOM   11698 C CA  . TYR   D 1 78  ? 9.573   -14.445 69.070  1.00 13.09  ?  78  TYR   D CA  1 
ATOM   11699 C C   . TYR   D 1 78  ? 9.767   -15.944 68.857  1.00 16.45  ?  78  TYR   D C   1 
ATOM   11700 O O   . TYR   D 1 78  ? 10.885  -16.403 68.589  1.00 16.97  ?  78  TYR   D O   1 
ATOM   11701 C CB  . TYR   D 1 78  ? 9.523   -14.126 70.568  1.00 12.85  ?  78  TYR   D CB  1 
ATOM   11702 C CG  . TYR   D 1 78  ? 10.523  -14.924 71.374  1.00 13.94  ?  78  TYR   D CG  1 
ATOM   11703 C CD1 . TYR   D 1 78  ? 11.845  -14.510 71.484  1.00 14.61  ?  78  TYR   D CD1 1 
ATOM   11704 C CD2 . TYR   D 1 78  ? 10.143  -16.097 72.020  1.00 16.27  ?  78  TYR   D CD2 1 
ATOM   11705 C CE1 . TYR   D 1 78  ? 12.764  -15.244 72.222  1.00 15.91  ?  78  TYR   D CE1 1 
ATOM   11706 C CE2 . TYR   D 1 78  ? 11.046  -16.836 72.750  1.00 18.34  ?  78  TYR   D CE2 1 
ATOM   11707 C CZ  . TYR   D 1 78  ? 12.354  -16.409 72.851  1.00 19.02  ?  78  TYR   D CZ  1 
ATOM   11708 O OH  . TYR   D 1 78  ? 13.244  -17.162 73.583  1.00 20.33  ?  78  TYR   D OH  1 
ATOM   11709 N N   . TYR   D 1 79  ? 8.694   -16.729 69.000  1.00 16.47  ?  79  TYR   D N   1 
ATOM   11710 C CA  . TYR   D 1 79  ? 8.818   -18.166 68.806  1.00 13.94  ?  79  TYR   D CA  1 
ATOM   11711 C C   . TYR   D 1 79  ? 9.107   -18.494 67.352  1.00 21.65  ?  79  TYR   D C   1 
ATOM   11712 O O   . TYR   D 1 79  ? 9.829   -19.458 67.069  1.00 19.71  ?  79  TYR   D O   1 
ATOM   11713 C CB  . TYR   D 1 79  ? 7.552   -18.878 69.276  1.00 20.03  ?  79  TYR   D CB  1 
ATOM   11714 C CG  . TYR   D 1 79  ? 7.283   -18.669 70.749  1.00 21.03  ?  79  TYR   D CG  1 
ATOM   11715 C CD1 . TYR   D 1 79  ? 8.027   -19.350 71.714  1.00 23.90  ?  79  TYR   D CD1 1 
ATOM   11716 C CD2 . TYR   D 1 79  ? 6.315   -17.769 71.182  1.00 22.32  ?  79  TYR   D CD2 1 
ATOM   11717 C CE1 . TYR   D 1 79  ? 7.801   -19.152 73.077  1.00 19.89  ?  79  TYR   D CE1 1 
ATOM   11718 C CE2 . TYR   D 1 79  ? 6.086   -17.566 72.545  1.00 20.52  ?  79  TYR   D CE2 1 
ATOM   11719 C CZ  . TYR   D 1 79  ? 6.837   -18.264 73.480  1.00 22.42  ?  79  TYR   D CZ  1 
ATOM   11720 O OH  . TYR   D 1 79  ? 6.618   -18.068 74.827  1.00 27.49  ?  79  TYR   D OH  1 
ATOM   11721 N N   . ASP   D 1 80  ? 8.556   -17.708 66.425  1.00 16.00  ?  80  ASP   D N   1 
ATOM   11722 C CA  . ASP   D 1 80  ? 8.894   -17.881 65.016  1.00 20.03  ?  80  ASP   D CA  1 
ATOM   11723 C C   . ASP   D 1 80  ? 10.371  -17.601 64.777  1.00 17.78  ?  80  ASP   D C   1 
ATOM   11724 O O   . ASP   D 1 80  ? 11.054  -18.358 64.076  1.00 18.55  ?  80  ASP   D O   1 
ATOM   11725 C CB  . ASP   D 1 80  ? 8.026   -16.968 64.153  1.00 16.69  ?  80  ASP   D CB  1 
ATOM   11726 C CG  . ASP   D 1 80  ? 6.589   -17.444 64.056  1.00 23.63  ?  80  ASP   D CG  1 
ATOM   11727 O OD1 . ASP   D 1 80  ? 6.333   -18.637 64.350  1.00 27.50  ?  80  ASP   D OD1 1 
ATOM   11728 O OD2 . ASP   D 1 80  ? 5.717   -16.632 63.666  1.00 21.53  ?  80  ASP   D OD2 1 
ATOM   11729 N N   . LEU   D 1 81  ? 10.882  -16.512 65.351  1.00 16.16  ?  81  LEU   D N   1 
ATOM   11730 C CA  . LEU   D 1 81  ? 12.285  -16.171 65.146  1.00 15.80  ?  81  LEU   D CA  1 
ATOM   11731 C C   . LEU   D 1 81  ? 13.195  -17.221 65.767  1.00 20.34  ?  81  LEU   D C   1 
ATOM   11732 O O   . LEU   D 1 81  ? 14.264  -17.534 65.227  1.00 18.37  ?  81  LEU   D O   1 
ATOM   11733 C CB  . LEU   D 1 81  ? 12.570  -14.787 65.727  1.00 16.84  ?  81  LEU   D CB  1 
ATOM   11734 C CG  . LEU   D 1 81  ? 13.985  -14.243 65.563  1.00 17.34  ?  81  LEU   D CG  1 
ATOM   11735 C CD1 . LEU   D 1 81  ? 14.349  -14.208 64.088  1.00 19.01  ?  81  LEU   D CD1 1 
ATOM   11736 C CD2 . LEU   D 1 81  ? 14.079  -12.858 66.166  1.00 16.39  ?  81  LEU   D CD2 1 
ATOM   11737 N N   . LYS   D 1 82  ? 12.784  -17.777 66.903  1.00 18.85  ?  82  LYS   D N   1 
ATOM   11738 C CA  . LYS   D 1 82  ? 13.565  -18.831 67.536  1.00 18.15  ?  82  LYS   D CA  1 
ATOM   11739 C C   . LYS   D 1 82  ? 13.618  -20.070 66.652  1.00 21.37  ?  82  LYS   D C   1 
ATOM   11740 O O   . LYS   D 1 82  ? 14.685  -20.673 66.477  1.00 21.45  ?  82  LYS   D O   1 
ATOM   11741 C CB  . LYS   D 1 82  ? 12.961  -19.148 68.906  1.00 17.34  ?  82  LYS   D CB  1 
ATOM   11742 C CG  . LYS   D 1 82  ? 13.715  -20.163 69.734  1.00 17.82  ?  82  LYS   D CG  1 
ATOM   11743 C CD  . LYS   D 1 82  ? 12.996  -20.390 71.050  1.00 18.85  ?  82  LYS   D CD  1 
ATOM   11744 C CE  . LYS   D 1 82  ? 13.127  -21.827 71.530  1.00 27.46  ?  82  LYS   D CE  1 
ATOM   11745 N NZ  . LYS   D 1 82  ? 14.519  -22.161 71.920  1.00 31.31  ?  82  LYS   D NZ  1 
ATOM   11746 N N   . ASP   D 1 83  ? 12.477  -20.453 66.074  1.00 17.27  ?  83  ASP   D N   1 
ATOM   11747 C CA  . ASP   D 1 83  ? 12.444  -21.601 65.171  1.00 22.02  ?  83  ASP   D CA  1 
ATOM   11748 C C   . ASP   D 1 83  ? 13.285  -21.351 63.926  1.00 21.09  ?  83  ASP   D C   1 
ATOM   11749 O O   . ASP   D 1 83  ? 13.897  -22.280 63.385  1.00 21.21  ?  83  ASP   D O   1 
ATOM   11750 C CB  . ASP   D 1 83  ? 11.003  -21.919 64.760  1.00 18.15  ?  83  ASP   D CB  1 
ATOM   11751 C CG  . ASP   D 1 83  ? 10.123  -22.335 65.928  1.00 24.37  ?  83  ASP   D CG  1 
ATOM   11752 O OD1 . ASP   D 1 83  ? 10.625  -22.469 67.065  1.00 25.89  ?  83  ASP   D OD1 1 
ATOM   11753 O OD2 . ASP   D 1 83  ? 8.905   -22.523 65.700  1.00 26.32  ?  83  ASP   D OD2 1 
ATOM   11754 N N   . LYS   D 1 84  ? 13.310  -20.104 63.444  1.00 19.46  ?  84  LYS   D N   1 
ATOM   11755 C CA  . LYS   D 1 84  ? 14.040  -19.793 62.217  1.00 19.12  ?  84  LYS   D CA  1 
ATOM   11756 C C   . LYS   D 1 84  ? 15.545  -19.868 62.437  1.00 21.85  ?  84  LYS   D C   1 
ATOM   11757 O O   . LYS   D 1 84  ? 16.288  -20.304 61.548  1.00 21.58  ?  84  LYS   D O   1 
ATOM   11758 C CB  . LYS   D 1 84  ? 13.643  -18.409 61.710  1.00 16.32  ?  84  LYS   D CB  1 
ATOM   11759 C CG  . LYS   D 1 84  ? 14.101  -18.108 60.296  1.00 18.56  ?  84  LYS   D CG  1 
ATOM   11760 C CD  . LYS   D 1 84  ? 13.418  -19.030 59.296  1.00 20.22  ?  84  LYS   D CD  1 
ATOM   11761 C CE  . LYS   D 1 84  ? 13.846  -18.718 57.865  1.00 25.28  ?  84  LYS   D CE  1 
ATOM   11762 N NZ  . LYS   D 1 84  ? 13.205  -19.617 56.857  1.00 27.17  ?  84  LYS   D NZ  1 
ATOM   11763 N N   . ALA   D 1 85  ? 16.017  -19.438 63.608  1.00 18.94  ?  85  ALA   D N   1 
ATOM   11764 C CA  . ALA   D 1 85  ? 17.439  -19.551 63.906  1.00 17.10  ?  85  ALA   D CA  1 
ATOM   11765 C C   . ALA   D 1 85  ? 17.847  -21.006 64.067  1.00 22.25  ?  85  ALA   D C   1 
ATOM   11766 O O   . ALA   D 1 85  ? 18.954  -21.395 63.676  1.00 21.34  ?  85  ALA   D O   1 
ATOM   11767 C CB  . ALA   D 1 85  ? 17.786  -18.758 65.161  1.00 14.87  ?  85  ALA   D CB  1 
ATOM   11768 N N   . LYS   D 1 86  ? 16.967  -21.827 64.642  1.00 19.86  ?  86  LYS   D N   1 
ATOM   11769 C CA  . LYS   D 1 86  ? 17.243  -23.256 64.711  1.00 17.93  ?  86  LYS   D CA  1 
ATOM   11770 C C   . LYS   D 1 86  ? 17.294  -23.874 63.322  1.00 19.50  ?  86  LYS   D C   1 
ATOM   11771 O O   . LYS   D 1 86  ? 18.109  -24.764 63.070  1.00 23.53  ?  86  LYS   D O   1 
ATOM   11772 C CB  . LYS   D 1 86  ? 16.191  -23.953 65.562  1.00 21.35  ?  86  LYS   D CB  1 
ATOM   11773 C CG  . LYS   D 1 86  ? 16.445  -25.432 65.744  1.00 25.63  ?  86  LYS   D CG  1 
ATOM   11774 C CD  . LYS   D 1 86  ? 17.806  -25.675 66.363  1.00 25.33  ?  86  LYS   D CD  1 
ATOM   11775 C CE  . LYS   D 1 86  ? 17.997  -27.141 66.698  1.00 23.61  ?  86  LYS   D CE  1 
ATOM   11776 N NZ  . LYS   D 1 86  ? 19.354  -27.371 67.242  1.00 24.44  ?  86  LYS   D NZ  1 
ATOM   11777 N N   . GLU   D 1 87  ? 16.446  -23.403 62.400  1.00 22.48  ?  87  GLU   D N   1 
ATOM   11778 C CA  . GLU   D 1 87  ? 16.471  -23.924 61.035  1.00 23.31  ?  87  GLU   D CA  1 
ATOM   11779 C C   . GLU   D 1 87  ? 17.726  -23.490 60.286  1.00 25.60  ?  87  GLU   D C   1 
ATOM   11780 O O   . GLU   D 1 87  ? 18.359  -24.303 59.602  1.00 28.80  ?  87  GLU   D O   1 
ATOM   11781 C CB  . GLU   D 1 87  ? 15.231  -23.472 60.263  1.00 22.87  ?  87  GLU   D CB  1 
ATOM   11782 C CG  . GLU   D 1 87  ? 15.424  -23.549 58.753  1.00 30.59  ?  87  GLU   D CG  1 
ATOM   11783 C CD  . GLU   D 1 87  ? 14.356  -22.804 57.960  1.00 32.61  ?  87  GLU   D CD  1 
ATOM   11784 O OE1 . GLU   D 1 87  ? 13.379  -22.325 58.573  1.00 33.81  ?  87  GLU   D OE1 1 
ATOM   11785 O OE2 . GLU   D 1 87  ? 14.496  -22.704 56.719  1.00 39.46  ?  87  GLU   D OE2 1 
ATOM   11786 N N   . LEU   D 1 88  ? 18.097  -22.213 60.392  1.00 25.47  ?  88  LEU   D N   1 
ATOM   11787 C CA  . LEU   D 1 88  ? 19.172  -21.676 59.563  1.00 23.49  ?  88  LEU   D CA  1 
ATOM   11788 C C   . LEU   D 1 88  ? 20.548  -22.066 60.091  1.00 24.58  ?  88  LEU   D C   1 
ATOM   11789 O O   . LEU   D 1 88  ? 21.410  -22.514 59.327  1.00 23.88  ?  88  LEU   D O   1 
ATOM   11790 C CB  . LEU   D 1 88  ? 19.066  -20.154 59.485  1.00 21.44  ?  88  LEU   D CB  1 
ATOM   11791 C CG  . LEU   D 1 88  ? 18.045  -19.551 58.538  1.00 23.58  ?  88  LEU   D CG  1 
ATOM   11792 C CD1 . LEU   D 1 88  ? 18.249  -18.048 58.497  1.00 19.26  ?  88  LEU   D CD1 1 
ATOM   11793 C CD2 . LEU   D 1 88  ? 18.191  -20.172 57.149  1.00 25.26  ?  88  LEU   D CD2 1 
ATOM   11794 N N   . PHE   D 1 89  ? 20.770  -21.890 61.392  1.00 23.83  ?  89  PHE   D N   1 
ATOM   11795 C CA  . PHE   D 1 89  ? 22.086  -22.037 61.991  1.00 23.01  ?  89  PHE   D CA  1 
ATOM   11796 C C   . PHE   D 1 89  ? 22.230  -23.268 62.873  1.00 24.88  ?  89  PHE   D C   1 
ATOM   11797 O O   . PHE   D 1 89  ? 23.354  -23.581 63.280  1.00 22.57  ?  89  PHE   D O   1 
ATOM   11798 C CB  . PHE   D 1 89  ? 22.411  -20.803 62.833  1.00 20.56  ?  89  PHE   D CB  1 
ATOM   11799 C CG  . PHE   D 1 89  ? 21.961  -19.513 62.223  1.00 20.56  ?  89  PHE   D CG  1 
ATOM   11800 C CD1 . PHE   D 1 89  ? 22.563  -19.029 61.072  1.00 22.68  ?  89  PHE   D CD1 1 
ATOM   11801 C CD2 . PHE   D 1 89  ? 20.959  -18.765 62.822  1.00 17.71  ?  89  PHE   D CD2 1 
ATOM   11802 C CE1 . PHE   D 1 89  ? 22.161  -17.824 60.519  1.00 21.83  ?  89  PHE   D CE1 1 
ATOM   11803 C CE2 . PHE   D 1 89  ? 20.552  -17.572 62.285  1.00 15.09  ?  89  PHE   D CE2 1 
ATOM   11804 C CZ  . PHE   D 1 89  ? 21.151  -17.098 61.124  1.00 19.17  ?  89  PHE   D CZ  1 
ATOM   11805 N N   . ASN   D 1 90  ? 21.131  -23.956 63.191  1.00 20.07  ?  90  ASN   D N   1 
ATOM   11806 C CA  . ASN   D 1 90  ? 21.113  -25.069 64.139  1.00 22.20  ?  90  ASN   D CA  1 
ATOM   11807 C C   . ASN   D 1 90  ? 21.436  -24.622 65.566  1.00 22.99  ?  90  ASN   D C   1 
ATOM   11808 O O   . ASN   D 1 90  ? 21.957  -25.404 66.364  1.00 25.88  ?  90  ASN   D O   1 
ATOM   11809 C CB  . ASN   D 1 90  ? 22.063  -26.191 63.703  1.00 27.01  ?  90  ASN   D CB  1 
ATOM   11810 C CG  . ASN   D 1 90  ? 21.701  -27.529 64.311  1.00 27.74  ?  90  ASN   D CG  1 
ATOM   11811 O OD1 . ASN   D 1 90  ? 20.599  -27.705 64.833  1.00 22.68  ?  90  ASN   D OD1 1 
ATOM   11812 N ND2 . ASN   D 1 90  ? 22.629  -28.483 64.245  1.00 25.06  ?  90  ASN   D ND2 1 
ATOM   11813 N N   . TYR   D 1 91  ? 21.120  -23.377 65.922  1.00 21.35  ?  91  TYR   D N   1 
ATOM   11814 C CA  . TYR   D 1 91  ? 21.403  -22.863 67.256  1.00 18.54  ?  91  TYR   D CA  1 
ATOM   11815 C C   . TYR   D 1 91  ? 20.148  -22.930 68.115  1.00 21.27  ?  91  TYR   D C   1 
ATOM   11816 O O   . TYR   D 1 91  ? 19.051  -22.604 67.654  1.00 18.57  ?  91  TYR   D O   1 
ATOM   11817 C CB  . TYR   D 1 91  ? 21.925  -21.428 67.198  1.00 18.97  ?  91  TYR   D CB  1 
ATOM   11818 C CG  . TYR   D 1 91  ? 23.332  -21.289 66.644  1.00 20.24  ?  91  TYR   D CG  1 
ATOM   11819 C CD1 . TYR   D 1 91  ? 24.018  -22.386 66.118  1.00 21.10  ?  91  TYR   D CD1 1 
ATOM   11820 C CD2 . TYR   D 1 91  ? 23.977  -20.058 66.659  1.00 17.12  ?  91  TYR   D CD2 1 
ATOM   11821 C CE1 . TYR   D 1 91  ? 25.315  -22.249 65.620  1.00 19.60  ?  91  TYR   D CE1 1 
ATOM   11822 C CE2 . TYR   D 1 91  ? 25.263  -19.911 66.164  1.00 16.93  ?  91  TYR   D CE2 1 
ATOM   11823 C CZ  . TYR   D 1 91  ? 25.924  -21.002 65.643  1.00 20.64  ?  91  TYR   D CZ  1 
ATOM   11824 O OH  . TYR   D 1 91  ? 27.202  -20.833 65.157  1.00 19.08  ?  91  TYR   D OH  1 
ATOM   11825 N N   . ASP   D 1 92  ? 20.317  -23.348 69.373  1.00 21.26  ?  92  ASP   D N   1 
ATOM   11826 C CA  . ASP   D 1 92  ? 19.170  -23.642 70.225  1.00 21.11  ?  92  ASP   D CA  1 
ATOM   11827 C C   . ASP   D 1 92  ? 18.586  -22.416 70.926  1.00 21.96  ?  92  ASP   D C   1 
ATOM   11828 O O   . ASP   D 1 92  ? 17.449  -22.490 71.401  1.00 21.02  ?  92  ASP   D O   1 
ATOM   11829 C CB  . ASP   D 1 92  ? 19.559  -24.690 71.271  1.00 22.46  ?  92  ASP   D CB  1 
ATOM   11830 C CG  . ASP   D 1 92  ? 19.731  -26.087 70.673  1.00 28.68  ?  92  ASP   D CG  1 
ATOM   11831 O OD1 . ASP   D 1 92  ? 19.091  -26.383 69.637  1.00 33.91  ?  92  ASP   D OD1 1 
ATOM   11832 O OD2 . ASP   D 1 92  ? 20.498  -26.893 71.242  1.00 28.62  ?  92  ASP   D OD2 1 
ATOM   11833 N N   . TYR   D 1 93  ? 19.321  -21.301 71.012  1.00 19.88  ?  93  TYR   D N   1 
ATOM   11834 C CA  . TYR   D 1 93  ? 18.927  -20.177 71.855  1.00 19.34  ?  93  TYR   D CA  1 
ATOM   11835 C C   . TYR   D 1 93  ? 19.011  -18.870 71.082  1.00 19.40  ?  93  TYR   D C   1 
ATOM   11836 O O   . TYR   D 1 93  ? 19.978  -18.642 70.351  1.00 19.10  ?  93  TYR   D O   1 
ATOM   11837 C CB  . TYR   D 1 93  ? 19.816  -20.079 73.106  1.00 19.41  ?  93  TYR   D CB  1 
ATOM   11838 C CG  . TYR   D 1 93  ? 19.882  -21.353 73.924  1.00 21.22  ?  93  TYR   D CG  1 
ATOM   11839 C CD1 . TYR   D 1 93  ? 18.771  -21.805 74.622  1.00 21.43  ?  93  TYR   D CD1 1 
ATOM   11840 C CD2 . TYR   D 1 93  ? 21.054  -22.097 74.004  1.00 22.09  ?  93  TYR   D CD2 1 
ATOM   11841 C CE1 . TYR   D 1 93  ? 18.815  -22.965 75.372  1.00 24.22  ?  93  TYR   D CE1 1 
ATOM   11842 C CE2 . TYR   D 1 93  ? 21.111  -23.270 74.765  1.00 24.42  ?  93  TYR   D CE2 1 
ATOM   11843 C CZ  . TYR   D 1 93  ? 19.982  -23.699 75.437  1.00 26.67  ?  93  TYR   D CZ  1 
ATOM   11844 O OH  . TYR   D 1 93  ? 20.000  -24.850 76.189  1.00 24.51  ?  93  TYR   D OH  1 
ATOM   11845 N N   . ILE   D 1 94  ? 18.011  -17.998 71.261  1.00 17.60  ?  94  ILE   D N   1 
ATOM   11846 C CA  . ILE   D 1 94  ? 18.020  -16.678 70.637  1.00 16.72  ?  94  ILE   D CA  1 
ATOM   11847 C C   . ILE   D 1 94  ? 17.682  -15.598 71.656  1.00 13.14  ?  94  ILE   D C   1 
ATOM   11848 O O   . ILE   D 1 94  ? 16.955  -15.824 72.629  1.00 15.46  ?  94  ILE   D O   1 
ATOM   11849 C CB  . ILE   D 1 94  ? 17.058  -16.582 69.430  1.00 16.03  ?  94  ILE   D CB  1 
ATOM   11850 C CG1 . ILE   D 1 94  ? 15.595  -16.661 69.876  1.00 18.22  ?  94  ILE   D CG1 1 
ATOM   11851 C CG2 . ILE   D 1 94  ? 17.391  -17.653 68.417  1.00 17.65  ?  94  ILE   D CG2 1 
ATOM   11852 C CD1 . ILE   D 1 94  ? 14.651  -15.821 69.023  1.00 15.95  ?  94  ILE   D CD1 1 
ATOM   11853 N N   . ILE   D 1 95  ? 18.250  -14.420 71.436  1.00 14.28  ?  95  ILE   D N   1 
ATOM   11854 C CA  . ILE   D 1 95  ? 17.883  -13.196 72.146  1.00 16.27  ?  95  ILE   D CA  1 
ATOM   11855 C C   . ILE   D 1 95  ? 17.774  -12.115 71.078  1.00 14.83  ?  95  ILE   D C   1 
ATOM   11856 O O   . ILE   D 1 95  ? 18.791  -11.771 70.463  1.00 13.57  ?  95  ILE   D O   1 
ATOM   11857 C CB  . ILE   D 1 95  ? 18.916  -12.794 73.213  1.00 14.95  ?  95  ILE   D CB  1 
ATOM   11858 C CG1 . ILE   D 1 95  ? 19.285  -13.963 74.125  1.00 15.72  ?  95  ILE   D CG1 1 
ATOM   11859 C CG2 . ILE   D 1 95  ? 18.392  -11.626 74.065  1.00 13.06  ?  95  ILE   D CG2 1 
ATOM   11860 C CD1 . ILE   D 1 95  ? 20.306  -13.576 75.171  1.00 13.54  ?  95  ILE   D CD1 1 
ATOM   11861 N N   . PRO   D 1 96  ? 16.596  -11.567 70.800  1.00 12.30  ?  96  PRO   D N   1 
ATOM   11862 C CA  . PRO   D 1 96  ? 16.531  -10.475 69.833  1.00 10.15  ?  96  PRO   D CA  1 
ATOM   11863 C C   . PRO   D 1 96  ? 17.173  -9.236  70.425  1.00 12.24  ?  96  PRO   D C   1 
ATOM   11864 O O   . PRO   D 1 96  ? 17.301  -9.091  71.642  1.00 12.28  ?  96  PRO   D O   1 
ATOM   11865 C CB  . PRO   D 1 96  ? 15.031  -10.290 69.588  1.00 12.51  ?  96  PRO   D CB  1 
ATOM   11866 C CG  . PRO   D 1 96  ? 14.372  -10.842 70.800  1.00 17.47  ?  96  PRO   D CG  1 
ATOM   11867 C CD  . PRO   D 1 96  ? 15.281  -11.889 71.379  1.00 15.12  ?  96  PRO   D CD  1 
ATOM   11868 N N   . ALA   D 1 97  ? 17.657  -8.376  69.535  1.00 13.03  ?  97  ALA   D N   1 
ATOM   11869 C CA  . ALA   D 1 97  ? 18.283  -7.118  69.908  1.00 14.14  ?  97  ALA   D CA  1 
ATOM   11870 C C   . ALA   D 1 97  ? 17.754  -6.050  68.965  1.00 13.47  ?  97  ALA   D C   1 
ATOM   11871 O O   . ALA   D 1 97  ? 17.213  -6.355  67.900  1.00 16.34  ?  97  ALA   D O   1 
ATOM   11872 C CB  . ALA   D 1 97  ? 19.813  -7.202  69.839  1.00 15.35  ?  97  ALA   D CB  1 
ATOM   11873 N N   . HIS   D 1 98  ? 17.888  -4.786  69.364  1.00 14.45  ?  98  HIS   D N   1 
ATOM   11874 C CA  . HIS   D 1 98  ? 17.293  -3.748  68.533  1.00 14.03  ?  98  HIS   D CA  1 
ATOM   11875 C C   . HIS   D 1 98  ? 18.116  -3.514  67.278  1.00 13.76  ?  98  HIS   D C   1 
ATOM   11876 O O   . HIS   D 1 98  ? 17.561  -3.096  66.260  1.00 13.95  ?  98  HIS   D O   1 
ATOM   11877 C CB  . HIS   D 1 98  ? 17.104  -2.449  69.315  1.00 14.83  ?  98  HIS   D CB  1 
ATOM   11878 C CG  . HIS   D 1 98  ? 18.365  -1.667  69.524  1.00 17.36  ?  98  HIS   D CG  1 
ATOM   11879 N ND1 . HIS   D 1 98  ? 19.196  -1.869  70.604  1.00 17.04  ?  98  HIS   D ND1 1 
ATOM   11880 C CD2 . HIS   D 1 98  ? 18.928  -0.675  68.796  1.00 17.39  ?  98  HIS   D CD2 1 
ATOM   11881 C CE1 . HIS   D 1 98  ? 20.221  -1.040  70.530  1.00 18.29  ?  98  HIS   D CE1 1 
ATOM   11882 N NE2 . HIS   D 1 98  ? 20.084  -0.306  69.440  1.00 17.59  ?  98  HIS   D NE2 1 
ATOM   11883 N N   . GLN   D 1 99  ? 19.420  -3.780  67.321  1.00 14.12  ?  99  GLN   D N   1 
ATOM   11884 C CA  . GLN   D 1 99  ? 20.236  -3.844  66.106  1.00 13.74  ?  99  GLN   D CA  1 
ATOM   11885 C C   . GLN   D 1 99  ? 21.589  -4.454  66.462  1.00 13.76  ?  99  GLN   D C   1 
ATOM   11886 O O   . GLN   D 1 99  ? 21.778  -4.994  67.560  1.00 13.61  ?  99  GLN   D O   1 
ATOM   11887 C CB  . GLN   D 1 99  ? 20.361  -2.477  65.428  1.00 11.88  ?  99  GLN   D CB  1 
ATOM   11888 C CG  . GLN   D 1 99  ? 21.140  -1.423  66.155  1.00 12.42  ?  99  GLN   D CG  1 
ATOM   11889 C CD  . GLN   D 1 99  ? 21.062  -0.095  65.429  1.00 15.51  ?  99  GLN   D CD  1 
ATOM   11890 O OE1 . GLN   D 1 99  ? 19.973  0.406   65.164  1.00 16.61  ?  99  GLN   D OE1 1 
ATOM   11891 N NE2 . GLN   D 1 99  ? 22.214  0.464   65.070  1.00 18.70  ?  99  GLN   D NE2 1 
ATOM   11892 N N   . GLY   D 1 100 ? 22.533  -4.373  65.520  1.00 13.91  ?  100 GLY   D N   1 
ATOM   11893 C CA  . GLY   D 1 100 ? 23.774  -5.121  65.654  1.00 10.03  ?  100 GLY   D CA  1 
ATOM   11894 C C   . GLY   D 1 100 ? 24.560  -4.762  66.898  1.00 13.54  ?  100 GLY   D C   1 
ATOM   11895 O O   . GLY   D 1 100 ? 24.979  -5.639  67.659  1.00 13.56  ?  100 GLY   D O   1 
ATOM   11896 N N   . ARG   D 1 101 ? 24.785  -3.469  67.122  1.00 11.81  ?  101 ARG   D N   1 
ATOM   11897 C CA  . ARG   D 1 101 ? 25.559  -3.090  68.293  1.00 12.67  ?  101 ARG   D CA  1 
ATOM   11898 C C   . ARG   D 1 101 ? 24.802  -3.340  69.590  1.00 12.47  ?  101 ARG   D C   1 
ATOM   11899 O O   . ARG   D 1 101 ? 25.433  -3.481  70.642  1.00 13.95  ?  101 ARG   D O   1 
ATOM   11900 C CB  . ARG   D 1 101 ? 25.993  -1.633  68.180  1.00 13.13  ?  101 ARG   D CB  1 
ATOM   11901 C CG  . ARG   D 1 101 ? 24.874  -0.637  68.303  1.00 13.78  ?  101 ARG   D CG  1 
ATOM   11902 C CD  . ARG   D 1 101 ? 25.314  0.654   67.669  1.00 16.05  ?  101 ARG   D CD  1 
ATOM   11903 N NE  . ARG   D 1 101 ? 25.435  0.497   66.224  1.00 19.14  ?  101 ARG   D NE  1 
ATOM   11904 C CZ  . ARG   D 1 101 ? 25.678  1.493   65.387  1.00 18.59  ?  101 ARG   D CZ  1 
ATOM   11905 N NH1 . ARG   D 1 101 ? 25.906  2.721   65.828  1.00 17.96  ?  101 ARG   D NH1 1 
ATOM   11906 N NH2 . ARG   D 1 101 ? 25.664  1.258   64.078  1.00 19.92  ?  101 ARG   D NH2 1 
ATOM   11907 N N   . GLY   D 1 102 ? 23.472  -3.422  69.544  1.00 11.02  ?  102 GLY   D N   1 
ATOM   11908 C CA  . GLY   D 1 102 ? 22.738  -3.898  70.708  1.00 14.25  ?  102 GLY   D CA  1 
ATOM   11909 C C   . GLY   D 1 102 ? 23.060  -5.346  71.026  1.00 13.78  ?  102 GLY   D C   1 
ATOM   11910 O O   . GLY   D 1 102 ? 23.249  -5.714  72.187  1.00 14.19  ?  102 GLY   D O   1 
ATOM   11911 N N   . ALA   D 1 103 ? 23.144  -6.181  69.992  1.00 11.87  ?  103 ALA   D N   1 
ATOM   11912 C CA  . ALA   D 1 103 ? 23.528  -7.571  70.181  1.00 12.43  ?  103 ALA   D CA  1 
ATOM   11913 C C   . ALA   D 1 103 ? 24.937  -7.673  70.750  1.00 17.63  ?  103 ALA   D C   1 
ATOM   11914 O O   . ALA   D 1 103 ? 25.211  -8.535  71.599  1.00 16.99  ?  103 ALA   D O   1 
ATOM   11915 C CB  . ALA   D 1 103 ? 23.416  -8.316  68.845  1.00 13.18  ?  103 ALA   D CB  1 
ATOM   11916 N N   . GLU   D 1 104 ? 25.848  -6.796  70.298  1.00 15.73  ?  104 GLU   D N   1 
ATOM   11917 C CA  . GLU   D 1 104 ? 27.210  -6.792  70.833  1.00 15.56  ?  104 GLU   D CA  1 
ATOM   11918 C C   . GLU   D 1 104 ? 27.217  -6.386  72.302  1.00 17.91  ?  104 GLU   D C   1 
ATOM   11919 O O   . GLU   D 1 104 ? 27.957  -6.963  73.114  1.00 18.49  ?  104 GLU   D O   1 
ATOM   11920 C CB  . GLU   D 1 104 ? 28.104  -5.855  70.008  1.00 16.02  ?  104 GLU   D CB  1 
ATOM   11921 C CG  . GLU   D 1 104 ? 28.360  -6.341  68.577  1.00 17.73  ?  104 GLU   D CG  1 
ATOM   11922 C CD  . GLU   D 1 104 ? 28.851  -5.252  67.600  1.00 21.11  ?  104 GLU   D CD  1 
ATOM   11923 O OE1 . GLU   D 1 104 ? 28.798  -4.045  67.922  1.00 19.01  ?  104 GLU   D OE1 1 
ATOM   11924 O OE2 . GLU   D 1 104 ? 29.287  -5.612  66.487  1.00 22.32  ?  104 GLU   D OE2 1 
ATOM   11925 N N   . ASN   D 1 105 ? 26.398  -5.393  72.661  1.00 15.98  ?  105 ASN   D N   1 
ATOM   11926 C CA  . ASN   D 1 105 ? 26.302  -4.977  74.057  1.00 15.69  ?  105 ASN   D CA  1 
ATOM   11927 C C   . ASN   D 1 105 ? 25.759  -6.105  74.925  1.00 16.93  ?  105 ASN   D C   1 
ATOM   11928 O O   . ASN   D 1 105 ? 26.186  -6.272  76.073  1.00 19.16  ?  105 ASN   D O   1 
ATOM   11929 C CB  . ASN   D 1 105 ? 25.421  -3.733  74.167  1.00 16.44  ?  105 ASN   D CB  1 
ATOM   11930 C CG  . ASN   D 1 105 ? 25.561  -3.033  75.499  1.00 18.86  ?  105 ASN   D CG  1 
ATOM   11931 O OD1 . ASN   D 1 105 ? 26.649  -2.957  76.063  1.00 16.95  ?  105 ASN   D OD1 1 
ATOM   11932 N ND2 . ASN   D 1 105 ? 24.452  -2.517  76.012  1.00 20.45  ?  105 ASN   D ND2 1 
ATOM   11933 N N   . ILE   D 1 106 ? 24.824  -6.898  74.393  1.00 16.79  ?  106 ILE   D N   1 
ATOM   11934 C CA  . ILE   D 1 106 ? 24.316  -8.047  75.144  1.00 18.95  ?  106 ILE   D CA  1 
ATOM   11935 C C   . ILE   D 1 106 ? 25.435  -9.044  75.417  1.00 21.06  ?  106 ILE   D C   1 
ATOM   11936 O O   . ILE   D 1 106 ? 25.658  -9.456  76.561  1.00 21.99  ?  106 ILE   D O   1 
ATOM   11937 C CB  . ILE   D 1 106 ? 23.156  -8.723  74.390  1.00 18.70  ?  106 ILE   D CB  1 
ATOM   11938 C CG1 . ILE   D 1 106 ? 21.855  -7.944  74.556  1.00 13.54  ?  106 ILE   D CG1 1 
ATOM   11939 C CG2 . ILE   D 1 106 ? 22.972  -10.154 74.888  1.00 18.35  ?  106 ILE   D CG2 1 
ATOM   11940 C CD1 . ILE   D 1 106 ? 20.743  -8.467  73.681  1.00 13.98  ?  106 ILE   D CD1 1 
ATOM   11941 N N   . LEU   D 1 107 ? 26.154  -9.449  74.370  1.00 18.43  ?  107 LEU   D N   1 
ATOM   11942 C CA  . LEU   D 1 107 ? 26.939  -10.677 74.438  1.00 18.76  ?  107 LEU   D CA  1 
ATOM   11943 C C   . LEU   D 1 107 ? 28.378  -10.473 74.892  1.00 17.40  ?  107 LEU   D C   1 
ATOM   11944 O O   . LEU   D 1 107 ? 28.899  -11.297 75.648  1.00 19.24  ?  107 LEU   D O   1 
ATOM   11945 C CB  . LEU   D 1 107 ? 26.941  -11.375 73.076  1.00 17.62  ?  107 LEU   D CB  1 
ATOM   11946 C CG  . LEU   D 1 107 ? 27.624  -12.746 73.076  1.00 17.37  ?  107 LEU   D CG  1 
ATOM   11947 C CD1 . LEU   D 1 107 ? 26.913  -13.664 74.055  1.00 14.44  ?  107 LEU   D CD1 1 
ATOM   11948 C CD2 . LEU   D 1 107 ? 27.659  -13.351 71.665  1.00 15.01  ?  107 LEU   D CD2 1 
ATOM   11949 N N   . PHE   D 1 108 ? 29.052  -9.426  74.436  1.00 17.99  ?  108 PHE   D N   1 
ATOM   11950 C CA  . PHE   D 1 108 ? 30.484  -9.349  74.715  1.00 15.30  ?  108 PHE   D CA  1 
ATOM   11951 C C   . PHE   D 1 108 ? 30.778  -9.148  76.198  1.00 15.46  ?  108 PHE   D C   1 
ATOM   11952 O O   . PHE   D 1 108 ? 31.702  -9.790  76.713  1.00 16.55  ?  108 PHE   D O   1 
ATOM   11953 C CB  . PHE   D 1 108 ? 31.154  -8.244  73.897  1.00 18.14  ?  108 PHE   D CB  1 
ATOM   11954 C CG  . PHE   D 1 108 ? 31.280  -8.558  72.433  1.00 21.13  ?  108 PHE   D CG  1 
ATOM   11955 C CD1 . PHE   D 1 108 ? 30.737  -9.718  71.904  1.00 17.08  ?  108 PHE   D CD1 1 
ATOM   11956 C CD2 . PHE   D 1 108 ? 31.947  -7.692  71.586  1.00 21.16  ?  108 PHE   D CD2 1 
ATOM   11957 C CE1 . PHE   D 1 108 ? 30.846  -10.003 70.559  1.00 20.63  ?  108 PHE   D CE1 1 
ATOM   11958 C CE2 . PHE   D 1 108 ? 32.066  -7.977  70.237  1.00 23.58  ?  108 PHE   D CE2 1 
ATOM   11959 C CZ  . PHE   D 1 108 ? 31.514  -9.133  69.723  1.00 20.13  ?  108 PHE   D CZ  1 
ATOM   11960 N N   . PRO   D 1 109 ? 30.053  -8.281  76.922  1.00 17.35  ?  109 PRO   D N   1 
ATOM   11961 C CA  . PRO   D 1 109 ? 30.286  -8.208  78.373  1.00 20.97  ?  109 PRO   D CA  1 
ATOM   11962 C C   . PRO   D 1 109 ? 30.058  -9.533  79.067  1.00 19.83  ?  109 PRO   D C   1 
ATOM   11963 O O   . PRO   D 1 109 ? 30.727  -9.826  80.062  1.00 21.64  ?  109 PRO   D O   1 
ATOM   11964 C CB  . PRO   D 1 109 ? 29.285  -7.143  78.837  1.00 21.70  ?  109 PRO   D CB  1 
ATOM   11965 C CG  . PRO   D 1 109 ? 29.041  -6.306  77.627  1.00 17.11  ?  109 PRO   D CG  1 
ATOM   11966 C CD  . PRO   D 1 109 ? 29.106  -7.241  76.471  1.00 16.79  ?  109 PRO   D CD  1 
ATOM   11967 N N   . VAL   D 1 110 ? 29.138  -10.355 78.561  1.00 16.65  ?  110 VAL   D N   1 
ATOM   11968 C CA  . VAL   D 1 110 ? 28.889  -11.650 79.181  1.00 18.86  ?  110 VAL   D CA  1 
ATOM   11969 C C   . VAL   D 1 110 ? 30.072  -12.584 78.967  1.00 19.14  ?  110 VAL   D C   1 
ATOM   11970 O O   . VAL   D 1 110 ? 30.491  -13.290 79.892  1.00 21.32  ?  110 VAL   D O   1 
ATOM   11971 C CB  . VAL   D 1 110 ? 27.583  -12.259 78.643  1.00 22.00  ?  110 VAL   D CB  1 
ATOM   11972 C CG1 . VAL   D 1 110 ? 27.520  -13.747 78.992  1.00 20.49  ?  110 VAL   D CG1 1 
ATOM   11973 C CG2 . VAL   D 1 110 ? 26.382  -11.507 79.216  1.00 20.17  ?  110 VAL   D CG2 1 
ATOM   11974 N N   . LEU   D 1 111 ? 30.621  -12.612 77.748  1.00 19.49  ?  111 LEU   D N   1 
ATOM   11975 C CA  . LEU   D 1 111 ? 31.737  -13.509 77.444  1.00 18.64  ?  111 LEU   D CA  1 
ATOM   11976 C C   . LEU   D 1 111 ? 32.965  -13.158 78.275  1.00 17.72  ?  111 LEU   D C   1 
ATOM   11977 O O   . LEU   D 1 111 ? 33.673  -14.050 78.763  1.00 17.48  ?  111 LEU   D O   1 
ATOM   11978 C CB  . LEU   D 1 111 ? 32.065  -13.460 75.947  1.00 14.16  ?  111 LEU   D CB  1 
ATOM   11979 C CG  . LEU   D 1 111 ? 30.961  -13.909 74.984  1.00 16.60  ?  111 LEU   D CG  1 
ATOM   11980 C CD1 . LEU   D 1 111 ? 31.329  -13.623 73.544  1.00 16.55  ?  111 LEU   D CD1 1 
ATOM   11981 C CD2 . LEU   D 1 111 ? 30.677  -15.383 75.166  1.00 16.52  ?  111 LEU   D CD2 1 
ATOM   11982 N N   . LEU   D 1 112 ? 33.229  -11.861 78.453  1.00 15.90  ?  112 LEU   D N   1 
ATOM   11983 C CA  . LEU   D 1 112 ? 34.326  -11.436 79.316  1.00 17.44  ?  112 LEU   D CA  1 
ATOM   11984 C C   . LEU   D 1 112 ? 34.135  -11.951 80.737  1.00 21.48  ?  112 LEU   D C   1 
ATOM   11985 O O   . LEU   D 1 112 ? 35.043  -12.558 81.319  1.00 23.27  ?  112 LEU   D O   1 
ATOM   11986 C CB  . LEU   D 1 112 ? 34.430  -9.914  79.303  1.00 17.79  ?  112 LEU   D CB  1 
ATOM   11987 C CG  . LEU   D 1 112 ? 35.520  -9.304  80.184  1.00 23.35  ?  112 LEU   D CG  1 
ATOM   11988 C CD1 . LEU   D 1 112 ? 36.875  -9.845  79.777  1.00 22.35  ?  112 LEU   D CD1 1 
ATOM   11989 C CD2 . LEU   D 1 112 ? 35.503  -7.798  80.073  1.00 18.10  ?  112 LEU   D CD2 1 
ATOM   11990 N N   . LYS   D 1 113 ? 32.952  -11.714 81.314  1.00 23.32  ?  113 LYS   D N   1 
ATOM   11991 C CA  . LYS   D 1 113 ? 32.673  -12.184 82.670  1.00 22.16  ?  113 LYS   D CA  1 
ATOM   11992 C C   . LYS   D 1 113 ? 32.813  -13.698 82.767  1.00 25.01  ?  113 LYS   D C   1 
ATOM   11993 O O   . LYS   D 1 113 ? 33.343  -14.222 83.756  1.00 29.41  ?  113 LYS   D O   1 
ATOM   11994 C CB  . LYS   D 1 113 ? 31.267  -11.747 83.089  1.00 21.74  ?  113 LYS   D CB  1 
ATOM   11995 C CG  . LYS   D 1 113 ? 30.889  -12.130 84.521  1.00 33.71  ?  113 LYS   D CG  1 
ATOM   11996 C CD  . LYS   D 1 113 ? 31.697  -11.345 85.544  1.00 39.35  ?  113 LYS   D CD  1 
ATOM   11997 C CE  . LYS   D 1 113 ? 31.359  -11.755 86.978  1.00 32.01  ?  113 LYS   D CE  1 
ATOM   11998 N NZ  . LYS   D 1 113 ? 32.174  -11.010 87.981  1.00 40.12  ?  113 LYS   D NZ  1 
ATOM   11999 N N   . TYR   D 1 114 ? 32.344  -14.414 81.743  1.00 22.52  ?  114 TYR   D N   1 
ATOM   12000 C CA  . TYR   D 1 114 ? 32.459  -15.868 81.692  1.00 25.50  ?  114 TYR   D CA  1 
ATOM   12001 C C   . TYR   D 1 114 ? 33.918  -16.317 81.623  1.00 28.59  ?  114 TYR   D C   1 
ATOM   12002 O O   . TYR   D 1 114 ? 34.324  -17.242 82.338  1.00 26.88  ?  114 TYR   D O   1 
ATOM   12003 C CB  . TYR   D 1 114 ? 31.667  -16.371 80.489  1.00 22.02  ?  114 TYR   D CB  1 
ATOM   12004 C CG  . TYR   D 1 114 ? 31.642  -17.862 80.272  1.00 25.53  ?  114 TYR   D CG  1 
ATOM   12005 C CD1 . TYR   D 1 114 ? 30.877  -18.697 81.085  1.00 30.61  ?  114 TYR   D CD1 1 
ATOM   12006 C CD2 . TYR   D 1 114 ? 32.335  -18.433 79.218  1.00 27.91  ?  114 TYR   D CD2 1 
ATOM   12007 C CE1 . TYR   D 1 114 ? 30.840  -20.065 80.868  1.00 30.55  ?  114 TYR   D CE1 1 
ATOM   12008 C CE2 . TYR   D 1 114 ? 32.301  -19.793 78.990  1.00 29.15  ?  114 TYR   D CE2 1 
ATOM   12009 C CZ  . TYR   D 1 114 ? 31.554  -20.603 79.810  1.00 29.35  ?  114 TYR   D CZ  1 
ATOM   12010 O OH  . TYR   D 1 114 ? 31.531  -21.954 79.563  1.00 32.96  ?  114 TYR   D OH  1 
ATOM   12011 N N   . LYS   D 1 115 ? 34.722  -15.670 80.774  1.00 20.90  ?  115 LYS   D N   1 
ATOM   12012 C CA  . LYS   D 1 115 ? 36.133  -16.021 80.664  1.00 22.76  ?  115 LYS   D CA  1 
ATOM   12013 C C   . LYS   D 1 115 ? 36.896  -15.735 81.950  1.00 28.64  ?  115 LYS   D C   1 
ATOM   12014 O O   . LYS   D 1 115 ? 37.871  -16.429 82.258  1.00 27.09  ?  115 LYS   D O   1 
ATOM   12015 C CB  . LYS   D 1 115 ? 36.773  -15.253 79.510  1.00 23.02  ?  115 LYS   D CB  1 
ATOM   12016 C CG  . LYS   D 1 115 ? 38.165  -15.721 79.140  1.00 23.38  ?  115 LYS   D CG  1 
ATOM   12017 C CD  . LYS   D 1 115 ? 38.091  -16.898 78.186  1.00 28.14  ?  115 LYS   D CD  1 
ATOM   12018 C CE  . LYS   D 1 115 ? 39.461  -17.392 77.797  1.00 25.80  ?  115 LYS   D CE  1 
ATOM   12019 N NZ  . LYS   D 1 115 ? 39.333  -18.668 77.037  1.00 27.84  ?  115 LYS   D NZ  1 
ATOM   12020 N N   . GLN   D 1 116 ? 36.492  -14.710 82.695  1.00 28.99  ?  116 GLN   D N   1 
ATOM   12021 C CA  . GLN   D 1 116 ? 37.201  -14.306 83.902  1.00 30.55  ?  116 GLN   D CA  1 
ATOM   12022 C C   . GLN   D 1 116 ? 36.782  -15.100 85.130  1.00 35.31  ?  116 GLN   D C   1 
ATOM   12023 O O   . GLN   D 1 116 ? 37.194  -14.754 86.243  1.00 41.21  ?  116 GLN   D O   1 
ATOM   12024 C CB  . GLN   D 1 116 ? 37.016  -12.803 84.144  1.00 27.87  ?  116 GLN   D CB  1 
ATOM   12025 C CG  . GLN   D 1 116 ? 37.711  -11.954 83.083  1.00 28.32  ?  116 GLN   D CG  1 
ATOM   12026 C CD  . GLN   D 1 116 ? 37.768  -10.478 83.427  1.00 29.35  ?  116 GLN   D CD  1 
ATOM   12027 O OE1 . GLN   D 1 116 ? 36.770  -9.884  83.834  1.00 24.73  ?  116 GLN   D OE1 1 
ATOM   12028 N NE2 . GLN   D 1 116 ? 38.948  -9.875  83.259  1.00 27.76  ?  116 GLN   D NE2 1 
ATOM   12029 N N   . LYS   D 1 117 ? 35.978  -16.148 84.958  1.00 34.03  ?  117 LYS   D N   1 
ATOM   12030 C CA  . LYS   D 1 117 ? 35.803  -17.127 86.020  1.00 38.83  ?  117 LYS   D CA  1 
ATOM   12031 C C   . LYS   D 1 117 ? 37.141  -17.774 86.351  1.00 45.72  ?  117 LYS   D C   1 
ATOM   12032 O O   . LYS   D 1 117 ? 38.047  -17.848 85.514  1.00 44.87  ?  117 LYS   D O   1 
ATOM   12033 C CB  . LYS   D 1 117 ? 34.789  -18.199 85.614  1.00 37.18  ?  117 LYS   D CB  1 
ATOM   12034 C CG  . LYS   D 1 117 ? 33.342  -17.730 85.638  1.00 40.43  ?  117 LYS   D CG  1 
ATOM   12035 C CD  . LYS   D 1 117 ? 32.356  -18.897 85.678  1.00 45.51  ?  117 LYS   D CD  1 
ATOM   12036 C CE  . LYS   D 1 117 ? 32.450  -19.784 84.433  1.00 42.06  ?  117 LYS   D CE  1 
ATOM   12037 N NZ  . LYS   D 1 117 ? 31.429  -20.891 84.436  1.00 35.10  ?  117 LYS   D NZ  1 
ATOM   12038 N N   . GLU   D 1 118 ? 37.262  -18.240 87.590  1.00 56.14  ?  118 GLU   D N   1 
ATOM   12039 C CA  . GLU   D 1 118 ? 38.480  -18.836 88.133  1.00 63.25  ?  118 GLU   D CA  1 
ATOM   12040 C C   . GLU   D 1 118 ? 39.667  -17.877 88.114  1.00 63.44  ?  118 GLU   D C   1 
ATOM   12041 O O   . GLU   D 1 118 ? 40.809  -18.310 88.309  1.00 64.97  ?  118 GLU   D O   1 
ATOM   12042 C CB  . GLU   D 1 118 ? 38.846  -20.140 87.405  1.00 65.90  ?  118 GLU   D CB  1 
ATOM   12043 C CG  . GLU   D 1 118 ? 37.829  -21.262 87.573  1.00 73.77  ?  118 GLU   D CG  1 
ATOM   12044 C CD  . GLU   D 1 118 ? 38.309  -22.584 86.989  1.00 84.22  ?  118 GLU   D CD  1 
ATOM   12045 O OE1 . GLU   D 1 118 ? 39.528  -22.718 86.737  1.00 84.50  ?  118 GLU   D OE1 1 
ATOM   12046 O OE2 . GLU   D 1 118 ? 37.466  -23.487 86.780  1.00 75.78  ?  118 GLU   D OE2 1 
ATOM   12047 N N   . GLY   D 1 119 ? 39.431  -16.587 87.878  1.00 59.85  ?  119 GLY   D N   1 
ATOM   12048 C CA  . GLY   D 1 119 ? 40.482  -15.595 87.986  1.00 55.12  ?  119 GLY   D CA  1 
ATOM   12049 C C   . GLY   D 1 119 ? 41.465  -15.543 86.841  1.00 54.20  ?  119 GLY   D C   1 
ATOM   12050 O O   . GLY   D 1 119 ? 42.572  -15.029 87.019  1.00 57.89  ?  119 GLY   D O   1 
ATOM   12051 N N   . LYS   D 1 120 ? 41.108  -16.059 85.674  1.00 42.64  ?  120 LYS   D N   1 
ATOM   12052 C CA  . LYS   D 1 120 ? 41.953  -15.937 84.500  1.00 38.05  ?  120 LYS   D CA  1 
ATOM   12053 C C   . LYS   D 1 120 ? 41.493  -14.739 83.668  1.00 33.36  ?  120 LYS   D C   1 
ATOM   12054 O O   . LYS   D 1 120 ? 40.669  -13.929 84.110  1.00 33.60  ?  120 LYS   D O   1 
ATOM   12055 C CB  . LYS   D 1 120 ? 41.939  -17.241 83.699  1.00 40.45  ?  120 LYS   D CB  1 
ATOM   12056 C CG  . LYS   D 1 120 ? 40.570  -17.656 83.208  1.00 41.98  ?  120 LYS   D CG  1 
ATOM   12057 C CD  . LYS   D 1 120 ? 40.642  -18.880 82.302  1.00 43.93  ?  120 LYS   D CD  1 
ATOM   12058 C CE  . LYS   D 1 120 ? 39.278  -19.189 81.691  1.00 45.81  ?  120 LYS   D CE  1 
ATOM   12059 N NZ  . LYS   D 1 120 ? 39.283  -20.410 80.831  1.00 53.24  ?  120 LYS   D NZ  1 
ATOM   12060 N N   . ALA   D 1 121 ? 42.036  -14.616 82.453  1.00 32.73  ?  121 ALA   D N   1 
ATOM   12061 C CA  . ALA   D 1 121 ? 41.694  -13.528 81.534  1.00 23.99  ?  121 ALA   D CA  1 
ATOM   12062 C C   . ALA   D 1 121 ? 42.033  -12.165 82.133  1.00 23.59  ?  121 ALA   D C   1 
ATOM   12063 O O   . ALA   D 1 121 ? 41.282  -11.197 81.992  1.00 25.48  ?  121 ALA   D O   1 
ATOM   12064 C CB  . ALA   D 1 121 ? 40.226  -13.592 81.120  1.00 27.32  ?  121 ALA   D CB  1 
ATOM   12065 N N   . LYS   D 1 122 ? 43.188  -12.086 82.794  1.00 25.04  ?  122 LYS   D N   1 
ATOM   12066 C CA  . LYS   D 1 122 ? 43.648  -10.837 83.395  1.00 24.27  ?  122 LYS   D CA  1 
ATOM   12067 C C   . LYS   D 1 122 ? 44.084  -9.809  82.358  1.00 22.35  ?  122 LYS   D C   1 
ATOM   12068 O O   . LYS   D 1 122 ? 44.124  -8.615  82.666  1.00 22.08  ?  122 LYS   D O   1 
ATOM   12069 C CB  . LYS   D 1 122 ? 44.804  -11.126 84.346  1.00 29.81  ?  122 LYS   D CB  1 
ATOM   12070 C CG  . LYS   D 1 122 ? 44.418  -11.930 85.574  1.00 32.99  ?  122 LYS   D CG  1 
ATOM   12071 C CD  . LYS   D 1 122 ? 43.571  -11.093 86.512  1.00 38.72  ?  122 LYS   D CD  1 
ATOM   12072 C CE  . LYS   D 1 122 ? 43.364  -11.783 87.847  1.00 40.48  ?  122 LYS   D CE  1 
ATOM   12073 N NZ  . LYS   D 1 122 ? 42.180  -11.202 88.548  1.00 51.91  ?  122 LYS   D NZ  1 
ATOM   12074 N N   . ASN   D 1 123 ? 44.433  -10.243 81.149  1.00 22.08  ?  123 ASN   D N   1 
ATOM   12075 C CA  . ASN   D 1 123 ? 44.817  -9.351  80.057  1.00 20.48  ?  123 ASN   D CA  1 
ATOM   12076 C C   . ASN   D 1 123 ? 43.940  -9.684  78.860  1.00 23.46  ?  123 ASN   D C   1 
ATOM   12077 O O   . ASN   D 1 123 ? 44.414  -10.217 77.848  1.00 19.99  ?  123 ASN   D O   1 
ATOM   12078 C CB  . ASN   D 1 123 ? 46.302  -9.494  79.725  1.00 23.09  ?  123 ASN   D CB  1 
ATOM   12079 C CG  . ASN   D 1 123 ? 47.177  -9.328  80.944  1.00 31.08  ?  123 ASN   D CG  1 
ATOM   12080 O OD1 . ASN   D 1 123 ? 47.992  -10.204 81.277  1.00 26.83  ?  123 ASN   D OD1 1 
ATOM   12081 N ND2 . ASN   D 1 123 ? 47.007  -8.200  81.633  1.00 26.75  ?  123 ASN   D ND2 1 
ATOM   12082 N N   . PRO   D 1 124 ? 42.648  -9.368  78.941  1.00 25.94  ?  124 PRO   D N   1 
ATOM   12083 C CA  . PRO   D 1 124 ? 41.680  -9.958  78.009  1.00 19.20  ?  124 PRO   D CA  1 
ATOM   12084 C C   . PRO   D 1 124 ? 41.729  -9.330  76.623  1.00 19.33  ?  124 PRO   D C   1 
ATOM   12085 O O   . PRO   D 1 124 ? 41.847  -8.111  76.465  1.00 22.38  ?  124 PRO   D O   1 
ATOM   12086 C CB  . PRO   D 1 124 ? 40.339  -9.679  78.690  1.00 16.12  ?  124 PRO   D CB  1 
ATOM   12087 C CG  . PRO   D 1 124 ? 40.588  -8.400  79.448  1.00 22.67  ?  124 PRO   D CG  1 
ATOM   12088 C CD  . PRO   D 1 124 ? 42.000  -8.497  79.944  1.00 20.82  ?  124 PRO   D CD  1 
ATOM   12089 N N   . VAL   D 1 125 ? 41.629  -10.180 75.605  1.00 15.57  ?  125 VAL   D N   1 
ATOM   12090 C CA  . VAL   D 1 125 ? 41.630  -9.723  74.223  1.00 15.59  ?  125 VAL   D CA  1 
ATOM   12091 C C   . VAL   D 1 125 ? 40.561  -10.468 73.437  1.00 19.27  ?  125 VAL   D C   1 
ATOM   12092 O O   . VAL   D 1 125 ? 40.126  -11.564 73.812  1.00 16.10  ?  125 VAL   D O   1 
ATOM   12093 C CB  . VAL   D 1 125 ? 43.011  -9.893  73.553  1.00 20.52  ?  125 VAL   D CB  1 
ATOM   12094 C CG1 . VAL   D 1 125 ? 44.070  -9.129  74.332  1.00 22.31  ?  125 VAL   D CG1 1 
ATOM   12095 C CG2 . VAL   D 1 125 ? 43.383  -11.366 73.437  1.00 18.49  ?  125 VAL   D CG2 1 
ATOM   12096 N N   . PHE   D 1 126 ? 40.110  -9.821  72.362  1.00 16.02  ?  126 PHE   D N   1 
ATOM   12097 C CA  . PHE   D 1 126 ? 39.289  -10.398 71.308  1.00 15.66  ?  126 PHE   D CA  1 
ATOM   12098 C C   . PHE   D 1 126 ? 40.132  -10.441 70.041  1.00 16.99  ?  126 PHE   D C   1 
ATOM   12099 O O   . PHE   D 1 126 ? 40.860  -9.487  69.747  1.00 16.58  ?  126 PHE   D O   1 
ATOM   12100 C CB  . PHE   D 1 126 ? 38.041  -9.547  71.043  1.00 19.89  ?  126 PHE   D CB  1 
ATOM   12101 C CG  . PHE   D 1 126 ? 36.930  -9.706  72.067  1.00 20.18  ?  126 PHE   D CG  1 
ATOM   12102 C CD1 . PHE   D 1 126 ? 37.130  -9.400  73.404  1.00 19.47  ?  126 PHE   D CD1 1 
ATOM   12103 C CD2 . PHE   D 1 126 ? 35.662  -10.115 71.664  1.00 19.45  ?  126 PHE   D CD2 1 
ATOM   12104 C CE1 . PHE   D 1 126 ? 36.101  -9.530  74.320  1.00 14.53  ?  126 PHE   D CE1 1 
ATOM   12105 C CE2 . PHE   D 1 126 ? 34.632  -10.242 72.579  1.00 18.54  ?  126 PHE   D CE2 1 
ATOM   12106 C CZ  . PHE   D 1 126 ? 34.856  -9.954  73.905  1.00 12.17  ?  126 PHE   D CZ  1 
ATOM   12107 N N   . ILE   D 1 127 ? 40.047  -11.532 69.286  1.00 13.12  ?  127 ILE   D N   1 
ATOM   12108 C CA  . ILE   D 1 127 ? 40.752  -11.635 68.012  1.00 14.92  ?  127 ILE   D CA  1 
ATOM   12109 C C   . ILE   D 1 127 ? 39.732  -11.813 66.896  1.00 17.58  ?  127 ILE   D C   1 
ATOM   12110 O O   . ILE   D 1 127 ? 38.835  -12.658 67.001  1.00 17.56  ?  127 ILE   D O   1 
ATOM   12111 C CB  . ILE   D 1 127 ? 41.767  -12.790 68.009  1.00 14.00  ?  127 ILE   D CB  1 
ATOM   12112 C CG1 . ILE   D 1 127 ? 42.780  -12.615 69.129  1.00 15.53  ?  127 ILE   D CG1 1 
ATOM   12113 C CG2 . ILE   D 1 127 ? 42.477  -12.863 66.653  1.00 17.30  ?  127 ILE   D CG2 1 
ATOM   12114 C CD1 . ILE   D 1 127 ? 43.679  -13.793 69.299  1.00 18.00  ?  127 ILE   D CD1 1 
ATOM   12115 N N   . SER   D 1 128 ? 39.883  -11.031 65.821  1.00 15.44  ?  128 SER   D N   1 
ATOM   12116 C CA  . SER   D 1 128 ? 38.999  -11.105 64.665  1.00 13.95  ?  128 SER   D CA  1 
ATOM   12117 C C   . SER   D 1 128 ? 39.822  -11.021 63.389  1.00 14.21  ?  128 SER   D C   1 
ATOM   12118 O O   . SER   D 1 128 ? 40.923  -10.459 63.378  1.00 16.01  ?  128 SER   D O   1 
ATOM   12119 C CB  . SER   D 1 128 ? 37.954  -9.981  64.672  1.00 13.31  ?  128 SER   D CB  1 
ATOM   12120 O OG  . SER   D 1 128 ? 37.033  -10.114 63.590  1.00 17.98  ?  128 SER   D OG  1 
ATOM   12121 N N   . ASN   D 1 129 ? 39.286  -11.592 62.309  1.00 14.55  ?  129 ASN   D N   1 
ATOM   12122 C CA  . ASN   D 1 129 ? 39.838  -11.266 61.000  1.00 22.95  ?  129 ASN   D CA  1 
ATOM   12123 C C   . ASN   D 1 129 ? 39.810  -9.756  60.787  1.00 20.66  ?  129 ASN   D C   1 
ATOM   12124 O O   . ASN   D 1 129 ? 40.813  -9.161  60.381  1.00 20.55  ?  129 ASN   D O   1 
ATOM   12125 C CB  . ASN   D 1 129 ? 39.102  -12.023 59.886  1.00 15.52  ?  129 ASN   D CB  1 
ATOM   12126 C CG  . ASN   D 1 129 ? 37.602  -11.720 59.823  1.00 18.72  ?  129 ASN   D CG  1 
ATOM   12127 O OD1 . ASN   D 1 129 ? 36.924  -11.579 60.840  1.00 17.27  ?  129 ASN   D OD1 1 
ATOM   12128 N ND2 . ASN   D 1 129 ? 37.080  -11.644 58.606  1.00 17.54  ?  129 ASN   D ND2 1 
ATOM   12129 N N   . PHE   D 1 130 ? 38.695  -9.113  61.128  1.00 18.14  ?  130 PHE   D N   1 
ATOM   12130 C CA  . PHE   D 1 130 ? 38.676  -7.663  61.312  1.00 22.35  ?  130 PHE   D CA  1 
ATOM   12131 C C   . PHE   D 1 130 ? 37.439  -7.288  62.109  1.00 21.35  ?  130 PHE   D C   1 
ATOM   12132 O O   . PHE   D 1 130 ? 36.315  -7.515  61.648  1.00 21.31  ?  130 PHE   D O   1 
ATOM   12133 C CB  . PHE   D 1 130 ? 38.698  -6.914  59.980  1.00 19.33  ?  130 PHE   D CB  1 
ATOM   12134 C CG  . PHE   D 1 130 ? 39.557  -5.691  60.011  1.00 22.63  ?  130 PHE   D CG  1 
ATOM   12135 C CD1 . PHE   D 1 130 ? 39.217  -4.615  60.807  1.00 20.04  ?  130 PHE   D CD1 1 
ATOM   12136 C CD2 . PHE   D 1 130 ? 40.726  -5.630  59.276  1.00 27.46  ?  130 PHE   D CD2 1 
ATOM   12137 C CE1 . PHE   D 1 130 ? 40.013  -3.487  60.850  1.00 24.41  ?  130 PHE   D CE1 1 
ATOM   12138 C CE2 . PHE   D 1 130 ? 41.531  -4.501  59.320  1.00 29.89  ?  130 PHE   D CE2 1 
ATOM   12139 C CZ  . PHE   D 1 130 ? 41.170  -3.431  60.109  1.00 24.84  ?  130 PHE   D CZ  1 
ATOM   12140 N N   . HIS   D 1 131 ? 37.645  -6.721  63.295  1.00 19.14  ?  131 HIS   D N   1 
ATOM   12141 C CA  . HIS   D 1 131 ? 36.547  -6.153  64.063  1.00 20.04  ?  131 HIS   D CA  1 
ATOM   12142 C C   . HIS   D 1 131 ? 35.953  -4.946  63.350  1.00 19.62  ?  131 HIS   D C   1 
ATOM   12143 O O   . HIS   D 1 131 ? 36.677  -4.009  62.994  1.00 23.87  ?  131 HIS   D O   1 
ATOM   12144 C CB  . HIS   D 1 131 ? 37.035  -5.696  65.433  1.00 21.33  ?  131 HIS   D CB  1 
ATOM   12145 C CG  . HIS   D 1 131 ? 37.374  -6.803  66.374  1.00 22.66  ?  131 HIS   D CG  1 
ATOM   12146 N ND1 . HIS   D 1 131 ? 38.668  -7.229  66.581  1.00 20.75  ?  131 HIS   D ND1 1 
ATOM   12147 C CD2 . HIS   D 1 131 ? 36.595  -7.540  67.200  1.00 22.00  ?  131 HIS   D CD2 1 
ATOM   12148 C CE1 . HIS   D 1 131 ? 38.668  -8.192  67.487  1.00 21.37  ?  131 HIS   D CE1 1 
ATOM   12149 N NE2 . HIS   D 1 131 ? 37.423  -8.401  67.876  1.00 22.38  ?  131 HIS   D NE2 1 
ATOM   12150 N N   . PHE   D 1 132 ? 34.637  -4.931  63.180  1.00 17.29  ?  132 PHE   D N   1 
ATOM   12151 C CA  A PHE   D 1 132 ? 33.953  -3.725  62.738  0.63 23.09  ?  132 PHE   D CA  1 
ATOM   12152 C CA  B PHE   D 1 132 ? 34.058  -3.688  62.702  0.37 23.09  ?  132 PHE   D CA  1 
ATOM   12153 C C   . PHE   D 1 132 ? 34.016  -2.662  63.836  1.00 20.40  ?  132 PHE   D C   1 
ATOM   12154 O O   . PHE   D 1 132 ? 34.278  -2.965  65.003  1.00 22.43  ?  132 PHE   D O   1 
ATOM   12155 C CB  A PHE   D 1 132 ? 32.505  -4.050  62.371  0.63 24.10  ?  132 PHE   D CB  1 
ATOM   12156 C CB  B PHE   D 1 132 ? 32.672  -3.908  62.103  0.37 24.16  ?  132 PHE   D CB  1 
ATOM   12157 C CG  A PHE   D 1 132 ? 31.712  -2.863  61.928  0.63 23.90  ?  132 PHE   D CG  1 
ATOM   12158 C CG  B PHE   D 1 132 ? 32.231  -2.786  61.205  0.37 25.03  ?  132 PHE   D CG  1 
ATOM   12159 C CD1 A PHE   D 1 132 ? 31.944  -2.287  60.690  0.63 25.23  ?  132 PHE   D CD1 1 
ATOM   12160 C CD1 B PHE   D 1 132 ? 33.063  -2.331  60.193  0.37 25.85  ?  132 PHE   D CD1 1 
ATOM   12161 C CD2 A PHE   D 1 132 ? 30.746  -2.315  62.755  0.63 22.41  ?  132 PHE   D CD2 1 
ATOM   12162 C CD2 B PHE   D 1 132 ? 31.003  -2.175  61.380  0.37 24.81  ?  132 PHE   D CD2 1 
ATOM   12163 C CE1 A PHE   D 1 132 ? 31.225  -1.189  60.282  0.63 26.72  ?  132 PHE   D CE1 1 
ATOM   12164 C CE1 B PHE   D 1 132 ? 32.678  -1.289  59.368  0.37 26.53  ?  132 PHE   D CE1 1 
ATOM   12165 C CE2 A PHE   D 1 132 ? 30.027  -1.217  62.356  0.63 24.55  ?  132 PHE   D CE2 1 
ATOM   12166 C CE2 B PHE   D 1 132 ? 30.609  -1.138  60.554  0.37 27.50  ?  132 PHE   D CE2 1 
ATOM   12167 C CZ  A PHE   D 1 132 ? 30.262  -0.654  61.116  0.63 28.62  ?  132 PHE   D CZ  1 
ATOM   12168 C CZ  B PHE   D 1 132 ? 31.448  -0.691  59.550  0.37 26.96  ?  132 PHE   D CZ  1 
ATOM   12169 N N   . ASP   D 1 133 ? 33.724  -1.409  63.466  1.00 21.51  ?  133 ASP   D N   1 
ATOM   12170 C CA  A ASP   D 1 133 ? 33.932  -0.283  64.378  0.61 22.71  ?  133 ASP   D CA  1 
ATOM   12171 C CA  B ASP   D 1 133 ? 33.954  -0.299  64.387  0.39 22.74  ?  133 ASP   D CA  1 
ATOM   12172 C C   . ASP   D 1 133 ? 33.133  -0.443  65.669  1.00 22.75  ?  133 ASP   D C   1 
ATOM   12173 O O   . ASP   D 1 133 ? 33.670  -0.282  66.769  1.00 19.43  ?  133 ASP   D O   1 
ATOM   12174 C CB  A ASP   D 1 133 ? 33.565  1.027   63.685  0.61 24.30  ?  133 ASP   D CB  1 
ATOM   12175 C CB  B ASP   D 1 133 ? 33.681  1.042   63.697  0.39 24.32  ?  133 ASP   D CB  1 
ATOM   12176 C CG  A ASP   D 1 133 ? 34.259  1.191   62.354  0.61 25.77  ?  133 ASP   D CG  1 
ATOM   12177 C CG  B ASP   D 1 133 ? 32.211  1.302   63.470  0.39 25.54  ?  133 ASP   D CG  1 
ATOM   12178 O OD1 A ASP   D 1 133 ? 34.830  0.198   61.857  0.61 30.25  ?  133 ASP   D OD1 1 
ATOM   12179 O OD1 B ASP   D 1 133 ? 31.511  0.388   62.997  0.39 25.22  ?  133 ASP   D OD1 1 
ATOM   12180 O OD2 A ASP   D 1 133 ? 34.233  2.312   61.801  0.61 31.91  ?  133 ASP   D OD2 1 
ATOM   12181 O OD2 B ASP   D 1 133 ? 31.749  2.423   63.774  0.39 29.42  ?  133 ASP   D OD2 1 
ATOM   12182 N N   . THR   D 1 134 ? 31.832  -0.748  65.561  1.00 18.99  ?  134 THR   D N   1 
ATOM   12183 C CA  . THR   D 1 134 ? 31.048  -0.909  66.788  1.00 18.19  ?  134 THR   D CA  1 
ATOM   12184 C C   . THR   D 1 134 ? 31.524  -2.118  67.578  1.00 17.18  ?  134 THR   D C   1 
ATOM   12185 O O   . THR   D 1 134 ? 31.542  -2.094  68.814  1.00 19.12  ?  134 THR   D O   1 
ATOM   12186 C CB  . THR   D 1 134 ? 29.550  -1.049  66.491  1.00 22.08  ?  134 THR   D CB  1 
ATOM   12187 O OG1 . THR   D 1 134 ? 29.265  -2.367  65.986  1.00 17.68  ?  134 THR   D OG1 1 
ATOM   12188 C CG2 . THR   D 1 134 ? 29.086  0.012   65.496  1.00 24.08  ?  134 THR   D CG2 1 
ATOM   12189 N N   . THR   D 1 135 ? 31.900  -3.187  66.876  1.00 20.48  ?  135 THR   D N   1 
ATOM   12190 C CA  . THR   D 1 135 ? 32.415  -4.380  67.539  1.00 20.63  ?  135 THR   D CA  1 
ATOM   12191 C C   . THR   D 1 135 ? 33.669  -4.053  68.340  1.00 19.54  ?  135 THR   D C   1 
ATOM   12192 O O   . THR   D 1 135 ? 33.754  -4.352  69.540  1.00 16.00  ?  135 THR   D O   1 
ATOM   12193 C CB  . THR   D 1 135 ? 32.698  -5.461  66.492  1.00 23.12  ?  135 THR   D CB  1 
ATOM   12194 O OG1 . THR   D 1 135 ? 31.569  -5.574  65.615  1.00 19.79  ?  135 THR   D OG1 1 
ATOM   12195 C CG2 . THR   D 1 135 ? 32.960  -6.804  67.150  1.00 18.33  ?  135 THR   D CG2 1 
ATOM   12196 N N   . ALA   D 1 136 ? 34.649  -3.419  67.692  1.00 17.72  ?  136 ALA   D N   1 
ATOM   12197 C CA  . ALA   D 1 136 ? 35.859  -2.998  68.390  1.00 20.41  ?  136 ALA   D CA  1 
ATOM   12198 C C   . ALA   D 1 136 ? 35.538  -2.041  69.532  1.00 22.85  ?  136 ALA   D C   1 
ATOM   12199 O O   . ALA   D 1 136 ? 36.170  -2.099  70.592  1.00 23.77  ?  136 ALA   D O   1 
ATOM   12200 C CB  . ALA   D 1 136 ? 36.832  -2.348  67.405  1.00 22.97  ?  136 ALA   D CB  1 
ATOM   12201 N N   . ALA   D 1 137 ? 34.564  -1.146  69.340  1.00 19.63  ?  137 ALA   D N   1 
ATOM   12202 C CA  . ALA   D 1 137 ? 34.232  -0.199  70.401  1.00 23.39  ?  137 ALA   D CA  1 
ATOM   12203 C C   . ALA   D 1 137 ? 33.740  -0.921  71.650  1.00 21.51  ?  137 ALA   D C   1 
ATOM   12204 O O   . ALA   D 1 137 ? 34.114  -0.564  72.771  1.00 22.73  ?  137 ALA   D O   1 
ATOM   12205 C CB  . ALA   D 1 137 ? 33.192  0.807   69.913  1.00 19.26  ?  137 ALA   D CB  1 
ATOM   12206 N N   . HIS   D 1 138 ? 32.915  -1.954  71.478  1.00 22.14  ?  138 HIS   D N   1 
ATOM   12207 C CA  . HIS   D 1 138 ? 32.428  -2.689  72.641  1.00 21.17  ?  138 HIS   D CA  1 
ATOM   12208 C C   . HIS   D 1 138 ? 33.537  -3.514  73.278  1.00 23.04  ?  138 HIS   D C   1 
ATOM   12209 O O   . HIS   D 1 138 ? 33.603  -3.628  74.510  1.00 19.96  ?  138 HIS   D O   1 
ATOM   12210 C CB  . HIS   D 1 138 ? 31.245  -3.571  72.250  1.00 18.37  ?  138 HIS   D CB  1 
ATOM   12211 C CG  . HIS   D 1 138 ? 29.971  -2.806  72.098  1.00 20.23  ?  138 HIS   D CG  1 
ATOM   12212 N ND1 . HIS   D 1 138 ? 29.230  -2.380  73.179  1.00 16.58  ?  138 HIS   D ND1 1 
ATOM   12213 C CD2 . HIS   D 1 138 ? 29.333  -2.346  70.996  1.00 15.81  ?  138 HIS   D CD2 1 
ATOM   12214 C CE1 . HIS   D 1 138 ? 28.177  -1.711  72.747  1.00 19.22  ?  138 HIS   D CE1 1 
ATOM   12215 N NE2 . HIS   D 1 138 ? 28.218  -1.672  71.427  1.00 16.24  ?  138 HIS   D NE2 1 
ATOM   12216 N N   . VAL   D 1 139 ? 34.413  -4.100  72.459  1.00 22.70  ?  139 VAL   D N   1 
ATOM   12217 C CA  . VAL   D 1 139 ? 35.570  -4.815  72.998  1.00 23.62  ?  139 VAL   D CA  1 
ATOM   12218 C C   . VAL   D 1 139 ? 36.366  -3.895  73.910  1.00 19.83  ?  139 VAL   D C   1 
ATOM   12219 O O   . VAL   D 1 139 ? 36.701  -4.248  75.047  1.00 20.19  ?  139 VAL   D O   1 
ATOM   12220 C CB  . VAL   D 1 139 ? 36.438  -5.374  71.856  1.00 20.84  ?  139 VAL   D CB  1 
ATOM   12221 C CG1 . VAL   D 1 139 ? 37.792  -5.809  72.384  1.00 21.94  ?  139 VAL   D CG1 1 
ATOM   12222 C CG2 . VAL   D 1 139 ? 35.724  -6.548  71.176  1.00 17.30  ?  139 VAL   D CG2 1 
ATOM   12223 N N   . GLU   D 1 140 ? 36.636  -2.679  73.441  1.00 23.00  ?  140 GLU   D N   1 
ATOM   12224 C CA  . GLU   D 1 140 ? 37.454  -1.748  74.206  1.00 19.65  ?  140 GLU   D CA  1 
ATOM   12225 C C   . GLU   D 1 140 ? 36.705  -1.154  75.399  1.00 23.06  ?  140 GLU   D C   1 
ATOM   12226 O O   . GLU   D 1 140 ? 37.299  -0.972  76.466  1.00 25.85  ?  140 GLU   D O   1 
ATOM   12227 C CB  . GLU   D 1 140 ? 37.967  -0.659  73.274  1.00 22.90  ?  140 GLU   D CB  1 
ATOM   12228 C CG  . GLU   D 1 140 ? 38.810  -1.226  72.140  1.00 26.66  ?  140 GLU   D CG  1 
ATOM   12229 C CD  . GLU   D 1 140 ? 39.173  -0.199  71.082  1.00 33.92  ?  140 GLU   D CD  1 
ATOM   12230 O OE1 . GLU   D 1 140 ? 38.509  0.864   71.014  1.00 35.01  ?  140 GLU   D OE1 1 
ATOM   12231 O OE2 . GLU   D 1 140 ? 40.126  -0.465  70.314  1.00 31.30  ?  140 GLU   D OE2 1 
ATOM   12232 N N   . LEU   D 1 141 ? 35.409  -0.850  75.255  1.00 20.58  ?  141 LEU   D N   1 
ATOM   12233 C CA  . LEU   D 1 141 ? 34.637  -0.329  76.386  1.00 21.68  ?  141 LEU   D CA  1 
ATOM   12234 C C   . LEU   D 1 141 ? 34.610  -1.309  77.545  1.00 23.64  ?  141 LEU   D C   1 
ATOM   12235 O O   . LEU   D 1 141 ? 34.387  -0.913  78.695  1.00 24.34  ?  141 LEU   D O   1 
ATOM   12236 C CB  . LEU   D 1 141 ? 33.198  -0.023  75.971  1.00 23.78  ?  141 LEU   D CB  1 
ATOM   12237 C CG  . LEU   D 1 141 ? 32.909  1.227   75.148  1.00 32.34  ?  141 LEU   D CG  1 
ATOM   12238 C CD1 . LEU   D 1 141 ? 31.514  1.151   74.540  1.00 29.13  ?  141 LEU   D CD1 1 
ATOM   12239 C CD2 . LEU   D 1 141 ? 33.040  2.451   76.021  1.00 34.37  ?  141 LEU   D CD2 1 
ATOM   12240 N N   . ASN   D 1 142 ? 34.789  -2.593  77.260  1.00 23.12  ?  142 ASN   D N   1 
ATOM   12241 C CA  . ASN   D 1 142 ? 34.862  -3.610  78.290  1.00 23.46  ?  142 ASN   D CA  1 
ATOM   12242 C C   . ASN   D 1 142 ? 36.297  -3.901  78.722  1.00 24.43  ?  142 ASN   D C   1 
ATOM   12243 O O   . ASN   D 1 142 ? 36.554  -4.958  79.300  1.00 26.27  ?  142 ASN   D O   1 
ATOM   12244 C CB  . ASN   D 1 142 ? 34.158  -4.881  77.808  1.00 22.85  ?  142 ASN   D CB  1 
ATOM   12245 C CG  . ASN   D 1 142 ? 32.636  -4.725  77.779  1.00 26.10  ?  142 ASN   D CG  1 
ATOM   12246 O OD1 . ASN   D 1 142 ? 31.962  -4.911  78.799  1.00 27.23  ?  142 ASN   D OD1 1 
ATOM   12247 N ND2 . ASN   D 1 142 ? 32.093  -4.371  76.616  1.00 19.82  ?  142 ASN   D ND2 1 
ATOM   12248 N N   . GLY   D 1 143 ? 37.231  -2.987  78.455  1.00 22.32  ?  143 GLY   D N   1 
ATOM   12249 C CA  . GLY   D 1 143 ? 38.595  -3.137  78.920  1.00 23.84  ?  143 GLY   D CA  1 
ATOM   12250 C C   . GLY   D 1 143 ? 39.409  -4.199  78.218  1.00 25.73  ?  143 GLY   D C   1 
ATOM   12251 O O   . GLY   D 1 143 ? 40.389  -4.683  78.786  1.00 29.82  ?  143 GLY   D O   1 
ATOM   12252 N N   . CYS   D 1 144 ? 39.036  -4.580  77.002  1.00 20.79  ?  144 CYS   D N   1 
ATOM   12253 C CA  . CYS   D 1 144 ? 39.775  -5.558  76.220  1.00 21.91  ?  144 CYS   D CA  1 
ATOM   12254 C C   . CYS   D 1 144 ? 40.431  -4.894  75.014  1.00 24.09  ?  144 CYS   D C   1 
ATOM   12255 O O   . CYS   D 1 144 ? 40.130  -3.752  74.654  1.00 22.88  ?  144 CYS   D O   1 
ATOM   12256 C CB  . CYS   D 1 144 ? 38.852  -6.686  75.746  1.00 21.40  ?  144 CYS   D CB  1 
ATOM   12257 S SG  . CYS   D 1 144 ? 37.923  -7.512  77.031  1.00 23.97  ?  144 CYS   D SG  1 
ATOM   12258 N N   . LYS   D 1 145 ? 41.316  -5.647  74.368  1.00 23.40  ?  145 LYS   D N   1 
ATOM   12259 C CA  . LYS   D 1 145 ? 41.993  -5.214  73.154  1.00 22.60  ?  145 LYS   D CA  1 
ATOM   12260 C C   . LYS   D 1 145 ? 41.374  -5.891  71.940  1.00 21.28  ?  145 LYS   D C   1 
ATOM   12261 O O   . LYS   D 1 145 ? 41.045  -7.081  71.979  1.00 21.24  ?  145 LYS   D O   1 
ATOM   12262 C CB  . LYS   D 1 145 ? 43.486  -5.539  73.213  1.00 25.30  ?  145 LYS   D CB  1 
ATOM   12263 C CG  . LYS   D 1 145 ? 44.234  -4.852  74.332  1.00 26.23  ?  145 LYS   D CG  1 
ATOM   12264 C CD  . LYS   D 1 145 ? 45.717  -5.215  74.291  1.00 32.75  ?  145 LYS   D CD  1 
ATOM   12265 C CE  . LYS   D 1 145 ? 46.497  -4.390  75.302  1.00 40.34  ?  145 LYS   D CE  1 
ATOM   12266 N NZ  . LYS   D 1 145 ? 46.055  -2.962  75.273  1.00 36.24  ?  145 LYS   D NZ  1 
ATOM   12267 N N   . ALA   D 1 146 ? 41.218  -5.131  70.862  1.00 20.48  ?  146 ALA   D N   1 
ATOM   12268 C CA  . ALA   D 1 146 ? 40.661  -5.644  69.616  1.00 22.36  ?  146 ALA   D CA  1 
ATOM   12269 C C   . ALA   D 1 146 ? 41.817  -5.888  68.657  1.00 22.31  ?  146 ALA   D C   1 
ATOM   12270 O O   . ALA   D 1 146 ? 42.442  -4.936  68.176  1.00 29.65  ?  146 ALA   D O   1 
ATOM   12271 C CB  . ALA   D 1 146 ? 39.640  -4.672  69.020  1.00 20.86  ?  146 ALA   D CB  1 
ATOM   12272 N N   . ILE   D 1 147 ? 42.102  -7.159  68.385  1.00 23.78  ?  147 ILE   D N   1 
ATOM   12273 C CA  . ILE   D 1 147 ? 43.220  -7.565  67.539  1.00 19.25  ?  147 ILE   D CA  1 
ATOM   12274 C C   . ILE   D 1 147 ? 42.662  -8.012  66.194  1.00 18.40  ?  147 ILE   D C   1 
ATOM   12275 O O   . ILE   D 1 147 ? 41.832  -8.930  66.132  1.00 19.16  ?  147 ILE   D O   1 
ATOM   12276 C CB  . ILE   D 1 147 ? 44.045  -8.684  68.192  1.00 20.47  ?  147 ILE   D CB  1 
ATOM   12277 C CG1 . ILE   D 1 147 ? 44.600  -8.223  69.551  1.00 20.48  ?  147 ILE   D CG1 1 
ATOM   12278 C CG2 . ILE   D 1 147 ? 45.168  -9.108  67.263  1.00 20.73  ?  147 ILE   D CG2 1 
ATOM   12279 C CD1 . ILE   D 1 147 ? 45.306  -9.302  70.330  1.00 19.76  ?  147 ILE   D CD1 1 
ATOM   12280 N N   . ASN   D 1 148 ? 43.115  -7.374  65.118  1.00 20.40  ?  148 ASN   D N   1 
ATOM   12281 C CA  . ASN   D 1 148 ? 42.673  -7.694  63.766  1.00 21.10  ?  148 ASN   D CA  1 
ATOM   12282 C C   . ASN   D 1 148 ? 43.800  -8.388  63.018  1.00 24.04  ?  148 ASN   D C   1 
ATOM   12283 O O   . ASN   D 1 148 ? 44.919  -7.869  62.965  1.00 27.65  ?  148 ASN   D O   1 
ATOM   12284 C CB  . ASN   D 1 148 ? 42.258  -6.435  63.009  1.00 22.61  ?  148 ASN   D CB  1 
ATOM   12285 C CG  . ASN   D 1 148 ? 41.210  -5.643  63.739  1.00 22.68  ?  148 ASN   D CG  1 
ATOM   12286 O OD1 . ASN   D 1 148 ? 40.200  -6.191  64.184  1.00 20.87  ?  148 ASN   D OD1 1 
ATOM   12287 N ND2 . ASN   D 1 148 ? 41.443  -4.341  63.877  1.00 23.15  ?  148 ASN   D ND2 1 
ATOM   12288 N N   . ILE   D 1 149 ? 43.505  -9.545  62.426  1.00 23.79  ?  149 ILE   D N   1 
ATOM   12289 C CA  . ILE   D 1 149 ? 44.542  -10.316 61.747  1.00 23.06  ?  149 ILE   D CA  1 
ATOM   12290 C C   . ILE   D 1 149 ? 44.077  -10.751 60.358  1.00 24.52  ?  149 ILE   D C   1 
ATOM   12291 O O   . ILE   D 1 149 ? 44.201  -11.926 59.985  1.00 23.80  ?  149 ILE   D O   1 
ATOM   12292 C CB  . ILE   D 1 149 ? 44.962  -11.529 62.601  1.00 22.43  ?  149 ILE   D CB  1 
ATOM   12293 C CG1 . ILE   D 1 149 ? 43.750  -12.392 62.951  1.00 23.40  ?  149 ILE   D CG1 1 
ATOM   12294 C CG2 . ILE   D 1 149 ? 45.644  -11.081 63.891  1.00 18.82  ?  149 ILE   D CG2 1 
ATOM   12295 C CD1 . ILE   D 1 149 ? 44.113  -13.712 63.547  1.00 20.52  ?  149 ILE   D CD1 1 
ATOM   12296 N N   . VAL   D 1 150 ? 43.561  -9.805  59.565  1.00 22.94  ?  150 VAL   D N   1 
ATOM   12297 C CA  . VAL   D 1 150 ? 43.075  -10.160 58.224  1.00 25.40  ?  150 VAL   D CA  1 
ATOM   12298 C C   . VAL   D 1 150 ? 44.245  -10.604 57.340  1.00 25.89  ?  150 VAL   D C   1 
ATOM   12299 O O   . VAL   D 1 150 ? 45.405  -10.247 57.557  1.00 23.00  ?  150 VAL   D O   1 
ATOM   12300 C CB  . VAL   D 1 150 ? 42.306  -8.987  57.589  1.00 24.15  ?  150 VAL   D CB  1 
ATOM   12301 C CG1 . VAL   D 1 150 ? 43.269  -7.919  57.073  1.00 24.84  ?  150 VAL   D CG1 1 
ATOM   12302 C CG2 . VAL   D 1 150 ? 41.386  -9.471  56.464  1.00 21.88  ?  150 VAL   D CG2 1 
ATOM   12303 N N   . THR   D 1 151 ? 43.931  -11.399 56.323  1.00 29.84  ?  151 THR   D N   1 
ATOM   12304 C CA  . THR   D 1 151 ? 44.978  -11.915 55.451  1.00 32.71  ?  151 THR   D CA  1 
ATOM   12305 C C   . THR   D 1 151 ? 45.668  -10.787 54.686  1.00 30.29  ?  151 THR   D C   1 
ATOM   12306 O O   . THR   D 1 151 ? 45.035  -9.813  54.268  1.00 25.04  ?  151 THR   D O   1 
ATOM   12307 C CB  . THR   D 1 151 ? 44.406  -12.941 54.474  1.00 24.53  ?  151 THR   D CB  1 
ATOM   12308 O OG1 . THR   D 1 151 ? 45.383  -13.222 53.469  1.00 32.26  ?  151 THR   D OG1 1 
ATOM   12309 C CG2 . THR   D 1 151 ? 43.156  -12.414 53.811  1.00 28.12  ?  151 THR   D CG2 1 
ATOM   12310 N N   . GLU   D 1 152 ? 46.983  -10.928 54.503  1.00 28.59  ?  152 GLU   D N   1 
ATOM   12311 C CA  . GLU   D 1 152 ? 47.756  -9.928  53.769  1.00 35.75  ?  152 GLU   D CA  1 
ATOM   12312 C C   . GLU   D 1 152 ? 47.235  -9.711  52.351  1.00 31.87  ?  152 GLU   D C   1 
ATOM   12313 O O   . GLU   D 1 152 ? 47.469  -8.639  51.779  1.00 32.85  ?  152 GLU   D O   1 
ATOM   12314 C CB  . GLU   D 1 152 ? 49.234  -10.330 53.717  1.00 37.39  ?  152 GLU   D CB  1 
ATOM   12315 C CG  . GLU   D 1 152 ? 49.780  -10.864 55.038  1.00 45.11  ?  152 GLU   D CG  1 
ATOM   12316 C CD  . GLU   D 1 152 ? 49.555  -9.904  56.196  1.00 52.52  ?  152 GLU   D CD  1 
ATOM   12317 O OE1 . GLU   D 1 152 ? 50.170  -8.812  56.181  1.00 49.09  ?  152 GLU   D OE1 1 
ATOM   12318 O OE2 . GLU   D 1 152 ? 48.757  -10.238 57.112  1.00 46.20  ?  152 GLU   D OE2 1 
ATOM   12319 N N   . LYS   D 1 153 ? 46.528  -10.694 51.779  1.00 28.79  ?  153 LYS   D N   1 
ATOM   12320 C CA  . LYS   D 1 153 ? 45.973  -10.532 50.439  1.00 31.61  ?  153 LYS   D CA  1 
ATOM   12321 C C   . LYS   D 1 153 ? 45.027  -9.341  50.360  1.00 30.80  ?  153 LYS   D C   1 
ATOM   12322 O O   . LYS   D 1 153 ? 44.914  -8.710  49.304  1.00 30.04  ?  153 LYS   D O   1 
ATOM   12323 C CB  . LYS   D 1 153 ? 45.247  -11.807 50.008  1.00 28.45  ?  153 LYS   D CB  1 
ATOM   12324 C CG  . LYS   D 1 153 ? 46.115  -13.049 49.989  1.00 33.80  ?  153 LYS   D CG  1 
ATOM   12325 C CD  . LYS   D 1 153 ? 45.271  -14.311 49.837  1.00 41.35  ?  153 LYS   D CD  1 
ATOM   12326 C CE  . LYS   D 1 153 ? 44.193  -14.410 50.924  1.00 43.22  ?  153 LYS   D CE  1 
ATOM   12327 N NZ  . LYS   D 1 153 ? 43.206  -15.512 50.701  1.00 37.16  ?  153 LYS   D NZ  1 
ATOM   12328 N N   . ALA   D 1 154 ? 44.350  -9.011  51.462  1.00 32.95  ?  154 ALA   D N   1 
ATOM   12329 C CA  . ALA   D 1 154 ? 43.405  -7.899  51.461  1.00 32.67  ?  154 ALA   D CA  1 
ATOM   12330 C C   . ALA   D 1 154 ? 44.087  -6.561  51.214  1.00 35.04  ?  154 ALA   D C   1 
ATOM   12331 O O   . ALA   D 1 154 ? 43.421  -5.603  50.805  1.00 29.85  ?  154 ALA   D O   1 
ATOM   12332 C CB  . ALA   D 1 154 ? 42.651  -7.852  52.791  1.00 28.73  ?  154 ALA   D CB  1 
ATOM   12333 N N   . PHE   D 1 155 ? 45.395  -6.478  51.459  1.00 31.25  ?  155 PHE   D N   1 
ATOM   12334 C CA  . PHE   D 1 155 ? 46.143  -5.232  51.360  1.00 36.38  ?  155 PHE   D CA  1 
ATOM   12335 C C   . PHE   D 1 155 ? 46.593  -4.928  49.939  1.00 39.38  ?  155 PHE   D C   1 
ATOM   12336 O O   . PHE   D 1 155 ? 47.007  -3.794  49.656  1.00 35.23  ?  155 PHE   D O   1 
ATOM   12337 C CB  . PHE   D 1 155 ? 47.361  -5.289  52.284  1.00 34.58  ?  155 PHE   D CB  1 
ATOM   12338 C CG  . PHE   D 1 155 ? 47.018  -5.541  53.730  1.00 35.87  ?  155 PHE   D CG  1 
ATOM   12339 C CD1 . PHE   D 1 155 ? 45.935  -4.913  54.320  1.00 42.74  ?  155 PHE   D CD1 1 
ATOM   12340 C CD2 . PHE   D 1 155 ? 47.783  -6.409  54.497  1.00 40.41  ?  155 PHE   D CD2 1 
ATOM   12341 C CE1 . PHE   D 1 155 ? 45.618  -5.143  55.655  1.00 42.43  ?  155 PHE   D CE1 1 
ATOM   12342 C CE2 . PHE   D 1 155 ? 47.472  -6.642  55.832  1.00 41.53  ?  155 PHE   D CE2 1 
ATOM   12343 C CZ  . PHE   D 1 155 ? 46.388  -6.008  56.407  1.00 34.35  ?  155 PHE   D CZ  1 
ATOM   12344 N N   . ASP   D 1 156 ? 46.535  -5.913  49.053  1.00 34.89  ?  156 ASP   D N   1 
ATOM   12345 C CA  . ASP   D 1 156 ? 46.856  -5.731  47.643  1.00 34.04  ?  156 ASP   D CA  1 
ATOM   12346 C C   . ASP   D 1 156 ? 45.523  -5.534  46.938  1.00 34.77  ?  156 ASP   D C   1 
ATOM   12347 O O   . ASP   D 1 156 ? 44.894  -6.492  46.491  1.00 35.67  ?  156 ASP   D O   1 
ATOM   12348 C CB  . ASP   D 1 156 ? 47.618  -6.935  47.114  1.00 36.36  ?  156 ASP   D CB  1 
ATOM   12349 C CG  . ASP   D 1 156 ? 48.222  -6.694  45.743  1.00 48.80  ?  156 ASP   D CG  1 
ATOM   12350 O OD1 . ASP   D 1 156 ? 47.818  -5.728  45.049  1.00 49.22  ?  156 ASP   D OD1 1 
ATOM   12351 O OD2 . ASP   D 1 156 ? 49.102  -7.492  45.356  1.00 53.34  ?  156 ASP   D OD2 1 
ATOM   12352 N N   . SER   D 1 157 ? 45.086  -4.273  46.852  1.00 38.59  ?  157 SER   D N   1 
ATOM   12353 C CA  . SER   D 1 157 ? 43.712  -3.986  46.440  1.00 41.13  ?  157 SER   D CA  1 
ATOM   12354 C C   . SER   D 1 157 ? 43.414  -4.540  45.054  1.00 41.87  ?  157 SER   D C   1 
ATOM   12355 O O   . SER   D 1 157 ? 42.451  -5.296  44.868  1.00 43.44  ?  157 SER   D O   1 
ATOM   12356 C CB  . SER   D 1 157 ? 43.449  -2.483  46.466  1.00 42.91  ?  157 SER   D CB  1 
ATOM   12357 O OG  . SER   D 1 157 ? 43.631  -1.959  47.762  1.00 49.47  ?  157 SER   D OG  1 
ATOM   12358 N N   . GLU   D 1 158 ? 44.233  -4.182  44.067  1.00 37.85  ?  158 GLU   D N   1 
ATOM   12359 C CA  . GLU   D 1 158 ? 43.867  -4.473  42.690  1.00 39.80  ?  158 GLU   D CA  1 
ATOM   12360 C C   . GLU   D 1 158 ? 44.163  -5.912  42.282  1.00 38.65  ?  158 GLU   D C   1 
ATOM   12361 O O   . GLU   D 1 158 ? 43.787  -6.310  41.176  1.00 38.53  ?  158 GLU   D O   1 
ATOM   12362 C CB  . GLU   D 1 158 ? 44.571  -3.489  41.745  1.00 50.00  ?  158 GLU   D CB  1 
ATOM   12363 C CG  . GLU   D 1 158 ? 44.285  -2.013  42.066  1.00 53.60  ?  158 GLU   D CG  1 
ATOM   12364 C CD  . GLU   D 1 158 ? 44.647  -1.064  40.926  1.00 63.10  ?  158 GLU   D CD  1 
ATOM   12365 O OE1 . GLU   D 1 158 ? 44.502  -1.456  39.745  1.00 62.50  ?  158 GLU   D OE1 1 
ATOM   12366 O OE2 . GLU   D 1 158 ? 45.074  0.077   41.212  1.00 62.69  ?  158 GLU   D OE2 1 
ATOM   12367 N N   . THR   D 1 159 ? 44.805  -6.706  43.135  1.00 40.32  ?  159 THR   D N   1 
ATOM   12368 C CA  . THR   D 1 159 ? 45.114  -8.092  42.798  1.00 40.01  ?  159 THR   D CA  1 
ATOM   12369 C C   . THR   D 1 159 ? 43.980  -8.998  43.270  1.00 34.58  ?  159 THR   D C   1 
ATOM   12370 O O   . THR   D 1 159 ? 43.689  -9.064  44.469  1.00 38.18  ?  159 THR   D O   1 
ATOM   12371 C CB  . THR   D 1 159 ? 46.441  -8.525  43.417  1.00 37.10  ?  159 THR   D CB  1 
ATOM   12372 O OG1 . THR   D 1 159 ? 47.497  -7.713  42.895  1.00 33.53  ?  159 THR   D OG1 1 
ATOM   12373 C CG2 . THR   D 1 159 ? 46.729  -9.980  43.085  1.00 34.33  ?  159 THR   D CG2 1 
ATOM   12374 N N   . TYR   D 1 160 ? 43.344  -9.692  42.328  1.00 29.83  ?  160 TYR   D N   1 
ATOM   12375 C CA  . TYR   D 1 160 ? 42.243  -10.581 42.670  1.00 33.56  ?  160 TYR   D CA  1 
ATOM   12376 C C   . TYR   D 1 160 ? 42.697  -11.641 43.667  1.00 36.06  ?  160 TYR   D C   1 
ATOM   12377 O O   . TYR   D 1 160 ? 43.827  -12.134 43.606  1.00 36.82  ?  160 TYR   D O   1 
ATOM   12378 C CB  . TYR   D 1 160 ? 41.688  -11.258 41.412  1.00 33.88  ?  160 TYR   D CB  1 
ATOM   12379 C CG  . TYR   D 1 160 ? 40.565  -12.230 41.702  1.00 32.81  ?  160 TYR   D CG  1 
ATOM   12380 C CD1 . TYR   D 1 160 ? 40.829  -13.555 42.053  1.00 33.19  ?  160 TYR   D CD1 1 
ATOM   12381 C CD2 . TYR   D 1 160 ? 39.238  -11.827 41.632  1.00 32.59  ?  160 TYR   D CD2 1 
ATOM   12382 C CE1 . TYR   D 1 160 ? 39.801  -14.441 42.343  1.00 30.92  ?  160 TYR   D CE1 1 
ATOM   12383 C CE2 . TYR   D 1 160 ? 38.205  -12.709 41.910  1.00 32.79  ?  160 TYR   D CE2 1 
ATOM   12384 C CZ  . TYR   D 1 160 ? 38.495  -14.013 42.266  1.00 31.46  ?  160 TYR   D CZ  1 
ATOM   12385 O OH  . TYR   D 1 160 ? 37.469  -14.891 42.542  1.00 34.74  ?  160 TYR   D OH  1 
ATOM   12386 N N   . ASP   D 1 161 ? 41.805  -11.979 44.594  1.00 30.90  ?  161 ASP   D N   1 
ATOM   12387 C CA  . ASP   D 1 161 ? 41.922  -13.174 45.415  1.00 28.82  ?  161 ASP   D CA  1 
ATOM   12388 C C   . ASP   D 1 161 ? 40.518  -13.625 45.780  1.00 28.90  ?  161 ASP   D C   1 
ATOM   12389 O O   . ASP   D 1 161 ? 39.608  -12.802 45.923  1.00 25.86  ?  161 ASP   D O   1 
ATOM   12390 C CB  . ASP   D 1 161 ? 42.747  -12.943 46.680  1.00 33.26  ?  161 ASP   D CB  1 
ATOM   12391 C CG  . ASP   D 1 161 ? 43.046  -14.237 47.420  1.00 37.98  ?  161 ASP   D CG  1 
ATOM   12392 O OD1 . ASP   D 1 161 ? 43.974  -14.963 47.005  1.00 35.27  ?  161 ASP   D OD1 1 
ATOM   12393 O OD2 . ASP   D 1 161 ? 42.351  -14.534 48.415  1.00 35.10  ?  161 ASP   D OD2 1 
ATOM   12394 N N   . ASP   D 1 162 ? 40.347  -14.944 45.910  1.00 28.84  ?  162 ASP   D N   1 
ATOM   12395 C CA  . ASP   D 1 162 ? 39.023  -15.506 46.172  1.00 29.97  ?  162 ASP   D CA  1 
ATOM   12396 C C   . ASP   D 1 162 ? 38.501  -15.135 47.557  1.00 27.30  ?  162 ASP   D C   1 
ATOM   12397 O O   . ASP   D 1 162 ? 37.284  -15.022 47.744  1.00 24.35  ?  162 ASP   D O   1 
ATOM   12398 C CB  . ASP   D 1 162 ? 39.053  -17.033 46.041  1.00 30.83  ?  162 ASP   D CB  1 
ATOM   12399 C CG  . ASP   D 1 162 ? 38.799  -17.523 44.620  1.00 33.92  ?  162 ASP   D CG  1 
ATOM   12400 O OD1 . ASP   D 1 162 ? 38.260  -16.762 43.785  1.00 35.70  ?  162 ASP   D OD1 1 
ATOM   12401 O OD2 . ASP   D 1 162 ? 39.116  -18.702 44.349  1.00 34.45  ?  162 ASP   D OD2 1 
ATOM   12402 N N   . TRP   D 1 163 ? 39.392  -14.957 48.537  1.00 24.92  ?  163 TRP   D N   1 
ATOM   12403 C CA  . TRP   D 1 163 ? 39.008  -14.911 49.948  1.00 28.07  ?  163 TRP   D CA  1 
ATOM   12404 C C   . TRP   D 1 163 ? 39.775  -13.827 50.715  1.00 25.29  ?  163 TRP   D C   1 
ATOM   12405 O O   . TRP   D 1 163 ? 40.492  -14.094 51.672  1.00 26.64  ?  163 TRP   D O   1 
ATOM   12406 C CB  . TRP   D 1 163 ? 39.241  -16.271 50.609  1.00 23.42  ?  163 TRP   D CB  1 
ATOM   12407 C CG  . TRP   D 1 163 ? 38.792  -17.452 49.799  1.00 23.25  ?  163 TRP   D CG  1 
ATOM   12408 C CD1 . TRP   D 1 163 ? 39.589  -18.347 49.164  1.00 25.17  ?  163 TRP   D CD1 1 
ATOM   12409 C CD2 . TRP   D 1 163 ? 37.440  -17.864 49.541  1.00 27.47  ?  163 TRP   D CD2 1 
ATOM   12410 N NE1 . TRP   D 1 163 ? 38.828  -19.296 48.527  1.00 27.92  ?  163 TRP   D NE1 1 
ATOM   12411 C CE2 . TRP   D 1 163 ? 37.503  -19.022 48.745  1.00 28.13  ?  163 TRP   D CE2 1 
ATOM   12412 C CE3 . TRP   D 1 163 ? 36.184  -17.372 49.915  1.00 27.65  ?  163 TRP   D CE3 1 
ATOM   12413 C CZ2 . TRP   D 1 163 ? 36.361  -19.693 48.307  1.00 25.25  ?  163 TRP   D CZ2 1 
ATOM   12414 C CZ3 . TRP   D 1 163 ? 35.049  -18.040 49.477  1.00 24.04  ?  163 TRP   D CZ3 1 
ATOM   12415 C CH2 . TRP   D 1 163 ? 35.147  -19.188 48.683  1.00 29.05  ?  163 TRP   D CH2 1 
ATOM   12416 N N   . LYS   D 1 164 ? 39.591  -12.562 50.334  1.00 23.38  ?  164 LYS   D N   1 
ATOM   12417 C CA  . LYS   D 1 164 ? 40.329  -11.497 51.010  1.00 23.88  ?  164 LYS   D CA  1 
ATOM   12418 C C   . LYS   D 1 164 ? 39.822  -11.196 52.415  1.00 24.41  ?  164 LYS   D C   1 
ATOM   12419 O O   . LYS   D 1 164 ? 40.340  -10.263 53.040  1.00 22.33  ?  164 LYS   D O   1 
ATOM   12420 C CB  . LYS   D 1 164 ? 40.295  -10.214 50.182  1.00 24.89  ?  164 LYS   D CB  1 
ATOM   12421 C CG  . LYS   D 1 164 ? 41.290  -10.195 49.040  1.00 28.90  ?  164 LYS   D CG  1 
ATOM   12422 C CD  . LYS   D 1 164 ? 41.120  -8.936  48.209  1.00 31.89  ?  164 LYS   D CD  1 
ATOM   12423 C CE  . LYS   D 1 164 ? 42.195  -8.826  47.149  1.00 29.79  ?  164 LYS   D CE  1 
ATOM   12424 N NZ  . LYS   D 1 164 ? 42.122  -7.519  46.436  1.00 28.66  ?  164 LYS   D NZ  1 
ATOM   12425 N N   . GLY   D 1 165 ? 38.833  -11.926 52.926  1.00 22.19  ?  165 GLY   D N   1 
ATOM   12426 C CA  . GLY   D 1 165 ? 38.383  -11.757 54.290  1.00 20.85  ?  165 GLY   D CA  1 
ATOM   12427 C C   . GLY   D 1 165 ? 38.902  -12.803 55.249  1.00 21.85  ?  165 GLY   D C   1 
ATOM   12428 O O   . GLY   D 1 165 ? 38.617  -12.719 56.450  1.00 23.10  ?  165 GLY   D O   1 
ATOM   12429 N N   . ASP   D 1 166 ? 39.662  -13.780 54.752  1.00 19.87  ?  166 ASP   D N   1 
ATOM   12430 C CA  . ASP   D 1 166 ? 40.204  -14.848 55.582  1.00 22.79  ?  166 ASP   D CA  1 
ATOM   12431 C C   . ASP   D 1 166 ? 40.998  -14.304 56.765  1.00 23.61  ?  166 ASP   D C   1 
ATOM   12432 O O   . ASP   D 1 166 ? 41.571  -13.208 56.718  1.00 23.37  ?  166 ASP   D O   1 
ATOM   12433 C CB  . ASP   D 1 166 ? 41.120  -15.759 54.757  1.00 25.43  ?  166 ASP   D CB  1 
ATOM   12434 C CG  . ASP   D 1 166 ? 40.358  -16.778 53.940  1.00 23.12  ?  166 ASP   D CG  1 
ATOM   12435 O OD1 . ASP   D 1 166 ? 39.120  -16.803 54.029  1.00 25.32  ?  166 ASP   D OD1 1 
ATOM   12436 O OD2 . ASP   D 1 166 ? 40.998  -17.559 53.202  1.00 33.47  ?  166 ASP   D OD2 1 
ATOM   12437 N N   . PHE   D 1 167 ? 41.021  -15.100 57.835  1.00 23.19  ?  167 PHE   D N   1 
ATOM   12438 C CA  . PHE   D 1 167 ? 41.992  -14.922 58.908  1.00 24.04  ?  167 PHE   D CA  1 
ATOM   12439 C C   . PHE   D 1 167 ? 43.395  -15.247 58.405  1.00 25.02  ?  167 PHE   D C   1 
ATOM   12440 O O   . PHE   D 1 167 ? 43.588  -16.178 57.619  1.00 23.18  ?  167 PHE   D O   1 
ATOM   12441 C CB  . PHE   D 1 167 ? 41.687  -15.859 60.082  1.00 17.63  ?  167 PHE   D CB  1 
ATOM   12442 C CG  . PHE   D 1 167 ? 40.549  -15.438 60.962  1.00 20.05  ?  167 PHE   D CG  1 
ATOM   12443 C CD1 . PHE   D 1 167 ? 39.240  -15.556 60.544  1.00 18.77  ?  167 PHE   D CD1 1 
ATOM   12444 C CD2 . PHE   D 1 167 ? 40.797  -15.003 62.256  1.00 18.47  ?  167 PHE   D CD2 1 
ATOM   12445 C CE1 . PHE   D 1 167 ? 38.195  -15.200 61.388  1.00 20.20  ?  167 PHE   D CE1 1 
ATOM   12446 C CE2 . PHE   D 1 167 ? 39.757  -14.647 63.105  1.00 15.95  ?  167 PHE   D CE2 1 
ATOM   12447 C CZ  . PHE   D 1 167 ? 38.457  -14.750 62.671  1.00 17.29  ?  167 PHE   D CZ  1 
ATOM   12448 N N   . ASP   D 1 168 ? 44.381  -14.499 58.887  1.00 21.75  ?  168 ASP   D N   1 
ATOM   12449 C CA  . ASP   D 1 168 ? 45.778  -14.903 58.759  1.00 28.54  ?  168 ASP   D CA  1 
ATOM   12450 C C   . ASP   D 1 168 ? 46.013  -16.001 59.789  1.00 23.58  ?  168 ASP   D C   1 
ATOM   12451 O O   . ASP   D 1 168 ? 46.200  -15.718 60.971  1.00 21.36  ?  168 ASP   D O   1 
ATOM   12452 C CB  . ASP   D 1 168 ? 46.701  -13.709 58.988  1.00 30.15  ?  168 ASP   D CB  1 
ATOM   12453 C CG  . ASP   D 1 168 ? 48.163  -14.014 58.678  1.00 32.02  ?  168 ASP   D CG  1 
ATOM   12454 O OD1 . ASP   D 1 168 ? 48.592  -15.182 58.813  1.00 29.69  ?  168 ASP   D OD1 1 
ATOM   12455 O OD2 . ASP   D 1 168 ? 48.892  -13.067 58.309  1.00 33.21  ?  168 ASP   D OD2 1 
ATOM   12456 N N   . ILE   D 1 169 ? 45.984  -17.263 59.351  1.00 23.09  ?  169 ILE   D N   1 
ATOM   12457 C CA  . ILE   D 1 169 ? 46.045  -18.377 60.300  1.00 25.99  ?  169 ILE   D CA  1 
ATOM   12458 C C   . ILE   D 1 169 ? 47.345  -18.336 61.098  1.00 31.41  ?  169 ILE   D C   1 
ATOM   12459 O O   . ILE   D 1 169 ? 47.364  -18.629 62.301  1.00 29.52  ?  169 ILE   D O   1 
ATOM   12460 C CB  . ILE   D 1 169 ? 45.871  -19.723 59.569  1.00 27.12  ?  169 ILE   D CB  1 
ATOM   12461 C CG1 . ILE   D 1 169 ? 44.457  -19.857 58.995  1.00 24.20  ?  169 ILE   D CG1 1 
ATOM   12462 C CG2 . ILE   D 1 169 ? 46.173  -20.880 60.508  1.00 29.00  ?  169 ILE   D CG2 1 
ATOM   12463 C CD1 . ILE   D 1 169 ? 43.362  -20.029 60.046  1.00 22.40  ?  169 ILE   D CD1 1 
ATOM   12464 N N   . LYS   D 1 170 ? 48.448  -17.963 60.446  1.00 28.11  ?  170 LYS   D N   1 
ATOM   12465 C CA  . LYS   D 1 170 ? 49.722  -17.853 61.149  1.00 31.13  ?  170 LYS   D CA  1 
ATOM   12466 C C   . LYS   D 1 170 ? 49.632  -16.849 62.296  1.00 27.85  ?  170 LYS   D C   1 
ATOM   12467 O O   . LYS   D 1 170 ? 50.093  -17.126 63.411  1.00 28.22  ?  170 LYS   D O   1 
ATOM   12468 C CB  . LYS   D 1 170 ? 50.818  -17.469 60.152  1.00 26.96  ?  170 LYS   D CB  1 
ATOM   12469 C CG  . LYS   D 1 170 ? 52.222  -17.333 60.714  1.00 35.17  ?  170 LYS   D CG  1 
ATOM   12470 C CD  . LYS   D 1 170 ? 53.209  -17.023 59.578  1.00 34.61  ?  170 LYS   D CD  1 
ATOM   12471 C CE  . LYS   D 1 170 ? 54.669  -17.214 59.986  1.00 37.09  ?  170 LYS   D CE  1 
ATOM   12472 N NZ  . LYS   D 1 170 ? 55.207  -16.125 60.854  1.00 39.38  ?  170 LYS   D NZ  1 
ATOM   12473 N N   . LYS   D 1 171 ? 49.020  -15.687 62.052  1.00 28.18  ?  171 LYS   D N   1 
ATOM   12474 C CA  . LYS   D 1 171 ? 48.911  -14.678 63.104  1.00 27.99  ?  171 LYS   D CA  1 
ATOM   12475 C C   . LYS   D 1 171 ? 47.935  -15.097 64.197  1.00 27.28  ?  171 LYS   D C   1 
ATOM   12476 O O   . LYS   D 1 171 ? 48.088  -14.677 65.352  1.00 23.98  ?  171 LYS   D O   1 
ATOM   12477 C CB  . LYS   D 1 171 ? 48.485  -13.332 62.516  1.00 30.15  ?  171 LYS   D CB  1 
ATOM   12478 C CG  . LYS   D 1 171 ? 49.503  -12.693 61.585  1.00 29.22  ?  171 LYS   D CG  1 
ATOM   12479 C CD  . LYS   D 1 171 ? 49.010  -11.344 61.098  1.00 27.46  ?  171 LYS   D CD  1 
ATOM   12480 C CE  . LYS   D 1 171 ? 50.015  -10.684 60.170  1.00 36.54  ?  171 LYS   D CE  1 
ATOM   12481 N NZ  . LYS   D 1 171 ? 49.550  -9.333  59.755  1.00 44.33  ?  171 LYS   D NZ  1 
ATOM   12482 N N   . LEU   D 1 172 ? 46.921  -15.899 63.855  1.00 25.25  ?  172 LEU   D N   1 
ATOM   12483 C CA  . LEU   D 1 172 ? 46.028  -16.431 64.881  1.00 25.37  ?  172 LEU   D CA  1 
ATOM   12484 C C   . LEU   D 1 172 ? 46.803  -17.283 65.877  1.00 31.35  ?  172 LEU   D C   1 
ATOM   12485 O O   . LEU   D 1 172 ? 46.679  -17.107 67.097  1.00 26.15  ?  172 LEU   D O   1 
ATOM   12486 C CB  . LEU   D 1 172 ? 44.904  -17.242 64.240  1.00 20.76  ?  172 LEU   D CB  1 
ATOM   12487 C CG  . LEU   D 1 172 ? 43.933  -17.860 65.246  1.00 27.20  ?  172 LEU   D CG  1 
ATOM   12488 C CD1 . LEU   D 1 172 ? 43.218  -16.774 66.047  1.00 20.16  ?  172 LEU   D CD1 1 
ATOM   12489 C CD2 . LEU   D 1 172 ? 42.936  -18.772 64.561  1.00 22.91  ?  172 LEU   D CD2 1 
ATOM   12490 N N   . LYS   D 1 173 ? 47.634  -18.197 65.372  1.00 24.15  ?  173 LYS   D N   1 
ATOM   12491 C CA  . LYS   D 1 173 ? 48.435  -19.037 66.253  1.00 28.53  ?  173 LYS   D CA  1 
ATOM   12492 C C   . LYS   D 1 173 ? 49.450  -18.215 67.038  1.00 29.43  ?  173 LYS   D C   1 
ATOM   12493 O O   . LYS   D 1 173 ? 49.637  -18.441 68.239  1.00 30.50  ?  173 LYS   D O   1 
ATOM   12494 C CB  . LYS   D 1 173 ? 49.138  -20.124 65.442  1.00 29.23  ?  173 LYS   D CB  1 
ATOM   12495 C CG  . LYS   D 1 173 ? 48.204  -21.144 64.840  1.00 23.53  ?  173 LYS   D CG  1 
ATOM   12496 C CD  . LYS   D 1 173 ? 48.950  -22.062 63.890  1.00 31.58  ?  173 LYS   D CD  1 
ATOM   12497 C CE  . LYS   D 1 173 ? 48.045  -23.171 63.368  1.00 41.73  ?  173 LYS   D CE  1 
ATOM   12498 N NZ  . LYS   D 1 173 ? 48.764  -24.117 62.467  1.00 42.71  ?  173 LYS   D NZ  1 
ATOM   12499 N N   . GLU   D 1 174 ? 50.124  -17.268 66.380  1.00 27.61  ?  174 GLU   D N   1 
ATOM   12500 C CA  . GLU   D 1 174 ? 51.081  -16.418 67.082  1.00 24.13  ?  174 GLU   D CA  1 
ATOM   12501 C C   . GLU   D 1 174 ? 50.414  -15.680 68.235  1.00 30.09  ?  174 GLU   D C   1 
ATOM   12502 O O   . GLU   D 1 174 ? 50.938  -15.657 69.355  1.00 28.24  ?  174 GLU   D O   1 
ATOM   12503 C CB  . GLU   D 1 174 ? 51.723  -15.428 66.112  1.00 28.97  ?  174 GLU   D CB  1 
ATOM   12504 C CG  . GLU   D 1 174 ? 52.680  -16.064 65.112  1.00 32.77  ?  174 GLU   D CG  1 
ATOM   12505 C CD  . GLU   D 1 174 ? 52.996  -15.157 63.919  1.00 41.37  ?  174 GLU   D CD  1 
ATOM   12506 O OE1 . GLU   D 1 174 ? 52.509  -14.002 63.876  1.00 38.01  ?  174 GLU   D OE1 1 
ATOM   12507 O OE2 . GLU   D 1 174 ? 53.736  -15.608 63.016  1.00 45.76  ?  174 GLU   D OE2 1 
ATOM   12508 N N   . ASN   D 1 175 ? 49.244  -15.083 67.981  1.00 23.53  ?  175 ASN   D N   1 
ATOM   12509 C CA  . ASN   D 1 175 ? 48.559  -14.313 69.018  1.00 28.40  ?  175 ASN   D CA  1 
ATOM   12510 C C   . ASN   D 1 175 ? 48.062  -15.206 70.144  1.00 24.87  ?  175 ASN   D C   1 
ATOM   12511 O O   . ASN   D 1 175 ? 48.067  -14.798 71.309  1.00 23.87  ?  175 ASN   D O   1 
ATOM   12512 C CB  . ASN   D 1 175 ? 47.390  -13.532 68.421  1.00 22.27  ?  175 ASN   D CB  1 
ATOM   12513 C CG  . ASN   D 1 175 ? 47.797  -12.162 67.941  1.00 24.84  ?  175 ASN   D CG  1 
ATOM   12514 O OD1 . ASN   D 1 175 ? 47.908  -11.225 68.733  1.00 30.31  ?  175 ASN   D OD1 1 
ATOM   12515 N ND2 . ASN   D 1 175 ? 48.039  -12.036 66.643  1.00 26.27  ?  175 ASN   D ND2 1 
ATOM   12516 N N   . ILE   D 1 176 ? 47.595  -16.411 69.818  1.00 24.26  ?  176 ILE   D N   1 
ATOM   12517 C CA  . ILE   D 1 176 ? 47.189  -17.339 70.867  1.00 23.67  ?  176 ILE   D CA  1 
ATOM   12518 C C   . ILE   D 1 176 ? 48.382  -17.678 71.748  1.00 27.02  ?  176 ILE   D C   1 
ATOM   12519 O O   . ILE   D 1 176 ? 48.268  -17.746 72.979  1.00 23.72  ?  176 ILE   D O   1 
ATOM   12520 C CB  . ILE   D 1 176 ? 46.543  -18.594 70.247  1.00 25.24  ?  176 ILE   D CB  1 
ATOM   12521 C CG1 . ILE   D 1 176 ? 45.234  -18.210 69.557  1.00 23.93  ?  176 ILE   D CG1 1 
ATOM   12522 C CG2 . ILE   D 1 176 ? 46.287  -19.659 71.301  1.00 25.61  ?  176 ILE   D CG2 1 
ATOM   12523 C CD1 . ILE   D 1 176 ? 44.472  -19.372 68.957  1.00 27.93  ?  176 ILE   D CD1 1 
ATOM   12524 N N   . ALA   D 1 177 ? 49.556  -17.849 71.137  1.00 26.32  ?  177 ALA   D N   1 
ATOM   12525 C CA  . ALA   D 1 177 ? 50.767  -18.104 71.907  1.00 27.57  ?  177 ALA   D CA  1 
ATOM   12526 C C   . ALA   D 1 177 ? 51.179  -16.878 72.711  1.00 28.00  ?  177 ALA   D C   1 
ATOM   12527 O O   . ALA   D 1 177 ? 51.509  -16.987 73.902  1.00 26.22  ?  177 ALA   D O   1 
ATOM   12528 C CB  . ALA   D 1 177 ? 51.899  -18.539 70.974  1.00 25.87  ?  177 ALA   D CB  1 
ATOM   12529 N N   . GLN   D 1 178 ? 51.163  -15.705 72.079  1.00 24.69  ?  178 GLN   D N   1 
ATOM   12530 C CA  . GLN   D 1 178 ? 51.647  -14.497 72.738  1.00 28.04  ?  178 GLN   D CA  1 
ATOM   12531 C C   . GLN   D 1 178 ? 50.776  -14.131 73.934  1.00 28.98  ?  178 GLN   D C   1 
ATOM   12532 O O   . GLN   D 1 178 ? 51.279  -13.921 75.044  1.00 23.50  ?  178 GLN   D O   1 
ATOM   12533 C CB  . GLN   D 1 178 ? 51.700  -13.346 71.737  1.00 30.59  ?  178 GLN   D CB  1 
ATOM   12534 C CG  . GLN   D 1 178 ? 51.912  -11.993 72.375  1.00 34.50  ?  178 GLN   D CG  1 
ATOM   12535 C CD  . GLN   D 1 178 ? 52.212  -10.915 71.352  1.00 50.06  ?  178 GLN   D CD  1 
ATOM   12536 O OE1 . GLN   D 1 178 ? 51.601  -9.840  71.361  1.00 49.12  ?  178 GLN   D OE1 1 
ATOM   12537 N NE2 . GLN   D 1 178 ? 53.164  -11.194 70.464  1.00 59.14  ?  178 GLN   D NE2 1 
ATOM   12538 N N   . HIS   D 1 179 ? 49.464  -14.053 73.730  1.00 25.88  ?  179 HIS   D N   1 
ATOM   12539 C CA  . HIS   D 1 179 ? 48.589  -13.626 74.811  1.00 24.79  ?  179 HIS   D CA  1 
ATOM   12540 C C   . HIS   D 1 179 ? 48.185  -14.784 75.711  1.00 29.20  ?  179 HIS   D C   1 
ATOM   12541 O O   . HIS   D 1 179 ? 47.921  -14.571 76.903  1.00 26.24  ?  179 HIS   D O   1 
ATOM   12542 C CB  . HIS   D 1 179 ? 47.351  -12.939 74.239  1.00 23.03  ?  179 HIS   D CB  1 
ATOM   12543 C CG  . HIS   D 1 179 ? 47.650  -11.651 73.536  1.00 25.95  ?  179 HIS   D CG  1 
ATOM   12544 N ND1 . HIS   D 1 179 ? 47.771  -10.450 74.202  1.00 20.18  ?  179 HIS   D ND1 1 
ATOM   12545 C CD2 . HIS   D 1 179 ? 47.845  -11.375 72.223  1.00 26.92  ?  179 HIS   D CD2 1 
ATOM   12546 C CE1 . HIS   D 1 179 ? 48.033  -9.491  73.331  1.00 26.48  ?  179 HIS   D CE1 1 
ATOM   12547 N NE2 . HIS   D 1 179 ? 48.083  -10.025 72.123  1.00 28.48  ?  179 HIS   D NE2 1 
ATOM   12548 N N   . GLY   D 1 180 ? 48.155  -16.004 75.178  1.00 22.41  ?  180 GLY   D N   1 
ATOM   12549 C CA  . GLY   D 1 180 ? 47.711  -17.141 75.951  1.00 20.30  ?  180 GLY   D CA  1 
ATOM   12550 C C   . GLY   D 1 180 ? 46.237  -17.392 75.746  1.00 22.01  ?  180 GLY   D C   1 
ATOM   12551 O O   . GLY   D 1 180 ? 45.443  -16.450 75.718  1.00 22.50  ?  180 GLY   D O   1 
ATOM   12552 N N   . ALA   D 1 181 ? 45.858  -18.662 75.597  1.00 25.92  ?  181 ALA   D N   1 
ATOM   12553 C CA  . ALA   D 1 181 ? 44.454  -18.996 75.385  1.00 25.49  ?  181 ALA   D CA  1 
ATOM   12554 C C   . ALA   D 1 181 ? 43.567  -18.468 76.506  1.00 28.78  ?  181 ALA   D C   1 
ATOM   12555 O O   . ALA   D 1 181 ? 42.405  -18.128 76.262  1.00 26.42  ?  181 ALA   D O   1 
ATOM   12556 C CB  . ALA   D 1 181 ? 44.295  -20.509 75.245  1.00 22.85  ?  181 ALA   D CB  1 
ATOM   12557 N N   . ASP   D 1 182 ? 44.099  -18.364 77.730  1.00 24.25  ?  182 ASP   D N   1 
ATOM   12558 C CA  . ASP   D 1 182 ? 43.296  -17.931 78.868  1.00 27.52  ?  182 ASP   D CA  1 
ATOM   12559 C C   . ASP   D 1 182 ? 42.920  -16.454 78.804  1.00 26.84  ?  182 ASP   D C   1 
ATOM   12560 O O   . ASP   D 1 182 ? 41.958  -16.053 79.468  1.00 26.49  ?  182 ASP   D O   1 
ATOM   12561 C CB  . ASP   D 1 182 ? 44.033  -18.222 80.178  1.00 30.14  ?  182 ASP   D CB  1 
ATOM   12562 C CG  . ASP   D 1 182 ? 44.036  -19.701 80.532  1.00 41.01  ?  182 ASP   D CG  1 
ATOM   12563 O OD1 . ASP   D 1 182 ? 43.369  -20.488 79.826  1.00 43.41  ?  182 ASP   D OD1 1 
ATOM   12564 O OD2 . ASP   D 1 182 ? 44.704  -20.082 81.521  1.00 45.71  ?  182 ASP   D OD2 1 
ATOM   12565 N N   . ASN   D 1 183 ? 43.645  -15.636 78.035  1.00 21.93  ?  183 ASN   D N   1 
ATOM   12566 C CA  . ASN   D 1 183 ? 43.303  -14.222 77.895  1.00 20.65  ?  183 ASN   D CA  1 
ATOM   12567 C C   . ASN   D 1 183 ? 42.414  -13.929 76.692  1.00 22.53  ?  183 ASN   D C   1 
ATOM   12568 O O   . ASN   D 1 183 ? 41.947  -12.794 76.546  1.00 19.51  ?  183 ASN   D O   1 
ATOM   12569 C CB  . ASN   D 1 183 ? 44.570  -13.364 77.788  1.00 21.35  ?  183 ASN   D CB  1 
ATOM   12570 C CG  . ASN   D 1 183 ? 45.246  -13.139 79.134  1.00 25.52  ?  183 ASN   D CG  1 
ATOM   12571 O OD1 . ASN   D 1 183 ? 44.600  -12.788 80.128  1.00 21.98  ?  183 ASN   D OD1 1 
ATOM   12572 N ND2 . ASN   D 1 183 ? 46.554  -13.349 79.172  1.00 26.41  ?  183 ASN   D ND2 1 
ATOM   12573 N N   . ILE   D 1 184 ? 42.161  -14.907 75.830  1.00 20.51  ?  184 ILE   D N   1 
ATOM   12574 C CA  . ILE   D 1 184 ? 41.408  -14.673 74.605  1.00 19.16  ?  184 ILE   D CA  1 
ATOM   12575 C C   . ILE   D 1 184 ? 39.932  -14.904 74.924  1.00 17.74  ?  184 ILE   D C   1 
ATOM   12576 O O   . ILE   D 1 184 ? 39.471  -16.043 75.040  1.00 17.20  ?  184 ILE   D O   1 
ATOM   12577 C CB  . ILE   D 1 184 ? 41.913  -15.552 73.462  1.00 18.47  ?  184 ILE   D CB  1 
ATOM   12578 C CG1 . ILE   D 1 184 ? 43.379  -15.220 73.186  1.00 16.82  ?  184 ILE   D CG1 1 
ATOM   12579 C CG2 . ILE   D 1 184 ? 41.103  -15.319 72.198  1.00 17.81  ?  184 ILE   D CG2 1 
ATOM   12580 C CD1 . ILE   D 1 184 ? 43.973  -16.024 72.094  1.00 26.01  ?  184 ILE   D CD1 1 
ATOM   12581 N N   . VAL   D 1 185 ? 39.186  -13.803 75.063  1.00 16.33  ?  185 VAL   D N   1 
ATOM   12582 C CA  . VAL   D 1 185 ? 37.781  -13.893 75.457  1.00 15.73  ?  185 VAL   D CA  1 
ATOM   12583 C C   . VAL   D 1 185 ? 36.966  -14.595 74.385  1.00 15.95  ?  185 VAL   D C   1 
ATOM   12584 O O   . VAL   D 1 185 ? 36.093  -15.417 74.686  1.00 17.14  ?  185 VAL   D O   1 
ATOM   12585 C CB  . VAL   D 1 185 ? 37.214  -12.495 75.757  1.00 15.81  ?  185 VAL   D CB  1 
ATOM   12586 C CG1 . VAL   D 1 185 ? 35.720  -12.592 76.080  1.00 17.38  ?  185 VAL   D CG1 1 
ATOM   12587 C CG2 . VAL   D 1 185 ? 37.980  -11.845 76.913  1.00 16.92  ?  185 VAL   D CG2 1 
ATOM   12588 N N   . ALA   D 1 186 ? 37.234  -14.287 73.123  1.00 14.62  ?  186 ALA   D N   1 
ATOM   12589 C CA  . ALA   D 1 186 ? 36.518  -14.905 72.024  1.00 15.38  ?  186 ALA   D CA  1 
ATOM   12590 C C   . ALA   D 1 186 ? 37.241  -14.558 70.737  1.00 14.61  ?  186 ALA   D C   1 
ATOM   12591 O O   . ALA   D 1 186 ? 37.988  -13.576 70.668  1.00 15.65  ?  186 ALA   D O   1 
ATOM   12592 C CB  . ALA   D 1 186 ? 35.057  -14.445 71.958  1.00 15.85  ?  186 ALA   D CB  1 
ATOM   12593 N N   . ILE   D 1 187 ? 37.034  -15.398 69.732  1.00 14.07  ?  187 ILE   D N   1 
ATOM   12594 C CA  . ILE   D 1 187 ? 37.416  -15.105 68.359  1.00 16.13  ?  187 ILE   D CA  1 
ATOM   12595 C C   . ILE   D 1 187 ? 36.165  -14.676 67.610  1.00 15.81  ?  187 ILE   D C   1 
ATOM   12596 O O   . ILE   D 1 187 ? 35.156  -15.391 67.623  1.00 20.27  ?  187 ILE   D O   1 
ATOM   12597 C CB  . ILE   D 1 187 ? 38.071  -16.323 67.692  1.00 18.43  ?  187 ILE   D CB  1 
ATOM   12598 C CG1 . ILE   D 1 187 ? 39.423  -16.613 68.360  1.00 18.49  ?  187 ILE   D CG1 1 
ATOM   12599 C CG2 . ILE   D 1 187 ? 38.206  -16.099 66.188  1.00 15.05  ?  187 ILE   D CG2 1 
ATOM   12600 C CD1 . ILE   D 1 187 ? 40.056  -17.906 67.928  1.00 21.47  ?  187 ILE   D CD1 1 
ATOM   12601 N N   . VAL   D 1 188 ? 36.218  -13.509 66.970  1.00 15.63  ?  188 VAL   D N   1 
ATOM   12602 C CA  . VAL   D 1 188 ? 35.087  -12.973 66.214  1.00 14.99  ?  188 VAL   D CA  1 
ATOM   12603 C C   . VAL   D 1 188 ? 35.360  -13.179 64.728  1.00 17.48  ?  188 VAL   D C   1 
ATOM   12604 O O   . VAL   D 1 188 ? 36.266  -12.560 64.157  1.00 18.16  ?  188 VAL   D O   1 
ATOM   12605 C CB  . VAL   D 1 188 ? 34.841  -11.489 66.515  1.00 15.21  ?  188 VAL   D CB  1 
ATOM   12606 C CG1 . VAL   D 1 188 ? 33.599  -11.005 65.751  1.00 15.80  ?  188 VAL   D CG1 1 
ATOM   12607 C CG2 . VAL   D 1 188 ? 34.727  -11.236 68.034  1.00 16.53  ?  188 VAL   D CG2 1 
ATOM   12608 N N   . SER   D 1 189 ? 34.575  -14.039 64.090  1.00 15.38  ?  189 SER   D N   1 
ATOM   12609 C CA  . SER   D 1 189 ? 34.651  -14.230 62.647  1.00 20.08  ?  189 SER   D CA  1 
ATOM   12610 C C   . SER   D 1 189 ? 33.615  -13.331 61.979  1.00 20.07  ?  189 SER   D C   1 
ATOM   12611 O O   . SER   D 1 189 ? 32.409  -13.570 62.097  1.00 20.77  ?  189 SER   D O   1 
ATOM   12612 C CB  . SER   D 1 189 ? 34.420  -15.694 62.283  1.00 16.41  ?  189 SER   D CB  1 
ATOM   12613 O OG  . SER   D 1 189 ? 35.443  -16.495 62.838  1.00 18.69  ?  189 SER   D OG  1 
ATOM   12614 N N   . THR   D 1 190 ? 34.081  -12.310 61.264  1.00 13.90  ?  190 THR   D N   1 
ATOM   12615 C CA  . THR   D 1 190 ? 33.190  -11.357 60.614  1.00 12.08  ?  190 THR   D CA  1 
ATOM   12616 C C   . THR   D 1 190 ? 32.952  -11.804 59.174  1.00 12.60  ?  190 THR   D C   1 
ATOM   12617 O O   . THR   D 1 190 ? 33.904  -11.922 58.397  1.00 17.48  ?  190 THR   D O   1 
ATOM   12618 C CB  . THR   D 1 190 ? 33.800  -9.957  60.676  1.00 14.22  ?  190 THR   D CB  1 
ATOM   12619 O OG1 . THR   D 1 190 ? 34.240  -9.678  62.023  1.00 16.85  ?  190 THR   D OG1 1 
ATOM   12620 C CG2 . THR   D 1 190 ? 32.795  -8.922  60.270  1.00 15.34  ?  190 THR   D CG2 1 
ATOM   12621 N N   . VAL   D 1 191 ? 31.691  -12.069 58.822  1.00 15.74  ?  191 VAL   D N   1 
ATOM   12622 C CA  . VAL   D 1 191 ? 31.310  -12.559 57.494  1.00 17.56  ?  191 VAL   D CA  1 
ATOM   12623 C C   . VAL   D 1 191 ? 30.157  -11.709 56.958  1.00 17.74  ?  191 VAL   D C   1 
ATOM   12624 O O   . VAL   D 1 191 ? 29.140  -11.539 57.639  1.00 17.88  ?  191 VAL   D O   1 
ATOM   12625 C CB  . VAL   D 1 191 ? 30.920  -14.050 57.523  1.00 16.40  ?  191 VAL   D CB  1 
ATOM   12626 C CG1 . VAL   D 1 191 ? 32.129  -14.901 57.858  1.00 14.71  ?  191 VAL   D CG1 1 
ATOM   12627 C CG2 . VAL   D 1 191 ? 29.818  -14.310 58.554  1.00 15.36  ?  191 VAL   D CG2 1 
ATOM   12628 N N   . THR   D 1 192 ? 30.330  -11.123 55.768  1.00 19.52  ?  192 THR   D N   1 
ATOM   12629 C CA  . THR   D 1 192 ? 31.634  -10.950 55.135  1.00 21.09  ?  192 THR   D CA  1 
ATOM   12630 C C   . THR   D 1 192 ? 32.470  -10.006 55.960  1.00 17.72  ?  192 THR   D C   1 
ATOM   12631 O O   . THR   D 1 192 ? 31.969  -9.371  56.888  1.00 14.40  ?  192 THR   D O   1 
ATOM   12632 C CB  . THR   D 1 192 ? 31.530  -10.349 53.733  1.00 19.14  ?  192 THR   D CB  1 
ATOM   12633 O OG1 . THR   D 1 192 ? 30.818  -9.111  53.829  1.00 18.30  ?  192 THR   D OG1 1 
ATOM   12634 C CG2 . THR   D 1 192 ? 30.814  -11.287 52.780  1.00 17.77  ?  192 THR   D CG2 1 
ATOM   12635 N N   . CYS   D 1 193 ? 33.749  -9.907  55.620  1.00 17.73  ?  193 CYS   D N   1 
ATOM   12636 C CA  . CYS   D 1 193 ? 34.656  -9.034  56.356  1.00 20.38  ?  193 CYS   D CA  1 
ATOM   12637 C C   . CYS   D 1 193 ? 34.425  -7.608  55.878  1.00 21.47  ?  193 CYS   D C   1 
ATOM   12638 O O   . CYS   D 1 193 ? 34.922  -7.201  54.828  1.00 22.96  ?  193 CYS   D O   1 
ATOM   12639 C CB  . CYS   D 1 193 ? 36.101  -9.470  56.160  1.00 17.16  ?  193 CYS   D CB  1 
ATOM   12640 S SG  . CYS   D 1 193 ? 37.228  -8.620  57.259  1.00 21.35  ?  193 CYS   D SG  1 
ATOM   12641 N N   . ASN   D 1 194 ? 33.653  -6.845  56.648  1.00 22.44  ?  194 ASN   D N   1 
ATOM   12642 C CA  . ASN   D 1 194 ? 33.255  -5.512  56.209  1.00 25.32  ?  194 ASN   D CA  1 
ATOM   12643 C C   . ASN   D 1 194 ? 34.475  -4.622  56.008  1.00 25.11  ?  194 ASN   D C   1 
ATOM   12644 O O   . ASN   D 1 194 ? 34.659  -4.027  54.942  1.00 27.26  ?  194 ASN   D O   1 
ATOM   12645 C CB  . ASN   D 1 194 ? 32.291  -4.902  57.234  1.00 24.75  ?  194 ASN   D CB  1 
ATOM   12646 C CG  . ASN   D 1 194 ? 31.584  -3.661  56.717  1.00 23.65  ?  194 ASN   D CG  1 
ATOM   12647 O OD1 . ASN   D 1 194 ? 31.705  -3.303  55.549  1.00 27.46  ?  194 ASN   D OD1 1 
ATOM   12648 N ND2 . ASN   D 1 194 ? 30.824  -3.012  57.586  1.00 26.63  ?  194 ASN   D ND2 1 
ATOM   12649 N N   . SER   D 1 195 ? 35.342  -4.554  57.013  1.00 25.02  ?  195 SER   D N   1 
ATOM   12650 C CA  . SER   D 1 195 ? 36.448  -3.609  56.982  1.00 25.50  ?  195 SER   D CA  1 
ATOM   12651 C C   . SER   D 1 195 ? 37.480  -3.946  55.916  1.00 28.00  ?  195 SER   D C   1 
ATOM   12652 O O   . SER   D 1 195 ? 38.203  -3.049  55.475  1.00 36.43  ?  195 SER   D O   1 
ATOM   12653 C CB  . SER   D 1 195 ? 37.105  -3.540  58.361  1.00 27.67  ?  195 SER   D CB  1 
ATOM   12654 O OG  . SER   D 1 195 ? 36.141  -3.261  59.374  1.00 33.36  ?  195 SER   D OG  1 
ATOM   12655 N N   . ALA   D 1 196 ? 37.563  -5.203  55.480  1.00 29.38  ?  196 ALA   D N   1 
ATOM   12656 C CA  . ALA   D 1 196 ? 38.436  -5.562  54.366  1.00 30.03  ?  196 ALA   D CA  1 
ATOM   12657 C C   . ALA   D 1 196 ? 37.792  -5.316  53.009  1.00 27.44  ?  196 ALA   D C   1 
ATOM   12658 O O   . ALA   D 1 196 ? 38.390  -5.652  51.980  1.00 28.30  ?  196 ALA   D O   1 
ATOM   12659 C CB  . ALA   D 1 196 ? 38.859  -7.028  54.469  1.00 23.61  ?  196 ALA   D CB  1 
ATOM   12660 N N   . GLY   D 1 197 ? 36.592  -4.749  52.981  1.00 28.21  ?  197 GLY   D N   1 
ATOM   12661 C CA  . GLY   D 1 197 ? 35.925  -4.464  51.731  1.00 29.76  ?  197 GLY   D CA  1 
ATOM   12662 C C   . GLY   D 1 197 ? 34.751  -5.379  51.460  1.00 27.71  ?  197 GLY   D C   1 
ATOM   12663 O O   . GLY   D 1 197 ? 34.390  -5.596  50.299  1.00 31.96  ?  197 GLY   D O   1 
ATOM   12664 N N   . GLY   D 1 198 ? 34.140  -5.915  52.513  1.00 21.93  ?  198 GLY   D N   1 
ATOM   12665 C CA  . GLY   D 1 198 ? 33.048  -6.862  52.326  1.00 22.72  ?  198 GLY   D CA  1 
ATOM   12666 C C   . GLY   D 1 198 ? 33.489  -8.144  51.654  1.00 21.55  ?  198 GLY   D C   1 
ATOM   12667 O O   . GLY   D 1 198 ? 32.726  -8.730  50.875  1.00 21.61  ?  198 GLY   D O   1 
ATOM   12668 N N   . GLN   D 1 199 ? 34.704  -8.600  51.948  1.00 18.38  ?  199 GLN   D N   1 
ATOM   12669 C CA  . GLN   D 1 199 ? 35.356  -9.713  51.274  1.00 19.62  ?  199 GLN   D CA  1 
ATOM   12670 C C   . GLN   D 1 199 ? 35.074  -11.029 52.000  1.00 20.39  ?  199 GLN   D C   1 
ATOM   12671 O O   . GLN   D 1 199 ? 35.043  -11.067 53.235  1.00 20.18  ?  199 GLN   D O   1 
ATOM   12672 C CB  . GLN   D 1 199 ? 36.856  -9.475  51.192  1.00 20.92  ?  199 GLN   D CB  1 
ATOM   12673 C CG  . GLN   D 1 199 ? 37.206  -8.247  50.383  1.00 22.10  ?  199 GLN   D CG  1 
ATOM   12674 C CD  . GLN   D 1 199 ? 36.858  -8.398  48.915  1.00 23.86  ?  199 GLN   D CD  1 
ATOM   12675 O OE1 . GLN   D 1 199 ? 37.158  -9.417  48.298  1.00 27.25  ?  199 GLN   D OE1 1 
ATOM   12676 N NE2 . GLN   D 1 199 ? 36.225  -7.383  48.347  1.00 26.40  ?  199 GLN   D NE2 1 
ATOM   12677 N N   . PRO   D 1 200 ? 34.858  -12.110 51.255  1.00 20.99  ?  200 PRO   D N   1 
ATOM   12678 C CA  . PRO   D 1 200 ? 34.371  -13.349 51.868  1.00 20.08  ?  200 PRO   D CA  1 
ATOM   12679 C C   . PRO   D 1 200 ? 35.437  -14.111 52.637  1.00 20.42  ?  200 PRO   D C   1 
ATOM   12680 O O   . PRO   D 1 200 ? 36.629  -14.073 52.325  1.00 20.39  ?  200 PRO   D O   1 
ATOM   12681 C CB  . PRO   D 1 200 ? 33.895  -14.168 50.665  1.00 21.15  ?  200 PRO   D CB  1 
ATOM   12682 C CG  . PRO   D 1 200 ? 34.712  -13.668 49.529  1.00 19.58  ?  200 PRO   D CG  1 
ATOM   12683 C CD  . PRO   D 1 200 ? 34.908  -12.201 49.787  1.00 20.88  ?  200 PRO   D CD  1 
ATOM   12684 N N   . VAL   D 1 201 ? 34.974  -14.808 53.670  1.00 20.25  ?  201 VAL   D N   1 
ATOM   12685 C CA  . VAL   D 1 201 ? 35.780  -15.772 54.407  1.00 21.64  ?  201 VAL   D CA  1 
ATOM   12686 C C   . VAL   D 1 201 ? 35.414  -17.159 53.902  1.00 26.60  ?  201 VAL   D C   1 
ATOM   12687 O O   . VAL   D 1 201 ? 34.229  -17.517 53.855  1.00 24.33  ?  201 VAL   D O   1 
ATOM   12688 C CB  . VAL   D 1 201 ? 35.544  -15.658 55.922  1.00 22.83  ?  201 VAL   D CB  1 
ATOM   12689 C CG1 . VAL   D 1 201 ? 36.531  -16.534 56.676  1.00 20.88  ?  201 VAL   D CG1 1 
ATOM   12690 C CG2 . VAL   D 1 201 ? 35.650  -14.207 56.371  1.00 19.34  ?  201 VAL   D CG2 1 
ATOM   12691 N N   . SER   D 1 202 ? 36.420  -17.939 53.521  1.00 21.06  ?  202 SER   D N   1 
ATOM   12692 C CA  . SER   D 1 202 ? 36.162  -19.245 52.937  1.00 19.86  ?  202 SER   D CA  1 
ATOM   12693 C C   . SER   D 1 202 ? 35.683  -20.230 53.998  1.00 17.17  ?  202 SER   D C   1 
ATOM   12694 O O   . SER   D 1 202 ? 35.913  -20.059 55.197  1.00 20.38  ?  202 SER   D O   1 
ATOM   12695 C CB  . SER   D 1 202 ? 37.423  -19.793 52.271  1.00 25.09  ?  202 SER   D CB  1 
ATOM   12696 O OG  . SER   D 1 202 ? 38.370  -20.194 53.250  1.00 22.32  ?  202 SER   D OG  1 
ATOM   12697 N N   . MET   D 1 203 ? 35.039  -21.299 53.535  1.00 18.16  ?  203 MET   D N   1 
ATOM   12698 C CA  . MET   D 1 203 ? 34.570  -22.320 54.463  1.00 20.93  ?  203 MET   D CA  1 
ATOM   12699 C C   . MET   D 1 203 ? 35.737  -23.007 55.165  1.00 24.38  ?  203 MET   D C   1 
ATOM   12700 O O   . MET   D 1 203 ? 35.637  -23.363 56.345  1.00 23.96  ?  203 MET   D O   1 
ATOM   12701 C CB  . MET   D 1 203 ? 33.702  -23.340 53.725  1.00 20.42  ?  203 MET   D CB  1 
ATOM   12702 C CG  . MET   D 1 203 ? 32.983  -24.287 54.657  1.00 25.23  ?  203 MET   D CG  1 
ATOM   12703 S SD  . MET   D 1 203 ? 31.741  -23.447 55.659  1.00 28.17  ?  203 MET   D SD  1 
ATOM   12704 C CE  . MET   D 1 203 ? 30.461  -23.232 54.430  1.00 23.65  ?  203 MET   D CE  1 
ATOM   12705 N N   . SER   D 1 204 ? 36.858  -23.191 54.469  1.00 22.12  ?  204 SER   D N   1 
ATOM   12706 C CA  . SER   D 1 204 ? 37.988  -23.861 55.099  1.00 23.38  ?  204 SER   D CA  1 
ATOM   12707 C C   . SER   D 1 204 ? 38.737  -22.943 56.054  1.00 22.40  ?  204 SER   D C   1 
ATOM   12708 O O   . SER   D 1 204 ? 39.378  -23.430 56.991  1.00 27.57  ?  204 SER   D O   1 
ATOM   12709 C CB  . SER   D 1 204 ? 38.937  -24.410 54.037  1.00 30.26  ?  204 SER   D CB  1 
ATOM   12710 O OG  . SER   D 1 204 ? 39.562  -23.359 53.326  1.00 38.55  ?  204 SER   D OG  1 
ATOM   12711 N N   . ASN   D 1 205 ? 38.674  -21.623 55.842  1.00 21.71  ?  205 ASN   D N   1 
ATOM   12712 C CA  . ASN   D 1 205 ? 39.223  -20.692 56.826  1.00 22.48  ?  205 ASN   D CA  1 
ATOM   12713 C C   . ASN   D 1 205 ? 38.380  -20.694 58.098  1.00 22.98  ?  205 ASN   D C   1 
ATOM   12714 O O   . ASN   D 1 205 ? 38.918  -20.786 59.207  1.00 21.49  ?  205 ASN   D O   1 
ATOM   12715 C CB  . ASN   D 1 205 ? 39.311  -19.285 56.226  1.00 25.07  ?  205 ASN   D CB  1 
ATOM   12716 C CG  . ASN   D 1 205 ? 40.195  -18.339 57.033  1.00 24.63  ?  205 ASN   D CG  1 
ATOM   12717 O OD1 . ASN   D 1 205 ? 39.706  -17.404 57.670  1.00 20.76  ?  205 ASN   D OD1 1 
ATOM   12718 N ND2 . ASN   D 1 205 ? 41.509  -18.567 56.990  1.00 23.27  ?  205 ASN   D ND2 1 
ATOM   12719 N N   . LEU   D 1 206 ? 37.051  -20.607 57.960  1.00 15.87  ?  206 LEU   D N   1 
ATOM   12720 C CA  . LEU   D 1 206 ? 36.183  -20.678 59.134  1.00 18.56  ?  206 LEU   D CA  1 
ATOM   12721 C C   . LEU   D 1 206 ? 36.402  -21.978 59.895  1.00 24.86  ?  206 LEU   D C   1 
ATOM   12722 O O   . LEU   D 1 206 ? 36.516  -21.977 61.127  1.00 20.89  ?  206 LEU   D O   1 
ATOM   12723 C CB  . LEU   D 1 206 ? 34.719  -20.552 58.722  1.00 17.37  ?  206 LEU   D CB  1 
ATOM   12724 C CG  . LEU   D 1 206 ? 34.305  -19.236 58.075  1.00 22.59  ?  206 LEU   D CG  1 
ATOM   12725 C CD1 . LEU   D 1 206 ? 32.904  -19.348 57.501  1.00 22.27  ?  206 LEU   D CD1 1 
ATOM   12726 C CD2 . LEU   D 1 206 ? 34.376  -18.108 59.090  1.00 22.70  ?  206 LEU   D CD2 1 
ATOM   12727 N N   . LYS   D 1 207 ? 36.470  -23.096 59.166  1.00 26.33  ?  207 LYS   D N   1 
ATOM   12728 C CA  . LYS   D 1 207 ? 36.725  -24.397 59.773  1.00 25.37  ?  207 LYS   D CA  1 
ATOM   12729 C C   . LYS   D 1 207 ? 38.045  -24.405 60.541  1.00 23.74  ?  207 LYS   D C   1 
ATOM   12730 O O   . LYS   D 1 207 ? 38.091  -24.784 61.717  1.00 22.87  ?  207 LYS   D O   1 
ATOM   12731 C CB  . LYS   D 1 207 ? 36.720  -25.464 58.675  1.00 29.19  ?  207 LYS   D CB  1 
ATOM   12732 C CG  . LYS   D 1 207 ? 36.676  -26.906 59.149  1.00 31.84  ?  207 LYS   D CG  1 
ATOM   12733 C CD  . LYS   D 1 207 ? 36.309  -27.812 57.979  1.00 32.34  ?  207 LYS   D CD  1 
ATOM   12734 C CE  . LYS   D 1 207 ? 35.965  -29.227 58.425  1.00 35.61  ?  207 LYS   D CE  1 
ATOM   12735 N NZ  . LYS   D 1 207 ? 37.143  -29.916 59.010  1.00 39.68  ?  207 LYS   D NZ  1 
ATOM   12736 N N   . GLU   D 1 208 ? 39.133  -23.982 59.897  1.00 22.92  ?  208 GLU   D N   1 
ATOM   12737 C CA  . GLU   D 1 208 ? 40.432  -24.047 60.560  1.00 26.26  ?  208 GLU   D CA  1 
ATOM   12738 C C   . GLU   D 1 208 ? 40.492  -23.107 61.758  1.00 26.44  ?  208 GLU   D C   1 
ATOM   12739 O O   . GLU   D 1 208 ? 41.096  -23.443 62.784  1.00 28.08  ?  208 GLU   D O   1 
ATOM   12740 C CB  . GLU   D 1 208 ? 41.556  -23.733 59.572  1.00 21.88  ?  208 GLU   D CB  1 
ATOM   12741 C CG  . GLU   D 1 208 ? 42.949  -23.955 60.155  1.00 28.61  ?  208 GLU   D CG  1 
ATOM   12742 C CD  . GLU   D 1 208 ? 44.062  -23.810 59.123  1.00 28.15  ?  208 GLU   D CD  1 
ATOM   12743 O OE1 . GLU   D 1 208 ? 43.767  -23.691 57.914  1.00 27.65  ?  208 GLU   D OE1 1 
ATOM   12744 O OE2 . GLU   D 1 208 ? 45.240  -23.816 59.524  1.00 35.05  ?  208 GLU   D OE2 1 
ATOM   12745 N N   . VAL   D 1 209 ? 39.875  -21.928 61.654  1.00 23.73  ?  209 VAL   D N   1 
ATOM   12746 C CA  . VAL   D 1 209 ? 39.857  -21.011 62.792  1.00 24.55  ?  209 VAL   D CA  1 
ATOM   12747 C C   . VAL   D 1 209 ? 39.083  -21.623 63.955  1.00 26.73  ?  209 VAL   D C   1 
ATOM   12748 O O   . VAL   D 1 209 ? 39.520  -21.559 65.112  1.00 25.07  ?  209 VAL   D O   1 
ATOM   12749 C CB  . VAL   D 1 209 ? 39.281  -19.644 62.375  1.00 23.67  ?  209 VAL   D CB  1 
ATOM   12750 C CG1 . VAL   D 1 209 ? 38.866  -18.841 63.601  1.00 18.70  ?  209 VAL   D CG1 1 
ATOM   12751 C CG2 . VAL   D 1 209 ? 40.313  -18.869 61.560  1.00 19.45  ?  209 VAL   D CG2 1 
ATOM   12752 N N   . TYR   D 1 210 ? 37.932  -22.242 63.669  1.00 25.89  ?  210 TYR   D N   1 
ATOM   12753 C CA  . TYR   D 1 210 ? 37.150  -22.858 64.738  1.00 21.96  ?  210 TYR   D CA  1 
ATOM   12754 C C   . TYR   D 1 210 ? 37.899  -24.026 65.375  1.00 24.04  ?  210 TYR   D C   1 
ATOM   12755 O O   . TYR   D 1 210 ? 37.921  -24.154 66.604  1.00 29.16  ?  210 TYR   D O   1 
ATOM   12756 C CB  . TYR   D 1 210 ? 35.786  -23.309 64.214  1.00 20.56  ?  210 TYR   D CB  1 
ATOM   12757 C CG  . TYR   D 1 210 ? 34.870  -23.805 65.317  1.00 25.05  ?  210 TYR   D CG  1 
ATOM   12758 C CD1 . TYR   D 1 210 ? 34.329  -22.921 66.248  1.00 21.38  ?  210 TYR   D CD1 1 
ATOM   12759 C CD2 . TYR   D 1 210 ? 34.569  -25.155 65.445  1.00 23.61  ?  210 TYR   D CD2 1 
ATOM   12760 C CE1 . TYR   D 1 210 ? 33.507  -23.367 67.272  1.00 22.03  ?  210 TYR   D CE1 1 
ATOM   12761 C CE2 . TYR   D 1 210 ? 33.746  -25.611 66.463  1.00 24.61  ?  210 TYR   D CE2 1 
ATOM   12762 C CZ  . TYR   D 1 210 ? 33.219  -24.714 67.371  1.00 27.52  ?  210 TYR   D CZ  1 
ATOM   12763 O OH  . TYR   D 1 210 ? 32.398  -25.165 68.380  1.00 27.22  ?  210 TYR   D OH  1 
ATOM   12764 N N   . GLU   D 1 211 ? 38.527  -24.885 64.566  1.00 25.75  ?  211 GLU   D N   1 
ATOM   12765 C CA  . GLU   D 1 211 ? 39.244  -26.030 65.131  1.00 26.43  ?  211 GLU   D CA  1 
ATOM   12766 C C   . GLU   D 1 211 ? 40.404  -25.577 66.005  1.00 28.49  ?  211 GLU   D C   1 
ATOM   12767 O O   . GLU   D 1 211 ? 40.663  -26.166 67.064  1.00 30.78  ?  211 GLU   D O   1 
ATOM   12768 C CB  . GLU   D 1 211 ? 39.736  -26.953 64.016  1.00 24.07  ?  211 GLU   D CB  1 
ATOM   12769 C CG  . GLU   D 1 211 ? 38.598  -27.723 63.348  1.00 31.43  ?  211 GLU   D CG  1 
ATOM   12770 C CD  . GLU   D 1 211 ? 38.964  -28.294 61.985  1.00 36.00  ?  211 GLU   D CD  1 
ATOM   12771 O OE1 . GLU   D 1 211 ? 40.140  -28.185 61.569  1.00 43.37  ?  211 GLU   D OE1 1 
ATOM   12772 O OE2 . GLU   D 1 211 ? 38.063  -28.852 61.324  1.00 40.03  ?  211 GLU   D OE2 1 
ATOM   12773 N N   . ILE   D 1 212 ? 41.107  -24.525 65.587  1.00 23.58  ?  212 ILE   D N   1 
ATOM   12774 C CA  . ILE   D 1 212 ? 42.191  -24.002 66.405  1.00 28.16  ?  212 ILE   D CA  1 
ATOM   12775 C C   . ILE   D 1 212 ? 41.644  -23.448 67.714  1.00 28.33  ?  212 ILE   D C   1 
ATOM   12776 O O   . ILE   D 1 212 ? 42.196  -23.700 68.791  1.00 32.44  ?  212 ILE   D O   1 
ATOM   12777 C CB  . ILE   D 1 212 ? 42.981  -22.949 65.610  1.00 29.97  ?  212 ILE   D CB  1 
ATOM   12778 C CG1 . ILE   D 1 212 ? 43.785  -23.633 64.496  1.00 24.85  ?  212 ILE   D CG1 1 
ATOM   12779 C CG2 . ILE   D 1 212 ? 43.881  -22.141 66.537  1.00 27.20  ?  212 ILE   D CG2 1 
ATOM   12780 C CD1 . ILE   D 1 212 ? 44.333  -22.690 63.450  1.00 23.32  ?  212 ILE   D CD1 1 
ATOM   12781 N N   . ALA   D 1 213 ? 40.533  -22.714 67.649  1.00 26.53  ?  213 ALA   D N   1 
ATOM   12782 C CA  . ALA   D 1 213 ? 39.961  -22.140 68.863  1.00 26.78  ?  213 ALA   D CA  1 
ATOM   12783 C C   . ALA   D 1 213 ? 39.408  -23.221 69.774  1.00 25.16  ?  213 ALA   D C   1 
ATOM   12784 O O   . ALA   D 1 213 ? 39.571  -23.153 70.998  1.00 25.39  ?  213 ALA   D O   1 
ATOM   12785 C CB  . ALA   D 1 213 ? 38.862  -21.140 68.506  1.00 26.45  ?  213 ALA   D CB  1 
ATOM   12786 N N   . LYS   D 1 214 ? 38.732  -24.213 69.194  1.00 25.61  ?  214 LYS   D N   1 
ATOM   12787 C CA  . LYS   D 1 214 ? 38.170  -25.301 69.984  1.00 27.68  ?  214 LYS   D CA  1 
ATOM   12788 C C   . LYS   D 1 214 ? 39.262  -26.053 70.735  1.00 29.39  ?  214 LYS   D C   1 
ATOM   12789 O O   . LYS   D 1 214 ? 39.105  -26.369 71.921  1.00 28.82  ?  214 LYS   D O   1 
ATOM   12790 C CB  . LYS   D 1 214 ? 37.387  -26.243 69.069  1.00 28.20  ?  214 LYS   D CB  1 
ATOM   12791 C CG  . LYS   D 1 214 ? 36.321  -27.060 69.768  1.00 36.93  ?  214 LYS   D CG  1 
ATOM   12792 C CD  . LYS   D 1 214 ? 35.683  -28.056 68.802  1.00 40.71  ?  214 LYS   D CD  1 
ATOM   12793 C CE  . LYS   D 1 214 ? 34.571  -28.870 69.459  1.00 37.38  ?  214 LYS   D CE  1 
ATOM   12794 N NZ  . LYS   D 1 214 ? 33.981  -29.852 68.493  1.00 42.81  ?  214 LYS   D NZ  1 
ATOM   12795 N N   . GLN   D 1 215 ? 40.382  -26.333 70.059  1.00 32.56  ?  215 GLN   D N   1 
ATOM   12796 C CA  . GLN   D 1 215 ? 41.526  -26.981 70.700  1.00 30.47  ?  215 GLN   D CA  1 
ATOM   12797 C C   . GLN   D 1 215 ? 42.023  -26.195 71.908  1.00 30.99  ?  215 GLN   D C   1 
ATOM   12798 O O   . GLN   D 1 215 ? 42.476  -26.788 72.896  1.00 28.91  ?  215 GLN   D O   1 
ATOM   12799 C CB  . GLN   D 1 215 ? 42.656  -27.155 69.681  1.00 34.79  ?  215 GLN   D CB  1 
ATOM   12800 C CG  . GLN   D 1 215 ? 44.060  -27.197 70.291  1.00 37.14  ?  215 GLN   D CG  1 
ATOM   12801 C CD  . GLN   D 1 215 ? 45.154  -26.775 69.310  1.00 46.25  ?  215 GLN   D CD  1 
ATOM   12802 O OE1 . GLN   D 1 215 ? 44.868  -26.337 68.191  1.00 41.37  ?  215 GLN   D OE1 1 
ATOM   12803 N NE2 . GLN   D 1 215 ? 46.416  -26.906 69.733  1.00 45.67  ?  215 GLN   D NE2 1 
ATOM   12804 N N   . HIS   D 1 216 ? 41.956  -24.869 71.849  1.00 30.76  ?  216 HIS   D N   1 
ATOM   12805 C CA  . HIS   D 1 216 ? 42.380  -24.027 72.956  1.00 27.74  ?  216 HIS   D CA  1 
ATOM   12806 C C   . HIS   D 1 216 ? 41.235  -23.637 73.875  1.00 31.39  ?  216 HIS   D C   1 
ATOM   12807 O O   . HIS   D 1 216 ? 41.449  -22.851 74.804  1.00 31.06  ?  216 HIS   D O   1 
ATOM   12808 C CB  . HIS   D 1 216 ? 43.063  -22.767 72.425  1.00 27.27  ?  216 HIS   D CB  1 
ATOM   12809 C CG  . HIS   D 1 216 ? 44.368  -23.032 71.745  1.00 30.50  ?  216 HIS   D CG  1 
ATOM   12810 N ND1 . HIS   D 1 216 ? 44.462  -23.321 70.401  1.00 34.05  ?  216 HIS   D ND1 1 
ATOM   12811 C CD2 . HIS   D 1 216 ? 45.631  -23.070 72.227  1.00 30.29  ?  216 HIS   D CD2 1 
ATOM   12812 C CE1 . HIS   D 1 216 ? 45.728  -23.515 70.083  1.00 32.54  ?  216 HIS   D CE1 1 
ATOM   12813 N NE2 . HIS   D 1 216 ? 46.458  -23.366 71.172  1.00 36.44  ?  216 HIS   D NE2 1 
ATOM   12814 N N   . GLY   D 1 217 ? 40.033  -24.162 73.648  1.00 28.19  ?  217 GLY   D N   1 
ATOM   12815 C CA  . GLY   D 1 217 ? 38.894  -23.788 74.467  1.00 25.62  ?  217 GLY   D CA  1 
ATOM   12816 C C   . GLY   D 1 217 ? 38.495  -22.337 74.339  1.00 26.84  ?  217 GLY   D C   1 
ATOM   12817 O O   . GLY   D 1 217 ? 38.011  -21.749 75.310  1.00 29.30  ?  217 GLY   D O   1 
ATOM   12818 N N   . ILE   D 1 218 ? 38.693  -21.737 73.168  1.00 25.91  ?  218 ILE   D N   1 
ATOM   12819 C CA  . ILE   D 1 218 ? 38.335  -20.343 72.921  1.00 24.37  ?  218 ILE   D CA  1 
ATOM   12820 C C   . ILE   D 1 218 ? 36.962  -20.296 72.260  1.00 23.11  ?  218 ILE   D C   1 
ATOM   12821 O O   . ILE   D 1 218 ? 36.706  -21.009 71.279  1.00 22.15  ?  218 ILE   D O   1 
ATOM   12822 C CB  . ILE   D 1 218 ? 39.393  -19.646 72.048  1.00 23.98  ?  218 ILE   D CB  1 
ATOM   12823 C CG1 . ILE   D 1 218 ? 40.746  -19.643 72.756  1.00 22.46  ?  218 ILE   D CG1 1 
ATOM   12824 C CG2 . ILE   D 1 218 ? 38.967  -18.227 71.705  1.00 17.52  ?  218 ILE   D CG2 1 
ATOM   12825 C CD1 . ILE   D 1 218 ? 41.864  -19.082 71.912  1.00 24.07  ?  218 ILE   D CD1 1 
ATOM   12826 N N   . PHE   D 1 219 ? 36.082  -19.454 72.800  1.00 21.68  ?  219 PHE   D N   1 
ATOM   12827 C CA  . PHE   D 1 219 ? 34.742  -19.245 72.267  1.00 18.70  ?  219 PHE   D CA  1 
ATOM   12828 C C   . PHE   D 1 219 ? 34.823  -18.488 70.946  1.00 16.17  ?  219 PHE   D C   1 
ATOM   12829 O O   . PHE   D 1 219 ? 35.682  -17.625 70.766  1.00 18.29  ?  219 PHE   D O   1 
ATOM   12830 C CB  . PHE   D 1 219 ? 33.917  -18.461 73.293  1.00 15.41  ?  219 PHE   D CB  1 
ATOM   12831 C CG  . PHE   D 1 219 ? 32.428  -18.507 73.078  1.00 17.89  ?  219 PHE   D CG  1 
ATOM   12832 C CD1 . PHE   D 1 219 ? 31.792  -17.555 72.288  1.00 20.54  ?  219 PHE   D CD1 1 
ATOM   12833 C CD2 . PHE   D 1 219 ? 31.657  -19.451 73.720  1.00 17.86  ?  219 PHE   D CD2 1 
ATOM   12834 C CE1 . PHE   D 1 219 ? 30.427  -17.572 72.109  1.00 15.03  ?  219 PHE   D CE1 1 
ATOM   12835 C CE2 . PHE   D 1 219 ? 30.286  -19.476 73.549  1.00 20.12  ?  219 PHE   D CE2 1 
ATOM   12836 C CZ  . PHE   D 1 219 ? 29.669  -18.534 72.742  1.00 19.88  ?  219 PHE   D CZ  1 
ATOM   12837 N N   . VAL   D 1 220 ? 33.927  -18.813 70.014  1.00 17.28  ?  220 VAL   D N   1 
ATOM   12838 C CA  . VAL   D 1 220 ? 33.911  -18.185 68.691  1.00 17.78  ?  220 VAL   D CA  1 
ATOM   12839 C C   . VAL   D 1 220 ? 32.541  -17.574 68.429  1.00 19.91  ?  220 VAL   D C   1 
ATOM   12840 O O   . VAL   D 1 220 ? 31.525  -18.283 68.433  1.00 17.54  ?  220 VAL   D O   1 
ATOM   12841 C CB  . VAL   D 1 220 ? 34.256  -19.173 67.568  1.00 15.22  ?  220 VAL   D CB  1 
ATOM   12842 C CG1 . VAL   D 1 220 ? 34.393  -18.414 66.249  1.00 16.82  ?  220 VAL   D CG1 1 
ATOM   12843 C CG2 . VAL   D 1 220 ? 35.516  -19.960 67.888  1.00 16.71  ?  220 VAL   D CG2 1 
ATOM   12844 N N   . VAL   D 1 221 ? 32.522  -16.272 68.143  1.00 17.98  ?  221 VAL   D N   1 
ATOM   12845 C CA  . VAL   D 1 221 ? 31.311  -15.559 67.758  1.00 14.86  ?  221 VAL   D CA  1 
ATOM   12846 C C   . VAL   D 1 221 ? 31.402  -15.222 66.280  1.00 15.23  ?  221 VAL   D C   1 
ATOM   12847 O O   . VAL   D 1 221 ? 32.424  -14.708 65.812  1.00 17.25  ?  221 VAL   D O   1 
ATOM   12848 C CB  . VAL   D 1 221 ? 31.110  -14.279 68.583  1.00 15.91  ?  221 VAL   D CB  1 
ATOM   12849 C CG1 . VAL   D 1 221 ? 29.779  -13.624 68.208  1.00 12.78  ?  221 VAL   D CG1 1 
ATOM   12850 C CG2 . VAL   D 1 221 ? 31.161  -14.591 70.061  1.00 16.82  ?  221 VAL   D CG2 1 
ATOM   12851 N N   . MET   D 1 222 ? 30.335  -15.505 65.550  1.00 19.44  ?  222 MET   D N   1 
ATOM   12852 C CA  . MET   D 1 222 ? 30.220  -15.146 64.144  1.00 17.93  ?  222 MET   D CA  1 
ATOM   12853 C C   . MET   D 1 222 ? 29.493  -13.810 64.056  1.00 17.67  ?  222 MET   D C   1 
ATOM   12854 O O   . MET   D 1 222 ? 28.293  -13.732 64.333  1.00 18.49  ?  222 MET   D O   1 
ATOM   12855 C CB  . MET   D 1 222 ? 29.475  -16.233 63.374  1.00 14.97  ?  222 MET   D CB  1 
ATOM   12856 C CG  . MET   D 1 222 ? 29.562  -16.092 61.873  1.00 17.60  ?  222 MET   D CG  1 
ATOM   12857 S SD  . MET   D 1 222 ? 30.989  -16.992 61.265  1.00 24.92  ?  222 MET   D SD  1 
ATOM   12858 C CE  . MET   D 1 222 ? 30.272  -18.625 61.150  1.00 18.38  ?  222 MET   D CE  1 
ATOM   12859 N N   . ASP   D 1 223 ? 30.221  -12.757 63.699  1.00 16.42  ?  223 ASP   D N   1 
ATOM   12860 C CA  . ASP   D 1 223 ? 29.584  -11.498 63.334  1.00 14.01  ?  223 ASP   D CA  1 
ATOM   12861 C C   . ASP   D 1 223 ? 28.923  -11.696 61.981  1.00 17.94  ?  223 ASP   D C   1 
ATOM   12862 O O   . ASP   D 1 223 ? 29.610  -11.871 60.969  1.00 17.92  ?  223 ASP   D O   1 
ATOM   12863 C CB  . ASP   D 1 223 ? 30.620  -10.376 63.306  1.00 17.23  ?  223 ASP   D CB  1 
ATOM   12864 C CG  . ASP   D 1 223 ? 30.005  -9.000  63.086  1.00 18.48  ?  223 ASP   D CG  1 
ATOM   12865 O OD1 . ASP   D 1 223 ? 29.068  -8.859  62.260  1.00 21.62  ?  223 ASP   D OD1 1 
ATOM   12866 O OD2 . ASP   D 1 223 ? 30.472  -8.052  63.744  1.00 19.68  ?  223 ASP   D OD2 1 
ATOM   12867 N N   . SER   D 1 224 ? 27.587  -11.665 61.958  1.00 17.12  ?  224 SER   D N   1 
ATOM   12868 C CA  . SER   D 1 224 ? 26.802  -12.272 60.886  1.00 18.74  ?  224 SER   D CA  1 
ATOM   12869 C C   . SER   D 1 224 ? 25.970  -11.272 60.095  1.00 16.74  ?  224 SER   D C   1 
ATOM   12870 O O   . SER   D 1 224 ? 25.024  -11.681 59.417  1.00 18.91  ?  224 SER   D O   1 
ATOM   12871 C CB  . SER   D 1 224 ? 25.877  -13.345 61.462  1.00 13.83  ?  224 SER   D CB  1 
ATOM   12872 O OG  . SER   D 1 224 ? 26.612  -14.244 62.262  1.00 16.99  ?  224 SER   D OG  1 
ATOM   12873 N N   . ALA   D 1 225 ? 26.288  -9.976  60.173  1.00 17.13  ?  225 ALA   D N   1 
ATOM   12874 C CA  . ALA   D 1 225 ? 25.514  -8.973  59.441  1.00 14.88  ?  225 ALA   D CA  1 
ATOM   12875 C C   . ALA   D 1 225 ? 25.364  -9.332  57.971  1.00 20.56  ?  225 ALA   D C   1 
ATOM   12876 O O   . ALA   D 1 225 ? 24.279  -9.178  57.393  1.00 19.87  ?  225 ALA   D O   1 
ATOM   12877 C CB  . ALA   D 1 225 ? 26.172  -7.599  59.573  1.00 16.95  ?  225 ALA   D CB  1 
ATOM   12878 N N   . ARG   D 1 226 ? 26.435  -9.813  57.340  1.00 17.27  ?  226 ARG   D N   1 
ATOM   12879 C CA  . ARG   D 1 226 ? 26.334  -10.119 55.918  1.00 18.01  ?  226 ARG   D CA  1 
ATOM   12880 C C   . ARG   D 1 226 ? 26.661  -11.581 55.637  1.00 17.93  ?  226 ARG   D C   1 
ATOM   12881 O O   . ARG   D 1 226 ? 27.380  -11.898 54.683  1.00 19.24  ?  226 ARG   D O   1 
ATOM   12882 C CB  . ARG   D 1 226 ? 27.227  -9.169  55.127  1.00 16.52  ?  226 ARG   D CB  1 
ATOM   12883 C CG  . ARG   D 1 226 ? 26.782  -7.729  55.303  1.00 15.57  ?  226 ARG   D CG  1 
ATOM   12884 C CD  . ARG   D 1 226 ? 27.674  -6.753  54.577  1.00 19.77  ?  226 ARG   D CD  1 
ATOM   12885 N NE  . ARG   D 1 226 ? 27.355  -5.378  54.945  1.00 20.43  ?  226 ARG   D NE  1 
ATOM   12886 C CZ  . ARG   D 1 226 ? 27.856  -4.760  56.008  1.00 22.77  ?  226 ARG   D CZ  1 
ATOM   12887 N NH1 . ARG   D 1 226 ? 28.715  -5.362  56.818  1.00 17.33  ?  226 ARG   D NH1 1 
ATOM   12888 N NH2 . ARG   D 1 226 ? 27.482  -3.511  56.268  1.00 20.14  ?  226 ARG   D NH2 1 
ATOM   12889 N N   . PHE   D 1 227 ? 26.086  -12.478 56.446  1.00 16.54  ?  227 PHE   D N   1 
ATOM   12890 C CA  . PHE   D 1 227 ? 26.406  -13.900 56.355  1.00 16.45  ?  227 PHE   D CA  1 
ATOM   12891 C C   . PHE   D 1 227 ? 25.886  -14.531 55.072  1.00 18.69  ?  227 PHE   D C   1 
ATOM   12892 O O   . PHE   D 1 227 ? 26.431  -15.547 54.623  1.00 17.91  ?  227 PHE   D O   1 
ATOM   12893 C CB  . PHE   D 1 227 ? 25.852  -14.644 57.575  1.00 15.24  ?  227 PHE   D CB  1 
ATOM   12894 C CG  . PHE   D 1 227 ? 24.347  -14.830 57.568  1.00 17.97  ?  227 PHE   D CG  1 
ATOM   12895 C CD1 . PHE   D 1 227 ? 23.492  -13.747 57.743  1.00 20.43  ?  227 PHE   D CD1 1 
ATOM   12896 C CD2 . PHE   D 1 227 ? 23.792  -16.094 57.426  1.00 15.76  ?  227 PHE   D CD2 1 
ATOM   12897 C CE1 . PHE   D 1 227 ? 22.121  -13.918 57.750  1.00 19.68  ?  227 PHE   D CE1 1 
ATOM   12898 C CE2 . PHE   D 1 227 ? 22.424  -16.278 57.430  1.00 17.73  ?  227 PHE   D CE2 1 
ATOM   12899 C CZ  . PHE   D 1 227 ? 21.581  -15.191 57.594  1.00 21.01  ?  227 PHE   D CZ  1 
ATOM   12900 N N   . CYS   D 1 228 ? 24.821  -13.972 54.484  1.00 19.08  ?  228 CYS   D N   1 
ATOM   12901 C CA  . CYS   D 1 228 ? 24.291  -14.513 53.238  1.00 18.51  ?  228 CYS   D CA  1 
ATOM   12902 C C   . CYS   D 1 228 ? 25.152  -14.108 52.053  1.00 22.29  ?  228 CYS   D C   1 
ATOM   12903 O O   . CYS   D 1 228 ? 25.334  -14.892 51.113  1.00 23.99  ?  228 CYS   D O   1 
ATOM   12904 C CB  . CYS   D 1 228 ? 22.851  -14.049 53.028  1.00 17.66  ?  228 CYS   D CB  1 
ATOM   12905 S SG  . CYS   D 1 228 ? 21.660  -14.784 54.186  1.00 23.61  ?  228 CYS   D SG  1 
ATOM   12906 N N   . GLU   D 1 229 ? 25.692  -12.890 52.081  1.00 24.73  ?  229 GLU   D N   1 
ATOM   12907 C CA  . GLU   D 1 229 ? 26.628  -12.494 51.040  1.00 20.22  ?  229 GLU   D CA  1 
ATOM   12908 C C   . GLU   D 1 229 ? 27.919  -13.289 51.133  1.00 19.79  ?  229 GLU   D C   1 
ATOM   12909 O O   . GLU   D 1 229 ? 28.532  -13.581 50.102  1.00 23.94  ?  229 GLU   D O   1 
ATOM   12910 C CB  . GLU   D 1 229 ? 26.884  -10.993 51.116  1.00 18.51  ?  229 GLU   D CB  1 
ATOM   12911 C CG  . GLU   D 1 229 ? 25.647  -10.209 50.728  1.00 20.75  ?  229 GLU   D CG  1 
ATOM   12912 C CD  . GLU   D 1 229 ? 25.740  -8.733  51.039  1.00 22.93  ?  229 GLU   D CD  1 
ATOM   12913 O OE1 . GLU   D 1 229 ? 26.821  -8.278  51.476  1.00 24.66  ?  229 GLU   D OE1 1 
ATOM   12914 O OE2 . GLU   D 1 229 ? 24.718  -8.031  50.839  1.00 22.83  ?  229 GLU   D OE2 1 
ATOM   12915 N N   . ASN   D 1 230 ? 28.320  -13.688 52.342  1.00 21.47  ?  230 ASN   D N   1 
ATOM   12916 C CA  . ASN   D 1 230 ? 29.452  -14.603 52.471  1.00 22.03  ?  230 ASN   D CA  1 
ATOM   12917 C C   . ASN   D 1 230 ? 29.104  -15.989 51.933  1.00 24.38  ?  230 ASN   D C   1 
ATOM   12918 O O   . ASN   D 1 230 ? 29.901  -16.595 51.208  1.00 23.63  ?  230 ASN   D O   1 
ATOM   12919 C CB  . ASN   D 1 230 ? 29.907  -14.694 53.931  1.00 19.51  ?  230 ASN   D CB  1 
ATOM   12920 C CG  . ASN   D 1 230 ? 31.361  -15.134 54.059  1.00 22.44  ?  230 ASN   D CG  1 
ATOM   12921 O OD1 . ASN   D 1 230 ? 32.276  -14.312 53.998  1.00 21.30  ?  230 ASN   D OD1 1 
ATOM   12922 N ND2 . ASN   D 1 230 ? 31.580  -16.437 54.222  1.00 18.26  ?  230 ASN   D ND2 1 
ATOM   12923 N N   . ALA   D 1 231 ? 27.911  -16.502 52.267  1.00 21.62  ?  231 ALA   D N   1 
ATOM   12924 C CA  . ALA   D 1 231 ? 27.523  -17.834 51.810  1.00 21.41  ?  231 ALA   D CA  1 
ATOM   12925 C C   . ALA   D 1 231 ? 27.488  -17.910 50.292  1.00 24.72  ?  231 ALA   D C   1 
ATOM   12926 O O   . ALA   D 1 231 ? 27.865  -18.933 49.709  1.00 28.09  ?  231 ALA   D O   1 
ATOM   12927 C CB  . ALA   D 1 231 ? 26.164  -18.224 52.389  1.00 20.18  ?  231 ALA   D CB  1 
ATOM   12928 N N   . TYR   D 1 232 ? 27.028  -16.841 49.636  1.00 24.44  ?  232 TYR   D N   1 
ATOM   12929 C CA  . TYR   D 1 232 ? 26.983  -16.823 48.176  1.00 23.60  ?  232 TYR   D CA  1 
ATOM   12930 C C   . TYR   D 1 232 ? 28.378  -16.952 47.581  1.00 22.25  ?  232 TYR   D C   1 
ATOM   12931 O O   . TYR   D 1 232 ? 28.585  -17.701 46.620  1.00 25.70  ?  232 TYR   D O   1 
ATOM   12932 C CB  . TYR   D 1 232 ? 26.310  -15.536 47.684  1.00 23.08  ?  232 TYR   D CB  1 
ATOM   12933 C CG  . TYR   D 1 232 ? 26.228  -15.419 46.170  1.00 27.24  ?  232 TYR   D CG  1 
ATOM   12934 C CD1 . TYR   D 1 232 ? 27.271  -14.860 45.435  1.00 27.01  ?  232 TYR   D CD1 1 
ATOM   12935 C CD2 . TYR   D 1 232 ? 25.115  -15.874 45.481  1.00 24.21  ?  232 TYR   D CD2 1 
ATOM   12936 C CE1 . TYR   D 1 232 ? 27.204  -14.760 44.061  1.00 28.23  ?  232 TYR   D CE1 1 
ATOM   12937 C CE2 . TYR   D 1 232 ? 25.036  -15.775 44.106  1.00 24.84  ?  232 TYR   D CE2 1 
ATOM   12938 C CZ  . TYR   D 1 232 ? 26.080  -15.218 43.403  1.00 27.78  ?  232 TYR   D CZ  1 
ATOM   12939 O OH  . TYR   D 1 232 ? 26.006  -15.128 42.034  1.00 34.00  ?  232 TYR   D OH  1 
ATOM   12940 N N   . PHE   D 1 233 ? 29.347  -16.221 48.138  1.00 27.44  ?  233 PHE   D N   1 
ATOM   12941 C CA  . PHE   D 1 233 ? 30.709  -16.263 47.612  1.00 26.48  ?  233 PHE   D CA  1 
ATOM   12942 C C   . PHE   D 1 233 ? 31.322  -17.647 47.781  1.00 25.06  ?  233 PHE   D C   1 
ATOM   12943 O O   . PHE   D 1 233 ? 32.049  -18.123 46.905  1.00 22.98  ?  233 PHE   D O   1 
ATOM   12944 C CB  . PHE   D 1 233 ? 31.576  -15.210 48.307  1.00 24.42  ?  233 PHE   D CB  1 
ATOM   12945 C CG  . PHE   D 1 233 ? 31.376  -13.813 47.788  1.00 24.44  ?  233 PHE   D CG  1 
ATOM   12946 C CD1 . PHE   D 1 233 ? 31.596  -13.518 46.456  1.00 24.59  ?  233 PHE   D CD1 1 
ATOM   12947 C CD2 . PHE   D 1 233 ? 30.989  -12.791 48.640  1.00 25.46  ?  233 PHE   D CD2 1 
ATOM   12948 C CE1 . PHE   D 1 233 ? 31.416  -12.225 45.974  1.00 28.49  ?  233 PHE   D CE1 1 
ATOM   12949 C CE2 . PHE   D 1 233 ? 30.804  -11.496 48.167  1.00 26.68  ?  233 PHE   D CE2 1 
ATOM   12950 C CZ  . PHE   D 1 233 ? 31.017  -11.214 46.833  1.00 25.11  ?  233 PHE   D CZ  1 
ATOM   12951 N N   . ILE   D 1 234 ? 31.045  -18.304 48.906  1.00 24.93  ?  234 ILE   D N   1 
ATOM   12952 C CA  . ILE   D 1 234 ? 31.516  -19.671 49.100  1.00 25.79  ?  234 ILE   D CA  1 
ATOM   12953 C C   . ILE   D 1 234 ? 30.939  -20.585 48.025  1.00 30.69  ?  234 ILE   D C   1 
ATOM   12954 O O   . ILE   D 1 234 ? 31.655  -21.394 47.426  1.00 30.83  ?  234 ILE   D O   1 
ATOM   12955 C CB  . ILE   D 1 234 ? 31.164  -20.164 50.513  1.00 27.74  ?  234 ILE   D CB  1 
ATOM   12956 C CG1 . ILE   D 1 234 ? 32.067  -19.481 51.550  1.00 21.33  ?  234 ILE   D CG1 1 
ATOM   12957 C CG2 . ILE   D 1 234 ? 31.264  -21.682 50.579  1.00 26.26  ?  234 ILE   D CG2 1 
ATOM   12958 C CD1 . ILE   D 1 234 ? 31.627  -19.689 52.988  1.00 21.59  ?  234 ILE   D CD1 1 
ATOM   12959 N N   . LYS   D 1 235 ? 29.649  -20.450 47.744  1.00 25.59  ?  235 LYS   D N   1 
ATOM   12960 C CA  . LYS   D 1 235 ? 29.048  -21.271 46.662  1.00 29.36  ?  235 LYS   D CA  1 
ATOM   12961 C C   . LYS   D 1 235 ? 29.657  -20.917 45.300  1.00 30.09  ?  235 LYS   D C   1 
ATOM   12962 O O   . LYS   D 1 235 ? 29.783  -21.810 44.461  1.00 30.16  ?  235 LYS   D O   1 
ATOM   12963 C CB  . LYS   D 1 235 ? 27.539  -21.064 46.564  1.00 30.89  ?  235 LYS   D CB  1 
ATOM   12964 C CG  . LYS   D 1 235 ? 26.767  -22.181 45.903  1.00 31.96  ?  235 LYS   D CG  1 
ATOM   12965 C CD  . LYS   D 1 235 ? 25.404  -21.747 45.390  1.00 27.17  ?  235 LYS   D CD  1 
ATOM   12966 C CE  . LYS   D 1 235 ? 25.078  -22.484 44.140  1.00 35.56  ?  235 LYS   D CE  1 
ATOM   12967 N NZ  . LYS   D 1 235 ? 24.687  -23.866 44.404  1.00 40.85  ?  235 LYS   D NZ  1 
ATOM   12968 N N   . ALA   D 1 236 ? 30.010  -19.662 45.098  1.00 31.24  ?  236 ALA   D N   1 
ATOM   12969 C CA  . ALA   D 1 236 ? 30.493  -19.233 43.772  1.00 29.55  ?  236 ALA   D CA  1 
ATOM   12970 C C   . ALA   D 1 236 ? 31.980  -19.526 43.572  1.00 32.91  ?  236 ALA   D C   1 
ATOM   12971 O O   . ALA   D 1 236 ? 32.401  -19.619 42.416  1.00 30.36  ?  236 ALA   D O   1 
ATOM   12972 C CB  . ALA   D 1 236 ? 30.223  -17.767 43.603  1.00 30.70  ?  236 ALA   D CB  1 
ATOM   12973 N N   . ARG   D 1 237 ? 32.748  -19.646 44.655  1.00 31.54  ?  237 ARG   D N   1 
ATOM   12974 C CA  . ARG   D 1 237 ? 34.221  -19.764 44.508  1.00 32.84  ?  237 ARG   D CA  1 
ATOM   12975 C C   . ARG   D 1 237 ? 34.785  -21.073 45.090  1.00 31.00  ?  237 ARG   D C   1 
ATOM   12976 O O   . ARG   D 1 237 ? 35.940  -21.376 44.810  1.00 31.80  ?  237 ARG   D O   1 
ATOM   12977 C CB  . ARG   D 1 237 ? 34.755  -18.494 45.172  1.00 28.89  ?  237 ARG   D CB  1 
ATOM   12978 C CG  . ARG   D 1 237 ? 34.287  -17.188 44.555  1.00 23.43  ?  237 ARG   D CG  1 
ATOM   12979 C CD  . ARG   D 1 237 ? 35.029  -16.015 45.148  1.00 23.96  ?  237 ARG   D CD  1 
ATOM   12980 N NE  . ARG   D 1 237 ? 34.569  -14.742 44.592  1.00 22.49  ?  237 ARG   D NE  1 
ATOM   12981 C CZ  . ARG   D 1 237 ? 34.871  -13.570 45.117  1.00 28.63  ?  237 ARG   D CZ  1 
ATOM   12982 N NH1 . ARG   D 1 237 ? 35.581  -13.513 46.228  1.00 20.06  ?  237 ARG   D NH1 1 
ATOM   12983 N NH2 . ARG   D 1 237 ? 34.459  -12.462 44.535  1.00 26.74  ?  237 ARG   D NH2 1 
ATOM   12984 N N   . ASP   D 1 238 ? 33.998  -21.795 45.876  1.00 31.52  ?  238 ASP   D N   1 
ATOM   12985 C CA  . ASP   D 1 238 ? 34.470  -23.055 46.500  1.00 32.25  ?  238 ASP   D CA  1 
ATOM   12986 C C   . ASP   D 1 238 ? 33.840  -24.239 45.768  1.00 34.76  ?  238 ASP   D C   1 
ATOM   12987 O O   . ASP   D 1 238 ? 32.657  -24.519 45.968  1.00 27.38  ?  238 ASP   D O   1 
ATOM   12988 C CB  . ASP   D 1 238 ? 34.233  -23.107 47.998  1.00 31.21  ?  238 ASP   D CB  1 
ATOM   12989 C CG  . ASP   D 1 238 ? 34.901  -24.256 48.740  1.00 36.55  ?  238 ASP   D CG  1 
ATOM   12990 O OD1 . ASP   D 1 238 ? 35.003  -25.357 48.165  1.00 37.89  ?  238 ASP   D OD1 1 
ATOM   12991 O OD2 . ASP   D 1 238 ? 35.305  -24.045 49.897  1.00 33.72  ?  238 ASP   D OD2 1 
ATOM   12992 N N   . PRO   D 1 239 ? 34.652  -24.978 44.985  1.00 32.19  ?  239 PRO   D N   1 
ATOM   12993 C CA  . PRO   D 1 239 ? 34.145  -26.107 44.225  1.00 32.97  ?  239 PRO   D CA  1 
ATOM   12994 C C   . PRO   D 1 239 ? 33.349  -27.121 45.022  1.00 35.27  ?  239 PRO   D C   1 
ATOM   12995 O O   . PRO   D 1 239 ? 32.409  -27.708 44.478  1.00 33.42  ?  239 PRO   D O   1 
ATOM   12996 C CB  . PRO   D 1 239 ? 35.473  -26.708 43.697  1.00 36.30  ?  239 PRO   D CB  1 
ATOM   12997 C CG  . PRO   D 1 239 ? 36.404  -25.531 43.590  1.00 30.34  ?  239 PRO   D CG  1 
ATOM   12998 C CD  . PRO   D 1 239 ? 36.076  -24.746 44.836  1.00 34.16  ?  239 PRO   D CD  1 
ATOM   12999 N N   . LYS   D 1 240 ? 33.706  -27.329 46.290  1.00 33.17  ?  240 LYS   D N   1 
ATOM   13000 C CA  . LYS   D 1 240 ? 32.990  -28.303 47.143  1.00 31.01  ?  240 LYS   D CA  1 
ATOM   13001 C C   . LYS   D 1 240 ? 31.533  -27.858 47.328  1.00 33.38  ?  240 LYS   D C   1 
ATOM   13002 O O   . LYS   D 1 240 ? 30.717  -28.686 47.757  1.00 31.66  ?  240 LYS   D O   1 
ATOM   13003 C CB  . LYS   D 1 240 ? 33.644  -28.381 48.524  1.00 34.67  ?  240 LYS   D CB  1 
ATOM   13004 C CG  . LYS   D 1 240 ? 33.136  -29.440 49.484  1.00 38.92  ?  240 LYS   D CG  1 
ATOM   13005 C CD  . LYS   D 1 240 ? 33.539  -29.181 50.930  1.00 43.70  ?  240 LYS   D CD  1 
ATOM   13006 C CE  . LYS   D 1 240 ? 33.013  -30.224 51.860  1.00 42.79  ?  240 LYS   D CE  1 
ATOM   13007 N NZ  . LYS   D 1 240 ? 33.866  -30.382 53.038  1.00 51.25  ?  240 LYS   D NZ  1 
ATOM   13008 N N   . TYR   D 1 241 ? 31.230  -26.607 46.987  1.00 30.81  ?  241 TYR   D N   1 
ATOM   13009 C CA  . TYR   D 1 241 ? 29.879  -26.074 47.299  1.00 34.38  ?  241 TYR   D CA  1 
ATOM   13010 C C   . TYR   D 1 241 ? 29.174  -25.509 46.072  1.00 35.83  ?  241 TYR   D C   1 
ATOM   13011 O O   . TYR   D 1 241 ? 28.068  -24.996 46.244  1.00 33.60  ?  241 TYR   D O   1 
ATOM   13012 C CB  . TYR   D 1 241 ? 30.076  -24.992 48.360  1.00 28.76  ?  241 TYR   D CB  1 
ATOM   13013 C CG  . TYR   D 1 241 ? 30.348  -25.506 49.765  1.00 29.30  ?  241 TYR   D CG  1 
ATOM   13014 C CD1 . TYR   D 1 241 ? 29.335  -26.061 50.531  1.00 30.01  ?  241 TYR   D CD1 1 
ATOM   13015 C CD2 . TYR   D 1 241 ? 31.615  -25.430 50.325  1.00 30.29  ?  241 TYR   D CD2 1 
ATOM   13016 C CE1 . TYR   D 1 241 ? 29.572  -26.531 51.810  1.00 26.37  ?  241 TYR   D CE1 1 
ATOM   13017 C CE2 . TYR   D 1 241 ? 31.866  -25.901 51.601  1.00 27.51  ?  241 TYR   D CE2 1 
ATOM   13018 C CZ  . TYR   D 1 241 ? 30.843  -26.453 52.346  1.00 28.18  ?  241 TYR   D CZ  1 
ATOM   13019 O OH  . TYR   D 1 241 ? 31.079  -26.914 53.605  1.00 27.15  ?  241 TYR   D OH  1 
ATOM   13020 N N   . LYS   D 1 242 ? 29.784  -25.609 44.890  1.00 36.23  ?  242 LYS   D N   1 
ATOM   13021 C CA  . LYS   D 1 242 ? 29.158  -25.096 43.641  1.00 36.44  ?  242 LYS   D CA  1 
ATOM   13022 C C   . LYS   D 1 242 ? 27.779  -25.756 43.425  1.00 33.86  ?  242 LYS   D C   1 
ATOM   13023 O O   . LYS   D 1 242 ? 26.942  -25.134 42.766  1.00 36.79  ?  242 LYS   D O   1 
ATOM   13024 C CB  . LYS   D 1 242 ? 30.079  -25.299 42.433  1.00 43.34  ?  242 LYS   D CB  1 
ATOM   13025 C CG  . LYS   D 1 242 ? 30.030  -24.184 41.402  1.00 47.79  ?  242 LYS   D CG  1 
ATOM   13026 C CD  . LYS   D 1 242 ? 30.966  -24.397 40.219  1.00 52.79  ?  242 LYS   D CD  1 
ATOM   13027 C CE  . LYS   D 1 242 ? 30.950  -25.801 39.704  1.00 55.68  ?  242 LYS   D CE  1 
ATOM   13028 N NZ  . LYS   D 1 242 ? 31.635  -25.905 38.413  1.00 58.78  ?  242 LYS   D NZ  1 
ATOM   13029 N N   . ASN   D 1 243 ? 27.556  -26.941 43.978  1.00 31.58  ?  243 ASN   D N   1 
ATOM   13030 C CA  . ASN   D 1 243 ? 26.286  -27.679 43.794  1.00 32.82  ?  243 ASN   D CA  1 
ATOM   13031 C C   . ASN   D 1 243 ? 25.384  -27.579 45.017  1.00 37.63  ?  243 ASN   D C   1 
ATOM   13032 O O   . ASN   D 1 243 ? 24.361  -28.272 45.050  1.00 39.22  ?  243 ASN   D O   1 
ATOM   13033 C CB  . ASN   D 1 243 ? 26.540  -29.173 43.721  1.00 46.10  ?  243 ASN   D CB  1 
ATOM   13034 C CG  . ASN   D 1 243 ? 25.563  -29.881 42.812  1.00 55.20  ?  243 ASN   D CG  1 
ATOM   13035 O OD1 . ASN   D 1 243 ? 25.563  -29.656 41.598  1.00 56.47  ?  243 ASN   D OD1 1 
ATOM   13036 N ND2 . ASN   D 1 243 ? 24.719  -30.729 43.378  1.00 54.09  ?  243 ASN   D ND2 1 
ATOM   13037 N N   . ALA   D 1 244 ? 25.773  -26.787 46.007  1.00 36.19  ?  244 ALA   D N   1 
ATOM   13038 C CA  . ALA   D 1 244 ? 24.991  -26.761 47.258  1.00 35.30  ?  244 ALA   D CA  1 
ATOM   13039 C C   . ALA   D 1 244 ? 24.060  -25.551 47.307  1.00 35.92  ?  244 ALA   D C   1 
ATOM   13040 O O   . ALA   D 1 244 ? 24.357  -24.533 46.695  1.00 34.40  ?  244 ALA   D O   1 
ATOM   13041 C CB  . ALA   D 1 244 ? 25.914  -26.789 48.446  1.00 34.75  ?  244 ALA   D CB  1 
ATOM   13042 N N   . THR   D 1 245 ? 22.964  -25.691 48.040  1.00 32.35  ?  245 THR   D N   1 
ATOM   13043 C CA  . THR   D 1 245 ? 22.040  -24.564 48.237  1.00 30.48  ?  245 THR   D CA  1 
ATOM   13044 C C   . THR   D 1 245 ? 22.684  -23.584 49.172  1.00 31.00  ?  245 THR   D C   1 
ATOM   13045 O O   . THR   D 1 245 ? 23.593  -23.957 49.918  1.00 28.02  ?  245 THR   D O   1 
ATOM   13046 C CB  . THR   D 1 245 ? 20.710  -25.030 48.825  1.00 36.09  ?  245 THR   D CB  1 
ATOM   13047 O OG1 . THR   D 1 245 ? 20.899  -25.439 50.173  1.00 28.52  ?  245 THR   D OG1 1 
ATOM   13048 C CG2 . THR   D 1 245 ? 20.091  -26.150 48.007  1.00 35.55  ?  245 THR   D CG2 1 
ATOM   13049 N N   . ILE   D 1 246 ? 22.188  -22.368 49.133  1.00 25.70  ?  246 ILE   D N   1 
ATOM   13050 C CA  . ILE   D 1 246 ? 22.729  -21.357 50.032  1.00 27.99  ?  246 ILE   D CA  1 
ATOM   13051 C C   . ILE   D 1 246 ? 22.472  -21.741 51.484  1.00 25.23  ?  246 ILE   D C   1 
ATOM   13052 O O   . ILE   D 1 246 ? 23.338  -21.563 52.348  1.00 24.62  ?  246 ILE   D O   1 
ATOM   13053 C CB  . ILE   D 1 246 ? 22.151  -19.975 49.689  1.00 28.70  ?  246 ILE   D CB  1 
ATOM   13054 C CG1 . ILE   D 1 246 ? 22.609  -19.556 48.290  1.00 25.82  ?  246 ILE   D CG1 1 
ATOM   13055 C CG2 . ILE   D 1 246 ? 22.568  -18.943 50.736  1.00 23.79  ?  246 ILE   D CG2 1 
ATOM   13056 C CD1 . ILE   D 1 246 ? 24.094  -19.317 48.194  1.00 24.21  ?  246 ILE   D CD1 1 
ATOM   13057 N N   . LYS   D 1 247 ? 21.294  -22.298 51.776  1.00 23.43  ?  247 LYS   D N   1 
ATOM   13058 C CA  . LYS   D 1 247 ? 21.018  -22.734 53.141  1.00 27.33  ?  247 LYS   D CA  1 
ATOM   13059 C C   . LYS   D 1 247 ? 21.994  -23.813 53.590  1.00 27.97  ?  247 LYS   D C   1 
ATOM   13060 O O   . LYS   D 1 247 ? 22.370  -23.857 54.768  1.00 28.33  ?  247 LYS   D O   1 
ATOM   13061 C CB  . LYS   D 1 247 ? 19.575  -23.225 53.255  1.00 27.09  ?  247 LYS   D CB  1 
ATOM   13062 C CG  . LYS   D 1 247 ? 18.566  -22.093 53.271  1.00 24.07  ?  247 LYS   D CG  1 
ATOM   13063 C CD  . LYS   D 1 247 ? 17.152  -22.615 53.417  1.00 31.81  ?  247 LYS   D CD  1 
ATOM   13064 C CE  . LYS   D 1 247 ? 16.175  -21.484 53.672  1.00 29.91  ?  247 LYS   D CE  1 
ATOM   13065 N NZ  . LYS   D 1 247 ? 14.768  -21.975 53.629  1.00 32.00  ?  247 LYS   D NZ  1 
ATOM   13066 N N   . GLU   D 1 248 ? 22.428  -24.673 52.667  1.00 26.47  ?  248 GLU   D N   1 
ATOM   13067 C CA  . GLU   D 1 248 ? 23.425  -25.683 52.999  1.00 25.68  ?  248 GLU   D CA  1 
ATOM   13068 C C   . GLU   D 1 248 ? 24.762  -25.045 53.343  1.00 27.79  ?  248 GLU   D C   1 
ATOM   13069 O O   . GLU   D 1 248 ? 25.446  -25.488 54.273  1.00 27.95  ?  248 GLU   D O   1 
ATOM   13070 C CB  . GLU   D 1 248 ? 23.596  -26.653 51.835  1.00 36.24  ?  248 GLU   D CB  1 
ATOM   13071 C CG  . GLU   D 1 248 ? 22.414  -27.568 51.592  1.00 42.35  ?  248 GLU   D CG  1 
ATOM   13072 C CD  . GLU   D 1 248 ? 22.541  -28.303 50.274  1.00 46.07  ?  248 GLU   D CD  1 
ATOM   13073 O OE1 . GLU   D 1 248 ? 22.783  -27.621 49.257  1.00 40.78  ?  248 GLU   D OE1 1 
ATOM   13074 O OE2 . GLU   D 1 248 ? 22.426  -29.552 50.257  1.00 45.71  ?  248 GLU   D OE2 1 
ATOM   13075 N N   . VAL   D 1 249 ? 25.157  -24.013 52.591  1.00 25.77  ?  249 VAL   D N   1 
ATOM   13076 C CA  . VAL   D 1 249 ? 26.396  -23.301 52.892  1.00 24.68  ?  249 VAL   D CA  1 
ATOM   13077 C C   . VAL   D 1 249 ? 26.306  -22.618 54.253  1.00 22.26  ?  249 VAL   D C   1 
ATOM   13078 O O   . VAL   D 1 249 ? 27.259  -22.643 55.042  1.00 23.57  ?  249 VAL   D O   1 
ATOM   13079 C CB  . VAL   D 1 249 ? 26.713  -22.293 51.775  1.00 24.06  ?  249 VAL   D CB  1 
ATOM   13080 C CG1 . VAL   D 1 249 ? 27.961  -21.507 52.122  1.00 26.26  ?  249 VAL   D CG1 1 
ATOM   13081 C CG2 . VAL   D 1 249 ? 26.874  -23.006 50.452  1.00 25.93  ?  249 VAL   D CG2 1 
ATOM   13082 N N   . ILE   D 1 250 ? 25.161  -22.001 54.551  1.00 20.83  ?  250 ILE   D N   1 
ATOM   13083 C CA  . ILE   D 1 250 ? 24.987  -21.331 55.840  1.00 21.28  ?  250 ILE   D CA  1 
ATOM   13084 C C   . ILE   D 1 250 ? 25.072  -22.336 56.980  1.00 21.84  ?  250 ILE   D C   1 
ATOM   13085 O O   . ILE   D 1 250 ? 25.775  -22.118 57.976  1.00 21.44  ?  250 ILE   D O   1 
ATOM   13086 C CB  . ILE   D 1 250 ? 23.653  -20.565 55.872  1.00 22.24  ?  250 ILE   D CB  1 
ATOM   13087 C CG1 . ILE   D 1 250 ? 23.662  -19.433 54.845  1.00 23.06  ?  250 ILE   D CG1 1 
ATOM   13088 C CG2 . ILE   D 1 250 ? 23.379  -20.019 57.265  1.00 18.91  ?  250 ILE   D CG2 1 
ATOM   13089 C CD1 . ILE   D 1 250 ? 22.358  -18.691 54.765  1.00 21.37  ?  250 ILE   D CD1 1 
ATOM   13090 N N   . PHE   D 1 251 ? 24.354  -23.455 56.848  1.00 23.21  ?  251 PHE   D N   1 
ATOM   13091 C CA  . PHE   D 1 251 ? 24.325  -24.462 57.903  1.00 22.77  ?  251 PHE   D CA  1 
ATOM   13092 C C   . PHE   D 1 251 ? 25.728  -24.951 58.247  1.00 24.80  ?  251 PHE   D C   1 
ATOM   13093 O O   . PHE   D 1 251 ? 26.054  -25.143 59.427  1.00 24.57  ?  251 PHE   D O   1 
ATOM   13094 C CB  . PHE   D 1 251 ? 23.430  -25.624 57.473  1.00 23.34  ?  251 PHE   D CB  1 
ATOM   13095 C CG  . PHE   D 1 251 ? 22.965  -26.488 58.610  1.00 29.43  ?  251 PHE   D CG  1 
ATOM   13096 C CD1 . PHE   D 1 251 ? 21.852  -26.132 59.358  1.00 31.44  ?  251 PHE   D CD1 1 
ATOM   13097 C CD2 . PHE   D 1 251 ? 23.634  -27.658 58.930  1.00 32.16  ?  251 PHE   D CD2 1 
ATOM   13098 C CE1 . PHE   D 1 251 ? 21.416  -26.928 60.397  1.00 30.51  ?  251 PHE   D CE1 1 
ATOM   13099 C CE2 . PHE   D 1 251 ? 23.206  -28.459 59.967  1.00 34.47  ?  251 PHE   D CE2 1 
ATOM   13100 C CZ  . PHE   D 1 251 ? 22.099  -28.093 60.705  1.00 34.30  ?  251 PHE   D CZ  1 
ATOM   13101 N N   . ASP   D 1 252 ? 26.579  -25.145 57.229  1.00 23.79  ?  252 ASP   D N   1 
ATOM   13102 C CA  . ASP   D 1 252 ? 27.970  -25.530 57.468  1.00 22.69  ?  252 ASP   D CA  1 
ATOM   13103 C C   . ASP   D 1 252 ? 28.771  -24.400 58.107  1.00 19.10  ?  252 ASP   D C   1 
ATOM   13104 O O   . ASP   D 1 252 ? 29.564  -24.646 59.024  1.00 21.34  ?  252 ASP   D O   1 
ATOM   13105 C CB  . ASP   D 1 252 ? 28.642  -25.961 56.161  1.00 26.64  ?  252 ASP   D CB  1 
ATOM   13106 C CG  . ASP   D 1 252 ? 28.245  -27.352 55.728  1.00 27.55  ?  252 ASP   D CG  1 
ATOM   13107 O OD1 . ASP   D 1 252 ? 27.494  -28.014 56.474  1.00 28.29  ?  252 ASP   D OD1 1 
ATOM   13108 O OD2 . ASP   D 1 252 ? 28.687  -27.784 54.638  1.00 34.92  ?  252 ASP   D OD2 1 
ATOM   13109 N N   . MET   D 1 253 ? 28.605  -23.163 57.617  1.00 22.42  ?  253 MET   D N   1 
ATOM   13110 C CA  . MET   D 1 253 ? 29.325  -22.020 58.188  1.00 20.38  ?  253 MET   D CA  1 
ATOM   13111 C C   . MET   D 1 253 ? 29.184  -21.967 59.702  1.00 21.35  ?  253 MET   D C   1 
ATOM   13112 O O   . MET   D 1 253 ? 30.145  -21.672 60.419  1.00 21.43  ?  253 MET   D O   1 
ATOM   13113 C CB  . MET   D 1 253 ? 28.814  -20.706 57.593  1.00 19.59  ?  253 MET   D CB  1 
ATOM   13114 C CG  . MET   D 1 253 ? 29.468  -20.261 56.300  1.00 23.15  ?  253 MET   D CG  1 
ATOM   13115 S SD  . MET   D 1 253 ? 28.564  -18.913 55.503  1.00 21.02  ?  253 MET   D SD  1 
ATOM   13116 C CE  . MET   D 1 253 ? 28.764  -17.588 56.703  1.00 18.86  ?  253 MET   D CE  1 
ATOM   13117 N N   . TYR   D 1 254 ? 27.999  -22.256 60.210  1.00 20.21  ?  254 TYR   D N   1 
ATOM   13118 C CA  . TYR   D 1 254 ? 27.731  -22.056 61.623  1.00 18.55  ?  254 TYR   D CA  1 
ATOM   13119 C C   . TYR   D 1 254 ? 28.043  -23.279 62.460  1.00 20.11  ?  254 TYR   D C   1 
ATOM   13120 O O   . TYR   D 1 254 ? 27.841  -23.248 63.677  1.00 21.10  ?  254 TYR   D O   1 
ATOM   13121 C CB  . TYR   D 1 254 ? 26.284  -21.590 61.803  1.00 19.90  ?  254 TYR   D CB  1 
ATOM   13122 C CG  . TYR   D 1 254 ? 26.200  -20.147 61.392  1.00 19.03  ?  254 TYR   D CG  1 
ATOM   13123 C CD1 . TYR   D 1 254 ? 26.124  -19.791 60.050  1.00 18.16  ?  254 TYR   D CD1 1 
ATOM   13124 C CD2 . TYR   D 1 254 ? 26.303  -19.137 62.336  1.00 18.70  ?  254 TYR   D CD2 1 
ATOM   13125 C CE1 . TYR   D 1 254 ? 26.110  -18.470 59.659  1.00 16.02  ?  254 TYR   D CE1 1 
ATOM   13126 C CE2 . TYR   D 1 254 ? 26.286  -17.809 61.954  1.00 16.88  ?  254 TYR   D CE2 1 
ATOM   13127 C CZ  . TYR   D 1 254 ? 26.186  -17.485 60.619  1.00 19.99  ?  254 TYR   D CZ  1 
ATOM   13128 O OH  . TYR   D 1 254 ? 26.166  -16.166 60.253  1.00 19.43  ?  254 TYR   D OH  1 
ATOM   13129 N N   . LYS   D 1 255 ? 28.551  -24.345 61.841  1.00 21.23  ?  255 LYS   D N   1 
ATOM   13130 C CA  . LYS   D 1 255 ? 29.263  -25.362 62.603  1.00 24.55  ?  255 LYS   D CA  1 
ATOM   13131 C C   . LYS   D 1 255 ? 30.565  -24.821 63.170  1.00 21.99  ?  255 LYS   D C   1 
ATOM   13132 O O   . LYS   D 1 255 ? 31.127  -25.422 64.090  1.00 22.55  ?  255 LYS   D O   1 
ATOM   13133 C CB  . LYS   D 1 255 ? 29.564  -26.575 61.725  1.00 20.86  ?  255 LYS   D CB  1 
ATOM   13134 C CG  . LYS   D 1 255 ? 28.353  -27.204 61.072  1.00 20.86  ?  255 LYS   D CG  1 
ATOM   13135 C CD  . LYS   D 1 255 ? 28.787  -28.193 59.998  1.00 30.77  ?  255 LYS   D CD  1 
ATOM   13136 C CE  . LYS   D 1 255 ? 27.658  -29.125 59.587  1.00 29.83  ?  255 LYS   D CE  1 
ATOM   13137 N NZ  . LYS   D 1 255 ? 27.223  -29.984 60.729  1.00 37.71  ?  255 LYS   D NZ  1 
ATOM   13138 N N   . TYR   D 1 256 ? 31.046  -23.693 62.652  1.00 20.33  ?  256 TYR   D N   1 
ATOM   13139 C CA  . TYR   D 1 256 ? 32.354  -23.155 62.992  1.00 19.71  ?  256 TYR   D CA  1 
ATOM   13140 C C   . TYR   D 1 256 ? 32.241  -21.892 63.835  1.00 21.47  ?  256 TYR   D C   1 
ATOM   13141 O O   . TYR   D 1 256 ? 33.083  -20.995 63.747  1.00 19.56  ?  256 TYR   D O   1 
ATOM   13142 C CB  . TYR   D 1 256 ? 33.144  -22.915 61.709  1.00 23.35  ?  256 TYR   D CB  1 
ATOM   13143 C CG  . TYR   D 1 256 ? 33.151  -24.166 60.860  1.00 25.71  ?  256 TYR   D CG  1 
ATOM   13144 C CD1 . TYR   D 1 256 ? 33.460  -25.401 61.428  1.00 25.54  ?  256 TYR   D CD1 1 
ATOM   13145 C CD2 . TYR   D 1 256 ? 32.795  -24.133 59.521  1.00 25.13  ?  256 TYR   D CD2 1 
ATOM   13146 C CE1 . TYR   D 1 256 ? 33.442  -26.560 60.677  1.00 26.52  ?  256 TYR   D CE1 1 
ATOM   13147 C CE2 . TYR   D 1 256 ? 32.777  -25.293 58.760  1.00 29.49  ?  256 TYR   D CE2 1 
ATOM   13148 C CZ  . TYR   D 1 256 ? 33.101  -26.503 59.349  1.00 27.82  ?  256 TYR   D CZ  1 
ATOM   13149 O OH  . TYR   D 1 256 ? 33.087  -27.664 58.607  1.00 35.16  ?  256 TYR   D OH  1 
ATOM   13150 N N   . ALA   D 1 257 ? 31.188  -21.818 64.648  1.00 16.28  ?  257 ALA   D N   1 
ATOM   13151 C CA  . ALA   D 1 257 ? 31.012  -20.772 65.635  1.00 15.00  ?  257 ALA   D CA  1 
ATOM   13152 C C   . ALA   D 1 257 ? 30.204  -21.355 66.785  1.00 19.96  ?  257 ALA   D C   1 
ATOM   13153 O O   . ALA   D 1 257 ? 29.539  -22.383 66.640  1.00 19.44  ?  257 ALA   D O   1 
ATOM   13154 C CB  . ALA   D 1 257 ? 30.327  -19.537 65.044  1.00 17.05  ?  257 ALA   D CB  1 
ATOM   13155 N N   . ASP   D 1 258 ? 30.288  -20.697 67.940  1.00 17.90  ?  258 ASP   D N   1 
ATOM   13156 C CA  . ASP   D 1 258 ? 29.551  -21.093 69.132  1.00 17.14  ?  258 ASP   D CA  1 
ATOM   13157 C C   . ASP   D 1 258 ? 28.334  -20.228 69.373  1.00 19.32  ?  258 ASP   D C   1 
ATOM   13158 O O   . ASP   D 1 258 ? 27.473  -20.600 70.183  1.00 19.82  ?  258 ASP   D O   1 
ATOM   13159 C CB  . ASP   D 1 258 ? 30.453  -21.015 70.358  1.00 18.55  ?  258 ASP   D CB  1 
ATOM   13160 C CG  . ASP   D 1 258 ? 31.683  -21.868 70.212  1.00 19.72  ?  258 ASP   D CG  1 
ATOM   13161 O OD1 . ASP   D 1 258 ? 31.510  -23.078 69.950  1.00 23.80  ?  258 ASP   D OD1 1 
ATOM   13162 O OD2 . ASP   D 1 258 ? 32.808  -21.327 70.319  1.00 18.09  ?  258 ASP   D OD2 1 
ATOM   13163 N N   . ALA   D 1 259 ? 28.267  -19.084 68.699  1.00 18.55  ?  259 ALA   D N   1 
ATOM   13164 C CA  . ALA   D 1 259 ? 27.226  -18.080 68.856  1.00 16.44  ?  259 ALA   D CA  1 
ATOM   13165 C C   . ALA   D 1 259 ? 27.372  -17.116 67.689  1.00 15.83  ?  259 ALA   D C   1 
ATOM   13166 O O   . ALA   D 1 259 ? 28.359  -17.155 66.951  1.00 13.99  ?  259 ALA   D O   1 
ATOM   13167 C CB  . ALA   D 1 259 ? 27.335  -17.347 70.195  1.00 16.92  ?  259 ALA   D CB  1 
ATOM   13168 N N   . LEU   D 1 260 ? 26.377  -16.252 67.525  1.00 15.90  ?  260 LEU   D N   1 
ATOM   13169 C CA  . LEU   D 1 260 ? 26.435  -15.221 66.502  1.00 16.24  ?  260 LEU   D CA  1 
ATOM   13170 C C   . LEU   D 1 260 ? 25.863  -13.920 67.053  1.00 16.08  ?  260 LEU   D C   1 
ATOM   13171 O O   . LEU   D 1 260 ? 24.983  -13.918 67.923  1.00 14.82  ?  260 LEU   D O   1 
ATOM   13172 C CB  . LEU   D 1 260 ? 25.684  -15.649 65.222  1.00 16.30  ?  260 LEU   D CB  1 
ATOM   13173 C CG  . LEU   D 1 260 ? 24.164  -15.851 65.283  1.00 15.00  ?  260 LEU   D CG  1 
ATOM   13174 C CD1 . LEU   D 1 260 ? 23.407  -14.552 65.105  1.00 14.76  ?  260 LEU   D CD1 1 
ATOM   13175 C CD2 . LEU   D 1 260 ? 23.718  -16.848 64.246  1.00 17.14  ?  260 LEU   D CD2 1 
ATOM   13176 N N   . THR   D 1 261 ? 26.397  -12.813 66.552  1.00 15.45  ?  261 THR   D N   1 
ATOM   13177 C CA  . THR   D 1 261 ? 25.790  -11.500 66.699  1.00 15.18  ?  261 THR   D CA  1 
ATOM   13178 C C   . THR   D 1 261 ? 25.465  -10.994 65.307  1.00 16.52  ?  261 THR   D C   1 
ATOM   13179 O O   . THR   D 1 261 ? 26.315  -11.046 64.412  1.00 21.17  ?  261 THR   D O   1 
ATOM   13180 C CB  . THR   D 1 261 ? 26.715  -10.516 67.411  1.00 13.72  ?  261 THR   D CB  1 
ATOM   13181 O OG1 . THR   D 1 261 ? 27.931  -10.400 66.669  1.00 20.15  ?  261 THR   D OG1 1 
ATOM   13182 C CG2 . THR   D 1 261 ? 27.026  -10.991 68.817  1.00 16.99  ?  261 THR   D CG2 1 
ATOM   13183 N N   . MET   D 1 262 ? 24.237  -10.525 65.119  1.00 13.53  ?  262 MET   D N   1 
ATOM   13184 C CA  . MET   D 1 262 ? 23.750  -10.175 63.800  1.00 16.64  ?  262 MET   D CA  1 
ATOM   13185 C C   . MET   D 1 262 ? 23.104  -8.803  63.828  1.00 15.88  ?  262 MET   D C   1 
ATOM   13186 O O   . MET   D 1 262 ? 22.275  -8.516  64.697  1.00 16.79  ?  262 MET   D O   1 
ATOM   13187 C CB  . MET   D 1 262 ? 22.747  -11.212 63.305  1.00 15.37  ?  262 MET   D CB  1 
ATOM   13188 C CG  . MET   D 1 262 ? 22.119  -10.855 61.980  1.00 19.87  ?  262 MET   D CG  1 
ATOM   13189 S SD  . MET   D 1 262 ? 20.924  -12.096 61.507  1.00 24.46  ?  262 MET   D SD  1 
ATOM   13190 C CE  . MET   D 1 262 ? 21.960  -13.555 61.433  1.00 22.98  ?  262 MET   D CE  1 
ATOM   13191 N N   . SER   D 1 263 ? 23.479  -7.964  62.875  1.00 15.23  ?  263 SER   D N   1 
ATOM   13192 C CA  . SER   D 1 263 ? 22.672  -6.805  62.523  1.00 14.21  ?  263 SER   D CA  1 
ATOM   13193 C C   . SER   D 1 263 ? 21.734  -7.232  61.408  1.00 15.32  ?  263 SER   D C   1 
ATOM   13194 O O   . SER   D 1 263 ? 22.172  -7.488  60.279  1.00 15.40  ?  263 SER   D O   1 
ATOM   13195 C CB  . SER   D 1 263 ? 23.542  -5.634  62.086  1.00 17.09  ?  263 SER   D CB  1 
ATOM   13196 O OG  . SER   D 1 263 ? 22.725  -4.622  61.543  1.00 18.04  ?  263 SER   D OG  1 
ATOM   13197 N N   . ALA   D 1 264 ? 20.443  -7.321  61.721  1.00 13.25  ?  264 ALA   D N   1 
ATOM   13198 C CA  . ALA   D 1 264 ? 19.456  -7.660  60.708  1.00 13.22  ?  264 ALA   D CA  1 
ATOM   13199 C C   . ALA   D 1 264 ? 19.170  -6.508  59.758  1.00 14.95  ?  264 ALA   D C   1 
ATOM   13200 O O   . ALA   D 1 264 ? 18.368  -6.673  58.836  1.00 18.19  ?  264 ALA   D O   1 
ATOM   13201 C CB  . ALA   D 1 264 ? 18.159  -8.125  61.373  1.00 17.71  ?  264 ALA   D CB  1 
ATOM   13202 N N   . LYS   D 1 265 ? 19.794  -5.347  59.961  1.00 15.26  ?  265 LYS   D N   1 
ATOM   13203 C CA  . LYS   D 1 265 ? 19.650  -4.213  59.053  1.00 13.93  ?  265 LYS   D CA  1 
ATOM   13204 C C   . LYS   D 1 265 ? 20.417  -4.409  57.758  1.00 13.33  ?  265 LYS   D C   1 
ATOM   13205 O O   . LYS   D 1 265 ? 20.349  -3.542  56.877  1.00 14.94  ?  265 LYS   D O   1 
ATOM   13206 C CB  . LYS   D 1 265 ? 20.115  -2.935  59.754  1.00 13.07  ?  265 LYS   D CB  1 
ATOM   13207 C CG  . LYS   D 1 265 ? 19.422  -2.705  61.096  1.00 12.77  ?  265 LYS   D CG  1 
ATOM   13208 C CD  . LYS   D 1 265 ? 20.085  -1.591  61.880  1.00 19.60  ?  265 LYS   D CD  1 
ATOM   13209 C CE  . LYS   D 1 265 ? 19.911  -0.234  61.208  1.00 17.09  ?  265 LYS   D CE  1 
ATOM   13210 N NZ  . LYS   D 1 265 ? 20.437  0.823   62.125  1.00 16.81  ?  265 LYS   D NZ  1 
ATOM   13211 N N   . LYS   D 1 266 ? 21.143  -5.524  57.632  1.00 16.22  ?  266 LYS   D N   1 
ATOM   13212 C CA  . LYS   D 1 266 ? 21.889  -5.864  56.423  1.00 16.18  ?  266 LYS   D CA  1 
ATOM   13213 C C   . LYS   D 1 266 ? 21.214  -7.011  55.671  1.00 15.91  ?  266 LYS   D C   1 
ATOM   13214 O O   . LYS   D 1 266 ? 20.152  -6.831  55.067  1.00 19.39  ?  266 LYS   D O   1 
ATOM   13215 C CB  . LYS   D 1 266 ? 23.333  -6.241  56.767  1.00 18.78  ?  266 LYS   D CB  1 
ATOM   13216 C CG  . LYS   D 1 266 ? 24.287  -5.071  57.061  1.00 16.04  ?  266 LYS   D CG  1 
ATOM   13217 C CD  . LYS   D 1 266 ? 23.805  -4.224  58.223  1.00 18.46  ?  266 LYS   D CD  1 
ATOM   13218 C CE  . LYS   D 1 266 ? 24.924  -3.536  58.938  1.00 23.63  ?  266 LYS   D CE  1 
ATOM   13219 N NZ  . LYS   D 1 266 ? 24.394  -2.937  60.197  1.00 26.15  ?  266 LYS   D NZ  1 
ATOM   13220 N N   . ASP   D 1 267 ? 21.819  -8.199  55.712  1.00 18.01  ?  267 ASP   D N   1 
ATOM   13221 C CA  . ASP   D 1 267 ? 21.341  -9.305  54.885  1.00 18.86  ?  267 ASP   D CA  1 
ATOM   13222 C C   . ASP   D 1 267 ? 19.910  -9.763  55.170  1.00 18.27  ?  267 ASP   D C   1 
ATOM   13223 O O   . ASP   D 1 267 ? 19.276  -10.286 54.237  1.00 19.43  ?  267 ASP   D O   1 
ATOM   13224 C CB  . ASP   D 1 267 ? 22.303  -10.494 55.024  1.00 21.06  ?  267 ASP   D CB  1 
ATOM   13225 C CG  . ASP   D 1 267 ? 23.518  -10.368 54.131  1.00 21.40  ?  267 ASP   D CG  1 
ATOM   13226 O OD1 . ASP   D 1 267 ? 23.782  -9.255  53.625  1.00 25.36  ?  267 ASP   D OD1 1 
ATOM   13227 O OD2 . ASP   D 1 267 ? 24.206  -11.388 53.922  1.00 24.21  ?  267 ASP   D OD2 1 
ATOM   13228 N N   . PRO   D 1 268 ? 19.368  -9.667  56.390  1.00 16.84  ?  268 PRO   D N   1 
ATOM   13229 C CA  . PRO   D 1 268 ? 17.938  -9.958  56.583  1.00 17.72  ?  268 PRO   D CA  1 
ATOM   13230 C C   . PRO   D 1 268 ? 16.988  -8.915  56.009  1.00 15.39  ?  268 PRO   D C   1 
ATOM   13231 O O   . PRO   D 1 268 ? 15.775  -9.054  56.199  1.00 15.38  ?  268 PRO   D O   1 
ATOM   13232 C CB  . PRO   D 1 268 ? 17.808  -10.035 58.112  1.00 16.81  ?  268 PRO   D CB  1 
ATOM   13233 C CG  . PRO   D 1 268 ? 19.130  -10.509 58.537  1.00 13.41  ?  268 PRO   D CG  1 
ATOM   13234 C CD  . PRO   D 1 268 ? 20.094  -9.754  57.670  1.00 17.09  ?  268 PRO   D CD  1 
ATOM   13235 N N   . LEU   D 1 269 ? 17.486  -7.863  55.350  1.00 16.39  ?  269 LEU   D N   1 
ATOM   13236 C CA  . LEU   D 1 269 ? 16.657  -6.980  54.522  1.00 14.39  ?  269 LEU   D CA  1 
ATOM   13237 C C   . LEU   D 1 269 ? 15.695  -6.134  55.353  1.00 15.12  ?  269 LEU   D C   1 
ATOM   13238 O O   . LEU   D 1 269 ? 14.569  -5.881  54.931  1.00 18.20  ?  269 LEU   D O   1 
ATOM   13239 C CB  . LEU   D 1 269 ? 15.878  -7.778  53.472  1.00 16.83  ?  269 LEU   D CB  1 
ATOM   13240 C CG  . LEU   D 1 269 ? 16.678  -8.450  52.353  1.00 17.46  ?  269 LEU   D CG  1 
ATOM   13241 C CD1 . LEU   D 1 269 ? 15.873  -9.585  51.729  1.00 21.56  ?  269 LEU   D CD1 1 
ATOM   13242 C CD2 . LEU   D 1 269 ? 17.026  -7.423  51.308  1.00 16.65  ?  269 LEU   D CD2 1 
ATOM   13243 N N   . LEU   D 1 270 ? 16.138  -5.666  56.518  1.00 18.23  ?  270 LEU   D N   1 
ATOM   13244 C CA  . LEU   D 1 270 ? 15.272  -4.903  57.412  1.00 15.30  ?  270 LEU   D CA  1 
ATOM   13245 C C   . LEU   D 1 270 ? 15.719  -3.449  57.501  1.00 14.21  ?  270 LEU   D C   1 
ATOM   13246 O O   . LEU   D 1 270 ? 16.789  -3.069  57.030  1.00 17.10  ?  270 LEU   D O   1 
ATOM   13247 C CB  . LEU   D 1 270 ? 15.254  -5.513  58.814  1.00 12.72  ?  270 LEU   D CB  1 
ATOM   13248 C CG  . LEU   D 1 270 ? 14.815  -6.964  58.959  1.00 17.61  ?  270 LEU   D CG  1 
ATOM   13249 C CD1 . LEU   D 1 270 ? 14.749  -7.327  60.438  1.00 17.75  ?  270 LEU   D CD1 1 
ATOM   13250 C CD2 . LEU   D 1 270 ? 13.477  -7.220  58.263  1.00 15.05  ?  270 LEU   D CD2 1 
ATOM   13251 N N   . ASN   D 1 271 ? 14.874  -2.631  58.128  1.00 13.32  ?  271 ASN   D N   1 
ATOM   13252 C CA  . ASN   D 1 271 ? 15.215  -1.250  58.434  1.00 14.67  ?  271 ASN   D CA  1 
ATOM   13253 C C   . ASN   D 1 271 ? 15.637  -1.050  59.887  1.00 16.25  ?  271 ASN   D C   1 
ATOM   13254 O O   . ASN   D 1 271 ? 16.103  0.039   60.244  1.00 15.88  ?  271 ASN   D O   1 
ATOM   13255 C CB  . ASN   D 1 271 ? 14.025  -0.346  58.103  1.00 15.10  ?  271 ASN   D CB  1 
ATOM   13256 C CG  . ASN   D 1 271 ? 13.423  -0.654  56.743  1.00 17.70  ?  271 ASN   D CG  1 
ATOM   13257 O OD1 . ASN   D 1 271 ? 12.248  -1.007  56.638  1.00 15.98  ?  271 ASN   D OD1 1 
ATOM   13258 N ND2 . ASN   D 1 271 ? 14.230  -0.536  55.695  1.00 16.66  ?  271 ASN   D ND2 1 
ATOM   13259 N N   . ILE   D 1 272 ? 15.470  -2.075  60.722  1.00 14.80  ?  272 ILE   D N   1 
ATOM   13260 C CA  . ILE   D 1 272 ? 15.893  -2.056  62.117  1.00 13.45  ?  272 ILE   D CA  1 
ATOM   13261 C C   . ILE   D 1 272 ? 15.866  -3.512  62.557  1.00 15.31  ?  272 ILE   D C   1 
ATOM   13262 O O   . ILE   D 1 272 ? 15.161  -4.342  61.961  1.00 14.94  ?  272 ILE   D O   1 
ATOM   13263 C CB  . ILE   D 1 272 ? 14.964  -1.169  62.995  1.00 11.92  ?  272 ILE   D CB  1 
ATOM   13264 C CG1 . ILE   D 1 272 ? 15.563  -0.928  64.388  1.00 16.02  ?  272 ILE   D CG1 1 
ATOM   13265 C CG2 . ILE   D 1 272 ? 13.581  -1.798  63.157  1.00 14.93  ?  272 ILE   D CG2 1 
ATOM   13266 C CD1 . ILE   D 1 272 ? 16.867  -0.081  64.410  1.00 15.51  ?  272 ILE   D CD1 1 
ATOM   13267 N N   . GLY   D 1 273 ? 16.650  -3.841  63.580  1.00 14.37  ?  273 GLY   D N   1 
ATOM   13268 C CA  . GLY   D 1 273 ? 16.626  -5.180  64.141  1.00 13.48  ?  273 GLY   D CA  1 
ATOM   13269 C C   . GLY   D 1 273 ? 17.982  -5.843  64.254  1.00 14.93  ?  273 GLY   D C   1 
ATOM   13270 O O   . GLY   D 1 273 ? 18.915  -5.542  63.508  1.00 15.88  ?  273 GLY   D O   1 
ATOM   13271 N N   . GLY   D 1 274 ? 18.091  -6.765  65.207  1.00 15.29  ?  274 GLY   D N   1 
ATOM   13272 C CA  . GLY   D 1 274 ? 19.330  -7.470  65.475  1.00 13.95  ?  274 GLY   D CA  1 
ATOM   13273 C C   . GLY   D 1 274 ? 19.022  -8.760  66.196  1.00 13.71  ?  274 GLY   D C   1 
ATOM   13274 O O   . GLY   D 1 274 ? 17.879  -9.033  66.571  1.00 11.90  ?  274 GLY   D O   1 
ATOM   13275 N N   . LEU   D 1 275 ? 20.063  -9.563  66.392  1.00 11.62  ?  275 LEU   D N   1 
ATOM   13276 C CA  . LEU   D 1 275 ? 19.847  -10.891 66.942  1.00 12.79  ?  275 LEU   D CA  1 
ATOM   13277 C C   . LEU   D 1 275 ? 21.116  -11.376 67.617  1.00 12.68  ?  275 LEU   D C   1 
ATOM   13278 O O   . LEU   D 1 275 ? 22.216  -11.157 67.109  1.00 14.73  ?  275 LEU   D O   1 
ATOM   13279 C CB  . LEU   D 1 275 ? 19.434  -11.878 65.845  1.00 13.77  ?  275 LEU   D CB  1 
ATOM   13280 C CG  . LEU   D 1 275 ? 19.062  -13.299 66.270  1.00 12.18  ?  275 LEU   D CG  1 
ATOM   13281 C CD1 . LEU   D 1 275 ? 17.743  -13.266 67.042  1.00 15.15  ?  275 LEU   D CD1 1 
ATOM   13282 C CD2 . LEU   D 1 275 ? 18.966  -14.235 65.065  1.00 11.84  ?  275 LEU   D CD2 1 
ATOM   13283 N N   . VAL   D 1 276 ? 20.947  -12.024 68.766  1.00 12.49  ?  276 VAL   D N   1 
ATOM   13284 C CA  . VAL   D 1 276 ? 21.953  -12.902 69.350  1.00 16.14  ?  276 VAL   D CA  1 
ATOM   13285 C C   . VAL   D 1 276 ? 21.424  -14.326 69.251  1.00 15.44  ?  276 VAL   D C   1 
ATOM   13286 O O   . VAL   D 1 276 ? 20.238  -14.572 69.495  1.00 16.07  ?  276 VAL   D O   1 
ATOM   13287 C CB  . VAL   D 1 276 ? 22.267  -12.541 70.815  1.00 14.35  ?  276 VAL   D CB  1 
ATOM   13288 C CG1 . VAL   D 1 276 ? 23.274  -13.517 71.399  1.00 14.48  ?  276 VAL   D CG1 1 
ATOM   13289 C CG2 . VAL   D 1 276 ? 22.787  -11.130 70.917  1.00 14.00  ?  276 VAL   D CG2 1 
ATOM   13290 N N   . ALA   D 1 277 ? 22.293  -15.257 68.873  1.00 14.51  ?  277 ALA   D N   1 
ATOM   13291 C CA  . ALA   D 1 277 ? 21.935  -16.665 68.843  1.00 15.87  ?  277 ALA   D CA  1 
ATOM   13292 C C   . ALA   D 1 277 ? 23.115  -17.474 69.360  1.00 18.90  ?  277 ALA   D C   1 
ATOM   13293 O O   . ALA   D 1 277 ? 24.269  -17.171 69.048  1.00 18.53  ?  277 ALA   D O   1 
ATOM   13294 C CB  . ALA   D 1 277 ? 21.534  -17.113 67.435  1.00 15.18  ?  277 ALA   D CB  1 
ATOM   13295 N N   . ILE   D 1 278 ? 22.828  -18.483 70.173  1.00 15.99  ?  278 ILE   D N   1 
ATOM   13296 C CA  . ILE   D 1 278 ? 23.857  -19.257 70.858  1.00 14.57  ?  278 ILE   D CA  1 
ATOM   13297 C C   . ILE   D 1 278 ? 23.615  -20.725 70.548  1.00 18.52  ?  278 ILE   D C   1 
ATOM   13298 O O   . ILE   D 1 278 ? 22.475  -21.193 70.635  1.00 18.08  ?  278 ILE   D O   1 
ATOM   13299 C CB  . ILE   D 1 278 ? 23.828  -19.000 72.373  1.00 15.50  ?  278 ILE   D CB  1 
ATOM   13300 C CG1 . ILE   D 1 278 ? 24.141  -17.528 72.655  1.00 14.14  ?  278 ILE   D CG1 1 
ATOM   13301 C CG2 . ILE   D 1 278 ? 24.801  -19.927 73.086  1.00 21.12  ?  278 ILE   D CG2 1 
ATOM   13302 C CD1 . ILE   D 1 278 ? 23.993  -17.143 74.102  1.00 19.88  ?  278 ILE   D CD1 1 
ATOM   13303 N N   . ARG   D 1 279 ? 24.670  -21.452 70.169  1.00 15.62  ?  279 ARG   D N   1 
ATOM   13304 C CA  . ARG   D 1 279 ? 24.458  -22.815 69.687  1.00 20.83  ?  279 ARG   D CA  1 
ATOM   13305 C C   . ARG   D 1 279 ? 23.897  -23.708 70.788  1.00 23.79  ?  279 ARG   D C   1 
ATOM   13306 O O   . ARG   D 1 279 ? 22.794  -24.248 70.660  1.00 26.98  ?  279 ARG   D O   1 
ATOM   13307 C CB  . ARG   D 1 279 ? 25.745  -23.421 69.123  1.00 21.24  ?  279 ARG   D CB  1 
ATOM   13308 C CG  . ARG   D 1 279 ? 25.474  -24.784 68.479  1.00 26.70  ?  279 ARG   D CG  1 
ATOM   13309 C CD  . ARG   D 1 279 ? 26.732  -25.617 68.269  1.00 34.93  ?  279 ARG   D CD  1 
ATOM   13310 N NE  . ARG   D 1 279 ? 27.591  -25.075 67.222  1.00 38.76  ?  279 ARG   D NE  1 
ATOM   13311 C CZ  . ARG   D 1 279 ? 28.746  -25.610 66.843  1.00 36.94  ?  279 ARG   D CZ  1 
ATOM   13312 N NH1 . ARG   D 1 279 ? 29.204  -26.732 67.378  1.00 39.42  ?  279 ARG   D NH1 1 
ATOM   13313 N NH2 . ARG   D 1 279 ? 29.466  -25.001 65.909  1.00 30.85  ?  279 ARG   D NH2 1 
ATOM   13314 N N   . ASP   D 1 280 ? 24.646  -23.876 71.887  1.00 22.54  ?  280 ASP   D N   1 
ATOM   13315 C CA  . ASP   D 1 280 ? 24.191  -24.792 72.926  1.00 24.35  ?  280 ASP   D CA  1 
ATOM   13316 C C   . ASP   D 1 280 ? 24.689  -24.451 74.329  1.00 26.28  ?  280 ASP   D C   1 
ATOM   13317 O O   . ASP   D 1 280 ? 24.568  -25.301 75.222  1.00 27.15  ?  280 ASP   D O   1 
ATOM   13318 C CB  . ASP   D 1 280 ? 24.610  -26.228 72.561  1.00 30.14  ?  280 ASP   D CB  1 
ATOM   13319 C CG  . ASP   D 1 280 ? 26.124  -26.382 72.396  1.00 32.63  ?  280 ASP   D CG  1 
ATOM   13320 O OD1 . ASP   D 1 280 ? 26.886  -25.570 72.976  1.00 28.74  ?  280 ASP   D OD1 1 
ATOM   13321 O OD2 . ASP   D 1 280 ? 26.553  -27.316 71.674  1.00 32.47  ?  280 ASP   D OD2 1 
ATOM   13322 N N   . ASN   D 1 281 ? 25.251  -23.267 74.566  1.00 23.63  ?  281 ASN   D N   1 
ATOM   13323 C CA  . ASN   D 1 281 ? 25.739  -22.902 75.895  1.00 23.47  ?  281 ASN   D CA  1 
ATOM   13324 C C   . ASN   D 1 281 ? 24.602  -22.242 76.668  1.00 24.40  ?  281 ASN   D C   1 
ATOM   13325 O O   . ASN   D 1 281 ? 24.376  -21.034 76.555  1.00 21.05  ?  281 ASN   D O   1 
ATOM   13326 C CB  . ASN   D 1 281 ? 26.954  -21.990 75.793  1.00 24.20  ?  281 ASN   D CB  1 
ATOM   13327 C CG  . ASN   D 1 281 ? 27.742  -21.917 77.098  1.00 27.90  ?  281 ASN   D CG  1 
ATOM   13328 O OD1 . ASN   D 1 281 ? 27.166  -21.830 78.179  1.00 24.62  ?  281 ASN   D OD1 1 
ATOM   13329 N ND2 . ASN   D 1 281 ? 29.066  -21.961 76.997  1.00 26.73  ?  281 ASN   D ND2 1 
ATOM   13330 N N   . GLU   D 1 282 ? 23.886  -23.041 77.469  1.00 24.94  ?  282 GLU   D N   1 
ATOM   13331 C CA  . GLU   D 1 282 ? 22.783  -22.498 78.260  1.00 24.38  ?  282 GLU   D CA  1 
ATOM   13332 C C   . GLU   D 1 282 ? 23.272  -21.459 79.264  1.00 22.39  ?  282 GLU   D C   1 
ATOM   13333 O O   . GLU   D 1 282 ? 22.584  -20.460 79.516  1.00 21.59  ?  282 GLU   D O   1 
ATOM   13334 C CB  . GLU   D 1 282 ? 22.041  -23.616 78.990  1.00 25.32  ?  282 GLU   D CB  1 
ATOM   13335 C CG  . GLU   D 1 282 ? 20.883  -23.098 79.833  1.00 31.72  ?  282 GLU   D CG  1 
ATOM   13336 C CD  . GLU   D 1 282 ? 20.384  -24.098 80.859  1.00 36.53  ?  282 GLU   D CD  1 
ATOM   13337 O OE1 . GLU   D 1 282 ? 19.807  -25.129 80.449  1.00 40.63  ?  282 GLU   D OE1 1 
ATOM   13338 O OE2 . GLU   D 1 282 ? 20.568  -23.852 82.076  1.00 37.47  ?  282 GLU   D OE2 1 
ATOM   13339 N N   . GLU   D 1 283 ? 24.454  -21.674 79.851  1.00 24.69  ?  283 GLU   D N   1 
ATOM   13340 C CA  . GLU   D 1 283 ? 24.943  -20.772 80.890  1.00 20.55  ?  283 GLU   D CA  1 
ATOM   13341 C C   . GLU   D 1 283 ? 25.198  -19.380 80.327  1.00 23.49  ?  283 GLU   D C   1 
ATOM   13342 O O   . GLU   D 1 283 ? 24.789  -18.373 80.918  1.00 21.20  ?  283 GLU   D O   1 
ATOM   13343 C CB  . GLU   D 1 283 ? 26.210  -21.340 81.529  1.00 20.27  ?  283 GLU   D CB  1 
ATOM   13344 C CG  . GLU   D 1 283 ? 26.853  -20.407 82.538  1.00 27.53  ?  283 GLU   D CG  1 
ATOM   13345 C CD  . GLU   D 1 283 ? 28.155  -20.956 83.081  1.00 30.69  ?  283 GLU   D CD  1 
ATOM   13346 O OE1 . GLU   D 1 283 ? 28.487  -22.112 82.736  1.00 35.63  ?  283 GLU   D OE1 1 
ATOM   13347 O OE2 . GLU   D 1 283 ? 28.841  -20.237 83.842  1.00 28.52  ?  283 GLU   D OE2 1 
ATOM   13348 N N   . ILE   D 1 284 ? 25.871  -19.306 79.175  1.00 18.31  ?  284 ILE   D N   1 
ATOM   13349 C CA  . ILE   D 1 284 ? 26.079  -18.022 78.511  1.00 18.05  ?  284 ILE   D CA  1 
ATOM   13350 C C   . ILE   D 1 284 ? 24.752  -17.431 78.034  1.00 19.37  ?  284 ILE   D C   1 
ATOM   13351 O O   . ILE   D 1 284 ? 24.561  -16.207 78.055  1.00 17.61  ?  284 ILE   D O   1 
ATOM   13352 C CB  . ILE   D 1 284 ? 27.085  -18.205 77.361  1.00 20.63  ?  284 ILE   D CB  1 
ATOM   13353 C CG1 . ILE   D 1 284 ? 28.491  -18.409 77.934  1.00 19.00  ?  284 ILE   D CG1 1 
ATOM   13354 C CG2 . ILE   D 1 284 ? 27.036  -17.025 76.394  1.00 19.30  ?  284 ILE   D CG2 1 
ATOM   13355 C CD1 . ILE   D 1 284 ? 29.536  -18.675 76.889  1.00 28.34  ?  284 ILE   D CD1 1 
ATOM   13356 N N   . PHE   D 1 285 ? 23.812  -18.280 77.615  1.00 17.48  ?  285 PHE   D N   1 
ATOM   13357 C CA  . PHE   D 1 285 ? 22.485  -17.802 77.241  1.00 17.51  ?  285 PHE   D CA  1 
ATOM   13358 C C   . PHE   D 1 285 ? 21.773  -17.164 78.428  1.00 18.44  ?  285 PHE   D C   1 
ATOM   13359 O O   . PHE   D 1 285 ? 21.208  -16.068 78.316  1.00 17.52  ?  285 PHE   D O   1 
ATOM   13360 C CB  . PHE   D 1 285 ? 21.675  -18.963 76.683  1.00 19.31  ?  285 PHE   D CB  1 
ATOM   13361 C CG  . PHE   D 1 285 ? 20.232  -18.649 76.463  1.00 20.89  ?  285 PHE   D CG  1 
ATOM   13362 C CD1 . PHE   D 1 285 ? 19.854  -17.634 75.607  1.00 16.74  ?  285 PHE   D CD1 1 
ATOM   13363 C CD2 . PHE   D 1 285 ? 19.247  -19.397 77.091  1.00 22.84  ?  285 PHE   D CD2 1 
ATOM   13364 C CE1 . PHE   D 1 285 ? 18.518  -17.356 75.392  1.00 16.86  ?  285 PHE   D CE1 1 
ATOM   13365 C CE2 . PHE   D 1 285 ? 17.908  -19.120 76.882  1.00 22.74  ?  285 PHE   D CE2 1 
ATOM   13366 C CZ  . PHE   D 1 285 ? 17.546  -18.102 76.019  1.00 17.70  ?  285 PHE   D CZ  1 
ATOM   13367 N N   . THR   D 1 286 ? 21.784  -17.839 79.577  1.00 19.84  ?  286 THR   D N   1 
ATOM   13368 C CA  . THR   D 1 286 ? 21.183  -17.265 80.774  1.00 21.01  ?  286 THR   D CA  1 
ATOM   13369 C C   . THR   D 1 286 ? 21.816  -15.921 81.118  1.00 19.53  ?  286 THR   D C   1 
ATOM   13370 O O   . THR   D 1 286 ? 21.114  -14.954 81.431  1.00 17.26  ?  286 THR   D O   1 
ATOM   13371 C CB  . THR   D 1 286 ? 21.328  -18.237 81.942  1.00 23.84  ?  286 THR   D CB  1 
ATOM   13372 O OG1 . THR   D 1 286 ? 20.707  -19.482 81.600  1.00 25.36  ?  286 THR   D OG1 1 
ATOM   13373 C CG2 . THR   D 1 286 ? 20.675  -17.659 83.201  1.00 24.21  ?  286 THR   D CG2 1 
ATOM   13374 N N   . LEU   D 1 287 ? 23.147  -15.842 81.073  1.00 17.74  ?  287 LEU   D N   1 
ATOM   13375 C CA  . LEU   D 1 287 ? 23.816  -14.604 81.455  1.00 17.73  ?  287 LEU   D CA  1 
ATOM   13376 C C   . LEU   D 1 287 ? 23.525  -13.490 80.460  1.00 15.61  ?  287 LEU   D C   1 
ATOM   13377 O O   . LEU   D 1 287 ? 23.374  -12.326 80.852  1.00 18.09  ?  287 LEU   D O   1 
ATOM   13378 C CB  . LEU   D 1 287 ? 25.326  -14.824 81.577  1.00 20.57  ?  287 LEU   D CB  1 
ATOM   13379 C CG  . LEU   D 1 287 ? 25.913  -15.606 82.753  1.00 20.16  ?  287 LEU   D CG  1 
ATOM   13380 C CD1 . LEU   D 1 287 ? 27.378  -15.892 82.478  1.00 20.23  ?  287 LEU   D CD1 1 
ATOM   13381 C CD2 . LEU   D 1 287 ? 25.757  -14.837 84.054  1.00 15.97  ?  287 LEU   D CD2 1 
ATOM   13382 N N   . ALA   D 1 288 ? 23.457  -13.816 79.169  1.00 15.16  ?  288 ALA   D N   1 
ATOM   13383 C CA  . ALA   D 1 288 ? 23.157  -12.786 78.179  1.00 16.44  ?  288 ALA   D CA  1 
ATOM   13384 C C   . ALA   D 1 288 ? 21.727  -12.273 78.336  1.00 17.89  ?  288 ALA   D C   1 
ATOM   13385 O O   . ALA   D 1 288 ? 21.464  -11.071 78.173  1.00 15.08  ?  288 ALA   D O   1 
ATOM   13386 C CB  . ALA   D 1 288 ? 23.409  -13.329 76.769  1.00 16.74  ?  288 ALA   D CB  1 
ATOM   13387 N N   . ARG   D 1 289 ? 20.789  -13.165 78.672  1.00 16.56  ?  289 ARG   D N   1 
ATOM   13388 C CA  . ARG   D 1 289 ? 19.424  -12.726 78.951  1.00 18.70  ?  289 ARG   D CA  1 
ATOM   13389 C C   . ARG   D 1 289 ? 19.377  -11.771 80.138  1.00 20.88  ?  289 ARG   D C   1 
ATOM   13390 O O   . ARG   D 1 289 ? 18.590  -10.814 80.144  1.00 17.04  ?  289 ARG   D O   1 
ATOM   13391 C CB  . ARG   D 1 289 ? 18.532  -13.929 79.220  1.00 19.11  ?  289 ARG   D CB  1 
ATOM   13392 C CG  . ARG   D 1 289 ? 18.002  -14.599 77.989  1.00 15.61  ?  289 ARG   D CG  1 
ATOM   13393 C CD  . ARG   D 1 289 ? 16.943  -15.580 78.422  1.00 20.25  ?  289 ARG   D CD  1 
ATOM   13394 N NE  . ARG   D 1 289 ? 15.971  -15.859 77.376  1.00 20.42  ?  289 ARG   D NE  1 
ATOM   13395 C CZ  . ARG   D 1 289 ? 14.859  -16.543 77.587  1.00 22.46  ?  289 ARG   D CZ  1 
ATOM   13396 N NH1 . ARG   D 1 289 ? 14.552  -16.992 78.793  1.00 21.68  ?  289 ARG   D NH1 1 
ATOM   13397 N NH2 . ARG   D 1 289 ? 14.036  -16.780 76.568  1.00 21.08  ?  289 ARG   D NH2 1 
ATOM   13398 N N   . GLN   D 1 290 ? 20.201  -12.025 81.162  1.00 16.57  ?  290 GLN   D N   1 
ATOM   13399 C CA  . GLN   D 1 290 ? 20.236  -11.143 82.324  1.00 16.94  ?  290 GLN   D CA  1 
ATOM   13400 C C   . GLN   D 1 290 ? 20.823  -9.781  81.974  1.00 17.00  ?  290 GLN   D C   1 
ATOM   13401 O O   . GLN   D 1 290 ? 20.505  -8.786  82.630  1.00 19.21  ?  290 GLN   D O   1 
ATOM   13402 C CB  . GLN   D 1 290 ? 21.018  -11.807 83.457  1.00 15.98  ?  290 GLN   D CB  1 
ATOM   13403 C CG  . GLN   D 1 290 ? 20.344  -13.089 83.918  1.00 20.97  ?  290 GLN   D CG  1 
ATOM   13404 C CD  . GLN   D 1 290 ? 21.165  -13.904 84.892  1.00 25.22  ?  290 GLN   D CD  1 
ATOM   13405 O OE1 . GLN   D 1 290 ? 22.309  -13.564 85.216  1.00 26.10  ?  290 GLN   D OE1 1 
ATOM   13406 N NE2 . GLN   D 1 290 ? 20.583  -14.993 85.369  1.00 26.70  ?  290 GLN   D NE2 1 
ATOM   13407 N N   . ARG   D 1 291 ? 21.656  -9.707  80.940  1.00 15.32  ?  291 ARG   D N   1 
ATOM   13408 C CA  . ARG   D 1 291 ? 22.098  -8.403  80.460  1.00 14.15  ?  291 ARG   D CA  1 
ATOM   13409 C C   . ARG   D 1 291 ? 21.095  -7.777  79.497  1.00 16.13  ?  291 ARG   D C   1 
ATOM   13410 O O   . ARG   D 1 291 ? 20.988  -6.545  79.435  1.00 17.21  ?  291 ARG   D O   1 
ATOM   13411 C CB  . ARG   D 1 291 ? 23.468  -8.523  79.790  1.00 15.56  ?  291 ARG   D CB  1 
ATOM   13412 C CG  . ARG   D 1 291 ? 23.931  -7.227  79.183  1.00 19.87  ?  291 ARG   D CG  1 
ATOM   13413 C CD  . ARG   D 1 291 ? 25.418  -7.072  79.251  1.00 19.54  ?  291 ARG   D CD  1 
ATOM   13414 N NE  . ARG   D 1 291 ? 25.806  -5.741  78.812  1.00 15.93  ?  291 ARG   D NE  1 
ATOM   13415 C CZ  . ARG   D 1 291 ? 26.225  -4.782  79.621  1.00 18.95  ?  291 ARG   D CZ  1 
ATOM   13416 N NH1 . ARG   D 1 291 ? 26.311  -4.972  80.927  1.00 22.45  ?  291 ARG   D NH1 1 
ATOM   13417 N NH2 . ARG   D 1 291 ? 26.577  -3.610  79.107  1.00 16.03  ?  291 ARG   D NH2 1 
ATOM   13418 N N   . CYS   D 1 292 ? 20.357  -8.600  78.744  1.00 15.27  ?  292 CYS   D N   1 
ATOM   13419 C CA  . CYS   D 1 292 ? 19.380  -8.070  77.793  1.00 16.62  ?  292 CYS   D CA  1 
ATOM   13420 C C   . CYS   D 1 292 ? 18.307  -7.237  78.486  1.00 17.90  ?  292 CYS   D C   1 
ATOM   13421 O O   . CYS   D 1 292 ? 17.893  -6.189  77.975  1.00 17.88  ?  292 CYS   D O   1 
ATOM   13422 C CB  . CYS   D 1 292 ? 18.725  -9.216  77.023  1.00 17.59  ?  292 CYS   D CB  1 
ATOM   13423 S SG  . CYS   D 1 292 ? 17.393  -8.686  75.897  1.00 19.40  ?  292 CYS   D SG  1 
ATOM   13424 N N   . VAL   D 1 293 ? 17.839  -7.694  79.647  1.00 19.35  ?  293 VAL   D N   1 
ATOM   13425 C CA  . VAL   D 1 293 ? 16.709  -7.037  80.307  1.00 19.43  ?  293 VAL   D CA  1 
ATOM   13426 C C   . VAL   D 1 293 ? 16.969  -5.558  80.591  1.00 17.70  ?  293 VAL   D C   1 
ATOM   13427 O O   . VAL   D 1 293 ? 16.154  -4.722  80.170  1.00 19.57  ?  293 VAL   D O   1 
ATOM   13428 C CB  . VAL   D 1 293 ? 16.299  -7.833  81.556  1.00 24.87  ?  293 VAL   D CB  1 
ATOM   13429 C CG1 . VAL   D 1 293 ? 15.377  -7.006  82.447  1.00 20.45  ?  293 VAL   D CG1 1 
ATOM   13430 C CG2 . VAL   D 1 293 ? 15.632  -9.151  81.126  1.00 19.31  ?  293 VAL   D CG2 1 
ATOM   13431 N N   . PRO   D 1 294 ? 18.055  -5.160  81.270  1.00 18.34  ?  294 PRO   D N   1 
ATOM   13432 C CA  . PRO   D 1 294 ? 18.237  -3.721  81.538  1.00 16.57  ?  294 PRO   D CA  1 
ATOM   13433 C C   . PRO   D 1 294 ? 18.686  -2.903  80.332  1.00 21.67  ?  294 PRO   D C   1 
ATOM   13434 O O   . PRO   D 1 294 ? 18.446  -1.689  80.311  1.00 18.37  ?  294 PRO   D O   1 
ATOM   13435 C CB  . PRO   D 1 294 ? 19.300  -3.701  82.646  1.00 21.56  ?  294 PRO   D CB  1 
ATOM   13436 C CG  . PRO   D 1 294 ? 20.068  -4.946  82.445  1.00 20.50  ?  294 PRO   D CG  1 
ATOM   13437 C CD  . PRO   D 1 294 ? 19.078  -5.968  81.963  1.00 19.69  ?  294 PRO   D CD  1 
ATOM   13438 N N   . MET   D 1 295 ? 19.319  -3.519  79.331  1.00 19.93  ?  295 MET   D N   1 
ATOM   13439 C CA  . MET   D 1 295 ? 19.936  -2.779  78.235  1.00 20.97  ?  295 MET   D CA  1 
ATOM   13440 C C   . MET   D 1 295 ? 19.029  -2.628  77.022  1.00 20.16  ?  295 MET   D C   1 
ATOM   13441 O O   . MET   D 1 295 ? 19.092  -1.604  76.328  1.00 18.42  ?  295 MET   D O   1 
ATOM   13442 C CB  . MET   D 1 295 ? 21.238  -3.475  77.807  1.00 19.01  ?  295 MET   D CB  1 
ATOM   13443 C CG  . MET   D 1 295 ? 22.339  -3.447  78.858  1.00 16.60  ?  295 MET   D CG  1 
ATOM   13444 S SD  . MET   D 1 295 ? 22.844  -1.750  79.191  1.00 25.22  ?  295 MET   D SD  1 
ATOM   13445 C CE  . MET   D 1 295 ? 23.851  -1.973  80.639  1.00 22.76  ?  295 MET   D CE  1 
ATOM   13446 N N   . GLU   D 1 296 ? 18.192  -3.626  76.749  1.00 18.60  ?  296 GLU   D N   1 
ATOM   13447 C CA  . GLU   D 1 296 ? 17.445  -3.708  75.502  1.00 17.31  ?  296 GLU   D CA  1 
ATOM   13448 C C   . GLU   D 1 296 ? 15.948  -3.815  75.728  1.00 14.82  ?  296 GLU   D C   1 
ATOM   13449 O O   . GLU   D 1 296 ? 15.187  -3.066  75.115  1.00 18.43  ?  296 GLU   D O   1 
ATOM   13450 C CB  . GLU   D 1 296 ? 17.941  -4.908  74.666  1.00 18.16  ?  296 GLU   D CB  1 
ATOM   13451 C CG  . GLU   D 1 296 ? 19.382  -4.784  74.166  1.00 18.19  ?  296 GLU   D CG  1 
ATOM   13452 C CD  . GLU   D 1 296 ? 19.508  -3.846  72.970  1.00 21.87  ?  296 GLU   D CD  1 
ATOM   13453 O OE1 . GLU   D 1 296 ? 18.558  -3.770  72.166  1.00 23.25  ?  296 GLU   D OE1 1 
ATOM   13454 O OE2 . GLU   D 1 296 ? 20.548  -3.169  72.839  1.00 26.50  ?  296 GLU   D OE2 1 
ATOM   13455 N N   . GLY   D 1 297 ? 15.511  -4.698  76.611  1.00 15.15  ?  297 GLY   D N   1 
ATOM   13456 C CA  . GLY   D 1 297 ? 14.103  -5.001  76.783  1.00 14.76  ?  297 GLY   D CA  1 
ATOM   13457 C C   . GLY   D 1 297 ? 13.951  -6.408  77.325  1.00 16.80  ?  297 GLY   D C   1 
ATOM   13458 O O   . GLY   D 1 297 ? 14.927  -7.097  77.607  1.00 17.35  ?  297 GLY   D O   1 
ATOM   13459 N N   . PHE   D 1 298 ? 12.695  -6.820  77.481  1.00 18.52  ?  298 PHE   D N   1 
ATOM   13460 C CA  . PHE   D 1 298 ? 12.446  -8.180  77.936  1.00 19.22  ?  298 PHE   D CA  1 
ATOM   13461 C C   . PHE   D 1 298 ? 12.919  -9.172  76.877  1.00 16.31  ?  298 PHE   D C   1 
ATOM   13462 O O   . PHE   D 1 298 ? 13.027  -8.850  75.690  1.00 18.70  ?  298 PHE   D O   1 
ATOM   13463 C CB  . PHE   D 1 298 ? 10.966  -8.397  78.259  1.00 21.54  ?  298 PHE   D CB  1 
ATOM   13464 C CG  . PHE   D 1 298 ? 10.665  -9.779  78.781  1.00 21.68  ?  298 PHE   D CG  1 
ATOM   13465 C CD1 . PHE   D 1 298 ? 11.179  -10.201 79.994  1.00 23.51  ?  298 PHE   D CD1 1 
ATOM   13466 C CD2 . PHE   D 1 298 ? 9.899   -10.664 78.045  1.00 18.80  ?  298 PHE   D CD2 1 
ATOM   13467 C CE1 . PHE   D 1 298 ? 10.922  -11.477 80.469  1.00 23.22  ?  298 PHE   D CE1 1 
ATOM   13468 C CE2 . PHE   D 1 298 ? 9.634   -11.936 78.521  1.00 17.03  ?  298 PHE   D CE2 1 
ATOM   13469 C CZ  . PHE   D 1 298 ? 10.146  -12.340 79.737  1.00 20.18  ?  298 PHE   D CZ  1 
ATOM   13470 N N   . VAL   D 1 299 ? 13.208  -10.399 77.319  1.00 17.09  ?  299 VAL   D N   1 
ATOM   13471 C CA  . VAL   D 1 299 ? 13.991  -11.315 76.492  1.00 15.70  ?  299 VAL   D CA  1 
ATOM   13472 C C   . VAL   D 1 299 ? 13.244  -11.825 75.267  1.00 18.72  ?  299 VAL   D C   1 
ATOM   13473 O O   . VAL   D 1 299 ? 13.880  -12.432 74.391  1.00 17.35  ?  299 VAL   D O   1 
ATOM   13474 C CB  . VAL   D 1 299 ? 14.504  -12.511 77.329  1.00 17.05  ?  299 VAL   D CB  1 
ATOM   13475 C CG1 . VAL   D 1 299 ? 15.368  -12.015 78.486  1.00 15.67  ?  299 VAL   D CG1 1 
ATOM   13476 C CG2 . VAL   D 1 299 ? 13.341  -13.375 77.839  1.00 16.45  ?  299 VAL   D CG2 1 
ATOM   13477 N N   . THR   D 1 300 ? 11.928  -11.592 75.162  1.00 15.28  ?  300 THR   D N   1 
ATOM   13478 C CA  . THR   D 1 300 ? 11.164  -12.051 74.008  1.00 16.32  ?  300 THR   D CA  1 
ATOM   13479 C C   . THR   D 1 300 ? 10.815  -10.929 73.036  1.00 16.84  ?  300 THR   D C   1 
ATOM   13480 O O   . THR   D 1 300 ? 9.999   -11.141 72.141  1.00 18.97  ?  300 THR   D O   1 
ATOM   13481 C CB  . THR   D 1 300 ? 9.887   -12.789 74.439  1.00 17.92  ?  300 THR   D CB  1 
ATOM   13482 O OG1 . THR   D 1 300 ? 8.974   -11.888 75.077  1.00 17.16  ?  300 THR   D OG1 1 
ATOM   13483 C CG2 . THR   D 1 300 ? 10.227  -13.912 75.402  1.00 16.99  ?  300 THR   D CG2 1 
ATOM   13484 N N   . TYR   D 1 301 ? 11.418  -9.747  73.180  1.00 18.37  ?  301 TYR   D N   1 
ATOM   13485 C CA  . TYR   D 1 301 ? 11.381  -8.752  72.109  1.00 14.39  ?  301 TYR   D CA  1 
ATOM   13486 C C   . TYR   D 1 301 ? 12.679  -7.967  71.972  1.00 14.20  ?  301 TYR   D C   1 
ATOM   13487 O O   . TYR   D 1 301 ? 13.000  -7.540  70.856  1.00 18.67  ?  301 TYR   D O   1 
ATOM   13488 C CB  . TYR   D 1 301 ? 10.189  -7.772  72.281  1.00 15.17  ?  301 TYR   D CB  1 
ATOM   13489 C CG  . TYR   D 1 301 ? 10.299  -6.831  73.459  1.00 15.56  ?  301 TYR   D CG  1 
ATOM   13490 C CD1 . TYR   D 1 301 ? 11.008  -5.639  73.353  1.00 15.78  ?  301 TYR   D CD1 1 
ATOM   13491 C CD2 . TYR   D 1 301 ? 9.697   -7.133  74.680  1.00 17.82  ?  301 TYR   D CD2 1 
ATOM   13492 C CE1 . TYR   D 1 301 ? 11.142  -4.785  74.431  1.00 14.66  ?  301 TYR   D CE1 1 
ATOM   13493 C CE2 . TYR   D 1 301 ? 9.813   -6.274  75.766  1.00 17.82  ?  301 TYR   D CE2 1 
ATOM   13494 C CZ  . TYR   D 1 301 ? 10.544  -5.103  75.629  1.00 19.95  ?  301 TYR   D CZ  1 
ATOM   13495 O OH  . TYR   D 1 301 ? 10.684  -4.233  76.686  1.00 18.60  ?  301 TYR   D OH  1 
ATOM   13496 N N   . GLY   D 1 302 ? 13.443  -7.778  73.042  1.00 14.29  ?  302 GLY   D N   1 
ATOM   13497 C CA  . GLY   D 1 302 ? 14.818  -7.309  72.947  1.00 13.45  ?  302 GLY   D CA  1 
ATOM   13498 C C   . GLY   D 1 302 ? 14.961  -5.928  72.354  1.00 15.95  ?  302 GLY   D C   1 
ATOM   13499 O O   . GLY   D 1 302 ? 15.929  -5.659  71.628  1.00 18.29  ?  302 GLY   D O   1 
ATOM   13500 N N   . GLY   D 1 303 ? 14.014  -5.041  72.640  1.00 14.87  ?  303 GLY   D N   1 
ATOM   13501 C CA  . GLY   D 1 303 ? 14.053  -3.713  72.072  1.00 14.85  ?  303 GLY   D CA  1 
ATOM   13502 C C   . GLY   D 1 303 ? 13.469  -3.595  70.686  1.00 13.64  ?  303 GLY   D C   1 
ATOM   13503 O O   . GLY   D 1 303 ? 13.678  -2.564  70.034  1.00 14.09  ?  303 GLY   D O   1 
ATOM   13504 N N   . LEU   D 1 304 ? 12.756  -4.618  70.206  1.00 14.61  ?  304 LEU   D N   1 
ATOM   13505 C CA  . LEU   D 1 304 ? 12.084  -4.595  68.911  1.00 15.97  ?  304 LEU   D CA  1 
ATOM   13506 C C   . LEU   D 1 304 ? 10.575  -4.618  69.096  1.00 15.28  ?  304 LEU   D C   1 
ATOM   13507 O O   . LEU   D 1 304 ? 10.066  -5.293  69.993  1.00 17.80  ?  304 LEU   D O   1 
ATOM   13508 C CB  . LEU   D 1 304 ? 12.474  -5.797  68.055  1.00 13.98  ?  304 LEU   D CB  1 
ATOM   13509 C CG  . LEU   D 1 304 ? 13.921  -5.880  67.607  1.00 17.73  ?  304 LEU   D CG  1 
ATOM   13510 C CD1 . LEU   D 1 304 ? 14.167  -7.237  66.974  1.00 12.20  ?  304 LEU   D CD1 1 
ATOM   13511 C CD2 . LEU   D 1 304 ? 14.162  -4.757  66.613  1.00 18.11  ?  304 LEU   D CD2 1 
ATOM   13512 N N   . ALA   D 1 305 ? 9.859   -3.890  68.244  1.00 17.04  ?  305 ALA   D N   1 
ATOM   13513 C CA  . ALA   D 1 305 ? 8.433   -4.140  68.119  1.00 17.42  ?  305 ALA   D CA  1 
ATOM   13514 C C   . ALA   D 1 305 ? 8.209   -5.569  67.634  1.00 17.13  ?  305 ALA   D C   1 
ATOM   13515 O O   . ALA   D 1 305 ? 9.064   -6.167  66.977  1.00 14.32  ?  305 ALA   D O   1 
ATOM   13516 C CB  . ALA   D 1 305 ? 7.796   -3.147  67.146  1.00 17.18  ?  305 ALA   D CB  1 
ATOM   13517 N N   . GLY   D 1 306 ? 7.049   -6.129  67.969  1.00 18.09  ?  306 GLY   D N   1 
ATOM   13518 C CA  . GLY   D 1 306 ? 6.725   -7.448  67.455  1.00 15.70  ?  306 GLY   D CA  1 
ATOM   13519 C C   . GLY   D 1 306 ? 6.682   -7.487  65.941  1.00 17.17  ?  306 GLY   D C   1 
ATOM   13520 O O   . GLY   D 1 306 ? 7.042   -8.501  65.334  1.00 17.67  ?  306 GLY   D O   1 
ATOM   13521 N N   . ARG   D 1 307 ? 6.236   -6.391  65.309  1.00 15.02  ?  307 ARG   D N   1 
ATOM   13522 C CA  . ARG   D 1 307 ? 6.205   -6.338  63.852  1.00 16.30  ?  307 ARG   D CA  1 
ATOM   13523 C C   . ARG   D 1 307 ? 7.600   -6.461  63.261  1.00 14.96  ?  307 ARG   D C   1 
ATOM   13524 O O   . ARG   D 1 307 ? 7.761   -7.011  62.166  1.00 15.95  ?  307 ARG   D O   1 
ATOM   13525 C CB  . ARG   D 1 307 ? 5.533   -5.047  63.368  1.00 15.97  ?  307 ARG   D CB  1 
ATOM   13526 C CG  . ARG   D 1 307 ? 6.178   -3.767  63.857  1.00 18.51  ?  307 ARG   D CG  1 
ATOM   13527 C CD  . ARG   D 1 307 ? 5.597   -2.520  63.189  1.00 15.28  ?  307 ARG   D CD  1 
ATOM   13528 N NE  . ARG   D 1 307 ? 6.113   -1.324  63.847  1.00 16.44  ?  307 ARG   D NE  1 
ATOM   13529 C CZ  . ARG   D 1 307 ? 5.473   -0.658  64.801  1.00 16.43  ?  307 ARG   D CZ  1 
ATOM   13530 N NH1 . ARG   D 1 307 ? 4.249   -0.994  65.179  1.00 16.85  ?  307 ARG   D NH1 1 
ATOM   13531 N NH2 . ARG   D 1 307 ? 6.074   0.374   65.390  1.00 16.26  ?  307 ARG   D NH2 1 
ATOM   13532 N N   . ASP   D 1 308 ? 8.628   -5.997  63.975  1.00 17.73  ?  308 ASP   D N   1 
ATOM   13533 C CA  . ASP   D 1 308 ? 9.967   -6.084  63.408  1.00 16.57  ?  308 ASP   D CA  1 
ATOM   13534 C C   . ASP   D 1 308 ? 10.551  -7.478  63.562  1.00 14.94  ?  308 ASP   D C   1 
ATOM   13535 O O   . ASP   D 1 308 ? 11.273  -7.940  62.675  1.00 14.24  ?  308 ASP   D O   1 
ATOM   13536 C CB  . ASP   D 1 308 ? 10.873  -5.022  64.030  1.00 16.93  ?  308 ASP   D CB  1 
ATOM   13537 C CG  . ASP   D 1 308 ? 10.519  -3.629  63.552  1.00 19.70  ?  308 ASP   D CG  1 
ATOM   13538 O OD1 . ASP   D 1 308 ? 10.672  -3.364  62.341  1.00 24.75  ?  308 ASP   D OD1 1 
ATOM   13539 O OD2 . ASP   D 1 308 ? 10.037  -2.815  64.367  1.00 20.58  ?  308 ASP   D OD2 1 
ATOM   13540 N N   . MET   D 1 309 ? 10.225  -8.182  64.642  1.00 12.86  ?  309 MET   D N   1 
ATOM   13541 C CA  . MET   D 1 309 ? 10.584  -9.595  64.700  1.00 15.54  ?  309 MET   D CA  1 
ATOM   13542 C C   . MET   D 1 309 ? 9.869   -10.376 63.604  1.00 15.16  ?  309 MET   D C   1 
ATOM   13543 O O   . MET   D 1 309 ? 10.433  -11.316 63.036  1.00 14.76  ?  309 MET   D O   1 
ATOM   13544 C CB  . MET   D 1 309 ? 10.260  -10.177 66.082  1.00 14.14  ?  309 MET   D CB  1 
ATOM   13545 C CG  . MET   D 1 309 ? 11.236  -9.774  67.182  1.00 13.76  ?  309 MET   D CG  1 
ATOM   13546 S SD  . MET   D 1 309 ? 10.824  -10.557 68.740  1.00 16.00  ?  309 MET   D SD  1 
ATOM   13547 C CE  . MET   D 1 309 ? 9.164   -9.948  68.984  1.00 13.90  ?  309 MET   D CE  1 
ATOM   13548 N N   . ALA   D 1 310 ? 8.630   -9.990  63.284  1.00 12.97  ?  310 ALA   D N   1 
ATOM   13549 C CA  . ALA   D 1 310 ? 7.901   -10.645 62.201  1.00 11.43  ?  310 ALA   D CA  1 
ATOM   13550 C C   . ALA   D 1 310 ? 8.546   -10.364 60.847  1.00 13.11  ?  310 ALA   D C   1 
ATOM   13551 O O   . ALA   D 1 310 ? 8.600   -11.244 59.977  1.00 14.94  ?  310 ALA   D O   1 
ATOM   13552 C CB  . ALA   D 1 310 ? 6.443   -10.191 62.212  1.00 11.62  ?  310 ALA   D CB  1 
ATOM   13553 N N   . ALA   D 1 311 ? 9.031   -9.140  60.643  1.00 14.48  ?  311 ALA   D N   1 
ATOM   13554 C CA  . ALA   D 1 311 ? 9.730   -8.823  59.407  1.00 14.85  ?  311 ALA   D CA  1 
ATOM   13555 C C   . ALA   D 1 311 ? 11.068  -9.548  59.332  1.00 14.98  ?  311 ALA   D C   1 
ATOM   13556 O O   . ALA   D 1 311 ? 11.497  -9.939  58.243  1.00 15.73  ?  311 ALA   D O   1 
ATOM   13557 C CB  . ALA   D 1 311 ? 9.917   -7.311  59.291  1.00 14.24  ?  311 ALA   D CB  1 
ATOM   13558 N N   . MET   D 1 312 ? 11.719  -9.758  60.477  1.00 11.96  ?  312 MET   D N   1 
ATOM   13559 C CA  . MET   D 1 312 ? 12.997  -10.463 60.505  1.00 13.40  ?  312 MET   D CA  1 
ATOM   13560 C C   . MET   D 1 312 ? 12.835  -11.922 60.113  1.00 15.41  ?  312 MET   D C   1 
ATOM   13561 O O   . MET   D 1 312 ? 13.675  -12.467 59.389  1.00 15.95  ?  312 MET   D O   1 
ATOM   13562 C CB  . MET   D 1 312 ? 13.615  -10.361 61.898  1.00 12.38  ?  312 MET   D CB  1 
ATOM   13563 C CG  . MET   D 1 312 ? 15.076  -10.765 61.975  1.00 11.37  ?  312 MET   D CG  1 
ATOM   13564 S SD  . MET   D 1 312 ? 15.766  -10.479 63.605  1.00 17.05  ?  312 MET   D SD  1 
ATOM   13565 C CE  . MET   D 1 312 ? 15.395  -8.748  63.850  1.00 20.43  ?  312 MET   D CE  1 
ATOM   13566 N N   . VAL   D 1 313 ? 11.777  -12.577 60.603  1.00 13.82  ?  313 VAL   D N   1 
ATOM   13567 C CA  . VAL   D 1 313 ? 11.541  -13.974 60.246  1.00 17.11  ?  313 VAL   D CA  1 
ATOM   13568 C C   . VAL   D 1 313 ? 11.421  -14.116 58.739  1.00 17.70  ?  313 VAL   D C   1 
ATOM   13569 O O   . VAL   D 1 313 ? 12.014  -15.019 58.137  1.00 20.32  ?  313 VAL   D O   1 
ATOM   13570 C CB  . VAL   D 1 313 ? 10.289  -14.519 60.957  1.00 20.21  ?  313 VAL   D CB  1 
ATOM   13571 C CG1 . VAL   D 1 313 ? 9.928   -15.889 60.404  1.00 15.25  ?  313 VAL   D CG1 1 
ATOM   13572 C CG2 . VAL   D 1 313 ? 10.531  -14.607 62.456  1.00 19.59  ?  313 VAL   D CG2 1 
ATOM   13573 N N   . GLN   D 1 314 ? 10.670  -13.210 58.102  1.00 17.70  ?  314 GLN   D N   1 
ATOM   13574 C CA  . GLN   D 1 314 ? 10.515  -13.259 56.652  1.00 17.46  ?  314 GLN   D CA  1 
ATOM   13575 C C   . GLN   D 1 314 ? 11.786  -12.823 55.936  1.00 19.25  ?  314 GLN   D C   1 
ATOM   13576 O O   . GLN   D 1 314 ? 12.177  -13.432 54.934  1.00 22.01  ?  314 GLN   D O   1 
ATOM   13577 C CB  . GLN   D 1 314 ? 9.334   -12.390 56.221  1.00 15.73  ?  314 GLN   D CB  1 
ATOM   13578 C CG  . GLN   D 1 314 ? 9.110   -12.371 54.718  1.00 16.89  ?  314 GLN   D CG  1 
ATOM   13579 C CD  . GLN   D 1 314 ? 8.705   -13.720 54.175  1.00 18.01  ?  314 GLN   D CD  1 
ATOM   13580 O OE1 . GLN   D 1 314 ? 8.184   -14.557 54.899  1.00 20.74  ?  314 GLN   D OE1 1 
ATOM   13581 N NE2 . GLN   D 1 314 ? 8.944   -13.939 52.891  1.00 21.06  ?  314 GLN   D NE2 1 
ATOM   13582 N N   . GLY   D 1 315 ? 12.444  -11.773 56.428  1.00 17.55  ?  315 GLY   D N   1 
ATOM   13583 C CA  . GLY   D 1 315 ? 13.640  -11.285 55.762  1.00 16.80  ?  315 GLY   D CA  1 
ATOM   13584 C C   . GLY   D 1 315 ? 14.823  -12.222 55.886  1.00 18.87  ?  315 GLY   D C   1 
ATOM   13585 O O   . GLY   D 1 315 ? 15.704  -12.228 55.021  1.00 17.04  ?  315 GLY   D O   1 
ATOM   13586 N N   . LEU   D 1 316 ? 14.870  -13.020 56.960  1.00 18.26  ?  316 LEU   D N   1 
ATOM   13587 C CA  . LEU   D 1 316 ? 15.916  -14.031 57.065  1.00 20.90  ?  316 LEU   D CA  1 
ATOM   13588 C C   . LEU   D 1 316 ? 15.783  -15.077 55.968  1.00 20.96  ?  316 LEU   D C   1 
ATOM   13589 O O   . LEU   D 1 316 ? 16.796  -15.574 55.469  1.00 25.27  ?  316 LEU   D O   1 
ATOM   13590 C CB  . LEU   D 1 316 ? 15.894  -14.693 58.446  1.00 20.10  ?  316 LEU   D CB  1 
ATOM   13591 C CG  . LEU   D 1 316 ? 16.540  -13.889 59.584  1.00 16.10  ?  316 LEU   D CG  1 
ATOM   13592 C CD1 . LEU   D 1 316 ? 16.078  -14.392 60.939  1.00 14.68  ?  316 LEU   D CD1 1 
ATOM   13593 C CD2 . LEU   D 1 316 ? 18.068  -13.926 59.500  1.00 17.14  ?  316 LEU   D CD2 1 
ATOM   13594 N N   . GLU   D 1 317 ? 14.553  -15.400 55.560  1.00 18.71  ?  317 GLU   D N   1 
ATOM   13595 C CA  . GLU   D 1 317 ? 14.353  -16.356 54.472  1.00 21.85  ?  317 GLU   D CA  1 
ATOM   13596 C C   . GLU   D 1 317 ? 14.676  -15.736 53.113  1.00 23.23  ?  317 GLU   D C   1 
ATOM   13597 O O   . GLU   D 1 317 ? 15.412  -16.322 52.307  1.00 22.17  ?  317 GLU   D O   1 
ATOM   13598 C CB  . GLU   D 1 317 ? 12.916  -16.876 54.494  1.00 21.39  ?  317 GLU   D CB  1 
ATOM   13599 C CG  . GLU   D 1 317 ? 12.573  -17.787 53.319  1.00 25.35  ?  317 GLU   D CG  1 
ATOM   13600 C CD  . GLU   D 1 317 ? 13.276  -19.127 53.392  1.00 26.58  ?  317 GLU   D CD  1 
ATOM   13601 O OE1 . GLU   D 1 317 ? 13.728  -19.507 54.492  1.00 26.12  ?  317 GLU   D OE1 1 
ATOM   13602 O OE2 . GLU   D 1 317 ? 13.374  -19.807 52.350  1.00 30.54  ?  317 GLU   D OE2 1 
ATOM   13603 N N   . GLU   D 1 318 ? 14.133  -14.548 52.841  1.00 19.58  ?  318 GLU   D N   1 
ATOM   13604 C CA  . GLU   D 1 318 ? 14.369  -13.897 51.554  1.00 19.37  ?  318 GLU   D CA  1 
ATOM   13605 C C   . GLU   D 1 318 ? 15.842  -13.603 51.307  1.00 17.83  ?  318 GLU   D C   1 
ATOM   13606 O O   . GLU   D 1 318 ? 16.282  -13.570 50.153  1.00 20.41  ?  318 GLU   D O   1 
ATOM   13607 C CB  . GLU   D 1 318 ? 13.576  -12.602 51.483  1.00 22.05  ?  318 GLU   D CB  1 
ATOM   13608 C CG  . GLU   D 1 318 ? 12.092  -12.793 51.630  1.00 21.23  ?  318 GLU   D CG  1 
ATOM   13609 C CD  . GLU   D 1 318 ? 11.339  -11.521 51.338  1.00 20.26  ?  318 GLU   D CD  1 
ATOM   13610 O OE1 . GLU   D 1 318 ? 11.979  -10.560 50.857  1.00 21.24  ?  318 GLU   D OE1 1 
ATOM   13611 O OE2 . GLU   D 1 318 ? 10.116  -11.479 51.577  1.00 19.76  ?  318 GLU   D OE2 1 
ATOM   13612 N N   . GLY   D 1 319 ? 16.610  -13.344 52.361  1.00 19.38  ?  319 GLY   D N   1 
ATOM   13613 C CA  . GLY   D 1 319 ? 18.028  -13.055 52.202  1.00 17.65  ?  319 GLY   D CA  1 
ATOM   13614 C C   . GLY   D 1 319 ? 18.888  -14.258 51.876  1.00 17.70  ?  319 GLY   D C   1 
ATOM   13615 O O   . GLY   D 1 319 ? 20.051  -14.080 51.491  1.00 16.61  ?  319 GLY   D O   1 
ATOM   13616 N N   . THR   D 1 320 ? 18.358  -15.472 52.023  1.00 19.50  ?  320 THR   D N   1 
ATOM   13617 C CA  . THR   D 1 320 ? 19.092  -16.662 51.610  1.00 22.06  ?  320 THR   D CA  1 
ATOM   13618 C C   . THR   D 1 320 ? 18.844  -17.031 50.153  1.00 20.88  ?  320 THR   D C   1 
ATOM   13619 O O   . THR   D 1 320 ? 19.522  -17.924 49.635  1.00 21.18  ?  320 THR   D O   1 
ATOM   13620 C CB  . THR   D 1 320 ? 18.733  -17.867 52.498  1.00 21.96  ?  320 THR   D CB  1 
ATOM   13621 O OG1 . THR   D 1 320 ? 17.396  -18.297 52.214  1.00 24.23  ?  320 THR   D OG1 1 
ATOM   13622 C CG2 . THR   D 1 320 ? 18.838  -17.512 53.972  1.00 19.06  ?  320 THR   D CG2 1 
ATOM   13623 N N   . GLU   D 1 321 ? 17.901  -16.372 49.479  1.00 19.57  ?  321 GLU   D N   1 
ATOM   13624 C CA  . GLU   D 1 321 ? 17.506  -16.792 48.138  1.00 24.73  ?  321 GLU   D CA  1 
ATOM   13625 C C   . GLU   D 1 321 ? 18.622  -16.491 47.140  1.00 27.46  ?  321 GLU   D C   1 
ATOM   13626 O O   . GLU   D 1 321 ? 19.062  -15.342 47.004  1.00 27.22  ?  321 GLU   D O   1 
ATOM   13627 C CB  . GLU   D 1 321 ? 16.193  -16.122 47.736  1.00 21.14  ?  321 GLU   D CB  1 
ATOM   13628 C CG  . GLU   D 1 321 ? 15.009  -16.693 48.535  1.00 24.59  ?  321 GLU   D CG  1 
ATOM   13629 C CD  . GLU   D 1 321 ? 13.666  -16.060 48.217  1.00 28.20  ?  321 GLU   D CD  1 
ATOM   13630 O OE1 . GLU   D 1 321 ? 13.588  -15.182 47.328  1.00 31.37  ?  321 GLU   D OE1 1 
ATOM   13631 O OE2 . GLU   D 1 321 ? 12.674  -16.451 48.871  1.00 28.63  ?  321 GLU   D OE2 1 
ATOM   13632 N N   . GLU   D 1 322 ? 19.087  -17.538 46.454  1.00 24.28  ?  322 GLU   D N   1 
ATOM   13633 C CA  . GLU   D 1 322 ? 20.266  -17.413 45.604  1.00 23.90  ?  322 GLU   D CA  1 
ATOM   13634 C C   . GLU   D 1 322 ? 20.023  -16.475 44.429  1.00 21.83  ?  322 GLU   D C   1 
ATOM   13635 O O   . GLU   D 1 322 ? 20.919  -15.718 44.041  1.00 22.32  ?  322 GLU   D O   1 
ATOM   13636 C CB  . GLU   D 1 322 ? 20.696  -18.787 45.102  1.00 26.19  ?  322 GLU   D CB  1 
ATOM   13637 C CG  . GLU   D 1 322 ? 21.855  -18.739 44.142  1.00 27.53  ?  322 GLU   D CG  1 
ATOM   13638 C CD  . GLU   D 1 322 ? 22.412  -20.109 43.853  1.00 37.06  ?  322 GLU   D CD  1 
ATOM   13639 O OE1 . GLU   D 1 322 ? 21.982  -21.070 44.528  1.00 36.28  ?  322 GLU   D OE1 1 
ATOM   13640 O OE2 . GLU   D 1 322 ? 23.279  -20.224 42.958  1.00 42.27  ?  322 GLU   D OE2 1 
ATOM   13641 N N   . GLU   D 1 323 ? 18.821  -16.500 43.852  1.00 26.70  ?  323 GLU   D N   1 
ATOM   13642 C CA  . GLU   D 1 323 ? 18.574  -15.637 42.703  1.00 28.87  ?  323 GLU   D CA  1 
ATOM   13643 C C   . GLU   D 1 323 ? 18.592  -14.159 43.097  1.00 25.41  ?  323 GLU   D C   1 
ATOM   13644 O O   . GLU   D 1 323 ? 19.048  -13.323 42.311  1.00 23.12  ?  323 GLU   D O   1 
ATOM   13645 C CB  . GLU   D 1 323 ? 17.266  -16.039 42.003  1.00 29.25  ?  323 GLU   D CB  1 
ATOM   13646 C CG  . GLU   D 1 323 ? 15.982  -15.885 42.804  1.00 34.65  ?  323 GLU   D CG  1 
ATOM   13647 C CD  . GLU   D 1 323 ? 15.651  -17.069 43.726  1.00 42.33  ?  323 GLU   D CD  1 
ATOM   13648 O OE1 . GLU   D 1 323 ? 16.560  -17.871 44.068  1.00 35.29  ?  323 GLU   D OE1 1 
ATOM   13649 O OE2 . GLU   D 1 323 ? 14.458  -17.178 44.114  1.00 36.61  ?  323 GLU   D OE2 1 
ATOM   13650 N N   . TYR   D 1 324 ? 18.150  -13.822 44.314  1.00 26.25  ?  324 TYR   D N   1 
ATOM   13651 C CA  . TYR   D 1 324 ? 18.286  -12.446 44.795  1.00 23.63  ?  324 TYR   D CA  1 
ATOM   13652 C C   . TYR   D 1 324 ? 19.751  -12.093 45.041  1.00 21.54  ?  324 TYR   D C   1 
ATOM   13653 O O   . TYR   D 1 324 ? 20.231  -11.039 44.606  1.00 23.10  ?  324 TYR   D O   1 
ATOM   13654 C CB  . TYR   D 1 324 ? 17.457  -12.233 46.073  1.00 25.39  ?  324 TYR   D CB  1 
ATOM   13655 C CG  . TYR   D 1 324 ? 18.109  -11.241 47.014  1.00 21.59  ?  324 TYR   D CG  1 
ATOM   13656 C CD1 . TYR   D 1 324 ? 18.065  -9.875  46.752  1.00 22.94  ?  324 TYR   D CD1 1 
ATOM   13657 C CD2 . TYR   D 1 324 ? 18.805  -11.670 48.139  1.00 19.79  ?  324 TYR   D CD2 1 
ATOM   13658 C CE1 . TYR   D 1 324 ? 18.687  -8.969  47.587  1.00 21.84  ?  324 TYR   D CE1 1 
ATOM   13659 C CE2 . TYR   D 1 324 ? 19.426  -10.771 48.977  1.00 17.78  ?  324 TYR   D CE2 1 
ATOM   13660 C CZ  . TYR   D 1 324 ? 19.363  -9.420  48.690  1.00 19.62  ?  324 TYR   D CZ  1 
ATOM   13661 O OH  . TYR   D 1 324 ? 19.981  -8.510  49.513  1.00 23.80  ?  324 TYR   D OH  1 
ATOM   13662 N N   . LEU   D 1 325 ? 20.478  -12.965 45.747  1.00 20.79  ?  325 LEU   D N   1 
ATOM   13663 C CA  . LEU   D 1 325 ? 21.880  -12.695 46.060  1.00 23.56  ?  325 LEU   D CA  1 
ATOM   13664 C C   . LEU   D 1 325 ? 22.715  -12.512 44.798  1.00 24.10  ?  325 LEU   D C   1 
ATOM   13665 O O   . LEU   D 1 325 ? 23.595  -11.644 44.744  1.00 20.13  ?  325 LEU   D O   1 
ATOM   13666 C CB  . LEU   D 1 325 ? 22.445  -13.833 46.907  1.00 21.68  ?  325 LEU   D CB  1 
ATOM   13667 C CG  . LEU   D 1 325 ? 21.990  -13.826 48.364  1.00 21.33  ?  325 LEU   D CG  1 
ATOM   13668 C CD1 . LEU   D 1 325 ? 22.176  -15.194 48.993  1.00 19.22  ?  325 LEU   D CD1 1 
ATOM   13669 C CD2 . LEU   D 1 325 ? 22.781  -12.764 49.109  1.00 22.42  ?  325 LEU   D CD2 1 
ATOM   13670 N N   . HIS   D 1 326 ? 22.470  -13.334 43.776  1.00 26.99  ?  326 HIS   D N   1 
ATOM   13671 C CA  . HIS   D 1 326 ? 23.192  -13.181 42.517  1.00 25.08  ?  326 HIS   D CA  1 
ATOM   13672 C C   . HIS   D 1 326 ? 22.956  -11.799 41.921  1.00 23.64  ?  326 HIS   D C   1 
ATOM   13673 O O   . HIS   D 1 326 ? 23.900  -11.134 41.473  1.00 21.63  ?  326 HIS   D O   1 
ATOM   13674 C CB  . HIS   D 1 326 ? 22.765  -14.277 41.546  1.00 22.16  ?  326 HIS   D CB  1 
ATOM   13675 C CG  . HIS   D 1 326 ? 23.223  -14.045 40.143  1.00 28.73  ?  326 HIS   D CG  1 
ATOM   13676 N ND1 . HIS   D 1 326 ? 24.534  -14.200 39.756  1.00 30.91  ?  326 HIS   D ND1 1 
ATOM   13677 C CD2 . HIS   D 1 326 ? 22.543  -13.667 39.035  1.00 27.56  ?  326 HIS   D CD2 1 
ATOM   13678 C CE1 . HIS   D 1 326 ? 24.645  -13.930 38.467  1.00 30.89  ?  326 HIS   D CE1 1 
ATOM   13679 N NE2 . HIS   D 1 326 ? 23.450  -13.605 38.005  1.00 27.42  ?  326 HIS   D NE2 1 
ATOM   13680 N N   . TYR   D 1 327 ? 21.696  -11.345 41.927  1.00 23.44  ?  327 TYR   D N   1 
ATOM   13681 C CA  A TYR   D 1 327 ? 21.384  -10.001 41.451  0.59 22.32  ?  327 TYR   D CA  1 
ATOM   13682 C CA  B TYR   D 1 327 ? 21.384  -10.001 41.451  0.41 22.32  ?  327 TYR   D CA  1 
ATOM   13683 C C   . TYR   D 1 327 ? 22.042  -8.943  42.323  1.00 22.54  ?  327 TYR   D C   1 
ATOM   13684 O O   . TYR   D 1 327 ? 22.611  -7.972  41.814  1.00 23.39  ?  327 TYR   D O   1 
ATOM   13685 C CB  A TYR   D 1 327 ? 19.869  -9.786  41.428  0.59 22.66  ?  327 TYR   D CB  1 
ATOM   13686 C CB  B TYR   D 1 327 ? 19.870  -9.785  41.428  0.41 22.64  ?  327 TYR   D CB  1 
ATOM   13687 C CG  A TYR   D 1 327 ? 19.455  -8.416  41.940  0.59 22.30  ?  327 TYR   D CG  1 
ATOM   13688 C CG  B TYR   D 1 327 ? 19.485  -8.317  41.386  0.41 22.49  ?  327 TYR   D CG  1 
ATOM   13689 C CD1 A TYR   D 1 327 ? 19.501  -7.298  41.112  0.59 21.70  ?  327 TYR   D CD1 1 
ATOM   13690 C CD1 B TYR   D 1 327 ? 19.401  -7.642  40.182  0.41 22.07  ?  327 TYR   D CD1 1 
ATOM   13691 C CD2 A TYR   D 1 327 ? 19.032  -8.240  43.253  0.59 21.73  ?  327 TYR   D CD2 1 
ATOM   13692 C CD2 B TYR   D 1 327 ? 19.221  -7.606  42.553  0.41 21.25  ?  327 TYR   D CD2 1 
ATOM   13693 C CE1 A TYR   D 1 327 ? 19.138  -6.048  41.579  0.59 21.91  ?  327 TYR   D CE1 1 
ATOM   13694 C CE1 B TYR   D 1 327 ? 19.064  -6.305  40.132  0.41 22.04  ?  327 TYR   D CE1 1 
ATOM   13695 C CE2 A TYR   D 1 327 ? 18.669  -6.992  43.729  0.59 22.73  ?  327 TYR   D CE2 1 
ATOM   13696 C CE2 B TYR   D 1 327 ? 18.887  -6.266  42.513  0.41 20.66  ?  327 TYR   D CE2 1 
ATOM   13697 C CZ  A TYR   D 1 327 ? 18.722  -5.899  42.887  0.59 20.35  ?  327 TYR   D CZ  1 
ATOM   13698 C CZ  B TYR   D 1 327 ? 18.808  -5.622  41.298  0.41 22.10  ?  327 TYR   D CZ  1 
ATOM   13699 O OH  A TYR   D 1 327 ? 18.351  -4.658  43.363  0.59 17.52  ?  327 TYR   D OH  1 
ATOM   13700 O OH  B TYR   D 1 327 ? 18.469  -4.287  41.245  0.41 21.37  ?  327 TYR   D OH  1 
ATOM   13701 N N   . ARG   D 1 328 ? 21.938  -9.101  43.647  1.00 21.51  ?  328 ARG   D N   1 
ATOM   13702 C CA  . ARG   D 1 328 ? 22.441  -8.098  44.578  1.00 19.55  ?  328 ARG   D CA  1 
ATOM   13703 C C   . ARG   D 1 328 ? 23.935  -7.905  44.389  1.00 20.99  ?  328 ARG   D C   1 
ATOM   13704 O O   . ARG   D 1 328 ? 24.409  -6.797  44.112  1.00 20.34  ?  328 ARG   D O   1 
ATOM   13705 C CB  . ARG   D 1 328 ? 22.104  -8.530  46.013  1.00 21.37  ?  328 ARG   D CB  1 
ATOM   13706 C CG  . ARG   D 1 328 ? 22.306  -7.485  47.128  1.00 20.43  ?  328 ARG   D CG  1 
ATOM   13707 C CD  . ARG   D 1 328 ? 23.780  -7.328  47.531  1.00 20.03  ?  328 ARG   D CD  1 
ATOM   13708 N NE  . ARG   D 1 328 ? 23.953  -6.587  48.773  1.00 19.05  ?  328 ARG   D NE  1 
ATOM   13709 C CZ  . ARG   D 1 328 ? 23.865  -5.268  48.891  1.00 18.50  ?  328 ARG   D CZ  1 
ATOM   13710 N NH1 . ARG   D 1 328 ? 23.510  -4.502  47.874  1.00 18.13  ?  328 ARG   D NH1 1 
ATOM   13711 N NH2 . ARG   D 1 328 ? 24.150  -4.702  50.060  1.00 19.97  ?  328 ARG   D NH2 1 
ATOM   13712 N N   . ILE   D 1 329 ? 24.692  -8.991  44.533  1.00 22.94  ?  329 ILE   D N   1 
ATOM   13713 C CA  . ILE   D 1 329 ? 26.142  -8.922  44.438  1.00 23.97  ?  329 ILE   D CA  1 
ATOM   13714 C C   . ILE   D 1 329 ? 26.576  -8.598  43.009  1.00 23.92  ?  329 ILE   D C   1 
ATOM   13715 O O   . ILE   D 1 329 ? 27.587  -7.917  42.795  1.00 25.25  ?  329 ILE   D O   1 
ATOM   13716 C CB  . ILE   D 1 329 ? 26.722  -10.245 44.975  1.00 27.63  ?  329 ILE   D CB  1 
ATOM   13717 C CG1 . ILE   D 1 329 ? 26.323  -10.406 46.452  1.00 27.89  ?  329 ILE   D CG1 1 
ATOM   13718 C CG2 . ILE   D 1 329 ? 28.232  -10.312 44.773  1.00 29.13  ?  329 ILE   D CG2 1 
ATOM   13719 C CD1 . ILE   D 1 329 ? 26.548  -11.809 47.049  1.00 22.60  ?  329 ILE   D CD1 1 
ATOM   13720 N N   . GLY   D 1 330 ? 25.807  -9.037  42.012  1.00 24.58  ?  330 GLY   D N   1 
ATOM   13721 C CA  . GLY   D 1 330 ? 26.103  -8.646  40.644  1.00 22.04  ?  330 GLY   D CA  1 
ATOM   13722 C C   . GLY   D 1 330 ? 25.941  -7.155  40.414  1.00 21.90  ?  330 GLY   D C   1 
ATOM   13723 O O   . GLY   D 1 330 ? 26.698  -6.553  39.649  1.00 24.13  ?  330 GLY   D O   1 
ATOM   13724 N N   . GLN   D 1 331 ? 24.943  -6.540  41.053  1.00 24.10  ?  331 GLN   D N   1 
ATOM   13725 C CA  . GLN   D 1 331 ? 24.781  -5.099  40.898  1.00 20.41  ?  331 GLN   D CA  1 
ATOM   13726 C C   . GLN   D 1 331 ? 25.967  -4.355  41.495  1.00 22.23  ?  331 GLN   D C   1 
ATOM   13727 O O   . GLN   D 1 331 ? 26.464  -3.385  40.914  1.00 24.99  ?  331 GLN   D O   1 
ATOM   13728 C CB  . GLN   D 1 331 ? 23.480  -4.636  41.539  1.00 19.68  ?  331 GLN   D CB  1 
ATOM   13729 C CG  . GLN   D 1 331 ? 23.444  -3.142  41.743  1.00 22.52  ?  331 GLN   D CG  1 
ATOM   13730 C CD  . GLN   D 1 331 ? 22.126  -2.652  42.279  1.00 23.04  ?  331 GLN   D CD  1 
ATOM   13731 O OE1 . GLN   D 1 331 ? 21.913  -2.593  43.492  1.00 21.02  ?  331 GLN   D OE1 1 
ATOM   13732 N NE2 . GLN   D 1 331 ? 21.232  -2.282  41.377  1.00 22.05  ?  331 GLN   D NE2 1 
ATOM   13733 N N   . VAL   D 1 332 ? 26.434  -4.799  42.657  1.00 21.64  ?  332 VAL   D N   1 
ATOM   13734 C CA  . VAL   D 1 332 ? 27.650  -4.234  43.232  1.00 22.63  ?  332 VAL   D CA  1 
ATOM   13735 C C   . VAL   D 1 332 ? 28.828  -4.444  42.292  1.00 24.17  ?  332 VAL   D C   1 
ATOM   13736 O O   . VAL   D 1 332 ? 29.620  -3.525  42.046  1.00 23.69  ?  332 VAL   D O   1 
ATOM   13737 C CB  . VAL   D 1 332 ? 27.909  -4.854  44.614  1.00 20.54  ?  332 VAL   D CB  1 
ATOM   13738 C CG1 . VAL   D 1 332 ? 29.290  -4.466  45.114  1.00 29.10  ?  332 VAL   D CG1 1 
ATOM   13739 C CG2 . VAL   D 1 332 ? 26.829  -4.430  45.605  1.00 22.43  ?  332 VAL   D CG2 1 
ATOM   13740 N N   . LYS   D 1 333 ? 28.952  -5.655  41.739  1.00 24.43  ?  333 LYS   D N   1 
ATOM   13741 C CA  . LYS   D 1 333 ? 30.041  -5.956  40.815  1.00 24.78  ?  333 LYS   D CA  1 
ATOM   13742 C C   . LYS   D 1 333 ? 29.940  -5.123  39.548  1.00 24.41  ?  333 LYS   D C   1 
ATOM   13743 O O   . LYS   D 1 333 ? 30.965  -4.717  38.985  1.00 28.18  ?  333 LYS   D O   1 
ATOM   13744 C CB  . LYS   D 1 333 ? 30.023  -7.446  40.471  1.00 29.26  ?  333 LYS   D CB  1 
ATOM   13745 C CG  . LYS   D 1 333 ? 31.184  -7.910  39.613  1.00 30.48  ?  333 LYS   D CG  1 
ATOM   13746 C CD  . LYS   D 1 333 ? 30.985  -9.341  39.139  1.00 25.09  ?  333 LYS   D CD  1 
ATOM   13747 C CE  . LYS   D 1 333 ? 32.219  -9.836  38.379  1.00 29.71  ?  333 LYS   D CE  1 
ATOM   13748 N NZ  . LYS   D 1 333 ? 32.504  -8.988  37.193  1.00 29.35  ?  333 LYS   D NZ  1 
ATOM   13749 N N   . TYR   D 1 334 ? 28.715  -4.855  39.090  1.00 24.13  ?  334 TYR   D N   1 
ATOM   13750 C CA  . TYR   D 1 334 ? 28.518  -4.018  37.912  1.00 25.95  ?  334 TYR   D CA  1 
ATOM   13751 C C   . TYR   D 1 334 ? 29.053  -2.609  38.145  1.00 24.34  ?  334 TYR   D C   1 
ATOM   13752 O O   . TYR   D 1 334 ? 29.754  -2.050  37.295  1.00 24.93  ?  334 TYR   D O   1 
ATOM   13753 C CB  . TYR   D 1 334 ? 27.031  -3.988  37.542  1.00 21.35  ?  334 TYR   D CB  1 
ATOM   13754 C CG  . TYR   D 1 334 ? 26.690  -2.998  36.457  1.00 25.20  ?  334 TYR   D CG  1 
ATOM   13755 C CD1 . TYR   D 1 334 ? 26.883  -3.318  35.113  1.00 23.80  ?  334 TYR   D CD1 1 
ATOM   13756 C CD2 . TYR   D 1 334 ? 26.172  -1.743  36.763  1.00 24.93  ?  334 TYR   D CD2 1 
ATOM   13757 C CE1 . TYR   D 1 334 ? 26.589  -2.415  34.109  1.00 23.13  ?  334 TYR   D CE1 1 
ATOM   13758 C CE2 . TYR   D 1 334 ? 25.859  -0.829  35.746  1.00 25.23  ?  334 TYR   D CE2 1 
ATOM   13759 C CZ  . TYR   D 1 334 ? 26.068  -1.178  34.426  1.00 26.80  ?  334 TYR   D CZ  1 
ATOM   13760 O OH  . TYR   D 1 334 ? 25.769  -0.294  33.409  1.00 22.54  ?  334 TYR   D OH  1 
ATOM   13761 N N   . LEU   D 1 335 ? 28.730  -2.018  39.297  1.00 24.97  ?  335 LEU   D N   1 
ATOM   13762 C CA  . LEU   D 1 335 ? 29.252  -0.691  39.607  1.00 23.78  ?  335 LEU   D CA  1 
ATOM   13763 C C   . LEU   D 1 335 ? 30.776  -0.696  39.629  1.00 28.31  ?  335 LEU   D C   1 
ATOM   13764 O O   . LEU   D 1 335 ? 31.420  0.217   39.091  1.00 24.99  ?  335 LEU   D O   1 
ATOM   13765 C CB  . LEU   D 1 335 ? 28.685  -0.210  40.945  1.00 22.72  ?  335 LEU   D CB  1 
ATOM   13766 C CG  . LEU   D 1 335 ? 29.246  1.097   41.504  1.00 23.58  ?  335 LEU   D CG  1 
ATOM   13767 C CD1 . LEU   D 1 335 ? 29.178  2.195   40.465  1.00 24.11  ?  335 LEU   D CD1 1 
ATOM   13768 C CD2 . LEU   D 1 335 ? 28.514  1.516   42.775  1.00 23.28  ?  335 LEU   D CD2 1 
ATOM   13769 N N   . GLY   D 1 336 ? 31.371  -1.726  40.239  1.00 26.61  ?  336 GLY   D N   1 
ATOM   13770 C CA  . GLY   D 1 336 ? 32.822  -1.807  40.287  1.00 28.76  ?  336 GLY   D CA  1 
ATOM   13771 C C   . GLY   D 1 336 ? 33.442  -1.936  38.911  1.00 28.35  ?  336 GLY   D C   1 
ATOM   13772 O O   . GLY   D 1 336 ? 34.464  -1.309  38.618  1.00 31.07  ?  336 GLY   D O   1 
ATOM   13773 N N   . ASP   D 1 337 ? 32.830  -2.742  38.043  1.00 31.91  ?  337 ASP   D N   1 
ATOM   13774 C CA  . ASP   D 1 337 ? 33.371  -2.917  36.698  1.00 29.54  ?  337 ASP   D CA  1 
ATOM   13775 C C   . ASP   D 1 337 ? 33.269  -1.638  35.882  1.00 29.20  ?  337 ASP   D C   1 
ATOM   13776 O O   . ASP   D 1 337 ? 34.193  -1.307  35.135  1.00 32.53  ?  337 ASP   D O   1 
ATOM   13777 C CB  . ASP   D 1 337 ? 32.660  -4.061  35.982  1.00 27.86  ?  337 ASP   D CB  1 
ATOM   13778 C CG  . ASP   D 1 337 ? 33.078  -5.415  36.508  1.00 32.17  ?  337 ASP   D CG  1 
ATOM   13779 O OD1 . ASP   D 1 337 ? 34.163  -5.500  37.129  1.00 31.54  ?  337 ASP   D OD1 1 
ATOM   13780 O OD2 . ASP   D 1 337 ? 32.327  -6.392  36.290  1.00 27.86  ?  337 ASP   D OD2 1 
ATOM   13781 N N   . ARG   D 1 338 ? 32.153  -0.913  35.990  1.00 29.06  ?  338 ARG   D N   1 
ATOM   13782 C CA  . ARG   D 1 338 ? 32.071  0.390   35.337  1.00 27.97  ?  338 ARG   D CA  1 
ATOM   13783 C C   . ARG   D 1 338 ? 33.222  1.282   35.781  1.00 31.32  ?  338 ARG   D C   1 
ATOM   13784 O O   . ARG   D 1 338 ? 33.815  2.002   34.969  1.00 33.85  ?  338 ARG   D O   1 
ATOM   13785 C CB  . ARG   D 1 338 ? 30.733  1.068   35.652  1.00 29.43  ?  338 ARG   D CB  1 
ATOM   13786 C CG  . ARG   D 1 338 ? 29.498  0.449   35.002  1.00 29.05  ?  338 ARG   D CG  1 
ATOM   13787 C CD  . ARG   D 1 338 ? 29.388  0.770   33.504  1.00 33.21  ?  338 ARG   D CD  1 
ATOM   13788 N NE  . ARG   D 1 338 ? 30.076  1.999   33.126  1.00 33.37  ?  338 ARG   D NE  1 
ATOM   13789 C CZ  . ARG   D 1 338 ? 29.550  3.217   33.166  1.00 35.05  ?  338 ARG   D CZ  1 
ATOM   13790 N NH1 . ARG   D 1 338 ? 28.318  3.427   33.596  1.00 35.42  ?  338 ARG   D NH1 1 
ATOM   13791 N NH2 . ARG   D 1 338 ? 30.282  4.254   32.759  1.00 37.08  ?  338 ARG   D NH2 1 
ATOM   13792 N N   . LEU   D 1 339 ? 33.570  1.225   37.069  1.00 33.37  ?  339 LEU   D N   1 
ATOM   13793 C CA  . LEU   D 1 339 ? 34.621  2.092   37.589  1.00 32.68  ?  339 LEU   D CA  1 
ATOM   13794 C C   . LEU   D 1 339 ? 35.998  1.646   37.107  1.00 35.83  ?  339 LEU   D C   1 
ATOM   13795 O O   . LEU   D 1 339 ? 36.777  2.459   36.596  1.00 39.90  ?  339 LEU   D O   1 
ATOM   13796 C CB  . LEU   D 1 339 ? 34.556  2.132   39.116  1.00 30.54  ?  339 LEU   D CB  1 
ATOM   13797 C CG  . LEU   D 1 339 ? 33.339  2.891   39.655  1.00 30.48  ?  339 LEU   D CG  1 
ATOM   13798 C CD1 . LEU   D 1 339 ? 33.219  2.764   41.166  1.00 28.19  ?  339 LEU   D CD1 1 
ATOM   13799 C CD2 . LEU   D 1 339 ? 33.393  4.352   39.245  1.00 30.72  ?  339 LEU   D CD2 1 
ATOM   13800 N N   . ARG   D 1 340 ? 36.324  0.360   37.252  1.00 31.33  ?  340 ARG   D N   1 
ATOM   13801 C CA  . ARG   D 1 340 ? 37.678  -0.038  36.897  1.00 34.76  ?  340 ARG   D CA  1 
ATOM   13802 C C   . ARG   D 1 340 ? 37.853  -0.172  35.390  1.00 39.20  ?  340 ARG   D C   1 
ATOM   13803 O O   . ARG   D 1 340 ? 38.970  0.005   34.889  1.00 40.02  ?  340 ARG   D O   1 
ATOM   13804 C CB  . ARG   D 1 340 ? 38.077  -1.329  37.618  1.00 33.53  ?  340 ARG   D CB  1 
ATOM   13805 C CG  . ARG   D 1 340 ? 37.494  -2.598  37.061  1.00 36.55  ?  340 ARG   D CG  1 
ATOM   13806 C CD  . ARG   D 1 340 ? 37.777  -3.765  38.002  1.00 40.90  ?  340 ARG   D CD  1 
ATOM   13807 N NE  . ARG   D 1 340 ? 39.192  -4.115  38.067  1.00 37.29  ?  340 ARG   D NE  1 
ATOM   13808 C CZ  . ARG   D 1 340 ? 39.753  -5.091  37.366  1.00 40.75  ?  340 ARG   D CZ  1 
ATOM   13809 N NH1 . ARG   D 1 340 ? 39.057  -5.811  36.501  1.00 37.92  ?  340 ARG   D NH1 1 
ATOM   13810 N NH2 . ARG   D 1 340 ? 41.046  -5.351  37.537  1.00 45.52  ?  340 ARG   D NH2 1 
ATOM   13811 N N   . GLU   D 1 341 ? 36.780  -0.452  34.642  1.00 32.66  ?  341 GLU   D N   1 
ATOM   13812 C CA  . GLU   D 1 341 ? 36.890  -0.341  33.191  1.00 32.87  ?  341 GLU   D CA  1 
ATOM   13813 C C   . GLU   D 1 341 ? 37.212  1.085   32.765  1.00 38.81  ?  341 GLU   D C   1 
ATOM   13814 O O   . GLU   D 1 341 ? 37.697  1.294   31.650  1.00 36.67  ?  341 GLU   D O   1 
ATOM   13815 C CB  . GLU   D 1 341 ? 35.610  -0.803  32.495  1.00 35.27  ?  341 GLU   D CB  1 
ATOM   13816 C CG  . GLU   D 1 341 ? 35.343  -2.306  32.541  1.00 36.89  ?  341 GLU   D CG  1 
ATOM   13817 C CD  . GLU   D 1 341 ? 33.917  -2.658  32.124  1.00 35.18  ?  341 GLU   D CD  1 
ATOM   13818 O OE1 . GLU   D 1 341 ? 33.299  -1.880  31.366  1.00 42.22  ?  341 GLU   D OE1 1 
ATOM   13819 O OE2 . GLU   D 1 341 ? 33.404  -3.710  32.559  1.00 33.29  ?  341 GLU   D OE2 1 
ATOM   13820 N N   . ALA   D 1 342 ? 36.954  2.068   33.627  1.00 33.77  ?  342 ALA   D N   1 
ATOM   13821 C CA  . ALA   D 1 342 ? 37.292  3.458   33.362  1.00 35.02  ?  342 ALA   D CA  1 
ATOM   13822 C C   . ALA   D 1 342 ? 38.606  3.872   34.012  1.00 42.38  ?  342 ALA   D C   1 
ATOM   13823 O O   . ALA   D 1 342 ? 38.962  5.054   33.970  1.00 45.94  ?  342 ALA   D O   1 
ATOM   13824 C CB  . ALA   D 1 342 ? 36.160  4.375   33.828  1.00 32.57  ?  342 ALA   D CB  1 
ATOM   13825 N N   . GLY   D 1 343 ? 39.331  2.928   34.612  1.00 36.31  ?  343 GLY   D N   1 
ATOM   13826 C CA  . GLY   D 1 343 ? 40.635  3.222   35.171  1.00 39.99  ?  343 GLY   D CA  1 
ATOM   13827 C C   . GLY   D 1 343 ? 40.615  3.786   36.569  1.00 45.97  ?  343 GLY   D C   1 
ATOM   13828 O O   . GLY   D 1 343 ? 41.567  4.464   36.966  1.00 46.34  ?  343 GLY   D O   1 
ATOM   13829 N N   . ILE   D 1 344 ? 39.554  3.540   37.327  1.00 42.66  ?  344 ILE   D N   1 
ATOM   13830 C CA  . ILE   D 1 344 ? 39.456  3.976   38.716  1.00 40.02  ?  344 ILE   D CA  1 
ATOM   13831 C C   . ILE   D 1 344 ? 39.793  2.784   39.604  1.00 43.64  ?  344 ILE   D C   1 
ATOM   13832 O O   . ILE   D 1 344 ? 39.166  1.724   39.459  1.00 44.96  ?  344 ILE   D O   1 
ATOM   13833 C CB  . ILE   D 1 344 ? 38.064  4.538   39.034  1.00 40.92  ?  344 ILE   D CB  1 
ATOM   13834 C CG1 . ILE   D 1 344 ? 37.884  5.886   38.328  1.00 40.03  ?  344 ILE   D CG1 1 
ATOM   13835 C CG2 . ILE   D 1 344 ? 37.874  4.667   40.537  1.00 40.69  ?  344 ILE   D CG2 1 
ATOM   13836 C CD1 . ILE   D 1 344 ? 36.564  6.548   38.592  1.00 47.70  ?  344 ILE   D CD1 1 
ATOM   13837 N N   . PRO   D 1 345 ? 40.769  2.898   40.503  1.00 49.32  ?  345 PRO   D N   1 
ATOM   13838 C CA  . PRO   D 1 345 ? 41.187  1.732   41.293  1.00 47.86  ?  345 PRO   D CA  1 
ATOM   13839 C C   . PRO   D 1 345 ? 40.174  1.376   42.372  1.00 49.61  ?  345 PRO   D C   1 
ATOM   13840 O O   . PRO   D 1 345 ? 39.671  2.238   43.094  1.00 49.39  ?  345 PRO   D O   1 
ATOM   13841 C CB  . PRO   D 1 345 ? 42.516  2.182   41.908  1.00 51.27  ?  345 PRO   D CB  1 
ATOM   13842 C CG  . PRO   D 1 345 ? 42.407  3.677   41.963  1.00 54.24  ?  345 PRO   D CG  1 
ATOM   13843 C CD  . PRO   D 1 345 ? 41.611  4.081   40.755  1.00 45.22  ?  345 PRO   D CD  1 
ATOM   13844 N N   . ILE   D 1 346 ? 39.888  0.079   42.482  1.00 41.09  ?  346 ILE   D N   1 
ATOM   13845 C CA  . ILE   D 1 346 ? 38.963  -0.440  43.479  1.00 47.51  ?  346 ILE   D CA  1 
ATOM   13846 C C   . ILE   D 1 346 ? 39.575  -1.688  44.094  1.00 40.10  ?  346 ILE   D C   1 
ATOM   13847 O O   . ILE   D 1 346 ? 40.462  -2.321  43.519  1.00 38.04  ?  346 ILE   D O   1 
ATOM   13848 C CB  . ILE   D 1 346 ? 37.573  -0.775  42.888  1.00 38.48  ?  346 ILE   D CB  1 
ATOM   13849 C CG1 . ILE   D 1 346 ? 37.704  -1.842  41.799  1.00 35.16  ?  346 ILE   D CG1 1 
ATOM   13850 C CG2 . ILE   D 1 346 ? 36.918  0.472   42.324  1.00 39.60  ?  346 ILE   D CG2 1 
ATOM   13851 C CD1 . ILE   D 1 346 ? 36.385  -2.389  41.327  1.00 34.05  ?  346 ILE   D CD1 1 
ATOM   13852 N N   . GLN   D 1 347 ? 39.099  -2.024  45.290  1.00 32.48  ?  347 GLN   D N   1 
ATOM   13853 C CA  . GLN   D 1 347 ? 39.393  -3.322  45.883  1.00 33.48  ?  347 GLN   D CA  1 
ATOM   13854 C C   . GLN   D 1 347 ? 38.824  -4.405  44.974  1.00 36.69  ?  347 GLN   D C   1 
ATOM   13855 O O   . GLN   D 1 347 ? 37.606  -4.620  44.932  1.00 36.93  ?  347 GLN   D O   1 
ATOM   13856 C CB  . GLN   D 1 347 ? 38.815  -3.418  47.302  1.00 41.14  ?  347 GLN   D CB  1 
ATOM   13857 C CG  . GLN   D 1 347 ? 38.767  -4.833  47.910  1.00 36.43  ?  347 GLN   D CG  1 
ATOM   13858 C CD  . GLN   D 1 347 ? 40.106  -5.312  48.466  1.00 44.50  ?  347 GLN   D CD  1 
ATOM   13859 O OE1 . GLN   D 1 347 ? 41.087  -5.476  47.731  1.00 39.44  ?  347 GLN   D OE1 1 
ATOM   13860 N NE2 . GLN   D 1 347 ? 40.144  -5.554  49.769  1.00 35.12  ?  347 GLN   D NE2 1 
ATOM   13861 N N   . TYR   D 1 348 ? 39.681  -5.062  44.231  1.00 28.89  ?  348 TYR   D N   1 
ATOM   13862 C CA  . TYR   D 1 348 ? 39.198  -6.086  43.322  1.00 35.00  ?  348 TYR   D CA  1 
ATOM   13863 C C   . TYR   D 1 348 ? 39.469  -7.464  43.906  1.00 34.42  ?  348 TYR   D C   1 
ATOM   13864 O O   . TYR   D 1 348 ? 40.575  -7.708  44.413  1.00 35.69  ?  348 TYR   D O   1 
ATOM   13865 C CB  . TYR   D 1 348 ? 39.874  -5.950  41.959  1.00 31.54  ?  348 TYR   D CB  1 
ATOM   13866 C CG  . TYR   D 1 348 ? 39.297  -6.834  40.877  1.00 36.88  ?  348 TYR   D CG  1 
ATOM   13867 C CD1 . TYR   D 1 348 ? 38.002  -6.645  40.414  1.00 39.32  ?  348 TYR   D CD1 1 
ATOM   13868 C CD2 . TYR   D 1 348 ? 40.054  -7.846  40.301  1.00 40.76  ?  348 TYR   D CD2 1 
ATOM   13869 C CE1 . TYR   D 1 348 ? 37.468  -7.452  39.424  1.00 36.96  ?  348 TYR   D CE1 1 
ATOM   13870 C CE2 . TYR   D 1 348 ? 39.527  -8.656  39.304  1.00 35.84  ?  348 TYR   D CE2 1 
ATOM   13871 C CZ  . TYR   D 1 348 ? 38.238  -8.453  38.869  1.00 39.65  ?  348 TYR   D CZ  1 
ATOM   13872 O OH  . TYR   D 1 348 ? 37.711  -9.254  37.877  1.00 37.92  ?  348 TYR   D OH  1 
ATOM   13873 N N   . PRO   D 1 349 ? 38.494  -8.380  43.881  1.00 27.91  ?  349 PRO   D N   1 
ATOM   13874 C CA  . PRO   D 1 349 ? 37.126  -8.219  43.381  1.00 28.13  ?  349 PRO   D CA  1 
ATOM   13875 C C   . PRO   D 1 349 ? 36.248  -7.422  44.338  1.00 30.39  ?  349 PRO   D C   1 
ATOM   13876 O O   . PRO   D 1 349 ? 36.592  -7.255  45.511  1.00 30.97  ?  349 PRO   D O   1 
ATOM   13877 C CB  . PRO   D 1 349 ? 36.647  -9.668  43.251  1.00 32.88  ?  349 PRO   D CB  1 
ATOM   13878 C CG  . PRO   D 1 349 ? 37.331  -10.359 44.386  1.00 31.46  ?  349 PRO   D CG  1 
ATOM   13879 C CD  . PRO   D 1 349 ? 38.708  -9.730  44.435  1.00 31.21  ?  349 PRO   D CD  1 
ATOM   13880 N N   . THR   D 1 350 ? 35.111  -6.924  43.857  1.00 27.65  ?  350 THR   D N   1 
ATOM   13881 C CA  . THR   D 1 350 ? 34.182  -6.214  44.720  1.00 28.13  ?  350 THR   D CA  1 
ATOM   13882 C C   . THR   D 1 350 ? 33.588  -7.161  45.753  1.00 30.04  ?  350 THR   D C   1 
ATOM   13883 O O   . THR   D 1 350 ? 33.378  -8.351  45.494  1.00 30.68  ?  350 THR   D O   1 
ATOM   13884 C CB  . THR   D 1 350 ? 33.059  -5.567  43.901  1.00 25.98  ?  350 THR   D CB  1 
ATOM   13885 O OG1 . THR   D 1 350 ? 32.415  -6.555  43.080  1.00 26.79  ?  350 THR   D OG1 1 
ATOM   13886 C CG2 . THR   D 1 350 ? 33.611  -4.455  43.018  1.00 26.48  ?  350 THR   D CG2 1 
ATOM   13887 N N   . GLY   D 1 351 ? 33.322  -6.617  46.939  1.00 24.10  ?  351 GLY   D N   1 
ATOM   13888 C CA  . GLY   D 1 351 ? 32.679  -7.354  48.002  1.00 27.64  ?  351 GLY   D CA  1 
ATOM   13889 C C   . GLY   D 1 351 ? 31.195  -7.528  47.747  1.00 26.42  ?  351 GLY   D C   1 
ATOM   13890 O O   . GLY   D 1 351 ? 30.682  -7.303  46.651  1.00 26.75  ?  351 GLY   D O   1 
ATOM   13891 N N   . GLY   D 1 352 ? 30.488  -7.927  48.802  1.00 22.28  ?  352 GLY   D N   1 
ATOM   13892 C CA  . GLY   D 1 352 ? 29.075  -8.208  48.649  1.00 20.65  ?  352 GLY   D CA  1 
ATOM   13893 C C   . GLY   D 1 352 ? 28.178  -6.987  48.638  1.00 26.26  ?  352 GLY   D C   1 
ATOM   13894 O O   . GLY   D 1 352 ? 27.123  -7.002  47.995  1.00 25.77  ?  352 GLY   D O   1 
ATOM   13895 N N   . HIS   D 1 353 ? 28.564  -5.922  49.339  1.00 23.79  ?  353 HIS   D N   1 
ATOM   13896 C CA  . HIS   D 1 353 ? 27.621  -4.859  49.659  1.00 24.83  ?  353 HIS   D CA  1 
ATOM   13897 C C   . HIS   D 1 353 ? 28.062  -3.470  49.221  1.00 24.66  ?  353 HIS   D C   1 
ATOM   13898 O O   . HIS   D 1 353 ? 27.240  -2.544  49.254  1.00 21.91  ?  353 HIS   D O   1 
ATOM   13899 C CB  . HIS   D 1 353 ? 27.344  -4.838  51.172  1.00 21.27  ?  353 HIS   D CB  1 
ATOM   13900 C CG  . HIS   D 1 353 ? 28.518  -4.404  51.993  1.00 23.78  ?  353 HIS   D CG  1 
ATOM   13901 N ND1 . HIS   D 1 353 ? 29.730  -5.056  51.959  1.00 22.90  ?  353 HIS   D ND1 1 
ATOM   13902 C CD2 . HIS   D 1 353 ? 28.669  -3.374  52.858  1.00 23.28  ?  353 HIS   D CD2 1 
ATOM   13903 C CE1 . HIS   D 1 353 ? 30.576  -4.452  52.775  1.00 26.31  ?  353 HIS   D CE1 1 
ATOM   13904 N NE2 . HIS   D 1 353 ? 29.959  -3.425  53.329  1.00 27.19  ?  353 HIS   D NE2 1 
ATOM   13905 N N   . ALA   D 1 354 ? 29.310  -3.298  48.800  1.00 22.30  ?  354 ALA   D N   1 
ATOM   13906 C CA  . ALA   D 1 354 ? 29.840  -1.972  48.524  1.00 24.46  ?  354 ALA   D CA  1 
ATOM   13907 C C   . ALA   D 1 354 ? 31.006  -2.076  47.553  1.00 31.75  ?  354 ALA   D C   1 
ATOM   13908 O O   . ALA   D 1 354 ? 31.709  -3.090  47.511  1.00 29.22  ?  354 ALA   D O   1 
ATOM   13909 C CB  . ALA   D 1 354 ? 30.292  -1.278  49.810  1.00 23.36  ?  354 ALA   D CB  1 
ATOM   13910 N N   . VAL   D 1 355 ? 31.192  -1.015  46.769  1.00 24.39  ?  355 VAL   D N   1 
ATOM   13911 C CA  . VAL   D 1 355 ? 32.415  -0.808  46.007  1.00 29.77  ?  355 VAL   D CA  1 
ATOM   13912 C C   . VAL   D 1 355 ? 33.332  0.071   46.845  1.00 32.15  ?  355 VAL   D C   1 
ATOM   13913 O O   . VAL   D 1 355 ? 32.898  1.097   47.385  1.00 30.20  ?  355 VAL   D O   1 
ATOM   13914 C CB  . VAL   D 1 355 ? 32.114  -0.171  44.637  1.00 25.61  ?  355 VAL   D CB  1 
ATOM   13915 C CG1 . VAL   D 1 355 ? 33.397  0.066   43.856  1.00 25.81  ?  355 VAL   D CG1 1 
ATOM   13916 C CG2 . VAL   D 1 355 ? 31.171  -1.059  43.837  1.00 23.82  ?  355 VAL   D CG2 1 
ATOM   13917 N N   . PHE   D 1 356 ? 34.586  -0.351  46.996  1.00 31.64  ?  356 PHE   D N   1 
ATOM   13918 C CA  . PHE   D 1 356 ? 35.586  0.387   47.767  1.00 39.20  ?  356 PHE   D CA  1 
ATOM   13919 C C   . PHE   D 1 356 ? 36.583  1.003   46.793  1.00 41.12  ?  356 PHE   D C   1 
ATOM   13920 O O   . PHE   D 1 356 ? 37.423  0.296   46.229  1.00 45.39  ?  356 PHE   D O   1 
ATOM   13921 C CB  . PHE   D 1 356 ? 36.301  -0.519  48.770  1.00 43.46  ?  356 PHE   D CB  1 
ATOM   13922 C CG  . PHE   D 1 356 ? 35.472  -0.882  49.963  1.00 41.49  ?  356 PHE   D CG  1 
ATOM   13923 C CD1 . PHE   D 1 356 ? 34.412  -1.769  49.845  1.00 38.34  ?  356 PHE   D CD1 1 
ATOM   13924 C CD2 . PHE   D 1 356 ? 35.754  -0.346  51.204  1.00 44.16  ?  356 PHE   D CD2 1 
ATOM   13925 C CE1 . PHE   D 1 356 ? 33.643  -2.103  50.945  1.00 38.83  ?  356 PHE   D CE1 1 
ATOM   13926 C CE2 . PHE   D 1 356 ? 34.993  -0.680  52.307  1.00 40.23  ?  356 PHE   D CE2 1 
ATOM   13927 C CZ  . PHE   D 1 356 ? 33.939  -1.560  52.180  1.00 33.77  ?  356 PHE   D CZ  1 
ATOM   13928 N N   . VAL   D 1 357 ? 36.489  2.311   46.592  1.00 45.19  ?  357 VAL   D N   1 
ATOM   13929 C CA  . VAL   D 1 357 ? 37.451  3.019   45.757  1.00 47.85  ?  357 VAL   D CA  1 
ATOM   13930 C C   . VAL   D 1 357 ? 38.747  3.187   46.543  1.00 65.88  ?  357 VAL   D C   1 
ATOM   13931 O O   . VAL   D 1 357 ? 38.732  3.651   47.687  1.00 66.14  ?  357 VAL   D O   1 
ATOM   13932 C CB  . VAL   D 1 357 ? 36.881  4.372   45.304  1.00 48.73  ?  357 VAL   D CB  1 
ATOM   13933 C CG1 . VAL   D 1 357 ? 37.892  5.125   44.464  1.00 53.60  ?  357 VAL   D CG1 1 
ATOM   13934 C CG2 . VAL   D 1 357 ? 35.596  4.163   44.515  1.00 45.32  ?  357 VAL   D CG2 1 
ATOM   13935 N N   . ASP   D 1 358 ? 39.871  2.815   45.929  1.00 79.80  ?  358 ASP   D N   1 
ATOM   13936 C CA  . ASP   D 1 358 ? 41.150  2.739   46.624  1.00 90.00  ?  358 ASP   D CA  1 
ATOM   13937 C C   . ASP   D 1 358 ? 41.710  4.137   46.895  1.00 98.19  ?  358 ASP   D C   1 
ATOM   13938 O O   . ASP   D 1 358 ? 41.080  5.160   46.607  1.00 97.42  ?  358 ASP   D O   1 
ATOM   13939 C CB  . ASP   D 1 358 ? 42.141  1.902   45.818  1.00 87.85  ?  358 ASP   D CB  1 
ATOM   13940 C CG  . ASP   D 1 358 ? 43.258  1.324   46.674  1.00 95.70  ?  358 ASP   D CG  1 
ATOM   13941 O OD1 . ASP   D 1 358 ? 43.252  1.552   47.904  1.00 95.86  ?  358 ASP   D OD1 1 
ATOM   13942 O OD2 . ASP   D 1 358 ? 44.143  0.644   46.115  1.00 97.51  ?  358 ASP   D OD2 1 
ATOM   13943 N N   . CYS   D 1 359 ? 42.925  4.168   47.452  1.00 104.87 ?  359 CYS   D N   1 
ATOM   13944 C CA  . CYS   D 1 359 ? 43.549  5.407   47.899  1.00 100.83 ?  359 CYS   D CA  1 
ATOM   13945 C C   . CYS   D 1 359 ? 43.606  6.423   46.766  1.00 98.35  ?  359 CYS   D C   1 
ATOM   13946 O O   . CYS   D 1 359 ? 43.671  6.071   45.584  1.00 96.82  ?  359 CYS   D O   1 
ATOM   13947 C CB  . CYS   D 1 359 ? 44.956  5.138   48.441  1.00 98.54  ?  359 CYS   D CB  1 
ATOM   13948 S SG  . CYS   D 1 359 ? 46.207  4.778   47.180  1.00 110.61 ?  359 CYS   D SG  1 
ATOM   13949 N N   . LYS   D 1 360 ? 43.578  7.701   47.142  1.00 84.80  ?  360 LYS   D N   1 
ATOM   13950 C CA  . LYS   D 1 360 ? 43.343  8.785   46.190  1.00 79.66  ?  360 LYS   D CA  1 
ATOM   13951 C C   . LYS   D 1 360 ? 44.553  8.959   45.280  1.00 78.87  ?  360 LYS   D C   1 
ATOM   13952 O O   . LYS   D 1 360 ? 45.435  9.793   45.497  1.00 76.42  ?  360 LYS   D O   1 
ATOM   13953 C CB  . LYS   D 1 360 ? 42.988  10.069  46.924  1.00 74.40  ?  360 LYS   D CB  1 
ATOM   13954 C CG  . LYS   D 1 360 ? 41.649  9.955   47.631  1.00 79.34  ?  360 LYS   D CG  1 
ATOM   13955 C CD  . LYS   D 1 360 ? 40.595  9.365   46.692  1.00 66.03  ?  360 LYS   D CD  1 
ATOM   13956 C CE  . LYS   D 1 360 ? 39.539  8.577   47.444  1.00 60.73  ?  360 LYS   D CE  1 
ATOM   13957 N NZ  . LYS   D 1 360 ? 38.200  8.815   46.861  1.00 52.03  ?  360 LYS   D NZ  1 
ATOM   13958 N N   . LYS   D 1 361 ? 44.587  8.130   44.243  1.00 75.29  ?  361 LYS   D N   1 
ATOM   13959 C CA  . LYS   D 1 361 ? 45.437  8.339   43.086  1.00 75.05  ?  361 LYS   D CA  1 
ATOM   13960 C C   . LYS   D 1 361 ? 44.775  9.259   42.066  1.00 76.25  ?  361 LYS   D C   1 
ATOM   13961 O O   . LYS   D 1 361 ? 45.248  9.359   40.927  1.00 72.07  ?  361 LYS   D O   1 
ATOM   13962 C CB  . LYS   D 1 361 ? 45.792  6.987   42.462  1.00 68.65  ?  361 LYS   D CB  1 
ATOM   13963 C CG  . LYS   D 1 361 ? 46.480  6.044   43.442  1.00 64.01  ?  361 LYS   D CG  1 
ATOM   13964 C CD  . LYS   D 1 361 ? 46.305  4.589   43.053  1.00 68.73  ?  361 LYS   D CD  1 
ATOM   13965 C CE  . LYS   D 1 361 ? 47.044  4.252   41.767  1.00 71.60  ?  361 LYS   D CE  1 
ATOM   13966 N NZ  . LYS   D 1 361 ? 46.803  2.842   41.338  1.00 74.48  ?  361 LYS   D NZ  1 
ATOM   13967 N N   . LEU   D 1 362 ? 43.681  9.917   42.457  1.00 73.20  ?  362 LEU   D N   1 
ATOM   13968 C CA  . LEU   D 1 362 ? 43.005  10.919  41.644  1.00 77.86  ?  362 LEU   D CA  1 
ATOM   13969 C C   . LEU   D 1 362 ? 43.091  12.310  42.250  1.00 81.34  ?  362 LEU   D C   1 
ATOM   13970 O O   . LEU   D 1 362 ? 42.575  13.262  41.660  1.00 76.04  ?  362 LEU   D O   1 
ATOM   13971 C CB  . LEU   D 1 362 ? 41.529  10.544  41.438  1.00 73.28  ?  362 LEU   D CB  1 
ATOM   13972 C CG  . LEU   D 1 362 ? 41.184  9.339   40.558  1.00 66.02  ?  362 LEU   D CG  1 
ATOM   13973 C CD1 . LEU   D 1 362 ? 39.701  9.030   40.641  1.00 58.54  ?  362 LEU   D CD1 1 
ATOM   13974 C CD2 . LEU   D 1 362 ? 41.602  9.570   39.105  1.00 77.26  ?  362 LEU   D CD2 1 
ATOM   13975 N N   . VAL   D 1 363 ? 43.682  12.448  43.432  1.00 102.82 ?  363 VAL   D N   1 
ATOM   13976 C CA  . VAL   D 1 363 ? 43.931  13.756  44.033  1.00 105.74 ?  363 VAL   D CA  1 
ATOM   13977 C C   . VAL   D 1 363 ? 45.323  13.721  44.656  1.00 105.47 ?  363 VAL   D C   1 
ATOM   13978 O O   . VAL   D 1 363 ? 45.451  13.604  45.885  1.00 105.87 ?  363 VAL   D O   1 
ATOM   13979 C CB  . VAL   D 1 363 ? 42.862  14.128  45.074  1.00 103.72 ?  363 VAL   D CB  1 
ATOM   13980 C CG1 . VAL   D 1 363 ? 42.990  15.578  45.437  1.00 107.86 ?  363 VAL   D CG1 1 
ATOM   13981 C CG2 . VAL   D 1 363 ? 41.469  13.869  44.547  1.00 101.74 ?  363 VAL   D CG2 1 
ATOM   13982 N N   . PRO   D 1 364 ? 46.388  13.813  43.855  1.00 86.82  ?  364 PRO   D N   1 
ATOM   13983 C CA  . PRO   D 1 364 ? 47.737  13.662  44.422  1.00 82.04  ?  364 PRO   D CA  1 
ATOM   13984 C C   . PRO   D 1 364 ? 48.177  14.843  45.268  1.00 78.52  ?  364 PRO   D C   1 
ATOM   13985 O O   . PRO   D 1 364 ? 48.962  14.655  46.206  1.00 72.93  ?  364 PRO   D O   1 
ATOM   13986 C CB  . PRO   D 1 364 ? 48.619  13.501  43.178  1.00 83.25  ?  364 PRO   D CB  1 
ATOM   13987 C CG  . PRO   D 1 364 ? 47.879  14.235  42.107  1.00 83.02  ?  364 PRO   D CG  1 
ATOM   13988 C CD  . PRO   D 1 364 ? 46.417  14.014  42.395  1.00 85.22  ?  364 PRO   D CD  1 
ATOM   13989 N N   . GLN   D 1 365 ? 47.690  16.050  44.973  1.00 80.03  ?  365 GLN   D N   1 
ATOM   13990 C CA  . GLN   D 1 365 ? 48.136  17.253  45.668  1.00 75.08  ?  365 GLN   D CA  1 
ATOM   13991 C C   . GLN   D 1 365 ? 47.619  17.350  47.097  1.00 80.28  ?  365 GLN   D C   1 
ATOM   13992 O O   . GLN   D 1 365 ? 48.093  18.209  47.851  1.00 77.36  ?  365 GLN   D O   1 
ATOM   13993 C CB  . GLN   D 1 365 ? 47.704  18.495  44.887  1.00 73.27  ?  365 GLN   D CB  1 
ATOM   13994 C CG  . GLN   D 1 365 ? 46.210  18.800  44.960  1.00 74.65  ?  365 GLN   D CG  1 
ATOM   13995 C CD  . GLN   D 1 365 ? 45.359  17.911  44.061  1.00 78.81  ?  365 GLN   D CD  1 
ATOM   13996 O OE1 . GLN   D 1 365 ? 45.843  16.944  43.473  1.00 74.05  ?  365 GLN   D OE1 1 
ATOM   13997 N NE2 . GLN   D 1 365 ? 44.080  18.250  43.944  1.00 79.15  ?  365 GLN   D NE2 1 
ATOM   13998 N N   . ILE   D 1 366 ? 46.670  16.510  47.488  1.00 80.49  ?  366 ILE   D N   1 
ATOM   13999 C CA  . ILE   D 1 366 ? 46.070  16.559  48.818  1.00 86.73  ?  366 ILE   D CA  1 
ATOM   14000 C C   . ILE   D 1 366 ? 46.671  15.432  49.651  1.00 92.05  ?  366 ILE   D C   1 
ATOM   14001 O O   . ILE   D 1 366 ? 46.505  14.256  49.291  1.00 90.36  ?  366 ILE   D O   1 
ATOM   14002 C CB  . ILE   D 1 366 ? 44.540  16.448  48.751  1.00 86.40  ?  366 ILE   D CB  1 
ATOM   14003 C CG1 . ILE   D 1 366 ? 43.947  17.682  48.068  1.00 81.21  ?  366 ILE   D CG1 1 
ATOM   14004 C CG2 . ILE   D 1 366 ? 43.960  16.299  50.138  1.00 81.92  ?  366 ILE   D CG2 1 
ATOM   14005 C CD1 . ILE   D 1 366 ? 42.432  17.734  48.107  1.00 80.30  ?  366 ILE   D CD1 1 
ATOM   14006 N N   . PRO   D 1 367 ? 47.378  15.735  50.749  1.00 108.71 ?  367 PRO   D N   1 
ATOM   14007 C CA  . PRO   D 1 367 ? 47.951  14.669  51.583  1.00 109.36 ?  367 PRO   D CA  1 
ATOM   14008 C C   . PRO   D 1 367 ? 46.919  13.997  52.473  1.00 110.47 ?  367 PRO   D C   1 
ATOM   14009 O O   . PRO   D 1 367 ? 45.713  14.109  52.235  1.00 109.21 ?  367 PRO   D O   1 
ATOM   14010 C CB  . PRO   D 1 367 ? 49.004  15.411  52.415  1.00 107.01 ?  367 PRO   D CB  1 
ATOM   14011 C CG  . PRO   D 1 367 ? 48.463  16.798  52.529  1.00 106.51 ?  367 PRO   D CG  1 
ATOM   14012 C CD  . PRO   D 1 367 ? 47.774  17.077  51.215  1.00 108.71 ?  367 PRO   D CD  1 
ATOM   14013 N N   . GLY   D 1 368 ? 47.391  13.308  53.514  1.00 93.47  ?  368 GLY   D N   1 
ATOM   14014 C CA  . GLY   D 1 368 ? 46.481  12.572  54.378  1.00 85.69  ?  368 GLY   D CA  1 
ATOM   14015 C C   . GLY   D 1 368 ? 45.631  13.475  55.252  1.00 82.92  ?  368 GLY   D C   1 
ATOM   14016 O O   . GLY   D 1 368 ? 44.404  13.348  55.287  1.00 84.74  ?  368 GLY   D O   1 
ATOM   14017 N N   . ASP   D 1 369 ? 46.267  14.398  55.974  1.00 84.25  ?  369 ASP   D N   1 
ATOM   14018 C CA  . ASP   D 1 369 ? 45.531  15.245  56.907  1.00 84.91  ?  369 ASP   D CA  1 
ATOM   14019 C C   . ASP   D 1 369 ? 44.802  16.397  56.224  1.00 83.21  ?  369 ASP   D C   1 
ATOM   14020 O O   . ASP   D 1 369 ? 44.168  17.203  56.915  1.00 80.42  ?  369 ASP   D O   1 
ATOM   14021 C CB  . ASP   D 1 369 ? 46.466  15.794  57.989  1.00 85.85  ?  369 ASP   D CB  1 
ATOM   14022 C CG  . ASP   D 1 369 ? 45.724  16.161  59.274  1.00 89.80  ?  369 ASP   D CG  1 
ATOM   14023 O OD1 . ASP   D 1 369 ? 44.548  15.760  59.421  1.00 76.49  ?  369 ASP   D OD1 1 
ATOM   14024 O OD2 . ASP   D 1 369 ? 46.313  16.852  60.137  1.00 91.03  ?  369 ASP   D OD2 1 
ATOM   14025 N N   . GLN   D 1 370 ? 44.877  16.506  54.899  1.00 83.81  ?  370 GLN   D N   1 
ATOM   14026 C CA  . GLN   D 1 370 ? 43.978  17.380  54.159  1.00 83.99  ?  370 GLN   D CA  1 
ATOM   14027 C C   . GLN   D 1 370 ? 42.753  16.633  53.646  1.00 78.23  ?  370 GLN   D C   1 
ATOM   14028 O O   . GLN   D 1 370 ? 41.919  17.235  52.960  1.00 77.69  ?  370 GLN   D O   1 
ATOM   14029 C CB  . GLN   D 1 370 ? 44.718  18.057  52.995  1.00 86.79  ?  370 GLN   D CB  1 
ATOM   14030 C CG  . GLN   D 1 370 ? 45.692  19.173  53.402  1.00 87.99  ?  370 GLN   D CG  1 
ATOM   14031 C CD  . GLN   D 1 370 ? 44.994  20.410  53.967  1.00 85.77  ?  370 GLN   D CD  1 
ATOM   14032 O OE1 . GLN   D 1 370 ? 44.613  20.444  55.139  1.00 81.30  ?  370 GLN   D OE1 1 
ATOM   14033 N NE2 . GLN   D 1 370 ? 44.831  21.432  53.132  1.00 81.10  ?  370 GLN   D NE2 1 
ATOM   14034 N N   . PHE   D 1 371 ? 42.636  15.335  53.966  1.00 80.62  ?  371 PHE   D N   1 
ATOM   14035 C CA  . PHE   D 1 371 ? 41.469  14.485  53.742  1.00 79.55  ?  371 PHE   D CA  1 
ATOM   14036 C C   . PHE   D 1 371 ? 41.163  14.311  52.260  1.00 75.69  ?  371 PHE   D C   1 
ATOM   14037 O O   . PHE   D 1 371 ? 40.164  14.846  51.760  1.00 72.51  ?  371 PHE   D O   1 
ATOM   14038 C CB  . PHE   D 1 371 ? 40.265  15.058  54.482  1.00 77.96  ?  371 PHE   D CB  1 
ATOM   14039 C CG  . PHE   D 1 371 ? 40.570  15.430  55.895  1.00 74.95  ?  371 PHE   D CG  1 
ATOM   14040 C CD1 . PHE   D 1 371 ? 40.739  14.450  56.854  1.00 71.07  ?  371 PHE   D CD1 1 
ATOM   14041 C CD2 . PHE   D 1 371 ? 40.717  16.754  56.259  1.00 75.70  ?  371 PHE   D CD2 1 
ATOM   14042 C CE1 . PHE   D 1 371 ? 41.026  14.781  58.151  1.00 75.62  ?  371 PHE   D CE1 1 
ATOM   14043 C CE2 . PHE   D 1 371 ? 41.009  17.094  57.557  1.00 81.67  ?  371 PHE   D CE2 1 
ATOM   14044 C CZ  . PHE   D 1 371 ? 41.163  16.105  58.505  1.00 83.29  ?  371 PHE   D CZ  1 
ATOM   14045 N N   . PRO   D 1 372 ? 41.981  13.542  51.535  1.00 76.86  ?  372 PRO   D N   1 
ATOM   14046 C CA  . PRO   D 1 372 ? 41.794  13.466  50.078  1.00 78.08  ?  372 PRO   D CA  1 
ATOM   14047 C C   . PRO   D 1 372 ? 40.534  12.726  49.677  1.00 64.97  ?  372 PRO   D C   1 
ATOM   14048 O O   . PRO   D 1 372 ? 39.860  13.142  48.727  1.00 67.39  ?  372 PRO   D O   1 
ATOM   14049 C CB  . PRO   D 1 372 ? 43.065  12.746  49.606  1.00 77.53  ?  372 PRO   D CB  1 
ATOM   14050 C CG  . PRO   D 1 372 ? 43.447  11.883  50.766  1.00 76.32  ?  372 PRO   D CG  1 
ATOM   14051 C CD  . PRO   D 1 372 ? 43.036  12.629  52.011  1.00 78.14  ?  372 PRO   D CD  1 
ATOM   14052 N N   . ALA   D 1 373 ? 40.196  11.636  50.374  1.00 68.53  ?  373 ALA   D N   1 
ATOM   14053 C CA  . ALA   D 1 373 ? 38.963  10.921  50.069  1.00 66.77  ?  373 ALA   D CA  1 
ATOM   14054 C C   . ALA   D 1 373 ? 37.749  11.805  50.307  1.00 63.06  ?  373 ALA   D C   1 
ATOM   14055 O O   . ALA   D 1 373 ? 36.770  11.740  49.556  1.00 58.68  ?  373 ALA   D O   1 
ATOM   14056 C CB  . ALA   D 1 373 ? 38.872  9.644   50.905  1.00 64.45  ?  373 ALA   D CB  1 
ATOM   14057 N N   . GLN   D 1 374 ? 37.802  12.649  51.339  1.00 59.30  ?  374 GLN   D N   1 
ATOM   14058 C CA  . GLN   D 1 374 ? 36.677  13.535  51.624  1.00 57.66  ?  374 GLN   D CA  1 
ATOM   14059 C C   . GLN   D 1 374 ? 36.465  14.539  50.497  1.00 62.04  ?  374 GLN   D C   1 
ATOM   14060 O O   . GLN   D 1 374 ? 35.331  14.765  50.057  1.00 62.52  ?  374 GLN   D O   1 
ATOM   14061 C CB  . GLN   D 1 374 ? 36.902  14.263  52.948  1.00 67.78  ?  374 GLN   D CB  1 
ATOM   14062 C CG  . GLN   D 1 374 ? 35.656  14.947  53.457  1.00 61.31  ?  374 GLN   D CG  1 
ATOM   14063 C CD  . GLN   D 1 374 ? 34.473  14.012  53.449  1.00 57.83  ?  374 GLN   D CD  1 
ATOM   14064 O OE1 . GLN   D 1 374 ? 34.491  12.958  54.093  1.00 56.73  ?  374 GLN   D OE1 1 
ATOM   14065 N NE2 . GLN   D 1 374 ? 33.441  14.377  52.701  1.00 50.15  ?  374 GLN   D NE2 1 
ATOM   14066 N N   . ALA   D 1 375 ? 37.552  15.161  50.022  1.00 62.78  ?  375 ALA   D N   1 
ATOM   14067 C CA  . ALA   D 1 375 ? 37.443  16.127  48.933  1.00 56.84  ?  375 ALA   D CA  1 
ATOM   14068 C C   . ALA   D 1 375 ? 36.876  15.486  47.675  1.00 58.45  ?  375 ALA   D C   1 
ATOM   14069 O O   . ALA   D 1 375 ? 36.144  16.137  46.918  1.00 61.28  ?  375 ALA   D O   1 
ATOM   14070 C CB  . ALA   D 1 375 ? 38.810  16.751  48.648  1.00 65.45  ?  375 ALA   D CB  1 
ATOM   14071 N N   . VAL   D 1 376 ? 37.205  14.217  47.432  1.00 61.22  ?  376 VAL   D N   1 
ATOM   14072 C CA  . VAL   D 1 376 ? 36.542  13.464  46.370  1.00 60.33  ?  376 VAL   D CA  1 
ATOM   14073 C C   . VAL   D 1 376 ? 35.057  13.324  46.679  1.00 56.39  ?  376 VAL   D C   1 
ATOM   14074 O O   . VAL   D 1 376 ? 34.194  13.591  45.834  1.00 51.58  ?  376 VAL   D O   1 
ATOM   14075 C CB  . VAL   D 1 376 ? 37.208  12.086  46.197  1.00 58.54  ?  376 VAL   D CB  1 
ATOM   14076 C CG1 . VAL   D 1 376 ? 36.478  11.265  45.141  1.00 50.39  ?  376 VAL   D CG1 1 
ATOM   14077 C CG2 . VAL   D 1 376 ? 38.665  12.250  45.833  1.00 59.70  ?  376 VAL   D CG2 1 
ATOM   14078 N N   . ILE   D 1 377 ? 34.744  12.909  47.906  1.00 56.80  ?  377 ILE   D N   1 
ATOM   14079 C CA  . ILE   D 1 377 ? 33.352  12.722  48.302  1.00 55.61  ?  377 ILE   D CA  1 
ATOM   14080 C C   . ILE   D 1 377 ? 32.580  14.027  48.171  1.00 54.15  ?  377 ILE   D C   1 
ATOM   14081 O O   . ILE   D 1 377 ? 31.436  14.040  47.703  1.00 53.84  ?  377 ILE   D O   1 
ATOM   14082 C CB  . ILE   D 1 377 ? 33.286  12.155  49.729  1.00 48.81  ?  377 ILE   D CB  1 
ATOM   14083 C CG1 . ILE   D 1 377 ? 33.871  10.745  49.747  1.00 45.34  ?  377 ILE   D CG1 1 
ATOM   14084 C CG2 . ILE   D 1 377 ? 31.862  12.143  50.235  1.00 50.32  ?  377 ILE   D CG2 1 
ATOM   14085 C CD1 . ILE   D 1 377 ? 34.026  10.162  51.121  1.00 49.88  ?  377 ILE   D CD1 1 
ATOM   14086 N N   . ASN   D 1 378 ? 33.203  15.148  48.543  1.00 49.07  ?  378 ASN   D N   1 
ATOM   14087 C CA  . ASN   D 1 378 ? 32.493  16.421  48.490  1.00 55.42  ?  378 ASN   D CA  1 
ATOM   14088 C C   . ASN   D 1 378 ? 32.278  16.885  47.051  1.00 63.27  ?  378 ASN   D C   1 
ATOM   14089 O O   . ASN   D 1 378 ? 31.188  17.357  46.702  1.00 61.98  ?  378 ASN   D O   1 
ATOM   14090 C CB  . ASN   D 1 378 ? 33.244  17.469  49.304  1.00 54.95  ?  378 ASN   D CB  1 
ATOM   14091 C CG  . ASN   D 1 378 ? 33.292  17.124  50.775  1.00 55.58  ?  378 ASN   D CG  1 
ATOM   14092 O OD1 . ASN   D 1 378 ? 33.049  15.982  51.157  1.00 59.73  ?  378 ASN   D OD1 1 
ATOM   14093 N ND2 . ASN   D 1 378 ? 33.598  18.108  51.608  1.00 54.50  ?  378 ASN   D ND2 1 
ATOM   14094 N N   . ALA   D 1 379 ? 33.299  16.761  46.200  1.00 60.83  ?  379 ALA   D N   1 
ATOM   14095 C CA  . ALA   D 1 379 ? 33.098  17.060  44.787  1.00 57.02  ?  379 ALA   D CA  1 
ATOM   14096 C C   . ALA   D 1 379 ? 32.123  16.075  44.163  1.00 54.16  ?  379 ALA   D C   1 
ATOM   14097 O O   . ALA   D 1 379 ? 31.255  16.467  43.374  1.00 54.66  ?  379 ALA   D O   1 
ATOM   14098 C CB  . ALA   D 1 379 ? 34.435  17.044  44.045  1.00 61.55  ?  379 ALA   D CB  1 
ATOM   14099 N N   . LEU   D 1 380 ? 32.247  14.791  44.514  1.00 54.65  ?  380 LEU   D N   1 
ATOM   14100 C CA  . LEU   D 1 380 ? 31.261  13.805  44.085  1.00 52.19  ?  380 LEU   D CA  1 
ATOM   14101 C C   . LEU   D 1 380 ? 29.862  14.203  44.530  1.00 53.40  ?  380 LEU   D C   1 
ATOM   14102 O O   . LEU   D 1 380 ? 28.893  14.052  43.775  1.00 53.38  ?  380 LEU   D O   1 
ATOM   14103 C CB  . LEU   D 1 380 ? 31.625  12.427  44.635  1.00 41.90  ?  380 LEU   D CB  1 
ATOM   14104 C CG  . LEU   D 1 380 ? 30.647  11.290  44.351  1.00 44.58  ?  380 LEU   D CG  1 
ATOM   14105 C CD1 . LEU   D 1 380 ? 30.391  11.168  42.856  1.00 42.11  ?  380 LEU   D CD1 1 
ATOM   14106 C CD2 . LEU   D 1 380 ? 31.201  9.992   44.917  1.00 45.87  ?  380 LEU   D CD2 1 
ATOM   14107 N N   . TYR   D 1 381 ? 29.737  14.722  45.753  1.00 51.78  ?  381 TYR   D N   1 
ATOM   14108 C CA  . TYR   D 1 381 ? 28.441  15.204  46.210  1.00 51.10  ?  381 TYR   D CA  1 
ATOM   14109 C C   . TYR   D 1 381 ? 28.043  16.485  45.493  1.00 59.61  ?  381 TYR   D C   1 
ATOM   14110 O O   . TYR   D 1 381 ? 26.888  16.636  45.077  1.00 56.87  ?  381 TYR   D O   1 
ATOM   14111 C CB  . TYR   D 1 381 ? 28.454  15.429  47.718  1.00 55.19  ?  381 TYR   D CB  1 
ATOM   14112 C CG  . TYR   D 1 381 ? 27.215  16.150  48.195  1.00 57.42  ?  381 TYR   D CG  1 
ATOM   14113 C CD1 . TYR   D 1 381 ? 25.968  15.532  48.150  1.00 49.33  ?  381 TYR   D CD1 1 
ATOM   14114 C CD2 . TYR   D 1 381 ? 27.285  17.452  48.668  1.00 56.46  ?  381 TYR   D CD2 1 
ATOM   14115 C CE1 . TYR   D 1 381 ? 24.835  16.186  48.569  1.00 44.51  ?  381 TYR   D CE1 1 
ATOM   14116 C CE2 . TYR   D 1 381 ? 26.153  18.115  49.091  1.00 59.50  ?  381 TYR   D CE2 1 
ATOM   14117 C CZ  . TYR   D 1 381 ? 24.930  17.476  49.042  1.00 52.84  ?  381 TYR   D CZ  1 
ATOM   14118 O OH  . TYR   D 1 381 ? 23.799  18.136  49.466  1.00 51.73  ?  381 TYR   D OH  1 
ATOM   14119 N N   . LEU   D 1 382 ? 28.980  17.425  45.342  1.00 86.03  ?  382 LEU   D N   1 
ATOM   14120 C CA  . LEU   D 1 382 ? 28.642  18.683  44.686  1.00 87.08  ?  382 LEU   D CA  1 
ATOM   14121 C C   . LEU   D 1 382 ? 28.357  18.486  43.205  1.00 86.81  ?  382 LEU   D C   1 
ATOM   14122 O O   . LEU   D 1 382 ? 27.572  19.243  42.623  1.00 89.10  ?  382 LEU   D O   1 
ATOM   14123 C CB  . LEU   D 1 382 ? 29.760  19.706  44.878  1.00 89.34  ?  382 LEU   D CB  1 
ATOM   14124 C CG  . LEU   D 1 382 ? 29.836  20.344  46.265  1.00 90.46  ?  382 LEU   D CG  1 
ATOM   14125 C CD1 . LEU   D 1 382 ? 30.677  21.611  46.236  1.00 92.55  ?  382 LEU   D CD1 1 
ATOM   14126 C CD2 . LEU   D 1 382 ? 28.441  20.636  46.790  1.00 89.53  ?  382 LEU   D CD2 1 
ATOM   14127 N N   . GLU   D 1 383 ? 28.967  17.482  42.580  1.00 62.72  ?  383 GLU   D N   1 
ATOM   14128 C CA  . GLU   D 1 383 ? 28.757  17.265  41.159  1.00 57.37  ?  383 GLU   D CA  1 
ATOM   14129 C C   . GLU   D 1 383 ? 27.523  16.436  40.853  1.00 57.78  ?  383 GLU   D C   1 
ATOM   14130 O O   . GLU   D 1 383 ? 27.000  16.529  39.738  1.00 57.54  ?  383 GLU   D O   1 
ATOM   14131 C CB  . GLU   D 1 383 ? 29.983  16.593  40.532  1.00 67.38  ?  383 GLU   D CB  1 
ATOM   14132 C CG  . GLU   D 1 383 ? 31.009  17.583  39.984  1.00 70.75  ?  383 GLU   D CG  1 
ATOM   14133 C CD  . GLU   D 1 383 ? 30.432  18.461  38.885  1.00 71.81  ?  383 GLU   D CD  1 
ATOM   14134 O OE1 . GLU   D 1 383 ? 30.020  17.913  37.839  1.00 76.84  ?  383 GLU   D OE1 1 
ATOM   14135 O OE2 . GLU   D 1 383 ? 30.377  19.695  39.074  1.00 71.15  ?  383 GLU   D OE2 1 
ATOM   14136 N N   . SER   D 1 384 ? 27.037  15.645  41.812  1.00 56.68  ?  384 SER   D N   1 
ATOM   14137 C CA  . SER   D 1 384 ? 25.964  14.694  41.530  1.00 47.23  ?  384 SER   D CA  1 
ATOM   14138 C C   . SER   D 1 384 ? 24.923  14.550  42.632  1.00 48.17  ?  384 SER   D C   1 
ATOM   14139 O O   . SER   D 1 384 ? 23.804  14.118  42.330  1.00 41.78  ?  384 SER   D O   1 
ATOM   14140 C CB  . SER   D 1 384 ? 26.553  13.311  41.237  1.00 43.80  ?  384 SER   D CB  1 
ATOM   14141 O OG  . SER   D 1 384 ? 27.382  12.875  42.305  1.00 47.16  ?  384 SER   D OG  1 
ATOM   14142 N N   . GLY   D 1 385 ? 25.226  14.884  43.881  1.00 44.93  ?  385 GLY   D N   1 
ATOM   14143 C CA  . GLY   D 1 385 ? 24.308  14.637  44.971  1.00 44.32  ?  385 GLY   D CA  1 
ATOM   14144 C C   . GLY   D 1 385 ? 24.418  13.265  45.591  1.00 41.56  ?  385 GLY   D C   1 
ATOM   14145 O O   . GLY   D 1 385 ? 23.544  12.886  46.376  1.00 39.02  ?  385 GLY   D O   1 
ATOM   14146 N N   . VAL   D 1 386 ? 25.463  12.512  45.270  1.00 41.60  ?  386 VAL   D N   1 
ATOM   14147 C CA  . VAL   D 1 386 ? 25.663  11.176  45.813  1.00 36.42  ?  386 VAL   D CA  1 
ATOM   14148 C C   . VAL   D 1 386 ? 26.467  11.292  47.099  1.00 35.53  ?  386 VAL   D C   1 
ATOM   14149 O O   . VAL   D 1 386 ? 27.599  11.786  47.094  1.00 43.50  ?  386 VAL   D O   1 
ATOM   14150 C CB  . VAL   D 1 386 ? 26.377  10.268  44.800  1.00 36.47  ?  386 VAL   D CB  1 
ATOM   14151 C CG1 . VAL   D 1 386 ? 26.879  9.004   45.481  1.00 29.91  ?  386 VAL   D CG1 1 
ATOM   14152 C CG2 . VAL   D 1 386 ? 25.442  9.930   43.651  1.00 38.12  ?  386 VAL   D CG2 1 
ATOM   14153 N N   . ARG   D 1 387 ? 25.889  10.832  48.202  1.00 38.02  ?  387 ARG   D N   1 
ATOM   14154 C CA  . ARG   D 1 387 ? 26.587  10.814  49.478  1.00 35.20  ?  387 ARG   D CA  1 
ATOM   14155 C C   . ARG   D 1 387 ? 27.258  9.460   49.664  1.00 29.77  ?  387 ARG   D C   1 
ATOM   14156 O O   . ARG   D 1 387 ? 26.579  8.431   49.757  1.00 30.26  ?  387 ARG   D O   1 
ATOM   14157 C CB  . ARG   D 1 387 ? 25.631  11.104  50.633  1.00 30.09  ?  387 ARG   D CB  1 
ATOM   14158 C CG  . ARG   D 1 387 ? 26.256  10.880  52.003  1.00 36.47  ?  387 ARG   D CG  1 
ATOM   14159 C CD  . ARG   D 1 387 ? 25.541  11.652  53.106  1.00 36.34  ?  387 ARG   D CD  1 
ATOM   14160 N NE  . ARG   D 1 387 ? 24.254  11.074  53.478  1.00 32.01  ?  387 ARG   D NE  1 
ATOM   14161 C CZ  . ARG   D 1 387 ? 23.478  11.551  54.444  1.00 34.45  ?  387 ARG   D CZ  1 
ATOM   14162 N NH1 . ARG   D 1 387 ? 23.828  12.612  55.154  1.00 35.46  ?  387 ARG   D NH1 1 
ATOM   14163 N NH2 . ARG   D 1 387 ? 22.327  10.944  54.712  1.00 31.33  ?  387 ARG   D NH2 1 
ATOM   14164 N N   . ALA   D 1 388 ? 28.581  9.463   49.706  1.00 33.46  ?  388 ALA   D N   1 
ATOM   14165 C CA  . ALA   D 1 388 ? 29.370  8.294   50.058  1.00 38.53  ?  388 ALA   D CA  1 
ATOM   14166 C C   . ALA   D 1 388 ? 29.979  8.493   51.440  1.00 39.42  ?  388 ALA   D C   1 
ATOM   14167 O O   . ALA   D 1 388 ? 29.848  9.553   52.060  1.00 41.87  ?  388 ALA   D O   1 
ATOM   14168 C CB  . ALA   D 1 388 ? 30.458  8.030   49.009  1.00 34.74  ?  388 ALA   D CB  1 
ATOM   14169 N N   . VAL   D 1 389 ? 30.641  7.450   51.934  1.00 35.47  ?  389 VAL   D N   1 
ATOM   14170 C CA  . VAL   D 1 389 ? 31.246  7.464   53.259  1.00 43.83  ?  389 VAL   D CA  1 
ATOM   14171 C C   . VAL   D 1 389 ? 32.749  7.294   53.099  1.00 47.87  ?  389 VAL   D C   1 
ATOM   14172 O O   . VAL   D 1 389 ? 33.213  6.594   52.191  1.00 46.74  ?  389 VAL   D O   1 
ATOM   14173 C CB  . VAL   D 1 389 ? 30.653  6.369   54.173  1.00 41.32  ?  389 VAL   D CB  1 
ATOM   14174 C CG1 . VAL   D 1 389 ? 30.957  4.977   53.634  1.00 35.90  ?  389 VAL   D CG1 1 
ATOM   14175 C CG2 . VAL   D 1 389 ? 31.148  6.532   55.614  1.00 50.20  ?  389 VAL   D CG2 1 
ATOM   14176 N N   . GLU   D 1 390 ? 33.509  7.955   53.961  1.00 47.98  ?  390 GLU   D N   1 
ATOM   14177 C CA  . GLU   D 1 390 ? 34.958  7.889   53.883  1.00 58.12  ?  390 GLU   D CA  1 
ATOM   14178 C C   . GLU   D 1 390 ? 35.504  6.810   54.804  1.00 54.38  ?  390 GLU   D C   1 
ATOM   14179 O O   . GLU   D 1 390 ? 35.005  6.605   55.913  1.00 57.40  ?  390 GLU   D O   1 
ATOM   14180 C CB  . GLU   D 1 390 ? 35.596  9.230   54.241  1.00 56.43  ?  390 GLU   D CB  1 
ATOM   14181 C CG  . GLU   D 1 390 ? 37.097  9.211   54.040  1.00 62.48  ?  390 GLU   D CG  1 
ATOM   14182 C CD  . GLU   D 1 390 ? 37.766  10.451  54.552  1.00 68.81  ?  390 GLU   D CD  1 
ATOM   14183 O OE1 . GLU   D 1 390 ? 37.110  11.513  54.552  1.00 71.21  ?  390 GLU   D OE1 1 
ATOM   14184 O OE2 . GLU   D 1 390 ? 38.944  10.359  54.963  1.00 75.36  ?  390 GLU   D OE2 1 
ATOM   14185 N N   . ILE   D 1 391 ? 36.529  6.114   54.325  1.00 58.50  ?  391 ILE   D N   1 
ATOM   14186 C CA  . ILE   D 1 391 ? 37.287  5.171   55.134  1.00 66.51  ?  391 ILE   D CA  1 
ATOM   14187 C C   . ILE   D 1 391 ? 38.763  5.503   54.947  1.00 69.80  ?  391 ILE   D C   1 
ATOM   14188 O O   . ILE   D 1 391 ? 39.449  4.898   54.114  1.00 71.96  ?  391 ILE   D O   1 
ATOM   14189 C CB  . ILE   D 1 391 ? 36.951  3.716   54.753  1.00 59.54  ?  391 ILE   D CB  1 
ATOM   14190 C CG1 . ILE   D 1 391 ? 35.455  3.470   54.948  1.00 49.97  ?  391 ILE   D CG1 1 
ATOM   14191 C CG2 . ILE   D 1 391 ? 37.759  2.728   55.590  1.00 62.32  ?  391 ILE   D CG2 1 
ATOM   14192 C CD1 . ILE   D 1 391 ? 35.000  2.093   54.563  1.00 53.77  ?  391 ILE   D CD1 1 
ATOM   14193 N N   . GLY   D 1 392 ? 39.251  6.491   55.700  1.00 64.78  ?  392 GLY   D N   1 
ATOM   14194 C CA  . GLY   D 1 392 ? 40.616  6.956   55.546  1.00 68.61  ?  392 GLY   D CA  1 
ATOM   14195 C C   . GLY   D 1 392 ? 41.119  7.783   56.712  1.00 67.94  ?  392 GLY   D C   1 
ATOM   14196 O O   . GLY   D 1 392 ? 40.921  7.410   57.872  1.00 66.86  ?  392 GLY   D O   1 
ATOM   14197 N N   . SER   D 1 393 ? 41.769  8.914   56.410  1.00 68.26  ?  393 SER   D N   1 
ATOM   14198 C CA  . SER   D 1 393 ? 42.374  9.751   57.443  1.00 72.60  ?  393 SER   D CA  1 
ATOM   14199 C C   . SER   D 1 393 ? 41.343  10.536  58.245  1.00 73.18  ?  393 SER   D C   1 
ATOM   14200 O O   . SER   D 1 393 ? 41.655  11.004  59.347  1.00 71.04  ?  393 SER   D O   1 
ATOM   14201 C CB  . SER   D 1 393 ? 43.381  10.721  56.814  1.00 75.40  ?  393 SER   D CB  1 
ATOM   14202 O OG  . SER   D 1 393 ? 44.489  10.039  56.252  1.00 67.20  ?  393 SER   D OG  1 
ATOM   14203 N N   . PHE   D 1 394 ? 40.131  10.701  57.718  1.00 67.15  ?  394 PHE   D N   1 
ATOM   14204 C CA  . PHE   D 1 394 ? 39.065  11.383  58.438  1.00 70.31  ?  394 PHE   D CA  1 
ATOM   14205 C C   . PHE   D 1 394 ? 38.244  10.437  59.307  1.00 66.58  ?  394 PHE   D C   1 
ATOM   14206 O O   . PHE   D 1 394 ? 37.555  10.899  60.225  1.00 65.15  ?  394 PHE   D O   1 
ATOM   14207 C CB  . PHE   D 1 394 ? 38.160  12.111  57.437  1.00 72.48  ?  394 PHE   D CB  1 
ATOM   14208 C CG  . PHE   D 1 394 ? 37.130  13.007  58.065  1.00 71.21  ?  394 PHE   D CG  1 
ATOM   14209 C CD1 . PHE   D 1 394 ? 37.499  14.007  58.951  1.00 74.26  ?  394 PHE   D CD1 1 
ATOM   14210 C CD2 . PHE   D 1 394 ? 35.797  12.872  57.734  1.00 69.00  ?  394 PHE   D CD2 1 
ATOM   14211 C CE1 . PHE   D 1 394 ? 36.551  14.836  59.513  1.00 69.31  ?  394 PHE   D CE1 1 
ATOM   14212 C CE2 . PHE   D 1 394 ? 34.846  13.698  58.290  1.00 71.40  ?  394 PHE   D CE2 1 
ATOM   14213 C CZ  . PHE   D 1 394 ? 35.224  14.681  59.182  1.00 69.66  ?  394 PHE   D CZ  1 
ATOM   14214 N N   . LEU   D 1 395 ? 38.300  9.130   59.040  1.00 65.85  ?  395 LEU   D N   1 
ATOM   14215 C CA  . LEU   D 1 395 ? 37.681  8.135   59.908  1.00 62.06  ?  395 LEU   D CA  1 
ATOM   14216 C C   . LEU   D 1 395 ? 38.642  7.634   60.979  1.00 66.88  ?  395 LEU   D C   1 
ATOM   14217 O O   . LEU   D 1 395 ? 38.251  7.490   62.144  1.00 62.26  ?  395 LEU   D O   1 
ATOM   14218 C CB  . LEU   D 1 395 ? 37.171  6.949   59.084  1.00 59.86  ?  395 LEU   D CB  1 
ATOM   14219 C CG  . LEU   D 1 395 ? 36.798  5.690   59.878  1.00 56.22  ?  395 LEU   D CG  1 
ATOM   14220 C CD1 . LEU   D 1 395 ? 35.688  5.983   60.862  1.00 55.64  ?  395 LEU   D CD1 1 
ATOM   14221 C CD2 . LEU   D 1 395 ? 36.399  4.542   58.964  1.00 54.54  ?  395 LEU   D CD2 1 
ATOM   14222 N N   . LEU   D 1 396 ? 39.898  7.375   60.605  1.00 67.23  ?  396 LEU   D N   1 
ATOM   14223 C CA  . LEU   D 1 396 ? 40.845  6.769   61.536  1.00 66.34  ?  396 LEU   D CA  1 
ATOM   14224 C C   . LEU   D 1 396 ? 41.069  7.657   62.757  1.00 65.39  ?  396 LEU   D C   1 
ATOM   14225 O O   . LEU   D 1 396 ? 40.928  7.207   63.900  1.00 63.44  ?  396 LEU   D O   1 
ATOM   14226 C CB  . LEU   D 1 396 ? 42.163  6.479   60.815  1.00 68.80  ?  396 LEU   D CB  1 
ATOM   14227 C CG  . LEU   D 1 396 ? 43.180  5.608   61.557  1.00 75.06  ?  396 LEU   D CG  1 
ATOM   14228 C CD1 . LEU   D 1 396 ? 42.488  4.436   62.240  1.00 79.95  ?  396 LEU   D CD1 1 
ATOM   14229 C CD2 . LEU   D 1 396 ? 44.248  5.110   60.598  1.00 71.90  ?  396 LEU   D CD2 1 
ATOM   14230 N N   . GLY   D 1 397 ? 41.420  8.920   62.534  1.00 68.97  ?  397 GLY   D N   1 
ATOM   14231 C CA  . GLY   D 1 397 ? 41.544  9.871   63.615  1.00 67.68  ?  397 GLY   D CA  1 
ATOM   14232 C C   . GLY   D 1 397 ? 42.874  9.809   64.348  1.00 77.26  ?  397 GLY   D C   1 
ATOM   14233 O O   . GLY   D 1 397 ? 43.863  9.218   63.899  1.00 73.81  ?  397 GLY   D O   1 
ATOM   14234 N N   . ARG   D 1 398 ? 42.878  10.446  65.513  1.00 75.34  ?  398 ARG   D N   1 
ATOM   14235 C CA  . ARG   D 1 398 ? 44.066  10.541  66.357  1.00 76.86  ?  398 ARG   D CA  1 
ATOM   14236 C C   . ARG   D 1 398 ? 44.329  9.235   67.106  1.00 71.66  ?  398 ARG   D C   1 
ATOM   14237 O O   . ARG   D 1 398 ? 43.469  8.739   67.838  1.00 68.43  ?  398 ARG   D O   1 
ATOM   14238 C CB  . ARG   D 1 398 ? 43.912  11.701  67.348  1.00 70.18  ?  398 ARG   D CB  1 
ATOM   14239 C CG  . ARG   D 1 398 ? 43.585  13.036  66.686  1.00 72.93  ?  398 ARG   D CG  1 
ATOM   14240 C CD  . ARG   D 1 398 ? 44.804  13.636  65.991  1.00 74.69  ?  398 ARG   D CD  1 
ATOM   14241 N NE  . ARG   D 1 398 ? 44.440  14.662  65.019  1.00 75.95  ?  398 ARG   D NE  1 
ATOM   14242 C CZ  . ARG   D 1 398 ? 44.118  15.912  65.327  1.00 73.81  ?  398 ARG   D CZ  1 
ATOM   14243 N NH1 . ARG   D 1 398 ? 44.075  16.326  66.581  1.00 70.40  ?  398 ARG   D NH1 1 
ATOM   14244 N NH2 . ARG   D 1 398 ? 43.825  16.766  64.351  1.00 75.68  ?  398 ARG   D NH2 1 
ATOM   14245 N N   . GLN   D 1 405 ? 47.536  11.492  64.275  1.00 84.48  ?  405 GLN   D N   1 
ATOM   14246 C CA  . GLN   D 1 405 ? 47.033  10.795  63.094  1.00 87.16  ?  405 GLN   D CA  1 
ATOM   14247 C C   . GLN   D 1 405 ? 47.581  9.371   62.997  1.00 89.07  ?  405 GLN   D C   1 
ATOM   14248 O O   . GLN   D 1 405 ? 48.713  9.160   62.552  1.00 95.05  ?  405 GLN   D O   1 
ATOM   14249 C CB  . GLN   D 1 405 ? 47.383  11.575  61.820  1.00 83.80  ?  405 GLN   D CB  1 
ATOM   14250 C CG  . GLN   D 1 405 ? 46.990  10.876  60.516  1.00 86.86  ?  405 GLN   D CG  1 
ATOM   14251 C CD  . GLN   D 1 405 ? 45.486  10.730  60.350  1.00 85.12  ?  405 GLN   D CD  1 
ATOM   14252 O OE1 . GLN   D 1 405 ? 44.817  11.617  59.811  1.00 79.18  ?  405 GLN   D OE1 1 
ATOM   14253 N NE2 . GLN   D 1 405 ? 44.946  9.604   60.807  1.00 82.22  ?  405 GLN   D NE2 1 
ATOM   14254 N N   . LYS   D 1 406 ? 46.776  8.403   63.432  1.00 81.18  ?  406 LYS   D N   1 
ATOM   14255 C CA  . LYS   D 1 406 ? 47.101  6.998   63.223  1.00 83.34  ?  406 LYS   D CA  1 
ATOM   14256 C C   . LYS   D 1 406 ? 47.328  6.741   61.734  1.00 88.44  ?  406 LYS   D C   1 
ATOM   14257 O O   . LYS   D 1 406 ? 46.624  7.292   60.883  1.00 87.94  ?  406 LYS   D O   1 
ATOM   14258 C CB  . LYS   D 1 406 ? 45.966  6.128   63.773  1.00 77.18  ?  406 LYS   D CB  1 
ATOM   14259 C CG  . LYS   D 1 406 ? 46.292  4.665   64.009  1.00 76.39  ?  406 LYS   D CG  1 
ATOM   14260 C CD  . LYS   D 1 406 ? 45.241  4.046   64.925  1.00 70.60  ?  406 LYS   D CD  1 
ATOM   14261 C CE  . LYS   D 1 406 ? 45.333  2.530   64.969  1.00 67.72  ?  406 LYS   D CE  1 
ATOM   14262 N NZ  . LYS   D 1 406 ? 44.867  1.912   63.701  1.00 68.92  ?  406 LYS   D NZ  1 
ATOM   14263 N N   . HIS   D 1 407 ? 48.336  5.919   61.420  1.00 86.48  ?  407 HIS   D N   1 
ATOM   14264 C CA  . HIS   D 1 407 ? 48.814  5.787   60.044  1.00 79.09  ?  407 HIS   D CA  1 
ATOM   14265 C C   . HIS   D 1 407 ? 47.696  5.348   59.104  1.00 83.28  ?  407 HIS   D C   1 
ATOM   14266 O O   . HIS   D 1 407 ? 47.108  4.275   59.276  1.00 84.61  ?  407 HIS   D O   1 
ATOM   14267 C CB  . HIS   D 1 407 ? 49.978  4.796   59.981  1.00 79.10  ?  407 HIS   D CB  1 
ATOM   14268 C CG  . HIS   D 1 407 ? 50.470  4.531   58.589  1.00 86.27  ?  407 HIS   D CG  1 
ATOM   14269 N ND1 . HIS   D 1 407 ? 50.273  3.327   57.944  1.00 87.43  ?  407 HIS   D ND1 1 
ATOM   14270 C CD2 . HIS   D 1 407 ? 51.143  5.317   57.716  1.00 83.57  ?  407 HIS   D CD2 1 
ATOM   14271 C CE1 . HIS   D 1 407 ? 50.806  3.383   56.737  1.00 81.11  ?  407 HIS   D CE1 1 
ATOM   14272 N NE2 . HIS   D 1 407 ? 51.341  4.580   56.573  1.00 83.73  ?  407 HIS   D NE2 1 
ATOM   14273 N N   . ALA   D 1 408 ? 47.415  6.181   58.099  1.00 84.47  ?  408 ALA   D N   1 
ATOM   14274 C CA  . ALA   D 1 408 ? 46.344  5.929   57.133  1.00 84.23  ?  408 ALA   D CA  1 
ATOM   14275 C C   . ALA   D 1 408 ? 46.885  5.040   56.021  1.00 85.50  ?  408 ALA   D C   1 
ATOM   14276 O O   . ALA   D 1 408 ? 47.346  5.514   54.981  1.00 79.04  ?  408 ALA   D O   1 
ATOM   14277 C CB  . ALA   D 1 408 ? 45.800  7.240   56.582  1.00 77.27  ?  408 ALA   D CB  1 
ATOM   14278 N N   . ASP   D 1 409 ? 46.813  3.725   56.239  1.00 93.71  ?  409 ASP   D N   1 
ATOM   14279 C CA  . ASP   D 1 409 ? 47.324  2.785   55.247  1.00 93.21  ?  409 ASP   D CA  1 
ATOM   14280 C C   . ASP   D 1 409 ? 46.501  2.810   53.963  1.00 92.26  ?  409 ASP   D C   1 
ATOM   14281 O O   . ASP   D 1 409 ? 47.039  2.541   52.883  1.00 91.65  ?  409 ASP   D O   1 
ATOM   14282 C CB  . ASP   D 1 409 ? 47.366  1.371   55.833  1.00 93.36  ?  409 ASP   D CB  1 
ATOM   14283 C CG  . ASP   D 1 409 ? 46.075  0.987   56.538  1.00 92.68  ?  409 ASP   D CG  1 
ATOM   14284 O OD1 . ASP   D 1 409 ? 45.315  1.897   56.937  1.00 93.11  ?  409 ASP   D OD1 1 
ATOM   14285 O OD2 . ASP   D 1 409 ? 45.827  -0.228  56.701  1.00 91.70  ?  409 ASP   D OD2 1 
ATOM   14286 N N   . MET   D 1 410 ? 45.211  3.141   54.053  1.00 85.95  ?  410 MET   D N   1 
ATOM   14287 C CA  A MET   D 1 410 ? 44.320  3.167   52.899  0.49 80.32  ?  410 MET   D CA  1 
ATOM   14288 C CA  B MET   D 1 410 ? 44.350  3.190   52.882  0.51 80.33  ?  410 MET   D CA  1 
ATOM   14289 C C   . MET   D 1 410 ? 43.446  4.411   52.949  1.00 77.96  ?  410 MET   D C   1 
ATOM   14290 O O   . MET   D 1 410 ? 42.968  4.794   54.021  1.00 78.80  ?  410 MET   D O   1 
ATOM   14291 C CB  A MET   D 1 410 ? 43.422  1.921   52.852  0.49 75.84  ?  410 MET   D CB  1 
ATOM   14292 C CB  B MET   D 1 410 ? 43.513  1.910   52.751  0.51 75.87  ?  410 MET   D CB  1 
ATOM   14293 C CG  A MET   D 1 410 ? 44.137  0.623   52.520  0.49 73.49  ?  410 MET   D CG  1 
ATOM   14294 C CG  B MET   D 1 410 ? 43.050  1.319   54.069  0.51 72.12  ?  410 MET   D CG  1 
ATOM   14295 S SD  A MET   D 1 410 ? 44.648  0.511   50.795  0.49 63.47  ?  410 MET   D SD  1 
ATOM   14296 S SD  B MET   D 1 410 ? 42.921  -0.475  53.962  0.51 68.70  ?  410 MET   D SD  1 
ATOM   14297 C CE  A MET   D 1 410 ? 45.095  -1.221  50.704  0.49 56.17  ?  410 MET   D CE  1 
ATOM   14298 C CE  B MET   D 1 410 ? 44.625  -0.910  53.617  0.51 70.43  ?  410 MET   D CE  1 
ATOM   14299 N N   . GLU   D 1 411 ? 43.233  5.027   51.786  1.00 74.88  ?  411 GLU   D N   1 
ATOM   14300 C CA  . GLU   D 1 411 ? 42.310  6.147   51.651  1.00 79.74  ?  411 GLU   D CA  1 
ATOM   14301 C C   . GLU   D 1 411 ? 41.092  5.697   50.855  1.00 81.01  ?  411 GLU   D C   1 
ATOM   14302 O O   . GLU   D 1 411 ? 40.815  6.228   49.774  1.00 78.19  ?  411 GLU   D O   1 
ATOM   14303 C CB  . GLU   D 1 411 ? 42.985  7.343   50.975  1.00 79.03  ?  411 GLU   D CB  1 
ATOM   14304 C CG  . GLU   D 1 411 ? 44.011  8.055   51.838  1.00 80.93  ?  411 GLU   D CG  1 
ATOM   14305 C CD  . GLU   D 1 411 ? 43.387  8.781   53.015  1.00 77.24  ?  411 GLU   D CD  1 
ATOM   14306 O OE1 . GLU   D 1 411 ? 42.331  9.424   52.833  1.00 75.48  ?  411 GLU   D OE1 1 
ATOM   14307 O OE2 . GLU   D 1 411 ? 43.953  8.702   54.126  1.00 79.19  ?  411 GLU   D OE2 1 
ATOM   14308 N N   . PHE   D 1 412 ? 40.371  4.710   51.383  1.00 82.98  ?  412 PHE   D N   1 
ATOM   14309 C CA  . PHE   D 1 412 ? 39.196  4.173   50.713  1.00 77.55  ?  412 PHE   D CA  1 
ATOM   14310 C C   . PHE   D 1 412 ? 38.078  5.209   50.622  1.00 71.65  ?  412 PHE   D C   1 
ATOM   14311 O O   . PHE   D 1 412 ? 38.000  6.150   51.417  1.00 73.84  ?  412 PHE   D O   1 
ATOM   14312 C CB  . PHE   D 1 412 ? 38.676  2.939   51.457  1.00 75.99  ?  412 PHE   D CB  1 
ATOM   14313 C CG  . PHE   D 1 412 ? 39.287  1.639   51.008  1.00 77.24  ?  412 PHE   D CG  1 
ATOM   14314 C CD1 . PHE   D 1 412 ? 40.071  1.575   49.867  1.00 76.19  ?  412 PHE   D CD1 1 
ATOM   14315 C CD2 . PHE   D 1 412 ? 39.055  0.472   51.725  1.00 76.72  ?  412 PHE   D CD2 1 
ATOM   14316 C CE1 . PHE   D 1 412 ? 40.623  0.371   49.456  1.00 74.13  ?  412 PHE   D CE1 1 
ATOM   14317 C CE2 . PHE   D 1 412 ? 39.602  -0.732  51.321  1.00 76.07  ?  412 PHE   D CE2 1 
ATOM   14318 C CZ  . PHE   D 1 412 ? 40.387  -0.784  50.183  1.00 74.71  ?  412 PHE   D CZ  1 
ATOM   14319 N N   . MET   D 1 413 ? 37.219  5.033   49.619  1.00 55.64  ?  413 MET   D N   1 
ATOM   14320 C CA  . MET   D 1 413 ? 35.877  5.601   49.599  1.00 50.83  ?  413 MET   D CA  1 
ATOM   14321 C C   . MET   D 1 413 ? 34.896  4.463   49.385  1.00 42.99  ?  413 MET   D C   1 
ATOM   14322 O O   . MET   D 1 413 ? 35.023  3.707   48.416  1.00 41.95  ?  413 MET   D O   1 
ATOM   14323 C CB  . MET   D 1 413 ? 35.688  6.648   48.501  1.00 47.42  ?  413 MET   D CB  1 
ATOM   14324 C CG  . MET   D 1 413 ? 34.242  7.117   48.414  1.00 36.96  ?  413 MET   D CG  1 
ATOM   14325 S SD  . MET   D 1 413 ? 33.896  8.373   47.173  1.00 44.44  ?  413 MET   D SD  1 
ATOM   14326 C CE  . MET   D 1 413 ? 34.216  7.478   45.656  1.00 42.83  ?  413 MET   D CE  1 
ATOM   14327 N N   . ARG   D 1 414 ? 33.922  4.341   50.280  1.00 41.81  ?  414 ARG   D N   1 
ATOM   14328 C CA  . ARG   D 1 414 ? 32.978  3.235   50.242  1.00 36.87  ?  414 ARG   D CA  1 
ATOM   14329 C C   . ARG   D 1 414 ? 31.679  3.691   49.588  1.00 33.63  ?  414 ARG   D C   1 
ATOM   14330 O O   . ARG   D 1 414 ? 30.995  4.583   50.100  1.00 30.25  ?  414 ARG   D O   1 
ATOM   14331 C CB  . ARG   D 1 414 ? 32.719  2.692   51.644  1.00 34.03  ?  414 ARG   D CB  1 
ATOM   14332 C CG  . ARG   D 1 414 ? 31.973  1.381   51.651  1.00 30.36  ?  414 ARG   D CG  1 
ATOM   14333 C CD  . ARG   D 1 414 ? 31.717  0.895   53.063  1.00 33.13  ?  414 ARG   D CD  1 
ATOM   14334 N NE  . ARG   D 1 414 ? 30.631  1.618   53.710  1.00 35.18  ?  414 ARG   D NE  1 
ATOM   14335 C CZ  . ARG   D 1 414 ? 30.030  1.213   54.822  1.00 42.61  ?  414 ARG   D CZ  1 
ATOM   14336 N NH1 . ARG   D 1 414 ? 30.399  0.101   55.441  1.00 37.92  ?  414 ARG   D NH1 1 
ATOM   14337 N NH2 . ARG   D 1 414 ? 29.027  1.933   55.319  1.00 36.50  ?  414 ARG   D NH2 1 
ATOM   14338 N N   . LEU   D 1 415 ? 31.353  3.085   48.456  1.00 30.67  ?  415 LEU   D N   1 
ATOM   14339 C CA  . LEU   D 1 415 ? 30.062  3.273   47.804  1.00 30.08  ?  415 LEU   D CA  1 
ATOM   14340 C C   . LEU   D 1 415 ? 29.181  2.111   48.253  1.00 28.26  ?  415 LEU   D C   1 
ATOM   14341 O O   . LEU   D 1 415 ? 29.190  1.038   47.646  1.00 25.71  ?  415 LEU   D O   1 
ATOM   14342 C CB  . LEU   D 1 415 ? 30.222  3.319   46.289  1.00 28.15  ?  415 LEU   D CB  1 
ATOM   14343 C CG  . LEU   D 1 415 ? 31.344  4.203   45.734  1.00 28.69  ?  415 LEU   D CG  1 
ATOM   14344 C CD1 . LEU   D 1 415 ? 31.507  3.979   44.235  1.00 28.46  ?  415 LEU   D CD1 1 
ATOM   14345 C CD2 . LEU   D 1 415 ? 31.039  5.655   46.024  1.00 30.46  ?  415 LEU   D CD2 1 
ATOM   14346 N N   . THR   D 1 416 ? 28.414  2.334   49.326  1.00 25.70  ?  416 THR   D N   1 
ATOM   14347 C CA  . THR   D 1 416 ? 27.607  1.295   49.957  1.00 24.67  ?  416 THR   D CA  1 
ATOM   14348 C C   . THR   D 1 416 ? 26.206  1.261   49.349  1.00 23.38  ?  416 THR   D C   1 
ATOM   14349 O O   . THR   D 1 416 ? 25.526  2.291   49.272  1.00 25.33  ?  416 THR   D O   1 
ATOM   14350 C CB  . THR   D 1 416 ? 27.513  1.531   51.466  1.00 25.42  ?  416 THR   D CB  1 
ATOM   14351 O OG1 . THR   D 1 416 ? 28.555  2.416   51.876  1.00 27.48  ?  416 THR   D OG1 1 
ATOM   14352 C CG2 . THR   D 1 416 ? 27.668  0.232   52.224  1.00 25.37  ?  416 THR   D CG2 1 
ATOM   14353 N N   . ILE   D 1 417 ? 25.766  0.070   48.952  1.00 23.02  ?  417 ILE   D N   1 
ATOM   14354 C CA  . ILE   D 1 417 ? 24.552  -0.109  48.160  1.00 23.30  ?  417 ILE   D CA  1 
ATOM   14355 C C   . ILE   D 1 417 ? 23.495  -0.794  49.010  1.00 20.03  ?  417 ILE   D C   1 
ATOM   14356 O O   . ILE   D 1 417 ? 23.678  -1.945  49.426  1.00 23.92  ?  417 ILE   D O   1 
ATOM   14357 C CB  . ILE   D 1 417 ? 24.825  -0.938  46.900  1.00 23.40  ?  417 ILE   D CB  1 
ATOM   14358 C CG1 . ILE   D 1 417 ? 26.148  -0.510  46.252  1.00 25.23  ?  417 ILE   D CG1 1 
ATOM   14359 C CG2 . ILE   D 1 417 ? 23.626  -0.861  45.959  1.00 24.48  ?  417 ILE   D CG2 1 
ATOM   14360 C CD1 . ILE   D 1 417 ? 26.166  0.899   45.707  1.00 28.49  ?  417 ILE   D CD1 1 
ATOM   14361 N N   . ALA   D 1 418 ? 22.381  -0.108  49.241  1.00 21.86  ?  418 ALA   D N   1 
ATOM   14362 C CA  . ALA   D 1 418 ? 21.251  -0.729  49.921  1.00 21.53  ?  418 ALA   D CA  1 
ATOM   14363 C C   . ALA   D 1 418 ? 20.648  -1.823  49.047  1.00 21.26  ?  418 ALA   D C   1 
ATOM   14364 O O   . ALA   D 1 418 ? 20.729  -1.781  47.815  1.00 22.23  ?  418 ALA   D O   1 
ATOM   14365 C CB  . ALA   D 1 418 ? 20.182  0.312   50.255  1.00 21.97  ?  418 ALA   D CB  1 
ATOM   14366 N N   . ARG   D 1 419 ? 20.040  -2.811  49.699  1.00 19.99  ?  419 ARG   D N   1 
ATOM   14367 C CA  . ARG   D 1 419 ? 19.501  -3.970  48.995  1.00 20.17  ?  419 ARG   D CA  1 
ATOM   14368 C C   . ARG   D 1 419 ? 18.129  -3.674  48.408  1.00 19.67  ?  419 ARG   D C   1 
ATOM   14369 O O   . ARG   D 1 419 ? 17.216  -3.259  49.132  1.00 17.97  ?  419 ARG   D O   1 
ATOM   14370 C CB  . ARG   D 1 419 ? 19.400  -5.165  49.941  1.00 17.75  ?  419 ARG   D CB  1 
ATOM   14371 C CG  . ARG   D 1 419 ? 20.733  -5.590  50.527  1.00 17.92  ?  419 ARG   D CG  1 
ATOM   14372 C CD  . ARG   D 1 419 ? 20.558  -6.415  51.805  1.00 18.73  ?  419 ARG   D CD  1 
ATOM   14373 N NE  . ARG   D 1 419 ? 21.869  -6.763  52.337  1.00 20.40  ?  419 ARG   D NE  1 
ATOM   14374 C CZ  . ARG   D 1 419 ? 22.692  -5.886  52.886  1.00 20.88  ?  419 ARG   D CZ  1 
ATOM   14375 N NH1 . ARG   D 1 419 ? 22.318  -4.632  53.095  1.00 20.53  ?  419 ARG   D NH1 1 
ATOM   14376 N NH2 . ARG   D 1 419 ? 23.927  -6.265  53.203  1.00 22.12  ?  419 ARG   D NH2 1 
ATOM   14377 N N   . ARG   D 1 420 ? 17.996  -3.913  47.093  1.00 17.74  ?  420 ARG   D N   1 
ATOM   14378 C CA  . ARG   D 1 420 ? 16.729  -3.858  46.344  1.00 15.35  ?  420 ARG   D CA  1 
ATOM   14379 C C   . ARG   D 1 420 ? 16.134  -2.452  46.315  1.00 16.72  ?  420 ARG   D C   1 
ATOM   14380 O O   . ARG   D 1 420 ? 14.915  -2.287  46.239  1.00 16.53  ?  420 ARG   D O   1 
ATOM   14381 C CB  . ARG   D 1 420 ? 15.704  -4.861  46.889  1.00 18.40  ?  420 ARG   D CB  1 
ATOM   14382 C CG  . ARG   D 1 420 ? 16.242  -6.281  47.038  1.00 17.79  ?  420 ARG   D CG  1 
ATOM   14383 C CD  . ARG   D 1 420 ? 15.141  -7.275  47.321  1.00 15.14  ?  420 ARG   D CD  1 
ATOM   14384 N NE  . ARG   D 1 420 ? 14.409  -6.965  48.544  1.00 16.75  ?  420 ARG   D NE  1 
ATOM   14385 C CZ  . ARG   D 1 420 ? 13.706  -7.853  49.239  1.00 18.02  ?  420 ARG   D CZ  1 
ATOM   14386 N NH1 . ARG   D 1 420 ? 13.604  -9.116  48.850  1.00 16.88  ?  420 ARG   D NH1 1 
ATOM   14387 N NH2 . ARG   D 1 420 ? 13.102  -7.469  50.361  1.00 15.76  ?  420 ARG   D NH2 1 
ATOM   14388 N N   . VAL   D 1 421 ? 16.992  -1.435  46.343  1.00 18.02  ?  421 VAL   D N   1 
ATOM   14389 C CA  . VAL   D 1 421 ? 16.574  -0.040  46.410  1.00 15.17  ?  421 VAL   D CA  1 
ATOM   14390 C C   . VAL   D 1 421 ? 16.868  0.697   45.108  1.00 16.65  ?  421 VAL   D C   1 
ATOM   14391 O O   . VAL   D 1 421 ? 16.009  1.400   44.576  1.00 18.17  ?  421 VAL   D O   1 
ATOM   14392 C CB  . VAL   D 1 421 ? 17.242  0.667   47.612  1.00 17.85  ?  421 VAL   D CB  1 
ATOM   14393 C CG1 . VAL   D 1 421 ? 17.087  2.171   47.501  1.00 18.63  ?  421 VAL   D CG1 1 
ATOM   14394 C CG2 . VAL   D 1 421 ? 16.639  0.159   48.912  1.00 17.30  ?  421 VAL   D CG2 1 
ATOM   14395 N N   . TYR   D 1 422 ? 18.088  0.564   44.590  1.00 15.84  ?  422 TYR   D N   1 
ATOM   14396 C CA  . TYR   D 1 422 ? 18.523  1.290   43.406  1.00 17.71  ?  422 TYR   D CA  1 
ATOM   14397 C C   . TYR   D 1 422 ? 18.702  0.337   42.231  1.00 23.00  ?  422 TYR   D C   1 
ATOM   14398 O O   . TYR   D 1 422 ? 19.053  -0.836  42.408  1.00 19.11  ?  422 TYR   D O   1 
ATOM   14399 C CB  . TYR   D 1 422 ? 19.836  2.039   43.656  1.00 17.84  ?  422 TYR   D CB  1 
ATOM   14400 C CG  . TYR   D 1 422 ? 19.766  3.020   44.805  1.00 18.21  ?  422 TYR   D CG  1 
ATOM   14401 C CD1 . TYR   D 1 422 ? 19.114  4.238   44.661  1.00 20.65  ?  422 TYR   D CD1 1 
ATOM   14402 C CD2 . TYR   D 1 422 ? 20.355  2.732   46.029  1.00 20.71  ?  422 TYR   D CD2 1 
ATOM   14403 C CE1 . TYR   D 1 422 ? 19.039  5.136   45.709  1.00 19.31  ?  422 TYR   D CE1 1 
ATOM   14404 C CE2 . TYR   D 1 422 ? 20.289  3.627   47.087  1.00 21.05  ?  422 TYR   D CE2 1 
ATOM   14405 C CZ  . TYR   D 1 422 ? 19.628  4.829   46.916  1.00 22.56  ?  422 TYR   D CZ  1 
ATOM   14406 O OH  . TYR   D 1 422 ? 19.554  5.728   47.950  1.00 25.55  ?  422 TYR   D OH  1 
ATOM   14407 N N   . THR   D 1 423 ? 18.452  0.860   41.030  1.00 21.43  ?  423 THR   D N   1 
ATOM   14408 C CA  . THR   D 1 423 ? 18.554  0.113   39.785  1.00 21.85  ?  423 THR   D CA  1 
ATOM   14409 C C   . THR   D 1 423 ? 19.956  0.268   39.201  1.00 21.24  ?  423 THR   D C   1 
ATOM   14410 O O   . THR   D 1 423 ? 20.777  1.054   39.681  1.00 19.93  ?  423 THR   D O   1 
ATOM   14411 C CB  . THR   D 1 423 ? 17.495  0.581   38.774  1.00 20.92  ?  423 THR   D CB  1 
ATOM   14412 O OG1 . THR   D 1 423 ? 17.877  1.841   38.216  1.00 21.07  ?  423 THR   D OG1 1 
ATOM   14413 C CG2 . THR   D 1 423 ? 16.118  0.736   39.446  1.00 18.86  ?  423 THR   D CG2 1 
ATOM   14414 N N   . ASN   D 1 424 ? 20.241  -0.516  38.161  1.00 19.26  ?  424 ASN   D N   1 
ATOM   14415 C CA  . ASN   D 1 424 ? 21.535  -0.387  37.502  1.00 20.49  ?  424 ASN   D CA  1 
ATOM   14416 C C   . ASN   D 1 424 ? 21.671  0.947   36.783  1.00 19.90  ?  424 ASN   D C   1 
ATOM   14417 O O   . ASN   D 1 424 ? 22.794  1.396   36.536  1.00 24.83  ?  424 ASN   D O   1 
ATOM   14418 C CB  . ASN   D 1 424 ? 21.754  -1.540  36.518  1.00 25.43  ?  424 ASN   D CB  1 
ATOM   14419 C CG  . ASN   D 1 424 ? 21.940  -2.880  37.217  1.00 26.70  ?  424 ASN   D CG  1 
ATOM   14420 O OD1 . ASN   D 1 424 ? 22.645  -2.980  38.222  1.00 25.62  ?  424 ASN   D OD1 1 
ATOM   14421 N ND2 . ASN   D 1 424 ? 21.300  -3.917  36.686  1.00 25.22  ?  424 ASN   D ND2 1 
ATOM   14422 N N   . ASP   D 1 425 ? 20.554  1.588   36.440  1.00 19.82  ?  425 ASP   D N   1 
ATOM   14423 C CA  . ASP   D 1 425 ? 20.619  2.953   35.938  1.00 19.24  ?  425 ASP   D CA  1 
ATOM   14424 C C   . ASP   D 1 425 ? 21.042  3.920   37.040  1.00 23.50  ?  425 ASP   D C   1 
ATOM   14425 O O   . ASP   D 1 425 ? 21.714  4.922   36.766  1.00 22.77  ?  425 ASP   D O   1 
ATOM   14426 C CB  . ASP   D 1 425 ? 19.271  3.350   35.341  1.00 20.21  ?  425 ASP   D CB  1 
ATOM   14427 C CG  . ASP   D 1 425 ? 18.995  2.659   34.011  1.00 23.09  ?  425 ASP   D CG  1 
ATOM   14428 O OD1 . ASP   D 1 425 ? 19.899  1.983   33.489  1.00 26.32  ?  425 ASP   D OD1 1 
ATOM   14429 O OD2 . ASP   D 1 425 ? 17.875  2.791   33.479  1.00 27.01  ?  425 ASP   D OD2 1 
ATOM   14430 N N   . HIS   D 1 426 ? 20.668  3.640   38.286  1.00 18.63  ?  426 HIS   D N   1 
ATOM   14431 C CA  . HIS   D 1 426 ? 21.236  4.396   39.395  1.00 21.77  ?  426 HIS   D CA  1 
ATOM   14432 C C   . HIS   D 1 426 ? 22.734  4.143   39.502  1.00 24.79  ?  426 HIS   D C   1 
ATOM   14433 O O   . HIS   D 1 426 ? 23.512  5.070   39.757  1.00 25.45  ?  426 HIS   D O   1 
ATOM   14434 C CB  . HIS   D 1 426 ? 20.536  4.037   40.708  1.00 23.38  ?  426 HIS   D CB  1 
ATOM   14435 C CG  . HIS   D 1 426 ? 19.133  4.555   40.816  1.00 21.36  ?  426 HIS   D CG  1 
ATOM   14436 N ND1 . HIS   D 1 426 ? 18.059  3.737   41.093  1.00 20.32  ?  426 HIS   D ND1 1 
ATOM   14437 C CD2 . HIS   D 1 426 ? 18.630  5.808   40.702  1.00 20.58  ?  426 HIS   D CD2 1 
ATOM   14438 C CE1 . HIS   D 1 426 ? 16.952  4.458   41.126  1.00 19.16  ?  426 HIS   D CE1 1 
ATOM   14439 N NE2 . HIS   D 1 426 ? 17.271  5.718   40.892  1.00 21.38  ?  426 HIS   D NE2 1 
ATOM   14440 N N   . MET   D 1 427 ? 23.159  2.891   39.299  1.00 20.50  ?  427 MET   D N   1 
ATOM   14441 C CA  . MET   D 1 427 ? 24.585  2.578   39.314  1.00 24.74  ?  427 MET   D CA  1 
ATOM   14442 C C   . MET   D 1 427 ? 25.329  3.341   38.225  1.00 24.57  ?  427 MET   D C   1 
ATOM   14443 O O   . MET   D 1 427 ? 26.414  3.881   38.475  1.00 26.44  ?  427 MET   D O   1 
ATOM   14444 C CB  . MET   D 1 427 ? 24.800  1.073   39.150  1.00 20.15  ?  427 MET   D CB  1 
ATOM   14445 C CG  . MET   D 1 427 ? 24.160  0.210   40.232  1.00 21.57  ?  427 MET   D CG  1 
ATOM   14446 S SD  . MET   D 1 427 ? 24.673  0.612   41.911  1.00 25.26  ?  427 MET   D SD  1 
ATOM   14447 C CE  . MET   D 1 427 ? 23.227  1.530   42.461  1.00 22.01  ?  427 MET   D CE  1 
ATOM   14448 N N   . ASP   D 1 428 ? 24.759  3.398   37.013  1.00 23.14  ?  428 ASP   D N   1 
ATOM   14449 C CA  . ASP   D 1 428 ? 25.382  4.153   35.926  1.00 25.45  ?  428 ASP   D CA  1 
ATOM   14450 C C   . ASP   D 1 428 ? 25.555  5.620   36.297  1.00 27.03  ?  428 ASP   D C   1 
ATOM   14451 O O   . ASP   D 1 428 ? 26.606  6.216   36.035  1.00 29.69  ?  428 ASP   D O   1 
ATOM   14452 C CB  . ASP   D 1 428 ? 24.554  4.027   34.648  1.00 22.28  ?  428 ASP   D CB  1 
ATOM   14453 C CG  . ASP   D 1 428 ? 24.766  2.704   33.944  1.00 25.17  ?  428 ASP   D CG  1 
ATOM   14454 O OD1 . ASP   D 1 428 ? 25.817  2.072   34.156  1.00 28.22  ?  428 ASP   D OD1 1 
ATOM   14455 O OD2 . ASP   D 1 428 ? 23.886  2.294   33.166  1.00 27.76  ?  428 ASP   D OD2 1 
ATOM   14456 N N   . TYR   D 1 429 ? 24.533  6.223   36.904  1.00 26.42  ?  429 TYR   D N   1 
ATOM   14457 C CA  . TYR   D 1 429 ? 24.662  7.607   37.342  1.00 28.90  ?  429 TYR   D CA  1 
ATOM   14458 C C   . TYR   D 1 429 ? 25.807  7.756   38.330  1.00 32.35  ?  429 TYR   D C   1 
ATOM   14459 O O   . TYR   D 1 429 ? 26.610  8.692   38.224  1.00 35.55  ?  429 TYR   D O   1 
ATOM   14460 C CB  . TYR   D 1 429 ? 23.345  8.085   37.952  1.00 29.49  ?  429 TYR   D CB  1 
ATOM   14461 C CG  . TYR   D 1 429 ? 23.378  9.498   38.499  1.00 33.02  ?  429 TYR   D CG  1 
ATOM   14462 C CD1 . TYR   D 1 429 ? 23.794  9.749   39.801  1.00 35.27  ?  429 TYR   D CD1 1 
ATOM   14463 C CD2 . TYR   D 1 429 ? 22.972  10.577  37.724  1.00 32.48  ?  429 TYR   D CD2 1 
ATOM   14464 C CE1 . TYR   D 1 429 ? 23.823  11.034  40.309  1.00 39.10  ?  429 TYR   D CE1 1 
ATOM   14465 C CE2 . TYR   D 1 429 ? 22.992  11.867  38.227  1.00 32.35  ?  429 TYR   D CE2 1 
ATOM   14466 C CZ  . TYR   D 1 429 ? 23.416  12.088  39.519  1.00 40.54  ?  429 TYR   D CZ  1 
ATOM   14467 O OH  . TYR   D 1 429 ? 23.440  13.363  40.037  1.00 41.48  ?  429 TYR   D OH  1 
ATOM   14468 N N   . ILE   D 1 430 ? 25.907  6.831   39.290  1.00 28.57  ?  430 ILE   D N   1 
ATOM   14469 C CA  . ILE   D 1 430 ? 27.022  6.848   40.235  1.00 33.11  ?  430 ILE   D CA  1 
ATOM   14470 C C   . ILE   D 1 430 ? 28.348  6.751   39.494  1.00 32.87  ?  430 ILE   D C   1 
ATOM   14471 O O   . ILE   D 1 430 ? 29.266  7.543   39.729  1.00 35.70  ?  430 ILE   D O   1 
ATOM   14472 C CB  . ILE   D 1 430 ? 26.880  5.711   41.263  1.00 27.03  ?  430 ILE   D CB  1 
ATOM   14473 C CG1 . ILE   D 1 430 ? 25.635  5.917   42.122  1.00 26.36  ?  430 ILE   D CG1 1 
ATOM   14474 C CG2 . ILE   D 1 430 ? 28.133  5.616   42.126  1.00 33.21  ?  430 ILE   D CG2 1 
ATOM   14475 C CD1 . ILE   D 1 430 ? 25.222  4.678   42.873  1.00 24.89  ?  430 ILE   D CD1 1 
ATOM   14476 N N   . ALA   D 1 431 ? 28.464  5.781   38.582  1.00 34.05  ?  431 ALA   D N   1 
ATOM   14477 C CA  . ALA   D 1 431 ? 29.721  5.584   37.867  1.00 32.83  ?  431 ALA   D CA  1 
ATOM   14478 C C   . ALA   D 1 431 ? 30.089  6.817   37.054  1.00 36.56  ?  431 ALA   D C   1 
ATOM   14479 O O   . ALA   D 1 431 ? 31.222  7.308   37.127  1.00 40.23  ?  431 ALA   D O   1 
ATOM   14480 C CB  . ALA   D 1 431 ? 29.625  4.356   36.959  1.00 32.06  ?  431 ALA   D CB  1 
ATOM   14481 N N   . ASP   D 1 432 ? 29.140  7.335   36.271  1.00 34.64  ?  432 ASP   D N   1 
ATOM   14482 C CA  . ASP   D 1 432 ? 29.448  8.466   35.400  1.00 37.86  ?  432 ASP   D CA  1 
ATOM   14483 C C   . ASP   D 1 432 ? 29.824  9.699   36.207  1.00 39.54  ?  432 ASP   D C   1 
ATOM   14484 O O   . ASP   D 1 432 ? 30.711  10.462  35.807  1.00 46.01  ?  432 ASP   D O   1 
ATOM   14485 C CB  . ASP   D 1 432 ? 28.263  8.765   34.488  1.00 40.90  ?  432 ASP   D CB  1 
ATOM   14486 C CG  . ASP   D 1 432 ? 27.888  7.584   33.630  1.00 37.42  ?  432 ASP   D CG  1 
ATOM   14487 O OD1 . ASP   D 1 432 ? 28.769  6.733   33.381  1.00 36.45  ?  432 ASP   D OD1 1 
ATOM   14488 O OD2 . ASP   D 1 432 ? 26.713  7.502   33.216  1.00 43.68  ?  432 ASP   D OD2 1 
ATOM   14489 N N   . ALA   D 1 433 ? 29.164  9.911   37.346  1.00 39.73  ?  433 ALA   D N   1 
ATOM   14490 C CA  . ALA   D 1 433 ? 29.533  11.020  38.219  1.00 39.86  ?  433 ALA   D CA  1 
ATOM   14491 C C   . ALA   D 1 433 ? 30.998  10.931  38.621  1.00 43.73  ?  433 ALA   D C   1 
ATOM   14492 O O   . ALA   D 1 433 ? 31.760  11.891  38.461  1.00 49.15  ?  433 ALA   D O   1 
ATOM   14493 C CB  . ALA   D 1 433 ? 28.643  11.032  39.458  1.00 37.47  ?  433 ALA   D CB  1 
ATOM   14494 N N   . LEU   D 1 434 ? 31.411  9.773   39.137  1.00 41.95  ?  434 LEU   D N   1 
ATOM   14495 C CA  . LEU   D 1 434 ? 32.775  9.634   39.626  1.00 39.75  ?  434 LEU   D CA  1 
ATOM   14496 C C   . LEU   D 1 434 ? 33.777  9.683   38.483  1.00 47.52  ?  434 LEU   D C   1 
ATOM   14497 O O   . LEU   D 1 434 ? 34.850  10.280  38.620  1.00 51.38  ?  434 LEU   D O   1 
ATOM   14498 C CB  . LEU   D 1 434 ? 32.918  8.335   40.415  1.00 41.42  ?  434 LEU   D CB  1 
ATOM   14499 C CG  . LEU   D 1 434 ? 34.239  8.184   41.161  1.00 44.93  ?  434 LEU   D CG  1 
ATOM   14500 C CD1 . LEU   D 1 434 ? 34.538  9.433   41.976  1.00 47.10  ?  434 LEU   D CD1 1 
ATOM   14501 C CD2 . LEU   D 1 434 ? 34.215  6.952   42.053  1.00 44.29  ?  434 LEU   D CD2 1 
ATOM   14502 N N   . ILE   D 1 435 ? 33.445  9.068   37.346  1.00 45.00  ?  435 ILE   D N   1 
ATOM   14503 C CA  . ILE   D 1 435 ? 34.340  9.123   36.195  1.00 45.97  ?  435 ILE   D CA  1 
ATOM   14504 C C   . ILE   D 1 435 ? 34.486  10.560  35.718  1.00 56.04  ?  435 ILE   D C   1 
ATOM   14505 O O   . ILE   D 1 435 ? 35.598  11.043  35.468  1.00 56.64  ?  435 ILE   D O   1 
ATOM   14506 C CB  . ILE   D 1 435 ? 33.833  8.206   35.070  1.00 37.76  ?  435 ILE   D CB  1 
ATOM   14507 C CG1 . ILE   D 1 435 ? 33.844  6.748   35.529  1.00 41.11  ?  435 ILE   D CG1 1 
ATOM   14508 C CG2 . ILE   D 1 435 ? 34.704  8.366   33.841  1.00 43.24  ?  435 ILE   D CG2 1 
ATOM   14509 C CD1 . ILE   D 1 435 ? 33.020  5.822   34.655  1.00 37.62  ?  435 ILE   D CD1 1 
ATOM   14510 N N   . GLY   D 1 436 ? 33.363  11.271  35.604  1.00 50.88  ?  436 GLY   D N   1 
ATOM   14511 C CA  . GLY   D 1 436 ? 33.372  12.661  35.180  1.00 51.60  ?  436 GLY   D CA  1 
ATOM   14512 C C   . GLY   D 1 436 ? 34.178  13.579  36.074  1.00 57.94  ?  436 GLY   D C   1 
ATOM   14513 O O   . GLY   D 1 436 ? 34.449  14.719  35.678  1.00 63.96  ?  436 GLY   D O   1 
ATOM   14514 N N   . LEU   D 1 437 ? 34.560  13.118  37.265  1.00 57.99  ?  437 LEU   D N   1 
ATOM   14515 C CA  . LEU   D 1 437 ? 35.434  13.886  38.140  1.00 64.38  ?  437 LEU   D CA  1 
ATOM   14516 C C   . LEU   D 1 437 ? 36.895  13.816  37.717  1.00 70.16  ?  437 LEU   D C   1 
ATOM   14517 O O   . LEU   D 1 437 ? 37.749  14.388  38.401  1.00 74.34  ?  437 LEU   D O   1 
ATOM   14518 C CB  . LEU   D 1 437 ? 35.291  13.413  39.592  1.00 55.77  ?  437 LEU   D CB  1 
ATOM   14519 C CG  . LEU   D 1 437 ? 34.028  13.826  40.352  1.00 53.10  ?  437 LEU   D CG  1 
ATOM   14520 C CD1 . LEU   D 1 437 ? 34.103  13.351  41.786  1.00 52.00  ?  437 LEU   D CD1 1 
ATOM   14521 C CD2 . LEU   D 1 437 ? 33.825  15.330  40.309  1.00 57.10  ?  437 LEU   D CD2 1 
ATOM   14522 N N   . LYS   D 1 438 ? 37.204  13.137  36.616  1.00 68.23  ?  438 LYS   D N   1 
ATOM   14523 C CA  . LYS   D 1 438 ? 38.546  13.178  36.052  1.00 77.76  ?  438 LYS   D CA  1 
ATOM   14524 C C   . LYS   D 1 438 ? 38.821  14.475  35.302  1.00 79.38  ?  438 LYS   D C   1 
ATOM   14525 O O   . LYS   D 1 438 ? 39.855  14.586  34.634  1.00 82.66  ?  438 LYS   D O   1 
ATOM   14526 C CB  . LYS   D 1 438 ? 38.780  11.980  35.128  1.00 72.54  ?  438 LYS   D CB  1 
ATOM   14527 C CG  . LYS   D 1 438 ? 38.830  10.640  35.848  1.00 73.71  ?  438 LYS   D CG  1 
ATOM   14528 C CD  . LYS   D 1 438 ? 40.096  9.873   35.502  1.00 76.86  ?  438 LYS   D CD  1 
ATOM   14529 C CE  . LYS   D 1 438 ? 39.956  8.395   35.836  1.00 69.15  ?  438 LYS   D CE  1 
ATOM   14530 N NZ  . LYS   D 1 438 ? 38.920  7.730   34.993  1.00 61.53  ?  438 LYS   D NZ  1 
ATOM   14531 N N   . GLU   D 1 439 ? 37.916  15.446  35.390  1.00 85.01  ?  439 GLU   D N   1 
ATOM   14532 C CA  . GLU   D 1 439 ? 38.128  16.769  34.820  1.00 91.38  ?  439 GLU   D CA  1 
ATOM   14533 C C   . GLU   D 1 439 ? 38.772  17.708  35.834  1.00 93.10  ?  439 GLU   D C   1 
ATOM   14534 O O   . GLU   D 1 439 ? 39.769  18.370  35.528  1.00 93.19  ?  439 GLU   D O   1 
ATOM   14535 C CB  . GLU   D 1 439 ? 36.794  17.341  34.321  1.00 93.11  ?  439 GLU   D CB  1 
ATOM   14536 C CG  . GLU   D 1 439 ? 36.875  18.748  33.744  1.00 101.43 ?  439 GLU   D CG  1 
ATOM   14537 C CD  . GLU   D 1 439 ? 37.507  18.791  32.365  1.00 102.45 ?  439 GLU   D CD  1 
ATOM   14538 O OE1 . GLU   D 1 439 ? 37.766  17.713  31.790  1.00 99.91  ?  439 GLU   D OE1 1 
ATOM   14539 O OE2 . GLU   D 1 439 ? 37.741  19.907  31.855  1.00 108.18 ?  439 GLU   D OE2 1 
ATOM   14540 N N   . LYS   D 1 440 ? 38.223  17.760  37.049  1.00 90.03  ?  440 LYS   D N   1 
ATOM   14541 C CA  . LYS   D 1 440 ? 38.736  18.617  38.111  1.00 88.81  ?  440 LYS   D CA  1 
ATOM   14542 C C   . LYS   D 1 440 ? 39.364  17.817  39.248  1.00 81.83  ?  440 LYS   D C   1 
ATOM   14543 O O   . LYS   D 1 440 ? 39.484  18.330  40.365  1.00 82.13  ?  440 LYS   D O   1 
ATOM   14544 C CB  . LYS   D 1 440 ? 37.622  19.519  38.647  1.00 88.83  ?  440 LYS   D CB  1 
ATOM   14545 C CG  . LYS   D 1 440 ? 36.885  20.312  37.570  1.00 92.40  ?  440 LYS   D CG  1 
ATOM   14546 C CD  . LYS   D 1 440 ? 37.853  21.120  36.712  1.00 93.94  ?  440 LYS   D CD  1 
ATOM   14547 C CE  . LYS   D 1 440 ? 37.132  21.860  35.593  1.00 92.58  ?  440 LYS   D CE  1 
ATOM   14548 N NZ  . LYS   D 1 440 ? 38.080  22.398  34.573  1.00 85.43  ?  440 LYS   D NZ  1 
ATOM   14549 N N   . PHE   D 1 441 ? 39.765  16.568  38.988  1.00 78.26  ?  441 PHE   D N   1 
ATOM   14550 C CA  . PHE   D 1 441 ? 40.369  15.754  40.038  1.00 72.94  ?  441 PHE   D CA  1 
ATOM   14551 C C   . PHE   D 1 441 ? 41.644  16.396  40.561  1.00 80.64  ?  441 PHE   D C   1 
ATOM   14552 O O   . PHE   D 1 441 ? 41.928  16.344  41.764  1.00 81.56  ?  441 PHE   D O   1 
ATOM   14553 C CB  . PHE   D 1 441 ? 40.651  14.338  39.524  1.00 75.50  ?  441 PHE   D CB  1 
ATOM   14554 C CG  . PHE   D 1 441 ? 41.764  14.259  38.501  1.00 85.25  ?  441 PHE   D CG  1 
ATOM   14555 C CD1 . PHE   D 1 441 ? 43.093  14.115  38.892  1.00 83.20  ?  441 PHE   D CD1 1 
ATOM   14556 C CD2 . PHE   D 1 441 ? 41.481  14.310  37.151  1.00 83.07  ?  441 PHE   D CD2 1 
ATOM   14557 C CE1 . PHE   D 1 441 ? 44.108  14.043  37.959  1.00 77.49  ?  441 PHE   D CE1 1 
ATOM   14558 C CE2 . PHE   D 1 441 ? 42.489  14.230  36.208  1.00 86.88  ?  441 PHE   D CE2 1 
ATOM   14559 C CZ  . PHE   D 1 441 ? 43.807  14.098  36.613  1.00 89.66  ?  441 PHE   D CZ  1 
ATOM   14560 N N   . ALA   D 1 442 ? 42.424  17.012  39.669  1.00 86.55  ?  442 ALA   D N   1 
ATOM   14561 C CA  . ALA   D 1 442 ? 43.694  17.614  40.058  1.00 82.51  ?  442 ALA   D CA  1 
ATOM   14562 C C   . ALA   D 1 442 ? 43.478  18.960  40.738  1.00 83.26  ?  442 ALA   D C   1 
ATOM   14563 O O   . ALA   D 1 442 ? 44.035  19.217  41.809  1.00 81.56  ?  442 ALA   D O   1 
ATOM   14564 C CB  . ALA   D 1 442 ? 44.599  17.764  38.836  1.00 79.98  ?  442 ALA   D CB  1 
ATOM   14565 N N   . THR   D 1 443 ? 42.668  19.830  40.132  1.00 85.67  ?  443 THR   D N   1 
ATOM   14566 C CA  . THR   D 1 443 ? 42.344  21.130  40.722  1.00 88.00  ?  443 THR   D CA  1 
ATOM   14567 C C   . THR   D 1 443 ? 41.318  20.922  41.836  1.00 88.48  ?  443 THR   D C   1 
ATOM   14568 O O   . THR   D 1 443 ? 40.131  21.228  41.712  1.00 94.22  ?  443 THR   D O   1 
ATOM   14569 C CB  . THR   D 1 443 ? 41.829  22.093  39.660  1.00 95.18  ?  443 THR   D CB  1 
ATOM   14570 O OG1 . THR   D 1 443 ? 42.694  22.059  38.517  1.00 98.59  ?  443 THR   D OG1 1 
ATOM   14571 C CG2 . THR   D 1 443 ? 41.783  23.516  40.206  1.00 93.66  ?  443 THR   D CG2 1 
ATOM   14572 N N   . LEU   D 1 444 ? 41.804  20.375  42.950  1.00 87.65  ?  444 LEU   D N   1 
ATOM   14573 C CA  . LEU   D 1 444 ? 40.958  20.040  44.089  1.00 83.12  ?  444 LEU   D CA  1 
ATOM   14574 C C   . LEU   D 1 444 ? 41.640  20.517  45.362  1.00 84.15  ?  444 LEU   D C   1 
ATOM   14575 O O   . LEU   D 1 444 ? 42.778  20.126  45.642  1.00 80.45  ?  444 LEU   D O   1 
ATOM   14576 C CB  . LEU   D 1 444 ? 40.685  18.533  44.147  1.00 81.68  ?  444 LEU   D CB  1 
ATOM   14577 C CG  . LEU   D 1 444 ? 39.246  18.115  44.476  1.00 80.04  ?  444 LEU   D CG  1 
ATOM   14578 C CD1 . LEU   D 1 444 ? 38.260  18.592  43.407  1.00 72.63  ?  444 LEU   D CD1 1 
ATOM   14579 C CD2 . LEU   D 1 444 ? 39.151  16.610  44.665  1.00 72.37  ?  444 LEU   D CD2 1 
ATOM   14580 N N   . LYS   D 1 445 ? 40.947  21.356  46.128  1.00 84.81  ?  445 LYS   D N   1 
ATOM   14581 C CA  . LYS   D 1 445 ? 41.510  21.921  47.346  1.00 85.54  ?  445 LYS   D CA  1 
ATOM   14582 C C   . LYS   D 1 445 ? 41.341  20.966  48.523  1.00 83.62  ?  445 LYS   D C   1 
ATOM   14583 O O   . LYS   D 1 445 ? 40.363  20.215  48.612  1.00 84.93  ?  445 LYS   D O   1 
ATOM   14584 C CB  . LYS   D 1 445 ? 40.849  23.262  47.676  1.00 92.36  ?  445 LYS   D CB  1 
ATOM   14585 C CG  . LYS   D 1 445 ? 41.182  24.393  46.710  1.00 101.36 ?  445 LYS   D CG  1 
ATOM   14586 C CD  . LYS   D 1 445 ? 40.348  25.635  47.002  1.00 101.56 ?  445 LYS   D CD  1 
ATOM   14587 C CE  . LYS   D 1 445 ? 40.750  26.798  46.106  1.00 104.35 ?  445 LYS   D CE  1 
ATOM   14588 N NZ  . LYS   D 1 445 ? 39.851  27.975  46.263  1.00 101.16 ?  445 LYS   D NZ  1 
ATOM   14589 N N   . GLY   D 1 446 ? 42.321  21.001  49.434  1.00 80.40  ?  446 GLY   D N   1 
ATOM   14590 C CA  . GLY   D 1 446 ? 42.233  20.253  50.668  1.00 78.03  ?  446 GLY   D CA  1 
ATOM   14591 C C   . GLY   D 1 446 ? 41.360  20.949  51.695  1.00 78.89  ?  446 GLY   D C   1 
ATOM   14592 O O   . GLY   D 1 446 ? 40.963  22.103  51.538  1.00 79.62  ?  446 GLY   D O   1 
ATOM   14593 N N   . LEU   D 1 447 ? 41.057  20.222  52.768  1.00 77.32  ?  447 LEU   D N   1 
ATOM   14594 C CA  . LEU   D 1 447 ? 40.149  20.695  53.801  1.00 75.01  ?  447 LEU   D CA  1 
ATOM   14595 C C   . LEU   D 1 447 ? 40.849  20.693  55.156  1.00 76.65  ?  447 LEU   D C   1 
ATOM   14596 O O   . LEU   D 1 447 ? 41.847  19.997  55.367  1.00 77.12  ?  447 LEU   D O   1 
ATOM   14597 C CB  . LEU   D 1 447 ? 38.870  19.840  53.852  1.00 75.03  ?  447 LEU   D CB  1 
ATOM   14598 C CG  . LEU   D 1 447 ? 37.813  20.015  52.746  1.00 77.03  ?  447 LEU   D CG  1 
ATOM   14599 C CD1 . LEU   D 1 447 ? 38.308  19.600  51.363  1.00 73.65  ?  447 LEU   D CD1 1 
ATOM   14600 C CD2 . LEU   D 1 447 ? 36.546  19.247  53.082  1.00 69.07  ?  447 LEU   D CD2 1 
ATOM   14601 N N   . GLU   D 1 448 ? 40.316  21.490  56.080  1.00 76.29  ?  448 GLU   D N   1 
ATOM   14602 C CA  . GLU   D 1 448 ? 40.924  21.662  57.392  1.00 82.76  ?  448 GLU   D CA  1 
ATOM   14603 C C   . GLU   D 1 448 ? 39.827  21.675  58.448  1.00 88.19  ?  448 GLU   D C   1 
ATOM   14604 O O   . GLU   D 1 448 ? 38.667  21.983  58.162  1.00 82.23  ?  448 GLU   D O   1 
ATOM   14605 C CB  . GLU   D 1 448 ? 41.762  22.952  57.455  1.00 70.27  ?  448 GLU   D CB  1 
ATOM   14606 C CG  . GLU   D 1 448 ? 42.547  23.153  58.749  1.00 71.28  ?  448 GLU   D CG  1 
ATOM   14607 C CD  . GLU   D 1 448 ? 43.346  24.442  58.753  1.00 76.38  ?  448 GLU   D CD  1 
ATOM   14608 O OE1 . GLU   D 1 448 ? 43.718  24.911  57.654  1.00 76.35  ?  448 GLU   D OE1 1 
ATOM   14609 O OE2 . GLU   D 1 448 ? 43.599  24.991  59.849  1.00 73.17  ?  448 GLU   D OE2 1 
ATOM   14610 N N   . PHE   D 1 449 ? 40.207  21.325  59.678  1.00 85.00  ?  449 PHE   D N   1 
ATOM   14611 C CA  . PHE   D 1 449 ? 39.274  21.322  60.800  1.00 85.74  ?  449 PHE   D CA  1 
ATOM   14612 C C   . PHE   D 1 449 ? 38.897  22.752  61.163  1.00 89.91  ?  449 PHE   D C   1 
ATOM   14613 O O   . PHE   D 1 449 ? 39.745  23.533  61.608  1.00 93.12  ?  449 PHE   D O   1 
ATOM   14614 C CB  . PHE   D 1 449 ? 39.884  20.612  62.004  1.00 84.39  ?  449 PHE   D CB  1 
ATOM   14615 C CG  . PHE   D 1 449 ? 39.838  19.117  61.916  1.00 84.61  ?  449 PHE   D CG  1 
ATOM   14616 C CD1 . PHE   D 1 449 ? 38.638  18.441  62.039  1.00 90.80  ?  449 PHE   D CD1 1 
ATOM   14617 C CD2 . PHE   D 1 449 ? 40.996  18.386  61.726  1.00 85.26  ?  449 PHE   D CD2 1 
ATOM   14618 C CE1 . PHE   D 1 449 ? 38.591  17.064  61.960  1.00 85.53  ?  449 PHE   D CE1 1 
ATOM   14619 C CE2 . PHE   D 1 449 ? 40.957  17.011  61.655  1.00 81.37  ?  449 PHE   D CE2 1 
ATOM   14620 C CZ  . PHE   D 1 449 ? 39.753  16.348  61.767  1.00 82.74  ?  449 PHE   D CZ  1 
ATOM   14621 N N   . GLU   D 1 450 ? 37.627  23.099  60.961  1.00 91.93  ?  450 GLU   D N   1 
ATOM   14622 C CA  . GLU   D 1 450 ? 37.067  24.317  61.530  1.00 89.44  ?  450 GLU   D CA  1 
ATOM   14623 C C   . GLU   D 1 450 ? 36.478  24.069  62.910  1.00 88.20  ?  450 GLU   D C   1 
ATOM   14624 O O   . GLU   D 1 450 ? 36.536  24.953  63.773  1.00 90.74  ?  450 GLU   D O   1 
ATOM   14625 C CB  . GLU   D 1 450 ? 35.997  24.896  60.599  1.00 87.55  ?  450 GLU   D CB  1 
ATOM   14626 C CG  . GLU   D 1 450 ? 35.577  26.314  60.948  1.00 100.04 ?  450 GLU   D CG  1 
ATOM   14627 C CD  . GLU   D 1 450 ? 34.485  26.849  60.039  1.00 105.29 ?  450 GLU   D CD  1 
ATOM   14628 O OE1 . GLU   D 1 450 ? 33.771  26.034  59.413  1.00 103.21 ?  450 GLU   D OE1 1 
ATOM   14629 O OE2 . GLU   D 1 450 ? 34.343  28.088  59.949  1.00 108.78 ?  450 GLU   D OE2 1 
ATOM   14630 N N   . TYR   D 1 451 ? 35.918  22.881  63.130  1.00 85.60  ?  451 TYR   D N   1 
ATOM   14631 C CA  . TYR   D 1 451 ? 35.480  22.443  64.453  1.00 85.59  ?  451 TYR   D CA  1 
ATOM   14632 C C   . TYR   D 1 451 ? 35.735  20.945  64.534  1.00 82.87  ?  451 TYR   D C   1 
ATOM   14633 O O   . TYR   D 1 451 ? 35.121  20.173  63.792  1.00 83.61  ?  451 TYR   D O   1 
ATOM   14634 C CB  . TYR   D 1 451 ? 34.006  22.768  64.693  1.00 82.22  ?  451 TYR   D CB  1 
ATOM   14635 C CG  . TYR   D 1 451 ? 33.325  21.868  65.706  1.00 84.67  ?  451 TYR   D CG  1 
ATOM   14636 C CD1 . TYR   D 1 451 ? 33.548  22.023  67.070  1.00 83.52  ?  451 TYR   D CD1 1 
ATOM   14637 C CD2 . TYR   D 1 451 ? 32.449  20.866  65.296  1.00 87.07  ?  451 TYR   D CD2 1 
ATOM   14638 C CE1 . TYR   D 1 451 ? 32.923  21.198  67.998  1.00 87.67  ?  451 TYR   D CE1 1 
ATOM   14639 C CE2 . TYR   D 1 451 ? 31.820  20.038  66.215  1.00 84.78  ?  451 TYR   D CE2 1 
ATOM   14640 C CZ  . TYR   D 1 451 ? 32.059  20.208  67.564  1.00 87.97  ?  451 TYR   D CZ  1 
ATOM   14641 O OH  . TYR   D 1 451 ? 31.432  19.385  68.478  1.00 84.46  ?  451 TYR   D OH  1 
ATOM   14642 N N   . GLU   D 1 452 ? 36.648  20.536  65.414  1.00 81.08  ?  452 GLU   D N   1 
ATOM   14643 C CA  . GLU   D 1 452 ? 36.944  19.123  65.569  1.00 74.53  ?  452 GLU   D CA  1 
ATOM   14644 C C   . GLU   D 1 452 ? 36.469  18.628  66.924  1.00 72.55  ?  452 GLU   D C   1 
ATOM   14645 O O   . GLU   D 1 452 ? 36.833  19.210  67.954  1.00 76.53  ?  452 GLU   D O   1 
ATOM   14646 C CB  . GLU   D 1 452 ? 38.444  18.854  65.421  1.00 75.65  ?  452 GLU   D CB  1 
ATOM   14647 C CG  . GLU   D 1 452 ? 38.789  17.376  65.518  1.00 76.25  ?  452 GLU   D CG  1 
ATOM   14648 C CD  . GLU   D 1 452 ? 40.240  17.088  65.212  1.00 79.86  ?  452 GLU   D CD  1 
ATOM   14649 O OE1 . GLU   D 1 452 ? 41.057  18.031  65.248  1.00 89.30  ?  452 GLU   D OE1 1 
ATOM   14650 O OE2 . GLU   D 1 452 ? 40.563  15.914  64.933  1.00 79.91  ?  452 GLU   D OE2 1 
ATOM   14651 N N   . PRO   D 1 453 ? 35.664  17.571  66.964  1.00 72.66  ?  453 PRO   D N   1 
ATOM   14652 C CA  . PRO   D 1 453 ? 35.252  16.995  68.244  1.00 73.59  ?  453 PRO   D CA  1 
ATOM   14653 C C   . PRO   D 1 453 ? 36.345  16.108  68.808  1.00 73.15  ?  453 PRO   D C   1 
ATOM   14654 O O   . PRO   D 1 453 ? 37.140  15.533  68.048  1.00 71.83  ?  453 PRO   D O   1 
ATOM   14655 C CB  . PRO   D 1 453 ? 34.003  16.172  67.880  1.00 67.64  ?  453 PRO   D CB  1 
ATOM   14656 C CG  . PRO   D 1 453 ? 33.680  16.531  66.455  1.00 71.72  ?  453 PRO   D CG  1 
ATOM   14657 C CD  . PRO   D 1 453 ? 34.973  16.932  65.839  1.00 67.12  ?  453 PRO   D CD  1 
ATOM   14658 N N   . PRO   D 1 454 ? 36.412  15.966  70.134  1.00 71.57  ?  454 PRO   D N   1 
ATOM   14659 C CA  . PRO   D 1 454 ? 37.469  15.132  70.731  1.00 69.54  ?  454 PRO   D CA  1 
ATOM   14660 C C   . PRO   D 1 454 ? 37.479  13.696  70.235  1.00 63.21  ?  454 PRO   D C   1 
ATOM   14661 O O   . PRO   D 1 454 ? 38.558  13.104  70.118  1.00 68.40  ?  454 PRO   D O   1 
ATOM   14662 C CB  . PRO   D 1 454 ? 37.159  15.203  72.234  1.00 70.98  ?  454 PRO   D CB  1 
ATOM   14663 C CG  . PRO   D 1 454 ? 36.391  16.470  72.406  1.00 73.30  ?  454 PRO   D CG  1 
ATOM   14664 C CD  . PRO   D 1 454 ? 35.573  16.614  71.156  1.00 73.35  ?  454 PRO   D CD  1 
ATOM   14665 N N   . VAL   D 1 455 ? 36.314  13.108  69.949  1.00 65.38  ?  455 VAL   D N   1 
ATOM   14666 C CA  . VAL   D 1 455 ? 36.226  11.724  69.498  1.00 65.56  ?  455 VAL   D CA  1 
ATOM   14667 C C   . VAL   D 1 455 ? 35.183  11.619  68.392  1.00 67.08  ?  455 VAL   D C   1 
ATOM   14668 O O   . VAL   D 1 455 ? 34.299  12.468  68.254  1.00 67.05  ?  455 VAL   D O   1 
ATOM   14669 C CB  . VAL   D 1 455 ? 35.868  10.746  70.641  1.00 62.65  ?  455 VAL   D CB  1 
ATOM   14670 C CG1 . VAL   D 1 455 ? 36.874  10.835  71.784  1.00 59.12  ?  455 VAL   D CG1 1 
ATOM   14671 C CG2 . VAL   D 1 455 ? 34.451  11.003  71.137  1.00 58.99  ?  455 VAL   D CG2 1 
ATOM   14672 N N   . LEU   D 1 456 ? 35.303  10.550  67.597  1.00 66.85  ?  456 LEU   D N   1 
ATOM   14673 C CA  . LEU   D 1 456 ? 34.325  10.206  66.560  1.00 65.84  ?  456 LEU   D CA  1 
ATOM   14674 C C   . LEU   D 1 456 ? 34.115  11.359  65.580  1.00 64.60  ?  456 LEU   D C   1 
ATOM   14675 O O   . LEU   D 1 456 ? 32.990  11.667  65.181  1.00 65.30  ?  456 LEU   D O   1 
ATOM   14676 C CB  . LEU   D 1 456 ? 33.001  9.775   67.193  1.00 71.99  ?  456 LEU   D CB  1 
ATOM   14677 C CG  . LEU   D 1 456 ? 33.079  8.516   68.060  1.00 69.65  ?  456 LEU   D CG  1 
ATOM   14678 C CD1 . LEU   D 1 456 ? 31.909  8.459   69.032  1.00 60.45  ?  456 LEU   D CD1 1 
ATOM   14679 C CD2 . LEU   D 1 456 ? 33.123  7.267   67.174  1.00 64.22  ?  456 LEU   D CD2 1 
ATOM   14680 N N   . ARG   D 1 457 ? 35.221  11.987  65.172  1.00 68.82  ?  457 ARG   D N   1 
ATOM   14681 C CA  . ARG   D 1 457 ? 35.144  13.267  64.474  1.00 68.78  ?  457 ARG   D CA  1 
ATOM   14682 C C   . ARG   D 1 457 ? 34.437  13.155  63.128  1.00 63.94  ?  457 ARG   D C   1 
ATOM   14683 O O   . ARG   D 1 457 ? 33.758  14.100  62.713  1.00 61.89  ?  457 ARG   D O   1 
ATOM   14684 C CB  . ARG   D 1 457 ? 36.551  13.848  64.301  1.00 68.45  ?  457 ARG   D CB  1 
ATOM   14685 C CG  . ARG   D 1 457 ? 37.504  12.946  63.544  1.00 67.42  ?  457 ARG   D CG  1 
ATOM   14686 C CD  . ARG   D 1 457 ? 38.921  13.472  63.574  1.00 64.06  ?  457 ARG   D CD  1 
ATOM   14687 N NE  . ARG   D 1 457 ? 39.718  12.866  62.515  1.00 73.99  ?  457 ARG   D NE  1 
ATOM   14688 C CZ  . ARG   D 1 457 ? 40.998  13.128  62.287  1.00 77.00  ?  457 ARG   D CZ  1 
ATOM   14689 N NH1 . ARG   D 1 457 ? 41.677  13.976  63.046  1.00 69.94  ?  457 ARG   D NH1 1 
ATOM   14690 N NH2 . ARG   D 1 457 ? 41.611  12.526  61.271  1.00 71.66  ?  457 ARG   D NH2 1 
ATOM   14691 N N   . HIS   D 1 458 ? 34.563  12.013  62.441  1.00 63.50  ?  458 HIS   D N   1 
ATOM   14692 C CA  . HIS   D 1 458 ? 33.937  11.863  61.130  1.00 62.45  ?  458 HIS   D CA  1 
ATOM   14693 C C   . HIS   D 1 458 ? 32.417  11.968  61.199  1.00 58.93  ?  458 HIS   D C   1 
ATOM   14694 O O   . HIS   D 1 458 ? 31.778  12.260  60.182  1.00 58.32  ?  458 HIS   D O   1 
ATOM   14695 C CB  . HIS   D 1 458 ? 34.348  10.533  60.488  1.00 62.31  ?  458 HIS   D CB  1 
ATOM   14696 C CG  . HIS   D 1 458 ? 33.853  9.325   61.221  1.00 56.56  ?  458 HIS   D CG  1 
ATOM   14697 N ND1 . HIS   D 1 458 ? 34.198  9.052   62.527  1.00 61.63  ?  458 HIS   D ND1 1 
ATOM   14698 C CD2 . HIS   D 1 458 ? 33.046  8.312   60.826  1.00 58.34  ?  458 HIS   D CD2 1 
ATOM   14699 C CE1 . HIS   D 1 458 ? 33.620  7.926   62.907  1.00 62.48  ?  458 HIS   D CE1 1 
ATOM   14700 N NE2 . HIS   D 1 458 ? 32.914  7.458   61.894  1.00 60.54  ?  458 HIS   D NE2 1 
ATOM   14701 N N   . PHE   D 1 459 ? 31.826  11.754  62.374  1.00 58.72  ?  459 PHE   D N   1 
ATOM   14702 C CA  . PHE   D 1 459 ? 30.394  11.969  62.534  1.00 60.35  ?  459 PHE   D CA  1 
ATOM   14703 C C   . PHE   D 1 459 ? 30.047  13.455  62.590  1.00 66.23  ?  459 PHE   D C   1 
ATOM   14704 O O   . PHE   D 1 459 ? 29.078  13.886  61.953  1.00 60.42  ?  459 PHE   D O   1 
ATOM   14705 C CB  . PHE   D 1 459 ? 29.891  11.257  63.792  1.00 51.92  ?  459 PHE   D CB  1 
ATOM   14706 C CG  . PHE   D 1 459 ? 29.882  9.757   63.677  1.00 49.57  ?  459 PHE   D CG  1 
ATOM   14707 C CD1 . PHE   D 1 459 ? 29.477  9.139   62.503  1.00 51.20  ?  459 PHE   D CD1 1 
ATOM   14708 C CD2 . PHE   D 1 459 ? 30.288  8.963   64.741  1.00 53.20  ?  459 PHE   D CD2 1 
ATOM   14709 C CE1 . PHE   D 1 459 ? 29.465  7.753   62.395  1.00 51.64  ?  459 PHE   D CE1 1 
ATOM   14710 C CE2 . PHE   D 1 459 ? 30.283  7.581   64.641  1.00 47.47  ?  459 PHE   D CE2 1 
ATOM   14711 C CZ  . PHE   D 1 459 ? 29.868  6.974   63.468  1.00 51.95  ?  459 PHE   D CZ  1 
ATOM   14712 N N   . THR   D 1 460 ? 30.836  14.261  63.321  1.00 67.08  ?  460 THR   D N   1 
ATOM   14713 C CA  . THR   D 1 460 ? 30.414  15.613  63.676  1.00 67.09  ?  460 THR   D CA  1 
ATOM   14714 C C   . THR   D 1 460 ? 31.464  16.709  63.474  1.00 71.55  ?  460 THR   D C   1 
ATOM   14715 O O   . THR   D 1 460 ? 31.239  17.842  63.921  1.00 75.80  ?  460 THR   D O   1 
ATOM   14716 C CB  . THR   D 1 460 ? 29.946  15.638  65.134  1.00 67.44  ?  460 THR   D CB  1 
ATOM   14717 O OG1 . THR   D 1 460 ? 30.824  14.827  65.924  1.00 62.86  ?  460 THR   D OG1 1 
ATOM   14718 C CG2 . THR   D 1 460 ? 28.515  15.111  65.247  1.00 65.66  ?  460 THR   D CG2 1 
ATOM   14719 N N   . ALA   D 1 461 ? 32.590  16.432  62.818  1.00 68.36  ?  461 ALA   D N   1 
ATOM   14720 C CA  . ALA   D 1 461 ? 33.580  17.479  62.584  1.00 68.37  ?  461 ALA   D CA  1 
ATOM   14721 C C   . ALA   D 1 461 ? 33.147  18.398  61.449  1.00 77.98  ?  461 ALA   D C   1 
ATOM   14722 O O   . ALA   D 1 461 ? 32.672  17.940  60.404  1.00 78.69  ?  461 ALA   D O   1 
ATOM   14723 C CB  . ALA   D 1 461 ? 34.947  16.878  62.258  1.00 74.61  ?  461 ALA   D CB  1 
ATOM   14724 N N   . ARG   D 1 462 ? 33.322  19.702  61.655  1.00 77.23  ?  462 ARG   D N   1 
ATOM   14725 C CA  . ARG   D 1 462 ? 33.029  20.705  60.635  1.00 79.98  ?  462 ARG   D CA  1 
ATOM   14726 C C   . ARG   D 1 462 ? 34.333  21.088  59.946  1.00 82.51  ?  462 ARG   D C   1 
ATOM   14727 O O   . ARG   D 1 462 ? 35.203  21.715  60.555  1.00 89.37  ?  462 ARG   D O   1 
ATOM   14728 C CB  . ARG   D 1 462 ? 32.351  21.930  61.244  1.00 77.96  ?  462 ARG   D CB  1 
ATOM   14729 C CG  . ARG   D 1 462 ? 30.956  21.659  61.782  1.00 75.27  ?  462 ARG   D CG  1 
ATOM   14730 C CD  . ARG   D 1 462 ? 30.188  22.952  61.985  1.00 78.24  ?  462 ARG   D CD  1 
ATOM   14731 N NE  . ARG   D 1 462 ? 30.016  23.684  60.735  1.00 75.69  ?  462 ARG   D NE  1 
ATOM   14732 C CZ  . ARG   D 1 462 ? 28.957  23.581  59.944  1.00 74.82  ?  462 ARG   D CZ  1 
ATOM   14733 N NH1 . ARG   D 1 462 ? 27.940  22.788  60.246  1.00 68.96  ?  462 ARG   D NH1 1 
ATOM   14734 N NH2 . ARG   D 1 462 ? 28.915  24.293  58.820  1.00 69.94  ?  462 ARG   D NH2 1 
ATOM   14735 N N   . LEU   D 1 463 ? 34.467  20.710  58.679  1.00 86.17  ?  463 LEU   D N   1 
ATOM   14736 C CA  . LEU   D 1 463 ? 35.665  20.993  57.908  1.00 87.48  ?  463 LEU   D CA  1 
ATOM   14737 C C   . LEU   D 1 463 ? 35.472  22.258  57.077  1.00 88.89  ?  463 LEU   D C   1 
ATOM   14738 O O   . LEU   D 1 463 ? 34.415  22.895  57.096  1.00 86.23  ?  463 LEU   D O   1 
ATOM   14739 C CB  . LEU   D 1 463 ? 36.031  19.803  57.019  1.00 84.65  ?  463 LEU   D CB  1 
ATOM   14740 C CG  . LEU   D 1 463 ? 36.383  18.506  57.748  1.00 86.57  ?  463 LEU   D CG  1 
ATOM   14741 C CD1 . LEU   D 1 463 ? 37.134  17.567  56.822  1.00 87.43  ?  463 LEU   D CD1 1 
ATOM   14742 C CD2 . LEU   D 1 463 ? 37.191  18.795  58.995  1.00 86.69  ?  463 LEU   D CD2 1 
ATOM   14743 N N   . LYS   D 1 464 ? 36.518  22.621  56.335  1.00 88.26  ?  464 LYS   D N   1 
ATOM   14744 C CA  . LYS   D 1 464 ? 36.554  23.853  55.558  1.00 87.88  ?  464 LYS   D CA  1 
ATOM   14745 C C   . LYS   D 1 464 ? 37.695  23.773  54.551  1.00 83.55  ?  464 LYS   D C   1 
ATOM   14746 O O   . LYS   D 1 464 ? 38.813  23.386  54.917  1.00 81.76  ?  464 LYS   D O   1 
ATOM   14747 C CB  . LYS   D 1 464 ? 36.729  25.063  56.480  1.00 87.86  ?  464 LYS   D CB  1 
ATOM   14748 C CG  . LYS   D 1 464 ? 36.340  26.398  55.865  1.00 87.69  ?  464 LYS   D CG  1 
ATOM   14749 C CD  . LYS   D 1 464 ? 34.843  26.474  55.618  1.00 88.80  ?  464 LYS   D CD  1 
ATOM   14750 C CE  . LYS   D 1 464 ? 34.420  27.877  55.220  1.00 93.11  ?  464 LYS   D CE  1 
ATOM   14751 N NZ  . LYS   D 1 464 ? 34.722  28.866  56.292  1.00 96.53  ?  464 LYS   D NZ  1 
ATOM   14752 N N   . PRO   D 1 465 ? 37.461  24.126  53.274  1.00 81.58  ?  465 PRO   D N   1 
ATOM   14753 C CA  . PRO   D 1 465 ? 38.496  24.057  52.236  1.00 79.47  ?  465 PRO   D CA  1 
ATOM   14754 C C   . PRO   D 1 465 ? 39.609  25.088  52.427  1.00 83.59  ?  465 PRO   D C   1 
ATOM   14755 O O   . PRO   D 1 465 ? 39.338  26.192  52.902  1.00 81.93  ?  465 PRO   D O   1 
ATOM   14756 C CB  . PRO   D 1 465 ? 37.716  24.333  50.947  1.00 77.90  ?  465 PRO   D CB  1 
ATOM   14757 C CG  . PRO   D 1 465 ? 36.553  25.145  51.384  1.00 78.45  ?  465 PRO   D CG  1 
ATOM   14758 C CD  . PRO   D 1 465 ? 36.179  24.618  52.740  1.00 77.73  ?  465 PRO   D CD  1 
HETATM 14759 K K   . K     E 2 .   ? -16.543 2.307   51.848  1.00 20.95  ?  501 K     A K   1 
HETATM 14760 K K   . K     F 2 .   ? -5.467  -4.175  39.460  1.00 17.44  ?  502 K     A K   1 
HETATM 14761 N N1  . BZI   G 3 .   ? -29.754 1.323   49.473  0.81 37.37  ?  503 BZI   A N1  1 
HETATM 14762 C C2  . BZI   G 3 .   ? -28.446 1.331   49.134  0.81 35.34  ?  503 BZI   A C2  1 
HETATM 14763 N N3  . BZI   G 3 .   ? -27.698 1.956   49.999  0.81 38.24  ?  503 BZI   A N3  1 
HETATM 14764 C C3A . BZI   G 3 .   ? -28.559 2.383   50.982  0.81 33.60  ?  503 BZI   A C3A 1 
HETATM 14765 C C4  . BZI   G 3 .   ? -28.314 3.104   52.154  0.81 32.03  ?  503 BZI   A C4  1 
HETATM 14766 C C5  . BZI   G 3 .   ? -29.393 3.405   52.966  0.81 35.23  ?  503 BZI   A C5  1 
HETATM 14767 C C6  . BZI   G 3 .   ? -30.702 3.006   52.638  0.81 32.10  ?  503 BZI   A C6  1 
HETATM 14768 C C7  . BZI   G 3 .   ? -30.956 2.291   51.480  0.81 38.45  ?  503 BZI   A C7  1 
HETATM 14769 C C7A . BZI   G 3 .   ? -29.870 1.991   50.665  0.81 40.53  ?  503 BZI   A C7A 1 
HETATM 14770 O O   . 0JO   H 4 .   ? -27.402 0.222   53.307  1.00 32.24  ?  504 0JO   A O   1 
HETATM 14771 C C   . 0JO   H 4 .   ? -27.671 -0.936  53.022  1.00 33.65  ?  504 0JO   A C   1 
HETATM 14772 O OXT . 0JO   H 4 .   ? -28.448 -1.628  53.654  1.00 30.04  ?  504 0JO   A OXT 1 
HETATM 14773 C CA  . 0JO   H 4 .   ? -27.121 -1.501  51.859  1.00 31.82  ?  504 0JO   A CA  1 
HETATM 14774 C CB  . 0JO   H 4 .   ? -26.533 -0.584  50.993  1.00 29.12  ?  504 0JO   A CB  1 
HETATM 14775 N N   . 0JO   H 4 .   ? -27.744 -2.470  51.169  1.00 32.47  ?  504 0JO   A N   1 
HETATM 14776 C C4A . 0JO   H 4 .   ? -27.309 -2.907  50.047  1.00 28.44  ?  504 0JO   A C4A 1 
HETATM 14777 C C4  . 0JO   H 4 .   ? -27.853 -4.115  49.416  1.00 30.13  ?  504 0JO   A C4  1 
HETATM 14778 C C3  . 0JO   H 4 .   ? -28.686 -5.002  50.124  1.00 29.11  ?  504 0JO   A C3  1 
HETATM 14779 O O3  . 0JO   H 4 .   ? -28.993 -4.805  51.449  1.00 25.62  ?  504 0JO   A O3  1 
HETATM 14780 C C2  . 0JO   H 4 .   ? -29.196 -6.136  49.477  1.00 24.47  ?  504 0JO   A C2  1 
HETATM 14781 C C2A . 0JO   H 4 .   ? -30.069 -7.095  50.218  1.00 25.08  ?  504 0JO   A C2A 1 
HETATM 14782 N N1  . 0JO   H 4 .   ? -28.920 -6.370  48.196  1.00 23.84  ?  504 0JO   A N1  1 
HETATM 14783 C C6  . 0JO   H 4 .   ? -28.133 -5.513  47.511  1.00 24.60  ?  504 0JO   A C6  1 
HETATM 14784 C C5  . 0JO   H 4 .   ? -27.585 -4.388  48.067  1.00 26.56  ?  504 0JO   A C5  1 
HETATM 14785 C C5A . 0JO   H 4 .   ? -26.727 -3.472  47.244  1.00 21.15  ?  504 0JO   A C5A 1 
HETATM 14786 O OP4 . 0JO   H 4 .   ? -25.314 -3.750  47.480  1.00 17.39  ?  504 0JO   A OP4 1 
HETATM 14787 P P   . 0JO   H 4 .   ? -24.261 -2.576  47.185  1.00 18.66  ?  504 0JO   A P   1 
HETATM 14788 O OP3 . 0JO   H 4 .   ? -22.886 -3.144  47.491  1.00 17.31  ?  504 0JO   A OP3 1 
HETATM 14789 O OP1 . 0JO   H 4 .   ? -24.664 -1.423  48.093  1.00 20.41  ?  504 0JO   A OP1 1 
HETATM 14790 O OP2 . 0JO   H 4 .   ? -24.440 -2.249  45.717  1.00 18.63  ?  504 0JO   A OP2 1 
HETATM 14791 S S   . DMS   I 5 .   ? -41.953 -7.811  20.474  1.00 48.16  ?  505 DMS   A S   1 
HETATM 14792 O O   . DMS   I 5 .   ? -42.631 -8.875  21.317  1.00 34.26  ?  505 DMS   A O   1 
HETATM 14793 C C1  . DMS   I 5 .   ? -40.171 -8.054  20.634  1.00 53.46  ?  505 DMS   A C1  1 
HETATM 14794 C C2  . DMS   I 5 .   ? -42.032 -6.261  21.399  1.00 38.11  ?  505 DMS   A C2  1 
HETATM 14795 S S   . DMS   J 5 .   ? 14.634  7.716   17.866  1.00 41.54  ?  501 DMS   B S   1 
HETATM 14796 O O   . DMS   J 5 .   ? 13.904  8.769   17.055  1.00 37.93  ?  501 DMS   B O   1 
HETATM 14797 C C1  . DMS   J 5 .   ? 14.632  6.224   16.857  1.00 31.16  ?  501 DMS   B C1  1 
HETATM 14798 C C2  . DMS   J 5 .   ? 16.399  8.083   17.732  1.00 41.47  ?  501 DMS   B C2  1 
HETATM 14799 N N1  . PLT   K 6 .   ? -10.586 4.269   27.539  1.00 28.77  ?  502 PLT   B N1  1 
HETATM 14800 C C2  . PLT   K 6 .   ? -9.358  3.910   27.172  1.00 29.98  ?  502 PLT   B C2  1 
HETATM 14801 C C2A . PLT   K 6 .   ? -8.626  4.758   26.182  1.00 24.64  ?  502 PLT   B C2A 1 
HETATM 14802 C C3  . PLT   K 6 .   ? -8.761  2.751   27.693  1.00 27.66  ?  502 PLT   B C3  1 
HETATM 14803 O O3  . PLT   K 6 .   ? -7.490  2.420   27.293  1.00 30.68  ?  502 PLT   B O3  1 
HETATM 14804 C C4  . PLT   K 6 .   ? -9.459  1.968   28.629  1.00 34.07  ?  502 PLT   B C4  1 
HETATM 14805 C C4A . PLT   K 6 .   ? -8.862  0.739   29.191  1.00 36.84  ?  502 PLT   B C4A 1 
HETATM 14806 C C5  . PLT   K 6 .   ? -10.754 2.375   28.993  1.00 30.09  ?  502 PLT   B C5  1 
HETATM 14807 C C6  . PLT   K 6 .   ? -11.263 3.515   28.432  1.00 28.20  ?  502 PLT   B C6  1 
HETATM 14808 C C5A . PLT   K 6 .   ? -11.575 1.593   29.974  1.00 25.38  ?  502 PLT   B C5A 1 
HETATM 14809 O O4P . PLT   K 6 .   ? -11.037 1.806   31.316  1.00 19.21  ?  502 PLT   B O4P 1 
HETATM 14810 P P   . PLT   K 6 .   ? -11.140 0.618   32.387  1.00 19.45  ?  502 PLT   B P   1 
HETATM 14811 O O1P . PLT   K 6 .   ? -10.523 1.186   33.639  1.00 19.19  ?  502 PLT   B O1P 1 
HETATM 14812 O O2P . PLT   K 6 .   ? -10.368 -0.550  31.797  1.00 17.30  ?  502 PLT   B O2P 1 
HETATM 14813 O O3P . PLT   K 6 .   ? -12.621 0.334   32.535  1.00 17.08  ?  502 PLT   B O3P 1 
HETATM 14814 N N   . PLT   K 6 .   ? -7.790  0.216   28.721  1.00 33.81  ?  502 PLT   B N   1 
HETATM 14815 C CA  . PLT   K 6 .   ? -6.948  -0.813  29.345  1.00 34.69  ?  502 PLT   B CA  1 
HETATM 14816 C C   . PLT   K 6 .   ? -5.832  -1.094  28.329  1.00 36.69  ?  502 PLT   B C   1 
HETATM 14817 O O   . PLT   K 6 .   ? -4.912  -1.868  28.676  1.00 32.25  ?  502 PLT   B O   1 
HETATM 14818 O OXT . PLT   K 6 .   ? -5.899  -0.494  27.238  1.00 32.44  ?  502 PLT   B OXT 1 
HETATM 14819 C CB  . PLT   K 6 .   ? -7.697  -2.074  29.783  1.00 36.54  ?  502 PLT   B CB  1 
HETATM 14820 C CG  . PLT   K 6 .   ? -8.278  -2.922  28.688  1.00 38.65  ?  502 PLT   B CG  1 
HETATM 14821 C CD1 . PLT   K 6 .   ? -9.585  -2.960  28.298  1.00 39.80  ?  502 PLT   B CD1 1 
HETATM 14822 N NE1 . PLT   K 6 .   ? -9.753  -3.853  27.274  1.00 42.06  ?  502 PLT   B NE1 1 
HETATM 14823 C CE2 . PLT   K 6 .   ? -8.547  -4.428  26.976  1.00 42.12  ?  502 PLT   B CE2 1 
HETATM 14824 C CZ2 . PLT   K 6 .   ? -8.219  -5.386  26.015  1.00 46.91  ?  502 PLT   B CZ2 1 
HETATM 14825 C CH2 . PLT   K 6 .   ? -6.904  -5.787  25.946  1.00 43.59  ?  502 PLT   B CH2 1 
HETATM 14826 C CZ3 . PLT   K 6 .   ? -5.938  -5.255  26.802  1.00 42.49  ?  502 PLT   B CZ3 1 
HETATM 14827 C CE3 . PLT   K 6 .   ? -6.261  -4.307  27.749  1.00 39.13  ?  502 PLT   B CE3 1 
HETATM 14828 C CD2 . PLT   K 6 .   ? -7.588  -3.876  27.855  1.00 38.90  ?  502 PLT   B CD2 1 
HETATM 14829 K K   . K     L 2 .   ? 16.599  2.631   59.040  1.00 19.20  ?  501 K     C K   1 
HETATM 14830 K K   . K     M 2 .   ? 5.574   -3.963  71.497  1.00 17.14  ?  502 K     C K   1 
HETATM 14831 N N   . A1A2Z N 7 .   ? 7.679   0.585   82.318  1.00 32.75  ?  503 A1A2Z C N   1 
HETATM 14832 N N1  . A1A2Z N 7 .   ? 10.560  4.535   83.491  1.00 21.80  ?  503 A1A2Z C N1  1 
HETATM 14833 C CG  . A1A2Z N 7 .   ? 8.211   -2.391  82.123  1.00 35.73  ?  503 A1A2Z C CG  1 
HETATM 14834 C CD1 . A1A2Z N 7 .   ? 9.572   -2.397  82.189  1.00 36.51  ?  503 A1A2Z C CD1 1 
HETATM 14835 C CD2 . A1A2Z N 7 .   ? 7.754   -3.265  83.181  1.00 38.14  ?  503 A1A2Z C CD2 1 
HETATM 14836 C CE2 . A1A2Z N 7 .   ? 8.906   -3.759  83.831  1.00 40.83  ?  503 A1A2Z C CE2 1 
HETATM 14837 C CE3 . A1A2Z N 7 .   ? 6.499   -3.680  83.643  1.00 37.17  ?  503 A1A2Z C CE3 1 
HETATM 14838 C CZ3 . A1A2Z N 7 .   ? 6.430   -4.544  84.713  1.00 36.65  ?  503 A1A2Z C CZ3 1 
HETATM 14839 C C2A . A1A2Z N 7 .   ? 8.560   5.225   84.689  1.00 26.96  ?  503 A1A2Z C C2A 1 
HETATM 14840 C C4  . A1A2Z N 7 .   ? 9.227   2.507   82.117  1.00 27.77  ?  503 A1A2Z C C4  1 
HETATM 14841 C C5  . A1A2Z N 7 .   ? 10.599  2.731   81.902  1.00 23.21  ?  503 A1A2Z C C5  1 
HETATM 14842 C CA  . A1A2Z N 7 .   ? 6.697   -0.342  81.744  1.00 33.81  ?  503 A1A2Z C CA  1 
HETATM 14843 C CH2 . A1A2Z N 7 .   ? 7.581   -5.017  85.338  1.00 42.69  ?  503 A1A2Z C CH2 1 
HETATM 14844 C C2  . A1A2Z N 7 .   ? 9.262   4.345   83.703  1.00 25.37  ?  503 A1A2Z C C2  1 
HETATM 14845 C C3  . A1A2Z N 7 .   ? 8.559   3.332   83.036  1.00 25.17  ?  503 A1A2Z C C3  1 
HETATM 14846 C C4A . A1A2Z N 7 .   ? 8.463   1.413   81.386  1.00 30.97  ?  503 A1A2Z C C4A 1 
HETATM 14847 C C5A . A1A2Z N 7 .   ? 11.396  1.883   80.951  1.00 20.45  ?  503 A1A2Z C C5A 1 
HETATM 14848 C C6  . A1A2Z N 7 .   ? 11.207  3.752   82.614  1.00 22.22  ?  503 A1A2Z C C6  1 
HETATM 14849 C C   . A1A2Z N 7 .   ? 5.667   -0.765  82.810  1.00 35.24  ?  503 A1A2Z C C   1 
HETATM 14850 C CB  . A1A2Z N 7 .   ? 7.369   -1.602  81.154  1.00 33.84  ?  503 A1A2Z C CB  1 
HETATM 14851 C CZ2 . A1A2Z N 7 .   ? 8.833   -4.639  84.911  1.00 40.28  ?  503 A1A2Z C CZ2 1 
HETATM 14852 N NE1 . A1A2Z N 7 .   ? 9.997   -3.215  83.203  1.00 39.92  ?  503 A1A2Z C NE1 1 
HETATM 14853 O O   . A1A2Z N 7 .   ? 5.822   -0.295  83.964  1.00 33.43  -1 503 A1A2Z C O   1 
HETATM 14854 O OXT . A1A2Z N 7 .   ? 4.745   -1.547  82.453  1.00 32.18  ?  503 A1A2Z C OXT 1 
HETATM 14855 O O3P . A1A2Z N 7 .   ? 10.371  -0.247  79.033  1.00 20.49  ?  503 A1A2Z C O3P 1 
HETATM 14856 O O1P . A1A2Z N 7 .   ? 12.634  0.579   78.433  1.00 16.99  -1 503 A1A2Z C O1P 1 
HETATM 14857 O O3  . A1A2Z N 7 .   ? 7.232   3.169   83.289  1.00 30.70  ?  503 A1A2Z C O3  1 
HETATM 14858 O O2P . A1A2Z N 7 .   ? 10.645  1.508   77.180  1.00 15.53  -1 503 A1A2Z C O2P 1 
HETATM 14859 O O4P . A1A2Z N 7 .   ? 10.966  2.097   79.573  1.00 19.56  ?  503 A1A2Z C O4P 1 
HETATM 14860 P P   . A1A2Z N 7 .   ? 11.156  0.924   78.481  1.00 17.32  ?  503 A1A2Z C P   1 
HETATM 14861 N N1  . BZI   O 3 .   ? 29.794  2.296   61.883  0.73 30.89  ?  501 BZI   D N1  1 
HETATM 14862 C C2  . BZI   O 3 .   ? 28.578  2.534   62.423  0.73 33.58  ?  501 BZI   D C2  1 
HETATM 14863 N N3  . BZI   O 3 .   ? 27.735  3.075   61.585  0.73 35.13  ?  501 BZI   D N3  1 
HETATM 14864 C C3A . BZI   O 3 .   ? 28.437  3.206   60.411  0.73 30.79  ?  501 BZI   D C3A 1 
HETATM 14865 C C4  . BZI   O 3 .   ? 28.038  3.726   59.182  0.73 33.42  ?  501 BZI   D C4  1 
HETATM 14866 C C5  . BZI   O 3 .   ? 28.964  3.732   58.156  0.73 33.80  ?  501 BZI   D C5  1 
HETATM 14867 C C6  . BZI   O 3 .   ? 30.267  3.238   58.341  0.73 32.87  ?  501 BZI   D C6  1 
HETATM 14868 C C7  . BZI   O 3 .   ? 30.685  2.718   59.553  0.73 30.82  ?  501 BZI   D C7  1 
HETATM 14869 C C7A . BZI   O 3 .   ? 29.746  2.714   60.578  0.73 34.50  ?  501 BZI   D C7A 1 
HETATM 14870 O O   . 0JO   P 4 .   ? 27.870  -0.952  57.269  0.99 36.05  ?  502 0JO   D O   1 
HETATM 14871 C C   . 0JO   P 4 .   ? 27.470  -0.217  58.155  0.99 37.42  ?  502 0JO   D C   1 
HETATM 14872 O OXT . 0JO   P 4 .   ? 27.344  0.988   58.031  0.99 37.11  ?  502 0JO   D OXT 1 
HETATM 14873 C CA  . 0JO   P 4 .   ? 27.060  -0.794  59.366  0.99 33.27  ?  502 0JO   D CA  1 
HETATM 14874 C CB  . 0JO   P 4 .   ? 26.836  0.143   60.383  0.99 29.22  ?  502 0JO   D CB  1 
HETATM 14875 N N   . 0JO   P 4 .   ? 27.615  -1.909  59.869  0.99 31.39  ?  502 0JO   D N   1 
HETATM 14876 C C4A . 0JO   P 4 .   ? 27.255  -2.398  60.996  0.99 27.62  ?  502 0JO   D C4A 1 
HETATM 14877 C C4  . 0JO   P 4 .   ? 27.861  -3.615  61.548  0.99 23.67  ?  502 0JO   D C4  1 
HETATM 14878 C C3  . 0JO   P 4 .   ? 28.705  -4.426  60.773  0.99 24.36  ?  502 0JO   D C3  1 
HETATM 14879 O O3  . 0JO   P 4 .   ? 28.953  -4.147  59.453  0.99 25.25  ?  502 0JO   D O3  1 
HETATM 14880 C C2  . 0JO   P 4 .   ? 29.295  -5.556  61.348  0.99 21.61  ?  502 0JO   D C2  1 
HETATM 14881 C C2A . 0JO   P 4 .   ? 30.184  -6.435  60.530  0.99 19.70  ?  502 0JO   D C2A 1 
HETATM 14882 N N1  . 0JO   P 4 .   ? 29.090  -5.852  62.629  0.99 19.70  ?  502 0JO   D N1  1 
HETATM 14883 C C6  . 0JO   P 4 .   ? 28.291  -5.065  63.382  0.99 18.88  ?  502 0JO   D C6  1 
HETATM 14884 C C5  . 0JO   P 4 .   ? 27.665  -3.950  62.895  0.99 20.29  ?  502 0JO   D C5  1 
HETATM 14885 C C5A . 0JO   P 4 .   ? 26.805  -3.103  63.787  0.99 16.51  ?  502 0JO   D C5A 1 
HETATM 14886 O OP4 . 0JO   P 4 .   ? 25.395  -3.334  63.494  0.99 15.27  ?  502 0JO   D OP4 1 
HETATM 14887 P P   . 0JO   P 4 .   ? 24.334  -2.162  63.774  0.99 15.84  ?  502 0JO   D P   1 
HETATM 14888 O OP3 . 0JO   P 4 .   ? 22.983  -2.751  63.463  0.99 14.56  ?  502 0JO   D OP3 1 
HETATM 14889 O OP1 . 0JO   P 4 .   ? 24.488  -1.789  65.243  0.99 13.43  ?  502 0JO   D OP1 1 
HETATM 14890 O OP2 . 0JO   P 4 .   ? 24.741  -1.043  62.831  0.99 13.93  ?  502 0JO   D OP2 1 
HETATM 14891 O O   . HOH   Q 8 .   ? -34.725 -22.699 60.072  1.00 26.04  ?  601 HOH   A O   1 
HETATM 14892 O O   . HOH   Q 8 .   ? -29.760 -8.961  53.598  1.00 17.51  ?  602 HOH   A O   1 
HETATM 14893 O O   . HOH   Q 8 .   ? -14.559 -14.870 65.805  1.00 24.80  ?  603 HOH   A O   1 
HETATM 14894 O O   . HOH   Q 8 .   ? -18.220 -2.778  73.667  1.00 24.17  ?  604 HOH   A O   1 
HETATM 14895 O O   . HOH   Q 8 .   ? -3.102  -16.651 47.595  1.00 27.60  ?  605 HOH   A O   1 
HETATM 14896 O O   . HOH   Q 8 .   ? -15.375 -23.950 37.899  1.00 30.05  ?  606 HOH   A O   1 
HETATM 14897 O O   . HOH   Q 8 .   ? -38.053 -0.675  80.976  1.00 36.94  ?  607 HOH   A O   1 
HETATM 14898 O O   . HOH   Q 8 .   ? -1.385  -5.691  47.140  1.00 18.18  ?  608 HOH   A O   1 
HETATM 14899 O O   . HOH   Q 8 .   ? -39.368 -29.094 43.596  1.00 36.55  ?  609 HOH   A O   1 
HETATM 14900 O O   . HOH   Q 8 .   ? -30.438 11.110  62.287  1.00 28.30  ?  610 HOH   A O   1 
HETATM 14901 O O   . HOH   Q 8 .   ? -32.605 -5.883  29.787  1.00 32.32  ?  611 HOH   A O   1 
HETATM 14902 O O   . HOH   Q 8 .   ? -18.354 -28.755 48.031  1.00 34.00  ?  612 HOH   A O   1 
HETATM 14903 O O   . HOH   Q 8 .   ? -28.880 -18.627 25.715  1.00 40.72  ?  613 HOH   A O   1 
HETATM 14904 O O   . HOH   Q 8 .   ? -12.121 -18.727 61.009  1.00 31.17  ?  614 HOH   A O   1 
HETATM 14905 O O   . HOH   Q 8 .   ? -29.212 -8.877  59.053  1.00 17.63  ?  615 HOH   A O   1 
HETATM 14906 O O   . HOH   Q 8 .   ? -40.998 -5.410  29.851  1.00 28.60  ?  616 HOH   A O   1 
HETATM 14907 O O   . HOH   Q 8 .   ? -36.448 -6.250  75.058  1.00 32.63  ?  617 HOH   A O   1 
HETATM 14908 O O   . HOH   Q 8 .   ? -29.200 -8.567  44.828  1.00 25.55  ?  618 HOH   A O   1 
HETATM 14909 O O   . HOH   Q 8 .   ? -35.259 1.113   37.912  1.00 33.32  ?  619 HOH   A O   1 
HETATM 14910 O O   . HOH   Q 8 .   ? -19.263 2.558   52.718  1.00 18.05  ?  620 HOH   A O   1 
HETATM 14911 O O   . HOH   Q 8 .   ? -26.926 -22.662 38.847  1.00 22.29  ?  621 HOH   A O   1 
HETATM 14912 O O   . HOH   Q 8 .   ? -22.558 -1.893  36.818  1.00 29.02  ?  622 HOH   A O   1 
HETATM 14913 O O   . HOH   Q 8 .   ? -31.391 13.304  73.246  1.00 37.34  ?  623 HOH   A O   1 
HETATM 14914 O O   . HOH   Q 8 .   ? -29.643 -7.603  75.037  1.00 27.09  ?  624 HOH   A O   1 
HETATM 14915 O O   . HOH   Q 8 .   ? -42.693 22.662  53.040  1.00 61.44  ?  625 HOH   A O   1 
HETATM 14916 O O   . HOH   Q 8 .   ? -30.022 -29.743 66.861  1.00 32.01  ?  626 HOH   A O   1 
HETATM 14917 O O   . HOH   Q 8 .   ? -35.133 -5.710  77.948  1.00 32.59  ?  627 HOH   A O   1 
HETATM 14918 O O   . HOH   Q 8 .   ? -37.585 -20.746 27.198  1.00 48.93  ?  628 HOH   A O   1 
HETATM 14919 O O   . HOH   Q 8 .   ? -35.483 -26.387 59.196  1.00 33.59  ?  629 HOH   A O   1 
HETATM 14920 O O   . HOH   Q 8 .   ? -31.351 9.569   56.456  1.00 34.20  ?  630 HOH   A O   1 
HETATM 14921 O O   . HOH   Q 8 .   ? -2.557  -3.633  45.756  1.00 18.94  ?  631 HOH   A O   1 
HETATM 14922 O O   . HOH   Q 8 .   ? -27.390 -8.084  73.767  1.00 20.94  ?  632 HOH   A O   1 
HETATM 14923 O O   . HOH   Q 8 .   ? -33.742 -6.315  71.308  1.00 27.98  ?  633 HOH   A O   1 
HETATM 14924 O O   . HOH   Q 8 .   ? -2.952  -11.715 49.484  1.00 14.15  ?  634 HOH   A O   1 
HETATM 14925 O O   . HOH   Q 8 .   ? -19.976 18.926  70.202  1.00 34.65  ?  635 HOH   A O   1 
HETATM 14926 O O   . HOH   Q 8 .   ? -3.962  -12.586 56.123  1.00 20.01  ?  636 HOH   A O   1 
HETATM 14927 O O   . HOH   Q 8 .   ? -22.951 0.087   49.375  1.00 17.37  ?  637 HOH   A O   1 
HETATM 14928 O O   . HOH   Q 8 .   ? -24.780 -25.585 48.886  1.00 22.09  ?  638 HOH   A O   1 
HETATM 14929 O O   . HOH   Q 8 .   ? -41.979 -2.958  40.467  1.00 30.23  ?  639 HOH   A O   1 
HETATM 14930 O O   . HOH   Q 8 .   ? -11.335 -2.315  44.348  1.00 18.09  ?  640 HOH   A O   1 
HETATM 14931 O O   . HOH   Q 8 .   ? -12.112 -19.686 36.428  1.00 18.55  ?  641 HOH   A O   1 
HETATM 14932 O O   . HOH   Q 8 .   ? -6.591  -14.389 48.125  1.00 17.36  ?  642 HOH   A O   1 
HETATM 14933 O O   . HOH   Q 8 .   ? -16.820 12.068  60.677  1.00 25.07  ?  643 HOH   A O   1 
HETATM 14934 O O   . HOH   Q 8 .   ? -14.463 -12.730 62.996  1.00 18.28  ?  644 HOH   A O   1 
HETATM 14935 O O   . HOH   Q 8 .   ? -19.737 -5.087  65.391  1.00 16.65  ?  645 HOH   A O   1 
HETATM 14936 O O   . HOH   Q 8 .   ? -19.949 -1.621  65.592  1.00 14.79  ?  646 HOH   A O   1 
HETATM 14937 O O   . HOH   Q 8 .   ? -19.314 -13.620 71.113  1.00 25.09  ?  647 HOH   A O   1 
HETATM 14938 O O   . HOH   Q 8 .   ? -27.973 -15.714 70.289  1.00 34.63  ?  648 HOH   A O   1 
HETATM 14939 O O   . HOH   Q 8 .   ? -12.381 -5.078  50.006  1.00 15.60  ?  649 HOH   A O   1 
HETATM 14940 O O   . HOH   Q 8 .   ? -21.508 -26.862 35.243  1.00 39.31  ?  650 HOH   A O   1 
HETATM 14941 O O   . HOH   Q 8 .   ? -47.965 -14.012 55.940  1.00 37.31  ?  651 HOH   A O   1 
HETATM 14942 O O   . HOH   Q 8 .   ? -29.963 -8.412  66.952  1.00 22.97  ?  652 HOH   A O   1 
HETATM 14943 O O   . HOH   Q 8 .   ? -48.985 -21.642 41.941  1.00 36.27  ?  653 HOH   A O   1 
HETATM 14944 O O   . HOH   Q 8 .   ? -46.847 -3.152  64.093  1.00 40.67  ?  654 HOH   A O   1 
HETATM 14945 O O   . HOH   Q 8 .   ? -35.936 0.553   43.907  1.00 34.40  ?  655 HOH   A O   1 
HETATM 14946 O O   . HOH   Q 8 .   ? -45.403 -14.619 65.933  1.00 28.12  ?  656 HOH   A O   1 
HETATM 14947 O O   . HOH   Q 8 .   ? -26.434 -8.438  48.183  1.00 19.10  ?  657 HOH   A O   1 
HETATM 14948 O O   . HOH   Q 8 .   ? -13.989 3.172   61.128  1.00 17.29  ?  658 HOH   A O   1 
HETATM 14949 O O   . HOH   Q 8 .   ? -40.686 -21.036 58.203  1.00 30.13  ?  659 HOH   A O   1 
HETATM 14950 O O   . HOH   Q 8 .   ? -16.558 13.141  63.601  1.00 29.21  ?  660 HOH   A O   1 
HETATM 14951 O O   . HOH   Q 8 .   ? -15.222 -15.374 36.266  1.00 17.09  ?  661 HOH   A O   1 
HETATM 14952 O O   . HOH   Q 8 .   ? -20.360 -23.167 54.344  1.00 19.01  ?  662 HOH   A O   1 
HETATM 14953 O O   . HOH   Q 8 .   ? -22.836 2.382   61.529  1.00 16.31  ?  663 HOH   A O   1 
HETATM 14954 O O   . HOH   Q 8 .   ? -7.208  -10.806 37.525  1.00 11.53  ?  664 HOH   A O   1 
HETATM 14955 O O   . HOH   Q 8 .   ? -33.958 -4.888  63.484  1.00 22.17  ?  665 HOH   A O   1 
HETATM 14956 O O   . HOH   Q 8 .   ? -24.549 -28.338 48.114  1.00 27.37  ?  666 HOH   A O   1 
HETATM 14957 O O   . HOH   Q 8 .   ? -1.451  0.016   65.997  1.00 17.43  ?  667 HOH   A O   1 
HETATM 14958 O O   . HOH   Q 8 .   ? -6.828  -13.560 51.096  1.00 15.47  ?  668 HOH   A O   1 
HETATM 14959 O O   . HOH   Q 8 .   ? -33.142 8.628   54.731  1.00 37.65  ?  669 HOH   A O   1 
HETATM 14960 O O   . HOH   Q 8 .   ? -12.533 -24.584 43.583  1.00 29.25  ?  670 HOH   A O   1 
HETATM 14961 O O   . HOH   Q 8 .   ? -35.232 -8.655  74.646  1.00 35.81  ?  671 HOH   A O   1 
HETATM 14962 O O   . HOH   Q 8 .   ? -13.477 5.652   57.625  1.00 28.13  ?  672 HOH   A O   1 
HETATM 14963 O O   . HOH   Q 8 .   ? -34.870 -6.505  51.312  1.00 24.27  ?  673 HOH   A O   1 
HETATM 14964 O O   . HOH   Q 8 .   ? -47.809 -11.434 53.258  1.00 41.59  ?  674 HOH   A O   1 
HETATM 14965 O O   . HOH   Q 8 .   ? -47.456 -8.613  47.742  1.00 34.64  ?  675 HOH   A O   1 
HETATM 14966 O O   . HOH   Q 8 .   ? -1.196  -11.520 71.526  1.00 27.70  ?  676 HOH   A O   1 
HETATM 14967 O O   . HOH   Q 8 .   ? -42.198 -7.981  26.465  1.00 32.81  ?  677 HOH   A O   1 
HETATM 14968 O O   . HOH   Q 8 .   ? -20.108 -22.074 64.354  1.00 24.30  ?  678 HOH   A O   1 
HETATM 14969 O O   . HOH   Q 8 .   ? -9.737  -19.943 49.214  1.00 23.14  ?  679 HOH   A O   1 
HETATM 14970 O O   . HOH   Q 8 .   ? -32.862 1.711   78.395  1.00 27.52  ?  680 HOH   A O   1 
HETATM 14971 O O   . HOH   Q 8 .   ? -14.209 -20.969 60.944  1.00 40.42  ?  681 HOH   A O   1 
HETATM 14972 O O   . HOH   Q 8 .   ? -6.147  -8.458  40.066  1.00 15.19  ?  682 HOH   A O   1 
HETATM 14973 O O   . HOH   Q 8 .   ? -30.703 -7.898  79.977  1.00 35.33  ?  683 HOH   A O   1 
HETATM 14974 O O   . HOH   Q 8 .   ? -52.586 -14.468 49.903  1.00 37.46  ?  684 HOH   A O   1 
HETATM 14975 O O   . HOH   Q 8 .   ? -36.587 -18.569 35.595  1.00 26.66  ?  685 HOH   A O   1 
HETATM 14976 O O   . HOH   Q 8 .   ? -43.446 -17.777 58.005  1.00 34.10  ?  686 HOH   A O   1 
HETATM 14977 O O   . HOH   Q 8 .   ? -44.636 -17.169 55.886  1.00 35.31  ?  687 HOH   A O   1 
HETATM 14978 O O   . HOH   Q 8 .   ? -21.173 6.281   56.647  1.00 17.02  ?  688 HOH   A O   1 
HETATM 14979 O O   . HOH   Q 8 .   ? -16.303 -21.879 42.604  1.00 18.58  ?  689 HOH   A O   1 
HETATM 14980 O O   . HOH   Q 8 .   ? -24.212 20.047  54.657  1.00 37.75  ?  690 HOH   A O   1 
HETATM 14981 O O   . HOH   Q 8 .   ? -22.681 -5.065  65.902  1.00 14.35  ?  691 HOH   A O   1 
HETATM 14982 O O   . HOH   Q 8 .   ? -23.074 13.303  51.107  1.00 23.94  ?  692 HOH   A O   1 
HETATM 14983 O O   . HOH   Q 8 .   ? -18.133 -26.626 59.766  1.00 28.26  ?  693 HOH   A O   1 
HETATM 14984 O O   . HOH   Q 8 .   ? -44.451 -7.984  50.736  1.00 30.48  ?  694 HOH   A O   1 
HETATM 14985 O O   . HOH   Q 8 .   ? -15.759 -26.544 41.518  1.00 25.49  ?  695 HOH   A O   1 
HETATM 14986 O O   . HOH   Q 8 .   ? -18.781 8.860   58.836  1.00 25.74  ?  696 HOH   A O   1 
HETATM 14987 O O   . HOH   Q 8 .   ? -33.799 -13.682 24.504  1.00 34.93  ?  697 HOH   A O   1 
HETATM 14988 O O   . HOH   Q 8 .   ? -16.715 3.218   59.886  1.00 21.44  ?  698 HOH   A O   1 
HETATM 14989 O O   . HOH   Q 8 .   ? -11.100 0.516   56.295  1.00 19.32  ?  699 HOH   A O   1 
HETATM 14990 O O   . HOH   Q 8 .   ? -0.592  -12.102 53.250  1.00 18.02  ?  700 HOH   A O   1 
HETATM 14991 O O   . HOH   Q 8 .   ? -6.103  -15.007 63.081  1.00 37.23  ?  701 HOH   A O   1 
HETATM 14992 O O   . HOH   Q 8 .   ? -37.728 -12.743 62.839  1.00 17.51  ?  702 HOH   A O   1 
HETATM 14993 O O   . HOH   Q 8 .   ? -14.809 -23.887 41.885  1.00 24.67  ?  703 HOH   A O   1 
HETATM 14994 O O   . HOH   Q 8 .   ? -24.209 1.947   80.401  1.00 28.57  ?  704 HOH   A O   1 
HETATM 14995 O O   . HOH   Q 8 .   ? -34.905 -19.955 48.524  1.00 24.94  ?  705 HOH   A O   1 
HETATM 14996 O O   . HOH   Q 8 .   ? -21.560 -27.584 66.161  1.00 34.01  ?  706 HOH   A O   1 
HETATM 14997 O O   . HOH   Q 8 .   ? -27.199 -3.113  28.827  1.00 31.21  ?  707 HOH   A O   1 
HETATM 14998 O O   . HOH   Q 8 .   ? -14.192 -10.723 64.445  1.00 19.21  ?  708 HOH   A O   1 
HETATM 14999 O O   . HOH   Q 8 .   ? -48.998 -5.637  51.953  1.00 43.42  ?  709 HOH   A O   1 
HETATM 15000 O O   . HOH   Q 8 .   ? -35.285 -3.488  65.197  1.00 26.01  ?  710 HOH   A O   1 
HETATM 15001 O O   . HOH   Q 8 .   ? -19.035 4.473   60.527  1.00 23.53  ?  711 HOH   A O   1 
HETATM 15002 O O   . HOH   Q 8 .   ? -15.751 -17.365 29.783  1.00 26.44  ?  712 HOH   A O   1 
HETATM 15003 O O   . HOH   Q 8 .   ? -24.977 -6.008  80.405  1.00 34.40  ?  713 HOH   A O   1 
HETATM 15004 O O   . HOH   Q 8 .   ? -20.321 -22.323 28.182  1.00 36.60  ?  714 HOH   A O   1 
HETATM 15005 O O   . HOH   Q 8 .   ? -15.550 -19.110 38.023  1.00 20.61  ?  715 HOH   A O   1 
HETATM 15006 O O   . HOH   Q 8 .   ? -10.549 -17.781 53.642  1.00 21.31  ?  716 HOH   A O   1 
HETATM 15007 O O   . HOH   Q 8 .   ? -22.040 -9.678  60.291  1.00 18.57  ?  717 HOH   A O   1 
HETATM 15008 O O   . HOH   Q 8 .   ? -13.118 -12.058 66.403  1.00 24.03  ?  718 HOH   A O   1 
HETATM 15009 O O   . HOH   Q 8 .   ? -45.363 -10.777 64.314  1.00 30.12  ?  719 HOH   A O   1 
HETATM 15010 O O   . HOH   Q 8 .   ? -33.069 -7.949  47.440  1.00 23.95  ?  720 HOH   A O   1 
HETATM 15011 O O   . HOH   Q 8 .   ? -20.673 -11.549 59.047  1.00 15.25  ?  721 HOH   A O   1 
HETATM 15012 O O   . HOH   Q 8 .   ? -22.107 -7.076  71.746  1.00 23.52  ?  722 HOH   A O   1 
HETATM 15013 O O   A HOH   Q 8 .   ? -22.235 6.320   76.469  0.50 26.84  ?  723 HOH   A O   1 
HETATM 15014 O O   . HOH   Q 8 .   ? -38.549 17.939  41.566  1.00 51.79  ?  724 HOH   A O   1 
HETATM 15015 O O   . HOH   Q 8 .   ? -41.256 -3.096  69.971  1.00 33.87  ?  725 HOH   A O   1 
HETATM 15016 O O   . HOH   Q 8 .   ? -21.775 4.165   78.265  1.00 19.55  ?  726 HOH   A O   1 
HETATM 15017 O O   . HOH   Q 8 .   ? -8.524  -17.303 34.330  1.00 31.48  ?  727 HOH   A O   1 
HETATM 15018 O O   . HOH   Q 8 .   ? -39.977 -12.439 24.586  1.00 39.67  ?  728 HOH   A O   1 
HETATM 15019 O O   . HOH   Q 8 .   ? -34.601 -11.394 64.142  1.00 20.25  ?  729 HOH   A O   1 
HETATM 15020 O O   . HOH   Q 8 .   ? -2.818  -11.343 64.613  1.00 28.89  ?  730 HOH   A O   1 
HETATM 15021 O O   . HOH   Q 8 .   ? -53.667 -16.385 41.810  1.00 35.56  ?  731 HOH   A O   1 
HETATM 15022 O O   . HOH   Q 8 .   ? -42.795 -16.135 59.913  1.00 36.92  ?  732 HOH   A O   1 
HETATM 15023 O O   . HOH   Q 8 .   ? -43.028 -24.748 33.917  1.00 37.61  ?  733 HOH   A O   1 
HETATM 15024 O O   . HOH   Q 8 .   ? -29.517 -3.454  34.882  1.00 26.34  ?  734 HOH   A O   1 
HETATM 15025 O O   . HOH   Q 8 .   ? -33.704 6.761   52.738  1.00 37.65  ?  735 HOH   A O   1 
HETATM 15026 O O   . HOH   Q 8 .   ? -28.096 -29.623 64.857  1.00 34.16  ?  736 HOH   A O   1 
HETATM 15027 O O   . HOH   Q 8 .   ? -16.312 15.231  55.234  1.00 23.27  ?  737 HOH   A O   1 
HETATM 15028 O O   . HOH   Q 8 .   ? -46.899 -11.711 34.192  1.00 29.68  ?  738 HOH   A O   1 
HETATM 15029 O O   . HOH   Q 8 .   ? -17.706 -12.679 73.345  1.00 23.49  ?  739 HOH   A O   1 
HETATM 15030 O O   . HOH   Q 8 .   ? -18.556 -23.081 60.922  1.00 25.25  ?  740 HOH   A O   1 
HETATM 15031 O O   . HOH   Q 8 .   ? -2.094  -12.783 57.529  1.00 29.92  ?  741 HOH   A O   1 
HETATM 15032 O O   . HOH   Q 8 .   ? -34.643 17.057  75.463  1.00 66.78  ?  742 HOH   A O   1 
HETATM 15033 O O   . HOH   Q 8 .   ? -7.433  -6.104  39.646  1.00 16.60  ?  743 HOH   A O   1 
HETATM 15034 O O   . HOH   Q 8 .   ? -41.909 -21.776 55.539  1.00 28.13  ?  744 HOH   A O   1 
HETATM 15035 O O   . HOH   Q 8 .   ? -21.083 2.946   59.615  1.00 20.35  ?  745 HOH   A O   1 
HETATM 15036 O O   . HOH   Q 8 .   ? -28.949 -9.648  51.650  1.00 18.59  ?  746 HOH   A O   1 
HETATM 15037 O O   . HOH   Q 8 .   ? -32.158 -14.928 68.237  1.00 30.03  ?  747 HOH   A O   1 
HETATM 15038 O O   . HOH   Q 8 .   ? -17.638 -20.286 30.773  1.00 37.43  ?  748 HOH   A O   1 
HETATM 15039 O O   . HOH   Q 8 .   ? -14.502 13.924  57.792  1.00 27.95  ?  749 HOH   A O   1 
HETATM 15040 O O   . HOH   Q 8 .   ? -46.370 -8.990  51.680  1.00 33.77  ?  750 HOH   A O   1 
HETATM 15041 O O   . HOH   Q 8 .   ? -34.657 -11.053 24.643  1.00 39.79  ?  751 HOH   A O   1 
HETATM 15042 O O   . HOH   Q 8 .   ? -13.728 -1.029  43.280  1.00 17.42  ?  752 HOH   A O   1 
HETATM 15043 O O   . HOH   Q 8 .   ? -22.912 -27.277 42.350  1.00 36.09  ?  753 HOH   A O   1 
HETATM 15044 O O   . HOH   Q 8 .   ? -31.751 8.293   77.911  1.00 41.02  ?  754 HOH   A O   1 
HETATM 15045 O O   . HOH   Q 8 .   ? -47.923 -10.902 64.465  1.00 28.88  ?  755 HOH   A O   1 
HETATM 15046 O O   . HOH   Q 8 .   ? -4.200  -19.153 43.912  1.00 30.45  ?  756 HOH   A O   1 
HETATM 15047 O O   . HOH   Q 8 .   ? -49.244 -17.004 63.811  1.00 44.29  ?  757 HOH   A O   1 
HETATM 15048 O O   . HOH   Q 8 .   ? -18.947 2.590   50.155  1.00 19.11  ?  758 HOH   A O   1 
HETATM 15049 O O   . HOH   Q 8 .   ? -55.538 -14.856 49.868  1.00 38.34  ?  759 HOH   A O   1 
HETATM 15050 O O   . HOH   Q 8 .   ? -18.084 -20.535 63.619  1.00 24.43  ?  760 HOH   A O   1 
HETATM 15051 O O   . HOH   Q 8 .   ? -43.770 15.145  44.380  1.00 47.35  ?  761 HOH   A O   1 
HETATM 15052 O O   . HOH   Q 8 .   ? -3.281  -11.883 74.436  1.00 27.40  ?  762 HOH   A O   1 
HETATM 15053 O O   . HOH   Q 8 .   ? -30.647 12.880  75.795  1.00 36.58  ?  763 HOH   A O   1 
HETATM 15054 O O   . HOH   Q 8 .   ? 0.608   -14.639 48.695  1.00 32.49  ?  764 HOH   A O   1 
HETATM 15055 O O   . HOH   Q 8 .   ? -16.937 -20.478 61.193  1.00 24.48  ?  765 HOH   A O   1 
HETATM 15056 O O   . HOH   Q 8 .   ? -24.705 -11.015 28.216  1.00 27.17  ?  766 HOH   A O   1 
HETATM 15057 O O   . HOH   Q 8 .   ? -35.264 -10.944 71.418  1.00 37.07  ?  767 HOH   A O   1 
HETATM 15058 O O   . HOH   Q 8 .   ? -44.609 -14.645 69.779  1.00 27.42  ?  768 HOH   A O   1 
HETATM 15059 O O   . HOH   Q 8 .   ? -8.742  -17.767 56.053  1.00 28.47  ?  769 HOH   A O   1 
HETATM 15060 O O   . HOH   Q 8 .   ? -26.804 -1.542  80.107  1.00 29.94  ?  770 HOH   A O   1 
HETATM 15061 O O   . HOH   Q 8 .   ? -34.132 -8.880  70.001  1.00 26.53  ?  771 HOH   A O   1 
HETATM 15062 O O   . HOH   Q 8 .   ? -43.404 -9.826  71.863  1.00 36.17  ?  772 HOH   A O   1 
HETATM 15063 O O   . HOH   Q 8 .   ? -10.824 -18.164 34.457  1.00 31.34  ?  773 HOH   A O   1 
HETATM 15064 O O   . HOH   Q 8 .   ? -41.105 -1.500  35.850  1.00 40.69  ?  774 HOH   A O   1 
HETATM 15065 O O   . HOH   Q 8 .   ? -32.307 -10.882 68.148  1.00 28.05  ?  775 HOH   A O   1 
HETATM 15066 O O   . HOH   Q 8 .   ? -47.012 -21.949 35.428  1.00 35.39  ?  776 HOH   A O   1 
HETATM 15067 O O   . HOH   Q 8 .   ? -18.769 -13.381 55.488  1.00 20.38  ?  777 HOH   A O   1 
HETATM 15068 O O   . HOH   Q 8 .   ? -46.682 -9.159  34.605  1.00 31.17  ?  778 HOH   A O   1 
HETATM 15069 O O   . HOH   Q 8 .   ? -48.917 -12.195 32.606  1.00 30.30  ?  779 HOH   A O   1 
HETATM 15070 O O   . HOH   Q 8 .   ? -6.968  -15.639 53.235  1.00 23.40  ?  780 HOH   A O   1 
HETATM 15071 O O   . HOH   Q 8 .   ? -5.676  -17.567 50.726  1.00 35.76  ?  781 HOH   A O   1 
HETATM 15072 O O   . HOH   Q 8 .   ? -48.847 -10.193 46.046  1.00 38.42  ?  782 HOH   A O   1 
HETATM 15073 O O   . HOH   Q 8 .   ? -38.840 -2.863  46.445  1.00 31.76  ?  783 HOH   A O   1 
HETATM 15074 O O   . HOH   Q 8 .   ? -47.871 -25.728 51.829  1.00 61.95  ?  784 HOH   A O   1 
HETATM 15075 O O   . HOH   Q 8 .   ? -46.753 -20.388 32.476  1.00 35.54  ?  785 HOH   A O   1 
HETATM 15076 O O   . HOH   Q 8 .   ? -34.382 -17.872 34.113  1.00 28.64  ?  786 HOH   A O   1 
HETATM 15077 O O   . HOH   Q 8 .   ? -42.280 -18.060 65.831  1.00 30.67  ?  787 HOH   A O   1 
HETATM 15078 O O   . HOH   Q 8 .   ? -16.151 -19.023 66.397  1.00 29.11  ?  788 HOH   A O   1 
HETATM 15079 O O   . HOH   Q 8 .   ? -19.195 12.121  73.390  1.00 30.61  ?  789 HOH   A O   1 
HETATM 15080 O O   . HOH   Q 8 .   ? -23.952 -15.551 23.475  1.00 37.56  ?  790 HOH   A O   1 
HETATM 15081 O O   . HOH   Q 8 .   ? -24.997 -7.866  28.064  1.00 26.91  ?  791 HOH   A O   1 
HETATM 15082 O O   . HOH   Q 8 .   ? -35.089 -27.482 56.778  1.00 24.49  ?  792 HOH   A O   1 
HETATM 15083 O O   . HOH   Q 8 .   ? -44.705 -5.229  45.718  1.00 26.24  ?  793 HOH   A O   1 
HETATM 15084 O O   . HOH   Q 8 .   ? -24.409 8.929   76.967  1.00 28.75  ?  794 HOH   A O   1 
HETATM 15085 O O   . HOH   Q 8 .   ? -18.766 6.421   58.367  1.00 17.52  ?  795 HOH   A O   1 
HETATM 15086 O O   . HOH   Q 8 .   ? -8.655  -17.201 59.676  1.00 36.02  ?  796 HOH   A O   1 
HETATM 15087 O O   . HOH   Q 8 .   ? -38.313 -23.755 61.130  1.00 35.17  ?  797 HOH   A O   1 
HETATM 15088 O O   . HOH   Q 8 .   ? -29.577 -2.173  32.677  1.00 30.82  ?  798 HOH   A O   1 
HETATM 15089 O O   . HOH   Q 8 .   ? -37.948 -23.523 63.322  1.00 25.55  ?  799 HOH   A O   1 
HETATM 15090 O O   . HOH   Q 8 .   ? -4.692  -17.035 62.262  1.00 41.10  ?  800 HOH   A O   1 
HETATM 15091 O O   . HOH   Q 8 .   ? -41.258 -2.873  29.365  1.00 36.71  ?  801 HOH   A O   1 
HETATM 15092 O O   . HOH   Q 8 .   ? -14.853 17.291  54.188  1.00 24.69  ?  802 HOH   A O   1 
HETATM 15093 O O   . HOH   Q 8 .   ? -12.776 2.282   58.002  1.00 26.04  ?  803 HOH   A O   1 
HETATM 15094 O O   . HOH   Q 8 .   ? -23.073 4.383   80.947  1.00 31.57  ?  804 HOH   A O   1 
HETATM 15095 O O   . HOH   Q 8 .   ? -4.047  -13.528 50.818  1.00 17.72  ?  805 HOH   A O   1 
HETATM 15096 O O   . HOH   Q 8 .   ? -18.707 -24.380 65.647  1.00 26.21  ?  806 HOH   A O   1 
HETATM 15097 O O   . HOH   Q 8 .   ? -29.998 -14.707 68.910  1.00 35.77  ?  807 HOH   A O   1 
HETATM 15098 O O   . HOH   Q 8 .   ? -16.184 11.937  73.297  1.00 32.48  ?  808 HOH   A O   1 
HETATM 15099 O O   . HOH   Q 8 .   ? -2.676  -13.923 53.320  1.00 22.81  ?  809 HOH   A O   1 
HETATM 15100 O O   . HOH   Q 8 .   ? -54.491 -18.634 42.731  1.00 43.14  ?  810 HOH   A O   1 
HETATM 15101 O O   . HOH   Q 8 .   ? -8.994  -19.502 51.296  1.00 26.76  ?  811 HOH   A O   1 
HETATM 15102 O O   . HOH   Q 8 .   ? -22.169 9.276   76.762  1.00 32.81  ?  812 HOH   A O   1 
HETATM 15103 O O   A HOH   R 8 .   ? 11.523  1.541   36.557  0.89 20.25  ?  601 HOH   B O   1 
HETATM 15104 O O   . HOH   R 8 .   ? -0.717  24.065  19.302  1.00 32.20  ?  602 HOH   B O   1 
HETATM 15105 O O   . HOH   R 8 .   ? -0.142  21.167  19.442  1.00 33.41  ?  603 HOH   B O   1 
HETATM 15106 O O   . HOH   R 8 .   ? -16.690 -14.444 24.608  1.00 48.35  ?  604 HOH   B O   1 
HETATM 15107 O O   . HOH   R 8 .   ? -15.051 -13.634 26.779  1.00 42.78  ?  605 HOH   B O   1 
HETATM 15108 O O   . HOH   R 8 .   ? 8.364   13.193  40.071  1.00 29.88  ?  606 HOH   B O   1 
HETATM 15109 O O   . HOH   R 8 .   ? 0.939   -8.777  41.221  1.00 27.94  ?  607 HOH   B O   1 
HETATM 15110 O O   . HOH   R 8 .   ? -1.298  -8.176  34.466  1.00 15.40  ?  608 HOH   B O   1 
HETATM 15111 O O   . HOH   R 8 .   ? 8.526   9.440   51.347  1.00 30.77  ?  609 HOH   B O   1 
HETATM 15112 O O   . HOH   R 8 .   ? -12.312 0.841   45.578  1.00 18.39  ?  610 HOH   B O   1 
HETATM 15113 O O   . HOH   R 8 .   ? -0.105  6.758   25.640  1.00 21.24  ?  611 HOH   B O   1 
HETATM 15114 O O   . HOH   R 8 .   ? -9.079  26.278  15.372  1.00 38.80  ?  612 HOH   B O   1 
HETATM 15115 O O   . HOH   R 8 .   ? -2.246  18.464  14.781  1.00 26.69  ?  613 HOH   B O   1 
HETATM 15116 O O   . HOH   R 8 .   ? 5.081   12.360  9.113   1.00 31.65  ?  614 HOH   B O   1 
HETATM 15117 O O   . HOH   R 8 .   ? 3.780   3.251   20.952  1.00 20.52  ?  615 HOH   B O   1 
HETATM 15118 O O   . HOH   R 8 .   ? -26.361 4.447   46.909  1.00 31.42  ?  616 HOH   B O   1 
HETATM 15119 O O   . HOH   R 8 .   ? -5.548  -5.073  3.918   1.00 63.51  ?  617 HOH   B O   1 
HETATM 15120 O O   . HOH   R 8 .   ? -6.644  9.720   53.137  1.00 22.00  ?  618 HOH   B O   1 
HETATM 15121 O O   . HOH   R 8 .   ? -14.154 6.954   27.415  1.00 29.33  ?  619 HOH   B O   1 
HETATM 15122 O O   . HOH   R 8 .   ? -15.452 21.608  42.439  1.00 26.70  ?  620 HOH   B O   1 
HETATM 15123 O O   . HOH   R 8 .   ? 2.556   25.225  17.603  1.00 32.16  ?  621 HOH   B O   1 
HETATM 15124 O O   . HOH   R 8 .   ? -10.359 -22.385 28.558  1.00 40.13  ?  622 HOH   B O   1 
HETATM 15125 O O   . HOH   R 8 .   ? -23.063 21.400  27.759  1.00 32.19  ?  623 HOH   B O   1 
HETATM 15126 O O   . HOH   R 8 .   ? -8.756  -0.544  47.635  1.00 20.36  ?  624 HOH   B O   1 
HETATM 15127 O O   . HOH   R 8 .   ? -16.326 9.098   58.182  1.00 28.13  ?  625 HOH   B O   1 
HETATM 15128 O O   . HOH   R 8 .   ? -14.656 19.798  40.886  1.00 24.16  ?  626 HOH   B O   1 
HETATM 15129 O O   . HOH   R 8 .   ? -8.015  14.642  53.430  1.00 36.57  ?  627 HOH   B O   1 
HETATM 15130 O O   . HOH   R 8 .   ? 1.302   -4.472  33.807  1.00 20.28  ?  628 HOH   B O   1 
HETATM 15131 O O   . HOH   R 8 .   ? -0.158  10.770  51.518  1.00 18.22  ?  629 HOH   B O   1 
HETATM 15132 O O   . HOH   R 8 .   ? 14.834  6.077   26.061  1.00 20.45  ?  630 HOH   B O   1 
HETATM 15133 O O   . HOH   R 8 .   ? -2.271  15.792  12.069  1.00 36.96  ?  631 HOH   B O   1 
HETATM 15134 O O   . HOH   R 8 .   ? 7.619   6.439   24.114  1.00 15.13  ?  632 HOH   B O   1 
HETATM 15135 O O   . HOH   R 8 .   ? -8.824  -1.991  33.433  1.00 17.24  ?  633 HOH   B O   1 
HETATM 15136 O O   . HOH   R 8 .   ? 5.591   11.522  40.139  1.00 24.03  ?  634 HOH   B O   1 
HETATM 15137 O O   . HOH   R 8 .   ? -9.845  1.532   54.012  1.00 20.10  ?  635 HOH   B O   1 
HETATM 15138 O O   . HOH   R 8 .   ? 21.023  5.521   21.643  1.00 32.94  ?  636 HOH   B O   1 
HETATM 15139 O O   . HOH   R 8 .   ? 10.521  3.653   11.039  1.00 32.82  ?  637 HOH   B O   1 
HETATM 15140 O O   . HOH   R 8 .   ? -7.894  -5.451  15.942  1.00 45.65  ?  638 HOH   B O   1 
HETATM 15141 O O   . HOH   R 8 .   ? 10.542  -1.118  52.665  1.00 19.18  ?  639 HOH   B O   1 
HETATM 15142 O O   . HOH   R 8 .   ? 2.037   7.621   32.901  1.00 19.27  ?  640 HOH   B O   1 
HETATM 15143 O O   . HOH   R 8 .   ? 14.360  -28.450 29.511  1.00 43.03  ?  641 HOH   B O   1 
HETATM 15144 O O   . HOH   R 8 .   ? -27.685 5.208   14.963  1.00 40.06  ?  642 HOH   B O   1 
HETATM 15145 O O   . HOH   R 8 .   ? 2.034   11.295  52.576  1.00 35.21  ?  643 HOH   B O   1 
HETATM 15146 O O   . HOH   R 8 .   ? 15.931  5.330   23.685  1.00 23.50  ?  644 HOH   B O   1 
HETATM 15147 O O   . HOH   R 8 .   ? -32.950 7.714   19.033  1.00 41.27  ?  645 HOH   B O   1 
HETATM 15148 O O   . HOH   R 8 .   ? 5.846   27.923  32.393  1.00 32.18  ?  646 HOH   B O   1 
HETATM 15149 O O   . HOH   R 8 .   ? 7.530   9.406   47.732  1.00 27.48  ?  647 HOH   B O   1 
HETATM 15150 O O   . HOH   R 8 .   ? -12.164 -15.925 12.619  1.00 54.84  ?  648 HOH   B O   1 
HETATM 15151 O O   . HOH   R 8 .   ? -14.013 22.490  44.252  1.00 32.57  ?  649 HOH   B O   1 
HETATM 15152 O O   . HOH   R 8 .   ? 2.628   10.512  17.104  1.00 18.71  ?  650 HOH   B O   1 
HETATM 15153 O O   . HOH   R 8 .   ? 7.660   0.032   34.436  1.00 15.71  ?  651 HOH   B O   1 
HETATM 15154 O O   . HOH   R 8 .   ? 4.520   9.318   19.988  1.00 16.72  ?  652 HOH   B O   1 
HETATM 15155 O O   . HOH   R 8 .   ? -3.048  -22.308 31.787  1.00 38.73  ?  653 HOH   B O   1 
HETATM 15156 O O   . HOH   R 8 .   ? 3.674   -12.783 25.071  1.00 25.57  ?  654 HOH   B O   1 
HETATM 15157 O O   . HOH   R 8 .   ? -2.523  -11.920 24.398  1.00 25.03  ?  655 HOH   B O   1 
HETATM 15158 O O   . HOH   R 8 .   ? -7.502  8.032   27.061  1.00 19.78  ?  656 HOH   B O   1 
HETATM 15159 O O   . HOH   R 8 .   ? -9.506  7.400   9.750   1.00 33.54  ?  657 HOH   B O   1 
HETATM 15160 O O   . HOH   R 8 .   ? 15.363  10.623  35.630  1.00 22.40  ?  658 HOH   B O   1 
HETATM 15161 O O   . HOH   R 8 .   ? 11.516  4.081   19.914  1.00 19.10  ?  659 HOH   B O   1 
HETATM 15162 O O   . HOH   R 8 .   ? -18.759 3.851   8.192   1.00 42.95  ?  660 HOH   B O   1 
HETATM 15163 O O   . HOH   R 8 .   ? -19.204 21.480  22.761  1.00 41.19  ?  661 HOH   B O   1 
HETATM 15164 O O   . HOH   R 8 .   ? 15.374  -12.309 27.217  1.00 24.69  ?  662 HOH   B O   1 
HETATM 15165 O O   . HOH   R 8 .   ? 18.690  -9.763  28.495  1.00 27.03  ?  663 HOH   B O   1 
HETATM 15166 O O   . HOH   R 8 .   ? 16.200  9.485   52.559  1.00 23.65  ?  664 HOH   B O   1 
HETATM 15167 O O   . HOH   R 8 .   ? -5.745  12.070  7.778   1.00 36.57  ?  665 HOH   B O   1 
HETATM 15168 O O   A HOH   R 8 .   ? 0.998   -15.271 40.806  0.96 28.16  ?  666 HOH   B O   1 
HETATM 15169 O O   . HOH   R 8 .   ? 1.882   24.829  36.706  1.00 32.48  ?  667 HOH   B O   1 
HETATM 15170 O O   . HOH   R 8 .   ? -27.108 20.390  21.014  1.00 43.76  ?  668 HOH   B O   1 
HETATM 15171 O O   . HOH   R 8 .   ? 14.377  27.440  23.764  1.00 34.52  ?  669 HOH   B O   1 
HETATM 15172 O O   . HOH   R 8 .   ? 15.905  0.790   34.987  1.00 21.41  ?  670 HOH   B O   1 
HETATM 15173 O O   . HOH   R 8 .   ? -3.647  22.665  37.718  1.00 32.48  ?  671 HOH   B O   1 
HETATM 15174 O O   . HOH   R 8 .   ? 18.273  10.005  49.649  1.00 30.35  ?  672 HOH   B O   1 
HETATM 15175 O O   . HOH   R 8 .   ? -16.089 6.370   51.228  1.00 15.75  ?  673 HOH   B O   1 
HETATM 15176 O O   . HOH   R 8 .   ? -7.706  16.184  7.351   1.00 36.81  ?  674 HOH   B O   1 
HETATM 15177 O O   . HOH   R 8 .   ? -18.776 9.126   50.416  1.00 19.10  ?  675 HOH   B O   1 
HETATM 15178 O O   . HOH   R 8 .   ? 20.098  -5.460  30.990  1.00 25.03  ?  676 HOH   B O   1 
HETATM 15179 O O   . HOH   R 8 .   ? -7.919  12.812  49.562  1.00 22.55  ?  677 HOH   B O   1 
HETATM 15180 O O   . HOH   R 8 .   ? -8.646  3.881   55.145  1.00 24.16  ?  678 HOH   B O   1 
HETATM 15181 O O   . HOH   R 8 .   ? 6.116   20.354  34.118  1.00 26.81  ?  679 HOH   B O   1 
HETATM 15182 O O   . HOH   R 8 .   ? 3.911   -10.182 5.343   1.00 42.94  ?  680 HOH   B O   1 
HETATM 15183 O O   . HOH   R 8 .   ? 7.032   9.094   40.381  1.00 18.54  ?  681 HOH   B O   1 
HETATM 15184 O O   . HOH   R 8 .   ? 3.441   -13.944 38.745  1.00 29.77  ?  682 HOH   B O   1 
HETATM 15185 O O   . HOH   R 8 .   ? -4.799  1.952   43.633  1.00 15.43  ?  683 HOH   B O   1 
HETATM 15186 O O   . HOH   R 8 .   ? 15.400  -13.041 34.138  1.00 30.97  ?  684 HOH   B O   1 
HETATM 15187 O O   . HOH   R 8 .   ? 7.426   3.140   31.622  1.00 16.73  ?  685 HOH   B O   1 
HETATM 15188 O O   . HOH   R 8 .   ? 5.140   1.399   19.325  1.00 23.49  ?  686 HOH   B O   1 
HETATM 15189 O O   . HOH   R 8 .   ? -28.813 0.268   31.370  1.00 40.67  ?  687 HOH   B O   1 
HETATM 15190 O O   . HOH   R 8 .   ? -23.831 1.737   28.886  1.00 27.23  ?  688 HOH   B O   1 
HETATM 15191 O O   . HOH   R 8 .   ? 18.211  -7.789  31.117  1.00 31.06  ?  689 HOH   B O   1 
HETATM 15192 O O   . HOH   R 8 .   ? -1.120  -21.497 39.875  1.00 35.84  ?  690 HOH   B O   1 
HETATM 15193 O O   . HOH   R 8 .   ? -5.358  6.319   26.091  1.00 23.14  ?  691 HOH   B O   1 
HETATM 15194 O O   . HOH   R 8 .   ? -15.490 4.090   12.175  1.00 36.14  ?  692 HOH   B O   1 
HETATM 15195 O O   . HOH   R 8 .   ? 3.265   -4.011  32.140  1.00 13.74  ?  693 HOH   B O   1 
HETATM 15196 O O   . HOH   R 8 .   ? 2.473   -4.928  38.389  1.00 15.89  ?  694 HOH   B O   1 
HETATM 15197 O O   . HOH   R 8 .   ? 1.224   -10.671 36.447  1.00 20.84  ?  695 HOH   B O   1 
HETATM 15198 O O   . HOH   R 8 .   ? 5.595   -29.324 29.634  1.00 42.82  ?  696 HOH   B O   1 
HETATM 15199 O O   . HOH   R 8 .   ? 7.536   3.132   34.369  1.00 16.05  ?  697 HOH   B O   1 
HETATM 15200 O O   . HOH   R 8 .   ? -4.426  27.173  23.148  1.00 37.23  ?  698 HOH   B O   1 
HETATM 15201 O O   . HOH   R 8 .   ? -4.275  -11.081 22.914  1.00 30.81  ?  699 HOH   B O   1 
HETATM 15202 O O   . HOH   R 8 .   ? -5.018  -4.720  36.814  1.00 16.11  ?  700 HOH   B O   1 
HETATM 15203 O O   . HOH   R 8 .   ? -11.386 18.076  21.729  1.00 24.08  ?  701 HOH   B O   1 
HETATM 15204 O O   . HOH   R 8 .   ? -19.968 21.779  42.056  1.00 37.94  ?  702 HOH   B O   1 
HETATM 15205 O O   . HOH   R 8 .   ? -16.681 4.259   49.794  1.00 17.22  ?  703 HOH   B O   1 
HETATM 15206 O O   . HOH   R 8 .   ? -0.389  -2.260  44.607  1.00 19.56  ?  704 HOH   B O   1 
HETATM 15207 O O   . HOH   R 8 .   ? 2.459   -25.297 33.896  1.00 32.89  ?  705 HOH   B O   1 
HETATM 15208 O O   . HOH   R 8 .   ? -21.138 13.136  42.421  1.00 19.78  ?  706 HOH   B O   1 
HETATM 15209 O O   . HOH   R 8 .   ? -7.377  17.804  46.588  1.00 30.00  ?  707 HOH   B O   1 
HETATM 15210 O O   . HOH   R 8 .   ? 1.643   -12.073 5.650   1.00 41.80  ?  708 HOH   B O   1 
HETATM 15211 O O   . HOH   R 8 .   ? -6.455  -15.528 33.331  1.00 24.63  ?  709 HOH   B O   1 
HETATM 15212 O O   . HOH   R 8 .   ? 11.186  8.567   17.784  1.00 28.18  ?  710 HOH   B O   1 
HETATM 15213 O O   . HOH   R 8 .   ? 5.695   -15.189 38.356  1.00 31.05  ?  711 HOH   B O   1 
HETATM 15214 O O   . HOH   R 8 .   ? -6.882  3.377   43.916  1.00 13.25  ?  712 HOH   B O   1 
HETATM 15215 O O   . HOH   R 8 .   ? 9.217   10.920  40.849  1.00 27.78  ?  713 HOH   B O   1 
HETATM 15216 O O   . HOH   R 8 .   ? 2.774   -6.246  35.902  1.00 16.78  ?  714 HOH   B O   1 
HETATM 15217 O O   . HOH   R 8 .   ? 18.793  -4.671  19.978  1.00 28.33  ?  715 HOH   B O   1 
HETATM 15218 O O   . HOH   R 8 .   ? 13.335  12.297  34.164  1.00 19.79  ?  716 HOH   B O   1 
HETATM 15219 O O   . HOH   R 8 .   ? -11.901 5.877   23.579  1.00 27.35  ?  717 HOH   B O   1 
HETATM 15220 O O   . HOH   R 8 .   ? -29.957 7.714   9.155   1.00 34.87  ?  718 HOH   B O   1 
HETATM 15221 O O   . HOH   R 8 .   ? -16.237 -15.510 17.300  1.00 46.66  ?  719 HOH   B O   1 
HETATM 15222 O O   . HOH   R 8 .   ? -3.647  21.666  35.623  1.00 24.41  ?  720 HOH   B O   1 
HETATM 15223 O O   . HOH   R 8 .   ? -12.146 -3.942  52.142  1.00 11.73  ?  721 HOH   B O   1 
HETATM 15224 O O   . HOH   R 8 .   ? 13.465  5.333   31.480  1.00 22.41  ?  722 HOH   B O   1 
HETATM 15225 O O   . HOH   R 8 .   ? 0.960   9.755   34.394  1.00 19.19  ?  723 HOH   B O   1 
HETATM 15226 O O   . HOH   R 8 .   ? 14.777  4.394   29.773  1.00 24.82  ?  724 HOH   B O   1 
HETATM 15227 O O   . HOH   R 8 .   ? -17.608 21.088  46.722  1.00 27.61  ?  725 HOH   B O   1 
HETATM 15228 O O   . HOH   R 8 .   ? -2.259  10.407  55.196  1.00 25.89  ?  726 HOH   B O   1 
HETATM 15229 O O   . HOH   R 8 .   ? -0.563  15.623  46.244  1.00 32.53  ?  727 HOH   B O   1 
HETATM 15230 O O   . HOH   R 8 .   ? 10.024  6.428   19.285  1.00 19.10  ?  728 HOH   B O   1 
HETATM 15231 O O   . HOH   R 8 .   ? -19.550 -4.371  20.961  1.00 37.59  ?  729 HOH   B O   1 
HETATM 15232 O O   . HOH   R 8 .   ? 7.081   -11.229 46.994  1.00 26.74  ?  730 HOH   B O   1 
HETATM 15233 O O   . HOH   R 8 .   ? -13.279 -5.700  17.032  1.00 50.78  ?  731 HOH   B O   1 
HETATM 15234 O O   . HOH   R 8 .   ? -10.596 6.132   30.124  1.00 21.18  ?  732 HOH   B O   1 
HETATM 15235 O O   . HOH   R 8 .   ? -11.691 -6.418  30.021  1.00 27.62  ?  733 HOH   B O   1 
HETATM 15236 O O   . HOH   R 8 .   ? -15.629 -11.807 5.972   1.00 65.76  ?  734 HOH   B O   1 
HETATM 15237 O O   . HOH   R 8 .   ? -27.663 15.502  42.670  1.00 39.34  ?  735 HOH   B O   1 
HETATM 15238 O O   . HOH   R 8 .   ? 15.988  11.858  37.930  1.00 29.61  ?  736 HOH   B O   1 
HETATM 15239 O O   . HOH   R 8 .   ? 9.951   0.217   12.863  1.00 31.51  ?  737 HOH   B O   1 
HETATM 15240 O O   . HOH   R 8 .   ? -24.139 16.702  21.269  1.00 35.06  ?  738 HOH   B O   1 
HETATM 15241 O O   . HOH   R 8 .   ? 2.499   0.195   8.017   1.00 38.95  ?  739 HOH   B O   1 
HETATM 15242 O O   . HOH   R 8 .   ? -2.522  12.027  36.746  1.00 22.31  ?  740 HOH   B O   1 
HETATM 15243 O O   . HOH   R 8 .   ? 10.966  10.546  27.375  1.00 24.87  ?  741 HOH   B O   1 
HETATM 15244 O O   . HOH   R 8 .   ? -7.429  -4.576  37.188  1.00 17.78  ?  742 HOH   B O   1 
HETATM 15245 O O   . HOH   R 8 .   ? 5.100   16.000  12.244  1.00 30.10  ?  743 HOH   B O   1 
HETATM 15246 O O   . HOH   R 8 .   ? -30.317 6.538   27.085  1.00 36.42  ?  744 HOH   B O   1 
HETATM 15247 O O   . HOH   R 8 .   ? -19.391 10.839  6.714   1.00 42.40  ?  745 HOH   B O   1 
HETATM 15248 O O   . HOH   R 8 .   ? -21.329 -3.574  22.487  1.00 35.27  ?  746 HOH   B O   1 
HETATM 15249 O O   . HOH   R 8 .   ? 3.079   20.789  36.227  1.00 25.85  ?  747 HOH   B O   1 
HETATM 15250 O O   . HOH   R 8 .   ? 5.701   18.757  36.334  1.00 25.20  ?  748 HOH   B O   1 
HETATM 15251 O O   . HOH   R 8 .   ? 14.040  3.165   49.711  1.00 20.00  ?  749 HOH   B O   1 
HETATM 15252 O O   . HOH   R 8 .   ? -15.734 24.190  41.650  1.00 35.76  ?  750 HOH   B O   1 
HETATM 15253 O O   . HOH   R 8 .   ? -30.520 5.033   33.981  1.00 26.35  ?  751 HOH   B O   1 
HETATM 15254 O O   . HOH   R 8 .   ? -5.088  14.866  10.769  1.00 35.13  ?  752 HOH   B O   1 
HETATM 15255 O O   . HOH   R 8 .   ? -12.450 28.481  27.554  1.00 37.55  ?  753 HOH   B O   1 
HETATM 15256 O O   . HOH   R 8 .   ? -5.408  12.238  49.109  1.00 17.22  ?  754 HOH   B O   1 
HETATM 15257 O O   . HOH   R 8 .   ? 2.974   8.890   9.247   1.00 24.75  ?  755 HOH   B O   1 
HETATM 15258 O O   . HOH   R 8 .   ? -16.192 1.161   16.126  1.00 38.85  ?  756 HOH   B O   1 
HETATM 15259 O O   . HOH   R 8 .   ? 3.742   18.477  40.206  1.00 31.96  ?  757 HOH   B O   1 
HETATM 15260 O O   . HOH   R 8 .   ? -7.620  -26.380 30.809  1.00 43.28  ?  758 HOH   B O   1 
HETATM 15261 O O   . HOH   R 8 .   ? -12.582 17.130  52.695  1.00 31.41  ?  759 HOH   B O   1 
HETATM 15262 O O   . HOH   R 8 .   ? -19.342 17.381  42.032  1.00 22.75  ?  760 HOH   B O   1 
HETATM 15263 O O   . HOH   R 8 .   ? 22.294  2.405   26.648  1.00 27.00  ?  761 HOH   B O   1 
HETATM 15264 O O   A HOH   R 8 .   ? -6.718  -9.267  22.450  1.00 34.06  ?  762 HOH   B O   1 
HETATM 15265 O O   . HOH   R 8 .   ? 10.687  -8.127  9.086   1.00 45.84  ?  763 HOH   B O   1 
HETATM 15266 O O   . HOH   R 8 .   ? -9.109  12.778  4.673   1.00 38.29  ?  764 HOH   B O   1 
HETATM 15267 O O   . HOH   R 8 .   ? -14.025 -11.133 18.982  1.00 58.02  ?  765 HOH   B O   1 
HETATM 15268 O O   . HOH   R 8 .   ? 19.417  9.009   32.957  1.00 24.75  ?  766 HOH   B O   1 
HETATM 15269 O O   . HOH   R 8 .   ? 15.458  3.312   16.763  1.00 32.87  ?  767 HOH   B O   1 
HETATM 15270 O O   . HOH   R 8 .   ? -13.320 6.255   30.315  1.00 25.64  ?  768 HOH   B O   1 
HETATM 15271 O O   . HOH   R 8 .   ? -30.281 9.056   34.300  1.00 35.81  ?  769 HOH   B O   1 
HETATM 15272 O O   . HOH   R 8 .   ? -10.164 4.875   11.480  1.00 31.33  ?  770 HOH   B O   1 
HETATM 15273 O O   . HOH   R 8 .   ? 21.012  -6.739  25.597  1.00 33.50  ?  771 HOH   B O   1 
HETATM 15274 O O   . HOH   R 8 .   ? 2.632   8.706   6.638   1.00 33.82  ?  772 HOH   B O   1 
HETATM 15275 O O   . HOH   R 8 .   ? 14.908  -15.532 22.521  1.00 38.26  ?  773 HOH   B O   1 
HETATM 15276 O O   . HOH   R 8 .   ? -3.240  13.790  48.466  1.00 30.20  ?  774 HOH   B O   1 
HETATM 15277 O O   . HOH   R 8 .   ? -22.818 16.224  47.365  1.00 31.03  ?  775 HOH   B O   1 
HETATM 15278 O O   . HOH   R 8 .   ? 3.125   14.639  47.822  1.00 37.80  ?  776 HOH   B O   1 
HETATM 15279 O O   . HOH   R 8 .   ? 5.574   11.056  45.716  1.00 34.56  ?  777 HOH   B O   1 
HETATM 15280 O O   . HOH   R 8 .   ? -16.537 -13.337 16.712  1.00 42.21  ?  778 HOH   B O   1 
HETATM 15281 O O   . HOH   R 8 .   ? -20.265 26.162  27.335  1.00 35.28  ?  779 HOH   B O   1 
HETATM 15282 O O   . HOH   R 8 .   ? -12.566 24.492  10.765  1.00 43.15  ?  780 HOH   B O   1 
HETATM 15283 O O   . HOH   R 8 .   ? -10.891 -3.313  10.254  1.00 57.32  ?  781 HOH   B O   1 
HETATM 15284 O O   . HOH   R 8 .   ? 3.432   18.511  37.862  1.00 26.32  ?  782 HOH   B O   1 
HETATM 15285 O O   . HOH   R 8 .   ? 22.144  4.717   27.868  1.00 32.64  ?  783 HOH   B O   1 
HETATM 15286 O O   . HOH   R 8 .   ? -0.392  -6.864  32.612  1.00 21.92  ?  784 HOH   B O   1 
HETATM 15287 O O   . HOH   R 8 .   ? 3.976   -19.828 18.362  1.00 31.30  ?  785 HOH   B O   1 
HETATM 15288 O O   . HOH   R 8 .   ? -16.155 25.448  34.188  1.00 42.03  ?  786 HOH   B O   1 
HETATM 15289 O O   . HOH   R 8 .   ? 8.762   8.861   21.127  1.00 22.03  ?  787 HOH   B O   1 
HETATM 15290 O O   . HOH   R 8 .   ? -2.133  -17.195 39.740  1.00 22.96  ?  788 HOH   B O   1 
HETATM 15291 O O   . HOH   R 8 .   ? -6.592  16.948  9.893   1.00 34.29  ?  789 HOH   B O   1 
HETATM 15292 O O   . HOH   R 8 .   ? 17.614  -0.769  35.334  1.00 20.50  ?  790 HOH   B O   1 
HETATM 15293 O O   . HOH   R 8 .   ? -26.638 6.958   11.271  1.00 39.67  ?  791 HOH   B O   1 
HETATM 15294 O O   . HOH   R 8 .   ? 0.840   -8.065  36.491  1.00 14.94  ?  792 HOH   B O   1 
HETATM 15295 O O   . HOH   R 8 .   ? 1.082   -3.365  42.170  1.00 24.80  ?  793 HOH   B O   1 
HETATM 15296 O O   . HOH   R 8 .   ? 7.037   30.349  29.682  1.00 45.72  ?  794 HOH   B O   1 
HETATM 15297 O O   . HOH   R 8 .   ? 1.117   -21.189 19.661  1.00 42.56  ?  795 HOH   B O   1 
HETATM 15298 O O   . HOH   R 8 .   ? 1.963   14.094  49.669  1.00 32.26  ?  796 HOH   B O   1 
HETATM 15299 O O   . HOH   R 8 .   ? -27.387 23.340  33.529  1.00 38.42  ?  797 HOH   B O   1 
HETATM 15300 O O   . HOH   R 8 .   ? -3.020  25.901  21.331  1.00 37.73  ?  798 HOH   B O   1 
HETATM 15301 O O   . HOH   R 8 .   ? 15.162  1.055   11.964  1.00 41.40  ?  799 HOH   B O   1 
HETATM 15302 O O   . HOH   R 8 .   ? -31.088 6.077   35.873  1.00 36.45  ?  800 HOH   B O   1 
HETATM 15303 O O   . HOH   R 8 .   ? 23.001  3.725   29.875  1.00 29.30  ?  801 HOH   B O   1 
HETATM 15304 O O   . HOH   R 8 .   ? 16.426  5.365   52.906  1.00 20.12  ?  802 HOH   B O   1 
HETATM 15305 O O   . HOH   R 8 .   ? 1.807   16.841  12.001  1.00 40.40  ?  803 HOH   B O   1 
HETATM 15306 O O   . HOH   R 8 .   ? -16.764 13.900  0.217   1.00 33.96  ?  804 HOH   B O   1 
HETATM 15307 O O   . HOH   R 8 .   ? -32.385 5.610   25.562  1.00 36.40  ?  805 HOH   B O   1 
HETATM 15308 O O   . HOH   R 8 .   ? 3.762   11.984  6.465   1.00 31.13  ?  806 HOH   B O   1 
HETATM 15309 O O   . HOH   R 8 .   ? 6.371   10.350  43.272  1.00 30.33  ?  807 HOH   B O   1 
HETATM 15310 O O   . HOH   R 8 .   ? 9.490   17.167  27.080  1.00 32.04  ?  808 HOH   B O   1 
HETATM 15311 O O   . HOH   R 8 .   ? 9.712   5.435   6.120   1.00 32.68  ?  809 HOH   B O   1 
HETATM 15312 O O   . HOH   R 8 .   ? -3.388  2.116   13.546  1.00 28.30  ?  810 HOH   B O   1 
HETATM 15313 O O   . HOH   R 8 .   ? 17.888  -0.069  11.577  1.00 43.85  ?  811 HOH   B O   1 
HETATM 15314 O O   . HOH   R 8 .   ? -16.130 -13.497 28.796  1.00 33.52  ?  812 HOH   B O   1 
HETATM 15315 O O   . HOH   R 8 .   ? 15.184  8.386   25.175  1.00 29.42  ?  813 HOH   B O   1 
HETATM 15316 O O   . HOH   R 8 .   ? -25.912 16.773  23.612  1.00 35.74  ?  814 HOH   B O   1 
HETATM 15317 O O   . HOH   R 8 .   ? 14.202  14.974  34.469  1.00 31.61  ?  815 HOH   B O   1 
HETATM 15318 O O   . HOH   R 8 .   ? -2.705  -18.930 41.358  1.00 28.88  ?  816 HOH   B O   1 
HETATM 15319 O O   . HOH   R 8 .   ? -21.283 19.162  43.025  1.00 27.00  ?  817 HOH   B O   1 
HETATM 15320 O O   . HOH   R 8 .   ? -28.269 9.410   9.164   1.00 26.94  ?  818 HOH   B O   1 
HETATM 15321 O O   . HOH   R 8 .   ? 8.056   -17.333 42.803  1.00 38.46  ?  819 HOH   B O   1 
HETATM 15322 O O   . HOH   R 8 .   ? -5.139  11.873  52.109  1.00 26.91  ?  820 HOH   B O   1 
HETATM 15323 O O   . HOH   R 8 .   ? -2.566  12.040  52.788  1.00 28.33  ?  821 HOH   B O   1 
HETATM 15324 O O   . HOH   R 8 .   ? 20.451  -6.097  18.760  1.00 43.16  ?  822 HOH   B O   1 
HETATM 15325 O O   . HOH   R 8 .   ? -4.667  17.069  46.755  1.00 33.10  ?  823 HOH   B O   1 
HETATM 15326 O O   . HOH   R 8 .   ? -15.973 -5.421  25.468  1.00 40.10  ?  824 HOH   B O   1 
HETATM 15327 O O   . HOH   R 8 .   ? -31.151 10.125  31.698  1.00 39.95  ?  825 HOH   B O   1 
HETATM 15328 O O   . HOH   R 8 .   ? -4.135  -21.844 38.811  1.00 28.87  ?  826 HOH   B O   1 
HETATM 15329 O O   . HOH   R 8 .   ? -11.438 -2.996  15.665  1.00 49.83  ?  827 HOH   B O   1 
HETATM 15330 O O   . HOH   S 8 .   ? 0.470   24.059  91.092  1.00 34.12  ?  601 HOH   C O   1 
HETATM 15331 O O   B HOH   S 8 .   ? -1.247  -6.558  101.493 1.00 64.06  ?  602 HOH   C O   1 
HETATM 15332 O O   . HOH   S 8 .   ? 20.029  -3.853  90.224  1.00 31.75  ?  603 HOH   C O   1 
HETATM 15333 O O   . HOH   S 8 .   ? -0.361  20.855  90.437  1.00 34.24  ?  604 HOH   C O   1 
HETATM 15334 O O   A HOH   S 8 .   ? -11.640 1.641   74.440  0.57 22.66  ?  605 HOH   C O   1 
HETATM 15335 O O   . HOH   S 8 .   ? -3.952  -13.611 85.670  1.00 35.31  ?  606 HOH   C O   1 
HETATM 15336 O O   . HOH   S 8 .   ? 8.026   -11.647 101.423 1.00 56.44  ?  607 HOH   C O   1 
HETATM 15337 O O   A HOH   S 8 .   ? 10.631  9.233   52.942  1.00 27.11  ?  608 HOH   C O   1 
HETATM 15338 O O   . HOH   S 8 .   ? 26.759  19.246  90.316  1.00 40.71  ?  609 HOH   C O   1 
HETATM 15339 O O   . HOH   S 8 .   ? 3.800   -12.419 88.044  1.00 42.61  ?  610 HOH   C O   1 
HETATM 15340 O O   . HOH   S 8 .   ? 16.335  -15.800 92.869  1.00 41.97  ?  611 HOH   C O   1 
HETATM 15341 O O   . HOH   S 8 .   ? 2.936   -12.459 96.222  1.00 46.34  ?  612 HOH   C O   1 
HETATM 15342 O O   A HOH   S 8 .   ? -2.840  -5.919  102.838 1.00 54.42  ?  613 HOH   C O   1 
HETATM 15343 O O   . HOH   S 8 .   ? 15.141  12.912  110.542 1.00 36.56  ?  614 HOH   C O   1 
HETATM 15344 O O   . HOH   S 8 .   ? 29.417  4.301   84.498  1.00 30.13  ?  615 HOH   C O   1 
HETATM 15345 O O   . HOH   S 8 .   ? -3.866  3.217   90.288  1.00 26.58  ?  616 HOH   C O   1 
HETATM 15346 O O   . HOH   S 8 .   ? 2.554   10.217  55.509  1.00 26.00  ?  617 HOH   C O   1 
HETATM 15347 O O   . HOH   S 8 .   ? 14.584  21.035  63.558  1.00 28.31  ?  618 HOH   C O   1 
HETATM 15348 O O   . HOH   S 8 .   ? -3.281  -4.453  78.818  1.00 17.10  ?  619 HOH   C O   1 
HETATM 15349 O O   . HOH   S 8 .   ? 11.532  -5.663  87.052  1.00 40.60  ?  620 HOH   C O   1 
HETATM 15350 O O   . HOH   S 8 .   ? -10.962 3.132   100.031 1.00 41.27  ?  621 HOH   C O   1 
HETATM 15351 O O   . HOH   S 8 .   ? 32.681  8.668   91.579  1.00 33.80  ?  622 HOH   C O   1 
HETATM 15352 O O   . HOH   S 8 .   ? 13.663  -13.895 100.912 1.00 58.46  ?  623 HOH   C O   1 
HETATM 15353 O O   . HOH   S 8 .   ? 2.595   26.899  80.382  1.00 31.71  ?  624 HOH   C O   1 
HETATM 15354 O O   . HOH   S 8 .   ? 4.057   -12.748 104.768 1.00 56.13  ?  625 HOH   C O   1 
HETATM 15355 O O   . HOH   S 8 .   ? 0.031   6.778   85.350  1.00 19.21  ?  626 HOH   C O   1 
HETATM 15356 O O   . HOH   S 8 .   ? -2.924  -6.200  75.055  1.00 17.61  ?  627 HOH   C O   1 
HETATM 15357 O O   . HOH   S 8 .   ? 23.744  16.754  89.616  1.00 23.66  ?  628 HOH   C O   1 
HETATM 15358 O O   . HOH   S 8 .   ? 9.971   2.017   57.002  1.00 19.40  ?  629 HOH   C O   1 
HETATM 15359 O O   . HOH   S 8 .   ? 4.793   -10.357 88.138  1.00 39.78  ?  630 HOH   C O   1 
HETATM 15360 O O   . HOH   S 8 .   ? 21.598  -2.967  87.992  1.00 27.65  ?  631 HOH   C O   1 
HETATM 15361 O O   . HOH   S 8 .   ? -16.045 5.401   87.363  1.00 29.43  ?  632 HOH   C O   1 
HETATM 15362 O O   . HOH   S 8 .   ? 14.053  7.448   83.443  1.00 28.87  ?  633 HOH   C O   1 
HETATM 15363 O O   . HOH   S 8 .   ? -10.322 -1.570  58.309  1.00 16.50  ?  634 HOH   C O   1 
HETATM 15364 O O   . HOH   S 8 .   ? 8.005   14.638  57.684  1.00 32.90  ?  635 HOH   C O   1 
HETATM 15365 O O   . HOH   S 8 .   ? -5.497  11.609  70.903  1.00 20.20  ?  636 HOH   C O   1 
HETATM 15366 O O   . HOH   S 8 .   ? -2.476  -4.549  72.447  1.00 22.34  ?  637 HOH   C O   1 
HETATM 15367 O O   . HOH   S 8 .   ? 18.638  9.572   60.656  1.00 17.39  ?  638 HOH   C O   1 
HETATM 15368 O O   . HOH   S 8 .   ? 6.917   3.445   66.994  1.00 15.00  ?  639 HOH   C O   1 
HETATM 15369 O O   . HOH   S 8 .   ? 9.005   -0.476  63.215  1.00 21.73  ?  640 HOH   C O   1 
HETATM 15370 O O   . HOH   S 8 .   ? -16.021 -13.973 100.700 1.00 50.79  ?  641 HOH   C O   1 
HETATM 15371 O O   . HOH   S 8 .   ? 7.420   18.267  64.644  1.00 26.32  ?  642 HOH   C O   1 
HETATM 15372 O O   . HOH   S 8 .   ? 20.244  0.925   95.018  1.00 27.59  ?  643 HOH   C O   1 
HETATM 15373 O O   . HOH   S 8 .   ? 12.243  0.791   65.386  1.00 20.37  ?  644 HOH   C O   1 
HETATM 15374 O O   . HOH   S 8 .   ? 15.097  -3.395  98.068  1.00 46.86  ?  645 HOH   C O   1 
HETATM 15375 O O   . HOH   S 8 .   ? 17.098  -8.732  96.630  1.00 56.53  ?  646 HOH   C O   1 
HETATM 15376 O O   . HOH   S 8 .   ? 8.849   -1.791  77.491  1.00 18.32  ?  647 HOH   C O   1 
HETATM 15377 O O   . HOH   S 8 .   ? 20.888  13.338  68.406  1.00 17.91  ?  648 HOH   C O   1 
HETATM 15378 O O   . HOH   S 8 .   ? 15.645  -2.293  89.712  1.00 23.15  ?  649 HOH   C O   1 
HETATM 15379 O O   . HOH   S 8 .   ? -3.065  10.371  93.931  1.00 23.36  ?  650 HOH   C O   1 
HETATM 15380 O O   . HOH   S 8 .   ? 22.402  25.454  74.841  1.00 27.04  ?  651 HOH   C O   1 
HETATM 15381 O O   . HOH   S 8 .   ? -11.028 11.041  83.302  1.00 28.66  ?  652 HOH   C O   1 
HETATM 15382 O O   . HOH   S 8 .   ? 6.206   10.219  57.906  1.00 20.34  ?  653 HOH   C O   1 
HETATM 15383 O O   . HOH   S 8 .   ? -1.255  -4.623  77.092  1.00 18.66  ?  654 HOH   C O   1 
HETATM 15384 O O   . HOH   S 8 .   ? 3.446   21.570  75.764  1.00 26.29  ?  655 HOH   C O   1 
HETATM 15385 O O   . HOH   S 8 .   ? 1.219   -8.239  76.411  1.00 20.26  ?  656 HOH   C O   1 
HETATM 15386 O O   . HOH   S 8 .   ? 30.519  3.482   93.378  1.00 41.19  ?  657 HOH   C O   1 
HETATM 15387 O O   . HOH   S 8 .   ? 26.746  9.215   99.459  1.00 23.53  ?  658 HOH   C O   1 
HETATM 15388 O O   . HOH   S 8 .   ? 5.727   12.631  103.005 1.00 31.02  ?  659 HOH   C O   1 
HETATM 15389 O O   . HOH   S 8 .   ? -9.031  9.696   59.818  1.00 36.86  ?  660 HOH   C O   1 
HETATM 15390 O O   . HOH   S 8 .   ? -15.978 0.604   75.842  1.00 28.06  ?  661 HOH   C O   1 
HETATM 15391 O O   . HOH   S 8 .   ? -7.637  0.277   76.555  1.00 15.97  ?  662 HOH   C O   1 
HETATM 15392 O O   . HOH   S 8 .   ? 5.201   6.263   85.034  1.00 22.36  ?  663 HOH   C O   1 
HETATM 15393 O O   . HOH   S 8 .   ? 32.462  9.997   75.197  1.00 34.71  ?  664 HOH   C O   1 
HETATM 15394 O O   . HOH   S 8 .   ? 13.316  1.569   92.878  1.00 28.62  ?  665 HOH   C O   1 
HETATM 15395 O O   . HOH   S 8 .   ? 34.612  6.449   94.918  1.00 38.85  ?  666 HOH   C O   1 
HETATM 15396 O O   . HOH   S 8 .   ? 11.481  19.183  60.412  1.00 31.51  ?  667 HOH   C O   1 
HETATM 15397 O O   . HOH   S 8 .   ? 16.202  6.840   59.802  1.00 17.74  ?  668 HOH   C O   1 
HETATM 15398 O O   . HOH   S 8 .   ? 26.692  4.778   63.839  1.00 30.00  ?  669 HOH   C O   1 
HETATM 15399 O O   . HOH   S 8 .   ? -0.375  -7.986  69.580  1.00 20.74  ?  670 HOH   C O   1 
HETATM 15400 O O   . HOH   S 8 .   ? 23.984  2.018   82.103  1.00 23.08  ?  671 HOH   C O   1 
HETATM 15401 O O   . HOH   S 8 .   ? 15.072  22.355  68.575  1.00 28.62  ?  672 HOH   C O   1 
HETATM 15402 O O   . HOH   S 8 .   ? 0.709   -1.988  66.227  1.00 20.78  ?  673 HOH   C O   1 
HETATM 15403 O O   . HOH   S 8 .   ? -7.710  6.526   86.735  1.00 21.15  ?  674 HOH   C O   1 
HETATM 15404 O O   . HOH   S 8 .   ? 13.492  6.064   53.524  1.00 30.39  ?  675 HOH   C O   1 
HETATM 15405 O O   . HOH   S 8 .   ? -13.521 -22.442 81.764  1.00 44.39  ?  676 HOH   C O   1 
HETATM 15406 O O   . HOH   S 8 .   ? 16.403  27.038  80.426  1.00 44.13  ?  677 HOH   C O   1 
HETATM 15407 O O   . HOH   S 8 .   ? 14.543  20.142  70.258  1.00 23.81  ?  678 HOH   C O   1 
HETATM 15408 O O   . HOH   S 8 .   ? -14.794 6.061   85.068  1.00 23.23  ?  679 HOH   C O   1 
HETATM 15409 O O   . HOH   S 8 .   ? 16.710  4.381   61.271  1.00 20.48  ?  680 HOH   C O   1 
HETATM 15410 O O   . HOH   S 8 .   ? -0.846  -10.594 74.581  1.00 18.91  ?  681 HOH   C O   1 
HETATM 15411 O O   . HOH   S 8 .   ? -19.949 -5.827  79.753  1.00 25.72  ?  682 HOH   C O   1 
HETATM 15412 O O   . HOH   S 8 .   ? -5.274  2.013   103.481 1.00 38.65  ?  683 HOH   C O   1 
HETATM 15413 O O   . HOH   S 8 .   ? 15.886  24.512  69.702  1.00 33.47  ?  684 HOH   C O   1 
HETATM 15414 O O   . HOH   S 8 .   ? 8.552   3.769   55.843  1.00 19.25  ?  685 HOH   C O   1 
HETATM 15415 O O   . HOH   S 8 .   ? -8.052  9.635   62.603  1.00 30.57  ?  686 HOH   C O   1 
HETATM 15416 O O   . HOH   S 8 .   ? -7.408  3.317   76.481  1.00 14.02  ?  687 HOH   C O   1 
HETATM 15417 O O   . HOH   S 8 .   ? 31.686  6.507   71.610  1.00 35.87  ?  688 HOH   C O   1 
HETATM 15418 O O   . HOH   S 8 .   ? -18.386 -10.380 82.472  1.00 35.36  ?  689 HOH   C O   1 
HETATM 15419 O O   . HOH   S 8 .   ? 9.328   7.404   101.242 1.00 24.78  ?  690 HOH   C O   1 
HETATM 15420 O O   . HOH   S 8 .   ? -7.526  3.127   79.323  1.00 20.01  ?  691 HOH   C O   1 
HETATM 15421 O O   . HOH   S 8 .   ? -13.421 11.979  76.655  1.00 22.51  ?  692 HOH   C O   1 
HETATM 15422 O O   . HOH   S 8 .   ? 12.853  11.316  107.414 1.00 36.58  ?  693 HOH   C O   1 
HETATM 15423 O O   . HOH   S 8 .   ? 6.574   -8.753  88.334  1.00 43.07  ?  694 HOH   C O   1 
HETATM 15424 O O   . HOH   S 8 .   ? -14.307 -16.014 83.751  1.00 44.05  ?  695 HOH   C O   1 
HETATM 15425 O O   . HOH   S 8 .   ? 7.525   21.710  101.522 1.00 43.19  ?  696 HOH   C O   1 
HETATM 15426 O O   . HOH   S 8 .   ? -1.262  9.889   76.548  1.00 21.62  ?  697 HOH   C O   1 
HETATM 15427 O O   . HOH   S 8 .   ? -6.199  20.362  76.708  1.00 30.07  ?  698 HOH   C O   1 
HETATM 15428 O O   . HOH   S 8 .   ? 27.183  5.238   96.541  1.00 30.58  ?  699 HOH   C O   1 
HETATM 15429 O O   . HOH   S 8 .   ? -5.674  -14.876 72.490  1.00 37.07  ?  700 HOH   C O   1 
HETATM 15430 O O   . HOH   S 8 .   ? 25.280  14.896  87.131  1.00 20.82  ?  701 HOH   C O   1 
HETATM 15431 O O   . HOH   S 8 .   ? 7.530   -4.157  73.765  1.00 17.59  ?  702 HOH   C O   1 
HETATM 15432 O O   . HOH   S 8 .   ? 20.806  18.088  65.413  1.00 21.98  ?  703 HOH   C O   1 
HETATM 15433 O O   . HOH   S 8 .   ? 8.258   4.449   89.515  1.00 23.02  ?  704 HOH   C O   1 
HETATM 15434 O O   . HOH   S 8 .   ? 7.975   9.362   102.934 1.00 32.86  ?  705 HOH   C O   1 
HETATM 15435 O O   . HOH   S 8 .   ? 3.191   16.064  65.703  1.00 27.21  ?  706 HOH   C O   1 
HETATM 15436 O O   . HOH   S 8 .   ? 12.293  24.644  100.011 1.00 44.62  ?  707 HOH   C O   1 
HETATM 15437 O O   . HOH   S 8 .   ? -2.054  8.059   78.032  1.00 23.56  ?  708 HOH   C O   1 
HETATM 15438 O O   . HOH   S 8 .   ? -3.923  -4.550  69.963  1.00 19.24  ?  709 HOH   C O   1 
HETATM 15439 O O   . HOH   S 8 .   ? 4.144   -27.461 86.119  1.00 51.63  ?  710 HOH   C O   1 
HETATM 15440 O O   . HOH   S 8 .   ? -6.844  -10.978 64.006  1.00 28.44  ?  711 HOH   C O   1 
HETATM 15441 O O   . HOH   S 8 .   ? 5.302   12.177  61.829  1.00 17.87  ?  712 HOH   C O   1 
HETATM 15442 O O   . HOH   S 8 .   ? -7.797  18.477  72.814  1.00 34.31  ?  713 HOH   C O   1 
HETATM 15443 O O   . HOH   S 8 .   ? -18.901 -4.362  90.798  1.00 23.43  ?  714 HOH   C O   1 
HETATM 15444 O O   . HOH   S 8 .   ? -3.165  8.530   101.627 1.00 29.63  ?  715 HOH   C O   1 
HETATM 15445 O O   . HOH   S 8 .   ? -3.226  14.589  63.892  1.00 31.78  ?  716 HOH   C O   1 
HETATM 15446 O O   . HOH   S 8 .   ? -1.680  -12.779 102.148 1.00 63.11  ?  717 HOH   C O   1 
HETATM 15447 O O   A HOH   S 8 .   ? 14.546  -14.123 84.022  1.00 39.48  ?  718 HOH   C O   1 
HETATM 15448 O O   . HOH   S 8 .   ? -5.478  1.397   91.728  1.00 27.94  ?  719 HOH   C O   1 
HETATM 15449 O O   . HOH   S 8 .   ? 19.893  21.139  80.068  1.00 26.89  ?  720 HOH   C O   1 
HETATM 15450 O O   . HOH   S 8 .   ? 0.211   -4.553  102.345 1.00 62.69  ?  721 HOH   C O   1 
HETATM 15451 O O   . HOH   S 8 .   ? -9.770  26.385  79.058  1.00 46.04  ?  722 HOH   C O   1 
HETATM 15452 O O   . HOH   S 8 .   ? 9.427   24.286  79.469  1.00 31.82  ?  723 HOH   C O   1 
HETATM 15453 O O   . HOH   S 8 .   ? 29.880  9.754   76.910  1.00 24.73  ?  724 HOH   C O   1 
HETATM 15454 O O   . HOH   S 8 .   ? 25.584  19.491  100.203 1.00 32.20  ?  725 HOH   C O   1 
HETATM 15455 O O   . HOH   S 8 .   ? 9.453   -0.407  104.896 1.00 54.36  ?  726 HOH   C O   1 
HETATM 15456 O O   . HOH   S 8 .   ? -3.677  18.421  73.509  1.00 27.74  ?  727 HOH   C O   1 
HETATM 15457 O O   . HOH   S 8 .   ? 11.750  -6.029  80.842  1.00 23.81  ?  728 HOH   C O   1 
HETATM 15458 O O   . HOH   S 8 .   ? -15.585 10.668  75.342  1.00 27.74  ?  729 HOH   C O   1 
HETATM 15459 O O   . HOH   S 8 .   ? -18.650 9.903   61.170  1.00 22.87  ?  730 HOH   C O   1 
HETATM 15460 O O   . HOH   S 8 .   ? 10.624  6.711   80.752  1.00 20.61  ?  731 HOH   C O   1 
HETATM 15461 O O   . HOH   S 8 .   ? 19.028  17.691  68.918  1.00 26.62  ?  732 HOH   C O   1 
HETATM 15462 O O   . HOH   S 8 .   ? 2.368   -12.667 86.394  1.00 34.45  ?  733 HOH   C O   1 
HETATM 15463 O O   . HOH   S 8 .   ? 13.223  1.998   98.086  1.00 36.73  ?  734 HOH   C O   1 
HETATM 15464 O O   . HOH   S 8 .   ? -10.885 -14.306 101.353 1.00 53.90  ?  735 HOH   C O   1 
HETATM 15465 O O   . HOH   S 8 .   ? 12.233  -3.634  58.702  1.00 11.43  ?  736 HOH   C O   1 
HETATM 15466 O O   . HOH   S 8 .   ? -13.412 5.088   79.650  1.00 28.03  ?  737 HOH   C O   1 
HETATM 15467 O O   . HOH   S 8 .   ? 22.141  15.961  61.042  1.00 36.82  ?  738 HOH   C O   1 
HETATM 15468 O O   . HOH   S 8 .   ? 7.803   12.958  61.454  1.00 19.42  ?  739 HOH   C O   1 
HETATM 15469 O O   . HOH   S 8 .   ? 25.219  24.594  77.280  1.00 34.54  ?  740 HOH   C O   1 
HETATM 15470 O O   . HOH   S 8 .   ? 19.181  3.395   58.313  1.00 19.08  ?  741 HOH   C O   1 
HETATM 15471 O O   . HOH   S 8 .   ? -6.090  18.676  74.463  1.00 27.77  ?  742 HOH   C O   1 
HETATM 15472 O O   . HOH   S 8 .   ? 13.007  -10.530 90.792  1.00 49.04  ?  743 HOH   C O   1 
HETATM 15473 O O   . HOH   S 8 .   ? -10.533 -29.252 83.166  1.00 42.90  ?  744 HOH   C O   1 
HETATM 15474 O O   . HOH   S 8 .   ? 12.123  6.157   87.440  1.00 21.78  ?  745 HOH   C O   1 
HETATM 15475 O O   . HOH   S 8 .   ? -8.933  9.666   89.541  1.00 33.49  ?  746 HOH   C O   1 
HETATM 15476 O O   . HOH   S 8 .   ? 15.295  4.233   98.924  1.00 27.45  ?  747 HOH   C O   1 
HETATM 15477 O O   . HOH   S 8 .   ? 2.706   -22.233 78.575  1.00 42.46  ?  748 HOH   C O   1 
HETATM 15478 O O   . HOH   S 8 .   ? 9.102   12.911  106.093 1.00 41.79  ?  749 HOH   C O   1 
HETATM 15479 O O   . HOH   S 8 .   ? -10.068 6.827   91.714  1.00 26.99  ?  750 HOH   C O   1 
HETATM 15480 O O   . HOH   S 8 .   ? -4.582  9.270   91.027  1.00 19.47  ?  751 HOH   C O   1 
HETATM 15481 O O   . HOH   S 8 .   ? -21.044 5.629   89.275  1.00 37.39  ?  752 HOH   C O   1 
HETATM 15482 O O   . HOH   S 8 .   ? 30.014  8.112   102.104 1.00 37.79  ?  753 HOH   C O   1 
HETATM 15483 O O   . HOH   S 8 .   ? -3.991  20.267  94.856  1.00 35.66  ?  754 HOH   C O   1 
HETATM 15484 O O   . HOH   S 8 .   ? 6.809   -15.451 77.592  1.00 28.38  ?  755 HOH   C O   1 
HETATM 15485 O O   . HOH   S 8 .   ? -8.752  17.301  93.771  1.00 35.94  ?  756 HOH   C O   1 
HETATM 15486 O O   . HOH   S 8 .   ? 9.515   30.210  94.570  1.00 41.82  ?  757 HOH   C O   1 
HETATM 15487 O O   . HOH   S 8 .   ? 7.383   8.088   83.865  1.00 22.46  ?  758 HOH   C O   1 
HETATM 15488 O O   . HOH   S 8 .   ? 11.068  18.287  89.463  1.00 25.26  ?  759 HOH   C O   1 
HETATM 15489 O O   . HOH   S 8 .   ? 28.082  1.678   82.621  1.00 36.36  ?  760 HOH   C O   1 
HETATM 15490 O O   . HOH   S 8 .   ? 15.216  8.622   102.712 1.00 33.23  ?  761 HOH   C O   1 
HETATM 15491 O O   . HOH   S 8 .   ? 34.636  7.994   100.071 1.00 34.96  ?  762 HOH   C O   1 
HETATM 15492 O O   . HOH   S 8 .   ? 0.004   11.350  59.731  1.00 19.93  ?  763 HOH   C O   1 
HETATM 15493 O O   . HOH   S 8 .   ? 0.497   -6.573  78.449  1.00 21.81  ?  764 HOH   C O   1 
HETATM 15494 O O   . HOH   S 8 .   ? -11.499 4.059   90.998  1.00 29.37  ?  765 HOH   C O   1 
HETATM 15495 O O   . HOH   S 8 .   ? -1.745  24.968  74.103  1.00 33.83  ?  766 HOH   C O   1 
HETATM 15496 O O   . HOH   S 8 .   ? -7.173  9.031   70.837  1.00 27.06  ?  767 HOH   C O   1 
HETATM 15497 O O   . HOH   S 8 .   ? 12.816  -4.078  100.634 1.00 50.43  ?  768 HOH   C O   1 
HETATM 15498 O O   . HOH   S 8 .   ? -14.892 4.119   81.155  1.00 26.30  ?  769 HOH   C O   1 
HETATM 15499 O O   . HOH   S 8 .   ? -1.367  -2.804  68.878  1.00 28.52  ?  770 HOH   C O   1 
HETATM 15500 O O   . HOH   S 8 .   ? -22.472 -1.274  93.156  1.00 35.68  ?  771 HOH   C O   1 
HETATM 15501 O O   B HOH   S 8 .   ? 10.708  -6.095  83.122  0.64 37.19  ?  772 HOH   C O   1 
HETATM 15502 O O   . HOH   S 8 .   ? 15.180  26.151  76.413  1.00 37.79  ?  773 HOH   C O   1 
HETATM 15503 O O   . HOH   S 8 .   ? 13.944  6.843   101.835 1.00 36.50  ?  774 HOH   C O   1 
HETATM 15504 O O   . HOH   S 8 .   ? 16.712  27.779  93.303  1.00 40.89  ?  775 HOH   C O   1 
HETATM 15505 O O   . HOH   S 8 .   ? 4.888   -10.427 102.795 1.00 60.39  ?  776 HOH   C O   1 
HETATM 15506 O O   . HOH   S 8 .   ? 2.285   -16.910 71.332  1.00 24.61  ?  777 HOH   C O   1 
HETATM 15507 O O   . HOH   S 8 .   ? 16.306  -13.330 94.185  1.00 33.61  ?  778 HOH   C O   1 
HETATM 15508 O O   . HOH   S 8 .   ? -9.672  -20.873 89.370  1.00 49.58  ?  779 HOH   C O   1 
HETATM 15509 O O   . HOH   S 8 .   ? 31.550  15.295  69.699  1.00 43.81  ?  780 HOH   C O   1 
HETATM 15510 O O   . HOH   S 8 .   ? 26.663  14.020  106.535 1.00 41.58  ?  781 HOH   C O   1 
HETATM 15511 O O   . HOH   S 8 .   ? 28.055  23.345  77.271  1.00 36.01  ?  782 HOH   C O   1 
HETATM 15512 O O   . HOH   S 8 .   ? 3.149   13.955  62.565  1.00 28.74  ?  783 HOH   C O   1 
HETATM 15513 O O   . HOH   S 8 .   ? -15.331 -12.942 83.809  1.00 34.67  ?  784 HOH   C O   1 
HETATM 15514 O O   . HOH   S 8 .   ? -1.747  8.677   104.953 1.00 47.56  ?  785 HOH   C O   1 
HETATM 15515 O O   . HOH   S 8 .   ? -18.962 -10.075 89.321  1.00 38.17  ?  786 HOH   C O   1 
HETATM 15516 O O   . HOH   S 8 .   ? -17.577 -1.266  76.006  1.00 24.60  ?  787 HOH   C O   1 
HETATM 15517 O O   . HOH   S 8 .   ? 13.291  6.319   80.617  1.00 20.47  ?  788 HOH   C O   1 
HETATM 15518 O O   . HOH   S 8 .   ? 22.073  16.729  63.732  1.00 35.54  ?  789 HOH   C O   1 
HETATM 15519 O O   . HOH   S 8 .   ? -3.432  -13.607 71.833  1.00 38.58  ?  790 HOH   C O   1 
HETATM 15520 O O   . HOH   S 8 .   ? 15.843  15.635  55.944  1.00 25.01  ?  791 HOH   C O   1 
HETATM 15521 O O   . HOH   S 8 .   ? 1.406   14.365  98.733  1.00 33.24  ?  792 HOH   C O   1 
HETATM 15522 O O   . HOH   S 8 .   ? 19.788  6.898   102.031 1.00 35.95  ?  793 HOH   C O   1 
HETATM 15523 O O   B HOH   S 8 .   ? -20.964 6.826   78.181  0.50 37.84  ?  794 HOH   C O   1 
HETATM 15524 O O   . HOH   S 8 .   ? -2.245  0.197   102.912 1.00 35.22  ?  795 HOH   C O   1 
HETATM 15525 O O   . HOH   S 8 .   ? 10.134  -13.089 99.273  1.00 43.06  ?  796 HOH   C O   1 
HETATM 15526 O O   . HOH   S 8 .   ? 29.483  0.794   79.164  1.00 29.04  ?  797 HOH   C O   1 
HETATM 15527 O O   . HOH   S 8 .   ? -19.494 9.153   77.906  1.00 32.43  ?  798 HOH   C O   1 
HETATM 15528 O O   . HOH   S 8 .   ? -16.319 5.329   58.103  1.00 23.19  ?  799 HOH   C O   1 
HETATM 15529 O O   . HOH   S 8 .   ? -1.914  11.264  57.795  1.00 29.55  ?  800 HOH   C O   1 
HETATM 15530 O O   . HOH   S 8 .   ? 7.882   26.154  95.269  1.00 40.46  ?  801 HOH   C O   1 
HETATM 15531 O O   . HOH   S 8 .   ? 7.878   1.068   103.660 1.00 51.68  ?  802 HOH   C O   1 
HETATM 15532 O O   . HOH   S 8 .   ? 13.370  29.423  72.151  1.00 42.41  ?  803 HOH   C O   1 
HETATM 15533 O O   . HOH   S 8 .   ? 9.861   -15.345 98.904  1.00 46.77  ?  804 HOH   C O   1 
HETATM 15534 O O   . HOH   S 8 .   ? -11.559 16.256  80.762  1.00 35.50  ?  805 HOH   C O   1 
HETATM 15535 O O   . HOH   S 8 .   ? -18.062 -8.740  79.896  1.00 27.74  ?  806 HOH   C O   1 
HETATM 15536 O O   . HOH   S 8 .   ? 7.678   -5.598  94.994  1.00 49.49  ?  807 HOH   C O   1 
HETATM 15537 O O   . HOH   S 8 .   ? 30.307  5.938   77.141  1.00 27.45  ?  808 HOH   C O   1 
HETATM 15538 O O   . HOH   S 8 .   ? 19.985  -10.956 99.415  1.00 37.43  ?  809 HOH   C O   1 
HETATM 15539 O O   . HOH   S 8 .   ? 1.349   29.615  85.915  1.00 33.77  ?  810 HOH   C O   1 
HETATM 15540 O O   . HOH   S 8 .   ? 15.113  -6.194  96.441  1.00 55.55  ?  811 HOH   C O   1 
HETATM 15541 O O   . HOH   S 8 .   ? -7.977  -15.320 61.360  1.00 40.48  ?  812 HOH   C O   1 
HETATM 15542 O O   . HOH   S 8 .   ? -18.401 -1.776  98.690  1.00 37.52  ?  813 HOH   C O   1 
HETATM 15543 O O   . HOH   S 8 .   ? -11.546 13.301  70.008  1.00 43.12  ?  814 HOH   C O   1 
HETATM 15544 O O   . HOH   S 8 .   ? 13.259  -5.263  94.306  1.00 48.66  ?  815 HOH   C O   1 
HETATM 15545 O O   . HOH   S 8 .   ? 28.551  19.139  98.992  1.00 37.17  ?  816 HOH   C O   1 
HETATM 15546 O O   . HOH   S 8 .   ? 1.767   0.485   94.377  1.00 40.42  ?  817 HOH   C O   1 
HETATM 15547 O O   . HOH   S 8 .   ? 5.958   15.810  101.361 1.00 34.30  ?  818 HOH   C O   1 
HETATM 15548 O O   . HOH   S 8 .   ? 7.111   -0.821  101.102 1.00 45.69  ?  819 HOH   C O   1 
HETATM 15549 O O   . HOH   S 8 .   ? 28.640  10.615  102.164 1.00 33.10  ?  820 HOH   C O   1 
HETATM 15550 O O   . HOH   S 8 .   ? 10.683  12.067  107.643 1.00 37.16  ?  821 HOH   C O   1 
HETATM 15551 O O   . HOH   S 8 .   ? -4.434  16.624  98.601  1.00 39.20  ?  822 HOH   C O   1 
HETATM 15552 O O   . HOH   S 8 .   ? -17.235 14.665  80.993  1.00 44.50  ?  823 HOH   C O   1 
HETATM 15553 O O   . HOH   S 8 .   ? 7.144   16.697  103.605 1.00 30.38  ?  824 HOH   C O   1 
HETATM 15554 O O   . HOH   S 8 .   ? 18.207  21.916  101.320 1.00 43.03  ?  825 HOH   C O   1 
HETATM 15555 O O   . HOH   S 8 .   ? -1.890  -12.169 105.132 1.00 50.62  ?  826 HOH   C O   1 
HETATM 15556 O O   . HOH   S 8 .   ? 14.299  10.563  110.338 1.00 36.70  ?  827 HOH   C O   1 
HETATM 15557 O O   . HOH   S 8 .   ? 10.842  -2.092  104.028 1.00 37.74  ?  828 HOH   C O   1 
HETATM 15558 O O   . HOH   S 8 .   ? -12.748 -12.374 100.086 1.00 56.03  ?  829 HOH   C O   1 
HETATM 15559 O O   . HOH   S 8 .   ? -6.535  10.594  67.520  1.00 27.95  ?  830 HOH   C O   1 
HETATM 15560 O O   . HOH   S 8 .   ? 26.525  6.094   99.627  1.00 39.92  ?  831 HOH   C O   1 
HETATM 15561 O O   . HOH   S 8 .   ? -0.627  -8.019  74.303  1.00 17.36  ?  832 HOH   C O   1 
HETATM 15562 O O   . HOH   S 8 .   ? 7.199   8.287   105.487 1.00 37.72  ?  833 HOH   C O   1 
HETATM 15563 O O   . HOH   S 8 .   ? 24.128  20.512  86.858  1.00 32.30  ?  834 HOH   C O   1 
HETATM 15564 O O   . HOH   S 8 .   ? 26.222  0.428   82.266  1.00 27.41  ?  835 HOH   C O   1 
HETATM 15565 O O   . HOH   S 8 .   ? 3.687   2.465   97.208  1.00 37.89  ?  836 HOH   C O   1 
HETATM 15566 O O   . HOH   S 8 .   ? -16.529 6.543   97.067  1.00 35.05  ?  837 HOH   C O   1 
HETATM 15567 O O   . HOH   S 8 .   ? 5.049   11.728  59.089  1.00 20.88  ?  838 HOH   C O   1 
HETATM 15568 O O   . HOH   S 8 .   ? 25.258  22.198  99.353  1.00 39.51  ?  839 HOH   C O   1 
HETATM 15569 O O   . HOH   S 8 .   ? 27.915  18.604  88.387  1.00 34.33  ?  840 HOH   C O   1 
HETATM 15570 O O   . HOH   S 8 .   ? 4.052   -1.745  89.353  1.00 30.92  ?  841 HOH   C O   1 
HETATM 15571 O O   . HOH   S 8 .   ? 2.805   -18.816 69.658  1.00 29.45  ?  842 HOH   C O   1 
HETATM 15572 O O   . HOH   S 8 .   ? 21.072  19.420  67.870  1.00 30.70  ?  843 HOH   C O   1 
HETATM 15573 O O   . HOH   S 8 .   ? 25.444  17.820  87.586  1.00 29.22  ?  844 HOH   C O   1 
HETATM 15574 O O   . HOH   S 8 .   ? 2.177   26.180  75.703  1.00 34.12  ?  845 HOH   C O   1 
HETATM 15575 O O   . HOH   S 8 .   ? 0.410   -19.135 68.343  1.00 33.54  ?  846 HOH   C O   1 
HETATM 15576 O O   . HOH   S 8 .   ? -17.734 11.218  77.712  1.00 24.65  ?  847 HOH   C O   1 
HETATM 15577 O O   . HOH   S 8 .   ? 18.493  17.436  107.510 1.00 38.35  ?  848 HOH   C O   1 
HETATM 15578 O O   . HOH   S 8 .   ? 4.363   17.928  64.220  1.00 29.82  ?  849 HOH   C O   1 
HETATM 15579 O O   . HOH   S 8 .   ? -2.819  15.261  61.469  1.00 33.93  ?  850 HOH   C O   1 
HETATM 15580 O O   . HOH   S 8 .   ? 17.335  20.128  58.269  1.00 35.49  ?  851 HOH   C O   1 
HETATM 15581 O O   . HOH   S 8 .   ? 2.412   27.596  77.836  1.00 37.35  ?  852 HOH   C O   1 
HETATM 15582 O O   . HOH   S 8 .   ? -14.899 8.776   85.465  1.00 28.00  ?  853 HOH   C O   1 
HETATM 15583 O O   . HOH   S 8 .   ? 4.342   15.979  61.593  1.00 31.19  ?  854 HOH   C O   1 
HETATM 15584 O O   . HOH   S 8 .   ? 30.451  10.339  79.384  1.00 28.39  ?  855 HOH   C O   1 
HETATM 15585 O O   . HOH   S 8 .   ? 14.386  26.743  68.270  1.00 37.15  ?  856 HOH   C O   1 
HETATM 15586 O O   . HOH   S 8 .   ? 21.132  -3.792  96.758  1.00 38.03  ?  857 HOH   C O   1 
HETATM 15587 O O   . HOH   S 8 .   ? 19.868  -8.393  88.917  1.00 47.24  ?  858 HOH   C O   1 
HETATM 15588 O O   . HOH   S 8 .   ? 11.054  -2.041  101.267 1.00 40.11  ?  859 HOH   C O   1 
HETATM 15589 O O   . HOH   S 8 .   ? -17.846 -12.916 81.995  1.00 33.68  ?  860 HOH   C O   1 
HETATM 15590 O O   . HOH   S 8 .   ? 9.286   2.318   101.987 1.00 38.97  ?  861 HOH   C O   1 
HETATM 15591 O O   . HOH   T 8 .   ? 54.980  -17.400 63.290  1.00 33.01  ?  601 HOH   D O   1 
HETATM 15592 O O   . HOH   T 8 .   ? -1.003  -10.321 66.634  1.00 29.06  ?  602 HOH   D O   1 
HETATM 15593 O O   . HOH   T 8 .   ? 48.926  12.621  47.239  1.00 53.61  ?  603 HOH   D O   1 
HETATM 15594 O O   . HOH   T 8 .   ? 28.704  -28.392 65.777  1.00 32.41  ?  604 HOH   D O   1 
HETATM 15595 O O   . HOH   T 8 .   ? 1.053   -10.661 39.148  1.00 21.88  ?  605 HOH   D O   1 
HETATM 15596 O O   . HOH   T 8 .   ? 40.853  11.266  53.812  1.00 67.74  ?  606 HOH   D O   1 
HETATM 15597 O O   . HOH   T 8 .   ? 9.860   -22.025 69.335  1.00 24.72  ?  607 HOH   D O   1 
HETATM 15598 O O   . HOH   T 8 .   ? 2.749   -3.553  65.219  1.00 19.25  ?  608 HOH   D O   1 
HETATM 15599 O O   . HOH   T 8 .   ? 18.431  -2.364  37.321  1.00 20.99  ?  609 HOH   D O   1 
HETATM 15600 O O   . HOH   T 8 .   ? 29.592  -7.971  52.037  1.00 19.70  ?  610 HOH   D O   1 
HETATM 15601 O O   . HOH   T 8 .   ? 41.896  -2.770  70.971  1.00 28.66  ?  611 HOH   D O   1 
HETATM 15602 O O   . HOH   T 8 .   ? 33.411  -7.036  63.517  1.00 18.27  ?  612 HOH   D O   1 
HETATM 15603 O O   . HOH   T 8 .   ? 29.936  -8.036  57.254  1.00 19.32  ?  613 HOH   D O   1 
HETATM 15604 O O   . HOH   T 8 .   ? 12.533  -19.227 74.715  1.00 25.50  ?  614 HOH   D O   1 
HETATM 15605 O O   . HOH   T 8 .   ? 31.949  13.110  68.639  1.00 45.44  ?  615 HOH   D O   1 
HETATM 15606 O O   . HOH   T 8 .   ? 37.077  -26.690 48.338  1.00 40.48  ?  616 HOH   D O   1 
HETATM 15607 O O   . HOH   T 8 .   ? 20.020  -1.374  45.481  1.00 16.58  ?  617 HOH   D O   1 
HETATM 15608 O O   . HOH   T 8 .   ? 44.685  -27.321 65.924  1.00 35.63  ?  618 HOH   D O   1 
HETATM 15609 O O   . HOH   T 8 .   ? 29.887  -6.458  35.837  1.00 22.76  ?  619 HOH   D O   1 
HETATM 15610 O O   . HOH   T 8 .   ? 37.542  -19.481 42.571  1.00 34.37  ?  620 HOH   D O   1 
HETATM 15611 O O   . HOH   T 8 .   ? 35.800  -29.318 62.297  1.00 34.01  ?  621 HOH   D O   1 
HETATM 15612 O O   . HOH   T 8 .   ? 22.928  0.704   61.850  1.00 17.65  ?  622 HOH   D O   1 
HETATM 15613 O O   . HOH   T 8 .   ? 29.477  -8.110  66.349  1.00 19.91  ?  623 HOH   D O   1 
HETATM 15614 O O   . HOH   T 8 .   ? 42.180  -22.599 56.288  1.00 28.30  ?  624 HOH   D O   1 
HETATM 15615 O O   . HOH   T 8 .   ? 14.599  -14.422 45.138  1.00 31.54  ?  625 HOH   D O   1 
HETATM 15616 O O   . HOH   T 8 .   ? 50.002  0.974   58.872  1.00 80.51  ?  626 HOH   D O   1 
HETATM 15617 O O   . HOH   T 8 .   ? -2.927  -11.448 68.320  1.00 39.03  ?  627 HOH   D O   1 
HETATM 15618 O O   . HOH   T 8 .   ? 8.228   -16.599 76.166  1.00 28.82  ?  628 HOH   D O   1 
HETATM 15619 O O   . HOH   T 8 .   ? 25.315  -30.451 39.179  1.00 40.83  ?  629 HOH   D O   1 
HETATM 15620 O O   . HOH   T 8 .   ? 42.339  -4.273  39.468  1.00 37.22  ?  630 HOH   D O   1 
HETATM 15621 O O   . HOH   T 8 .   ? 6.685   -20.574 66.001  1.00 30.09  ?  631 HOH   D O   1 
HETATM 15622 O O   . HOH   T 8 .   ? 21.046  6.645   54.275  1.00 20.18  ?  632 HOH   D O   1 
HETATM 15623 O O   . HOH   T 8 .   ? 19.478  -13.750 39.803  1.00 19.64  ?  633 HOH   D O   1 
HETATM 15624 O O   . HOH   T 8 .   ? 20.470  24.268  50.036  1.00 49.98  ?  634 HOH   D O   1 
HETATM 15625 O O   . HOH   T 8 .   ? 3.496   -11.576 36.634  1.00 21.41  ?  635 HOH   D O   1 
HETATM 15626 O O   . HOH   T 8 .   ? 8.231   -15.864 51.321  1.00 29.33  ?  636 HOH   D O   1 
HETATM 15627 O O   . HOH   T 8 .   ? 46.686  -10.583 76.647  1.00 23.61  ?  637 HOH   D O   1 
HETATM 15628 O O   . HOH   T 8 .   ? 22.984  2.841   49.416  1.00 19.99  ?  638 HOH   D O   1 
HETATM 15629 O O   . HOH   T 8 .   ? 32.220  -5.731  81.258  1.00 29.61  ?  639 HOH   D O   1 
HETATM 15630 O O   . HOH   T 8 .   ? 35.335  -2.645  46.010  1.00 30.93  ?  640 HOH   D O   1 
HETATM 15631 O O   . HOH   T 8 .   ? 19.979  -4.481  45.497  1.00 19.81  ?  641 HOH   D O   1 
HETATM 15632 O O   . HOH   T 8 .   ? 14.800  -12.782 48.148  1.00 19.47  ?  642 HOH   D O   1 
HETATM 15633 O O   . HOH   T 8 .   ? 34.967  -22.865 70.655  1.00 27.30  ?  643 HOH   D O   1 
HETATM 15634 O O   . HOH   T 8 .   ? 20.739  -23.056 56.846  1.00 23.59  ?  644 HOH   D O   1 
HETATM 15635 O O   . HOH   T 8 .   ? 32.572  2.589   32.514  1.00 30.87  ?  645 HOH   D O   1 
HETATM 15636 O O   . HOH   T 8 .   ? 7.376   -10.641 73.384  1.00 13.93  ?  646 HOH   D O   1 
HETATM 15637 O O   . HOH   T 8 .   ? 3.224   -11.492 61.562  1.00 15.32  ?  647 HOH   D O   1 
HETATM 15638 O O   . HOH   T 8 .   ? 22.169  -9.340  50.748  1.00 17.05  ?  648 HOH   D O   1 
HETATM 15639 O O   . HOH   T 8 .   ? 25.172  -25.367 61.915  1.00 23.16  ?  649 HOH   D O   1 
HETATM 15640 O O   . HOH   T 8 .   ? 28.506  -17.911 85.066  1.00 31.24  ?  650 HOH   D O   1 
HETATM 15641 O O   . HOH   T 8 .   ? 8.970   -17.093 54.971  1.00 28.28  ?  651 HOH   D O   1 
HETATM 15642 O O   . HOH   T 8 .   ? 22.828  -4.441  45.186  1.00 17.36  ?  652 HOH   D O   1 
HETATM 15643 O O   . HOH   T 8 .   ? 32.280  -27.826 64.336  1.00 25.41  ?  653 HOH   D O   1 
HETATM 15644 O O   . HOH   T 8 .   ? 30.307  -7.923  44.047  1.00 23.06  ?  654 HOH   D O   1 
HETATM 15645 O O   . HOH   T 8 .   ? 40.331  -27.636 58.937  1.00 33.58  ?  655 HOH   D O   1 
HETATM 15646 O O   . HOH   T 8 .   ? 6.838   -14.360 62.733  1.00 15.92  ?  656 HOH   D O   1 
HETATM 15647 O O   . HOH   T 8 .   ? 18.744  9.127   52.115  1.00 25.04  ?  657 HOH   D O   1 
HETATM 15648 O O   . HOH   T 8 .   ? 34.250  -4.241  47.827  1.00 30.06  ?  658 HOH   D O   1 
HETATM 15649 O O   . HOH   T 8 .   ? 18.082  -15.971 85.071  1.00 35.88  ?  659 HOH   D O   1 
HETATM 15650 O O   . HOH   T 8 .   ? 22.473  -1.703  74.044  1.00 26.52  ?  660 HOH   D O   1 
HETATM 15651 O O   . HOH   T 8 .   ? 33.525  -13.983 86.451  1.00 32.06  ?  661 HOH   D O   1 
HETATM 15652 O O   . HOH   T 8 .   ? 7.188   -13.560 60.004  1.00 16.01  ?  662 HOH   D O   1 
HETATM 15653 O O   . HOH   T 8 .   ? 35.216  -19.189 62.565  1.00 17.54  ?  663 HOH   D O   1 
HETATM 15654 O O   . HOH   T 8 .   ? 37.976  -11.991 47.989  1.00 19.61  ?  664 HOH   D O   1 
HETATM 15655 O O   . HOH   T 8 .   ? 45.133  -16.500 55.404  1.00 31.36  ?  665 HOH   D O   1 
HETATM 15656 O O   . HOH   T 8 .   ? 4.153   -12.668 54.960  1.00 17.39  ?  666 HOH   D O   1 
HETATM 15657 O O   . HOH   T 8 .   ? 18.317  -24.403 56.878  1.00 30.71  ?  667 HOH   D O   1 
HETATM 15658 O O   . HOH   T 8 .   ? 16.629  -21.528 68.296  1.00 18.54  ?  668 HOH   D O   1 
HETATM 15659 O O   . HOH   T 8 .   ? 0.767   -12.301 57.846  1.00 18.24  ?  669 HOH   D O   1 
HETATM 15660 O O   . HOH   T 8 .   ? 40.560  -1.176  67.713  1.00 35.06  ?  670 HOH   D O   1 
HETATM 15661 O O   . HOH   T 8 .   ? 23.746  -11.242 85.069  1.00 26.04  ?  671 HOH   D O   1 
HETATM 15662 O O   . HOH   T 8 .   ? 27.809  -7.325  37.271  1.00 25.56  ?  672 HOH   D O   1 
HETATM 15663 O O   . HOH   T 8 .   ? 34.157  -5.760  39.853  1.00 30.25  ?  673 HOH   D O   1 
HETATM 15664 O O   . HOH   T 8 .   ? 29.386  -2.941  75.986  1.00 19.38  ?  674 HOH   D O   1 
HETATM 15665 O O   . HOH   T 8 .   ? 3.080   -11.263 46.216  1.00 24.97  ?  675 HOH   D O   1 
HETATM 15666 O O   . HOH   T 8 .   ? 15.536  -14.800 74.747  1.00 13.60  ?  676 HOH   D O   1 
HETATM 15667 O O   . HOH   T 8 .   ? 39.258  -28.472 67.574  1.00 35.04  ?  677 HOH   D O   1 
HETATM 15668 O O   . HOH   T 8 .   ? 16.349  13.428  47.578  1.00 34.78  ?  678 HOH   D O   1 
HETATM 15669 O O   . HOH   T 8 .   ? 39.757  -7.262  82.977  1.00 35.19  ?  679 HOH   D O   1 
HETATM 15670 O O   . HOH   T 8 .   ? 1.365   -5.427  63.946  1.00 21.55  ?  680 HOH   D O   1 
HETATM 15671 O O   . HOH   T 8 .   ? 33.056  -23.398 77.787  1.00 34.96  ?  681 HOH   D O   1 
HETATM 15672 O O   . HOH   T 8 .   ? 40.963  -20.876 77.221  1.00 31.33  ?  682 HOH   D O   1 
HETATM 15673 O O   . HOH   T 8 .   ? 14.459  -10.345 46.539  1.00 21.03  ?  683 HOH   D O   1 
HETATM 15674 O O   . HOH   T 8 .   ? 7.591   -15.099 57.533  1.00 26.06  ?  684 HOH   D O   1 
HETATM 15675 O O   . HOH   T 8 .   ? 12.432  -4.887  60.868  1.00 15.11  ?  685 HOH   D O   1 
HETATM 15676 O O   . HOH   T 8 .   ? 19.091  4.694   50.461  1.00 18.11  ?  686 HOH   D O   1 
HETATM 15677 O O   . HOH   T 8 .   ? 35.273  -19.774 81.810  1.00 32.69  ?  687 HOH   D O   1 
HETATM 15678 O O   . HOH   T 8 .   ? 32.837  4.733   62.309  1.00 38.20  ?  688 HOH   D O   1 
HETATM 15679 O O   . HOH   T 8 .   ? 34.896  -5.686  59.874  1.00 23.52  ?  689 HOH   D O   1 
HETATM 15680 O O   . HOH   T 8 .   ? 36.957  -17.999 75.212  1.00 19.49  ?  690 HOH   D O   1 
HETATM 15681 O O   . HOH   T 8 .   ? 42.575  -20.360 55.156  1.00 24.61  ?  691 HOH   D O   1 
HETATM 15682 O O   . HOH   T 8 .   ? 10.806  -17.358 57.251  1.00 24.50  ?  692 HOH   D O   1 
HETATM 15683 O O   . HOH   T 8 .   ? 23.867  -6.165  37.722  1.00 23.50  ?  693 HOH   D O   1 
HETATM 15684 O O   . HOH   T 8 .   ? 16.049  -17.098 81.135  1.00 30.67  ?  694 HOH   D O   1 
HETATM 15685 O O   . HOH   T 8 .   ? 43.829  -6.576  77.671  1.00 28.19  ?  695 HOH   D O   1 
HETATM 15686 O O   . HOH   T 8 .   ? 7.602   -5.654  71.236  1.00 17.71  ?  696 HOH   D O   1 
HETATM 15687 O O   . HOH   T 8 .   ? 21.225  3.577   51.652  1.00 20.39  ?  697 HOH   D O   1 
HETATM 15688 O O   . HOH   T 8 .   ? 27.308  -22.318 72.369  1.00 19.81  ?  698 HOH   D O   1 
HETATM 15689 O O   . HOH   T 8 .   ? 25.121  -30.901 62.317  1.00 35.01  ?  699 HOH   D O   1 
HETATM 15690 O O   . HOH   T 8 .   ? 17.533  -19.994 49.999  1.00 27.84  ?  700 HOH   D O   1 
HETATM 15691 O O   . HOH   T 8 .   ? 42.493  -16.794 45.502  1.00 35.71  ?  701 HOH   D O   1 
HETATM 15692 O O   . HOH   T 8 .   ? 34.837  -10.607 46.592  1.00 19.35  ?  702 HOH   D O   1 
HETATM 15693 O O   A HOH   T 8 .   ? 17.164  -2.711  41.522  0.59 21.20  ?  703 HOH   D O   1 
HETATM 15694 O O   . HOH   T 8 .   ? 13.330  -11.933 44.558  1.00 24.81  ?  704 HOH   D O   1 
HETATM 15695 O O   . HOH   T 8 .   ? 20.832  -10.914 51.989  1.00 16.12  ?  705 HOH   D O   1 
HETATM 15696 O O   . HOH   T 8 .   ? 48.943  -17.414 57.149  1.00 32.43  ?  706 HOH   D O   1 
HETATM 15697 O O   A HOH   T 8 .   ? 45.812  -1.597  54.250  1.00 60.69  ?  707 HOH   D O   1 
HETATM 15698 O O   . HOH   T 8 .   ? 36.438  -5.263  35.494  1.00 33.59  ?  708 HOH   D O   1 
HETATM 15699 O O   . HOH   T 8 .   ? 17.913  -12.175 37.589  1.00 23.10  ?  709 HOH   D O   1 
HETATM 15700 O O   . HOH   T 8 .   ? 26.436  -8.030  62.829  1.00 18.10  ?  710 HOH   D O   1 
HETATM 15701 O O   . HOH   T 8 .   ? 19.111  2.932   60.805  1.00 20.76  ?  711 HOH   D O   1 
HETATM 15702 O O   . HOH   T 8 .   ? 9.850   -19.673 61.891  1.00 18.50  ?  712 HOH   D O   1 
HETATM 15703 O O   . HOH   T 8 .   ? 44.829  -14.933 82.687  1.00 33.55  ?  713 HOH   D O   1 
HETATM 15704 O O   . HOH   T 8 .   ? 10.954  0.368   54.542  1.00 22.29  ?  714 HOH   D O   1 
HETATM 15705 O O   . HOH   T 8 .   ? 11.606  -2.178  66.628  1.00 20.25  ?  715 HOH   D O   1 
HETATM 15706 O O   . HOH   T 8 .   ? 44.675  -6.928  60.310  1.00 28.38  ?  716 HOH   D O   1 
HETATM 15707 O O   . HOH   T 8 .   ? 29.135  -9.176  59.448  1.00 16.21  ?  717 HOH   D O   1 
HETATM 15708 O O   . HOH   T 8 .   ? 1.338   -0.047  45.107  1.00 19.95  ?  718 HOH   D O   1 
HETATM 15709 O O   . HOH   T 8 .   ? 45.786  -13.660 44.968  1.00 31.36  ?  719 HOH   D O   1 
HETATM 15710 O O   . HOH   T 8 .   ? 35.244  -8.069  36.611  1.00 39.11  ?  720 HOH   D O   1 
HETATM 15711 O O   . HOH   T 8 .   ? 6.352   -8.210  70.857  1.00 16.99  ?  721 HOH   D O   1 
HETATM 15712 O O   . HOH   T 8 .   ? 49.026  -20.915 69.485  1.00 34.43  ?  722 HOH   D O   1 
HETATM 15713 O O   . HOH   T 8 .   ? 5.113   -4.779  74.152  1.00 18.84  ?  723 HOH   D O   1 
HETATM 15714 O O   . HOH   T 8 .   ? 22.262  -6.739  39.197  1.00 24.47  ?  724 HOH   D O   1 
HETATM 15715 O O   . HOH   T 8 .   ? 45.478  -10.157 46.923  1.00 31.93  ?  725 HOH   D O   1 
HETATM 15716 O O   . HOH   T 8 .   ? 44.681  7.421   38.917  1.00 50.87  ?  726 HOH   D O   1 
HETATM 15717 O O   . HOH   T 8 .   ? 15.959  -23.791 73.769  1.00 26.66  ?  727 HOH   D O   1 
HETATM 15718 O O   . HOH   T 8 .   ? 4.841   2.229   67.188  1.00 15.38  ?  728 HOH   D O   1 
HETATM 15719 O O   . HOH   T 8 .   ? 13.791  -0.784  67.786  1.00 18.36  ?  729 HOH   D O   1 
HETATM 15720 O O   . HOH   T 8 .   ? 21.140  0.225   75.489  1.00 23.96  ?  730 HOH   D O   1 
HETATM 15721 O O   . HOH   T 8 .   ? 12.817  -24.155 67.853  1.00 24.15  ?  731 HOH   D O   1 
HETATM 15722 O O   . HOH   T 8 .   ? 3.913   -4.471  41.047  1.00 22.67  ?  732 HOH   D O   1 
HETATM 15723 O O   . HOH   T 8 .   ? 34.356  -16.157 76.859  1.00 19.35  ?  733 HOH   D O   1 
HETATM 15724 O O   . HOH   T 8 .   ? 39.059  -21.778 47.078  1.00 35.99  ?  734 HOH   D O   1 
HETATM 15725 O O   . HOH   T 8 .   ? 17.868  -27.626 62.781  1.00 29.39  ?  735 HOH   D O   1 
HETATM 15726 O O   . HOH   T 8 .   ? 40.533  4.554   57.710  1.00 53.97  ?  736 HOH   D O   1 
HETATM 15727 O O   . HOH   T 8 .   ? 30.500  -22.824 74.631  1.00 30.98  ?  737 HOH   D O   1 
HETATM 15728 O O   . HOH   T 8 .   ? 20.442  -21.971 46.821  1.00 25.78  ?  738 HOH   D O   1 
HETATM 15729 O O   . HOH   T 8 .   ? 19.038  -21.811 50.006  1.00 25.53  ?  739 HOH   D O   1 
HETATM 15730 O O   . HOH   T 8 .   ? 45.084  -5.238  65.345  1.00 19.83  ?  740 HOH   D O   1 
HETATM 15731 O O   . HOH   T 8 .   ? 47.487  -21.083 75.366  1.00 26.61  ?  741 HOH   D O   1 
HETATM 15732 O O   . HOH   T 8 .   ? 48.343  -9.938  46.774  1.00 36.33  ?  742 HOH   D O   1 
HETATM 15733 O O   . HOH   T 8 .   ? 23.224  20.912  55.701  1.00 47.69  ?  743 HOH   D O   1 
HETATM 15734 O O   . HOH   T 8 .   ? 43.484  -1.568  57.866  1.00 44.69  ?  744 HOH   D O   1 
HETATM 15735 O O   . HOH   T 8 .   ? 22.562  -7.518  84.311  1.00 29.81  ?  745 HOH   D O   1 
HETATM 15736 O O   . HOH   T 8 .   ? 40.111  -12.169 86.404  1.00 32.42  ?  746 HOH   D O   1 
HETATM 15737 O O   . HOH   T 8 .   ? 36.134  1.335   66.691  1.00 24.54  ?  747 HOH   D O   1 
HETATM 15738 O O   B HOH   T 8 .   ? 43.914  -2.238  50.684  1.00 49.03  ?  748 HOH   D O   1 
HETATM 15739 O O   . HOH   T 8 .   ? 46.798  -8.331  59.321  1.00 28.27  ?  749 HOH   D O   1 
HETATM 15740 O O   . HOH   T 8 .   ? 24.791  -10.719 82.885  1.00 19.59  ?  750 HOH   D O   1 
HETATM 15741 O O   . HOH   T 8 .   ? 25.119  -27.323 63.153  1.00 30.28  ?  751 HOH   D O   1 
HETATM 15742 O O   . HOH   T 8 .   ? 40.865  -1.389  76.273  1.00 34.78  ?  752 HOH   D O   1 
HETATM 15743 O O   . HOH   T 8 .   ? -0.528  -14.264 62.345  1.00 33.51  ?  753 HOH   D O   1 
HETATM 15744 O O   . HOH   T 8 .   ? 24.286  -14.093 87.368  1.00 24.62  ?  754 HOH   D O   1 
HETATM 15745 O O   . HOH   T 8 .   ? 16.616  3.743   51.036  1.00 24.65  ?  755 HOH   D O   1 
HETATM 15746 O O   . HOH   T 8 .   ? 17.843  -19.028 80.948  1.00 30.73  ?  756 HOH   D O   1 
HETATM 15747 O O   . HOH   T 8 .   ? 23.130  -24.270 41.895  1.00 35.99  ?  757 HOH   D O   1 
HETATM 15748 O O   . HOH   T 8 .   ? 21.774  4.369   32.673  1.00 27.28  ?  758 HOH   D O   1 
HETATM 15749 O O   . HOH   T 8 .   ? 46.615  -19.716 78.684  1.00 35.84  ?  759 HOH   D O   1 
HETATM 15750 O O   . HOH   T 8 .   ? 16.095  -26.095 69.765  1.00 29.96  ?  760 HOH   D O   1 
HETATM 15751 O O   . HOH   T 8 .   ? 30.493  -20.753 40.378  1.00 39.15  ?  761 HOH   D O   1 
HETATM 15752 O O   . HOH   T 8 .   ? 15.659  -18.854 72.946  1.00 19.49  ?  762 HOH   D O   1 
HETATM 15753 O O   . HOH   T 8 .   ? 38.952  -2.787  64.588  1.00 22.62  ?  763 HOH   D O   1 
HETATM 15754 O O   . HOH   T 8 .   ? 40.038  -26.378 56.963  1.00 30.02  ?  764 HOH   D O   1 
HETATM 15755 O O   . HOH   T 8 .   ? 42.008  -7.771  84.654  1.00 26.75  ?  765 HOH   D O   1 
HETATM 15756 O O   . HOH   T 8 .   ? 48.846  -11.552 78.354  1.00 23.03  ?  766 HOH   D O   1 
HETATM 15757 O O   . HOH   T 8 .   ? 29.174  20.062  64.023  1.00 61.07  ?  767 HOH   D O   1 
HETATM 15758 O O   . HOH   T 8 .   ? 22.647  5.025   53.390  1.00 21.93  ?  768 HOH   D O   1 
HETATM 15759 O O   . HOH   T 8 .   ? 25.287  -29.367 51.252  1.00 46.23  ?  769 HOH   D O   1 
HETATM 15760 O O   . HOH   T 8 .   ? 43.918  -8.916  39.447  1.00 37.12  ?  770 HOH   D O   1 
HETATM 15761 O O   . HOH   T 8 .   ? 26.790  -12.073 41.159  1.00 31.26  ?  771 HOH   D O   1 
HETATM 15762 O O   . HOH   T 8 .   ? 47.359  -13.546 82.117  1.00 31.61  ?  772 HOH   D O   1 
HETATM 15763 O O   . HOH   T 8 .   ? 30.759  8.745   32.209  1.00 38.00  ?  773 HOH   D O   1 
HETATM 15764 O O   . HOH   T 8 .   ? 34.349  -8.157  41.151  1.00 25.89  ?  774 HOH   D O   1 
HETATM 15765 O O   . HOH   T 8 .   ? 48.282  -13.644 55.110  1.00 33.68  ?  775 HOH   D O   1 
HETATM 15766 O O   . HOH   T 8 .   ? 29.343  -23.781 72.455  1.00 25.98  ?  776 HOH   D O   1 
HETATM 15767 O O   . HOH   T 8 .   ? 54.208  -14.060 76.005  1.00 39.80  ?  777 HOH   D O   1 
HETATM 15768 O O   . HOH   T 8 .   ? 15.120  -23.444 69.177  1.00 22.57  ?  778 HOH   D O   1 
HETATM 15769 O O   . HOH   T 8 .   ? 46.464  -0.718  47.813  1.00 49.11  ?  779 HOH   D O   1 
HETATM 15770 O O   . HOH   T 8 .   ? 25.458  -7.214  82.885  1.00 22.19  ?  780 HOH   D O   1 
HETATM 15771 O O   . HOH   T 8 .   ? 18.182  -26.369 51.335  1.00 40.33  ?  781 HOH   D O   1 
HETATM 15772 O O   . HOH   T 8 .   ? 36.454  -13.516 88.987  1.00 47.92  ?  782 HOH   D O   1 
HETATM 15773 O O   . HOH   T 8 .   ? 26.675  -1.422  30.667  1.00 28.66  ?  783 HOH   D O   1 
HETATM 15774 O O   . HOH   T 8 .   ? 26.586  -7.471  65.707  1.00 18.20  ?  784 HOH   D O   1 
HETATM 15775 O O   . HOH   T 8 .   ? 2.243   -13.898 47.169  1.00 30.66  ?  785 HOH   D O   1 
HETATM 15776 O O   . HOH   T 8 .   ? 32.354  -13.570 42.474  1.00 25.41  ?  786 HOH   D O   1 
HETATM 15777 O O   . HOH   T 8 .   ? 18.935  -13.163 55.474  1.00 17.20  ?  787 HOH   D O   1 
HETATM 15778 O O   . HOH   T 8 .   ? 11.101  -17.935 76.873  1.00 28.78  ?  788 HOH   D O   1 
HETATM 15779 O O   . HOH   T 8 .   ? 51.261  -11.331 76.884  1.00 29.70  ?  789 HOH   D O   1 
HETATM 15780 O O   . HOH   T 8 .   ? 22.159  -27.305 74.582  1.00 36.36  ?  790 HOH   D O   1 
HETATM 15781 O O   . HOH   T 8 .   ? 32.791  -10.467 42.662  1.00 31.68  ?  791 HOH   D O   1 
HETATM 15782 O O   . HOH   T 8 .   ? 25.809  -3.550  30.342  1.00 26.51  ?  792 HOH   D O   1 
HETATM 15783 O O   . HOH   T 8 .   ? 23.813  -9.168  30.701  1.00 37.80  ?  793 HOH   D O   1 
HETATM 15784 O O   . HOH   T 8 .   ? 4.276   -18.998 67.157  1.00 27.70  ?  794 HOH   D O   1 
HETATM 15785 O O   . HOH   T 8 .   ? 45.103  -12.896 40.727  1.00 43.42  ?  795 HOH   D O   1 
HETATM 15786 O O   . HOH   T 8 .   ? 25.903  11.267  36.353  1.00 36.05  ?  796 HOH   D O   1 
HETATM 15787 O O   . HOH   T 8 .   ? 14.971  -20.990 74.965  1.00 25.41  ?  797 HOH   D O   1 
HETATM 15788 O O   . HOH   T 8 .   ? 18.051  26.211  42.616  1.00 53.24  ?  798 HOH   D O   1 
HETATM 15789 O O   . HOH   T 8 .   ? 32.380  3.354   66.933  1.00 34.66  ?  799 HOH   D O   1 
HETATM 15790 O O   . HOH   T 8 .   ? 21.805  7.114   34.226  1.00 29.38  ?  800 HOH   D O   1 
HETATM 15791 O O   . HOH   T 8 .   ? 0.491   -6.683  39.083  1.00 16.53  ?  801 HOH   D O   1 
HETATM 15792 O O   . HOH   T 8 .   ? 38.480  -22.755 49.931  1.00 34.45  ?  802 HOH   D O   1 
HETATM 15793 O O   . HOH   T 8 .   ? 42.041  -19.365 46.088  1.00 31.41  ?  803 HOH   D O   1 
HETATM 15794 O O   . HOH   T 8 .   ? 28.920  -16.228 40.509  1.00 41.44  ?  804 HOH   D O   1 
HETATM 15795 O O   . HOH   T 8 .   ? 30.816  -7.922  31.054  1.00 27.27  ?  805 HOH   D O   1 
HETATM 15796 O O   . HOH   T 8 .   ? -0.365  -6.638  71.861  1.00 19.05  ?  806 HOH   D O   1 
HETATM 15797 O O   . HOH   T 8 .   ? 18.696  6.378   52.395  1.00 19.52  ?  807 HOH   D O   1 
HETATM 15798 O O   . HOH   T 8 .   ? 52.974  -19.441 66.647  1.00 28.06  ?  808 HOH   D O   1 
HETATM 15799 O O   . HOH   T 8 .   ? 33.457  -8.419  84.025  1.00 29.31  ?  809 HOH   D O   1 
HETATM 15800 O O   . HOH   T 8 .   ? 26.768  -18.685 41.862  1.00 32.64  ?  810 HOH   D O   1 
HETATM 15801 O O   . HOH   T 8 .   ? 36.311  2.729   75.508  1.00 30.91  ?  811 HOH   D O   1 
HETATM 15802 O O   . HOH   T 8 .   ? 5.964   -16.441 51.286  1.00 37.49  ?  812 HOH   D O   1 
HETATM 15803 O O   . HOH   T 8 .   ? 10.885  -11.909 47.560  1.00 35.87  ?  813 HOH   D O   1 
HETATM 15804 O O   . HOH   T 8 .   ? 21.381  -26.056 44.140  1.00 44.08  ?  814 HOH   D O   1 
HETATM 15805 O O   . HOH   T 8 .   ? 9.033   -14.204 48.893  1.00 38.27  ?  815 HOH   D O   1 
HETATM 15806 O O   . HOH   T 8 .   ? 22.831  -6.233  29.890  1.00 34.36  ?  816 HOH   D O   1 
HETATM 15807 O O   . HOH   T 8 .   ? 29.749  -1.357  78.128  1.00 25.51  ?  817 HOH   D O   1 
HETATM 15808 O O   . HOH   T 8 .   ? 14.386  17.409  56.590  1.00 26.90  ?  818 HOH   D O   1 
HETATM 15809 O O   . HOH   T 8 .   ? 12.634  2.480   52.942  1.00 27.80  ?  819 HOH   D O   1 
HETATM 15810 O O   A HOH   T 8 .   ? 16.663  -13.519 82.668  1.00 33.02  ?  820 HOH   D O   1 
HETATM 15811 O O   . HOH   T 8 .   ? 46.024  -23.787 75.301  1.00 27.68  ?  821 HOH   D O   1 
HETATM 15812 O O   . HOH   T 8 .   ? 35.091  -18.761 76.983  1.00 19.33  ?  822 HOH   D O   1 
HETATM 15813 O O   . HOH   T 8 .   ? 42.288  -3.670  54.387  1.00 39.82  ?  823 HOH   D O   1 
HETATM 15814 O O   . HOH   T 8 .   ? 35.757  0.164   56.930  1.00 38.75  ?  824 HOH   D O   1 
HETATM 15815 O O   . HOH   T 8 .   ? 4.186   -13.339 60.078  1.00 17.55  ?  825 HOH   D O   1 
HETATM 15816 O O   . HOH   T 8 .   ? 36.179  7.564   70.594  1.00 49.90  ?  826 HOH   D O   1 
HETATM 15817 O O   . HOH   T 8 .   ? 24.060  10.850  34.263  1.00 29.63  ?  827 HOH   D O   1 
HETATM 15818 O O   . HOH   T 8 .   ? 32.897  3.734   72.809  1.00 34.65  ?  828 HOH   D O   1 
HETATM 15819 O O   . HOH   T 8 .   ? 5.602   -21.400 68.607  1.00 36.15  ?  829 HOH   D O   1 
HETATM 15820 O O   . HOH   T 8 .   ? 30.482  -14.296 41.408  1.00 37.91  ?  830 HOH   D O   1 
HETATM 15821 O O   . HOH   T 8 .   ? 27.500  -11.805 83.084  1.00 21.97  ?  831 HOH   D O   1 
HETATM 15822 O O   . HOH   T 8 .   ? 9.423   -19.247 59.539  1.00 26.97  ?  832 HOH   D O   1 
HETATM 15823 O O   . HOH   T 8 .   ? 44.340  1.925   68.427  1.00 58.80  ?  833 HOH   D O   1 
HETATM 15824 O O   . HOH   T 8 .   ? 34.515  6.012   69.747  1.00 53.56  ?  834 HOH   D O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1     N N   . ALA A 2   ? 0.2909 0.5353 0.3228 0.0235  0.0649  -0.0079 2   ALA A N   
2     C CA  . ALA A 2   ? 0.2909 0.5217 0.3247 0.0240  0.0627  -0.0046 2   ALA A CA  
3     C C   . ALA A 2   ? 0.3377 0.5599 0.3601 0.0212  0.0611  -0.0031 2   ALA A C   
4     O O   . ALA A 2   ? 0.3135 0.5386 0.3309 0.0227  0.0616  -0.0092 2   ALA A O   
5     C CB  . ALA A 2   ? 0.2467 0.4733 0.2929 0.0320  0.0633  -0.0121 2   ALA A CB  
6     N N   . LYS A 3   ? 0.2634 0.4753 0.2819 0.0172  0.0588  0.0049  3   LYS A N   
7     C CA  . LYS A 3   ? 0.2675 0.4709 0.2745 0.0139  0.0568  0.0084  3   LYS A CA  
8     C C   . LYS A 3   ? 0.2664 0.4582 0.2760 0.0166  0.0554  0.0072  3   LYS A C   
9     O O   . LYS A 3   ? 0.2595 0.4410 0.2735 0.0154  0.0531  0.0120  3   LYS A O   
10    C CB  . LYS A 3   ? 0.3103 0.5096 0.3094 0.0063  0.0551  0.0190  3   LYS A CB  
11    C CG  . LYS A 3   ? 0.3514 0.5399 0.3390 0.0032  0.0527  0.0237  3   LYS A CG  
12    C CD  . LYS A 3   ? 0.4146 0.5997 0.3952 -0.0037 0.0515  0.0326  3   LYS A CD  
13    C CE  . LYS A 3   ? 0.6150 0.7872 0.5856 -0.0060 0.0486  0.0378  3   LYS A CE  
14    N NZ  . LYS A 3   ? 0.7477 0.9138 0.7129 -0.0125 0.0477  0.0459  3   LYS A NZ  
15    N N   . ARG A 4   ? 0.2630 0.4516 0.2696 0.0195  0.0548  0.0004  4   ARG A N   
16    C CA  A ARG A 4   ? 0.2270 0.3983 0.2347 0.0208  0.0512  -0.0010 4   ARG A CA  
17    C CA  B ARG A 4   ? 0.2280 0.3994 0.2358 0.0208  0.0512  -0.0010 4   ARG A CA  
18    C C   . ARG A 4   ? 0.2797 0.4416 0.2766 0.0161  0.0482  0.0070  4   ARG A C   
19    O O   . ARG A 4   ? 0.2556 0.4237 0.2425 0.0141  0.0486  0.0088  4   ARG A O   
20    C CB  A ARG A 4   ? 0.2577 0.4302 0.2673 0.0254  0.0517  -0.0123 4   ARG A CB  
21    C CB  B ARG A 4   ? 0.2579 0.4302 0.2674 0.0254  0.0517  -0.0122 4   ARG A CB  
22    C CG  A ARG A 4   ? 0.2635 0.4412 0.2851 0.0309  0.0544  -0.0212 4   ARG A CG  
23    C CG  B ARG A 4   ? 0.2629 0.4420 0.2838 0.0309  0.0547  -0.0214 4   ARG A CG  
24    C CD  A ARG A 4   ? 0.2753 0.4580 0.2969 0.0344  0.0559  -0.0333 4   ARG A CD  
25    C CD  B ARG A 4   ? 0.2736 0.4495 0.2969 0.0345  0.0547  -0.0329 4   ARG A CD  
26    N NE  A ARG A 4   ? 0.2775 0.4548 0.3119 0.0398  0.0570  -0.0421 4   ARG A NE  
27    N NE  B ARG A 4   ? 0.2779 0.4662 0.2917 0.0337  0.0559  -0.0376 4   ARG A NE  
28    C CZ  A ARG A 4   ? 0.2415 0.4036 0.2804 0.0410  0.0549  -0.0457 4   ARG A CZ  
29    C CZ  B ARG A 4   ? 0.2743 0.4707 0.2895 0.0358  0.0574  -0.0462 4   ARG A CZ  
30    N NH1 A ARG A 4   ? 0.2699 0.4220 0.3021 0.0374  0.0515  -0.0420 4   ARG A NH1 
31    N NH1 B ARG A 4   ? 0.2450 0.4421 0.2713 0.0400  0.0597  -0.0524 4   ARG A NH1 
32    N NH2 A ARG A 4   ? 0.2451 0.4020 0.2958 0.0459  0.0563  -0.0532 4   ARG A NH2 
33    N NH2 B ARG A 4   ? 0.2580 0.4618 0.2634 0.0337  0.0565  -0.0482 4   ARG A NH2 
34    N N   . ILE A 5   ? 0.2221 0.3695 0.2211 0.0145  0.0452  0.0118  5   ILE A N   
35    C CA  . ILE A 5   ? 0.2384 0.3750 0.2286 0.0106  0.0422  0.0189  5   ILE A CA  
36    C C   . ILE A 5   ? 0.2516 0.3764 0.2427 0.0130  0.0394  0.0147  5   ILE A C   
37    O O   . ILE A 5   ? 0.2667 0.3851 0.2666 0.0153  0.0388  0.0111  5   ILE A O   
38    C CB  . ILE A 5   ? 0.2026 0.3329 0.1938 0.0063  0.0412  0.0274  5   ILE A CB  
39    C CG1 . ILE A 5   ? 0.2797 0.4220 0.2678 0.0024  0.0439  0.0324  5   ILE A CG1 
40    C CG2 . ILE A 5   ? 0.2445 0.3607 0.2289 0.0035  0.0379  0.0326  5   ILE A CG2 
41    C CD1 . ILE A 5   ? 0.2876 0.4268 0.2785 -0.0022 0.0434  0.0392  5   ILE A CD1 
42    N N   . VAL A 6   ? 0.1808 0.3034 0.1631 0.0124  0.0377  0.0156  6   VAL A N   
43    C CA  . VAL A 6   ? 0.2415 0.3565 0.2243 0.0145  0.0352  0.0106  6   VAL A CA  
44    C C   . VAL A 6   ? 0.2462 0.3463 0.2302 0.0127  0.0324  0.0154  6   VAL A C   
45    O O   . VAL A 6   ? 0.2101 0.3054 0.1906 0.0094  0.0317  0.0233  6   VAL A O   
46    C CB  . VAL A 6   ? 0.2862 0.4072 0.2590 0.0150  0.0344  0.0097  6   VAL A CB  
47    C CG1 . VAL A 6   ? 0.2548 0.3723 0.2178 0.0119  0.0331  0.0199  6   VAL A CG1 
48    C CG2 . VAL A 6   ? 0.2361 0.3527 0.2103 0.0173  0.0321  0.0031  6   VAL A CG2 
49    N N   . GLU A 7   ? 0.2423 0.3355 0.2316 0.0145  0.0310  0.0102  7   GLU A N   
50    C CA  . GLU A 7   ? 0.2330 0.3134 0.2240 0.0130  0.0286  0.0137  7   GLU A CA  
51    C C   . GLU A 7   ? 0.2804 0.3561 0.2622 0.0113  0.0262  0.0189  7   GLU A C   
52    O O   . GLU A 7   ? 0.3167 0.3967 0.2928 0.0128  0.0254  0.0168  7   GLU A O   
53    C CB  . GLU A 7   ? 0.2228 0.2982 0.2206 0.0150  0.0279  0.0067  7   GLU A CB  
54    C CG  . GLU A 7   ? 0.2174 0.2926 0.2257 0.0169  0.0298  0.0026  7   GLU A CG  
55    C CD  . GLU A 7   ? 0.2662 0.3525 0.2769 0.0197  0.0326  -0.0042 7   GLU A CD  
56    O OE1 . GLU A 7   ? 0.2644 0.3593 0.2683 0.0200  0.0329  -0.0069 7   GLU A OE1 
57    O OE2 . GLU A 7   ? 0.2735 0.3603 0.2929 0.0219  0.0344  -0.0070 7   GLU A OE2 
58    N N   . PRO A 8   ? 0.2211 0.2883 0.2014 0.0086  0.0250  0.0255  8   PRO A N   
59    C CA  . PRO A 8   ? 0.2303 0.2910 0.2032 0.0078  0.0227  0.0296  8   PRO A CA  
60    C C   . PRO A 8   ? 0.2367 0.2904 0.2126 0.0090  0.0206  0.0262  8   PRO A C   
61    O O   . PRO A 8   ? 0.2504 0.2961 0.2237 0.0079  0.0188  0.0296  8   PRO A O   
62    C CB  . PRO A 8   ? 0.2565 0.3116 0.2273 0.0039  0.0228  0.0370  8   PRO A CB  
63    C CG  . PRO A 8   ? 0.2162 0.2717 0.1957 0.0031  0.0238  0.0359  8   PRO A CG  
64    C CD  . PRO A 8   ? 0.2347 0.2993 0.2194 0.0061  0.0257  0.0297  8   PRO A CD  
65    N N   . PHE A 9   ? 0.2178 0.2749 0.1995 0.0110  0.0210  0.0190  9   PHE A N   
66    C CA  . PHE A 9   ? 0.2300 0.2821 0.2156 0.0115  0.0195  0.0150  9   PHE A CA  
67    C C   . PHE A 9   ? 0.1884 0.2470 0.1780 0.0136  0.0204  0.0064  9   PHE A C   
68    O O   . PHE A 9   ? 0.2434 0.3099 0.2332 0.0148  0.0222  0.0035  9   PHE A O   
69    C CB  . PHE A 9   ? 0.1733 0.2174 0.1654 0.0097  0.0196  0.0168  9   PHE A CB  
70    C CG  . PHE A 9   ? 0.1928 0.2390 0.1919 0.0099  0.0218  0.0159  9   PHE A CG  
71    C CD1 . PHE A 9   ? 0.1489 0.1964 0.1551 0.0117  0.0230  0.0092  9   PHE A CD1 
72    C CD2 . PHE A 9   ? 0.1677 0.2146 0.1666 0.0084  0.0225  0.0214  9   PHE A CD2 
73    C CE1 . PHE A 9   ? 0.2335 0.2825 0.2467 0.0129  0.0249  0.0084  9   PHE A CE1 
74    C CE2 . PHE A 9   ? 0.1960 0.2461 0.2018 0.0094  0.0243  0.0207  9   PHE A CE2 
75    C CZ  . PHE A 9   ? 0.1844 0.2353 0.1976 0.0121  0.0255  0.0143  9   PHE A CZ  
76    N N   . ARG A 10  ? 0.2151 0.2710 0.2083 0.0136  0.0192  0.0018  10  ARG A N   
77    C CA  . ARG A 10  ? 0.2180 0.2782 0.2169 0.0145  0.0202  -0.0072 10  ARG A CA  
78    C C   . ARG A 10  ? 0.2137 0.2654 0.2213 0.0129  0.0206  -0.0091 10  ARG A C   
79    O O   . ARG A 10  ? 0.1753 0.2196 0.1833 0.0113  0.0198  -0.0037 10  ARG A O   
80    C CB  . ARG A 10  ? 0.2344 0.3026 0.2290 0.0157  0.0186  -0.0124 10  ARG A CB  
81    C CG  . ARG A 10  ? 0.2290 0.2940 0.2212 0.0153  0.0160  -0.0103 10  ARG A CG  
82    C CD  . ARG A 10  ? 0.3059 0.3811 0.2928 0.0173  0.0140  -0.0139 10  ARG A CD  
83    N NE  . ARG A 10  ? 0.3529 0.4255 0.3380 0.0177  0.0115  -0.0116 10  ARG A NE  
84    C CZ  . ARG A 10  ? 0.3587 0.4378 0.3373 0.0203  0.0091  -0.0103 10  ARG A CZ  
85    N NH1 . ARG A 10  ? 0.3264 0.4152 0.2988 0.0225  0.0086  -0.0106 10  ARG A NH1 
86    N NH2 . ARG A 10  ? 0.3790 0.4554 0.3573 0.0211  0.0070  -0.0085 10  ARG A NH2 
87    N N   . ILE A 11  ? 0.1981 0.2508 0.2125 0.0132  0.0220  -0.0169 11  ILE A N   
88    C CA  . ILE A 11  ? 0.1524 0.1961 0.1755 0.0116  0.0229  -0.0182 11  ILE A CA  
89    C C   . ILE A 11  ? 0.2167 0.2588 0.2404 0.0093  0.0213  -0.0208 11  ILE A C   
90    O O   . ILE A 11  ? 0.1990 0.2484 0.2206 0.0095  0.0204  -0.0268 11  ILE A O   
91    C CB  . ILE A 11  ? 0.1903 0.2342 0.2211 0.0129  0.0253  -0.0257 11  ILE A CB  
92    C CG1 . ILE A 11  ? 0.1533 0.2011 0.1837 0.0156  0.0270  -0.0234 11  ILE A CG1 
93    C CG2 . ILE A 11  ? 0.1548 0.1879 0.1949 0.0112  0.0263  -0.0263 11  ILE A CG2 
94    C CD1 . ILE A 11  ? 0.1826 0.2335 0.2194 0.0179  0.0296  -0.0321 11  ILE A CD1 
95    N N   . LYS A 12  ? 0.1936 0.2275 0.2201 0.0071  0.0210  -0.0162 12  LYS A N   
96    C CA  . LYS A 12  ? 0.1764 0.2091 0.2047 0.0044  0.0200  -0.0185 12  LYS A CA  
97    C C   . LYS A 12  ? 0.2046 0.2298 0.2421 0.0017  0.0217  -0.0212 12  LYS A C   
98    O O   . LYS A 12  ? 0.2208 0.2469 0.2613 -0.0010 0.0216  -0.0260 12  LYS A O   
99    C CB  . LYS A 12  ? 0.2053 0.2359 0.2285 0.0036  0.0183  -0.0115 12  LYS A CB  
100   C CG  . LYS A 12  ? 0.2472 0.2805 0.2708 0.0017  0.0171  -0.0146 12  LYS A CG  
101   C CD  . LYS A 12  ? 0.2973 0.3308 0.3145 0.0024  0.0153  -0.0091 12  LYS A CD  
102   C CE  . LYS A 12  ? 0.3007 0.3384 0.3190 0.0011  0.0142  -0.0124 12  LYS A CE  
103   N NZ  . LYS A 12  ? 0.2750 0.3148 0.2863 0.0037  0.0122  -0.0087 12  LYS A NZ  
104   N N   . MET A 13  ? 0.1551 0.1732 0.1974 0.0022  0.0234  -0.0179 13  MET A N   
105   C CA  . MET A 13  ? 0.1704 0.1800 0.2216 0.0000  0.0251  -0.0198 13  MET A CA  
106   C C   . MET A 13  ? 0.1589 0.1642 0.2155 0.0030  0.0270  -0.0198 13  MET A C   
107   O O   . MET A 13  ? 0.1633 0.1701 0.2171 0.0057  0.0268  -0.0143 13  MET A O   
108   C CB  . MET A 13  ? 0.1576 0.1608 0.2097 -0.0031 0.0247  -0.0125 13  MET A CB  
109   C CG  . MET A 13  ? 0.1982 0.1922 0.2592 -0.0062 0.0266  -0.0135 13  MET A CG  
110   S SD  . MET A 13  ? 0.3198 0.3074 0.3808 -0.0094 0.0264  -0.0030 13  MET A SD  
111   C CE  . MET A 13  ? 0.1630 0.1598 0.2160 -0.0113 0.0243  -0.0036 13  MET A CE  
112   N N   . VAL A 14  ? 0.1864 0.1864 0.2509 0.0024  0.0289  -0.0264 14  VAL A N   
113   C CA  . VAL A 14  ? 0.1845 0.1805 0.2552 0.0061  0.0310  -0.0279 14  VAL A CA  
114   C C   . VAL A 14  ? 0.1461 0.1289 0.2254 0.0050  0.0323  -0.0241 14  VAL A C   
115   O O   . VAL A 14  ? 0.1871 0.1643 0.2682 0.0006  0.0322  -0.0225 14  VAL A O   
116   C CB  . VAL A 14  ? 0.1792 0.1801 0.2523 0.0075  0.0324  -0.0399 14  VAL A CB  
117   C CG1 . VAL A 14  ? 0.1925 0.2072 0.2562 0.0086  0.0309  -0.0424 14  VAL A CG1 
118   C CG2 . VAL A 14  ? 0.1559 0.1521 0.2346 0.0032  0.0332  -0.0479 14  VAL A CG2 
119   N N   . GLU A 15  ? 0.1992 0.1775 0.2839 0.0093  0.0337  -0.0223 15  GLU A N   
120   C CA  . GLU A 15  ? 0.2074 0.1728 0.3006 0.0097  0.0350  -0.0177 15  GLU A CA  
121   C C   . GLU A 15  ? 0.2167 0.1776 0.3183 0.0142  0.0374  -0.0247 15  GLU A C   
122   O O   . GLU A 15  ? 0.2234 0.1920 0.3240 0.0190  0.0378  -0.0268 15  GLU A O   
123   C CB  . GLU A 15  ? 0.2655 0.2305 0.3566 0.0114  0.0335  -0.0052 15  GLU A CB  
124   C CG  . GLU A 15  ? 0.2978 0.2513 0.3975 0.0136  0.0346  0.0008  15  GLU A CG  
125   C CD  . GLU A 15  ? 0.3118 0.2680 0.4090 0.0157  0.0328  0.0126  15  GLU A CD  
126   O OE1 . GLU A 15  ? 0.3139 0.2804 0.4067 0.0184  0.0318  0.0139  15  GLU A OE1 
127   O OE2 . GLU A 15  ? 0.4064 0.3551 0.5061 0.0143  0.0325  0.0208  15  GLU A OE2 
128   N N   . LYS A 16  ? 0.2664 0.2148 0.3765 0.0126  0.0394  -0.0285 16  LYS A N   
129   C CA  . LYS A 16  ? 0.2619 0.2042 0.3809 0.0168  0.0420  -0.0365 16  LYS A CA  
130   C C   . LYS A 16  ? 0.3257 0.2650 0.4494 0.0238  0.0424  -0.0292 16  LYS A C   
131   O O   . LYS A 16  ? 0.3102 0.2444 0.4344 0.0241  0.0412  -0.0175 16  LYS A O   
132   C CB  . LYS A 16  ? 0.3709 0.2982 0.4983 0.0128  0.0440  -0.0411 16  LYS A CB  
133   C CG  . LYS A 16  ? 0.4128 0.3302 0.5508 0.0171  0.0470  -0.0494 16  LYS A CG  
134   C CD  . LYS A 16  ? 0.4794 0.4033 0.6176 0.0155  0.0484  -0.0655 16  LYS A CD  
135   C CE  . LYS A 16  ? 0.6019 0.5117 0.7519 0.0174  0.0518  -0.0752 16  LYS A CE  
136   N NZ  . LYS A 16  ? 0.5869 0.4815 0.7429 0.0102  0.0531  -0.0775 16  LYS A NZ  
137   N N   . ILE A 17  ? 0.3093 0.2534 0.4364 0.0296  0.0440  -0.0363 17  ILE A N   
138   C CA  . ILE A 17  ? 0.3155 0.2565 0.4497 0.0371  0.0449  -0.0319 17  ILE A CA  
139   C C   . ILE A 17  ? 0.3612 0.2969 0.5045 0.0412  0.0481  -0.0443 17  ILE A C   
140   O O   . ILE A 17  ? 0.4100 0.3502 0.5516 0.0388  0.0493  -0.0564 17  ILE A O   
141   C CB  . ILE A 17  ? 0.3019 0.2588 0.4304 0.0410  0.0435  -0.0267 17  ILE A CB  
142   C CG1 . ILE A 17  ? 0.2955 0.2668 0.4183 0.0411  0.0443  -0.0371 17  ILE A CG1 
143   C CG2 . ILE A 17  ? 0.3340 0.2949 0.4541 0.0369  0.0404  -0.0149 17  ILE A CG2 
144   C CD1 . ILE A 17  ? 0.2860 0.2725 0.4040 0.0446  0.0436  -0.0328 17  ILE A CD1 
145   N N   . ARG A 18  ? 0.3951 0.3214 0.5484 0.0478  0.0495  -0.0414 18  ARG A N   
146   C CA  . ARG A 18  ? 0.3973 0.3163 0.5605 0.0526  0.0528  -0.0532 18  ARG A CA  
147   C C   . ARG A 18  ? 0.3931 0.3145 0.5635 0.0625  0.0537  -0.0498 18  ARG A C   
148   O O   . ARG A 18  ? 0.3928 0.3184 0.5618 0.0651  0.0516  -0.0372 18  ARG A O   
149   C CB  . ARG A 18  ? 0.4089 0.3069 0.5799 0.0492  0.0543  -0.0552 18  ARG A CB  
150   C CG  . ARG A 18  ? 0.4448 0.3302 0.6187 0.0501  0.0527  -0.0402 18  ARG A CG  
151   C CD  . ARG A 18  ? 0.5644 0.4320 0.7425 0.0459  0.0534  -0.0416 18  ARG A CD  
152   N NE  . ARG A 18  ? 0.5393 0.4018 0.7230 0.0508  0.0551  -0.0507 18  ARG A NE  
153   C CZ  . ARG A 18  ? 0.5465 0.4011 0.7354 0.0576  0.0548  -0.0449 18  ARG A CZ  
154   N NH1 . ARG A 18  ? 0.5349 0.3867 0.7237 0.0601  0.0527  -0.0298 18  ARG A NH1 
155   N NH2 . ARG A 18  ? 0.6268 0.4767 0.8207 0.0620  0.0566  -0.0545 18  ARG A NH2 
156   N N   . VAL A 19  ? 0.4009 0.3221 0.5755 0.0666  0.0556  -0.0605 19  VAL A N   
157   C CA  . VAL A 19  ? 0.3850 0.3104 0.5641 0.0756  0.0560  -0.0590 19  VAL A CA  
158   C C   . VAL A 19  ? 0.4322 0.3385 0.6183 0.0781  0.0560  -0.0567 19  VAL A C   
159   O O   . VAL A 19  ? 0.4335 0.3305 0.6218 0.0761  0.0576  -0.0669 19  VAL A O   
160   C CB  . VAL A 19  ? 0.3831 0.3235 0.5602 0.0787  0.0580  -0.0721 19  VAL A CB  
161   C CG1 . VAL A 19  ? 0.4155 0.3625 0.5974 0.0882  0.0584  -0.0699 19  VAL A CG1 
162   C CG2 . VAL A 19  ? 0.4033 0.3621 0.5723 0.0750  0.0580  -0.0744 19  VAL A CG2 
163   N N   . PRO A 20  ? 0.4432 0.3439 0.6326 0.0823  0.0541  -0.0436 20  PRO A N   
164   C CA  . PRO A 20  ? 0.4605 0.3438 0.6561 0.0857  0.0541  -0.0411 20  PRO A CA  
165   C C   . PRO A 20  ? 0.4507 0.3364 0.6512 0.0939  0.0559  -0.0506 20  PRO A C   
166   O O   . PRO A 20  ? 0.4478 0.3504 0.6477 0.0993  0.0564  -0.0534 20  PRO A O   
167   C CB  . PRO A 20  ? 0.4176 0.2997 0.6138 0.0887  0.0512  -0.0241 20  PRO A CB  
168   C CG  . PRO A 20  ? 0.4826 0.3777 0.6723 0.0841  0.0497  -0.0178 20  PRO A CG  
169   C CD  . PRO A 20  ? 0.3911 0.3011 0.5779 0.0835  0.0517  -0.0300 20  PRO A CD  
170   N N   . SER A 21  ? 0.4812 0.3502 0.6866 0.0945  0.0572  -0.0555 21  SER A N   
171   C CA  . SER A 21  ? 0.4711 0.3401 0.6815 0.1026  0.0591  -0.0645 21  SER A CA  
172   C C   . SER A 21  ? 0.4819 0.3552 0.6962 0.1129  0.0575  -0.0549 21  SER A C   
173   O O   . SER A 21  ? 0.4781 0.3495 0.6922 0.1134  0.0548  -0.0407 21  SER A O   
174   C CB  . SER A 21  ? 0.4712 0.3194 0.6863 0.1009  0.0607  -0.0708 21  SER A CB  
175   O OG  . SER A 21  ? 0.4739 0.3053 0.6923 0.1019  0.0590  -0.0583 21  SER A OG  
176   N N   . ARG A 22  ? 0.4540 0.3344 0.6717 0.1212  0.0593  -0.0631 22  ARG A N   
177   C CA  . ARG A 22  ? 0.4494 0.3361 0.6716 0.1319  0.0580  -0.0557 22  ARG A CA  
178   C C   . ARG A 22  ? 0.4689 0.3362 0.6959 0.1351  0.0560  -0.0451 22  ARG A C   
179   O O   . ARG A 22  ? 0.5118 0.3836 0.7402 0.1403  0.0531  -0.0329 22  ARG A O   
180   C CB  . ARG A 22  ? 0.4335 0.3293 0.6587 0.1400  0.0609  -0.0679 22  ARG A CB  
181   C CG  . ARG A 22  ? 0.5259 0.4286 0.7567 0.1520  0.0599  -0.0621 22  ARG A CG  
182   C CD  . ARG A 22  ? 0.5674 0.4888 0.7958 0.1528  0.0569  -0.0506 22  ARG A CD  
183   N NE  . ARG A 22  ? 0.6066 0.5403 0.8401 0.1641  0.0561  -0.0475 22  ARG A NE  
184   C CZ  . ARG A 22  ? 0.5787 0.5351 0.8118 0.1683  0.0578  -0.0529 22  ARG A CZ  
185   N NH1 . ARG A 22  ? 0.5591 0.5284 0.7863 0.1623  0.0605  -0.0612 22  ARG A NH1 
186   N NH2 . ARG A 22  ? 0.5048 0.4722 0.7434 0.1787  0.0569  -0.0496 22  ARG A NH2 
187   N N   . GLU A 23  ? 0.5083 0.3544 0.7376 0.1318  0.0573  -0.0493 23  GLU A N   
188   C CA  . GLU A 23  ? 0.5525 0.3791 0.7853 0.1335  0.0555  -0.0385 23  GLU A CA  
189   C C   . GLU A 23  ? 0.5117 0.3390 0.7400 0.1275  0.0523  -0.0231 23  GLU A C   
190   O O   . GLU A 23  ? 0.4895 0.3161 0.7190 0.1325  0.0494  -0.0102 23  GLU A O   
191   C CB  . GLU A 23  ? 0.6228 0.4275 0.8582 0.1288  0.0579  -0.0463 23  GLU A CB  
192   C CG  . GLU A 23  ? 0.6943 0.4773 0.9322 0.1282  0.0563  -0.0347 23  GLU A CG  
193   C CD  . GLU A 23  ? 0.7489 0.5216 0.9937 0.1400  0.0562  -0.0331 23  GLU A CD  
194   O OE1 . GLU A 23  ? 0.7320 0.5185 0.9792 0.1499  0.0560  -0.0353 23  GLU A OE1 
195   O OE2 . GLU A 23  ? 0.7857 0.5367 1.0335 0.1395  0.0564  -0.0297 23  GLU A OE2 
196   N N   . GLU A 24  ? 0.5393 0.3689 0.7620 0.1168  0.0527  -0.0245 24  GLU A N   
197   C CA  . GLU A 24  ? 0.5018 0.3335 0.7192 0.1107  0.0500  -0.0108 24  GLU A CA  
198   C C   . GLU A 24  ? 0.4787 0.3291 0.6946 0.1161  0.0472  -0.0015 24  GLU A C   
199   O O   . GLU A 24  ? 0.5050 0.3545 0.7195 0.1166  0.0443  0.0125  24  GLU A O   
200   C CB  . GLU A 24  ? 0.4979 0.3328 0.7096 0.0996  0.0510  -0.0159 24  GLU A CB  
201   C CG  . GLU A 24  ? 0.4835 0.3017 0.6964 0.0926  0.0534  -0.0248 24  GLU A CG  
202   C CD  . GLU A 24  ? 0.5679 0.3917 0.7752 0.0822  0.0542  -0.0303 24  GLU A CD  
203   O OE1 . GLU A 24  ? 0.6563 0.4893 0.8583 0.0784  0.0524  -0.0219 24  GLU A OE1 
204   O OE2 . GLU A 24  ? 0.5460 0.3655 0.7542 0.0778  0.0565  -0.0433 24  GLU A OE2 
205   N N   . ARG A 25  ? 0.4750 0.3435 0.6908 0.1200  0.0482  -0.0093 25  ARG A N   
206   C CA  A ARG A 25  ? 0.4760 0.3640 0.6906 0.1242  0.0458  -0.0012 25  ARG A CA  
207   C CA  B ARG A 25  ? 0.4753 0.3633 0.6898 0.1242  0.0458  -0.0012 25  ARG A CA  
208   C C   . ARG A 25  ? 0.5033 0.3902 0.7233 0.1341  0.0435  0.0069  25  ARG A C   
209   O O   . ARG A 25  ? 0.4994 0.3939 0.7178 0.1350  0.0402  0.0195  25  ARG A O   
210   C CB  A ARG A 25  ? 0.4625 0.3703 0.6761 0.1262  0.0478  -0.0119 25  ARG A CB  
211   C CB  B ARG A 25  ? 0.4621 0.3698 0.6756 0.1261  0.0478  -0.0120 25  ARG A CB  
212   C CG  A ARG A 25  ? 0.4583 0.3690 0.6661 0.1171  0.0499  -0.0204 25  ARG A CG  
213   C CG  B ARG A 25  ? 0.4581 0.3687 0.6656 0.1166  0.0497  -0.0194 25  ARG A CG  
214   C CD  A ARG A 25  ? 0.4366 0.3701 0.6420 0.1186  0.0513  -0.0275 25  ARG A CD  
215   C CD  B ARG A 25  ? 0.4340 0.3675 0.6386 0.1175  0.0509  -0.0259 25  ARG A CD  
216   N NE  A ARG A 25  ? 0.4446 0.3792 0.6466 0.1136  0.0543  -0.0415 25  ARG A NE  
217   N NE  B ARG A 25  ? 0.4654 0.4060 0.6737 0.1247  0.0534  -0.0372 25  ARG A NE  
218   C CZ  A ARG A 25  ? 0.4432 0.3805 0.6470 0.1174  0.0571  -0.0544 25  ARG A CZ  
219   C CZ  B ARG A 25  ? 0.4488 0.3895 0.6555 0.1228  0.0566  -0.0513 25  ARG A CZ  
220   N NH1 A ARG A 25  ? 0.4493 0.3884 0.6589 0.1269  0.0576  -0.0555 25  ARG A NH1 
221   N NH1 B ARG A 25  ? 0.4303 0.3642 0.6326 0.1139  0.0574  -0.0566 25  ARG A NH1 
222   N NH2 A ARG A 25  ? 0.4393 0.3785 0.6389 0.1117  0.0593  -0.0663 25  ARG A NH2 
223   N NH2 B ARG A 25  ? 0.4210 0.3700 0.6305 0.1298  0.0589  -0.0604 25  ARG A NH2 
224   N N   . GLU A 26  ? 0.5239 0.4016 0.7501 0.1415  0.0452  -0.0005 26  GLU A N   
225   C CA  . GLU A 26  ? 0.5116 0.3881 0.7436 0.1521  0.0431  0.0062  26  GLU A CA  
226   C C   . GLU A 26  ? 0.5282 0.3900 0.7593 0.1501  0.0401  0.0208  26  GLU A C   
227   O O   . GLU A 26  ? 0.5029 0.3722 0.7349 0.1550  0.0366  0.0321  26  GLU A O   
228   C CB  . GLU A 26  ? 0.4752 0.3424 0.7136 0.1601  0.0459  -0.0054 26  GLU A CB  
229   C CG  . GLU A 26  ? 0.4699 0.3551 0.7093 0.1644  0.0486  -0.0186 26  GLU A CG  
230   C CD  . GLU A 26  ? 0.5568 0.4599 0.8007 0.1754  0.0469  -0.0153 26  GLU A CD  
231   O OE1 . GLU A 26  ? 0.6451 0.5472 0.8910 0.1792  0.0430  -0.0027 26  GLU A OE1 
232   O OE2 . GLU A 26  ? 0.5303 0.4494 0.7754 0.1801  0.0493  -0.0254 26  GLU A OE2 
233   N N   . ALA A 27  ? 0.4933 0.3352 0.7226 0.1427  0.0414  0.0205  27  ALA A N   
234   C CA  . ALA A 27  ? 0.4743 0.3029 0.7018 0.1398  0.0390  0.0343  27  ALA A CA  
235   C C   . ALA A 27  ? 0.5566 0.3982 0.7770 0.1334  0.0362  0.0461  27  ALA A C   
236   O O   . ALA A 27  ? 0.5442 0.3867 0.7633 0.1354  0.0329  0.0593  27  ALA A O   
237   C CB  . ALA A 27  ? 0.5421 0.3484 0.7691 0.1322  0.0415  0.0303  27  ALA A CB  
238   N N   . ALA A 28  ? 0.5195 0.3715 0.7348 0.1258  0.0373  0.0413  28  ALA A N   
239   C CA  . ALA A 28  ? 0.4732 0.3366 0.6813 0.1192  0.0349  0.0515  28  ALA A CA  
240   C C   . ALA A 28  ? 0.4879 0.3703 0.6962 0.1255  0.0317  0.0596  28  ALA A C   
241   O O   . ALA A 28  ? 0.5018 0.3890 0.7057 0.1230  0.0286  0.0721  28  ALA A O   
242   C CB  . ALA A 28  ? 0.4305 0.3013 0.6338 0.1111  0.0369  0.0435  28  ALA A CB  
243   N N   . LEU A 29  ? 0.4961 0.3909 0.7094 0.1333  0.0323  0.0521  29  LEU A N   
244   C CA  . LEU A 29  ? 0.4798 0.3950 0.6938 0.1388  0.0293  0.0587  29  LEU A CA  
245   C C   . LEU A 29  ? 0.4844 0.3949 0.7023 0.1462  0.0262  0.0687  29  LEU A C   
246   O O   . LEU A 29  ? 0.4244 0.3471 0.6399 0.1465  0.0227  0.0796  29  LEU A O   
247   C CB  . LEU A 29  ? 0.4183 0.3493 0.6368 0.1448  0.0311  0.0473  29  LEU A CB  
248   C CG  . LEU A 29  ? 0.4298 0.3849 0.6494 0.1491  0.0283  0.0525  29  LEU A CG  
249   C CD1 . LEU A 29  ? 0.4375 0.4048 0.6490 0.1402  0.0266  0.0602  29  LEU A CD1 
250   C CD2 . LEU A 29  ? 0.4293 0.3994 0.6539 0.1551  0.0306  0.0404  29  LEU A CD2 
251   N N   . LYS A 30  ? 0.5029 0.3958 0.7266 0.1521  0.0274  0.0650  30  LYS A N   
252   C CA  . LYS A 30  ? 0.4899 0.3754 0.7169 0.1588  0.0245  0.0753  30  LYS A CA  
253   C C   . LYS A 30  ? 0.4718 0.3489 0.6920 0.1510  0.0226  0.0884  30  LYS A C   
254   O O   . LYS A 30  ? 0.5123 0.3963 0.7311 0.1534  0.0189  0.1003  30  LYS A O   
255   C CB  . LYS A 30  ? 0.5373 0.4035 0.7715 0.1662  0.0266  0.0682  30  LYS A CB  
256   C CG  . LYS A 30  ? 0.5650 0.4410 0.8061 0.1756  0.0284  0.0556  30  LYS A CG  
257   C CD  . LYS A 30  ? 0.7014 0.5584 0.9496 0.1843  0.0300  0.0498  30  LYS A CD  
258   C CE  . LYS A 30  ? 0.7058 0.5738 0.9602 0.1934  0.0322  0.0362  30  LYS A CE  
259   N NZ  . LYS A 30  ? 0.7413 0.5914 1.0026 0.2029  0.0337  0.0306  30  LYS A NZ  
260   N N   . GLU A 31  ? 0.5162 0.3800 0.7317 0.1413  0.0250  0.0859  31  GLU A N   
261   C CA  . GLU A 31  ? 0.4813 0.3387 0.6898 0.1332  0.0235  0.0975  31  GLU A CA  
262   C C   . GLU A 31  ? 0.5037 0.3818 0.7053 0.1288  0.0206  0.1056  31  GLU A C   
263   O O   . GLU A 31  ? 0.5943 0.4737 0.7912 0.1265  0.0180  0.1177  31  GLU A O   
264   C CB  . GLU A 31  ? 0.4457 0.2878 0.6509 0.1233  0.0267  0.0918  31  GLU A CB  
265   C CG  . GLU A 31  ? 0.5195 0.3537 0.7178 0.1149  0.0256  0.1029  31  GLU A CG  
266   C CD  . GLU A 31  ? 0.7065 0.5293 0.9069 0.1202  0.0236  0.1137  31  GLU A CD  
267   O OE1 . GLU A 31  ? 0.6750 0.4842 0.8826 0.1278  0.0246  0.1097  31  GLU A OE1 
268   O OE2 . GLU A 31  ? 0.7198 0.5474 0.9142 0.1170  0.0210  0.1259  31  GLU A OE2 
269   N N   . ALA A 32  ? 0.5185 0.4132 0.7191 0.1275  0.0213  0.0990  32  ALA A N   
270   C CA  . ALA A 32  ? 0.4578 0.3725 0.6519 0.1232  0.0188  0.1055  32  ALA A CA  
271   C C   . ALA A 32  ? 0.4446 0.3764 0.6417 0.1310  0.0154  0.1115  32  ALA A C   
272   O O   . ALA A 32  ? 0.4420 0.3931 0.6350 0.1283  0.0135  0.1147  32  ALA A O   
273   C CB  . ALA A 32  ? 0.4226 0.3474 0.6143 0.1182  0.0209  0.0962  32  ALA A CB  
274   N N   . GLY A 33  ? 0.5117 0.4370 0.7160 0.1406  0.0145  0.1129  33  GLY A N   
275   C CA  . GLY A 33  ? 0.5393 0.4814 0.7476 0.1488  0.0111  0.1181  33  GLY A CA  
276   C C   . GLY A 33  ? 0.4936 0.4557 0.7054 0.1520  0.0117  0.1097  33  GLY A C   
277   O O   . GLY A 33  ? 0.4832 0.4655 0.6951 0.1540  0.0088  0.1146  33  GLY A O   
278   N N   . TYR A 34  ? 0.4606 0.4184 0.6754 0.1522  0.0154  0.0969  34  TYR A N   
279   C CA  . TYR A 34  ? 0.4282 0.4052 0.6458 0.1542  0.0166  0.0879  34  TYR A CA  
280   C C   . TYR A 34  ? 0.4107 0.4067 0.6209 0.1462  0.0152  0.0925  34  TYR A C   
281   O O   . TYR A 34  ? 0.3762 0.3931 0.5882 0.1481  0.0146  0.0901  34  TYR A O   
282   C CB  . TYR A 34  ? 0.5294 0.5174 0.7561 0.1659  0.0152  0.0859  34  TYR A CB  
283   C CG  . TYR A 34  ? 0.5019 0.4720 0.7362 0.1744  0.0170  0.0790  34  TYR A CG  
284   C CD1 . TYR A 34  ? 0.4718 0.4396 0.7098 0.1768  0.0210  0.0646  34  TYR A CD1 
285   C CD2 . TYR A 34  ? 0.5101 0.4657 0.7473 0.1800  0.0149  0.0869  34  TYR A CD2 
286   C CE1 . TYR A 34  ? 0.5304 0.4818 0.7746 0.1845  0.0229  0.0577  34  TYR A CE1 
287   C CE2 . TYR A 34  ? 0.5961 0.5342 0.8399 0.1878  0.0167  0.0806  34  TYR A CE2 
288   C CZ  . TYR A 34  ? 0.6487 0.5846 0.8960 0.1900  0.0207  0.0657  34  TYR A CZ  
289   O OH  . TYR A 34  ? 0.7146 0.6331 0.9679 0.1977  0.0227  0.0586  34  TYR A OH  
290   N N   . ASN A 35  ? 0.3811 0.3702 0.5827 0.1369  0.0148  0.0988  35  ASN A N   
291   C CA  . ASN A 35  ? 0.3969 0.4012 0.5906 0.1285  0.0137  0.1024  35  ASN A CA  
292   C C   . ASN A 35  ? 0.3767 0.3706 0.5647 0.1201  0.0166  0.0972  35  ASN A C   
293   O O   . ASN A 35  ? 0.3859 0.3648 0.5693 0.1147  0.0166  0.1015  35  ASN A O   
294   C CB  . ASN A 35  ? 0.3425 0.3518 0.5304 0.1254  0.0098  0.1155  35  ASN A CB  
295   C CG  . ASN A 35  ? 0.3943 0.4214 0.5742 0.1174  0.0083  0.1186  35  ASN A CG  
296   O OD1 . ASN A 35  ? 0.4347 0.4664 0.6122 0.1129  0.0104  0.1120  35  ASN A OD1 
297   N ND2 . ASN A 35  ? 0.3912 0.4285 0.5670 0.1156  0.0048  0.1285  35  ASN A ND2 
298   N N   . PRO A 36  ? 0.3716 0.3737 0.5597 0.1184  0.0191  0.0880  36  PRO A N   
299   C CA  . PRO A 36  ? 0.3151 0.3074 0.4984 0.1109  0.0218  0.0824  36  PRO A CA  
300   C C   . PRO A 36  ? 0.3244 0.3157 0.4982 0.1017  0.0200  0.0907  36  PRO A C   
301   O O   . PRO A 36  ? 0.3404 0.3200 0.5105 0.0956  0.0218  0.0876  36  PRO A O   
302   C CB  . PRO A 36  ? 0.2996 0.3068 0.4840 0.1113  0.0241  0.0730  36  PRO A CB  
303   C CG  . PRO A 36  ? 0.3277 0.3546 0.5161 0.1171  0.0223  0.0751  36  PRO A CG  
304   C CD  . PRO A 36  ? 0.3615 0.3817 0.5548 0.1237  0.0199  0.0814  36  PRO A CD  
305   N N   . PHE A 37  ? 0.3104 0.3142 0.4802 0.1002  0.0165  0.1004  37  PHE A N   
306   C CA  . PHE A 37  ? 0.3222 0.3248 0.4827 0.0917  0.0146  0.1079  37  PHE A CA  
307   C C   . PHE A 37  ? 0.3308 0.3139 0.4901 0.0897  0.0149  0.1118  37  PHE A C   
308   O O   . PHE A 37  ? 0.3813 0.3594 0.5332 0.0818  0.0148  0.1144  37  PHE A O   
309   C CB  . PHE A 37  ? 0.3381 0.3586 0.4947 0.0908  0.0108  0.1167  37  PHE A CB  
310   C CG  . PHE A 37  ? 0.3188 0.3543 0.4685 0.0842  0.0100  0.1164  37  PHE A CG  
311   C CD1 . PHE A 37  ? 0.3316 0.3625 0.4725 0.0755  0.0099  0.1179  37  PHE A CD1 
312   C CD2 . PHE A 37  ? 0.3571 0.4118 0.5089 0.0863  0.0093  0.1145  37  PHE A CD2 
313   C CE1 . PHE A 37  ? 0.3144 0.3582 0.4487 0.0695  0.0090  0.1175  37  PHE A CE1 
314   C CE2 . PHE A 37  ? 0.2865 0.3544 0.4318 0.0797  0.0085  0.1143  37  PHE A CE2 
315   C CZ  . PHE A 37  ? 0.2563 0.3182 0.3928 0.0715  0.0082  0.1160  37  PHE A CZ  
316   N N   . LEU A 38  ? 0.3686 0.3409 0.5348 0.0965  0.0153  0.1119  38  LEU A N   
317   C CA  . LEU A 38  ? 0.3252 0.2787 0.4908 0.0948  0.0157  0.1157  38  LEU A CA  
318   C C   . LEU A 38  ? 0.3645 0.2999 0.5336 0.0936  0.0195  0.1060  38  LEU A C   
319   O O   . LEU A 38  ? 0.3585 0.2772 0.5285 0.0926  0.0203  0.1079  38  LEU A O   
320   C CB  . LEU A 38  ? 0.3001 0.2511 0.4709 0.1027  0.0137  0.1225  38  LEU A CB  
321   C CG  . LEU A 38  ? 0.4005 0.3703 0.5684 0.1040  0.0097  0.1319  38  LEU A CG  
322   C CD1 . LEU A 38  ? 0.4561 0.4222 0.6291 0.1121  0.0076  0.1390  38  LEU A CD1 
323   C CD2 . LEU A 38  ? 0.4076 0.3833 0.5651 0.0944  0.0082  0.1385  38  LEU A CD2 
324   N N   . LEU A 39  ? 0.3145 0.2536 0.4855 0.0936  0.0220  0.0955  39  LEU A N   
325   C CA  . LEU A 39  ? 0.2955 0.2197 0.4693 0.0916  0.0256  0.0850  39  LEU A CA  
326   C C   . LEU A 39  ? 0.3248 0.2435 0.4912 0.0813  0.0264  0.0853  39  LEU A C   
327   O O   . LEU A 39  ? 0.2485 0.1791 0.4082 0.0765  0.0249  0.0888  39  LEU A O   
328   C CB  . LEU A 39  ? 0.3093 0.2419 0.4873 0.0955  0.0280  0.0733  39  LEU A CB  
329   C CG  . LEU A 39  ? 0.3750 0.3126 0.5613 0.1057  0.0283  0.0688  39  LEU A CG  
330   C CD1 . LEU A 39  ? 0.3466 0.2976 0.5346 0.1075  0.0306  0.0580  39  LEU A CD1 
331   C CD2 . LEU A 39  ? 0.3549 0.2730 0.5472 0.1096  0.0300  0.0643  39  LEU A CD2 
332   N N   . PRO A 40  ? 0.3310 0.2323 0.4984 0.0776  0.0285  0.0814  40  PRO A N   
333   C CA  . PRO A 40  ? 0.2822 0.1795 0.4436 0.0680  0.0296  0.0792  40  PRO A CA  
334   C C   . PRO A 40  ? 0.3323 0.2351 0.4942 0.0669  0.0319  0.0680  40  PRO A C   
335   O O   . PRO A 40  ? 0.3564 0.2601 0.5245 0.0727  0.0337  0.0589  40  PRO A O   
336   C CB  . PRO A 40  ? 0.2812 0.1590 0.4452 0.0652  0.0314  0.0773  40  PRO A CB  
337   C CG  . PRO A 40  ? 0.3192 0.1899 0.4921 0.0740  0.0325  0.0726  40  PRO A CG  
338   C CD  . PRO A 40  ? 0.2926 0.1771 0.4666 0.0817  0.0298  0.0793  40  PRO A CD  
339   N N   . SER A 41  ? 0.2909 0.1981 0.4459 0.0595  0.0317  0.0682  41  SER A N   
340   C CA  . SER A 41  ? 0.2502 0.1626 0.4049 0.0583  0.0338  0.0581  41  SER A CA  
341   C C   . SER A 41  ? 0.2715 0.1725 0.4322 0.0586  0.0372  0.0450  41  SER A C   
342   O O   . SER A 41  ? 0.2632 0.1701 0.4262 0.0611  0.0392  0.0346  41  SER A O   
343   C CB  . SER A 41  ? 0.2651 0.1811 0.4108 0.0497  0.0329  0.0604  41  SER A CB  
344   O OG  . SER A 41  ? 0.3162 0.2187 0.4613 0.0432  0.0343  0.0587  41  SER A OG  
345   N N   . SER A 42  ? 0.2968 0.1824 0.4595 0.0557  0.0380  0.0449  42  SER A N   
346   C CA  . SER A 42  ? 0.2965 0.1711 0.4646 0.0552  0.0411  0.0322  42  SER A CA  
347   C C   . SER A 42  ? 0.3428 0.2190 0.5180 0.0643  0.0423  0.0250  42  SER A C   
348   O O   . SER A 42  ? 0.4295 0.3017 0.6082 0.0645  0.0449  0.0119  42  SER A O   
349   C CB  . SER A 42  ? 0.2742 0.1324 0.4433 0.0505  0.0415  0.0351  42  SER A CB  
350   O OG  . SER A 42  ? 0.3476 0.2015 0.5186 0.0555  0.0397  0.0453  42  SER A OG  
351   N N   . ALA A 43  ? 0.2820 0.1650 0.4590 0.0715  0.0404  0.0326  43  ALA A N   
352   C CA  . ALA A 43  ? 0.3423 0.2287 0.5258 0.0805  0.0414  0.0260  43  ALA A CA  
353   C C   . ALA A 43  ? 0.3153 0.2209 0.4979 0.0839  0.0418  0.0209  43  ALA A C   
354   O O   . ALA A 43  ? 0.3595 0.2719 0.5468 0.0914  0.0426  0.0161  43  ALA A O   
355   C CB  . ALA A 43  ? 0.3219 0.2058 0.5088 0.0873  0.0391  0.0363  43  ALA A CB  
356   N N   . VAL A 44  ? 0.3072 0.2221 0.4838 0.0784  0.0416  0.0218  44  VAL A N   
357   C CA  . VAL A 44  ? 0.2849 0.2189 0.4598 0.0808  0.0419  0.0190  44  VAL A CA  
358   C C   . VAL A 44  ? 0.3156 0.2536 0.4842 0.0748  0.0437  0.0064  44  VAL A C   
359   O O   . VAL A 44  ? 0.2939 0.2242 0.4573 0.0671  0.0435  0.0051  44  VAL A O   
360   C CB  . VAL A 44  ? 0.2814 0.2273 0.4485 0.0776  0.0383  0.0315  44  VAL A CB  
361   C CG1 . VAL A 44  ? 0.2626 0.2294 0.4230 0.0770  0.0378  0.0280  44  VAL A CG1 
362   C CG2 . VAL A 44  ? 0.2547 0.1991 0.4260 0.0828  0.0359  0.0435  44  VAL A CG2 
363   N N   . TYR A 45  ? 0.3059 0.2574 0.4745 0.0782  0.0453  -0.0027 45  TYR A N   
364   C CA  . TYR A 45  ? 0.2721 0.2304 0.4332 0.0729  0.0466  -0.0141 45  TYR A CA  
365   C C   . TYR A 45  ? 0.2826 0.2563 0.4312 0.0672  0.0441  -0.0089 45  TYR A C   
366   O O   . TYR A 45  ? 0.3799 0.3501 0.5207 0.0599  0.0423  -0.0053 45  TYR A O   
367   C CB  . TYR A 45  ? 0.2850 0.2506 0.4519 0.0790  0.0499  -0.0267 45  TYR A CB  
368   C CG  . TYR A 45  ? 0.3038 0.2807 0.4622 0.0744  0.0510  -0.0378 45  TYR A CG  
369   C CD1 . TYR A 45  ? 0.2599 0.2316 0.4113 0.0664  0.0503  -0.0414 45  TYR A CD1 
370   C CD2 . TYR A 45  ? 0.2908 0.2846 0.4483 0.0783  0.0528  -0.0444 45  TYR A CD2 
371   C CE1 . TYR A 45  ? 0.3276 0.3106 0.4711 0.0627  0.0510  -0.0508 45  TYR A CE1 
372   C CE2 . TYR A 45  ? 0.2913 0.2961 0.4406 0.0742  0.0537  -0.0537 45  TYR A CE2 
373   C CZ  . TYR A 45  ? 0.3046 0.3040 0.4468 0.0666  0.0527  -0.0566 45  TYR A CZ  
374   O OH  . TYR A 45  ? 0.3304 0.3417 0.4641 0.0630  0.0533  -0.0652 45  TYR A OH  
375   N N   . ILE A 46  ? 0.2403 0.2307 0.3870 0.0703  0.0440  -0.0085 46  ILE A N   
376   C CA  . ILE A 46  ? 0.2080 0.2122 0.3438 0.0653  0.0418  -0.0028 46  ILE A CA  
377   C C   . ILE A 46  ? 0.1895 0.1974 0.3271 0.0674  0.0393  0.0099  46  ILE A C   
378   O O   . ILE A 46  ? 0.1938 0.2085 0.3389 0.0743  0.0399  0.0114  46  ILE A O   
379   C CB  . ILE A 46  ? 0.2472 0.2683 0.3791 0.0663  0.0435  -0.0103 46  ILE A CB  
380   C CG1 . ILE A 46  ? 0.2257 0.2454 0.3537 0.0632  0.0454  -0.0223 46  ILE A CG1 
381   C CG2 . ILE A 46  ? 0.2015 0.2360 0.3238 0.0619  0.0413  -0.0027 46  ILE A CG2 
382   C CD1 . ILE A 46  ? 0.2272 0.2629 0.3530 0.0654  0.0479  -0.0309 46  ILE A CD1 
383   N N   . ASP A 47  ? 0.1874 0.1920 0.3182 0.0616  0.0365  0.0186  47  ASP A N   
384   C CA  . ASP A 47  ? 0.2404 0.2465 0.3731 0.0630  0.0338  0.0308  47  ASP A CA  
385   C C   . ASP A 47  ? 0.1553 0.1784 0.2808 0.0602  0.0321  0.0351  47  ASP A C   
386   O O   . ASP A 47  ? 0.2161 0.2412 0.3315 0.0531  0.0306  0.0368  47  ASP A O   
387   C CB  . ASP A 47  ? 0.2462 0.2391 0.3761 0.0582  0.0320  0.0375  47  ASP A CB  
388   C CG  . ASP A 47  ? 0.2044 0.1942 0.3401 0.0620  0.0301  0.0489  47  ASP A CG  
389   O OD1 . ASP A 47  ? 0.1720 0.1720 0.3128 0.0679  0.0295  0.0522  47  ASP A OD1 
390   O OD2 . ASP A 47  ? 0.2082 0.1862 0.3434 0.0592  0.0292  0.0547  47  ASP A OD2 
391   N N   . LEU A 48  ? 0.2132 0.2485 0.3445 0.0657  0.0323  0.0366  48  LEU A N   
392   C CA  . LEU A 48  ? 0.1542 0.2064 0.2804 0.0631  0.0308  0.0408  48  LEU A CA  
393   C C   . LEU A 48  ? 0.1882 0.2452 0.3177 0.0648  0.0278  0.0519  48  LEU A C   
394   O O   . LEU A 48  ? 0.1707 0.2435 0.3003 0.0650  0.0269  0.0549  48  LEU A O   
395   C CB  . LEU A 48  ? 0.1767 0.2432 0.3067 0.0672  0.0335  0.0340  48  LEU A CB  
396   C CG  . LEU A 48  ? 0.1589 0.2233 0.2871 0.0672  0.0368  0.0223  48  LEU A CG  
397   C CD1 . LEU A 48  ? 0.1441 0.2257 0.2752 0.0707  0.0394  0.0169  48  LEU A CD1 
398   C CD2 . LEU A 48  ? 0.1513 0.2118 0.2672 0.0587  0.0361  0.0207  48  LEU A CD2 
399   N N   . LEU A 49  ? 0.1871 0.2315 0.3195 0.0660  0.0263  0.0579  49  LEU A N   
400   C CA  . LEU A 49  ? 0.2047 0.2541 0.3394 0.0676  0.0231  0.0690  49  LEU A CA  
401   C C   . LEU A 49  ? 0.2115 0.2724 0.3363 0.0599  0.0205  0.0736  49  LEU A C   
402   O O   . LEU A 49  ? 0.1844 0.2595 0.3109 0.0610  0.0186  0.0790  49  LEU A O   
403   C CB  . LEU A 49  ? 0.1794 0.2124 0.3166 0.0685  0.0220  0.0752  49  LEU A CB  
404   C CG  . LEU A 49  ? 0.1942 0.2313 0.3365 0.0729  0.0190  0.0869  49  LEU A CG  
405   C CD1 . LEU A 49  ? 0.2305 0.2721 0.3856 0.0837  0.0199  0.0864  49  LEU A CD1 
406   C CD2 . LEU A 49  ? 0.1765 0.1979 0.3179 0.0713  0.0180  0.0940  49  LEU A CD2 
407   N N   . THR A 50  ? 0.1946 0.2495 0.3091 0.0520  0.0205  0.0712  50  THR A N   
408   C CA  . THR A 50  ? 0.1925 0.2556 0.2974 0.0445  0.0183  0.0748  50  THR A CA  
409   C C   . THR A 50  ? 0.1819 0.2411 0.2773 0.0381  0.0196  0.0682  50  THR A C   
410   O O   . THR A 50  ? 0.1744 0.2234 0.2697 0.0386  0.0217  0.0620  50  THR A O   
411   C CB  . THR A 50  ? 0.2753 0.3340 0.3772 0.0417  0.0154  0.0835  50  THR A CB  
412   O OG1 . THR A 50  ? 0.2801 0.3489 0.3738 0.0351  0.0132  0.0864  50  THR A OG1 
413   C CG2 . THR A 50  ? 0.1974 0.2397 0.2955 0.0386  0.0162  0.0816  50  THR A CG2 
414   N N   . ASP A 51  ? 0.1971 0.2647 0.2846 0.0320  0.0183  0.0696  51  ASP A N   
415   C CA  . ASP A 51  ? 0.1534 0.2161 0.2309 0.0256  0.0187  0.0658  51  ASP A CA  
416   C C   . ASP A 51  ? 0.1745 0.2310 0.2455 0.0205  0.0165  0.0703  51  ASP A C   
417   O O   . ASP A 51  ? 0.1876 0.2416 0.2501 0.0150  0.0163  0.0682  51  ASP A O   
418   C CB  . ASP A 51  ? 0.1824 0.2563 0.2548 0.0219  0.0192  0.0639  51  ASP A CB  
419   C CG  . ASP A 51  ? 0.1825 0.2674 0.2537 0.0185  0.0168  0.0701  51  ASP A CG  
420   O OD1 . ASP A 51  ? 0.1914 0.2810 0.2687 0.0217  0.0152  0.0754  51  ASP A OD1 
421   O OD2 . ASP A 51  ? 0.1504 0.2394 0.2143 0.0126  0.0166  0.0696  51  ASP A OD2 
422   N N   . SER A 52  ? 0.1816 0.2357 0.2566 0.0224  0.0149  0.0765  52  SER A N   
423   C CA  . SER A 52  ? 0.1908 0.2427 0.2599 0.0175  0.0127  0.0817  52  SER A CA  
424   C C   . SER A 52  ? 0.1886 0.2267 0.2572 0.0170  0.0135  0.0811  52  SER A C   
425   O O   . SER A 52  ? 0.2078 0.2395 0.2837 0.0215  0.0141  0.0834  52  SER A O   
426   C CB  . SER A 52  ? 0.1952 0.2561 0.2681 0.0193  0.0101  0.0900  52  SER A CB  
427   O OG  . SER A 52  ? 0.1811 0.2434 0.2470 0.0137  0.0079  0.0944  52  SER A OG  
428   N N   . GLY A 53  ? 0.1492 0.1829 0.2098 0.0116  0.0136  0.0781  53  GLY A N   
429   C CA  . GLY A 53  ? 0.1141 0.1369 0.1738 0.0100  0.0143  0.0776  53  GLY A CA  
430   C C   . GLY A 53  ? 0.1653 0.1793 0.2292 0.0125  0.0168  0.0709  53  GLY A C   
431   O O   . GLY A 53  ? 0.1611 0.1661 0.2251 0.0108  0.0176  0.0699  53  GLY A O   
432   N N   . THR A 54  ? 0.1456 0.1626 0.2129 0.0161  0.0181  0.0658  54  THR A N   
433   C CA  . THR A 54  ? 0.1630 0.1732 0.2345 0.0187  0.0205  0.0584  54  THR A CA  
434   C C   . THR A 54  ? 0.1888 0.2006 0.2536 0.0160  0.0213  0.0510  54  THR A C   
435   O O   . THR A 54  ? 0.1908 0.2000 0.2583 0.0180  0.0232  0.0438  54  THR A O   
436   C CB  . THR A 54  ? 0.1966 0.2096 0.2768 0.0252  0.0217  0.0571  54  THR A CB  
437   O OG1 . THR A 54  ? 0.1725 0.1983 0.2508 0.0257  0.0210  0.0585  54  THR A OG1 
438   C CG2 . THR A 54  ? 0.2248 0.2329 0.3130 0.0291  0.0212  0.0639  54  THR A CG2 
439   N N   . ASN A 55  ? 0.1517 0.1680 0.2081 0.0117  0.0199  0.0525  55  ASN A N   
440   C CA  . ASN A 55  ? 0.1597 0.1784 0.2096 0.0098  0.0204  0.0470  55  ASN A CA  
441   C C   . ASN A 55  ? 0.1417 0.1534 0.1894 0.0080  0.0209  0.0420  55  ASN A C   
442   O O   . ASN A 55  ? 0.1552 0.1608 0.2044 0.0064  0.0206  0.0437  55  ASN A O   
443   C CB  . ASN A 55  ? 0.1515 0.1754 0.1936 0.0059  0.0187  0.0505  55  ASN A CB  
444   C CG  . ASN A 55  ? 0.1574 0.1893 0.2019 0.0065  0.0179  0.0558  55  ASN A CG  
445   O OD1 . ASN A 55  ? 0.1433 0.1819 0.1904 0.0088  0.0188  0.0547  55  ASN A OD1 
446   N ND2 . ASN A 55  ? 0.1556 0.1881 0.1991 0.0042  0.0160  0.0616  55  ASN A ND2 
447   N N   . ALA A 56  ? 0.1580 0.1719 0.2024 0.0083  0.0217  0.0358  56  ALA A N   
448   C CA  . ALA A 56  ? 0.1130 0.1232 0.1544 0.0065  0.0218  0.0307  56  ALA A CA  
449   C C   . ALA A 56  ? 0.1428 0.1545 0.1755 0.0033  0.0201  0.0327  56  ALA A C   
450   O O   . ALA A 56  ? 0.1633 0.1797 0.1907 0.0031  0.0197  0.0337  56  ALA A O   
451   C CB  . ALA A 56  ? 0.1253 0.1384 0.1672 0.0089  0.0232  0.0229  56  ALA A CB  
452   N N   . MET A 57  ? 0.1602 0.1677 0.1916 0.0007  0.0195  0.0333  57  MET A N   
453   C CA  . MET A 57  ? 0.1861 0.1943 0.2100 -0.0019 0.0181  0.0344  57  MET A CA  
454   C C   . MET A 57  ? 0.1895 0.1990 0.2097 -0.0012 0.0180  0.0286  57  MET A C   
455   O O   . MET A 57  ? 0.2000 0.2104 0.2234 0.0006  0.0190  0.0234  57  MET A O   
456   C CB  . MET A 57  ? 0.1526 0.1575 0.1770 -0.0048 0.0176  0.0371  57  MET A CB  
457   C CG  . MET A 57  ? 0.1488 0.1540 0.1750 -0.0057 0.0171  0.0439  57  MET A CG  
458   S SD  . MET A 57  ? 0.1797 0.1839 0.2029 -0.0098 0.0164  0.0475  57  MET A SD  
459   C CE  . MET A 57  ? 0.1512 0.1505 0.1805 -0.0104 0.0179  0.0452  57  MET A CE  
460   N N   . SER A 58  ? 0.1369 0.1468 0.1504 -0.0024 0.0168  0.0293  58  SER A N   
461   C CA  . SER A 58  ? 0.1768 0.1885 0.1864 -0.0012 0.0163  0.0248  58  SER A CA  
462   C C   . SER A 58  ? 0.1994 0.2098 0.2102 -0.0025 0.0160  0.0221  58  SER A C   
463   O O   . SER A 58  ? 0.1781 0.1860 0.1912 -0.0048 0.0162  0.0245  58  SER A O   
464   C CB  . SER A 58  ? 0.2037 0.2157 0.2055 -0.0011 0.0152  0.0274  58  SER A CB  
465   O OG  . SER A 58  ? 0.2001 0.2090 0.1994 -0.0034 0.0144  0.0304  58  SER A OG  
466   N N   . ASP A 59  ? 0.1917 0.2053 0.2009 -0.0010 0.0154  0.0172  59  ASP A N   
467   C CA  . ASP A 59  ? 0.1515 0.1659 0.1616 -0.0021 0.0150  0.0145  59  ASP A CA  
468   C C   . ASP A 59  ? 0.1656 0.1782 0.1713 -0.0032 0.0142  0.0180  59  ASP A C   
469   O O   . ASP A 59  ? 0.1876 0.2002 0.1953 -0.0054 0.0145  0.0177  59  ASP A O   
470   C CB  . ASP A 59  ? 0.1785 0.1986 0.1874 0.0001  0.0142  0.0087  59  ASP A CB  
471   C CG  . ASP A 59  ? 0.1932 0.2154 0.1950 0.0033  0.0129  0.0101  59  ASP A CG  
472   O OD1 . ASP A 59  ? 0.2699 0.2887 0.2681 0.0032  0.0129  0.0151  59  ASP A OD1 
473   O OD2 . ASP A 59  ? 0.2589 0.2866 0.2587 0.0056  0.0118  0.0063  59  ASP A OD2 
474   N N   . HIS A 60  ? 0.1743 0.1854 0.1741 -0.0021 0.0133  0.0211  60  HIS A N   
475   C CA  . HIS A 60  ? 0.2049 0.2135 0.2006 -0.0033 0.0126  0.0237  60  HIS A CA  
476   C C   . HIS A 60  ? 0.1860 0.1927 0.1839 -0.0067 0.0133  0.0273  60  HIS A C   
477   O O   . HIS A 60  ? 0.1691 0.1757 0.1657 -0.0085 0.0133  0.0277  60  HIS A O   
478   C CB  . HIS A 60  ? 0.2121 0.2180 0.2014 -0.0019 0.0118  0.0263  60  HIS A CB  
479   C CG  . HIS A 60  ? 0.3069 0.3142 0.2926 0.0018  0.0107  0.0240  60  HIS A CG  
480   N ND1 . HIS A 60  ? 0.3342 0.3413 0.3179 0.0035  0.0098  0.0220  60  HIS A ND1 
481   C CD2 . HIS A 60  ? 0.3178 0.3276 0.3014 0.0044  0.0104  0.0234  60  HIS A CD2 
482   C CE1 . HIS A 60  ? 0.3956 0.4047 0.3763 0.0073  0.0086  0.0209  60  HIS A CE1 
483   N NE2 . HIS A 60  ? 0.3086 0.3195 0.2888 0.0077  0.0089  0.0219  60  HIS A NE2 
484   N N   . GLN A 61  ? 0.1875 0.1938 0.1887 -0.0074 0.0140  0.0300  61  GLN A N   
485   C CA  . GLN A 61  ? 0.1652 0.1709 0.1688 -0.0102 0.0144  0.0341  61  GLN A CA  
486   C C   . GLN A 61  ? 0.1813 0.1873 0.1894 -0.0119 0.0153  0.0329  61  GLN A C   
487   O O   . GLN A 61  ? 0.1866 0.1932 0.1939 -0.0145 0.0154  0.0352  61  GLN A O   
488   C CB  . GLN A 61  ? 0.1523 0.1582 0.1593 -0.0096 0.0148  0.0372  61  GLN A CB  
489   C CG  . GLN A 61  ? 0.1846 0.1914 0.1875 -0.0101 0.0141  0.0402  61  GLN A CG  
490   C CD  . GLN A 61  ? 0.1843 0.1933 0.1914 -0.0090 0.0146  0.0428  61  GLN A CD  
491   O OE1 . GLN A 61  ? 0.1549 0.1648 0.1645 -0.0065 0.0154  0.0403  61  GLN A OE1 
492   N NE2 . GLN A 61  ? 0.1544 0.1655 0.1624 -0.0108 0.0141  0.0475  61  GLN A NE2 
493   N N   . TRP A 62  ? 0.1717 0.1777 0.1844 -0.0108 0.0161  0.0291  62  TRP A N   
494   C CA  . TRP A 62  ? 0.1612 0.1672 0.1786 -0.0131 0.0172  0.0277  62  TRP A CA  
495   C C   . TRP A 62  ? 0.1969 0.2062 0.2112 -0.0144 0.0169  0.0253  62  TRP A C   
496   O O   . TRP A 62  ? 0.1784 0.1888 0.1941 -0.0175 0.0178  0.0269  62  TRP A O   
497   C CB  . TRP A 62  ? 0.1908 0.1962 0.2137 -0.0122 0.0181  0.0229  62  TRP A CB  
498   C CG  . TRP A 62  ? 0.2778 0.2790 0.3061 -0.0117 0.0191  0.0254  62  TRP A CG  
499   C CD1 . TRP A 62  ? 0.2751 0.2760 0.3038 -0.0087 0.0190  0.0254  62  TRP A CD1 
500   C CD2 . TRP A 62  ? 0.2948 0.2916 0.3290 -0.0140 0.0205  0.0285  62  TRP A CD2 
501   N NE1 . TRP A 62  ? 0.2611 0.2579 0.2962 -0.0083 0.0202  0.0279  62  TRP A NE1 
502   C CE2 . TRP A 62  ? 0.3159 0.3094 0.3544 -0.0115 0.0210  0.0301  62  TRP A CE2 
503   C CE3 . TRP A 62  ? 0.3053 0.3010 0.3417 -0.0179 0.0214  0.0304  62  TRP A CE3 
504   C CZ2 . TRP A 62  ? 0.3194 0.3070 0.3644 -0.0122 0.0222  0.0338  62  TRP A CZ2 
505   C CZ3 . TRP A 62  ? 0.3099 0.2998 0.3523 -0.0193 0.0228  0.0346  62  TRP A CZ3 
506   C CH2 . TRP A 62  ? 0.2795 0.2647 0.3261 -0.0162 0.0230  0.0364  62  TRP A CH2 
507   N N   . ALA A 63  ? 0.1488 0.1603 0.1589 -0.0117 0.0158  0.0219  63  ALA A N   
508   C CA  . ALA A 63  ? 0.1713 0.1863 0.1789 -0.0118 0.0154  0.0194  63  ALA A CA  
509   C C   . ALA A 63  ? 0.1400 0.1543 0.1439 -0.0139 0.0155  0.0230  63  ALA A C   
510   O O   . ALA A 63  ? 0.1651 0.1830 0.1691 -0.0157 0.0161  0.0219  63  ALA A O   
511   C CB  . ALA A 63  ? 0.1818 0.1985 0.1855 -0.0076 0.0139  0.0160  63  ALA A CB  
512   N N   . ALA A 64  ? 0.2216 0.2326 0.2223 -0.0139 0.0148  0.0270  64  ALA A N   
513   C CA  . ALA A 64  ? 0.1957 0.2070 0.1929 -0.0164 0.0147  0.0299  64  ALA A CA  
514   C C   . ALA A 64  ? 0.1995 0.2131 0.1999 -0.0201 0.0159  0.0332  64  ALA A C   
515   O O   . ALA A 64  ? 0.1826 0.1995 0.1807 -0.0225 0.0163  0.0337  64  ALA A O   
516   C CB  . ALA A 64  ? 0.2288 0.2371 0.2227 -0.0163 0.0138  0.0333  64  ALA A CB  
517   N N   . MET A 65  ? 0.1889 0.2007 0.1945 -0.0205 0.0165  0.0357  65  MET A N   
518   C CA  . MET A 65  ? 0.1815 0.1943 0.1904 -0.0238 0.0176  0.0400  65  MET A CA  
519   C C   . MET A 65  ? 0.1932 0.2095 0.2037 -0.0263 0.0191  0.0373  65  MET A C   
520   O O   . MET A 65  ? 0.2139 0.2334 0.2237 -0.0297 0.0200  0.0405  65  MET A O   
521   C CB  . MET A 65  ? 0.1524 0.1609 0.1672 -0.0230 0.0181  0.0427  65  MET A CB  
522   C CG  . MET A 65  ? 0.2247 0.2318 0.2389 -0.0210 0.0170  0.0464  65  MET A CG  
523   S SD  . MET A 65  ? 0.3140 0.3163 0.3364 -0.0193 0.0179  0.0491  65  MET A SD  
524   C CE  . MET A 65  ? 0.1985 0.2017 0.2219 -0.0221 0.0180  0.0577  65  MET A CE  
525   N N   . ILE A 66  ? 0.1898 0.2069 0.2025 -0.0247 0.0194  0.0314  66  ILE A N   
526   C CA  . ILE A 66  ? 0.2049 0.2266 0.2206 -0.0273 0.0208  0.0282  66  ILE A CA  
527   C C   . ILE A 66  ? 0.1597 0.1876 0.1708 -0.0281 0.0210  0.0267  66  ILE A C   
528   O O   . ILE A 66  ? 0.1892 0.2224 0.2019 -0.0316 0.0227  0.0265  66  ILE A O   
529   C CB  . ILE A 66  ? 0.2140 0.2368 0.2331 -0.0251 0.0207  0.0217  66  ILE A CB  
530   C CG1 . ILE A 66  ? 0.2572 0.2742 0.2811 -0.0247 0.0209  0.0222  66  ILE A CG1 
531   C CG2 . ILE A 66  ? 0.2296 0.2591 0.2523 -0.0281 0.0221  0.0178  66  ILE A CG2 
532   C CD1 . ILE A 66  ? 0.2992 0.3176 0.3244 -0.0214 0.0200  0.0159  66  ILE A CD1 
533   N N   . THR A 67  ? 0.1506 0.1780 0.1561 -0.0251 0.0195  0.0254  67  THR A N   
534   C CA  . THR A 67  ? 0.1581 0.1906 0.1594 -0.0256 0.0198  0.0235  67  THR A CA  
535   C C   . THR A 67  ? 0.1967 0.2288 0.1936 -0.0281 0.0196  0.0282  67  THR A C   
536   O O   . THR A 67  ? 0.2090 0.2442 0.2013 -0.0283 0.0196  0.0261  67  THR A O   
537   C CB  . THR A 67  ? 0.1785 0.2102 0.1767 -0.0208 0.0184  0.0183  67  THR A CB  
538   O OG1 . THR A 67  ? 0.2377 0.2624 0.2337 -0.0182 0.0168  0.0201  67  THR A OG1 
539   C CG2 . THR A 67  ? 0.1897 0.2257 0.1921 -0.0186 0.0186  0.0132  67  THR A CG2 
540   N N   . GLY A 68  ? 0.1927 0.2216 0.1910 -0.0298 0.0194  0.0343  68  GLY A N   
541   C CA  . GLY A 68  ? 0.1564 0.1868 0.1508 -0.0321 0.0188  0.0390  68  GLY A CA  
542   C C   . GLY A 68  ? 0.1728 0.2110 0.1651 -0.0360 0.0203  0.0399  68  GLY A C   
543   O O   . GLY A 68  ? 0.1861 0.2277 0.1816 -0.0382 0.0221  0.0400  68  GLY A O   
544   N N   . ASP A 69  ? 0.1647 0.2063 0.1513 -0.0373 0.0196  0.0403  69  ASP A N   
545   C CA  . ASP A 69  ? 0.1848 0.2352 0.1679 -0.0410 0.0209  0.0404  69  ASP A CA  
546   C C   . ASP A 69  ? 0.2183 0.2696 0.2017 -0.0424 0.0197  0.0467  69  ASP A C   
547   O O   . ASP A 69  ? 0.2127 0.2625 0.1940 -0.0416 0.0175  0.0486  69  ASP A O   
548   C CB  . ASP A 69  ? 0.2121 0.2648 0.1893 -0.0403 0.0203  0.0346  69  ASP A CB  
549   C CG  . ASP A 69  ? 0.2073 0.2704 0.1803 -0.0440 0.0217  0.0337  69  ASP A CG  
550   O OD1 . ASP A 69  ? 0.2159 0.2850 0.1905 -0.0470 0.0232  0.0376  69  ASP A OD1 
551   O OD2 . ASP A 69  ? 0.2354 0.3004 0.2035 -0.0438 0.0214  0.0287  69  ASP A OD2 
552   N N   . GLU A 70  ? 0.1892 0.2424 0.1754 -0.0440 0.0209  0.0491  70  GLU A N   
553   C CA  . GLU A 70  ? 0.2048 0.2570 0.1920 -0.0442 0.0197  0.0549  70  GLU A CA  
554   C C   . GLU A 70  ? 0.2202 0.2814 0.2022 -0.0466 0.0191  0.0558  70  GLU A C   
555   O O   . GLU A 70  ? 0.2061 0.2683 0.1885 -0.0470 0.0182  0.0612  70  GLU A O   
556   C CB  . GLU A 70  ? 0.2120 0.2604 0.2046 -0.0451 0.0216  0.0577  70  GLU A CB  
557   C CG  . GLU A 70  ? 0.1742 0.2137 0.1725 -0.0431 0.0219  0.0577  70  GLU A CG  
558   C CD  . GLU A 70  ? 0.2124 0.2463 0.2114 -0.0397 0.0194  0.0605  70  GLU A CD  
559   O OE1 . GLU A 70  ? 0.1908 0.2272 0.1874 -0.0393 0.0177  0.0642  70  GLU A OE1 
560   O OE2 . GLU A 70  ? 0.1873 0.2157 0.1895 -0.0375 0.0192  0.0592  70  GLU A OE2 
561   N N   . ALA A 71  ? 0.1904 0.2585 0.1674 -0.0481 0.0197  0.0507  71  ALA A N   
562   C CA  . ALA A 71  ? 0.1497 0.2278 0.1216 -0.0508 0.0194  0.0504  71  ALA A CA  
563   C C   . ALA A 71  ? 0.1588 0.2380 0.1294 -0.0505 0.0163  0.0553  71  ALA A C   
564   O O   . ALA A 71  ? 0.2368 0.3109 0.2087 -0.0484 0.0144  0.0565  71  ALA A O   
565   C CB  . ALA A 71  ? 0.1616 0.2455 0.1282 -0.0519 0.0204  0.0430  71  ALA A CB  
566   N N   . TYR A 72  ? 0.2146 0.3021 0.1829 -0.0529 0.0159  0.0583  72  TYR A N   
567   C CA  . TYR A 72  ? 0.2224 0.3135 0.1897 -0.0528 0.0130  0.0633  72  TYR A CA  
568   C C   . TYR A 72  ? 0.2046 0.3011 0.1674 -0.0540 0.0112  0.0592  72  TYR A C   
569   O O   . TYR A 72  ? 0.2291 0.3249 0.1930 -0.0529 0.0087  0.0618  72  TYR A O   
570   C CB  . TYR A 72  ? 0.2349 0.3347 0.2006 -0.0553 0.0131  0.0679  72  TYR A CB  
571   C CG  . TYR A 72  ? 0.2812 0.3837 0.2478 -0.0545 0.0101  0.0749  72  TYR A CG  
572   C CD1 . TYR A 72  ? 0.2392 0.3523 0.2019 -0.0563 0.0076  0.0743  72  TYR A CD1 
573   C CD2 . TYR A 72  ? 0.2479 0.3431 0.2196 -0.0521 0.0099  0.0818  72  TYR A CD2 
574   C CE1 . TYR A 72  ? 0.2741 0.3916 0.2383 -0.0555 0.0048  0.0809  72  TYR A CE1 
575   C CE2 . TYR A 72  ? 0.2632 0.3618 0.2361 -0.0509 0.0072  0.0884  72  TYR A CE2 
576   C CZ  . TYR A 72  ? 0.2652 0.3755 0.2347 -0.0525 0.0046  0.0882  72  TYR A CZ  
577   O OH  . TYR A 72  ? 0.3882 0.5037 0.3595 -0.0512 0.0019  0.0949  72  TYR A OH  
578   N N   . ALA A 73  ? 0.2240 0.3262 0.1819 -0.0565 0.0128  0.0523  73  ALA A N   
579   C CA  . ALA A 73  ? 0.2100 0.3171 0.1629 -0.0585 0.0117  0.0473  73  ALA A CA  
580   C C   . ALA A 73  ? 0.2195 0.3212 0.1702 -0.0582 0.0141  0.0397  73  ALA A C   
581   O O   . ALA A 73  ? 0.2171 0.3198 0.1677 -0.0580 0.0169  0.0360  73  ALA A O   
582   C CB  . ALA A 73  ? 0.1735 0.2945 0.1212 -0.0624 0.0115  0.0453  73  ALA A CB  
583   N N   . GLY A 74  ? 0.1852 0.2820 0.1345 -0.0581 0.0131  0.0376  74  GLY A N   
584   C CA  . GLY A 74  ? 0.2397 0.3314 0.1855 -0.0581 0.0154  0.0304  74  GLY A CA  
585   C C   . GLY A 74  ? 0.2261 0.3079 0.1763 -0.0546 0.0170  0.0312  74  GLY A C   
586   O O   . GLY A 74  ? 0.2250 0.3026 0.1753 -0.0521 0.0185  0.0240  74  GLY A O   
587   N N   . SER A 75  ? 0.2035 0.2791 0.1601 -0.0518 0.0153  0.0376  75  SER A N   
588   C CA  . SER A 75  ? 0.1981 0.2651 0.1591 -0.0487 0.0165  0.0379  75  SER A CA  
589   C C   . SER A 75  ? 0.2478 0.3061 0.2077 -0.0462 0.0161  0.0317  75  SER A C   
590   O O   . SER A 75  ? 0.2376 0.2937 0.1948 -0.0472 0.0145  0.0309  75  SER A O   
591   C CB  . SER A 75  ? 0.2277 0.2886 0.1953 -0.0459 0.0146  0.0443  75  SER A CB  
592   O OG  . SER A 75  ? 0.2596 0.3119 0.2305 -0.0431 0.0151  0.0439  75  SER A OG  
593   N N   . ARG A 76  ? 0.2374 0.2905 0.1998 -0.0425 0.0173  0.0271  76  ARG A N   
594   C CA  A ARG A 76  ? 0.2409 0.2843 0.2029 -0.0388 0.0166  0.0218  76  ARG A CA  
595   C CA  B ARG A 76  ? 0.2344 0.2779 0.1962 -0.0389 0.0166  0.0217  76  ARG A CA  
596   C C   . ARG A 76  ? 0.2477 0.2837 0.2111 -0.0380 0.0148  0.0259  76  ARG A C   
597   O O   . ARG A 76  ? 0.2661 0.2955 0.2271 -0.0373 0.0139  0.0231  76  ARG A O   
598   C CB  A ARG A 76  ? 0.2779 0.3188 0.2436 -0.0344 0.0178  0.0181  76  ARG A CB  
599   C CB  B ARG A 76  ? 0.2780 0.3189 0.2430 -0.0344 0.0178  0.0173  76  ARG A CB  
600   C CG  A ARG A 76  ? 0.2776 0.3089 0.2429 -0.0296 0.0171  0.0132  76  ARG A CG  
601   C CG  B ARG A 76  ? 0.2843 0.3221 0.2549 -0.0323 0.0176  0.0213  76  ARG A CG  
602   C CD  A ARG A 76  ? 0.2652 0.2963 0.2348 -0.0252 0.0177  0.0109  76  ARG A CD  
603   C CD  B ARG A 76  ? 0.2658 0.3041 0.2395 -0.0285 0.0187  0.0164  76  ARG A CD  
604   N NE  A ARG A 76  ? 0.2809 0.3095 0.2548 -0.0245 0.0171  0.0158  76  ARG A NE  
605   N NE  B ARG A 76  ? 0.2471 0.2947 0.2234 -0.0310 0.0207  0.0168  76  ARG A NE  
606   C CZ  A ARG A 76  ? 0.2388 0.2727 0.2170 -0.0260 0.0181  0.0184  76  ARG A CZ  
607   C CZ  B ARG A 76  ? 0.2379 0.2938 0.2121 -0.0325 0.0223  0.0129  76  ARG A CZ  
608   N NH1 A ARG A 76  ? 0.2407 0.2832 0.2193 -0.0288 0.0199  0.0176  76  ARG A NH1 
609   N NH1 B ARG A 76  ? 0.2216 0.2772 0.1913 -0.0314 0.0222  0.0076  76  ARG A NH1 
610   N NH2 A ARG A 76  ? 0.2265 0.2569 0.2087 -0.0251 0.0175  0.0217  76  ARG A NH2 
611   N NH2 B ARG A 76  ? 0.2422 0.3070 0.2190 -0.0354 0.0243  0.0142  76  ARG A NH2 
612   N N   . ASN A 77  ? 0.1910 0.2278 0.1584 -0.0382 0.0144  0.0325  77  ASN A N   
613   C CA  . ASN A 77  ? 0.2197 0.2509 0.1891 -0.0370 0.0129  0.0362  77  ASN A CA  
614   C C   . ASN A 77  ? 0.2195 0.2544 0.1863 -0.0405 0.0114  0.0390  77  ASN A C   
615   O O   . ASN A 77  ? 0.1972 0.2279 0.1647 -0.0400 0.0103  0.0404  77  ASN A O   
616   C CB  . ASN A 77  ? 0.2255 0.2564 0.2008 -0.0355 0.0132  0.0413  77  ASN A CB  
617   C CG  . ASN A 77  ? 0.2327 0.2621 0.2110 -0.0331 0.0147  0.0382  77  ASN A CG  
618   O OD1 . ASN A 77  ? 0.2147 0.2494 0.1941 -0.0348 0.0160  0.0388  77  ASN A OD1 
619   N ND2 . ASN A 77  ? 0.1925 0.2157 0.1718 -0.0294 0.0145  0.0347  77  ASN A ND2 
620   N N   . TYR A 78  ? 0.2077 0.2515 0.1715 -0.0443 0.0113  0.0401  78  TYR A N   
621   C CA  . TYR A 78  ? 0.1842 0.2331 0.1450 -0.0480 0.0096  0.0415  78  TYR A CA  
622   C C   . TYR A 78  ? 0.1877 0.2306 0.1448 -0.0488 0.0094  0.0347  78  TYR A C   
623   O O   . TYR A 78  ? 0.2468 0.2873 0.2039 -0.0502 0.0082  0.0356  78  TYR A O   
624   C CB  . TYR A 78  ? 0.1899 0.2496 0.1485 -0.0506 0.0091  0.0420  78  TYR A CB  
625   C CG  . TYR A 78  ? 0.2136 0.2801 0.1677 -0.0552 0.0075  0.0406  78  TYR A CG  
626   C CD1 . TYR A 78  ? 0.1827 0.2521 0.1402 -0.0550 0.0047  0.0447  78  TYR A CD1 
627   C CD2 . TYR A 78  ? 0.2174 0.2872 0.1648 -0.0590 0.0085  0.0338  78  TYR A CD2 
628   C CE1 . TYR A 78  ? 0.1714 0.2486 0.1250 -0.0599 0.0032  0.0433  78  TYR A CE1 
629   C CE2 . TYR A 78  ? 0.2072 0.2832 0.1506 -0.0636 0.0070  0.0314  78  TYR A CE2 
630   C CZ  . TYR A 78  ? 0.1895 0.2704 0.1351 -0.0652 0.0046  0.0370  78  TYR A CZ  
631   O OH  . TYR A 78  ? 0.2429 0.3316 0.1846 -0.0705 0.0031  0.0344  78  TYR A OH  
632   N N   . TYR A 79  ? 0.2198 0.2597 0.1741 -0.0480 0.0108  0.0278  79  TYR A N   
633   C CA  . TYR A 79  ? 0.2087 0.2407 0.1599 -0.0483 0.0108  0.0211  79  TYR A CA  
634   C C   . TYR A 79  ? 0.2544 0.2748 0.2079 -0.0450 0.0105  0.0222  79  TYR A C   
635   O O   . TYR A 79  ? 0.2480 0.2625 0.1997 -0.0469 0.0098  0.0207  79  TYR A O   
636   C CB  . TYR A 79  ? 0.1843 0.2155 0.1329 -0.0468 0.0125  0.0136  79  TYR A CB  
637   C CG  . TYR A 79  ? 0.2554 0.2993 0.2008 -0.0506 0.0130  0.0120  79  TYR A CG  
638   C CD1 . TYR A 79  ? 0.2863 0.3352 0.2272 -0.0556 0.0123  0.0089  79  TYR A CD1 
639   C CD2 . TYR A 79  ? 0.2684 0.3202 0.2150 -0.0497 0.0144  0.0136  79  TYR A CD2 
640   C CE1 . TYR A 79  ? 0.2188 0.2810 0.1560 -0.0593 0.0127  0.0074  79  TYR A CE1 
641   C CE2 . TYR A 79  ? 0.2949 0.3595 0.2379 -0.0535 0.0152  0.0127  79  TYR A CE2 
642   C CZ  . TYR A 79  ? 0.2448 0.3148 0.1829 -0.0581 0.0142  0.0096  79  TYR A CZ  
643   O OH  . TYR A 79  ? 0.3678 0.4518 0.3015 -0.0620 0.0149  0.0086  79  TYR A OH  
644   N N   . ASP A 80  ? 0.2057 0.2233 0.1631 -0.0405 0.0109  0.0248  80  ASP A N   
645   C CA  . ASP A 80  ? 0.2077 0.2165 0.1671 -0.0375 0.0106  0.0265  80  ASP A CA  
646   C C   . ASP A 80  ? 0.2463 0.2570 0.2071 -0.0401 0.0094  0.0316  80  ASP A C   
647   O O   . ASP A 80  ? 0.2111 0.2153 0.1711 -0.0403 0.0092  0.0317  80  ASP A O   
648   C CB  . ASP A 80  ? 0.2611 0.2694 0.2247 -0.0329 0.0112  0.0281  80  ASP A CB  
649   C CG  . ASP A 80  ? 0.2834 0.2892 0.2465 -0.0292 0.0122  0.0227  80  ASP A CG  
650   O OD1 . ASP A 80  ? 0.3472 0.3507 0.3068 -0.0296 0.0125  0.0177  80  ASP A OD1 
651   O OD2 . ASP A 80  ? 0.3478 0.3542 0.3144 -0.0259 0.0126  0.0231  80  ASP A OD2 
652   N N   . LEU A 81  ? 0.2538 0.2736 0.2168 -0.0420 0.0088  0.0363  81  LEU A N   
653   C CA  . LEU A 81  ? 0.2407 0.2646 0.2058 -0.0440 0.0076  0.0412  81  LEU A CA  
654   C C   . LEU A 81  ? 0.2371 0.2624 0.1984 -0.0492 0.0068  0.0388  81  LEU A C   
655   O O   . LEU A 81  ? 0.2480 0.2721 0.2103 -0.0508 0.0062  0.0404  81  LEU A O   
656   C CB  . LEU A 81  ? 0.1726 0.2054 0.1418 -0.0433 0.0068  0.0458  81  LEU A CB  
657   C CG  . LEU A 81  ? 0.1694 0.2061 0.1437 -0.0418 0.0051  0.0492  81  LEU A CG  
658   C CD1 . LEU A 81  ? 0.1872 0.2174 0.1645 -0.0387 0.0057  0.0495  81  LEU A CD1 
659   C CD2 . LEU A 81  ? 0.1979 0.2402 0.1770 -0.0392 0.0042  0.0530  81  LEU A CD2 
660   N N   . LYS A 82  ? 0.2274 0.2560 0.1846 -0.0522 0.0068  0.0346  82  LYS A N   
661   C CA  . LYS A 82  ? 0.2565 0.2865 0.2101 -0.0577 0.0060  0.0309  82  LYS A CA  
662   C C   . LYS A 82  ? 0.2653 0.2822 0.2174 -0.0577 0.0068  0.0272  82  LYS A C   
663   O O   . LYS A 82  ? 0.2761 0.2921 0.2280 -0.0617 0.0062  0.0276  82  LYS A O   
664   C CB  . LYS A 82  ? 0.2468 0.2825 0.1960 -0.0604 0.0063  0.0258  82  LYS A CB  
665   C CG  . LYS A 82  ? 0.2501 0.2893 0.1955 -0.0667 0.0055  0.0211  82  LYS A CG  
666   C CD  . LYS A 82  ? 0.2871 0.3348 0.2282 -0.0690 0.0058  0.0164  82  LYS A CD  
667   C CE  . LYS A 82  ? 0.3226 0.3636 0.2594 -0.0720 0.0067  0.0066  82  LYS A CE  
668   N NZ  . LYS A 82  ? 0.2864 0.3281 0.2221 -0.0783 0.0054  0.0048  82  LYS A NZ  
669   N N   . ASP A 83  ? 0.2644 0.2713 0.2156 -0.0533 0.0081  0.0239  83  ASP A N   
670   C CA  . ASP A 83  ? 0.2765 0.2700 0.2263 -0.0523 0.0087  0.0216  83  ASP A CA  
671   C C   . ASP A 83  ? 0.2549 0.2462 0.2074 -0.0515 0.0085  0.0273  83  ASP A C   
672   O O   . ASP A 83  ? 0.3015 0.2863 0.2527 -0.0545 0.0086  0.0272  83  ASP A O   
673   C CB  . ASP A 83  ? 0.2840 0.2692 0.2330 -0.0463 0.0098  0.0181  83  ASP A CB  
674   C CG  . ASP A 83  ? 0.3560 0.3438 0.3025 -0.0467 0.0104  0.0116  83  ASP A CG  
675   O OD1 . ASP A 83  ? 0.3560 0.3487 0.3000 -0.0522 0.0101  0.0086  83  ASP A OD1 
676   O OD2 . ASP A 83  ? 0.4156 0.4019 0.3627 -0.0417 0.0113  0.0092  83  ASP A OD2 
677   N N   . LYS A 84  ? 0.2394 0.2361 0.1959 -0.0479 0.0083  0.0321  84  LYS A N   
678   C CA  . LYS A 84  ? 0.2631 0.2589 0.2224 -0.0467 0.0083  0.0367  84  LYS A CA  
679   C C   . LYS A 84  ? 0.2860 0.2885 0.2463 -0.0523 0.0076  0.0392  84  LYS A C   
680   O O   . LYS A 84  ? 0.3217 0.3208 0.2821 -0.0538 0.0080  0.0410  84  LYS A O   
681   C CB  . LYS A 84  ? 0.2198 0.2204 0.1836 -0.0419 0.0084  0.0402  84  LYS A CB  
682   C CG  . LYS A 84  ? 0.2460 0.2446 0.2121 -0.0393 0.0089  0.0435  84  LYS A CG  
683   C CD  . LYS A 84  ? 0.3025 0.2903 0.2655 -0.0364 0.0096  0.0414  84  LYS A CD  
684   C CE  . LYS A 84  ? 0.3470 0.3345 0.3117 -0.0340 0.0101  0.0447  84  LYS A CE  
685   N NZ  . LYS A 84  ? 0.3971 0.3750 0.3583 -0.0307 0.0106  0.0437  84  LYS A NZ  
686   N N   . ALA A 85  ? 0.2535 0.2667 0.2144 -0.0555 0.0065  0.0397  85  ALA A N   
687   C CA  . ALA A 85  ? 0.1739 0.1958 0.1361 -0.0609 0.0054  0.0417  85  ALA A CA  
688   C C   . ALA A 85  ? 0.2479 0.2635 0.2062 -0.0668 0.0057  0.0372  85  ALA A C   
689   O O   . ALA A 85  ? 0.2668 0.2842 0.2263 -0.0709 0.0057  0.0388  85  ALA A O   
690   C CB  . ALA A 85  ? 0.2059 0.2415 0.1692 -0.0626 0.0038  0.0434  85  ALA A CB  
691   N N   . LYS A 86  ? 0.2680 0.2761 0.2220 -0.0675 0.0062  0.0314  86  LYS A N   
692   C CA  . LYS A 86  ? 0.2831 0.2818 0.2335 -0.0727 0.0068  0.0266  86  LYS A CA  
693   C C   . LYS A 86  ? 0.3281 0.3143 0.2785 -0.0711 0.0081  0.0288  86  LYS A C   
694   O O   . LYS A 86  ? 0.3492 0.3311 0.2988 -0.0766 0.0086  0.0285  86  LYS A O   
695   C CB  . LYS A 86  ? 0.3194 0.3113 0.2657 -0.0722 0.0074  0.0194  86  LYS A CB  
696   C CG  . LYS A 86  ? 0.3397 0.3195 0.2828 -0.0770 0.0082  0.0137  86  LYS A CG  
697   C CD  . LYS A 86  ? 0.4001 0.3887 0.3433 -0.0859 0.0073  0.0128  86  LYS A CD  
698   C CE  . LYS A 86  ? 0.3528 0.3303 0.2927 -0.0919 0.0082  0.0055  86  LYS A CE  
699   N NZ  . LYS A 86  ? 0.3553 0.3416 0.2963 -0.1012 0.0073  0.0051  86  LYS A NZ  
700   N N   . GLU A 87  ? 0.2989 0.2797 0.2501 -0.0639 0.0087  0.0312  87  GLU A N   
701   C CA  . GLU A 87  ? 0.2830 0.2530 0.2334 -0.0618 0.0099  0.0338  87  GLU A CA  
702   C C   . GLU A 87  ? 0.3327 0.3097 0.2861 -0.0645 0.0100  0.0392  87  GLU A C   
703   O O   . GLU A 87  ? 0.3736 0.3443 0.3256 -0.0683 0.0110  0.0406  87  GLU A O   
704   C CB  . GLU A 87  ? 0.3086 0.2743 0.2593 -0.0535 0.0102  0.0348  87  GLU A CB  
705   C CG  . GLU A 87  ? 0.3943 0.3533 0.3446 -0.0507 0.0110  0.0389  87  GLU A CG  
706   C CD  . GLU A 87  ? 0.4275 0.3882 0.3795 -0.0431 0.0109  0.0405  87  GLU A CD  
707   O OE1 . GLU A 87  ? 0.4286 0.3916 0.3815 -0.0396 0.0105  0.0377  87  GLU A OE1 
708   O OE2 . GLU A 87  ? 0.4491 0.4098 0.4016 -0.0411 0.0114  0.0444  87  GLU A OE2 
709   N N   . LEU A 88  ? 0.2970 0.2871 0.2549 -0.0625 0.0092  0.0424  88  LEU A N   
710   C CA  . LEU A 88  ? 0.2711 0.2689 0.2343 -0.0606 0.0091  0.0451  88  LEU A CA  
711   C C   . LEU A 88  ? 0.2967 0.3023 0.2614 -0.0674 0.0084  0.0447  88  LEU A C   
712   O O   . LEU A 88  ? 0.2272 0.2332 0.1934 -0.0690 0.0092  0.0458  88  LEU A O   
713   C CB  . LEU A 88  ? 0.2987 0.3061 0.2673 -0.0543 0.0084  0.0470  88  LEU A CB  
714   C CG  . LEU A 88  ? 0.3195 0.3214 0.2883 -0.0474 0.0093  0.0476  88  LEU A CG  
715   C CD1 . LEU A 88  ? 0.2470 0.2577 0.2211 -0.0429 0.0087  0.0487  88  LEU A CD1 
716   C CD2 . LEU A 88  ? 0.3550 0.3524 0.3233 -0.0457 0.0107  0.0489  88  LEU A CD2 
717   N N   . PHE A 89  ? 0.2981 0.3116 0.2624 -0.0717 0.0070  0.0430  89  PHE A N   
718   C CA  . PHE A 89  ? 0.3319 0.3573 0.2986 -0.0776 0.0057  0.0429  89  PHE A CA  
719   C C   . PHE A 89  ? 0.3159 0.3377 0.2780 -0.0869 0.0058  0.0385  89  PHE A C   
720   O O   . PHE A 89  ? 0.2749 0.3057 0.2387 -0.0928 0.0049  0.0376  89  PHE A O   
721   C CB  . PHE A 89  ? 0.2572 0.2981 0.2279 -0.0753 0.0036  0.0450  89  PHE A CB  
722   C CG  . PHE A 89  ? 0.2710 0.3133 0.2462 -0.0664 0.0036  0.0483  89  PHE A CG  
723   C CD1 . PHE A 89  ? 0.2648 0.3086 0.2441 -0.0630 0.0044  0.0505  89  PHE A CD1 
724   C CD2 . PHE A 89  ? 0.2458 0.2882 0.2209 -0.0620 0.0031  0.0488  89  PHE A CD2 
725   C CE1 . PHE A 89  ? 0.2643 0.3091 0.2476 -0.0556 0.0047  0.0527  89  PHE A CE1 
726   C CE2 . PHE A 89  ? 0.2276 0.2703 0.2070 -0.0547 0.0034  0.0512  89  PHE A CE2 
727   C CZ  . PHE A 89  ? 0.2228 0.2664 0.2062 -0.0516 0.0042  0.0529  89  PHE A CZ  
728   N N   . ASN A 90  ? 0.2707 0.2800 0.2274 -0.0883 0.0069  0.0350  90  ASN A N   
729   C CA  . ASN A 90  ? 0.2998 0.3042 0.2527 -0.0950 0.0068  0.0282  90  ASN A CA  
730   C C   . ASN A 90  ? 0.3399 0.3604 0.2932 -0.0982 0.0047  0.0258  90  ASN A C   
731   O O   . ASN A 90  ? 0.4242 0.4477 0.3758 -0.1059 0.0042  0.0207  90  ASN A O   
732   C CB  . ASN A 90  ? 0.3790 0.3779 0.3317 -0.1030 0.0079  0.0276  90  ASN A CB  
733   C CG  . ASN A 90  ? 0.4041 0.3884 0.3522 -0.1079 0.0089  0.0203  90  ASN A CG  
734   O OD1 . ASN A 90  ? 0.3901 0.3660 0.3351 -0.1038 0.0090  0.0159  90  ASN A OD1 
735   N ND2 . ASN A 90  ? 0.3624 0.3435 0.3106 -0.1168 0.0096  0.0187  90  ASN A ND2 
736   N N   . TYR A 91  ? 0.2800 0.3110 0.2355 -0.0926 0.0035  0.0294  91  TYR A N   
737   C CA  . TYR A 91  ? 0.2817 0.3288 0.2372 -0.0946 0.0014  0.0288  91  TYR A CA  
738   C C   . TYR A 91  ? 0.2849 0.3279 0.2361 -0.0917 0.0017  0.0243  91  TYR A C   
739   O O   . TYR A 91  ? 0.2551 0.2886 0.2060 -0.0851 0.0029  0.0251  91  TYR A O   
740   C CB  . TYR A 91  ? 0.2835 0.3451 0.2443 -0.0903 0.0000  0.0365  91  TYR A CB  
741   C CG  . TYR A 91  ? 0.3020 0.3724 0.2679 -0.0923 -0.0009 0.0398  91  TYR A CG  
742   C CD1 . TYR A 91  ? 0.2480 0.3122 0.2134 -0.0978 0.0001  0.0371  91  TYR A CD1 
743   C CD2 . TYR A 91  ? 0.2777 0.3618 0.2494 -0.0873 -0.0030 0.0452  91  TYR A CD2 
744   C CE1 . TYR A 91  ? 0.2691 0.3418 0.2392 -0.0985 -0.0007 0.0394  91  TYR A CE1 
745   C CE2 . TYR A 91  ? 0.2510 0.3437 0.2277 -0.0880 -0.0039 0.0474  91  TYR A CE2 
746   C CZ  . TYR A 91  ? 0.2487 0.3362 0.2244 -0.0937 -0.0027 0.0443  91  TYR A CZ  
747   O OH  . TYR A 91  ? 0.2398 0.3368 0.2203 -0.0947 -0.0033 0.0464  91  TYR A OH  
748   N N   . ASP A 92  ? 0.3097 0.3616 0.2579 -0.0969 0.0005  0.0193  92  ASP A N   
749   C CA  . ASP A 92  ? 0.3116 0.3606 0.2551 -0.0958 0.0011  0.0132  92  ASP A CA  
750   C C   . ASP A 92  ? 0.3203 0.3825 0.2637 -0.0921 0.0000  0.0170  92  ASP A C   
751   O O   . ASP A 92  ? 0.3579 0.4190 0.2976 -0.0907 0.0009  0.0125  92  ASP A O   
752   C CB  . ASP A 92  ? 0.3178 0.3692 0.2573 -0.1041 0.0008  0.0044  92  ASP A CB  
753   C CG  . ASP A 92  ? 0.3732 0.4075 0.3118 -0.1080 0.0024  -0.0007 92  ASP A CG  
754   O OD1 . ASP A 92  ? 0.4021 0.4198 0.3409 -0.1028 0.0043  0.0002  92  ASP A OD1 
755   O OD2 . ASP A 92  ? 0.4278 0.4656 0.3656 -0.1164 0.0019  -0.0054 92  ASP A OD2 
756   N N   . TYR A 93  ? 0.3028 0.3777 0.2502 -0.0905 -0.0017 0.0250  93  TYR A N   
757   C CA  . TYR A 93  ? 0.2660 0.3536 0.2131 -0.0879 -0.0028 0.0294  93  TYR A CA  
758   C C   . TYR A 93  ? 0.2829 0.3713 0.2358 -0.0814 -0.0030 0.0386  93  TYR A C   
759   O O   . TYR A 93  ? 0.2803 0.3699 0.2378 -0.0811 -0.0036 0.0426  93  TYR A O   
760   C CB  . TYR A 93  ? 0.3092 0.4159 0.2547 -0.0937 -0.0055 0.0296  93  TYR A CB  
761   C CG  . TYR A 93  ? 0.3522 0.4600 0.2922 -0.1009 -0.0054 0.0196  93  TYR A CG  
762   C CD1 . TYR A 93  ? 0.3993 0.5052 0.3339 -0.1008 -0.0041 0.0133  93  TYR A CD1 
763   C CD2 . TYR A 93  ? 0.3467 0.4583 0.2871 -0.1081 -0.0065 0.0158  93  TYR A CD2 
764   C CE1 . TYR A 93  ? 0.4011 0.5078 0.3307 -0.1071 -0.0039 0.0031  93  TYR A CE1 
765   C CE2 . TYR A 93  ? 0.3948 0.5067 0.3303 -0.1152 -0.0063 0.0057  93  TYR A CE2 
766   C CZ  . TYR A 93  ? 0.4094 0.5185 0.3394 -0.1144 -0.0050 -0.0009 93  TYR A CZ  
767   O OH  . TYR A 93  ? 0.4901 0.5992 0.4154 -0.1210 -0.0046 -0.0119 93  TYR A OH  
768   N N   . ILE A 94  ? 0.2565 0.3442 0.2093 -0.0765 -0.0023 0.0415  94  ILE A N   
769   C CA  . ILE A 94  ? 0.2640 0.3500 0.2241 -0.0687 -0.0030 0.0478  94  ILE A CA  
770   C C   . ILE A 94  ? 0.2562 0.3514 0.2180 -0.0659 -0.0046 0.0514  94  ILE A C   
771   O O   . ILE A 94  ? 0.2268 0.3263 0.1835 -0.0685 -0.0041 0.0487  94  ILE A O   
772   C CB  . ILE A 94  ? 0.2410 0.3117 0.2026 -0.0636 -0.0005 0.0469  94  ILE A CB  
773   C CG1 . ILE A 94  ? 0.2192 0.2861 0.1760 -0.0634 0.0015  0.0436  94  ILE A CG1 
774   C CG2 . ILE A 94  ? 0.2789 0.3402 0.2391 -0.0661 0.0008  0.0442  94  ILE A CG2 
775   C CD1 . ILE A 94  ? 0.2318 0.2897 0.1926 -0.0567 0.0028  0.0451  94  ILE A CD1 
776   N N   . ILE A 95  ? 0.2168 0.3155 0.1858 -0.0609 -0.0061 0.0575  95  ILE A N   
777   C CA  . ILE A 95  ? 0.1999 0.3031 0.1719 -0.0570 -0.0069 0.0621  95  ILE A CA  
778   C C   . ILE A 95  ? 0.2718 0.3663 0.2508 -0.0503 -0.0061 0.0658  95  ILE A C   
779   O O   . ILE A 95  ? 0.2761 0.3725 0.2600 -0.0484 -0.0070 0.0686  95  ILE A O   
780   C CB  . ILE A 95  ? 0.2137 0.3335 0.1872 -0.0590 -0.0100 0.0664  95  ILE A CB  
781   C CG1 . ILE A 95  ? 0.2180 0.3480 0.1847 -0.0667 -0.0110 0.0618  95  ILE A CG1 
782   C CG2 . ILE A 95  ? 0.1732 0.2964 0.1488 -0.0557 -0.0103 0.0712  95  ILE A CG2 
783   C CD1 . ILE A 95  ? 0.2586 0.4067 0.2274 -0.0690 -0.0142 0.0658  95  ILE A CD1 
784   N N   . PRO A 96  ? 0.2064 0.2921 0.1861 -0.0468 -0.0041 0.0655  96  PRO A N   
785   C CA  . PRO A 96  ? 0.1588 0.2371 0.1448 -0.0411 -0.0032 0.0685  96  PRO A CA  
786   C C   . PRO A 96  ? 0.1953 0.2810 0.1866 -0.0386 -0.0049 0.0755  96  PRO A C   
787   O O   . PRO A 96  ? 0.1739 0.2694 0.1638 -0.0406 -0.0064 0.0782  96  PRO A O   
788   C CB  . PRO A 96  ? 0.1960 0.2649 0.1804 -0.0397 -0.0007 0.0659  96  PRO A CB  
789   C CG  . PRO A 96  ? 0.1937 0.2683 0.1722 -0.0438 -0.0007 0.0636  96  PRO A CG  
790   C CD  . PRO A 96  ? 0.2119 0.2944 0.1864 -0.0485 -0.0023 0.0616  96  PRO A CD  
791   N N   . ALA A 97  ? 0.2202 0.3017 0.2178 -0.0341 -0.0044 0.0786  97  ALA A N   
792   C CA  . ALA A 97  ? 0.2033 0.2902 0.2068 -0.0309 -0.0056 0.0857  97  ALA A CA  
793   C C   . ALA A 97  ? 0.2126 0.2885 0.2210 -0.0262 -0.0035 0.0869  97  ALA A C   
794   O O   . ALA A 97  ? 0.2465 0.3135 0.2546 -0.0254 -0.0016 0.0826  97  ALA A O   
795   C CB  . ALA A 97  ? 0.2399 0.3381 0.2472 -0.0307 -0.0077 0.0893  97  ALA A CB  
796   N N   . HIS A 98  ? 0.1705 0.2469 0.1833 -0.0233 -0.0036 0.0930  98  HIS A N   
797   C CA  . HIS A 98  ? 0.1438 0.2090 0.1612 -0.0196 -0.0014 0.0938  98  HIS A CA  
798   C C   . HIS A 98  ? 0.1810 0.2447 0.2041 -0.0160 -0.0010 0.0944  98  HIS A C   
799   O O   . HIS A 98  ? 0.1768 0.2308 0.2022 -0.0140 0.0012  0.0921  98  HIS A O   
800   C CB  . HIS A 98  ? 0.1818 0.2461 0.2022 -0.0177 -0.0014 0.1002  98  HIS A CB  
801   C CG  . HIS A 98  ? 0.2253 0.2962 0.2521 -0.0140 -0.0030 0.1075  98  HIS A CG  
802   N ND1 . HIS A 98  ? 0.2332 0.3174 0.2592 -0.0151 -0.0055 0.1116  98  HIS A ND1 
803   C CD2 . HIS A 98  ? 0.2241 0.2906 0.2586 -0.0089 -0.0022 0.1116  98  HIS A CD2 
804   C CE1 . HIS A 98  ? 0.2523 0.3404 0.2852 -0.0106 -0.0063 0.1180  98  HIS A CE1 
805   N NE2 . HIS A 98  ? 0.2317 0.3087 0.2698 -0.0066 -0.0043 0.1181  98  HIS A NE2 
806   N N   . GLN A 99  ? 0.1708 0.2449 0.1962 -0.0155 -0.0028 0.0972  99  GLN A N   
807   C CA  . GLN A 99  ? 0.1684 0.2432 0.1984 -0.0129 -0.0022 0.0972  99  GLN A CA  
808   C C   . GLN A 99  ? 0.1795 0.2688 0.2102 -0.0144 -0.0045 0.0996  99  GLN A C   
809   O O   . GLN A 99  ? 0.1530 0.2507 0.1797 -0.0182 -0.0066 0.0998  99  GLN A O   
810   C CB  . GLN A 99  ? 0.1770 0.2459 0.2151 -0.0070 -0.0007 0.1016  99  GLN A CB  
811   C CG  . GLN A 99  ? 0.1870 0.2613 0.2306 -0.0034 -0.0021 0.1094  99  GLN A CG  
812   C CD  . GLN A 99  ? 0.2203 0.2857 0.2720 0.0027  -0.0002 0.1125  99  GLN A CD  
813   O OE1 . GLN A 99  ? 0.2487 0.3020 0.3005 0.0029  0.0017  0.1108  99  GLN A OE1 
814   N NE2 . GLN A 99  ? 0.2613 0.3326 0.3201 0.0077  -0.0006 0.1164  99  GLN A NE2 
815   N N   . GLY A 100 ? 0.1615 0.2548 0.1974 -0.0116 -0.0041 0.1015  100 GLY A N   
816   C CA  . GLY A 100 ? 0.1791 0.2866 0.2152 -0.0141 -0.0060 0.1027  100 GLY A CA  
817   C C   . GLY A 100 ? 0.1761 0.2976 0.2145 -0.0139 -0.0088 0.1087  100 GLY A C   
818   O O   . GLY A 100 ? 0.1721 0.3046 0.2068 -0.0190 -0.0109 0.1077  100 GLY A O   
819   N N   . ARG A 101 ? 0.1574 0.2787 0.2022 -0.0080 -0.0088 0.1149  101 ARG A N   
820   C CA  . ARG A 101 ? 0.1476 0.2821 0.1946 -0.0073 -0.0113 0.1208  101 ARG A CA  
821   C C   . ARG A 101 ? 0.1896 0.3245 0.2301 -0.0118 -0.0124 0.1199  101 ARG A C   
822   O O   . ARG A 101 ? 0.1815 0.3299 0.2216 -0.0134 -0.0147 0.1234  101 ARG A O   
823   C CB  . ARG A 101 ? 0.1783 0.3107 0.2338 0.0007  -0.0108 0.1275  101 ARG A CB  
824   C CG  . ARG A 101 ? 0.1882 0.3040 0.2438 0.0031  -0.0089 0.1280  101 ARG A CG  
825   C CD  . ARG A 101 ? 0.2181 0.3280 0.2828 0.0113  -0.0077 0.1325  101 ARG A CD  
826   N NE  . ARG A 101 ? 0.2375 0.3407 0.3057 0.0139  -0.0056 0.1287  101 ARG A NE  
827   C CZ  . ARG A 101 ? 0.2052 0.3017 0.2815 0.0212  -0.0041 0.1303  101 ARG A CZ  
828   N NH1 . ARG A 101 ? 0.1933 0.2880 0.2752 0.0266  -0.0045 0.1357  101 ARG A NH1 
829   N NH2 . ARG A 101 ? 0.2074 0.2987 0.2864 0.0231  -0.0021 0.1261  101 ARG A NH2 
830   N N   . GLY A 102 ? 0.1781 0.2996 0.2134 -0.0138 -0.0108 0.1152  102 GLY A N   
831   C CA  . GLY A 102 ? 0.1809 0.3046 0.2091 -0.0188 -0.0118 0.1131  102 GLY A CA  
832   C C   . GLY A 102 ? 0.1936 0.3268 0.2163 -0.0250 -0.0134 0.1083  102 GLY A C   
833   O O   . GLY A 102 ? 0.2002 0.3450 0.2198 -0.0287 -0.0154 0.1093  102 GLY A O   
834   N N   . ALA A 103 ? 0.2262 0.3548 0.2477 -0.0266 -0.0124 0.1031  103 ALA A N   
835   C CA  . ALA A 103 ? 0.1928 0.3287 0.2091 -0.0329 -0.0136 0.0984  103 ALA A CA  
836   C C   . ALA A 103 ? 0.2362 0.3915 0.2557 -0.0345 -0.0164 0.1028  103 ALA A C   
837   O O   . ALA A 103 ? 0.2128 0.3786 0.2277 -0.0405 -0.0182 0.1007  103 ALA A O   
838   C CB  . ALA A 103 ? 0.2104 0.3369 0.2258 -0.0335 -0.0117 0.0933  103 ALA A CB  
839   N N   . GLU A 104 ? 0.2377 0.3989 0.2652 -0.0293 -0.0165 0.1088  104 GLU A N   
840   C CA  . GLU A 104 ? 0.1930 0.3740 0.2243 -0.0300 -0.0189 0.1134  104 GLU A CA  
841   C C   . GLU A 104 ? 0.2535 0.4434 0.2837 -0.0305 -0.0206 0.1172  104 GLU A C   
842   O O   . GLU A 104 ? 0.2468 0.4530 0.2754 -0.0350 -0.0227 0.1174  104 GLU A O   
843   C CB  . GLU A 104 ? 0.2026 0.3868 0.2430 -0.0229 -0.0183 0.1190  104 GLU A CB  
844   C CG  . GLU A 104 ? 0.2006 0.3797 0.2423 -0.0226 -0.0166 0.1159  104 GLU A CG  
845   C CD  . GLU A 104 ? 0.2320 0.4089 0.2826 -0.0139 -0.0152 0.1206  104 GLU A CD  
846   O OE1 . GLU A 104 ? 0.2570 0.4310 0.3122 -0.0078 -0.0151 0.1255  104 GLU A OE1 
847   O OE2 . GLU A 104 ? 0.2639 0.4416 0.3167 -0.0132 -0.0142 0.1193  104 GLU A OE2 
848   N N   . ASN A 105 ? 0.2007 0.3804 0.2314 -0.0263 -0.0196 0.1202  105 ASN A N   
849   C CA  . ASN A 105 ? 0.2178 0.4054 0.2470 -0.0267 -0.0210 0.1243  105 ASN A CA  
850   C C   . ASN A 105 ? 0.2070 0.3985 0.2275 -0.0343 -0.0218 0.1187  105 ASN A C   
851   O O   . ASN A 105 ? 0.2841 0.4888 0.3027 -0.0367 -0.0235 0.1210  105 ASN A O   
852   C CB  . ASN A 105 ? 0.2515 0.4261 0.2829 -0.0211 -0.0195 0.1288  105 ASN A CB  
853   C CG  . ASN A 105 ? 0.3076 0.4909 0.3385 -0.0204 -0.0209 0.1352  105 ASN A CG  
854   O OD1 . ASN A 105 ? 0.2716 0.4717 0.3035 -0.0212 -0.0230 0.1385  105 ASN A OD1 
855   N ND2 . ASN A 105 ? 0.2820 0.4544 0.3110 -0.0191 -0.0197 0.1370  105 ASN A ND2 
856   N N   . ILE A 106 ? 0.2723 0.4526 0.2876 -0.0378 -0.0206 0.1112  106 ILE A N   
857   C CA  . ILE A 106 ? 0.2628 0.4463 0.2697 -0.0449 -0.0211 0.1050  106 ILE A CA  
858   C C   . ILE A 106 ? 0.2826 0.4820 0.2879 -0.0511 -0.0231 0.1024  106 ILE A C   
859   O O   . ILE A 106 ? 0.3042 0.5168 0.3059 -0.0557 -0.0245 0.1017  106 ILE A O   
860   C CB  . ILE A 106 ? 0.2677 0.4336 0.2693 -0.0462 -0.0188 0.0978  106 ILE A CB  
861   C CG1 . ILE A 106 ? 0.2334 0.3872 0.2347 -0.0423 -0.0169 0.0994  106 ILE A CG1 
862   C CG2 . ILE A 106 ? 0.2566 0.4264 0.2499 -0.0539 -0.0192 0.0905  106 ILE A CG2 
863   C CD1 . ILE A 106 ? 0.1959 0.3330 0.1933 -0.0426 -0.0142 0.0928  106 ILE A CD1 
864   N N   . LEU A 107 ? 0.2435 0.4426 0.2514 -0.0516 -0.0230 0.1009  107 LEU A N   
865   C CA  . LEU A 107 ? 0.2303 0.4411 0.2351 -0.0592 -0.0243 0.0965  107 LEU A CA  
866   C C   . LEU A 107 ? 0.2588 0.4903 0.2690 -0.0596 -0.0261 0.1014  107 LEU A C   
867   O O   . LEU A 107 ? 0.2077 0.4534 0.2144 -0.0665 -0.0272 0.0985  107 LEU A O   
868   C CB  . LEU A 107 ? 0.2583 0.4576 0.2617 -0.0608 -0.0229 0.0917  107 LEU A CB  
869   C CG  . LEU A 107 ? 0.1982 0.4067 0.1977 -0.0697 -0.0239 0.0866  107 LEU A CG  
870   C CD1 . LEU A 107 ? 0.2053 0.4139 0.1955 -0.0775 -0.0240 0.0796  107 LEU A CD1 
871   C CD2 . LEU A 107 ? 0.1915 0.3875 0.1911 -0.0698 -0.0218 0.0836  107 LEU A CD2 
872   N N   . PHE A 108 ? 0.2267 0.4602 0.2451 -0.0522 -0.0259 0.1083  108 PHE A N   
873   C CA  . PHE A 108 ? 0.2180 0.4707 0.2410 -0.0520 -0.0271 0.1124  108 PHE A CA  
874   C C   . PHE A 108 ? 0.2145 0.4819 0.2354 -0.0538 -0.0286 0.1147  108 PHE A C   
875   O O   . PHE A 108 ? 0.1893 0.4720 0.2075 -0.0599 -0.0296 0.1121  108 PHE A O   
876   C CB  . PHE A 108 ? 0.2221 0.4727 0.2539 -0.0427 -0.0264 0.1191  108 PHE A CB  
877   C CG  . PHE A 108 ? 0.2516 0.4953 0.2861 -0.0420 -0.0251 0.1168  108 PHE A CG  
878   C CD1 . PHE A 108 ? 0.2387 0.4756 0.2675 -0.0490 -0.0246 0.1097  108 PHE A CD1 
879   C CD2 . PHE A 108 ? 0.2673 0.5112 0.3099 -0.0342 -0.0242 0.1216  108 PHE A CD2 
880   C CE1 . PHE A 108 ? 0.2940 0.5250 0.3248 -0.0485 -0.0234 0.1081  108 PHE A CE1 
881   C CE2 . PHE A 108 ? 0.2760 0.5150 0.3210 -0.0334 -0.0229 0.1194  108 PHE A CE2 
882   C CZ  . PHE A 108 ? 0.2274 0.4606 0.2665 -0.0408 -0.0226 0.1132  108 PHE A CZ  
883   N N   . PRO A 109 ? 0.2547 0.5187 0.2758 -0.0494 -0.0288 0.1194  109 PRO A N   
884   C CA  . PRO A 109 ? 0.2755 0.5552 0.2941 -0.0515 -0.0303 0.1218  109 PRO A CA  
885   C C   . PRO A 109 ? 0.2677 0.5542 0.2781 -0.0613 -0.0307 0.1137  109 PRO A C   
886   O O   . PRO A 109 ? 0.2699 0.5739 0.2782 -0.0652 -0.0319 0.1134  109 PRO A O   
887   C CB  . PRO A 109 ? 0.2324 0.5028 0.2516 -0.0458 -0.0300 0.1274  109 PRO A CB  
888   C CG  . PRO A 109 ? 0.2381 0.4911 0.2627 -0.0388 -0.0283 0.1299  109 PRO A CG  
889   C CD  . PRO A 109 ? 0.2350 0.4810 0.2581 -0.0427 -0.0274 0.1226  109 PRO A CD  
890   N N   . VAL A 110 ? 0.2218 0.4944 0.2270 -0.0652 -0.0295 0.1067  110 VAL A N   
891   C CA  . VAL A 110 ? 0.2325 0.5092 0.2294 -0.0746 -0.0295 0.0980  110 VAL A CA  
892   C C   . VAL A 110 ? 0.2841 0.5726 0.2803 -0.0807 -0.0297 0.0941  110 VAL A C   
893   O O   . VAL A 110 ? 0.2331 0.5350 0.2246 -0.0871 -0.0301 0.0901  110 VAL A O   
894   C CB  . VAL A 110 ? 0.2436 0.5010 0.2353 -0.0764 -0.0280 0.0914  110 VAL A CB  
895   C CG1 . VAL A 110 ? 0.3000 0.5599 0.2836 -0.0862 -0.0275 0.0815  110 VAL A CG1 
896   C CG2 . VAL A 110 ? 0.2476 0.4961 0.2377 -0.0722 -0.0273 0.0936  110 VAL A CG2 
897   N N   . LEU A 111 ? 0.2733 0.5569 0.2738 -0.0790 -0.0293 0.0950  111 LEU A N   
898   C CA  . LEU A 111 ? 0.2319 0.5251 0.2310 -0.0848 -0.0293 0.0913  111 LEU A CA  
899   C C   . LEU A 111 ? 0.2495 0.5631 0.2517 -0.0834 -0.0307 0.0958  111 LEU A C   
900   O O   . LEU A 111 ? 0.1811 0.5062 0.1793 -0.0900 -0.0311 0.0908  111 LEU A O   
901   C CB  . LEU A 111 ? 0.1920 0.4759 0.1950 -0.0825 -0.0285 0.0921  111 LEU A CB  
902   C CG  . LEU A 111 ? 0.2149 0.4798 0.2145 -0.0850 -0.0273 0.0871  111 LEU A CG  
903   C CD1 . LEU A 111 ? 0.2360 0.4951 0.2400 -0.0821 -0.0266 0.0891  111 LEU A CD1 
904   C CD2 . LEU A 111 ? 0.2424 0.5041 0.2315 -0.0952 -0.0267 0.0774  111 LEU A CD2 
905   N N   . LEU A 112 ? 0.2255 0.5432 0.2344 -0.0746 -0.0316 0.1047  112 LEU A N   
906   C CA  . LEU A 112 ? 0.2149 0.5522 0.2267 -0.0725 -0.0332 0.1095  112 LEU A CA  
907   C C   . LEU A 112 ? 0.2773 0.6275 0.2829 -0.0785 -0.0340 0.1064  112 LEU A C   
908   O O   . LEU A 112 ? 0.2505 0.6170 0.2541 -0.0831 -0.0349 0.1038  112 LEU A O   
909   C CB  . LEU A 112 ? 0.1687 0.5049 0.1884 -0.0616 -0.0338 0.1198  112 LEU A CB  
910   C CG  . LEU A 112 ? 0.2629 0.6192 0.2854 -0.0585 -0.0357 0.1257  112 LEU A CG  
911   C CD1 . LEU A 112 ? 0.2613 0.6308 0.2857 -0.0608 -0.0363 0.1232  112 LEU A CD1 
912   C CD2 . LEU A 112 ? 0.2736 0.6259 0.3031 -0.0476 -0.0362 0.1357  112 LEU A CD2 
913   N N   . LYS A 113 ? 0.2717 0.6152 0.2739 -0.0786 -0.0338 0.1062  113 LYS A N   
914   C CA  . LYS A 113 ? 0.3073 0.6645 0.3037 -0.0840 -0.0345 0.1033  113 LYS A CA  
915   C C   . LYS A 113 ? 0.3055 0.6635 0.2941 -0.0945 -0.0334 0.0917  113 LYS A C   
916   O O   . LYS A 113 ? 0.3008 0.6748 0.2856 -0.0999 -0.0341 0.0880  113 LYS A O   
917   C CB  . LYS A 113 ? 0.3312 0.6821 0.3258 -0.0811 -0.0345 0.1063  113 LYS A CB  
918   C CG  . LYS A 113 ? 0.4173 0.7464 0.4100 -0.0807 -0.0328 0.1028  113 LYS A CG  
919   C CD  . LYS A 113 ? 0.4929 0.8175 0.4845 -0.0767 -0.0329 0.1073  113 LYS A CD  
920   C CE  . LYS A 113 ? 0.2914 0.5945 0.2804 -0.0760 -0.0313 0.1035  113 LYS A CE  
921   N NZ  . LYS A 113 ? 0.3432 0.6424 0.3251 -0.0842 -0.0301 0.0923  113 LYS A NZ  
922   N N   . TYR A 114 ? 0.2643 0.6050 0.2502 -0.0975 -0.0318 0.0856  114 TYR A N   
923   C CA  . TYR A 114 ? 0.3212 0.6601 0.2996 -0.1072 -0.0307 0.0744  114 TYR A CA  
924   C C   . TYR A 114 ? 0.3645 0.7168 0.3437 -0.1108 -0.0315 0.0725  114 TYR A C   
925   O O   . TYR A 114 ? 0.3500 0.7112 0.3239 -0.1184 -0.0314 0.0648  114 TYR A O   
926   C CB  . TYR A 114 ? 0.3129 0.6299 0.2890 -0.1085 -0.0291 0.0697  114 TYR A CB  
927   C CG  . TYR A 114 ? 0.3757 0.6864 0.3435 -0.1181 -0.0277 0.0576  114 TYR A CG  
928   C CD1 . TYR A 114 ? 0.4509 0.7576 0.4118 -0.1226 -0.0266 0.0501  114 TYR A CD1 
929   C CD2 . TYR A 114 ? 0.4669 0.7747 0.4343 -0.1222 -0.0276 0.0534  114 TYR A CD2 
930   C CE1 . TYR A 114 ? 0.4502 0.7492 0.4043 -0.1307 -0.0252 0.0384  114 TYR A CE1 
931   C CE2 . TYR A 114 ? 0.4720 0.7716 0.4331 -0.1307 -0.0263 0.0420  114 TYR A CE2 
932   C CZ  . TYR A 114 ? 0.4836 0.7783 0.4381 -0.1347 -0.0251 0.0345  114 TYR A CZ  
933   O OH  . TYR A 114 ? 0.6515 0.9366 0.6008 -0.1427 -0.0236 0.0227  114 TYR A OH  
934   N N   . LYS A 115 ? 0.3351 0.6892 0.3213 -0.1054 -0.0322 0.0789  115 LYS A N   
935   C CA  . LYS A 115 ? 0.3170 0.6832 0.3044 -0.1087 -0.0330 0.0766  115 LYS A CA  
936   C C   . LYS A 115 ? 0.3455 0.7351 0.3333 -0.1095 -0.0347 0.0784  115 LYS A C   
937   O O   . LYS A 115 ? 0.3511 0.7519 0.3363 -0.1162 -0.0351 0.0723  115 LYS A O   
938   C CB  . LYS A 115 ? 0.2791 0.6428 0.2744 -0.1017 -0.0333 0.0831  115 LYS A CB  
939   C CG  . LYS A 115 ? 0.2472 0.6220 0.2443 -0.1052 -0.0340 0.0801  115 LYS A CG  
940   C CD  . LYS A 115 ? 0.3224 0.6828 0.3156 -0.1123 -0.0326 0.0713  115 LYS A CD  
941   C CE  . LYS A 115 ? 0.2793 0.6508 0.2754 -0.1160 -0.0332 0.0683  115 LYS A CE  
942   N NZ  . LYS A 115 ? 0.2215 0.5774 0.2154 -0.1223 -0.0316 0.0606  115 LYS A NZ  
943   N N   . GLN A 116 ? 0.3609 0.7579 0.3518 -0.1030 -0.0357 0.0867  116 GLN A N   
944   C CA  . GLN A 116 ? 0.3664 0.7863 0.3580 -0.1028 -0.0376 0.0898  116 GLN A CA  
945   C C   . GLN A 116 ? 0.3537 0.7798 0.3387 -0.1078 -0.0375 0.0856  116 GLN A C   
946   O O   . GLN A 116 ? 0.4163 0.8598 0.4021 -0.1058 -0.0391 0.0905  116 GLN A O   
947   C CB  . GLN A 116 ? 0.3464 0.7723 0.3462 -0.0918 -0.0392 0.1023  116 GLN A CB  
948   C CG  . GLN A 116 ? 0.3332 0.7450 0.3352 -0.0848 -0.0387 0.1089  116 GLN A CG  
949   C CD  . GLN A 116 ? 0.3460 0.7607 0.3564 -0.0739 -0.0401 0.1204  116 GLN A CD  
950   O OE1 . GLN A 116 ? 0.3610 0.7696 0.3734 -0.0677 -0.0403 0.1274  116 GLN A OE1 
951   N NE2 . GLN A 116 ? 0.2779 0.7016 0.2933 -0.0713 -0.0409 0.1222  116 GLN A NE2 
952   N N   . LYS A 117 ? 0.3549 0.7679 0.3332 -0.1143 -0.0356 0.0764  117 LYS A N   
953   C CA  . LYS A 117 ? 0.3804 0.7987 0.3524 -0.1189 -0.0352 0.0715  117 LYS A CA  
954   C C   . LYS A 117 ? 0.4782 0.9171 0.4466 -0.1260 -0.0359 0.0654  117 LYS A C   
955   O O   . LYS A 117 ? 0.5394 0.9887 0.5037 -0.1287 -0.0361 0.0632  117 LYS A O   
956   C CB  . LYS A 117 ? 0.4395 0.8376 0.4055 -0.1235 -0.0328 0.0625  117 LYS A CB  
957   C CG  . LYS A 117 ? 0.4612 0.8516 0.4232 -0.1315 -0.0315 0.0515  117 LYS A CG  
958   C CD  . LYS A 117 ? 0.4496 0.8168 0.4068 -0.1341 -0.0293 0.0443  117 LYS A CD  
959   C CE  . LYS A 117 ? 0.5125 0.8798 0.4637 -0.1371 -0.0281 0.0383  117 LYS A CE  
960   N NZ  . LYS A 117 ? 0.5680 0.9127 0.5145 -0.1394 -0.0259 0.0305  117 LYS A NZ  
961   N N   . GLU A 118 ? 0.4782 0.9236 0.4480 -0.1294 -0.0364 0.0623  118 GLU A N   
962   C CA  . GLU A 118 ? 0.5532 1.0187 0.5203 -0.1364 -0.0372 0.0560  118 GLU A CA  
963   C C   . GLU A 118 ? 0.5869 1.0735 0.5601 -0.1318 -0.0398 0.0643  118 GLU A C   
964   O O   . GLU A 118 ? 0.6007 1.1007 0.5739 -0.1370 -0.0405 0.0596  118 GLU A O   
965   C CB  . GLU A 118 ? 0.5822 1.0388 0.5454 -0.1456 -0.0357 0.0436  118 GLU A CB  
966   C CG  . GLU A 118 ? 0.7512 1.1970 0.7067 -0.1527 -0.0335 0.0323  118 GLU A CG  
967   C CD  . GLU A 118 ? 0.9431 1.3742 0.8956 -0.1608 -0.0317 0.0207  118 GLU A CD  
968   O OE1 . GLU A 118 ? 0.8982 1.3132 0.8534 -0.1587 -0.0312 0.0224  118 GLU A OE1 
969   O OE2 . GLU A 118 ? 1.0700 1.5056 1.0180 -0.1691 -0.0309 0.0098  118 GLU A OE2 
970   N N   . GLY A 119 ? 0.4744 0.9637 0.4531 -0.1220 -0.0411 0.0766  119 GLY A N   
971   C CA  . GLY A 119 ? 0.4880 0.9969 0.4728 -0.1164 -0.0436 0.0851  119 GLY A CA  
972   C C   . GLY A 119 ? 0.4681 0.9768 0.4583 -0.1149 -0.0440 0.0857  119 GLY A C   
973   O O   . GLY A 119 ? 0.4925 1.0205 0.4870 -0.1123 -0.0461 0.0898  119 GLY A O   
974   N N   . LYS A 120 ? 0.4173 0.9057 0.4076 -0.1162 -0.0422 0.0816  120 LYS A N   
975   C CA  . LYS A 120 ? 0.4292 0.9164 0.4250 -0.1141 -0.0424 0.0827  120 LYS A CA  
976   C C   . LYS A 120 ? 0.3082 0.7795 0.3101 -0.1041 -0.0419 0.0913  120 LYS A C   
977   O O   . LYS A 120 ? 0.3269 0.7914 0.3296 -0.0982 -0.0419 0.0977  120 LYS A O   
978   C CB  . LYS A 120 ? 0.3911 0.8691 0.3826 -0.1241 -0.0408 0.0709  120 LYS A CB  
979   C CG  . LYS A 120 ? 0.4598 0.9119 0.4467 -0.1267 -0.0384 0.0659  120 LYS A CG  
980   C CD  . LYS A 120 ? 0.5627 1.0055 0.5467 -0.1357 -0.0370 0.0553  120 LYS A CD  
981   C CE  . LYS A 120 ? 0.4841 0.9000 0.4652 -0.1364 -0.0350 0.0521  120 LYS A CE  
982   N NZ  . LYS A 120 ? 0.4155 0.8220 0.4023 -0.1262 -0.0351 0.0619  120 LYS A NZ  
983   N N   . ALA A 121 ? 0.3049 0.7709 0.3115 -0.1022 -0.0416 0.0914  121 ALA A N   
984   C CA  . ALA A 121 ? 0.2636 0.7163 0.2768 -0.0924 -0.0411 0.0990  121 ALA A CA  
985   C C   . ALA A 121 ? 0.3035 0.7662 0.3231 -0.0818 -0.0429 0.1103  121 ALA A C   
986   O O   . ALA A 121 ? 0.3034 0.7533 0.3257 -0.0744 -0.0424 0.1168  121 ALA A O   
987   C CB  . ALA A 121 ? 0.3338 0.7622 0.3436 -0.0927 -0.0390 0.0972  121 ALA A CB  
988   N N   . LYS A 122 ? 0.2853 0.7708 0.3074 -0.0810 -0.0450 0.1126  122 LYS A N   
989   C CA  . LYS A 122 ? 0.2521 0.7482 0.2801 -0.0708 -0.0470 0.1235  122 LYS A CA  
990   C C   . LYS A 122 ? 0.2341 0.7235 0.2712 -0.0603 -0.0470 0.1301  122 LYS A C   
991   O O   . LYS A 122 ? 0.2704 0.7599 0.3125 -0.0505 -0.0481 0.1395  122 LYS A O   
992   C CB  . LYS A 122 ? 0.2392 0.7626 0.2670 -0.0731 -0.0495 0.1237  122 LYS A CB  
993   C CG  . LYS A 122 ? 0.3209 0.8535 0.3401 -0.0851 -0.0493 0.1143  122 LYS A CG  
994   C CD  . LYS A 122 ? 0.3905 0.9208 0.4041 -0.0862 -0.0492 0.1159  122 LYS A CD  
995   C CE  . LYS A 122 ? 0.3281 0.8789 0.3439 -0.0806 -0.0520 0.1246  122 LYS A CE  
996   N NZ  . LYS A 122 ? 0.4405 0.9889 0.4512 -0.0813 -0.0518 0.1267  122 LYS A NZ  
997   N N   . ASN A 123 ? 0.2263 0.7099 0.2658 -0.0621 -0.0458 0.1252  123 ASN A N   
998   C CA  . ASN A 123 ? 0.2116 0.6877 0.2597 -0.0527 -0.0452 0.1299  123 ASN A CA  
999   C C   . ASN A 123 ? 0.2273 0.6805 0.2738 -0.0552 -0.0425 0.1252  123 ASN A C   
1000  O O   . ASN A 123 ? 0.1969 0.6482 0.2447 -0.0584 -0.0415 0.1200  123 ASN A O   
1001  C CB  . ASN A 123 ? 0.2158 0.7098 0.2696 -0.0519 -0.0464 0.1286  123 ASN A CB  
1002  C CG  . ASN A 123 ? 0.2846 0.8036 0.3391 -0.0512 -0.0493 0.1319  123 ASN A CG  
1003  O OD1 . ASN A 123 ? 0.2751 0.7976 0.3304 -0.0450 -0.0508 0.1396  123 ASN A OD1 
1004  N ND2 . ASN A 123 ? 0.2850 0.8217 0.3392 -0.0578 -0.0501 0.1261  123 ASN A ND2 
1005  N N   . PRO A 124 ? 0.2383 0.6740 0.2820 -0.0536 -0.0414 0.1272  124 PRO A N   
1006  C CA  . PRO A 124 ? 0.2376 0.6526 0.2778 -0.0577 -0.0390 0.1218  124 PRO A CA  
1007  C C   . PRO A 124 ? 0.2349 0.6382 0.2824 -0.0502 -0.0376 0.1242  124 PRO A C   
1008  O O   . PRO A 124 ? 0.2425 0.6442 0.2971 -0.0398 -0.0380 0.1316  124 PRO A O   
1009  C CB  . PRO A 124 ? 0.2181 0.6214 0.2539 -0.0576 -0.0385 0.1238  124 PRO A CB  
1010  C CG  . PRO A 124 ? 0.2165 0.6272 0.2575 -0.0483 -0.0401 0.1334  124 PRO A CG  
1011  C CD  . PRO A 124 ? 0.2596 0.6938 0.3030 -0.0483 -0.0423 0.1344  124 PRO A CD  
1012  N N   . VAL A 125 ? 0.1980 0.5924 0.2437 -0.0556 -0.0360 0.1175  125 VAL A N   
1013  C CA  . VAL A 125 ? 0.2076 0.5912 0.2596 -0.0497 -0.0344 0.1185  125 VAL A CA  
1014  C C   . VAL A 125 ? 0.2231 0.5869 0.2700 -0.0548 -0.0324 0.1133  125 VAL A C   
1015  O O   . VAL A 125 ? 0.1596 0.5198 0.1982 -0.0643 -0.0324 0.1073  125 VAL A O   
1016  C CB  . VAL A 125 ? 0.2675 0.6643 0.3248 -0.0499 -0.0345 0.1159  125 VAL A CB  
1017  C CG1 . VAL A 125 ? 0.2527 0.6701 0.3154 -0.0444 -0.0367 0.1210  125 VAL A CG1 
1018  C CG2 . VAL A 125 ? 0.2280 0.6274 0.2787 -0.0623 -0.0342 0.1069  125 VAL A CG2 
1019  N N   . PHE A 126 ? 0.2022 0.5529 0.2543 -0.0480 -0.0308 0.1156  126 PHE A N   
1020  C CA  . PHE A 126 ? 0.1919 0.5253 0.2412 -0.0514 -0.0289 0.1110  126 PHE A CA  
1021  C C   . PHE A 126 ? 0.2123 0.5476 0.2677 -0.0496 -0.0275 0.1087  126 PHE A C   
1022  O O   . PHE A 126 ? 0.2076 0.5508 0.2714 -0.0413 -0.0274 0.1127  126 PHE A O   
1023  C CB  . PHE A 126 ? 0.2248 0.5414 0.2757 -0.0450 -0.0278 0.1152  126 PHE A CB  
1024  C CG  . PHE A 126 ? 0.2778 0.5888 0.3221 -0.0481 -0.0284 0.1159  126 PHE A CG  
1025  C CD1 . PHE A 126 ? 0.2372 0.5579 0.2818 -0.0456 -0.0299 0.1205  126 PHE A CD1 
1026  C CD2 . PHE A 126 ? 0.2609 0.5567 0.2991 -0.0532 -0.0274 0.1118  126 PHE A CD2 
1027  C CE1 . PHE A 126 ? 0.2204 0.5364 0.2596 -0.0484 -0.0302 0.1206  126 PHE A CE1 
1028  C CE2 . PHE A 126 ? 0.2192 0.5103 0.2522 -0.0558 -0.0278 0.1116  126 PHE A CE2 
1029  C CZ  . PHE A 126 ? 0.2271 0.5282 0.2606 -0.0535 -0.0291 0.1158  126 PHE A CZ  
1030  N N   . ILE A 127 ? 0.1688 0.4959 0.2200 -0.0572 -0.0262 0.1019  127 ILE A N   
1031  C CA  . ILE A 127 ? 0.1710 0.4988 0.2273 -0.0568 -0.0243 0.0990  127 ILE A CA  
1032  C C   . ILE A 127 ? 0.1646 0.4726 0.2200 -0.0565 -0.0218 0.0967  127 ILE A C   
1033  O O   . ILE A 127 ? 0.2306 0.5254 0.2786 -0.0626 -0.0216 0.0932  127 ILE A O   
1034  C CB  . ILE A 127 ? 0.1892 0.5261 0.2420 -0.0668 -0.0245 0.0925  127 ILE A CB  
1035  C CG1 . ILE A 127 ? 0.2605 0.6181 0.3140 -0.0676 -0.0269 0.0943  127 ILE A CG1 
1036  C CG2 . ILE A 127 ? 0.2002 0.5382 0.2585 -0.0663 -0.0221 0.0900  127 ILE A CG2 
1037  C CD1 . ILE A 127 ? 0.1789 0.5464 0.2295 -0.0777 -0.0271 0.0878  127 ILE A CD1 
1038  N N   . SER A 128 ? 0.1480 0.4542 0.2111 -0.0492 -0.0196 0.0983  128 SER A N   
1039  C CA  . SER A 128 ? 0.1564 0.4452 0.2193 -0.0482 -0.0167 0.0962  128 SER A CA  
1040  C C   . SER A 128 ? 0.1445 0.4368 0.2134 -0.0458 -0.0139 0.0940  128 SER A C   
1041  O O   . SER A 128 ? 0.1703 0.4779 0.2458 -0.0415 -0.0142 0.0956  128 SER A O   
1042  C CB  . SER A 128 ? 0.1929 0.4722 0.2591 -0.0395 -0.0165 0.1014  128 SER A CB  
1043  O OG  . SER A 128 ? 0.1818 0.4442 0.2468 -0.0395 -0.0136 0.0988  128 SER A OG  
1044  N N   . ASN A 129 ? 0.1515 0.4295 0.2179 -0.0482 -0.0108 0.0901  129 ASN A N   
1045  C CA  . ASN A 129 ? 0.1996 0.4800 0.2721 -0.0440 -0.0076 0.0889  129 ASN A CA  
1046  C C   . ASN A 129 ? 0.2168 0.5012 0.2986 -0.0318 -0.0072 0.0935  129 ASN A C   
1047  O O   . ASN A 129 ? 0.1706 0.4672 0.2598 -0.0265 -0.0064 0.0938  129 ASN A O   
1048  C CB  . ASN A 129 ? 0.1474 0.4106 0.2149 -0.0478 -0.0042 0.0846  129 ASN A CB  
1049  C CG  . ASN A 129 ? 0.1729 0.4179 0.2363 -0.0460 -0.0038 0.0854  129 ASN A CG  
1050  O OD1 . ASN A 129 ? 0.1854 0.4288 0.2471 -0.0454 -0.0063 0.0881  129 ASN A OD1 
1051  N ND2 . ASN A 129 ? 0.2114 0.4428 0.2727 -0.0453 -0.0004 0.0829  129 ASN A ND2 
1052  N N   . PHE A 130 ? 0.1921 0.4663 0.2739 -0.0271 -0.0079 0.0971  130 PHE A N   
1053  C CA  . PHE A 130 ? 0.1945 0.4712 0.2847 -0.0156 -0.0085 0.1022  130 PHE A CA  
1054  C C   . PHE A 130 ? 0.1832 0.4480 0.2708 -0.0135 -0.0101 0.1062  130 PHE A C   
1055  O O   . PHE A 130 ? 0.2090 0.4594 0.2945 -0.0142 -0.0081 0.1047  130 PHE A O   
1056  C CB  . PHE A 130 ? 0.2147 0.4883 0.3123 -0.0078 -0.0049 0.1003  130 PHE A CB  
1057  C CG  . PHE A 130 ? 0.2425 0.5252 0.3498 0.0031  -0.0054 0.1033  130 PHE A CG  
1058  C CD1 . PHE A 130 ? 0.2527 0.5292 0.3634 0.0112  -0.0071 0.1086  130 PHE A CD1 
1059  C CD2 . PHE A 130 ? 0.2821 0.5785 0.3949 0.0051  -0.0042 0.1007  130 PHE A CD2 
1060  C CE1 . PHE A 130 ? 0.2474 0.5296 0.3666 0.0214  -0.0076 0.1111  130 PHE A CE1 
1061  C CE2 . PHE A 130 ? 0.2904 0.5945 0.4124 0.0154  -0.0047 0.1029  130 PHE A CE2 
1062  C CZ  . PHE A 130 ? 0.3008 0.5971 0.4260 0.0238  -0.0064 0.1081  130 PHE A CZ  
1063  N N   . HIS A 131 ? 0.2019 0.4727 0.2892 -0.0115 -0.0133 0.1112  131 HIS A N   
1064  C CA  . HIS A 131 ? 0.1875 0.4472 0.2728 -0.0084 -0.0147 0.1157  131 HIS A CA  
1065  C C   . HIS A 131 ? 0.1911 0.4392 0.2835 0.0022  -0.0127 0.1177  131 HIS A C   
1066  O O   . HIS A 131 ? 0.2371 0.4900 0.3373 0.0104  -0.0120 0.1189  131 HIS A O   
1067  C CB  . HIS A 131 ? 0.2198 0.4887 0.3039 -0.0070 -0.0178 0.1209  131 HIS A CB  
1068  C CG  . HIS A 131 ? 0.2102 0.4910 0.2872 -0.0170 -0.0198 0.1188  131 HIS A CG  
1069  N ND1 . HIS A 131 ? 0.1822 0.4795 0.2609 -0.0193 -0.0205 0.1170  131 HIS A ND1 
1070  C CD2 . HIS A 131 ? 0.2513 0.5298 0.3194 -0.0250 -0.0213 0.1177  131 HIS A CD2 
1071  C CE1 . HIS A 131 ? 0.1879 0.4920 0.2590 -0.0286 -0.0223 0.1147  131 HIS A CE1 
1072  N NE2 . HIS A 131 ? 0.2030 0.4959 0.2676 -0.0321 -0.0228 0.1149  131 HIS A NE2 
1073  N N   . PHE A 132 ? 0.2213 0.4536 0.3111 0.0022  -0.0118 0.1176  132 PHE A N   
1074  C CA  . PHE A 132 ? 0.2434 0.4626 0.3388 0.0121  -0.0102 0.1195  132 PHE A CA  
1075  C C   . PHE A 132 ? 0.2367 0.4533 0.3328 0.0175  -0.0121 0.1258  132 PHE A C   
1076  O O   . PHE A 132 ? 0.2929 0.5185 0.3847 0.0135  -0.0146 0.1286  132 PHE A O   
1077  C CB  . PHE A 132 ? 0.3255 0.5230 0.4140 0.0096  -0.0076 0.1154  132 PHE A CB  
1078  C CG  . PHE A 132 ? 0.3297 0.5131 0.4238 0.0185  -0.0048 0.1145  132 PHE A CG  
1079  C CD1 . PHE A 132 ? 0.3345 0.5241 0.4377 0.0246  -0.0026 0.1118  132 PHE A CD1 
1080  C CD2 . PHE A 132 ? 0.3315 0.4966 0.4223 0.0203  -0.0043 0.1158  132 PHE A CD2 
1081  C CE1 . PHE A 132 ? 0.3493 0.5263 0.4580 0.0327  0.0000  0.1100  132 PHE A CE1 
1082  C CE2 . PHE A 132 ? 0.3431 0.4954 0.4395 0.0277  -0.0018 0.1143  132 PHE A CE2 
1083  C CZ  . PHE A 132 ? 0.3002 0.4580 0.4055 0.0340  0.0004  0.1111  132 PHE A CZ  
1084  N N   . ASP A 133 ? 0.2456 0.4495 0.3471 0.0264  -0.0106 0.1277  133 ASP A N   
1085  C CA  . ASP A 133 ? 0.2714 0.4743 0.3756 0.0323  -0.0120 0.1336  133 ASP A CA  
1086  C C   . ASP A 133 ? 0.2952 0.4932 0.3913 0.0271  -0.0138 0.1374  133 ASP A C   
1087  O O   . ASP A 133 ? 0.2395 0.4480 0.3344 0.0264  -0.0160 0.1414  133 ASP A O   
1088  C CB  . ASP A 133 ? 0.3117 0.5007 0.4238 0.0423  -0.0099 0.1339  133 ASP A CB  
1089  C CG  . ASP A 133 ? 0.4717 0.6397 0.5806 0.0419  -0.0080 0.1329  133 ASP A CG  
1090  O OD1 . ASP A 133 ? 0.5079 0.6727 0.6104 0.0351  -0.0075 0.1297  133 ASP A OD1 
1091  O OD2 . ASP A 133 ? 0.5272 0.6817 0.6399 0.0481  -0.0070 0.1351  133 ASP A OD2 
1092  N N   . THR A 134 ? 0.3151 0.4981 0.4052 0.0233  -0.0126 0.1356  134 THR A N   
1093  C CA  . THR A 134 ? 0.3069 0.4861 0.3892 0.0180  -0.0138 0.1377  134 THR A CA  
1094  C C   . THR A 134 ? 0.2343 0.4296 0.3105 0.0094  -0.0161 0.1364  134 THR A C   
1095  O O   . THR A 134 ? 0.2362 0.4376 0.3089 0.0068  -0.0179 0.1392  134 THR A O   
1096  C CB  . THR A 134 ? 0.3298 0.4903 0.4066 0.0151  -0.0119 0.1344  134 THR A CB  
1097  O OG1 . THR A 134 ? 0.2326 0.3941 0.3035 0.0082  -0.0116 0.1290  134 THR A OG1 
1098  C CG2 . THR A 134 ? 0.3599 0.5045 0.4429 0.0225  -0.0093 0.1342  134 THR A CG2 
1099  N N   . THR A 135 ? 0.2588 0.4609 0.3335 0.0047  -0.0161 0.1318  135 THR A N   
1100  C CA  . THR A 135 ? 0.2669 0.4842 0.3363 -0.0040 -0.0181 0.1296  135 THR A CA  
1101  C C   . THR A 135 ? 0.2671 0.5019 0.3400 -0.0021 -0.0200 0.1333  135 THR A C   
1102  O O   . THR A 135 ? 0.2352 0.4781 0.3036 -0.0064 -0.0218 0.1348  135 THR A O   
1103  C CB  . THR A 135 ? 0.2522 0.4735 0.3211 -0.0088 -0.0175 0.1244  135 THR A CB  
1104  O OG1 . THR A 135 ? 0.2462 0.4500 0.3132 -0.0077 -0.0153 0.1218  135 THR A OG1 
1105  C CG2 . THR A 135 ? 0.2431 0.4735 0.3041 -0.0198 -0.0192 0.1207  135 THR A CG2 
1106  N N   . ALA A 136 ? 0.2221 0.4635 0.3033 0.0046  -0.0195 0.1344  136 ALA A N   
1107  C CA  . ALA A 136 ? 0.2144 0.4722 0.2994 0.0075  -0.0214 0.1379  136 ALA A CA  
1108  C C   . ALA A 136 ? 0.2850 0.5397 0.3700 0.0120  -0.0226 0.1445  136 ALA A C   
1109  O O   . ALA A 136 ? 0.2857 0.5547 0.3696 0.0107  -0.0248 0.1474  136 ALA A O   
1110  C CB  . ALA A 136 ? 0.2653 0.5282 0.3596 0.0151  -0.0203 0.1373  136 ALA A CB  
1111  N N   . ALA A 137 ? 0.2647 0.5012 0.3510 0.0170  -0.0212 0.1467  137 ALA A N   
1112  C CA  . ALA A 137 ? 0.3210 0.5534 0.4072 0.0207  -0.0222 0.1530  137 ALA A CA  
1113  C C   . ALA A 137 ? 0.3141 0.5514 0.3916 0.0125  -0.0236 0.1532  137 ALA A C   
1114  O O   . ALA A 137 ? 0.2868 0.5334 0.3636 0.0133  -0.0256 0.1581  137 ALA A O   
1115  C CB  . ALA A 137 ? 0.3593 0.5698 0.4481 0.0265  -0.0200 0.1544  137 ALA A CB  
1116  N N   . HIS A 138 ? 0.3086 0.5403 0.3795 0.0047  -0.0228 0.1475  138 HIS A N   
1117  C CA  . HIS A 138 ? 0.2893 0.5262 0.3522 -0.0032 -0.0241 0.1461  138 HIS A CA  
1118  C C   . HIS A 138 ? 0.2627 0.5214 0.3238 -0.0084 -0.0263 0.1451  138 HIS A C   
1119  O O   . HIS A 138 ? 0.2600 0.5284 0.3173 -0.0117 -0.0280 0.1469  138 HIS A O   
1120  C CB  . HIS A 138 ? 0.2703 0.4947 0.3269 -0.0095 -0.0228 0.1395  138 HIS A CB  
1121  C CG  . HIS A 138 ? 0.2570 0.4618 0.3130 -0.0062 -0.0210 0.1403  138 HIS A CG  
1122  N ND1 . HIS A 138 ? 0.2304 0.4321 0.2833 -0.0064 -0.0215 0.1433  138 HIS A ND1 
1123  C CD2 . HIS A 138 ? 0.2546 0.4424 0.3128 -0.0026 -0.0186 0.1384  138 HIS A CD2 
1124  C CE1 . HIS A 138 ? 0.2336 0.4171 0.2866 -0.0036 -0.0195 0.1431  138 HIS A CE1 
1125  N NE2 . HIS A 138 ? 0.2384 0.4130 0.2946 -0.0013 -0.0177 0.1399  138 HIS A NE2 
1126  N N   . VAL A 139 ? 0.2891 0.5560 0.3528 -0.0095 -0.0262 0.1419  139 VAL A N   
1127  C CA  . VAL A 139 ? 0.2937 0.5814 0.3562 -0.0142 -0.0280 0.1407  139 VAL A CA  
1128  C C   . VAL A 139 ? 0.2384 0.5380 0.3047 -0.0082 -0.0299 0.1477  139 VAL A C   
1129  O O   . VAL A 139 ? 0.2387 0.5509 0.3010 -0.0124 -0.0317 0.1487  139 VAL A O   
1130  C CB  . VAL A 139 ? 0.2650 0.5585 0.3308 -0.0151 -0.0273 0.1366  139 VAL A CB  
1131  C CG1 . VAL A 139 ? 0.2588 0.5736 0.3249 -0.0180 -0.0292 0.1360  139 VAL A CG1 
1132  C CG2 . VAL A 139 ? 0.2533 0.5382 0.3135 -0.0231 -0.0260 0.1297  139 VAL A CG2 
1133  N N   . GLU A 140 ? 0.2839 0.5795 0.3583 0.0018  -0.0295 0.1524  140 GLU A N   
1134  C CA  . GLU A 140 ? 0.2251 0.5312 0.3038 0.0085  -0.0315 0.1594  140 GLU A CA  
1135  C C   . GLU A 140 ? 0.3140 0.6145 0.3891 0.0093  -0.0323 0.1649  140 GLU A C   
1136  O O   . GLU A 140 ? 0.2812 0.5956 0.3558 0.0101  -0.0346 0.1696  140 GLU A O   
1137  C CB  . GLU A 140 ? 0.3298 0.6305 0.4181 0.0194  -0.0308 0.1623  140 GLU A CB  
1138  C CG  . GLU A 140 ? 0.2975 0.6070 0.3902 0.0194  -0.0301 0.1571  140 GLU A CG  
1139  C CD  . GLU A 140 ? 0.3611 0.6602 0.4627 0.0293  -0.0284 0.1575  140 GLU A CD  
1140  O OE1 . GLU A 140 ? 0.4256 0.7080 0.5294 0.0355  -0.0275 0.1611  140 GLU A OE1 
1141  O OE2 . GLU A 140 ? 0.4131 0.7208 0.5198 0.0308  -0.0278 0.1537  140 GLU A OE2 
1142  N N   . LEU A 141 ? 0.2720 0.5533 0.3448 0.0090  -0.0305 0.1643  141 LEU A N   
1143  C CA  . LEU A 141 ? 0.2829 0.5587 0.3521 0.0093  -0.0311 0.1692  141 LEU A CA  
1144  C C   . LEU A 141 ? 0.3077 0.5977 0.3694 0.0006  -0.0327 0.1673  141 LEU A C   
1145  O O   . LEU A 141 ? 0.3203 0.6144 0.3796 0.0011  -0.0340 0.1725  141 LEU A O   
1146  C CB  . LEU A 141 ? 0.3135 0.5664 0.3811 0.0095  -0.0286 0.1675  141 LEU A CB  
1147  C CG  . LEU A 141 ? 0.3798 0.6223 0.4461 0.0124  -0.0286 0.1735  141 LEU A CG  
1148  C CD1 . LEU A 141 ? 0.3841 0.6282 0.4571 0.0218  -0.0297 0.1819  141 LEU A CD1 
1149  C CD2 . LEU A 141 ? 0.4211 0.6413 0.4867 0.0126  -0.0259 0.1703  141 LEU A CD2 
1150  N N   . ASN A 142 ? 0.3126 0.6101 0.3702 -0.0075 -0.0326 0.1598  142 ASN A N   
1151  C CA  . ASN A 142 ? 0.3247 0.6367 0.3754 -0.0161 -0.0340 0.1568  142 ASN A CA  
1152  C C   . ASN A 142 ? 0.3327 0.6677 0.3848 -0.0169 -0.0362 0.1579  142 ASN A C   
1153  O O   . ASN A 142 ? 0.3390 0.6875 0.3855 -0.0250 -0.0371 0.1536  142 ASN A O   
1154  C CB  . ASN A 142 ? 0.2147 0.5206 0.2594 -0.0251 -0.0327 0.1475  142 ASN A CB  
1155  C CG  . ASN A 142 ? 0.2926 0.5805 0.3334 -0.0261 -0.0314 0.1460  142 ASN A CG  
1156  O OD1 . ASN A 142 ? 0.2858 0.5764 0.3215 -0.0293 -0.0321 0.1463  142 ASN A OD1 
1157  N ND2 . ASN A 142 ? 0.2640 0.5341 0.3069 -0.0233 -0.0294 0.1441  142 ASN A ND2 
1158  N N   . GLY A 143 ? 0.2560 0.5958 0.3155 -0.0085 -0.0370 0.1634  143 GLY A N   
1159  C CA  . GLY A 143 ? 0.2594 0.6215 0.3206 -0.0084 -0.0392 0.1649  143 GLY A CA  
1160  C C   . GLY A 143 ? 0.2767 0.6487 0.3379 -0.0141 -0.0389 0.1575  143 GLY A C   
1161  O O   . GLY A 143 ? 0.3639 0.7557 0.4240 -0.0174 -0.0407 0.1565  143 GLY A O   
1162  N N   . CYS A 144 ? 0.2433 0.6022 0.3053 -0.0154 -0.0368 0.1525  144 CYS A N   
1163  C CA  . CYS A 144 ? 0.2731 0.6392 0.3346 -0.0211 -0.0363 0.1455  144 CYS A CA  
1164  C C   . CYS A 144 ? 0.2659 0.6301 0.3363 -0.0132 -0.0355 0.1466  144 CYS A C   
1165  O O   . CYS A 144 ? 0.3151 0.6677 0.3912 -0.0039 -0.0348 0.1516  144 CYS A O   
1166  C CB  . CYS A 144 ? 0.2488 0.6025 0.3036 -0.0299 -0.0345 0.1379  144 CYS A CB  
1167  S SG  . CYS A 144 ? 0.3284 0.6835 0.3730 -0.0396 -0.0350 0.1345  144 CYS A SG  
1168  N N   . LYS A 145 ? 0.2529 0.6280 0.3241 -0.0173 -0.0355 0.1414  145 LYS A N   
1169  C CA  . LYS A 145 ? 0.2881 0.6623 0.3672 -0.0114 -0.0343 0.1406  145 LYS A CA  
1170  C C   . LYS A 145 ? 0.2797 0.6391 0.3567 -0.0159 -0.0317 0.1345  145 LYS A C   
1171  O O   . LYS A 145 ? 0.2303 0.5876 0.2995 -0.0260 -0.0314 0.1289  145 LYS A O   
1172  C CB  . LYS A 145 ? 0.3044 0.7005 0.3866 -0.0131 -0.0357 0.1385  145 LYS A CB  
1173  C CG  . LYS A 145 ? 0.3339 0.7313 0.4245 -0.0078 -0.0343 0.1365  145 LYS A CG  
1174  C CD  . LYS A 145 ? 0.3693 0.7900 0.4637 -0.0086 -0.0359 0.1353  145 LYS A CD  
1175  C CE  . LYS A 145 ? 0.4510 0.8743 0.5550 -0.0016 -0.0345 0.1340  145 LYS A CE  
1176  N NZ  . LYS A 145 ? 0.3761 0.7879 0.4877 0.0114  -0.0340 0.1397  145 LYS A NZ  
1177  N N   . ALA A 146 ? 0.2478 0.5964 0.3316 -0.0080 -0.0299 0.1355  146 ALA A N   
1178  C CA  . ALA A 146 ? 0.2579 0.5929 0.3408 -0.0108 -0.0274 0.1304  146 ALA A CA  
1179  C C   . ALA A 146 ? 0.2626 0.6069 0.3513 -0.0099 -0.0263 0.1265  146 ALA A C   
1180  O O   . ALA A 146 ? 0.3106 0.6564 0.4081 -0.0003 -0.0256 0.1288  146 ALA A O   
1181  C CB  . ALA A 146 ? 0.2183 0.5337 0.3042 -0.0032 -0.0257 0.1334  146 ALA A CB  
1182  N N   . ILE A 147 ? 0.2422 0.5921 0.3261 -0.0200 -0.0260 0.1202  147 ILE A N   
1183  C CA  . ILE A 147 ? 0.1810 0.5409 0.2694 -0.0212 -0.0247 0.1159  147 ILE A CA  
1184  C C   . ILE A 147 ? 0.1907 0.5362 0.2787 -0.0232 -0.0216 0.1113  147 ILE A C   
1185  O O   . ILE A 147 ? 0.2046 0.5374 0.2852 -0.0301 -0.0211 0.1086  147 ILE A O   
1186  C CB  . ILE A 147 ? 0.2128 0.5881 0.2963 -0.0314 -0.0263 0.1118  147 ILE A CB  
1187  C CG1 . ILE A 147 ? 0.2708 0.6612 0.3543 -0.0295 -0.0293 0.1164  147 ILE A CG1 
1188  C CG2 . ILE A 147 ? 0.1719 0.5580 0.2605 -0.0328 -0.0248 0.1076  147 ILE A CG2 
1189  C CD1 . ILE A 147 ? 0.2521 0.6559 0.3290 -0.0406 -0.0309 0.1120  147 ILE A CD1 
1190  N N   . ASN A 148 ? 0.2031 0.5506 0.2991 -0.0170 -0.0194 0.1103  148 ASN A N   
1191  C CA  . ASN A 148 ? 0.2182 0.5540 0.3145 -0.0181 -0.0160 0.1059  148 ASN A CA  
1192  C C   . ASN A 148 ? 0.2419 0.5890 0.3399 -0.0231 -0.0144 0.1008  148 ASN A C   
1193  O O   . ASN A 148 ? 0.2252 0.5876 0.3303 -0.0183 -0.0147 0.1015  148 ASN A O   
1194  C CB  . ASN A 148 ? 0.2151 0.5418 0.3192 -0.0064 -0.0140 0.1083  148 ASN A CB  
1195  C CG  . ASN A 148 ? 0.1921 0.5061 0.2948 -0.0016 -0.0154 0.1135  148 ASN A CG  
1196  O OD1 . ASN A 148 ? 0.1683 0.4724 0.2634 -0.0078 -0.0160 0.1133  148 ASN A OD1 
1197  N ND2 . ASN A 148 ? 0.1955 0.5090 0.3055 0.0095  -0.0158 0.1180  148 ASN A ND2 
1198  N N   . ILE A 149 ? 0.2093 0.5482 0.3008 -0.0325 -0.0127 0.0957  149 ILE A N   
1199  C CA  . ILE A 149 ? 0.2718 0.6198 0.3637 -0.0387 -0.0110 0.0909  149 ILE A CA  
1200  C C   . ILE A 149 ? 0.2409 0.5753 0.3309 -0.0411 -0.0071 0.0870  149 ILE A C   
1201  O O   . ILE A 149 ? 0.2116 0.5418 0.2957 -0.0509 -0.0060 0.0829  149 ILE A O   
1202  C CB  . ILE A 149 ? 0.2072 0.5615 0.2920 -0.0503 -0.0132 0.0882  149 ILE A CB  
1203  C CG1 . ILE A 149 ? 0.2443 0.5815 0.3195 -0.0570 -0.0139 0.0868  149 ILE A CG1 
1204  C CG2 . ILE A 149 ? 0.2761 0.6488 0.3638 -0.0478 -0.0165 0.0915  149 ILE A CG2 
1205  C CD1 . ILE A 149 ? 0.1950 0.5352 0.2630 -0.0690 -0.0153 0.0824  149 ILE A CD1 
1206  N N   . VAL A 150 ? 0.2472 0.5745 0.3423 -0.0321 -0.0048 0.0883  150 VAL A N   
1207  C CA  . VAL A 150 ? 0.2257 0.5414 0.3188 -0.0337 -0.0008 0.0846  150 VAL A CA  
1208  C C   . VAL A 150 ? 0.2630 0.5910 0.3590 -0.0365 0.0015  0.0812  150 VAL A C   
1209  O O   . VAL A 150 ? 0.1706 0.5164 0.2734 -0.0331 0.0007  0.0819  150 VAL A O   
1210  C CB  . VAL A 150 ? 0.2039 0.5103 0.3021 -0.0233 0.0013  0.0861  150 VAL A CB  
1211  C CG1 . VAL A 150 ? 0.2394 0.5591 0.3482 -0.0135 0.0026  0.0863  150 VAL A CG1 
1212  C CG2 . VAL A 150 ? 0.1813 0.4720 0.2742 -0.0264 0.0048  0.0828  150 VAL A CG2 
1213  N N   . THR A 151 ? 0.2895 0.6079 0.3802 -0.0428 0.0045  0.0777  151 THR A N   
1214  C CA  . THR A 151 ? 0.2437 0.5723 0.3363 -0.0463 0.0071  0.0747  151 THR A CA  
1215  C C   . THR A 151 ? 0.2681 0.6099 0.3708 -0.0360 0.0090  0.0748  151 THR A C   
1216  O O   . THR A 151 ? 0.2906 0.6265 0.3974 -0.0267 0.0100  0.0757  151 THR A O   
1217  C CB  . THR A 151 ? 0.2457 0.5588 0.3310 -0.0524 0.0104  0.0720  151 THR A CB  
1218  O OG1 . THR A 151 ? 0.3431 0.6664 0.4307 -0.0547 0.0134  0.0697  151 THR A OG1 
1219  C CG2 . THR A 151 ? 0.2065 0.5050 0.2911 -0.0455 0.0124  0.0724  151 THR A CG2 
1220  N N   . GLU A 152 ? 0.3075 0.6671 0.4146 -0.0377 0.0095  0.0733  152 GLU A N   
1221  C CA  . GLU A 152 ? 0.3455 0.7181 0.4623 -0.0283 0.0116  0.0724  152 GLU A CA  
1222  C C   . GLU A 152 ? 0.2765 0.6401 0.3929 -0.0252 0.0161  0.0696  152 GLU A C   
1223  O O   . GLU A 152 ? 0.2448 0.6138 0.3690 -0.0152 0.0180  0.0684  152 GLU A O   
1224  C CB  . GLU A 152 ? 0.3572 0.7507 0.4780 -0.0323 0.0116  0.0708  152 GLU A CB  
1225  C CG  . GLU A 152 ? 0.4815 0.8869 0.6034 -0.0344 0.0072  0.0733  152 GLU A CG  
1226  C CD  . GLU A 152 ? 0.6251 1.0515 0.7504 -0.0395 0.0072  0.0714  152 GLU A CD  
1227  O OE1 . GLU A 152 ? 0.5627 0.9935 0.6888 -0.0424 0.0108  0.0684  152 GLU A OE1 
1228  O OE2 . GLU A 152 ? 0.5320 0.9709 0.6589 -0.0408 0.0038  0.0730  152 GLU A OE2 
1229  N N   . LYS A 153 ? 0.2443 0.5936 0.3515 -0.0332 0.0178  0.0684  153 LYS A N   
1230  C CA  . LYS A 153 ? 0.2842 0.6249 0.3897 -0.0307 0.0220  0.0659  153 LYS A CA  
1231  C C   . LYS A 153 ? 0.2608 0.5925 0.3701 -0.0199 0.0224  0.0663  153 LYS A C   
1232  O O   . LYS A 153 ? 0.2843 0.6155 0.3964 -0.0140 0.0258  0.0635  153 LYS A O   
1233  C CB  . LYS A 153 ? 0.2902 0.6148 0.3844 -0.0407 0.0230  0.0655  153 LYS A CB  
1234  C CG  . LYS A 153 ? 0.2668 0.5983 0.3576 -0.0509 0.0241  0.0643  153 LYS A CG  
1235  C CD  . LYS A 153 ? 0.3318 0.6739 0.4258 -0.0487 0.0282  0.0619  153 LYS A CD  
1236  C CE  . LYS A 153 ? 0.4644 0.8089 0.5533 -0.0597 0.0299  0.0614  153 LYS A CE  
1237  N NZ  . LYS A 153 ? 0.4974 0.8515 0.5881 -0.0580 0.0342  0.0593  153 LYS A NZ  
1238  N N   . ALA A 154 ? 0.2562 0.5811 0.3657 -0.0173 0.0190  0.0696  154 ALA A N   
1239  C CA  . ALA A 154 ? 0.2601 0.5751 0.3734 -0.0075 0.0193  0.0704  154 ALA A CA  
1240  C C   . ALA A 154 ? 0.2778 0.6035 0.4026 0.0043  0.0203  0.0691  154 ALA A C   
1241  O O   . ALA A 154 ? 0.2515 0.5689 0.3802 0.0127  0.0218  0.0679  154 ALA A O   
1242  C CB  . ALA A 154 ? 0.2311 0.5379 0.3423 -0.0078 0.0153  0.0749  154 ALA A CB  
1243  N N   . PHE A 155 ? 0.2421 0.5858 0.3729 0.0052  0.0194  0.0690  155 PHE A N   
1244  C CA  . PHE A 155 ? 0.2575 0.6114 0.3998 0.0168  0.0199  0.0678  155 PHE A CA  
1245  C C   . PHE A 155 ? 0.3614 0.7220 0.5074 0.0197  0.0245  0.0620  155 PHE A C   
1246  O O   . PHE A 155 ? 0.2796 0.6464 0.4354 0.0301  0.0255  0.0597  155 PHE A O   
1247  C CB  . PHE A 155 ? 0.2624 0.6334 0.4098 0.0170  0.0165  0.0706  155 PHE A CB  
1248  C CG  . PHE A 155 ? 0.3321 0.6990 0.4754 0.0137  0.0118  0.0760  155 PHE A CG  
1249  C CD1 . PHE A 155 ? 0.4173 0.7678 0.5585 0.0172  0.0104  0.0791  155 PHE A CD1 
1250  C CD2 . PHE A 155 ? 0.4344 0.8145 0.5758 0.0069  0.0090  0.0779  155 PHE A CD2 
1251  C CE1 . PHE A 155 ? 0.3826 0.7300 0.5195 0.0140  0.0063  0.0841  155 PHE A CE1 
1252  C CE2 . PHE A 155 ? 0.4199 0.7972 0.5571 0.0036  0.0049  0.0823  155 PHE A CE2 
1253  C CZ  . PHE A 155 ? 0.3565 0.7175 0.4912 0.0072  0.0036  0.0855  155 PHE A CZ  
1254  N N   . ASP A 156 ? 0.2941 0.6530 0.4322 0.0110  0.0274  0.0596  156 ASP A N   
1255  C CA  . ASP A 156 ? 0.2523 0.6170 0.3919 0.0126  0.0320  0.0543  156 ASP A CA  
1256  C C   . ASP A 156 ? 0.2624 0.6098 0.3967 0.0143  0.0345  0.0521  156 ASP A C   
1257  O O   . ASP A 156 ? 0.2885 0.6259 0.4125 0.0058  0.0352  0.0529  156 ASP A O   
1258  C CB  . ASP A 156 ? 0.2685 0.6431 0.4023 0.0015  0.0332  0.0538  156 ASP A CB  
1259  C CG  . ASP A 156 ? 0.3299 0.7146 0.4660 0.0032  0.0378  0.0489  156 ASP A CG  
1260  O OD1 . ASP A 156 ? 0.3253 0.7049 0.4638 0.0109  0.0405  0.0450  156 ASP A OD1 
1261  O OD2 . ASP A 156 ? 0.4578 0.8556 0.5928 -0.0036 0.0386  0.0485  156 ASP A OD2 
1262  N N   . SER A 157 ? 0.2633 0.6065 0.4049 0.0255  0.0357  0.0492  157 SER A N   
1263  C CA  . SER A 157 ? 0.3350 0.6610 0.4725 0.0280  0.0373  0.0474  157 SER A CA  
1264  C C   . SER A 157 ? 0.3083 0.6326 0.4378 0.0226  0.0414  0.0434  157 SER A C   
1265  O O   . SER A 157 ? 0.2854 0.5976 0.4050 0.0160  0.0416  0.0449  157 SER A O   
1266  C CB  . SER A 157 ? 0.3366 0.6586 0.4844 0.0411  0.0380  0.0442  157 SER A CB  
1267  O OG  . SER A 157 ? 0.3137 0.6287 0.4656 0.0454  0.0339  0.0492  157 SER A OG  
1268  N N   . GLU A 158 ? 0.2855 0.6221 0.4191 0.0257  0.0447  0.0384  158 GLU A N   
1269  C CA  . GLU A 158 ? 0.2946 0.6299 0.4209 0.0223  0.0487  0.0344  158 GLU A CA  
1270  C C   . GLU A 158 ? 0.2532 0.5902 0.3688 0.0097  0.0487  0.0377  158 GLU A C   
1271  O O   . GLU A 158 ? 0.2775 0.6102 0.3850 0.0057  0.0513  0.0361  158 GLU A O   
1272  C CB  . GLU A 158 ? 0.3491 0.6979 0.4831 0.0293  0.0522  0.0279  158 GLU A CB  
1273  C CG  . GLU A 158 ? 0.4220 0.7665 0.5668 0.0421  0.0526  0.0235  158 GLU A CG  
1274  C CD  . GLU A 158 ? 0.5749 0.9256 0.7309 0.0484  0.0493  0.0263  158 GLU A CD  
1275  O OE1 . GLU A 158 ? 0.5548 0.9178 0.7113 0.0433  0.0474  0.0302  158 GLU A OE1 
1276  O OE2 . GLU A 158 ? 0.5449 0.8878 0.7092 0.0583  0.0485  0.0246  158 GLU A OE2 
1277  N N   . THR A 159 ? 0.1951 0.5377 0.3105 0.0033  0.0459  0.0423  159 THR A N   
1278  C CA  . THR A 159 ? 0.2495 0.5934 0.3561 -0.0086 0.0460  0.0449  159 THR A CA  
1279  C C   . THR A 159 ? 0.2018 0.5268 0.2985 -0.0154 0.0438  0.0488  159 THR A C   
1280  O O   . THR A 159 ? 0.2337 0.5531 0.3313 -0.0163 0.0403  0.0521  159 THR A O   
1281  C CB  . THR A 159 ? 0.2628 0.6223 0.3743 -0.0125 0.0440  0.0469  159 THR A CB  
1282  O OG1 . THR A 159 ? 0.2636 0.6405 0.3851 -0.0050 0.0459  0.0431  159 THR A OG1 
1283  C CG2 . THR A 159 ? 0.2250 0.5859 0.3282 -0.0249 0.0446  0.0489  159 THR A CG2 
1284  N N   . TYR A 160 ? 0.2257 0.5411 0.3129 -0.0201 0.0459  0.0485  160 TYR A N   
1285  C CA  . TYR A 160 ? 0.2427 0.5393 0.3202 -0.0263 0.0442  0.0519  160 TYR A CA  
1286  C C   . TYR A 160 ? 0.2273 0.5223 0.3024 -0.0352 0.0410  0.0557  160 TYR A C   
1287  O O   . TYR A 160 ? 0.2485 0.5558 0.3254 -0.0403 0.0412  0.0560  160 TYR A O   
1288  C CB  . TYR A 160 ? 0.2335 0.5226 0.3012 -0.0304 0.0469  0.0514  160 TYR A CB  
1289  C CG  . TYR A 160 ? 0.2463 0.5151 0.3040 -0.0362 0.0451  0.0547  160 TYR A CG  
1290  C CD1 . TYR A 160 ? 0.2486 0.5115 0.3007 -0.0460 0.0437  0.0580  160 TYR A CD1 
1291  C CD2 . TYR A 160 ? 0.3142 0.5694 0.3687 -0.0317 0.0450  0.0540  160 TYR A CD2 
1292  C CE1 . TYR A 160 ? 0.2499 0.4931 0.2935 -0.0504 0.0421  0.0604  160 TYR A CE1 
1293  C CE2 . TYR A 160 ? 0.2842 0.5208 0.3298 -0.0364 0.0432  0.0568  160 TYR A CE2 
1294  C CZ  . TYR A 160 ? 0.2223 0.4527 0.2626 -0.0455 0.0418  0.0599  160 TYR A CZ  
1295  O OH  . TYR A 160 ? 0.2890 0.5001 0.3210 -0.0493 0.0402  0.0620  160 TYR A OH  
1296  N N   . ASP A 161 ? 0.2248 0.5051 0.2961 -0.0371 0.0380  0.0582  161 ASP A N   
1297  C CA  . ASP A 161 ? 0.2176 0.4913 0.2838 -0.0464 0.0353  0.0609  161 ASP A CA  
1298  C C   . ASP A 161 ? 0.2238 0.4759 0.2821 -0.0482 0.0339  0.0623  161 ASP A C   
1299  O O   . ASP A 161 ? 0.1754 0.4206 0.2347 -0.0414 0.0338  0.0619  161 ASP A O   
1300  C CB  . ASP A 161 ? 0.2568 0.5418 0.3300 -0.0464 0.0321  0.0620  161 ASP A CB  
1301  C CG  . ASP A 161 ? 0.3305 0.6121 0.3989 -0.0570 0.0298  0.0636  161 ASP A CG  
1302  O OD1 . ASP A 161 ? 0.2379 0.5047 0.3010 -0.0601 0.0274  0.0648  161 ASP A OD1 
1303  O OD2 . ASP A 161 ? 0.3408 0.6347 0.4107 -0.0622 0.0306  0.0631  161 ASP A OD2 
1304  N N   . ASP A 162 ? 0.2099 0.4512 0.2608 -0.0571 0.0329  0.0638  162 ASP A N   
1305  C CA  . ASP A 162 ? 0.2421 0.4620 0.2850 -0.0587 0.0317  0.0647  162 ASP A CA  
1306  C C   . ASP A 162 ? 0.2325 0.4473 0.2773 -0.0566 0.0282  0.0654  162 ASP A C   
1307  O O   . ASP A 162 ? 0.2203 0.4208 0.2613 -0.0538 0.0276  0.0656  162 ASP A O   
1308  C CB  . ASP A 162 ? 0.2806 0.4895 0.3157 -0.0682 0.0319  0.0658  162 ASP A CB  
1309  C CG  . ASP A 162 ? 0.2776 0.4818 0.3071 -0.0694 0.0353  0.0662  162 ASP A CG  
1310  O OD1 . ASP A 162 ? 0.2360 0.4410 0.2654 -0.0630 0.0370  0.0653  162 ASP A OD1 
1311  O OD2 . ASP A 162 ? 0.3342 0.5341 0.3593 -0.0769 0.0362  0.0676  162 ASP A OD2 
1312  N N   . TRP A 163 ? 0.2461 0.4728 0.2965 -0.0581 0.0258  0.0659  163 TRP A N   
1313  C CA  . TRP A 163 ? 0.2196 0.4419 0.2704 -0.0580 0.0221  0.0670  163 TRP A CA  
1314  C C   . TRP A 163 ? 0.2041 0.4443 0.2648 -0.0522 0.0204  0.0681  163 TRP A C   
1315  O O   . TRP A 163 ? 0.2158 0.4651 0.2786 -0.0557 0.0178  0.0688  163 TRP A O   
1316  C CB  . TRP A 163 ? 0.2366 0.4524 0.2819 -0.0677 0.0202  0.0668  163 TRP A CB  
1317  C CG  . TRP A 163 ? 0.2282 0.4296 0.2654 -0.0736 0.0224  0.0661  163 TRP A CG  
1318  C CD1 . TRP A 163 ? 0.2268 0.4320 0.2625 -0.0804 0.0242  0.0659  163 TRP A CD1 
1319  C CD2 . TRP A 163 ? 0.2580 0.4390 0.2878 -0.0729 0.0231  0.0660  163 TRP A CD2 
1320  N NE1 . TRP A 163 ? 0.2296 0.4177 0.2575 -0.0838 0.0260  0.0662  163 TRP A NE1 
1321  C CE2 . TRP A 163 ? 0.2164 0.3896 0.2405 -0.0790 0.0253  0.0661  163 TRP A CE2 
1322  C CE3 . TRP A 163 ? 0.2642 0.4329 0.2916 -0.0676 0.0222  0.0660  163 TRP A CE3 
1323  C CZ2 . TRP A 163 ? 0.2719 0.4258 0.2882 -0.0793 0.0265  0.0665  163 TRP A CZ2 
1324  C CZ3 . TRP A 163 ? 0.1759 0.3259 0.1954 -0.0682 0.0232  0.0658  163 TRP A CZ3 
1325  C CH2 . TRP A 163 ? 0.2174 0.3604 0.2316 -0.0737 0.0253  0.0661  163 TRP A CH2 
1326  N N   . LYS A 164 ? 0.1723 0.4174 0.2391 -0.0429 0.0220  0.0681  164 LYS A N   
1327  C CA  . LYS A 164 ? 0.1661 0.4268 0.2431 -0.0357 0.0206  0.0694  164 LYS A CA  
1328  C C   . LYS A 164 ? 0.1776 0.4351 0.2557 -0.0341 0.0167  0.0724  164 LYS A C   
1329  O O   . LYS A 164 ? 0.1804 0.4498 0.2667 -0.0278 0.0151  0.0744  164 LYS A O   
1330  C CB  . LYS A 164 ? 0.1896 0.4544 0.2734 -0.0255 0.0236  0.0679  164 LYS A CB  
1331  C CG  . LYS A 164 ? 0.2064 0.4824 0.2922 -0.0255 0.0270  0.0648  164 LYS A CG  
1332  C CD  . LYS A 164 ? 0.2181 0.4997 0.3119 -0.0145 0.0297  0.0622  164 LYS A CD  
1333  C CE  . LYS A 164 ? 0.2163 0.5126 0.3134 -0.0140 0.0327  0.0589  164 LYS A CE  
1334  N NZ  . LYS A 164 ? 0.1901 0.4921 0.2959 -0.0027 0.0352  0.0553  164 LYS A NZ  
1335  N N   . GLY A 165 ? 0.1694 0.4110 0.2394 -0.0391 0.0152  0.0729  165 GLY A N   
1336  C CA  . GLY A 165 ? 0.1718 0.4113 0.2417 -0.0391 0.0115  0.0756  165 GLY A CA  
1337  C C   . GLY A 165 ? 0.1981 0.4411 0.2637 -0.0479 0.0086  0.0753  165 GLY A C   
1338  O O   . GLY A 165 ? 0.1878 0.4301 0.2523 -0.0487 0.0053  0.0772  165 GLY A O   
1339  N N   . ASP A 166 ? 0.1803 0.4277 0.2436 -0.0548 0.0097  0.0728  166 ASP A N   
1340  C CA  . ASP A 166 ? 0.1952 0.4445 0.2541 -0.0642 0.0074  0.0716  166 ASP A CA  
1341  C C   . ASP A 166 ? 0.2299 0.4964 0.2940 -0.0627 0.0039  0.0737  166 ASP A C   
1342  O O   . ASP A 166 ? 0.1927 0.4733 0.2651 -0.0551 0.0037  0.0760  166 ASP A O   
1343  C CB  . ASP A 166 ? 0.2135 0.4670 0.2710 -0.0711 0.0096  0.0692  166 ASP A CB  
1344  C CG  . ASP A 166 ? 0.2308 0.4647 0.2800 -0.0765 0.0120  0.0672  166 ASP A CG  
1345  O OD1 . ASP A 166 ? 0.2056 0.4224 0.2496 -0.0752 0.0117  0.0672  166 ASP A OD1 
1346  O OD2 . ASP A 166 ? 0.2928 0.5287 0.3407 -0.0819 0.0142  0.0660  166 ASP A OD2 
1347  N N   . PHE A 167 ? 0.1965 0.4617 0.2557 -0.0699 0.0011  0.0728  167 PHE A N   
1348  C CA  . PHE A 167 ? 0.2360 0.5197 0.2985 -0.0711 -0.0020 0.0740  167 PHE A CA  
1349  C C   . PHE A 167 ? 0.2602 0.5593 0.3266 -0.0743 -0.0007 0.0723  167 PHE A C   
1350  O O   . PHE A 167 ? 0.2902 0.5834 0.3538 -0.0801 0.0020  0.0695  167 PHE A O   
1351  C CB  . PHE A 167 ? 0.1862 0.4653 0.2415 -0.0795 -0.0047 0.0720  167 PHE A CB  
1352  C CG  . PHE A 167 ? 0.1698 0.4404 0.2222 -0.0763 -0.0069 0.0742  167 PHE A CG  
1353  C CD1 . PHE A 167 ? 0.1869 0.4375 0.2350 -0.0747 -0.0054 0.0737  167 PHE A CD1 
1354  C CD2 . PHE A 167 ? 0.1835 0.4665 0.2367 -0.0752 -0.0105 0.0767  167 PHE A CD2 
1355  C CE1 . PHE A 167 ? 0.1930 0.4365 0.2384 -0.0722 -0.0073 0.0755  167 PHE A CE1 
1356  C CE2 . PHE A 167 ? 0.1907 0.4666 0.2408 -0.0728 -0.0124 0.0790  167 PHE A CE2 
1357  C CZ  . PHE A 167 ? 0.1582 0.4144 0.2046 -0.0714 -0.0108 0.0783  167 PHE A CZ  
1358  N N   . ASP A 168 ? 0.2382 0.5574 0.3113 -0.0706 -0.0026 0.0742  168 ASP A N   
1359  C CA  . ASP A 168 ? 0.2549 0.5915 0.3312 -0.0751 -0.0023 0.0724  168 ASP A CA  
1360  C C   . ASP A 168 ? 0.2284 0.5671 0.2989 -0.0855 -0.0048 0.0701  168 ASP A C   
1361  O O   . ASP A 168 ? 0.2369 0.5851 0.3077 -0.0844 -0.0081 0.0717  168 ASP A O   
1362  C CB  . ASP A 168 ? 0.2281 0.5849 0.3142 -0.0657 -0.0032 0.0753  168 ASP A CB  
1363  C CG  . ASP A 168 ? 0.3195 0.6963 0.4099 -0.0696 -0.0028 0.0734  168 ASP A CG  
1364  O OD1 . ASP A 168 ? 0.2537 0.6342 0.3398 -0.0799 -0.0037 0.0707  168 ASP A OD1 
1365  O OD2 . ASP A 168 ? 0.3377 0.7270 0.4364 -0.0619 -0.0014 0.0743  168 ASP A OD2 
1366  N N   . ILE A 169 ? 0.2455 0.5751 0.3104 -0.0956 -0.0030 0.0662  169 ILE A N   
1367  C CA  . ILE A 169 ? 0.3225 0.6500 0.3813 -0.1058 -0.0048 0.0630  169 ILE A CA  
1368  C C   . ILE A 169 ? 0.2598 0.6107 0.3223 -0.1086 -0.0071 0.0625  169 ILE A C   
1369  O O   . ILE A 169 ? 0.2824 0.6373 0.3414 -0.1130 -0.0098 0.0612  169 ILE A O   
1370  C CB  . ILE A 169 ? 0.3498 0.6613 0.4029 -0.1154 -0.0019 0.0592  169 ILE A CB  
1371  C CG1 . ILE A 169 ? 0.3755 0.6633 0.4240 -0.1122 0.0000  0.0598  169 ILE A CG1 
1372  C CG2 . ILE A 169 ? 0.2883 0.5980 0.3358 -0.1264 -0.0033 0.0551  169 ILE A CG2 
1373  C CD1 . ILE A 169 ? 0.2590 0.5351 0.3027 -0.1105 -0.0024 0.0600  169 ILE A CD1 
1374  N N   . LYS A 170 ? 0.1943 0.5619 0.2640 -0.1060 -0.0058 0.0632  170 LYS A N   
1375  C CA  . LYS A 170 ? 0.2580 0.6491 0.3318 -0.1081 -0.0079 0.0628  170 LYS A CA  
1376  C C   . LYS A 170 ? 0.2726 0.6748 0.3493 -0.0995 -0.0115 0.0668  170 LYS A C   
1377  O O   . LYS A 170 ? 0.2676 0.6828 0.3433 -0.1031 -0.0143 0.0661  170 LYS A O   
1378  C CB  . LYS A 170 ? 0.2422 0.6487 0.3233 -0.1067 -0.0055 0.0626  170 LYS A CB  
1379  C CG  . LYS A 170 ? 0.2590 0.6901 0.3443 -0.1103 -0.0073 0.0614  170 LYS A CG  
1380  C CD  . LYS A 170 ? 0.3398 0.7858 0.4325 -0.1087 -0.0046 0.0611  170 LYS A CD  
1381  C CE  . LYS A 170 ? 0.2849 0.7575 0.3828 -0.1111 -0.0065 0.0601  170 LYS A CE  
1382  N NZ  . LYS A 170 ? 0.3823 0.8701 0.4874 -0.1102 -0.0037 0.0594  170 LYS A NZ  
1383  N N   . LYS A 171 ? 0.2234 0.6204 0.3037 -0.0882 -0.0113 0.0710  171 LYS A N   
1384  C CA  . LYS A 171 ? 0.2356 0.6402 0.3185 -0.0798 -0.0145 0.0757  171 LYS A CA  
1385  C C   . LYS A 171 ? 0.2271 0.6207 0.3015 -0.0841 -0.0168 0.0756  171 LYS A C   
1386  O O   . LYS A 171 ? 0.1973 0.6016 0.2716 -0.0820 -0.0199 0.0781  171 LYS A O   
1387  C CB  . LYS A 171 ? 0.2750 0.6747 0.3641 -0.0669 -0.0133 0.0800  171 LYS A CB  
1388  C CG  . LYS A 171 ? 0.2467 0.6598 0.3453 -0.0605 -0.0112 0.0802  171 LYS A CG  
1389  C CD  . LYS A 171 ? 0.3190 0.7244 0.4233 -0.0479 -0.0099 0.0836  171 LYS A CD  
1390  C CE  . LYS A 171 ? 0.3728 0.7944 0.4879 -0.0387 -0.0088 0.0845  171 LYS A CE  
1391  N NZ  . LYS A 171 ? 0.3636 0.7785 0.4849 -0.0253 -0.0085 0.0882  171 LYS A NZ  
1392  N N   . LEU A 172 ? 0.2628 0.6355 0.3302 -0.0898 -0.0154 0.0726  172 LEU A N   
1393  C CA  . LEU A 172 ? 0.2422 0.6047 0.3013 -0.0947 -0.0173 0.0714  172 LEU A CA  
1394  C C   . LEU A 172 ? 0.2701 0.6448 0.3257 -0.1043 -0.0191 0.0675  172 LEU A C   
1395  O O   . LEU A 172 ? 0.2031 0.5836 0.2554 -0.1048 -0.0218 0.0683  172 LEU A O   
1396  C CB  . LEU A 172 ? 0.2490 0.5869 0.3018 -0.0993 -0.0151 0.0682  172 LEU A CB  
1397  C CG  . LEU A 172 ? 0.2625 0.5887 0.3065 -0.1053 -0.0166 0.0654  172 LEU A CG  
1398  C CD1 . LEU A 172 ? 0.2520 0.5801 0.2958 -0.0978 -0.0192 0.0703  172 LEU A CD1 
1399  C CD2 . LEU A 172 ? 0.2299 0.5317 0.2683 -0.1098 -0.0140 0.0618  172 LEU A CD2 
1400  N N   . LYS A 173 ? 0.2429 0.6222 0.2991 -0.1122 -0.0174 0.0631  173 LYS A N   
1401  C CA  . LYS A 173 ? 0.2373 0.6295 0.2911 -0.1217 -0.0188 0.0589  173 LYS A CA  
1402  C C   . LYS A 173 ? 0.2353 0.6532 0.2946 -0.1165 -0.0215 0.0623  173 LYS A C   
1403  O O   . LYS A 173 ? 0.2395 0.6671 0.2954 -0.1204 -0.0239 0.0610  173 LYS A O   
1404  C CB  . LYS A 173 ? 0.2881 0.6795 0.3425 -0.1309 -0.0160 0.0542  173 LYS A CB  
1405  C CG  . LYS A 173 ? 0.2699 0.6356 0.3184 -0.1370 -0.0132 0.0508  173 LYS A CG  
1406  C CD  . LYS A 173 ? 0.3967 0.7628 0.4471 -0.1446 -0.0100 0.0479  173 LYS A CD  
1407  C CE  . LYS A 173 ? 0.4816 0.8217 0.5265 -0.1501 -0.0068 0.0455  173 LYS A CE  
1408  N NZ  . LYS A 173 ? 0.5020 0.8300 0.5396 -0.1594 -0.0073 0.0403  173 LYS A NZ  
1409  N N   . GLU A 174 ? 0.2468 0.6761 0.3147 -0.1076 -0.0210 0.0664  174 GLU A N   
1410  C CA  . GLU A 174 ? 0.2143 0.6675 0.2884 -0.1013 -0.0235 0.0702  174 GLU A CA  
1411  C C   . GLU A 174 ? 0.2256 0.6789 0.2976 -0.0946 -0.0263 0.0751  174 GLU A C   
1412  O O   . GLU A 174 ? 0.2274 0.6980 0.2998 -0.0945 -0.0289 0.0764  174 GLU A O   
1413  C CB  . GLU A 174 ? 0.2223 0.6847 0.3064 -0.0918 -0.0220 0.0735  174 GLU A CB  
1414  C CG  . GLU A 174 ? 0.2496 0.7226 0.3375 -0.0978 -0.0198 0.0694  174 GLU A CG  
1415  C CD  . GLU A 174 ? 0.3930 0.8697 0.4897 -0.0885 -0.0174 0.0717  174 GLU A CD  
1416  O OE1 . GLU A 174 ? 0.3459 0.8142 0.4454 -0.0778 -0.0172 0.0759  174 GLU A OE1 
1417  O OE2 . GLU A 174 ? 0.3969 0.8851 0.4978 -0.0921 -0.0155 0.0691  174 GLU A OE2 
1418  N N   . ASN A 175 ? 0.2413 0.6760 0.3114 -0.0889 -0.0257 0.0780  175 ASN A N   
1419  C CA  . ASN A 175 ? 0.2237 0.6575 0.2920 -0.0826 -0.0280 0.0833  175 ASN A CA  
1420  C C   . ASN A 175 ? 0.2573 0.6886 0.3161 -0.0917 -0.0296 0.0798  175 ASN A C   
1421  O O   . ASN A 175 ? 0.2983 0.7392 0.3558 -0.0891 -0.0320 0.0832  175 ASN A O   
1422  C CB  . ASN A 175 ? 0.2561 0.6708 0.3254 -0.0744 -0.0267 0.0871  175 ASN A CB  
1423  C CG  . ASN A 175 ? 0.2739 0.6950 0.3536 -0.0615 -0.0262 0.0928  175 ASN A CG  
1424  O OD1 . ASN A 175 ? 0.3441 0.7718 0.4271 -0.0532 -0.0281 0.0987  175 ASN A OD1 
1425  N ND2 . ASN A 175 ? 0.2073 0.6258 0.2920 -0.0598 -0.0235 0.0908  175 ASN A ND2 
1426  N N   . ILE A 176 ? 0.2805 0.6984 0.3326 -0.1022 -0.0281 0.0730  176 ILE A N   
1427  C CA  . ILE A 176 ? 0.2409 0.6564 0.2843 -0.1112 -0.0292 0.0683  176 ILE A CA  
1428  C C   . ILE A 176 ? 0.2669 0.7057 0.3109 -0.1162 -0.0310 0.0661  176 ILE A C   
1429  O O   . ILE A 176 ? 0.3307 0.7767 0.3701 -0.1185 -0.0329 0.0657  176 ILE A O   
1430  C CB  . ILE A 176 ? 0.2318 0.6268 0.2691 -0.1209 -0.0269 0.0611  176 ILE A CB  
1431  C CG1 . ILE A 176 ? 0.3459 0.7182 0.3814 -0.1157 -0.0256 0.0634  176 ILE A CG1 
1432  C CG2 . ILE A 176 ? 0.2312 0.6255 0.2603 -0.1310 -0.0277 0.0547  176 ILE A CG2 
1433  C CD1 . ILE A 176 ? 0.3533 0.7045 0.3848 -0.1230 -0.0227 0.0576  176 ILE A CD1 
1434  N N   . ALA A 177 ? 0.3063 0.7581 0.3561 -0.1180 -0.0304 0.0647  177 ALA A N   
1435  C CA  . ALA A 177 ? 0.2830 0.7585 0.3341 -0.1228 -0.0321 0.0625  177 ALA A CA  
1436  C C   . ALA A 177 ? 0.2395 0.7342 0.2957 -0.1126 -0.0348 0.0698  177 ALA A C   
1437  O O   . ALA A 177 ? 0.3029 0.8134 0.3568 -0.1153 -0.0369 0.0693  177 ALA A O   
1438  C CB  . ALA A 177 ? 0.2359 0.7199 0.2920 -0.1280 -0.0304 0.0588  177 ALA A CB  
1439  N N   . GLN A 178 ? 0.2315 0.7247 0.2947 -0.1006 -0.0345 0.0767  178 GLN A N   
1440  C CA  . GLN A 178 ? 0.2645 0.7751 0.3339 -0.0901 -0.0369 0.0840  178 GLN A CA  
1441  C C   . GLN A 178 ? 0.2671 0.7743 0.3314 -0.0870 -0.0387 0.0882  178 GLN A C   
1442  O O   . GLN A 178 ? 0.2277 0.7528 0.2923 -0.0855 -0.0411 0.0909  178 GLN A O   
1443  C CB  . GLN A 178 ? 0.3240 0.8316 0.4026 -0.0781 -0.0357 0.0894  178 GLN A CB  
1444  C CG  . GLN A 178 ? 0.3719 0.8917 0.4570 -0.0656 -0.0380 0.0977  178 GLN A CG  
1445  C CD  . GLN A 178 ? 0.5243 1.0342 0.6173 -0.0531 -0.0366 0.1027  178 GLN A CD  
1446  O OE1 . GLN A 178 ? 0.4901 0.9874 0.5845 -0.0538 -0.0338 0.0998  178 GLN A OE1 
1447  N NE2 . GLN A 178 ? 0.4963 1.0115 0.5946 -0.0417 -0.0384 0.1103  178 GLN A NE2 
1448  N N   . HIS A 179 ? 0.3063 0.7914 0.3660 -0.0860 -0.0375 0.0890  179 HIS A N   
1449  C CA  . HIS A 179 ? 0.2476 0.7281 0.3025 -0.0832 -0.0388 0.0930  179 HIS A CA  
1450  C C   . HIS A 179 ? 0.2695 0.7477 0.3142 -0.0948 -0.0390 0.0864  179 HIS A C   
1451  O O   . HIS A 179 ? 0.2845 0.7685 0.3255 -0.0943 -0.0405 0.0887  179 HIS A O   
1452  C CB  . HIS A 179 ? 0.2292 0.6875 0.2845 -0.0760 -0.0374 0.0972  179 HIS A CB  
1453  C CG  . HIS A 179 ? 0.2859 0.7453 0.3514 -0.0636 -0.0371 0.1039  179 HIS A CG  
1454  N ND1 . HIS A 179 ? 0.2821 0.7488 0.3526 -0.0531 -0.0387 0.1120  179 HIS A ND1 
1455  C CD2 . HIS A 179 ? 0.2726 0.7260 0.3441 -0.0598 -0.0351 0.1032  179 HIS A CD2 
1456  C CE1 . HIS A 179 ? 0.3054 0.7698 0.3847 -0.0433 -0.0379 0.1157  179 HIS A CE1 
1457  N NE2 . HIS A 179 ? 0.2919 0.7491 0.3721 -0.0471 -0.0356 0.1103  179 HIS A NE2 
1458  N N   . GLY A 180 ? 0.3053 0.7752 0.3457 -0.1052 -0.0375 0.0779  180 GLY A N   
1459  C CA  . GLY A 180 ? 0.2149 0.6807 0.2462 -0.1161 -0.0373 0.0705  180 GLY A CA  
1460  C C   . GLY A 180 ? 0.2771 0.7185 0.3023 -0.1167 -0.0360 0.0693  180 GLY A C   
1461  O O   . GLY A 180 ? 0.2718 0.7054 0.2986 -0.1079 -0.0361 0.0761  180 GLY A O   
1462  N N   . ALA A 181 ? 0.2792 0.7081 0.2977 -0.1271 -0.0345 0.0605  181 ALA A N   
1463  C CA  . ALA A 181 ? 0.2989 0.7041 0.3116 -0.1279 -0.0331 0.0586  181 ALA A CA  
1464  C C   . ALA A 181 ? 0.2980 0.7042 0.3066 -0.1245 -0.0342 0.0620  181 ALA A C   
1465  O O   . ALA A 181 ? 0.3305 0.7208 0.3374 -0.1200 -0.0335 0.0649  181 ALA A O   
1466  C CB  . ALA A 181 ? 0.3200 0.7126 0.3269 -0.1398 -0.0313 0.0481  181 ALA A CB  
1467  N N   . ASP A 182 ? 0.2924 0.7175 0.2994 -0.1265 -0.0358 0.0618  182 ASP A N   
1468  C CA  . ASP A 182 ? 0.2969 0.7243 0.3000 -0.1239 -0.0365 0.0649  182 ASP A CA  
1469  C C   . ASP A 182 ? 0.2965 0.7250 0.3054 -0.1116 -0.0374 0.0763  182 ASP A C   
1470  O O   . ASP A 182 ? 0.2827 0.7083 0.2891 -0.1087 -0.0375 0.0796  182 ASP A O   
1471  C CB  . ASP A 182 ? 0.3345 0.7836 0.3352 -0.1290 -0.0380 0.0620  182 ASP A CB  
1472  C CG  . ASP A 182 ? 0.4842 0.9311 0.4791 -0.1415 -0.0369 0.0500  182 ASP A CG  
1473  O OD1 . ASP A 182 ? 0.4708 0.8966 0.4610 -0.1460 -0.0350 0.0440  182 ASP A OD1 
1474  O OD2 . ASP A 182 ? 0.5722 1.0380 0.5675 -0.1467 -0.0379 0.0465  182 ASP A OD2 
1475  N N   . ASN A 183 ? 0.2692 0.7014 0.2862 -0.1044 -0.0377 0.0820  183 ASN A N   
1476  C CA  . ASN A 183 ? 0.2190 0.6498 0.2425 -0.0923 -0.0382 0.0923  183 ASN A CA  
1477  C C   . ASN A 183 ? 0.1863 0.5955 0.2119 -0.0877 -0.0364 0.0939  183 ASN A C   
1478  O O   . ASN A 183 ? 0.2421 0.6463 0.2726 -0.0781 -0.0364 0.1017  183 ASN A O   
1479  C CB  . ASN A 183 ? 0.2233 0.6729 0.2555 -0.0856 -0.0397 0.0977  183 ASN A CB  
1480  C CG  . ASN A 183 ? 0.2963 0.7673 0.3284 -0.0849 -0.0420 0.1009  183 ASN A CG  
1481  O OD1 . ASN A 183 ? 0.2437 0.7145 0.2744 -0.0809 -0.0427 0.1062  183 ASN A OD1 
1482  N ND2 . ASN A 183 ? 0.2991 0.7893 0.3326 -0.0892 -0.0432 0.0976  183 ASN A ND2 
1483  N N   . ILE A 184 ? 0.2053 0.6014 0.2278 -0.0942 -0.0349 0.0869  184 ILE A N   
1484  C CA  . ILE A 184 ? 0.2301 0.6063 0.2544 -0.0903 -0.0332 0.0880  184 ILE A CA  
1485  C C   . ILE A 184 ? 0.2199 0.5802 0.2373 -0.0923 -0.0325 0.0865  184 ILE A C   
1486  O O   . ILE A 184 ? 0.2656 0.6181 0.2755 -0.1012 -0.0319 0.0787  184 ILE A O   
1487  C CB  . ILE A 184 ? 0.1738 0.5434 0.1986 -0.0959 -0.0317 0.0815  184 ILE A CB  
1488  C CG1 . ILE A 184 ? 0.1781 0.5667 0.2095 -0.0949 -0.0324 0.0823  184 ILE A CG1 
1489  C CG2 . ILE A 184 ? 0.1663 0.5172 0.1938 -0.0909 -0.0300 0.0832  184 ILE A CG2 
1490  C CD1 . ILE A 184 ? 0.2861 0.6706 0.3185 -0.1010 -0.0307 0.0762  184 ILE A CD1 
1491  N N   . VAL A 185 ? 0.2128 0.5680 0.2332 -0.0839 -0.0325 0.0939  185 VAL A N   
1492  C CA  . VAL A 185 ? 0.2244 0.5660 0.2390 -0.0854 -0.0318 0.0930  185 VAL A CA  
1493  C C   . VAL A 185 ? 0.2576 0.5791 0.2687 -0.0890 -0.0303 0.0876  185 VAL A C   
1494  O O   . VAL A 185 ? 0.2318 0.5436 0.2352 -0.0955 -0.0298 0.0815  185 VAL A O   
1495  C CB  . VAL A 185 ? 0.2140 0.5537 0.2340 -0.0755 -0.0320 0.1022  185 VAL A CB  
1496  C CG1 . VAL A 185 ? 0.2596 0.5848 0.2748 -0.0769 -0.0311 0.1008  185 VAL A CG1 
1497  C CG2 . VAL A 185 ? 0.2473 0.6061 0.2697 -0.0726 -0.0338 0.1071  185 VAL A CG2 
1498  N N   . ALA A 186 ? 0.1868 0.5018 0.2036 -0.0846 -0.0295 0.0893  186 ALA A N   
1499  C CA  . ALA A 186 ? 0.1921 0.4884 0.2066 -0.0874 -0.0280 0.0843  186 ALA A CA  
1500  C C   . ALA A 186 ? 0.1867 0.4824 0.2089 -0.0830 -0.0268 0.0858  186 ALA A C   
1501  O O   . ALA A 186 ? 0.2052 0.5124 0.2350 -0.0757 -0.0272 0.0917  186 ALA A O   
1502  C CB  . ALA A 186 ? 0.2261 0.5070 0.2386 -0.0840 -0.0274 0.0866  186 ALA A CB  
1503  N N   . ILE A 187 ? 0.1892 0.4710 0.2098 -0.0873 -0.0250 0.0800  187 ILE A N   
1504  C CA  . ILE A 187 ? 0.1585 0.4354 0.1858 -0.0829 -0.0229 0.0809  187 ILE A CA  
1505  C C   . ILE A 187 ? 0.1869 0.4454 0.2145 -0.0780 -0.0212 0.0824  187 ILE A C   
1506  O O   . ILE A 187 ? 0.2109 0.4545 0.2320 -0.0821 -0.0206 0.0783  187 ILE A O   
1507  C CB  . ILE A 187 ? 0.2063 0.4798 0.2318 -0.0909 -0.0211 0.0740  187 ILE A CB  
1508  C CG1 . ILE A 187 ? 0.2529 0.5470 0.2802 -0.0945 -0.0226 0.0733  187 ILE A CG1 
1509  C CG2 . ILE A 187 ? 0.2059 0.4709 0.2366 -0.0868 -0.0182 0.0744  187 ILE A CG2 
1510  C CD1 . ILE A 187 ? 0.2546 0.5461 0.2777 -0.1053 -0.0214 0.0656  187 ILE A CD1 
1511  N N   . VAL A 188 ? 0.1906 0.4501 0.2261 -0.0689 -0.0203 0.0879  188 VAL A N   
1512  C CA  . VAL A 188 ? 0.1531 0.3963 0.1901 -0.0635 -0.0181 0.0893  188 VAL A CA  
1513  C C   . VAL A 188 ? 0.1532 0.3889 0.1932 -0.0625 -0.0148 0.0863  188 VAL A C   
1514  O O   . VAL A 188 ? 0.1914 0.4386 0.2384 -0.0586 -0.0142 0.0884  188 VAL A O   
1515  C CB  . VAL A 188 ? 0.1659 0.4144 0.2099 -0.0537 -0.0190 0.0976  188 VAL A CB  
1516  C CG1 . VAL A 188 ? 0.2010 0.4315 0.2459 -0.0491 -0.0163 0.0984  188 VAL A CG1 
1517  C CG2 . VAL A 188 ? 0.1892 0.4474 0.2298 -0.0546 -0.0221 0.1014  188 VAL A CG2 
1518  N N   . SER A 189 ? 0.1579 0.3747 0.1922 -0.0659 -0.0124 0.0813  189 SER A N   
1519  C CA  . SER A 189 ? 0.1597 0.3679 0.1953 -0.0651 -0.0089 0.0787  189 SER A CA  
1520  C C   . SER A 189 ? 0.1704 0.3661 0.2079 -0.0574 -0.0067 0.0808  189 SER A C   
1521  O O   . SER A 189 ? 0.2168 0.3955 0.2482 -0.0581 -0.0058 0.0785  189 SER A O   
1522  C CB  . SER A 189 ? 0.2011 0.3966 0.2289 -0.0737 -0.0076 0.0723  189 SER A CB  
1523  O OG  . SER A 189 ? 0.2275 0.4339 0.2533 -0.0814 -0.0096 0.0699  189 SER A OG  
1524  N N   . THR A 190 ? 0.1969 0.4010 0.2430 -0.0500 -0.0055 0.0847  190 THR A N   
1525  C CA  . THR A 190 ? 0.1529 0.3477 0.2024 -0.0423 -0.0031 0.0870  190 THR A CA  
1526  C C   . THR A 190 ? 0.1455 0.3290 0.1927 -0.0424 0.0006  0.0828  190 THR A C   
1527  O O   . THR A 190 ? 0.1731 0.3655 0.2240 -0.0425 0.0020  0.0818  190 THR A O   
1528  C CB  . THR A 190 ? 0.1324 0.3426 0.1937 -0.0337 -0.0034 0.0929  190 THR A CB  
1529  O OG1 . THR A 190 ? 0.1711 0.3934 0.2342 -0.0335 -0.0073 0.0974  190 THR A OG1 
1530  C CG2 . THR A 190 ? 0.2083 0.4065 0.2727 -0.0255 -0.0012 0.0945  190 THR A CG2 
1531  N N   . VAL A 191 ? 0.1723 0.3370 0.2131 -0.0422 0.0020  0.0803  191 VAL A N   
1532  C CA  . VAL A 191 ? 0.1616 0.3151 0.1988 -0.0426 0.0051  0.0765  191 VAL A CA  
1533  C C   . VAL A 191 ? 0.1719 0.3137 0.2091 -0.0363 0.0071  0.0770  191 VAL A C   
1534  O O   . VAL A 191 ? 0.1651 0.2964 0.1984 -0.0355 0.0060  0.0770  191 VAL A O   
1535  C CB  . VAL A 191 ? 0.1978 0.3390 0.2256 -0.0502 0.0049  0.0718  191 VAL A CB  
1536  C CG1 . VAL A 191 ? 0.1504 0.3032 0.1787 -0.0570 0.0037  0.0710  191 VAL A CG1 
1537  C CG2 . VAL A 191 ? 0.1702 0.2998 0.1921 -0.0516 0.0031  0.0706  191 VAL A CG2 
1538  N N   . THR A 192 ? 0.1646 0.3092 0.2063 -0.0317 0.0102  0.0771  192 THR A N   
1539  C CA  . THR A 192 ? 0.1568 0.3173 0.2053 -0.0308 0.0116  0.0775  192 THR A CA  
1540  C C   . THR A 192 ? 0.1977 0.3754 0.2564 -0.0266 0.0099  0.0819  192 THR A C   
1541  O O   . THR A 192 ? 0.1502 0.3251 0.2102 -0.0236 0.0079  0.0849  192 THR A O   
1542  C CB  . THR A 192 ? 0.1863 0.3466 0.2380 -0.0255 0.0157  0.0760  192 THR A CB  
1543  O OG1 . THR A 192 ? 0.1928 0.3479 0.2491 -0.0171 0.0157  0.0766  192 THR A OG1 
1544  C CG2 . THR A 192 ? 0.1666 0.3115 0.2082 -0.0289 0.0172  0.0723  192 THR A CG2 
1545  N N   . CYS A 193 ? 0.2026 0.3963 0.2675 -0.0258 0.0102  0.0819  193 CYS A N   
1546  C CA  . CYS A 193 ? 0.1971 0.4073 0.2718 -0.0208 0.0080  0.0858  193 CYS A CA  
1547  C C   . CYS A 193 ? 0.1896 0.3996 0.2735 -0.0097 0.0096  0.0869  193 CYS A C   
1548  O O   . CYS A 193 ? 0.2218 0.4391 0.3116 -0.0053 0.0124  0.0846  193 CYS A O   
1549  C CB  . CYS A 193 ? 0.1696 0.3954 0.2464 -0.0237 0.0074  0.0845  193 CYS A CB  
1550  S SG  . CYS A 193 ? 0.2041 0.4496 0.2910 -0.0175 0.0040  0.0890  193 CYS A SG  
1551  N N   . ASN A 194 ? 0.2400 0.4387 0.3234 -0.0048 0.0076  0.0892  194 ASN A N   
1552  C CA  . ASN A 194 ? 0.2121 0.4034 0.3017 0.0055  0.0087  0.0890  194 ASN A CA  
1553  C C   . ASN A 194 ? 0.2510 0.4594 0.3530 0.0133  0.0089  0.0904  194 ASN A C   
1554  O O   . ASN A 194 ? 0.2338 0.4420 0.3412 0.0194  0.0119  0.0868  194 ASN A O   
1555  C CB  . ASN A 194 ? 0.2260 0.4049 0.3136 0.0082  0.0061  0.0928  194 ASN A CB  
1556  C CG  . ASN A 194 ? 0.2666 0.4324 0.3586 0.0170  0.0078  0.0917  194 ASN A CG  
1557  O OD1 . ASN A 194 ? 0.2464 0.4116 0.3425 0.0212  0.0108  0.0872  194 ASN A OD1 
1558  N ND2 . ASN A 194 ? 0.2284 0.3834 0.3193 0.0192  0.0059  0.0955  194 ASN A ND2 
1559  N N   . SER A 195 ? 0.2164 0.4408 0.3232 0.0132  0.0056  0.0952  195 SER A N   
1560  C CA  . SER A 195 ? 0.1837 0.4202 0.3004 0.0218  0.0052  0.0964  195 SER A CA  
1561  C C   . SER A 195 ? 0.2529 0.5004 0.3716 0.0208  0.0082  0.0910  195 SER A C   
1562  O O   . SER A 195 ? 0.2986 0.5514 0.4252 0.0291  0.0095  0.0893  195 SER A O   
1563  C CB  . SER A 195 ? 0.1783 0.4245 0.2947 0.0210  0.0009  0.1017  195 SER A CB  
1564  O OG  . SER A 195 ? 0.2902 0.5267 0.4025 0.0199  -0.0018 0.1065  195 SER A OG  
1565  N N   . ALA A 196 ? 0.2170 0.4667 0.3281 0.0107  0.0095  0.0880  196 ALA A N   
1566  C CA  . ALA A 196 ? 0.2375 0.4959 0.3491 0.0090  0.0126  0.0831  196 ALA A CA  
1567  C C   . ALA A 196 ? 0.2225 0.4721 0.3340 0.0121  0.0170  0.0785  196 ALA A C   
1568  O O   . ALA A 196 ? 0.2012 0.4578 0.3130 0.0113  0.0200  0.0742  196 ALA A O   
1569  C CB  . ALA A 196 ? 0.1879 0.4499 0.2906 -0.0032 0.0120  0.0820  196 ALA A CB  
1570  N N   . GLY A 197 ? 0.2338 0.4691 0.3448 0.0154  0.0176  0.0790  197 GLY A N   
1571  C CA  . GLY A 197 ? 0.2213 0.4486 0.3322 0.0187  0.0218  0.0743  197 GLY A CA  
1572  C C   . GLY A 197 ? 0.2216 0.4313 0.3196 0.0114  0.0224  0.0725  197 GLY A C   
1573  O O   . GLY A 197 ? 0.2083 0.4137 0.3023 0.0107  0.0257  0.0681  197 GLY A O   
1574  N N   . GLY A 198 ? 0.1787 0.3787 0.2702 0.0063  0.0193  0.0760  198 GLY A N   
1575  C CA  . GLY A 198 ? 0.1739 0.3587 0.2534 -0.0008 0.0197  0.0745  198 GLY A CA  
1576  C C   . GLY A 198 ? 0.1569 0.3488 0.2311 -0.0096 0.0217  0.0736  198 GLY A C   
1577  O O   . GLY A 198 ? 0.1257 0.3070 0.1916 -0.0131 0.0236  0.0713  198 GLY A O   
1578  N N   . GLN A 199 ? 0.1237 0.3295 0.2004 -0.0129 0.0204  0.0746  199 GLN A N   
1579  C CA  . GLN A 199 ? 0.1657 0.3745 0.2364 -0.0200 0.0213  0.0721  199 GLN A CA  
1580  C C   . GLN A 199 ? 0.2090 0.4078 0.2699 -0.0295 0.0187  0.0726  199 GLN A C   
1581  O O   . GLN A 199 ? 0.1728 0.3730 0.2343 -0.0312 0.0154  0.0749  199 GLN A O   
1582  C CB  . GLN A 199 ? 0.1824 0.4103 0.2606 -0.0184 0.0212  0.0719  199 GLN A CB  
1583  C CG  . GLN A 199 ? 0.1432 0.3802 0.2309 -0.0087 0.0240  0.0698  199 GLN A CG  
1584  C CD  . GLN A 199 ? 0.1637 0.3968 0.2474 -0.0086 0.0281  0.0656  199 GLN A CD  
1585  O OE1 . GLN A 199 ? 0.2187 0.4514 0.2952 -0.0159 0.0291  0.0645  199 GLN A OE1 
1586  N NE2 . GLN A 199 ? 0.1492 0.3793 0.2374 -0.0004 0.0305  0.0632  199 GLN A NE2 
1587  N N   . PRO A 200 ? 0.1712 0.3600 0.2235 -0.0353 0.0200  0.0703  200 PRO A N   
1588  C CA  . PRO A 200 ? 0.1771 0.3528 0.2206 -0.0429 0.0178  0.0698  200 PRO A CA  
1589  C C   . PRO A 200 ? 0.1777 0.3631 0.2220 -0.0495 0.0156  0.0700  200 PRO A C   
1590  O O   . PRO A 200 ? 0.1941 0.3950 0.2436 -0.0499 0.0162  0.0701  200 PRO A O   
1591  C CB  . PRO A 200 ? 0.2342 0.3978 0.2699 -0.0458 0.0203  0.0677  200 PRO A CB  
1592  C CG  . PRO A 200 ? 0.1763 0.3523 0.2164 -0.0427 0.0234  0.0670  200 PRO A CG  
1593  C CD  . PRO A 200 ? 0.1344 0.3220 0.1844 -0.0344 0.0237  0.0679  200 PRO A CD  
1594  N N   . VAL A 201 ? 0.1891 0.3655 0.2280 -0.0546 0.0130  0.0697  201 VAL A N   
1595  C CA  . VAL A 201 ? 0.2341 0.4157 0.2713 -0.0626 0.0112  0.0687  201 VAL A CA  
1596  C C   . VAL A 201 ? 0.2398 0.4062 0.2687 -0.0693 0.0128  0.0663  201 VAL A C   
1597  O O   . VAL A 201 ? 0.2564 0.4056 0.2795 -0.0684 0.0133  0.0654  201 VAL A O   
1598  C CB  . VAL A 201 ? 0.2123 0.3951 0.2490 -0.0640 0.0075  0.0695  201 VAL A CB  
1599  C CG1 . VAL A 201 ? 0.2269 0.4199 0.2633 -0.0719 0.0057  0.0683  201 VAL A CG1 
1600  C CG2 . VAL A 201 ? 0.1626 0.3560 0.2068 -0.0560 0.0062  0.0732  201 VAL A CG2 
1601  N N   . SER A 202 ? 0.2253 0.3981 0.2542 -0.0757 0.0137  0.0654  202 SER A N   
1602  C CA  . SER A 202 ? 0.2225 0.3813 0.2445 -0.0820 0.0155  0.0640  202 SER A CA  
1603  C C   . SER A 202 ? 0.2091 0.3567 0.2259 -0.0878 0.0136  0.0622  202 SER A C   
1604  O O   . SER A 202 ? 0.2384 0.3938 0.2571 -0.0894 0.0107  0.0617  202 SER A O   
1605  C CB  . SER A 202 ? 0.2657 0.4349 0.2895 -0.0875 0.0174  0.0640  202 SER A CB  
1606  O OG  . SER A 202 ? 0.2209 0.3996 0.2464 -0.0943 0.0154  0.0629  202 SER A OG  
1607  N N   . MET A 203 ? 0.2468 0.3764 0.2569 -0.0907 0.0153  0.0613  203 MET A N   
1608  C CA  . MET A 203 ? 0.2412 0.3591 0.2463 -0.0963 0.0141  0.0591  203 MET A CA  
1609  C C   . MET A 203 ? 0.3027 0.4309 0.3094 -0.1049 0.0130  0.0575  203 MET A C   
1610  O O   . MET A 203 ? 0.2521 0.3814 0.2578 -0.1085 0.0106  0.0554  203 MET A O   
1611  C CB  . MET A 203 ? 0.2272 0.3252 0.2258 -0.0977 0.0166  0.0591  203 MET A CB  
1612  C CG  . MET A 203 ? 0.2754 0.3600 0.2691 -0.1028 0.0157  0.0566  203 MET A CG  
1613  S SD  . MET A 203 ? 0.2593 0.3380 0.2512 -0.0971 0.0132  0.0552  203 MET A SD  
1614  C CE  . MET A 203 ? 0.2012 0.2656 0.1899 -0.0888 0.0154  0.0571  203 MET A CE  
1615  N N   . SER A 204 ? 0.2758 0.4124 0.2849 -0.1087 0.0149  0.0583  204 SER A N   
1616  C CA  . SER A 204 ? 0.2589 0.4059 0.2697 -0.1173 0.0141  0.0565  204 SER A CA  
1617  C C   . SER A 204 ? 0.2648 0.4327 0.2814 -0.1157 0.0109  0.0564  204 SER A C   
1618  O O   . SER A 204 ? 0.2855 0.4609 0.3022 -0.1221 0.0090  0.0541  204 SER A O   
1619  C CB  . SER A 204 ? 0.2958 0.4464 0.3077 -0.1219 0.0171  0.0577  204 SER A CB  
1620  O OG  . SER A 204 ? 0.3481 0.5140 0.3654 -0.1167 0.0179  0.0598  204 SER A OG  
1621  N N   . ASN A 205 ? 0.3150 0.4928 0.3363 -0.1071 0.0103  0.0588  205 ASN A N   
1622  C CA  . ASN A 205 ? 0.2510 0.4474 0.2778 -0.1043 0.0071  0.0596  205 ASN A CA  
1623  C C   . ASN A 205 ? 0.2364 0.4273 0.2599 -0.1042 0.0041  0.0587  205 ASN A C   
1624  O O   . ASN A 205 ? 0.2378 0.4394 0.2617 -0.1086 0.0015  0.0574  205 ASN A O   
1625  C CB  . ASN A 205 ? 0.2243 0.4313 0.2576 -0.0946 0.0075  0.0627  205 ASN A CB  
1626  C CG  . ASN A 205 ? 0.2885 0.5173 0.3287 -0.0915 0.0047  0.0644  205 ASN A CG  
1627  O OD1 . ASN A 205 ? 0.2303 0.4620 0.2731 -0.0847 0.0028  0.0668  205 ASN A OD1 
1628  N ND2 . ASN A 205 ? 0.2313 0.4758 0.2747 -0.0963 0.0045  0.0636  205 ASN A ND2 
1629  N N   . LEU A 206 ? 0.2465 0.4214 0.2665 -0.0995 0.0045  0.0591  206 LEU A N   
1630  C CA  . LEU A 206 ? 0.2910 0.4598 0.3073 -0.0998 0.0021  0.0579  206 LEU A CA  
1631  C C   . LEU A 206 ? 0.2748 0.4387 0.2859 -0.1097 0.0016  0.0538  206 LEU A C   
1632  O O   . LEU A 206 ? 0.2343 0.4041 0.2440 -0.1124 -0.0011 0.0522  206 LEU A O   
1633  C CB  . LEU A 206 ? 0.2416 0.3920 0.2541 -0.0942 0.0033  0.0584  206 LEU A CB  
1634  C CG  . LEU A 206 ? 0.2493 0.4017 0.2662 -0.0843 0.0039  0.0618  206 LEU A CG  
1635  C CD1 . LEU A 206 ? 0.2328 0.3653 0.2448 -0.0805 0.0059  0.0611  206 LEU A CD1 
1636  C CD2 . LEU A 206 ? 0.2369 0.4014 0.2581 -0.0796 0.0010  0.0645  206 LEU A CD2 
1637  N N   . LYS A 207 ? 0.2722 0.4256 0.2804 -0.1153 0.0043  0.0519  207 LYS A N   
1638  C CA  . LYS A 207 ? 0.2773 0.4247 0.2812 -0.1251 0.0044  0.0477  207 LYS A CA  
1639  C C   . LYS A 207 ? 0.3098 0.4771 0.3170 -0.1311 0.0026  0.0462  207 LYS A C   
1640  O O   . LYS A 207 ? 0.3313 0.5016 0.3360 -0.1367 0.0007  0.0427  207 LYS A O   
1641  C CB  . LYS A 207 ? 0.3141 0.4452 0.3150 -0.1290 0.0080  0.0473  207 LYS A CB  
1642  C CG  . LYS A 207 ? 0.3806 0.5037 0.3778 -0.1393 0.0086  0.0430  207 LYS A CG  
1643  C CD  . LYS A 207 ? 0.3660 0.4725 0.3607 -0.1426 0.0124  0.0438  207 LYS A CD  
1644  C CE  . LYS A 207 ? 0.4477 0.5439 0.4391 -0.1526 0.0131  0.0394  207 LYS A CE  
1645  N NZ  . LYS A 207 ? 0.5829 0.6663 0.5733 -0.1570 0.0167  0.0410  207 LYS A NZ  
1646  N N   . GLU A 208 ? 0.2681 0.4500 0.2809 -0.1301 0.0032  0.0485  208 GLU A N   
1647  C CA  . GLU A 208 ? 0.3081 0.5101 0.3243 -0.1355 0.0015  0.0471  208 GLU A CA  
1648  C C   . GLU A 208 ? 0.2916 0.5090 0.3096 -0.1319 -0.0024 0.0479  208 GLU A C   
1649  O O   . GLU A 208 ? 0.3501 0.5787 0.3674 -0.1379 -0.0044 0.0451  208 GLU A O   
1650  C CB  . GLU A 208 ? 0.2998 0.5153 0.3221 -0.1343 0.0031  0.0496  208 GLU A CB  
1651  C CG  . GLU A 208 ? 0.3302 0.5672 0.3562 -0.1399 0.0016  0.0481  208 GLU A CG  
1652  C CD  . GLU A 208 ? 0.4741 0.7235 0.5057 -0.1400 0.0038  0.0498  208 GLU A CD  
1653  O OE1 . GLU A 208 ? 0.4795 0.7247 0.5129 -0.1339 0.0059  0.0527  208 GLU A OE1 
1654  O OE2 . GLU A 208 ? 0.5116 0.7760 0.5457 -0.1464 0.0033  0.0480  208 GLU A OE2 
1655  N N   . VAL A 209 ? 0.2812 0.4993 0.3013 -0.1223 -0.0035 0.0518  209 VAL A N   
1656  C CA  . VAL A 209 ? 0.2621 0.4934 0.2837 -0.1183 -0.0071 0.0537  209 VAL A CA  
1657  C C   . VAL A 209 ? 0.3107 0.5338 0.3254 -0.1232 -0.0086 0.0500  209 VAL A C   
1658  O O   . VAL A 209 ? 0.3176 0.5545 0.3316 -0.1259 -0.0113 0.0490  209 VAL A O   
1659  C CB  . VAL A 209 ? 0.2696 0.5009 0.2953 -0.1070 -0.0073 0.0589  209 VAL A CB  
1660  C CG1 . VAL A 209 ? 0.2646 0.5027 0.2899 -0.1032 -0.0107 0.0613  209 VAL A CG1 
1661  C CG2 . VAL A 209 ? 0.2061 0.4525 0.2398 -0.1018 -0.0066 0.0622  209 VAL A CG2 
1662  N N   . TYR A 210 ? 0.2934 0.4947 0.3028 -0.1243 -0.0067 0.0478  210 TYR A N   
1663  C CA  . TYR A 210 ? 0.2516 0.4447 0.2545 -0.1287 -0.0078 0.0438  210 TYR A CA  
1664  C C   . TYR A 210 ? 0.3273 0.5240 0.3275 -0.1395 -0.0078 0.0380  210 TYR A C   
1665  O O   . TYR A 210 ? 0.3344 0.5355 0.3308 -0.1433 -0.0096 0.0346  210 TYR A O   
1666  C CB  . TYR A 210 ? 0.2782 0.4471 0.2766 -0.1272 -0.0054 0.0426  210 TYR A CB  
1667  C CG  . TYR A 210 ? 0.3470 0.5082 0.3391 -0.1307 -0.0064 0.0384  210 TYR A CG  
1668  C CD1 . TYR A 210 ? 0.2968 0.4654 0.2885 -0.1261 -0.0089 0.0403  210 TYR A CD1 
1669  C CD2 . TYR A 210 ? 0.3453 0.4923 0.3323 -0.1386 -0.0045 0.0324  210 TYR A CD2 
1670  C CE1 . TYR A 210 ? 0.3061 0.4692 0.2919 -0.1295 -0.0095 0.0361  210 TYR A CE1 
1671  C CE2 . TYR A 210 ? 0.3145 0.4552 0.2961 -0.1417 -0.0051 0.0278  210 TYR A CE2 
1672  C CZ  . TYR A 210 ? 0.3157 0.4651 0.2965 -0.1373 -0.0076 0.0294  210 TYR A CZ  
1673  O OH  . TYR A 210 ? 0.3566 0.5010 0.3318 -0.1406 -0.0080 0.0244  210 TYR A OH  
1674  N N   . GLU A 211 ? 0.3500 0.5450 0.3518 -0.1446 -0.0055 0.0366  211 GLU A N   
1675  C CA  . GLU A 211 ? 0.3585 0.5559 0.3581 -0.1553 -0.0052 0.0309  211 GLU A CA  
1676  C C   . GLU A 211 ? 0.2998 0.5229 0.3024 -0.1572 -0.0080 0.0307  211 GLU A C   
1677  O O   . GLU A 211 ? 0.3537 0.5824 0.3533 -0.1641 -0.0092 0.0257  211 GLU A O   
1678  C CB  . GLU A 211 ? 0.3715 0.5583 0.3719 -0.1604 -0.0017 0.0301  211 GLU A CB  
1679  C CG  . GLU A 211 ? 0.4424 0.6025 0.4385 -0.1597 0.0012  0.0297  211 GLU A CG  
1680  C CD  . GLU A 211 ? 0.4967 0.6464 0.4939 -0.1626 0.0048  0.0311  211 GLU A CD  
1681  O OE1 . GLU A 211 ? 0.4754 0.6383 0.4775 -0.1620 0.0053  0.0340  211 GLU A OE1 
1682  O OE2 . GLU A 211 ? 0.5216 0.6499 0.5147 -0.1652 0.0071  0.0295  211 GLU A OE2 
1683  N N   . ILE A 212 ? 0.3225 0.5617 0.3314 -0.1509 -0.0091 0.0361  212 ILE A N   
1684  C CA  . ILE A 212 ? 0.2703 0.5349 0.2826 -0.1508 -0.0119 0.0371  212 ILE A CA  
1685  C C   . ILE A 212 ? 0.3518 0.6230 0.3609 -0.1481 -0.0150 0.0374  212 ILE A C   
1686  O O   . ILE A 212 ? 0.4033 0.6891 0.4110 -0.1526 -0.0169 0.0347  212 ILE A O   
1687  C CB  . ILE A 212 ? 0.2791 0.5578 0.2992 -0.1428 -0.0121 0.0432  212 ILE A CB  
1688  C CG1 . ILE A 212 ? 0.2625 0.5394 0.2857 -0.1470 -0.0090 0.0423  212 ILE A CG1 
1689  C CG2 . ILE A 212 ? 0.3268 0.6311 0.3505 -0.1403 -0.0153 0.0454  212 ILE A CG2 
1690  C CD1 . ILE A 212 ? 0.2221 0.5099 0.2527 -0.1388 -0.0084 0.0475  212 ILE A CD1 
1691  N N   . ALA A 213 ? 0.3125 0.5734 0.3202 -0.1407 -0.0154 0.0408  213 ALA A N   
1692  C CA  . ALA A 213 ? 0.3172 0.5837 0.3216 -0.1380 -0.0180 0.0418  213 ALA A CA  
1693  C C   . ALA A 213 ? 0.2958 0.5547 0.2927 -0.1467 -0.0178 0.0343  213 ALA A C   
1694  O O   . ALA A 213 ? 0.3379 0.6097 0.3322 -0.1484 -0.0199 0.0330  213 ALA A O   
1695  C CB  . ALA A 213 ? 0.3108 0.5667 0.3159 -0.1288 -0.0181 0.0470  213 ALA A CB  
1696  N N   . LYS A 214 ? 0.3304 0.5685 0.3241 -0.1519 -0.0149 0.0294  214 LYS A N   
1697  C CA  . LYS A 214 ? 0.3756 0.6046 0.3626 -0.1596 -0.0143 0.0217  214 LYS A CA  
1698  C C   . LYS A 214 ? 0.3548 0.5981 0.3415 -0.1684 -0.0149 0.0163  214 LYS A C   
1699  O O   . LYS A 214 ? 0.4144 0.6647 0.3969 -0.1719 -0.0161 0.0119  214 LYS A O   
1700  C CB  . LYS A 214 ? 0.3533 0.5558 0.3376 -0.1625 -0.0109 0.0182  214 LYS A CB  
1701  C CG  . LYS A 214 ? 0.3620 0.5493 0.3448 -0.1550 -0.0104 0.0215  214 LYS A CG  
1702  C CD  . LYS A 214 ? 0.4556 0.6490 0.4347 -0.1523 -0.0127 0.0212  214 LYS A CD  
1703  C CE  . LYS A 214 ? 0.3472 0.5524 0.3302 -0.1424 -0.0150 0.0297  214 LYS A CE  
1704  N NZ  . LYS A 214 ? 0.3200 0.5315 0.2993 -0.1402 -0.0171 0.0301  214 LYS A NZ  
1705  N N   . GLN A 215 ? 0.3648 0.6134 0.3558 -0.1722 -0.0138 0.0163  215 GLN A N   
1706  C CA  . GLN A 215 ? 0.3861 0.6489 0.3771 -0.1810 -0.0143 0.0110  215 GLN A CA  
1707  C C   . GLN A 215 ? 0.3823 0.6712 0.3742 -0.1781 -0.0177 0.0133  215 GLN A C   
1708  O O   . GLN A 215 ? 0.3888 0.6894 0.3789 -0.1850 -0.0184 0.0078  215 GLN A O   
1709  C CB  . GLN A 215 ? 0.4423 0.7071 0.4383 -0.1853 -0.0124 0.0113  215 GLN A CB  
1710  C CG  . GLN A 215 ? 0.4288 0.7085 0.4316 -0.1777 -0.0134 0.0189  215 GLN A CG  
1711  C CD  . GLN A 215 ? 0.5458 0.8259 0.5530 -0.1825 -0.0109 0.0188  215 GLN A CD  
1712  O OE1 . GLN A 215 ? 0.5005 0.7621 0.5058 -0.1885 -0.0079 0.0155  215 GLN A OE1 
1713  N NE2 . GLN A 215 ? 0.4761 0.7775 0.4893 -0.1796 -0.0121 0.0225  215 GLN A NE2 
1714  N N   . HIS A 216 ? 0.3812 0.6790 0.3761 -0.1679 -0.0196 0.0213  216 HIS A N   
1715  C CA  . HIS A 216 ? 0.3598 0.6804 0.3554 -0.1637 -0.0227 0.0250  216 HIS A CA  
1716  C C   . HIS A 216 ? 0.3847 0.7018 0.3749 -0.1602 -0.0239 0.0257  216 HIS A C   
1717  O O   . HIS A 216 ? 0.3555 0.6908 0.3455 -0.1571 -0.0261 0.0289  216 HIS A O   
1718  C CB  . HIS A 216 ? 0.3144 0.6480 0.3173 -0.1541 -0.0240 0.0340  216 HIS A CB  
1719  C CG  . HIS A 216 ? 0.3578 0.7040 0.3666 -0.1573 -0.0235 0.0336  216 HIS A CG  
1720  N ND1 . HIS A 216 ? 0.4036 0.7391 0.4159 -0.1579 -0.0210 0.0337  216 HIS A ND1 
1721  C CD2 . HIS A 216 ? 0.3318 0.7009 0.3434 -0.1601 -0.0249 0.0329  216 HIS A CD2 
1722  C CE1 . HIS A 216 ? 0.3192 0.6706 0.3362 -0.1612 -0.0209 0.0332  216 HIS A CE1 
1723  N NE2 . HIS A 216 ? 0.4273 0.7992 0.4441 -0.1625 -0.0234 0.0326  216 HIS A NE2 
1724  N N   . GLY A 217 ? 0.3634 0.6585 0.3494 -0.1604 -0.0223 0.0231  217 GLY A N   
1725  C CA  . GLY A 217 ? 0.3655 0.6572 0.3465 -0.1574 -0.0231 0.0234  217 GLY A CA  
1726  C C   . GLY A 217 ? 0.3319 0.6285 0.3159 -0.1464 -0.0248 0.0333  217 GLY A C   
1727  O O   . GLY A 217 ? 0.3569 0.6635 0.3386 -0.1433 -0.0264 0.0362  217 GLY A O   
1728  N N   . ILE A 218 ? 0.3644 0.6537 0.3536 -0.1404 -0.0242 0.0387  218 ILE A N   
1729  C CA  . ILE A 218 ? 0.2987 0.5918 0.2921 -0.1296 -0.0255 0.0481  218 ILE A CA  
1730  C C   . ILE A 218 ? 0.2531 0.5245 0.2448 -0.1263 -0.0242 0.0486  218 ILE A C   
1731  O O   . ILE A 218 ? 0.2541 0.5085 0.2455 -0.1290 -0.0218 0.0448  218 ILE A O   
1732  C CB  . ILE A 218 ? 0.2811 0.5845 0.2830 -0.1244 -0.0258 0.0536  218 ILE A CB  
1733  C CG1 . ILE A 218 ? 0.2809 0.6075 0.2848 -0.1275 -0.0273 0.0532  218 ILE A CG1 
1734  C CG2 . ILE A 218 ? 0.2705 0.5751 0.2776 -0.1131 -0.0266 0.0628  218 ILE A CG2 
1735  C CD1 . ILE A 218 ? 0.2694 0.6069 0.2815 -0.1239 -0.0272 0.0568  218 ILE A CD1 
1736  N N   . PHE A 219 ? 0.2851 0.5571 0.2757 -0.1204 -0.0253 0.0535  219 PHE A N   
1737  C CA  . PHE A 219 ? 0.2089 0.4624 0.1983 -0.1166 -0.0242 0.0545  219 PHE A CA  
1738  C C   . PHE A 219 ? 0.2361 0.4839 0.2329 -0.1089 -0.0234 0.0602  219 PHE A C   
1739  O O   . PHE A 219 ? 0.2507 0.5120 0.2539 -0.1034 -0.0245 0.0663  219 PHE A O   
1740  C CB  . PHE A 219 ? 0.2280 0.4866 0.2145 -0.1128 -0.0257 0.0586  219 PHE A CB  
1741  C CG  . PHE A 219 ? 0.2506 0.4914 0.2341 -0.1112 -0.0246 0.0576  219 PHE A CG  
1742  C CD1 . PHE A 219 ? 0.2839 0.5156 0.2599 -0.1177 -0.0235 0.0496  219 PHE A CD1 
1743  C CD2 . PHE A 219 ? 0.2404 0.4742 0.2290 -0.1028 -0.0244 0.0642  219 PHE A CD2 
1744  C CE1 . PHE A 219 ? 0.2682 0.4846 0.2417 -0.1159 -0.0222 0.0485  219 PHE A CE1 
1745  C CE2 . PHE A 219 ? 0.2359 0.4535 0.2219 -0.1011 -0.0229 0.0630  219 PHE A CE2 
1746  C CZ  . PHE A 219 ? 0.2481 0.4574 0.2265 -0.1077 -0.0217 0.0554  219 PHE A CZ  
1747  N N   . VAL A 220 ? 0.2262 0.4536 0.2224 -0.1083 -0.0209 0.0578  220 VAL A N   
1748  C CA  . VAL A 220 ? 0.2096 0.4296 0.2121 -0.1015 -0.0192 0.0617  220 VAL A CA  
1749  C C   . VAL A 220 ? 0.2125 0.4185 0.2147 -0.0951 -0.0182 0.0645  220 VAL A C   
1750  O O   . VAL A 220 ? 0.2156 0.4062 0.2119 -0.0979 -0.0167 0.0600  220 VAL A O   
1751  C CB  . VAL A 220 ? 0.2476 0.4556 0.2496 -0.1062 -0.0162 0.0567  220 VAL A CB  
1752  C CG1 . VAL A 220 ? 0.2297 0.4300 0.2372 -0.0990 -0.0140 0.0603  220 VAL A CG1 
1753  C CG2 . VAL A 220 ? 0.2101 0.4322 0.2130 -0.1127 -0.0169 0.0541  220 VAL A CG2 
1754  N N   . VAL A 221 ? 0.2321 0.4431 0.2409 -0.0863 -0.0186 0.0716  221 VAL A N   
1755  C CA  . VAL A 221 ? 0.1711 0.3685 0.1805 -0.0795 -0.0172 0.0743  221 VAL A CA  
1756  C C   . VAL A 221 ? 0.1830 0.3705 0.1972 -0.0740 -0.0143 0.0751  221 VAL A C   
1757  O O   . VAL A 221 ? 0.1945 0.3936 0.2157 -0.0706 -0.0145 0.0787  221 VAL A O   
1758  C CB  . VAL A 221 ? 0.1780 0.3870 0.1910 -0.0735 -0.0196 0.0821  221 VAL A CB  
1759  C CG1 . VAL A 221 ? 0.1542 0.3460 0.1673 -0.0663 -0.0176 0.0839  221 VAL A CG1 
1760  C CG2 . VAL A 221 ? 0.2238 0.4444 0.2312 -0.0791 -0.0225 0.0815  221 VAL A CG2 
1761  N N   . MET A 222 ? 0.2009 0.3682 0.2113 -0.0728 -0.0116 0.0717  222 MET A N   
1762  C CA  . MET A 222 ? 0.2165 0.3740 0.2302 -0.0675 -0.0088 0.0721  222 MET A CA  
1763  C C   . MET A 222 ? 0.2064 0.3603 0.2237 -0.0588 -0.0084 0.0768  222 MET A C   
1764  O O   . MET A 222 ? 0.2046 0.3454 0.2176 -0.0570 -0.0078 0.0753  222 MET A O   
1765  C CB  . MET A 222 ? 0.2417 0.3799 0.2491 -0.0705 -0.0061 0.0664  222 MET A CB  
1766  C CG  . MET A 222 ? 0.2177 0.3484 0.2277 -0.0663 -0.0032 0.0665  222 MET A CG  
1767  S SD  . MET A 222 ? 0.2986 0.4368 0.3101 -0.0724 -0.0023 0.0647  222 MET A SD  
1768  C CE  . MET A 222 ? 0.2368 0.3560 0.2394 -0.0792 -0.0006 0.0590  222 MET A CE  
1769  N N   . ASP A 223 ? 0.2292 0.3950 0.2549 -0.0533 -0.0084 0.0823  223 ASP A N   
1770  C CA  . ASP A 223 ? 0.2167 0.3767 0.2465 -0.0449 -0.0071 0.0864  223 ASP A CA  
1771  C C   . ASP A 223 ? 0.2139 0.3577 0.2419 -0.0429 -0.0037 0.0823  223 ASP A C   
1772  O O   . ASP A 223 ? 0.2049 0.3520 0.2359 -0.0430 -0.0019 0.0812  223 ASP A O   
1773  C CB  . ASP A 223 ? 0.2387 0.4163 0.2788 -0.0395 -0.0075 0.0938  223 ASP A CB  
1774  C CG  . ASP A 223 ? 0.2566 0.4263 0.3011 -0.0302 -0.0065 0.0978  223 ASP A CG  
1775  O OD1 . ASP A 223 ? 0.2776 0.4314 0.3198 -0.0281 -0.0038 0.0948  223 ASP A OD1 
1776  O OD2 . ASP A 223 ? 0.2252 0.4040 0.2753 -0.0248 -0.0087 0.1035  223 ASP A OD2 
1777  N N   . SER A 224 ? 0.1909 0.3185 0.2140 -0.0410 -0.0029 0.0799  224 SER A N   
1778  C CA  . SER A 224 ? 0.2235 0.3355 0.2424 -0.0408 -0.0003 0.0749  224 SER A CA  
1779  C C   . SER A 224 ? 0.2250 0.3288 0.2466 -0.0339 0.0018  0.0761  224 SER A C   
1780  O O   . SER A 224 ? 0.2462 0.3366 0.2634 -0.0333 0.0034  0.0721  224 SER A O   
1781  C CB  . SER A 224 ? 0.2022 0.3024 0.2126 -0.0452 -0.0007 0.0700  224 SER A CB  
1782  O OG  . SER A 224 ? 0.2258 0.3324 0.2333 -0.0524 -0.0021 0.0683  224 SER A OG  
1783  N N   . ALA A 225 ? 0.2074 0.3191 0.2365 -0.0286 0.0019  0.0817  225 ALA A N   
1784  C CA  . ALA A 225 ? 0.1950 0.2984 0.2271 -0.0225 0.0042  0.0828  225 ALA A CA  
1785  C C   . ALA A 225 ? 0.1964 0.2941 0.2273 -0.0220 0.0072  0.0789  225 ALA A C   
1786  O O   . ALA A 225 ? 0.1901 0.2759 0.2184 -0.0199 0.0087  0.0762  225 ALA A O   
1787  C CB  . ALA A 225 ? 0.1596 0.2710 0.2011 -0.0156 0.0037  0.0876  225 ALA A CB  
1788  N N   . ARG A 226 ? 0.1839 0.2906 0.2165 -0.0242 0.0081  0.0783  226 ARG A N   
1789  C CA  . ARG A 226 ? 0.1271 0.2304 0.1585 -0.0237 0.0110  0.0752  226 ARG A CA  
1790  C C   . ARG A 226 ? 0.1664 0.2671 0.1911 -0.0300 0.0105  0.0713  226 ARG A C   
1791  O O   . ARG A 226 ? 0.1670 0.2730 0.1925 -0.0312 0.0123  0.0705  226 ARG A O   
1792  C CB  . ARG A 226 ? 0.1371 0.2507 0.1773 -0.0179 0.0124  0.0756  226 ARG A CB  
1793  C CG  . ARG A 226 ? 0.1543 0.2642 0.2006 -0.0102 0.0120  0.0766  226 ARG A CG  
1794  C CD  . ARG A 226 ? 0.1831 0.3019 0.2388 -0.0035 0.0136  0.0761  226 ARG A CD  
1795  N NE  . ARG A 226 ? 0.1839 0.2978 0.2459 0.0036  0.0130  0.0776  226 ARG A NE  
1796  C CZ  . ARG A 226 ? 0.2299 0.3493 0.2970 0.0062  0.0106  0.0828  226 ARG A CZ  
1797  N NH1 . ARG A 226 ? 0.1823 0.3135 0.2489 0.0020  0.0082  0.0864  226 ARG A NH1 
1798  N NH2 . ARG A 226 ? 0.1680 0.2808 0.2408 0.0128  0.0104  0.0844  226 ARG A NH2 
1799  N N   . PHE A 227 ? 0.1536 0.2457 0.1718 -0.0341 0.0085  0.0689  227 PHE A N   
1800  C CA  . PHE A 227 ? 0.2028 0.2909 0.2152 -0.0402 0.0084  0.0658  227 PHE A CA  
1801  C C   . PHE A 227 ? 0.1819 0.2600 0.1898 -0.0398 0.0109  0.0634  227 PHE A C   
1802  O O   . PHE A 227 ? 0.2232 0.3014 0.2287 -0.0439 0.0118  0.0624  227 PHE A O   
1803  C CB  . PHE A 227 ? 0.2150 0.2964 0.2220 -0.0441 0.0064  0.0639  227 PHE A CB  
1804  C CG  . PHE A 227 ? 0.1966 0.2636 0.1988 -0.0416 0.0069  0.0615  227 PHE A CG  
1805  C CD1 . PHE A 227 ? 0.2145 0.2801 0.2191 -0.0366 0.0066  0.0628  227 PHE A CD1 
1806  C CD2 . PHE A 227 ? 0.2255 0.2809 0.2211 -0.0444 0.0077  0.0583  227 PHE A CD2 
1807  C CE1 . PHE A 227 ? 0.2349 0.2890 0.2355 -0.0347 0.0071  0.0604  227 PHE A CE1 
1808  C CE2 . PHE A 227 ? 0.2619 0.3060 0.2535 -0.0419 0.0081  0.0564  227 PHE A CE2 
1809  C CZ  . PHE A 227 ? 0.2238 0.2679 0.2179 -0.0372 0.0078  0.0571  227 PHE A CZ  
1810  N N   . CYS A 228 ? 0.2264 0.2962 0.2329 -0.0352 0.0120  0.0626  228 CYS A N   
1811  C CA  . CYS A 228 ? 0.1916 0.2529 0.1932 -0.0347 0.0139  0.0608  228 CYS A CA  
1812  C C   . CYS A 228 ? 0.1962 0.2668 0.2011 -0.0334 0.0162  0.0620  228 CYS A C   
1813  O O   . CYS A 228 ? 0.2581 0.3257 0.2588 -0.0353 0.0176  0.0612  228 CYS A O   
1814  C CB  . CYS A 228 ? 0.1821 0.2343 0.1816 -0.0303 0.0143  0.0596  228 CYS A CB  
1815  S SG  . CYS A 228 ? 0.2487 0.2898 0.2432 -0.0317 0.0124  0.0574  228 CYS A SG  
1816  N N   . GLU A 229 ? 0.1926 0.2747 0.2051 -0.0298 0.0169  0.0642  229 GLU A N   
1817  C CA  . GLU A 229 ? 0.1843 0.2783 0.2010 -0.0287 0.0194  0.0649  229 GLU A CA  
1818  C C   . GLU A 229 ? 0.2244 0.3253 0.2409 -0.0342 0.0189  0.0651  229 GLU A C   
1819  O O   . GLU A 229 ? 0.2257 0.3292 0.2403 -0.0360 0.0208  0.0645  229 GLU A O   
1820  C CB  . GLU A 229 ? 0.1874 0.2929 0.2139 -0.0229 0.0207  0.0673  229 GLU A CB  
1821  C CG  . GLU A 229 ? 0.2249 0.3193 0.2509 -0.0170 0.0207  0.0645  229 GLU A CG  
1822  C CD  . GLU A 229 ? 0.2119 0.3099 0.2470 -0.0099 0.0205  0.0639  229 GLU A CD  
1823  O OE1 . GLU A 229 ? 0.2304 0.3400 0.2726 -0.0085 0.0201  0.0661  229 GLU A OE1 
1824  O OE2 . GLU A 229 ? 0.2446 0.3337 0.2800 -0.0056 0.0207  0.0613  229 GLU A OE2 
1825  N N   . ASN A 230 ? 0.2025 0.3064 0.2204 -0.0376 0.0163  0.0659  230 ASN A N   
1826  C CA  . ASN A 230 ? 0.1823 0.2929 0.1999 -0.0437 0.0158  0.0658  230 ASN A CA  
1827  C C   . ASN A 230 ? 0.1980 0.2961 0.2075 -0.0485 0.0167  0.0638  230 ASN A C   
1828  O O   . ASN A 230 ? 0.2511 0.3534 0.2601 -0.0521 0.0181  0.0639  230 ASN A O   
1829  C CB  . ASN A 230 ? 0.1166 0.2326 0.1363 -0.0467 0.0128  0.0667  230 ASN A CB  
1830  C CG  . ASN A 230 ? 0.1896 0.3196 0.2126 -0.0514 0.0123  0.0673  230 ASN A CG  
1831  O OD1 . ASN A 230 ? 0.2293 0.3751 0.2599 -0.0486 0.0123  0.0694  230 ASN A OD1 
1832  N ND2 . ASN A 230 ? 0.2108 0.3354 0.2286 -0.0584 0.0122  0.0654  230 ASN A ND2 
1833  N N   . ALA A 231 ? 0.2058 0.2888 0.2094 -0.0483 0.0160  0.0624  231 ALA A N   
1834  C CA  . ALA A 231 ? 0.2140 0.2844 0.2105 -0.0517 0.0171  0.0613  231 ALA A CA  
1835  C C   . ALA A 231 ? 0.2422 0.3123 0.2368 -0.0498 0.0197  0.0620  231 ALA A C   
1836  O O   . ALA A 231 ? 0.2618 0.3296 0.2533 -0.0538 0.0211  0.0626  231 ALA A O   
1837  C CB  . ALA A 231 ? 0.1816 0.2374 0.1730 -0.0503 0.0161  0.0597  231 ALA A CB  
1838  N N   . TYR A 232 ? 0.2296 0.3023 0.2260 -0.0439 0.0205  0.0621  232 TYR A N   
1839  C CA  . TYR A 232 ? 0.2149 0.2895 0.2093 -0.0419 0.0230  0.0625  232 TYR A CA  
1840  C C   . TYR A 232 ? 0.2518 0.3391 0.2493 -0.0450 0.0247  0.0635  232 TYR A C   
1841  O O   . TYR A 232 ? 0.2630 0.3482 0.2562 -0.0475 0.0264  0.0643  232 TYR A O   
1842  C CB  . TYR A 232 ? 0.2102 0.2892 0.2076 -0.0353 0.0239  0.0620  232 TYR A CB  
1843  C CG  . TYR A 232 ? 0.2428 0.3253 0.2376 -0.0332 0.0265  0.0619  232 TYR A CG  
1844  C CD1 . TYR A 232 ? 0.2324 0.3041 0.2199 -0.0319 0.0266  0.0617  232 TYR A CD1 
1845  C CD2 . TYR A 232 ? 0.2440 0.3416 0.2435 -0.0322 0.0288  0.0620  232 TYR A CD2 
1846  C CE1 . TYR A 232 ? 0.2360 0.3121 0.2203 -0.0300 0.0288  0.0617  232 TYR A CE1 
1847  C CE2 . TYR A 232 ? 0.3173 0.4193 0.3139 -0.0303 0.0313  0.0614  232 TYR A CE2 
1848  C CZ  . TYR A 232 ? 0.3141 0.4052 0.3028 -0.0294 0.0311  0.0614  232 TYR A CZ  
1849  O OH  . TYR A 232 ? 0.3075 0.4040 0.2926 -0.0275 0.0333  0.0609  232 TYR A OH  
1850  N N   . PHE A 233 ? 0.2379 0.3390 0.2430 -0.0449 0.0241  0.0639  233 PHE A N   
1851  C CA  . PHE A 233 ? 0.2413 0.3562 0.2500 -0.0477 0.0256  0.0645  233 PHE A CA  
1852  C C   . PHE A 233 ? 0.2083 0.3189 0.2132 -0.0553 0.0253  0.0651  233 PHE A C   
1853  O O   . PHE A 233 ? 0.2311 0.3472 0.2355 -0.0584 0.0273  0.0658  233 PHE A O   
1854  C CB  . PHE A 233 ? 0.1865 0.3177 0.2046 -0.0452 0.0249  0.0650  233 PHE A CB  
1855  C CG  . PHE A 233 ? 0.2046 0.3432 0.2281 -0.0375 0.0266  0.0646  233 PHE A CG  
1856  C CD1 . PHE A 233 ? 0.2422 0.3865 0.2655 -0.0348 0.0298  0.0634  233 PHE A CD1 
1857  C CD2 . PHE A 233 ? 0.1857 0.3256 0.2146 -0.0329 0.0253  0.0654  233 PHE A CD2 
1858  C CE1 . PHE A 233 ? 0.2394 0.3907 0.2682 -0.0275 0.0318  0.0620  233 PHE A CE1 
1859  C CE2 . PHE A 233 ? 0.1899 0.3360 0.2250 -0.0255 0.0274  0.0650  233 PHE A CE2 
1860  C CZ  . PHE A 233 ? 0.1930 0.3448 0.2282 -0.0227 0.0308  0.0627  233 PHE A CZ  
1861  N N   . ILE A 234 ? 0.1946 0.2957 0.1971 -0.0587 0.0231  0.0646  234 ILE A N   
1862  C CA  . ILE A 234 ? 0.2170 0.3133 0.2162 -0.0663 0.0233  0.0648  234 ILE A CA  
1863  C C   . ILE A 234 ? 0.2583 0.3422 0.2505 -0.0672 0.0256  0.0660  234 ILE A C   
1864  O O   . ILE A 234 ? 0.2669 0.3523 0.2578 -0.0722 0.0274  0.0673  234 ILE A O   
1865  C CB  . ILE A 234 ? 0.2585 0.3474 0.2564 -0.0695 0.0207  0.0635  234 ILE A CB  
1866  C CG1 . ILE A 234 ? 0.1924 0.2965 0.1970 -0.0702 0.0184  0.0632  234 ILE A CG1 
1867  C CG2 . ILE A 234 ? 0.2382 0.3181 0.2316 -0.0770 0.0215  0.0635  234 ILE A CG2 
1868  C CD1 . ILE A 234 ? 0.1897 0.2886 0.1928 -0.0727 0.0157  0.0618  234 ILE A CD1 
1869  N N   . LYS A 235 ? 0.2395 0.3120 0.2272 -0.0624 0.0257  0.0658  235 LYS A N   
1870  C CA  . LYS A 235 ? 0.2581 0.3202 0.2391 -0.0623 0.0277  0.0675  235 LYS A CA  
1871  C C   . LYS A 235 ? 0.3141 0.3871 0.2957 -0.0609 0.0301  0.0689  235 LYS A C   
1872  O O   . LYS A 235 ? 0.2659 0.3354 0.2431 -0.0636 0.0322  0.0712  235 LYS A O   
1873  C CB  . LYS A 235 ? 0.2599 0.3092 0.2364 -0.0570 0.0269  0.0669  235 LYS A CB  
1874  C CG  . LYS A 235 ? 0.3143 0.3535 0.2836 -0.0559 0.0286  0.0691  235 LYS A CG  
1875  C CD  . LYS A 235 ? 0.2984 0.3270 0.2637 -0.0505 0.0273  0.0682  235 LYS A CD  
1876  C CE  . LYS A 235 ? 0.3504 0.3724 0.3086 -0.0482 0.0287  0.0709  235 LYS A CE  
1877  N NZ  . LYS A 235 ? 0.4100 0.4226 0.3641 -0.0528 0.0302  0.0741  235 LYS A NZ  
1878  N N   . ALA A 236 ? 0.2591 0.3458 0.2464 -0.0567 0.0301  0.0676  236 ALA A N   
1879  C CA  . ALA A 236 ? 0.2337 0.3325 0.2221 -0.0551 0.0326  0.0681  236 ALA A CA  
1880  C C   . ALA A 236 ? 0.2651 0.3746 0.2561 -0.0609 0.0341  0.0693  236 ALA A C   
1881  O O   . ALA A 236 ? 0.3125 0.4254 0.3006 -0.0624 0.0365  0.0709  236 ALA A O   
1882  C CB  . ALA A 236 ? 0.2410 0.3518 0.2356 -0.0488 0.0326  0.0660  236 ALA A CB  
1883  N N   . ARG A 237 ? 0.2386 0.3540 0.2348 -0.0644 0.0326  0.0686  237 ARG A N   
1884  C CA  . ARG A 237 ? 0.2688 0.3988 0.2694 -0.0691 0.0338  0.0692  237 ARG A CA  
1885  C C   . ARG A 237 ? 0.3128 0.4376 0.3118 -0.0775 0.0333  0.0702  237 ARG A C   
1886  O O   . ARG A 237 ? 0.3216 0.4579 0.3235 -0.0823 0.0345  0.0708  237 ARG A O   
1887  C CB  . ARG A 237 ? 0.1893 0.3365 0.1990 -0.0658 0.0326  0.0675  237 ARG A CB  
1888  C CG  . ARG A 237 ? 0.1982 0.3497 0.2105 -0.0573 0.0332  0.0661  237 ARG A CG  
1889  C CD  . ARG A 237 ? 0.2197 0.3883 0.2419 -0.0532 0.0327  0.0650  237 ARG A CD  
1890  N NE  . ARG A 237 ? 0.2080 0.3812 0.2334 -0.0450 0.0341  0.0635  237 ARG A NE  
1891  C CZ  . ARG A 237 ? 0.1974 0.3817 0.2315 -0.0391 0.0338  0.0626  237 ARG A CZ  
1892  N NH1 . ARG A 237 ? 0.1960 0.3879 0.2360 -0.0403 0.0316  0.0636  237 ARG A NH1 
1893  N NH2 . ARG A 237 ? 0.1792 0.3673 0.2165 -0.0317 0.0359  0.0605  237 ARG A NH2 
1894  N N   . ASP A 238 ? 0.2739 0.3824 0.2686 -0.0795 0.0319  0.0702  238 ASP A N   
1895  C CA  . ASP A 238 ? 0.2727 0.3759 0.2662 -0.0876 0.0317  0.0706  238 ASP A CA  
1896  C C   . ASP A 238 ? 0.3226 0.4092 0.3087 -0.0903 0.0338  0.0732  238 ASP A C   
1897  O O   . ASP A 238 ? 0.3219 0.3929 0.3032 -0.0873 0.0331  0.0733  238 ASP A O   
1898  C CB  . ASP A 238 ? 0.2979 0.3962 0.2926 -0.0885 0.0285  0.0683  238 ASP A CB  
1899  C CG  . ASP A 238 ? 0.3428 0.4397 0.3376 -0.0975 0.0281  0.0677  238 ASP A CG  
1900  O OD1 . ASP A 238 ? 0.3548 0.4472 0.3469 -0.1030 0.0305  0.0696  238 ASP A OD1 
1901  O OD2 . ASP A 238 ? 0.2898 0.3903 0.2871 -0.0993 0.0254  0.0654  238 ASP A OD2 
1902  N N   . PRO A 239 ? 0.3443 0.4336 0.3292 -0.0957 0.0364  0.0757  239 PRO A N   
1903  C CA  . PRO A 239 ? 0.3582 0.4315 0.3361 -0.0979 0.0387  0.0793  239 PRO A CA  
1904  C C   . PRO A 239 ? 0.3784 0.4338 0.3534 -0.1008 0.0376  0.0790  239 PRO A C   
1905  O O   . PRO A 239 ? 0.3436 0.3833 0.3127 -0.0997 0.0389  0.0818  239 PRO A O   
1906  C CB  . PRO A 239 ? 0.3531 0.4351 0.3321 -0.1049 0.0415  0.0818  239 PRO A CB  
1907  C CG  . PRO A 239 ? 0.3375 0.4376 0.3241 -0.1079 0.0401  0.0788  239 PRO A CG  
1908  C CD  . PRO A 239 ? 0.3376 0.4452 0.3278 -0.1001 0.0375  0.0757  239 PRO A CD  
1909  N N   . LYS A 240 ? 0.3437 0.4016 0.3225 -0.1043 0.0353  0.0757  240 LYS A N   
1910  C CA  . LYS A 240 ? 0.3126 0.3545 0.2889 -0.1069 0.0341  0.0745  240 LYS A CA  
1911  C C   . LYS A 240 ? 0.3439 0.3744 0.3167 -0.0991 0.0328  0.0738  240 LYS A C   
1912  O O   . LYS A 240 ? 0.3848 0.3988 0.3537 -0.0995 0.0328  0.0743  240 LYS A O   
1913  C CB  . LYS A 240 ? 0.3610 0.4110 0.3419 -0.1122 0.0317  0.0705  240 LYS A CB  
1914  C CG  . LYS A 240 ? 0.4102 0.4455 0.3887 -0.1158 0.0303  0.0682  240 LYS A CG  
1915  C CD  . LYS A 240 ? 0.4636 0.5096 0.4462 -0.1219 0.0280  0.0642  240 LYS A CD  
1916  C CE  . LYS A 240 ? 0.4984 0.5562 0.4844 -0.1298 0.0294  0.0648  240 LYS A CE  
1917  N NZ  . LYS A 240 ? 0.5305 0.5984 0.5199 -0.1367 0.0271  0.0607  240 LYS A NZ  
1918  N N   . TYR A 241 ? 0.2869 0.3259 0.2612 -0.0919 0.0317  0.0727  241 TYR A N   
1919  C CA  . TYR A 241 ? 0.2877 0.3181 0.2595 -0.0848 0.0301  0.0715  241 TYR A CA  
1920  C C   . TYR A 241 ? 0.3144 0.3440 0.2828 -0.0781 0.0315  0.0736  241 TYR A C   
1921  O O   . TYR A 241 ? 0.3506 0.3751 0.3172 -0.0719 0.0302  0.0724  241 TYR A O   
1922  C CB  . TYR A 241 ? 0.2944 0.3345 0.2711 -0.0823 0.0273  0.0680  241 TYR A CB  
1923  C CG  . TYR A 241 ? 0.3036 0.3422 0.2818 -0.0882 0.0254  0.0656  241 TYR A CG  
1924  C CD1 . TYR A 241 ? 0.3055 0.3296 0.2801 -0.0883 0.0244  0.0642  241 TYR A CD1 
1925  C CD2 . TYR A 241 ? 0.3460 0.3983 0.3290 -0.0937 0.0246  0.0645  241 TYR A CD2 
1926  C CE1 . TYR A 241 ? 0.3588 0.3820 0.3342 -0.0942 0.0227  0.0614  241 TYR A CE1 
1927  C CE2 . TYR A 241 ? 0.3214 0.3733 0.3052 -0.0996 0.0228  0.0619  241 TYR A CE2 
1928  C CZ  . TYR A 241 ? 0.3631 0.4002 0.3429 -0.1000 0.0219  0.0602  241 TYR A CZ  
1929  O OH  . TYR A 241 ? 0.3723 0.4095 0.3522 -0.1062 0.0202  0.0569  241 TYR A OH  
1930  N N   . LYS A 242 ? 0.3244 0.3594 0.2916 -0.0796 0.0340  0.0765  242 LYS A N   
1931  C CA  . LYS A 242 ? 0.3505 0.3881 0.3145 -0.0738 0.0351  0.0780  242 LYS A CA  
1932  C C   . LYS A 242 ? 0.3660 0.3873 0.3229 -0.0695 0.0351  0.0797  242 LYS A C   
1933  O O   . LYS A 242 ? 0.3589 0.3815 0.3133 -0.0634 0.0348  0.0795  242 LYS A O   
1934  C CB  . LYS A 242 ? 0.3533 0.3993 0.3165 -0.0773 0.0380  0.0811  242 LYS A CB  
1935  C CG  . LYS A 242 ? 0.4415 0.4926 0.4012 -0.0720 0.0393  0.0825  242 LYS A CG  
1936  C CD  . LYS A 242 ? 0.5110 0.5723 0.4702 -0.0759 0.0422  0.0854  242 LYS A CD  
1937  C CE  . LYS A 242 ? 0.4889 0.5587 0.4453 -0.0706 0.0432  0.0857  242 LYS A CE  
1938  N NZ  . LYS A 242 ? 0.5353 0.5920 0.4849 -0.0651 0.0421  0.0867  242 LYS A NZ  
1939  N N   . ASN A 243 ? 0.3429 0.3495 0.2971 -0.0725 0.0353  0.0813  243 ASN A N   
1940  C CA  . ASN A 243 ? 0.3577 0.3488 0.3056 -0.0682 0.0353  0.0835  243 ASN A CA  
1941  C C   . ASN A 243 ? 0.4031 0.3844 0.3518 -0.0668 0.0330  0.0806  243 ASN A C   
1942  O O   . ASN A 243 ? 0.4509 0.4183 0.3953 -0.0643 0.0329  0.0825  243 ASN A O   
1943  C CB  . ASN A 243 ? 0.3817 0.3626 0.3249 -0.0719 0.0380  0.0889  243 ASN A CB  
1944  C CG  . ASN A 243 ? 0.4081 0.3987 0.3492 -0.0729 0.0404  0.0922  243 ASN A CG  
1945  O OD1 . ASN A 243 ? 0.4144 0.4054 0.3502 -0.0679 0.0408  0.0941  243 ASN A OD1 
1946  N ND2 . ASN A 243 ? 0.3720 0.3715 0.3170 -0.0797 0.0419  0.0926  243 ASN A ND2 
1947  N N   . ALA A 244 ? 0.3569 0.3457 0.3112 -0.0684 0.0310  0.0763  244 ALA A N   
1948  C CA  . ALA A 244 ? 0.3362 0.3181 0.2911 -0.0668 0.0287  0.0732  244 ALA A CA  
1949  C C   . ALA A 244 ? 0.3417 0.3266 0.2963 -0.0592 0.0272  0.0714  244 ALA A C   
1950  O O   . ALA A 244 ? 0.3494 0.3434 0.3042 -0.0558 0.0276  0.0716  244 ALA A O   
1951  C CB  . ALA A 244 ? 0.3060 0.2951 0.2663 -0.0724 0.0272  0.0699  244 ALA A CB  
1952  N N   . THR A 245 ? 0.3443 0.3215 0.2981 -0.0568 0.0254  0.0693  245 THR A N   
1953  C CA  . THR A 245 ? 0.3176 0.2982 0.2720 -0.0506 0.0238  0.0670  245 THR A CA  
1954  C C   . THR A 245 ? 0.3361 0.3288 0.2968 -0.0518 0.0223  0.0639  245 THR A C   
1955  O O   . THR A 245 ? 0.3617 0.3590 0.3255 -0.0572 0.0220  0.0631  245 THR A O   
1956  C CB  . THR A 245 ? 0.3259 0.2944 0.2773 -0.0478 0.0225  0.0662  245 THR A CB  
1957  O OG1 . THR A 245 ? 0.3126 0.2780 0.2660 -0.0525 0.0213  0.0638  245 THR A OG1 
1958  C CG2 . THR A 245 ? 0.3454 0.3015 0.2912 -0.0464 0.0236  0.0700  245 THR A CG2 
1959  N N   . ILE A 246 ? 0.2731 0.2714 0.2356 -0.0466 0.0213  0.0624  246 ILE A N   
1960  C CA  . ILE A 246 ? 0.2977 0.3065 0.2661 -0.0467 0.0199  0.0602  246 ILE A CA  
1961  C C   . ILE A 246 ? 0.2928 0.2975 0.2618 -0.0498 0.0183  0.0584  246 ILE A C   
1962  O O   . ILE A 246 ? 0.2748 0.2874 0.2476 -0.0535 0.0173  0.0576  246 ILE A O   
1963  C CB  . ILE A 246 ? 0.2554 0.2690 0.2257 -0.0407 0.0194  0.0593  246 ILE A CB  
1964  C CG1 . ILE A 246 ? 0.2692 0.2908 0.2402 -0.0386 0.0210  0.0607  246 ILE A CG1 
1965  C CG2 . ILE A 246 ? 0.2429 0.2645 0.2192 -0.0404 0.0178  0.0579  246 ILE A CG2 
1966  C CD1 . ILE A 246 ? 0.2405 0.2753 0.2170 -0.0414 0.0217  0.0613  246 ILE A CD1 
1967  N N   . LYS A 247 ? 0.2557 0.2487 0.2205 -0.0484 0.0178  0.0577  247 LYS A N   
1968  C CA  . LYS A 247 ? 0.3177 0.3069 0.2823 -0.0516 0.0163  0.0556  247 LYS A CA  
1969  C C   . LYS A 247 ? 0.2822 0.2693 0.2461 -0.0591 0.0166  0.0555  247 LYS A C   
1970  O O   . LYS A 247 ? 0.2645 0.2551 0.2298 -0.0635 0.0152  0.0533  247 LYS A O   
1971  C CB  . LYS A 247 ? 0.3396 0.3170 0.2997 -0.0485 0.0159  0.0549  247 LYS A CB  
1972  C CG  . LYS A 247 ? 0.3014 0.2819 0.2626 -0.0424 0.0151  0.0541  247 LYS A CG  
1973  C CD  . LYS A 247 ? 0.3473 0.3173 0.3042 -0.0403 0.0144  0.0533  247 LYS A CD  
1974  C CE  . LYS A 247 ? 0.3195 0.2932 0.2777 -0.0349 0.0137  0.0525  247 LYS A CE  
1975  N NZ  . LYS A 247 ? 0.3502 0.3143 0.3039 -0.0331 0.0129  0.0518  247 LYS A NZ  
1976  N N   . GLU A 248 ? 0.3263 0.3082 0.2882 -0.0612 0.0184  0.0577  248 GLU A N   
1977  C CA  . GLU A 248 ? 0.3119 0.2922 0.2738 -0.0691 0.0189  0.0576  248 GLU A CA  
1978  C C   . GLU A 248 ? 0.3219 0.3181 0.2891 -0.0726 0.0183  0.0571  248 GLU A C   
1979  O O   . GLU A 248 ? 0.3053 0.3047 0.2736 -0.0791 0.0174  0.0551  248 GLU A O   
1980  C CB  . GLU A 248 ? 0.3183 0.2894 0.2771 -0.0700 0.0211  0.0610  248 GLU A CB  
1981  C CG  . GLU A 248 ? 0.3796 0.3332 0.3334 -0.0687 0.0213  0.0616  248 GLU A CG  
1982  C CD  . GLU A 248 ? 0.4043 0.3493 0.3550 -0.0671 0.0234  0.0663  248 GLU A CD  
1983  O OE1 . GLU A 248 ? 0.3527 0.3053 0.3043 -0.0675 0.0250  0.0689  248 GLU A OE1 
1984  O OE2 . GLU A 248 ? 0.4571 0.3877 0.4041 -0.0653 0.0233  0.0676  248 GLU A OE2 
1985  N N   . VAL A 249 ? 0.3083 0.3149 0.2785 -0.0686 0.0188  0.0586  249 VAL A N   
1986  C CA  . VAL A 249 ? 0.2659 0.2887 0.2417 -0.0709 0.0181  0.0584  249 VAL A CA  
1987  C C   . VAL A 249 ? 0.2526 0.2818 0.2311 -0.0709 0.0154  0.0563  249 VAL A C   
1988  O O   . VAL A 249 ? 0.2533 0.2913 0.2343 -0.0762 0.0142  0.0554  249 VAL A O   
1989  C CB  . VAL A 249 ? 0.2085 0.2405 0.1871 -0.0659 0.0192  0.0602  249 VAL A CB  
1990  C CG1 . VAL A 249 ? 0.2234 0.2726 0.2086 -0.0671 0.0181  0.0601  249 VAL A CG1 
1991  C CG2 . VAL A 249 ? 0.2512 0.2797 0.2269 -0.0672 0.0218  0.0626  249 VAL A CG2 
1992  N N   . ILE A 250 ? 0.2677 0.2934 0.2456 -0.0651 0.0146  0.0556  250 ILE A N   
1993  C CA  . ILE A 250 ? 0.2438 0.2753 0.2238 -0.0648 0.0122  0.0542  250 ILE A CA  
1994  C C   . ILE A 250 ? 0.2826 0.3110 0.2598 -0.0718 0.0112  0.0520  250 ILE A C   
1995  O O   . ILE A 250 ? 0.2726 0.3117 0.2523 -0.0756 0.0094  0.0513  250 ILE A O   
1996  C CB  . ILE A 250 ? 0.2576 0.2833 0.2364 -0.0581 0.0119  0.0538  250 ILE A CB  
1997  C CG1 . ILE A 250 ? 0.2529 0.2848 0.2355 -0.0519 0.0126  0.0554  250 ILE A CG1 
1998  C CG2 . ILE A 250 ? 0.2586 0.2871 0.2378 -0.0590 0.0098  0.0524  250 ILE A CG2 
1999  C CD1 . ILE A 250 ? 0.2693 0.2939 0.2502 -0.0460 0.0128  0.0547  250 ILE A CD1 
2000  N N   . PHE A 251 ? 0.2848 0.2985 0.2567 -0.0738 0.0123  0.0508  251 PHE A N   
2001  C CA  . PHE A 251 ? 0.2713 0.2799 0.2400 -0.0811 0.0116  0.0478  251 PHE A CA  
2002  C C   . PHE A 251 ? 0.3119 0.3300 0.2829 -0.0887 0.0113  0.0472  251 PHE A C   
2003  O O   . PHE A 251 ? 0.3168 0.3420 0.2881 -0.0938 0.0096  0.0447  251 PHE A O   
2004  C CB  . PHE A 251 ? 0.2818 0.2720 0.2451 -0.0818 0.0133  0.0473  251 PHE A CB  
2005  C CG  . PHE A 251 ? 0.2876 0.2690 0.2467 -0.0876 0.0128  0.0432  251 PHE A CG  
2006  C CD1 . PHE A 251 ? 0.2815 0.2601 0.2381 -0.0853 0.0119  0.0411  251 PHE A CD1 
2007  C CD2 . PHE A 251 ? 0.3249 0.3007 0.2826 -0.0957 0.0135  0.0410  251 PHE A CD2 
2008  C CE1 . PHE A 251 ? 0.3528 0.3233 0.3051 -0.0911 0.0118  0.0365  251 PHE A CE1 
2009  C CE2 . PHE A 251 ? 0.3256 0.2924 0.2793 -0.1013 0.0133  0.0360  251 PHE A CE2 
2010  C CZ  . PHE A 251 ? 0.3873 0.3515 0.3382 -0.0991 0.0125  0.0335  251 PHE A CZ  
2011  N N   . ASP A 252 ? 0.3045 0.3242 0.2773 -0.0896 0.0129  0.0494  252 ASP A N   
2012  C CA  . ASP A 252 ? 0.2750 0.3042 0.2503 -0.0970 0.0127  0.0488  252 ASP A CA  
2013  C C   . ASP A 252 ? 0.2785 0.3274 0.2591 -0.0964 0.0105  0.0492  252 ASP A C   
2014  O O   . ASP A 252 ? 0.2957 0.3537 0.2773 -0.1029 0.0090  0.0472  252 ASP A O   
2015  C CB  . ASP A 252 ? 0.2891 0.3163 0.2651 -0.0977 0.0152  0.0516  252 ASP A CB  
2016  C CG  . ASP A 252 ? 0.3696 0.3797 0.3411 -0.1023 0.0172  0.0513  252 ASP A CG  
2017  O OD1 . ASP A 252 ? 0.3679 0.3656 0.3355 -0.1035 0.0168  0.0488  252 ASP A OD1 
2018  O OD2 . ASP A 252 ? 0.3685 0.3774 0.3404 -0.1049 0.0193  0.0537  252 ASP A OD2 
2019  N N   . MET A 253 ? 0.2707 0.3263 0.2546 -0.0887 0.0101  0.0517  253 MET A N   
2020  C CA  . MET A 253 ? 0.2577 0.3313 0.2472 -0.0870 0.0079  0.0530  253 MET A CA  
2021  C C   . MET A 253 ? 0.2880 0.3666 0.2764 -0.0903 0.0052  0.0510  253 MET A C   
2022  O O   . MET A 253 ? 0.2702 0.3638 0.2616 -0.0942 0.0033  0.0509  253 MET A O   
2023  C CB  . MET A 253 ? 0.2556 0.3313 0.2482 -0.0778 0.0080  0.0555  253 MET A CB  
2024  C CG  . MET A 253 ? 0.2607 0.3376 0.2555 -0.0745 0.0104  0.0574  253 MET A CG  
2025  S SD  . MET A 253 ? 0.2905 0.3693 0.2887 -0.0644 0.0107  0.0594  253 MET A SD  
2026  C CE  . MET A 253 ? 0.2585 0.3523 0.2625 -0.0630 0.0076  0.0610  253 MET A CE  
2027  N N   . TYR A 254 ? 0.2648 0.3321 0.2488 -0.0890 0.0051  0.0492  254 TYR A N   
2028  C CA  . TYR A 254 ? 0.2561 0.3291 0.2387 -0.0913 0.0028  0.0476  254 TYR A CA  
2029  C C   . TYR A 254 ? 0.2945 0.3660 0.2732 -0.1010 0.0025  0.0431  254 TYR A C   
2030  O O   . TYR A 254 ? 0.2828 0.3595 0.2594 -0.1040 0.0007  0.0409  254 TYR A O   
2031  C CB  . TYR A 254 ? 0.2562 0.3195 0.2361 -0.0856 0.0030  0.0475  254 TYR A CB  
2032  C CG  . TYR A 254 ? 0.2621 0.3322 0.2471 -0.0771 0.0024  0.0515  254 TYR A CG  
2033  C CD1 . TYR A 254 ? 0.2461 0.3111 0.2331 -0.0716 0.0043  0.0532  254 TYR A CD1 
2034  C CD2 . TYR A 254 ? 0.2424 0.3251 0.2304 -0.0752 0.0001  0.0537  254 TYR A CD2 
2035  C CE1 . TYR A 254 ? 0.2496 0.3207 0.2416 -0.0646 0.0041  0.0562  254 TYR A CE1 
2036  C CE2 . TYR A 254 ? 0.2340 0.3219 0.2273 -0.0678 -0.0002 0.0575  254 TYR A CE2 
2037  C CZ  . TYR A 254 ? 0.2542 0.3361 0.2496 -0.0627 0.0019  0.0584  254 TYR A CZ  
2038  O OH  . TYR A 254 ? 0.2538 0.3406 0.2546 -0.0560 0.0019  0.0617  254 TYR A OH  
2039  N N   . LYS A 255 ? 0.2672 0.3322 0.2449 -0.1062 0.0042  0.0416  255 LYS A N   
2040  C CA  . LYS A 255 ? 0.3255 0.3927 0.3012 -0.1159 0.0038  0.0372  255 LYS A CA  
2041  C C   . LYS A 255 ? 0.2966 0.3854 0.2768 -0.1190 0.0016  0.0379  255 LYS A C   
2042  O O   . LYS A 255 ? 0.3021 0.3964 0.2809 -0.1270 0.0007  0.0337  255 LYS A O   
2043  C CB  . LYS A 255 ? 0.3151 0.3682 0.2889 -0.1204 0.0065  0.0360  255 LYS A CB  
2044  C CG  . LYS A 255 ? 0.3484 0.3796 0.3174 -0.1178 0.0086  0.0355  255 LYS A CG  
2045  C CD  . LYS A 255 ? 0.3356 0.3540 0.3036 -0.1212 0.0112  0.0360  255 LYS A CD  
2046  C CE  . LYS A 255 ? 0.3394 0.3377 0.3034 -0.1165 0.0131  0.0372  255 LYS A CE  
2047  N NZ  . LYS A 255 ? 0.4548 0.4414 0.4181 -0.1192 0.0156  0.0392  255 LYS A NZ  
2048  N N   . TYR A 256 ? 0.2656 0.3666 0.2511 -0.1127 0.0007  0.0426  256 TYR A N   
2049  C CA  . TYR A 256 ? 0.2745 0.3964 0.2651 -0.1143 -0.0013 0.0442  256 TYR A CA  
2050  C C   . TYR A 256 ? 0.2685 0.4047 0.2621 -0.1088 -0.0042 0.0475  256 TYR A C   
2051  O O   . TYR A 256 ? 0.2671 0.4186 0.2666 -0.1049 -0.0055 0.0514  256 TYR A O   
2052  C CB  . TYR A 256 ? 0.2986 0.4237 0.2939 -0.1121 0.0005  0.0472  256 TYR A CB  
2053  C CG  . TYR A 256 ? 0.3104 0.4205 0.3024 -0.1172 0.0035  0.0451  256 TYR A CG  
2054  C CD1 . TYR A 256 ? 0.2925 0.3994 0.2814 -0.1267 0.0038  0.0407  256 TYR A CD1 
2055  C CD2 . TYR A 256 ? 0.2937 0.3923 0.2855 -0.1126 0.0063  0.0475  256 TYR A CD2 
2056  C CE1 . TYR A 256 ? 0.3250 0.4171 0.3113 -0.1313 0.0067  0.0394  256 TYR A CE1 
2057  C CE2 . TYR A 256 ? 0.3523 0.4373 0.3410 -0.1171 0.0090  0.0466  256 TYR A CE2 
2058  C CZ  . TYR A 256 ? 0.3601 0.4413 0.3463 -0.1263 0.0092  0.0429  256 TYR A CZ  
2059  O OH  . TYR A 256 ? 0.3999 0.4666 0.3835 -0.1306 0.0120  0.0426  256 TYR A OH  
2060  N N   . ALA A 257 ? 0.2646 0.3958 0.2541 -0.1085 -0.0052 0.0460  257 ALA A N   
2061  C CA  . ALA A 257 ? 0.2552 0.4001 0.2463 -0.1050 -0.0081 0.0489  257 ALA A CA  
2062  C C   . ALA A 257 ? 0.2579 0.3986 0.2425 -0.1098 -0.0088 0.0445  257 ALA A C   
2063  O O   . ALA A 257 ? 0.2904 0.4152 0.2701 -0.1139 -0.0067 0.0396  257 ALA A O   
2064  C CB  . ALA A 257 ? 0.2161 0.3585 0.2111 -0.0948 -0.0079 0.0543  257 ALA A CB  
2065  N N   . ASP A 258 ? 0.2389 0.3948 0.2237 -0.1093 -0.0117 0.0464  258 ASP A N   
2066  C CA  . ASP A 258 ? 0.2056 0.3608 0.1844 -0.1133 -0.0124 0.0425  258 ASP A CA  
2067  C C   . ASP A 258 ? 0.2412 0.3922 0.2193 -0.1064 -0.0124 0.0462  258 ASP A C   
2068  O O   . ASP A 258 ? 0.2348 0.3830 0.2077 -0.1092 -0.0122 0.0427  258 ASP A O   
2069  C CB  . ASP A 258 ? 0.2259 0.4020 0.2037 -0.1183 -0.0155 0.0414  258 ASP A CB  
2070  C CG  . ASP A 258 ? 0.2609 0.4417 0.2391 -0.1253 -0.0152 0.0372  258 ASP A CG  
2071  O OD1 . ASP A 258 ? 0.3120 0.4785 0.2866 -0.1314 -0.0129 0.0306  258 ASP A OD1 
2072  O OD2 . ASP A 258 ? 0.2387 0.4367 0.2211 -0.1243 -0.0171 0.0408  258 ASP A OD2 
2073  N N   . ALA A 259 ? 0.2063 0.3569 0.1898 -0.0975 -0.0123 0.0526  259 ALA A N   
2074  C CA  . ALA A 259 ? 0.1911 0.3371 0.1747 -0.0900 -0.0123 0.0565  259 ALA A CA  
2075  C C   . ALA A 259 ? 0.2115 0.3537 0.2020 -0.0813 -0.0114 0.0616  259 ALA A C   
2076  O O   . ALA A 259 ? 0.2264 0.3739 0.2215 -0.0813 -0.0113 0.0629  259 ALA A O   
2077  C CB  . ALA A 259 ? 0.1899 0.3529 0.1732 -0.0899 -0.0153 0.0602  259 ALA A CB  
2078  N N   . LEU A 260 ? 0.2009 0.3342 0.1919 -0.0741 -0.0106 0.0639  260 LEU A N   
2079  C CA  . LEU A 260 ? 0.2199 0.3499 0.2174 -0.0660 -0.0096 0.0681  260 LEU A CA  
2080  C C   . LEU A 260 ? 0.2092 0.3412 0.2094 -0.0594 -0.0106 0.0729  260 LEU A C   
2081  O O   . LEU A 260 ? 0.1945 0.3228 0.1903 -0.0599 -0.0110 0.0717  260 LEU A O   
2082  C CB  . LEU A 260 ? 0.2136 0.3253 0.2095 -0.0635 -0.0064 0.0646  260 LEU A CB  
2083  C CG  . LEU A 260 ? 0.1865 0.2828 0.1768 -0.0621 -0.0049 0.0611  260 LEU A CG  
2084  C CD1 . LEU A 260 ? 0.1760 0.2674 0.1696 -0.0541 -0.0044 0.0639  260 LEU A CD1 
2085  C CD2 . LEU A 260 ? 0.1990 0.2813 0.1857 -0.0641 -0.0024 0.0568  260 LEU A CD2 
2086  N N   . THR A 261 ? 0.2259 0.3641 0.2336 -0.0535 -0.0109 0.0785  261 THR A N   
2087  C CA  . THR A 261 ? 0.1797 0.3146 0.1912 -0.0462 -0.0107 0.0831  261 THR A CA  
2088  C C   . THR A 261 ? 0.1725 0.2956 0.1873 -0.0410 -0.0078 0.0824  261 THR A C   
2089  O O   . THR A 261 ? 0.2382 0.3642 0.2560 -0.0412 -0.0067 0.0822  261 THR A O   
2090  C CB  . THR A 261 ? 0.1805 0.3327 0.1986 -0.0433 -0.0132 0.0909  261 THR A CB  
2091  O OG1 . THR A 261 ? 0.2762 0.4398 0.3000 -0.0431 -0.0131 0.0936  261 THR A OG1 
2092  C CG2 . THR A 261 ? 0.1877 0.3528 0.2023 -0.0483 -0.0162 0.0915  261 THR A CG2 
2093  N N   . MET A 262 ? 0.1872 0.2978 0.2013 -0.0367 -0.0064 0.0816  262 MET A N   
2094  C CA  . MET A 262 ? 0.1777 0.2768 0.1936 -0.0327 -0.0036 0.0799  262 MET A CA  
2095  C C   . MET A 262 ? 0.1707 0.2644 0.1905 -0.0267 -0.0029 0.0831  262 MET A C   
2096  O O   . MET A 262 ? 0.1855 0.2746 0.2025 -0.0268 -0.0034 0.0825  262 MET A O   
2097  C CB  . MET A 262 ? 0.1897 0.2756 0.1987 -0.0354 -0.0020 0.0730  262 MET A CB  
2098  C CG  . MET A 262 ? 0.2343 0.3103 0.2447 -0.0315 0.0007  0.0713  262 MET A CG  
2099  S SD  . MET A 262 ? 0.3002 0.3618 0.3027 -0.0338 0.0023  0.0645  262 MET A SD  
2100  C CE  . MET A 262 ? 0.2749 0.3405 0.2741 -0.0403 0.0019  0.0625  262 MET A CE  
2101  N N   . SER A 263 ? 0.1917 0.2859 0.2181 -0.0217 -0.0014 0.0865  263 SER A N   
2102  C CA  . SER A 263 ? 0.1513 0.2360 0.1809 -0.0165 0.0002  0.0879  263 SER A CA  
2103  C C   . SER A 263 ? 0.1244 0.1971 0.1504 -0.0170 0.0027  0.0818  263 SER A C   
2104  O O   . SER A 263 ? 0.1494 0.2226 0.1768 -0.0163 0.0044  0.0807  263 SER A O   
2105  C CB  . SER A 263 ? 0.1723 0.2623 0.2110 -0.0105 0.0010  0.0946  263 SER A CB  
2106  O OG  . SER A 263 ? 0.1919 0.2703 0.2336 -0.0061 0.0029  0.0950  263 SER A OG  
2107  N N   . ALA A 264 ? 0.1612 0.2244 0.1824 -0.0181 0.0029  0.0781  264 ALA A N   
2108  C CA  . ALA A 264 ? 0.1742 0.2273 0.1921 -0.0181 0.0050  0.0729  264 ALA A CA  
2109  C C   . ALA A 264 ? 0.1626 0.2109 0.1862 -0.0134 0.0072  0.0745  264 ALA A C   
2110  O O   . ALA A 264 ? 0.2233 0.2643 0.2448 -0.0131 0.0089  0.0708  264 ALA A O   
2111  C CB  . ALA A 264 ? 0.1569 0.2031 0.1683 -0.0206 0.0048  0.0687  264 ALA A CB  
2112  N N   . LYS A 265 ? 0.1439 0.1961 0.1748 -0.0097 0.0072  0.0804  265 LYS A N   
2113  C CA  . LYS A 265 ? 0.1561 0.2026 0.1935 -0.0046 0.0093  0.0801  265 LYS A CA  
2114  C C   . LYS A 265 ? 0.1480 0.1981 0.1882 -0.0021 0.0106  0.0765  265 LYS A C   
2115  O O   . LYS A 265 ? 0.1583 0.2047 0.2040 0.0024  0.0123  0.0740  265 LYS A O   
2116  C CB  . LYS A 265 ? 0.1356 0.1830 0.1802 -0.0005 0.0086  0.0863  265 LYS A CB  
2117  C CG  . LYS A 265 ? 0.1538 0.2018 0.1949 -0.0034 0.0067  0.0896  265 LYS A CG  
2118  C CD  . LYS A 265 ? 0.1278 0.1698 0.1744 0.0000  0.0070  0.0936  265 LYS A CD  
2119  C CE  . LYS A 265 ? 0.1783 0.2224 0.2342 0.0063  0.0072  0.0994  265 LYS A CE  
2120  N NZ  . LYS A 265 ? 0.2086 0.2489 0.2687 0.0088  0.0066  0.1040  265 LYS A NZ  
2121  N N   . LYS A 266 ? 0.1533 0.2109 0.1898 -0.0055 0.0101  0.0760  266 LYS A N   
2122  C CA  . LYS A 266 ? 0.1599 0.2225 0.1982 -0.0042 0.0115  0.0732  266 LYS A CA  
2123  C C   . LYS A 266 ? 0.1544 0.2118 0.1850 -0.0078 0.0125  0.0687  266 LYS A C   
2124  O O   . LYS A 266 ? 0.2124 0.2613 0.2413 -0.0064 0.0137  0.0650  266 LYS A O   
2125  C CB  . LYS A 266 ? 0.1493 0.2255 0.1907 -0.0052 0.0103  0.0768  266 LYS A CB  
2126  C CG  . LYS A 266 ? 0.1553 0.2381 0.2062 0.0007  0.0098  0.0807  266 LYS A CG  
2127  C CD  . LYS A 266 ? 0.1480 0.2266 0.2002 0.0021  0.0080  0.0856  266 LYS A CD  
2128  C CE  . LYS A 266 ? 0.2046 0.2940 0.2641 0.0059  0.0062  0.0917  266 LYS A CE  
2129  N NZ  . LYS A 266 ? 0.2422 0.3264 0.3025 0.0074  0.0047  0.0972  266 LYS A NZ  
2130  N N   . ASP A 267 ? 0.1932 0.2552 0.2189 -0.0127 0.0121  0.0689  267 ASP A N   
2131  C CA  . ASP A 267 ? 0.2182 0.2749 0.2373 -0.0153 0.0133  0.0654  267 ASP A CA  
2132  C C   . ASP A 267 ? 0.2084 0.2542 0.2214 -0.0165 0.0129  0.0630  267 ASP A C   
2133  O O   . ASP A 267 ? 0.2537 0.2943 0.2629 -0.0158 0.0141  0.0599  267 ASP A O   
2134  C CB  . ASP A 267 ? 0.2116 0.2736 0.2270 -0.0206 0.0127  0.0659  267 ASP A CB  
2135  C CG  . ASP A 267 ? 0.2305 0.3034 0.2505 -0.0199 0.0144  0.0673  267 ASP A CG  
2136  O OD1 . ASP A 267 ? 0.2373 0.3138 0.2640 -0.0142 0.0153  0.0668  267 ASP A OD1 
2137  O OD2 . ASP A 267 ? 0.2234 0.2996 0.2405 -0.0242 0.0142  0.0665  267 ASP A OD2 
2138  N N   . PRO A 268 ? 0.1631 0.2057 0.1747 -0.0177 0.0111  0.0632  268 PRO A N   
2139  C CA  . PRO A 268 ? 0.1568 0.1902 0.1635 -0.0181 0.0111  0.0598  268 PRO A CA  
2140  C C   . PRO A 268 ? 0.1713 0.2005 0.1815 -0.0143 0.0125  0.0593  268 PRO A C   
2141  O O   . PRO A 268 ? 0.1910 0.2144 0.1984 -0.0146 0.0125  0.0570  268 PRO A O   
2142  C CB  . PRO A 268 ? 0.2207 0.2544 0.2254 -0.0205 0.0090  0.0598  268 PRO A CB  
2143  C CG  . PRO A 268 ? 0.1545 0.1966 0.1605 -0.0228 0.0077  0.0620  268 PRO A CG  
2144  C CD  . PRO A 268 ? 0.1731 0.2215 0.1856 -0.0198 0.0089  0.0654  268 PRO A CD  
2145  N N   . LEU A 269 ? 0.1644 0.1964 0.1811 -0.0104 0.0135  0.0594  269 LEU A N   
2146  C CA  . LEU A 269 ? 0.1447 0.1719 0.1646 -0.0067 0.0148  0.0557  269 LEU A CA  
2147  C C   . LEU A 269 ? 0.1639 0.1861 0.1863 -0.0065 0.0145  0.0564  269 LEU A C   
2148  O O   . LEU A 269 ? 0.1565 0.1736 0.1783 -0.0060 0.0152  0.0526  269 LEU A O   
2149  C CB  . LEU A 269 ? 0.1488 0.1727 0.1633 -0.0068 0.0155  0.0511  269 LEU A CB  
2150  C CG  . LEU A 269 ? 0.1473 0.1755 0.1592 -0.0068 0.0163  0.0503  269 LEU A CG  
2151  C CD1 . LEU A 269 ? 0.1721 0.1963 0.1764 -0.0080 0.0162  0.0481  269 LEU A CD1 
2152  C CD2 . LEU A 269 ? 0.1494 0.1812 0.1668 -0.0027 0.0180  0.0476  269 LEU A CD2 
2153  N N   . LEU A 270 ? 0.1276 0.1521 0.1529 -0.0071 0.0136  0.0615  270 LEU A N   
2154  C CA  . LEU A 270 ? 0.1765 0.1966 0.2033 -0.0077 0.0134  0.0634  270 LEU A CA  
2155  C C   . LEU A 270 ? 0.1371 0.1561 0.1723 -0.0041 0.0139  0.0666  270 LEU A C   
2156  O O   . LEU A 270 ? 0.1600 0.1828 0.1999 -0.0008 0.0141  0.0678  270 LEU A O   
2157  C CB  . LEU A 270 ? 0.1390 0.1622 0.1610 -0.0117 0.0117  0.0670  270 LEU A CB  
2158  C CG  . LEU A 270 ? 0.2006 0.2240 0.2144 -0.0149 0.0108  0.0626  270 LEU A CG  
2159  C CD1 . LEU A 270 ? 0.1695 0.1957 0.1796 -0.0177 0.0089  0.0629  270 LEU A CD1 
2160  C CD2 . LEU A 270 ? 0.1653 0.1830 0.1766 -0.0151 0.0123  0.0589  270 LEU A CD2 
2161  N N   . ASN A 271 ? 0.1368 0.1502 0.1739 -0.0047 0.0143  0.0682  271 ASN A N   
2162  C CA  . ASN A 271 ? 0.1490 0.1589 0.1938 -0.0018 0.0148  0.0724  271 ASN A CA  
2163  C C   . ASN A 271 ? 0.1359 0.1497 0.1802 -0.0030 0.0131  0.0809  271 ASN A C   
2164  O O   . ASN A 271 ? 0.1870 0.1993 0.2378 0.0002  0.0130  0.0861  271 ASN A O   
2165  C CB  . ASN A 271 ? 0.1287 0.1294 0.1763 -0.0024 0.0166  0.0692  271 ASN A CB  
2166  C CG  . ASN A 271 ? 0.1441 0.1422 0.1921 -0.0012 0.0181  0.0606  271 ASN A CG  
2167  O OD1 . ASN A 271 ? 0.1403 0.1361 0.1850 -0.0039 0.0186  0.0560  271 ASN A OD1 
2168  N ND2 . ASN A 271 ? 0.1551 0.1548 0.2070 0.0029  0.0187  0.0581  271 ASN A ND2 
2169  N N   . ILE A 272 ? 0.1498 0.1690 0.1863 -0.0070 0.0112  0.0793  272 ILE A N   
2170  C CA  . ILE A 272 ? 0.1506 0.1757 0.1848 -0.0082 0.0089  0.0828  272 ILE A CA  
2171  C C   . ILE A 272 ? 0.1703 0.2013 0.1965 -0.0121 0.0074  0.0790  272 ILE A C   
2172  O O   . ILE A 272 ? 0.1928 0.2207 0.2148 -0.0138 0.0083  0.0738  272 ILE A O   
2173  C CB  . ILE A 272 ? 0.1177 0.1379 0.1518 -0.0095 0.0093  0.0843  272 ILE A CB  
2174  C CG1 . ILE A 272 ? 0.1522 0.1792 0.1856 -0.0098 0.0071  0.0896  272 ILE A CG1 
2175  C CG2 . ILE A 272 ? 0.1519 0.1698 0.1794 -0.0136 0.0100  0.0789  272 ILE A CG2 
2176  C CD1 . ILE A 272 ? 0.1653 0.1954 0.2059 -0.0052 0.0063  0.0961  272 ILE A CD1 
2177  N N   . GLY A 273 ? 0.1661 0.2054 0.1906 -0.0133 0.0052  0.0818  273 GLY A N   
2178  C CA  . GLY A 273 ? 0.1478 0.1918 0.1652 -0.0174 0.0039  0.0782  273 GLY A CA  
2179  C C   . GLY A 273 ? 0.1238 0.1774 0.1417 -0.0181 0.0021  0.0800  273 GLY A C   
2180  O O   . GLY A 273 ? 0.1630 0.2193 0.1859 -0.0155 0.0023  0.0823  273 GLY A O   
2181  N N   . GLY A 274 ? 0.1830 0.2428 0.1959 -0.0220 0.0003  0.0789  274 GLY A N   
2182  C CA  . GLY A 274 ? 0.1825 0.2528 0.1953 -0.0241 -0.0016 0.0803  274 GLY A CA  
2183  C C   . GLY A 274 ? 0.1764 0.2482 0.1817 -0.0294 -0.0023 0.0758  274 GLY A C   
2184  O O   . GLY A 274 ? 0.1746 0.2404 0.1755 -0.0307 -0.0013 0.0724  274 GLY A O   
2185  N N   . LEU A 275 ? 0.1452 0.2260 0.1495 -0.0327 -0.0039 0.0760  275 LEU A N   
2186  C CA  . LEU A 275 ? 0.2048 0.2860 0.2021 -0.0383 -0.0043 0.0712  275 LEU A CA  
2187  C C   . LEU A 275 ? 0.1777 0.2725 0.1747 -0.0426 -0.0067 0.0730  275 LEU A C   
2188  O O   . LEU A 275 ? 0.1732 0.2746 0.1750 -0.0417 -0.0074 0.0760  275 LEU A O   
2189  C CB  . LEU A 275 ? 0.2616 0.3320 0.2557 -0.0391 -0.0022 0.0659  275 LEU A CB  
2190  C CG  . LEU A 275 ? 0.1844 0.2525 0.1716 -0.0448 -0.0019 0.0610  275 LEU A CG  
2191  C CD1 . LEU A 275 ? 0.2023 0.2673 0.1846 -0.0459 -0.0013 0.0587  275 LEU A CD1 
2192  C CD2 . LEU A 275 ? 0.2054 0.2635 0.1913 -0.0446 0.0001  0.0578  275 LEU A CD2 
2193  N N   . VAL A 276 ? 0.1743 0.2746 0.1658 -0.0476 -0.0079 0.0711  276 VAL A N   
2194  C CA  . VAL A 276 ? 0.1774 0.2897 0.1665 -0.0539 -0.0099 0.0704  276 VAL A CA  
2195  C C   . VAL A 276 ? 0.1892 0.2938 0.1710 -0.0595 -0.0083 0.0635  276 VAL A C   
2196  O O   . VAL A 276 ? 0.2237 0.3202 0.2010 -0.0594 -0.0068 0.0603  276 VAL A O   
2197  C CB  . VAL A 276 ? 0.1925 0.3195 0.1810 -0.0558 -0.0125 0.0737  276 VAL A CB  
2198  C CG1 . VAL A 276 ? 0.1683 0.3094 0.1540 -0.0631 -0.0146 0.0723  276 VAL A CG1 
2199  C CG2 . VAL A 276 ? 0.2226 0.3558 0.2188 -0.0497 -0.0137 0.0814  276 VAL A CG2 
2200  N N   . ALA A 277 ? 0.2010 0.3075 0.1818 -0.0644 -0.0083 0.0613  277 ALA A N   
2201  C CA  . ALA A 277 ? 0.2240 0.3234 0.1979 -0.0709 -0.0067 0.0550  277 ALA A CA  
2202  C C   . ALA A 277 ? 0.2143 0.3257 0.1865 -0.0792 -0.0081 0.0534  277 ALA A C   
2203  O O   . ALA A 277 ? 0.2176 0.3384 0.1949 -0.0792 -0.0096 0.0565  277 ALA A O   
2204  C CB  . ALA A 277 ? 0.1769 0.2604 0.1510 -0.0688 -0.0040 0.0526  277 ALA A CB  
2205  N N   . ILE A 278 ? 0.2342 0.3466 0.1996 -0.0867 -0.0075 0.0481  278 ILE A N   
2206  C CA  . ILE A 278 ? 0.2335 0.3580 0.1973 -0.0956 -0.0090 0.0448  278 ILE A CA  
2207  C C   . ILE A 278 ? 0.2965 0.4067 0.2563 -0.1012 -0.0070 0.0363  278 ILE A C   
2208  O O   . ILE A 278 ? 0.2947 0.3915 0.2502 -0.0996 -0.0052 0.0316  278 ILE A O   
2209  C CB  . ILE A 278 ? 0.2684 0.4090 0.2286 -0.0982 -0.0114 0.0446  278 ILE A CB  
2210  C CG1 . ILE A 278 ? 0.2610 0.4157 0.2268 -0.0923 -0.0143 0.0537  278 ILE A CG1 
2211  C CG2 . ILE A 278 ? 0.2525 0.4034 0.2102 -0.1076 -0.0130 0.0380  278 ILE A CG2 
2212  C CD1 . ILE A 278 ? 0.3050 0.4686 0.2687 -0.0901 -0.0161 0.0556  278 ILE A CD1 
2213  N N   . ARG A 279 ? 0.2771 0.3899 0.2390 -0.1074 -0.0071 0.0344  279 ARG A N   
2214  C CA  . ARG A 279 ? 0.2791 0.3759 0.2380 -0.1126 -0.0049 0.0276  279 ARG A CA  
2215  C C   . ARG A 279 ? 0.3427 0.4365 0.2952 -0.1175 -0.0049 0.0186  279 ARG A C   
2216  O O   . ARG A 279 ? 0.3893 0.4667 0.3379 -0.1151 -0.0029 0.0142  279 ARG A O   
2217  C CB  . ARG A 279 ? 0.3467 0.4485 0.3091 -0.1185 -0.0052 0.0276  279 ARG A CB  
2218  C CG  . ARG A 279 ? 0.3427 0.4254 0.3034 -0.1217 -0.0025 0.0237  279 ARG A CG  
2219  C CD  . ARG A 279 ? 0.3981 0.4874 0.3622 -0.1253 -0.0031 0.0242  279 ARG A CD  
2220  N NE  . ARG A 279 ? 0.4906 0.5623 0.4536 -0.1278 -0.0004 0.0221  279 ARG A NE  
2221  C CZ  . ARG A 279 ? 0.5912 0.6652 0.5564 -0.1320 0.0000  0.0219  279 ARG A CZ  
2222  N NH1 . ARG A 279 ? 0.4621 0.5555 0.4307 -0.1343 -0.0021 0.0230  279 ARG A NH1 
2223  N NH2 . ARG A 279 ? 0.4942 0.5510 0.4582 -0.1338 0.0027  0.0208  279 ARG A NH2 
2224  N N   . ASP A 280 ? 0.3443 0.4548 0.2958 -0.1243 -0.0072 0.0154  280 ASP A N   
2225  C CA  . ASP A 280 ? 0.3858 0.4946 0.3311 -0.1296 -0.0071 0.0056  280 ASP A CA  
2226  C C   . ASP A 280 ? 0.3826 0.5147 0.3259 -0.1338 -0.0102 0.0042  280 ASP A C   
2227  O O   . ASP A 280 ? 0.4105 0.5435 0.3485 -0.1391 -0.0101 -0.0049 280 ASP A O   
2228  C CB  . ASP A 280 ? 0.4320 0.5279 0.3763 -0.1378 -0.0054 -0.0022 280 ASP A CB  
2229  C CG  . ASP A 280 ? 0.4597 0.5657 0.4084 -0.1434 -0.0065 0.0002  280 ASP A CG  
2230  O OD1 . ASP A 280 ? 0.4930 0.6191 0.4444 -0.1417 -0.0090 0.0057  280 ASP A OD1 
2231  O OD2 . ASP A 280 ? 0.5127 0.6051 0.4616 -0.1470 -0.0044 -0.0030 280 ASP A OD2 
2232  N N   . ASN A 281 ? 0.3913 0.5424 0.3385 -0.1315 -0.0129 0.0127  281 ASN A N   
2233  C CA  . ASN A 281 ? 0.3676 0.5420 0.3126 -0.1347 -0.0161 0.0126  281 ASN A CA  
2234  C C   . ASN A 281 ? 0.3379 0.5149 0.2784 -0.1292 -0.0162 0.0147  281 ASN A C   
2235  O O   . ASN A 281 ? 0.3946 0.5748 0.3379 -0.1216 -0.0168 0.0243  281 ASN A O   
2236  C CB  . ASN A 281 ? 0.3410 0.5319 0.2915 -0.1319 -0.0182 0.0215  281 ASN A CB  
2237  C CG  . ASN A 281 ? 0.3664 0.5782 0.3145 -0.1341 -0.0198 0.0214  281 ASN A CG  
2238  O OD1 . ASN A 281 ? 0.3764 0.5948 0.3203 -0.1337 -0.0197 0.0199  281 ASN A OD1 
2239  N ND2 . ASN A 281 ? 0.3972 0.6198 0.3486 -0.1360 -0.0206 0.0231  281 ASN A ND2 
2240  N N   . GLU A 282 ? 0.3812 0.5566 0.3149 -0.1329 -0.0154 0.0054  282 GLU A N   
2241  C CA  . GLU A 282 ? 0.3620 0.5391 0.2910 -0.1280 -0.0148 0.0067  282 GLU A CA  
2242  C C   . GLU A 282 ? 0.3796 0.5781 0.3104 -0.1255 -0.0163 0.0143  282 GLU A C   
2243  O O   . GLU A 282 ? 0.3858 0.5861 0.3175 -0.1193 -0.0160 0.0203  282 GLU A O   
2244  C CB  . GLU A 282 ? 0.5093 0.6789 0.4316 -0.1319 -0.0126 -0.0059 282 GLU A CB  
2245  C CG  . GLU A 282 ? 0.5559 0.7216 0.4742 -0.1260 -0.0107 -0.0056 282 GLU A CG  
2246  C CD  . GLU A 282 ? 0.6865 0.8471 0.5990 -0.1293 -0.0083 -0.0187 282 GLU A CD  
2247  O OE1 . GLU A 282 ? 0.7926 0.9620 0.7045 -0.1344 -0.0080 -0.0251 282 GLU A OE1 
2248  O OE2 . GLU A 282 ? 0.6548 0.8009 0.5656 -0.1248 -0.0056 -0.0219 282 GLU A OE2 
2249  N N   . GLU A 283 ? 0.3655 0.5790 0.2987 -0.1295 -0.0174 0.0142  283 GLU A N   
2250  C CA  . GLU A 283 ? 0.2956 0.5291 0.2322 -0.1269 -0.0187 0.0214  283 GLU A CA  
2251  C C   . GLU A 283 ? 0.2999 0.5364 0.2444 -0.1193 -0.0205 0.0343  283 GLU A C   
2252  O O   . GLU A 283 ? 0.2893 0.5320 0.2370 -0.1137 -0.0212 0.0410  283 GLU A O   
2253  C CB  . GLU A 283 ? 0.3564 0.6054 0.2931 -0.1328 -0.0193 0.0180  283 GLU A CB  
2254  C CG  . GLU A 283 ? 0.3841 0.6546 0.3237 -0.1304 -0.0208 0.0248  283 GLU A CG  
2255  C CD  . GLU A 283 ? 0.4929 0.7801 0.4321 -0.1361 -0.0214 0.0213  283 GLU A CD  
2256  O OE1 . GLU A 283 ? 0.5144 0.7959 0.4517 -0.1419 -0.0208 0.0137  283 GLU A OE1 
2257  O OE2 . GLU A 283 ? 0.5396 0.8454 0.4809 -0.1347 -0.0227 0.0263  283 GLU A OE2 
2258  N N   . ILE A 284 ? 0.2863 0.5178 0.2347 -0.1186 -0.0213 0.0376  284 ILE A N   
2259  C CA  . ILE A 284 ? 0.2838 0.5165 0.2406 -0.1106 -0.0227 0.0488  284 ILE A CA  
2260  C C   . ILE A 284 ? 0.3230 0.5389 0.2796 -0.1037 -0.0217 0.0512  284 ILE A C   
2261  O O   . ILE A 284 ? 0.2805 0.4970 0.2432 -0.0959 -0.0224 0.0590  284 ILE A O   
2262  C CB  . ILE A 284 ? 0.3297 0.5622 0.2905 -0.1117 -0.0234 0.0510  284 ILE A CB  
2263  C CG1 . ILE A 284 ? 0.3200 0.5712 0.2827 -0.1148 -0.0243 0.0517  284 ILE A CG1 
2264  C CG2 . ILE A 284 ? 0.2910 0.5177 0.2600 -0.1028 -0.0241 0.0601  284 ILE A CG2 
2265  C CD1 . ILE A 284 ? 0.3283 0.5796 0.2941 -0.1162 -0.0248 0.0523  284 ILE A CD1 
2266  N N   . PHE A 285 ? 0.2983 0.4983 0.2476 -0.1062 -0.0194 0.0440  285 PHE A N   
2267  C CA  . PHE A 285 ? 0.2964 0.4806 0.2450 -0.0998 -0.0172 0.0452  285 PHE A CA  
2268  C C   . PHE A 285 ? 0.2784 0.4697 0.2268 -0.0970 -0.0174 0.0467  285 PHE A C   
2269  O O   . PHE A 285 ? 0.2510 0.4367 0.2038 -0.0897 -0.0171 0.0527  285 PHE A O   
2270  C CB  . PHE A 285 ? 0.3086 0.4765 0.2489 -0.1036 -0.0138 0.0367  285 PHE A CB  
2271  C CG  . PHE A 285 ? 0.3450 0.4992 0.2839 -0.0980 -0.0110 0.0363  285 PHE A CG  
2272  C CD1 . PHE A 285 ? 0.2895 0.4330 0.2353 -0.0897 -0.0103 0.0427  285 PHE A CD1 
2273  C CD2 . PHE A 285 ? 0.3159 0.4678 0.2477 -0.1006 -0.0093 0.0281  285 PHE A CD2 
2274  C CE1 . PHE A 285 ? 0.2508 0.3828 0.1956 -0.0851 -0.0079 0.0419  285 PHE A CE1 
2275  C CE2 . PHE A 285 ? 0.3172 0.4583 0.2479 -0.0958 -0.0066 0.0276  285 PHE A CE2 
2276  C CZ  . PHE A 285 ? 0.2981 0.4298 0.2351 -0.0884 -0.0059 0.0348  285 PHE A CZ  
2277  N N   . THR A 286 ? 0.2523 0.4554 0.1959 -0.1029 -0.0175 0.0409  286 THR A N   
2278  C CA  . THR A 286 ? 0.3277 0.5392 0.2710 -0.1009 -0.0174 0.0427  286 THR A CA  
2279  C C   . THR A 286 ? 0.2705 0.4938 0.2216 -0.0959 -0.0199 0.0535  286 THR A C   
2280  O O   . THR A 286 ? 0.2355 0.4576 0.1887 -0.0907 -0.0197 0.0589  286 THR A O   
2281  C CB  . THR A 286 ? 0.2952 0.5179 0.2321 -0.1082 -0.0166 0.0337  286 THR A CB  
2282  O OG1 . THR A 286 ? 0.3020 0.5116 0.2318 -0.1122 -0.0141 0.0230  286 THR A OG1 
2283  C CG2 . THR A 286 ? 0.2487 0.4806 0.1847 -0.1064 -0.0163 0.0355  286 THR A CG2 
2284  N N   . LEU A 287 ? 0.2374 0.4724 0.1928 -0.0975 -0.0219 0.0567  287 LEU A N   
2285  C CA  . LEU A 287 ? 0.2373 0.4833 0.2001 -0.0922 -0.0239 0.0669  287 LEU A CA  
2286  C C   . LEU A 287 ? 0.2399 0.4721 0.2089 -0.0837 -0.0238 0.0742  287 LEU A C   
2287  O O   . LEU A 287 ? 0.2620 0.4953 0.2348 -0.0781 -0.0242 0.0815  287 LEU A O   
2288  C CB  . LEU A 287 ? 0.2794 0.5410 0.2455 -0.0955 -0.0255 0.0683  287 LEU A CB  
2289  C CG  . LEU A 287 ? 0.2517 0.5295 0.2125 -0.1033 -0.0254 0.0620  287 LEU A CG  
2290  C CD1 . LEU A 287 ? 0.2573 0.5472 0.2206 -0.1067 -0.0264 0.0622  287 LEU A CD1 
2291  C CD2 . LEU A 287 ? 0.2156 0.5066 0.1760 -0.1017 -0.0262 0.0660  287 LEU A CD2 
2292  N N   . ALA A 288 ? 0.2012 0.4194 0.1709 -0.0828 -0.0229 0.0719  288 ALA A N   
2293  C CA  . ALA A 288 ? 0.2402 0.4446 0.2157 -0.0747 -0.0222 0.0776  288 ALA A CA  
2294  C C   . ALA A 288 ? 0.2351 0.4276 0.2084 -0.0710 -0.0203 0.0777  288 ALA A C   
2295  O O   . ALA A 288 ? 0.2586 0.4461 0.2369 -0.0646 -0.0200 0.0843  288 ALA A O   
2296  C CB  . ALA A 288 ? 0.2382 0.4306 0.2141 -0.0750 -0.0212 0.0744  288 ALA A CB  
2297  N N   . ARG A 289 ? 0.2353 0.4235 0.2010 -0.0752 -0.0186 0.0703  289 ARG A N   
2298  C CA  . ARG A 289 ? 0.2534 0.4330 0.2169 -0.0723 -0.0166 0.0702  289 ARG A CA  
2299  C C   . ARG A 289 ? 0.2564 0.4474 0.2217 -0.0707 -0.0178 0.0766  289 ARG A C   
2300  O O   . ARG A 289 ? 0.2664 0.4502 0.2341 -0.0660 -0.0167 0.0812  289 ARG A O   
2301  C CB  . ARG A 289 ? 0.2397 0.4160 0.1947 -0.0775 -0.0145 0.0608  289 ARG A CB  
2302  C CG  . ARG A 289 ? 0.2552 0.4146 0.2079 -0.0771 -0.0120 0.0555  289 ARG A CG  
2303  C CD  . ARG A 289 ? 0.2941 0.4510 0.2386 -0.0813 -0.0095 0.0467  289 ARG A CD  
2304  N NE  . ARG A 289 ? 0.2832 0.4231 0.2263 -0.0787 -0.0064 0.0435  289 ARG A NE  
2305  C CZ  . ARG A 289 ? 0.2707 0.4062 0.2076 -0.0806 -0.0036 0.0364  289 ARG A CZ  
2306  N NH1 . ARG A 289 ? 0.2900 0.4361 0.2214 -0.0849 -0.0033 0.0309  289 ARG A NH1 
2307  N NH2 . ARG A 289 ? 0.2804 0.4014 0.2170 -0.0778 -0.0008 0.0343  289 ARG A NH2 
2308  N N   . GLN A 290 ? 0.2448 0.4537 0.2088 -0.0750 -0.0197 0.0768  290 GLN A N   
2309  C CA  . GLN A 290 ? 0.2239 0.4449 0.1893 -0.0736 -0.0208 0.0834  290 GLN A CA  
2310  C C   . GLN A 290 ? 0.2265 0.4451 0.1998 -0.0667 -0.0217 0.0936  290 GLN A C   
2311  O O   . GLN A 290 ? 0.1921 0.4113 0.1665 -0.0637 -0.0216 0.0998  290 GLN A O   
2312  C CB  . GLN A 290 ? 0.2774 0.5189 0.2403 -0.0794 -0.0225 0.0814  290 GLN A CB  
2313  C CG  . GLN A 290 ? 0.2811 0.5256 0.2358 -0.0864 -0.0210 0.0707  290 GLN A CG  
2314  C CD  . GLN A 290 ? 0.3116 0.5759 0.2639 -0.0926 -0.0223 0.0674  290 GLN A CD  
2315  O OE1 . GLN A 290 ? 0.3380 0.6139 0.2948 -0.0922 -0.0243 0.0726  290 GLN A OE1 
2316  N NE2 . GLN A 290 ? 0.3133 0.5818 0.2587 -0.0983 -0.0207 0.0583  290 GLN A NE2 
2317  N N   . ARG A 291 ? 0.2293 0.4452 0.2080 -0.0643 -0.0225 0.0955  291 ARG A N   
2318  C CA  . ARG A 291 ? 0.1848 0.3972 0.1712 -0.0573 -0.0229 0.1045  291 ARG A CA  
2319  C C   . ARG A 291 ? 0.2139 0.4060 0.2020 -0.0525 -0.0205 0.1047  291 ARG A C   
2320  O O   . ARG A 291 ? 0.2672 0.4543 0.2596 -0.0473 -0.0201 0.1116  291 ARG A O   
2321  C CB  . ARG A 291 ? 0.2634 0.4827 0.2554 -0.0563 -0.0244 0.1065  291 ARG A CB  
2322  C CG  . ARG A 291 ? 0.2757 0.4922 0.2758 -0.0487 -0.0246 0.1156  291 ARG A CG  
2323  C CD  . ARG A 291 ? 0.2440 0.4730 0.2496 -0.0478 -0.0262 0.1187  291 ARG A CD  
2324  N NE  . ARG A 291 ? 0.2051 0.4298 0.2183 -0.0399 -0.0259 0.1269  291 ARG A NE  
2325  C CZ  . ARG A 291 ? 0.2777 0.5100 0.2937 -0.0362 -0.0269 0.1350  291 ARG A CZ  
2326  N NH1 . ARG A 291 ? 0.2516 0.4973 0.2635 -0.0396 -0.0282 0.1365  291 ARG A NH1 
2327  N NH2 . ARG A 291 ? 0.1978 0.4241 0.2207 -0.0288 -0.0264 0.1418  291 ARG A NH2 
2328  N N   . CYS A 292 ? 0.2363 0.4166 0.2209 -0.0542 -0.0188 0.0972  292 CYS A N   
2329  C CA  . CYS A 292 ? 0.2305 0.3923 0.2165 -0.0501 -0.0163 0.0965  292 CYS A CA  
2330  C C   . CYS A 292 ? 0.2306 0.3888 0.2151 -0.0487 -0.0149 0.0996  292 CYS A C   
2331  O O   . CYS A 292 ? 0.2654 0.4127 0.2539 -0.0442 -0.0135 0.1034  292 CYS A O   
2332  C CB  . CYS A 292 ? 0.2382 0.3900 0.2194 -0.0529 -0.0145 0.0877  292 CYS A CB  
2333  S SG  . CYS A 292 ? 0.2661 0.3969 0.2486 -0.0484 -0.0111 0.0857  292 CYS A SG  
2334  N N   . VAL A 293 ? 0.2704 0.4383 0.2492 -0.0531 -0.0153 0.0978  293 VAL A N   
2335  C CA  . VAL A 293 ? 0.2693 0.4340 0.2457 -0.0528 -0.0136 0.0996  293 VAL A CA  
2336  C C   . VAL A 293 ? 0.2411 0.4056 0.2224 -0.0485 -0.0140 0.1095  293 VAL A C   
2337  O O   . VAL A 293 ? 0.2367 0.3892 0.2194 -0.0460 -0.0119 0.1115  293 VAL A O   
2338  C CB  . VAL A 293 ? 0.2847 0.4620 0.2540 -0.0585 -0.0138 0.0955  293 VAL A CB  
2339  C CG1 . VAL A 293 ? 0.3203 0.4981 0.2876 -0.0584 -0.0125 0.0992  293 VAL A CG1 
2340  C CG2 . VAL A 293 ? 0.2501 0.4225 0.2141 -0.0621 -0.0123 0.0852  293 VAL A CG2 
2341  N N   . PRO A 294 ? 0.2563 0.4337 0.2404 -0.0477 -0.0165 0.1161  294 PRO A N   
2342  C CA  . PRO A 294 ? 0.1972 0.3729 0.1858 -0.0433 -0.0166 0.1259  294 PRO A CA  
2343  C C   . PRO A 294 ? 0.2403 0.4036 0.2363 -0.0375 -0.0159 0.1292  294 PRO A C   
2344  O O   . PRO A 294 ? 0.2566 0.4116 0.2557 -0.0338 -0.0149 0.1354  294 PRO A O   
2345  C CB  . PRO A 294 ? 0.2876 0.4827 0.2765 -0.0444 -0.0195 0.1312  294 PRO A CB  
2346  C CG  . PRO A 294 ? 0.2297 0.4336 0.2175 -0.0478 -0.0209 0.1246  294 PRO A CG  
2347  C CD  . PRO A 294 ? 0.2200 0.4154 0.2024 -0.0515 -0.0190 0.1149  294 PRO A CD  
2348  N N   . MET A 295 ? 0.2504 0.4123 0.2490 -0.0368 -0.0164 0.1250  295 MET A N   
2349  C CA  . MET A 295 ? 0.2470 0.4001 0.2529 -0.0313 -0.0160 0.1279  295 MET A CA  
2350  C C   . MET A 295 ? 0.2279 0.3626 0.2345 -0.0296 -0.0131 0.1232  295 MET A C   
2351  O O   . MET A 295 ? 0.2365 0.3610 0.2485 -0.0250 -0.0119 0.1271  295 MET A O   
2352  C CB  . MET A 295 ? 0.1987 0.3614 0.2074 -0.0316 -0.0178 0.1263  295 MET A CB  
2353  C CG  . MET A 295 ? 0.2512 0.4329 0.2613 -0.0320 -0.0205 0.1319  295 MET A CG  
2354  S SD  . MET A 295 ? 0.3374 0.5188 0.3538 -0.0251 -0.0208 0.1439  295 MET A SD  
2355  C CE  . MET A 295 ? 0.2892 0.4940 0.3030 -0.0280 -0.0238 0.1486  295 MET A CE  
2356  N N   . GLU A 296 ? 0.2475 0.3779 0.2491 -0.0332 -0.0120 0.1149  296 GLU A N   
2357  C CA  . GLU A 296 ? 0.2333 0.3479 0.2355 -0.0318 -0.0095 0.1098  296 GLU A CA  
2358  C C   . GLU A 296 ? 0.2024 0.3102 0.1994 -0.0343 -0.0072 0.1059  296 GLU A C   
2359  O O   . GLU A 296 ? 0.2710 0.3668 0.2700 -0.0323 -0.0049 0.1061  296 GLU A O   
2360  C CB  . GLU A 296 ? 0.1898 0.3041 0.1913 -0.0331 -0.0097 0.1034  296 GLU A CB  
2361  C CG  . GLU A 296 ? 0.2433 0.3649 0.2503 -0.0308 -0.0116 0.1068  296 GLU A CG  
2362  C CD  . GLU A 296 ? 0.2948 0.4073 0.3093 -0.0249 -0.0104 0.1107  296 GLU A CD  
2363  O OE1 . GLU A 296 ? 0.3184 0.4177 0.3333 -0.0235 -0.0080 0.1069  296 GLU A OE1 
2364  O OE2 . GLU A 296 ? 0.3523 0.4715 0.3725 -0.0214 -0.0116 0.1175  296 GLU A OE2 
2365  N N   . GLY A 297 ? 0.2136 0.3294 0.2042 -0.0389 -0.0077 0.1022  297 GLY A N   
2366  C CA  . GLY A 297 ? 0.2070 0.3182 0.1927 -0.0414 -0.0054 0.0981  297 GLY A CA  
2367  C C   . GLY A 297 ? 0.2067 0.3259 0.1858 -0.0462 -0.0058 0.0914  297 GLY A C   
2368  O O   . GLY A 297 ? 0.2497 0.3785 0.2277 -0.0482 -0.0080 0.0905  297 GLY A O   
2369  N N   . PHE A 298 ? 0.1869 0.3024 0.1618 -0.0483 -0.0035 0.0866  298 PHE A N   
2370  C CA  . PHE A 298 ? 0.2130 0.3350 0.1815 -0.0527 -0.0033 0.0795  298 PHE A CA  
2371  C C   . PHE A 298 ? 0.2437 0.3596 0.2118 -0.0527 -0.0033 0.0738  298 PHE A C   
2372  O O   . PHE A 298 ? 0.2375 0.3420 0.2096 -0.0493 -0.0023 0.0737  298 PHE A O   
2373  C CB  . PHE A 298 ? 0.2630 0.3835 0.2275 -0.0545 -0.0006 0.0757  298 PHE A CB  
2374  C CG  . PHE A 298 ? 0.2492 0.3767 0.2071 -0.0589 0.0000  0.0679  298 PHE A CG  
2375  C CD1 . PHE A 298 ? 0.2492 0.3912 0.2030 -0.0628 -0.0017 0.0674  298 PHE A CD1 
2376  C CD2 . PHE A 298 ? 0.2238 0.3436 0.1795 -0.0592 0.0024  0.0608  298 PHE A CD2 
2377  C CE1 . PHE A 298 ? 0.2916 0.4399 0.2392 -0.0671 -0.0008 0.0592  298 PHE A CE1 
2378  C CE2 . PHE A 298 ? 0.2311 0.3568 0.1804 -0.0632 0.0033  0.0531  298 PHE A CE2 
2379  C CZ  . PHE A 298 ? 0.2210 0.3606 0.1662 -0.0672 0.0018  0.0519  298 PHE A CZ  
2380  N N   . VAL A 299 ? 0.2421 0.3659 0.2052 -0.0570 -0.0042 0.0688  299 VAL A N   
2381  C CA  . VAL A 299 ? 0.2129 0.3330 0.1757 -0.0579 -0.0047 0.0650  299 VAL A CA  
2382  C C   . VAL A 299 ? 0.2244 0.3307 0.1865 -0.0564 -0.0020 0.0601  299 VAL A C   
2383  O O   . VAL A 299 ? 0.2669 0.3681 0.2296 -0.0565 -0.0022 0.0581  299 VAL A O   
2384  C CB  . VAL A 299 ? 0.2406 0.3723 0.1974 -0.0640 -0.0059 0.0602  299 VAL A CB  
2385  C CG1 . VAL A 299 ? 0.2206 0.3675 0.1789 -0.0653 -0.0088 0.0655  299 VAL A CG1 
2386  C CG2 . VAL A 299 ? 0.2147 0.3475 0.1647 -0.0673 -0.0035 0.0533  299 VAL A CG2 
2387  N N   . THR A 300 ? 0.2139 0.3149 0.1752 -0.0553 0.0005  0.0583  300 THR A N   
2388  C CA  . THR A 300 ? 0.2386 0.3279 0.1998 -0.0537 0.0030  0.0540  300 THR A CA  
2389  C C   . THR A 300 ? 0.2324 0.3119 0.2001 -0.0487 0.0039  0.0577  300 THR A C   
2390  O O   . THR A 300 ? 0.2315 0.3024 0.1998 -0.0471 0.0059  0.0547  300 THR A O   
2391  C CB  . THR A 300 ? 0.2169 0.3075 0.1726 -0.0561 0.0057  0.0480  300 THR A CB  
2392  O OG1 . THR A 300 ? 0.2071 0.3017 0.1638 -0.0556 0.0066  0.0505  300 THR A OG1 
2393  C CG2 . THR A 300 ? 0.1796 0.2789 0.1280 -0.0614 0.0054  0.0425  300 THR A CG2 
2394  N N   . TYR A 301 ? 0.2199 0.3008 0.1924 -0.0463 0.0025  0.0640  301 TYR A N   
2395  C CA  . TYR A 301 ? 0.1981 0.2695 0.1768 -0.0419 0.0032  0.0668  301 TYR A CA  
2396  C C   . TYR A 301 ? 0.2260 0.2994 0.2098 -0.0395 0.0011  0.0724  301 TYR A C   
2397  O O   . TYR A 301 ? 0.1995 0.2654 0.1879 -0.0361 0.0016  0.0731  301 TYR A O   
2398  C CB  . TYR A 301 ? 0.2164 0.2842 0.1968 -0.0411 0.0053  0.0685  301 TYR A CB  
2399  C CG  . TYR A 301 ? 0.1652 0.2397 0.1462 -0.0418 0.0044  0.0745  301 TYR A CG  
2400  C CD1 . TYR A 301 ? 0.2114 0.2839 0.1976 -0.0389 0.0034  0.0809  301 TYR A CD1 
2401  C CD2 . TYR A 301 ? 0.1915 0.2744 0.1677 -0.0452 0.0046  0.0739  301 TYR A CD2 
2402  C CE1 . TYR A 301 ? 0.1772 0.2554 0.1637 -0.0395 0.0026  0.0871  301 TYR A CE1 
2403  C CE2 . TYR A 301 ? 0.1940 0.2834 0.1704 -0.0460 0.0038  0.0798  301 TYR A CE2 
2404  C CZ  . TYR A 301 ? 0.2191 0.3058 0.2005 -0.0431 0.0028  0.0867  301 TYR A CZ  
2405  O OH  . TYR A 301 ? 0.2317 0.3248 0.2132 -0.0438 0.0020  0.0933  301 TYR A OH  
2406  N N   . GLY A 302 ? 0.2002 0.2842 0.1835 -0.0409 -0.0012 0.0764  302 GLY A N   
2407  C CA  . GLY A 302 ? 0.2013 0.2897 0.1895 -0.0387 -0.0034 0.0816  302 GLY A CA  
2408  C C   . GLY A 302 ? 0.1846 0.2658 0.1794 -0.0340 -0.0026 0.0866  302 GLY A C   
2409  O O   . GLY A 302 ? 0.2181 0.2982 0.2177 -0.0312 -0.0033 0.0883  302 GLY A O   
2410  N N   . GLY A 303 ? 0.1798 0.2569 0.1751 -0.0334 -0.0011 0.0890  303 GLY A N   
2411  C CA  . GLY A 303 ? 0.1999 0.2695 0.2014 -0.0296 -0.0002 0.0936  303 GLY A CA  
2412  C C   . GLY A 303 ? 0.1988 0.2564 0.2028 -0.0277 0.0020  0.0895  303 GLY A C   
2413  O O   . GLY A 303 ? 0.1992 0.2508 0.2090 -0.0243 0.0027  0.0927  303 GLY A O   
2414  N N   . LEU A 304 ? 0.1912 0.2459 0.1912 -0.0296 0.0033  0.0828  304 LEU A N   
2415  C CA  . LEU A 304 ? 0.2018 0.2466 0.2036 -0.0282 0.0054  0.0787  304 LEU A CA  
2416  C C   . LEU A 304 ? 0.1868 0.2284 0.1856 -0.0306 0.0076  0.0754  304 LEU A C   
2417  O O   . LEU A 304 ? 0.1869 0.2343 0.1808 -0.0335 0.0076  0.0736  304 LEU A O   
2418  C CB  . LEU A 304 ? 0.1864 0.2308 0.1866 -0.0281 0.0050  0.0739  304 LEU A CB  
2419  C CG  . LEU A 304 ? 0.1824 0.2290 0.1865 -0.0257 0.0035  0.0763  304 LEU A CG  
2420  C CD1 . LEU A 304 ? 0.1941 0.2405 0.1952 -0.0267 0.0034  0.0715  304 LEU A CD1 
2421  C CD2 . LEU A 304 ? 0.2056 0.2454 0.2163 -0.0219 0.0047  0.0788  304 LEU A CD2 
2422  N N   . ALA A 305 ? 0.2130 0.2466 0.2153 -0.0296 0.0097  0.0746  305 ALA A N   
2423  C CA  . ALA A 305 ? 0.1928 0.2245 0.1932 -0.0319 0.0120  0.0708  305 ALA A CA  
2424  C C   . ALA A 305 ? 0.1858 0.2185 0.1826 -0.0325 0.0121  0.0649  305 ALA A C   
2425  O O   . ALA A 305 ? 0.1683 0.2000 0.1651 -0.0308 0.0110  0.0636  305 ALA A O   
2426  C CB  . ALA A 305 ? 0.1962 0.2199 0.2020 -0.0312 0.0141  0.0710  305 ALA A CB  
2427  N N   . GLY A 306 ? 0.2143 0.2495 0.2081 -0.0350 0.0137  0.0616  306 GLY A N   
2428  C CA  . GLY A 306 ? 0.2066 0.2425 0.1970 -0.0354 0.0141  0.0565  306 GLY A CA  
2429  C C   . GLY A 306 ? 0.1946 0.2241 0.1881 -0.0330 0.0146  0.0546  306 GLY A C   
2430  O O   . GLY A 306 ? 0.2330 0.2614 0.2240 -0.0322 0.0138  0.0523  306 GLY A O   
2431  N N   . ARG A 307 ? 0.1798 0.2050 0.1787 -0.0322 0.0158  0.0558  307 ARG A N   
2432  C CA  . ARG A 307 ? 0.1589 0.1793 0.1613 -0.0301 0.0163  0.0542  307 ARG A CA  
2433  C C   . ARG A 307 ? 0.1861 0.2040 0.1892 -0.0273 0.0146  0.0556  307 ARG A C   
2434  O O   . ARG A 307 ? 0.1583 0.1741 0.1615 -0.0256 0.0146  0.0538  307 ARG A O   
2435  C CB  . ARG A 307 ? 0.1585 0.1753 0.1674 -0.0306 0.0181  0.0552  307 ARG A CB  
2436  C CG  . ARG A 307 ? 0.1784 0.1925 0.1903 -0.0304 0.0179  0.0598  307 ARG A CG  
2437  C CD  . ARG A 307 ? 0.1746 0.1829 0.1938 -0.0308 0.0198  0.0603  307 ARG A CD  
2438  N NE  . ARG A 307 ? 0.2096 0.2142 0.2315 -0.0304 0.0196  0.0653  307 ARG A NE  
2439  C CZ  . ARG A 307 ? 0.2212 0.2256 0.2430 -0.0333 0.0207  0.0677  307 ARG A CZ  
2440  N NH1 . ARG A 307 ? 0.1734 0.1817 0.1933 -0.0370 0.0223  0.0651  307 ARG A NH1 
2441  N NH2 . ARG A 307 ? 0.1925 0.1932 0.2164 -0.0323 0.0202  0.0731  307 ARG A NH2 
2442  N N   . ASP A 308 ? 0.2035 0.2229 0.2071 -0.0267 0.0132  0.0592  308 ASP A N   
2443  C CA  . ASP A 308 ? 0.1768 0.1961 0.1818 -0.0243 0.0117  0.0606  308 ASP A CA  
2444  C C   . ASP A 308 ? 0.1694 0.1919 0.1691 -0.0252 0.0104  0.0584  308 ASP A C   
2445  O O   . ASP A 308 ? 0.1837 0.2051 0.1837 -0.0239 0.0100  0.0576  308 ASP A O   
2446  C CB  . ASP A 308 ? 0.1848 0.2058 0.1934 -0.0231 0.0107  0.0659  308 ASP A CB  
2447  C CG  . ASP A 308 ? 0.2463 0.2614 0.2615 -0.0214 0.0122  0.0682  308 ASP A CG  
2448  O OD1 . ASP A 308 ? 0.2474 0.2587 0.2664 -0.0194 0.0132  0.0668  308 ASP A OD1 
2449  O OD2 . ASP A 308 ? 0.2189 0.2331 0.2358 -0.0222 0.0125  0.0715  308 ASP A OD2 
2450  N N   . MET A 309 ? 0.1956 0.2222 0.1905 -0.0280 0.0100  0.0573  309 MET A N   
2451  C CA  . MET A 309 ? 0.1873 0.2152 0.1771 -0.0296 0.0093  0.0545  309 MET A CA  
2452  C C   . MET A 309 ? 0.1725 0.1953 0.1607 -0.0290 0.0106  0.0511  309 MET A C   
2453  O O   . MET A 309 ? 0.1404 0.1611 0.1262 -0.0289 0.0101  0.0497  309 MET A O   
2454  C CB  . MET A 309 ? 0.1646 0.1983 0.1495 -0.0331 0.0090  0.0536  309 MET A CB  
2455  C CG  . MET A 309 ? 0.1961 0.2369 0.1811 -0.0342 0.0069  0.0571  309 MET A CG  
2456  S SD  . MET A 309 ? 0.2459 0.2952 0.2246 -0.0388 0.0066  0.0555  309 MET A SD  
2457  C CE  . MET A 309 ? 0.2052 0.2541 0.1843 -0.0389 0.0088  0.0554  309 MET A CE  
2458  N N   . ALA A 310 ? 0.1778 0.1991 0.1673 -0.0287 0.0122  0.0500  310 ALA A N   
2459  C CA  . ALA A 310 ? 0.1536 0.1706 0.1423 -0.0267 0.0129  0.0458  310 ALA A CA  
2460  C C   . ALA A 310 ? 0.1931 0.2063 0.1847 -0.0237 0.0126  0.0462  310 ALA A C   
2461  O O   . ALA A 310 ? 0.2134 0.2234 0.2023 -0.0221 0.0122  0.0435  310 ALA A O   
2462  C CB  . ALA A 310 ? 0.1472 0.1648 0.1383 -0.0263 0.0143  0.0430  310 ALA A CB  
2463  N N   . ALA A 311 ? 0.1782 0.1916 0.1753 -0.0229 0.0129  0.0496  311 ALA A N   
2464  C CA  . ALA A 311 ? 0.1632 0.1744 0.1634 -0.0200 0.0129  0.0496  311 ALA A CA  
2465  C C   . ALA A 311 ? 0.1814 0.1943 0.1789 -0.0206 0.0119  0.0516  311 ALA A C   
2466  O O   . ALA A 311 ? 0.1666 0.1779 0.1636 -0.0189 0.0119  0.0501  311 ALA A O   
2467  C CB  . ALA A 311 ? 0.1435 0.1543 0.1506 -0.0188 0.0137  0.0527  311 ALA A CB  
2468  N N   . MET A 312 ? 0.1589 0.1751 0.1546 -0.0226 0.0105  0.0526  312 MET A N   
2469  C CA  . MET A 312 ? 0.1434 0.1622 0.1377 -0.0234 0.0093  0.0531  312 MET A CA  
2470  C C   . MET A 312 ? 0.1864 0.2020 0.1750 -0.0251 0.0094  0.0504  312 MET A C   
2471  O O   . MET A 312 ? 0.2028 0.2181 0.1908 -0.0252 0.0093  0.0505  312 MET A O   
2472  C CB  . MET A 312 ? 0.1746 0.1993 0.1688 -0.0255 0.0078  0.0552  312 MET A CB  
2473  C CG  . MET A 312 ? 0.1879 0.2175 0.1822 -0.0267 0.0065  0.0566  312 MET A CG  
2474  S SD  . MET A 312 ? 0.2133 0.2526 0.2076 -0.0294 0.0042  0.0596  312 MET A SD  
2475  C CE  . MET A 312 ? 0.1867 0.2266 0.1860 -0.0264 0.0043  0.0636  312 MET A CE  
2476  N N   . VAL A 313 ? 0.1816 0.1950 0.1660 -0.0267 0.0098  0.0484  313 VAL A N   
2477  C CA  . VAL A 313 ? 0.1745 0.1830 0.1535 -0.0277 0.0099  0.0459  313 VAL A CA  
2478  C C   . VAL A 313 ? 0.1895 0.1932 0.1689 -0.0242 0.0104  0.0447  313 VAL A C   
2479  O O   . VAL A 313 ? 0.2243 0.2247 0.2009 -0.0248 0.0103  0.0448  313 VAL A O   
2480  C CB  . VAL A 313 ? 0.1995 0.2062 0.1751 -0.0281 0.0102  0.0418  313 VAL A CB  
2481  C CG1 . VAL A 313 ? 0.2112 0.2103 0.1826 -0.0267 0.0102  0.0380  313 VAL A CG1 
2482  C CG2 . VAL A 313 ? 0.2112 0.2232 0.1846 -0.0323 0.0097  0.0423  313 VAL A CG2 
2483  N N   . GLN A 314 ? 0.1694 0.1730 0.1522 -0.0208 0.0110  0.0437  314 GLN A N   
2484  C CA  . GLN A 314 ? 0.1971 0.1982 0.1802 -0.0175 0.0114  0.0424  314 GLN A CA  
2485  C C   . GLN A 314 ? 0.2075 0.2113 0.1931 -0.0174 0.0116  0.0453  314 GLN A C   
2486  O O   . GLN A 314 ? 0.1986 0.2009 0.1817 -0.0167 0.0118  0.0454  314 GLN A O   
2487  C CB  . GLN A 314 ? 0.1971 0.1989 0.1837 -0.0145 0.0119  0.0396  314 GLN A CB  
2488  C CG  . GLN A 314 ? 0.2208 0.2218 0.2075 -0.0110 0.0121  0.0377  314 GLN A CG  
2489  C CD  . GLN A 314 ? 0.2456 0.2427 0.2265 -0.0094 0.0115  0.0364  314 GLN A CD  
2490  O OE1 . GLN A 314 ? 0.2253 0.2193 0.2028 -0.0101 0.0110  0.0354  314 GLN A OE1 
2491  N NE2 . GLN A 314 ? 0.2776 0.2749 0.2572 -0.0071 0.0115  0.0365  314 GLN A NE2 
2492  N N   . GLY A 315 ? 0.1785 0.1869 0.1691 -0.0179 0.0118  0.0480  315 GLY A N   
2493  C CA  . GLY A 315 ? 0.1631 0.1753 0.1571 -0.0171 0.0122  0.0503  315 GLY A CA  
2494  C C   . GLY A 315 ? 0.1972 0.2112 0.1884 -0.0199 0.0116  0.0516  315 GLY A C   
2495  O O   . GLY A 315 ? 0.2026 0.2194 0.1948 -0.0193 0.0123  0.0526  315 GLY A O   
2496  N N   . LEU A 316 ? 0.2071 0.2201 0.1950 -0.0230 0.0105  0.0507  316 LEU A N   
2497  C CA  . LEU A 316 ? 0.2221 0.2361 0.2076 -0.0262 0.0100  0.0508  316 LEU A CA  
2498  C C   . LEU A 316 ? 0.2464 0.2547 0.2275 -0.0262 0.0109  0.0500  316 LEU A C   
2499  O O   . LEU A 316 ? 0.2579 0.2677 0.2386 -0.0278 0.0113  0.0508  316 LEU A O   
2500  C CB  . LEU A 316 ? 0.2079 0.2221 0.1905 -0.0300 0.0089  0.0500  316 LEU A CB  
2501  C CG  . LEU A 316 ? 0.2036 0.2260 0.1898 -0.0311 0.0076  0.0518  316 LEU A CG  
2502  C CD1 . LEU A 316 ? 0.1586 0.1821 0.1412 -0.0347 0.0067  0.0507  316 LEU A CD1 
2503  C CD2 . LEU A 316 ? 0.1757 0.2055 0.1651 -0.0324 0.0069  0.0539  316 LEU A CD2 
2504  N N   . GLU A 317 ? 0.2174 0.2197 0.1953 -0.0243 0.0113  0.0491  317 GLU A N   
2505  C CA  . GLU A 317 ? 0.2348 0.2315 0.2081 -0.0235 0.0119  0.0493  317 GLU A CA  
2506  C C   . GLU A 317 ? 0.2622 0.2629 0.2375 -0.0207 0.0129  0.0505  317 GLU A C   
2507  O O   . GLU A 317 ? 0.2624 0.2633 0.2359 -0.0217 0.0135  0.0514  317 GLU A O   
2508  C CB  . GLU A 317 ? 0.2849 0.2751 0.2549 -0.0209 0.0115  0.0467  317 GLU A CB  
2509  C CG  . GLU A 317 ? 0.3556 0.3402 0.3213 -0.0183 0.0117  0.0468  317 GLU A CG  
2510  C CD  . GLU A 317 ? 0.4250 0.4031 0.3859 -0.0219 0.0119  0.0490  317 GLU A CD  
2511  O OE1 . GLU A 317 ? 0.3771 0.3538 0.3376 -0.0264 0.0117  0.0486  317 GLU A OE1 
2512  O OE2 . GLU A 317 ? 0.4704 0.4450 0.4279 -0.0206 0.0123  0.0510  317 GLU A OE2 
2513  N N   . GLU A 318 ? 0.2444 0.2484 0.2238 -0.0171 0.0131  0.0490  318 GLU A N   
2514  C CA  . GLU A 318 ? 0.2508 0.2591 0.2324 -0.0141 0.0141  0.0486  318 GLU A CA  
2515  C C   . GLU A 318 ? 0.2442 0.2594 0.2290 -0.0158 0.0151  0.0513  318 GLU A C   
2516  O O   . GLU A 318 ? 0.2373 0.2561 0.2213 -0.0148 0.0162  0.0517  318 GLU A O   
2517  C CB  . GLU A 318 ? 0.2297 0.2396 0.2161 -0.0106 0.0142  0.0455  318 GLU A CB  
2518  C CG  . GLU A 318 ? 0.1944 0.1997 0.1785 -0.0090 0.0134  0.0425  318 GLU A CG  
2519  C CD  . GLU A 318 ? 0.2247 0.2321 0.2140 -0.0064 0.0137  0.0390  318 GLU A CD  
2520  O OE1 . GLU A 318 ? 0.2295 0.2407 0.2235 -0.0052 0.0147  0.0385  318 GLU A OE1 
2521  O OE2 . GLU A 318 ? 0.2128 0.2181 0.2017 -0.0058 0.0132  0.0365  318 GLU A OE2 
2522  N N   . GLY A 319 ? 0.2291 0.2476 0.2174 -0.0181 0.0146  0.0531  319 GLY A N   
2523  C CA  . GLY A 319 ? 0.2033 0.2297 0.1956 -0.0192 0.0150  0.0550  319 GLY A CA  
2524  C C   . GLY A 319 ? 0.2059 0.2325 0.1945 -0.0224 0.0152  0.0551  319 GLY A C   
2525  O O   . GLY A 319 ? 0.2025 0.2372 0.1943 -0.0230 0.0162  0.0565  319 GLY A O   
2526  N N   . THR A 320 ? 0.2140 0.2322 0.1966 -0.0246 0.0146  0.0539  320 THR A N   
2527  C CA  . THR A 320 ? 0.2297 0.2462 0.2087 -0.0279 0.0153  0.0545  320 THR A CA  
2528  C C   . THR A 320 ? 0.1954 0.2099 0.1704 -0.0262 0.0166  0.0553  320 THR A C   
2529  O O   . THR A 320 ? 0.2487 0.2622 0.2210 -0.0289 0.0175  0.0565  320 THR A O   
2530  C CB  . THR A 320 ? 0.2760 0.2837 0.2506 -0.0314 0.0145  0.0536  320 THR A CB  
2531  O OG1 . THR A 320 ? 0.2824 0.2809 0.2521 -0.0290 0.0144  0.0531  320 THR A OG1 
2532  C CG2 . THR A 320 ? 0.2087 0.2193 0.1861 -0.0333 0.0130  0.0527  320 THR A CG2 
2533  N N   . GLU A 321 ? 0.2244 0.2391 0.1989 -0.0220 0.0169  0.0551  321 GLU A N   
2534  C CA  . GLU A 321 ? 0.2058 0.2192 0.1753 -0.0201 0.0178  0.0560  321 GLU A CA  
2535  C C   . GLU A 321 ? 0.2703 0.2931 0.2413 -0.0207 0.0197  0.0572  321 GLU A C   
2536  O O   . GLU A 321 ? 0.2582 0.2909 0.2348 -0.0189 0.0208  0.0570  321 GLU A O   
2537  C CB  . GLU A 321 ? 0.2286 0.2423 0.1975 -0.0154 0.0177  0.0553  321 GLU A CB  
2538  C CG  . GLU A 321 ? 0.3193 0.3241 0.2864 -0.0146 0.0159  0.0536  321 GLU A CG  
2539  C CD  . GLU A 321 ? 0.3781 0.3831 0.3461 -0.0095 0.0151  0.0497  321 GLU A CD  
2540  O OE1 . GLU A 321 ? 0.4043 0.4161 0.3746 -0.0067 0.0159  0.0477  321 GLU A OE1 
2541  O OE2 . GLU A 321 ? 0.4512 0.4504 0.4179 -0.0083 0.0138  0.0480  321 GLU A OE2 
2542  N N   . GLU A 322 ? 0.2425 0.2625 0.2089 -0.0231 0.0204  0.0588  322 GLU A N   
2543  C CA  . GLU A 322 ? 0.2557 0.2852 0.2234 -0.0245 0.0223  0.0600  322 GLU A CA  
2544  C C   . GLU A 322 ? 0.2266 0.2654 0.1945 -0.0203 0.0238  0.0596  322 GLU A C   
2545  O O   . GLU A 322 ? 0.2280 0.2789 0.2006 -0.0199 0.0256  0.0592  322 GLU A O   
2546  C CB  . GLU A 322 ? 0.2436 0.2670 0.2059 -0.0281 0.0230  0.0622  322 GLU A CB  
2547  C CG  . GLU A 322 ? 0.3008 0.3345 0.2648 -0.0305 0.0250  0.0635  322 GLU A CG  
2548  C CD  . GLU A 322 ? 0.3751 0.4022 0.3338 -0.0344 0.0261  0.0663  322 GLU A CD  
2549  O OE1 . GLU A 322 ? 0.3470 0.3618 0.3026 -0.0362 0.0253  0.0670  322 GLU A OE1 
2550  O OE2 . GLU A 322 ? 0.4167 0.4512 0.3744 -0.0356 0.0279  0.0680  322 GLU A OE2 
2551  N N   . GLU A 323 ? 0.2218 0.2566 0.1848 -0.0170 0.0232  0.0594  323 GLU A N   
2552  C CA  . GLU A 323 ? 0.2585 0.3036 0.2213 -0.0127 0.0247  0.0582  323 GLU A CA  
2553  C C   . GLU A 323 ? 0.2181 0.2686 0.1896 -0.0096 0.0249  0.0532  323 GLU A C   
2554  O O   . GLU A 323 ? 0.2174 0.2777 0.1924 -0.0071 0.0265  0.0499  323 GLU A O   
2555  C CB  . GLU A 323 ? 0.3255 0.3652 0.2817 -0.0093 0.0233  0.0582  323 GLU A CB  
2556  C CG  . GLU A 323 ? 0.3430 0.3923 0.2977 -0.0051 0.0240  0.0548  323 GLU A CG  
2557  C CD  . GLU A 323 ? 0.5971 0.6533 0.5463 -0.0068 0.0259  0.0583  323 GLU A CD  
2558  O OE1 . GLU A 323 ? 0.6028 0.6576 0.5531 -0.0112 0.0267  0.0605  323 GLU A OE1 
2559  O OE2 . GLU A 323 ? 0.6106 0.6732 0.5552 -0.0036 0.0260  0.0572  323 GLU A OE2 
2560  N N   . TYR A 324 ? 0.2219 0.2655 0.1971 -0.0098 0.0231  0.0522  324 TYR A N   
2561  C CA  . TYR A 324 ? 0.2216 0.2688 0.2055 -0.0073 0.0232  0.0485  324 TYR A CA  
2562  C C   . TYR A 324 ? 0.2163 0.2722 0.2058 -0.0089 0.0247  0.0501  324 TYR A C   
2563  O O   . TYR A 324 ? 0.2082 0.2717 0.2039 -0.0056 0.0261  0.0469  324 TYR A O   
2564  C CB  . TYR A 324 ? 0.2401 0.2786 0.2260 -0.0076 0.0211  0.0480  324 TYR A CB  
2565  C CG  . TYR A 324 ? 0.2092 0.2509 0.2035 -0.0070 0.0211  0.0475  324 TYR A CG  
2566  C CD1 . TYR A 324 ? 0.1767 0.2216 0.1775 -0.0028 0.0219  0.0433  324 TYR A CD1 
2567  C CD2 . TYR A 324 ? 0.1895 0.2314 0.1855 -0.0105 0.0204  0.0511  324 TYR A CD2 
2568  C CE1 . TYR A 324 ? 0.1714 0.2183 0.1801 -0.0016 0.0220  0.0436  324 TYR A CE1 
2569  C CE2 . TYR A 324 ? 0.1717 0.2176 0.1752 -0.0094 0.0202  0.0516  324 TYR A CE2 
2570  C CZ  . TYR A 324 ? 0.1886 0.2363 0.1984 -0.0047 0.0210  0.0482  324 TYR A CZ  
2571  O OH  . TYR A 324 ? 0.2240 0.2746 0.2416 -0.0030 0.0207  0.0494  324 TYR A OH  
2572  N N   . LEU A 325 ? 0.1888 0.2443 0.1767 -0.0140 0.0245  0.0547  325 LEU A N   
2573  C CA  . LEU A 325 ? 0.1843 0.2498 0.1782 -0.0158 0.0257  0.0563  325 LEU A CA  
2574  C C   . LEU A 325 ? 0.2269 0.3040 0.2213 -0.0148 0.0285  0.0556  325 LEU A C   
2575  O O   . LEU A 325 ? 0.2220 0.3095 0.2238 -0.0128 0.0298  0.0542  325 LEU A O   
2576  C CB  . LEU A 325 ? 0.1690 0.2307 0.1608 -0.0217 0.0241  0.0590  325 LEU A CB  
2577  C CG  . LEU A 325 ? 0.1526 0.2058 0.1449 -0.0228 0.0215  0.0588  325 LEU A CG  
2578  C CD1 . LEU A 325 ? 0.1873 0.2336 0.1754 -0.0280 0.0200  0.0587  325 LEU A CD1 
2579  C CD2 . LEU A 325 ? 0.1786 0.2401 0.1793 -0.0213 0.0213  0.0599  325 LEU A CD2 
2580  N N   . HIS A 326 ? 0.2166 0.2927 0.2031 -0.0161 0.0295  0.0569  326 HIS A N   
2581  C CA  . HIS A 326 ? 0.2030 0.2911 0.1889 -0.0154 0.0324  0.0562  326 HIS A CA  
2582  C C   . HIS A 326 ? 0.2187 0.3133 0.2107 -0.0088 0.0333  0.0496  326 HIS A C   
2583  O O   . HIS A 326 ? 0.1801 0.2869 0.1777 -0.0072 0.0356  0.0476  326 HIS A O   
2584  C CB  . HIS A 326 ? 0.1994 0.2816 0.1757 -0.0167 0.0319  0.0574  326 HIS A CB  
2585  C CG  . HIS A 326 ? 0.2936 0.3875 0.2680 -0.0159 0.0344  0.0565  326 HIS A CG  
2586  N ND1 . HIS A 326 ? 0.3217 0.4231 0.2981 -0.0194 0.0358  0.0576  326 HIS A ND1 
2587  C CD2 . HIS A 326 ? 0.2635 0.3637 0.2342 -0.0122 0.0358  0.0540  326 HIS A CD2 
2588  C CE1 . HIS A 326 ? 0.3175 0.4289 0.2914 -0.0178 0.0379  0.0562  326 HIS A CE1 
2589  N NE2 . HIS A 326 ? 0.2443 0.3552 0.2146 -0.0135 0.0379  0.0538  326 HIS A NE2 
2590  N N   . TYR A 327 ? 0.2185 0.3051 0.2098 -0.0051 0.0316  0.0458  327 TYR A N   
2591  C CA  A TYR A 327 ? 0.2125 0.3032 0.2096 0.0005  0.0325  0.0388  327 TYR A CA  
2592  C CA  B TYR A 327 ? 0.2127 0.3033 0.2098 0.0005  0.0325  0.0389  327 TYR A CA  
2593  C C   . TYR A 327 ? 0.1890 0.2814 0.1968 0.0028  0.0326  0.0374  327 TYR A C   
2594  O O   . TYR A 327 ? 0.2013 0.3025 0.2155 0.0065  0.0346  0.0333  327 TYR A O   
2595  C CB  A TYR A 327 ? 0.2253 0.3068 0.2198 0.0030  0.0305  0.0353  327 TYR A CB  
2596  C CB  B TYR A 327 ? 0.2441 0.3256 0.2386 0.0029  0.0305  0.0353  327 TYR A CB  
2597  C CG  A TYR A 327 ? 0.2276 0.3062 0.2308 0.0069  0.0302  0.0296  327 TYR A CG  
2598  C CG  B TYR A 327 ? 0.2258 0.3077 0.2282 0.0077  0.0309  0.0281  327 TYR A CG  
2599  C CD1 A TYR A 327 ? 0.2120 0.2973 0.2201 0.0111  0.0322  0.0227  327 TYR A CD1 
2600  C CD1 B TYR A 327 ? 0.2198 0.3100 0.2232 0.0110  0.0329  0.0217  327 TYR A CD1 
2601  C CD2 A TYR A 327 ? 0.2087 0.2775 0.2152 0.0063  0.0281  0.0312  327 TYR A CD2 
2602  C CD2 B TYR A 327 ? 0.2092 0.2828 0.2179 0.0086  0.0295  0.0277  327 TYR A CD2 
2603  C CE1 A TYR A 327 ? 0.1965 0.2773 0.2129 0.0144  0.0320  0.0178  327 TYR A CE1 
2604  C CE1 B TYR A 327 ? 0.2099 0.2991 0.2208 0.0149  0.0335  0.0145  327 TYR A CE1 
2605  C CE2 A TYR A 327 ? 0.1971 0.2624 0.2114 0.0095  0.0280  0.0271  327 TYR A CE2 
2606  C CE2 B TYR A 327 ? 0.1894 0.2617 0.2055 0.0125  0.0300  0.0216  327 TYR A CE2 
2607  C CZ  A TYR A 327 ? 0.1860 0.2564 0.2054 0.0134  0.0300  0.0205  327 TYR A CZ  
2608  C CZ  B TYR A 327 ? 0.2020 0.2814 0.2195 0.0156  0.0320  0.0147  327 TYR A CZ  
2609  O OH  A TYR A 327 ? 0.1765 0.2414 0.2040 0.0163  0.0300  0.0166  327 TYR A OH  
2610  O OH  B TYR A 327 ? 0.2089 0.2858 0.2341 0.0191  0.0328  0.0079  327 TYR A OH  
2611  N N   . ARG A 328 ? 0.1866 0.2710 0.1963 0.0009  0.0303  0.0408  328 ARG A N   
2612  C CA  . ARG A 328 ? 0.1636 0.2490 0.1830 0.0034  0.0299  0.0406  328 ARG A CA  
2613  C C   . ARG A 328 ? 0.1693 0.2679 0.1939 0.0034  0.0317  0.0420  328 ARG A C   
2614  O O   . ARG A 328 ? 0.1215 0.2265 0.1544 0.0083  0.0332  0.0386  328 ARG A O   
2615  C CB  . ARG A 328 ? 0.1564 0.2327 0.1749 0.0004  0.0271  0.0448  328 ARG A CB  
2616  C CG  . ARG A 328 ? 0.1893 0.2646 0.2166 0.0031  0.0261  0.0454  328 ARG A CG  
2617  C CD  . ARG A 328 ? 0.1418 0.2278 0.1748 0.0027  0.0264  0.0488  328 ARG A CD  
2618  N NE  . ARG A 328 ? 0.1770 0.2611 0.2164 0.0043  0.0246  0.0516  328 ARG A NE  
2619  C CZ  . ARG A 328 ? 0.1695 0.2520 0.2169 0.0100  0.0248  0.0497  328 ARG A CZ  
2620  N NH1 . ARG A 328 ? 0.1642 0.2459 0.2144 0.0145  0.0269  0.0439  328 ARG A NH1 
2621  N NH2 . ARG A 328 ? 0.1661 0.2479 0.2187 0.0113  0.0230  0.0538  328 ARG A NH2 
2622  N N   . ILE A 329 ? 0.1626 0.2655 0.1831 -0.0021 0.0318  0.0469  329 ILE A N   
2623  C CA  . ILE A 329 ? 0.1651 0.2823 0.1908 -0.0030 0.0336  0.0486  329 ILE A CA  
2624  C C   . ILE A 329 ? 0.1961 0.3245 0.2225 -0.0001 0.0370  0.0444  329 ILE A C   
2625  O O   . ILE A 329 ? 0.1917 0.3325 0.2260 0.0029  0.0388  0.0427  329 ILE A O   
2626  C CB  . ILE A 329 ? 0.1808 0.2991 0.2015 -0.0108 0.0329  0.0544  329 ILE A CB  
2627  C CG1 . ILE A 329 ? 0.1758 0.2840 0.1965 -0.0128 0.0296  0.0571  329 ILE A CG1 
2628  C CG2 . ILE A 329 ? 0.2125 0.3475 0.2387 -0.0126 0.0349  0.0560  329 ILE A CG2 
2629  C CD1 . ILE A 329 ? 0.1978 0.3050 0.2141 -0.0206 0.0285  0.0616  329 ILE A CD1 
2630  N N   . GLY A 330 ? 0.1965 0.3216 0.2147 -0.0006 0.0378  0.0426  330 GLY A N   
2631  C CA  . GLY A 330 ? 0.1527 0.2892 0.1707 0.0022  0.0410  0.0380  330 GLY A CA  
2632  C C   . GLY A 330 ? 0.1662 0.3050 0.1929 0.0096  0.0420  0.0304  330 GLY A C   
2633  O O   . GLY A 330 ? 0.1785 0.3303 0.2094 0.0127  0.0450  0.0263  330 GLY A O   
2634  N N   . GLN A 331 ? 0.1791 0.3053 0.2085 0.0125  0.0397  0.0283  331 GLN A N   
2635  C CA  . GLN A 331 ? 0.1551 0.2812 0.1935 0.0191  0.0407  0.0212  331 GLN A CA  
2636  C C   . GLN A 331 ? 0.1571 0.2907 0.2063 0.0224  0.0415  0.0222  331 GLN A C   
2637  O O   . GLN A 331 ? 0.1810 0.3222 0.2375 0.0279  0.0439  0.0163  331 GLN A O   
2638  C CB  . GLN A 331 ? 0.1632 0.2737 0.2021 0.0204  0.0382  0.0196  331 GLN A CB  
2639  C CG  . GLN A 331 ? 0.1937 0.3015 0.2430 0.0267  0.0392  0.0133  331 GLN A CG  
2640  C CD  . GLN A 331 ? 0.2032 0.2960 0.2532 0.0271  0.0371  0.0117  331 GLN A CD  
2641  O OE1 . GLN A 331 ? 0.1910 0.2755 0.2420 0.0254  0.0348  0.0172  331 GLN A OE1 
2642  N NE2 . GLN A 331 ? 0.1614 0.2518 0.2108 0.0290  0.0381  0.0039  331 GLN A NE2 
2643  N N   . VAL A 332 ? 0.1341 0.2661 0.1847 0.0194  0.0393  0.0292  332 VAL A N   
2644  C CA  . VAL A 332 ? 0.1631 0.3047 0.2236 0.0222  0.0396  0.0313  332 VAL A CA  
2645  C C   . VAL A 332 ? 0.1581 0.3179 0.2204 0.0224  0.0430  0.0295  332 VAL A C   
2646  O O   . VAL A 332 ? 0.1523 0.3218 0.2243 0.0284  0.0449  0.0258  332 VAL A O   
2647  C CB  . VAL A 332 ? 0.1304 0.2695 0.1898 0.0172  0.0366  0.0392  332 VAL A CB  
2648  C CG1 . VAL A 332 ? 0.1461 0.2981 0.2156 0.0199  0.0366  0.0417  332 VAL A CG1 
2649  C CG2 . VAL A 332 ? 0.1348 0.2573 0.1925 0.0172  0.0336  0.0408  332 VAL A CG2 
2650  N N   . LYS A 333 ? 0.1887 0.3536 0.2419 0.0159  0.0440  0.0322  333 LYS A N   
2651  C CA  . LYS A 333 ? 0.1602 0.3432 0.2138 0.0147  0.0475  0.0313  333 LYS A CA  
2652  C C   . LYS A 333 ? 0.1507 0.3404 0.2065 0.0207  0.0508  0.0227  333 LYS A C   
2653  O O   . LYS A 333 ? 0.1779 0.3843 0.2394 0.0232  0.0540  0.0198  333 LYS A O   
2654  C CB  . LYS A 333 ? 0.2007 0.3844 0.2428 0.0061  0.0479  0.0365  333 LYS A CB  
2655  C CG  . LYS A 333 ? 0.2063 0.4044 0.2464 0.0033  0.0504  0.0360  333 LYS A CG  
2656  C CD  . LYS A 333 ? 0.2484 0.4398 0.2770 -0.0056 0.0489  0.0416  333 LYS A CD  
2657  C CE  . LYS A 333 ? 0.2957 0.4988 0.3234 -0.0093 0.0503  0.0420  333 LYS A CE  
2658  N NZ  . LYS A 333 ? 0.2497 0.4629 0.2768 -0.0053 0.0534  0.0362  333 LYS A NZ  
2659  N N   . TYR A 334 ? 0.1988 0.3768 0.2505 0.0229  0.0501  0.0181  334 TYR A N   
2660  C CA  . TYR A 334 ? 0.1833 0.3672 0.2364 0.0280  0.0531  0.0088  334 TYR A CA  
2661  C C   . TYR A 334 ? 0.1661 0.3521 0.2328 0.0363  0.0542  0.0028  334 TYR A C   
2662  O O   . TYR A 334 ? 0.1607 0.3604 0.2325 0.0405  0.0577  -0.0035 334 TYR A O   
2663  C CB  . TYR A 334 ? 0.1836 0.3548 0.2290 0.0276  0.0516  0.0053  334 TYR A CB  
2664  C CG  . TYR A 334 ? 0.1745 0.3496 0.2228 0.0332  0.0540  -0.0055 334 TYR A CG  
2665  C CD1 . TYR A 334 ? 0.2023 0.3928 0.2460 0.0330  0.0574  -0.0099 334 TYR A CD1 
2666  C CD2 . TYR A 334 ? 0.2163 0.3797 0.2715 0.0381  0.0531  -0.0116 334 TYR A CD2 
2667  C CE1 . TYR A 334 ? 0.2249 0.4201 0.2710 0.0380  0.0597  -0.0210 334 TYR A CE1 
2668  C CE2 . TYR A 334 ? 0.1930 0.3595 0.2511 0.0427  0.0555  -0.0227 334 TYR A CE2 
2669  C CZ  . TYR A 334 ? 0.2279 0.4106 0.2815 0.0427  0.0587  -0.0277 334 TYR A CZ  
2670  O OH  . TYR A 334 ? 0.2515 0.4382 0.3078 0.0471  0.0611  -0.0396 334 TYR A OH  
2671  N N   . LEU A 335 ? 0.1273 0.3000 0.2002 0.0388  0.0513  0.0049  335 LEU A N   
2672  C CA  . LEU A 335 ? 0.1377 0.3113 0.2239 0.0469  0.0522  0.0008  335 LEU A CA  
2673  C C   . LEU A 335 ? 0.1688 0.3604 0.2625 0.0486  0.0538  0.0034  335 LEU A C   
2674  O O   . LEU A 335 ? 0.1734 0.3743 0.2766 0.0557  0.0565  -0.0027 335 LEU A O   
2675  C CB  . LEU A 335 ? 0.1472 0.3032 0.2377 0.0484  0.0486  0.0046  335 LEU A CB  
2676  C CG  . LEU A 335 ? 0.1666 0.3206 0.2709 0.0568  0.0488  0.0031  335 LEU A CG  
2677  C CD1 . LEU A 335 ? 0.1890 0.3448 0.2998 0.0637  0.0523  -0.0081 335 LEU A CD1 
2678  C CD2 . LEU A 335 ? 0.2321 0.3679 0.3381 0.0568  0.0453  0.0079  335 LEU A CD2 
2679  N N   . GLY A 336 ? 0.1878 0.3849 0.2774 0.0422  0.0522  0.0119  336 GLY A N   
2680  C CA  . GLY A 336 ? 0.1641 0.3805 0.2606 0.0428  0.0537  0.0144  336 GLY A CA  
2681  C C   . GLY A 336 ? 0.2036 0.4322 0.2968 0.0418  0.0570  0.0087  336 GLY A C   
2682  O O   . GLY A 336 ? 0.1992 0.4374 0.3002 0.0463  0.0583  0.0049  336 GLY A O   
2683  N N   . ASP A 337 ? 0.1816 0.4091 0.2626 0.0359  0.0580  0.0082  337 ASP A N   
2684  C CA  . ASP A 337 ? 0.1979 0.4360 0.2744 0.0345  0.0607  0.0035  337 ASP A CA  
2685  C C   . ASP A 337 ? 0.2210 0.4605 0.3037 0.0427  0.0632  -0.0072 337 ASP A C   
2686  O O   . ASP A 337 ? 0.2616 0.5124 0.3468 0.0445  0.0654  -0.0118 337 ASP A O   
2687  C CB  . ASP A 337 ? 0.2808 0.5158 0.3426 0.0271  0.0607  0.0061  337 ASP A CB  
2688  C CG  . ASP A 337 ? 0.2521 0.4865 0.3072 0.0181  0.0587  0.0158  337 ASP A CG  
2689  O OD1 . ASP A 337 ? 0.3005 0.5428 0.3608 0.0165  0.0582  0.0190  337 ASP A OD1 
2690  O OD2 . ASP A 337 ? 0.2681 0.4936 0.3126 0.0128  0.0575  0.0198  337 ASP A OD2 
2691  N N   . ARG A 338 ? 0.2085 0.4361 0.2936 0.0474  0.0628  -0.0117 338 ARG A N   
2692  C CA  . ARG A 338 ? 0.2451 0.4714 0.3371 0.0550  0.0649  -0.0225 338 ARG A CA  
2693  C C   . ARG A 338 ? 0.1842 0.4159 0.2899 0.0617  0.0657  -0.0242 338 ARG A C   
2694  O O   . ARG A 338 ? 0.2598 0.4991 0.3692 0.0654  0.0683  -0.0312 338 ARG A O   
2695  C CB  . ARG A 338 ? 0.1712 0.3821 0.2647 0.0584  0.0640  -0.0265 338 ARG A CB  
2696  C CG  . ARG A 338 ? 0.2156 0.4231 0.2966 0.0539  0.0640  -0.0294 338 ARG A CG  
2697  C CD  . ARG A 338 ? 0.2618 0.4743 0.3409 0.0560  0.0665  -0.0402 338 ARG A CD  
2698  N NE  . ARG A 338 ? 0.3604 0.5613 0.4458 0.0616  0.0668  -0.0494 338 ARG A NE  
2699  C CZ  . ARG A 338 ? 0.2554 0.4541 0.3517 0.0684  0.0686  -0.0566 338 ARG A CZ  
2700  N NH1 . ARG A 338 ? 0.3096 0.5188 0.4116 0.0712  0.0704  -0.0567 338 ARG A NH1 
2701  N NH2 . ARG A 338 ? 0.2917 0.4766 0.3933 0.0724  0.0685  -0.0639 338 ARG A NH2 
2702  N N   . LEU A 339 ? 0.1809 0.4096 0.2939 0.0634  0.0632  -0.0172 339 LEU A N   
2703  C CA  . LEU A 339 ? 0.2076 0.4412 0.3338 0.0701  0.0633  -0.0176 339 LEU A CA  
2704  C C   . LEU A 339 ? 0.2640 0.5151 0.3895 0.0668  0.0643  -0.0155 339 LEU A C   
2705  O O   . LEU A 339 ? 0.2288 0.4880 0.3630 0.0724  0.0661  -0.0201 339 LEU A O   
2706  C CB  . LEU A 339 ? 0.1880 0.4135 0.3208 0.0725  0.0597  -0.0098 339 LEU A CB  
2707  C CG  . LEU A 339 ? 0.2133 0.4208 0.3484 0.0768  0.0587  -0.0114 339 LEU A CG  
2708  C CD1 . LEU A 339 ? 0.2163 0.4159 0.3539 0.0763  0.0547  -0.0010 339 LEU A CD1 
2709  C CD2 . LEU A 339 ? 0.1760 0.3769 0.3219 0.0862  0.0607  -0.0206 339 LEU A CD2 
2710  N N   . ARG A 340 ? 0.2536 0.5103 0.3691 0.0576  0.0632  -0.0084 340 ARG A N   
2711  C CA  . ARG A 340 ? 0.2252 0.4980 0.3395 0.0533  0.0641  -0.0062 340 ARG A CA  
2712  C C   . ARG A 340 ? 0.2520 0.5341 0.3632 0.0541  0.0679  -0.0140 340 ARG A C   
2713  O O   . ARG A 340 ? 0.2496 0.5452 0.3663 0.0561  0.0696  -0.0162 340 ARG A O   
2714  C CB  . ARG A 340 ? 0.2261 0.4994 0.3297 0.0427  0.0621  0.0027  340 ARG A CB  
2715  C CG  . ARG A 340 ? 0.2326 0.5208 0.3343 0.0369  0.0626  0.0062  340 ARG A CG  
2716  C CD  . ARG A 340 ? 0.2901 0.5746 0.3850 0.0276  0.0596  0.0155  340 ARG A CD  
2717  N NE  . ARG A 340 ? 0.2713 0.5690 0.3649 0.0214  0.0597  0.0188  340 ARG A NE  
2718  C CZ  . ARG A 340 ? 0.3125 0.6143 0.3965 0.0140  0.0612  0.0201  340 ARG A CZ  
2719  N NH1 . ARG A 340 ? 0.3044 0.5990 0.3789 0.0122  0.0625  0.0184  340 ARG A NH1 
2720  N NH2 . ARG A 340 ? 0.3363 0.6498 0.4203 0.0083  0.0612  0.0232  340 ARG A NH2 
2721  N N   . GLU A 341 ? 0.2228 0.4986 0.3252 0.0526  0.0691  -0.0183 341 GLU A N   
2722  C CA  . GLU A 341 ? 0.2340 0.5185 0.3325 0.0532  0.0723  -0.0258 341 GLU A CA  
2723  C C   . GLU A 341 ? 0.3048 0.5913 0.4151 0.0629  0.0746  -0.0352 341 GLU A C   
2724  O O   . GLU A 341 ? 0.3330 0.6312 0.4429 0.0640  0.0774  -0.0408 341 GLU A O   
2725  C CB  . GLU A 341 ? 0.2932 0.5701 0.3798 0.0499  0.0724  -0.0285 341 GLU A CB  
2726  C CG  . GLU A 341 ? 0.3163 0.5939 0.3895 0.0401  0.0709  -0.0201 341 GLU A CG  
2727  C CD  . GLU A 341 ? 0.3570 0.6227 0.4206 0.0380  0.0697  -0.0206 341 GLU A CD  
2728  O OE1 . GLU A 341 ? 0.4143 0.6751 0.4793 0.0431  0.0706  -0.0292 341 GLU A OE1 
2729  O OE2 . GLU A 341 ? 0.3376 0.5983 0.3923 0.0312  0.0678  -0.0126 341 GLU A OE2 
2730  N N   . ALA A 342 ? 0.2686 0.4948 0.3704 0.0880  0.0739  0.0380  342 ALA A N   
2731  C CA  . ALA A 342 ? 0.2540 0.4804 0.3667 0.0934  0.0740  0.0379  342 ALA A CA  
2732  C C   . ALA A 342 ? 0.3329 0.5744 0.4609 0.0899  0.0743  0.0472  342 ALA A C   
2733  O O   . ALA A 342 ? 0.3885 0.6314 0.5274 0.0934  0.0739  0.0480  342 ALA A O   
2734  C CB  . ALA A 342 ? 0.2404 0.4579 0.3555 0.0951  0.0689  0.0320  342 ALA A CB  
2735  N N   . GLY A 343 ? 0.2918 0.5441 0.4212 0.0828  0.0747  0.0540  343 GLY A N   
2736  C CA  . GLY A 343 ? 0.2385 0.5048 0.3821 0.0792  0.0746  0.0629  343 GLY A CA  
2737  C C   . GLY A 343 ? 0.2906 0.5644 0.4430 0.0732  0.0683  0.0678  343 GLY A C   
2738  O O   . GLY A 343 ? 0.2905 0.5752 0.4555 0.0710  0.0673  0.0751  343 GLY A O   
2739  N N   . ILE A 344 ? 0.2220 0.4902 0.3684 0.0706  0.0639  0.0643  344 ILE A N   
2740  C CA  . ILE A 344 ? 0.2598 0.5345 0.4125 0.0646  0.0579  0.0690  344 ILE A CA  
2741  C C   . ILE A 344 ? 0.2986 0.5834 0.4492 0.0547  0.0558  0.0744  344 ILE A C   
2742  O O   . ILE A 344 ? 0.2366 0.5175 0.3761 0.0514  0.0567  0.0707  344 ILE A O   
2743  C CB  . ILE A 344 ? 0.2770 0.5410 0.4246 0.0660  0.0545  0.0628  344 ILE A CB  
2744  C CG1 . ILE A 344 ? 0.2511 0.5039 0.4009 0.0752  0.0562  0.0561  344 ILE A CG1 
2745  C CG2 . ILE A 344 ? 0.2202 0.4908 0.3740 0.0601  0.0489  0.0683  344 ILE A CG2 
2746  C CD1 . ILE A 344 ? 0.3371 0.5946 0.5011 0.0780  0.0556  0.0604  344 ILE A CD1 
2747  N N   . PRO A 345 ? 0.2507 0.5478 0.4113 0.0495  0.0527  0.0827  345 PRO A N   
2748  C CA  . PRO A 345 ? 0.3292 0.6357 0.4880 0.0394  0.0499  0.0872  345 PRO A CA  
2749  C C   . PRO A 345 ? 0.2804 0.5852 0.4315 0.0328  0.0447  0.0856  345 PRO A C   
2750  O O   . PRO A 345 ? 0.2226 0.5267 0.3767 0.0333  0.0408  0.0869  345 PRO A O   
2751  C CB  . PRO A 345 ? 0.2697 0.5891 0.4424 0.0372  0.0477  0.0961  345 PRO A CB  
2752  C CG  . PRO A 345 ? 0.3008 0.6170 0.4813 0.0442  0.0469  0.0966  345 PRO A CG  
2753  C CD  . PRO A 345 ? 0.2833 0.5862 0.4578 0.0529  0.0518  0.0881  345 PRO A CD  
2754  N N   . ILE A 346 ? 0.2270 0.5307 0.3683 0.0264  0.0448  0.0829  346 ILE A N   
2755  C CA  . ILE A 346 ? 0.2464 0.5482 0.3792 0.0192  0.0404  0.0806  346 ILE A CA  
2756  C C   . ILE A 346 ? 0.1767 0.4858 0.3063 0.0086  0.0384  0.0830  346 ILE A C   
2757  O O   . ILE A 346 ? 0.1734 0.4868 0.3062 0.0077  0.0413  0.0851  346 ILE A O   
2758  C CB  . ILE A 346 ? 0.2378 0.5260 0.3593 0.0227  0.0428  0.0714  346 ILE A CB  
2759  C CG1 . ILE A 346 ? 0.2191 0.5021 0.3333 0.0240  0.0482  0.0673  346 ILE A CG1 
2760  C CG2 . ILE A 346 ? 0.2140 0.4939 0.3390 0.0326  0.0438  0.0681  346 ILE A CG2 
2761  C CD1 . ILE A 346 ? 0.2252 0.4947 0.3273 0.0269  0.0502  0.0584  346 ILE A CD1 
2762  N N   . GLN A 347 ? 0.1771 0.4870 0.3002 0.0005  0.0336  0.0824  347 GLN A N   
2763  C CA  . GLN A 347 ? 0.2282 0.5421 0.3460 -0.0101 0.0315  0.0825  347 GLN A CA  
2764  C C   . GLN A 347 ? 0.2357 0.5393 0.3436 -0.0101 0.0364  0.0753  347 GLN A C   
2765  O O   . GLN A 347 ? 0.2402 0.5334 0.3389 -0.0089 0.0373  0.0687  347 GLN A O   
2766  C CB  . GLN A 347 ? 0.2062 0.5224 0.3182 -0.0185 0.0252  0.0829  347 GLN A CB  
2767  C CG  . GLN A 347 ? 0.2315 0.5497 0.3361 -0.0298 0.0229  0.0813  347 GLN A CG  
2768  C CD  . GLN A 347 ? 0.2826 0.6141 0.3954 -0.0353 0.0194  0.0885  347 GLN A CD  
2769  O OE1 . GLN A 347 ? 0.2644 0.5991 0.3837 -0.0341 0.0227  0.0902  347 GLN A OE1 
2770  N NE2 . GLN A 347 ? 0.3004 0.6399 0.4131 -0.0413 0.0129  0.0928  347 GLN A NE2 
2771  N N   . TYR A 348 ? 0.1678 0.4739 0.2779 -0.0115 0.0398  0.0766  348 TYR A N   
2772  C CA  . TYR A 348 ? 0.2245 0.5206 0.3257 -0.0108 0.0451  0.0707  348 TYR A CA  
2773  C C   . TYR A 348 ? 0.2231 0.5207 0.3202 -0.0218 0.0436  0.0702  348 TYR A C   
2774  O O   . TYR A 348 ? 0.2009 0.5088 0.3062 -0.0266 0.0421  0.0755  348 TYR A O   
2775  C CB  . TYR A 348 ? 0.2235 0.5190 0.3299 -0.0022 0.0518  0.0722  348 TYR A CB  
2776  C CG  . TYR A 348 ? 0.2331 0.5165 0.3289 0.0007  0.0577  0.0663  348 TYR A CG  
2777  C CD1 . TYR A 348 ? 0.2876 0.5589 0.3730 0.0057  0.0587  0.0594  348 TYR A CD1 
2778  C CD2 . TYR A 348 ? 0.3149 0.5989 0.4114 -0.0013 0.0624  0.0678  348 TYR A CD2 
2779  C CE1 . TYR A 348 ? 0.3192 0.5789 0.3941 0.0086  0.0637  0.0543  348 TYR A CE1 
2780  C CE2 . TYR A 348 ? 0.3280 0.6001 0.4139 0.0016  0.0679  0.0631  348 TYR A CE2 
2781  C CZ  . TYR A 348 ? 0.3523 0.6123 0.4269 0.0066  0.0683  0.0564  348 TYR A CZ  
2782  O OH  . TYR A 348 ? 0.4176 0.6654 0.4810 0.0098  0.0733  0.0519  348 TYR A OH  
2783  N N   . PRO A 349 ? 0.2188 0.5058 0.3039 -0.0259 0.0442  0.0636  349 PRO A N   
2784  C CA  . PRO A 349 ? 0.2321 0.5058 0.3071 -0.0208 0.0464  0.0565  349 PRO A CA  
2785  C C   . PRO A 349 ? 0.1507 0.4239 0.2241 -0.0208 0.0417  0.0550  349 PRO A C   
2786  O O   . PRO A 349 ? 0.1482 0.4297 0.2247 -0.0273 0.0363  0.0586  349 PRO A O   
2787  C CB  . PRO A 349 ? 0.2295 0.4942 0.2942 -0.0279 0.0477  0.0513  349 PRO A CB  
2788  C CG  . PRO A 349 ? 0.2013 0.4750 0.2691 -0.0391 0.0428  0.0544  349 PRO A CG  
2789  C CD  . PRO A 349 ? 0.1957 0.4831 0.2769 -0.0369 0.0423  0.0624  349 PRO A CD  
2790  N N   . THR A 350 ? 0.1463 0.4101 0.2152 -0.0135 0.0437  0.0498  350 THR A N   
2791  C CA  . THR A 350 ? 0.2007 0.4629 0.2685 -0.0139 0.0399  0.0479  350 THR A CA  
2792  C C   . THR A 350 ? 0.1821 0.4403 0.2406 -0.0247 0.0368  0.0442  350 THR A C   
2793  O O   . THR A 350 ? 0.2037 0.4551 0.2546 -0.0292 0.0387  0.0401  350 THR A O   
2794  C CB  . THR A 350 ? 0.1679 0.4197 0.2331 -0.0038 0.0428  0.0421  350 THR A CB  
2795  O OG1 . THR A 350 ? 0.2118 0.4520 0.2667 -0.0027 0.0466  0.0354  350 THR A OG1 
2796  C CG2 . THR A 350 ? 0.1803 0.4352 0.2547 0.0070  0.0451  0.0454  350 THR A CG2 
2797  N N   . GLY A 351 ? 0.1262 0.3883 0.1853 -0.0290 0.0322  0.0457  351 GLY A N   
2798  C CA  . GLY A 351 ? 0.1820 0.4400 0.2319 -0.0390 0.0291  0.0419  351 GLY A CA  
2799  C C   . GLY A 351 ? 0.1591 0.4036 0.2013 -0.0371 0.0311  0.0337  351 GLY A C   
2800  O O   . GLY A 351 ? 0.2023 0.4395 0.2447 -0.0283 0.0350  0.0300  351 GLY A O   
2801  N N   . GLY A 352 ? 0.1572 0.3980 0.1923 -0.0452 0.0283  0.0307  352 GLY A N   
2802  C CA  . GLY A 352 ? 0.1544 0.3813 0.1819 -0.0447 0.0304  0.0223  352 GLY A CA  
2803  C C   . GLY A 352 ? 0.1903 0.4151 0.2225 -0.0374 0.0311  0.0212  352 GLY A C   
2804  O O   . GLY A 352 ? 0.1710 0.3850 0.2007 -0.0321 0.0342  0.0143  352 GLY A O   
2805  N N   . HIS A 353 ? 0.1517 0.3865 0.1913 -0.0367 0.0283  0.0279  353 HIS A N   
2806  C CA  . HIS A 353 ? 0.1329 0.3649 0.1769 -0.0318 0.0287  0.0269  353 HIS A CA  
2807  C C   . HIS A 353 ? 0.1427 0.3816 0.2000 -0.0212 0.0290  0.0324  353 HIS A C   
2808  O O   . HIS A 353 ? 0.1867 0.4223 0.2495 -0.0159 0.0296  0.0312  353 HIS A O   
2809  C CB  . HIS A 353 ? 0.1104 0.3451 0.1506 -0.0404 0.0253  0.0294  353 HIS A CB  
2810  C CG  . HIS A 353 ? 0.1288 0.3783 0.1739 -0.0433 0.0210  0.0393  353 HIS A CG  
2811  N ND1 . HIS A 353 ? 0.1178 0.3753 0.1619 -0.0479 0.0187  0.0432  353 HIS A ND1 
2812  C CD2 . HIS A 353 ? 0.1409 0.3985 0.1923 -0.0423 0.0184  0.0465  353 HIS A CD2 
2813  C CE1 . HIS A 353 ? 0.1253 0.3957 0.1748 -0.0495 0.0146  0.0519  353 HIS A CE1 
2814  N NE2 . HIS A 353 ? 0.1755 0.4462 0.2291 -0.0462 0.0143  0.0544  353 HIS A NE2 
2815  N N   . ALA A 354 ? 0.1574 0.4044 0.2204 -0.0180 0.0287  0.0380  354 ALA A N   
2816  C CA  . ALA A 354 ? 0.1209 0.3735 0.1964 -0.0088 0.0286  0.0436  354 ALA A CA  
2817  C C   . ALA A 354 ? 0.1797 0.4376 0.2593 -0.0050 0.0300  0.0470  354 ALA A C   
2818  O O   . ALA A 354 ? 0.1680 0.4291 0.2426 -0.0112 0.0299  0.0478  354 ALA A O   
2819  C CB  . ALA A 354 ? 0.1248 0.3869 0.2056 -0.0125 0.0243  0.0517  354 ALA A CB  
2820  N N   . VAL A 355 ? 0.1447 0.4025 0.2338 0.0054  0.0315  0.0488  355 VAL A N   
2821  C CA  . VAL A 355 ? 0.1816 0.4457 0.2770 0.0094  0.0328  0.0536  355 VAL A CA  
2822  C C   . VAL A 355 ? 0.1842 0.4591 0.2894 0.0082  0.0292  0.0629  355 VAL A C   
2823  O O   . VAL A 355 ? 0.1640 0.4375 0.2747 0.0115  0.0276  0.0644  355 VAL A O   
2824  C CB  . VAL A 355 ? 0.1847 0.4401 0.2828 0.0213  0.0370  0.0490  355 VAL A CB  
2825  C CG1 . VAL A 355 ? 0.1413 0.4032 0.2456 0.0249  0.0390  0.0540  355 VAL A CG1 
2826  C CG2 . VAL A 355 ? 0.1493 0.3934 0.2365 0.0230  0.0401  0.0399  355 VAL A CG2 
2827  N N   . PHE A 356 ? 0.1131 0.3985 0.2208 0.0035  0.0277  0.0692  356 PHE A N   
2828  C CA  . PHE A 356 ? 0.2413 0.5380 0.3582 0.0020  0.0239  0.0784  356 PHE A CA  
2829  C C   . PHE A 356 ? 0.2271 0.5267 0.3541 0.0096  0.0267  0.0818  356 PHE A C   
2830  O O   . PHE A 356 ? 0.2399 0.5431 0.3670 0.0083  0.0288  0.0824  356 PHE A O   
2831  C CB  . PHE A 356 ? 0.2734 0.5802 0.3862 -0.0094 0.0194  0.0830  356 PHE A CB  
2832  C CG  . PHE A 356 ? 0.2166 0.5216 0.3195 -0.0176 0.0161  0.0807  356 PHE A CG  
2833  C CD1 . PHE A 356 ? 0.2125 0.5070 0.3047 -0.0203 0.0183  0.0720  356 PHE A CD1 
2834  C CD2 . PHE A 356 ? 0.2525 0.5662 0.3564 -0.0229 0.0108  0.0875  356 PHE A CD2 
2835  C CE1 . PHE A 356 ? 0.1770 0.4690 0.2600 -0.0281 0.0158  0.0694  356 PHE A CE1 
2836  C CE2 . PHE A 356 ? 0.2442 0.5562 0.3381 -0.0307 0.0082  0.0854  356 PHE A CE2 
2837  C CZ  . PHE A 356 ? 0.1916 0.4925 0.2751 -0.0334 0.0108  0.0760  356 PHE A CZ  
2838  N N   . VAL A 357 ? 0.1861 0.4835 0.3219 0.0173  0.0270  0.0836  357 VAL A N   
2839  C CA  . VAL A 357 ? 0.1751 0.4738 0.3207 0.0249  0.0300  0.0859  357 VAL A CA  
2840  C C   . VAL A 357 ? 0.2973 0.6095 0.4520 0.0211  0.0267  0.0958  357 VAL A C   
2841  O O   . VAL A 357 ? 0.2869 0.6038 0.4450 0.0185  0.0223  0.1013  357 VAL A O   
2842  C CB  . VAL A 357 ? 0.2169 0.5056 0.3677 0.0343  0.0317  0.0823  357 VAL A CB  
2843  C CG1 . VAL A 357 ? 0.2797 0.5700 0.4408 0.0414  0.0345  0.0846  357 VAL A CG1 
2844  C CG2 . VAL A 357 ? 0.1720 0.4473 0.3141 0.0384  0.0346  0.0720  357 VAL A CG2 
2845  N N   . ASP A 358 ? 0.2685 0.5869 0.4274 0.0209  0.0288  0.0983  358 ASP A N   
2846  C CA  . ASP A 358 ? 0.3383 0.6698 0.5067 0.0172  0.0257  0.1073  358 ASP A CA  
2847  C C   . ASP A 358 ? 0.3670 0.6988 0.5479 0.0252  0.0268  0.1110  358 ASP A C   
2848  O O   . ASP A 358 ? 0.3458 0.6759 0.5327 0.0315  0.0315  0.1097  358 ASP A O   
2849  C CB  . ASP A 358 ? 0.3425 0.6801 0.5118 0.0138  0.0280  0.1081  358 ASP A CB  
2850  C CG  . ASP A 358 ? 0.3696 0.7214 0.5472 0.0075  0.0235  0.1167  358 ASP A CG  
2851  O OD1 . ASP A 358 ? 0.4674 0.8248 0.6509 0.0070  0.0190  0.1228  358 ASP A OD1 
2852  O OD2 . ASP A 358 ? 0.4417 0.7991 0.6204 0.0031  0.0245  0.1175  358 ASP A OD2 
2853  N N   . CYS A 359 ? 0.3279 0.6613 0.5125 0.0248  0.0227  0.1154  359 CYS A N   
2854  C CA  . CYS A 359 ? 0.3967 0.7291 0.5930 0.0320  0.0236  0.1185  359 CYS A CA  
2855  C C   . CYS A 359 ? 0.4729 0.8176 0.6812 0.0310  0.0221  0.1272  359 CYS A C   
2856  O O   . CYS A 359 ? 0.4569 0.8010 0.6762 0.0374  0.0240  0.1290  359 CYS A O   
2857  C CB  . CYS A 359 ? 0.4029 0.7317 0.5990 0.0322  0.0201  0.1203  359 CYS A CB  
2858  S SG  . CYS A 359 ? 0.3104 0.6237 0.4954 0.0347  0.0222  0.1097  359 CYS A SG  
2859  N N   . LYS A 360 ? 0.4293 0.7852 0.6364 0.0227  0.0185  0.1321  360 LYS A N   
2860  C CA  . LYS A 360 ? 0.4850 0.8530 0.7044 0.0215  0.0171  0.1397  360 LYS A CA  
2861  C C   . LYS A 360 ? 0.4714 0.8373 0.6991 0.0286  0.0237  0.1372  360 LYS A C   
2862  O O   . LYS A 360 ? 0.5104 0.8824 0.7513 0.0317  0.0241  0.1425  360 LYS A O   
2863  C CB  . LYS A 360 ? 0.4944 0.8727 0.7098 0.0114  0.0130  0.1427  360 LYS A CB  
2864  C CG  . LYS A 360 ? 0.5104 0.9019 0.7389 0.0093  0.0112  0.1501  360 LYS A CG  
2865  C CD  . LYS A 360 ? 0.5501 0.9477 0.7895 0.0114  0.0073  0.1584  360 LYS A CD  
2866  C CE  . LYS A 360 ? 0.5480 0.9596 0.8003 0.0081  0.0044  0.1660  360 LYS A CE  
2867  N NZ  . LYS A 360 ? 0.5588 0.9711 0.8191 0.0115  0.0105  0.1634  360 LYS A NZ  
2868  N N   . LYS A 361 ? 0.4789 0.8362 0.6989 0.0314  0.0290  0.1292  361 LYS A N   
2869  C CA  . LYS A 361 ? 0.4947 0.8491 0.7206 0.0386  0.0359  0.1262  361 LYS A CA  
2870  C C   . LYS A 361 ? 0.4588 0.8016 0.6857 0.0479  0.0393  0.1209  361 LYS A C   
2871  O O   . LYS A 361 ? 0.4106 0.7531 0.6464 0.0542  0.0435  0.1207  361 LYS A O   
2872  C CB  . LYS A 361 ? 0.5450 0.8963 0.7618 0.0369  0.0402  0.1208  361 LYS A CB  
2873  C CG  . LYS A 361 ? 0.5544 0.9154 0.7692 0.0271  0.0369  0.1245  361 LYS A CG  
2874  C CD  . LYS A 361 ? 0.6126 0.9704 0.8208 0.0262  0.0424  0.1196  361 LYS A CD  
2875  C CE  . LYS A 361 ? 0.6789 1.0376 0.8961 0.0329  0.0493  0.1201  361 LYS A CE  
2876  N NZ  . LYS A 361 ? 0.6739 1.0285 0.8840 0.0327  0.0554  0.1157  361 LYS A NZ  
2877  N N   . LEU A 362 ? 0.4559 0.7892 0.6743 0.0487  0.0375  0.1162  362 LEU A N   
2878  C CA  . LEU A 362 ? 0.4598 0.7811 0.6791 0.0571  0.0403  0.1099  362 LEU A CA  
2879  C C   . LEU A 362 ? 0.4651 0.7892 0.6979 0.0607  0.0389  0.1149  362 LEU A C   
2880  O O   . LEU A 362 ? 0.4163 0.7347 0.6551 0.0680  0.0426  0.1112  362 LEU A O   
2881  C CB  . LEU A 362 ? 0.4242 0.7352 0.6327 0.0564  0.0384  0.1039  362 LEU A CB  
2882  C CG  . LEU A 362 ? 0.4221 0.7231 0.6179 0.0579  0.0418  0.0947  362 LEU A CG  
2883  C CD1 . LEU A 362 ? 0.4269 0.7164 0.6164 0.0594  0.0400  0.0884  362 LEU A CD1 
2884  C CD2 . LEU A 362 ? 0.3265 0.6225 0.5236 0.0653  0.0479  0.0897  362 LEU A CD2 
2885  N N   . VAL A 363 ? 0.4863 0.8189 0.7236 0.0555  0.0334  0.1233  363 VAL A N   
2886  C CA  . VAL A 363 ? 0.4607 0.7961 0.7106 0.0585  0.0316  0.1290  363 VAL A CA  
2887  C C   . VAL A 363 ? 0.5364 0.8872 0.7952 0.0534  0.0281  0.1396  363 VAL A C   
2888  O O   . VAL A 363 ? 0.4994 0.8562 0.7597 0.0489  0.0225  0.1468  363 VAL A O   
2889  C CB  . VAL A 363 ? 0.4239 0.7527 0.6707 0.0583  0.0282  0.1288  363 VAL A CB  
2890  C CG1 . VAL A 363 ? 0.4429 0.7565 0.6864 0.0653  0.0318  0.1183  363 VAL A CG1 
2891  C CG2 . VAL A 363 ? 0.4390 0.7703 0.6741 0.0505  0.0241  0.1302  363 VAL A CG2 
2892  N N   . PRO A 364 ? 0.5191 0.8767 0.7843 0.0539  0.0311  0.1410  364 PRO A N   
2893  C CA  . PRO A 364 ? 0.5120 0.8844 0.7862 0.0484  0.0273  0.1505  364 PRO A CA  
2894  C C   . PRO A 364 ? 0.5139 0.8920 0.8023 0.0509  0.0247  0.1582  364 PRO A C   
2895  O O   . PRO A 364 ? 0.5218 0.9123 0.8174 0.0459  0.0201  0.1668  364 PRO A O   
2896  C CB  . PRO A 364 ? 0.4638 0.8400 0.7421 0.0497  0.0325  0.1486  364 PRO A CB  
2897  C CG  . PRO A 364 ? 0.4717 0.8362 0.7492 0.0585  0.0393  0.1405  364 PRO A CG  
2898  C CD  . PRO A 364 ? 0.5447 0.8969 0.8101 0.0597  0.0381  0.1341  364 PRO A CD  
2899  N N   . GLN A 365 ? 0.4693 0.8387 0.7623 0.0581  0.0272  0.1553  365 GLN A N   
2900  C CA  . GLN A 365 ? 0.4367 0.8110 0.7436 0.0604  0.0250  0.1627  365 GLN A CA  
2901  C C   . GLN A 365 ? 0.5545 0.9318 0.8587 0.0557  0.0183  0.1696  365 GLN A C   
2902  O O   . GLN A 365 ? 0.6173 1.0027 0.9324 0.0552  0.0149  0.1786  365 GLN A O   
2903  C CB  . GLN A 365 ? 0.4854 0.8493 0.7982 0.0693  0.0298  0.1569  365 GLN A CB  
2904  C CG  . GLN A 365 ? 0.4996 0.8504 0.8041 0.0718  0.0295  0.1508  365 GLN A CG  
2905  C CD  . GLN A 365 ? 0.5954 0.9359 0.8853 0.0722  0.0325  0.1403  365 GLN A CD  
2906  O OE1 . GLN A 365 ? 0.5547 0.8972 0.8406 0.0714  0.0355  0.1372  365 GLN A OE1 
2907  N NE2 . GLN A 365 ? 0.5180 0.8475 0.8005 0.0734  0.0317  0.1349  365 GLN A NE2 
2908  N N   . ILE A 366 ? 0.5623 0.9336 0.8524 0.0523  0.0166  0.1661  366 ILE A N   
2909  C CA  . ILE A 366 ? 0.5678 0.9412 0.8539 0.0480  0.0109  0.1722  366 ILE A CA  
2910  C C   . ILE A 366 ? 0.5732 0.9583 0.8528 0.0386  0.0056  0.1775  366 ILE A C   
2911  O O   . ILE A 366 ? 0.4984 0.8816 0.7667 0.0349  0.0064  0.1717  366 ILE A O   
2912  C CB  . ILE A 366 ? 0.5087 0.8686 0.7840 0.0498  0.0124  0.1649  366 ILE A CB  
2913  C CG1 . ILE A 366 ? 0.4449 0.7932 0.7271 0.0587  0.0171  0.1589  366 ILE A CG1 
2914  C CG2 . ILE A 366 ? 0.5344 0.8975 0.8051 0.0449  0.0070  0.1718  366 ILE A CG2 
2915  C CD1 . ILE A 366 ? 0.5123 0.8462 0.7846 0.0611  0.0191  0.1494  366 ILE A CD1 
2916  N N   . PRO A 367 ? 0.5756 0.9728 0.8617 0.0345  -0.0001 0.1880  367 PRO A N   
2917  C CA  . PRO A 367 ? 0.5413 0.9499 0.8211 0.0251  -0.0058 0.1924  367 PRO A CA  
2918  C C   . PRO A 367 ? 0.5488 0.9542 0.8128 0.0197  -0.0089 0.1910  367 PRO A C   
2919  O O   . PRO A 367 ? 0.5536 0.9498 0.8138 0.0230  -0.0075 0.1890  367 PRO A O   
2920  C CB  . PRO A 367 ? 0.4921 0.9137 0.7845 0.0234  -0.0110 0.2038  367 PRO A CB  
2921  C CG  . PRO A 367 ? 0.5833 0.9986 0.8838 0.0305  -0.0092 0.2065  367 PRO A CG  
2922  C CD  . PRO A 367 ? 0.5615 0.9626 0.8616 0.0382  -0.0016 0.1961  367 PRO A CD  
2923  N N   . GLY A 368 ? 0.5809 0.9945 0.8364 0.0109  -0.0132 0.1919  368 GLY A N   
2924  C CA  . GLY A 368 ? 0.5338 0.9445 0.7731 0.0050  -0.0155 0.1891  368 GLY A CA  
2925  C C   . GLY A 368 ? 0.6145 1.0271 0.8515 0.0035  -0.0196 0.1961  368 GLY A C   
2926  O O   . GLY A 368 ? 0.5127 0.9184 0.7387 0.0023  -0.0191 0.1926  368 GLY A O   
2927  N N   . ASP A 369 ? 0.5527 0.9748 0.8004 0.0036  -0.0235 0.2062  369 ASP A N   
2928  C CA  . ASP A 369 ? 0.5472 0.9719 0.7937 0.0024  -0.0272 0.2142  369 ASP A CA  
2929  C C   . ASP A 369 ? 0.5497 0.9618 0.8001 0.0108  -0.0221 0.2121  369 ASP A C   
2930  O O   . ASP A 369 ? 0.4975 0.9088 0.7445 0.0101  -0.0238 0.2168  369 ASP A O   
2931  C CB  . ASP A 369 ? 0.5702 1.0085 0.8281 0.0007  -0.0327 0.2257  369 ASP A CB  
2932  C CG  . ASP A 369 ? 0.5677 1.0060 0.8433 0.0081  -0.0294 0.2269  369 ASP A CG  
2933  O OD1 . ASP A 369 ? 0.5876 1.0180 0.8652 0.0127  -0.0236 0.2184  369 ASP A OD1 
2934  O OD2 . ASP A 369 ? 0.6061 1.0525 0.8934 0.0092  -0.0327 0.2363  369 ASP A OD2 
2935  N N   . GLN A 370 ? 0.5373 0.9394 0.7947 0.0186  -0.0160 0.2051  370 GLN A N   
2936  C CA  . GLN A 370 ? 0.5348 0.9232 0.7954 0.0264  -0.0110 0.2007  370 GLN A CA  
2937  C C   . GLN A 370 ? 0.5093 0.8851 0.7583 0.0275  -0.0069 0.1889  370 GLN A C   
2938  O O   . GLN A 370 ? 0.4891 0.8521 0.7406 0.0342  -0.0024 0.1827  370 GLN A O   
2939  C CB  . GLN A 370 ? 0.5196 0.9049 0.7955 0.0344  -0.0071 0.2000  370 GLN A CB  
2940  C CG  . GLN A 370 ? 0.5487 0.9470 0.8375 0.0335  -0.0111 0.2114  370 GLN A CG  
2941  C CD  . GLN A 370 ? 0.5633 0.9575 0.8679 0.0418  -0.0073 0.2117  370 GLN A CD  
2942  O OE1 . GLN A 370 ? 0.6236 1.0057 0.9293 0.0481  -0.0015 0.2025  370 GLN A OE1 
2943  N NE2 . GLN A 370 ? 0.5162 0.9208 0.8332 0.0417  -0.0106 0.2220  370 GLN A NE2 
2944  N N   . PHE A 371 ? 0.4222 0.8012 0.6587 0.0206  -0.0087 0.1853  371 PHE A N   
2945  C CA  . PHE A 371 ? 0.4900 0.8586 0.7143 0.0201  -0.0058 0.1750  371 PHE A CA  
2946  C C   . PHE A 371 ? 0.4766 0.8331 0.7044 0.0279  0.0006  0.1648  371 PHE A C   
2947  O O   . PHE A 371 ? 0.4151 0.7598 0.6452 0.0342  0.0040  0.1598  371 PHE A O   
2948  C CB  . PHE A 371 ? 0.4672 0.8304 0.6861 0.0197  -0.0064 0.1759  371 PHE A CB  
2949  C CG  . PHE A 371 ? 0.4867 0.8621 0.7038 0.0133  -0.0123 0.1874  371 PHE A CG  
2950  C CD1 . PHE A 371 ? 0.4743 0.8607 0.6812 0.0037  -0.0172 0.1899  371 PHE A CD1 
2951  C CD2 . PHE A 371 ? 0.5001 0.8761 0.7254 0.0166  -0.0131 0.1956  371 PHE A CD2 
2952  C CE1 . PHE A 371 ? 0.5323 0.9303 0.7366 -0.0025 -0.0230 0.2001  371 PHE A CE1 
2953  C CE2 . PHE A 371 ? 0.4577 0.8456 0.6809 0.0107  -0.0186 0.2067  371 PHE A CE2 
2954  C CZ  . PHE A 371 ? 0.5030 0.9021 0.7153 0.0011  -0.0237 0.2088  371 PHE A CZ  
2955  N N   . PRO A 372 ? 0.4074 0.7668 0.6358 0.0275  0.0023  0.1614  372 PRO A N   
2956  C CA  . PRO A 372 ? 0.3590 0.7077 0.5896 0.0347  0.0085  0.1518  372 PRO A CA  
2957  C C   . PRO A 372 ? 0.3586 0.6949 0.5776 0.0356  0.0112  0.1415  372 PRO A C   
2958  O O   . PRO A 372 ? 0.3733 0.6977 0.5945 0.0427  0.0152  0.1342  372 PRO A O   
2959  C CB  . PRO A 372 ? 0.4495 0.8064 0.6822 0.0325  0.0092  0.1522  372 PRO A CB  
2960  C CG  . PRO A 372 ? 0.4438 0.8119 0.6694 0.0225  0.0036  0.1576  372 PRO A CG  
2961  C CD  . PRO A 372 ? 0.4182 0.7906 0.6450 0.0202  -0.0012 0.1657  372 PRO A CD  
2962  N N   . ALA A 373 ? 0.3280 0.6670 0.5351 0.0283  0.0088  0.1403  373 ALA A N   
2963  C CA  . ALA A 373 ? 0.3203 0.6479 0.5168 0.0288  0.0113  0.1306  373 ALA A CA  
2964  C C   . ALA A 373 ? 0.3315 0.6498 0.5290 0.0324  0.0116  0.1291  373 ALA A C   
2965  O O   . ALA A 373 ? 0.3445 0.6501 0.5394 0.0372  0.0150  0.1197  373 ALA A O   
2966  C CB  . ALA A 373 ? 0.3340 0.6671 0.5180 0.0194  0.0085  0.1300  373 ALA A CB  
2967  N N   . GLN A 374 ? 0.3156 0.6399 0.5173 0.0304  0.0081  0.1381  374 GLN A N   
2968  C CA  . GLN A 374 ? 0.2976 0.6132 0.5016 0.0340  0.0088  0.1374  374 GLN A CA  
2969  C C   . GLN A 374 ? 0.3175 0.6232 0.5325 0.0433  0.0124  0.1335  374 GLN A C   
2970  O O   . GLN A 374 ? 0.3169 0.6109 0.5331 0.0476  0.0144  0.1278  374 GLN A O   
2971  C CB  . GLN A 374 ? 0.2975 0.6228 0.5031 0.0295  0.0043  0.1491  374 GLN A CB  
2972  C CG  . GLN A 374 ? 0.3383 0.6553 0.5447 0.0318  0.0053  0.1487  374 GLN A CG  
2973  C CD  . GLN A 374 ? 0.3122 0.6211 0.5077 0.0296  0.0069  0.1395  374 GLN A CD  
2974  O OE1 . GLN A 374 ? 0.3303 0.6461 0.5151 0.0219  0.0045  0.1402  374 GLN A OE1 
2975  N NE2 . GLN A 374 ? 0.2583 0.5523 0.4566 0.0361  0.0109  0.1303  374 GLN A NE2 
2976  N N   . ALA A 375 ? 0.2758 0.5861 0.4993 0.0463  0.0133  0.1359  375 ALA A N   
2977  C CA  . ALA A 375 ? 0.2996 0.6008 0.5327 0.0547  0.0169  0.1309  375 ALA A CA  
2978  C C   . ALA A 375 ? 0.2716 0.5610 0.4990 0.0588  0.0208  0.1177  375 ALA A C   
2979  O O   . ALA A 375 ? 0.3028 0.5805 0.5339 0.0650  0.0232  0.1102  375 ALA A O   
2980  C CB  . ALA A 375 ? 0.3197 0.6301 0.5636 0.0564  0.0169  0.1372  375 ALA A CB  
2981  N N   . VAL A 376 ? 0.3065 0.5988 0.5249 0.0553  0.0214  0.1146  376 VAL A N   
2982  C CA  . VAL A 376 ? 0.2722 0.5536 0.4840 0.0589  0.0250  0.1027  376 VAL A CA  
2983  C C   . VAL A 376 ? 0.2372 0.5079 0.4420 0.0586  0.0247  0.0960  376 VAL A C   
2984  O O   . VAL A 376 ? 0.2095 0.4676 0.4132 0.0639  0.0270  0.0858  376 VAL A O   
2985  C CB  . VAL A 376 ? 0.3100 0.5980 0.5144 0.0550  0.0260  0.1023  376 VAL A CB  
2986  C CG1 . VAL A 376 ? 0.3400 0.6170 0.5366 0.0587  0.0298  0.0908  376 VAL A CG1 
2987  C CG2 . VAL A 376 ? 0.2740 0.5722 0.4873 0.0558  0.0268  0.1085  376 VAL A CG2 
2988  N N   . ILE A 377 ? 0.2410 0.5167 0.4413 0.0524  0.0217  0.1015  377 ILE A N   
2989  C CA  . ILE A 377 ? 0.2220 0.4883 0.4161 0.0516  0.0217  0.0956  377 ILE A CA  
2990  C C   . ILE A 377 ? 0.2487 0.5041 0.4510 0.0577  0.0225  0.0922  377 ILE A C   
2991  O O   . ILE A 377 ? 0.2367 0.4793 0.4368 0.0612  0.0241  0.0819  377 ILE A O   
2992  C CB  . ILE A 377 ? 0.2507 0.5261 0.4386 0.0432  0.0183  0.1030  377 ILE A CB  
2993  C CG1 . ILE A 377 ? 0.2410 0.5233 0.4182 0.0367  0.0177  0.1018  377 ILE A CG1 
2994  C CG2 . ILE A 377 ? 0.2258 0.4923 0.4118 0.0434  0.0186  0.0991  377 ILE A CG2 
2995  C CD1 . ILE A 377 ? 0.2683 0.5643 0.4410 0.0277  0.0134  0.1111  377 ILE A CD1 
2996  N N   . ASN A 378 ? 0.2315 0.4918 0.4435 0.0587  0.0212  0.1008  378 ASN A N   
2997  C CA  . ASN A 378 ? 0.2478 0.4981 0.4682 0.0641  0.0221  0.0981  378 ASN A CA  
2998  C C   . ASN A 378 ? 0.2586 0.4989 0.4828 0.0713  0.0245  0.0873  378 ASN A C   
2999  O O   . ASN A 378 ? 0.2864 0.5148 0.5131 0.0755  0.0251  0.0790  378 ASN A O   
3000  C CB  . ASN A 378 ? 0.2417 0.5005 0.4719 0.0636  0.0203  0.1106  378 ASN A CB  
3001  C CG  . ASN A 378 ? 0.3080 0.5776 0.5339 0.0565  0.0173  0.1216  378 ASN A CG  
3002  O OD1 . ASN A 378 ? 0.3177 0.5872 0.5337 0.0520  0.0168  0.1190  378 ASN A OD1 
3003  N ND2 . ASN A 378 ? 0.2861 0.5654 0.5192 0.0552  0.0152  0.1338  378 ASN A ND2 
3004  N N   . ALA A 379 ? 0.2332 0.4786 0.4577 0.0726  0.0257  0.0869  379 ALA A N   
3005  C CA  . ALA A 379 ? 0.2848 0.5216 0.5114 0.0790  0.0281  0.0764  379 ALA A CA  
3006  C C   . ALA A 379 ? 0.2422 0.4681 0.4590 0.0800  0.0289  0.0643  379 ALA A C   
3007  O O   . ALA A 379 ? 0.2547 0.4692 0.4728 0.0851  0.0292  0.0537  379 ALA A O   
3008  C CB  . ALA A 379 ? 0.2297 0.4755 0.4590 0.0800  0.0297  0.0800  379 ALA A CB  
3009  N N   . LEU A 380 ? 0.2567 0.4861 0.4635 0.0750  0.0288  0.0654  380 LEU A N   
3010  C CA  . LEU A 380 ? 0.2458 0.4649 0.4434 0.0756  0.0296  0.0547  380 LEU A CA  
3011  C C   . LEU A 380 ? 0.2311 0.4394 0.4297 0.0764  0.0281  0.0489  380 LEU A C   
3012  O O   . LEU A 380 ? 0.2235 0.4199 0.4188 0.0795  0.0281  0.0374  380 LEU A O   
3013  C CB  . LEU A 380 ? 0.1913 0.4176 0.3785 0.0694  0.0297  0.0581  380 LEU A CB  
3014  C CG  . LEU A 380 ? 0.2733 0.4898 0.4505 0.0693  0.0306  0.0483  380 LEU A CG  
3015  C CD1 . LEU A 380 ? 0.2997 0.5072 0.4749 0.0754  0.0328  0.0388  380 LEU A CD1 
3016  C CD2 . LEU A 380 ? 0.2536 0.4788 0.4209 0.0623  0.0305  0.0525  380 LEU A CD2 
3017  N N   . TYR A 381 ? 0.2693 0.4816 0.4726 0.0737  0.0266  0.0569  381 TYR A N   
3018  C CA  . TYR A 381 ? 0.2560 0.4585 0.4608 0.0743  0.0257  0.0521  381 TYR A CA  
3019  C C   . TYR A 381 ? 0.2622 0.4551 0.4744 0.0808  0.0253  0.0445  381 TYR A C   
3020  O O   . TYR A 381 ? 0.2827 0.4641 0.4924 0.0837  0.0244  0.0328  381 TYR A O   
3021  C CB  . TYR A 381 ? 0.1850 0.3949 0.3926 0.0696  0.0248  0.0638  381 TYR A CB  
3022  C CG  . TYR A 381 ? 0.3100 0.5098 0.5217 0.0712  0.0247  0.0601  381 TYR A CG  
3023  C CD1 . TYR A 381 ? 0.2517 0.4427 0.4575 0.0702  0.0250  0.0517  381 TYR A CD1 
3024  C CD2 . TYR A 381 ? 0.3438 0.5426 0.5655 0.0738  0.0246  0.0650  381 TYR A CD2 
3025  C CE1 . TYR A 381 ? 0.2947 0.4765 0.5045 0.0717  0.0251  0.0483  381 TYR A CE1 
3026  C CE2 . TYR A 381 ? 0.3007 0.4902 0.5262 0.0752  0.0249  0.0621  381 TYR A CE2 
3027  C CZ  . TYR A 381 ? 0.2883 0.4694 0.5078 0.0741  0.0251  0.0537  381 TYR A CZ  
3028  O OH  . TYR A 381 ? 0.3211 0.4928 0.5445 0.0753  0.0256  0.0509  381 TYR A OH  
3029  N N   . LEU A 382 ? 0.2925 0.4906 0.5137 0.0831  0.0254  0.0509  382 LEU A N   
3030  C CA  . LEU A 382 ? 0.3095 0.5000 0.5376 0.0892  0.0249  0.0439  382 LEU A CA  
3031  C C   . LEU A 382 ? 0.3728 0.5559 0.5962 0.0938  0.0246  0.0301  382 LEU A C   
3032  O O   . LEU A 382 ? 0.4202 0.5942 0.6437 0.0983  0.0229  0.0198  382 LEU A O   
3033  C CB  . LEU A 382 ? 0.2948 0.4935 0.5332 0.0907  0.0256  0.0533  382 LEU A CB  
3034  C CG  . LEU A 382 ? 0.3161 0.5221 0.5605 0.0869  0.0253  0.0674  382 LEU A CG  
3035  C CD1 . LEU A 382 ? 0.3675 0.5814 0.6223 0.0889  0.0257  0.0760  382 LEU A CD1 
3036  C CD2 . LEU A 382 ? 0.3283 0.5253 0.5750 0.0874  0.0249  0.0654  382 LEU A CD2 
3037  N N   . GLU A 383 ? 0.3492 0.5366 0.5678 0.0927  0.0262  0.0302  383 GLU A N   
3038  C CA  . GLU A 383 ? 0.3379 0.5187 0.5528 0.0969  0.0264  0.0185  383 GLU A CA  
3039  C C   . GLU A 383 ? 0.3183 0.4880 0.5252 0.0966  0.0245  0.0074  383 GLU A C   
3040  O O   . GLU A 383 ? 0.3565 0.5179 0.5626 0.1008  0.0228  -0.0045 383 GLU A O   
3041  C CB  . GLU A 383 ? 0.3465 0.5352 0.5585 0.0957  0.0295  0.0236  383 GLU A CB  
3042  C CG  . GLU A 383 ? 0.4084 0.5905 0.6163 0.0994  0.0308  0.0135  383 GLU A CG  
3043  C CD  . GLU A 383 ? 0.5475 0.7268 0.7633 0.1057  0.0304  0.0071  383 GLU A CD  
3044  O OE1 . GLU A 383 ? 0.5332 0.7186 0.7575 0.1072  0.0302  0.0128  383 GLU A OE1 
3045  O OE2 . GLU A 383 ? 0.5566 0.7276 0.7705 0.1089  0.0305  -0.0033 383 GLU A OE2 
3046  N N   . SER A 384 ? 0.3350 0.5049 0.5367 0.0916  0.0245  0.0109  384 SER A N   
3047  C CA  . SER A 384 ? 0.2773 0.4375 0.4716 0.0907  0.0234  0.0011  384 SER A CA  
3048  C C   . SER A 384 ? 0.3222 0.4793 0.5137 0.0875  0.0221  0.0012  384 SER A C   
3049  O O   . SER A 384 ? 0.3556 0.5036 0.5417 0.0876  0.0205  -0.0083 384 SER A O   
3050  C CB  . SER A 384 ? 0.3110 0.4740 0.4975 0.0879  0.0265  0.0039  384 SER A CB  
3051  O OG  . SER A 384 ? 0.3039 0.4790 0.4876 0.0828  0.0280  0.0160  384 SER A OG  
3052  N N   . GLY A 385 ? 0.3342 0.4982 0.5296 0.0844  0.0229  0.0119  385 GLY A N   
3053  C CA  . GLY A 385 ? 0.3215 0.4831 0.5148 0.0809  0.0227  0.0132  385 GLY A CA  
3054  C C   . GLY A 385 ? 0.2483 0.4148 0.4345 0.0749  0.0244  0.0175  385 GLY A C   
3055  O O   . GLY A 385 ? 0.2289 0.3934 0.4132 0.0717  0.0247  0.0179  385 GLY A O   
3056  N N   . VAL A 386 ? 0.2292 0.4024 0.4106 0.0735  0.0258  0.0207  386 VAL A N   
3057  C CA  . VAL A 386 ? 0.2335 0.4149 0.4066 0.0675  0.0272  0.0263  386 VAL A CA  
3058  C C   . VAL A 386 ? 0.2090 0.4050 0.3847 0.0626  0.0269  0.0403  386 VAL A C   
3059  O O   . VAL A 386 ? 0.2538 0.4569 0.4350 0.0639  0.0266  0.0468  386 VAL A O   
3060  C CB  . VAL A 386 ? 0.2514 0.4344 0.4170 0.0683  0.0287  0.0239  386 VAL A CB  
3061  C CG1 . VAL A 386 ? 0.1388 0.3344 0.2957 0.0615  0.0295  0.0313  386 VAL A CG1 
3062  C CG2 . VAL A 386 ? 0.2379 0.4058 0.3992 0.0718  0.0288  0.0111  386 VAL A CG2 
3063  N N   . ARG A 387 ? 0.2112 0.4122 0.3834 0.0566  0.0268  0.0449  387 ARG A N   
3064  C CA  . ARG A 387 ? 0.1714 0.3868 0.3446 0.0508  0.0256  0.0581  387 ARG A CA  
3065  C C   . ARG A 387 ? 0.1630 0.3900 0.3258 0.0436  0.0250  0.0617  387 ARG A C   
3066  O O   . ARG A 387 ? 0.1744 0.3994 0.3289 0.0396  0.0258  0.0568  387 ARG A O   
3067  C CB  . ARG A 387 ? 0.1436 0.3578 0.3201 0.0483  0.0256  0.0616  387 ARG A CB  
3068  C CG  . ARG A 387 ? 0.1672 0.3973 0.3412 0.0407  0.0238  0.0747  387 ARG A CG  
3069  C CD  . ARG A 387 ? 0.2318 0.4615 0.4107 0.0391  0.0242  0.0803  387 ARG A CD  
3070  N NE  . ARG A 387 ? 0.1394 0.3606 0.3152 0.0374  0.0265  0.0727  387 ARG A NE  
3071  C CZ  . ARG A 387 ? 0.1549 0.3750 0.3341 0.0354  0.0280  0.0765  387 ARG A CZ  
3072  N NH1 . ARG A 387 ? 0.1808 0.4080 0.3663 0.0350  0.0271  0.0882  387 ARG A NH1 
3073  N NH2 . ARG A 387 ? 0.1216 0.3332 0.2983 0.0339  0.0307  0.0687  387 ARG A NH2 
3074  N N   . ALA A 388 ? 0.1910 0.4298 0.3543 0.0416  0.0236  0.0699  388 ALA A N   
3075  C CA  . ALA A 388 ? 0.1805 0.4313 0.3348 0.0338  0.0222  0.0742  388 ALA A CA  
3076  C C   . ALA A 388 ? 0.2044 0.4690 0.3597 0.0273  0.0187  0.0864  388 ALA A C   
3077  O O   . ALA A 388 ? 0.1830 0.4478 0.3458 0.0292  0.0179  0.0920  388 ALA A O   
3078  C CB  . ALA A 388 ? 0.1284 0.3815 0.2824 0.0366  0.0233  0.0729  388 ALA A CB  
3079  N N   . VAL A 389 ? 0.2024 0.4784 0.3498 0.0193  0.0164  0.0905  389 VAL A N   
3080  C CA  . VAL A 389 ? 0.1853 0.4747 0.3310 0.0118  0.0122  0.1012  389 VAL A CA  
3081  C C   . VAL A 389 ? 0.2393 0.5401 0.3849 0.0086  0.0097  0.1067  389 VAL A C   
3082  O O   . VAL A 389 ? 0.2059 0.5051 0.3491 0.0095  0.0115  0.1017  389 VAL A O   
3083  C CB  . VAL A 389 ? 0.2135 0.5052 0.3475 0.0023  0.0110  0.0997  389 VAL A CB  
3084  C CG1 . VAL A 389 ? 0.1816 0.4752 0.3041 -0.0046 0.0107  0.0943  389 VAL A CG1 
3085  C CG2 . VAL A 389 ? 0.2447 0.5485 0.3781 -0.0038 0.0067  0.1108  389 VAL A CG2 
3086  N N   . GLU A 390 ? 0.3225 0.6353 0.4711 0.0050  0.0056  0.1176  390 GLU A N   
3087  C CA  A GLU A 390 ? 0.2959 0.6201 0.4469 0.0023  0.0028  0.1240  390 GLU A CA  
3088  C CA  B GLU A 390 ? 0.2960 0.6203 0.4470 0.0023  0.0028  0.1241  390 GLU A CA  
3089  C C   . GLU A 390 ? 0.2749 0.6091 0.4143 -0.0092 -0.0013 0.1258  390 GLU A C   
3090  O O   . GLU A 390 ? 0.3595 0.6982 0.4923 -0.0156 -0.0044 0.1291  390 GLU A O   
3091  C CB  A GLU A 390 ? 0.3152 0.6464 0.4774 0.0055  0.0005  0.1349  390 GLU A CB  
3092  C CB  B GLU A 390 ? 0.3154 0.6468 0.4776 0.0053  0.0004  0.1350  390 GLU A CB  
3093  C CG  A GLU A 390 ? 0.3485 0.6886 0.5179 0.0060  -0.0009 0.1402  390 GLU A CG  
3094  C CG  B GLU A 390 ? 0.3429 0.6799 0.5140 0.0084  0.0004  0.1387  390 GLU A CG  
3095  C CD  A GLU A 390 ? 0.3981 0.7536 0.5641 -0.0030 -0.0069 0.1494  390 GLU A CD  
3096  C CD  B GLU A 390 ? 0.3756 0.7271 0.5508 0.0038  -0.0049 0.1508  390 GLU A CD  
3097  O OE1 A GLU A 390 ? 0.3691 0.7284 0.5251 -0.0104 -0.0101 0.1507  390 GLU A OE1 
3098  O OE1 B GLU A 390 ? 0.3941 0.7552 0.5606 -0.0054 -0.0093 0.1538  390 GLU A OE1 
3099  O OE2 A GLU A 390 ? 0.3964 0.7603 0.5701 -0.0028 -0.0086 0.1551  390 GLU A OE2 
3100  O OE2 B GLU A 390 ? 0.3556 0.7088 0.5428 0.0092  -0.0048 0.1569  390 GLU A OE2 
3101  N N   . ILE A 391 ? 0.3166 0.6539 0.4535 -0.0119 -0.0013 0.1232  391 ILE A N   
3102  C CA  . ILE A 391 ? 0.3596 0.7058 0.4864 -0.0229 -0.0053 0.1242  391 ILE A CA  
3103  C C   . ILE A 391 ? 0.3937 0.7512 0.5281 -0.0239 -0.0080 0.1314  391 ILE A C   
3104  O O   . ILE A 391 ? 0.3656 0.7241 0.4995 -0.0255 -0.0068 0.1281  391 ILE A O   
3105  C CB  . ILE A 391 ? 0.3640 0.7023 0.4802 -0.0267 -0.0026 0.1136  391 ILE A CB  
3106  C CG1 . ILE A 391 ? 0.2685 0.5938 0.3802 -0.0237 0.0012  0.1057  391 ILE A CG1 
3107  C CG2 . ILE A 391 ? 0.3195 0.6650 0.4240 -0.0391 -0.0069 0.1137  391 ILE A CG2 
3108  C CD1 . ILE A 391 ? 0.2753 0.6020 0.3800 -0.0296 -0.0013 0.1075  391 ILE A CD1 
3109  N N   . GLY A 392 ? 0.4449 0.8106 0.5872 -0.0226 -0.0113 0.1413  392 GLY A N   
3110  C CA  . GLY A 392 ? 0.4438 0.8203 0.5951 -0.0231 -0.0139 0.1484  392 GLY A CA  
3111  C C   . GLY A 392 ? 0.4776 0.8658 0.6317 -0.0268 -0.0197 0.1594  392 GLY A C   
3112  O O   . GLY A 392 ? 0.4484 0.8424 0.5920 -0.0355 -0.0241 0.1614  392 GLY A O   
3113  N N   . SER A 393 ? 0.5821 0.9735 0.7501 -0.0203 -0.0196 0.1665  393 SER A N   
3114  C CA  . SER A 393 ? 0.5849 0.9882 0.7573 -0.0234 -0.0252 0.1779  393 SER A CA  
3115  C C   . SER A 393 ? 0.5903 0.9921 0.7581 -0.0237 -0.0265 0.1818  393 SER A C   
3116  O O   . SER A 393 ? 0.6797 1.0914 0.8416 -0.0309 -0.0319 0.1885  393 SER A O   
3117  C CB  . SER A 393 ? 0.5610 0.9670 0.7504 -0.0160 -0.0242 0.1837  393 SER A CB  
3118  O OG  . SER A 393 ? 0.6411 1.0346 0.8372 -0.0059 -0.0180 0.1790  393 SER A OG  
3119  N N   . PHE A 394 ? 0.5303 0.9199 0.7009 -0.0160 -0.0214 0.1777  394 PHE A N   
3120  C CA  . PHE A 394 ? 0.4192 0.8066 0.5873 -0.0155 -0.0217 0.1812  394 PHE A CA  
3121  C C   . PHE A 394 ? 0.4465 0.8374 0.5983 -0.0254 -0.0247 0.1792  394 PHE A C   
3122  O O   . PHE A 394 ? 0.4518 0.8514 0.5993 -0.0305 -0.0288 0.1870  394 PHE A O   
3123  C CB  . PHE A 394 ? 0.4269 0.7987 0.6006 -0.0058 -0.0153 0.1743  394 PHE A CB  
3124  C CG  . PHE A 394 ? 0.4855 0.8541 0.6628 -0.0025 -0.0147 0.1795  394 PHE A CG  
3125  C CD1 . PHE A 394 ? 0.4244 0.8044 0.6037 -0.0058 -0.0192 0.1917  394 PHE A CD1 
3126  C CD2 . PHE A 394 ? 0.4616 0.8158 0.6409 0.0039  -0.0095 0.1720  394 PHE A CD2 
3127  C CE1 . PHE A 394 ? 0.4762 0.8534 0.6595 -0.0026 -0.0181 0.1972  394 PHE A CE1 
3128  C CE2 . PHE A 394 ? 0.4066 0.7574 0.5905 0.0070  -0.0085 0.1767  394 PHE A CE2 
3129  C CZ  . PHE A 394 ? 0.4295 0.7920 0.6156 0.0039  -0.0126 0.1898  394 PHE A CZ  
3130  N N   . LEU A 395 ? 0.4026 0.7873 0.5449 -0.0285 -0.0226 0.1685  395 LEU A N   
3131  C CA  . LEU A 395 ? 0.4167 0.8026 0.5431 -0.0381 -0.0245 0.1644  395 LEU A CA  
3132  C C   . LEU A 395 ? 0.6007 1.0000 0.7185 -0.0492 -0.0309 0.1688  395 LEU A C   
3133  O O   . LEU A 395 ? 0.6388 1.0413 0.7432 -0.0580 -0.0335 0.1678  395 LEU A O   
3134  C CB  . LEU A 395 ? 0.4312 0.8052 0.5510 -0.0379 -0.0199 0.1512  395 LEU A CB  
3135  C CG  . LEU A 395 ? 0.4233 0.7943 0.5272 -0.0468 -0.0202 0.1440  395 LEU A CG  
3136  C CD1 . LEU A 395 ? 0.3880 0.7430 0.4912 -0.0415 -0.0137 0.1330  395 LEU A CD1 
3137  C CD2 . LEU A 395 ? 0.4179 0.7942 0.5115 -0.0567 -0.0233 0.1406  395 LEU A CD2 
3138  N N   . LEU A 396 ? 0.5946 1.0014 0.7199 -0.0492 -0.0334 0.1731  396 LEU A N   
3139  C CA  . LEU A 396 ? 0.5589 0.9767 0.6765 -0.0597 -0.0391 0.1750  396 LEU A CA  
3140  C C   . LEU A 396 ? 0.5927 1.0218 0.7070 -0.0653 -0.0449 0.1849  396 LEU A C   
3141  O O   . LEU A 396 ? 0.5571 0.9927 0.6597 -0.0758 -0.0495 0.1842  396 LEU A O   
3142  C CB  . LEU A 396 ? 0.5817 1.0040 0.7102 -0.0577 -0.0397 0.1762  396 LEU A CB  
3143  C CG  . LEU A 396 ? 0.5724 1.0013 0.6936 -0.0678 -0.0436 0.1732  396 LEU A CG  
3144  C CD1 . LEU A 396 ? 0.4469 0.8669 0.5535 -0.0733 -0.0410 0.1618  396 LEU A CD1 
3145  C CD2 . LEU A 396 ? 0.5676 1.0004 0.7023 -0.0644 -0.0432 0.1744  396 LEU A CD2 
3146  N N   . GLY A 397 ? 0.7257 1.1564 0.8499 -0.0586 -0.0448 0.1936  397 GLY A N   
3147  C CA  . GLY A 397 ? 0.8001 1.2409 0.9214 -0.0631 -0.0499 0.2034  397 GLY A CA  
3148  C C   . GLY A 397 ? 0.7803 1.2337 0.9038 -0.0687 -0.0565 0.2095  397 GLY A C   
3149  O O   . GLY A 397 ? 0.8218 1.2781 0.9588 -0.0640 -0.0568 0.2126  397 GLY A O   
3150  N N   . GLN A 405 ? 0.7901 1.2800 0.9906 -0.0501 -0.0692 0.2453  405 GLN A N   
3151  C CA  . GLN A 405 ? 0.7970 1.2746 0.9873 -0.0494 -0.0630 0.2347  405 GLN A CA  
3152  C C   . GLN A 405 ? 0.7897 1.2679 0.9729 -0.0559 -0.0636 0.2260  405 GLN A C   
3153  O O   . GLN A 405 ? 0.8924 1.3754 1.0856 -0.0555 -0.0647 0.2260  405 GLN A O   
3154  C CB  . GLN A 405 ? 0.7765 1.2426 0.9780 -0.0380 -0.0551 0.2320  405 GLN A CB  
3155  C CG  . GLN A 405 ? 0.8444 1.2972 1.0364 -0.0362 -0.0488 0.2211  405 GLN A CG  
3156  C CD  . GLN A 405 ? 0.7759 1.2165 0.9775 -0.0249 -0.0417 0.2188  405 GLN A CD  
3157  O OE1 . GLN A 405 ? 0.7633 1.1942 0.9653 -0.0207 -0.0363 0.2098  405 GLN A OE1 
3158  N NE2 . GLN A 405 ? 0.7680 1.2088 0.9775 -0.0201 -0.0418 0.2268  405 GLN A NE2 
3159  N N   . LYS A 406 ? 0.8016 1.2747 0.9679 -0.0620 -0.0628 0.2186  406 LYS A N   
3160  C CA  . LYS A 406 ? 0.7549 1.2276 0.9130 -0.0690 -0.0633 0.2099  406 LYS A CA  
3161  C C   . LYS A 406 ? 0.7544 1.2200 0.9220 -0.0624 -0.0571 0.2038  406 LYS A C   
3162  O O   . LYS A 406 ? 0.7978 1.2529 0.9686 -0.0541 -0.0507 0.2006  406 LYS A O   
3163  C CB  . LYS A 406 ? 0.5985 1.0651 0.7372 -0.0757 -0.0624 0.2027  406 LYS A CB  
3164  C CG  . LYS A 406 ? 0.6154 1.0827 0.7433 -0.0853 -0.0643 0.1946  406 LYS A CG  
3165  C CD  . LYS A 406 ? 0.5431 1.0029 0.6521 -0.0914 -0.0626 0.1869  406 LYS A CD  
3166  C CE  . LYS A 406 ? 0.4824 0.9471 0.5820 -0.0962 -0.0668 0.1924  406 LYS A CE  
3167  N NZ  . LYS A 406 ? 0.4749 0.9318 0.5568 -0.1020 -0.0644 0.1845  406 LYS A NZ  
3168  N N   . HIS A 407 ? 0.6819 1.1530 0.8541 -0.0661 -0.0590 0.2017  407 HIS A N   
3169  C CA  . HIS A 407 ? 0.6890 1.1554 0.8722 -0.0598 -0.0533 0.1973  407 HIS A CA  
3170  C C   . HIS A 407 ? 0.6601 1.1142 0.8326 -0.0597 -0.0474 0.1863  407 HIS A C   
3171  O O   . HIS A 407 ? 0.6070 1.0602 0.7659 -0.0682 -0.0492 0.1807  407 HIS A O   
3172  C CB  . HIS A 407 ? 0.7370 1.2138 0.9296 -0.0641 -0.0571 0.1990  407 HIS A CB  
3173  C CG  . HIS A 407 ? 0.7401 1.2141 0.9466 -0.0572 -0.0513 0.1964  407 HIS A CG  
3174  N ND1 . HIS A 407 ? 0.7768 1.2534 1.0004 -0.0490 -0.0496 0.2024  407 HIS A ND1 
3175  C CD2 . HIS A 407 ? 0.7080 1.1767 0.9137 -0.0574 -0.0465 0.1885  407 HIS A CD2 
3176  C CE1 . HIS A 407 ? 0.8243 1.2976 1.0567 -0.0445 -0.0438 0.1981  407 HIS A CE1 
3177  N NE2 . HIS A 407 ? 0.8059 1.2745 1.0278 -0.0494 -0.0419 0.1899  407 HIS A NE2 
3178  N N   . ALA A 408 ? 0.6877 1.1321 0.8666 -0.0502 -0.0404 0.1828  408 ALA A N   
3179  C CA  . ALA A 408 ? 0.6033 1.0352 0.7734 -0.0486 -0.0344 0.1725  408 ALA A CA  
3180  C C   . ALA A 408 ? 0.5494 0.9801 0.7264 -0.0469 -0.0304 0.1678  408 ALA A C   
3181  O O   . ALA A 408 ? 0.5443 0.9784 0.7361 -0.0411 -0.0286 0.1715  408 ALA A O   
3182  C CB  . ALA A 408 ? 0.5184 0.9392 0.6900 -0.0391 -0.0292 0.1709  408 ALA A CB  
3183  N N   . ASP A 409 ? 0.4867 0.9123 0.6531 -0.0521 -0.0288 0.1595  409 ASP A N   
3184  C CA  . ASP A 409 ? 0.4817 0.9049 0.6532 -0.0507 -0.0241 0.1545  409 ASP A CA  
3185  C C   . ASP A 409 ? 0.4546 0.8643 0.6243 -0.0425 -0.0163 0.1474  409 ASP A C   
3186  O O   . ASP A 409 ? 0.5034 0.9104 0.6781 -0.0396 -0.0113 0.1438  409 ASP A O   
3187  C CB  . ASP A 409 ? 0.4242 0.8494 0.5863 -0.0613 -0.0266 0.1496  409 ASP A CB  
3188  C CG  . ASP A 409 ? 0.4858 0.9250 0.6536 -0.0688 -0.0336 0.1557  409 ASP A CG  
3189  O OD1 . ASP A 409 ? 0.5548 1.0014 0.7382 -0.0655 -0.0335 0.1606  409 ASP A OD1 
3190  O OD2 . ASP A 409 ? 0.5436 0.9862 0.7003 -0.0778 -0.0392 0.1552  409 ASP A OD2 
3191  N N   . MET A 410 ? 0.4681 0.8694 0.6311 -0.0387 -0.0150 0.1454  410 MET A N   
3192  C CA  . MET A 410 ? 0.4423 0.8303 0.6029 -0.0311 -0.0082 0.1380  410 MET A CA  
3193  C C   . MET A 410 ? 0.4494 0.8324 0.6126 -0.0239 -0.0076 0.1404  410 MET A C   
3194  O O   . MET A 410 ? 0.4996 0.8850 0.6574 -0.0277 -0.0118 0.1437  410 MET A O   
3195  C CB  . MET A 410 ? 0.4716 0.8512 0.6170 -0.0366 -0.0069 0.1290  410 MET A CB  
3196  C CG  . MET A 410 ? 0.4690 0.8521 0.6110 -0.0445 -0.0074 0.1260  410 MET A CG  
3197  S SD  . MET A 410 ? 0.5132 0.8896 0.6362 -0.0548 -0.0090 0.1176  410 MET A SD  
3198  C CE  . MET A 410 ? 0.3330 0.7171 0.4495 -0.0616 -0.0167 0.1234  410 MET A CE  
3199  N N   . GLU A 411 ? 0.4217 0.7979 0.5932 -0.0139 -0.0022 0.1387  411 GLU A N   
3200  C CA  . GLU A 411 ? 0.3608 0.7302 0.5362 -0.0063 -0.0007 0.1395  411 GLU A CA  
3201  C C   . GLU A 411 ? 0.3866 0.7415 0.5563 -0.0005 0.0050  0.1296  411 GLU A C   
3202  O O   . GLU A 411 ? 0.3833 0.7325 0.5589 0.0071  0.0101  0.1261  411 GLU A O   
3203  C CB  . GLU A 411 ? 0.4051 0.7784 0.5960 0.0007  0.0003  0.1457  411 GLU A CB  
3204  C CG  . GLU A 411 ? 0.4786 0.8659 0.6764 -0.0041 -0.0057 0.1560  411 GLU A CG  
3205  C CD  . GLU A 411 ? 0.5555 0.9451 0.7495 -0.0069 -0.0105 0.1616  411 GLU A CD  
3206  O OE1 . GLU A 411 ? 0.5280 0.9078 0.7185 -0.0027 -0.0082 0.1583  411 GLU A OE1 
3207  O OE2 . GLU A 411 ? 0.5515 0.9529 0.7462 -0.0133 -0.0164 0.1692  411 GLU A OE2 
3208  N N   . PHE A 412 ? 0.3630 0.7121 0.5212 -0.0042 0.0042  0.1249  412 PHE A N   
3209  C CA  . PHE A 412 ? 0.3255 0.6614 0.4770 -0.0005 0.0089  0.1149  412 PHE A CA  
3210  C C   . PHE A 412 ? 0.2737 0.6004 0.4269 0.0058  0.0101  0.1130  412 PHE A C   
3211  O O   . PHE A 412 ? 0.2557 0.5856 0.4087 0.0031  0.0066  0.1180  412 PHE A O   
3212  C CB  . PHE A 412 ? 0.3254 0.6597 0.4629 -0.0093 0.0077  0.1095  412 PHE A CB  
3213  C CG  . PHE A 412 ? 0.3381 0.6773 0.4730 -0.0147 0.0080  0.1084  412 PHE A CG  
3214  C CD1 . PHE A 412 ? 0.3227 0.6625 0.4653 -0.0093 0.0119  0.1084  412 PHE A CD1 
3215  C CD2 . PHE A 412 ? 0.3259 0.6685 0.4504 -0.0253 0.0046  0.1070  412 PHE A CD2 
3216  C CE1 . PHE A 412 ? 0.3866 0.7307 0.5278 -0.0143 0.0127  0.1077  412 PHE A CE1 
3217  C CE2 . PHE A 412 ? 0.3673 0.7134 0.4902 -0.0304 0.0050  0.1056  412 PHE A CE2 
3218  C CZ  . PHE A 412 ? 0.3326 0.6796 0.4644 -0.0248 0.0091  0.1063  412 PHE A CZ  
3219  N N   . MET A 413 ? 0.2678 0.5830 0.4226 0.0139  0.0151  0.1056  413 MET A N   
3220  C CA  . MET A 413 ? 0.2324 0.5359 0.3857 0.0185  0.0167  0.0999  413 MET A CA  
3221  C C   . MET A 413 ? 0.2017 0.4980 0.3429 0.0152  0.0185  0.0911  413 MET A C   
3222  O O   . MET A 413 ? 0.1979 0.4908 0.3358 0.0169  0.0217  0.0858  413 MET A O   
3223  C CB  . MET A 413 ? 0.2334 0.5274 0.3954 0.0293  0.0206  0.0961  413 MET A CB  
3224  C CG  . MET A 413 ? 0.2220 0.5017 0.3807 0.0338  0.0227  0.0871  413 MET A CG  
3225  S SD  . MET A 413 ? 0.2672 0.5338 0.4347 0.0457  0.0263  0.0805  413 MET A SD  
3226  C CE  . MET A 413 ? 0.2503 0.5165 0.4146 0.0489  0.0304  0.0759  413 MET A CE  
3227  N N   . ARG A 414 ? 0.1832 0.4773 0.3181 0.0105  0.0167  0.0896  414 ARG A N   
3228  C CA  . ARG A 414 ? 0.1933 0.4809 0.3167 0.0061  0.0181  0.0815  414 ARG A CA  
3229  C C   . ARG A 414 ? 0.1518 0.4254 0.2761 0.0136  0.0215  0.0730  414 ARG A C   
3230  O O   . ARG A 414 ? 0.1367 0.4067 0.2657 0.0160  0.0209  0.0739  414 ARG A O   
3231  C CB  . ARG A 414 ? 0.1693 0.4626 0.2843 -0.0046 0.0143  0.0840  414 ARG A CB  
3232  C CG  . ARG A 414 ? 0.1904 0.4775 0.2926 -0.0110 0.0157  0.0756  414 ARG A CG  
3233  C CD  . ARG A 414 ? 0.1647 0.4555 0.2573 -0.0220 0.0122  0.0770  414 ARG A CD  
3234  N NE  . ARG A 414 ? 0.2230 0.5094 0.3166 -0.0208 0.0126  0.0768  414 ARG A NE  
3235  C CZ  . ARG A 414 ? 0.2631 0.5508 0.3481 -0.0294 0.0107  0.0773  414 ARG A CZ  
3236  N NH1 . ARG A 414 ? 0.2321 0.5248 0.3061 -0.0399 0.0077  0.0773  414 ARG A NH1 
3237  N NH2 . ARG A 414 ? 0.2054 0.4886 0.2928 -0.0275 0.0121  0.0774  414 ARG A NH2 
3238  N N   . LEU A 415 ? 0.1443 0.4100 0.2645 0.0173  0.0250  0.0650  415 LEU A N   
3239  C CA  . LEU A 415 ? 0.1260 0.3778 0.2449 0.0235  0.0277  0.0556  415 LEU A CA  
3240  C C   . LEU A 415 ? 0.1465 0.3955 0.2541 0.0159  0.0279  0.0503  415 LEU A C   
3241  O O   . LEU A 415 ? 0.1386 0.3855 0.2380 0.0137  0.0297  0.0457  415 LEU A O   
3242  C CB  . LEU A 415 ? 0.1104 0.3548 0.2300 0.0321  0.0311  0.0500  415 LEU A CB  
3243  C CG  . LEU A 415 ? 0.1151 0.3637 0.2441 0.0377  0.0315  0.0552  415 LEU A CG  
3244  C CD1 . LEU A 415 ? 0.1267 0.3698 0.2532 0.0440  0.0353  0.0499  415 LEU A CD1 
3245  C CD2 . LEU A 415 ? 0.1916 0.4352 0.3309 0.0434  0.0305  0.0560  415 LEU A CD2 
3246  N N   . THR A 416 ? 0.1338 0.3825 0.2409 0.0115  0.0263  0.0512  416 THR A N   
3247  C CA  . THR A 416 ? 0.1050 0.3517 0.2010 0.0023  0.0264  0.0470  416 THR A CA  
3248  C C   . THR A 416 ? 0.0923 0.3254 0.1865 0.0070  0.0295  0.0365  416 THR A C   
3249  O O   . THR A 416 ? 0.1098 0.3365 0.2122 0.0138  0.0301  0.0347  416 THR A O   
3250  C CB  . THR A 416 ? 0.1175 0.3706 0.2125 -0.0053 0.0235  0.0532  416 THR A CB  
3251  O OG1 . THR A 416 ? 0.1352 0.3990 0.2383 -0.0039 0.0204  0.0636  416 THR A OG1 
3252  C CG2 . THR A 416 ? 0.1049 0.3603 0.1860 -0.0177 0.0220  0.0520  416 THR A CG2 
3253  N N   . ILE A 417 ? 0.1333 0.3613 0.2168 0.0030  0.0312  0.0294  417 ILE A N   
3254  C CA  . ILE A 417 ? 0.1467 0.3602 0.2271 0.0085  0.0338  0.0186  417 ILE A CA  
3255  C C   . ILE A 417 ? 0.1139 0.3166 0.1848 0.0003  0.0334  0.0132  417 ILE A C   
3256  O O   . ILE A 417 ? 0.1562 0.3598 0.2162 -0.0095 0.0332  0.0124  417 ILE A O   
3257  C CB  . ILE A 417 ? 0.1083 0.3183 0.1817 0.0112  0.0357  0.0139  417 ILE A CB  
3258  C CG1 . ILE A 417 ? 0.1756 0.3915 0.2559 0.0185  0.0359  0.0191  417 ILE A CG1 
3259  C CG2 . ILE A 417 ? 0.1535 0.3448 0.2219 0.0173  0.0369  0.0023  417 ILE A CG2 
3260  C CD1 . ILE A 417 ? 0.1747 0.3848 0.2659 0.0293  0.0355  0.0185  417 ILE A CD1 
3261  N N   . ALA A 418 ? 0.1292 0.3216 0.2052 0.0045  0.0337  0.0091  418 ALA A N   
3262  C CA  . ALA A 418 ? 0.1296 0.3101 0.1978 -0.0020 0.0343  0.0030  418 ALA A CA  
3263  C C   . ALA A 418 ? 0.1587 0.3262 0.2171 -0.0022 0.0355  -0.0071 418 ALA A C   
3264  O O   . ALA A 418 ? 0.1708 0.3346 0.2302 0.0058  0.0359  -0.0110 418 ALA A O   
3265  C CB  . ALA A 418 ? 0.1125 0.2843 0.1907 0.0037  0.0349  0.0008  418 ALA A CB  
3266  N N   . ARG A 419 ? 0.1251 0.2852 0.1738 -0.0112 0.0362  -0.0115 419 ARG A N   
3267  C CA  . ARG A 419 ? 0.1282 0.2765 0.1675 -0.0127 0.0372  -0.0204 419 ARG A CA  
3268  C C   . ARG A 419 ? 0.1305 0.2619 0.1737 -0.0052 0.0377  -0.0300 419 ARG A C   
3269  O O   . ARG A 419 ? 0.1272 0.2521 0.1745 -0.0065 0.0383  -0.0323 419 ARG A O   
3270  C CB  . ARG A 419 ? 0.1238 0.2715 0.1518 -0.0257 0.0378  -0.0213 419 ARG A CB  
3271  C CG  . ARG A 419 ? 0.1150 0.2785 0.1385 -0.0334 0.0367  -0.0133 419 ARG A CG  
3272  C CD  . ARG A 419 ? 0.1364 0.3008 0.1501 -0.0465 0.0369  -0.0134 419 ARG A CD  
3273  N NE  . ARG A 419 ? 0.1538 0.3331 0.1651 -0.0529 0.0342  -0.0052 419 ARG A NE  
3274  C CZ  . ARG A 419 ? 0.1383 0.3301 0.1551 -0.0528 0.0317  0.0038  419 ARG A CZ  
3275  N NH1 . ARG A 419 ? 0.1206 0.3137 0.1458 -0.0477 0.0325  0.0063  419 ARG A NH1 
3276  N NH2 . ARG A 419 ? 0.1389 0.3415 0.1538 -0.0573 0.0280  0.0105  419 ARG A NH2 
3277  N N   . ARG A 420 ? 0.1409 0.2656 0.1833 0.0028  0.0374  -0.0355 420 ARG A N   
3278  C CA  . ARG A 420 ? 0.1461 0.2545 0.1907 0.0101  0.0369  -0.0457 420 ARG A CA  
3279  C C   . ARG A 420 ? 0.1217 0.2272 0.1804 0.0190  0.0360  -0.0469 420 ARG A C   
3280  O O   . ARG A 420 ? 0.1643 0.2567 0.2274 0.0223  0.0356  -0.0548 420 ARG A O   
3281  C CB  . ARG A 420 ? 0.1455 0.2421 0.1836 0.0023  0.0379  -0.0524 420 ARG A CB  
3282  C CG  . ARG A 420 ? 0.1149 0.2135 0.1400 -0.0073 0.0390  -0.0518 420 ARG A CG  
3283  C CD  . ARG A 420 ? 0.1215 0.2056 0.1410 -0.0123 0.0401  -0.0604 420 ARG A CD  
3284  N NE  . ARG A 420 ? 0.1049 0.1868 0.1271 -0.0189 0.0416  -0.0607 420 ARG A NE  
3285  C CZ  . ARG A 420 ? 0.1288 0.2039 0.1444 -0.0279 0.0436  -0.0649 420 ARG A CZ  
3286  N NH1 . ARG A 420 ? 0.1651 0.2346 0.1722 -0.0316 0.0441  -0.0692 420 ARG A NH1 
3287  N NH2 . ARG A 420 ? 0.1130 0.1871 0.1307 -0.0335 0.0456  -0.0644 420 ARG A NH2 
3288  N N   . VAL A 421 ? 0.1284 0.2456 0.1954 0.0233  0.0357  -0.0393 421 VAL A N   
3289  C CA  . VAL A 421 ? 0.0916 0.2076 0.1736 0.0308  0.0352  -0.0391 421 VAL A CA  
3290  C C   . VAL A 421 ? 0.1273 0.2396 0.2136 0.0423  0.0334  -0.0398 421 VAL A C   
3291  O O   . VAL A 421 ? 0.1332 0.2288 0.2222 0.0473  0.0309  -0.0419 421 VAL A O   
3292  C CB  . VAL A 421 ? 0.1488 0.2777 0.2369 0.0259  0.0359  -0.0283 421 VAL A CB  
3293  C CG1 . VAL A 421 ? 0.0939 0.2228 0.1986 0.0348  0.0357  -0.0268 421 VAL A CG1 
3294  C CG2 . VAL A 421 ? 0.0939 0.2202 0.1757 0.0147  0.0373  -0.0276 421 VAL A CG2 
3295  N N   . TYR A 422 ? 0.1150 0.2384 0.1981 0.0440  0.0338  -0.0350 422 TYR A N   
3296  C CA  . TYR A 422 ? 0.1560 0.2726 0.2407 0.0522  0.0323  -0.0333 422 TYR A CA  
3297  C C   . TYR A 422 ? 0.1657 0.2752 0.2373 0.0540  0.0318  -0.0374 422 TYR A C   
3298  O O   . TYR A 422 ? 0.1779 0.2950 0.2409 0.0492  0.0335  -0.0381 422 TYR A O   
3299  C CB  . TYR A 422 ? 0.1285 0.2618 0.2216 0.0531  0.0333  -0.0238 422 TYR A CB  
3300  C CG  . TYR A 422 ? 0.1104 0.2500 0.2167 0.0517  0.0334  -0.0184 422 TYR A CG  
3301  C CD1 . TYR A 422 ? 0.1060 0.2331 0.2226 0.0568  0.0325  -0.0191 422 TYR A CD1 
3302  C CD2 . TYR A 422 ? 0.1757 0.3331 0.2831 0.0440  0.0345  -0.0110 422 TYR A CD2 
3303  C CE1 . TYR A 422 ? 0.1056 0.2378 0.2350 0.0557  0.0327  -0.0143 422 TYR A CE1 
3304  C CE2 . TYR A 422 ? 0.1443 0.3070 0.2625 0.0426  0.0345  -0.0048 422 TYR A CE2 
3305  C CZ  . TYR A 422 ? 0.1790 0.3293 0.3087 0.0492  0.0336  -0.0074 422 TYR A CZ  
3306  O OH  . TYR A 422 ? 0.1967 0.3514 0.3368 0.0480  0.0336  -0.0017 422 TYR A OH  
3307  N N   . THR A 423 ? 0.1604 0.2557 0.2301 0.0599  0.0299  -0.0395 423 THR A N   
3308  C CA  . THR A 423 ? 0.1914 0.2795 0.2490 0.0621  0.0292  -0.0427 423 THR A CA  
3309  C C   . THR A 423 ? 0.1705 0.2703 0.2281 0.0652  0.0314  -0.0378 423 THR A C   
3310  O O   . THR A 423 ? 0.1680 0.2791 0.2357 0.0662  0.0327  -0.0320 423 THR A O   
3311  C CB  . THR A 423 ? 0.2351 0.3038 0.2894 0.0651  0.0260  -0.0467 423 THR A CB  
3312  O OG1 . THR A 423 ? 0.1990 0.2670 0.2607 0.0696  0.0261  -0.0438 423 THR A OG1 
3313  C CG2 . THR A 423 ? 0.2084 0.2663 0.2644 0.0619  0.0237  -0.0495 423 THR A CG2 
3314  N N   . ASN A 424 ? 0.1732 0.2699 0.2194 0.0668  0.0320  -0.0395 424 ASN A N   
3315  C CA  . ASN A 424 ? 0.2038 0.3101 0.2495 0.0702  0.0345  -0.0348 424 ASN A CA  
3316  C C   . ASN A 424 ? 0.1850 0.2857 0.2379 0.0757  0.0334  -0.0345 424 ASN A C   
3317  O O   . ASN A 424 ? 0.2388 0.3490 0.2958 0.0783  0.0356  -0.0299 424 ASN A O   
3318  C CB  . ASN A 424 ? 0.2536 0.3562 0.2853 0.0709  0.0357  -0.0366 424 ASN A CB  
3319  C CG  . ASN A 424 ? 0.2385 0.3499 0.2642 0.0642  0.0382  -0.0350 424 ASN A CG  
3320  O OD1 . ASN A 424 ? 0.2351 0.3625 0.2667 0.0591  0.0403  -0.0294 424 ASN A OD1 
3321  N ND2 . ASN A 424 ? 0.2624 0.3634 0.2766 0.0629  0.0378  -0.0392 424 ASN A ND2 
3322  N N   . ASP A 425 ? 0.2061 0.2920 0.2613 0.0767  0.0305  -0.0389 425 ASP A N   
3323  C CA  . ASP A 425 ? 0.2084 0.2898 0.2719 0.0805  0.0302  -0.0382 425 ASP A CA  
3324  C C   . ASP A 425 ? 0.2181 0.3088 0.2970 0.0797  0.0314  -0.0329 425 ASP A C   
3325  O O   . ASP A 425 ? 0.2283 0.3223 0.3158 0.0827  0.0326  -0.0303 425 ASP A O   
3326  C CB  . ASP A 425 ? 0.2544 0.3189 0.3149 0.0808  0.0272  -0.0429 425 ASP A CB  
3327  C CG  . ASP A 425 ? 0.3076 0.3642 0.3545 0.0824  0.0255  -0.0473 425 ASP A CG  
3328  O OD1 . ASP A 425 ? 0.3100 0.3725 0.3514 0.0854  0.0274  -0.0464 425 ASP A OD1 
3329  O OD2 . ASP A 425 ? 0.3123 0.3577 0.3542 0.0807  0.0223  -0.0510 425 ASP A OD2 
3330  N N   . HIS A 426 ? 0.2016 0.2972 0.2849 0.0755  0.0312  -0.0313 426 HIS A N   
3331  C CA  . HIS A 426 ? 0.1504 0.2585 0.2476 0.0741  0.0321  -0.0251 426 HIS A CA  
3332  C C   . HIS A 426 ? 0.1456 0.2712 0.2427 0.0739  0.0339  -0.0193 426 HIS A C   
3333  O O   . HIS A 426 ? 0.1675 0.3012 0.2753 0.0749  0.0343  -0.0143 426 HIS A O   
3334  C CB  . HIS A 426 ? 0.1140 0.2257 0.2139 0.0692  0.0317  -0.0244 426 HIS A CB  
3335  C CG  . HIS A 426 ? 0.1321 0.2277 0.2329 0.0695  0.0305  -0.0278 426 HIS A CG  
3336  N ND1 . HIS A 426 ? 0.1259 0.2144 0.2180 0.0663  0.0293  -0.0327 426 HIS A ND1 
3337  C CD2 . HIS A 426 ? 0.1424 0.2283 0.2498 0.0723  0.0305  -0.0261 426 HIS A CD2 
3338  C CE1 . HIS A 426 ? 0.1492 0.2246 0.2422 0.0672  0.0279  -0.0342 426 HIS A CE1 
3339  N NE2 . HIS A 426 ? 0.1431 0.2173 0.2438 0.0711  0.0288  -0.0299 426 HIS A NE2 
3340  N N   . MET A 427 ? 0.1304 0.2619 0.2156 0.0721  0.0353  -0.0191 427 MET A N   
3341  C CA  . MET A 427 ? 0.1579 0.3056 0.2425 0.0710  0.0378  -0.0119 427 MET A CA  
3342  C C   . MET A 427 ? 0.2249 0.3705 0.3121 0.0770  0.0389  -0.0113 427 MET A C   
3343  O O   . MET A 427 ? 0.2421 0.4000 0.3363 0.0769  0.0403  -0.0043 427 MET A O   
3344  C CB  . MET A 427 ? 0.1257 0.2776 0.1972 0.0675  0.0397  -0.0122 427 MET A CB  
3345  C CG  . MET A 427 ? 0.1440 0.3003 0.2125 0.0599  0.0393  -0.0127 427 MET A CG  
3346  S SD  . MET A 427 ? 0.1499 0.3244 0.2295 0.0521  0.0388  -0.0030 427 MET A SD  
3347  C CE  . MET A 427 ? 0.1174 0.2810 0.2010 0.0518  0.0367  -0.0094 427 MET A CE  
3348  N N   . ASP A 428 ? 0.2164 0.3468 0.2977 0.0817  0.0383  -0.0183 428 ASP A N   
3349  C CA  . ASP A 428 ? 0.2468 0.3751 0.3302 0.0870  0.0396  -0.0185 428 ASP A CA  
3350  C C   . ASP A 428 ? 0.2393 0.3687 0.3389 0.0882  0.0388  -0.0166 428 ASP A C   
3351  O O   . ASP A 428 ? 0.2256 0.3618 0.3313 0.0909  0.0406  -0.0134 428 ASP A O   
3352  C CB  . ASP A 428 ? 0.1979 0.3099 0.2712 0.0907  0.0386  -0.0261 428 ASP A CB  
3353  C CG  . ASP A 428 ? 0.2181 0.3295 0.2754 0.0910  0.0399  -0.0274 428 ASP A CG  
3354  O OD1 . ASP A 428 ? 0.2126 0.3367 0.2675 0.0899  0.0431  -0.0219 428 ASP A OD1 
3355  O OD2 . ASP A 428 ? 0.2197 0.3179 0.2674 0.0918  0.0376  -0.0333 428 ASP A OD2 
3356  N N   . TYR A 429 ? 0.2106 0.3330 0.3180 0.0862  0.0364  -0.0186 429 TYR A N   
3357  C CA  . TYR A 429 ? 0.2172 0.3408 0.3413 0.0867  0.0356  -0.0167 429 TYR A CA  
3358  C C   . TYR A 429 ? 0.2396 0.3812 0.3701 0.0847  0.0358  -0.0087 429 TYR A C   
3359  O O   . TYR A 429 ? 0.2528 0.3997 0.3928 0.0870  0.0361  -0.0062 429 TYR A O   
3360  C CB  . TYR A 429 ? 0.2304 0.3438 0.3613 0.0843  0.0338  -0.0187 429 TYR A CB  
3361  C CG  . TYR A 429 ? 0.2000 0.3146 0.3495 0.0843  0.0327  -0.0172 429 TYR A CG  
3362  C CD1 . TYR A 429 ? 0.2533 0.3818 0.4094 0.0819  0.0304  -0.0133 429 TYR A CD1 
3363  C CD2 . TYR A 429 ? 0.1934 0.2948 0.3474 0.0860  0.0333  -0.0182 429 TYR A CD2 
3364  C CE1 . TYR A 429 ? 0.2463 0.3771 0.4147 0.0827  0.0274  -0.0140 429 TYR A CE1 
3365  C CE2 . TYR A 429 ? 0.2836 0.3846 0.4507 0.0843  0.0309  -0.0176 429 TYR A CE2 
3366  C CZ  . TYR A 429 ? 0.2793 0.3961 0.4519 0.0835  0.0258  -0.0191 429 TYR A CZ  
3367  O OH  . TYR A 429 ? 0.2896 0.4113 0.4669 0.0857  0.0205  -0.0227 429 TYR A OH  
3368  N N   . ILE A 430 ? 0.2001 0.3516 0.3253 0.0800  0.0359  -0.0039 430 ILE A N   
3369  C CA  . ILE A 430 ? 0.1972 0.3659 0.3272 0.0765  0.0363  0.0060  430 ILE A CA  
3370  C C   . ILE A 430 ? 0.2480 0.4250 0.3769 0.0787  0.0390  0.0103  430 ILE A C   
3371  O O   . ILE A 430 ? 0.2391 0.4240 0.3773 0.0794  0.0391  0.0160  430 ILE A O   
3372  C CB  . ILE A 430 ? 0.2230 0.4005 0.3464 0.0695  0.0362  0.0102  430 ILE A CB  
3373  C CG1 . ILE A 430 ? 0.1610 0.3312 0.2871 0.0675  0.0341  0.0064  430 ILE A CG1 
3374  C CG2 . ILE A 430 ? 0.2271 0.4226 0.3546 0.0644  0.0362  0.0215  430 ILE A CG2 
3375  C CD1 . ILE A 430 ? 0.1625 0.3360 0.2792 0.0615  0.0345  0.0060  430 ILE A CD1 
3376  N N   . ALA A 431 ? 0.1882 0.3630 0.3055 0.0800  0.0413  0.0076  431 ALA A N   
3377  C CA  . ALA A 431 ? 0.2381 0.4210 0.3540 0.0819  0.0446  0.0119  431 ALA A CA  
3378  C C   . ALA A 431 ? 0.3021 0.4804 0.4260 0.0881  0.0454  0.0096  431 ALA A C   
3379  O O   . ALA A 431 ? 0.2710 0.4593 0.4026 0.0887  0.0469  0.0158  431 ALA A O   
3380  C CB  . ALA A 431 ? 0.2669 0.4461 0.3681 0.0826  0.0472  0.0085  431 ALA A CB  
3381  N N   . ASP A 432 ? 0.2817 0.4448 0.4046 0.0922  0.0443  0.0007  432 ASP A N   
3382  C CA  . ASP A 432 ? 0.3116 0.4702 0.4423 0.0974  0.0451  -0.0024 432 ASP A CA  
3383  C C   . ASP A 432 ? 0.2793 0.4436 0.4261 0.0968  0.0430  0.0010  432 ASP A C   
3384  O O   . ASP A 432 ? 0.3614 0.5299 0.5161 0.1001  0.0444  0.0024  432 ASP A O   
3385  C CB  . ASP A 432 ? 0.3512 0.4922 0.4781 0.1004  0.0440  -0.0120 432 ASP A CB  
3386  C CG  . ASP A 432 ? 0.2749 0.4100 0.3841 0.1018  0.0455  -0.0152 432 ASP A CG  
3387  O OD1 . ASP A 432 ? 0.3509 0.4945 0.4533 0.1028  0.0489  -0.0114 432 ASP A OD1 
3388  O OD2 . ASP A 432 ? 0.3705 0.4925 0.4728 0.1015  0.0435  -0.0212 432 ASP A OD2 
3389  N N   . ALA A 433 ? 0.2314 0.3961 0.3826 0.0929  0.0398  0.0023  433 ALA A N   
3390  C CA  . ALA A 433 ? 0.2765 0.4478 0.4408 0.0921  0.0377  0.0068  433 ALA A CA  
3391  C C   . ALA A 433 ? 0.3300 0.5174 0.4970 0.0906  0.0397  0.0176  433 ALA A C   
3392  O O   . ALA A 433 ? 0.3838 0.5755 0.5605 0.0933  0.0399  0.0202  433 ALA A O   
3393  C CB  . ALA A 433 ? 0.2740 0.4441 0.4398 0.0879  0.0345  0.0076  433 ALA A CB  
3394  N N   . LEU A 434 ? 0.2552 0.4516 0.4144 0.0860  0.0408  0.0239  434 LEU A N   
3395  C CA  . LEU A 434 ? 0.2910 0.5028 0.4541 0.0831  0.0420  0.0346  434 LEU A CA  
3396  C C   . LEU A 434 ? 0.3959 0.6102 0.5598 0.0876  0.0459  0.0346  434 LEU A C   
3397  O O   . LEU A 434 ? 0.3923 0.6153 0.5658 0.0883  0.0467  0.0408  434 LEU A O   
3398  C CB  . LEU A 434 ? 0.2580 0.4786 0.4131 0.0760  0.0417  0.0402  434 LEU A CB  
3399  C CG  . LEU A 434 ? 0.3137 0.5505 0.4735 0.0714  0.0418  0.0513  434 LEU A CG  
3400  C CD1 . LEU A 434 ? 0.3231 0.5651 0.4948 0.0708  0.0390  0.0578  434 LEU A CD1 
3401  C CD2 . LEU A 434 ? 0.2876 0.5322 0.4391 0.0633  0.0407  0.0552  434 LEU A CD2 
3402  N N   . ILE A 435 ? 0.3531 0.5598 0.5070 0.0907  0.0486  0.0280  435 ILE A N   
3403  C CA  . ILE A 435 ? 0.3793 0.5873 0.5329 0.0955  0.0530  0.0275  435 ILE A CA  
3404  C C   . ILE A 435 ? 0.4886 0.6933 0.6538 0.1007  0.0529  0.0245  435 ILE A C   
3405  O O   . ILE A 435 ? 0.5105 0.7226 0.6822 0.1031  0.0558  0.0284  435 ILE A O   
3406  C CB  . ILE A 435 ? 0.3554 0.5535 0.4948 0.0985  0.0554  0.0202  435 ILE A CB  
3407  C CG1 . ILE A 435 ? 0.3331 0.5363 0.4616 0.0933  0.0561  0.0236  435 ILE A CG1 
3408  C CG2 . ILE A 435 ? 0.4415 0.6395 0.5803 0.1042  0.0601  0.0190  435 ILE A CG2 
3409  C CD1 . ILE A 435 ? 0.2771 0.4686 0.3903 0.0957  0.0573  0.0160  435 ILE A CD1 
3410  N N   . GLY A 436 ? 0.4422 0.6362 0.6112 0.1023  0.0495  0.0174  436 GLY A N   
3411  C CA  . GLY A 436 ? 0.4640 0.6541 0.6443 0.1069  0.0488  0.0129  436 GLY A CA  
3412  C C   . GLY A 436 ? 0.5203 0.7210 0.7136 0.1062  0.0477  0.0206  436 GLY A C   
3413  O O   . GLY A 436 ? 0.6131 0.8115 0.8162 0.1102  0.0470  0.0170  436 GLY A O   
3414  N N   . LEU A 437 ? 0.4841 0.6962 0.6779 0.1010  0.0472  0.0311  437 LEU A N   
3415  C CA  . LEU A 437 ? 0.5686 0.7913 0.7743 0.0997  0.0462  0.0401  437 LEU A CA  
3416  C C   . LEU A 437 ? 0.5725 0.8076 0.7814 0.0992  0.0497  0.0482  437 LEU A C   
3417  O O   . LEU A 437 ? 0.5852 0.8308 0.8028 0.0967  0.0485  0.0576  437 LEU A O   
3418  C CB  . LEU A 437 ? 0.4857 0.7125 0.6913 0.0935  0.0424  0.0467  437 LEU A CB  
3419  C CG  . LEU A 437 ? 0.4442 0.6605 0.6501 0.0937  0.0389  0.0406  437 LEU A CG  
3420  C CD1 . LEU A 437 ? 0.3337 0.5560 0.5395 0.0876  0.0360  0.0490  437 LEU A CD1 
3421  C CD2 . LEU A 437 ? 0.5012 0.7126 0.7176 0.0991  0.0380  0.0361  437 LEU A CD2 
3422  N N   . LYS A 438 ? 0.4852 0.9107 0.7376 0.2204  0.0729  0.0992  438 LYS A N   
3423  C CA  . LYS A 438 ? 0.5508 1.0038 0.7970 0.2175  0.0783  0.1064  438 LYS A CA  
3424  C C   . LYS A 438 ? 0.6418 1.1035 0.9011 0.2313  0.0762  0.1062  438 LYS A C   
3425  O O   . LYS A 438 ? 0.6569 1.1409 0.9187 0.2270  0.0784  0.1176  438 LYS A O   
3426  C CB  . LYS A 438 ? 0.5638 1.0226 0.7904 0.2175  0.0843  0.0980  438 LYS A CB  
3427  C CG  . LYS A 438 ? 0.5390 1.0025 0.7511 0.1990  0.0874  0.1045  438 LYS A CG  
3428  C CD  . LYS A 438 ? 0.5566 1.0202 0.7498 0.1995  0.0919  0.0947  438 LYS A CD  
3429  C CE  . LYS A 438 ? 0.6705 1.1550 0.8594 0.2073  0.0958  0.0948  438 LYS A CE  
3430  N NZ  . LYS A 438 ? 0.6720 1.1818 0.8633 0.1968  0.0970  0.1116  438 LYS A NZ  
3431  N N   . GLU A 439 ? 0.8825 1.3261 1.1504 0.2475  0.0712  0.0933  439 GLU A N   
3432  C CA  . GLU A 439 ? 0.8992 1.3491 1.1799 0.2617  0.0680  0.0912  439 GLU A CA  
3433  C C   . GLU A 439 ? 0.8988 1.3436 1.1994 0.2611  0.0607  0.1010  439 GLU A C   
3434  O O   . GLU A 439 ? 0.9111 1.3643 1.2232 0.2707  0.0580  0.1021  439 GLU A O   
3435  C CB  . GLU A 439 ? 0.9187 1.3500 1.1993 0.2796  0.0643  0.0721  439 GLU A CB  
3436  C CG  . GLU A 439 ? 0.9242 1.3225 1.2167 0.2846  0.0545  0.0643  439 GLU A CG  
3437  C CD  . GLU A 439 ? 0.9929 1.3747 1.2756 0.2739  0.0554  0.0625  439 GLU A CD  
3438  O OE1 . GLU A 439 ? 1.0057 1.3994 1.2708 0.2645  0.0635  0.0640  439 GLU A OE1 
3439  O OE2 . GLU A 439 ? 0.9751 1.3317 1.2680 0.2747  0.0475  0.0598  439 GLU A OE2 
3440  N N   . LYS A 440 ? 0.6535 1.0856 0.9585 0.2500  0.0573  0.1086  440 LYS A N   
3441  C CA  . LYS A 440 ? 0.5991 1.0244 0.9225 0.2487  0.0497  0.1187  440 LYS A CA  
3442  C C   . LYS A 440 ? 0.6063 1.0512 0.9299 0.2325  0.0526  0.1378  440 LYS A C   
3443  O O   . LYS A 440 ? 0.5686 1.0104 0.9063 0.2301  0.0468  0.1481  440 LYS A O   
3444  C CB  . LYS A 440 ? 0.5770 0.9732 0.9070 0.2479  0.0425  0.1152  440 LYS A CB  
3445  C CG  . LYS A 440 ? 0.5791 0.9519 0.9096 0.2633  0.0377  0.0958  440 LYS A CG  
3446  C CD  . LYS A 440 ? 0.5427 0.8861 0.8813 0.2618  0.0293  0.0939  440 LYS A CD  
3447  C CE  . LYS A 440 ? 0.5996 0.9176 0.9377 0.2760  0.0236  0.0737  440 LYS A CE  
3448  N NZ  . LYS A 440 ? 0.5240 0.8123 0.8703 0.2740  0.0146  0.0720  440 LYS A NZ  
3449  N N   . PHE A 441 ? 0.5178 0.9816 0.8259 0.2212  0.0605  0.1429  441 PHE A N   
3450  C CA  . PHE A 441 ? 0.4651 0.9457 0.7716 0.2051  0.0621  0.1601  441 PHE A CA  
3451  C C   . PHE A 441 ? 0.5652 1.0609 0.8837 0.2098  0.0603  0.1683  441 PHE A C   
3452  O O   . PHE A 441 ? 0.5004 0.9981 0.8273 0.2018  0.0566  0.1813  441 PHE A O   
3453  C CB  . PHE A 441 ? 0.3798 0.8756 0.6670 0.1933  0.0692  0.1621  441 PHE A CB  
3454  C CG  . PHE A 441 ? 0.4708 0.9528 0.7457 0.1853  0.0704  0.1565  441 PHE A CG  
3455  C CD1 . PHE A 441 ? 0.4440 0.9077 0.7249 0.1805  0.0659  0.1584  441 PHE A CD1 
3456  C CD2 . PHE A 441 ? 0.4448 0.9322 0.7025 0.1824  0.0759  0.1499  441 PHE A CD2 
3457  C CE1 . PHE A 441 ? 0.3886 0.8403 0.6585 0.1734  0.0670  0.1529  441 PHE A CE1 
3458  C CE2 . PHE A 441 ? 0.4124 0.8867 0.6588 0.1751  0.0767  0.1442  441 PHE A CE2 
3459  C CZ  . PHE A 441 ? 0.3910 0.8476 0.6435 0.1709  0.0724  0.1453  441 PHE A CZ  
3460  N N   . ALA A 442 ? 0.6213 1.1282 0.9405 0.2229  0.0627  0.1608  442 ALA A N   
3461  C CA  . ALA A 442 ? 0.5440 1.0655 0.8753 0.2289  0.0608  0.1673  442 ALA A CA  
3462  C C   . ALA A 442 ? 0.6054 1.1098 0.9558 0.2365  0.0515  0.1679  442 ALA A C   
3463  O O   . ALA A 442 ? 0.6081 1.1201 0.9688 0.2331  0.0483  0.1796  442 ALA A O   
3464  C CB  . ALA A 442 ? 0.5182 1.0535 0.8466 0.2432  0.0647  0.1573  442 ALA A CB  
3465  N N   . THR A 443 ? 0.7349 1.2150 1.0902 0.2465  0.0462  0.1556  443 THR A N   
3466  C CA  . THR A 443 ? 0.7843 1.2444 1.1579 0.2537  0.0356  0.1557  443 THR A CA  
3467  C C   . THR A 443 ? 0.8073 1.2550 1.1834 0.2387  0.0323  0.1677  443 THR A C   
3468  O O   . THR A 443 ? 0.8357 1.2595 1.2164 0.2404  0.0265  0.1631  443 THR A O   
3469  C CB  . THR A 443 ? 0.8319 1.2699 1.2097 0.2707  0.0298  0.1370  443 THR A CB  
3470  O OG1 . THR A 443 ? 0.8509 1.3022 1.2200 0.2815  0.0356  0.1253  443 THR A OG1 
3471  C CG2 . THR A 443 ? 0.8652 1.2870 1.2635 0.2819  0.0173  0.1357  443 THR A CG2 
3472  N N   . LEU A 444 ? 0.6434 1.1078 1.0157 0.2236  0.0359  0.1836  444 LEU A N   
3473  C CA  . LEU A 444 ? 0.6279 1.0845 1.0012 0.2084  0.0335  0.1965  444 LEU A CA  
3474  C C   . LEU A 444 ? 0.5705 1.0400 0.9515 0.2013  0.0313  0.2125  444 LEU A C   
3475  O O   . LEU A 444 ? 0.5635 1.0534 0.9423 0.2020  0.0350  0.2158  444 LEU A O   
3476  C CB  . LEU A 444 ? 0.5281 0.9898 0.8831 0.1936  0.0403  0.1983  444 LEU A CB  
3477  C CG  . LEU A 444 ? 0.4447 0.8889 0.7925 0.1963  0.0413  0.1854  444 LEU A CG  
3478  C CD1 . LEU A 444 ? 0.4260 0.8768 0.7561 0.1806  0.0472  0.1885  444 LEU A CD1 
3479  C CD2 . LEU A 444 ? 0.4135 0.8323 0.7747 0.1995  0.0329  0.1849  444 LEU A CD2 
3480  N N   . LYS A 445 ? 0.5667 1.0242 0.9565 0.1942  0.0252  0.2231  445 LYS A N   
3481  C CA  . LYS A 445 ? 0.5323 0.9984 0.9305 0.1883  0.0218  0.2382  445 LYS A CA  
3482  C C   . LYS A 445 ? 0.5050 0.9764 0.8937 0.1690  0.0239  0.2523  445 LYS A C   
3483  O O   . LYS A 445 ? 0.4535 0.9141 0.8358 0.1614  0.0243  0.2518  445 LYS A O   
3484  C CB  . LYS A 445 ? 0.5994 1.0472 1.0169 0.1967  0.0114  0.2400  445 LYS A CB  
3485  C CG  . LYS A 445 ? 0.6280 1.0729 1.0562 0.2164  0.0071  0.2276  445 LYS A CG  
3486  C CD  . LYS A 445 ? 0.4784 0.9490 0.9040 0.2195  0.0123  0.2291  445 LYS A CD  
3487  C CE  . LYS A 445 ? 0.4510 0.9332 0.8814 0.2092  0.0108  0.2467  445 LYS A CE  
3488  N NZ  . LYS A 445 ? 0.7057 1.2127 1.1338 0.2119  0.0157  0.2482  445 LYS A NZ  
3489  N N   . GLY A 446 ? 0.4904 0.9784 0.8781 0.1618  0.0247  0.2644  446 GLY A N   
3490  C CA  . GLY A 446 ? 0.4691 0.9624 0.8479 0.1447  0.0252  0.2780  446 GLY A CA  
3491  C C   . GLY A 446 ? 0.4808 0.9586 0.8689 0.1399  0.0189  0.2867  446 GLY A C   
3492  O O   . GLY A 446 ? 0.4972 0.9580 0.8991 0.1493  0.0135  0.2823  446 GLY A O   
3493  N N   . LEU A 447 ? 0.4342 0.9173 0.8144 0.1254  0.0190  0.2991  447 LEU A N   
3494  C CA  . LEU A 447 ? 0.4947 0.9658 0.8816 0.1190  0.0139  0.3089  447 LEU A CA  
3495  C C   . LEU A 447 ? 0.5072 0.9896 0.8943 0.1101  0.0120  0.3249  447 LEU A C   
3496  O O   . LEU A 447 ? 0.4619 0.9606 0.8385 0.1051  0.0152  0.3282  447 LEU A O   
3497  C CB  . LEU A 447 ? 0.4410 0.9050 0.8155 0.1100  0.0161  0.3063  447 LEU A CB  
3498  C CG  . LEU A 447 ? 0.4208 0.8700 0.7974 0.1188  0.0168  0.2911  447 LEU A CG  
3499  C CD1 . LEU A 447 ? 0.3623 0.8135 0.7201 0.1110  0.0222  0.2842  447 LEU A CD1 
3500  C CD2 . LEU A 447 ? 0.4329 0.8612 0.8254 0.1223  0.0100  0.2930  447 LEU A CD2 
3501  N N   . GLU A 448 ? 0.4806 0.9538 0.8799 0.1080  0.0062  0.3352  448 GLU A N   
3502  C CA  . GLU A 448 ? 0.4601 0.9426 0.8621 0.1011  0.0038  0.3506  448 GLU A CA  
3503  C C   . GLU A 448 ? 0.5225 0.9986 0.9244 0.0906  0.0011  0.3618  448 GLU A C   
3504  O O   . GLU A 448 ? 0.5492 1.0092 0.9599 0.0926  -0.0021 0.3599  448 GLU A O   
3505  C CB  . GLU A 448 ? 0.5614 1.0416 0.9822 0.1117  -0.0016 0.3528  448 GLU A CB  
3506  C CG  . GLU A 448 ? 0.5084 0.9980 0.9334 0.1054  -0.0045 0.3684  448 GLU A CG  
3507  C CD  . GLU A 448 ? 0.5381 1.0227 0.9826 0.1165  -0.0109 0.3697  448 GLU A CD  
3508  O OE1 . GLU A 448 ? 0.5114 0.9836 0.9661 0.1291  -0.0139 0.3583  448 GLU A OE1 
3509  O OE2 . GLU A 448 ? 0.4868 0.9796 0.9362 0.1131  -0.0135 0.3813  448 GLU A OE2 
3510  N N   . PHE A 449 ? 0.5072 0.9962 0.8993 0.0796  0.0023  0.3735  449 PHE A N   
3511  C CA  . PHE A 449 ? 0.4661 0.9533 0.8555 0.0691  0.0010  0.3843  449 PHE A CA  
3512  C C   . PHE A 449 ? 0.4949 0.9724 0.9048 0.0709  -0.0055 0.3946  449 PHE A C   
3513  O O   . PHE A 449 ? 0.5388 1.0174 0.9611 0.0766  -0.0090 0.3985  449 PHE A O   
3514  C CB  . PHE A 449 ? 0.4560 0.9605 0.8291 0.0581  0.0036  0.3931  449 PHE A CB  
3515  C CG  . PHE A 449 ? 0.4487 0.9597 0.7992 0.0532  0.0082  0.3845  449 PHE A CG  
3516  C CD1 . PHE A 449 ? 0.4633 0.9688 0.8028 0.0481  0.0097  0.3804  449 PHE A CD1 
3517  C CD2 . PHE A 449 ? 0.4376 0.9600 0.7780 0.0535  0.0103  0.3808  449 PHE A CD2 
3518  C CE1 . PHE A 449 ? 0.4254 0.9354 0.7436 0.0437  0.0127  0.3718  449 PHE A CE1 
3519  C CE2 . PHE A 449 ? 0.4758 1.0025 0.7954 0.0484  0.0132  0.3731  449 PHE A CE2 
3520  C CZ  . PHE A 449 ? 0.3746 0.8945 0.6827 0.0437  0.0141  0.3682  449 PHE A CZ  
3521  N N   . GLU A 450 ? 0.6059 1.0738 1.0196 0.0658  -0.0074 0.3992  450 GLU A N   
3522  C CA  . GLU A 450 ? 0.6742 1.1365 1.1041 0.0625  -0.0133 0.4130  450 GLU A CA  
3523  C C   . GLU A 450 ? 0.6409 1.1143 1.0619 0.0491  -0.0110 0.4253  450 GLU A C   
3524  O O   . GLU A 450 ? 0.6688 1.1430 1.1017 0.0444  -0.0149 0.4389  450 GLU A O   
3525  C CB  . GLU A 450 ? 0.6677 1.1072 1.1150 0.0691  -0.0193 0.4084  450 GLU A CB  
3526  C CG  . GLU A 450 ? 0.6728 1.1045 1.1154 0.0633  -0.0180 0.4065  450 GLU A CG  
3527  C CD  . GLU A 450 ? 0.7501 1.1575 1.2100 0.0706  -0.0247 0.4003  450 GLU A CD  
3528  O OE1 . GLU A 450 ? 0.8478 1.2444 1.3186 0.0825  -0.0292 0.3921  450 GLU A OE1 
3529  O OE2 . GLU A 450 ? 0.6743 1.0735 1.1367 0.0647  -0.0260 0.4032  450 GLU A OE2 
3530  N N   . TYR A 451 ? 0.5104 0.9929 0.9109 0.0431  -0.0052 0.4206  451 TYR A N   
3531  C CA  . TYR A 451 ? 0.5288 1.0261 0.9178 0.0314  -0.0023 0.4300  451 TYR A CA  
3532  C C   . TYR A 451 ? 0.4878 0.9955 0.8518 0.0283  0.0032  0.4208  451 TYR A C   
3533  O O   . TYR A 451 ? 0.5171 1.0166 0.8724 0.0307  0.0050  0.4089  451 TYR A O   
3534  C CB  . TYR A 451 ? 0.4964 0.9867 0.8919 0.0264  -0.0036 0.4345  451 TYR A CB  
3535  C CG  . TYR A 451 ? 0.4727 0.9792 0.8507 0.0166  0.0013  0.4362  451 TYR A CG  
3536  C CD1 . TYR A 451 ? 0.5517 1.0791 0.9287 0.0090  0.0025  0.4466  451 TYR A CD1 
3537  C CD2 . TYR A 451 ? 0.4627 0.9649 0.8260 0.0158  0.0044  0.4254  451 TYR A CD2 
3538  C CE1 . TYR A 451 ? 0.4991 1.0388 0.8591 0.0036  0.0039  0.4404  451 TYR A CE1 
3539  C CE2 . TYR A 451 ? 0.4962 1.0124 0.8430 0.0085  0.0073  0.4232  451 TYR A CE2 
3540  C CZ  . TYR A 451 ? 0.5001 1.0313 0.8434 0.0043  0.0050  0.4264  451 TYR A CZ  
3541  O OH  . TYR A 451 ? 0.4512 0.9903 0.7760 0.0013  0.0036  0.4158  451 TYR A OH  
3542  N N   . GLU A 452 ? 0.4686 0.9938 0.8216 0.0228  0.0052  0.4256  452 GLU A N   
3543  C CA  . GLU A 452 ? 0.5111 1.0452 0.8407 0.0194  0.0090  0.4168  452 GLU A CA  
3544  C C   . GLU A 452 ? 0.5133 1.0610 0.8306 0.0109  0.0091  0.4173  452 GLU A C   
3545  O O   . GLU A 452 ? 0.4645 1.0241 0.7868 0.0082  0.0074  0.4248  452 GLU A O   
3546  C CB  . GLU A 452 ? 0.5201 1.0597 0.8461 0.0232  0.0089  0.4139  452 GLU A CB  
3547  C CG  . GLU A 452 ? 0.4231 0.9695 0.7257 0.0195  0.0114  0.4047  452 GLU A CG  
3548  C CD  . GLU A 452 ? 0.4656 1.0185 0.7661 0.0224  0.0110  0.4030  452 GLU A CD  
3549  O OE1 . GLU A 452 ? 0.4806 1.0315 0.7977 0.0290  0.0094  0.4067  452 GLU A OE1 
3550  O OE2 . GLU A 452 ? 0.4499 1.0099 0.7327 0.0179  0.0119  0.3977  452 GLU A OE2 
3551  N N   . PRO A 453 ? 0.5099 1.0526 0.8102 0.0089  0.0085  0.4041  453 PRO A N   
3552  C CA  . PRO A 453 ? 0.5067 1.0596 0.7935 0.0039  0.0061  0.3969  453 PRO A CA  
3553  C C   . PRO A 453 ? 0.5358 1.0977 0.8089 0.0024  0.0052  0.3900  453 PRO A C   
3554  O O   . PRO A 453 ? 0.5129 1.0703 0.7803 0.0047  0.0066  0.3860  453 PRO A O   
3555  C CB  . PRO A 453 ? 0.4988 1.0430 0.7732 0.0034  0.0060  0.3840  453 PRO A CB  
3556  C CG  . PRO A 453 ? 0.5020 1.0310 0.7873 0.0071  0.0082  0.3887  453 PRO A CG  
3557  C CD  . PRO A 453 ? 0.4665 0.9951 0.7627 0.0115  0.0100  0.3967  453 PRO A CD  
3558  N N   . PRO A 454 ? 0.5757 1.1515 0.8440 -0.0011 0.0027  0.3893  454 PRO A N   
3559  C CA  . PRO A 454 ? 0.5065 1.0907 0.7627 -0.0032 0.0015  0.3829  454 PRO A CA  
3560  C C   . PRO A 454 ? 0.6166 1.1953 0.8544 -0.0045 0.0007  0.3662  454 PRO A C   
3561  O O   . PRO A 454 ? 0.6713 1.2499 0.9018 -0.0052 0.0005  0.3613  454 PRO A O   
3562  C CB  . PRO A 454 ? 0.4905 1.0909 0.7477 -0.0061 -0.0009 0.3880  454 PRO A CB  
3563  C CG  . PRO A 454 ? 0.4733 1.0746 0.7472 -0.0053 -0.0006 0.4008  454 PRO A CG  
3564  C CD  . PRO A 454 ? 0.5410 1.1267 0.8168 -0.0032 0.0009  0.3969  454 PRO A CD  
3565  N N   . VAL A 455 ? 0.6276 1.2023 0.8583 -0.0051 -0.0001 0.3579  455 VAL A N   
3566  C CA  . VAL A 455 ? 0.6145 1.1852 0.8279 -0.0069 -0.0015 0.3421  455 VAL A CA  
3567  C C   . VAL A 455 ? 0.6452 1.2008 0.8579 -0.0042 -0.0001 0.3362  455 VAL A C   
3568  O O   . VAL A 455 ? 0.7508 1.3024 0.9709 -0.0024 0.0002  0.3403  455 VAL A O   
3569  C CB  . VAL A 455 ? 0.6364 1.2171 0.8402 -0.0098 -0.0038 0.3369  455 VAL A CB  
3570  C CG1 . VAL A 455 ? 0.5617 1.1371 0.7483 -0.0119 -0.0050 0.3208  455 VAL A CG1 
3571  C CG2 . VAL A 455 ? 0.5830 1.1798 0.7876 -0.0120 -0.0049 0.3432  455 VAL A CG2 
3572  N N   . LEU A 456 ? 0.5860 1.1338 0.7903 -0.0040 0.0005  0.3273  456 LEU A N   
3573  C CA  . LEU A 456 ? 0.5070 1.0413 0.7091 -0.0012 0.0017  0.3207  456 LEU A CA  
3574  C C   . LEU A 456 ? 0.5241 1.0467 0.7361 0.0026  0.0062  0.3342  456 LEU A C   
3575  O O   . LEU A 456 ? 0.4897 1.0017 0.7006 0.0048  0.0052  0.3361  456 LEU A O   
3576  C CB  . LEU A 456 ? 0.4233 0.9549 0.6134 -0.0025 -0.0017 0.3094  456 LEU A CB  
3577  C CG  . LEU A 456 ? 0.4253 0.9607 0.5987 -0.0076 -0.0037 0.2965  456 LEU A CG  
3578  C CD1 . LEU A 456 ? 0.3004 0.8358 0.4632 -0.0097 -0.0051 0.2879  456 LEU A CD1 
3579  C CD2 . LEU A 456 ? 0.3358 0.8633 0.5027 -0.0076 -0.0039 0.2883  456 LEU A CD2 
3580  N N   . ARG A 457 ? 0.5318 1.0562 0.7536 0.0060  0.0071  0.3452  457 ARG A N   
3581  C CA  . ARG A 457 ? 0.4606 0.9818 0.7030 0.0109  0.0094  0.3588  457 ARG A CA  
3582  C C   . ARG A 457 ? 0.4385 0.9475 0.6840 0.0154  0.0114  0.3560  457 ARG A C   
3583  O O   . ARG A 457 ? 0.4247 0.9285 0.6864 0.0174  0.0129  0.3645  457 ARG A O   
3584  C CB  . ARG A 457 ? 0.4683 0.9966 0.7220 0.0140  0.0109  0.3684  457 ARG A CB  
3585  C CG  . ARG A 457 ? 0.4254 0.9533 0.6695 0.0164  0.0118  0.3609  457 ARG A CG  
3586  C CD  . ARG A 457 ? 0.4564 0.9938 0.7105 0.0193  0.0133  0.3704  457 ARG A CD  
3587  N NE  . ARG A 457 ? 0.4525 0.9906 0.6968 0.0210  0.0133  0.3612  457 ARG A NE  
3588  C CZ  . ARG A 457 ? 0.4056 0.9522 0.6535 0.0224  0.0131  0.3637  457 ARG A CZ  
3589  N NH1 . ARG A 457 ? 0.4245 0.9788 0.6850 0.0230  0.0127  0.3746  457 ARG A NH1 
3590  N NH2 . ARG A 457 ? 0.4797 1.0276 0.7186 0.0229  0.0129  0.3553  457 ARG A NH2 
3591  N N   . HIS A 458 ? 0.3344 0.8394 0.5663 0.0167  0.0116  0.3444  458 HIS A N   
3592  C CA  . HIS A 458 ? 0.3361 0.8304 0.5744 0.0220  0.0144  0.3375  458 HIS A CA  
3593  C C   . HIS A 458 ? 0.3304 0.8155 0.5709 0.0211  0.0143  0.3355  458 HIS A C   
3594  O O   . HIS A 458 ? 0.3117 0.7857 0.5664 0.0260  0.0166  0.3290  458 HIS A O   
3595  C CB  . HIS A 458 ? 0.3614 0.8546 0.5837 0.0219  0.0144  0.3232  458 HIS A CB  
3596  C CG  . HIS A 458 ? 0.4556 0.9505 0.6551 0.0156  0.0098  0.3154  458 HIS A CG  
3597  N ND1 . HIS A 458 ? 0.3872 0.8745 0.5761 0.0148  0.0093  0.3037  458 HIS A ND1 
3598  C CD2 . HIS A 458 ? 0.3991 0.8999 0.5881 0.0100  0.0055  0.3115  458 HIS A CD2 
3599  C CE1 . HIS A 458 ? 0.3987 0.8880 0.5724 0.0090  0.0046  0.2933  458 HIS A CE1 
3600  N NE2 . HIS A 458 ? 0.3669 0.8645 0.5409 0.0064  0.0021  0.2976  458 HIS A NE2 
3601  N N   . PHE A 459 ? 0.3490 0.8375 0.5781 0.0158  0.0108  0.3363  459 PHE A N   
3602  C CA  . PHE A 459 ? 0.2945 0.7760 0.5248 0.0149  0.0101  0.3344  459 PHE A CA  
3603  C C   . PHE A 459 ? 0.3320 0.8103 0.5864 0.0161  0.0118  0.3497  459 PHE A C   
3604  O O   . PHE A 459 ? 0.2715 0.7392 0.5365 0.0175  0.0130  0.3468  459 PHE A O   
3605  C CB  . PHE A 459 ? 0.2956 0.7837 0.5108 0.0101  0.0052  0.3262  459 PHE A CB  
3606  C CG  . PHE A 459 ? 0.2608 0.7497 0.4556 0.0079  0.0033  0.3098  459 PHE A CG  
3607  C CD1 . PHE A 459 ? 0.2577 0.7377 0.4447 0.0084  0.0046  0.3002  459 PHE A CD1 
3608  C CD2 . PHE A 459 ? 0.3544 0.8534 0.5400 0.0048  0.0002  0.3040  459 PHE A CD2 
3609  C CE1 . PHE A 459 ? 0.3117 0.7918 0.4806 0.0055  0.0026  0.2852  459 PHE A CE1 
3610  C CE2 . PHE A 459 ? 0.3664 0.8655 0.5358 0.0016  -0.0016 0.2893  459 PHE A CE2 
3611  C CZ  . PHE A 459 ? 0.3013 0.7905 0.4619 0.0018  -0.0007 0.2799  459 PHE A CZ  
3612  N N   . THR A 460 ? 0.3022 0.7880 0.5685 0.0150  0.0114  0.3614  460 THR A N   
3613  C CA  . THR A 460 ? 0.3535 0.8379 0.6438 0.0143  0.0114  0.3761  460 THR A CA  
3614  C C   . THR A 460 ? 0.3047 0.7893 0.6166 0.0186  0.0112  0.3850  460 THR A C   
3615  O O   . THR A 460 ? 0.2896 0.7720 0.6221 0.0182  0.0088  0.3962  460 THR A O   
3616  C CB  . THR A 460 ? 0.3595 0.8530 0.6460 0.0083  0.0085  0.3785  460 THR A CB  
3617  O OG1 . THR A 460 ? 0.3255 0.8338 0.6048 0.0062  0.0080  0.3768  460 THR A OG1 
3618  C CG2 . THR A 460 ? 0.3142 0.8064 0.5843 0.0087  0.0034  0.3664  460 THR A CG2 
3619  N N   . ALA A 461 ? 0.3591 0.8444 0.6668 0.0235  0.0118  0.3776  461 ALA A N   
3620  C CA  . ALA A 461 ? 0.3915 0.8758 0.7172 0.0294  0.0100  0.3824  461 ALA A CA  
3621  C C   . ALA A 461 ? 0.3640 0.8304 0.7116 0.0381  0.0072  0.3780  461 ALA A C   
3622  O O   . ALA A 461 ? 0.3528 0.8084 0.6993 0.0421  0.0081  0.3656  461 ALA A O   
3623  C CB  . ALA A 461 ? 0.3490 0.8400 0.6640 0.0324  0.0118  0.3751  461 ALA A CB  
3624  N N   . ARG A 462 ? 0.3763 0.8389 0.7440 0.0413  0.0032  0.3874  462 ARG A N   
3625  C CA  . ARG A 462 ? 0.4044 0.8483 0.7931 0.0507  -0.0013 0.3828  462 ARG A CA  
3626  C C   . ARG A 462 ? 0.4747 0.9188 0.8694 0.0607  -0.0020 0.3770  462 ARG A C   
3627  O O   . ARG A 462 ? 0.5157 0.9713 0.9111 0.0592  -0.0023 0.3854  462 ARG A O   
3628  C CB  . ARG A 462 ? 0.4386 0.8750 0.8464 0.0476  -0.0071 0.3968  462 ARG A CB  
3629  C CG  . ARG A 462 ? 0.4836 0.9183 0.8893 0.0391  -0.0068 0.4017  462 ARG A CG  
3630  C CD  . ARG A 462 ? 0.4368 0.8603 0.8652 0.0371  -0.0136 0.4136  462 ARG A CD  
3631  N NE  . ARG A 462 ? 0.3883 0.7879 0.8339 0.0475  -0.0198 0.4047  462 ARG A NE  
3632  C CZ  . ARG A 462 ? 0.3780 0.7609 0.8275 0.0502  -0.0216 0.3956  462 ARG A CZ  
3633  N NH1 . ARG A 462 ? 0.3317 0.7193 0.7697 0.0434  -0.0175 0.3945  462 ARG A NH1 
3634  N NH2 . ARG A 462 ? 0.4081 0.7688 0.8729 0.0605  -0.0280 0.3866  462 ARG A NH2 
3635  N N   . LEU A 463 ? 0.4886 0.9210 0.8876 0.0710  -0.0020 0.3622  463 LEU A N   
3636  C CA  . LEU A 463 ? 0.4856 0.9209 0.8872 0.0814  -0.0012 0.3538  463 LEU A CA  
3637  C C   . LEU A 463 ? 0.5369 0.9535 0.9587 0.0941  -0.0073 0.3474  463 LEU A C   
3638  O O   . LEU A 463 ? 0.4646 0.8638 0.8967 0.0949  -0.0120 0.3470  463 LEU A O   
3639  C CB  . LEU A 463 ? 0.4460 0.8881 0.8301 0.0829  0.0053  0.3397  463 LEU A CB  
3640  C CG  . LEU A 463 ? 0.3856 0.8453 0.7479 0.0720  0.0101  0.3433  463 LEU A CG  
3641  C CD1 . LEU A 463 ? 0.3590 0.8197 0.7046 0.0718  0.0150  0.3290  463 LEU A CD1 
3642  C CD2 . LEU A 463 ? 0.4885 0.9624 0.8505 0.0726  0.0103  0.3495  463 LEU A CD2 
3643  N N   . LYS A 464 ? 0.6635 1.0838 1.0902 0.1043  -0.0078 0.3418  464 LYS A N   
3644  C CA  . LYS A 464 ? 0.6777 1.0821 1.1212 0.1187  -0.0139 0.3332  464 LYS A CA  
3645  C C   . LYS A 464 ? 0.6784 1.0919 1.1166 0.1298  -0.0096 0.3198  464 LYS A C   
3646  O O   . LYS A 464 ? 0.6704 1.1034 1.0997 0.1265  -0.0048 0.3235  464 LYS A O   
3647  C CB  . LYS A 464 ? 0.6936 1.0929 1.1543 0.1201  -0.0221 0.3450  464 LYS A CB  
3648  C CG  . LYS A 464 ? 0.7576 1.1369 1.2318 0.1165  -0.0299 0.3518  464 LYS A CG  
3649  C CD  . LYS A 464 ? 0.7923 1.1654 1.2842 0.1185  -0.0389 0.3624  464 LYS A CD  
3650  C CE  . LYS A 464 ? 0.7356 1.0848 1.2428 0.1173  -0.0483 0.3659  464 LYS A CE  
3651  N NZ  . LYS A 464 ? 0.7268 1.0779 1.2291 0.1024  -0.0455 0.3765  464 LYS A NZ  
3652  N N   . PRO A 465 ? 0.5701 0.9703 1.0131 0.1430  -0.0113 0.3042  465 PRO A N   
3653  C CA  . PRO A 465 ? 0.5278 0.9384 0.9659 0.1543  -0.0069 0.2912  465 PRO A CA  
3654  C C   . PRO A 465 ? 0.5566 0.9781 1.0034 0.1603  -0.0095 0.2961  465 PRO A C   
3655  O O   . PRO A 465 ? 0.6341 1.0503 1.0932 0.1588  -0.0164 0.3071  465 PRO A O   
3656  C CB  . PRO A 465 ? 0.5277 0.9180 0.9722 0.1684  -0.0108 0.2746  465 PRO A CB  
3657  C CG  . PRO A 465 ? 0.3989 0.7706 0.8459 0.1609  -0.0144 0.2778  465 PRO A CG  
3658  C CD  . PRO A 465 ? 0.4930 0.8681 0.9455 0.1480  -0.0176 0.2974  465 PRO A CD  
3659  N N   . ILE A 466 ? 0.5765 1.0139 1.0167 0.1670  -0.0039 0.2882  466 ILE A N   
3660  C CA  . ILE A 466 ? 0.5598 1.0096 1.0077 0.1738  -0.0057 0.2912  466 ILE A CA  
3661  C C   . ILE A 466 ? 0.5099 0.9530 0.9669 0.1934  -0.0093 0.2754  466 ILE A C   
3662  O O   . ILE A 466 ? 0.4713 0.9083 0.9429 0.2028  -0.0173 0.2760  466 ILE A O   
3663  C CB  . ILE A 466 ? 0.4723 0.9477 0.9064 0.1658  0.0027  0.2961  466 ILE A CB  
3664  C CG1 . ILE A 466 ? 0.4480 0.9293 0.8740 0.1479  0.0039  0.3120  466 ILE A CG1 
3665  C CG2 . ILE A 466 ? 0.5268 1.0158 0.9691 0.1749  0.0015  0.2966  466 ILE A CG2 
3666  C CD1 . ILE A 466 ? 0.4638 0.9661 0.8731 0.1385  0.0111  0.3154  466 ILE A CD1 
3667  N N   . ALA B 2   ? 0.3285 0.4623 0.3106 -0.0036 0.0365  0.1326  2   ALA B N   
3668  C CA  . ALA B 2   ? 0.2886 0.4103 0.2722 -0.0045 0.0317  0.1283  2   ALA B CA  
3669  C C   . ALA B 2   ? 0.3196 0.4554 0.3188 -0.0073 0.0282  0.1309  2   ALA B C   
3670  O O   . ALA B 2   ? 0.3967 0.5493 0.4023 -0.0022 0.0313  0.1338  2   ALA B O   
3671  C CB  . ALA B 2   ? 0.2553 0.3663 0.2283 0.0042  0.0355  0.1238  2   ALA B CB  
3672  N N   . LYS B 3   ? 0.2829 0.4120 0.2877 -0.0152 0.0218  0.1301  3   LYS B N   
3673  C CA  . LYS B 3   ? 0.2917 0.4318 0.3091 -0.0199 0.0178  0.1323  3   LYS B CA  
3674  C C   . LYS B 3   ? 0.3150 0.4457 0.3330 -0.0176 0.0152  0.1278  3   LYS B C   
3675  O O   . LYS B 3   ? 0.2769 0.3897 0.2902 -0.0194 0.0121  0.1235  3   LYS B O   
3676  C CB  . LYS B 3   ? 0.3271 0.4646 0.3494 -0.0305 0.0130  0.1344  3   LYS B CB  
3677  C CG  . LYS B 3   ? 0.4336 0.5801 0.4665 -0.0369 0.0087  0.1362  3   LYS B CG  
3678  C CD  . LYS B 3   ? 0.4496 0.5878 0.4847 -0.0472 0.0042  0.1373  3   LYS B CD  
3679  C CE  . LYS B 3   ? 0.4765 0.5919 0.5066 -0.0474 0.0010  0.1325  3   LYS B CE  
3680  N NZ  . LYS B 3   ? 0.4496 0.5547 0.4814 -0.0558 -0.0029 0.1332  3   LYS B NZ  
3681  N N   . ARG B 4   ? 0.2528 0.3969 0.2768 -0.0133 0.0165  0.1291  4   ARG B N   
3682  C CA  A ARG B 4   ? 0.2628 0.4008 0.2887 -0.0120 0.0138  0.1257  4   ARG B CA  
3683  C CA  B ARG B 4   ? 0.2629 0.4009 0.2888 -0.0120 0.0138  0.1257  4   ARG B CA  
3684  C C   . ARG B 4   ? 0.2453 0.3843 0.2795 -0.0218 0.0076  0.1265  4   ARG B C   
3685  O O   . ARG B 4   ? 0.2618 0.4149 0.3030 -0.0281 0.0062  0.1310  4   ARG B O   
3686  C CB  A ARG B 4   ? 0.2566 0.4095 0.2857 -0.0033 0.0175  0.1274  4   ARG B CB  
3687  C CB  B ARG B 4   ? 0.2567 0.4096 0.2859 -0.0034 0.0175  0.1274  4   ARG B CB  
3688  C CG  A ARG B 4   ? 0.2477 0.3966 0.2670 0.0075  0.0244  0.1263  4   ARG B CG  
3689  C CG  B ARG B 4   ? 0.2481 0.3958 0.2672 0.0076  0.0242  0.1258  4   ARG B CG  
3690  C CD  A ARG B 4   ? 0.2279 0.3944 0.2516 0.0173  0.0289  0.1295  4   ARG B CD  
3691  C CD  B ARG B 4   ? 0.2404 0.3983 0.2619 0.0175  0.0277  0.1268  4   ARG B CD  
3692  N NE  A ARG B 4   ? 0.2609 0.4228 0.2853 0.0212  0.0276  0.1268  4   ARG B NE  
3693  N NE  B ARG B 4   ? 0.2506 0.4333 0.2794 0.0222  0.0314  0.1332  4   ARG B NE  
3694  C CZ  A ARG B 4   ? 0.2214 0.3701 0.2364 0.0304  0.0315  0.1230  4   ARG B CZ  
3695  C CZ  B ARG B 4   ? 0.2644 0.4509 0.2878 0.0335  0.0385  0.1346  4   ARG B CZ  
3696  N NH1 A ARG B 4   ? 0.2265 0.3641 0.2295 0.0366  0.0371  0.1213  4   ARG B NH1 
3697  N NH1 B ARG B 4   ? 0.2560 0.4219 0.2655 0.0405  0.0428  0.1299  4   ARG B NH1 
3698  N NH2 A ARG B 4   ? 0.2116 0.3572 0.2282 0.0329  0.0299  0.1209  4   ARG B NH2 
3699  N NH2 B ARG B 4   ? 0.1997 0.4109 0.2313 0.0378  0.0411  0.1411  4   ARG B NH2 
3700  N N   . ILE B 5   ? 0.2685 0.3915 0.3008 -0.0232 0.0041  0.1220  5   ILE B N   
3701  C CA  . ILE B 5   ? 0.2423 0.3617 0.2799 -0.0318 -0.0013 0.1218  5   ILE B CA  
3702  C C   . ILE B 5   ? 0.2385 0.3585 0.2786 -0.0298 -0.0028 0.1196  5   ILE B C   
3703  O O   . ILE B 5   ? 0.2296 0.3394 0.2646 -0.0231 -0.0016 0.1154  5   ILE B O   
3704  C CB  . ILE B 5   ? 0.2448 0.3440 0.2780 -0.0354 -0.0040 0.1187  5   ILE B CB  
3705  C CG1 . ILE B 5   ? 0.3070 0.4074 0.3383 -0.0384 -0.0027 0.1219  5   ILE B CG1 
3706  C CG2 . ILE B 5   ? 0.2352 0.3268 0.2722 -0.0424 -0.0086 0.1176  5   ILE B CG2 
3707  C CD1 . ILE B 5   ? 0.3145 0.3974 0.3420 -0.0416 -0.0052 0.1200  5   ILE B CD1 
3708  N N   . VAL B 6   ? 0.2171 0.3482 0.2640 -0.0363 -0.0058 0.1221  6   VAL B N   
3709  C CA  . VAL B 6   ? 0.2086 0.3447 0.2582 -0.0350 -0.0072 0.1212  6   VAL B CA  
3710  C C   . VAL B 6   ? 0.2455 0.3608 0.2916 -0.0364 -0.0102 0.1159  6   VAL B C   
3711  O O   . VAL B 6   ? 0.2634 0.3638 0.3077 -0.0415 -0.0125 0.1141  6   VAL B O   
3712  C CB  . VAL B 6   ? 0.2179 0.3729 0.2745 -0.0433 -0.0099 0.1251  6   VAL B CB  
3713  C CG1 . VAL B 6   ? 0.2149 0.3584 0.2715 -0.0553 -0.0141 0.1237  6   VAL B CG1 
3714  C CG2 . VAL B 6   ? 0.2196 0.3849 0.2789 -0.0410 -0.0108 0.1251  6   VAL B CG2 
3715  N N   . GLU B 7   ? 0.2345 0.3488 0.2794 -0.0309 -0.0099 0.1136  7   GLU B N   
3716  C CA  . GLU B 7   ? 0.2361 0.3335 0.2784 -0.0317 -0.0127 0.1089  7   GLU B CA  
3717  C C   . GLU B 7   ? 0.2266 0.3230 0.2724 -0.0422 -0.0168 0.1097  7   GLU B C   
3718  O O   . GLU B 7   ? 0.2769 0.3898 0.3270 -0.0475 -0.0178 0.1128  7   GLU B O   
3719  C CB  . GLU B 7   ? 0.2296 0.3287 0.2701 -0.0240 -0.0113 0.1066  7   GLU B CB  
3720  C CG  . GLU B 7   ? 0.2213 0.3127 0.2553 -0.0145 -0.0072 0.1031  7   GLU B CG  
3721  C CD  . GLU B 7   ? 0.2783 0.3834 0.3123 -0.0089 -0.0027 0.1065  7   GLU B CD  
3722  O OE1 . GLU B 7   ? 0.2461 0.3701 0.2866 -0.0120 -0.0026 0.1122  7   GLU B OE1 
3723  O OE2 . GLU B 7   ? 0.3056 0.4022 0.3324 -0.0016 0.0011  0.1036  7   GLU B OE2 
3724  N N   . PRO B 8   ? 0.2694 0.3466 0.3128 -0.0456 -0.0189 0.1063  8   PRO B N   
3725  C CA  . PRO B 8   ? 0.2425 0.3139 0.2871 -0.0551 -0.0220 0.1052  8   PRO B CA  
3726  C C   . PRO B 8   ? 0.2476 0.3142 0.2911 -0.0536 -0.0232 0.1024  8   PRO B C   
3727  O O   . PRO B 8   ? 0.2421 0.2926 0.2838 -0.0568 -0.0248 0.0989  8   PRO B O   
3728  C CB  . PRO B 8   ? 0.2522 0.3044 0.2941 -0.0570 -0.0225 0.1032  8   PRO B CB  
3729  C CG  . PRO B 8   ? 0.2389 0.2846 0.2779 -0.0472 -0.0207 0.1013  8   PRO B CG  
3730  C CD  . PRO B 8   ? 0.2538 0.3148 0.2931 -0.0412 -0.0182 0.1031  8   PRO B CD  
3731  N N   . PHE B 9   ? 0.2558 0.3359 0.2998 -0.0478 -0.0220 0.1039  9   PHE B N   
3732  C CA  . PHE B 9   ? 0.2383 0.3167 0.2807 -0.0435 -0.0230 0.0988  9   PHE B CA  
3733  C C   . PHE B 9   ? 0.2610 0.3595 0.3048 -0.0374 -0.0214 0.1014  9   PHE B C   
3734  O O   . PHE B 9   ? 0.2294 0.3408 0.2752 -0.0353 -0.0189 0.1066  9   PHE B O   
3735  C CB  . PHE B 9   ? 0.2554 0.3160 0.2933 -0.0364 -0.0223 0.0960  9   PHE B CB  
3736  C CG  . PHE B 9   ? 0.2424 0.3017 0.2781 -0.0282 -0.0192 0.0954  9   PHE B CG  
3737  C CD1 . PHE B 9   ? 0.1792 0.2467 0.2132 -0.0204 -0.0164 0.0948  9   PHE B CD1 
3738  C CD2 . PHE B 9   ? 0.2042 0.2530 0.2387 -0.0283 -0.0187 0.0939  9   PHE B CD2 
3739  C CE1 . PHE B 9   ? 0.1852 0.2483 0.2151 -0.0143 -0.0129 0.0925  9   PHE B CE1 
3740  C CE2 . PHE B 9   ? 0.2215 0.2688 0.2524 -0.0223 -0.0158 0.0921  9   PHE B CE2 
3741  C CZ  . PHE B 9   ? 0.1398 0.1932 0.1678 -0.0158 -0.0129 0.0912  9   PHE B CZ  
3742  N N   . ARG B 10  ? 0.1771 0.2785 0.2198 -0.0339 -0.0223 0.0980  10  ARG B N   
3743  C CA  . ARG B 10  ? 0.1899 0.3072 0.2330 -0.0255 -0.0201 0.1009  10  ARG B CA  
3744  C C   . ARG B 10  ? 0.1369 0.2418 0.1743 -0.0169 -0.0189 0.0977  10  ARG B C   
3745  O O   . ARG B 10  ? 0.1588 0.2467 0.1934 -0.0182 -0.0202 0.0933  10  ARG B O   
3746  C CB  . ARG B 10  ? 0.1932 0.3319 0.2408 -0.0301 -0.0225 0.1018  10  ARG B CB  
3747  C CG  . ARG B 10  ? 0.2306 0.3636 0.2763 -0.0352 -0.0261 0.0957  10  ARG B CG  
3748  C CD  . ARG B 10  ? 0.2191 0.3745 0.2689 -0.0425 -0.0292 0.0969  10  ARG B CD  
3749  N NE  . ARG B 10  ? 0.2461 0.3937 0.2922 -0.0495 -0.0327 0.0901  10  ARG B NE  
3750  C CZ  . ARG B 10  ? 0.3181 0.4744 0.3651 -0.0617 -0.0364 0.0883  10  ARG B CZ  
3751  N NH1 . ARG B 10  ? 0.3207 0.4964 0.3734 -0.0689 -0.0376 0.0932  10  ARG B NH1 
3752  N NH2 . ARG B 10  ? 0.2994 0.4449 0.3409 -0.0673 -0.0389 0.0812  10  ARG B NH2 
3753  N N   . ILE B 11  ? 0.1459 0.2583 0.1824 -0.0079 -0.0153 0.0977  11  ILE B N   
3754  C CA  . ILE B 11  ? 0.1326 0.2309 0.1634 -0.0003 -0.0124 0.0922  11  ILE B CA  
3755  C C   . ILE B 11  ? 0.1528 0.2540 0.1828 -0.0006 -0.0150 0.0905  11  ILE B C   
3756  O O   . ILE B 11  ? 0.1390 0.2579 0.1723 -0.0016 -0.0164 0.0932  11  ILE B O   
3757  C CB  . ILE B 11  ? 0.1833 0.2841 0.2116 0.0089  -0.0067 0.0922  11  ILE B CB  
3758  C CG1 . ILE B 11  ? 0.1613 0.2580 0.1887 0.0091  -0.0043 0.0933  11  ILE B CG1 
3759  C CG2 . ILE B 11  ? 0.1397 0.2261 0.1607 0.0151  -0.0044 0.0871  11  ILE B CG2 
3760  C CD1 . ILE B 11  ? 0.1964 0.3014 0.2226 0.0170  0.0011  0.0959  11  ILE B CD1 
3761  N N   . LYS B 12  ? 0.1944 0.2797 0.2203 0.0001  -0.0157 0.0861  12  LYS B N   
3762  C CA  . LYS B 12  ? 0.1637 0.2503 0.1876 0.0006  -0.0175 0.0842  12  LYS B CA  
3763  C C   . LYS B 12  ? 0.1872 0.2655 0.2059 0.0085  -0.0135 0.0805  12  LYS B C   
3764  O O   . LYS B 12  ? 0.2213 0.3058 0.2387 0.0108  -0.0136 0.0802  12  LYS B O   
3765  C CB  . LYS B 12  ? 0.1948 0.2703 0.2180 -0.0054 -0.0213 0.0816  12  LYS B CB  
3766  C CG  . LYS B 12  ? 0.2401 0.3214 0.2628 -0.0088 -0.0237 0.0779  12  LYS B CG  
3767  C CD  . LYS B 12  ? 0.2444 0.3103 0.2655 -0.0133 -0.0249 0.0718  12  LYS B CD  
3768  C CE  . LYS B 12  ? 0.3038 0.3747 0.3226 -0.0172 -0.0270 0.0674  12  LYS B CE  
3769  N NZ  . LYS B 12  ? 0.2829 0.3579 0.3031 -0.0275 -0.0297 0.0650  12  LYS B NZ  
3770  N N   . MET B 13  ? 0.1532 0.2173 0.1678 0.0117  -0.0104 0.0778  13  MET B N   
3771  C CA  . MET B 13  ? 0.1584 0.2131 0.1665 0.0174  -0.0072 0.0747  13  MET B CA  
3772  C C   . MET B 13  ? 0.1712 0.2182 0.1750 0.0208  -0.0037 0.0741  13  MET B C   
3773  O O   . MET B 13  ? 0.1631 0.2053 0.1672 0.0179  -0.0042 0.0739  13  MET B O   
3774  C CB  . MET B 13  ? 0.1552 0.1974 0.1601 0.0157  -0.0086 0.0709  13  MET B CB  
3775  C CG  . MET B 13  ? 0.1966 0.2317 0.1950 0.0201  -0.0062 0.0687  13  MET B CG  
3776  S SD  . MET B 13  ? 0.3372 0.3583 0.3319 0.0177  -0.0072 0.0649  13  MET B SD  
3777  C CE  . MET B 13  ? 0.2448 0.2740 0.2450 0.0146  -0.0106 0.0660  13  MET B CE  
3778  N N   . VAL B 14  ? 0.1678 0.2130 0.1668 0.0268  -0.0001 0.0741  14  VAL B N   
3779  C CA  . VAL B 14  ? 0.1875 0.2253 0.1808 0.0306  0.0036  0.0742  14  VAL B CA  
3780  C C   . VAL B 14  ? 0.2432 0.2640 0.2272 0.0316  0.0047  0.0707  14  VAL B C   
3781  O O   . VAL B 14  ? 0.2168 0.2345 0.1995 0.0313  0.0037  0.0691  14  VAL B O   
3782  C CB  . VAL B 14  ? 0.2150 0.2653 0.2101 0.0374  0.0076  0.0784  14  VAL B CB  
3783  C CG1 . VAL B 14  ? 0.1961 0.2637 0.1999 0.0351  0.0065  0.0826  14  VAL B CG1 
3784  C CG2 . VAL B 14  ? 0.1919 0.2488 0.1877 0.0413  0.0084  0.0794  14  VAL B CG2 
3785  N N   . GLU B 15  ? 0.2199 0.2305 0.1972 0.0325  0.0068  0.0700  15  GLU B N   
3786  C CA  . GLU B 15  ? 0.2196 0.2142 0.1869 0.0327  0.0081  0.0676  15  GLU B CA  
3787  C C   . GLU B 15  ? 0.2365 0.2273 0.1972 0.0389  0.0135  0.0696  15  GLU B C   
3788  O O   . GLU B 15  ? 0.2518 0.2443 0.2122 0.0392  0.0147  0.0708  15  GLU B O   
3789  C CB  . GLU B 15  ? 0.2689 0.2532 0.2330 0.0256  0.0046  0.0648  15  GLU B CB  
3790  C CG  . GLU B 15  ? 0.3790 0.3483 0.3329 0.0236  0.0052  0.0633  15  GLU B CG  
3791  C CD  . GLU B 15  ? 0.4535 0.4158 0.4047 0.0164  0.0016  0.0616  15  GLU B CD  
3792  O OE1 . GLU B 15  ? 0.3505 0.3173 0.3055 0.0146  0.0001  0.0617  15  GLU B OE1 
3793  O OE2 . GLU B 15  ? 0.5332 0.4863 0.4784 0.0125  0.0004  0.0607  15  GLU B OE2 
3794  N N   . LYS B 16  ? 0.2886 0.2741 0.2437 0.0446  0.0173  0.0700  16  LYS B N   
3795  C CA  . LYS B 16  ? 0.3223 0.3026 0.2699 0.0524  0.0238  0.0719  16  LYS B CA  
3796  C C   . LYS B 16  ? 0.3388 0.3033 0.2760 0.0491  0.0247  0.0699  16  LYS B C   
3797  O O   . LYS B 16  ? 0.3902 0.3449 0.3238 0.0416  0.0210  0.0673  16  LYS B O   
3798  C CB  . LYS B 16  ? 0.3598 0.3346 0.3020 0.0590  0.0280  0.0726  16  LYS B CB  
3799  C CG  . LYS B 16  ? 0.4637 0.4318 0.3970 0.0693  0.0362  0.0748  16  LYS B CG  
3800  C CD  . LYS B 16  ? 0.5547 0.5204 0.4843 0.0769  0.0405  0.0764  16  LYS B CD  
3801  C CE  . LYS B 16  ? 0.6539 0.6119 0.5735 0.0887  0.0498  0.0788  16  LYS B CE  
3802  N NZ  . LYS B 16  ? 0.6517 0.6069 0.5670 0.0969  0.0547  0.0811  16  LYS B NZ  
3803  N N   . ILE B 17  ? 0.3344 0.2977 0.2667 0.0548  0.0298  0.0717  17  ILE B N   
3804  C CA  . ILE B 17  ? 0.3642 0.3105 0.2833 0.0534  0.0323  0.0700  17  ILE B CA  
3805  C C   . ILE B 17  ? 0.3880 0.3264 0.2967 0.0651  0.0415  0.0716  17  ILE B C   
3806  O O   . ILE B 17  ? 0.4565 0.4072 0.3709 0.0741  0.0454  0.0751  17  ILE B O   
3807  C CB  . ILE B 17  ? 0.4225 0.3730 0.3437 0.0476  0.0294  0.0702  17  ILE B CB  
3808  C CG1 . ILE B 17  ? 0.3710 0.3377 0.2997 0.0538  0.0322  0.0741  17  ILE B CG1 
3809  C CG2 . ILE B 17  ? 0.4032 0.3583 0.3327 0.0369  0.0211  0.0686  17  ILE B CG2 
3810  C CD1 . ILE B 17  ? 0.3257 0.2969 0.2566 0.0479  0.0294  0.0747  17  ILE B CD1 
3811  N N   . ARG B 18  ? 0.4141 0.3315 0.3064 0.0651  0.0453  0.0692  18  ARG B N   
3812  C CA  . ARG B 18  ? 0.4607 0.3648 0.3392 0.0768  0.0551  0.0700  18  ARG B CA  
3813  C C   . ARG B 18  ? 0.4918 0.3786 0.3543 0.0757  0.0588  0.0679  18  ARG B C   
3814  O O   . ARG B 18  ? 0.4600 0.3392 0.3181 0.0647  0.0539  0.0650  18  ARG B O   
3815  C CB  . ARG B 18  ? 0.4801 0.3687 0.3494 0.0795  0.0582  0.0683  18  ARG B CB  
3816  C CG  . ARG B 18  ? 0.5972 0.4676 0.4568 0.0684  0.0544  0.0639  18  ARG B CG  
3817  C CD  . ARG B 18  ? 0.6628 0.5167 0.5119 0.0710  0.0581  0.0626  18  ARG B CD  
3818  N NE  . ARG B 18  ? 0.6098 0.4423 0.4393 0.0811  0.0686  0.0620  18  ARG B NE  
3819  C CZ  . ARG B 18  ? 0.6343 0.4404 0.4428 0.0777  0.0723  0.0580  18  ARG B CZ  
3820  N NH1 . ARG B 18  ? 0.6830 0.4829 0.4884 0.0642  0.0661  0.0546  18  ARG B NH1 
3821  N NH2 . ARG B 18  ? 0.6796 0.4649 0.4688 0.0881  0.0829  0.0574  18  ARG B NH2 
3822  N N   . VAL B 19  ? 0.5011 0.3826 0.3544 0.0876  0.0679  0.0698  19  VAL B N   
3823  C CA  . VAL B 19  ? 0.5296 0.3900 0.3631 0.0886  0.0736  0.0674  19  VAL B CA  
3824  C C   . VAL B 19  ? 0.5734 0.4037 0.3854 0.0917  0.0800  0.0637  19  VAL B C   
3825  O O   . VAL B 19  ? 0.5315 0.3574 0.3391 0.1043  0.0878  0.0657  19  VAL B O   
3826  C CB  . VAL B 19  ? 0.4561 0.3248 0.2893 0.1005  0.0809  0.0715  19  VAL B CB  
3827  C CG1 . VAL B 19  ? 0.4390 0.2833 0.2493 0.1014  0.0872  0.0685  19  VAL B CG1 
3828  C CG2 . VAL B 19  ? 0.4395 0.3379 0.2937 0.0961  0.0744  0.0752  19  VAL B CG2 
3829  N N   . PRO B 20  ? 0.5993 0.4096 0.3976 0.0805  0.0772  0.0587  20  PRO B N   
3830  C CA  . PRO B 20  ? 0.6776 0.4554 0.4512 0.0828  0.0845  0.0547  20  PRO B CA  
3831  C C   . PRO B 20  ? 0.7111 0.4704 0.4649 0.0949  0.0962  0.0545  20  PRO B C   
3832  O O   . PRO B 20  ? 0.6954 0.4611 0.4498 0.0957  0.0967  0.0557  20  PRO B O   
3833  C CB  . PRO B 20  ? 0.6011 0.3656 0.3654 0.0661  0.0780  0.0498  20  PRO B CB  
3834  C CG  . PRO B 20  ? 0.5591 0.3527 0.3480 0.0566  0.0667  0.0521  20  PRO B CG  
3835  C CD  . PRO B 20  ? 0.5414 0.3580 0.3455 0.0650  0.0675  0.0568  20  PRO B CD  
3836  N N   . SER B 21  ? 0.7379 0.4745 0.4739 0.1047  0.1059  0.0534  21  SER B N   
3837  C CA  . SER B 21  ? 0.7991 0.5140 0.5133 0.1175  0.1186  0.0530  21  SER B CA  
3838  C C   . SER B 21  ? 0.7882 0.4777 0.4804 0.1074  0.1187  0.0473  21  SER B C   
3839  O O   . SER B 21  ? 0.8020 0.4837 0.4897 0.0910  0.1111  0.0428  21  SER B O   
3840  C CB  . SER B 21  ? 0.8098 0.5027 0.5053 0.1282  0.1296  0.0524  21  SER B CB  
3841  O OG  . SER B 21  ? 0.8305 0.4940 0.5049 0.1164  0.1288  0.0460  21  SER B OG  
3842  N N   . ARG B 22  ? 0.7711 0.4497 0.4505 0.1171  0.1272  0.0481  22  ARG B N   
3843  C CA  . ARG B 22  ? 0.7962 0.4512 0.4538 0.1075  0.1277  0.0431  22  ARG B CA  
3844  C C   . ARG B 22  ? 0.8149 0.4337 0.4460 0.0957  0.1283  0.0354  22  ARG B C   
3845  O O   . ARG B 22  ? 0.8240 0.4369 0.4480 0.0784  0.1211  0.0309  22  ARG B O   
3846  C CB  . ARG B 22  ? 0.8070 0.4478 0.4504 0.1224  0.1390  0.0456  22  ARG B CB  
3847  C CG  . ARG B 22  ? 0.8777 0.4902 0.4944 0.1129  0.1411  0.0402  22  ARG B CG  
3848  C CD  . ARG B 22  ? 0.8355 0.4699 0.4627 0.0944  0.1295  0.0372  22  ARG B CD  
3849  N NE  . ARG B 22  ? 0.8663 0.4798 0.4700 0.0853  0.1314  0.0317  22  ARG B NE  
3850  C CZ  . ARG B 22  ? 0.8105 0.4395 0.4177 0.0862  0.1319  0.0326  22  ARG B CZ  
3851  N NH1 . ARG B 22  ? 0.8313 0.4951 0.4635 0.0955  0.1309  0.0391  22  ARG B NH1 
3852  N NH2 . ARG B 22  ? 0.8518 0.4619 0.4369 0.0765  0.1331  0.0267  22  ARG B NH2 
3853  N N   . GLU B 23  ? 0.8184 0.4166 0.4349 0.1041  0.1368  0.0337  23  GLU B N   
3854  C CA  . GLU B 23  ? 0.8635 0.4323 0.4556 0.0911  0.1370  0.0274  23  GLU B CA  
3855  C C   . GLU B 23  ? 0.8397 0.4226 0.4461 0.0745  0.1244  0.0255  23  GLU B C   
3856  O O   . GLU B 23  ? 0.8308 0.3963 0.4217 0.0577  0.1198  0.0198  23  GLU B O   
3857  C CB  . GLU B 23  ? 0.8655 0.4234 0.4462 0.1010  0.1462  0.0307  23  GLU B CB  
3858  C CG  . GLU B 23  ? 0.9166 0.4608 0.4813 0.1128  0.1570  0.0351  23  GLU B CG  
3859  C CD  . GLU B 23  ? 0.8618 0.4350 0.4493 0.1305  0.1597  0.0428  23  GLU B CD  
3860  O OE1 . GLU B 23  ? 0.9509 0.5549 0.5663 0.1346  0.1542  0.0455  23  GLU B OE1 
3861  O OE2 . GLU B 23  ? 0.8446 0.4072 0.4206 0.1389  0.1662  0.0509  23  GLU B OE2 
3862  N N   . GLU B 24  ? 0.8489 0.4666 0.4874 0.0777  0.1174  0.0313  24  GLU B N   
3863  C CA  . GLU B 24  ? 0.7770 0.4132 0.4343 0.0624  0.1044  0.0312  24  GLU B CA  
3864  C C   . GLU B 24  ? 0.7708 0.4154 0.4320 0.0473  0.0952  0.0295  24  GLU B C   
3865  O O   . GLU B 24  ? 0.7702 0.4116 0.4287 0.0314  0.0879  0.0264  24  GLU B O   
3866  C CB  . GLU B 24  ? 0.7329 0.4054 0.4235 0.0691  0.0990  0.0378  24  GLU B CB  
3867  C CG  . GLU B 24  ? 0.7570 0.4270 0.4478 0.0806  0.1053  0.0402  24  GLU B CG  
3868  C CD  . GLU B 24  ? 0.7653 0.4702 0.4879 0.0826  0.0978  0.0457  24  GLU B CD  
3869  O OE1 . GLU B 24  ? 0.7979 0.5173 0.5354 0.0699  0.0872  0.0453  24  GLU B OE1 
3870  O OE2 . GLU B 24  ? 0.8154 0.5337 0.5473 0.0965  0.1027  0.0504  24  GLU B OE2 
3871  N N   . ARG B 25  ? 0.7433 0.4015 0.4116 0.0518  0.0955  0.0321  25  ARG B N   
3872  C CA  . ARG B 25  ? 0.7455 0.4145 0.4174 0.0379  0.0872  0.0310  25  ARG B CA  
3873  C C   . ARG B 25  ? 0.8112 0.4462 0.4507 0.0271  0.0902  0.0242  25  ARG B C   
3874  O O   . ARG B 25  ? 0.7945 0.4330 0.4329 0.0105  0.0818  0.0218  25  ARG B O   
3875  C CB  . ARG B 25  ? 0.7508 0.4442 0.4382 0.0456  0.0873  0.0358  25  ARG B CB  
3876  C CG  . ARG B 25  ? 0.7027 0.4255 0.4178 0.0572  0.0862  0.0422  25  ARG B CG  
3877  C CD  . ARG B 25  ? 0.6639 0.4143 0.3962 0.0606  0.0840  0.0468  25  ARG B CD  
3878  N NE  . ARG B 25  ? 0.6681 0.4074 0.3857 0.0713  0.0939  0.0470  25  ARG B NE  
3879  C CZ  . ARG B 25  ? 0.6761 0.4241 0.4004 0.0877  0.1012  0.0516  25  ARG B CZ  
3880  N NH1 . ARG B 25  ? 0.5961 0.3635 0.3403 0.0948  0.0997  0.0560  25  ARG B NH1 
3881  N NH2 . ARG B 25  ? 0.7385 0.4771 0.4496 0.0970  0.1100  0.0521  25  ARG B NH2 
3882  N N   . GLU B 26  ? 0.8407 0.4424 0.4530 0.0362  0.1023  0.0210  26  GLU B N   
3883  C CA  . GLU B 26  ? 0.8430 0.4076 0.4213 0.0251  0.1058  0.0139  26  GLU B CA  
3884  C C   . GLU B 26  ? 0.8690 0.4183 0.4356 0.0098  0.1012  0.0089  26  GLU B C   
3885  O O   . GLU B 26  ? 0.8805 0.4186 0.4327 -0.0080 0.0961  0.0043  26  GLU B O   
3886  C CB  . GLU B 26  ? 0.8675 0.3964 0.4192 0.0397  0.1207  0.0124  26  GLU B CB  
3887  C CG  . GLU B 26  ? 0.8750 0.4140 0.4305 0.0498  0.1250  0.0162  26  GLU B CG  
3888  C CD  . GLU B 26  ? 0.9376 0.4711 0.4792 0.0346  0.1213  0.0119  26  GLU B CD  
3889  O OE1 . GLU B 26  ? 1.0156 0.5370 0.5452 0.0158  0.1149  0.0068  26  GLU B OE1 
3890  O OE2 . GLU B 26  ? 1.0373 0.5809 0.5806 0.0411  0.1245  0.0134  26  GLU B OE2 
3891  N N   . ALA B 27  ? 0.8122 0.3644 0.3861 0.0157  0.1026  0.0102  27  ALA B N   
3892  C CA  . ALA B 27  ? 0.8611 0.4041 0.4267 0.0014  0.0979  0.0067  27  ALA B CA  
3893  C C   . ALA B 27  ? 0.8701 0.4446 0.4616 -0.0132 0.0834  0.0092  27  ALA B C   
3894  O O   . ALA B 27  ? 0.8805 0.4474 0.4606 -0.0310 0.0775  0.0052  27  ALA B O   
3895  C CB  . ALA B 27  ? 0.8013 0.3433 0.3709 0.0122  0.1031  0.0092  27  ALA B CB  
3896  N N   . ALA B 28  ? 0.7866 0.3975 0.4124 -0.0058 0.0777  0.0159  28  ALA B N   
3897  C CA  . ALA B 28  ? 0.8045 0.4461 0.4554 -0.0172 0.0651  0.0188  28  ALA B CA  
3898  C C   . ALA B 28  ? 0.7563 0.4014 0.4016 -0.0311 0.0590  0.0171  28  ALA B C   
3899  O O   . ALA B 28  ? 0.7661 0.4192 0.4147 -0.0461 0.0505  0.0163  28  ALA B O   
3900  C CB  . ALA B 28  ? 0.7323 0.4092 0.4173 -0.0060 0.0616  0.0258  28  ALA B CB  
3901  N N   . LEU B 29  ? 0.7176 0.3592 0.3553 -0.0262 0.0631  0.0169  29  LEU B N   
3902  C CA  . LEU B 29  ? 0.7914 0.4396 0.4251 -0.0392 0.0569  0.0158  29  LEU B CA  
3903  C C   . LEU B 29  ? 0.8560 0.4743 0.4590 -0.0559 0.0568  0.0088  29  LEU B C   
3904  O O   . LEU B 29  ? 0.8016 0.4306 0.4058 -0.0716 0.0481  0.0083  29  LEU B O   
3905  C CB  . LEU B 29  ? 0.7948 0.4467 0.4268 -0.0300 0.0618  0.0171  29  LEU B CB  
3906  C CG  . LEU B 29  ? 0.7524 0.4189 0.3856 -0.0413 0.0550  0.0172  29  LEU B CG  
3907  C CD1 . LEU B 29  ? 0.7262 0.4269 0.3876 -0.0489 0.0430  0.0220  29  LEU B CD1 
3908  C CD2 . LEU B 29  ? 0.7185 0.3938 0.3543 -0.0303 0.0600  0.0194  29  LEU B CD2 
3909  N N   . LYS B 30  ? 0.9065 0.4873 0.4814 -0.0531 0.0665  0.0035  30  LYS B N   
3910  C CA  . LYS B 30  ? 0.9004 0.4501 0.4440 -0.0704 0.0666  -0.0037 30  LYS B CA  
3911  C C   . LYS B 30  ? 0.8674 0.4294 0.4199 -0.0829 0.0580  -0.0035 30  LYS B C   
3912  O O   . LYS B 30  ? 0.8842 0.4457 0.4275 -0.1021 0.0507  -0.0062 30  LYS B O   
3913  C CB  . LYS B 30  ? 0.9741 0.4788 0.4835 -0.0626 0.0804  -0.0095 30  LYS B CB  
3914  C CG  . LYS B 30  ? 1.1064 0.5940 0.6040 -0.0524 0.0893  -0.0090 30  LYS B CG  
3915  C CD  . LYS B 30  ? 1.3004 0.7591 0.7772 -0.0425 0.1019  -0.0087 30  LYS B CD  
3916  C CE  . LYS B 30  ? 1.3142 0.7546 0.7763 -0.0337 0.1111  -0.0066 30  LYS B CE  
3917  N NZ  . LYS B 30  ? 1.1914 0.6025 0.6296 -0.0248 0.1239  -0.0041 30  LYS B NZ  
3918  N N   . GLU B 31  ? 0.7872 0.3625 0.3592 -0.0726 0.0584  0.0004  31  GLU B N   
3919  C CA  . GLU B 31  ? 0.8213 0.4133 0.4071 -0.0831 0.0500  0.0021  31  GLU B CA  
3920  C C   . GLU B 31  ? 0.8439 0.4702 0.4539 -0.0931 0.0379  0.0063  31  GLU B C   
3921  O O   . GLU B 31  ? 0.8632 0.4963 0.4723 -0.1090 0.0303  0.0056  31  GLU B O   
3922  C CB  . GLU B 31  ? 0.8479 0.4519 0.4548 -0.0691 0.0522  0.0065  31  GLU B CB  
3923  C CG  . GLU B 31  ? 0.8896 0.5212 0.5212 -0.0769 0.0424  0.0105  31  GLU B CG  
3924  C CD  . GLU B 31  ? 0.9964 0.6318 0.6405 -0.0672 0.0452  0.0133  31  GLU B CD  
3925  O OE1 . GLU B 31  ? 1.0679 0.6829 0.6991 -0.0557 0.0546  0.0120  31  GLU B OE1 
3926  O OE2 . GLU B 31  ? 1.0052 0.6644 0.6717 -0.0709 0.0382  0.0171  31  GLU B OE2 
3927  N N   . ALA B 32  ? 0.8212 0.4708 0.4527 -0.0836 0.0361  0.0111  32  ALA B N   
3928  C CA  . ALA B 32  ? 0.7167 0.3989 0.3703 -0.0910 0.0258  0.0155  32  ALA B CA  
3929  C C   . ALA B 32  ? 0.8010 0.4766 0.4366 -0.1061 0.0222  0.0124  32  ALA B C   
3930  O O   . ALA B 32  ? 0.7887 0.4915 0.4413 -0.1119 0.0138  0.0164  32  ALA B O   
3931  C CB  . ALA B 32  ? 0.6568 0.3652 0.3372 -0.0759 0.0258  0.0215  32  ALA B CB  
3932  N N   . GLY B 33  ? 0.8519 0.4922 0.4536 -0.1125 0.0283  0.0056  33  GLY B N   
3933  C CA  . GLY B 33  ? 0.9031 0.5364 0.4872 -0.1281 0.0249  0.0025  33  GLY B CA  
3934  C C   . GLY B 33  ? 0.8223 0.4747 0.4182 -0.1212 0.0241  0.0060  33  GLY B C   
3935  O O   . GLY B 33  ? 0.8305 0.5020 0.4324 -0.1324 0.0161  0.0079  33  GLY B O   
3936  N N   . TYR B 34  ? 0.7590 0.4095 0.3597 -0.1027 0.0320  0.0075  34  TYR B N   
3937  C CA  . TYR B 34  ? 0.8395 0.5074 0.4499 -0.0949 0.0324  0.0105  34  TYR B CA  
3938  C C   . TYR B 34  ? 0.7674 0.4759 0.4082 -0.0977 0.0216  0.0172  34  TYR B C   
3939  O O   . TYR B 34  ? 0.7421 0.4657 0.3871 -0.0994 0.0186  0.0191  34  TYR B O   
3940  C CB  . TYR B 34  ? 0.8488 0.4952 0.4313 -0.1027 0.0361  0.0051  34  TYR B CB  
3941  C CG  . TYR B 34  ? 0.8983 0.5040 0.4521 -0.0956 0.0489  -0.0005 34  TYR B CG  
3942  C CD1 . TYR B 34  ? 0.9733 0.5456 0.5034 -0.1050 0.0520  -0.0055 34  TYR B CD1 
3943  C CD2 . TYR B 34  ? 0.9029 0.5034 0.4538 -0.0790 0.0582  -0.0001 34  TYR B CD2 
3944  C CE1 . TYR B 34  ? 1.0548 0.5873 0.5585 -0.0975 0.0645  -0.0096 34  TYR B CE1 
3945  C CE2 . TYR B 34  ? 1.0489 0.6122 0.5747 -0.0706 0.0705  -0.0042 34  TYR B CE2 
3946  C CZ  . TYR B 34  ? 1.1466 0.6748 0.6486 -0.0796 0.0738  -0.0087 34  TYR B CZ  
3947  O OH  . TYR B 34  ? 1.0910 0.5804 0.5679 -0.0706 0.0867  -0.0111 34  TYR B OH  
3948  N N   . ASN B 35  ? 0.6978 0.4237 0.3599 -0.0975 0.0163  0.0209  35  ASN B N   
3949  C CA  . ASN B 35  ? 0.6398 0.4021 0.3321 -0.0970 0.0076  0.0277  35  ASN B CA  
3950  C C   . ASN B 35  ? 0.6101 0.3864 0.3266 -0.0826 0.0093  0.0320  35  ASN B C   
3951  O O   . ASN B 35  ? 0.5830 0.3570 0.3041 -0.0835 0.0085  0.0317  35  ASN B O   
3952  C CB  . ASN B 35  ? 0.6043 0.3775 0.2997 -0.1134 -0.0019 0.0285  35  ASN B CB  
3953  C CG  . ASN B 35  ? 0.6217 0.4305 0.3473 -0.1118 -0.0100 0.0357  35  ASN B CG  
3954  O OD1 . ASN B 35  ? 0.6346 0.4586 0.3770 -0.0999 -0.0089 0.0397  35  ASN B OD1 
3955  N ND2 . ASN B 35  ? 0.6422 0.4641 0.3741 -0.1239 -0.0180 0.0376  35  ASN B ND2 
3956  N N   . PRO B 36  ? 0.5727 0.3640 0.3047 -0.0701 0.0114  0.0360  36  PRO B N   
3957  C CA  . PRO B 36  ? 0.5311 0.3352 0.2850 -0.0574 0.0131  0.0398  36  PRO B CA  
3958  C C   . PRO B 36  ? 0.4724 0.2976 0.2490 -0.0604 0.0059  0.0434  36  PRO B C   
3959  O O   . PRO B 36  ? 0.4603 0.2914 0.2509 -0.0522 0.0074  0.0452  36  PRO B O   
3960  C CB  . PRO B 36  ? 0.4748 0.2937 0.2400 -0.0473 0.0152  0.0436  36  PRO B CB  
3961  C CG  . PRO B 36  ? 0.5534 0.3724 0.3073 -0.0552 0.0130  0.0428  36  PRO B CG  
3962  C CD  . PRO B 36  ? 0.5803 0.3745 0.3074 -0.0669 0.0137  0.0366  36  PRO B CD  
3963  N N   . PHE B 37  ? 0.5055 0.3426 0.2861 -0.0714 -0.0017 0.0447  37  PHE B N   
3964  C CA  . PHE B 37  ? 0.4858 0.3414 0.2862 -0.0740 -0.0079 0.0480  37  PHE B CA  
3965  C C   . PHE B 37  ? 0.4701 0.3135 0.2644 -0.0774 -0.0067 0.0453  37  PHE B C   
3966  O O   . PHE B 37  ? 0.4601 0.3173 0.2716 -0.0756 -0.0095 0.0480  37  PHE B O   
3967  C CB  . PHE B 37  ? 0.4625 0.3326 0.2661 -0.0856 -0.0160 0.0502  37  PHE B CB  
3968  C CG  . PHE B 37  ? 0.4459 0.3408 0.2726 -0.0798 -0.0198 0.0558  37  PHE B CG  
3969  C CD1 . PHE B 37  ? 0.4324 0.3429 0.2808 -0.0743 -0.0218 0.0591  37  PHE B CD1 
3970  C CD2 . PHE B 37  ? 0.5176 0.4189 0.3432 -0.0803 -0.0211 0.0575  37  PHE B CD2 
3971  C CE1 . PHE B 37  ? 0.4176 0.3471 0.2849 -0.0692 -0.0247 0.0634  37  PHE B CE1 
3972  C CE2 . PHE B 37  ? 0.4616 0.3832 0.3072 -0.0751 -0.0242 0.0624  37  PHE B CE2 
3973  C CZ  . PHE B 37  ? 0.4316 0.3662 0.2976 -0.0696 -0.0258 0.0651  37  PHE B CZ  
3974  N N   . LEU B 38  ? 0.5473 0.3641 0.3165 -0.0820 -0.0022 0.0400  38  LEU B N   
3975  C CA  . LEU B 38  ? 0.5481 0.3498 0.3083 -0.0854 -0.0002 0.0371  38  LEU B CA  
3976  C C   . LEU B 38  ? 0.4987 0.2874 0.2575 -0.0718 0.0080  0.0360  38  LEU B C   
3977  O O   . LEU B 38  ? 0.5575 0.3334 0.3095 -0.0727 0.0104  0.0339  38  LEU B O   
3978  C CB  . LEU B 38  ? 0.5678 0.3458 0.2988 -0.1003 -0.0003 0.0315  38  LEU B CB  
3979  C CG  . LEU B 38  ? 0.6111 0.4037 0.3428 -0.1154 -0.0092 0.0329  38  LEU B CG  
3980  C CD1 . LEU B 38  ? 0.6616 0.4301 0.3630 -0.1320 -0.0094 0.0270  38  LEU B CD1 
3981  C CD2 . LEU B 38  ? 0.5622 0.3827 0.3190 -0.1176 -0.0164 0.0382  38  LEU B CD2 
3982  N N   . LEU B 39  ? 0.4754 0.2684 0.2407 -0.0594 0.0121  0.0378  39  LEU B N   
3983  C CA  . LEU B 39  ? 0.4670 0.2527 0.2342 -0.0461 0.0191  0.0380  39  LEU B CA  
3984  C C   . LEU B 39  ? 0.4574 0.2648 0.2503 -0.0406 0.0161  0.0422  39  LEU B C   
3985  O O   . LEU B 39  ? 0.4221 0.2529 0.2347 -0.0416 0.0104  0.0460  39  LEU B O   
3986  C CB  . LEU B 39  ? 0.4545 0.2415 0.2218 -0.0352 0.0241  0.0392  39  LEU B CB  
3987  C CG  . LEU B 39  ? 0.5553 0.3192 0.2965 -0.0361 0.0298  0.0352  39  LEU B CG  
3988  C CD1 . LEU B 39  ? 0.5606 0.3367 0.3100 -0.0262 0.0325  0.0383  39  LEU B CD1 
3989  C CD2 . LEU B 39  ? 0.5759 0.3087 0.2943 -0.0317 0.0386  0.0307  39  LEU B CD2 
3990  N N   . PRO B 40  ? 0.4359 0.2355 0.2283 -0.0347 0.0201  0.0417  40  PRO B N   
3991  C CA  . PRO B 40  ? 0.4433 0.2634 0.2593 -0.0285 0.0179  0.0457  40  PRO B CA  
3992  C C   . PRO B 40  ? 0.3781 0.2130 0.2084 -0.0174 0.0193  0.0490  40  PRO B C   
3993  O O   . PRO B 40  ? 0.3933 0.2195 0.2140 -0.0118 0.0240  0.0481  40  PRO B O   
3994  C CB  . PRO B 40  ? 0.4156 0.2202 0.2229 -0.0257 0.0224  0.0440  40  PRO B CB  
3995  C CG  . PRO B 40  ? 0.4502 0.2272 0.2322 -0.0235 0.0294  0.0398  40  PRO B CG  
3996  C CD  . PRO B 40  ? 0.4482 0.2190 0.2176 -0.0331 0.0271  0.0374  40  PRO B CD  
3997  N N   . SER B 41  ? 0.3488 0.2061 0.2015 -0.0147 0.0155  0.0528  41  SER B N   
3998  C CA  . SER B 41  ? 0.3800 0.2526 0.2467 -0.0062 0.0158  0.0559  41  SER B CA  
3999  C C   . SER B 41  ? 0.4116 0.2746 0.2715 0.0035  0.0219  0.0551  41  SER B C   
4000  O O   . SER B 41  ? 0.4143 0.2840 0.2783 0.0102  0.0238  0.0566  41  SER B O   
4001  C CB  . SER B 41  ? 0.3212 0.2152 0.2098 -0.0059 0.0111  0.0592  41  SER B CB  
4002  O OG  . SER B 41  ? 0.3476 0.2405 0.2389 -0.0026 0.0122  0.0592  41  SER B OG  
4003  N N   . SER B 42  ? 0.3987 0.2466 0.2484 0.0047  0.0254  0.0531  42  SER B N   
4004  C CA  . SER B 42  ? 0.4266 0.2651 0.2693 0.0154  0.0322  0.0528  42  SER B CA  
4005  C C   . SER B 42  ? 0.4014 0.2222 0.2256 0.0201  0.0390  0.0507  42  SER B C   
4006  O O   . SER B 42  ? 0.5105 0.3277 0.3314 0.0314  0.0454  0.0516  42  SER B O   
4007  C CB  . SER B 42  ? 0.4165 0.2420 0.2518 0.0155  0.0346  0.0515  42  SER B CB  
4008  O OG  . SER B 42  ? 0.4689 0.2718 0.2843 0.0079  0.0364  0.0477  42  SER B OG  
4009  N N   . ALA B 43  ? 0.4271 0.2369 0.2386 0.0122  0.0382  0.0482  43  ALA B N   
4010  C CA  . ALA B 43  ? 0.4523 0.2436 0.2439 0.0159  0.0450  0.0459  43  ALA B CA  
4011  C C   . ALA B 43  ? 0.5014 0.3092 0.3026 0.0194  0.0441  0.0488  43  ALA B C   
4012  O O   . ALA B 43  ? 0.4493 0.2448 0.2357 0.0233  0.0498  0.0475  43  ALA B O   
4013  C CB  . ALA B 43  ? 0.4786 0.2484 0.2488 0.0042  0.0445  0.0412  43  ALA B CB  
4014  N N   . VAL B 44  ? 0.4318 0.2663 0.2564 0.0179  0.0374  0.0525  44  VAL B N   
4015  C CA  . VAL B 44  ? 0.4333 0.2843 0.2676 0.0182  0.0351  0.0553  44  VAL B CA  
4016  C C   . VAL B 44  ? 0.4382 0.3063 0.2880 0.0276  0.0362  0.0588  44  VAL B C   
4017  O O   . VAL B 44  ? 0.4240 0.3007 0.2855 0.0294  0.0340  0.0598  44  VAL B O   
4018  C CB  . VAL B 44  ? 0.3982 0.2646 0.2451 0.0074  0.0263  0.0569  44  VAL B CB  
4019  C CG1 . VAL B 44  ? 0.3841 0.2656 0.2393 0.0075  0.0244  0.0599  44  VAL B CG1 
4020  C CG2 . VAL B 44  ? 0.4217 0.2728 0.2535 -0.0025 0.0249  0.0534  44  VAL B CG2 
4021  N N   . TYR B 45  ? 0.4278 0.3009 0.2769 0.0334  0.0398  0.0606  45  TYR B N   
4022  C CA  . TYR B 45  ? 0.3958 0.2873 0.2596 0.0413  0.0407  0.0642  45  TYR B CA  
4023  C C   . TYR B 45  ? 0.4007 0.3126 0.2818 0.0338  0.0326  0.0664  45  TYR B C   
4024  O O   . TYR B 45  ? 0.4665 0.3880 0.3604 0.0299  0.0269  0.0667  45  TYR B O   
4025  C CB  . TYR B 45  ? 0.4322 0.3196 0.2865 0.0517  0.0493  0.0656  45  TYR B CB  
4026  C CG  . TYR B 45  ? 0.4872 0.3965 0.3569 0.0593  0.0505  0.0701  45  TYR B CG  
4027  C CD1 . TYR B 45  ? 0.3834 0.3069 0.2679 0.0622  0.0483  0.0719  45  TYR B CD1 
4028  C CD2 . TYR B 45  ? 0.4113 0.3279 0.2802 0.0631  0.0541  0.0727  45  TYR B CD2 
4029  C CE1 . TYR B 45  ? 0.4134 0.3580 0.3114 0.0683  0.0493  0.0763  45  TYR B CE1 
4030  C CE2 . TYR B 45  ? 0.4566 0.3952 0.3401 0.0695  0.0552  0.0773  45  TYR B CE2 
4031  C CZ  . TYR B 45  ? 0.3867 0.3393 0.2847 0.0718  0.0527  0.0792  45  TYR B CZ  
4032  O OH  . TYR B 45  ? 0.4558 0.4316 0.3681 0.0770  0.0536  0.0841  45  TYR B OH  
4033  N N   . ILE B 46  ? 0.3809 0.2977 0.2610 0.0317  0.0324  0.0679  46  ILE B N   
4034  C CA  . ILE B 46  ? 0.3814 0.3132 0.2746 0.0239  0.0252  0.0698  46  ILE B CA  
4035  C C   . ILE B 46  ? 0.3005 0.2263 0.1886 0.0137  0.0203  0.0688  46  ILE B C   
4036  O O   . ILE B 46  ? 0.3034 0.2181 0.1770 0.0124  0.0234  0.0676  46  ILE B O   
4037  C CB  . ILE B 46  ? 0.3083 0.2501 0.2039 0.0271  0.0277  0.0727  46  ILE B CB  
4038  C CG1 . ILE B 46  ? 0.3371 0.2904 0.2414 0.0373  0.0321  0.0750  46  ILE B CG1 
4039  C CG2 . ILE B 46  ? 0.2233 0.1753 0.1282 0.0185  0.0208  0.0741  46  ILE B CG2 
4040  C CD1 . ILE B 46  ? 0.2995 0.2639 0.2057 0.0421  0.0363  0.0786  46  ILE B CD1 
4041  N N   . ASP B 47  ? 0.2626 0.1958 0.1621 0.0069  0.0132  0.0693  47  ASP B N   
4042  C CA  . ASP B 47  ? 0.2989 0.2321 0.1983 -0.0008 0.0093  0.0701  47  ASP B CA  
4043  C C   . ASP B 47  ? 0.2905 0.2370 0.1997 -0.0053 0.0049  0.0731  47  ASP B C   
4044  O O   . ASP B 47  ? 0.2689 0.2092 0.1782 -0.0070 0.0005  0.0675  47  ASP B O   
4045  C CB  . ASP B 47  ? 0.2877 0.2233 0.1958 -0.0026 0.0064  0.0696  47  ASP B CB  
4046  C CG  . ASP B 47  ? 0.3200 0.2479 0.2208 -0.0067 0.0068  0.0677  47  ASP B CG  
4047  O OD1 . ASP B 47  ? 0.3036 0.2245 0.1924 -0.0102 0.0074  0.0666  47  ASP B OD1 
4048  O OD2 . ASP B 47  ? 0.2776 0.2047 0.1821 -0.0081 0.0056  0.0665  47  ASP B OD2 
4049  N N   . LEU B 48  ? 0.2754 0.2199 0.1759 -0.0057 0.0077  0.0748  48  LEU B N   
4050  C CA  . LEU B 48  ? 0.2535 0.2034 0.1580 -0.0032 0.0089  0.0750  48  LEU B CA  
4051  C C   . LEU B 48  ? 0.2992 0.2420 0.1954 -0.0102 0.0053  0.0731  48  LEU B C   
4052  O O   . LEU B 48  ? 0.2677 0.2123 0.1612 -0.0136 0.0033  0.0736  48  LEU B O   
4053  C CB  . LEU B 48  ? 0.2510 0.2063 0.1512 -0.0062 0.0086  0.0779  48  LEU B CB  
4054  C CG  . LEU B 48  ? 0.2462 0.1931 0.1379 -0.0056 0.0092  0.0763  48  LEU B CG  
4055  C CD1 . LEU B 48  ? 0.2265 0.1749 0.1110 -0.0039 0.0132  0.0778  48  LEU B CD1 
4056  C CD2 . LEU B 48  ? 0.2047 0.1538 0.1071 -0.0026 0.0072  0.0742  48  LEU B CD2 
4057  N N   . LEU B 49  ? 0.2568 0.1943 0.1511 -0.0142 0.0032  0.0706  49  LEU B N   
4058  C CA  . LEU B 49  ? 0.2922 0.2274 0.1818 -0.0231 -0.0020 0.0687  49  LEU B CA  
4059  C C   . LEU B 49  ? 0.2611 0.2082 0.1644 -0.0247 -0.0071 0.0700  49  LEU B C   
4060  O O   . LEU B 49  ? 0.2822 0.2332 0.1834 -0.0307 -0.0111 0.0711  49  LEU B O   
4061  C CB  . LEU B 49  ? 0.2449 0.1727 0.1308 -0.0267 -0.0030 0.0660  49  LEU B CB  
4062  C CG  . LEU B 49  ? 0.3579 0.2802 0.2330 -0.0378 -0.0075 0.0641  49  LEU B CG  
4063  C CD1 . LEU B 49  ? 0.3914 0.2989 0.2446 -0.0423 -0.0051 0.0615  49  LEU B CD1 
4064  C CD2 . LEU B 49  ? 0.3516 0.2698 0.2271 -0.0410 -0.0088 0.0622  49  LEU B CD2 
4065  N N   . THR B 50  ? 0.2579 0.2109 0.1745 -0.0200 -0.0073 0.0699  50  THR B N   
4066  C CA  . THR B 50  ? 0.2660 0.2295 0.1960 -0.0217 -0.0121 0.0709  50  THR B CA  
4067  C C   . THR B 50  ? 0.2550 0.2221 0.1953 -0.0162 -0.0109 0.0703  50  THR B C   
4068  O O   . THR B 50  ? 0.2782 0.2405 0.2161 -0.0117 -0.0073 0.0688  50  THR B O   
4069  C CB  . THR B 50  ? 0.2458 0.2137 0.1816 -0.0261 -0.0166 0.0708  50  THR B CB  
4070  O OG1 . THR B 50  ? 0.3634 0.3423 0.3122 -0.0267 -0.0206 0.0730  50  THR B OG1 
4071  C CG2 . THR B 50  ? 0.2179 0.1830 0.1572 -0.0225 -0.0145 0.0686  50  THR B CG2 
4072  N N   . ASP B 51  ? 0.2282 0.2040 0.1798 -0.0172 -0.0143 0.0719  51  ASP B N   
4073  C CA  . ASP B 51  ? 0.2129 0.1932 0.1758 -0.0143 -0.0145 0.0713  51  ASP B CA  
4074  C C   . ASP B 51  ? 0.2390 0.2242 0.2117 -0.0150 -0.0174 0.0710  51  ASP B C   
4075  O O   . ASP B 51  ? 0.2389 0.2284 0.2214 -0.0136 -0.0183 0.0714  51  ASP B O   
4076  C CB  . ASP B 51  ? 0.2407 0.2259 0.2087 -0.0145 -0.0152 0.0737  51  ASP B CB  
4077  C CG  . ASP B 51  ? 0.2285 0.2192 0.2015 -0.0176 -0.0189 0.0766  51  ASP B CG  
4078  O OD1 . ASP B 51  ? 0.2710 0.2617 0.2390 -0.0206 -0.0207 0.0773  51  ASP B OD1 
4079  O OD2 . ASP B 51  ? 0.2420 0.2370 0.2235 -0.0172 -0.0201 0.0785  51  ASP B OD2 
4080  N N   . SER B 52  ? 0.2747 0.2591 0.2446 -0.0175 -0.0188 0.0708  52  SER B N   
4081  C CA  . SER B 52  ? 0.2429 0.2335 0.2219 -0.0187 -0.0217 0.0717  52  SER B CA  
4082  C C   . SER B 52  ? 0.2191 0.2065 0.1980 -0.0167 -0.0201 0.0690  52  SER B C   
4083  O O   . SER B 52  ? 0.2549 0.2365 0.2251 -0.0182 -0.0188 0.0679  52  SER B O   
4084  C CB  . SER B 52  ? 0.2206 0.2155 0.1977 -0.0241 -0.0254 0.0746  52  SER B CB  
4085  O OG  . SER B 52  ? 0.2571 0.2598 0.2439 -0.0248 -0.0280 0.0766  52  SER B OG  
4086  N N   . GLY B 53  ? 0.1938 0.1843 0.1815 -0.0138 -0.0199 0.0683  53  GLY B N   
4087  C CA  . GLY B 53  ? 0.1963 0.1854 0.1850 -0.0122 -0.0188 0.0664  53  GLY B CA  
4088  C C   . GLY B 53  ? 0.2268 0.2093 0.2089 -0.0092 -0.0154 0.0636  53  GLY B C   
4089  O O   . GLY B 53  ? 0.2258 0.2071 0.2082 -0.0077 -0.0144 0.0622  53  GLY B O   
4090  N N   . THR B 54  ? 0.2363 0.2151 0.2126 -0.0081 -0.0135 0.0635  54  THR B N   
4091  C CA  . THR B 54  ? 0.2318 0.2051 0.2016 -0.0047 -0.0103 0.0620  54  THR B CA  
4092  C C   . THR B 54  ? 0.2282 0.2070 0.2051 -0.0028 -0.0104 0.0622  54  THR B C   
4093  O O   . THR B 54  ? 0.2624 0.2398 0.2356 -0.0003 -0.0084 0.0622  54  THR B O   
4094  C CB  . THR B 54  ? 0.1985 0.1640 0.1559 -0.0045 -0.0077 0.0625  54  THR B CB  
4095  O OG1 . THR B 54  ? 0.2184 0.1877 0.1777 -0.0060 -0.0088 0.0643  54  THR B OG1 
4096  C CG2 . THR B 54  ? 0.2189 0.1792 0.1689 -0.0074 -0.0074 0.0629  54  THR B CG2 
4097  N N   . ASN B 55  ? 0.1849 0.1700 0.1719 -0.0041 -0.0126 0.0632  55  ASN B N   
4098  C CA  . ASN B 55  ? 0.1835 0.1733 0.1767 -0.0036 -0.0127 0.0643  55  ASN B CA  
4099  C C   . ASN B 55  ? 0.1612 0.1530 0.1571 -0.0016 -0.0121 0.0634  55  ASN B C   
4100  O O   . ASN B 55  ? 0.2020 0.1918 0.1967 -0.0007 -0.0121 0.0618  55  ASN B O   
4101  C CB  . ASN B 55  ? 0.1588 0.1517 0.1601 -0.0055 -0.0150 0.0660  55  ASN B CB  
4102  C CG  . ASN B 55  ? 0.2105 0.2028 0.2099 -0.0073 -0.0160 0.0675  55  ASN B CG  
4103  O OD1 . ASN B 55  ? 0.2155 0.2080 0.2121 -0.0082 -0.0155 0.0689  55  ASN B OD1 
4104  N ND2 . ASN B 55  ? 0.1894 0.1823 0.1907 -0.0081 -0.0176 0.0677  55  ASN B ND2 
4105  N N   . ALA B 56  ? 0.1555 0.1523 0.1550 -0.0014 -0.0119 0.0652  56  ALA B N   
4106  C CA  . ALA B 56  ? 0.1762 0.1773 0.1794 -0.0002 -0.0119 0.0655  56  ALA B CA  
4107  C C   . ALA B 56  ? 0.1577 0.1604 0.1686 -0.0027 -0.0142 0.0666  56  ALA B C   
4108  O O   . ALA B 56  ? 0.1789 0.1826 0.1935 -0.0053 -0.0153 0.0688  56  ALA B O   
4109  C CB  . ALA B 56  ? 0.1502 0.1581 0.1536 0.0011  -0.0104 0.0681  56  ALA B CB  
4110  N N   . MET B 57  ? 0.1780 0.1797 0.1903 -0.0019 -0.0148 0.0654  57  MET B N   
4111  C CA  . MET B 57  ? 0.1675 0.1679 0.1853 -0.0037 -0.0167 0.0665  57  MET B CA  
4112  C C   . MET B 57  ? 0.1734 0.1787 0.1940 -0.0056 -0.0179 0.0693  57  MET B C   
4113  O O   . MET B 57  ? 0.1698 0.1820 0.1888 -0.0045 -0.0172 0.0702  57  MET B O   
4114  C CB  . MET B 57  ? 0.2045 0.2018 0.2222 -0.0018 -0.0167 0.0646  57  MET B CB  
4115  C CG  . MET B 57  ? 0.1619 0.1565 0.1787 -0.0013 -0.0164 0.0635  57  MET B CG  
4116  S SD  . MET B 57  ? 0.2128 0.2062 0.2323 0.0005  -0.0165 0.0631  57  MET B SD  
4117  C CE  . MET B 57  ? 0.2113 0.2063 0.2255 0.0019  -0.0152 0.0614  57  MET B CE  
4118  N N   . SER B 58  ? 0.1708 0.1723 0.1952 -0.0087 -0.0199 0.0711  58  SER B N   
4119  C CA  . SER B 58  ? 0.1908 0.1957 0.2167 -0.0129 -0.0220 0.0745  58  SER B CA  
4120  C C   . SER B 58  ? 0.1877 0.1929 0.2121 -0.0115 -0.0221 0.0710  58  SER B C   
4121  O O   . SER B 58  ? 0.1859 0.1865 0.2094 -0.0077 -0.0213 0.0698  58  SER B O   
4122  C CB  . SER B 58  ? 0.1692 0.1667 0.1976 -0.0185 -0.0232 0.0756  58  SER B CB  
4123  O OG  . SER B 58  ? 0.2197 0.2060 0.2483 -0.0172 -0.0228 0.0725  58  SER B OG  
4124  N N   . ASP B 59  ? 0.1918 0.2037 0.2156 -0.0152 -0.0230 0.0686  59  ASP B N   
4125  C CA  . ASP B 59  ? 0.2054 0.2178 0.2268 -0.0146 -0.0230 0.0639  59  ASP B CA  
4126  C C   . ASP B 59  ? 0.1772 0.1760 0.1983 -0.0153 -0.0223 0.0599  59  ASP B C   
4127  O O   . ASP B 59  ? 0.1849 0.1812 0.2041 -0.0117 -0.0210 0.0570  59  ASP B O   
4128  C CB  . ASP B 59  ? 0.1880 0.2117 0.2084 -0.0195 -0.0246 0.0623  59  ASP B CB  
4129  C CG  . ASP B 59  ? 0.2224 0.2444 0.2444 -0.0276 -0.0261 0.0620  59  ASP B CG  
4130  O OD1 . ASP B 59  ? 0.3010 0.3133 0.3249 -0.0285 -0.0256 0.0640  59  ASP B OD1 
4131  O OD2 . ASP B 59  ? 0.2179 0.2489 0.2389 -0.0336 -0.0279 0.0603  59  ASP B OD2 
4132  N N   . HIS B 60  ? 0.1801 0.1697 0.2027 -0.0190 -0.0225 0.0602  60  HIS B N   
4133  C CA  . HIS B 60  ? 0.1815 0.1567 0.2035 -0.0179 -0.0210 0.0572  60  HIS B CA  
4134  C C   . HIS B 60  ? 0.2108 0.1832 0.2354 -0.0107 -0.0196 0.0597  60  HIS B C   
4135  O O   . HIS B 60  ? 0.1993 0.1654 0.2234 -0.0071 -0.0176 0.0569  60  HIS B O   
4136  C CB  . HIS B 60  ? 0.2396 0.2041 0.2622 -0.0228 -0.0212 0.0583  60  HIS B CB  
4137  C CG  . HIS B 60  ? 0.3110 0.2767 0.3304 -0.0316 -0.0226 0.0551  60  HIS B CG  
4138  N ND1 . HIS B 60  ? 0.3130 0.2744 0.3269 -0.0350 -0.0223 0.0484  60  HIS B ND1 
4139  C CD2 . HIS B 60  ? 0.3797 0.3523 0.4003 -0.0384 -0.0245 0.0579  60  HIS B CD2 
4140  C CE1 . HIS B 60  ? 0.3454 0.3108 0.3570 -0.0443 -0.0243 0.0471  60  HIS B CE1 
4141  N NE2 . HIS B 60  ? 0.3840 0.3569 0.4003 -0.0465 -0.0256 0.0530  60  HIS B NE2 
4142  N N   . GLN B 61  ? 0.1657 0.1432 0.1927 -0.0088 -0.0203 0.0650  61  GLN B N   
4143  C CA  . GLN B 61  ? 0.1898 0.1669 0.2188 -0.0035 -0.0196 0.0675  61  GLN B CA  
4144  C C   . GLN B 61  ? 0.1931 0.1754 0.2200 -0.0004 -0.0185 0.0650  61  GLN B C   
4145  O O   . GLN B 61  ? 0.1819 0.1619 0.2101 0.0032  -0.0171 0.0642  61  GLN B O   
4146  C CB  . GLN B 61  ? 0.1632 0.1461 0.1913 -0.0034 -0.0194 0.0681  61  GLN B CB  
4147  C CG  . GLN B 61  ? 0.1472 0.1256 0.1772 -0.0042 -0.0193 0.0690  61  GLN B CG  
4148  C CD  . GLN B 61  ? 0.1614 0.1458 0.1895 -0.0049 -0.0191 0.0688  61  GLN B CD  
4149  O OE1 . GLN B 61  ? 0.1915 0.1805 0.2179 -0.0068 -0.0193 0.0692  61  GLN B OE1 
4150  N NE2 . GLN B 61  ? 0.1601 0.1445 0.1884 -0.0033 -0.0187 0.0687  61  GLN B NE2 
4151  N N   . TRP B 62  ? 0.1821 0.1722 0.2057 -0.0013 -0.0189 0.0642  62  TRP B N   
4152  C CA  . TRP B 62  ? 0.2238 0.2182 0.2446 0.0016  -0.0178 0.0625  62  TRP B CA  
4153  C C   . TRP B 62  ? 0.2095 0.2011 0.2291 0.0018  -0.0166 0.0573  62  TRP B C   
4154  O O   . TRP B 62  ? 0.2285 0.2201 0.2479 0.0051  -0.0149 0.0563  62  TRP B O   
4155  C CB  . TRP B 62  ? 0.2329 0.2358 0.2502 0.0014  -0.0182 0.0635  62  TRP B CB  
4156  C CG  . TRP B 62  ? 0.2959 0.2997 0.3110 0.0032  -0.0170 0.0647  62  TRP B CG  
4157  C CD1 . TRP B 62  ? 0.2870 0.2914 0.3019 0.0020  -0.0166 0.0646  62  TRP B CD1 
4158  C CD2 . TRP B 62  ? 0.3457 0.3486 0.3570 0.0056  -0.0149 0.0625  62  TRP B CD2 
4159  N NE1 . TRP B 62  ? 0.3358 0.3386 0.3462 0.0038  -0.0146 0.0624  62  TRP B NE1 
4160  C CE2 . TRP B 62  ? 0.3549 0.3562 0.3629 0.0055  -0.0137 0.0611  62  TRP B CE2 
4161  C CE3 . TRP B 62  ? 0.3569 0.3597 0.3667 0.0073  -0.0141 0.0621  62  TRP B CE3 
4162  C CZ2 . TRP B 62  ? 0.3967 0.3946 0.3992 0.0065  -0.0121 0.0595  62  TRP B CZ2 
4163  C CZ3 . TRP B 62  ? 0.3638 0.3647 0.3692 0.0080  -0.0123 0.0606  62  TRP B CZ3 
4164  C CH2 . TRP B 62  ? 0.3227 0.3204 0.3242 0.0073  -0.0115 0.0593  62  TRP B CH2 
4165  N N   . ALA B 63  ? 0.2115 0.2006 0.2297 -0.0022 -0.0172 0.0538  63  ALA B N   
4166  C CA  . ALA B 63  ? 0.2302 0.2141 0.2453 -0.0024 -0.0156 0.0480  63  ALA B CA  
4167  C C   . ALA B 63  ? 0.2086 0.1835 0.2264 0.0021  -0.0130 0.0479  63  ALA B C   
4168  O O   . ALA B 63  ? 0.2091 0.1836 0.2254 0.0055  -0.0106 0.0451  63  ALA B O   
4169  C CB  . ALA B 63  ? 0.2016 0.1814 0.2136 -0.0089 -0.0168 0.0442  63  ALA B CB  
4170  N N   . ALA B 64  ? 0.2169 0.1859 0.2391 0.0027  -0.0134 0.0516  64  ALA B N   
4171  C CA  . ALA B 64  ? 0.2669 0.2294 0.2928 0.0079  -0.0110 0.0530  64  ALA B CA  
4172  C C   . ALA B 64  ? 0.2305 0.2018 0.2592 0.0126  -0.0100 0.0555  64  ALA B C   
4173  O O   . ALA B 64  ? 0.2091 0.1791 0.2394 0.0173  -0.0071 0.0544  64  ALA B O   
4174  C CB  . ALA B 64  ? 0.1906 0.1477 0.2208 0.0077  -0.0121 0.0581  64  ALA B CB  
4175  N N   . MET B 65  ? 0.1902 0.1701 0.2190 0.0111  -0.0121 0.0588  65  MET B N   
4176  C CA  . MET B 65  ? 0.1870 0.1742 0.2171 0.0138  -0.0114 0.0612  65  MET B CA  
4177  C C   . MET B 65  ? 0.2049 0.1951 0.2315 0.0153  -0.0091 0.0570  65  MET B C   
4178  O O   . MET B 65  ? 0.1636 0.1576 0.1924 0.0185  -0.0070 0.0578  65  MET B O   
4179  C CB  . MET B 65  ? 0.1601 0.1523 0.1882 0.0113  -0.0136 0.0647  65  MET B CB  
4180  C CG  . MET B 65  ? 0.2241 0.2155 0.2533 0.0092  -0.0147 0.0655  65  MET B CG  
4181  S SD  . MET B 65  ? 0.3339 0.3292 0.3566 0.0062  -0.0149 0.0634  65  MET B SD  
4182  C CE  . MET B 65  ? 0.1257 0.1248 0.1476 0.0065  -0.0140 0.0639  65  MET B CE  
4183  N N   . ILE B 66  ? 0.2037 0.1937 0.2248 0.0128  -0.0095 0.0529  66  ILE B N   
4184  C CA  . ILE B 66  ? 0.1594 0.1532 0.1760 0.0138  -0.0076 0.0492  66  ILE B CA  
4185  C C   . ILE B 66  ? 0.1951 0.1839 0.2119 0.0171  -0.0041 0.0453  66  ILE B C   
4186  O O   . ILE B 66  ? 0.1928 0.1860 0.2080 0.0197  -0.0016 0.0441  66  ILE B O   
4187  C CB  . ILE B 66  ? 0.2013 0.1975 0.2121 0.0100  -0.0094 0.0462  66  ILE B CB  
4188  C CG1 . ILE B 66  ? 0.3079 0.3093 0.3187 0.0084  -0.0119 0.0507  66  ILE B CG1 
4189  C CG2 . ILE B 66  ? 0.2267 0.2278 0.2319 0.0109  -0.0077 0.0430  66  ILE B CG2 
4190  C CD1 . ILE B 66  ? 0.2934 0.2989 0.3036 0.0108  -0.0112 0.0548  66  ILE B CD1 
4191  N N   . THR B 67  ? 0.1982 0.1771 0.2162 0.0174  -0.0034 0.0435  67  THR B N   
4192  C CA  . THR B 67  ? 0.2408 0.2128 0.2583 0.0219  0.0009  0.0400  67  THR B CA  
4193  C C   . THR B 67  ? 0.2195 0.1918 0.2452 0.0277  0.0027  0.0451  67  THR B C   
4194  O O   . THR B 67  ? 0.2185 0.1833 0.2450 0.0329  0.0066  0.0434  67  THR B O   
4195  C CB  . THR B 67  ? 0.1979 0.1563 0.2097 0.0189  0.0015  0.0343  67  THR B CB  
4196  O OG1 . THR B 67  ? 0.2423 0.1955 0.2573 0.0160  -0.0012 0.0376  67  THR B OG1 
4197  C CG2 . THR B 67  ? 0.2228 0.1839 0.2262 0.0129  -0.0002 0.0290  67  THR B CG2 
4198  N N   . GLY B 68  ? 0.2052 0.1863 0.2365 0.0272  0.0000  0.0515  68  GLY B N   
4199  C CA  . GLY B 68  ? 0.1719 0.1564 0.2115 0.0317  0.0007  0.0574  68  GLY B CA  
4200  C C   . GLY B 68  ? 0.1931 0.1848 0.2359 0.0375  0.0049  0.0578  68  GLY B C   
4201  O O   . GLY B 68  ? 0.2171 0.2158 0.2569 0.0366  0.0060  0.0559  68  GLY B O   
4202  N N   . ASP B 69  ? 0.1940 0.1849 0.2433 0.0439  0.0074  0.0610  69  ASP B N   
4203  C CA  . ASP B 69  ? 0.2039 0.2026 0.2577 0.0510  0.0122  0.0622  69  ASP B CA  
4204  C C   . ASP B 69  ? 0.1987 0.2149 0.2612 0.0505  0.0100  0.0701  69  ASP B C   
4205  O O   . ASP B 69  ? 0.1803 0.1998 0.2495 0.0517  0.0079  0.0764  69  ASP B O   
4206  C CB  . ASP B 69  ? 0.2220 0.2099 0.2778 0.0592  0.0167  0.0618  69  ASP B CB  
4207  C CG  . ASP B 69  ? 0.2369 0.2334 0.2980 0.0684  0.0227  0.0634  69  ASP B CG  
4208  O OD1 . ASP B 69  ? 0.2750 0.2858 0.3376 0.0676  0.0235  0.0640  69  ASP B OD1 
4209  O OD2 . ASP B 69  ? 0.2166 0.2049 0.2800 0.0769  0.0272  0.0643  69  ASP B OD2 
4210  N N   . GLU B 70  ? 0.1817 0.2092 0.2433 0.0480  0.0105  0.0701  70  GLU B N   
4211  C CA  . GLU B 70  ? 0.2095 0.2528 0.2771 0.0447  0.0079  0.0770  70  GLU B CA  
4212  C C   . GLU B 70  ? 0.2163 0.2743 0.2939 0.0512  0.0113  0.0823  70  GLU B C   
4213  O O   . GLU B 70  ? 0.2275 0.3010 0.3100 0.0475  0.0094  0.0879  70  GLU B O   
4214  C CB  . GLU B 70  ? 0.1968 0.2441 0.2578 0.0380  0.0067  0.0752  70  GLU B CB  
4215  C CG  . GLU B 70  ? 0.1670 0.2041 0.2196 0.0317  0.0028  0.0724  70  GLU B CG  
4216  C CD  . GLU B 70  ? 0.2128 0.2485 0.2676 0.0281  -0.0017 0.0768  70  GLU B CD  
4217  O OE1 . GLU B 70  ? 0.1630 0.2088 0.2242 0.0273  -0.0031 0.0827  70  GLU B OE1 
4218  O OE2 . GLU B 70  ? 0.1934 0.2190 0.2434 0.0257  -0.0040 0.0745  70  GLU B OE2 
4219  N N   . ALA B 71  ? 0.1746 0.2280 0.2550 0.0606  0.0164  0.0810  71  ALA B N   
4220  C CA  . ALA B 71  ? 0.2310 0.2995 0.3215 0.0686  0.0207  0.0864  71  ALA B CA  
4221  C C   . ALA B 71  ? 0.2122 0.2962 0.3133 0.0674  0.0165  0.0962  71  ALA B C   
4222  O O   . ALA B 71  ? 0.2419 0.3187 0.3415 0.0634  0.0121  0.0972  71  ALA B O   
4223  C CB  . ALA B 71  ? 0.2342 0.2906 0.3246 0.0800  0.0270  0.0835  71  ALA B CB  
4224  N N   . TYR B 72  ? 0.1568 0.2619 0.2659 0.0685  0.0181  0.1017  72  TYR B N   
4225  C CA  . TYR B 72  ? 0.1798 0.2991 0.2946 0.0635  0.0143  0.1083  72  TYR B CA  
4226  C C   . TYR B 72  ? 0.1681 0.2824 0.2858 0.0702  0.0158  0.1100  72  TYR B C   
4227  O O   . TYR B 72  ? 0.2546 0.3701 0.3731 0.0653  0.0114  0.1132  72  TYR B O   
4228  C CB  . TYR B 72  ? 0.1924 0.3356 0.3143 0.0623  0.0160  0.1136  72  TYR B CB  
4229  C CG  . TYR B 72  ? 0.1922 0.3515 0.3186 0.0543  0.0111  0.1208  72  TYR B CG  
4230  C CD1 . TYR B 72  ? 0.2030 0.3664 0.3260 0.0419  0.0051  0.1224  72  TYR B CD1 
4231  C CD2 . TYR B 72  ? 0.2084 0.3779 0.3414 0.0592  0.0125  0.1261  72  TYR B CD2 
4232  C CE1 . TYR B 72  ? 0.2297 0.4070 0.3554 0.0338  0.0007  0.1286  72  TYR B CE1 
4233  C CE2 . TYR B 72  ? 0.2706 0.4555 0.4070 0.0515  0.0079  0.1329  72  TYR B CE2 
4234  C CZ  . TYR B 72  ? 0.2120 0.4005 0.3445 0.0385  0.0020  0.1338  72  TYR B CZ  
4235  O OH  . TYR B 72  ? 0.3118 0.5149 0.4464 0.0302  -0.0024 0.1402  72  TYR B OH  
4236  N N   . ALA B 73  ? 0.1784 0.2864 0.2971 0.0814  0.0224  0.1078  73  ALA B N   
4237  C CA  . ALA B 73  ? 0.1984 0.3013 0.3195 0.0889  0.0247  0.1100  73  ALA B CA  
4238  C C   . ALA B 73  ? 0.2062 0.2835 0.3201 0.0958  0.0286  0.1032  73  ALA B C   
4239  O O   . ALA B 73  ? 0.2582 0.3283 0.3685 0.1014  0.0341  0.0981  73  ALA B O   
4240  C CB  . ALA B 73  ? 0.1738 0.2941 0.3027 0.0968  0.0298  0.1153  73  ALA B CB  
4241  N N   . GLY B 74  ? 0.1905 0.2539 0.3014 0.0948  0.0260  0.1029  74  GLY B N   
4242  C CA  . GLY B 74  ? 0.2489 0.2875 0.3528 0.1010  0.0299  0.0973  74  GLY B CA  
4243  C C   . GLY B 74  ? 0.2735 0.2947 0.3685 0.0960  0.0285  0.0902  74  GLY B C   
4244  O O   . GLY B 74  ? 0.2703 0.2727 0.3585 0.1013  0.0337  0.0842  74  GLY B O   
4245  N N   . SER B 75  ? 0.2431 0.2698 0.3371 0.0855  0.0221  0.0906  75  SER B N   
4246  C CA  . SER B 75  ? 0.2166 0.2287 0.3025 0.0800  0.0201  0.0851  75  SER B CA  
4247  C C   . SER B 75  ? 0.2470 0.2350 0.3262 0.0818  0.0214  0.0812  75  SER B C   
4248  O O   . SER B 75  ? 0.2533 0.2374 0.3337 0.0828  0.0204  0.0839  75  SER B O   
4249  C CB  . SER B 75  ? 0.2159 0.2362 0.3012 0.0686  0.0126  0.0870  75  SER B CB  
4250  O OG  . SER B 75  ? 0.2180 0.2239 0.2954 0.0632  0.0103  0.0824  75  SER B OG  
4251  N N   . ARG B 76  ? 0.2652 0.2371 0.3356 0.0807  0.0238  0.0739  76  ARG B N   
4252  C CA  . ARG B 76  ? 0.2669 0.2146 0.3290 0.0796  0.0248  0.0692  76  ARG B CA  
4253  C C   . ARG B 76  ? 0.2659 0.2114 0.3291 0.0724  0.0184  0.0734  76  ARG B C   
4254  O O   . ARG B 76  ? 0.2757 0.2066 0.3355 0.0725  0.0187  0.0730  76  ARG B O   
4255  C CB  . ARG B 76  ? 0.2831 0.2192 0.3327 0.0737  0.0261  0.0582  76  ARG B CB  
4256  C CG  . ARG B 76  ? 0.3446 0.2559 0.3841 0.0701  0.0270  0.0524  76  ARG B CG  
4257  C CD  . ARG B 76  ? 0.3623 0.2675 0.3900 0.0613  0.0261  0.0424  76  ARG B CD  
4258  N NE  . ARG B 76  ? 0.4056 0.3209 0.4337 0.0510  0.0190  0.0433  76  ARG B NE  
4259  C CZ  . ARG B 76  ? 0.3923 0.3241 0.4214 0.0475  0.0163  0.0431  76  ARG B CZ  
4260  N NH1 . ARG B 76  ? 0.3494 0.2900 0.3787 0.0520  0.0198  0.0415  76  ARG B NH1 
4261  N NH2 . ARG B 76  ? 0.3061 0.2451 0.3356 0.0396  0.0105  0.0448  76  ARG B NH2 
4262  N N   . ASN B 77  ? 0.2364 0.1971 0.3020 0.0646  0.0125  0.0758  77  ASN B N   
4263  C CA  . ASN B 77  ? 0.2456 0.2065 0.3095 0.0562  0.0065  0.0772  77  ASN B CA  
4264  C C   . ASN B 77  ? 0.2459 0.2158 0.3144 0.0571  0.0046  0.0823  77  ASN B C   
4265  O O   . ASN B 77  ? 0.2741 0.2401 0.3401 0.0522  0.0013  0.0831  77  ASN B O   
4266  C CB  . ASN B 77  ? 0.2071 0.1788 0.2696 0.0481  0.0021  0.0768  77  ASN B CB  
4267  C CG  . ASN B 77  ? 0.2329 0.1994 0.2886 0.0455  0.0036  0.0697  77  ASN B CG  
4268  O OD1 . ASN B 77  ? 0.2438 0.2197 0.2995 0.0465  0.0051  0.0678  77  ASN B OD1 
4269  N ND2 . ASN B 77  ? 0.2141 0.1670 0.2625 0.0408  0.0030  0.0646  77  ASN B ND2 
4270  N N   . TYR B 78  ? 0.2290 0.2119 0.3044 0.0631  0.0068  0.0861  78  TYR B N   
4271  C CA  . TYR B 78  ? 0.2327 0.2226 0.3127 0.0650  0.0056  0.0914  78  TYR B CA  
4272  C C   . TYR B 78  ? 0.2358 0.2075 0.3126 0.0705  0.0084  0.0910  78  TYR B C   
4273  O O   . TYR B 78  ? 0.2808 0.2495 0.3564 0.0681  0.0057  0.0936  78  TYR B O   
4274  C CB  . TYR B 78  ? 0.2279 0.2367 0.3165 0.0704  0.0077  0.0963  78  TYR B CB  
4275  C CG  . TYR B 78  ? 0.2233 0.2372 0.3171 0.0760  0.0086  0.1023  78  TYR B CG  
4276  C CD1 . TYR B 78  ? 0.2307 0.2564 0.3273 0.0708  0.0041  0.1073  78  TYR B CD1 
4277  C CD2 . TYR B 78  ? 0.2029 0.2092 0.2981 0.0866  0.0144  0.1029  78  TYR B CD2 
4278  C CE1 . TYR B 78  ? 0.1978 0.2289 0.2993 0.0761  0.0048  0.1134  78  TYR B CE1 
4279  C CE2 . TYR B 78  ? 0.2128 0.2238 0.3127 0.0923  0.0154  0.1090  78  TYR B CE2 
4280  C CZ  . TYR B 78  ? 0.2058 0.2298 0.3092 0.0870  0.0104  0.1145  78  TYR B CZ  
4281  O OH  . TYR B 78  ? 0.2535 0.2831 0.3617 0.0930  0.0114  0.1212  78  TYR B OH  
4282  N N   . TYR B 79  ? 0.2417 0.1997 0.3159 0.0777  0.0142  0.0876  79  TYR B N   
4283  C CA  . TYR B 79  ? 0.2588 0.1962 0.3283 0.0825  0.0174  0.0866  79  TYR B CA  
4284  C C   . TYR B 79  ? 0.3332 0.2536 0.3946 0.0744  0.0143  0.0835  79  TYR B C   
4285  O O   . TYR B 79  ? 0.2996 0.2085 0.3581 0.0747  0.0140  0.0852  79  TYR B O   
4286  C CB  . TYR B 79  ? 0.2615 0.1863 0.3281 0.0915  0.0252  0.0822  79  TYR B CB  
4287  C CG  . TYR B 79  ? 0.3079 0.2511 0.3827 0.1000  0.0288  0.0859  79  TYR B CG  
4288  C CD1 . TYR B 79  ? 0.2781 0.2256 0.3578 0.1081  0.0314  0.0913  79  TYR B CD1 
4289  C CD2 . TYR B 79  ? 0.2995 0.2571 0.3775 0.0998  0.0297  0.0846  79  TYR B CD2 
4290  C CE1 . TYR B 79  ? 0.2725 0.2389 0.3604 0.1155  0.0348  0.0954  79  TYR B CE1 
4291  C CE2 . TYR B 79  ? 0.3144 0.2905 0.4001 0.1067  0.0331  0.0885  79  TYR B CE2 
4292  C CZ  . TYR B 79  ? 0.3123 0.2932 0.4032 0.1144  0.0356  0.0939  79  TYR B CZ  
4293  O OH  . TYR B 79  ? 0.3107 0.3113 0.4095 0.1209  0.0390  0.0984  79  TYR B OH  
4294  N N   . ASP B 80  ? 0.3048 0.2245 0.3629 0.0668  0.0120  0.0796  80  ASP B N   
4295  C CA  . ASP B 80  ? 0.2392 0.1472 0.2908 0.0580  0.0087  0.0776  80  ASP B CA  
4296  C C   . ASP B 80  ? 0.2181 0.1371 0.2715 0.0530  0.0034  0.0822  80  ASP B C   
4297  O O   . ASP B 80  ? 0.2677 0.1758 0.3165 0.0495  0.0021  0.0827  80  ASP B O   
4298  C CB  . ASP B 80  ? 0.2658 0.1748 0.3148 0.0514  0.0072  0.0736  80  ASP B CB  
4299  C CG  . ASP B 80  ? 0.3756 0.2678 0.4196 0.0542  0.0128  0.0680  80  ASP B CG  
4300  O OD1 . ASP B 80  ? 0.4449 0.3217 0.4854 0.0607  0.0181  0.0659  80  ASP B OD1 
4301  O OD2 . ASP B 80  ? 0.3877 0.2852 0.4273 0.0476  0.0111  0.0619  80  ASP B OD2 
4302  N N   . LEU B 81  ? 0.2376 0.1777 0.2968 0.0520  0.0007  0.0851  81  LEU B N   
4303  C CA  . LEU B 81  ? 0.2289 0.1797 0.2894 0.0474  -0.0035 0.0888  81  LEU B CA  
4304  C C   . LEU B 81  ? 0.2552 0.2038 0.3179 0.0530  -0.0025 0.0938  81  LEU B C   
4305  O O   . LEU B 81  ? 0.2594 0.2066 0.3199 0.0495  -0.0049 0.0961  81  LEU B O   
4306  C CB  . LEU B 81  ? 0.2160 0.1875 0.2812 0.0446  -0.0059 0.0902  81  LEU B CB  
4307  C CG  . LEU B 81  ? 0.1884 0.1712 0.2543 0.0392  -0.0098 0.0932  81  LEU B CG  
4308  C CD1 . LEU B 81  ? 0.1648 0.1400 0.2239 0.0322  -0.0119 0.0902  81  LEU B CD1 
4309  C CD2 . LEU B 81  ? 0.1996 0.1996 0.2691 0.0361  -0.0115 0.0942  81  LEU B CD2 
4310  N N   . LYS B 82  ? 0.2279 0.1770 0.2952 0.0620  0.0014  0.0959  82  LYS B N   
4311  C CA  . LYS B 82  ? 0.2652 0.2118 0.3348 0.0684  0.0027  0.1012  82  LYS B CA  
4312  C C   . LYS B 82  ? 0.3195 0.2423 0.3812 0.0683  0.0039  0.0996  82  LYS B C   
4313  O O   . LYS B 82  ? 0.3291 0.2492 0.3897 0.0681  0.0024  0.1038  82  LYS B O   
4314  C CB  . LYS B 82  ? 0.3058 0.2580 0.3818 0.0788  0.0075  0.1035  82  LYS B CB  
4315  C CG  . LYS B 82  ? 0.2942 0.2467 0.3739 0.0869  0.0094  0.1100  82  LYS B CG  
4316  C CD  . LYS B 82  ? 0.3179 0.2805 0.4048 0.0970  0.0145  0.1127  82  LYS B CD  
4317  C CE  . LYS B 82  ? 0.3125 0.2741 0.4029 0.1063  0.0173  0.1193  82  LYS B CE  
4318  N NZ  . LYS B 82  ? 0.3379 0.2715 0.4198 0.1095  0.0201  0.1167  82  LYS B NZ  
4319  N N   . ASP B 83  ? 0.2825 0.1873 0.3380 0.0676  0.0066  0.0936  83  ASP B N   
4320  C CA  . ASP B 83  ? 0.3030 0.1835 0.3498 0.0655  0.0077  0.0917  83  ASP B CA  
4321  C C   . ASP B 83  ? 0.3102 0.1905 0.3525 0.0552  0.0030  0.0920  83  ASP B C   
4322  O O   . ASP B 83  ? 0.3609 0.2279 0.3979 0.0536  0.0027  0.0939  83  ASP B O   
4323  C CB  . ASP B 83  ? 0.3247 0.1862 0.3654 0.0656  0.0119  0.0846  83  ASP B CB  
4324  C CG  . ASP B 83  ? 0.4295 0.2872 0.4725 0.0769  0.0183  0.0836  83  ASP B CG  
4325  O OD1 . ASP B 83  ? 0.4450 0.3099 0.4934 0.0849  0.0196  0.0891  83  ASP B OD1 
4326  O OD2 . ASP B 83  ? 0.5249 0.3725 0.5638 0.0778  0.0223  0.0774  83  ASP B OD2 
4327  N N   . LYS B 84  ? 0.2979 0.1927 0.3417 0.0485  -0.0003 0.0903  84  LYS B N   
4328  C CA  . LYS B 84  ? 0.3254 0.2220 0.3653 0.0395  -0.0038 0.0904  84  LYS B CA  
4329  C C   . LYS B 84  ? 0.3124 0.2184 0.3546 0.0400  -0.0060 0.0962  84  LYS B C   
4330  O O   . LYS B 84  ? 0.3112 0.2102 0.3486 0.0356  -0.0071 0.0975  84  LYS B O   
4331  C CB  . LYS B 84  ? 0.2638 0.1744 0.3054 0.0334  -0.0062 0.0873  84  LYS B CB  
4332  C CG  . LYS B 84  ? 0.2659 0.1768 0.3033 0.0244  -0.0086 0.0862  84  LYS B CG  
4333  C CD  . LYS B 84  ? 0.3207 0.2116 0.3516 0.0202  -0.0069 0.0837  84  LYS B CD  
4334  C CE  . LYS B 84  ? 0.3807 0.2751 0.4091 0.0113  -0.0090 0.0833  84  LYS B CE  
4335  N NZ  . LYS B 84  ? 0.3929 0.2687 0.4154 0.0054  -0.0074 0.0815  84  LYS B NZ  
4336  N N   . ALA B 85  ? 0.2959 0.2182 0.3454 0.0449  -0.0066 0.0999  85  ALA B N   
4337  C CA  . ALA B 85  ? 0.3169 0.2489 0.3690 0.0451  -0.0088 0.1057  85  ALA B CA  
4338  C C   . ALA B 85  ? 0.3461 0.2638 0.3960 0.0508  -0.0069 0.1100  85  ALA B C   
4339  O O   . ALA B 85  ? 0.3482 0.2672 0.3969 0.0493  -0.0087 0.1143  85  ALA B O   
4340  C CB  . ALA B 85  ? 0.2627 0.2161 0.3234 0.0480  -0.0099 0.1090  85  ALA B CB  
4341  N N   . LYS B 86  ? 0.3159 0.2194 0.3650 0.0577  -0.0030 0.1089  86  LYS B N   
4342  C CA  . LYS B 86  ? 0.3152 0.2004 0.3605 0.0629  -0.0008 0.1121  86  LYS B CA  
4343  C C   . LYS B 86  ? 0.3710 0.2365 0.4060 0.0553  -0.0014 0.1097  86  LYS B C   
4344  O O   . LYS B 86  ? 0.3962 0.2536 0.4275 0.0550  -0.0020 0.1140  86  LYS B O   
4345  C CB  . LYS B 86  ? 0.4050 0.2791 0.4515 0.0720  0.0043  0.1104  86  LYS B CB  
4346  C CG  . LYS B 86  ? 0.4893 0.3418 0.5313 0.0779  0.0074  0.1130  86  LYS B CG  
4347  C CD  . LYS B 86  ? 0.4000 0.2625 0.4468 0.0829  0.0062  0.1218  86  LYS B CD  
4348  C CE  . LYS B 86  ? 0.4169 0.2574 0.4594 0.0898  0.0098  0.1247  86  LYS B CE  
4349  N NZ  . LYS B 86  ? 0.5104 0.3592 0.5563 0.0933  0.0080  0.1338  86  LYS B NZ  
4350  N N   . GLU B 87  ? 0.3497 0.2078 0.3800 0.0488  -0.0012 0.1033  87  GLU B N   
4351  C CA  . GLU B 87  ? 0.3694 0.2108 0.3903 0.0402  -0.0015 0.1011  87  GLU B CA  
4352  C C   . GLU B 87  ? 0.3495 0.2031 0.3701 0.0338  -0.0047 0.1043  87  GLU B C   
4353  O O   . GLU B 87  ? 0.3915 0.2333 0.4059 0.0303  -0.0046 0.1067  87  GLU B O   
4354  C CB  . GLU B 87  ? 0.3964 0.2319 0.4141 0.0342  -0.0007 0.0942  87  GLU B CB  
4355  C CG  . GLU B 87  ? 0.5039 0.3346 0.5153 0.0228  -0.0019 0.0924  87  GLU B CG  
4356  C CD  . GLU B 87  ? 0.5758 0.4094 0.5874 0.0166  -0.0018 0.0866  87  GLU B CD  
4357  O OE1 . GLU B 87  ? 0.5969 0.4282 0.6105 0.0208  -0.0002 0.0832  87  GLU B OE1 
4358  O OE2 . GLU B 87  ? 0.5580 0.3974 0.5687 0.0078  -0.0032 0.0859  87  GLU B OE2 
4359  N N   . LEU B 88  ? 0.3447 0.2212 0.3717 0.0321  -0.0072 0.1041  88  LEU B N   
4360  C CA  . LEU B 88  ? 0.3381 0.2262 0.3650 0.0257  -0.0098 0.1059  88  LEU B CA  
4361  C C   . LEU B 88  ? 0.3454 0.2387 0.3741 0.0293  -0.0109 0.1127  88  LEU B C   
4362  O O   . LEU B 88  ? 0.3171 0.2061 0.3417 0.0255  -0.0114 0.1154  88  LEU B O   
4363  C CB  . LEU B 88  ? 0.3222 0.2306 0.3541 0.0223  -0.0121 0.1029  88  LEU B CB  
4364  C CG  . LEU B 88  ? 0.3613 0.2682 0.3912 0.0163  -0.0118 0.0972  88  LEU B CG  
4365  C CD1 . LEU B 88  ? 0.2909 0.2175 0.3246 0.0130  -0.0144 0.0952  88  LEU B CD1 
4366  C CD2 . LEU B 88  ? 0.3779 0.2721 0.4017 0.0097  -0.0110 0.0967  88  LEU B CD2 
4367  N N   . PHE B 89  ? 0.3453 0.2490 0.3807 0.0364  -0.0113 0.1160  89  PHE B N   
4368  C CA  . PHE B 89  ? 0.3727 0.2870 0.4117 0.0391  -0.0130 0.1228  89  PHE B CA  
4369  C C   . PHE B 89  ? 0.3810 0.2851 0.4207 0.0479  -0.0111 0.1285  89  PHE B C   
4370  O O   . PHE B 89  ? 0.3445 0.2546 0.3861 0.0500  -0.0124 0.1350  89  PHE B O   
4371  C CB  . PHE B 89  ? 0.3458 0.2841 0.3928 0.0391  -0.0154 0.1236  89  PHE B CB  
4372  C CG  . PHE B 89  ? 0.2960 0.2432 0.3425 0.0318  -0.0169 0.1177  89  PHE B CG  
4373  C CD1 . PHE B 89  ? 0.3152 0.2641 0.3575 0.0245  -0.0185 0.1163  89  PHE B CD1 
4374  C CD2 . PHE B 89  ? 0.3264 0.2805 0.3766 0.0326  -0.0165 0.1139  89  PHE B CD2 
4375  C CE1 . PHE B 89  ? 0.3058 0.2627 0.3476 0.0187  -0.0196 0.1111  89  PHE B CE1 
4376  C CE2 . PHE B 89  ? 0.2743 0.2356 0.3234 0.0263  -0.0178 0.1088  89  PHE B CE2 
4377  C CZ  . PHE B 89  ? 0.2864 0.2489 0.3313 0.0196  -0.0194 0.1073  89  PHE B CZ  
4378  N N   . ASN B 90  ? 0.3921 0.2806 0.4302 0.0532  -0.0079 0.1262  90  ASN B N   
4379  C CA  . ASN B 90  ? 0.3723 0.2514 0.4121 0.0632  -0.0052 0.1310  90  ASN B CA  
4380  C C   . ASN B 90  ? 0.3908 0.2918 0.4418 0.0705  -0.0053 0.1358  90  ASN B C   
4381  O O   . ASN B 90  ? 0.4070 0.3081 0.4615 0.0786  -0.0039 0.1425  90  ASN B O   
4382  C CB  . ASN B 90  ? 0.3721 0.2375 0.4061 0.0635  -0.0054 0.1366  90  ASN B CB  
4383  C CG  . ASN B 90  ? 0.4873 0.3337 0.5200 0.0729  -0.0017 0.1394  90  ASN B CG  
4384  O OD1 . ASN B 90  ? 0.4814 0.3146 0.5126 0.0760  0.0016  0.1346  90  ASN B OD1 
4385  N ND2 . ASN B 90  ? 0.5251 0.3698 0.5583 0.0777  -0.0018 0.1474  90  ASN B ND2 
4386  N N   . TYR B 91  ? 0.4141 0.3338 0.4706 0.0676  -0.0068 0.1328  91  TYR B N   
4387  C CA  . TYR B 91  ? 0.3598 0.3017 0.4267 0.0727  -0.0070 0.1372  91  TYR B CA  
4388  C C   . TYR B 91  ? 0.3744 0.3143 0.4449 0.0795  -0.0029 0.1343  91  TYR B C   
4389  O O   . TYR B 91  ? 0.3382 0.2677 0.4045 0.0768  -0.0016 0.1272  91  TYR B O   
4390  C CB  . TYR B 91  ? 0.2656 0.2291 0.3358 0.0645  -0.0111 0.1363  91  TYR B CB  
4391  C CG  . TYR B 91  ? 0.3244 0.2942 0.3927 0.0592  -0.0146 0.1405  91  TYR B CG  
4392  C CD1 . TYR B 91  ? 0.3216 0.2769 0.3845 0.0605  -0.0142 0.1438  91  TYR B CD1 
4393  C CD2 . TYR B 91  ? 0.3153 0.3049 0.3868 0.0526  -0.0182 0.1411  91  TYR B CD2 
4394  C CE1 . TYR B 91  ? 0.3284 0.2898 0.3894 0.0559  -0.0171 0.1478  91  TYR B CE1 
4395  C CE2 . TYR B 91  ? 0.2960 0.2911 0.3653 0.0479  -0.0211 0.1447  91  TYR B CE2 
4396  C CZ  . TYR B 91  ? 0.3161 0.2978 0.3806 0.0498  -0.0205 0.1482  91  TYR B CZ  
4397  O OH  . TYR B 91  ? 0.2895 0.2769 0.3517 0.0453  -0.0232 0.1520  91  TYR B OH  
4398  N N   . ASP B 92  ? 0.3913 0.3419 0.4699 0.0887  -0.0006 0.1402  92  ASP B N   
4399  C CA  . ASP B 92  ? 0.3324 0.2796 0.4142 0.0973  0.0045  0.1383  92  ASP B CA  
4400  C C   . ASP B 92  ? 0.3584 0.3279 0.4480 0.0965  0.0043  0.1375  92  ASP B C   
4401  O O   . ASP B 92  ? 0.3121 0.2796 0.4038 0.1026  0.0087  0.1350  92  ASP B O   
4402  C CB  . ASP B 92  ? 0.3578 0.3019 0.4435 0.1093  0.0086  0.1455  92  ASP B CB  
4403  C CG  . ASP B 92  ? 0.4725 0.3885 0.5492 0.1115  0.0104  0.1452  92  ASP B CG  
4404  O OD1 . ASP B 92  ? 0.4388 0.3344 0.5064 0.1061  0.0107  0.1378  92  ASP B OD1 
4405  O OD2 . ASP B 92  ? 0.4516 0.3657 0.5300 0.1183  0.0117  0.1526  92  ASP B OD2 
4406  N N   . TYR B 93  ? 0.2991 0.2888 0.3924 0.0889  -0.0004 0.1394  93  TYR B N   
4407  C CA  . TYR B 93  ? 0.3301 0.3415 0.4307 0.0875  -0.0009 0.1398  93  TYR B CA  
4408  C C   . TYR B 93  ? 0.3219 0.3391 0.4191 0.0755  -0.0054 0.1349  93  TYR B C   
4409  O O   . TYR B 93  ? 0.2979 0.3139 0.3909 0.0686  -0.0091 0.1350  93  TYR B O   
4410  C CB  . TYR B 93  ? 0.3196 0.3541 0.4296 0.0909  -0.0017 0.1493  93  TYR B CB  
4411  C CG  . TYR B 93  ? 0.3259 0.3580 0.4403 0.1037  0.0031  0.1555  93  TYR B CG  
4412  C CD1 . TYR B 93  ? 0.3217 0.3519 0.4392 0.1128  0.0089  0.1544  93  TYR B CD1 
4413  C CD2 . TYR B 93  ? 0.3341 0.3665 0.4495 0.1071  0.0022  0.1628  93  TYR B CD2 
4414  C CE1 . TYR B 93  ? 0.3647 0.3924 0.4858 0.1252  0.0140  0.1601  93  TYR B CE1 
4415  C CE2 . TYR B 93  ? 0.3806 0.4106 0.4999 0.1194  0.0070  0.1689  93  TYR B CE2 
4416  C CZ  . TYR B 93  ? 0.3773 0.4048 0.4994 0.1286  0.0130  0.1675  93  TYR B CZ  
4417  O OH  . TYR B 93  ? 0.4427 0.4674 0.5684 0.1417  0.0185  0.1736  93  TYR B OH  
4418  N N   . ILE B 94  ? 0.2616 0.2851 0.3605 0.0736  -0.0047 0.1309  94  ILE B N   
4419  C CA  . ILE B 94  ? 0.2532 0.2824 0.3490 0.0630  -0.0084 0.1265  94  ILE B CA  
4420  C C   . ILE B 94  ? 0.2117 0.2609 0.3140 0.0616  -0.0087 0.1283  94  ILE B C   
4421  O O   . ILE B 94  ? 0.2431 0.2974 0.3507 0.0687  -0.0049 0.1298  94  ILE B O   
4422  C CB  . ILE B 94  ? 0.2493 0.2603 0.3370 0.0599  -0.0077 0.1181  94  ILE B CB  
4423  C CG1 . ILE B 94  ? 0.2633 0.2705 0.3528 0.0660  -0.0033 0.1150  94  ILE B CG1 
4424  C CG2 . ILE B 94  ? 0.3030 0.2942 0.3838 0.0604  -0.0073 0.1168  94  ILE B CG2 
4425  C CD1 . ILE B 94  ? 0.2408 0.2438 0.3257 0.0601  -0.0040 0.1081  94  ILE B CD1 
4426  N N   . ILE B 95  ? 0.1763 0.2365 0.2777 0.0520  -0.0129 0.1281  95  ILE B N   
4427  C CA  . ILE B 95  ? 0.1752 0.2517 0.2804 0.0478  -0.0138 0.1288  95  ILE B CA  
4428  C C   . ILE B 95  ? 0.2038 0.2752 0.3017 0.0380  -0.0168 0.1227  95  ILE B C   
4429  O O   . ILE B 95  ? 0.1913 0.2646 0.2857 0.0311  -0.0204 0.1232  95  ILE B O   
4430  C CB  . ILE B 95  ? 0.2006 0.2991 0.3125 0.0456  -0.0162 0.1370  95  ILE B CB  
4431  C CG1 . ILE B 95  ? 0.2204 0.3244 0.3394 0.0558  -0.0132 0.1439  95  ILE B CG1 
4432  C CG2 . ILE B 95  ? 0.1742 0.2887 0.2894 0.0407  -0.0170 0.1380  95  ILE B CG2 
4433  C CD1 . ILE B 95  ? 0.2190 0.3461 0.3447 0.0534  -0.0158 0.1527  95  ILE B CD1 
4434  N N   . PRO B 96  ? 0.2101 0.2751 0.3051 0.0374  -0.0153 0.1171  96  PRO B N   
4435  C CA  . PRO B 96  ? 0.2400 0.3017 0.3282 0.0285  -0.0180 0.1121  96  PRO B CA  
4436  C C   . PRO B 96  ? 0.1698 0.2478 0.2596 0.0209  -0.0214 0.1157  96  PRO B C   
4437  O O   . PRO B 96  ? 0.1776 0.2714 0.2745 0.0220  -0.0214 0.1216  96  PRO B O   
4438  C CB  . PRO B 96  ? 0.1847 0.2398 0.2712 0.0307  -0.0154 0.1072  96  PRO B CB  
4439  C CG  . PRO B 96  ? 0.1838 0.2445 0.2777 0.0395  -0.0116 0.1106  96  PRO B CG  
4440  C CD  . PRO B 96  ? 0.1817 0.2425 0.2793 0.0450  -0.0109 0.1153  96  PRO B CD  
4441  N N   . ALA B 97  ? 0.1464 0.2204 0.2291 0.0130  -0.0244 0.1124  97  ALA B N   
4442  C CA  . ALA B 97  ? 0.1688 0.2540 0.2500 0.0044  -0.0277 0.1144  97  ALA B CA  
4443  C C   . ALA B 97  ? 0.1553 0.2303 0.2278 -0.0006 -0.0282 0.1077  97  ALA B C   
4444  O O   . ALA B 97  ? 0.1727 0.2336 0.2403 0.0018  -0.0265 0.1021  97  ALA B O   
4445  C CB  . ALA B 97  ? 0.1384 0.2295 0.2185 -0.0002 -0.0312 0.1182  97  ALA B CB  
4446  N N   . HIS B 98  ? 0.1695 0.2517 0.2395 -0.0077 -0.0306 0.1086  98  HIS B N   
4447  C CA  . HIS B 98  ? 0.1736 0.2452 0.2344 -0.0116 -0.0306 0.1025  98  HIS B CA  
4448  C C   . HIS B 98  ? 0.1748 0.2355 0.2265 -0.0146 -0.0318 0.0982  98  HIS B C   
4449  O O   . HIS B 98  ? 0.2124 0.2614 0.2567 -0.0146 -0.0304 0.0923  98  HIS B O   
4450  C CB  . HIS B 98  ? 0.2123 0.2924 0.2713 -0.0187 -0.0328 0.1045  98  HIS B CB  
4451  C CG  . HIS B 98  ? 0.2236 0.3096 0.2777 -0.0279 -0.0371 0.1070  98  HIS B CG  
4452  N ND1 . HIS B 98  ? 0.2123 0.3151 0.2733 -0.0310 -0.0396 0.1142  98  HIS B ND1 
4453  C CD2 . HIS B 98  ? 0.1810 0.2580 0.2230 -0.0347 -0.0393 0.1030  98  HIS B CD2 
4454  C CE1 . HIS B 98  ? 0.2148 0.3192 0.2682 -0.0404 -0.0437 0.1146  98  HIS B CE1 
4455  N NE2 . HIS B 98  ? 0.2109 0.2988 0.2521 -0.0426 -0.0435 0.1076  98  HIS B NE2 
4456  N N   . GLN B 99  ? 0.1866 0.2516 0.2388 -0.0167 -0.0341 0.1013  99  GLN B N   
4457  C CA  . GLN B 99  ? 0.1721 0.2277 0.2170 -0.0180 -0.0345 0.0980  99  GLN B CA  
4458  C C   . GLN B 99  ? 0.1518 0.2161 0.2000 -0.0194 -0.0370 0.1036  99  GLN B C   
4459  O O   . GLN B 99  ? 0.1338 0.2107 0.1903 -0.0184 -0.0378 0.1097  99  GLN B O   
4460  C CB  . GLN B 99  ? 0.1828 0.2307 0.2158 -0.0236 -0.0353 0.0935  99  GLN B CB  
4461  C CG  . GLN B 99  ? 0.1916 0.2472 0.2206 -0.0320 -0.0391 0.0964  99  GLN B CG  
4462  C CD  . GLN B 99  ? 0.2006 0.2444 0.2156 -0.0365 -0.0388 0.0911  99  GLN B CD  
4463  O OE1 . GLN B 99  ? 0.2323 0.2684 0.2438 -0.0346 -0.0362 0.0872  99  GLN B OE1 
4464  N NE2 . GLN B 99  ? 0.2017 0.2430 0.2075 -0.0421 -0.0410 0.0910  99  GLN B NE2 
4465  N N   . GLY B 100 ? 0.1574 0.4870 0.2014 0.0022  -0.0159 0.1366  100 GLY B N   
4466  C CA  . GLY B 100 ? 0.1588 0.4927 0.2058 -0.0009 -0.0155 0.1423  100 GLY B CA  
4467  C C   . GLY B 100 ? 0.1599 0.4920 0.2107 -0.0015 -0.0165 0.1460  100 GLY B C   
4468  O O   . GLY B 100 ? 0.1621 0.4947 0.2174 -0.0017 -0.0160 0.1528  100 GLY B O   
4469  N N   . ARG B 101 ? 0.1609 0.4898 0.2087 -0.0020 -0.0192 0.1418  101 ARG B N   
4470  C CA  . ARG B 101 ? 0.1635 0.4914 0.2144 -0.0042 -0.0214 0.1457  101 ARG B CA  
4471  C C   . ARG B 101 ? 0.1622 0.4916 0.2206 -0.0034 -0.0197 0.1519  101 ARG B C   
4472  O O   . ARG B 101 ? 0.1640 0.4971 0.2276 -0.0053 -0.0207 0.1570  101 ARG B O   
4473  C CB  . ARG B 101 ? 0.1691 0.4911 0.2123 -0.0055 -0.0270 0.1398  101 ARG B CB  
4474  C CG  . ARG B 101 ? 0.1720 0.4856 0.2107 -0.0048 -0.0299 0.1367  101 ARG B CG  
4475  C CD  . ARG B 101 ? 0.1995 0.5033 0.2262 -0.0036 -0.0374 0.1288  101 ARG B CD  
4476  N NE  . ARG B 101 ? 0.1975 0.5042 0.2184 0.0018  -0.0368 0.1205  101 ARG B NE  
4477  C CZ  . ARG B 101 ? 0.1918 0.4924 0.2016 0.0065  -0.0430 0.1117  101 ARG B CZ  
4478  N NH1 . ARG B 101 ? 0.2047 0.4921 0.2056 0.0061  -0.0515 0.1101  101 ARG B NH1 
4479  N NH2 . ARG B 101 ? 0.1907 0.4991 0.1976 0.0122  -0.0413 0.1042  101 ARG B NH2 
4480  N N   . GLY B 102 ? 0.1600 0.4890 0.2187 -0.0005 -0.0171 0.1516  102 GLY B N   
4481  C CA  . GLY B 102 ? 0.1593 0.4949 0.2255 0.0020  -0.0141 0.1579  102 GLY B CA  
4482  C C   . GLY B 102 ? 0.1604 0.4991 0.2318 0.0073  -0.0115 0.1625  102 GLY B C   
4483  O O   . GLY B 102 ? 0.1622 0.5084 0.2411 0.0104  -0.0102 0.1679  102 GLY B O   
4484  N N   . ALA B 103 ? 0.1616 0.4948 0.2284 0.0084  -0.0116 0.1606  103 ALA B N   
4485  C CA  . ALA B 103 ? 0.1677 0.4987 0.2360 0.0122  -0.0118 0.1658  103 ALA B CA  
4486  C C   . ALA B 103 ? 0.2112 0.5443 0.2830 0.0098  -0.0141 0.1696  103 ALA B C   
4487  O O   . ALA B 103 ? 0.2083 0.5411 0.2841 0.0150  -0.0149 0.1750  103 ALA B O   
4488  C CB  . ALA B 103 ? 0.1719 0.4947 0.2320 0.0096  -0.0123 0.1636  103 ALA B CB  
4489  N N   . GLU B 104 ? 0.1679 0.5023 0.2372 0.0032  -0.0160 0.1665  104 GLU B N   
4490  C CA  . GLU B 104 ? 0.1781 0.5144 0.2494 0.0008  -0.0187 0.1699  104 GLU B CA  
4491  C C   . GLU B 104 ? 0.1718 0.5145 0.2511 0.0024  -0.0189 0.1733  104 GLU B C   
4492  O O   . GLU B 104 ? 0.1998 0.5453 0.2835 0.0042  -0.0206 0.1782  104 GLU B O   
4493  C CB  . GLU B 104 ? 0.1802 0.5165 0.2449 -0.0053 -0.0211 0.1649  104 GLU B CB  
4494  C CG  . GLU B 104 ? 0.2171 0.5536 0.2751 -0.0076 -0.0206 0.1628  104 GLU B CG  
4495  C CD  . GLU B 104 ? 0.2444 0.5845 0.2952 -0.0105 -0.0218 0.1555  104 GLU B CD  
4496  O OE1 . GLU B 104 ? 0.2130 0.5504 0.2619 -0.0099 -0.0239 0.1510  104 GLU B OE1 
4497  O OE2 . GLU B 104 ? 0.2726 0.6188 0.3187 -0.0132 -0.0212 0.1544  104 GLU B OE2 
4498  N N   . ASN B 105 ? 0.1677 0.5138 0.2483 0.0012  -0.0176 0.1715  105 ASN B N   
4499  C CA  . ASN B 105 ? 0.1689 0.5250 0.2568 0.0004  -0.0178 0.1760  105 ASN B CA  
4500  C C   . ASN B 105 ? 0.1865 0.5513 0.2825 0.0094  -0.0142 0.1805  105 ASN B C   
4501  O O   . ASN B 105 ? 0.2006 0.5760 0.3039 0.0110  -0.0147 0.1850  105 ASN B O   
4502  C CB  . ASN B 105 ? 0.1667 0.5242 0.2523 -0.0048 -0.0184 0.1742  105 ASN B CB  
4503  C CG  . ASN B 105 ? 0.2315 0.6018 0.3238 -0.0093 -0.0198 0.1804  105 ASN B CG  
4504  O OD1 . ASN B 105 ? 0.2535 0.6292 0.3502 -0.0108 -0.0221 0.1840  105 ASN B OD1 
4505  N ND2 . ASN B 105 ? 0.1815 0.5583 0.2742 -0.0124 -0.0188 0.1823  105 ASN B ND2 
4506  N N   . ILE B 106 ? 0.1818 0.5425 0.2762 0.0164  -0.0113 0.1789  106 ILE B N   
4507  C CA  . ILE B 106 ? 0.1763 0.5428 0.2768 0.0280  -0.0089 0.1816  106 ILE B CA  
4508  C C   . ILE B 106 ? 0.2144 0.5767 0.3167 0.0328  -0.0126 0.1850  106 ILE B C   
4509  O O   . ILE B 106 ? 0.2513 0.6236 0.3614 0.0396  -0.0127 0.1879  106 ILE B O   
4510  C CB  . ILE B 106 ? 0.1769 0.5364 0.2727 0.0344  -0.0067 0.1787  106 ILE B CB  
4511  C CG1 . ILE B 106 ? 0.1738 0.5406 0.2692 0.0321  -0.0029 0.1762  106 ILE B CG1 
4512  C CG2 . ILE B 106 ? 0.2181 0.5779 0.3172 0.0490  -0.0061 0.1806  106 ILE B CG2 
4513  C CD1 . ILE B 106 ? 0.1786 0.5335 0.2666 0.0377  0.0008  0.1705  106 ILE B CD1 
4514  N N   . LEU B 107 ? 0.1885 0.5367 0.2827 0.0291  -0.0162 0.1850  107 LEU B N   
4515  C CA  . LEU B 107 ? 0.2016 0.5403 0.2933 0.0341  -0.0208 0.1892  107 LEU B CA  
4516  C C   . LEU B 107 ? 0.2094 0.5508 0.3029 0.0289  -0.0248 0.1919  107 LEU B C   
4517  O O   . LEU B 107 ? 0.2427 0.5828 0.3386 0.0360  -0.0284 0.1959  107 LEU B O   
4518  C CB  . LEU B 107 ? 0.2081 0.5295 0.2874 0.0309  -0.0230 0.1896  107 LEU B CB  
4519  C CG  . LEU B 107 ? 0.2275 0.5325 0.2987 0.0341  -0.0291 0.1954  107 LEU B CG  
4520  C CD1 . LEU B 107 ? 0.2416 0.5401 0.3138 0.0499  -0.0309 0.1975  107 LEU B CD1 
4521  C CD2 . LEU B 107 ? 0.2342 0.5245 0.2914 0.0245  -0.0309 0.1966  107 LEU B CD2 
4522  N N   . PHE B 108 ? 0.2003 0.5440 0.2912 0.0179  -0.0250 0.1895  108 PHE B N   
4523  C CA  . PHE B 108 ? 0.2022 0.5460 0.2921 0.0135  -0.0296 0.1921  108 PHE B CA  
4524  C C   . PHE B 108 ? 0.2067 0.5628 0.3066 0.0170  -0.0311 0.1950  108 PHE B C   
4525  O O   . PHE B 108 ? 0.2148 0.5696 0.3154 0.0197  -0.0357 0.1989  108 PHE B O   
4526  C CB  . PHE B 108 ? 0.1963 0.5397 0.2800 0.0030  -0.0303 0.1879  108 PHE B CB  
4527  C CG  . PHE B 108 ? 0.2395 0.5751 0.3133 -0.0010 -0.0298 0.1854  108 PHE B CG  
4528  C CD1 . PHE B 108 ? 0.2070 0.5342 0.2770 0.0023  -0.0295 0.1881  108 PHE B CD1 
4529  C CD2 . PHE B 108 ? 0.2459 0.5830 0.3133 -0.0079 -0.0303 0.1805  108 PHE B CD2 
4530  C CE1 . PHE B 108 ? 0.2472 0.5699 0.3081 -0.0036 -0.0291 0.1868  108 PHE B CE1 
4531  C CE2 . PHE B 108 ? 0.2654 0.6008 0.3247 -0.0115 -0.0292 0.1782  108 PHE B CE2 
4532  C CZ  . PHE B 108 ? 0.2288 0.5583 0.2856 -0.0106 -0.0284 0.1818  108 PHE B CZ  
4533  N N   . PRO B 109 ? 0.2029 0.5716 0.3098 0.0162  -0.0278 0.1941  109 PRO B N   
4534  C CA  . PRO B 109 ? 0.2021 0.5861 0.3191 0.0194  -0.0290 0.1977  109 PRO B CA  
4535  C C   . PRO B 109 ? 0.2117 0.5990 0.3347 0.0339  -0.0291 0.1998  109 PRO B C   
4536  O O   . PRO B 109 ? 0.2202 0.6155 0.3493 0.0385  -0.0329 0.2028  109 PRO B O   
4537  C CB  . PRO B 109 ? 0.2049 0.6011 0.3256 0.0145  -0.0251 0.1970  109 PRO B CB  
4538  C CG  . PRO B 109 ? 0.1875 0.5716 0.2986 0.0060  -0.0247 0.1927  109 PRO B CG  
4539  C CD  . PRO B 109 ? 0.2146 0.5846 0.3192 0.0105  -0.0241 0.1902  109 PRO B CD  
4540  N N   . VAL B 110 ? 0.2150 0.5954 0.3356 0.0424  -0.0260 0.1979  110 VAL B N   
4541  C CA  . VAL B 110 ? 0.2295 0.6081 0.3529 0.0585  -0.0277 0.1989  110 VAL B CA  
4542  C C   . VAL B 110 ? 0.2409 0.6021 0.3570 0.0609  -0.0357 0.2024  110 VAL B C   
4543  O O   . VAL B 110 ? 0.2552 0.6178 0.3748 0.0721  -0.0403 0.2043  110 VAL B O   
4544  C CB  . VAL B 110 ? 0.2264 0.5980 0.3460 0.0666  -0.0236 0.1958  110 VAL B CB  
4545  C CG1 . VAL B 110 ? 0.2538 0.6126 0.3698 0.0836  -0.0280 0.1965  110 VAL B CG1 
4546  C CG2 . VAL B 110 ? 0.2171 0.6094 0.3448 0.0678  -0.0160 0.1930  110 VAL B CG2 
4547  N N   . LEU B 111 ? 0.2396 0.5850 0.3445 0.0502  -0.0379 0.2032  111 LEU B N   
4548  C CA  . LEU B 111 ? 0.2561 0.5843 0.3511 0.0498  -0.0456 0.2076  111 LEU B CA  
4549  C C   . LEU B 111 ? 0.2598 0.5973 0.3598 0.0478  -0.0501 0.2100  111 LEU B C   
4550  O O   . LEU B 111 ? 0.2913 0.6196 0.3877 0.0548  -0.0573 0.2138  111 LEU B O   
4551  C CB  . LEU B 111 ? 0.2538 0.5684 0.3359 0.0370  -0.0456 0.2077  111 LEU B CB  
4552  C CG  . LEU B 111 ? 0.2550 0.5574 0.3295 0.0382  -0.0431 0.2065  111 LEU B CG  
4553  C CD1 . LEU B 111 ? 0.2530 0.5473 0.3160 0.0242  -0.0427 0.2064  111 LEU B CD1 
4554  C CD2 . LEU B 111 ? 0.2782 0.5618 0.3459 0.0512  -0.0487 0.2105  111 LEU B CD2 
4555  N N   . LEU B 112 ? 0.2456 0.5990 0.3522 0.0382  -0.0472 0.2080  112 LEU B N   
4556  C CA  . LEU B 112 ? 0.2504 0.6130 0.3614 0.0357  -0.0521 0.2105  112 LEU B CA  
4557  C C   . LEU B 112 ? 0.2583 0.6354 0.3814 0.0485  -0.0537 0.2119  112 LEU B C   
4558  O O   . LEU B 112 ? 0.2722 0.6489 0.3962 0.0538  -0.0607 0.2149  112 LEU B O   
4559  C CB  . LEU B 112 ? 0.2374 0.6104 0.3502 0.0226  -0.0499 0.2082  112 LEU B CB  
4560  C CG  . LEU B 112 ? 0.2648 0.6510 0.3842 0.0198  -0.0548 0.2108  112 LEU B CG  
4561  C CD1 . LEU B 112 ? 0.3322 0.7084 0.4443 0.0196  -0.0625 0.2137  112 LEU B CD1 
4562  C CD2 . LEU B 112 ? 0.2545 0.6475 0.3738 0.0071  -0.0538 0.2088  112 LEU B CD2 
4563  N N   . LYS B 113 ? 0.2539 0.6454 0.3863 0.0541  -0.0473 0.2094  113 LYS B N   
4564  C CA  . LYS B 113 ? 0.2878 0.6971 0.4322 0.0677  -0.0476 0.2095  113 LYS B CA  
4565  C C   . LYS B 113 ? 0.2797 0.6737 0.4197 0.0847  -0.0539 0.2101  113 LYS B C   
4566  O O   . LYS B 113 ? 0.2934 0.6961 0.4401 0.0955  -0.0591 0.2110  113 LYS B O   
4567  C CB  . LYS B 113 ? 0.2495 0.6753 0.4012 0.0706  -0.0387 0.2063  113 LYS B CB  
4568  C CG  . LYS B 113 ? 0.2900 0.7419 0.4553 0.0824  -0.0370 0.2057  113 LYS B CG  
4569  C CD  . LYS B 113 ? 0.3514 0.8254 0.5254 0.0714  -0.0386 0.2092  113 LYS B CD  
4570  C CE  . LYS B 113 ? 0.4157 0.9216 0.6033 0.0792  -0.0344 0.2086  113 LYS B CE  
4571  N NZ  . LYS B 113 ? 0.4275 0.9380 0.6210 0.1012  -0.0373 0.2058  113 LYS B NZ  
4572  N N   . TYR B 114 ? 0.2849 0.6546 0.4125 0.0872  -0.0545 0.2098  114 TYR B N   
4573  C CA  . TYR B 114 ? 0.3098 0.6582 0.4289 0.1032  -0.0621 0.2110  114 TYR B CA  
4574  C C   . TYR B 114 ? 0.3588 0.6928 0.4697 0.1015  -0.0727 0.2161  114 TYR B C   
4575  O O   . TYR B 114 ? 0.4534 0.7831 0.5647 0.1164  -0.0806 0.2170  114 TYR B O   
4576  C CB  . TYR B 114 ? 0.3282 0.6517 0.4332 0.1028  -0.0611 0.2108  114 TYR B CB  
4577  C CG  . TYR B 114 ? 0.4546 0.7490 0.5461 0.1187  -0.0699 0.2126  114 TYR B CG  
4578  C CD1 . TYR B 114 ? 0.5004 0.7963 0.5954 0.1392  -0.0692 0.2078  114 TYR B CD1 
4579  C CD2 . TYR B 114 ? 0.4846 0.7478 0.5572 0.1129  -0.0792 0.2188  114 TYR B CD2 
4580  C CE1 . TYR B 114 ? 0.5563 0.8199 0.6357 0.1549  -0.0788 0.2088  114 TYR B CE1 
4581  C CE2 . TYR B 114 ? 0.5172 0.7475 0.5734 0.1261  -0.0890 0.2214  114 TYR B CE2 
4582  C CZ  . TYR B 114 ? 0.6029 0.8317 0.6621 0.1478  -0.0894 0.2161  114 TYR B CZ  
4583  O OH  . TYR B 114 ? 0.7318 0.9226 0.7717 0.1622  -0.1006 0.2180  114 TYR B OH  
4584  N N   . LYS B 115 ? 0.3212 0.6479 0.4240 0.0842  -0.0734 0.2190  115 LYS B N   
4585  C CA  . LYS B 115 ? 0.3932 0.7070 0.4865 0.0811  -0.0829 0.2239  115 LYS B CA  
4586  C C   . LYS B 115 ? 0.5032 0.8391 0.6097 0.0845  -0.0862 0.2240  115 LYS B C   
4587  O O   . LYS B 115 ? 0.5278 0.8542 0.6287 0.0897  -0.0960 0.2276  115 LYS B O   
4588  C CB  . LYS B 115 ? 0.3287 0.6338 0.4104 0.0620  -0.0813 0.2257  115 LYS B CB  
4589  C CG  . LYS B 115 ? 0.4053 0.6881 0.4696 0.0582  -0.0907 0.2317  115 LYS B CG  
4590  C CD  . LYS B 115 ? 0.4578 0.7089 0.5047 0.0643  -0.0964 0.2357  115 LYS B CD  
4591  C CE  . LYS B 115 ? 0.4386 0.6651 0.4649 0.0585  -0.1060 0.2428  115 LYS B CE  
4592  N NZ  . LYS B 115 ? 0.3955 0.6240 0.4133 0.0386  -0.1015 0.2437  115 LYS B NZ  
4593  N N   . GLN B 116 ? 0.4352 0.7996 0.5579 0.0810  -0.0789 0.2208  116 GLN B N   
4594  C CA  . GLN B 116 ? 0.4591 0.8465 0.5943 0.0811  -0.0819 0.2216  116 GLN B CA  
4595  C C   . GLN B 116 ? 0.5217 0.9186 0.6663 0.1010  -0.0871 0.2209  116 GLN B C   
4596  O O   . GLN B 116 ? 0.6415 1.0548 0.7949 0.1029  -0.0923 0.2223  116 GLN B O   
4597  C CB  . GLN B 116 ? 0.3795 0.7922 0.5266 0.0698  -0.0735 0.2195  116 GLN B CB  
4598  C CG  . GLN B 116 ? 0.3269 0.7368 0.4676 0.0510  -0.0735 0.2205  116 GLN B CG  
4599  C CD  . GLN B 116 ? 0.3221 0.7498 0.4703 0.0400  -0.0666 0.2188  116 GLN B CD  
4600  O OE1 . GLN B 116 ? 0.3432 0.7845 0.4998 0.0449  -0.0603 0.2172  116 GLN B OE1 
4601  N NE2 . GLN B 116 ? 0.3284 0.7544 0.4715 0.0254  -0.0685 0.2192  116 GLN B NE2 
4602  N N   . LYS B 117 ? 0.4914 0.8791 0.6342 0.1166  -0.0863 0.2182  117 LYS B N   
4603  C CA  . LYS B 117 ? 0.6835 1.0779 0.8335 0.1382  -0.0923 0.2162  117 LYS B CA  
4604  C C   . LYS B 117 ? 0.8162 1.1896 0.9555 0.1435  -0.1066 0.2206  117 LYS B C   
4605  O O   . LYS B 117 ? 0.7964 1.1414 0.9176 0.1340  -0.1115 0.2251  117 LYS B O   
4606  C CB  . LYS B 117 ? 0.6889 1.0709 0.8348 0.1550  -0.0900 0.2118  117 LYS B CB  
4607  C CG  . LYS B 117 ? 0.7519 1.0897 0.8748 0.1583  -0.0980 0.2147  117 LYS B CG  
4608  C CD  . LYS B 117 ? 0.6476 0.9728 0.7655 0.1732  -0.0949 0.2099  117 LYS B CD  
4609  C CE  . LYS B 117 ? 0.6036 0.8813 0.6958 0.1743  -0.1040 0.2141  117 LYS B CE  
4610  N NZ  . LYS B 117 ? 0.6268 0.8888 0.7119 0.1888  -0.1019 0.2093  117 LYS B NZ  
4611  N N   . GLU B 118 ? 1.0176 1.4067 1.1679 0.1583  -0.1132 0.2194  118 GLU B N   
4612  C CA  . GLU B 118 ? 1.0441 1.4170 1.1859 0.1642  -0.1279 0.2234  118 GLU B CA  
4613  C C   . GLU B 118 ? 1.0336 1.4075 1.1707 0.1436  -0.1297 0.2286  118 GLU B C   
4614  O O   . GLU B 118 ? 1.0853 1.4336 1.2056 0.1418  -0.1402 0.2333  118 GLU B O   
4615  C CB  . GLU B 118 ? 1.1135 1.4411 1.2320 0.1752  -0.1386 0.2257  118 GLU B CB  
4616  C CG  . GLU B 118 ? 1.1736 1.4955 1.2948 0.2014  -0.1432 0.2205  118 GLU B CG  
4617  C CD  . GLU B 118 ? 1.2307 1.5010 1.3249 0.2104  -0.1554 0.2237  118 GLU B CD  
4618  O OE1 . GLU B 118 ? 1.1438 1.3892 1.2210 0.1974  -0.1520 0.2270  118 GLU B OE1 
4619  O OE2 . GLU B 118 ? 1.1804 1.4340 1.2698 0.2296  -0.1691 0.2234  118 GLU B OE2 
4620  N N   . GLY B 119 ? 0.8053 1.2066 0.9550 0.1280  -0.1200 0.2277  119 GLY B N   
4621  C CA  . GLY B 119 ? 0.7114 1.1181 0.8592 0.1111  -0.1224 0.2312  119 GLY B CA  
4622  C C   . GLY B 119 ? 0.7505 1.1294 0.8777 0.0960  -0.1228 0.2343  119 GLY B C   
4623  O O   . GLY B 119 ? 0.6182 0.9993 0.7415 0.0832  -0.1255 0.2366  119 GLY B O   
4624  N N   . LYS B 120 ? 0.8646 1.2187 0.9783 0.0970  -0.1202 0.2343  120 LYS B N   
4625  C CA  . LYS B 120 ? 0.7840 1.1157 0.8790 0.0818  -0.1191 0.2370  120 LYS B CA  
4626  C C   . LYS B 120 ? 0.7211 1.0683 0.8220 0.0649  -0.1082 0.2338  120 LYS B C   
4627  O O   . LYS B 120 ? 0.7219 1.0936 0.8391 0.0640  -0.1020 0.2306  120 LYS B O   
4628  C CB  . LYS B 120 ? 0.7781 1.0799 0.8570 0.0869  -0.1200 0.2384  120 LYS B CB  
4629  C CG  . LYS B 120 ? 0.8960 1.1760 0.9657 0.1053  -0.1324 0.2412  120 LYS B CG  
4630  C CD  . LYS B 120 ? 0.9261 1.1723 0.9769 0.1085  -0.1340 0.2433  120 LYS B CD  
4631  C CE  . LYS B 120 ? 0.8258 1.0823 0.8875 0.1121  -0.1233 0.2378  120 LYS B CE  
4632  N NZ  . LYS B 120 ? 0.8777 1.1549 0.9581 0.1317  -0.1230 0.2324  120 LYS B NZ  
4633  N N   . ALA B 121 ? 0.5474 0.8795 0.6332 0.0515  -0.1065 0.2348  121 ALA B N   
4634  C CA  . ALA B 121 ? 0.4492 0.7905 0.5368 0.0370  -0.0977 0.2309  121 ALA B CA  
4635  C C   . ALA B 121 ? 0.4228 0.7843 0.5199 0.0298  -0.0985 0.2296  121 ALA B C   
4636  O O   . ALA B 121 ? 0.3075 0.6828 0.4131 0.0234  -0.0922 0.2262  121 ALA B O   
4637  C CB  . ALA B 121 ? 0.4579 0.8043 0.5531 0.0393  -0.0883 0.2270  121 ALA B CB  
4638  N N   . LYS B 122 ? 0.3723 0.7336 0.4661 0.0303  -0.1075 0.2329  122 LYS B N   
4639  C CA  . LYS B 122 ? 0.3375 0.7160 0.4386 0.0229  -0.1103 0.2324  122 LYS B CA  
4640  C C   . LYS B 122 ? 0.3272 0.7014 0.4186 0.0081  -0.1072 0.2291  122 LYS B C   
4641  O O   . LYS B 122 ? 0.3182 0.7051 0.4161 0.0005  -0.1063 0.2269  122 LYS B O   
4642  C CB  . LYS B 122 ? 0.3584 0.7360 0.4567 0.0277  -0.1216 0.2366  122 LYS B CB  
4643  C CG  . LYS B 122 ? 0.4635 0.8488 0.5733 0.0444  -0.1265 0.2386  122 LYS B CG  
4644  C CD  . LYS B 122 ? 0.4796 0.8690 0.5894 0.0486  -0.1384 0.2420  122 LYS B CD  
4645  C CE  . LYS B 122 ? 0.4718 0.8337 0.5595 0.0494  -0.1463 0.2460  122 LYS B CE  
4646  N NZ  . LYS B 122 ? 0.5594 0.9011 0.6396 0.0632  -0.1490 0.2479  122 LYS B NZ  
4647  N N   . ASN B 123 ? 0.3583 0.7148 0.4331 0.0039  -0.1063 0.2287  123 ASN B N   
4648  C CA  . ASN B 123 ? 0.3233 0.6759 0.3878 -0.0075 -0.1028 0.2241  123 ASN B CA  
4649  C C   . ASN B 123 ? 0.3381 0.6807 0.3963 -0.0077 -0.0952 0.2222  123 ASN B C   
4650  O O   . ASN B 123 ? 0.3245 0.6553 0.3680 -0.0111 -0.0955 0.2233  123 ASN B O   
4651  C CB  . ASN B 123 ? 0.3553 0.7008 0.4045 -0.0130 -0.1095 0.2252  123 ASN B CB  
4652  C CG  . ASN B 123 ? 0.3902 0.7457 0.4450 -0.0137 -0.1178 0.2267  123 ASN B CG  
4653  O OD1 . ASN B 123 ? 0.3936 0.7557 0.4498 -0.0207 -0.1189 0.2231  123 ASN B OD1 
4654  N ND2 . ASN B 123 ? 0.3630 0.7184 0.4201 -0.0062 -0.1249 0.2322  123 ASN B ND2 
4655  N N   . PRO B 124 ? 0.2999 0.6481 0.3685 -0.0052 -0.0883 0.2196  124 PRO B N   
4656  C CA  . PRO B 124 ? 0.3258 0.6646 0.3900 -0.0037 -0.0822 0.2186  124 PRO B CA  
4657  C C   . PRO B 124 ? 0.3549 0.6900 0.4079 -0.0127 -0.0779 0.2138  124 PRO B C   
4658  O O   . PRO B 124 ? 0.3082 0.6490 0.3602 -0.0183 -0.0774 0.2087  124 PRO B O   
4659  C CB  . PRO B 124 ? 0.3183 0.6669 0.3972 0.0018  -0.0766 0.2167  124 PRO B CB  
4660  C CG  . PRO B 124 ? 0.3204 0.6835 0.4079 -0.0028 -0.0777 0.2148  124 PRO B CG  
4661  C CD  . PRO B 124 ? 0.3345 0.6984 0.4189 -0.0039 -0.0863 0.2182  124 PRO B CD  
4662  N N   . VAL B 125 ? 0.2920 0.6171 0.3358 -0.0137 -0.0754 0.2152  125 VAL B N   
4663  C CA  . VAL B 125 ? 0.3108 0.6362 0.3455 -0.0209 -0.0705 0.2104  125 VAL B CA  
4664  C C   . VAL B 125 ? 0.2886 0.6085 0.3235 -0.0196 -0.0653 0.2108  125 VAL B C   
4665  O O   . VAL B 125 ? 0.2888 0.5996 0.3255 -0.0138 -0.0671 0.2160  125 VAL B O   
4666  C CB  . VAL B 125 ? 0.3433 0.6652 0.3621 -0.0274 -0.0736 0.2122  125 VAL B CB  
4667  C CG1 . VAL B 125 ? 0.3092 0.6356 0.3257 -0.0289 -0.0793 0.2108  125 VAL B CG1 
4668  C CG2 . VAL B 125 ? 0.3677 0.6764 0.3786 -0.0267 -0.0777 0.2207  125 VAL B CG2 
4669  N N   . PHE B 126 ? 0.2892 0.6142 0.3213 -0.0242 -0.0597 0.2050  126 PHE B N   
4670  C CA  . PHE B 126 ? 0.2860 0.6073 0.3150 -0.0259 -0.0552 0.2050  126 PHE B CA  
4671  C C   . PHE B 126 ? 0.2751 0.5994 0.2909 -0.0347 -0.0542 0.2046  126 PHE B C   
4672  O O   . PHE B 126 ? 0.2933 0.6272 0.3049 -0.0375 -0.0538 0.1995  126 PHE B O   
4673  C CB  . PHE B 126 ? 0.2966 0.6245 0.3337 -0.0237 -0.0494 0.1982  126 PHE B CB  
4674  C CG  . PHE B 126 ? 0.3312 0.6574 0.3802 -0.0159 -0.0486 0.1993  126 PHE B CG  
4675  C CD1 . PHE B 126 ? 0.3009 0.6317 0.3585 -0.0119 -0.0512 0.2002  126 PHE B CD1 
4676  C CD2 . PHE B 126 ? 0.2928 0.6148 0.3440 -0.0127 -0.0450 0.1992  126 PHE B CD2 
4677  C CE1 . PHE B 126 ? 0.2586 0.5924 0.3275 -0.0046 -0.0495 0.2011  126 PHE B CE1 
4678  C CE2 . PHE B 126 ? 0.2990 0.6214 0.3602 -0.0045 -0.0437 0.1998  126 PHE B CE2 
4679  C CZ  . PHE B 126 ? 0.2320 0.5618 0.3024 -0.0003 -0.0455 0.2006  126 PHE B CZ  
4680  N N   . ILE B 127 ? 0.2868 0.6027 0.2948 -0.0392 -0.0542 0.2098  127 ILE B N   
4681  C CA  . ILE B 127 ? 0.2965 0.6178 0.2923 -0.0493 -0.0527 0.2104  127 ILE B CA  
4682  C C   . ILE B 127 ? 0.2975 0.6232 0.2938 -0.0535 -0.0473 0.2077  127 ILE B C   
4683  O O   . ILE B 127 ? 0.3421 0.6549 0.3401 -0.0517 -0.0477 0.2111  127 ILE B O   
4684  C CB  . ILE B 127 ? 0.3228 0.6294 0.3059 -0.0546 -0.0585 0.2200  127 ILE B CB  
4685  C CG1 . ILE B 127 ? 0.3306 0.6354 0.3123 -0.0507 -0.0642 0.2220  127 ILE B CG1 
4686  C CG2 . ILE B 127 ? 0.3344 0.6482 0.3050 -0.0670 -0.0560 0.2212  127 ILE B CG2 
4687  C CD1 . ILE B 127 ? 0.3587 0.6467 0.3268 -0.0546 -0.0709 0.2316  127 ILE B CD1 
4688  N N   . SER B 128 ? 0.2825 0.6268 0.2765 -0.0581 -0.0428 0.2013  128 SER B N   
4689  C CA  . SER B 128 ? 0.2759 0.6291 0.2710 -0.0623 -0.0379 0.1979  128 SER B CA  
4690  C C   . SER B 128 ? 0.2837 0.6555 0.2704 -0.0716 -0.0354 0.1961  128 SER B C   
4691  O O   . SER B 128 ? 0.2900 0.6699 0.2709 -0.0723 -0.0364 0.1952  128 SER B O   
4692  C CB  . SER B 128 ? 0.2541 0.6166 0.2592 -0.0542 -0.0341 0.1886  128 SER B CB  
4693  O OG  . SER B 128 ? 0.2485 0.6211 0.2544 -0.0579 -0.0300 0.1850  128 SER B OG  
4694  N N   . ASN B 129 ? 0.2844 0.6645 0.2704 -0.0789 -0.0322 0.1952  129 ASN B N   
4695  C CA  . ASN B 129 ? 0.2870 0.6936 0.2689 -0.0853 -0.0286 0.1906  129 ASN B CA  
4696  C C   . ASN B 129 ? 0.2705 0.6970 0.2570 -0.0748 -0.0254 0.1791  129 ASN B C   
4697  O O   . ASN B 129 ? 0.2758 0.7192 0.2564 -0.0746 -0.0242 0.1752  129 ASN B O   
4698  C CB  . ASN B 129 ? 0.2909 0.7051 0.2727 -0.0954 -0.0264 0.1912  129 ASN B CB  
4699  C CG  . ASN B 129 ? 0.2750 0.6847 0.2659 -0.0896 -0.0247 0.1870  129 ASN B CG  
4700  O OD1 . ASN B 129 ? 0.2657 0.6586 0.2617 -0.0802 -0.0260 0.1872  129 ASN B OD1 
4701  N ND2 . ASN B 129 ? 0.2733 0.6991 0.2659 -0.0957 -0.0220 0.1834  129 ASN B ND2 
4702  N N   . PHE B 130 ? 0.2535 0.6761 0.2485 -0.0656 -0.0243 0.1735  130 PHE B N   
4703  C CA  . PHE B 130 ? 0.2689 0.6993 0.2651 -0.0546 -0.0234 0.1637  130 PHE B CA  
4704  C C   . PHE B 130 ? 0.2420 0.6575 0.2464 -0.0467 -0.0240 0.1614  130 PHE B C   
4705  O O   . PHE B 130 ? 0.2443 0.6631 0.2537 -0.0463 -0.0215 0.1592  130 PHE B O   
4706  C CB  . PHE B 130 ? 0.2730 0.7316 0.2667 -0.0526 -0.0192 0.1540  130 PHE B CB  
4707  C CG  . PHE B 130 ? 0.2470 0.7129 0.2326 -0.0443 -0.0198 0.1458  130 PHE B CG  
4708  C CD1 . PHE B 130 ? 0.3102 0.7611 0.2949 -0.0337 -0.0228 0.1395  130 PHE B CD1 
4709  C CD2 . PHE B 130 ? 0.2767 0.7620 0.2540 -0.0473 -0.0184 0.1442  130 PHE B CD2 
4710  C CE1 . PHE B 130 ? 0.3243 0.7761 0.2984 -0.0261 -0.0256 0.1314  130 PHE B CE1 
4711  C CE2 . PHE B 130 ? 0.3041 0.7936 0.2714 -0.0384 -0.0198 0.1359  130 PHE B CE2 
4712  C CZ  . PHE B 130 ? 0.3132 0.7842 0.2781 -0.0276 -0.0240 0.1292  130 PHE B CZ  
4713  N N   . HIS B 131 ? 0.2441 0.6444 0.2496 -0.0412 -0.0275 0.1620  131 HIS B N   
4714  C CA  . HIS B 131 ? 0.2212 0.6097 0.2338 -0.0341 -0.0280 0.1587  131 HIS B CA  
4715  C C   . HIS B 131 ? 0.2110 0.6080 0.2208 -0.0278 -0.0263 0.1474  131 HIS B C   
4716  O O   . HIS B 131 ? 0.2351 0.6391 0.2365 -0.0243 -0.0277 0.1406  131 HIS B O   
4717  C CB  . HIS B 131 ? 0.2194 0.5939 0.2334 -0.0310 -0.0328 0.1607  131 HIS B CB  
4718  C CG  . HIS B 131 ? 0.2454 0.6099 0.2633 -0.0339 -0.0353 0.1709  131 HIS B CG  
4719  N ND1 . HIS B 131 ? 0.2794 0.6440 0.2907 -0.0382 -0.0382 0.1761  131 HIS B ND1 
4720  C CD2 . HIS B 131 ? 0.2886 0.6422 0.3149 -0.0317 -0.0359 0.1764  131 HIS B CD2 
4721  C CE1 . HIS B 131 ? 0.3049 0.6575 0.3201 -0.0382 -0.0411 0.1844  131 HIS B CE1 
4722  N NE2 . HIS B 131 ? 0.2594 0.6061 0.2840 -0.0336 -0.0396 0.1845  131 HIS B NE2 
4723  N N   A PHE B 132 ? 0.2238 0.6186 0.2390 -0.0250 -0.0242 0.1448  132 PHE B N   
4724  N N   B PHE B 132 ? 0.2237 0.6186 0.2390 -0.0253 -0.0242 0.1450  132 PHE B N   
4725  C CA  A PHE B 132 ? 0.2160 0.6135 0.2271 -0.0174 -0.0244 0.1335  132 PHE B CA  
4726  C CA  B PHE B 132 ? 0.2158 0.6124 0.2279 -0.0177 -0.0242 0.1342  132 PHE B CA  
4727  C C   A PHE B 132 ? 0.2224 0.6000 0.2325 -0.0124 -0.0297 0.1307  132 PHE B C   
4728  C C   B PHE B 132 ? 0.2223 0.6004 0.2322 -0.0127 -0.0297 0.1310  132 PHE B C   
4729  O O   A PHE B 132 ? 0.2396 0.6058 0.2548 -0.0151 -0.0317 0.1376  132 PHE B O   
4730  O O   B PHE B 132 ? 0.2422 0.6094 0.2558 -0.0154 -0.0321 0.1376  132 PHE B O   
4731  C CB  A PHE B 132 ? 0.2231 0.6265 0.2386 -0.0164 -0.0209 0.1309  132 PHE B CB  
4732  C CB  B PHE B 132 ? 0.2286 0.6260 0.2465 -0.0170 -0.0212 0.1332  132 PHE B CB  
4733  C CG  A PHE B 132 ? 0.2376 0.6501 0.2474 -0.0083 -0.0210 0.1185  132 PHE B CG  
4734  C CG  B PHE B 132 ? 0.2492 0.6467 0.2632 -0.0085 -0.0221 0.1218  132 PHE B CG  
4735  C CD1 A PHE B 132 ? 0.2100 0.6435 0.2132 -0.0061 -0.0198 0.1123  132 PHE B CD1 
4736  C CD1 B PHE B 132 ? 0.2307 0.6473 0.2388 -0.0044 -0.0209 0.1129  132 PHE B CD1 
4737  C CD2 A PHE B 132 ? 0.2507 0.6507 0.2611 -0.0019 -0.0229 0.1125  132 PHE B CD2 
4738  C CD2 B PHE B 132 ? 0.2447 0.6236 0.2604 -0.0043 -0.0248 0.1196  132 PHE B CD2 
4739  C CE1 A PHE B 132 ? 0.2149 0.6572 0.2127 0.0041  -0.0205 0.0996  132 PHE B CE1 
4740  C CE1 B PHE B 132 ? 0.2680 0.6821 0.2717 0.0054  -0.0232 0.1015  132 PHE B CE1 
4741  C CE2 A PHE B 132 ? 0.2782 0.6837 0.2825 0.0072  -0.0246 0.1004  132 PHE B CE2 
4742  C CE2 B PHE B 132 ? 0.2640 0.6390 0.2746 0.0035  -0.0275 0.1093  132 PHE B CE2 
4743  C CZ  A PHE B 132 ? 0.2742 0.7008 0.2723 0.0111  -0.0235 0.0935  132 PHE B CZ  
4744  C CZ  B PHE B 132 ? 0.3013 0.6925 0.3057 0.0091  -0.0272 0.0999  132 PHE B CZ  
4745  N N   A ASP B 133 ? 0.2219 0.5958 0.2250 -0.0052 -0.0328 0.1203  133 ASP B N   
4746  N N   B ASP B 133 ? 0.2214 0.5960 0.2245 -0.0054 -0.0327 0.1206  133 ASP B N   
4747  C CA  A ASP B 133 ? 0.2491 0.6048 0.2465 -0.0023 -0.0405 0.1172  133 ASP B CA  
4748  C CA  B ASP B 133 ? 0.2490 0.6051 0.2464 -0.0022 -0.0402 0.1172  133 ASP B CA  
4749  C C   A ASP B 133 ? 0.2403 0.5815 0.2468 -0.0057 -0.0416 0.1239  133 ASP B C   
4750  C C   B ASP B 133 ? 0.2398 0.5818 0.2467 -0.0059 -0.0412 0.1243  133 ASP B C   
4751  O O   A ASP B 133 ? 0.2356 0.5682 0.2428 -0.0088 -0.0460 0.1280  133 ASP B O   
4752  O O   B ASP B 133 ? 0.2335 0.5681 0.2417 -0.0093 -0.0451 0.1291  133 ASP B O   
4753  C CB  A ASP B 133 ? 0.2756 0.6264 0.2617 0.0068  -0.0457 0.1048  133 ASP B CB  
4754  C CB  B ASP B 133 ? 0.2737 0.6252 0.2613 0.0067  -0.0448 0.1050  133 ASP B CB  
4755  C CG  A ASP B 133 ? 0.2969 0.6452 0.2865 0.0105  -0.0440 0.1009  133 ASP B CG  
4756  C CG  B ASP B 133 ? 0.2652 0.6343 0.2434 0.0126  -0.0438 0.0965  133 ASP B CG  
4757  O OD1 A ASP B 133 ? 0.2891 0.6420 0.2895 0.0060  -0.0379 0.1073  133 ASP B OD1 
4758  O OD1 B ASP B 133 ? 0.2877 0.6636 0.2611 0.0104  -0.0443 0.0983  133 ASP B OD1 
4759  O OD2 A ASP B 133 ? 0.3251 0.6652 0.3052 0.0187  -0.0499 0.0911  133 ASP B OD2 
4760  O OD2 B ASP B 133 ? 0.3601 0.7384 0.3361 0.0198  -0.0424 0.0879  133 ASP B OD2 
4761  N N   . THR B 134 ? 0.2128 0.5532 0.2262 -0.0053 -0.0377 0.1250  134 THR B N   
4762  C CA  . THR B 134 ? 0.1927 0.5239 0.2150 -0.0081 -0.0376 0.1316  134 THR B CA  
4763  C C   . THR B 134 ? 0.2144 0.5507 0.2459 -0.0123 -0.0344 0.1415  134 THR B C   
4764  O O   . THR B 134 ? 0.2084 0.5405 0.2461 -0.0142 -0.0361 0.1470  134 THR B O   
4765  C CB  . THR B 134 ? 0.1916 0.5208 0.2177 -0.0059 -0.0344 0.1303  134 THR B CB  
4766  O OG1 . THR B 134 ? 0.1931 0.5322 0.2249 -0.0070 -0.0282 0.1341  134 THR B OG1 
4767  C CG2 . THR B 134 ? 0.2339 0.5587 0.2501 -0.0003 -0.0379 0.1199  134 THR B CG2 
4768  N N   . THR B 135 ? 0.2204 0.5662 0.2524 -0.0138 -0.0307 0.1443  135 THR B N   
4769  C CA  . THR B 135 ? 0.2133 0.5603 0.2515 -0.0168 -0.0297 0.1537  135 THR B CA  
4770  C C   . THR B 135 ? 0.2209 0.5660 0.2576 -0.0187 -0.0341 0.1565  135 THR B C   
4771  O O   . THR B 135 ? 0.2589 0.6010 0.3028 -0.0189 -0.0354 0.1629  135 THR B O   
4772  C CB  . THR B 135 ? 0.2207 0.5762 0.2567 -0.0200 -0.0269 0.1564  135 THR B CB  
4773  O OG1 . THR B 135 ? 0.2211 0.5815 0.2562 -0.0189 -0.0238 0.1516  135 THR B OG1 
4774  C CG2 . THR B 135 ? 0.2139 0.5639 0.2550 -0.0216 -0.0270 0.1660  135 THR B CG2 
4775  N N   . ALA B 136 ? 0.2184 0.5664 0.2453 -0.0191 -0.0369 0.1514  136 ALA B N   
4776  C CA  . ALA B 136 ? 0.2227 0.5679 0.2462 -0.0210 -0.0422 0.1533  136 ALA B CA  
4777  C C   . ALA B 136 ? 0.2447 0.5806 0.2710 -0.0209 -0.0472 0.1526  136 ALA B C   
4778  O O   . ALA B 136 ? 0.2228 0.5575 0.2529 -0.0233 -0.0508 0.1578  136 ALA B O   
4779  C CB  . ALA B 136 ? 0.2211 0.5717 0.2313 -0.0203 -0.0443 0.1470  136 ALA B CB  
4780  N N   . ALA B 137 ? 0.2533 0.5834 0.2776 -0.0188 -0.0481 0.1468  137 ALA B N   
4781  C CA  . ALA B 137 ? 0.2587 0.5804 0.2847 -0.0210 -0.0536 0.1474  137 ALA B CA  
4782  C C   . ALA B 137 ? 0.2330 0.5601 0.2738 -0.0234 -0.0505 0.1565  137 ALA B C   
4783  O O   . ALA B 137 ? 0.2454 0.5732 0.2904 -0.0274 -0.0550 0.1608  137 ALA B O   
4784  C CB  . ALA B 137 ? 0.2147 0.5277 0.2346 -0.0186 -0.0556 0.1405  137 ALA B CB  
4785  N N   . HIS B 138 ? 0.2760 0.6080 0.3242 -0.0206 -0.0435 0.1592  138 HIS B N   
4786  C CA  . HIS B 138 ? 0.2070 0.5452 0.2678 -0.0200 -0.0406 0.1670  138 HIS B CA  
4787  C C   . HIS B 138 ? 0.2692 0.6116 0.3337 -0.0200 -0.0422 0.1730  138 HIS B C   
4788  O O   . HIS B 138 ? 0.2491 0.5975 0.3222 -0.0203 -0.0436 0.1786  138 HIS B O   
4789  C CB  . HIS B 138 ? 0.2359 0.5754 0.3007 -0.0156 -0.0341 0.1675  138 HIS B CB  
4790  C CG  . HIS B 138 ? 0.2090 0.5460 0.2731 -0.0153 -0.0327 0.1638  138 HIS B CG  
4791  N ND1 . HIS B 138 ? 0.2348 0.5760 0.3054 -0.0169 -0.0328 0.1676  138 HIS B ND1 
4792  C CD2 . HIS B 138 ? 0.1910 0.5229 0.2482 -0.0139 -0.0317 0.1572  138 HIS B CD2 
4793  C CE1 . HIS B 138 ? 0.1766 0.5135 0.2435 -0.0170 -0.0322 0.1638  138 HIS B CE1 
4794  N NE2 . HIS B 138 ? 0.1809 0.5111 0.2396 -0.0145 -0.0318 0.1570  138 HIS B NE2 
4795  N N   . VAL B 139 ? 0.2142 0.5552 0.2722 -0.0199 -0.0424 0.1725  139 VAL B N   
4796  C CA  . VAL B 139 ? 0.2642 0.6069 0.3232 -0.0204 -0.0458 0.1782  139 VAL B CA  
4797  C C   . VAL B 139 ? 0.2166 0.5601 0.2750 -0.0240 -0.0521 0.1783  139 VAL B C   
4798  O O   . VAL B 139 ? 0.2287 0.5773 0.2951 -0.0238 -0.0546 0.1840  139 VAL B O   
4799  C CB  . VAL B 139 ? 0.2528 0.5943 0.3021 -0.0219 -0.0457 0.1778  139 VAL B CB  
4800  C CG1 . VAL B 139 ? 0.2431 0.5845 0.2904 -0.0232 -0.0508 0.1832  139 VAL B CG1 
4801  C CG2 . VAL B 139 ? 0.2897 0.6302 0.3402 -0.0200 -0.0412 0.1802  139 VAL B CG2 
4802  N N   . GLU B 140 ? 0.2524 0.5910 0.3010 -0.0269 -0.0557 0.1717  140 GLU B N   
4803  C CA  . GLU B 140 ? 0.2457 0.5820 0.2908 -0.0311 -0.0637 0.1715  140 GLU B CA  
4804  C C   . GLU B 140 ? 0.2727 0.6125 0.3274 -0.0346 -0.0656 0.1749  140 GLU B C   
4805  O O   . GLU B 140 ? 0.2938 0.6379 0.3524 -0.0387 -0.0712 0.1792  140 GLU B O   
4806  C CB  . GLU B 140 ? 0.2864 0.6138 0.3152 -0.0315 -0.0684 0.1627  140 GLU B CB  
4807  C CG  . GLU B 140 ? 0.2789 0.6082 0.2976 -0.0297 -0.0676 0.1608  140 GLU B CG  
4808  C CD  . GLU B 140 ? 0.4013 0.7263 0.4042 -0.0267 -0.0692 0.1508  140 GLU B CD  
4809  O OE1 . GLU B 140 ? 0.4454 0.7622 0.4441 -0.0252 -0.0724 0.1448  140 GLU B OE1 
4810  O OE2 . GLU B 140 ? 0.3757 0.7064 0.3699 -0.0254 -0.0677 0.1491  140 GLU B OE2 
4811  N N   . LEU B 141 ? 0.2487 0.5886 0.3074 -0.0338 -0.0613 0.1738  141 LEU B N   
4812  C CA  . LEU B 141 ? 0.2364 0.5830 0.3041 -0.0384 -0.0625 0.1785  141 LEU B CA  
4813  C C   . LEU B 141 ? 0.2299 0.5919 0.3118 -0.0367 -0.0598 0.1870  141 LEU B C   
4814  O O   . LEU B 141 ? 0.2954 0.6674 0.3842 -0.0422 -0.0634 0.1924  141 LEU B O   
4815  C CB  . LEU B 141 ? 0.3485 0.6932 0.4169 -0.0370 -0.0576 0.1763  141 LEU B CB  
4816  C CG  . LEU B 141 ? 0.2792 0.6111 0.3363 -0.0419 -0.0644 0.1710  141 LEU B CG  
4817  C CD1 . LEU B 141 ? 0.2958 0.6233 0.3509 -0.0384 -0.0596 0.1673  141 LEU B CD1 
4818  C CD2 . LEU B 141 ? 0.2476 0.5846 0.3090 -0.0518 -0.0709 0.1776  141 LEU B CD2 
4819  N N   . ASN B 142 ? 0.2391 0.6244 0.3690 -0.0580 -0.0415 0.2447  142 ASN B N   
4820  C CA  . ASN B 142 ? 0.2492 0.6426 0.3865 -0.0519 -0.0411 0.2554  142 ASN B CA  
4821  C C   . ASN B 142 ? 0.2725 0.6821 0.4115 -0.0557 -0.0447 0.2652  142 ASN B C   
4822  O O   . ASN B 142 ? 0.3244 0.7396 0.4692 -0.0502 -0.0448 0.2747  142 ASN B O   
4823  C CB  . ASN B 142 ? 0.2491 0.6294 0.3890 -0.0424 -0.0389 0.2562  142 ASN B CB  
4824  C CG  . ASN B 142 ? 0.2105 0.5771 0.3505 -0.0377 -0.0350 0.2485  142 ASN B CG  
4825  O OD1 . ASN B 142 ? 0.2430 0.6112 0.3882 -0.0329 -0.0326 0.2516  142 ASN B OD1 
4826  N ND2 . ASN B 142 ? 0.2690 0.6223 0.4032 -0.0393 -0.0344 0.2384  142 ASN B ND2 
4827  N N   . GLY B 143 ? 0.2308 0.6480 0.3649 -0.0649 -0.0474 0.2633  143 GLY B N   
4828  C CA  . GLY B 143 ? 0.2810 0.7150 0.4167 -0.0694 -0.0508 0.2726  143 GLY B CA  
4829  C C   . GLY B 143 ? 0.2856 0.7186 0.4211 -0.0671 -0.0529 0.2779  143 GLY B C   
4830  O O   . GLY B 143 ? 0.2627 0.7086 0.4021 -0.0670 -0.0550 0.2881  143 GLY B O   
4831  N N   . CYS B 144 ? 0.2475 0.6654 0.3785 -0.0652 -0.0525 0.2714  144 CYS B N   
4832  C CA  . CYS B 144 ? 0.2562 0.6717 0.3856 -0.0637 -0.0545 0.2755  144 CYS B CA  
4833  C C   . CYS B 144 ? 0.2785 0.6902 0.3996 -0.0715 -0.0567 0.2685  144 CYS B C   
4834  O O   . CYS B 144 ? 0.3179 0.7253 0.4347 -0.0767 -0.0560 0.2594  144 CYS B O   
4835  C CB  . CYS B 144 ? 0.2813 0.6816 0.4125 -0.0537 -0.0518 0.2750  144 CYS B CB  
4836  S SG  . CYS B 144 ? 0.3132 0.7140 0.4537 -0.0440 -0.0481 0.2809  144 CYS B SG  
4837  N N   . LYS B 145 ? 0.2701 0.6832 0.3890 -0.0724 -0.0592 0.2729  145 LYS B N   
4838  C CA  . LYS B 145 ? 0.2614 0.6701 0.3725 -0.0791 -0.0613 0.2669  145 LYS B CA  
4839  C C   . LYS B 145 ? 0.2761 0.6664 0.3836 -0.0734 -0.0598 0.2618  145 LYS B C   
4840  O O   . LYS B 145 ? 0.2967 0.6820 0.4075 -0.0653 -0.0587 0.2670  145 LYS B O   
4841  C CB  . LYS B 145 ? 0.2737 0.6962 0.3837 -0.0847 -0.0651 0.2750  145 LYS B CB  
4842  C CG  . LYS B 145 ? 0.4249 0.8446 0.5267 -0.0928 -0.0674 0.2692  145 LYS B CG  
4843  C CD  . LYS B 145 ? 0.3797 0.8130 0.4806 -0.0979 -0.0712 0.2778  145 LYS B CD  
4844  C CE  . LYS B 145 ? 0.4700 0.8991 0.5625 -0.1054 -0.0733 0.2722  145 LYS B CE  
4845  N NZ  . LYS B 145 ? 0.5115 0.9496 0.6028 -0.1079 -0.0766 0.2807  145 LYS B NZ  
4846  N N   . ALA B 146 ? 0.2694 0.6495 0.3702 -0.0777 -0.0597 0.2516  146 ALA B N   
4847  C CA  . ALA B 146 ? 0.2675 0.6298 0.3640 -0.0732 -0.0583 0.2457  146 ALA B CA  
4848  C C   . ALA B 146 ? 0.2874 0.6494 0.3779 -0.0774 -0.0612 0.2469  146 ALA B C   
4849  O O   . ALA B 146 ? 0.3174 0.6805 0.4023 -0.0855 -0.0628 0.2414  146 ALA B O   
4850  C CB  . ALA B 146 ? 0.2330 0.5838 0.3262 -0.0747 -0.0561 0.2338  146 ALA B CB  
4851  N N   . ILE B 147 ? 0.3245 0.6848 0.4162 -0.0719 -0.0616 0.2543  147 ILE B N   
4852  C CA  . ILE B 147 ? 0.2740 0.6335 0.3600 -0.0750 -0.0642 0.2564  147 ILE B CA  
4853  C C   . ILE B 147 ? 0.2726 0.6132 0.3524 -0.0721 -0.0627 0.2486  147 ILE B C   
4854  O O   . ILE B 147 ? 0.2670 0.5960 0.3488 -0.0639 -0.0598 0.2476  147 ILE B O   
4855  C CB  . ILE B 147 ? 0.2880 0.6552 0.3782 -0.0706 -0.0654 0.2687  147 ILE B CB  
4856  C CG1 . ILE B 147 ? 0.2919 0.6767 0.3896 -0.0715 -0.0662 0.2768  147 ILE B CG1 
4857  C CG2 . ILE B 147 ? 0.2977 0.6669 0.3819 -0.0754 -0.0685 0.2714  147 ILE B CG2 
4858  C CD1 . ILE B 147 ? 0.3142 0.7143 0.4099 -0.0817 -0.0696 0.2782  147 ILE B CD1 
4859  N N   . ASN B 148 ? 0.2754 0.6131 0.3478 -0.0789 -0.0645 0.2434  148 ASN B N   
4860  C CA  . ASN B 148 ? 0.2650 0.5856 0.3307 -0.0774 -0.0633 0.2357  148 ASN B CA  
4861  C C   . ASN B 148 ? 0.3073 0.6272 0.3675 -0.0794 -0.0657 0.2396  148 ASN B C   
4862  O O   . ASN B 148 ? 0.2803 0.6098 0.3374 -0.0876 -0.0685 0.2406  148 ASN B O   
4863  C CB  . ASN B 148 ? 0.2641 0.5801 0.3254 -0.0838 -0.0631 0.2244  148 ASN B CB  
4864  C CG  . ASN B 148 ? 0.3020 0.6170 0.3680 -0.0818 -0.0606 0.2197  148 ASN B CG  
4865  O OD1 . ASN B 148 ? 0.3554 0.6648 0.4259 -0.0737 -0.0581 0.2213  148 ASN B OD1 
4866  N ND2 . ASN B 148 ? 0.2340 0.5543 0.2989 -0.0892 -0.0611 0.2140  148 ASN B ND2 
4867  N N   . ILE B 149 ? 0.2815 0.5898 0.3402 -0.0724 -0.0642 0.2417  149 ILE B N   
4868  C CA  . ILE B 149 ? 0.2933 0.6004 0.3469 -0.0734 -0.0661 0.2464  149 ILE B CA  
4869  C C   . ILE B 149 ? 0.2912 0.5799 0.3375 -0.0710 -0.0644 0.2396  149 ILE B C   
4870  O O   . ILE B 149 ? 0.3001 0.5815 0.3445 -0.0659 -0.0636 0.2440  149 ILE B O   
4871  C CB  . ILE B 149 ? 0.3057 0.6189 0.3647 -0.0673 -0.0662 0.2583  149 ILE B CB  
4872  C CG1 . ILE B 149 ? 0.3032 0.6063 0.3671 -0.0571 -0.0624 0.2590  149 ILE B CG1 
4873  C CG2 . ILE B 149 ? 0.3099 0.6431 0.3750 -0.0711 -0.0686 0.2659  149 ILE B CG2 
4874  C CD1 . ILE B 149 ? 0.3159 0.6227 0.3849 -0.0505 -0.0620 0.2704  149 ILE B CD1 
4875  N N   . VAL B 150 ? 0.2798 0.5609 0.3220 -0.0746 -0.0636 0.2289  150 VAL B N   
4876  C CA  . VAL B 150 ? 0.2845 0.5484 0.3196 -0.0728 -0.0620 0.2221  150 VAL B CA  
4877  C C   . VAL B 150 ? 0.2882 0.5518 0.3165 -0.0767 -0.0642 0.2249  150 VAL B C   
4878  O O   . VAL B 150 ? 0.2935 0.5698 0.3210 -0.0836 -0.0673 0.2284  150 VAL B O   
4879  C CB  . VAL B 150 ? 0.2868 0.5442 0.3190 -0.0768 -0.0610 0.2103  150 VAL B CB  
4880  C CG1 . VAL B 150 ? 0.3184 0.5846 0.3468 -0.0873 -0.0639 0.2071  150 VAL B CG1 
4881  C CG2 . VAL B 150 ? 0.2596 0.4981 0.2862 -0.0728 -0.0585 0.2034  150 VAL B CG2 
4882  N N   . THR B 151 ? 0.3049 0.5540 0.3281 -0.0722 -0.0624 0.2237  151 THR B N   
4883  C CA  . THR B 151 ? 0.3065 0.5531 0.3225 -0.0756 -0.0640 0.2253  151 THR B CA  
4884  C C   . THR B 151 ? 0.3179 0.5693 0.3288 -0.0856 -0.0664 0.2192  151 THR B C   
4885  O O   . THR B 151 ? 0.2856 0.5330 0.2955 -0.0885 -0.0656 0.2100  151 THR B O   
4886  C CB  . THR B 151 ? 0.3188 0.5466 0.3291 -0.0700 -0.0611 0.2219  151 THR B CB  
4887  O OG1 . THR B 151 ? 0.3293 0.5539 0.3315 -0.0747 -0.0626 0.2211  151 THR B OG1 
4888  C CG2 . THR B 151 ? 0.2886 0.5051 0.2980 -0.0687 -0.0586 0.2113  151 THR B CG2 
4889  N N   . GLU B 152 ? 0.3554 0.6156 0.3633 -0.0911 -0.0694 0.2243  152 GLU B N   
4890  C CA  . GLU B 152 ? 0.3924 0.6572 0.3952 -0.1011 -0.0716 0.2189  152 GLU B CA  
4891  C C   . GLU B 152 ? 0.3830 0.6324 0.3786 -0.1022 -0.0699 0.2089  152 GLU B C   
4892  O O   . GLU B 152 ? 0.3281 0.5787 0.3208 -0.1096 -0.0707 0.2016  152 GLU B O   
4893  C CB  . GLU B 152 ? 0.3944 0.6691 0.3944 -0.1059 -0.0747 0.2265  152 GLU B CB  
4894  C CG  . GLU B 152 ? 0.5385 0.8292 0.5455 -0.1051 -0.0766 0.2372  152 GLU B CG  
4895  C CD  . GLU B 152 ? 0.5326 0.8373 0.5447 -0.1108 -0.0779 0.2359  152 GLU B CD  
4896  O OE1 . GLU B 152 ? 0.5390 0.8422 0.5564 -0.1072 -0.0759 0.2328  152 GLU B OE1 
4897  O OE2 . GLU B 152 ? 0.5742 0.8913 0.5849 -0.1192 -0.0808 0.2380  152 GLU B OE2 
4898  N N   . LYS B 153 ? 0.3616 0.5963 0.3544 -0.0951 -0.0674 0.2084  153 LYS B N   
4899  C CA  . LYS B 153 ? 0.3492 0.5690 0.3353 -0.0956 -0.0655 0.1990  153 LYS B CA  
4900  C C   . LYS B 153 ? 0.3185 0.5357 0.3066 -0.0975 -0.0644 0.1893  153 LYS B C   
4901  O O   . LYS B 153 ? 0.3322 0.5413 0.3151 -0.1011 -0.0638 0.1810  153 LYS B O   
4902  C CB  . LYS B 153 ? 0.3063 0.5109 0.2902 -0.0868 -0.0625 0.2003  153 LYS B CB  
4903  C CG  . LYS B 153 ? 0.3355 0.5413 0.3178 -0.0840 -0.0631 0.2101  153 LYS B CG  
4904  C CD  . LYS B 153 ? 0.4482 0.6566 0.4234 -0.0913 -0.0655 0.2103  153 LYS B CD  
4905  C CE  . LYS B 153 ? 0.5355 0.7432 0.5084 -0.0881 -0.0659 0.2197  153 LYS B CE  
4906  N NZ  . LYS B 153 ? 0.5129 0.7038 0.4831 -0.0799 -0.0622 0.2195  153 LYS B NZ  
4907  N N   . ALA B 154 ? 0.3352 0.5590 0.3308 -0.0952 -0.0639 0.1904  154 ALA B N   
4908  C CA  . ALA B 154 ? 0.3344 0.5549 0.3319 -0.0965 -0.0626 0.1813  154 ALA B CA  
4909  C C   . ALA B 154 ? 0.3662 0.5946 0.3619 -0.1067 -0.0647 0.1760  154 ALA B C   
4910  O O   . ALA B 154 ? 0.3563 0.5786 0.3507 -0.1092 -0.0636 0.1669  154 ALA B O   
4911  C CB  . ALA B 154 ? 0.3066 0.5320 0.3125 -0.0913 -0.0614 0.1840  154 ALA B CB  
4912  N N   . PHE B 155 ? 0.3119 0.5536 0.3074 -0.1128 -0.0675 0.1817  155 PHE B N   
4913  C CA  . PHE B 155 ? 0.4008 0.6505 0.3945 -0.1231 -0.0693 0.1772  155 PHE B CA  
4914  C C   . PHE B 155 ? 0.4044 0.6459 0.3901 -0.1282 -0.0695 0.1710  155 PHE B C   
4915  O O   . PHE B 155 ? 0.4760 0.7209 0.4598 -0.1365 -0.0703 0.1654  155 PHE B O   
4916  C CB  . PHE B 155 ? 0.4662 0.7331 0.4623 -0.1281 -0.0722 0.1856  155 PHE B CB  
4917  C CG  . PHE B 155 ? 0.4386 0.7147 0.4426 -0.1233 -0.0721 0.1927  155 PHE B CG  
4918  C CD1 . PHE B 155 ? 0.5630 0.8456 0.5724 -0.1252 -0.0715 0.1899  155 PHE B CD1 
4919  C CD2 . PHE B 155 ? 0.4617 0.7401 0.4680 -0.1170 -0.0725 0.2023  155 PHE B CD2 
4920  C CE1 . PHE B 155 ? 0.4802 0.7715 0.4969 -0.1209 -0.0713 0.1964  155 PHE B CE1 
4921  C CE2 . PHE B 155 ? 0.4813 0.7685 0.4954 -0.1126 -0.0723 0.2089  155 PHE B CE2 
4922  C CZ  . PHE B 155 ? 0.5062 0.7999 0.5254 -0.1145 -0.0718 0.2060  155 PHE B CZ  
4923  N N   . ASP B 156 ? 0.3996 0.6302 0.3805 -0.1236 -0.0687 0.1720  156 ASP B N   
4924  C CA  . ASP B 156 ? 0.3966 0.6187 0.3697 -0.1279 -0.0687 0.1665  156 ASP B CA  
4925  C C   . ASP B 156 ? 0.3355 0.5427 0.3072 -0.1242 -0.0659 0.1573  156 ASP B C   
4926  O O   . ASP B 156 ? 0.3480 0.5431 0.3171 -0.1175 -0.0639 0.1572  156 ASP B O   
4927  C CB  . ASP B 156 ? 0.3321 0.5516 0.3007 -0.1254 -0.0694 0.1734  156 ASP B CB  
4928  C CG  . ASP B 156 ? 0.4825 0.6988 0.4433 -0.1322 -0.0703 0.1699  156 ASP B CG  
4929  O OD1 . ASP B 156 ? 0.5290 0.7389 0.4870 -0.1361 -0.0695 0.1606  156 ASP B OD1 
4930  O OD2 . ASP B 156 ? 0.5842 0.8044 0.5418 -0.1335 -0.0720 0.1765  156 ASP B OD2 
4931  N N   . SER B 157 ? 0.3107 0.5187 0.2841 -0.1287 -0.0655 0.1496  157 SER B N   
4932  C CA  . SER B 157 ? 0.4038 0.5996 0.3779 -0.1245 -0.0629 0.1416  157 SER B CA  
4933  C C   . SER B 157 ? 0.3828 0.5646 0.3500 -0.1238 -0.0617 0.1362  157 SER B C   
4934  O O   . SER B 157 ? 0.3272 0.4969 0.2938 -0.1172 -0.0593 0.1330  157 SER B O   
4935  C CB  . SER B 157 ? 0.3610 0.5611 0.3386 -0.1300 -0.0628 0.1347  157 SER B CB  
4936  O OG  . SER B 157 ? 0.4978 0.6998 0.4712 -0.1393 -0.0640 0.1300  157 SER B OG  
4937  N N   . GLU B 158 ? 0.3920 0.5751 0.3536 -0.1307 -0.0631 0.1351  158 GLU B N   
4938  C CA  . GLU B 158 ? 0.3113 0.4816 0.2663 -0.1306 -0.0619 0.1297  158 GLU B CA  
4939  C C   . GLU B 158 ? 0.3799 0.5440 0.3309 -0.1248 -0.0612 0.1360  158 GLU B C   
4940  O O   . GLU B 158 ? 0.3170 0.4691 0.2628 -0.1230 -0.0596 0.1320  158 GLU B O   
4941  C CB  . GLU B 158 ? 0.3808 0.5541 0.3315 -0.1407 -0.0634 0.1251  158 GLU B CB  
4942  C CG  . GLU B 158 ? 0.4909 0.6750 0.4391 -0.1460 -0.0660 0.1322  158 GLU B CG  
4943  C CD  . GLU B 158 ? 0.5725 0.7720 0.5251 -0.1525 -0.0680 0.1346  158 GLU B CD  
4944  O OE1 . GLU B 158 ? 0.4569 0.6615 0.4160 -0.1496 -0.0676 0.1361  158 GLU B OE1 
4945  O OE2 . GLU B 158 ? 0.5940 0.8005 0.5435 -0.1608 -0.0698 0.1351  158 GLU B OE2 
4946  N N   . THR B 159 ? 0.3018 0.4736 0.2552 -0.1218 -0.0622 0.1456  159 THR B N   
4947  C CA  . THR B 159 ? 0.3278 0.4938 0.2777 -0.1163 -0.0615 0.1521  159 THR B CA  
4948  C C   . THR B 159 ? 0.3495 0.5070 0.3026 -0.1062 -0.0586 0.1540  159 THR B C   
4949  O O   . THR B 159 ? 0.3771 0.5411 0.3367 -0.1027 -0.0587 0.1581  159 THR B O   
4950  C CB  . THR B 159 ? 0.2938 0.4724 0.2445 -0.1186 -0.0641 0.1620  159 THR B CB  
4951  O OG1 . THR B 159 ? 0.3019 0.4867 0.2483 -0.1280 -0.0664 0.1603  159 THR B OG1 
4952  C CG2 . THR B 159 ? 0.3199 0.4922 0.2679 -0.1119 -0.0630 0.1693  159 THR B CG2 
4953  N N   . TYR B 160 ? 0.3318 0.4748 0.2803 -0.1017 -0.0559 0.1510  160 TYR B N   
4954  C CA  . TYR B 160 ? 0.3392 0.4726 0.2900 -0.0924 -0.0528 0.1522  160 TYR B CA  
4955  C C   . TYR B 160 ? 0.3768 0.5148 0.3305 -0.0872 -0.0529 0.1630  160 TYR B C   
4956  O O   . TYR B 160 ? 0.3315 0.4742 0.2824 -0.0893 -0.0546 0.1694  160 TYR B O   
4957  C CB  . TYR B 160 ? 0.2881 0.4052 0.2324 -0.0894 -0.0498 0.1476  160 TYR B CB  
4958  C CG  . TYR B 160 ? 0.2844 0.3904 0.2299 -0.0800 -0.0462 0.1492  160 TYR B CG  
4959  C CD1 . TYR B 160 ? 0.2971 0.4006 0.2420 -0.0747 -0.0451 0.1577  160 TYR B CD1 
4960  C CD2 . TYR B 160 ? 0.2977 0.3954 0.2450 -0.0767 -0.0438 0.1421  160 TYR B CD2 
4961  C CE1 . TYR B 160 ? 0.2818 0.3749 0.2278 -0.0665 -0.0416 0.1591  160 TYR B CE1 
4962  C CE2 . TYR B 160 ? 0.3051 0.3926 0.2533 -0.0685 -0.0403 0.1434  160 TYR B CE2 
4963  C CZ  . TYR B 160 ? 0.3247 0.4098 0.2723 -0.0635 -0.0392 0.1519  160 TYR B CZ  
4964  O OH  . TYR B 160 ? 0.3817 0.4562 0.3301 -0.0558 -0.0355 0.1532  160 TYR B OH  
4965  N N   . ASP B 161 ? 0.2851 0.4216 0.2446 -0.0804 -0.0512 0.1651  161 ASP B N   
4966  C CA  . ASP B 161 ? 0.2866 0.4231 0.2486 -0.0737 -0.0502 0.1745  161 ASP B CA  
4967  C C   . ASP B 161 ? 0.2802 0.4067 0.2455 -0.0656 -0.0467 0.1727  161 ASP B C   
4968  O O   . ASP B 161 ? 0.2678 0.3930 0.2360 -0.0655 -0.0459 0.1660  161 ASP B O   
4969  C CB  . ASP B 161 ? 0.2907 0.4439 0.2587 -0.0755 -0.0532 0.1827  161 ASP B CB  
4970  C CG  . ASP B 161 ? 0.3300 0.4835 0.2997 -0.0694 -0.0526 0.1930  161 ASP B CG  
4971  O OD1 . ASP B 161 ? 0.3350 0.4872 0.2997 -0.0707 -0.0533 0.1974  161 ASP B OD1 
4972  O OD2 . ASP B 161 ? 0.3268 0.4815 0.3029 -0.0635 -0.0513 0.1968  161 ASP B OD2 
4973  N N   . ASP B 162 ? 0.2898 0.4094 0.2547 -0.0589 -0.0445 0.1789  162 ASP B N   
4974  C CA  . ASP B 162 ? 0.2863 0.3950 0.2536 -0.0513 -0.0407 0.1774  162 ASP B CA  
4975  C C   . ASP B 162 ? 0.2802 0.3977 0.2567 -0.0485 -0.0410 0.1796  162 ASP B C   
4976  O O   . ASP B 162 ? 0.3262 0.4368 0.3053 -0.0444 -0.0385 0.1750  162 ASP B O   
4977  C CB  . ASP B 162 ? 0.3180 0.4174 0.2828 -0.0453 -0.0383 0.1839  162 ASP B CB  
4978  C CG  . ASP B 162 ? 0.3426 0.4273 0.2984 -0.0455 -0.0359 0.1795  162 ASP B CG  
4979  O OD1 . ASP B 162 ? 0.3224 0.3994 0.2753 -0.0468 -0.0345 0.1704  162 ASP B OD1 
4980  O OD2 . ASP B 162 ? 0.3853 0.4661 0.3369 -0.0443 -0.0354 0.1852  162 ASP B OD2 
4981  N N   . TRP B 163 ? 0.2847 0.4173 0.2663 -0.0505 -0.0439 0.1868  163 TRP B N   
4982  C CA  . TRP B 163 ? 0.2815 0.4227 0.2721 -0.0471 -0.0440 0.1907  163 TRP B CA  
4983  C C   . TRP B 163 ? 0.2778 0.4363 0.2723 -0.0538 -0.0478 0.1917  163 TRP B C   
4984  O O   . TRP B 163 ? 0.2850 0.4558 0.2840 -0.0542 -0.0498 0.2000  163 TRP B O   
4985  C CB  . TRP B 163 ? 0.2939 0.4353 0.2879 -0.0406 -0.0428 0.2008  163 TRP B CB  
4986  C CG  . TRP B 163 ? 0.3013 0.4264 0.2898 -0.0355 -0.0395 0.2010  163 TRP B CG  
4987  C CD1 . TRP B 163 ? 0.3145 0.4358 0.2977 -0.0354 -0.0396 0.2062  163 TRP B CD1 
4988  C CD2 . TRP B 163 ? 0.2964 0.4064 0.2839 -0.0302 -0.0354 0.1956  163 TRP B CD2 
4989  N NE1 . TRP B 163 ? 0.3182 0.4230 0.2972 -0.0303 -0.0358 0.2045  163 TRP B NE1 
4990  C CE2 . TRP B 163 ? 0.3074 0.4051 0.2889 -0.0272 -0.0332 0.1979  163 TRP B CE2 
4991  C CE3 . TRP B 163 ? 0.2841 0.3899 0.2750 -0.0279 -0.0334 0.1890  163 TRP B CE3 
4992  C CZ2 . TRP B 163 ? 0.3446 0.4261 0.3233 -0.0222 -0.0290 0.1939  163 TRP B CZ2 
4993  C CZ3 . TRP B 163 ? 0.2850 0.3750 0.2733 -0.0228 -0.0294 0.1850  163 TRP B CZ3 
4994  C CH2 . TRP B 163 ? 0.3399 0.4180 0.3222 -0.0201 -0.0272 0.1874  163 TRP B CH2 
4995  N N   . LYS B 164 ? 0.2665 0.4260 0.2596 -0.0593 -0.0487 0.1832  164 LYS B N   
4996  C CA  . LYS B 164 ? 0.2631 0.4385 0.2596 -0.0663 -0.0520 0.1837  164 LYS B CA  
4997  C C   . LYS B 164 ? 0.2585 0.4435 0.2640 -0.0637 -0.0519 0.1868  164 LYS B C   
4998  O O   . LYS B 164 ? 0.2567 0.4557 0.2655 -0.0692 -0.0545 0.1883  164 LYS B O   
4999  C CB  . LYS B 164 ? 0.2527 0.4262 0.2453 -0.0731 -0.0528 0.1736  164 LYS B CB  
5000  C CG  . LYS B 164 ? 0.2586 0.4303 0.2435 -0.0790 -0.0544 0.1721  164 LYS B CG  
5001  C CD  . LYS B 164 ? 0.2529 0.4244 0.2351 -0.0863 -0.0552 0.1625  164 LYS B CD  
5002  C CE  . LYS B 164 ? 0.3054 0.4792 0.2811 -0.0935 -0.0574 0.1622  164 LYS B CE  
5003  N NZ  . LYS B 164 ? 0.2466 0.4190 0.2195 -0.1007 -0.0580 0.1526  164 LYS B NZ  
5004  N N   . GLY B 165 ? 0.2569 0.4350 0.2664 -0.0558 -0.0490 0.1880  165 GLY B N   
5005  C CA  . GLY B 165 ? 0.2538 0.4408 0.2720 -0.0528 -0.0486 0.1918  165 GLY B CA  
5006  C C   . GLY B 165 ? 0.2658 0.4603 0.2889 -0.0485 -0.0489 0.2032  165 GLY B C   
5007  O O   . GLY B 165 ? 0.2641 0.4665 0.2948 -0.0457 -0.0485 0.2071  165 GLY B O   
5008  N N   . ASP B 166 ? 0.2782 0.4705 0.2971 -0.0479 -0.0496 0.2088  166 ASP B N   
5009  C CA  . ASP B 166 ? 0.2905 0.4882 0.3138 -0.0431 -0.0496 0.2198  166 ASP B CA  
5010  C C   . ASP B 166 ? 0.2921 0.5090 0.3224 -0.0463 -0.0524 0.2263  166 ASP B C   
5011  O O   . ASP B 166 ? 0.2880 0.5148 0.3173 -0.0540 -0.0552 0.2237  166 ASP B O   
5012  C CB  . ASP B 166 ? 0.3035 0.4969 0.3204 -0.0436 -0.0504 0.2243  166 ASP B CB  
5013  C CG  . ASP B 166 ? 0.3069 0.4823 0.3197 -0.0372 -0.0467 0.2226  166 ASP B CG  
5014  O OD1 . ASP B 166 ? 0.3216 0.4884 0.3369 -0.0323 -0.0436 0.2183  166 ASP B OD1 
5015  O OD2 . ASP B 166 ? 0.3296 0.4992 0.3363 -0.0373 -0.0468 0.2255  166 ASP B OD2 
5016  N N   . PHE B 167 ? 0.2986 0.5205 0.3359 -0.0404 -0.0515 0.2348  167 PHE B N   
5017  C CA  . PHE B 167 ? 0.3052 0.5452 0.3482 -0.0428 -0.0543 0.2437  167 PHE B CA  
5018  C C   . PHE B 167 ? 0.3168 0.5617 0.3546 -0.0474 -0.0574 0.2488  167 PHE B C   
5019  O O   . PHE B 167 ? 0.3238 0.5577 0.3556 -0.0454 -0.0565 0.2492  167 PHE B O   
5020  C CB  . PHE B 167 ? 0.3118 0.5546 0.3630 -0.0348 -0.0524 0.2525  167 PHE B CB  
5021  C CG  . PHE B 167 ? 0.3019 0.5460 0.3602 -0.0314 -0.0502 0.2500  167 PHE B CG  
5022  C CD1 . PHE B 167 ? 0.2932 0.5226 0.3505 -0.0270 -0.0466 0.2424  167 PHE B CD1 
5023  C CD2 . PHE B 167 ? 0.3017 0.5619 0.3677 -0.0325 -0.0515 0.2554  167 PHE B CD2 
5024  C CE1 . PHE B 167 ? 0.2843 0.5149 0.3481 -0.0239 -0.0445 0.2401  167 PHE B CE1 
5025  C CE2 . PHE B 167 ? 0.2928 0.5542 0.3653 -0.0293 -0.0493 0.2532  167 PHE B CE2 
5026  C CZ  . PHE B 167 ? 0.2841 0.5306 0.3555 -0.0250 -0.0458 0.2455  167 PHE B CZ  
5027  N N   . ASP B 168 ? 0.3431 0.6047 0.3831 -0.0536 -0.0608 0.2530  168 ASP B N   
5028  C CA  . ASP B 168 ? 0.3324 0.6018 0.3695 -0.0571 -0.0638 0.2604  168 ASP B CA  
5029  C C   . ASP B 168 ? 0.3433 0.6198 0.3876 -0.0509 -0.0636 0.2721  168 ASP B C   
5030  O O   . ASP B 168 ? 0.3427 0.6329 0.3946 -0.0511 -0.0645 0.2769  168 ASP B O   
5031  C CB  . ASP B 168 ? 0.3305 0.6147 0.3665 -0.0672 -0.0676 0.2594  168 ASP B CB  
5032  C CG  . ASP B 168 ? 0.4291 0.7190 0.4601 -0.0720 -0.0707 0.2649  168 ASP B CG  
5033  O OD1 . ASP B 168 ? 0.3550 0.6458 0.3874 -0.0675 -0.0708 0.2739  168 ASP B OD1 
5034  O OD2 . ASP B 168 ? 0.4508 0.7442 0.4764 -0.0805 -0.0729 0.2601  168 ASP B OD2 
5035  N N   . ILE B 169 ? 0.3535 0.6202 0.3955 -0.0453 -0.0620 0.2766  169 ILE B N   
5036  C CA  . ILE B 169 ? 0.3641 0.6355 0.4130 -0.0385 -0.0612 0.2874  169 ILE B CA  
5037  C C   . ILE B 169 ? 0.3733 0.6637 0.4255 -0.0429 -0.0651 0.2968  169 ILE B C   
5038  O O   . ILE B 169 ? 0.3768 0.6784 0.4376 -0.0398 -0.0652 0.3045  169 ILE B O   
5039  C CB  . ILE B 169 ? 0.4018 0.6580 0.4467 -0.0322 -0.0587 0.2900  169 ILE B CB  
5040  C CG1 . ILE B 169 ? 0.3647 0.6022 0.4062 -0.0283 -0.0547 0.2805  169 ILE B CG1 
5041  C CG2 . ILE B 169 ? 0.3849 0.6454 0.4375 -0.0249 -0.0575 0.3011  169 ILE B CG2 
5042  C CD1 . ILE B 169 ? 0.3559 0.5926 0.4052 -0.0229 -0.0518 0.2786  169 ILE B CD1 
5043  N N   . LYS B 170 ? 0.3932 0.6878 0.4388 -0.0504 -0.0683 0.2964  170 LYS B N   
5044  C CA  . LYS B 170 ? 0.3942 0.7071 0.4422 -0.0555 -0.0723 0.3049  170 LYS B CA  
5045  C C   . LYS B 170 ? 0.3792 0.7078 0.4341 -0.0591 -0.0737 0.3052  170 LYS B C   
5046  O O   . LYS B 170 ? 0.3855 0.7275 0.4478 -0.0574 -0.0747 0.3144  170 LYS B O   
5047  C CB  . LYS B 170 ? 0.4162 0.7299 0.4552 -0.0637 -0.0752 0.3025  170 LYS B CB  
5048  C CG  . LYS B 170 ? 0.4014 0.7329 0.4416 -0.0693 -0.0794 0.3115  170 LYS B CG  
5049  C CD  . LYS B 170 ? 0.4432 0.7734 0.4738 -0.0773 -0.0819 0.3084  170 LYS B CD  
5050  C CE  . LYS B 170 ? 0.5262 0.8744 0.5577 -0.0835 -0.0861 0.3170  170 LYS B CE  
5051  N NZ  . LYS B 170 ? 0.4810 0.8461 0.5183 -0.0890 -0.0880 0.3175  170 LYS B NZ  
5052  N N   . LYS B 171 ? 0.3736 0.7005 0.4263 -0.0641 -0.0735 0.2951  171 LYS B N   
5053  C CA  . LYS B 171 ? 0.3667 0.7072 0.4254 -0.0676 -0.0744 0.2946  171 LYS B CA  
5054  C C   . LYS B 171 ? 0.3557 0.6965 0.4235 -0.0594 -0.0716 0.2980  171 LYS B C   
5055  O O   . LYS B 171 ? 0.3547 0.7098 0.4293 -0.0608 -0.0725 0.3022  171 LYS B O   
5056  C CB  . LYS B 171 ? 0.3447 0.6811 0.3990 -0.0740 -0.0743 0.2826  171 LYS B CB  
5057  C CG  . LYS B 171 ? 0.3738 0.7128 0.4201 -0.0836 -0.0772 0.2788  171 LYS B CG  
5058  C CD  . LYS B 171 ? 0.3985 0.7319 0.4411 -0.0888 -0.0764 0.2666  171 LYS B CD  
5059  C CE  . LYS B 171 ? 0.4667 0.8025 0.5015 -0.0987 -0.0790 0.2623  171 LYS B CE  
5060  N NZ  . LYS B 171 ? 0.5002 0.8339 0.5330 -0.1045 -0.0784 0.2516  171 LYS B NZ  
5061  N N   . LEU B 172 ? 0.3546 0.6797 0.4225 -0.0511 -0.0679 0.2962  172 LEU B N   
5062  C CA  . LEU B 172 ? 0.3529 0.6779 0.4295 -0.0430 -0.0650 0.2997  172 LEU B CA  
5063  C C   . LEU B 172 ? 0.3661 0.7036 0.4497 -0.0397 -0.0660 0.3128  172 LEU B C   
5064  O O   . LEU B 172 ? 0.3653 0.7148 0.4570 -0.0384 -0.0660 0.3176  172 LEU B O   
5065  C CB  . LEU B 172 ? 0.3501 0.6552 0.4249 -0.0352 -0.0607 0.2950  172 LEU B CB  
5066  C CG  . LEU B 172 ? 0.4043 0.7074 0.4878 -0.0263 -0.0572 0.2987  172 LEU B CG  
5067  C CD1 . LEU B 172 ? 0.3372 0.6469 0.4259 -0.0279 -0.0565 0.2943  172 LEU B CD1 
5068  C CD2 . LEU B 172 ? 0.3495 0.6326 0.4303 -0.0190 -0.0530 0.2950  172 LEU B CD2 
5069  N N   . LYS B 173 ? 0.3787 0.7136 0.4591 -0.0382 -0.0669 0.3189  173 LYS B N   
5070  C CA  . LYS B 173 ? 0.3921 0.7390 0.4788 -0.0352 -0.0682 0.3317  173 LYS B CA  
5071  C C   . LYS B 173 ? 0.3938 0.7618 0.4835 -0.0428 -0.0722 0.3363  173 LYS B C   
5072  O O   . LYS B 173 ? 0.3985 0.7796 0.4966 -0.0405 -0.0726 0.3448  173 LYS B O   
5073  C CB  . LYS B 173 ? 0.4051 0.7447 0.4867 -0.0331 -0.0686 0.3366  173 LYS B CB  
5074  C CG  . LYS B 173 ? 0.4054 0.7245 0.4844 -0.0252 -0.0643 0.3332  173 LYS B CG  
5075  C CD  . LYS B 173 ? 0.4827 0.7954 0.5566 -0.0233 -0.0647 0.3389  173 LYS B CD  
5076  C CE  . LYS B 173 ? 0.4615 0.7537 0.5327 -0.0156 -0.0602 0.3359  173 LYS B CE  
5077  N NZ  . LYS B 173 ? 0.5446 0.8304 0.6107 -0.0139 -0.0604 0.3416  173 LYS B NZ  
5078  N N   . GLU B 174 ? 0.3902 0.7617 0.4730 -0.0521 -0.0751 0.3308  174 GLU B N   
5079  C CA  . GLU B 174 ? 0.3918 0.7829 0.4767 -0.0602 -0.0789 0.3345  174 GLU B CA  
5080  C C   . GLU B 174 ? 0.3823 0.7818 0.4743 -0.0602 -0.0778 0.3329  174 GLU B C   
5081  O O   . GLU B 174 ? 0.3868 0.8034 0.4849 -0.0624 -0.0797 0.3404  174 GLU B O   
5082  C CB  . GLU B 174 ? 0.3888 0.7802 0.4647 -0.0703 -0.0816 0.3275  174 GLU B CB  
5083  C CG  . GLU B 174 ? 0.4371 0.8260 0.5064 -0.0723 -0.0837 0.3313  174 GLU B CG  
5084  C CD  . GLU B 174 ? 0.5741 0.9577 0.6336 -0.0807 -0.0852 0.3220  174 GLU B CD  
5085  O OE1 . GLU B 174 ? 0.5758 0.9557 0.6336 -0.0842 -0.0842 0.3123  174 GLU B OE1 
5086  O OE2 . GLU B 174 ? 0.6632 1.0461 0.7167 -0.0839 -0.0872 0.3246  174 GLU B OE2 
5087  N N   . ASN B 175 ? 0.3694 0.7570 0.4608 -0.0579 -0.0748 0.3234  175 ASN B N   
5088  C CA  . ASN B 175 ? 0.3747 0.7693 0.4724 -0.0578 -0.0735 0.3214  175 ASN B CA  
5089  C C   . ASN B 175 ? 0.3648 0.7629 0.4722 -0.0490 -0.0713 0.3299  175 ASN B C   
5090  O O   . ASN B 175 ? 0.3635 0.7749 0.4775 -0.0499 -0.0716 0.3337  175 ASN B O   
5091  C CB  . ASN B 175 ? 0.3451 0.7260 0.4391 -0.0581 -0.0710 0.3087  175 ASN B CB  
5092  C CG  . ASN B 175 ? 0.3381 0.7224 0.4258 -0.0684 -0.0733 0.3008  175 ASN B CG  
5093  O OD1 . ASN B 175 ? 0.3348 0.7325 0.4251 -0.0742 -0.0747 0.3010  175 ASN B OD1 
5094  N ND2 . ASN B 175 ? 0.3553 0.7277 0.4346 -0.0710 -0.0736 0.2939  175 ASN B ND2 
5095  N N   . ILE B 176 ? 0.3707 0.7570 0.4789 -0.0405 -0.0688 0.3329  176 ILE B N   
5096  C CA  . ILE B 176 ? 0.3774 0.7679 0.4950 -0.0322 -0.0667 0.3422  176 ILE B CA  
5097  C C   . ILE B 176 ? 0.3899 0.7993 0.5120 -0.0346 -0.0700 0.3542  176 ILE B C   
5098  O O   . ILE B 176 ? 0.3936 0.8136 0.5246 -0.0308 -0.0693 0.3619  176 ILE B O   
5099  C CB  . ILE B 176 ? 0.3824 0.7556 0.4991 -0.0232 -0.0632 0.3429  176 ILE B CB  
5100  C CG1 . ILE B 176 ? 0.3696 0.7248 0.4823 -0.0210 -0.0599 0.3310  176 ILE B CG1 
5101  C CG2 . ILE B 176 ? 0.3909 0.7684 0.5175 -0.0146 -0.0609 0.3531  176 ILE B CG2 
5102  C CD1 . ILE B 176 ? 0.3740 0.7116 0.4854 -0.0126 -0.0561 0.3309  176 ILE B CD1 
5103  N N   . ALA B 177 ? 0.3967 0.8110 0.5128 -0.0411 -0.0736 0.3560  177 ALA B N   
5104  C CA  . ALA B 177 ? 0.4090 0.8415 0.5289 -0.0440 -0.0771 0.3674  177 ALA B CA  
5105  C C   . ALA B 177 ? 0.4046 0.8551 0.5272 -0.0518 -0.0796 0.3677  177 ALA B C   
5106  O O   . ALA B 177 ? 0.4254 0.8912 0.5558 -0.0508 -0.0804 0.3769  177 ALA B O   
5107  C CB  . ALA B 177 ? 0.4181 0.8488 0.5301 -0.0483 -0.0800 0.3689  177 ALA B CB  
5108  N N   . GLN B 178 ? 0.3943 0.8430 0.5106 -0.0597 -0.0806 0.3576  178 GLN B N   
5109  C CA  . GLN B 178 ? 0.3911 0.8564 0.5086 -0.0683 -0.0831 0.3575  178 GLN B CA  
5110  C C   . GLN B 178 ? 0.3828 0.8524 0.5076 -0.0654 -0.0807 0.3566  178 GLN B C   
5111  O O   . GLN B 178 ? 0.3838 0.8702 0.5126 -0.0702 -0.0824 0.3607  178 GLN B O   
5112  C CB  . GLN B 178 ? 0.3833 0.8447 0.4916 -0.0778 -0.0847 0.3470  178 GLN B CB  
5113  C CG  . GLN B 178 ? 0.4261 0.8850 0.5267 -0.0821 -0.0874 0.3478  178 GLN B CG  
5114  C CD  . GLN B 178 ? 0.4035 0.8816 0.5054 -0.0885 -0.0915 0.3573  178 GLN B CD  
5115  O OE1 . GLN B 178 ? 0.4116 0.9055 0.5192 -0.0912 -0.0926 0.3621  178 GLN B OE1 
5116  N NE2 . GLN B 178 ? 0.4783 0.9552 0.5745 -0.0911 -0.0938 0.3600  178 GLN B NE2 
5117  N N   . HIS B 179 ? 0.3748 0.8298 0.5013 -0.0579 -0.0767 0.3513  179 HIS B N   
5118  C CA  . HIS B 179 ? 0.3669 0.8244 0.4999 -0.0547 -0.0741 0.3500  179 HIS B CA  
5119  C C   . HIS B 179 ? 0.3736 0.8321 0.5157 -0.0447 -0.0715 0.3590  179 HIS B C   
5120  O O   . HIS B 179 ? 0.3723 0.8408 0.5215 -0.0432 -0.0706 0.3628  179 HIS B O   
5121  C CB  . HIS B 179 ? 0.3651 0.8064 0.4940 -0.0539 -0.0711 0.3371  179 HIS B CB  
5122  C CG  . HIS B 179 ? 0.3443 0.7850 0.4652 -0.0637 -0.0731 0.3277  179 HIS B CG  
5123  N ND1 . HIS B 179 ? 0.3388 0.7913 0.4602 -0.0711 -0.0743 0.3254  179 HIS B ND1 
5124  C CD2 . HIS B 179 ? 0.3416 0.7715 0.4538 -0.0675 -0.0739 0.3203  179 HIS B CD2 
5125  C CE1 . HIS B 179 ? 0.3627 0.8115 0.4763 -0.0790 -0.0756 0.3168  179 HIS B CE1 
5126  N NE2 . HIS B 179 ? 0.3492 0.7844 0.4572 -0.0769 -0.0755 0.3135  179 HIS B NE2 
5127  N N   . GLY B 180 ? 0.3813 0.8298 0.5233 -0.0378 -0.0703 0.3627  180 GLY B N   
5128  C CA  . GLY B 180 ? 0.3879 0.8355 0.5383 -0.0279 -0.0673 0.3707  180 GLY B CA  
5129  C C   . GLY B 180 ? 0.3787 0.8091 0.5300 -0.0207 -0.0625 0.3635  180 GLY B C   
5130  O O   . GLY B 180 ? 0.3670 0.7935 0.5165 -0.0233 -0.0614 0.3543  180 GLY B O   
5131  N N   . ALA B 181 ? 0.3853 0.8054 0.5394 -0.0117 -0.0595 0.3674  181 ALA B N   
5132  C CA  . ALA B 181 ? 0.3776 0.7807 0.5324 -0.0048 -0.0547 0.3607  181 ALA B CA  
5133  C C   . ALA B 181 ? 0.3708 0.7795 0.5331 -0.0022 -0.0523 0.3606  181 ALA B C   
5134  O O   . ALA B 181 ? 0.3613 0.7574 0.5234 0.0014  -0.0487 0.3530  181 ALA B O   
5135  C CB  . ALA B 181 ? 0.3879 0.7801 0.5447 0.0042  -0.0518 0.3662  181 ALA B CB  
5136  N N   . ASP B 182 ? 0.3756 0.8031 0.5445 -0.0042 -0.0542 0.3690  182 ASP B N   
5137  C CA  . ASP B 182 ? 0.3693 0.8030 0.5447 -0.0026 -0.0521 0.3688  182 ASP B CA  
5138  C C   . ASP B 182 ? 0.3553 0.7898 0.5259 -0.0102 -0.0532 0.3585  182 ASP B C   
5139  O O   . ASP B 182 ? 0.4247 0.8581 0.5986 -0.0084 -0.0506 0.3548  182 ASP B O   
5140  C CB  . ASP B 182 ? 0.3795 0.8334 0.5633 -0.0025 -0.0538 0.3813  182 ASP B CB  
5141  C CG  . ASP B 182 ? 0.4492 0.9019 0.6401 0.0069  -0.0514 0.3915  182 ASP B CG  
5142  O OD1 . ASP B 182 ? 0.5129 0.9489 0.7018 0.0129  -0.0485 0.3888  182 ASP B OD1 
5143  O OD2 . ASP B 182 ? 0.5425 1.0109 0.7410 0.0081  -0.0524 0.4024  182 ASP B OD2 
5144  N N   . ASN B 183 ? 0.3528 0.7890 0.5156 -0.0187 -0.0567 0.3537  183 ASN B N   
5145  C CA  . ASN B 183 ? 0.3401 0.7768 0.4981 -0.0262 -0.0576 0.3438  183 ASN B CA  
5146  C C   . ASN B 183 ? 0.3293 0.7468 0.4799 -0.0261 -0.0558 0.3315  183 ASN B C   
5147  O O   . ASN B 183 ? 0.3180 0.7340 0.4647 -0.0316 -0.0560 0.3226  183 ASN B O   
5148  C CB  . ASN B 183 ? 0.3433 0.7944 0.4972 -0.0365 -0.0624 0.3455  183 ASN B CB  
5149  C CG  . ASN B 183 ? 0.3501 0.8219 0.5108 -0.0388 -0.0642 0.3553  183 ASN B CG  
5150  O OD1 . ASN B 183 ? 0.3439 0.8220 0.5079 -0.0400 -0.0632 0.3538  183 ASN B OD1 
5151  N ND2 . ASN B 183 ? 0.3631 0.8457 0.5257 -0.0395 -0.0670 0.3653  183 ASN B ND2 
5152  N N   A ILE B 184 ? 0.3328 0.7357 0.4814 -0.0201 -0.0540 0.3309  184 ILE B N   
5153  N N   B ILE B 184 ? 0.3327 0.7355 0.4813 -0.0201 -0.0539 0.3308  184 ILE B N   
5154  C CA  A ILE B 184 ? 0.3234 0.7074 0.4651 -0.0194 -0.0521 0.3196  184 ILE B CA  
5155  C CA  B ILE B 184 ? 0.3232 0.7074 0.4648 -0.0196 -0.0521 0.3195  184 ILE B CA  
5156  C C   A ILE B 184 ? 0.3160 0.6904 0.4622 -0.0123 -0.0474 0.3159  184 ILE B C   
5157  C C   B ILE B 184 ? 0.3159 0.6899 0.4618 -0.0124 -0.0474 0.3156  184 ILE B C   
5158  O O   A ILE B 184 ? 0.3219 0.6897 0.4724 -0.0041 -0.0444 0.3204  184 ILE B O   
5159  O O   B ILE B 184 ? 0.3217 0.6885 0.4717 -0.0042 -0.0444 0.3199  184 ILE B O   
5160  C CB  A ILE B 184 ? 0.3311 0.7039 0.4679 -0.0166 -0.0522 0.3206  184 ILE B CB  
5161  C CB  B ILE B 184 ? 0.3308 0.7040 0.4672 -0.0173 -0.0524 0.3203  184 ILE B CB  
5162  C CG1 A ILE B 184 ? 0.3424 0.7272 0.4771 -0.0218 -0.0565 0.3281  184 ILE B CG1 
5163  C CG1 B ILE B 184 ? 0.3388 0.7230 0.4712 -0.0245 -0.0571 0.3247  184 ILE B CG1 
5164  C CG2 A ILE B 184 ? 0.3213 0.6774 0.4494 -0.0187 -0.0514 0.3085  184 ILE B CG2 
5165  C CG2 B ILE B 184 ? 0.3209 0.6753 0.4498 -0.0172 -0.0506 0.3084  184 ILE B CG2 
5166  C CD1 A ILE B 184 ? 0.3371 0.7285 0.4654 -0.0323 -0.0602 0.3225  184 ILE B CD1 
5167  C CD1 B ILE B 184 ? 0.3472 0.7214 0.4742 -0.0225 -0.0576 0.3261  184 ILE B CD1 
5168  N N   . VAL B 185 ? 0.3033 0.6768 0.4484 -0.0157 -0.0466 0.3076  185 VAL B N   
5169  C CA  . VAL B 185 ? 0.2959 0.6602 0.4447 -0.0095 -0.0423 0.3036  185 VAL B CA  
5170  C C   . VAL B 185 ? 0.2932 0.6373 0.4379 -0.0043 -0.0394 0.2973  185 VAL B C   
5171  O O   . VAL B 185 ? 0.2950 0.6309 0.4441 0.0035  -0.0355 0.2989  185 VAL B O   
5172  C CB  . VAL B 185 ? 0.2830 0.6504 0.4308 -0.0147 -0.0422 0.2959  185 VAL B CB  
5173  C CG1 . VAL B 185 ? 0.2757 0.6336 0.4274 -0.0083 -0.0376 0.2920  185 VAL B CG1 
5174  C CG2 . VAL B 185 ? 0.2865 0.6738 0.4381 -0.0199 -0.0448 0.3024  185 VAL B CG2 
5175  N N   . ALA B 186 ? 0.2894 0.6252 0.4257 -0.0088 -0.0410 0.2902  186 ALA B N   
5176  C CA  . ALA B 186 ? 0.2872 0.6040 0.4188 -0.0046 -0.0385 0.2840  186 ALA B CA  
5177  C C   . ALA B 186 ? 0.2867 0.5991 0.4091 -0.0106 -0.0415 0.2791  186 ALA B C   
5178  O O   . ALA B 186 ? 0.2844 0.6067 0.4039 -0.0186 -0.0450 0.2778  186 ALA B O   
5179  C CB  . ALA B 186 ? 0.2742 0.5796 0.4058 -0.0022 -0.0350 0.2745  186 ALA B CB  
5180  N N   . ILE B 187 ? 0.2893 0.5866 0.4073 -0.0069 -0.0399 0.2766  187 ILE B N   
5181  C CA  . ILE B 187 ? 0.2870 0.5758 0.3956 -0.0116 -0.0417 0.2699  187 ILE B CA  
5182  C C   . ILE B 187 ? 0.2745 0.5478 0.3794 -0.0104 -0.0389 0.2585  187 ILE B C   
5183  O O   . ILE B 187 ? 0.2733 0.5367 0.3812 -0.0034 -0.0350 0.2576  187 ILE B O   
5184  C CB  . ILE B 187 ? 0.2999 0.5828 0.4052 -0.0088 -0.0421 0.2755  187 ILE B CB  
5185  C CG1 . ILE B 187 ? 0.3117 0.6113 0.4202 -0.0112 -0.0454 0.2864  187 ILE B CG1 
5186  C CG2 . ILE B 187 ? 0.2970 0.5681 0.3922 -0.0127 -0.0431 0.2677  187 ILE B CG2 
5187  C CD1 . ILE B 187 ? 0.3259 0.6214 0.4337 -0.0067 -0.0452 0.2941  187 ILE B CD1 
5188  N N   . VAL B 188 ? 0.2653 0.5370 0.3640 -0.0172 -0.0408 0.2499  188 VAL B N   
5189  C CA  . VAL B 188 ? 0.2527 0.5111 0.3477 -0.0171 -0.0386 0.2388  188 VAL B CA  
5190  C C   . VAL B 188 ? 0.2534 0.4997 0.3393 -0.0191 -0.0394 0.2334  188 VAL B C   
5191  O O   . VAL B 188 ? 0.2582 0.5090 0.3390 -0.0263 -0.0426 0.2310  188 VAL B O   
5192  C CB  . VAL B 188 ? 0.2589 0.5248 0.3546 -0.0231 -0.0397 0.2327  188 VAL B CB  
5193  C CG1 . VAL B 188 ? 0.2702 0.5221 0.3621 -0.0228 -0.0375 0.2212  188 VAL B CG1 
5194  C CG2 . VAL B 188 ? 0.2452 0.5231 0.3495 -0.0211 -0.0388 0.2385  188 VAL B CG2 
5195  N N   . SER B 189 ? 0.2553 0.4864 0.3393 -0.0131 -0.0363 0.2316  189 SER B N   
5196  C CA  . SER B 189 ? 0.2557 0.4737 0.3308 -0.0145 -0.0365 0.2260  189 SER B CA  
5197  C C   . SER B 189 ? 0.2414 0.4500 0.3128 -0.0166 -0.0353 0.2142  189 SER B C   
5198  O O   . SER B 189 ? 0.2355 0.4356 0.3093 -0.0117 -0.0319 0.2105  189 SER B O   
5199  C CB  . SER B 189 ? 0.2653 0.4711 0.3395 -0.0073 -0.0335 0.2297  189 SER B CB  
5200  O OG  . SER B 189 ? 0.2791 0.4931 0.3562 -0.0055 -0.0347 0.2406  189 SER B OG  
5201  N N   . THR B 190 ? 0.2361 0.4463 0.3017 -0.0239 -0.0380 0.2084  190 THR B N   
5202  C CA  . THR B 190 ? 0.2225 0.4250 0.2846 -0.0266 -0.0372 0.1973  190 THR B CA  
5203  C C   . THR B 190 ? 0.2228 0.4093 0.2767 -0.0259 -0.0362 0.1915  190 THR B C   
5204  O O   . THR B 190 ? 0.2281 0.4147 0.2762 -0.0301 -0.0385 0.1919  190 THR B O   
5205  C CB  . THR B 190 ? 0.2163 0.4299 0.2773 -0.0353 -0.0405 0.1940  190 THR B CB  
5206  O OG1 . THR B 190 ? 0.2179 0.4473 0.2861 -0.0364 -0.0415 0.2004  190 THR B OG1 
5207  C CG2 . THR B 190 ? 0.2020 0.4085 0.2609 -0.0375 -0.0394 0.1830  190 THR B CG2 
5208  N N   . VAL B 191 ? 0.2172 0.3902 0.2706 -0.0209 -0.0328 0.1860  191 VAL B N   
5209  C CA  . VAL B 191 ? 0.2180 0.3751 0.2639 -0.0195 -0.0312 0.1809  191 VAL B CA  
5210  C C   . VAL B 191 ? 0.2501 0.3983 0.2936 -0.0204 -0.0298 0.1699  191 VAL B C   
5211  O O   . VAL B 191 ? 0.1991 0.3459 0.2476 -0.0170 -0.0275 0.1677  191 VAL B O   
5212  C CB  . VAL B 191 ? 0.2277 0.3752 0.2744 -0.0118 -0.0279 0.1858  191 VAL B CB  
5213  C CG1 . VAL B 191 ? 0.2420 0.3973 0.2900 -0.0112 -0.0295 0.1964  191 VAL B CG1 
5214  C CG2 . VAL B 191 ? 0.2234 0.3699 0.2778 -0.0059 -0.0246 0.1863  191 VAL B CG2 
5215  N N   . THR B 192 ? 0.2043 0.3470 0.2405 -0.0253 -0.0311 0.1631  192 THR B N   
5216  C CA  . THR B 192 ? 0.2165 0.3642 0.2477 -0.0311 -0.0343 0.1652  192 THR B CA  
5217  C C   . THR B 192 ? 0.2049 0.3697 0.2402 -0.0370 -0.0376 0.1679  192 THR B C   
5218  O O   . THR B 192 ? 0.2063 0.3775 0.2474 -0.0369 -0.0373 0.1669  192 THR B O   
5219  C CB  . THR B 192 ? 0.2272 0.3656 0.2503 -0.0354 -0.0348 0.1562  192 THR B CB  
5220  O OG1 . THR B 192 ? 0.1872 0.3263 0.2119 -0.0382 -0.0349 0.1481  192 THR B OG1 
5221  C CG2 . THR B 192 ? 0.2399 0.3612 0.2574 -0.0305 -0.0317 0.1536  192 THR B CG2 
5222  N N   . CYS B 193 ? 0.2149 0.3870 0.2470 -0.0424 -0.0406 0.1713  193 CYS B N   
5223  C CA  . CYS B 193 ? 0.2112 0.3999 0.2467 -0.0486 -0.0437 0.1741  193 CYS B CA  
5224  C C   . CYS B 193 ? 0.1992 0.3881 0.2324 -0.0552 -0.0446 0.1645  193 CYS B C   
5225  O O   . CYS B 193 ? 0.2182 0.4047 0.2453 -0.0606 -0.0462 0.1605  193 CYS B O   
5226  C CB  . CYS B 193 ? 0.2235 0.4201 0.2564 -0.0522 -0.0465 0.1812  193 CYS B CB  
5227  S SG  . CYS B 193 ? 0.2246 0.4422 0.2621 -0.0595 -0.0499 0.1859  193 CYS B SG  
5228  N N   . ASN B 194 ? 0.1909 0.3822 0.2291 -0.0547 -0.0435 0.1609  194 ASN B N   
5229  C CA  . ASN B 194 ? 0.2066 0.3970 0.2432 -0.0603 -0.0439 0.1516  194 ASN B CA  
5230  C C   . ASN B 194 ? 0.1987 0.3997 0.2329 -0.0695 -0.0471 0.1516  194 ASN B C   
5231  O O   . ASN B 194 ? 0.2657 0.4616 0.2942 -0.0744 -0.0480 0.1455  194 ASN B O   
5232  C CB  . ASN B 194 ? 0.2072 0.4011 0.2503 -0.0585 -0.0424 0.1496  194 ASN B CB  
5233  C CG  . ASN B 194 ? 0.2713 0.4605 0.3128 -0.0625 -0.0419 0.1391  194 ASN B CG  
5234  O OD1 . ASN B 194 ? 0.2813 0.4644 0.3171 -0.0666 -0.0428 0.1331  194 ASN B OD1 
5235  N ND2 . ASN B 194 ? 0.3026 0.4945 0.3494 -0.0613 -0.0405 0.1371  194 ASN B ND2 
5236  N N   . SER B 195 ? 0.2060 0.4219 0.2446 -0.0721 -0.0488 0.1587  195 SER B N   
5237  C CA  . SER B 195 ? 0.2614 0.4886 0.2982 -0.0813 -0.0516 0.1591  195 SER B CA  
5238  C C   . SER B 195 ? 0.3299 0.5535 0.3595 -0.0847 -0.0533 0.1592  195 SER B C   
5239  O O   . SER B 195 ? 0.3408 0.5667 0.3667 -0.0925 -0.0548 0.1547  195 SER B O   
5240  C CB  . SER B 195 ? 0.3107 0.5540 0.3531 -0.0822 -0.0529 0.1684  195 SER B CB  
5241  O OG  . SER B 195 ? 0.3472 0.5909 0.3961 -0.0756 -0.0508 0.1708  195 SER B OG  
5242  N N   . ALA B 196 ? 0.3432 0.5609 0.3708 -0.0791 -0.0529 0.1644  196 ALA B N   
5243  C CA  . ALA B 196 ? 0.2208 0.4341 0.2413 -0.0820 -0.0543 0.1645  196 ALA B CA  
5244  C C   . ALA B 196 ? 0.2885 0.4873 0.3030 -0.0826 -0.0530 0.1548  196 ALA B C   
5245  O O   . ALA B 196 ? 0.2804 0.4745 0.2885 -0.0852 -0.0538 0.1540  196 ALA B O   
5246  C CB  . ALA B 196 ? 0.2505 0.4612 0.2706 -0.0757 -0.0539 0.1730  196 ALA B CB  
5247  N N   . GLY B 197 ? 0.2831 0.4748 0.2993 -0.0804 -0.0510 0.1476  197 GLY B N   
5248  C CA  . GLY B 197 ? 0.2450 0.4234 0.2560 -0.0811 -0.0498 0.1384  197 GLY B CA  
5249  C C   . GLY B 197 ? 0.2102 0.3745 0.2206 -0.0725 -0.0467 0.1364  197 GLY B C   
5250  O O   . GLY B 197 ? 0.2284 0.3805 0.2331 -0.0717 -0.0456 0.1311  197 GLY B O   
5251  N N   . GLY B 198 ? 0.2022 0.3679 0.2184 -0.0662 -0.0451 0.1407  198 GLY B N   
5252  C CA  . GLY B 198 ? 0.2026 0.3552 0.2184 -0.0581 -0.0420 0.1396  198 GLY B CA  
5253  C C   . GLY B 198 ? 0.2341 0.3791 0.2450 -0.0546 -0.0412 0.1442  198 GLY B C   
5254  O O   . GLY B 198 ? 0.2277 0.3588 0.2350 -0.0501 -0.0386 0.1408  198 GLY B O   
5255  N N   . GLN B 199 ? 0.2048 0.3586 0.2153 -0.0568 -0.0433 0.1519  199 GLN B N   
5256  C CA  . GLN B 199 ? 0.2174 0.3666 0.2229 -0.0553 -0.0433 0.1571  199 GLN B CA  
5257  C C   . GLN B 199 ? 0.2257 0.3727 0.2349 -0.0474 -0.0413 0.1650  199 GLN B C   
5258  O O   . GLN B 199 ? 0.2268 0.3841 0.2431 -0.0456 -0.0417 0.1708  199 GLN B O   
5259  C CB  . GLN B 199 ? 0.2250 0.3864 0.2289 -0.0621 -0.0469 0.1617  199 GLN B CB  
5260  C CG  . GLN B 199 ? 0.2308 0.3935 0.2303 -0.0705 -0.0488 0.1543  199 GLN B CG  
5261  C CD  . GLN B 199 ? 0.2253 0.3731 0.2174 -0.0701 -0.0472 0.1473  199 GLN B CD  
5262  O OE1 . GLN B 199 ? 0.2360 0.3750 0.2241 -0.0661 -0.0457 0.1501  199 GLN B OE1 
5263  N NE2 . GLN B 199 ? 0.2098 0.3546 0.2005 -0.0744 -0.0473 0.1381  199 GLN B NE2 
5264  N N   . PRO B 200 ? 0.2320 0.3658 0.2365 -0.0428 -0.0389 0.1655  200 PRO B N   
5265  C CA  . PRO B 200 ? 0.2446 0.3740 0.2526 -0.0350 -0.0363 0.1718  200 PRO B CA  
5266  C C   . PRO B 200 ? 0.2520 0.3920 0.2630 -0.0344 -0.0380 0.1828  200 PRO B C   
5267  O O   . PRO B 200 ? 0.2626 0.4102 0.2708 -0.0396 -0.0410 0.1858  200 PRO B O   
5268  C CB  . PRO B 200 ? 0.2454 0.3575 0.2462 -0.0318 -0.0333 0.1684  200 PRO B CB  
5269  C CG  . PRO B 200 ? 0.2436 0.3549 0.2369 -0.0383 -0.0354 0.1647  200 PRO B CG  
5270  C CD  . PRO B 200 ? 0.2332 0.3557 0.2290 -0.0449 -0.0383 0.1602  200 PRO B CD  
5271  N N   . VAL B 201 ? 0.2625 0.4032 0.2798 -0.0279 -0.0361 0.1888  201 VAL B N   
5272  C CA  . VAL B 201 ? 0.2695 0.4180 0.2901 -0.0256 -0.0370 0.1998  201 VAL B CA  
5273  C C   . VAL B 201 ? 0.2790 0.4137 0.2968 -0.0192 -0.0337 0.2026  201 VAL B C   
5274  O O   . VAL B 201 ? 0.3342 0.4580 0.3531 -0.0141 -0.0302 0.1990  201 VAL B O   
5275  C CB  . VAL B 201 ? 0.2677 0.4285 0.2984 -0.0231 -0.0372 0.2052  201 VAL B CB  
5276  C CG1 . VAL B 201 ? 0.2816 0.4518 0.3160 -0.0211 -0.0384 0.2168  201 VAL B CG1 
5277  C CG2 . VAL B 201 ? 0.2567 0.4292 0.2900 -0.0293 -0.0397 0.2009  201 VAL B CG2 
5278  N N   . SER B 202 ? 0.2918 0.4265 0.3057 -0.0198 -0.0348 0.2087  202 SER B N   
5279  C CA  . SER B 202 ? 0.3017 0.4225 0.3119 -0.0145 -0.0317 0.2111  202 SER B CA  
5280  C C   . SER B 202 ? 0.3181 0.4392 0.3362 -0.0070 -0.0291 0.2178  202 SER B C   
5281  O O   . SER B 202 ? 0.3064 0.4404 0.3326 -0.0062 -0.0304 0.2230  202 SER B O   
5282  C CB  . SER B 202 ? 0.3145 0.4361 0.3188 -0.0171 -0.0336 0.2166  202 SER B CB  
5283  O OG  . SER B 202 ? 0.3241 0.4586 0.3342 -0.0160 -0.0356 0.2270  202 SER B OG  
5284  N N   . MET B 203 ? 0.3128 0.4192 0.3284 -0.0017 -0.0254 0.2177  203 MET B N   
5285  C CA  . MET B 203 ? 0.3194 0.4248 0.3422 0.0055  -0.0225 0.2242  203 MET B CA  
5286  C C   . MET B 203 ? 0.3363 0.4522 0.3628 0.0067  -0.0244 0.2358  203 MET B C   
5287  O O   . MET B 203 ? 0.3701 0.4940 0.4054 0.0108  -0.0237 0.2423  203 MET B O   
5288  C CB  . MET B 203 ? 0.3324 0.4194 0.3511 0.0103  -0.0180 0.2213  203 MET B CB  
5289  C CG  . MET B 203 ? 0.3288 0.4138 0.3554 0.0177  -0.0144 0.2265  203 MET B CG  
5290  S SD  . MET B 203 ? 0.3620 0.4499 0.3965 0.0198  -0.0126 0.2207  203 MET B SD  
5291  C CE  . MET B 203 ? 0.3331 0.4030 0.3593 0.0187  -0.0099 0.2084  203 MET B CE  
5292  N N   . SER B 204 ? 0.3418 0.4580 0.3618 0.0032  -0.0266 0.2387  204 SER B N   
5293  C CA  . SER B 204 ? 0.3551 0.4815 0.3784 0.0041  -0.0285 0.2499  204 SER B CA  
5294  C C   . SER B 204 ? 0.3514 0.4975 0.3807 0.0001  -0.0325 0.2536  204 SER B C   
5295  O O   . SER B 204 ? 0.3598 0.5167 0.3956 0.0025  -0.0335 0.2632  204 SER B O   
5296  C CB  . SER B 204 ? 0.3660 0.4868 0.3802 0.0014  -0.0297 0.2519  204 SER B CB  
5297  O OG  . SER B 204 ? 0.4355 0.5577 0.4428 -0.0059 -0.0324 0.2452  204 SER B OG  
5298  N N   . ASN B 205 ? 0.3392 0.4904 0.3666 -0.0060 -0.0348 0.2464  205 ASN B N   
5299  C CA  . ASN B 205 ? 0.3348 0.5044 0.3681 -0.0101 -0.0383 0.2491  205 ASN B CA  
5300  C C   . ASN B 205 ? 0.3291 0.5039 0.3724 -0.0054 -0.0364 0.2506  205 ASN B C   
5301  O O   . ASN B 205 ? 0.3327 0.5221 0.3833 -0.0051 -0.0381 0.2582  205 ASN B O   
5302  C CB  . ASN B 205 ? 0.3235 0.4960 0.3519 -0.0180 -0.0408 0.2404  205 ASN B CB  
5303  C CG  . ASN B 205 ? 0.3202 0.5117 0.3535 -0.0234 -0.0446 0.2432  205 ASN B CG  
5304  O OD1 . ASN B 205 ? 0.3093 0.5063 0.3476 -0.0243 -0.0445 0.2394  205 ASN B OD1 
5305  N ND2 . ASN B 205 ? 0.3611 0.5629 0.3931 -0.0274 -0.0479 0.2498  205 ASN B ND2 
5306  N N   . LEU B 206 ? 0.3205 0.4836 0.3642 -0.0017 -0.0328 0.2436  206 LEU B N   
5307  C CA  . LEU B 206 ? 0.3161 0.4825 0.3690 0.0034  -0.0304 0.2451  206 LEU B CA  
5308  C C   . LEU B 206 ? 0.3294 0.4974 0.3882 0.0100  -0.0286 0.2556  206 LEU B C   
5309  O O   . LEU B 206 ? 0.3302 0.5097 0.3979 0.0123  -0.0286 0.2615  206 LEU B O   
5310  C CB  . LEU B 206 ? 0.3059 0.4579 0.3573 0.0062  -0.0266 0.2358  206 LEU B CB  
5311  C CG  . LEU B 206 ? 0.2905 0.4414 0.3387 0.0011  -0.0277 0.2251  206 LEU B CG  
5312  C CD1 . LEU B 206 ? 0.2831 0.4184 0.3297 0.0049  -0.0235 0.2171  206 LEU B CD1 
5313  C CD2 . LEU B 206 ? 0.2824 0.4491 0.3375 -0.0018 -0.0298 0.2258  206 LEU B CD2 
5314  N N   . LYS B 207 ? 0.3401 0.4966 0.3943 0.0131  -0.0268 0.2581  207 LYS B N   
5315  C CA  . LYS B 207 ? 0.3532 0.5095 0.4128 0.0198  -0.0245 0.2677  207 LYS B CA  
5316  C C   . LYS B 207 ? 0.3628 0.5357 0.4266 0.0182  -0.0281 0.2782  207 LYS B C   
5317  O O   . LYS B 207 ? 0.3686 0.5493 0.4411 0.0228  -0.0271 0.2862  207 LYS B O   
5318  C CB  . LYS B 207 ? 0.3626 0.5019 0.4152 0.0227  -0.0219 0.2673  207 LYS B CB  
5319  C CG  . LYS B 207 ? 0.3778 0.5159 0.4350 0.0292  -0.0196 0.2774  207 LYS B CG  
5320  C CD  . LYS B 207 ? 0.4649 0.5844 0.5150 0.0321  -0.0162 0.2754  207 LYS B CD  
5321  C CE  . LYS B 207 ? 0.4320 0.5490 0.4869 0.0390  -0.0134 0.2850  207 LYS B CE  
5322  N NZ  . LYS B 207 ? 0.5356 0.6657 0.5927 0.0380  -0.0168 0.2955  207 LYS B NZ  
5323  N N   . GLU B 208 ? 0.3649 0.5437 0.4228 0.0117  -0.0322 0.2785  208 GLU B N   
5324  C CA  . GLU B 208 ? 0.3745 0.5694 0.4359 0.0097  -0.0357 0.2886  208 GLU B CA  
5325  C C   . GLU B 208 ? 0.3677 0.5798 0.4374 0.0078  -0.0376 0.2907  208 GLU B C   
5326  O O   . GLU B 208 ? 0.3757 0.5999 0.4528 0.0101  -0.0384 0.3004  208 GLU B O   
5327  C CB  . GLU B 208 ? 0.3781 0.5749 0.4307 0.0026  -0.0395 0.2877  208 GLU B CB  
5328  C CG  . GLU B 208 ? 0.3897 0.6019 0.4451 0.0006  -0.0430 0.2984  208 GLU B CG  
5329  C CD  . GLU B 208 ? 0.4486 0.6600 0.4949 -0.0051 -0.0460 0.2985  208 GLU B CD  
5330  O OE1 . GLU B 208 ? 0.4856 0.6861 0.5234 -0.0086 -0.0457 0.2896  208 GLU B OE1 
5331  O OE2 . GLU B 208 ? 0.4508 0.6726 0.4984 -0.0062 -0.0485 0.3077  208 GLU B OE2 
5332  N N   . VAL B 209 ? 0.3532 0.5668 0.4220 0.0035  -0.0384 0.2819  209 VAL B N   
5333  C CA  . VAL B 209 ? 0.3462 0.5756 0.4226 0.0013  -0.0400 0.2833  209 VAL B CA  
5334  C C   . VAL B 209 ? 0.3477 0.5783 0.4338 0.0089  -0.0365 0.2882  209 VAL B C   
5335  O O   . VAL B 209 ? 0.3512 0.5966 0.4450 0.0095  -0.0377 0.2958  209 VAL B O   
5336  C CB  . VAL B 209 ? 0.3303 0.5585 0.4034 -0.0042 -0.0408 0.2721  209 VAL B CB  
5337  C CG1 . VAL B 209 ? 0.3226 0.5644 0.4039 -0.0052 -0.0413 0.2730  209 VAL B CG1 
5338  C CG2 . VAL B 209 ? 0.3296 0.5607 0.3946 -0.0126 -0.0446 0.2687  209 VAL B CG2 
5339  N N   . TYR B 210 ? 0.3453 0.5604 0.4311 0.0148  -0.0321 0.2838  210 TYR B N   
5340  C CA  . TYR B 210 ? 0.3468 0.5621 0.4417 0.0220  -0.0283 0.2879  210 TYR B CA  
5341  C C   . TYR B 210 ? 0.3775 0.5981 0.4775 0.0269  -0.0279 0.3002  210 TYR B C   
5342  O O   . TYR B 210 ? 0.4374 0.6682 0.5465 0.0303  -0.0270 0.3070  210 TYR B O   
5343  C CB  . TYR B 210 ? 0.3417 0.5387 0.4344 0.0267  -0.0235 0.2805  210 TYR B CB  
5344  C CG  . TYR B 210 ? 0.3418 0.5380 0.4436 0.0338  -0.0193 0.2832  210 TYR B CG  
5345  C CD1 . TYR B 210 ? 0.3317 0.5365 0.4397 0.0332  -0.0190 0.2811  210 TYR B CD1 
5346  C CD2 . TYR B 210 ? 0.3523 0.5386 0.4560 0.0409  -0.0152 0.2876  210 TYR B CD2 
5347  C CE1 . TYR B 210 ? 0.3410 0.5449 0.4570 0.0395  -0.0150 0.2835  210 TYR B CE1 
5348  C CE2 . TYR B 210 ? 0.3527 0.5380 0.4647 0.0472  -0.0110 0.2900  210 TYR B CE2 
5349  C CZ  . TYR B 210 ? 0.3425 0.5367 0.4605 0.0465  -0.0109 0.2879  210 TYR B CZ  
5350  O OH  . TYR B 210 ? 0.3667 0.5600 0.4928 0.0527  -0.0065 0.2901  210 TYR B OH  
5351  N N   . GLU B 211 ? 0.3893 0.6028 0.4834 0.0273  -0.0283 0.3031  211 GLU B N   
5352  C CA  . GLU B 211 ? 0.3895 0.6076 0.4880 0.0318  -0.0280 0.3149  211 GLU B CA  
5353  C C   . GLU B 211 ? 0.3936 0.6325 0.4969 0.0280  -0.0324 0.3232  211 GLU B C   
5354  O O   . GLU B 211 ? 0.4021 0.6503 0.5137 0.0323  -0.0317 0.3328  211 GLU B O   
5355  C CB  . GLU B 211 ? 0.3997 0.6056 0.4899 0.0322  -0.0277 0.3157  211 GLU B CB  
5356  C CG  . GLU B 211 ? 0.4002 0.5864 0.4878 0.0378  -0.0226 0.3109  211 GLU B CG  
5357  C CD  . GLU B 211 ? 0.4504 0.6229 0.5275 0.0363  -0.0226 0.3082  211 GLU B CD  
5358  O OE1 . GLU B 211 ? 0.4140 0.5922 0.4859 0.0312  -0.0265 0.3107  211 GLU B OE1 
5359  O OE2 . GLU B 211 ? 0.5060 0.6619 0.5798 0.0400  -0.0185 0.3035  211 GLU B OE2 
5360  N N   . ILE B 212 ? 0.3880 0.6345 0.4861 0.0198  -0.0368 0.3195  212 ILE B N   
5361  C CA  . ILE B 212 ? 0.3910 0.6578 0.4933 0.0152  -0.0410 0.3265  212 ILE B CA  
5362  C C   . ILE B 212 ? 0.3860 0.6639 0.4980 0.0170  -0.0401 0.3282  212 ILE B C   
5363  O O   . ILE B 212 ? 0.4074 0.6988 0.5271 0.0190  -0.0409 0.3381  212 ILE B O   
5364  C CB  . ILE B 212 ? 0.3851 0.6565 0.4795 0.0056  -0.0454 0.3207  212 ILE B CB  
5365  C CG1 . ILE B 212 ? 0.3948 0.6586 0.4805 0.0039  -0.0467 0.3220  212 ILE B CG1 
5366  C CG2 . ILE B 212 ? 0.3851 0.6777 0.4842 0.0001  -0.0494 0.3260  212 ILE B CG2 
5367  C CD1 . ILE B 212 ? 0.3892 0.6546 0.4662 -0.0052 -0.0504 0.3152  212 ILE B CD1 
5368  N N   . ALA B 213 ? 0.3707 0.6426 0.4824 0.0165  -0.0382 0.3188  213 ALA B N   
5369  C CA  . ALA B 213 ? 0.3640 0.6459 0.4843 0.0177  -0.0372 0.3197  213 ALA B CA  
5370  C C   . ALA B 213 ? 0.3791 0.6587 0.5079 0.0269  -0.0330 0.3265  213 ALA B C   
5371  O O   . ALA B 213 ? 0.4132 0.7058 0.5506 0.0286  -0.0329 0.3330  213 ALA B O   
5372  C CB  . ALA B 213 ? 0.3475 0.6225 0.4650 0.0151  -0.0361 0.3076  213 ALA B CB  
5373  N N   . LYS B 214 ? 0.4454 0.7084 0.5719 0.0327  -0.0292 0.3252  214 LYS B N   
5374  C CA  . LYS B 214 ? 0.4516 0.7106 0.5858 0.0414  -0.0245 0.3304  214 LYS B CA  
5375  C C   . LYS B 214 ? 0.5001 0.7715 0.6411 0.0444  -0.0255 0.3439  214 LYS B C   
5376  O O   . LYS B 214 ? 0.5336 0.8131 0.6840 0.0488  -0.0236 0.3500  214 LYS B O   
5377  C CB  . LYS B 214 ? 0.4539 0.6921 0.5834 0.0462  -0.0203 0.3258  214 LYS B CB  
5378  C CG  . LYS B 214 ? 0.4875 0.7150 0.6185 0.0493  -0.0159 0.3173  214 LYS B CG  
5379  C CD  . LYS B 214 ? 0.4983 0.7344 0.6404 0.0543  -0.0133 0.3229  214 LYS B CD  
5380  C CE  . LYS B 214 ? 0.5229 0.7484 0.6665 0.0575  -0.0087 0.3148  214 LYS B CE  
5381  N NZ  . LYS B 214 ? 0.5759 0.8107 0.7301 0.0616  -0.0063 0.3199  214 LYS B NZ  
5382  N N   . GLN B 215 ? 0.5275 0.8009 0.6639 0.0421  -0.0285 0.3488  215 GLN B N   
5383  C CA  . GLN B 215 ? 0.5418 0.8277 0.6846 0.0447  -0.0297 0.3618  215 GLN B CA  
5384  C C   . GLN B 215 ? 0.5429 0.8504 0.6916 0.0402  -0.0334 0.3669  215 GLN B C   
5385  O O   . GLN B 215 ? 0.5571 0.8766 0.7130 0.0430  -0.0340 0.3781  215 GLN B O   
5386  C CB  . GLN B 215 ? 0.5533 0.8356 0.6892 0.0430  -0.0320 0.3657  215 GLN B CB  
5387  C CG  . GLN B 215 ? 0.5488 0.8376 0.6769 0.0336  -0.0373 0.3618  215 GLN B CG  
5388  C CD  . GLN B 215 ? 0.5874 0.8738 0.7091 0.0321  -0.0395 0.3665  215 GLN B CD  
5389  O OE1 . GLN B 215 ? 0.6667 0.9615 0.7835 0.0248  -0.0441 0.3665  215 GLN B OE1 
5390  N NE2 . GLN B 215 ? 0.5967 0.8713 0.7184 0.0388  -0.0362 0.3705  215 GLN B NE2 
5391  N N   . HIS B 216 ? 0.4619 0.7746 0.6078 0.0334  -0.0359 0.3593  216 HIS B N   
5392  C CA  . HIS B 216 ? 0.4212 0.7539 0.5724 0.0288  -0.0392 0.3634  216 HIS B CA  
5393  C C   . HIS B 216 ? 0.3934 0.7290 0.5512 0.0308  -0.0366 0.3603  216 HIS B C   
5394  O O   . HIS B 216 ? 0.3895 0.7407 0.5511 0.0265  -0.0390 0.3621  216 HIS B O   
5395  C CB  . HIS B 216 ? 0.3972 0.7361 0.5407 0.0187  -0.0441 0.3580  216 HIS B CB  
5396  C CG  . HIS B 216 ? 0.4819 0.8231 0.6200 0.0156  -0.0475 0.3629  216 HIS B CG  
5397  N ND1 . HIS B 216 ? 0.4799 0.8054 0.6093 0.0157  -0.0469 0.3584  216 HIS B ND1 
5398  C CD2 . HIS B 216 ? 0.4379 0.7951 0.5778 0.0120  -0.0514 0.3721  216 HIS B CD2 
5399  C CE1 . HIS B 216 ? 0.4787 0.8104 0.6048 0.0125  -0.0503 0.3645  216 HIS B CE1 
5400  N NE2 . HIS B 216 ? 0.5386 0.8896 0.6711 0.0102  -0.0531 0.3729  216 HIS B NE2 
5401  N N   . GLY B 217 ? 0.3894 0.7104 0.5485 0.0371  -0.0316 0.3556  217 GLY B N   
5402  C CA  . GLY B 217 ? 0.3803 0.7029 0.5455 0.0394  -0.0287 0.3525  217 GLY B CA  
5403  C C   . GLY B 217 ? 0.3871 0.7107 0.5481 0.0326  -0.0304 0.3420  217 GLY B C   
5404  O O   . GLY B 217 ? 0.4043 0.7381 0.5705 0.0314  -0.0305 0.3423  217 GLY B O   
5405  N N   . ILE B 218 ? 0.3578 0.6707 0.5093 0.0283  -0.0317 0.3328  218 ILE B N   
5406  C CA  . ILE B 218 ? 0.3467 0.6606 0.4935 0.0212  -0.0336 0.3229  218 ILE B CA  
5407  C C   . ILE B 218 ? 0.3328 0.6286 0.4760 0.0239  -0.0298 0.3120  218 ILE B C   
5408  O O   . ILE B 218 ? 0.3875 0.6684 0.5251 0.0261  -0.0283 0.3084  218 ILE B O   
5409  C CB  . ILE B 218 ? 0.3436 0.6614 0.4823 0.0130  -0.0384 0.3207  218 ILE B CB  
5410  C CG1 . ILE B 218 ? 0.3540 0.6908 0.4964 0.0099  -0.0422 0.3315  218 ILE B CG1 
5411  C CG2 . ILE B 218 ? 0.3286 0.6459 0.4623 0.0059  -0.0399 0.3097  218 ILE B CG2 
5412  C CD1 . ILE B 218 ? 0.3564 0.6969 0.4909 0.0021  -0.0468 0.3304  218 ILE B CD1 
5413  N N   . PHE B 219 ? 0.3217 0.6192 0.4680 0.0234  -0.0283 0.3069  219 PHE B N   
5414  C CA  . PHE B 219 ? 0.3105 0.5926 0.4539 0.0253  -0.0249 0.2963  219 PHE B CA  
5415  C C   . PHE B 219 ? 0.3017 0.5761 0.4353 0.0189  -0.0272 0.2863  219 PHE B C   
5416  O O   . PHE B 219 ? 0.2980 0.5822 0.4286 0.0115  -0.0312 0.2848  219 PHE B O   
5417  C CB  . PHE B 219 ? 0.3015 0.5895 0.4508 0.0257  -0.0232 0.2943  219 PHE B CB  
5418  C CG  . PHE B 219 ? 0.2921 0.5652 0.4407 0.0294  -0.0188 0.2856  219 PHE B CG  
5419  C CD1 . PHE B 219 ? 0.2786 0.5449 0.4212 0.0248  -0.0194 0.2743  219 PHE B CD1 
5420  C CD2 . PHE B 219 ? 0.2969 0.5634 0.4513 0.0374  -0.0140 0.2888  219 PHE B CD2 
5421  C CE1 . PHE B 219 ? 0.2700 0.5231 0.4120 0.0281  -0.0154 0.2664  219 PHE B CE1 
5422  C CE2 . PHE B 219 ? 0.2886 0.5417 0.4423 0.0405  -0.0099 0.2808  219 PHE B CE2 
5423  C CZ  . PHE B 219 ? 0.2750 0.5216 0.4226 0.0358  -0.0107 0.2697  219 PHE B CZ  
5424  N N   . VAL B 220 ? 0.2988 0.5555 0.4271 0.0216  -0.0245 0.2793  220 VAL B N   
5425  C CA  . VAL B 220 ? 0.2913 0.5391 0.4101 0.0163  -0.0263 0.2699  220 VAL B CA  
5426  C C   . VAL B 220 ? 0.2774 0.5145 0.3947 0.0168  -0.0235 0.2591  220 VAL B C   
5427  O O   . VAL B 220 ? 0.2772 0.5032 0.3966 0.0230  -0.0192 0.2575  220 VAL B O   
5428  C CB  . VAL B 220 ? 0.3003 0.5361 0.4130 0.0183  -0.0259 0.2707  220 VAL B CB  
5429  C CG1 . VAL B 220 ? 0.2929 0.5205 0.3956 0.0123  -0.0279 0.2612  220 VAL B CG1 
5430  C CG2 . VAL B 220 ? 0.3150 0.5608 0.4296 0.0186  -0.0282 0.2820  220 VAL B CG2 
5431  N N   . VAL B 221 ? 0.2871 0.5274 0.4006 0.0100  -0.0259 0.2517  221 VAL B N   
5432  C CA  . VAL B 221 ? 0.2522 0.4832 0.3635 0.0093  -0.0240 0.2409  221 VAL B CA  
5433  C C   . VAL B 221 ? 0.2474 0.4680 0.3491 0.0051  -0.0254 0.2325  221 VAL B C   
5434  O O   . VAL B 221 ? 0.2475 0.4748 0.3450 -0.0015 -0.0293 0.2320  221 VAL B O   
5435  C CB  . VAL B 221 ? 0.2427 0.4855 0.3575 0.0050  -0.0253 0.2387  221 VAL B CB  
5436  C CG1 . VAL B 221 ? 0.2282 0.4612 0.3397 0.0035  -0.0237 0.2271  221 VAL B CG1 
5437  C CG2 . VAL B 221 ? 0.2468 0.4986 0.3709 0.0096  -0.0233 0.2464  221 VAL B CG2 
5438  N N   . MET B 222 ? 0.2435 0.4478 0.3418 0.0086  -0.0223 0.2259  222 MET B N   
5439  C CA  . MET B 222 ? 0.2382 0.4313 0.3274 0.0050  -0.0232 0.2173  222 MET B CA  
5440  C C   . MET B 222 ? 0.2229 0.4153 0.3108 0.0010  -0.0234 0.2075  222 MET B C   
5441  O O   . MET B 222 ? 0.2624 0.4476 0.3525 0.0044  -0.0202 0.2027  222 MET B O   
5442  C CB  . MET B 222 ? 0.2421 0.4180 0.3281 0.0106  -0.0196 0.2151  222 MET B CB  
5443  C CG  . MET B 222 ? 0.2432 0.4073 0.3193 0.0073  -0.0204 0.2076  222 MET B CG  
5444  S SD  . MET B 222 ? 0.2888 0.4499 0.3593 0.0074  -0.0219 0.2143  222 MET B SD  
5445  C CE  . MET B 222 ? 0.2697 0.4248 0.3460 0.0166  -0.0175 0.2219  222 MET B CE  
5446  N N   . ASP B 223 ? 0.2209 0.4208 0.3053 -0.0065 -0.0271 0.2046  223 ASP B N   
5447  C CA  . ASP B 223 ? 0.2295 0.4275 0.3116 -0.0108 -0.0274 0.1947  223 ASP B CA  
5448  C C   . ASP B 223 ? 0.2055 0.3866 0.2805 -0.0100 -0.0260 0.1860  223 ASP B C   
5449  O O   . ASP B 223 ? 0.2181 0.3956 0.2864 -0.0136 -0.0279 0.1839  223 ASP B O   
5450  C CB  . ASP B 223 ? 0.2199 0.4302 0.3001 -0.0192 -0.0316 0.1942  223 ASP B CB  
5451  C CG  . ASP B 223 ? 0.2355 0.4448 0.3139 -0.0239 -0.0318 0.1844  223 ASP B CG  
5452  O OD1 . ASP B 223 ? 0.2317 0.4279 0.3064 -0.0227 -0.0300 0.1761  223 ASP B OD1 
5453  O OD2 . ASP B 223 ? 0.2060 0.4278 0.2868 -0.0291 -0.0337 0.1852  223 ASP B OD2 
5454  N N   . SER B 224 ? 0.1921 0.3634 0.2686 -0.0057 -0.0225 0.1808  224 SER B N   
5455  C CA  . SER B 224 ? 0.2110 0.3654 0.2820 -0.0027 -0.0200 0.1750  224 SER B CA  
5456  C C   . SER B 224 ? 0.1911 0.3380 0.2576 -0.0059 -0.0200 0.1638  224 SER B C   
5457  O O   . SER B 224 ? 0.2470 0.3805 0.3108 -0.0026 -0.0172 0.1583  224 SER B O   
5458  C CB  . SER B 224 ? 0.2484 0.3959 0.3241 0.0051  -0.0156 0.1779  224 SER B CB  
5459  O OG  . SER B 224 ? 0.2891 0.4409 0.3678 0.0084  -0.0155 0.1880  224 SER B OG  
5460  N N   . ALA B 225 ? 0.2106 0.3657 0.2761 -0.0124 -0.0230 0.1603  225 ALA B N   
5461  C CA  . ALA B 225 ? 0.1919 0.3406 0.2539 -0.0155 -0.0229 0.1498  225 ALA B CA  
5462  C C   . ALA B 225 ? 0.1976 0.3321 0.2515 -0.0154 -0.0224 0.1441  225 ALA B C   
5463  O O   . ALA B 225 ? 0.2130 0.3369 0.2647 -0.0139 -0.0205 0.1364  225 ALA B O   
5464  C CB  . ALA B 225 ? 0.2204 0.3805 0.2822 -0.0232 -0.0263 0.1476  225 ALA B CB  
5465  N N   . ARG B 226 ? 0.1905 0.3248 0.2398 -0.0171 -0.0242 0.1478  226 ARG B N   
5466  C CA  . ARG B 226 ? 0.1976 0.3187 0.2387 -0.0175 -0.0237 0.1426  226 ARG B CA  
5467  C C   . ARG B 226 ? 0.1815 0.2958 0.2204 -0.0130 -0.0221 0.1487  226 ARG B C   
5468  O O   . ARG B 226 ? 0.2009 0.3115 0.2335 -0.0152 -0.0233 0.1494  226 ARG B O   
5469  C CB  . ARG B 226 ? 0.1876 0.3128 0.2235 -0.0252 -0.0272 0.1390  226 ARG B CB  
5470  C CG  . ARG B 226 ? 0.2126 0.3433 0.2507 -0.0298 -0.0284 0.1322  226 ARG B CG  
5471  C CD  . ARG B 226 ? 0.2387 0.3741 0.2724 -0.0379 -0.0317 0.1285  226 ARG B CD  
5472  N NE  . ARG B 226 ? 0.1820 0.3230 0.2184 -0.0424 -0.0327 0.1227  226 ARG B NE  
5473  C CZ  . ARG B 226 ? 0.2209 0.3755 0.2627 -0.0456 -0.0340 0.1261  226 ARG B CZ  
5474  N NH1 . ARG B 226 ? 0.2102 0.3748 0.2556 -0.0446 -0.0348 0.1354  226 ARG B NH1 
5475  N NH2 . ARG B 226 ? 0.1520 0.3101 0.1956 -0.0499 -0.0345 0.1202  226 ARG B NH2 
5476  N N   . PHE B 227 ? 0.1855 0.2976 0.2296 -0.0066 -0.0190 0.1530  227 PHE B N   
5477  C CA  . PHE B 227 ? 0.2278 0.3344 0.2709 -0.0022 -0.0173 0.1598  227 PHE B CA  
5478  C C   . PHE B 227 ? 0.2363 0.3263 0.2718 -0.0006 -0.0150 0.1546  227 PHE B C   
5479  O O   . PHE B 227 ? 0.2339 0.3191 0.2654 0.0005  -0.0147 0.1588  227 PHE B O   
5480  C CB  . PHE B 227 ? 0.2061 0.3151 0.2574 0.0041  -0.0144 0.1657  227 PHE B CB  
5481  C CG  . PHE B 227 ? 0.2077 0.3063 0.2605 0.0083  -0.0104 0.1598  227 PHE B CG  
5482  C CD1 . PHE B 227 ? 0.2529 0.3539 0.3083 0.0068  -0.0103 0.1534  227 PHE B CD1 
5483  C CD2 . PHE B 227 ? 0.2030 0.2895 0.2544 0.0134  -0.0067 0.1606  227 PHE B CD2 
5484  C CE1 . PHE B 227 ? 0.2941 0.3859 0.3509 0.0105  -0.0065 0.1479  227 PHE B CE1 
5485  C CE2 . PHE B 227 ? 0.2325 0.3099 0.2853 0.0169  -0.0029 0.1550  227 PHE B CE2 
5486  C CZ  . PHE B 227 ? 0.2798 0.3601 0.3353 0.0155  -0.0028 0.1487  227 PHE B CZ  
5487  N N   . CYS B 228 ? 0.2128 0.2940 0.2461 -0.0005 -0.0133 0.1456  228 CYS B N   
5488  C CA  . CYS B 228 ? 0.2238 0.2896 0.2495 0.0006  -0.0111 0.1403  228 CYS B CA  
5489  C C   . CYS B 228 ? 0.2341 0.2981 0.2516 -0.0048 -0.0138 0.1380  228 CYS B C   
5490  O O   . CYS B 228 ? 0.2097 0.2640 0.2209 -0.0040 -0.0126 0.1384  228 CYS B O   
5491  C CB  . CYS B 228 ? 0.2301 0.2878 0.2555 0.0017  -0.0088 0.1313  228 CYS B CB  
5492  S SG  . CYS B 228 ? 0.2935 0.3502 0.3275 0.0083  -0.0046 0.1331  228 CYS B SG  
5493  N N   . GLU B 229 ? 0.2030 0.2765 0.2206 -0.0104 -0.0172 0.1354  229 GLU B N   
5494  C CA  . GLU B 229 ? 0.2164 0.2896 0.2269 -0.0158 -0.0197 0.1336  229 GLU B CA  
5495  C C   . GLU B 229 ? 0.2569 0.3350 0.2663 -0.0162 -0.0212 0.1426  229 GLU B C   
5496  O O   . GLU B 229 ? 0.2466 0.3184 0.2489 -0.0179 -0.0214 0.1424  229 GLU B O   
5497  C CB  . GLU B 229 ? 0.2266 0.3093 0.2382 -0.0221 -0.0230 0.1288  229 GLU B CB  
5498  C CG  . GLU B 229 ? 0.2514 0.3267 0.2617 -0.0224 -0.0217 0.1188  229 GLU B CG  
5499  C CD  . GLU B 229 ? 0.2221 0.3076 0.2362 -0.0273 -0.0243 0.1149  229 GLU B CD  
5500  O OE1 . GLU B 229 ? 0.2577 0.3557 0.2741 -0.0316 -0.0272 0.1191  229 GLU B OE1 
5501  O OE2 . GLU B 229 ? 0.2302 0.3110 0.2448 -0.0269 -0.0232 0.1075  229 GLU B OE2 
5502  N N   . ASN B 230 ? 0.2132 0.3026 0.2297 -0.0146 -0.0221 0.1506  230 ASN B N   
5503  C CA  . ASN B 230 ? 0.2214 0.3148 0.2373 -0.0139 -0.0231 0.1598  230 ASN B CA  
5504  C C   . ASN B 230 ? 0.2317 0.3111 0.2437 -0.0088 -0.0197 0.1615  230 ASN B C   
5505  O O   . ASN B 230 ? 0.2554 0.3308 0.2614 -0.0101 -0.0203 0.1641  230 ASN B O   
5506  C CB  . ASN B 230 ? 0.2252 0.3324 0.2499 -0.0121 -0.0241 0.1682  230 ASN B CB  
5507  C CG  . ASN B 230 ? 0.2743 0.3904 0.2985 -0.0141 -0.0268 0.1771  230 ASN B CG  
5508  O OD1 . ASN B 230 ? 0.2581 0.3839 0.2808 -0.0202 -0.0303 0.1772  230 ASN B OD1 
5509  N ND2 . ASN B 230 ? 0.2498 0.3625 0.2752 -0.0090 -0.0250 0.1845  230 ASN B ND2 
5510  N N   . ALA B 231 ? 0.2444 0.3161 0.2596 -0.0034 -0.0161 0.1599  231 ALA B N   
5511  C CA  . ALA B 231 ? 0.2858 0.3443 0.2980 0.0014  -0.0126 0.1617  231 ALA B CA  
5512  C C   . ALA B 231 ? 0.3074 0.3533 0.3094 -0.0011 -0.0120 0.1557  231 ALA B C   
5513  O O   . ALA B 231 ? 0.3024 0.3408 0.2997 0.0003  -0.0108 0.1592  231 ALA B O   
5514  C CB  . ALA B 231 ? 0.2338 0.2864 0.2511 0.0068  -0.0087 0.1595  231 ALA B CB  
5515  N N   . TYR B 232 ? 0.2394 0.2827 0.2379 -0.0047 -0.0126 0.1468  232 TYR B N   
5516  C CA  . TYR B 232 ? 0.2276 0.2595 0.2166 -0.0073 -0.0119 0.1409  232 TYR B CA  
5517  C C   . TYR B 232 ? 0.2704 0.3060 0.2543 -0.0112 -0.0145 0.1450  232 TYR B C   
5518  O O   . TYR B 232 ? 0.3018 0.3273 0.2786 -0.0111 -0.0130 0.1450  232 TYR B O   
5519  C CB  . TYR B 232 ? 0.2648 0.2954 0.2521 -0.0106 -0.0125 0.1310  232 TYR B CB  
5520  C CG  . TYR B 232 ? 0.2726 0.2932 0.2507 -0.0136 -0.0119 0.1246  232 TYR B CG  
5521  C CD1 . TYR B 232 ? 0.3222 0.3478 0.2962 -0.0190 -0.0147 0.1247  232 TYR B CD1 
5522  C CD2 . TYR B 232 ? 0.2407 0.2472 0.2143 -0.0113 -0.0084 0.1187  232 TYR B CD2 
5523  C CE1 . TYR B 232 ? 0.3112 0.3283 0.2775 -0.0217 -0.0140 0.1191  232 TYR B CE1 
5524  C CE2 . TYR B 232 ? 0.2674 0.2651 0.2328 -0.0140 -0.0076 0.1131  232 TYR B CE2 
5525  C CZ  . TYR B 232 ? 0.2867 0.2899 0.2488 -0.0190 -0.0103 0.1134  232 TYR B CZ  
5526  O OH  . TYR B 232 ? 0.3191 0.3146 0.2739 -0.0216 -0.0094 0.1081  232 TYR B OH  
5527  N N   . PHE B 233 ? 0.2755 0.3257 0.2630 -0.0151 -0.0182 0.1484  233 PHE B N   
5528  C CA  . PHE B 233 ? 0.2966 0.3517 0.2797 -0.0194 -0.0209 0.1522  233 PHE B CA  
5529  C C   . PHE B 233 ? 0.2836 0.3366 0.2661 -0.0159 -0.0200 0.1613  233 PHE B C   
5530  O O   . PHE B 233 ? 0.2932 0.3421 0.2690 -0.0179 -0.0204 0.1630  233 PHE B O   
5531  C CB  . PHE B 233 ? 0.2389 0.3109 0.2264 -0.0245 -0.0252 0.1541  233 PHE B CB  
5532  C CG  . PHE B 233 ? 0.2258 0.2999 0.2118 -0.0300 -0.0268 0.1452  233 PHE B CG  
5533  C CD1 . PHE B 233 ? 0.2515 0.3182 0.2299 -0.0337 -0.0268 0.1393  233 PHE B CD1 
5534  C CD2 . PHE B 233 ? 0.2280 0.3116 0.2204 -0.0315 -0.0282 0.1429  233 PHE B CD2 
5535  C CE1 . PHE B 233 ? 0.2755 0.3442 0.2529 -0.0387 -0.0283 0.1311  233 PHE B CE1 
5536  C CE2 . PHE B 233 ? 0.2071 0.2924 0.1982 -0.0367 -0.0297 0.1348  233 PHE B CE2 
5537  C CZ  . PHE B 233 ? 0.2204 0.2982 0.2042 -0.0402 -0.0298 0.1289  233 PHE B CZ  
5538  N N   . ILE B 234 ? 0.2669 0.3230 0.2564 -0.0108 -0.0188 0.1674  234 ILE B N   
5539  C CA  . ILE B 234 ? 0.3139 0.3672 0.3034 -0.0068 -0.0176 0.1760  234 ILE B CA  
5540  C C   . ILE B 234 ? 0.3420 0.3777 0.3241 -0.0045 -0.0140 0.1730  234 ILE B C   
5541  O O   . ILE B 234 ? 0.3058 0.3371 0.2825 -0.0049 -0.0139 0.1769  234 ILE B O   
5542  C CB  . ILE B 234 ? 0.3270 0.3866 0.3263 -0.0014 -0.0165 0.1824  234 ILE B CB  
5543  C CG1 . ILE B 234 ? 0.2834 0.3615 0.2893 -0.0041 -0.0203 0.1877  234 ILE B CG1 
5544  C CG2 . ILE B 234 ? 0.3205 0.3736 0.3198 0.0036  -0.0141 0.1899  234 ILE B CG2 
5545  C CD1 . ILE B 234 ? 0.2793 0.3648 0.2954 0.0009  -0.0191 0.1936  234 ILE B CD1 
5546  N N   . LYS B 235 ? 0.3239 0.3495 0.3056 -0.0023 -0.0110 0.1659  235 LYS B N   
5547  C CA  . LYS B 235 ? 0.3769 0.3861 0.3510 -0.0010 -0.0077 0.1621  235 LYS B CA  
5548  C C   . LYS B 235 ? 0.3746 0.3796 0.3392 -0.0064 -0.0089 0.1577  235 LYS B C   
5549  O O   . LYS B 235 ? 0.3859 0.3807 0.3435 -0.0062 -0.0073 0.1585  235 LYS B O   
5550  C CB  . LYS B 235 ? 0.3016 0.3019 0.2771 0.0016  -0.0046 0.1549  235 LYS B CB  
5551  C CG  . LYS B 235 ? 0.3182 0.3018 0.2859 0.0025  -0.0012 0.1507  235 LYS B CG  
5552  C CD  . LYS B 235 ? 0.3316 0.3077 0.3019 0.0055  0.0019  0.1448  235 LYS B CD  
5553  C CE  . LYS B 235 ? 0.3413 0.3018 0.3031 0.0049  0.0046  0.1397  235 LYS B CE  
5554  N NZ  . LYS B 235 ? 0.4177 0.3713 0.3829 0.0081  0.0078  0.1354  235 LYS B NZ  
5555  N N   . ALA B 236 ? 0.3558 0.3692 0.3205 -0.0112 -0.0117 0.1532  236 ALA B N   
5556  C CA  . ALA B 236 ? 0.3562 0.3662 0.3129 -0.0163 -0.0126 0.1483  236 ALA B CA  
5557  C C   . ALA B 236 ? 0.3440 0.3596 0.2976 -0.0192 -0.0150 0.1550  236 ALA B C   
5558  O O   . ALA B 236 ? 0.3544 0.3634 0.3003 -0.0219 -0.0144 0.1527  236 ALA B O   
5559  C CB  . ALA B 236 ? 0.3251 0.3424 0.2836 -0.0207 -0.0149 0.1412  236 ALA B CB  
5560  N N   . ARG B 237 ? 0.3003 0.3283 0.2596 -0.0189 -0.0175 0.1632  237 ARG B N   
5561  C CA  . ARG B 237 ? 0.3133 0.3489 0.2700 -0.0225 -0.0204 0.1693  237 ARG B CA  
5562  C C   . ARG B 237 ? 0.3335 0.3699 0.2919 -0.0186 -0.0201 0.1796  237 ARG B C   
5563  O O   . ARG B 237 ? 0.4177 0.4559 0.3718 -0.0209 -0.0215 0.1842  237 ARG B O   
5564  C CB  . ARG B 237 ? 0.3712 0.4238 0.3326 -0.0276 -0.0248 0.1697  237 ARG B CB  
5565  C CG  . ARG B 237 ? 0.3561 0.4094 0.3164 -0.0321 -0.0257 0.1599  237 ARG B CG  
5566  C CD  . ARG B 237 ? 0.3232 0.3933 0.2881 -0.0377 -0.0300 0.1605  237 ARG B CD  
5567  N NE  . ARG B 237 ? 0.2812 0.3512 0.2455 -0.0417 -0.0306 0.1509  237 ARG B NE  
5568  C CZ  . ARG B 237 ? 0.2456 0.3279 0.2143 -0.0463 -0.0337 0.1489  237 ARG B CZ  
5569  N NH1 . ARG B 237 ? 0.2683 0.3644 0.2424 -0.0476 -0.0363 0.1558  237 ARG B NH1 
5570  N NH2 . ARG B 237 ? 0.2608 0.3414 0.2286 -0.0499 -0.0340 0.1400  237 ARG B NH2 
5571  N N   . ASP B 238 ? 0.3489 0.3846 0.3137 -0.0128 -0.0182 0.1834  238 ASP B N   
5572  C CA  . ASP B 238 ? 0.3909 0.4268 0.3578 -0.0087 -0.0176 0.1932  238 ASP B CA  
5573  C C   . ASP B 238 ? 0.4294 0.4478 0.3908 -0.0050 -0.0134 0.1920  238 ASP B C   
5574  O O   . ASP B 238 ? 0.4059 0.4162 0.3695 -0.0012 -0.0103 0.1882  238 ASP B O   
5575  C CB  . ASP B 238 ? 0.3372 0.3826 0.3149 -0.0044 -0.0177 0.1985  238 ASP B CB  
5576  C CG  . ASP B 238 ? 0.4166 0.4636 0.3975 0.0000  -0.0171 0.2092  238 ASP B CG  
5577  O OD1 . ASP B 238 ? 0.4470 0.4852 0.4215 0.0005  -0.0160 0.2120  238 ASP B OD1 
5578  O OD2 . ASP B 238 ? 0.3533 0.4104 0.3432 0.0031  -0.0177 0.2150  238 ASP B OD2 
5579  N N   . PRO B 239 ? 0.3933 0.4054 0.3474 -0.0061 -0.0131 0.1951  239 PRO B N   
5580  C CA  . PRO B 239 ? 0.4347 0.4295 0.3827 -0.0033 -0.0091 0.1935  239 PRO B CA  
5581  C C   . PRO B 239 ? 0.4328 0.4232 0.3869 0.0033  -0.0063 0.1980  239 PRO B C   
5582  O O   . PRO B 239 ? 0.4728 0.4492 0.4236 0.0056  -0.0027 0.1945  239 PRO B O   
5583  C CB  . PRO B 239 ? 0.3909 0.3836 0.3316 -0.0057 -0.0100 0.1983  239 PRO B CB  
5584  C CG  . PRO B 239 ? 0.3964 0.4062 0.3419 -0.0078 -0.0143 0.2053  239 PRO B CG  
5585  C CD  . PRO B 239 ? 0.4398 0.4608 0.3911 -0.0102 -0.0165 0.2005  239 PRO B CD  
5586  N N   . LYS B 240 ? 0.4623 0.4646 0.4255 0.0062  -0.0077 0.2055  240 LYS B N   
5587  C CA  . LYS B 240 ? 0.3751 0.3743 0.3452 0.0127  -0.0047 0.2099  240 LYS B CA  
5588  C C   . LYS B 240 ? 0.4024 0.3943 0.3750 0.0148  -0.0017 0.2020  240 LYS B C   
5589  O O   . LYS B 240 ? 0.4177 0.3996 0.3915 0.0191  0.0020  0.2023  240 LYS B O   
5590  C CB  . LYS B 240 ? 0.4144 0.4296 0.3945 0.0150  -0.0069 0.2186  240 LYS B CB  
5591  C CG  . LYS B 240 ? 0.4656 0.4790 0.4535 0.0220  -0.0037 0.2249  240 LYS B CG  
5592  C CD  . LYS B 240 ? 0.4499 0.4801 0.4478 0.0239  -0.0060 0.2334  240 LYS B CD  
5593  C CE  . LYS B 240 ? 0.4953 0.5238 0.5001 0.0310  -0.0028 0.2415  240 LYS B CE  
5594  N NZ  . LYS B 240 ? 0.5836 0.6038 0.5928 0.0354  0.0016  0.2368  240 LYS B NZ  
5595  N N   . TYR B 241 ? 0.4144 0.4113 0.3879 0.0117  -0.0032 0.1949  241 TYR B N   
5596  C CA  . TYR B 241 ? 0.4331 0.4251 0.4098 0.0137  -0.0007 0.1877  241 TYR B CA  
5597  C C   . TYR B 241 ? 0.4610 0.4415 0.4290 0.0101  0.0003  0.1775  241 TYR B C   
5598  O O   . TYR B 241 ? 0.3991 0.3780 0.3689 0.0100  0.0013  0.1702  241 TYR B O   
5599  C CB  . TYR B 241 ? 0.3842 0.3900 0.3694 0.0135  -0.0027 0.1871  241 TYR B CB  
5600  C CG  . TYR B 241 ? 0.3608 0.3775 0.3556 0.0176  -0.0031 0.1967  241 TYR B CG  
5601  C CD1 . TYR B 241 ? 0.3612 0.3899 0.3574 0.0158  -0.0066 0.2044  241 TYR B CD1 
5602  C CD2 . TYR B 241 ? 0.3806 0.3959 0.3832 0.0232  0.0002  0.1982  241 TYR B CD2 
5603  C CE1 . TYR B 241 ? 0.3545 0.3936 0.3595 0.0195  -0.0069 0.2134  241 TYR B CE1 
5604  C CE2 . TYR B 241 ? 0.3300 0.3553 0.3415 0.0271  0.0001  0.2071  241 TYR B CE2 
5605  C CZ  . TYR B 241 ? 0.3955 0.4327 0.4082 0.0253  -0.0035 0.2148  241 TYR B CZ  
5606  O OH  . TYR B 241 ? 0.4173 0.4650 0.4390 0.0292  -0.0035 0.2239  241 TYR B OH  
5607  N N   . LYS B 242 ? 0.4854 0.4581 0.4440 0.0072  0.0003  0.1770  242 LYS B N   
5608  C CA  . LYS B 242 ? 0.4388 0.4007 0.3889 0.0039  0.0015  0.1676  242 LYS B CA  
5609  C C   . LYS B 242 ? 0.4071 0.3570 0.3575 0.0069  0.0053  0.1628  242 LYS B C   
5610  O O   . LYS B 242 ? 0.4312 0.3756 0.3784 0.0048  0.0061  0.1540  242 LYS B O   
5611  C CB  . LYS B 242 ? 0.5211 0.4766 0.4614 0.0007  0.0012  0.1690  242 LYS B CB  
5612  C CG  . LYS B 242 ? 0.6402 0.5870 0.5717 -0.0035 0.0021  0.1597  242 LYS B CG  
5613  C CD  . LYS B 242 ? 0.7077 0.6515 0.6306 -0.0069 0.0015  0.1616  242 LYS B CD  
5614  C CE  . LYS B 242 ? 0.6724 0.6079 0.5925 -0.0043 0.0033  0.1683  242 LYS B CE  
5615  N NZ  . LYS B 242 ? 0.7095 0.6310 0.6277 -0.0020 0.0068  0.1642  242 LYS B NZ  
5616  N N   . ASN B 243 ? 0.4843 0.4310 0.4394 0.0117  0.0076  0.1684  243 ASN B N   
5617  C CA  . ASN B 243 ? 0.5028 0.4391 0.4592 0.0146  0.0114  0.1646  243 ASN B CA  
5618  C C   . ASN B 243 ? 0.4786 0.4212 0.4459 0.0191  0.0129  0.1650  243 ASN B C   
5619  O O   . ASN B 243 ? 0.4800 0.4157 0.4504 0.0224  0.0165  0.1631  243 ASN B O   
5620  C CB  . ASN B 243 ? 0.5399 0.4669 0.4936 0.0169  0.0138  0.1700  243 ASN B CB  
5621  C CG  . ASN B 243 ? 0.5072 0.4250 0.4492 0.0124  0.0132  0.1678  243 ASN B CG  
5622  O OD1 . ASN B 243 ? 0.5411 0.4540 0.4769 0.0083  0.0129  0.1597  243 ASN B OD1 
5623  N ND2 . ASN B 243 ? 0.5139 0.4294 0.4529 0.0130  0.0131  0.1751  243 ASN B ND2 
5624  N N   . ALA B 244 ? 0.4190 0.3749 0.3926 0.0193  0.0104  0.1675  244 ALA B N   
5625  C CA  . ALA B 244 ? 0.3747 0.3373 0.3587 0.0234  0.0118  0.1684  244 ALA B CA  
5626  C C   . ALA B 244 ? 0.4039 0.3673 0.3885 0.0213  0.0116  0.1590  244 ALA B C   
5627  O O   . ALA B 244 ? 0.4741 0.4374 0.4525 0.0165  0.0092  0.1534  244 ALA B O   
5628  C CB  . ALA B 244 ? 0.3913 0.3686 0.3824 0.0246  0.0092  0.1766  244 ALA B CB  
5629  N N   . THR B 245 ? 0.3881 0.3523 0.3802 0.0251  0.0143  0.1574  245 THR B N   
5630  C CA  . THR B 245 ? 0.3840 0.3512 0.3780 0.0235  0.0138  0.1495  245 THR B CA  
5631  C C   . THR B 245 ? 0.3471 0.3291 0.3468 0.0225  0.0104  0.1524  245 THR B C   
5632  O O   . THR B 245 ? 0.3231 0.3135 0.3271 0.0240  0.0091  0.1609  245 THR B O   
5633  C CB  . THR B 245 ? 0.3663 0.3294 0.3662 0.0276  0.0181  0.1462  245 THR B CB  
5634  O OG1 . THR B 245 ? 0.3067 0.2769 0.3160 0.0325  0.0197  0.1535  245 THR B OG1 
5635  C CG2 . THR B 245 ? 0.3985 0.3481 0.3935 0.0286  0.0216  0.1440  245 THR B CG2 
5636  N N   . ILE B 246 ? 0.3623 0.3477 0.3619 0.0196  0.0089  0.1453  246 ILE B N   
5637  C CA  . ILE B 246 ? 0.3381 0.3376 0.3429 0.0180  0.0056  0.1471  246 ILE B CA  
5638  C C   . ILE B 246 ? 0.3053 0.3129 0.3208 0.0227  0.0071  0.1531  246 ILE B C   
5639  O O   . ILE B 246 ? 0.3583 0.3781 0.3787 0.0226  0.0046  0.1597  246 ILE B O   
5640  C CB  . ILE B 246 ? 0.3100 0.3104 0.3129 0.0143  0.0042  0.1377  246 ILE B CB  
5641  C CG1 . ILE B 246 ? 0.2886 0.2828 0.2812 0.0093  0.0024  0.1328  246 ILE B CG1 
5642  C CG2 . ILE B 246 ? 0.2482 0.2632 0.2578 0.0129  0.0013  0.1393  246 ILE B CG2 
5643  C CD1 . ILE B 246 ? 0.2778 0.2805 0.2683 0.0058  -0.0012 0.1380  246 ILE B CD1 
5644  N N   . LYS B 247 ? 0.2960 0.2976 0.3153 0.0269  0.0113  0.1512  247 LYS B N   
5645  C CA  . LYS B 247 ? 0.3307 0.3393 0.3602 0.0317  0.0134  0.1569  247 LYS B CA  
5646  C C   . LYS B 247 ? 0.3122 0.3236 0.3442 0.0347  0.0136  0.1675  247 LYS B C   
5647  O O   . LYS B 247 ? 0.3616 0.3838 0.4013 0.0370  0.0131  0.1743  247 LYS B O   
5648  C CB  . LYS B 247 ? 0.3427 0.3435 0.3752 0.0354  0.0183  0.1524  247 LYS B CB  
5649  C CG  . LYS B 247 ? 0.3314 0.3331 0.3646 0.0335  0.0182  0.1434  247 LYS B CG  
5650  C CD  . LYS B 247 ? 0.3507 0.3465 0.3880 0.0375  0.0235  0.1401  247 LYS B CD  
5651  C CE  . LYS B 247 ? 0.3461 0.3428 0.3840 0.0356  0.0235  0.1313  247 LYS B CE  
5652  N NZ  . LYS B 247 ? 0.3263 0.3199 0.3695 0.0396  0.0287  0.1291  247 LYS B NZ  
5653  N N   . GLU B 248 ? 0.3235 0.3253 0.3493 0.0349  0.0145  0.1691  248 GLU B N   
5654  C CA  . GLU B 248 ? 0.3355 0.3398 0.3631 0.0375  0.0145  0.1792  248 GLU B CA  
5655  C C   . GLU B 248 ? 0.3629 0.3797 0.3904 0.0342  0.0095  0.1845  248 GLU B C   
5656  O O   . GLU B 248 ? 0.3975 0.4230 0.4306 0.0366  0.0089  0.1935  248 GLU B O   
5657  C CB  . GLU B 248 ? 0.3885 0.3794 0.4086 0.0379  0.0165  0.1793  248 GLU B CB  
5658  C CG  . GLU B 248 ? 0.4746 0.4551 0.4971 0.0424  0.0220  0.1775  248 GLU B CG  
5659  C CD  . GLU B 248 ? 0.4351 0.4014 0.4490 0.0413  0.0238  0.1746  248 GLU B CD  
5660  O OE1 . GLU B 248 ? 0.4241 0.3882 0.4301 0.0374  0.0208  0.1749  248 GLU B OE1 
5661  O OE2 . GLU B 248 ? 0.4953 0.4528 0.5104 0.0443  0.0284  0.1720  248 GLU B OE2 
5662  N N   . VAL B 249 ? 0.3624 0.3806 0.3835 0.0284  0.0061  0.1790  249 VAL B N   
5663  C CA  . VAL B 249 ? 0.3308 0.3618 0.3520 0.0247  0.0014  0.1833  249 VAL B CA  
5664  C C   . VAL B 249 ? 0.3370 0.3823 0.3679 0.0256  0.0002  0.1859  249 VAL B C   
5665  O O   . VAL B 249 ? 0.2863 0.3431 0.3220 0.0261  -0.0018 0.1943  249 VAL B O   
5666  C CB  . VAL B 249 ? 0.3420 0.3710 0.3545 0.0183  -0.0015 0.1761  249 VAL B CB  
5667  C CG1 . VAL B 249 ? 0.2896 0.3334 0.3033 0.0139  -0.0063 0.1797  249 VAL B CG1 
5668  C CG2 . VAL B 249 ? 0.3517 0.3676 0.3546 0.0172  -0.0005 0.1748  249 VAL B CG2 
5669  N N   . ILE B 250 ? 0.2707 0.3155 0.3044 0.0257  0.0014  0.1790  250 ILE B N   
5670  C CA  . ILE B 250 ? 0.2555 0.3129 0.2982 0.0265  0.0007  0.1809  250 ILE B CA  
5671  C C   . ILE B 250 ? 0.2792 0.3409 0.3301 0.0323  0.0031  0.1901  250 ILE B C   
5672  O O   . ILE B 250 ? 0.2680 0.3433 0.3250 0.0324  0.0010  0.1970  250 ILE B O   
5673  C CB  . ILE B 250 ? 0.3125 0.3661 0.3564 0.0264  0.0025  0.1717  250 ILE B CB  
5674  C CG1 . ILE B 250 ? 0.2637 0.3179 0.3015 0.0202  -0.0007 0.1638  250 ILE B CG1 
5675  C CG2 . ILE B 250 ? 0.2443 0.3082 0.2983 0.0290  0.0034  0.1745  250 ILE B CG2 
5676  C CD1 . ILE B 250 ? 0.3032 0.3501 0.3399 0.0201  0.0013  0.1540  250 ILE B CD1 
5677  N N   . PHE B 251 ? 0.3419 0.3925 0.3933 0.0371  0.0076  0.1904  251 PHE B N   
5678  C CA  . PHE B 251 ? 0.3188 0.3722 0.3780 0.0431  0.0106  0.1988  251 PHE B CA  
5679  C C   . PHE B 251 ? 0.3351 0.3969 0.3955 0.0432  0.0080  0.2091  251 PHE B C   
5680  O O   . PHE B 251 ? 0.3022 0.3739 0.3708 0.0464  0.0083  0.2169  251 PHE B O   
5681  C CB  . PHE B 251 ? 0.3269 0.3656 0.3846 0.0473  0.0158  0.1970  251 PHE B CB  
5682  C CG  . PHE B 251 ? 0.3743 0.4144 0.4407 0.0538  0.0200  0.2035  251 PHE B CG  
5683  C CD1 . PHE B 251 ? 0.3735 0.4150 0.4464 0.0563  0.0231  0.2005  251 PHE B CD1 
5684  C CD2 . PHE B 251 ? 0.3447 0.3842 0.4127 0.0573  0.0211  0.2126  251 PHE B CD2 
5685  C CE1 . PHE B 251 ? 0.3485 0.3911 0.4294 0.0622  0.0273  0.2064  251 PHE B CE1 
5686  C CE2 . PHE B 251 ? 0.3810 0.4216 0.4572 0.0634  0.0253  0.2187  251 PHE B CE2 
5687  C CZ  . PHE B 251 ? 0.3572 0.3993 0.4398 0.0658  0.0285  0.2155  251 PHE B CZ  
5688  N N   . ASP B 252 ? 0.3106 0.3690 0.3629 0.0397  0.0054  0.2093  252 ASP B N   
5689  C CA  . ASP B 252 ? 0.3665 0.4332 0.4193 0.0393  0.0026  0.2188  252 ASP B CA  
5690  C C   . ASP B 252 ? 0.3059 0.3893 0.3617 0.0350  -0.0021 0.2211  252 ASP B C   
5691  O O   . ASP B 252 ? 0.3135 0.4085 0.3750 0.0363  -0.0036 0.2302  252 ASP B O   
5692  C CB  . ASP B 252 ? 0.3590 0.4164 0.4017 0.0366  0.0015  0.2182  252 ASP B CB  
5693  C CG  . ASP B 252 ? 0.3891 0.4335 0.4302 0.0415  0.0057  0.2210  252 ASP B CG  
5694  O OD1 . ASP B 252 ? 0.3830 0.4208 0.4281 0.0457  0.0100  0.2185  252 ASP B OD1 
5695  O OD2 . ASP B 252 ? 0.4200 0.4613 0.4563 0.0410  0.0048  0.2258  252 ASP B OD2 
5696  N N   . MET B 253 ? 0.2928 0.3779 0.3451 0.0298  -0.0044 0.2130  253 MET B N   
5697  C CA  . MET B 253 ? 0.2869 0.3879 0.3419 0.0252  -0.0088 0.2145  253 MET B CA  
5698  C C   . MET B 253 ? 0.2872 0.4006 0.3529 0.0284  -0.0083 0.2209  253 MET B C   
5699  O O   . MET B 253 ? 0.2908 0.4185 0.3601 0.0264  -0.0115 0.2276  253 MET B O   
5700  C CB  . MET B 253 ? 0.2895 0.3892 0.3404 0.0201  -0.0103 0.2040  253 MET B CB  
5701  C CG  . MET B 253 ? 0.2709 0.3641 0.3115 0.0148  -0.0125 0.1988  253 MET B CG  
5702  S SD  . MET B 253 ? 0.2781 0.3673 0.3147 0.0102  -0.0131 0.1859  253 MET B SD  
5703  C CE  . MET B 253 ? 0.2446 0.3529 0.2889 0.0069  -0.0164 0.1878  253 MET B CE  
5704  N N   . TYR B 254 ? 0.2839 0.3923 0.3548 0.0333  -0.0042 0.2191  254 TYR B N   
5705  C CA  . TYR B 254 ? 0.2820 0.4016 0.3629 0.0361  -0.0033 0.2237  254 TYR B CA  
5706  C C   . TYR B 254 ? 0.3178 0.4394 0.4052 0.0423  -0.0008 0.2340  254 TYR B C   
5707  O O   . TYR B 254 ? 0.3796 0.5095 0.4756 0.0454  0.0006  0.2383  254 TYR B O   
5708  C CB  . TYR B 254 ? 0.2912 0.4055 0.3745 0.0374  -0.0003 0.2155  254 TYR B CB  
5709  C CG  . TYR B 254 ? 0.2874 0.4046 0.3667 0.0312  -0.0034 0.2071  254 TYR B CG  
5710  C CD1 . TYR B 254 ? 0.2655 0.3727 0.3357 0.0275  -0.0043 0.1992  254 TYR B CD1 
5711  C CD2 . TYR B 254 ? 0.2472 0.3775 0.3318 0.0287  -0.0053 0.2073  254 TYR B CD2 
5712  C CE1 . TYR B 254 ? 0.2383 0.3482 0.3051 0.0219  -0.0070 0.1917  254 TYR B CE1 
5713  C CE2 . TYR B 254 ? 0.2349 0.3678 0.3160 0.0229  -0.0080 0.1997  254 TYR B CE2 
5714  C CZ  . TYR B 254 ? 0.2419 0.3646 0.3142 0.0196  -0.0089 0.1920  254 TYR B CZ  
5715  O OH  . TYR B 254 ? 0.2405 0.3658 0.3096 0.0139  -0.0114 0.1845  254 TYR B OH  
5716  N N   . LYS B 255 ? 0.3104 0.4247 0.3937 0.0441  -0.0002 0.2381  255 LYS B N   
5717  C CA  . LYS B 255 ? 0.3229 0.4431 0.4117 0.0483  0.0004  0.2495  255 LYS B CA  
5718  C C   . LYS B 255 ? 0.3256 0.4631 0.4169 0.0447  -0.0045 0.2565  255 LYS B C   
5719  O O   . LYS B 255 ? 0.3478 0.4939 0.4455 0.0480  -0.0044 0.2664  255 LYS B O   
5720  C CB  . LYS B 255 ? 0.3356 0.4437 0.4184 0.0503  0.0019  0.2520  255 LYS B CB  
5721  C CG  . LYS B 255 ? 0.3567 0.4473 0.4368 0.0542  0.0071  0.2465  255 LYS B CG  
5722  C CD  . LYS B 255 ? 0.3475 0.4265 0.4196 0.0542  0.0075  0.2477  255 LYS B CD  
5723  C CE  . LYS B 255 ? 0.3542 0.4178 0.4258 0.0593  0.0132  0.2459  255 LYS B CE  
5724  N NZ  . LYS B 255 ? 0.4594 0.5167 0.5318 0.0596  0.0161  0.2365  255 LYS B NZ  
5725  N N   . TYR B 256 ? 0.3170 0.4598 0.4033 0.0378  -0.0087 0.2515  256 TYR B N   
5726  C CA  . TYR B 256 ? 0.3197 0.4784 0.4069 0.0331  -0.0137 0.2572  256 TYR B CA  
5727  C C   . TYR B 256 ? 0.3077 0.4793 0.3994 0.0294  -0.0158 0.2546  256 TYR B C   
5728  O O   . TYR B 256 ? 0.3035 0.4843 0.3924 0.0229  -0.0200 0.2533  256 TYR B O   
5729  C CB  . TYR B 256 ? 0.3217 0.4767 0.3989 0.0276  -0.0169 0.2545  256 TYR B CB  
5730  C CG  . TYR B 256 ? 0.3632 0.5033 0.4349 0.0310  -0.0144 0.2554  256 TYR B CG  
5731  C CD1 . TYR B 256 ? 0.3944 0.5349 0.4699 0.0361  -0.0128 0.2653  256 TYR B CD1 
5732  C CD2 . TYR B 256 ? 0.3276 0.4529 0.3903 0.0290  -0.0134 0.2466  256 TYR B CD2 
5733  C CE1 . TYR B 256 ? 0.3568 0.4833 0.4271 0.0391  -0.0103 0.2661  256 TYR B CE1 
5734  C CE2 . TYR B 256 ? 0.3602 0.4718 0.4177 0.0319  -0.0109 0.2474  256 TYR B CE2 
5735  C CZ  . TYR B 256 ? 0.3521 0.4641 0.4133 0.0369  -0.0094 0.2572  256 TYR B CZ  
5736  O OH  . TYR B 256 ? 0.4172 0.5153 0.4731 0.0395  -0.0068 0.2580  256 TYR B OH  
5737  N N   . ALA B 257 ? 0.3267 0.4987 0.4255 0.0335  -0.0126 0.2538  257 ALA B N   
5738  C CA  . ALA B 257 ? 0.2934 0.4783 0.3980 0.0312  -0.0139 0.2533  257 ALA B CA  
5739  C C   . ALA B 257 ? 0.2954 0.4811 0.4091 0.0379  -0.0097 0.2573  257 ALA B C   
5740  O O   . ALA B 257 ? 0.3007 0.4746 0.4151 0.0437  -0.0054 0.2576  257 ALA B O   
5741  C CB  . ALA B 257 ? 0.3089 0.4899 0.4089 0.0263  -0.0147 0.2418  257 ALA B CB  
5742  N N   . ASP B 258 ? 0.2916 0.4913 0.4121 0.0369  -0.0108 0.2604  258 ASP B N   
5743  C CA  . ASP B 258 ? 0.2920 0.4936 0.4212 0.0426  -0.0068 0.2636  258 ASP B CA  
5744  C C   . ASP B 258 ? 0.2773 0.4767 0.4073 0.0412  -0.0053 0.2548  258 ASP B C   
5745  O O   . ASP B 258 ? 0.2765 0.4737 0.4123 0.0461  -0.0013 0.2553  258 ASP B O   
5746  C CB  . ASP B 258 ? 0.2995 0.5188 0.4365 0.0431  -0.0086 0.2744  258 ASP B CB  
5747  C CG  . ASP B 258 ? 0.3139 0.5375 0.4504 0.0438  -0.0107 0.2836  258 ASP B CG  
5748  O OD1 . ASP B 258 ? 0.3231 0.5359 0.4588 0.0489  -0.0078 0.2861  258 ASP B OD1 
5749  O OD2 . ASP B 258 ? 0.3163 0.5538 0.4528 0.0390  -0.0152 0.2882  258 ASP B OD2 
5750  N N   . ALA B 259 ? 0.2662 0.4662 0.3904 0.0347  -0.0084 0.2469  259 ALA B N   
5751  C CA  . ALA B 259 ? 0.2519 0.4495 0.3761 0.0330  -0.0072 0.2380  259 ALA B CA  
5752  C C   . ALA B 259 ? 0.2425 0.4349 0.3580 0.0267  -0.0100 0.2287  259 ALA B C   
5753  O O   . ALA B 259 ? 0.2471 0.4401 0.3572 0.0232  -0.0131 0.2298  259 ALA B O   
5754  C CB  . ALA B 259 ? 0.2482 0.4613 0.3792 0.0312  -0.0084 0.2416  259 ALA B CB  
5755  N N   . LEU B 260 ? 0.2294 0.4166 0.3435 0.0251  -0.0088 0.2195  260 LEU B N   
5756  C CA  . LEU B 260 ? 0.2193 0.4036 0.3262 0.0188  -0.0116 0.2107  260 LEU B CA  
5757  C C   . LEU B 260 ? 0.2068 0.3973 0.3160 0.0155  -0.0120 0.2055  260 LEU B C   
5758  O O   . LEU B 260 ? 0.2403 0.4325 0.3555 0.0189  -0.0091 0.2065  260 LEU B O   
5759  C CB  . LEU B 260 ? 0.2162 0.3828 0.3162 0.0202  -0.0095 0.2027  260 LEU B CB  
5760  C CG  . LEU B 260 ? 0.2508 0.4055 0.3523 0.0248  -0.0047 0.1969  260 LEU B CG  
5761  C CD1 . LEU B 260 ? 0.1949 0.3481 0.2946 0.0211  -0.0050 0.1871  260 LEU B CD1 
5762  C CD2 . LEU B 260 ? 0.2372 0.3761 0.3334 0.0280  -0.0022 0.1943  260 LEU B CD2 
5763  N N   . THR B 261 ? 0.2025 0.3967 0.3069 0.0086  -0.0154 0.2003  261 THR B N   
5764  C CA  . THR B 261 ? 0.1860 0.3823 0.2902 0.0047  -0.0158 0.1927  261 THR B CA  
5765  C C   . THR B 261 ? 0.1886 0.3736 0.2847 0.0013  -0.0166 0.1829  261 THR B C   
5766  O O   . THR B 261 ? 0.2102 0.3942 0.3010 -0.0017 -0.0191 0.1832  261 THR B O   
5767  C CB  . THR B 261 ? 0.1850 0.3978 0.2913 -0.0013 -0.0192 0.1960  261 THR B CB  
5768  O OG1 . THR B 261 ? 0.2031 0.4200 0.3043 -0.0066 -0.0231 0.1973  261 THR B OG1 
5769  C CG2 . THR B 261 ? 0.1993 0.4239 0.3135 0.0019  -0.0186 0.2062  261 THR B CG2 
5770  N N   . MET B 262 ? 0.1672 0.3439 0.2625 0.0020  -0.0144 0.1745  262 MET B N   
5771  C CA  . MET B 262 ? 0.1846 0.3493 0.2727 -0.0001 -0.0146 0.1652  262 MET B CA  
5772  C C   . MET B 262 ? 0.1589 0.3247 0.2464 -0.0043 -0.0151 0.1569  262 MET B C   
5773  O O   . MET B 262 ? 0.1546 0.3219 0.2468 -0.0023 -0.0129 0.1558  262 MET B O   
5774  C CB  . MET B 262 ? 0.1865 0.3360 0.2732 0.0061  -0.0107 0.1626  262 MET B CB  
5775  C CG  . MET B 262 ? 0.2448 0.3816 0.3236 0.0042  -0.0109 0.1537  262 MET B CG  
5776  S SD  . MET B 262 ? 0.3399 0.4597 0.4173 0.0110  -0.0059 0.1505  262 MET B SD  
5777  C CE  . MET B 262 ? 0.2641 0.3841 0.3429 0.0152  -0.0051 0.1612  262 MET B CE  
5778  N N   . SER B 263 ? 0.1460 0.3111 0.2278 -0.0102 -0.0179 0.1512  263 SER B N   
5779  C CA  . SER B 263 ? 0.1630 0.3236 0.2426 -0.0133 -0.0178 0.1414  263 SER B CA  
5780  C C   . SER B 263 ? 0.2039 0.3482 0.2789 -0.0098 -0.0156 0.1348  263 SER B C   
5781  O O   . SER B 263 ? 0.1808 0.3184 0.2497 -0.0110 -0.0168 0.1330  263 SER B O   
5782  C CB  . SER B 263 ? 0.1872 0.3539 0.2629 -0.0213 -0.0215 0.1380  263 SER B CB  
5783  O OG  . SER B 263 ? 0.1253 0.2880 0.1998 -0.0240 -0.0211 0.1288  263 SER B OG  
5784  N N   . ALA B 264 ? 0.1699 0.3078 0.2475 -0.0057 -0.0122 0.1312  264 ALA B N   
5785  C CA  . ALA B 264 ? 0.1635 0.2864 0.2367 -0.0028 -0.0099 0.1244  264 ALA B CA  
5786  C C   . ALA B 264 ? 0.1554 0.2737 0.2236 -0.0074 -0.0116 0.1147  264 ALA B C   
5787  O O   . ALA B 264 ? 0.1545 0.2606 0.2185 -0.0056 -0.0100 0.1083  264 ALA B O   
5788  C CB  . ALA B 264 ? 0.1641 0.2820 0.2419 0.0030  -0.0055 0.1240  264 ALA B CB  
5789  N N   . LYS B 265 ? 0.1664 0.2940 0.2348 -0.0134 -0.0146 0.1134  265 LYS B N   
5790  C CA  . LYS B 265 ? 0.1210 0.2447 0.1848 -0.0183 -0.0164 0.1045  265 LYS B CA  
5791  C C   . LYS B 265 ? 0.1306 0.2495 0.1874 -0.0211 -0.0187 0.1032  265 LYS B C   
5792  O O   . LYS B 265 ? 0.1316 0.2468 0.1843 -0.0252 -0.0202 0.0959  265 LYS B O   
5793  C CB  . LYS B 265 ? 0.1280 0.2635 0.1949 -0.0243 -0.0184 0.1037  265 LYS B CB  
5794  C CG  . LYS B 265 ? 0.1258 0.2667 0.1992 -0.0222 -0.0162 0.1052  265 LYS B CG  
5795  C CD  . LYS B 265 ? 0.1717 0.3177 0.2412 -0.0264 -0.0181 0.1043  265 LYS B CD  
5796  C CE  . LYS B 265 ? 0.1230 0.2568 0.1820 -0.0292 -0.0189 0.0923  265 LYS B CE  
5797  N NZ  . LYS B 265 ? 0.1399 0.2786 0.1961 -0.0325 -0.0198 0.0918  265 LYS B NZ  
5798  N N   . LYS B 266 ? 0.1470 0.2657 0.2024 -0.0190 -0.0187 0.1100  266 LYS B N   
5799  C CA  . LYS B 266 ? 0.1341 0.2475 0.1825 -0.0212 -0.0204 0.1092  266 LYS B CA  
5800  C C   . LYS B 266 ? 0.1801 0.2794 0.2246 -0.0156 -0.0175 0.1082  266 LYS B C   
5801  O O   . LYS B 266 ? 0.1951 0.2843 0.2372 -0.0140 -0.0157 0.1009  266 LYS B O   
5802  C CB  . LYS B 266 ? 0.2015 0.3254 0.2503 -0.0239 -0.0229 0.1176  266 LYS B CB  
5803  C CG  . LYS B 266 ? 0.1962 0.3329 0.2462 -0.0314 -0.0262 0.1174  266 LYS B CG  
5804  C CD  . LYS B 266 ? 0.1719 0.3169 0.2286 -0.0319 -0.0256 0.1170  266 LYS B CD  
5805  C CE  . LYS B 266 ? 0.2063 0.3665 0.2657 -0.0379 -0.0281 0.1211  266 LYS B CE  
5806  N NZ  . LYS B 266 ? 0.2946 0.4626 0.3555 -0.0368 -0.0292 0.1312  266 LYS B NZ  
5807  N N   . ASP B 267 ? 0.2292 0.3276 0.2731 -0.0127 -0.0168 0.1155  267 ASP B N   
5808  C CA  . ASP B 267 ? 0.2381 0.3228 0.2772 -0.0085 -0.0141 0.1144  267 ASP B CA  
5809  C C   . ASP B 267 ? 0.2304 0.3063 0.2718 -0.0031 -0.0100 0.1111  267 ASP B C   
5810  O O   . ASP B 267 ? 0.2800 0.3432 0.3160 -0.0013 -0.0080 0.1065  267 ASP B O   
5811  C CB  . ASP B 267 ? 0.1867 0.2729 0.2256 -0.0064 -0.0141 0.1236  267 ASP B CB  
5812  C CG  . ASP B 267 ? 0.2679 0.3553 0.3003 -0.0113 -0.0171 0.1245  267 ASP B CG  
5813  O OD1 . ASP B 267 ? 0.2907 0.3804 0.3202 -0.0167 -0.0196 0.1188  267 ASP B OD1 
5814  O OD2 . ASP B 267 ? 0.2423 0.3284 0.2728 -0.0097 -0.0170 0.1308  267 ASP B OD2 
5815  N N   . PRO B 268 ? 0.1824 0.2640 0.2313 -0.0005 -0.0085 0.1129  268 PRO B N   
5816  C CA  . PRO B 268 ? 0.1791 0.2526 0.2299 0.0038  -0.0046 0.1084  268 PRO B CA  
5817  C C   . PRO B 268 ? 0.2145 0.2834 0.2627 0.0015  -0.0048 0.0984  268 PRO B C   
5818  O O   . PRO B 268 ? 0.2245 0.2882 0.2746 0.0046  -0.0017 0.0945  268 PRO B O   
5819  C CB  . PRO B 268 ? 0.2045 0.2875 0.2642 0.0066  -0.0031 0.1143  268 PRO B CB  
5820  C CG  . PRO B 268 ? 0.1973 0.2899 0.2590 0.0057  -0.0054 0.1236  268 PRO B CG  
5821  C CD  . PRO B 268 ? 0.1665 0.2616 0.2224 -0.0003 -0.0094 0.1212  268 PRO B CD  
5822  N N   . LEU B 269 ? 0.1804 0.2514 0.2245 -0.0039 -0.0082 0.0941  269 LEU B N   
5823  C CA  . LEU B 269 ? 0.1316 0.1959 0.1719 -0.0058 -0.0084 0.0843  269 LEU B CA  
5824  C C   . LEU B 269 ? 0.1939 0.2620 0.2399 -0.0051 -0.0074 0.0809  269 LEU B C   
5825  O O   . LEU B 269 ? 0.1705 0.2308 0.2151 -0.0032 -0.0054 0.0742  269 LEU B O   
5826  C CB  . LEU B 269 ? 0.2094 0.2593 0.2434 -0.0028 -0.0058 0.0800  269 LEU B CB  
5827  C CG  . LEU B 269 ? 0.1779 0.2222 0.2052 -0.0037 -0.0064 0.0824  269 LEU B CG  
5828  C CD1 . LEU B 269 ? 0.2012 0.2335 0.2253 0.0007  -0.0025 0.0821  269 LEU B CD1 
5829  C CD2 . LEU B 269 ? 0.1792 0.2211 0.2002 -0.0087 -0.0091 0.0761  269 LEU B CD2 
5830  N N   . LEU B 270 ? 0.1538 0.2341 0.2059 -0.0068 -0.0087 0.0853  270 LEU B N   
5831  C CA  . LEU B 270 ? 0.1519 0.2366 0.2095 -0.0065 -0.0076 0.0828  270 LEU B CA  
5832  C C   . LEU B 270 ? 0.1628 0.2553 0.2210 -0.0127 -0.0109 0.0793  270 LEU B C   
5833  O O   . LEU B 270 ? 0.1910 0.2876 0.2464 -0.0175 -0.0141 0.0801  270 LEU B O   
5834  C CB  . LEU B 270 ? 0.1728 0.2651 0.2376 -0.0031 -0.0055 0.0908  270 LEU B CB  
5835  C CG  . LEU B 270 ? 0.1807 0.2660 0.2464 0.0030  -0.0017 0.0946  270 LEU B CG  
5836  C CD1 . LEU B 270 ? 0.1672 0.2608 0.2404 0.0060  0.0002  0.1024  270 LEU B CD1 
5837  C CD2 . LEU B 270 ? 0.1757 0.2493 0.2389 0.0057  0.0015  0.0869  270 LEU B CD2 
5838  N N   . ASN B 271 ? 0.1548 0.2455 0.2134 -0.0124 -0.0099 0.0740  271 ASN B N   
5839  C CA  . ASN B 271 ? 0.1710 0.2592 0.2227 -0.0159 -0.0118 0.0680  271 ASN B CA  
5840  C C   . ASN B 271 ? 0.1632 0.2613 0.2190 -0.0164 -0.0117 0.0740  271 ASN B C   
5841  O O   . ASN B 271 ? 0.1558 0.2551 0.2072 -0.0198 -0.0133 0.0714  271 ASN B O   
5842  C CB  . ASN B 271 ? 0.1368 0.2111 0.1814 -0.0143 -0.0104 0.0566  271 ASN B CB  
5843  C CG  . ASN B 271 ? 0.1599 0.2244 0.1995 -0.0141 -0.0106 0.0502  271 ASN B CG  
5844  O OD1 . ASN B 271 ? 0.1972 0.2542 0.2359 -0.0108 -0.0085 0.0458  271 ASN B OD1 
5845  N ND2 . ASN B 271 ? 0.1822 0.2469 0.2183 -0.0176 -0.0129 0.0497  271 ASN B ND2 
5846  N N   . ILE B 272 ? 0.1173 0.2225 0.1817 -0.0127 -0.0095 0.0821  272 ILE B N   
5847  C CA  . ILE B 272 ? 0.1373 0.2531 0.2066 -0.0126 -0.0092 0.0891  272 ILE B CA  
5848  C C   . ILE B 272 ? 0.1493 0.2734 0.2290 -0.0083 -0.0065 0.0997  272 ILE B C   
5849  O O   . ILE B 272 ? 0.1691 0.2851 0.2489 -0.0043 -0.0042 0.0986  272 ILE B O   
5850  C CB  . ILE B 272 ? 0.1416 0.2510 0.2074 -0.0114 -0.0078 0.0829  272 ILE B CB  
5851  C CG1 . ILE B 272 ? 0.1271 0.2477 0.1961 -0.0128 -0.0084 0.0891  272 ILE B CG1 
5852  C CG2 . ILE B 272 ? 0.1179 0.2203 0.1863 -0.0062 -0.0041 0.0812  272 ILE B CG2 
5853  C CD1 . ILE B 272 ? 0.1850 0.3135 0.2517 -0.0182 -0.0117 0.0914  272 ILE B CD1 
5854  N N   . GLY B 273 ? 0.1339 0.2710 0.2198 -0.0086 -0.0068 0.1091  273 GLY B N   
5855  C CA  . GLY B 273 ? 0.1374 0.2743 0.2269 -0.0027 -0.0043 0.1165  273 GLY B CA  
5856  C C   . GLY B 273 ? 0.1267 0.2711 0.2168 -0.0032 -0.0066 0.1253  273 GLY B C   
5857  O O   . GLY B 273 ? 0.1229 0.2691 0.2088 -0.0073 -0.0098 0.1248  273 GLY B O   
5858  N N   . GLY B 274 ? 0.1564 0.3054 0.2517 0.0011  -0.0047 0.1335  274 GLY B N   
5859  C CA  . GLY B 274 ? 0.1196 0.2765 0.2163 0.0013  -0.0066 0.1427  274 GLY B CA  
5860  C C   . GLY B 274 ? 0.1279 0.2832 0.2295 0.0081  -0.0032 0.1496  274 GLY B C   
5861  O O   . GLY B 274 ? 0.1795 0.3287 0.2836 0.0120  0.0006  0.1472  274 GLY B O   
5862  N N   . LEU B 275 ? 0.1823 0.3434 0.2855 0.0094  -0.0044 0.1583  275 LEU B N   
5863  C CA  . LEU B 275 ? 0.1500 0.3083 0.2575 0.0160  -0.0011 0.1650  275 LEU B CA  
5864  C C   . LEU B 275 ? 0.1811 0.3506 0.2920 0.0164  -0.0031 0.1758  275 LEU B C   
5865  O O   . LEU B 275 ? 0.1756 0.3480 0.2827 0.0133  -0.0064 0.1777  275 LEU B O   
5866  C CB  . LEU B 275 ? 0.1529 0.2962 0.2559 0.0194  0.0011  0.1615  275 LEU B CB  
5867  C CG  . LEU B 275 ? 0.1952 0.3346 0.3026 0.0262  0.0050  0.1680  275 LEU B CG  
5868  C CD1 . LEU B 275 ? 0.1597 0.2976 0.2725 0.0298  0.0092  0.1667  275 LEU B CD1 
5869  C CD2 . LEU B 275 ? 0.2069 0.3326 0.3088 0.0284  0.0064  0.1655  275 LEU B CD2 
5870  N N   . VAL B 276 ? 0.2044 0.3802 0.3224 0.0204  -0.0009 0.1828  276 VAL B N   
5871  C CA  . VAL B 276 ? 0.2106 0.3943 0.3327 0.0230  -0.0016 0.1937  276 VAL B CA  
5872  C C   . VAL B 276 ? 0.1899 0.3629 0.3135 0.0300  0.0026  0.1963  276 VAL B C   
5873  O O   . VAL B 276 ? 0.1867 0.3529 0.3130 0.0338  0.0068  0.1935  276 VAL B O   
5874  C CB  . VAL B 276 ? 0.1835 0.3818 0.3126 0.0230  -0.0018 0.2005  276 VAL B CB  
5875  C CG1 . VAL B 276 ? 0.1976 0.4048 0.3309 0.0254  -0.0028 0.2120  276 VAL B CG1 
5876  C CG2 . VAL B 276 ? 0.1746 0.3824 0.3019 0.0159  -0.0053 0.1970  276 VAL B CG2 
5877  N N   . ALA B 277 ? 0.2007 0.3719 0.3226 0.0315  0.0018  0.2015  277 ALA B N   
5878  C CA  . ALA B 277 ? 0.2109 0.3738 0.3351 0.0382  0.0058  0.2057  277 ALA B CA  
5879  C C   . ALA B 277 ? 0.2247 0.3972 0.3529 0.0401  0.0043  0.2172  277 ALA B C   
5880  O O   . ALA B 277 ? 0.2355 0.4161 0.3612 0.0358  0.0000  0.2202  277 ALA B O   
5881  C CB  . ALA B 277 ? 0.2109 0.3581 0.3280 0.0389  0.0071  0.1996  277 ALA B CB  
5882  N N   . ILE B 278 ? 0.2494 0.4215 0.3840 0.0463  0.0081  0.2238  278 ILE B N   
5883  C CA  . ILE B 278 ? 0.2472 0.4290 0.3867 0.0488  0.0072  0.2354  278 ILE B CA  
5884  C C   . ILE B 278 ? 0.2586 0.4296 0.3990 0.0552  0.0113  0.2391  278 ILE B C   
5885  O O   . ILE B 278 ? 0.3323 0.4940 0.4747 0.0595  0.0162  0.2362  278 ILE B O   
5886  C CB  . ILE B 278 ? 0.2940 0.4893 0.4420 0.0501  0.0077  0.2416  278 ILE B CB  
5887  C CG1 . ILE B 278 ? 0.2383 0.4454 0.3851 0.0432  0.0032  0.2390  278 ILE B CG1 
5888  C CG2 . ILE B 278 ? 0.3080 0.5117 0.4620 0.0541  0.0078  0.2539  278 ILE B CG2 
5889  C CD1 . ILE B 278 ? 0.2349 0.4517 0.3883 0.0437  0.0043  0.2414  278 ILE B CD1 
5890  N N   . ARG B 279 ? 0.2698 0.4421 0.4085 0.0556  0.0094  0.2455  279 ARG B N   
5891  C CA  . ARG B 279 ? 0.3020 0.4631 0.4401 0.0610  0.0129  0.2486  279 ARG B CA  
5892  C C   . ARG B 279 ? 0.3447 0.5065 0.4914 0.0679  0.0178  0.2551  279 ARG B C   
5893  O O   . ARG B 279 ? 0.3550 0.5050 0.5020 0.0716  0.0228  0.2510  279 ARG B O   
5894  C CB  . ARG B 279 ? 0.2921 0.4564 0.4271 0.0598  0.0096  0.2551  279 ARG B CB  
5895  C CG  . ARG B 279 ? 0.3324 0.4832 0.4640 0.0638  0.0125  0.2565  279 ARG B CG  
5896  C CD  . ARG B 279 ? 0.3425 0.4969 0.4695 0.0611  0.0083  0.2615  279 ARG B CD  
5897  N NE  . ARG B 279 ? 0.4235 0.5660 0.5471 0.0646  0.0107  0.2639  279 ARG B NE  
5898  C CZ  . ARG B 279 ? 0.4953 0.6395 0.6153 0.0634  0.0079  0.2695  279 ARG B CZ  
5899  N NH1 . ARG B 279 ? 0.4587 0.6165 0.5783 0.0587  0.0027  0.2734  279 ARG B NH1 
5900  N NH2 . ARG B 279 ? 0.5254 0.6576 0.6420 0.0668  0.0105  0.2713  279 ARG B NH2 
5901  N N   . ASP B 280 ? 0.3107 0.4862 0.4644 0.0695  0.0167  0.2652  280 ASP B N   
5902  C CA  . ASP B 280 ? 0.3650 0.5412 0.5271 0.0763  0.0215  0.2719  280 ASP B CA  
5903  C C   . ASP B 280 ? 0.3599 0.5531 0.5301 0.0765  0.0201  0.2795  280 ASP B C   
5904  O O   . ASP B 280 ? 0.3415 0.5364 0.5192 0.0818  0.0241  0.2846  280 ASP B O   
5905  C CB  . ASP B 280 ? 0.3651 0.5354 0.5277 0.0813  0.0236  0.2791  280 ASP B CB  
5906  C CG  . ASP B 280 ? 0.4866 0.6646 0.6465 0.0784  0.0185  0.2853  280 ASP B CG  
5907  O OD1 . ASP B 280 ? 0.5796 0.7718 0.7404 0.0739  0.0138  0.2876  280 ASP B OD1 
5908  O OD2 . ASP B 280 ? 0.4797 0.6496 0.6362 0.0805  0.0193  0.2879  280 ASP B OD2 
5909  N N   . ASN B 281 ? 0.3350 0.5411 0.5040 0.0706  0.0146  0.2801  281 ASN B N   
5910  C CA  . ASN B 281 ? 0.4044 0.6274 0.5810 0.0704  0.0131  0.2875  281 ASN B CA  
5911  C C   . ASN B 281 ? 0.3268 0.5503 0.5067 0.0706  0.0157  0.2827  281 ASN B C   
5912  O O   . ASN B 281 ? 0.3093 0.5361 0.4859 0.0651  0.0131  0.2760  281 ASN B O   
5913  C CB  . ASN B 281 ? 0.3705 0.6070 0.5443 0.0634  0.0067  0.2893  281 ASN B CB  
5914  C CG  . ASN B 281 ? 0.3755 0.6301 0.5572 0.0638  0.0050  0.2998  281 ASN B CG  
5915  O OD1 . ASN B 281 ? 0.3053 0.5656 0.4931 0.0657  0.0070  0.3014  281 ASN B OD1 
5916  N ND2 . ASN B 281 ? 0.3663 0.6303 0.5477 0.0620  0.0012  0.3072  281 ASN B ND2 
5917  N N   . GLU B 282 ? 0.3289 0.5496 0.5154 0.0770  0.0208  0.2864  282 GLU B N   
5918  C CA  . GLU B 282 ? 0.3027 0.5223 0.4919 0.0775  0.0237  0.2816  282 GLU B CA  
5919  C C   . GLU B 282 ? 0.3061 0.5425 0.4996 0.0742  0.0206  0.2853  282 GLU B C   
5920  O O   . GLU B 282 ? 0.3119 0.5485 0.5048 0.0718  0.0211  0.2792  282 GLU B O   
5921  C CB  . GLU B 282 ? 0.3396 0.5518 0.5347 0.0851  0.0302  0.2849  282 GLU B CB  
5922  C CG  . GLU B 282 ? 0.4270 0.6345 0.6233 0.0855  0.0337  0.2782  282 GLU B CG  
5923  C CD  . GLU B 282 ? 0.4625 0.6630 0.6645 0.0926  0.0403  0.2813  282 GLU B CD  
5924  O OE1 . GLU B 282 ? 0.5616 0.7676 0.7699 0.0973  0.0418  0.2916  282 GLU B OE1 
5925  O OE2 . GLU B 282 ? 0.4209 0.6103 0.6209 0.0933  0.0442  0.2736  282 GLU B OE2 
5926  N N   . GLU B 283 ? 0.3089 0.5594 0.5064 0.0739  0.0176  0.2953  283 GLU B N   
5927  C CA  . GLU B 283 ? 0.2996 0.5667 0.5005 0.0702  0.0144  0.2989  283 GLU B CA  
5928  C C   . GLU B 283 ? 0.2797 0.5498 0.4735 0.0619  0.0097  0.2910  283 GLU B C   
5929  O O   . GLU B 283 ? 0.2836 0.5594 0.4778 0.0586  0.0090  0.2876  283 GLU B O   
5930  C CB  . GLU B 283 ? 0.3205 0.6023 0.5271 0.0715  0.0121  0.3116  283 GLU B CB  
5931  C CG  . GLU B 283 ? 0.3912 0.6908 0.6017 0.0677  0.0090  0.3160  283 GLU B CG  
5932  C CD  . GLU B 283 ? 0.4911 0.8062 0.7069 0.0684  0.0063  0.3285  283 GLU B CD  
5933  O OE1 . GLU B 283 ? 0.4921 0.8037 0.7094 0.0726  0.0073  0.3343  283 GLU B OE1 
5934  O OE2 . GLU B 283 ? 0.5360 0.8667 0.7543 0.0644  0.0031  0.3324  283 GLU B OE2 
5935  N N   . ILE B 284 ? 0.2794 0.5458 0.4667 0.0585  0.0066  0.2882  284 ILE B N   
5936  C CA  . ILE B 284 ? 0.2846 0.5521 0.4647 0.0507  0.0026  0.2799  284 ILE B CA  
5937  C C   . ILE B 284 ? 0.2545 0.5101 0.4311 0.0501  0.0053  0.2686  284 ILE B C   
5938  O O   . ILE B 284 ? 0.2439 0.5037 0.4183 0.0450  0.0035  0.2631  284 ILE B O   
5939  C CB  . ILE B 284 ? 0.3171 0.5806 0.4904 0.0478  -0.0006 0.2786  284 ILE B CB  
5940  C CG1 . ILE B 284 ? 0.3593 0.6356 0.5358 0.0477  -0.0036 0.2900  284 ILE B CG1 
5941  C CG2 . ILE B 284 ? 0.2582 0.5218 0.4241 0.0398  -0.0043 0.2695  284 ILE B CG2 
5942  C CD1 . ILE B 284 ? 0.3355 0.6295 0.5133 0.0416  -0.0080 0.2933  284 ILE B CD1 
5943  N N   . PHE B 285 ? 0.2555 0.4961 0.4317 0.0553  0.0098  0.2652  285 PHE B N   
5944  C CA  . PHE B 285 ? 0.2451 0.4738 0.4179 0.0549  0.0126  0.2545  285 PHE B CA  
5945  C C   . PHE B 285 ? 0.2386 0.4731 0.4163 0.0554  0.0145  0.2545  285 PHE B C   
5946  O O   . PHE B 285 ? 0.2264 0.4590 0.4007 0.0514  0.0139  0.2464  285 PHE B O   
5947  C CB  . PHE B 285 ? 0.2656 0.4781 0.4376 0.0605  0.0174  0.2520  285 PHE B CB  
5948  C CG  . PHE B 285 ? 0.3167 0.5178 0.4871 0.0615  0.0213  0.2429  285 PHE B CG  
5949  C CD1 . PHE B 285 ? 0.2493 0.4438 0.4127 0.0566  0.0198  0.2321  285 PHE B CD1 
5950  C CD2 . PHE B 285 ? 0.2744 0.4712 0.4503 0.0672  0.0266  0.2451  285 PHE B CD2 
5951  C CE1 . PHE B 285 ? 0.2586 0.4428 0.4206 0.0574  0.0233  0.2238  285 PHE B CE1 
5952  C CE2 . PHE B 285 ? 0.2998 0.4861 0.4739 0.0678  0.0303  0.2366  285 PHE B CE2 
5953  C CZ  . PHE B 285 ? 0.2760 0.4561 0.4432 0.0628  0.0285  0.2261  285 PHE B CZ  
5954  N N   . THR B 286 ? 0.2817 0.5234 0.4673 0.0602  0.0166  0.2637  286 THR B N   
5955  C CA  . THR B 286 ? 0.2444 0.4920 0.4346 0.0607  0.0183  0.2644  286 THR B CA  
5956  C C   . THR B 286 ? 0.2639 0.5251 0.4527 0.0539  0.0137  0.2640  286 THR B C   
5957  O O   . THR B 286 ? 0.2674 0.5283 0.4548 0.0512  0.0141  0.2581  286 THR B O   
5958  C CB  . THR B 286 ? 0.2771 0.5307 0.4762 0.0671  0.0213  0.2753  286 THR B CB  
5959  O OG1 . THR B 286 ? 0.3394 0.5794 0.5395 0.0733  0.0263  0.2749  286 THR B OG1 
5960  C CG2 . THR B 286 ? 0.2543 0.5146 0.4579 0.0675  0.0228  0.2764  286 THR B CG2 
5961  N N   . LEU B 287 ? 0.2553 0.5283 0.4441 0.0508  0.0093  0.2702  287 LEU B N   
5962  C CA  . LEU B 287 ? 0.2753 0.5615 0.4624 0.0438  0.0049  0.2698  287 LEU B CA  
5963  C C   . LEU B 287 ? 0.2567 0.5358 0.4355 0.0376  0.0030  0.2581  287 LEU B C   
5964  O O   . LEU B 287 ? 0.2272 0.5112 0.4044 0.0331  0.0019  0.2540  287 LEU B O   
5965  C CB  . LEU B 287 ? 0.2754 0.5750 0.4639 0.0416  0.0007  0.2788  287 LEU B CB  
5966  C CG  . LEU B 287 ? 0.2606 0.5715 0.4579 0.0464  0.0017  0.2912  287 LEU B CG  
5967  C CD1 . LEU B 287 ? 0.3206 0.6430 0.5184 0.0442  -0.0025 0.2994  287 LEU B CD1 
5968  C CD2 . LEU B 287 ? 0.2578 0.5794 0.4591 0.0451  0.0019  0.2933  287 LEU B CD2 
5969  N N   . ALA B 288 ? 0.2226 0.4902 0.3960 0.0375  0.0028  0.2527  288 ALA B N   
5970  C CA  . ALA B 288 ? 0.2100 0.4698 0.3757 0.0321  0.0014  0.2415  288 ALA B CA  
5971  C C   . ALA B 288 ? 0.2473 0.4976 0.4123 0.0334  0.0050  0.2335  288 ALA B C   
5972  O O   . ALA B 288 ? 0.2141 0.4635 0.3746 0.0282  0.0037  0.2257  288 ALA B O   
5973  C CB  . ALA B 288 ? 0.2113 0.4601 0.3715 0.0324  0.0008  0.2379  288 ALA B CB  
5974  N N   . ARG B 289 ? 0.2148 0.4577 0.3840 0.0400  0.0097  0.2352  289 ARG B N   
5975  C CA  . ARG B 289 ? 0.2212 0.4560 0.3902 0.0412  0.0132  0.2283  289 ARG B CA  
5976  C C   . ARG B 289 ? 0.2111 0.4569 0.3825 0.0384  0.0124  0.2298  289 ARG B C   
5977  O O   . ARG B 289 ? 0.2202 0.4617 0.3882 0.0356  0.0130  0.2220  289 ARG B O   
5978  C CB  . ARG B 289 ? 0.2348 0.4605 0.4082 0.0487  0.0186  0.2308  289 ARG B CB  
5979  C CG  . ARG B 289 ? 0.2309 0.4397 0.3997 0.0505  0.0213  0.2229  289 ARG B CG  
5980  C CD  . ARG B 289 ? 0.3398 0.5402 0.5128 0.0569  0.0271  0.2241  289 ARG B CD  
5981  N NE  . ARG B 289 ? 0.3383 0.5227 0.5067 0.0582  0.0302  0.2156  289 ARG B NE  
5982  C CZ  . ARG B 289 ? 0.2901 0.4651 0.4609 0.0631  0.0355  0.2149  289 ARG B CZ  
5983  N NH1 . ARG B 289 ? 0.2470 0.4263 0.4246 0.0675  0.0386  0.2220  289 ARG B NH1 
5984  N NH2 . ARG B 289 ? 0.2614 0.4224 0.4273 0.0634  0.0380  0.2069  289 ARG B NH2 
5985  N N   . GLN B 290 ? 0.2167 0.4767 0.3936 0.0391  0.0109  0.2399  290 GLN B N   
5986  C CA  . GLN B 290 ? 0.2325 0.5035 0.4116 0.0365  0.0101  0.2421  290 GLN B CA  
5987  C C   . GLN B 290 ? 0.2135 0.4907 0.3868 0.0283  0.0060  0.2369  290 GLN B C   
5988  O O   . GLN B 290 ? 0.1949 0.4752 0.3671 0.0254  0.0060  0.2338  290 GLN B O   
5989  C CB  . GLN B 290 ? 0.2746 0.5597 0.4613 0.0395  0.0096  0.2546  290 GLN B CB  
5990  C CG  . GLN B 290 ? 0.3327 0.6128 0.5260 0.0476  0.0145  0.2599  290 GLN B CG  
5991  C CD  . GLN B 290 ? 0.4673 0.7600 0.6680 0.0511  0.0139  0.2728  290 GLN B CD  
5992  O OE1 . GLN B 290 ? 0.4020 0.7079 0.6030 0.0473  0.0097  0.2780  290 GLN B OE1 
5993  N NE2 . GLN B 290 ? 0.4256 0.7145 0.6325 0.0583  0.0182  0.2780  290 GLN B NE2 
5994  N N   . ARG B 291 ? 0.2072 0.4858 0.3765 0.0245  0.0025  0.2358  291 ARG B N   
5995  C CA  . ARG B 291 ? 0.1938 0.4763 0.3571 0.0165  -0.0010 0.2299  291 ARG B CA  
5996  C C   . ARG B 291 ? 0.2230 0.4912 0.3800 0.0147  0.0003  0.2177  291 ARG B C   
5997  O O   . ARG B 291 ? 0.2241 0.4938 0.3770 0.0092  -0.0009 0.2117  291 ARG B O   
5998  C CB  . ARG B 291 ? 0.2278 0.5178 0.3890 0.0126  -0.0052 0.2334  291 ARG B CB  
5999  C CG  . ARG B 291 ? 0.2328 0.5284 0.3882 0.0040  -0.0087 0.2280  291 ARG B CG  
6000  C CD  . ARG B 291 ? 0.2046 0.5112 0.3589 -0.0006 -0.0130 0.2331  291 ARG B CD  
6001  N NE  . ARG B 291 ? 0.1882 0.4990 0.3368 -0.0091 -0.0157 0.2272  291 ARG B NE  
6002  C CZ  . ARG B 291 ? 0.2519 0.5749 0.4008 -0.0139 -0.0169 0.2291  291 ARG B CZ  
6003  N NH1 . ARG B 291 ? 0.1834 0.5164 0.3381 -0.0114 -0.0162 0.2370  291 ARG B NH1 
6004  N NH2 . ARG B 291 ? 0.2698 0.5949 0.4130 -0.0217 -0.0189 0.2230  291 ARG B NH2 
6005  N N   . CYS B 292 ? 0.2210 0.4753 0.3771 0.0192  0.0029  0.2141  292 CYS B N   
6006  C CA  . CYS B 292 ? 0.2009 0.4417 0.3514 0.0178  0.0041  0.2027  292 CYS B CA  
6007  C C   . CYS B 292 ? 0.2108 0.4494 0.3610 0.0170  0.0064  0.1977  292 CYS B C   
6008  O O   . CYS B 292 ? 0.1911 0.4248 0.3359 0.0126  0.0058  0.1890  292 CYS B O   
6009  C CB  . CYS B 292 ? 0.1661 0.3928 0.3164 0.0234  0.0072  0.2007  292 CYS B CB  
6010  S SG  . CYS B 292 ? 0.1973 0.4068 0.3412 0.0225  0.0093  0.1870  292 CYS B SG  
6011  N N   . VAL B 293 ? 0.2265 0.4688 0.3821 0.0210  0.0089  0.2033  293 VAL B N   
6012  C CA  . VAL B 293 ? 0.1877 0.4256 0.3427 0.0212  0.0116  0.1987  293 VAL B CA  
6013  C C   . VAL B 293 ? 0.1882 0.4338 0.3395 0.0146  0.0091  0.1956  293 VAL B C   
6014  O O   . VAL B 293 ? 0.1429 0.3797 0.2889 0.0123  0.0098  0.1865  293 VAL B O   
6015  C CB  . VAL B 293 ? 0.1949 0.4353 0.3567 0.0272  0.0148  0.2060  293 VAL B CB  
6016  C CG1 . VAL B 293 ? 0.2313 0.4702 0.3923 0.0264  0.0167  0.2024  293 VAL B CG1 
6017  C CG2 . VAL B 293 ? 0.2478 0.4768 0.4121 0.0337  0.0186  0.2063  293 VAL B CG2 
6018  N N   . PRO B 294 ? 0.1726 0.4332 0.3256 0.0112  0.0060  0.2023  294 PRO B N   
6019  C CA  . PRO B 294 ? 0.1590 0.4248 0.3068 0.0046  0.0035  0.1982  294 PRO B CA  
6020  C C   . PRO B 294 ? 0.1755 0.4329 0.3139 -0.0004 0.0003  0.1882  294 PRO B C   
6021  O O   . PRO B 294 ? 0.2340 0.4832 0.3634 -0.0036 -0.0014 0.1786  294 PRO B O   
6022  C CB  . PRO B 294 ? 0.1633 0.4479 0.3157 0.0025  0.0012  0.2088  294 PRO B CB  
6023  C CG  . PRO B 294 ? 0.2019 0.4887 0.3614 0.0092  0.0026  0.2176  294 PRO B CG  
6024  C CD  . PRO B 294 ? 0.2004 0.4731 0.3592 0.0134  0.0046  0.2136  294 PRO B CD  
6025  N N   . MET B 295 ? 0.1569 0.4159 0.2971 -0.0010 -0.0005 0.1904  295 MET B N   
6026  C CA  . MET B 295 ? 0.1698 0.4251 0.3021 -0.0065 -0.0042 0.1834  295 MET B CA  
6027  C C   . MET B 295 ? 0.2039 0.4409 0.3296 -0.0056 -0.0033 0.1719  295 MET B C   
6028  O O   . MET B 295 ? 0.1777 0.4064 0.2942 -0.0097 -0.0057 0.1621  295 MET B O   
6029  C CB  . MET B 295 ? 0.1832 0.4505 0.3204 -0.0081 -0.0060 0.1920  295 MET B CB  
6030  C CG  . MET B 295 ? 0.2400 0.5243 0.3809 -0.0100 -0.0082 0.2018  295 MET B CG  
6031  S SD  . MET B 295 ? 0.2607 0.5499 0.3933 -0.0181 -0.0117 0.1965  295 MET B SD  
6032  C CE  . MET B 295 ? 0.2328 0.5450 0.3738 -0.0191 -0.0127 0.2109  295 MET B CE  
6033  N N   . GLU B 296 ? 0.1888 0.4195 0.3194 -0.0003 0.0001  0.1732  296 GLU B N   
6034  C CA  . GLU B 296 ? 0.1690 0.3837 0.2944 0.0007  0.0010  0.1636  296 GLU B CA  
6035  C C   . GLU B 296 ? 0.2062 0.4083 0.3304 0.0049  0.0045  0.1578  296 GLU B C   
6036  O O   . GLU B 296 ? 0.1993 0.3884 0.3150 0.0034  0.0039  0.1466  296 GLU B O   
6037  C CB  . GLU B 296 ? 0.1511 0.3662 0.2807 0.0033  0.0016  0.1683  296 GLU B CB  
6038  C CG  . GLU B 296 ? 0.1611 0.3848 0.2889 -0.0012 -0.0027 0.1717  296 GLU B CG  
6039  C CD  . GLU B 296 ? 0.1966 0.4153 0.3170 -0.0071 -0.0052 0.1623  296 GLU B CD  
6040  O OE1 . GLU B 296 ? 0.2376 0.4419 0.3534 -0.0057 -0.0041 0.1536  296 GLU B OE1 
6041  O OE2 . GLU B 296 ? 0.2574 0.4832 0.3741 -0.0126 -0.0088 0.1625  296 GLU B OE2 
6042  N N   . GLY B 297 ? 0.1511 0.3569 0.2837 0.0101  0.0084  0.1654  297 GLY B N   
6043  C CA  . GLY B 297 ? 0.1995 0.3938 0.3314 0.0140  0.0120  0.1607  297 GLY B CA  
6044  C C   . GLY B 297 ? 0.1988 0.3958 0.3398 0.0203  0.0163  0.1696  297 GLY B C   
6045  O O   . GLY B 297 ? 0.2226 0.4272 0.3673 0.0222  0.0150  0.1779  297 GLY B O   
6046  N N   . PHE B 298 ? 0.2198 0.4067 0.3613 0.0239  0.0204  0.1661  298 PHE B N   
6047  C CA  . PHE B 298 ? 0.1933 0.3771 0.3400 0.0305  0.0238  0.1719  298 PHE B CA  
6048  C C   . PHE B 298 ? 0.2174 0.3965 0.3635 0.0325  0.0233  0.1729  298 PHE B C   
6049  O O   . PHE B 298 ? 0.2205 0.3946 0.3614 0.0295  0.0213  0.1666  298 PHE B O   
6050  C CB  . PHE B 298 ? 0.1992 0.3719 0.3457 0.0333  0.0285  0.1669  298 PHE B CB  
6051  C CG  . PHE B 298 ? 0.1504 0.3210 0.3027 0.0398  0.0324  0.1734  298 PHE B CG  
6052  C CD1 . PHE B 298 ? 0.2260 0.4072 0.3844 0.0423  0.0325  0.1831  298 PHE B CD1 
6053  C CD2 . PHE B 298 ? 0.1666 0.3250 0.3182 0.0432  0.0362  0.1698  298 PHE B CD2 
6054  C CE1 . PHE B 298 ? 0.2176 0.3969 0.3817 0.0484  0.0363  0.1893  298 PHE B CE1 
6055  C CE2 . PHE B 298 ? 0.2346 0.3908 0.3915 0.0491  0.0403  0.1758  298 PHE B CE2 
6056  C CZ  . PHE B 298 ? 0.2778 0.4443 0.4411 0.0518  0.0404  0.1856  298 PHE B CZ  
6057  N N   . VAL B 299 ? 0.1983 0.3791 0.3496 0.0378  0.0252  0.1810  299 VAL B N   
6058  C CA  . VAL B 299 ? 0.1596 0.3384 0.3106 0.0396  0.0242  0.1841  299 VAL B CA  
6059  C C   . VAL B 299 ? 0.2029 0.3666 0.3498 0.0414  0.0267  0.1770  299 VAL B C   
6060  O O   . VAL B 299 ? 0.2020 0.3625 0.3471 0.0423  0.0257  0.1783  299 VAL B O   
6061  C CB  . VAL B 299 ? 0.2541 0.4392 0.4121 0.0448  0.0258  0.1954  299 VAL B CB  
6062  C CG1 . VAL B 299 ? 0.2328 0.4337 0.3947 0.0428  0.0231  0.2024  299 VAL B CG1 
6063  C CG2 . VAL B 299 ? 0.2311 0.4080 0.3926 0.0504  0.0315  0.1957  299 VAL B CG2 
6064  N N   . THR B 300 ? 0.1655 0.3200 0.3106 0.0417  0.0300  0.1697  300 THR B N   
6065  C CA  . THR B 300 ? 0.1797 0.3205 0.3206 0.0429  0.0324  0.1625  300 THR B CA  
6066  C C   . THR B 300 ? 0.2237 0.3597 0.3580 0.0377  0.0300  0.1522  300 THR B C   
6067  O O   . THR B 300 ? 0.2049 0.3298 0.3352 0.0382  0.0318  0.1455  300 THR B O   
6068  C CB  . THR B 300 ? 0.1396 0.2722 0.2829 0.0471  0.0381  0.1614  300 THR B CB  
6069  O OG1 . THR B 300 ? 0.1652 0.2995 0.3085 0.0449  0.0388  0.1578  300 THR B OG1 
6070  C CG2 . THR B 300 ? 0.1670 0.3034 0.3170 0.0526  0.0407  0.1716  300 THR B CG2 
6071  N N   . TYR B 301 ? 0.1826 0.3267 0.3154 0.0328  0.0263  0.1509  301 TYR B N   
6072  C CA  . TYR B 301 ? 0.1840 0.3249 0.3107 0.0277  0.0234  0.1423  301 TYR B CA  
6073  C C   . TYR B 301 ? 0.1592 0.3108 0.2848 0.0230  0.0182  0.1449  301 TYR B C   
6074  O O   . TYR B 301 ? 0.1758 0.3246 0.2965 0.0196  0.0155  0.1395  301 TYR B O   
6075  C CB  . TYR B 301 ? 0.1484 0.2838 0.2717 0.0255  0.0245  0.1337  301 TYR B CB  
6076  C CG  . TYR B 301 ? 0.2097 0.3505 0.3314 0.0231  0.0220  0.1341  301 TYR B CG  
6077  C CD1 . TYR B 301 ? 0.2015 0.3447 0.3169 0.0179  0.0170  0.1298  301 TYR B CD1 
6078  C CD2 . TYR B 301 ? 0.1926 0.3359 0.3188 0.0260  0.0250  0.1386  301 TYR B CD2 
6079  C CE1 . TYR B 301 ? 0.1513 0.2995 0.2650 0.0157  0.0151  0.1301  301 TYR B CE1 
6080  C CE2 . TYR B 301 ? 0.2087 0.3573 0.3334 0.0239  0.0228  0.1391  301 TYR B CE2 
6081  C CZ  . TYR B 301 ? 0.1761 0.3272 0.2945 0.0187  0.0179  0.1349  301 TYR B CZ  
6082  O OH  . TYR B 301 ? 0.2056 0.3617 0.3222 0.0167  0.0161  0.1355  301 TYR B OH  
6083  N N   . GLY B 302 ? 0.1727 0.3365 0.3025 0.0226  0.0169  0.1528  302 GLY B N   
6084  C CA  . GLY B 302 ? 0.1423 0.3168 0.2712 0.0183  0.0122  0.1565  302 GLY B CA  
6085  C C   . GLY B 302 ? 0.1030 0.2780 0.2265 0.0118  0.0092  0.1488  302 GLY B C   
6086  O O   . GLY B 302 ? 0.1601 0.3383 0.2808 0.0082  0.0057  0.1487  302 GLY B O   
6087  N N   . GLY B 303 ? 0.1379 0.3047 0.2559 0.0107  0.0094  0.1404  303 GLY B N   
6088  C CA  . GLY B 303 ? 0.1611 0.3212 0.2689 0.0056  0.0056  0.1302  303 GLY B CA  
6089  C C   . GLY B 303 ? 0.1542 0.3010 0.2558 0.0051  0.0054  0.1206  303 GLY B C   
6090  O O   . GLY B 303 ? 0.1574 0.2993 0.2511 0.0009  0.0022  0.1130  303 GLY B O   
6091  N N   . LEU B 304 ? 0.1469 0.2873 0.2515 0.0093  0.0088  0.1207  304 LEU B N   
6092  C CA  . LEU B 304 ? 0.1652 0.2928 0.2640 0.0092  0.0089  0.1115  304 LEU B CA  
6093  C C   . LEU B 304 ? 0.1723 0.2877 0.2680 0.0119  0.0120  0.1046  304 LEU B C   
6094  O O   . LEU B 304 ? 0.1208 0.2380 0.2223 0.0156  0.0156  0.1097  304 LEU B O   
6095  C CB  . LEU B 304 ? 0.2209 0.3508 0.3250 0.0114  0.0104  0.1169  304 LEU B CB  
6096  C CG  . LEU B 304 ? 0.1674 0.3057 0.2718 0.0082  0.0068  0.1214  304 LEU B CG  
6097  C CD1 . LEU B 304 ? 0.1451 0.2768 0.2483 0.0121  0.0074  0.1244  304 LEU B CD1 
6098  C CD2 . LEU B 304 ? 0.1476 0.2800 0.2432 0.0032  0.0030  0.1120  304 LEU B CD2 
6099  N N   . ALA B 305 ? 0.1854 0.2889 0.2721 0.0098  0.0105  0.0932  305 ALA B N   
6100  C CA  . ALA B 305 ? 0.1601 0.2517 0.2435 0.0120  0.0133  0.0863  305 ALA B CA  
6101  C C   . ALA B 305 ? 0.1377 0.2278 0.2263 0.0159  0.0171  0.0900  305 ALA B C   
6102  O O   . ALA B 305 ? 0.1076 0.2014 0.1990 0.0161  0.0167  0.0939  305 ALA B O   
6103  C CB  . ALA B 305 ? 0.1729 0.2529 0.2457 0.0089  0.0108  0.0737  305 ALA B CB  
6104  N N   . GLY B 306 ? 0.1395 0.2238 0.2292 0.0190  0.0210  0.0892  306 GLY B N   
6105  C CA  . GLY B 306 ? 0.1418 0.2233 0.2356 0.0228  0.0254  0.0921  306 GLY B CA  
6106  C C   . GLY B 306 ? 0.1490 0.2239 0.2380 0.0217  0.0244  0.0863  306 GLY B C   
6107  O O   . GLY B 306 ? 0.1361 0.2127 0.2296 0.0242  0.0269  0.0913  306 GLY B O   
6108  N N   . ARG B 307 ? 0.1554 0.2227 0.2349 0.0181  0.0209  0.0758  307 ARG B N   
6109  C CA  . ARG B 307 ? 0.1251 0.1862 0.1997 0.0170  0.0198  0.0701  307 ARG B CA  
6110  C C   . ARG B 307 ? 0.1369 0.2061 0.2154 0.0161  0.0177  0.0761  307 ARG B C   
6111  O O   . ARG B 307 ? 0.1143 0.1812 0.1930 0.0170  0.0186  0.0761  307 ARG B O   
6112  C CB  . ARG B 307 ? 0.1409 0.1932 0.2049 0.0134  0.0164  0.0581  307 ARG B CB  
6113  C CG  . ARG B 307 ? 0.1500 0.2053 0.2110 0.0100  0.0125  0.0561  307 ARG B CG  
6114  C CD  . ARG B 307 ? 0.1652 0.2111 0.2155 0.0068  0.0094  0.0443  307 ARG B CD  
6115  N NE  . ARG B 307 ? 0.1843 0.2318 0.2316 0.0041  0.0067  0.0421  307 ARG B NE  
6116  C CZ  . ARG B 307 ? 0.2174 0.2531 0.2532 0.0050  0.0050  0.0437  307 ARG B CZ  
6117  N NH1 . ARG B 307 ? 0.1658 0.1980 0.2024 0.0067  0.0071  0.0429  307 ARG B NH1 
6118  N NH2 . ARG B 307 ? 0.1865 0.2360 0.2317 0.0034  0.0032  0.0402  307 ARG B NH2 
6119  N N   . ASP B 308 ? 0.1550 0.2338 0.2365 0.0142  0.0150  0.0814  308 ASP B N   
6120  C CA  . ASP B 308 ? 0.1392 0.2262 0.2235 0.0124  0.0124  0.0869  308 ASP B CA  
6121  C C   . ASP B 308 ? 0.1462 0.2361 0.2356 0.0163  0.0146  0.0962  308 ASP B C   
6122  O O   . ASP B 308 ? 0.1505 0.2366 0.2360 0.0162  0.0129  0.0970  308 ASP B O   
6123  C CB  . ASP B 308 ? 0.1123 0.2068 0.1950 0.0082  0.0082  0.0881  308 ASP B CB  
6124  C CG  . ASP B 308 ? 0.1582 0.2438 0.2306 0.0044  0.0050  0.0767  308 ASP B CG  
6125  O OD1 . ASP B 308 ? 0.1813 0.2605 0.2486 0.0029  0.0035  0.0707  308 ASP B OD1 
6126  O OD2 . ASP B 308 ? 0.2188 0.3034 0.2883 0.0033  0.0043  0.0737  308 ASP B OD2 
6127  N N   . MET B 309 ? 0.1485 0.2414 0.2434 0.0198  0.0179  0.1022  309 MET B N   
6128  C CA  . MET B 309 ? 0.1186 0.2090 0.2153 0.0243  0.0201  0.1091  309 MET B CA  
6129  C C   . MET B 309 ? 0.1272 0.2051 0.2195 0.0265  0.0228  0.1042  309 MET B C   
6130  O O   . MET B 309 ? 0.1086 0.1825 0.1989 0.0284  0.0228  0.1076  309 MET B O   
6131  C CB  . MET B 309 ? 0.1737 0.2684 0.2771 0.0279  0.0236  0.1154  309 MET B CB  
6132  C CG  . MET B 309 ? 0.1511 0.2589 0.2592 0.0265  0.0212  0.1227  309 MET B CG  
6133  S SD  . MET B 309 ? 0.2423 0.3537 0.3580 0.0318  0.0256  0.1310  309 MET B SD  
6134  C CE  . MET B 309 ? 0.1219 0.2314 0.2381 0.0304  0.0283  0.1243  309 MET B CE  
6135  N N   . ALA B 310 ? 0.1529 0.2246 0.2432 0.0262  0.0252  0.0962  310 ALA B N   
6136  C CA  . ALA B 310 ? 0.1564 0.2168 0.2419 0.0277  0.0277  0.0909  310 ALA B CA  
6137  C C   . ALA B 310 ? 0.1809 0.2374 0.2599 0.0252  0.0239  0.0875  310 ALA B C   
6138  O O   . ALA B 310 ? 0.1642 0.2134 0.2396 0.0268  0.0250  0.0881  310 ALA B O   
6139  C CB  . ALA B 310 ? 0.1836 0.2400 0.2682 0.0272  0.0307  0.0830  310 ALA B CB  
6140  N N   . ALA B 311 ? 0.1285 0.1893 0.2054 0.0209  0.0196  0.0839  311 ALA B N   
6141  C CA  . ALA B 311 ? 0.1279 0.1853 0.1984 0.0180  0.0158  0.0809  311 ALA B CA  
6142  C C   . ALA B 311 ? 0.1211 0.1813 0.1913 0.0183  0.0137  0.0889  311 ALA B C   
6143  O O   . ALA B 311 ? 0.1502 0.2042 0.2146 0.0175  0.0124  0.0879  311 ALA B O   
6144  C CB  . ALA B 311 ? 0.1095 0.1718 0.1786 0.0133  0.0118  0.0759  311 ALA B CB  
6145  N N   . MET B 312 ? 0.1387 0.2082 0.2149 0.0192  0.0135  0.0970  312 MET B N   
6146  C CA  . MET B 312 ? 0.1685 0.2421 0.2449 0.0195  0.0115  0.1052  312 MET B CA  
6147  C C   . MET B 312 ? 0.1281 0.1932 0.2032 0.0238  0.0147  0.1083  312 MET B C   
6148  O O   . MET B 312 ? 0.1715 0.2341 0.2426 0.0233  0.0130  0.1112  312 MET B O   
6149  C CB  . MET B 312 ? 0.1429 0.2291 0.2263 0.0198  0.0108  0.1132  312 MET B CB  
6150  C CG  . MET B 312 ? 0.1441 0.2367 0.2277 0.0193  0.0081  0.1218  312 MET B CG  
6151  S SD  . MET B 312 ? 0.2112 0.3201 0.3028 0.0192  0.0069  0.1314  312 MET B SD  
6152  C CE  . MET B 312 ? 0.1738 0.2896 0.2654 0.0135  0.0043  0.1250  312 MET B CE  
6153  N N   . VAL B 313 ? 0.1665 0.2271 0.2448 0.0278  0.0196  0.1080  313 VAL B N   
6154  C CA  . VAL B 313 ? 0.1757 0.2282 0.2533 0.0318  0.0231  0.1110  313 VAL B CA  
6155  C C   . VAL B 313 ? 0.1939 0.2358 0.2634 0.0304  0.0228  0.1049  313 VAL B C   
6156  O O   . VAL B 313 ? 0.2184 0.2550 0.2849 0.0317  0.0231  0.1082  313 VAL B O   
6157  C CB  . VAL B 313 ? 0.1950 0.2450 0.2775 0.0358  0.0287  0.1109  313 VAL B CB  
6158  C CG1 . VAL B 313 ? 0.2199 0.2611 0.3014 0.0397  0.0327  0.1135  313 VAL B CG1 
6159  C CG2 . VAL B 313 ? 0.1640 0.2244 0.2542 0.0372  0.0290  0.1176  313 VAL B CG2 
6160  N N   . GLN B 314 ? 0.1933 0.2317 0.2589 0.0277  0.0221  0.0959  314 GLN B N   
6161  C CA  . GLN B 314 ? 0.1967 0.2254 0.2544 0.0262  0.0217  0.0897  314 GLN B CA  
6162  C C   . GLN B 314 ? 0.2035 0.2334 0.2558 0.0224  0.0166  0.0905  314 GLN B C   
6163  O O   . GLN B 314 ? 0.2313 0.2541 0.2778 0.0221  0.0163  0.0907  314 GLN B O   
6164  C CB  . GLN B 314 ? 0.1891 0.2142 0.2446 0.0249  0.0228  0.0801  314 GLN B CB  
6165  C CG  . GLN B 314 ? 0.2019 0.2177 0.2490 0.0230  0.0223  0.0733  314 GLN B CG  
6166  C CD  . GLN B 314 ? 0.2371 0.2441 0.2820 0.0259  0.0264  0.0742  314 GLN B CD  
6167  O OE1 . GLN B 314 ? 0.3146 0.3213 0.3643 0.0295  0.0308  0.0772  314 GLN B OE1 
6168  N NE2 . GLN B 314 ? 0.2039 0.2037 0.2415 0.0243  0.0251  0.0716  314 GLN B NE2 
6169  N N   . GLY B 315 ? 0.2254 0.2646 0.2794 0.0191  0.0128  0.0910  315 GLY B N   
6170  C CA  . GLY B 315 ? 0.2097 0.2513 0.2589 0.0150  0.0082  0.0919  315 GLY B CA  
6171  C C   . GLY B 315 ? 0.2383 0.2822 0.2876 0.0160  0.0074  0.1008  315 GLY B C   
6172  O O   . GLY B 315 ? 0.2408 0.2817 0.2841 0.0136  0.0051  0.1011  315 GLY B O   
6173  N N   . LEU B 316 ? 0.2047 0.2542 0.2611 0.0196  0.0093  0.1083  316 LEU B N   
6174  C CA  . LEU B 316 ? 0.2177 0.2689 0.2745 0.0213  0.0090  0.1171  316 LEU B CA  
6175  C C   . LEU B 316 ? 0.2308 0.2696 0.2815 0.0228  0.0110  0.1160  316 LEU B C   
6176  O O   . LEU B 316 ? 0.2240 0.2617 0.2706 0.0217  0.0091  0.1200  316 LEU B O   
6177  C CB  . LEU B 316 ? 0.1871 0.2446 0.2525 0.0256  0.0116  0.1247  316 LEU B CB  
6178  C CG  . LEU B 316 ? 0.1670 0.2392 0.2383 0.0240  0.0089  0.1301  316 LEU B CG  
6179  C CD1 . LEU B 316 ? 0.1526 0.2295 0.2323 0.0286  0.0122  0.1359  316 LEU B CD1 
6180  C CD2 . LEU B 316 ? 0.1756 0.2540 0.2449 0.0216  0.0051  0.1367  316 LEU B CD2 
6181  N N   . GLU B 317 ? 0.2659 0.2953 0.3156 0.0251  0.0149  0.1105  317 GLU B N   
6182  C CA  . GLU B 317 ? 0.2912 0.3088 0.3350 0.0262  0.0170  0.1088  317 GLU B CA  
6183  C C   . GLU B 317 ? 0.2288 0.2408 0.2634 0.0217  0.0140  0.1029  317 GLU B C   
6184  O O   . GLU B 317 ? 0.2896 0.2965 0.3186 0.0208  0.0132  0.1051  317 GLU B O   
6185  C CB  . GLU B 317 ? 0.2614 0.2719 0.3070 0.0295  0.0222  0.1043  317 GLU B CB  
6186  C CG  . GLU B 317 ? 0.3268 0.3253 0.3663 0.0302  0.0247  0.1016  317 GLU B CG  
6187  C CD  . GLU B 317 ? 0.3348 0.3305 0.3745 0.0329  0.0260  0.1097  317 GLU B CD  
6188  O OE1 . GLU B 317 ? 0.3412 0.3442 0.3871 0.0353  0.0260  0.1176  317 GLU B OE1 
6189  O OE2 . GLU B 317 ? 0.3902 0.3766 0.4241 0.0326  0.0271  0.1083  317 GLU B OE2 
6190  N N   . GLU B 318 ? 0.2240 0.2371 0.2570 0.0187  0.0124  0.0954  318 GLU B N   
6191  C CA  . GLU B 318 ? 0.2346 0.2421 0.2589 0.0146  0.0099  0.0892  318 GLU B CA  
6192  C C   . GLU B 318 ? 0.2475 0.2598 0.2685 0.0110  0.0058  0.0934  318 GLU B C   
6193  O O   . GLU B 318 ? 0.2302 0.2361 0.2434 0.0085  0.0047  0.0913  318 GLU B O   
6194  C CB  . GLU B 318 ? 0.2111 0.2198 0.2351 0.0124  0.0089  0.0809  318 GLU B CB  
6195  C CG  . GLU B 318 ? 0.2316 0.2355 0.2577 0.0152  0.0129  0.0756  318 GLU B CG  
6196  C CD  . GLU B 318 ? 0.2970 0.3015 0.3217 0.0128  0.0117  0.0671  318 GLU B CD  
6197  O OE1 . GLU B 318 ? 0.2672 0.2747 0.2888 0.0089  0.0077  0.0650  318 GLU B OE1 
6198  O OE2 . GLU B 318 ? 0.2099 0.2120 0.2365 0.0148  0.0148  0.0624  318 GLU B OE2 
6199  N N   . GLY B 319 ? 0.2075 0.2315 0.2343 0.0106  0.0037  0.0994  319 GLY B N   
6200  C CA  . GLY B 319 ? 0.2321 0.2626 0.2564 0.0068  -0.0001 0.1034  319 GLY B CA  
6201  C C   . GLY B 319 ? 0.2347 0.2620 0.2560 0.0080  0.0002  0.1102  319 GLY B C   
6202  O O   . GLY B 319 ? 0.2900 0.3212 0.3079 0.0046  -0.0028 0.1129  319 GLY B O   
6203  N N   . THR B 320 ? 0.2253 0.2461 0.2483 0.0127  0.0039  0.1131  320 THR B N   
6204  C CA  . THR B 320 ? 0.2582 0.2746 0.2782 0.0141  0.0046  0.1193  320 THR B CA  
6205  C C   . THR B 320 ? 0.2650 0.2678 0.2757 0.0129  0.0058  0.1142  320 THR B C   
6206  O O   . THR B 320 ? 0.2768 0.2752 0.2835 0.0132  0.0060  0.1186  320 THR B O   
6207  C CB  . THR B 320 ? 0.2773 0.2935 0.3040 0.0198  0.0081  0.1256  320 THR B CB  
6208  O OG1 . THR B 320 ? 0.2807 0.2883 0.3081 0.0226  0.0122  0.1200  320 THR B OG1 
6209  C CG2 . THR B 320 ? 0.2182 0.2478 0.2542 0.0213  0.0072  0.1314  320 THR B CG2 
6210  N N   . GLU B 321 ? 0.2573 0.2538 0.2646 0.0115  0.0066  0.1052  321 GLU B N   
6211  C CA  . GLU B 321 ? 0.2508 0.2346 0.2499 0.0106  0.0081  0.1003  321 GLU B CA  
6212  C C   . GLU B 321 ? 0.2723 0.2548 0.2632 0.0061  0.0052  0.1000  321 GLU B C   
6213  O O   . GLU B 321 ? 0.3262 0.3138 0.3156 0.0024  0.0025  0.0965  321 GLU B O   
6214  C CB  . GLU B 321 ? 0.2594 0.2384 0.2576 0.0103  0.0096  0.0910  321 GLU B CB  
6215  C CG  . GLU B 321 ? 0.2791 0.2590 0.2852 0.0149  0.0133  0.0911  321 GLU B CG  
6216  C CD  . GLU B 321 ? 0.4290 0.4057 0.4349 0.0146  0.0148  0.0821  321 GLU B CD  
6217  O OE1 . GLU B 321 ? 0.3883 0.3614 0.3876 0.0110  0.0129  0.0755  321 GLU B OE1 
6218  O OE2 . GLU B 321 ? 0.4009 0.3790 0.4131 0.0181  0.0181  0.0815  321 GLU B OE2 
6219  N N   . GLU B 322 ? 0.2882 0.2638 0.2740 0.0063  0.0061  0.1036  322 GLU B N   
6220  C CA  . GLU B 322 ? 0.2819 0.2572 0.2605 0.0024  0.0038  0.1049  322 GLU B CA  
6221  C C   . GLU B 322 ? 0.2999 0.2701 0.2713 -0.0016 0.0031  0.0960  322 GLU B C   
6222  O O   . GLU B 322 ? 0.2892 0.2646 0.2581 -0.0054 0.0006  0.0955  322 GLU B O   
6223  C CB  . GLU B 322 ? 0.2439 0.2114 0.2183 0.0037  0.0053  0.1099  322 GLU B CB  
6224  C CG  . GLU B 322 ? 0.3262 0.2923 0.2928 -0.0001 0.0035  0.1112  322 GLU B CG  
6225  C CD  . GLU B 322 ? 0.3669 0.3265 0.3303 0.0015  0.0050  0.1173  322 GLU B CD  
6226  O OE1 . GLU B 322 ? 0.3940 0.3528 0.3628 0.0058  0.0069  0.1221  322 GLU B OE1 
6227  O OE2 . GLU B 322 ? 0.4784 0.4336 0.4340 -0.0014 0.0044  0.1174  322 GLU B OE2 
6228  N N   . GLU B 323 ? 0.2551 0.2159 0.2236 -0.0010 0.0054  0.0893  323 GLU B N   
6229  C CA  A GLU B 323 ? 0.2875 0.2431 0.2489 -0.0044 0.0052  0.0809  323 GLU B CA  
6230  C CA  B GLU B 323 ? 0.2877 0.2431 0.2492 -0.0044 0.0053  0.0808  323 GLU B CA  
6231  C C   . GLU B 323 ? 0.3039 0.2688 0.2692 -0.0062 0.0030  0.0771  323 GLU B C   
6232  O O   . GLU B 323 ? 0.2904 0.2563 0.2521 -0.0094 0.0019  0.0729  323 GLU B O   
6233  C CB  A GLU B 323 ? 0.3000 0.2451 0.2583 -0.0038 0.0075  0.0749  323 GLU B CB  
6234  C CB  B GLU B 323 ? 0.3001 0.2457 0.2593 -0.0035 0.0075  0.0748  323 GLU B CB  
6235  C CG  A GLU B 323 ? 0.3302 0.2785 0.2966 -0.0008 0.0086  0.0726  323 GLU B CG  
6236  C CG  B GLU B 323 ? 0.3260 0.2638 0.2761 -0.0070 0.0078  0.0669  323 GLU B CG  
6237  C CD  A GLU B 323 ? 0.3405 0.2899 0.3142 0.0039  0.0111  0.0791  323 GLU B CD  
6238  C CD  B GLU B 323 ? 0.3909 0.3241 0.3423 -0.0075 0.0080  0.0616  323 GLU B CD  
6239  O OE1 A GLU B 323 ? 0.2472 0.1966 0.2206 0.0049  0.0111  0.0864  323 GLU B OE1 
6240  O OE1 B GLU B 323 ? 0.3682 0.3053 0.3284 -0.0037 0.0095  0.0623  323 GLU B OE1 
6241  O OE2 A GLU B 323 ? 0.3587 0.3092 0.3386 0.0069  0.0135  0.0768  323 GLU B OE2 
6242  O OE2 B GLU B 323 ? 0.4235 0.3546 0.3722 -0.0109 0.0066  0.0567  323 GLU B OE2 
6243  N N   . TYR B 324 ? 0.2318 0.2046 0.2055 -0.0042 0.0024  0.0787  324 TYR B N   
6244  C CA  . TYR B 324 ? 0.2146 0.1974 0.1925 -0.0065 -0.0003 0.0760  324 TYR B CA  
6245  C C   . TYR B 324 ? 0.2744 0.2679 0.2539 -0.0097 -0.0038 0.0815  324 TYR B C   
6246  O O   . TYR B 324 ? 0.2661 0.2651 0.2449 -0.0140 -0.0065 0.0780  324 TYR B O   
6247  C CB  . TYR B 324 ? 0.2789 0.2675 0.2653 -0.0036 0.0001  0.0765  324 TYR B CB  
6248  C CG  . TYR B 324 ? 0.2474 0.2498 0.2401 -0.0058 -0.0033 0.0787  324 TYR B CG  
6249  C CD1 . TYR B 324 ? 0.2053 0.2116 0.1976 -0.0096 -0.0056 0.0725  324 TYR B CD1 
6250  C CD2 . TYR B 324 ? 0.2533 0.2651 0.2522 -0.0046 -0.0043 0.0871  324 TYR B CD2 
6251  C CE1 . TYR B 324 ? 0.1887 0.2078 0.1866 -0.0125 -0.0090 0.0745  324 TYR B CE1 
6252  C CE2 . TYR B 324 ? 0.2221 0.2470 0.2264 -0.0073 -0.0075 0.0892  324 TYR B CE2 
6253  C CZ  . TYR B 324 ? 0.2063 0.2347 0.2100 -0.0115 -0.0098 0.0827  324 TYR B CZ  
6254  O OH  . TYR B 324 ? 0.2523 0.2938 0.2613 -0.0149 -0.0131 0.0847  324 TYR B OH  
6255  N N   . LEU B 325 ? 0.2356 0.2330 0.2176 -0.0081 -0.0041 0.0902  325 LEU B N   
6256  C CA  . LEU B 325 ? 0.2407 0.2494 0.2244 -0.0114 -0.0076 0.0958  325 LEU B CA  
6257  C C   . LEU B 325 ? 0.2503 0.2562 0.2266 -0.0157 -0.0089 0.0937  325 LEU B C   
6258  O O   . LEU B 325 ? 0.2266 0.2418 0.2036 -0.0205 -0.0123 0.0934  325 LEU B O   
6259  C CB  . LEU B 325 ? 0.2398 0.2521 0.2271 -0.0083 -0.0073 0.1056  325 LEU B CB  
6260  C CG  . LEU B 325 ? 0.2058 0.2259 0.2025 -0.0048 -0.0068 0.1097  325 LEU B CG  
6261  C CD1 . LEU B 325 ? 0.2309 0.2506 0.2301 -0.0007 -0.0053 0.1186  325 LEU B CD1 
6262  C CD2 . LEU B 325 ? 0.2379 0.2729 0.2398 -0.0084 -0.0106 0.1113  325 LEU B CD2 
6263  N N   . HIS B 326 ? 0.2562 0.2496 0.2255 -0.0143 -0.0060 0.0922  326 HIS B N   
6264  C CA  . HIS B 326 ? 0.2393 0.2295 0.2018 -0.0181 -0.0066 0.0897  326 HIS B CA  
6265  C C   . HIS B 326 ? 0.2785 0.2722 0.2411 -0.0222 -0.0085 0.0817  326 HIS B C   
6266  O O   . HIS B 326 ? 0.2502 0.2510 0.2121 -0.0273 -0.0118 0.0814  326 HIS B O   
6267  C CB  . HIS B 326 ? 0.2500 0.2253 0.2054 -0.0155 -0.0025 0.0882  326 HIS B CB  
6268  C CG  . HIS B 326 ? 0.3049 0.2767 0.2538 -0.0187 -0.0024 0.0862  326 HIS B CG  
6269  N ND1 . HIS B 326 ? 0.3154 0.2922 0.2625 -0.0215 -0.0045 0.0918  326 HIS B ND1 
6270  C CD2 . HIS B 326 ? 0.2937 0.2583 0.2383 -0.0195 -0.0003 0.0794  326 HIS B CD2 
6271  C CE1 . HIS B 326 ? 0.3682 0.3410 0.3102 -0.0241 -0.0039 0.0883  326 HIS B CE1 
6272  N NE2 . HIS B 326 ? 0.3105 0.2763 0.2514 -0.0229 -0.0014 0.0809  326 HIS B NE2 
6273  N N   . TYR B 327 ? 0.2466 0.2359 0.2105 -0.0204 -0.0069 0.0751  327 TYR B N   
6274  C CA  A TYR B 327 ? 0.2440 0.2369 0.2087 -0.0242 -0.0091 0.0674  327 TYR B CA  
6275  C CA  B TYR B 327 ? 0.2411 0.2339 0.2058 -0.0242 -0.0090 0.0674  327 TYR B CA  
6276  C C   . TYR B 327 ? 0.2169 0.2234 0.1875 -0.0282 -0.0136 0.0687  327 TYR B C   
6277  O O   . TYR B 327 ? 0.2325 0.2445 0.2025 -0.0340 -0.0169 0.0653  327 TYR B O   
6278  C CB  A TYR B 327 ? 0.2781 0.2639 0.2433 -0.0209 -0.0063 0.0606  327 TYR B CB  
6279  C CB  B TYR B 327 ? 0.2769 0.2629 0.2423 -0.0208 -0.0063 0.0607  327 TYR B CB  
6280  C CG  A TYR B 327 ? 0.2708 0.2639 0.2410 -0.0233 -0.0092 0.0554  327 TYR B CG  
6281  C CG  B TYR B 327 ? 0.2721 0.2637 0.2404 -0.0244 -0.0094 0.0536  327 TYR B CG  
6282  C CD1 A TYR B 327 ? 0.2677 0.2627 0.2367 -0.0282 -0.0121 0.0484  327 TYR B CD1 
6283  C CD1 B TYR B 327 ? 0.2759 0.2655 0.2411 -0.0282 -0.0109 0.0468  327 TYR B CD1 
6284  C CD2 A TYR B 327 ? 0.2569 0.2549 0.2329 -0.0211 -0.0093 0.0573  327 TYR B CD2 
6285  C CD2 B TYR B 327 ? 0.2644 0.2636 0.2389 -0.0245 -0.0112 0.0536  327 TYR B CD2 
6286  C CE1 A TYR B 327 ? 0.2644 0.2651 0.2374 -0.0308 -0.0151 0.0434  327 TYR B CE1 
6287  C CE1 B TYR B 327 ? 0.2705 0.2642 0.2375 -0.0322 -0.0144 0.0398  327 TYR B CE1 
6288  C CE2 A TYR B 327 ? 0.2477 0.2522 0.2282 -0.0233 -0.0119 0.0526  327 TYR B CE2 
6289  C CE2 B TYR B 327 ? 0.2542 0.2578 0.2309 -0.0282 -0.0142 0.0470  327 TYR B CE2 
6290  C CZ  A TYR B 327 ? 0.2474 0.2529 0.2261 -0.0282 -0.0147 0.0456  327 TYR B CZ  
6291  C CZ  B TYR B 327 ? 0.2669 0.2673 0.2396 -0.0321 -0.0159 0.0400  327 TYR B CZ  
6292  O OH  A TYR B 327 ? 0.2090 0.2199 0.1918 -0.0308 -0.0174 0.0408  327 TYR B OH  
6293  O OH  B TYR B 327 ? 0.2760 0.2796 0.2503 -0.0363 -0.0193 0.0329  327 TYR B OH  
6294  N N   . ARG B 328 ? 0.2559 0.2683 0.2323 -0.0257 -0.0136 0.0734  328 ARG B N   
6295  C CA  . ARG B 328 ? 0.2073 0.2330 0.1897 -0.0294 -0.0174 0.0746  328 ARG B CA  
6296  C C   . ARG B 328 ? 0.2231 0.2574 0.2044 -0.0346 -0.0207 0.0791  328 ARG B C   
6297  O O   . ARG B 328 ? 0.2286 0.2701 0.2107 -0.0406 -0.0239 0.0759  328 ARG B O   
6298  C CB  . ARG B 328 ? 0.2442 0.2749 0.2334 -0.0252 -0.0165 0.0798  328 ARG B CB  
6299  C CG  . ARG B 328 ? 0.2027 0.2469 0.1989 -0.0284 -0.0195 0.0801  328 ARG B CG  
6300  C CD  . ARG B 328 ? 0.1708 0.2270 0.1684 -0.0332 -0.0229 0.0862  328 ARG B CD  
6301  N NE  . ARG B 328 ? 0.2116 0.2806 0.2167 -0.0343 -0.0246 0.0897  328 ARG B NE  
6302  C CZ  . ARG B 328 ? 0.1712 0.2475 0.1795 -0.0389 -0.0268 0.0855  328 ARG B CZ  
6303  N NH1 . ARG B 328 ? 0.1542 0.2260 0.1594 -0.0426 -0.0277 0.0771  328 ARG B NH1 
6304  N NH2 . ARG B 328 ? 0.1721 0.2606 0.1869 -0.0402 -0.0281 0.0898  328 ARG B NH2 
6305  N N   . ILE B 329 ? 0.2090 0.2429 0.1887 -0.0326 -0.0198 0.0867  329 ILE B N   
6306  C CA  . ILE B 329 ? 0.1778 0.2202 0.1563 -0.0373 -0.0228 0.0916  329 ILE B CA  
6307  C C   . ILE B 329 ? 0.2207 0.2589 0.1928 -0.0420 -0.0238 0.0866  329 ILE B C   
6308  O O   . ILE B 329 ? 0.1857 0.2322 0.1574 -0.0483 -0.0271 0.0867  329 ILE B O   
6309  C CB  . ILE B 329 ? 0.2142 0.2562 0.1925 -0.0334 -0.0215 0.1010  329 ILE B CB  
6310  C CG1 . ILE B 329 ? 0.2140 0.2629 0.2001 -0.0296 -0.0213 0.1062  329 ILE B CG1 
6311  C CG2 . ILE B 329 ? 0.2540 0.3026 0.2295 -0.0380 -0.0242 0.1059  329 ILE B CG2 
6312  C CD1 . ILE B 329 ? 0.2768 0.3240 0.2636 -0.0249 -0.0196 0.1150  329 ILE B CD1 
6313  N N   . GLY B 330 ? 0.2194 0.2449 0.1866 -0.0395 -0.0208 0.0818  330 GLY B N   
6314  C CA  . GLY B 330 ? 0.2081 0.2296 0.1697 -0.0439 -0.0216 0.0766  330 GLY B CA  
6315  C C   . GLY B 330 ? 0.2192 0.2452 0.1825 -0.0495 -0.0246 0.0687  330 GLY B C   
6316  O O   . GLY B 330 ? 0.2348 0.2634 0.1953 -0.0557 -0.0272 0.0660  330 GLY B O   
6317  N N   . GLN B 331 ? 0.1959 0.2225 0.1637 -0.0477 -0.0244 0.0648  331 GLN B N   
6318  C CA  . GLN B 331 ? 0.1677 0.1991 0.1377 -0.0534 -0.0275 0.0579  331 GLN B CA  
6319  C C   . GLN B 331 ? 0.1880 0.2322 0.1607 -0.0597 -0.0311 0.0613  331 GLN B C   
6320  O O   . GLN B 331 ? 0.2006 0.2476 0.1719 -0.0666 -0.0336 0.0569  331 GLN B O   
6321  C CB  . GLN B 331 ? 0.1957 0.2261 0.1703 -0.0501 -0.0266 0.0541  331 GLN B CB  
6322  C CG  . GLN B 331 ? 0.2165 0.2516 0.1936 -0.0561 -0.0297 0.0471  331 GLN B CG  
6323  C CD  . GLN B 331 ? 0.2263 0.2598 0.2076 -0.0529 -0.0289 0.0430  331 GLN B CD  
6324  O OE1 . GLN B 331 ? 0.2206 0.2598 0.2072 -0.0499 -0.0282 0.0475  331 GLN B OE1 
6325  N NE2 . GLN B 331 ? 0.2144 0.2383 0.1923 -0.0513 -0.0274 0.0340  331 GLN B NE2 
6326  N N   . VAL B 332 ? 0.1896 0.2420 0.1665 -0.0577 -0.0312 0.0692  332 VAL B N   
6327  C CA  . VAL B 332 ? 0.1698 0.2352 0.1492 -0.0637 -0.0343 0.0733  332 VAL B CA  
6328  C C   . VAL B 332 ? 0.1887 0.2541 0.1623 -0.0683 -0.0357 0.0746  332 VAL B C   
6329  O O   . VAL B 332 ? 0.2069 0.2793 0.1804 -0.0757 -0.0384 0.0727  332 VAL B O   
6330  C CB  . VAL B 332 ? 0.1386 0.2122 0.1230 -0.0600 -0.0341 0.0822  332 VAL B CB  
6331  C CG1 . VAL B 332 ? 0.1426 0.2299 0.1288 -0.0662 -0.0372 0.0873  332 VAL B CG1 
6332  C CG2 . VAL B 332 ? 0.1444 0.2194 0.1350 -0.0564 -0.0330 0.0807  332 VAL B CG2 
6333  N N   . LYS B 333 ? 0.2089 0.2664 0.1778 -0.0642 -0.0336 0.0778  333 LYS B N   
6334  C CA  . LYS B 333 ? 0.1873 0.2441 0.1505 -0.0682 -0.0345 0.0792  333 LYS B CA  
6335  C C   . LYS B 333 ? 0.1962 0.2486 0.1558 -0.0738 -0.0357 0.0702  333 LYS B C   
6336  O O   . LYS B 333 ? 0.2542 0.3109 0.2112 -0.0803 -0.0379 0.0697  333 LYS B O   
6337  C CB  . LYS B 333 ? 0.2115 0.2590 0.1703 -0.0623 -0.0315 0.0837  333 LYS B CB  
6338  C CG  . LYS B 333 ? 0.2288 0.2762 0.1820 -0.0659 -0.0324 0.0863  333 LYS B CG  
6339  C CD  . LYS B 333 ? 0.2268 0.2642 0.1756 -0.0602 -0.0290 0.0907  333 LYS B CD  
6340  C CE  . LYS B 333 ? 0.3160 0.3556 0.2599 -0.0639 -0.0303 0.0951  333 LYS B CE  
6341  N NZ  . LYS B 333 ? 0.2465 0.2842 0.1861 -0.0703 -0.0317 0.0881  333 LYS B NZ  
6342  N N   . TYR B 334 ? 0.2396 0.2836 0.1992 -0.0714 -0.0342 0.0630  334 TYR B N   
6343  C CA  . TYR B 334 ? 0.2459 0.2849 0.2023 -0.0764 -0.0353 0.0541  334 TYR B CA  
6344  C C   . TYR B 334 ? 0.2370 0.2849 0.1965 -0.0843 -0.0384 0.0508  334 TYR B C   
6345  O O   . TYR B 334 ? 0.2454 0.2901 0.2001 -0.0863 -0.0373 0.0473  334 TYR B O   
6346  C CB  . TYR B 334 ? 0.2294 0.2584 0.1857 -0.0720 -0.0333 0.0474  334 TYR B CB  
6347  C CG  . TYR B 334 ? 0.2755 0.2977 0.2288 -0.0742 -0.0329 0.0377  334 TYR B CG  
6348  C CD1 . TYR B 334 ? 0.3060 0.3210 0.2533 -0.0753 -0.0321 0.0348  334 TYR B CD1 
6349  C CD2 . TYR B 334 ? 0.3025 0.3218 0.2587 -0.0685 -0.0292 0.0314  334 TYR B CD2 
6350  C CE1 . TYR B 334 ? 0.2824 0.2893 0.2284 -0.0702 -0.0277 0.0266  334 TYR B CE1 
6351  C CE2 . TYR B 334 ? 0.2856 0.2969 0.2409 -0.0634 -0.0251 0.0235  334 TYR B CE2 
6352  C CZ  . TYR B 334 ? 0.3087 0.3146 0.2597 -0.0640 -0.0243 0.0214  334 TYR B CZ  
6353  O OH  . TYR B 334 ? 0.3036 0.3042 0.2566 -0.0583 -0.0205 0.0149  334 TYR B OH  
6354  N N   . LEU B 335 ? 0.1998 0.2524 0.1644 -0.0818 -0.0376 0.0512  335 LEU B N   
6355  C CA  . LEU B 335 ? 0.1801 0.2348 0.1445 -0.0819 -0.0359 0.0480  335 LEU B CA  
6356  C C   . LEU B 335 ? 0.2196 0.2843 0.1828 -0.0889 -0.0386 0.0536  335 LEU B C   
6357  O O   . LEU B 335 ? 0.2446 0.3072 0.2044 -0.0904 -0.0371 0.0496  335 LEU B O   
6358  C CB  . LEU B 335 ? 0.2031 0.2627 0.1733 -0.0790 -0.0353 0.0490  335 LEU B CB  
6359  C CG  . LEU B 335 ? 0.2205 0.2831 0.1910 -0.0796 -0.0338 0.0466  335 LEU B CG  
6360  C CD1 . LEU B 335 ? 0.1991 0.2504 0.1664 -0.0761 -0.0300 0.0374  335 LEU B CD1 
6361  C CD2 . LEU B 335 ? 0.1775 0.2442 0.1534 -0.0765 -0.0333 0.0477  335 LEU B CD2 
6362  N N   . GLY B 336 ? 0.2235 0.2999 0.1905 -0.0929 -0.0426 0.0634  336 GLY B N   
6363  C CA  . GLY B 336 ? 0.1871 0.2728 0.1526 -0.0984 -0.0447 0.0692  336 GLY B CA  
6364  C C   . GLY B 336 ? 0.2512 0.3312 0.2100 -0.1022 -0.0451 0.0665  336 GLY B C   
6365  O O   . GLY B 336 ? 0.2579 0.3409 0.2136 -0.1067 -0.0453 0.0658  336 GLY B O   
6366  N N   . ASP B 337 ? 0.2525 0.3207 0.2070 -0.0974 -0.0430 0.0644  337 ASP B N   
6367  C CA  . ASP B 337 ? 0.2523 0.3143 0.2002 -0.1007 -0.0431 0.0616  337 ASP B CA  
6368  C C   . ASP B 337 ? 0.2853 0.3402 0.2303 -0.1012 -0.0407 0.0520  337 ASP B C   
6369  O O   . ASP B 337 ? 0.2753 0.3297 0.2160 -0.1047 -0.0405 0.0507  337 ASP B O   
6370  C CB  . ASP B 337 ? 0.2284 0.2782 0.1723 -0.0937 -0.0402 0.0613  337 ASP B CB  
6371  C CG  . ASP B 337 ? 0.2635 0.3138 0.2064 -0.0880 -0.0387 0.0708  337 ASP B CG  
6372  O OD1 . ASP B 337 ? 0.3053 0.3652 0.2492 -0.0904 -0.0404 0.0774  337 ASP B OD1 
6373  O OD2 . ASP B 337 ? 0.2832 0.3243 0.2243 -0.0813 -0.0357 0.0718  337 ASP B OD2 
6374  N N   . ARG B 338 ? 0.2807 0.3281 0.2277 -0.0944 -0.0371 0.0454  338 ARG B N   
6375  C CA  . ARG B 338 ? 0.2729 0.3128 0.2188 -0.0906 -0.0330 0.0373  338 ARG B CA  
6376  C C   . ARG B 338 ? 0.2727 0.3201 0.2188 -0.0947 -0.0334 0.0386  338 ARG B C   
6377  O O   . ARG B 338 ? 0.2835 0.3276 0.2272 -0.0952 -0.0316 0.0347  338 ARG B O   
6378  C CB  . ARG B 338 ? 0.2650 0.2983 0.2151 -0.0826 -0.0296 0.0315  338 ARG B CB  
6379  C CG  . ARG B 338 ? 0.2858 0.3096 0.2354 -0.0772 -0.0279 0.0279  338 ARG B CG  
6380  C CD  . ARG B 338 ? 0.2770 0.2919 0.2253 -0.0730 -0.0245 0.0213  338 ARG B CD  
6381  N NE  . ARG B 338 ? 0.3142 0.3281 0.2660 -0.0736 -0.0191 0.0210  338 ARG B NE  
6382  C CZ  . ARG B 338 ? 0.3043 0.3170 0.2558 -0.0720 -0.0173 0.0188  338 ARG B CZ  
6383  N NH1 . ARG B 338 ? 0.3428 0.3529 0.2963 -0.0676 -0.0162 0.0175  338 ARG B NH1 
6384  N NH2 . ARG B 338 ? 0.3456 0.3598 0.2947 -0.0749 -0.0164 0.0181  338 ARG B NH2 
6385  N N   . LEU B 339 ? 0.2521 0.3101 0.2014 -0.0976 -0.0358 0.0444  339 LEU B N   
6386  C CA  . LEU B 339 ? 0.3113 0.3771 0.2605 -0.1019 -0.0364 0.0460  339 LEU B CA  
6387  C C   . LEU B 339 ? 0.2947 0.3670 0.2399 -0.1093 -0.0392 0.0508  339 LEU B C   
6388  O O   . LEU B 339 ? 0.2753 0.3483 0.2177 -0.1123 -0.0384 0.0489  339 LEU B O   
6389  C CB  . LEU B 339 ? 0.2895 0.3652 0.2437 -0.1023 -0.0379 0.0509  339 LEU B CB  
6390  C CG  . LEU B 339 ? 0.2672 0.3375 0.2252 -0.0955 -0.0350 0.0461  339 LEU B CG  
6391  C CD1 . LEU B 339 ? 0.2277 0.3091 0.1906 -0.0966 -0.0369 0.0519  339 LEU B CD1 
6392  C CD2 . LEU B 339 ? 0.2309 0.2940 0.1881 -0.0926 -0.0313 0.0385  339 LEU B CD2 
6393  N N   . ARG B 340 ? 0.2595 0.3370 0.2048 -0.1125 -0.0427 0.0576  340 ARG B N   
6394  C CA  . ARG B 340 ? 0.3034 0.3874 0.2452 -0.1196 -0.0456 0.0627  340 ARG B CA  
6395  C C   . ARG B 340 ? 0.3349 0.4085 0.2704 -0.1198 -0.0434 0.0564  340 ARG B C   
6396  O O   . ARG B 340 ? 0.3220 0.3986 0.2539 -0.1248 -0.0439 0.0569  340 ARG B O   
6397  C CB  . ARG B 340 ? 0.2943 0.3857 0.2389 -0.1220 -0.0497 0.0716  340 ARG B CB  
6398  C CG  . ARG B 340 ? 0.3599 0.4615 0.3098 -0.1192 -0.0505 0.0795  340 ARG B CG  
6399  C CD  . ARG B 340 ? 0.3530 0.4513 0.3011 -0.1115 -0.0492 0.0871  340 ARG B CD  
6400  N NE  . ARG B 340 ? 0.3996 0.4954 0.3412 -0.1136 -0.0495 0.0895  340 ARG B NE  
6401  C CZ  . ARG B 340 ? 0.4313 0.5362 0.3714 -0.1180 -0.0515 0.0953  340 ARG B CZ  
6402  N NH1 . ARG B 340 ? 0.4715 0.5891 0.4162 -0.1212 -0.0535 0.0993  340 ARG B NH1 
6403  N NH2 . ARG B 340 ? 0.4611 0.5626 0.3951 -0.1194 -0.0516 0.0973  340 ARG B NH2 
6404  N N   . GLU B 341 ? 0.3253 0.3868 0.2597 -0.1143 -0.0408 0.0506  341 GLU B N   
6405  C CA  . GLU B 341 ? 0.3394 0.3913 0.2688 -0.1136 -0.0384 0.0448  341 GLU B CA  
6406  C C   . GLU B 341 ? 0.3949 0.4450 0.3243 -0.1125 -0.0353 0.0394  341 GLU B C   
6407  O O   . GLU B 341 ? 0.4048 0.4515 0.3305 -0.1143 -0.0342 0.0368  341 GLU B O   
6408  C CB  . GLU B 341 ? 0.3098 0.3501 0.2392 -0.1070 -0.0358 0.0397  341 GLU B CB  
6409  C CG  . GLU B 341 ? 0.3880 0.4284 0.3158 -0.1091 -0.0388 0.0446  341 GLU B CG  
6410  C CD  . GLU B 341 ? 0.4591 0.4891 0.3874 -0.1023 -0.0365 0.0400  341 GLU B CD  
6411  O OE1 . GLU B 341 ? 0.4922 0.5140 0.4213 -0.0962 -0.0322 0.0325  341 GLU B OE1 
6412  O OE2 . GLU B 341 ? 0.3945 0.4255 0.3234 -0.1030 -0.0389 0.0445  341 GLU B OE2 
6413  N N   . ALA B 342 ? 0.3416 0.3687 0.2013 -0.0081 0.0766  0.0355  342 ALA B N   
6414  C CA  . ALA B 342 ? 0.3756 0.4050 0.2230 -0.0126 0.0797  0.0316  342 ALA B CA  
6415  C C   . ALA B 342 ? 0.4233 0.4445 0.2519 -0.0218 0.0787  0.0285  342 ALA B C   
6416  O O   . ALA B 342 ? 0.4067 0.4195 0.2224 -0.0285 0.0807  0.0227  342 ALA B O   
6417  C CB  . ALA B 342 ? 0.3990 0.4272 0.2514 -0.0140 0.0792  0.0281  342 ALA B CB  
6418  N N   . GLY B 343 ? 0.3867 0.4092 0.2131 -0.0241 0.0752  0.0316  343 GLY B N   
6419  C CA  . GLY B 343 ? 0.3701 0.3909 0.1805 -0.0342 0.0721  0.0295  343 GLY B CA  
6420  C C   . GLY B 343 ? 0.4042 0.4269 0.2121 -0.0447 0.0657  0.0271  343 GLY B C   
6421  O O   . GLY B 343 ? 0.4460 0.4677 0.2392 -0.0548 0.0629  0.0247  343 GLY B O   
6422  N N   . ILE B 344 ? 0.3844 0.4105 0.2058 -0.0430 0.0631  0.0280  344 ILE B N   
6423  C CA  . ILE B 344 ? 0.3579 0.3887 0.1793 -0.0525 0.0568  0.0269  344 ILE B CA  
6424  C C   . ILE B 344 ? 0.3795 0.4245 0.2071 -0.0565 0.0491  0.0323  344 ILE B C   
6425  O O   . ILE B 344 ? 0.3993 0.4498 0.2406 -0.0497 0.0480  0.0366  344 ILE B O   
6426  C CB  . ILE B 344 ? 0.4370 0.4666 0.2707 -0.0482 0.0575  0.0263  344 ILE B CB  
6427  C CG1 . ILE B 344 ? 0.4531 0.4715 0.2828 -0.0436 0.0650  0.0218  344 ILE B CG1 
6428  C CG2 . ILE B 344 ? 0.3450 0.3804 0.1785 -0.0582 0.0514  0.0258  344 ILE B CG2 
6429  C CD1 . ILE B 344 ? 0.4680 0.4756 0.2790 -0.0541 0.0669  0.0153  344 ILE B CD1 
6430  N N   . PRO B 345 ? 0.3908 0.4430 0.2092 -0.0680 0.0434  0.0324  345 PRO B N   
6431  C CA  . PRO B 345 ? 0.3986 0.4685 0.2248 -0.0713 0.0357  0.0390  345 PRO B CA  
6432  C C   . PRO B 345 ? 0.3649 0.4469 0.2085 -0.0705 0.0306  0.0430  345 PRO B C   
6433  O O   . PRO B 345 ? 0.3585 0.4400 0.2020 -0.0754 0.0291  0.0408  345 PRO B O   
6434  C CB  . PRO B 345 ? 0.4284 0.5027 0.2386 -0.0848 0.0314  0.0378  345 PRO B CB  
6435  C CG  . PRO B 345 ? 0.4665 0.5216 0.2581 -0.0877 0.0379  0.0298  345 PRO B CG  
6436  C CD  . PRO B 345 ? 0.4529 0.4972 0.2524 -0.0791 0.0438  0.0267  345 PRO B CD  
6437  N N   . ILE B 346 ? 0.2951 0.3878 0.1531 -0.0642 0.0280  0.0490  346 ILE B N   
6438  C CA  . ILE B 346 ? 0.3499 0.4547 0.2251 -0.0615 0.0235  0.0537  346 ILE B CA  
6439  C C   . ILE B 346 ? 0.3516 0.4755 0.2367 -0.0610 0.0179  0.0621  346 ILE B C   
6440  O O   . ILE B 346 ? 0.2967 0.4220 0.1770 -0.0605 0.0185  0.0640  346 ILE B O   
6441  C CB  . ILE B 346 ? 0.3373 0.4324 0.2233 -0.0508 0.0279  0.0521  346 ILE B CB  
6442  C CG1 . ILE B 346 ? 0.2905 0.3837 0.1814 -0.0434 0.0301  0.0543  346 ILE B CG1 
6443  C CG2 . ILE B 346 ? 0.2864 0.3634 0.1640 -0.0493 0.0346  0.0449  346 ILE B CG2 
6444  C CD1 . ILE B 346 ? 0.2695 0.3568 0.1724 -0.0348 0.0324  0.0537  346 ILE B CD1 
6445  N N   . GLN B 347 ? 0.3176 0.4567 0.2171 -0.0602 0.0130  0.0677  347 GLN B N   
6446  C CA  . GLN B 347 ? 0.3079 0.4654 0.2201 -0.0567 0.0090  0.0767  347 GLN B CA  
6447  C C   . GLN B 347 ? 0.3150 0.4638 0.2335 -0.0457 0.0134  0.0770  347 GLN B C   
6448  O O   . GLN B 347 ? 0.2746 0.4153 0.2006 -0.0389 0.0158  0.0749  347 GLN B O   
6449  C CB  . GLN B 347 ? 0.2870 0.4625 0.2143 -0.0566 0.0040  0.0832  347 GLN B CB  
6450  C CG  . GLN B 347 ? 0.3027 0.4975 0.2453 -0.0504 0.0014  0.0936  347 GLN B CG  
6451  C CD  . GLN B 347 ? 0.3958 0.6078 0.3349 -0.0573 -0.0025 0.0997  347 GLN B CD  
6452  O OE1 . GLN B 347 ? 0.3706 0.5772 0.3015 -0.0566 -0.0005 0.0990  347 GLN B OE1 
6453  N NE2 . GLN B 347 ? 0.3801 0.6139 0.3260 -0.0640 -0.0082 0.1064  347 GLN B NE2 
6454  N N   . TYR B 348 ? 0.2387 0.3891 0.1536 -0.0445 0.0143  0.0796  348 TYR B N   
6455  C CA  . TYR B 348 ? 0.2665 0.4070 0.1843 -0.0363 0.0187  0.0793  348 TYR B CA  
6456  C C   . TYR B 348 ? 0.2874 0.4420 0.2159 -0.0313 0.0167  0.0882  348 TYR B C   
6457  O O   . TYR B 348 ? 0.3282 0.4962 0.2545 -0.0352 0.0138  0.0935  348 TYR B O   
6458  C CB  . TYR B 348 ? 0.2849 0.4118 0.1876 -0.0385 0.0231  0.0743  348 TYR B CB  
6459  C CG  . TYR B 348 ? 0.3590 0.4756 0.2638 -0.0317 0.0278  0.0737  348 TYR B CG  
6460  C CD1 . TYR B 348 ? 0.3776 0.4828 0.2878 -0.0267 0.0310  0.0698  348 TYR B CD1 
6461  C CD2 . TYR B 348 ? 0.3851 0.5037 0.2859 -0.0311 0.0289  0.0772  348 TYR B CD2 
6462  C CE1 . TYR B 348 ? 0.3736 0.4708 0.2857 -0.0222 0.0346  0.0694  348 TYR B CE1 
6463  C CE2 . TYR B 348 ? 0.3645 0.4742 0.2671 -0.0260 0.0331  0.0769  348 TYR B CE2 
6464  C CZ  . TYR B 348 ? 0.3817 0.4810 0.2900 -0.0221 0.0357  0.0729  348 TYR B CZ  
6465  O OH  . TYR B 348 ? 0.4845 0.5764 0.3947 -0.0186 0.0393  0.0728  348 TYR B OH  
6466  N N   . PRO B 349 ? 0.2712 0.4234 0.2109 -0.0227 0.0184  0.0905  349 PRO B N   
6467  C CA  . PRO B 349 ? 0.2346 0.3733 0.1784 -0.0178 0.0212  0.0854  349 PRO B CA  
6468  C C   . PRO B 349 ? 0.2437 0.3867 0.1941 -0.0182 0.0188  0.0846  349 PRO B C   
6469  O O   . PRO B 349 ? 0.2361 0.3954 0.1921 -0.0205 0.0147  0.0901  349 PRO B O   
6470  C CB  . PRO B 349 ? 0.2184 0.3572 0.1713 -0.0094 0.0231  0.0903  349 PRO B CB  
6471  C CG  . PRO B 349 ? 0.1975 0.3554 0.1576 -0.0083 0.0200  0.0996  349 PRO B CG  
6472  C CD  . PRO B 349 ? 0.2521 0.4171 0.2020 -0.0169 0.0176  0.0996  349 PRO B CD  
6473  N N   . THR B 350 ? 0.2521 0.3819 0.2024 -0.0160 0.0212  0.0783  350 THR B N   
6474  C CA  . THR B 350 ? 0.2003 0.3329 0.1576 -0.0149 0.0195  0.0778  350 THR B CA  
6475  C C   . THR B 350 ? 0.2246 0.3683 0.1964 -0.0074 0.0180  0.0851  350 THR B C   
6476  O O   . THR B 350 ? 0.2392 0.3801 0.2149 -0.0010 0.0202  0.0877  350 THR B O   
6477  C CB  . THR B 350 ? 0.2178 0.3340 0.1728 -0.0128 0.0230  0.0702  350 THR B CB  
6478  O OG1 . THR B 350 ? 0.2314 0.3400 0.1901 -0.0065 0.0256  0.0699  350 THR B OG1 
6479  C CG2 . THR B 350 ? 0.2347 0.3393 0.1755 -0.0191 0.0261  0.0635  350 THR B CG2 
6480  N N   . GLY B 351 ? 0.1735 0.3295 0.1529 -0.0079 0.0149  0.0888  351 GLY B N   
6481  C CA  . GLY B 351 ? 0.1941 0.3614 0.1881 0.0002  0.0146  0.0962  351 GLY B CA  
6482  C C   . GLY B 351 ? 0.1937 0.3498 0.1931 0.0078  0.0172  0.0928  351 GLY B C   
6483  O O   . GLY B 351 ? 0.1957 0.3355 0.1886 0.0078  0.0195  0.0855  351 GLY B O   
6484  N N   . GLY B 352 ? 0.1404 0.3068 0.1525 0.0144  0.0172  0.0985  352 GLY B N   
6485  C CA  . GLY B 352 ? 0.1382 0.2946 0.1558 0.0229  0.0203  0.0961  352 GLY B CA  
6486  C C   . GLY B 352 ? 0.1945 0.3444 0.2107 0.0208  0.0192  0.0902  352 GLY B C   
6487  O O   . GLY B 352 ? 0.2017 0.3382 0.2172 0.0252  0.0216  0.0851  352 GLY B O   
6488  N N   . HIS B 353 ? 0.1349 0.2939 0.1500 0.0135  0.0157  0.0908  353 HIS B N   
6489  C CA  . HIS B 353 ? 0.1279 0.2841 0.1450 0.0135  0.0152  0.0878  353 HIS B CA  
6490  C C   . HIS B 353 ? 0.1454 0.2942 0.1498 0.0031  0.0141  0.0814  353 HIS B C   
6491  O O   . HIS B 353 ? 0.1279 0.2714 0.1321 0.0030  0.0145  0.0782  353 HIS B O   
6492  C CB  . HIS B 353 ? 0.1620 0.3371 0.1931 0.0166  0.0133  0.0960  353 HIS B CB  
6493  C CG  . HIS B 353 ? 0.1294 0.3219 0.1600 0.0070  0.0088  0.1012  353 HIS B CG  
6494  N ND1 . HIS B 353 ? 0.1690 0.3706 0.1971 0.0029  0.0073  0.1051  353 HIS B ND1 
6495  C CD2 . HIS B 353 ? 0.2142 0.4175 0.2465 0.0002  0.0051  0.1035  353 HIS B CD2 
6496  C CE1 . HIS B 353 ? 0.2027 0.4209 0.2313 -0.0063 0.0027  0.1096  353 HIS B CE1 
6497  N NE2 . HIS B 353 ? 0.1582 0.3777 0.1893 -0.0086 0.0012  0.1087  353 HIS B NE2 
6498  N N   . ALA B 354 ? 0.1540 0.3009 0.1471 -0.0050 0.0137  0.0792  354 ALA B N   
6499  C CA  . ALA B 354 ? 0.2029 0.3432 0.1829 -0.0152 0.0138  0.0738  354 ALA B CA  
6500  C C   . ALA B 354 ? 0.2091 0.3435 0.1767 -0.0209 0.0152  0.0707  354 ALA B C   
6501  O O   . ALA B 354 ? 0.2386 0.3810 0.2087 -0.0196 0.0138  0.0752  354 ALA B O   
6502  C CB  . ALA B 354 ? 0.2127 0.3691 0.1954 -0.0224 0.0093  0.0787  354 ALA B CB  
6503  N N   . VAL B 355 ? 0.2215 0.3416 0.1755 -0.0264 0.0186  0.0634  355 VAL B N   
6504  C CA  . VAL B 355 ? 0.2224 0.3370 0.1629 -0.0326 0.0203  0.0605  355 VAL B CA  
6505  C C   . VAL B 355 ? 0.2149 0.3367 0.1471 -0.0437 0.0172  0.0610  355 VAL B C   
6506  O O   . VAL B 355 ? 0.2047 0.3233 0.1346 -0.0473 0.0176  0.0586  355 VAL B O   
6507  C CB  . VAL B 355 ? 0.1899 0.2837 0.1207 -0.0305 0.0272  0.0527  355 VAL B CB  
6508  C CG1 . VAL B 355 ? 0.2550 0.3433 0.1716 -0.0358 0.0295  0.0502  355 VAL B CG1 
6509  C CG2 . VAL B 355 ? 0.1887 0.2776 0.1282 -0.0216 0.0291  0.0525  355 VAL B CG2 
6510  N N   . PHE B 356 ? 0.1982 0.3304 0.1261 -0.0496 0.0138  0.0643  356 PHE B N   
6511  C CA  . PHE B 356 ? 0.2516 0.3930 0.1712 -0.0620 0.0096  0.0652  356 PHE B CA  
6512  C C   . PHE B 356 ? 0.3170 0.4449 0.2176 -0.0681 0.0131  0.0588  356 PHE B C   
6513  O O   . PHE B 356 ? 0.2681 0.3962 0.1654 -0.0664 0.0138  0.0598  356 PHE B O   
6514  C CB  . PHE B 356 ? 0.2877 0.4543 0.2173 -0.0648 0.0027  0.0749  356 PHE B CB  
6515  C CG  . PHE B 356 ? 0.2603 0.4431 0.2083 -0.0600 -0.0009 0.0824  356 PHE B CG  
6516  C CD1 . PHE B 356 ? 0.2681 0.4509 0.2297 -0.0471 0.0012  0.0855  356 PHE B CD1 
6517  C CD2 . PHE B 356 ? 0.2467 0.4450 0.1982 -0.0686 -0.0061 0.0866  356 PHE B CD2 
6518  C CE1 . PHE B 356 ? 0.2807 0.4779 0.2589 -0.0414 -0.0011 0.0925  356 PHE B CE1 
6519  C CE2 . PHE B 356 ? 0.2723 0.4869 0.2418 -0.0632 -0.0089 0.0944  356 PHE B CE2 
6520  C CZ  . PHE B 356 ? 0.2564 0.4702 0.2394 -0.0489 -0.0060 0.0973  356 PHE B CZ  
6521  N N   . VAL B 357 ? 0.2771 0.3933 0.1652 -0.0750 0.0156  0.0525  357 VAL B N   
6522  C CA  . VAL B 357 ? 0.3401 0.4413 0.2093 -0.0799 0.0200  0.0458  357 VAL B CA  
6523  C C   . VAL B 357 ? 0.4027 0.5136 0.2605 -0.0947 0.0143  0.0467  357 VAL B C   
6524  O O   . VAL B 357 ? 0.3634 0.4846 0.2208 -0.1063 0.0093  0.0479  357 VAL B O   
6525  C CB  . VAL B 357 ? 0.3601 0.4414 0.2215 -0.0780 0.0272  0.0383  357 VAL B CB  
6526  C CG1 . VAL B 357 ? 0.3711 0.4375 0.2131 -0.0825 0.0321  0.0319  357 VAL B CG1 
6527  C CG2 . VAL B 357 ? 0.2679 0.3415 0.1413 -0.0638 0.0324  0.0382  357 VAL B CG2 
6528  N N   . ASP B 358 ? 0.4122 0.5227 0.2600 -0.0972 0.0144  0.0465  358 ASP B N   
6529  C CA  . ASP B 358 ? 0.5158 0.6376 0.3513 -0.1135 0.0084  0.0475  358 ASP B CA  
6530  C C   . ASP B 358 ? 0.5165 0.6201 0.3298 -0.1252 0.0121  0.0381  358 ASP B C   
6531  O O   . ASP B 358 ? 0.5477 0.6321 0.3481 -0.1205 0.0191  0.0322  358 ASP B O   
6532  C CB  . ASP B 358 ? 0.5794 0.7060 0.4121 -0.1102 0.0077  0.0509  358 ASP B CB  
6533  C CG  . ASP B 358 ? 0.7095 0.8576 0.5371 -0.1260 -0.0007 0.0559  358 ASP B CG  
6534  O OD1 . ASP B 358 ? 0.7572 0.9078 0.5734 -0.1429 -0.0042 0.0531  358 ASP B OD1 
6535  O OD2 . ASP B 358 ? 0.6199 0.7821 0.4545 -0.1220 -0.0035 0.0629  358 ASP B OD2 
6536  N N   . CYS B 359 ? 0.5204 0.6295 0.3291 -0.1408 0.0077  0.0370  359 CYS B N   
6537  C CA  . CYS B 359 ? 0.6443 0.7322 0.4312 -0.1529 0.0121  0.0272  359 CYS B CA  
6538  C C   . CYS B 359 ? 0.6986 0.7849 0.4631 -0.1715 0.0090  0.0242  359 CYS B C   
6539  O O   . CYS B 359 ? 0.7272 0.7905 0.4697 -0.1812 0.0141  0.0152  359 CYS B O   
6540  C CB  . CYS B 359 ? 0.6203 0.7107 0.4108 -0.1618 0.0099  0.0267  359 CYS B CB  
6541  S SG  . CYS B 359 ? 0.5188 0.6047 0.3312 -0.1398 0.0154  0.0282  359 CYS B SG  
6542  N N   . LYS B 360 ? 0.7564 0.8654 0.5254 -0.1764 0.0014  0.0318  360 LYS B N   
6543  C CA  . LYS B 360 ? 0.8331 0.9400 0.5804 -0.1920 -0.0011 0.0293  360 LYS B CA  
6544  C C   . LYS B 360 ? 0.8391 0.9183 0.5682 -0.1838 0.0084  0.0209  360 LYS B C   
6545  O O   . LYS B 360 ? 0.8796 0.9404 0.5835 -0.1968 0.0111  0.0133  360 LYS B O   
6546  C CB  . LYS B 360 ? 0.8390 0.9761 0.5978 -0.1935 -0.0096 0.0401  360 LYS B CB  
6547  C CG  . LYS B 360 ? 0.8389 1.0059 0.6233 -0.1935 -0.0172 0.0509  360 LYS B CG  
6548  C CD  . LYS B 360 ? 0.9835 1.1783 0.7839 -0.1876 -0.0227 0.0624  360 LYS B CD  
6549  C CE  . LYS B 360 ? 0.9664 1.1754 0.7533 -0.2056 -0.0291 0.0654  360 LYS B CE  
6550  N NZ  . LYS B 360 ? 0.9954 1.2354 0.8009 -0.2001 -0.0346 0.0783  360 LYS B NZ  
6551  N N   . LYS B 361 ? 0.7789 0.8540 0.5201 -0.1624 0.0140  0.0226  361 LYS B N   
6552  C CA  . LYS B 361 ? 0.7389 0.7927 0.4671 -0.1522 0.0229  0.0172  361 LYS B CA  
6553  C C   . LYS B 361 ? 0.7650 0.7933 0.4872 -0.1458 0.0327  0.0092  361 LYS B C   
6554  O O   . LYS B 361 ? 0.7593 0.7690 0.4681 -0.1400 0.0406  0.0042  361 LYS B O   
6555  C CB  . LYS B 361 ? 0.6384 0.7011 0.3830 -0.1333 0.0242  0.0239  361 LYS B CB  
6556  C CG  . LYS B 361 ? 0.6814 0.7714 0.4386 -0.1366 0.0149  0.0335  361 LYS B CG  
6557  C CD  . LYS B 361 ? 0.7326 0.8282 0.5069 -0.1184 0.0170  0.0399  361 LYS B CD  
6558  C CE  . LYS B 361 ? 0.7445 0.8300 0.5059 -0.1132 0.0223  0.0383  361 LYS B CE  
6559  N NZ  . LYS B 361 ? 0.7500 0.8419 0.5269 -0.0999 0.0241  0.0445  361 LYS B NZ  
6560  N N   . LEU B 362 ? 0.6758 0.7038 0.4080 -0.1464 0.0327  0.0085  362 LEU B N   
6561  C CA  . LEU B 362 ? 0.7181 0.7233 0.4463 -0.1397 0.0422  0.0017  362 LEU B CA  
6562  C C   . LEU B 362 ? 0.7650 0.7486 0.4669 -0.1578 0.0453  -0.0073 362 LEU B C   
6563  O O   . LEU B 362 ? 0.8102 0.7695 0.4995 -0.1532 0.0550  -0.0139 362 LEU B O   
6564  C CB  . LEU B 362 ? 0.6990 0.7118 0.4486 -0.1316 0.0416  0.0048  362 LEU B CB  
6565  C CG  . LEU B 362 ? 0.6320 0.6530 0.4051 -0.1095 0.0436  0.0109  362 LEU B CG  
6566  C CD1 . LEU B 362 ? 0.4769 0.4995 0.2658 -0.1032 0.0444  0.0121  362 LEU B CD1 
6567  C CD2 . LEU B 362 ? 0.6246 0.6316 0.3928 -0.0977 0.0525  0.0083  362 LEU B CD2 
6568  N N   . VAL B 363 ? 0.7713 0.7633 0.4651 -0.1787 0.0374  -0.0072 363 VAL B N   
6569  C CA  . VAL B 363 ? 0.8056 0.7753 0.4734 -0.1985 0.0402  -0.0156 363 VAL B CA  
6570  C C   . VAL B 363 ? 0.8404 0.8178 0.4908 -0.2189 0.0325  -0.0149 363 VAL B C   
6571  O O   . VAL B 363 ? 0.8550 0.8470 0.5045 -0.2377 0.0239  -0.0120 363 VAL B O   
6572  C CB  . VAL B 363 ? 0.7534 0.7232 0.4272 -0.2067 0.0388  -0.0163 363 VAL B CB  
6573  C CG1 . VAL B 363 ? 0.7346 0.6835 0.4134 -0.1905 0.0500  -0.0209 363 VAL B CG1 
6574  C CG2 . VAL B 363 ? 0.7197 0.7246 0.4202 -0.2046 0.0282  -0.0059 363 VAL B CG2 
6575  N N   . PRO B 364 ? 0.9024 0.8720 0.5389 -0.2158 0.0351  -0.0168 364 PRO B N   
6576  C CA  . PRO B 364 ? 0.8725 0.8503 0.4920 -0.2346 0.0277  -0.0158 364 PRO B CA  
6577  C C   . PRO B 364 ? 0.8883 0.8475 0.4814 -0.2601 0.0276  -0.0226 364 PRO B C   
6578  O O   . PRO B 364 ? 0.8019 0.7775 0.3885 -0.2799 0.0181  -0.0189 364 PRO B O   
6579  C CB  . PRO B 364 ? 0.7430 0.7089 0.3505 -0.2231 0.0336  -0.0181 364 PRO B CB  
6580  C CG  . PRO B 364 ? 0.7421 0.6835 0.3506 -0.2053 0.0463  -0.0234 364 PRO B CG  
6581  C CD  . PRO B 364 ? 0.8457 0.7987 0.4805 -0.1958 0.0454  -0.0196 364 PRO B CD  
6582  N N   . GLN B 365 ? 0.8595 0.7854 0.4379 -0.2602 0.0383  -0.0315 365 GLN B N   
6583  C CA  . GLN B 365 ? 0.9400 0.8421 0.4900 -0.2842 0.0403  -0.0386 365 GLN B CA  
6584  C C   . GLN B 365 ? 1.0163 0.9349 0.5748 -0.3017 0.0324  -0.0346 365 GLN B C   
6585  O O   . GLN B 365 ? 1.0599 0.9599 0.5955 -0.3233 0.0339  -0.0394 365 GLN B O   
6586  C CB  . GLN B 365 ? 1.0087 0.8686 0.5413 -0.2770 0.0557  -0.0484 365 GLN B CB  
6587  C CG  . GLN B 365 ? 1.0022 0.8576 0.5537 -0.2639 0.0616  -0.0486 365 GLN B CG  
6588  C CD  . GLN B 365 ? 0.9139 0.7834 0.4930 -0.2350 0.0641  -0.0439 365 GLN B CD  
6589  O OE1 . GLN B 365 ? 0.9548 0.8329 0.5370 -0.2238 0.0635  -0.0412 365 GLN B OE1 
6590  N NE2 . GLN B 365 ? 0.9098 0.7819 0.5087 -0.2232 0.0671  -0.0425 365 GLN B NE2 
6591  N N   . ILE B 366 ? 1.0007 0.9532 0.5906 -0.2932 0.0245  -0.0253 366 ILE B N   
6592  C CA  . ILE B 366 ? 0.9433 0.9153 0.5449 -0.3073 0.0168  -0.0198 366 ILE B CA  
6593  C C   . ILE B 366 ? 0.9247 0.9400 0.5433 -0.3143 0.0028  -0.0075 366 ILE B C   
6594  O O   . ILE B 366 ? 0.9197 0.9583 0.5622 -0.2961 -0.0008 -0.0003 366 ILE B O   
6595  C CB  . ILE B 366 ? 0.9106 0.8848 0.5356 -0.2899 0.0205  -0.0188 366 ILE B CB  
6596  C CG1 . ILE B 366 ? 0.8680 0.8004 0.4771 -0.2822 0.0353  -0.0300 366 ILE B CG1 
6597  C CG2 . ILE B 366 ? 0.9211 0.9184 0.5592 -0.3038 0.0121  -0.0120 366 ILE B CG2 
6598  C CD1 . ILE B 366 ? 0.8650 0.7971 0.4947 -0.2657 0.0397  -0.0295 366 ILE B CD1 
6599  N N   . PRO B 367 ? 0.9400 0.9671 0.5473 -0.3399 -0.0049 -0.0037 367 PRO B N   
6600  C CA  . PRO B 367 ? 0.9216 0.9922 0.5467 -0.3460 -0.0177 0.0098  367 PRO B CA  
6601  C C   . PRO B 367 ? 0.8956 0.9995 0.5545 -0.3393 -0.0241 0.0210  367 PRO B C   
6602  O O   . PRO B 367 ? 0.9011 0.9950 0.5671 -0.3342 -0.0199 0.0182  367 PRO B O   
6603  C CB  . PRO B 367 ? 0.9549 1.0242 0.5550 -0.3762 -0.0223 0.0101  367 PRO B CB  
6604  C CG  . PRO B 367 ? 0.9961 1.0298 0.5753 -0.3872 -0.0138 0.0002  367 PRO B CG  
6605  C CD  . PRO B 367 ? 0.9883 0.9885 0.5648 -0.3644 -0.0012 -0.0109 367 PRO B CD  
6606  N N   . GLY B 368 ? 0.9075 1.0517 0.5873 -0.3391 -0.0340 0.0346  368 GLY B N   
6607  C CA  . GLY B 368 ? 0.8256 1.0036 0.5393 -0.3305 -0.0398 0.0469  368 GLY B CA  
6608  C C   . GLY B 368 ? 0.9144 1.1000 0.6293 -0.3488 -0.0427 0.0510  368 GLY B C   
6609  O O   . GLY B 368 ? 0.8612 1.0578 0.5982 -0.3388 -0.0433 0.0554  368 GLY B O   
6610  N N   . ASP B 369 ? 0.9911 1.1702 0.6812 -0.3754 -0.0443 0.0502  369 ASP B N   
6611  C CA  . ASP B 369 ? 0.9541 1.1392 0.6419 -0.3940 -0.0460 0.0555  369 ASP B CA  
6612  C C   . ASP B 369 ? 0.9609 1.1090 0.6369 -0.3915 -0.0366 0.0429  369 ASP B C   
6613  O O   . ASP B 369 ? 1.0108 1.1642 0.6937 -0.3922 -0.0380 0.0468  369 ASP B O   
6614  C CB  . ASP B 369 ? 0.9963 1.1814 0.6566 -0.4225 -0.0496 0.0580  369 ASP B CB  
6615  C CG  . ASP B 369 ? 1.0986 1.2392 0.7207 -0.4306 -0.0424 0.0412  369 ASP B CG  
6616  O OD1 . ASP B 369 ? 1.0877 1.1906 0.6887 -0.4356 -0.0335 0.0297  369 ASP B OD1 
6617  O OD2 . ASP B 369 ? 1.1994 1.3421 0.8124 -0.4313 -0.0449 0.0399  369 ASP B OD2 
6618  N N   . GLN B 370 ? 0.9469 1.0555 0.6044 -0.3815 -0.0271 0.0274  370 GLN B N   
6619  C CA  . GLN B 370 ? 0.9826 1.0544 0.6299 -0.3754 -0.0165 0.0152  370 GLN B CA  
6620  C C   . GLN B 370 ? 0.9277 1.0044 0.6025 -0.3461 -0.0143 0.0146  370 GLN B C   
6621  O O   . GLN B 370 ? 0.8840 0.9286 0.5510 -0.3346 -0.0040 0.0037  370 GLN B O   
6622  C CB  . GLN B 370 ? 1.0316 1.0569 0.6441 -0.3784 -0.0054 0.0002  370 GLN B CB  
6623  C CG  . GLN B 370 ? 1.0298 1.0394 0.6086 -0.4073 -0.0051 -0.0020 370 GLN B CG  
6624  C CD  . GLN B 370 ? 1.0752 1.0367 0.6202 -0.4078 0.0069  -0.0169 370 GLN B CD  
6625  O OE1 . GLN B 370 ? 1.1063 1.0489 0.6543 -0.3860 0.0149  -0.0242 370 GLN B OE1 
6626  N NE2 . GLN B 370 ? 1.0970 1.0388 0.6094 -0.4319 0.0086  -0.0205 370 GLN B NE2 
6627  N N   . PHE B 371 ? 0.8555 0.9708 0.5614 -0.3326 -0.0229 0.0267  371 PHE B N   
6628  C CA  . PHE B 371 ? 0.8526 0.9774 0.5859 -0.3049 -0.0222 0.0292  371 PHE B CA  
6629  C C   . PHE B 371 ? 0.8136 0.9070 0.5396 -0.2829 -0.0108 0.0185  371 PHE B C   
6630  O O   . PHE B 371 ? 0.8491 0.9161 0.5696 -0.2744 -0.0018 0.0101  371 PHE B O   
6631  C CB  . PHE B 371 ? 0.8423 0.9693 0.5853 -0.3060 -0.0230 0.0301  371 PHE B CB  
6632  C CG  . PHE B 371 ? 0.8404 0.9891 0.5833 -0.3280 -0.0314 0.0392  371 PHE B CG  
6633  C CD1 . PHE B 371 ? 0.7985 0.9891 0.5666 -0.3231 -0.0417 0.0556  371 PHE B CD1 
6634  C CD2 . PHE B 371 ? 0.9119 1.0349 0.6273 -0.3458 -0.0270 0.0323  371 PHE B CD2 
6635  C CE1 . PHE B 371 ? 0.8228 1.0308 0.5896 -0.3362 -0.0478 0.0654  371 PHE B CE1 
6636  C CE2 . PHE B 371 ? 0.8596 1.0001 0.5721 -0.3600 -0.0336 0.0420  371 PHE B CE2 
6637  C CZ  . PHE B 371 ? 0.8141 0.9979 0.5526 -0.3554 -0.0442 0.0589  371 PHE B CZ  
6638  N N   . PRO B 372 ? 0.8076 0.9038 0.5341 -0.2727 -0.0104 0.0195  372 PRO B N   
6639  C CA  . PRO B 372 ? 0.7991 0.8691 0.5218 -0.2509 0.0004  0.0116  372 PRO B CA  
6640  C C   . PRO B 372 ? 0.6654 0.7393 0.4125 -0.2262 0.0038  0.0145  372 PRO B C   
6641  O O   . PRO B 372 ? 0.6187 0.6665 0.3613 -0.2140 0.0142  0.0068  372 PRO B O   
6642  C CB  . PRO B 372 ? 0.7058 0.7864 0.4279 -0.2463 -0.0024 0.0152  372 PRO B CB  
6643  C CG  . PRO B 372 ? 0.8340 0.9353 0.5490 -0.2705 -0.0123 0.0209  372 PRO B CG  
6644  C CD  . PRO B 372 ? 0.8494 0.9721 0.5791 -0.2807 -0.0190 0.0282  372 PRO B CD  
6645  N N   . ALA B 373 ? 0.5892 0.6951 0.3627 -0.2180 -0.0041 0.0260  373 ALA B N   
6646  C CA  . ALA B 373 ? 0.6354 0.7439 0.4315 -0.1941 -0.0006 0.0294  373 ALA B CA  
6647  C C   . ALA B 373 ? 0.5857 0.6805 0.3812 -0.1939 0.0040  0.0249  373 ALA B C   
6648  O O   . ALA B 373 ? 0.5527 0.6311 0.3543 -0.1754 0.0127  0.0215  373 ALA B O   
6649  C CB  . ALA B 373 ? 0.6071 0.7505 0.4297 -0.1869 -0.0095 0.0428  373 ALA B CB  
6650  N N   . GLN B 374 ? 0.5782 0.6801 0.3668 -0.2146 -0.0017 0.0257  374 GLN B N   
6651  C CA  . GLN B 374 ? 0.5418 0.6296 0.3284 -0.2148 0.0030  0.0214  374 GLN B CA  
6652  C C   . GLN B 374 ? 0.5512 0.5989 0.3157 -0.2136 0.0162  0.0080  374 GLN B C   
6653  O O   . GLN B 374 ? 0.5254 0.5576 0.2950 -0.2000 0.0246  0.0046  374 GLN B O   
6654  C CB  . GLN B 374 ? 0.6526 0.7558 0.4341 -0.2395 -0.0062 0.0250  374 GLN B CB  
6655  C CG  . GLN B 374 ? 0.5060 0.6062 0.2949 -0.2350 -0.0042 0.0254  374 GLN B CG  
6656  C CD  . GLN B 374 ? 0.5201 0.6344 0.3392 -0.2069 -0.0029 0.0339  374 GLN B CD  
6657  O OE1 . GLN B 374 ? 0.5145 0.6597 0.3546 -0.2013 -0.0118 0.0457  374 GLN B OE1 
6658  N NE2 . GLN B 374 ? 0.4495 0.5401 0.2711 -0.1889 0.0090  0.0281  374 GLN B NE2 
6659  N N   . ALA B 375 ? 0.5739 0.6045 0.3151 -0.2260 0.0188  0.0011  375 ALA B N   
6660  C CA  . ALA B 375 ? 0.6412 0.6326 0.3614 -0.2237 0.0321  -0.0108 375 ALA B CA  
6661  C C   . ALA B 375 ? 0.5547 0.5383 0.2893 -0.1949 0.0407  -0.0110 375 ALA B C   
6662  O O   . ALA B 375 ? 0.5699 0.5308 0.3023 -0.1847 0.0512  -0.0166 375 ALA B O   
6663  C CB  . ALA B 375 ? 0.6983 0.6739 0.3912 -0.2412 0.0329  -0.0165 375 ALA B CB  
6664  N N   . VAL B 376 ? 0.5567 0.5596 0.3067 -0.1819 0.0363  -0.0042 376 VAL B N   
6665  C CA  . VAL B 376 ? 0.5472 0.5467 0.3132 -0.1558 0.0430  -0.0027 376 VAL B CA  
6666  C C   . VAL B 376 ? 0.4860 0.4918 0.2729 -0.1421 0.0446  0.0012  376 VAL B C   
6667  O O   . VAL B 376 ? 0.4998 0.4912 0.2920 -0.1268 0.0534  -0.0014 376 VAL B O   
6668  C CB  . VAL B 376 ? 0.4769 0.4955 0.2543 -0.1468 0.0376  0.0042  376 VAL B CB  
6669  C CG1 . VAL B 376 ? 0.5509 0.5664 0.3445 -0.1220 0.0439  0.0064  376 VAL B CG1 
6670  C CG2 . VAL B 376 ? 0.5326 0.5442 0.2888 -0.1592 0.0368  0.0004  376 VAL B CG2 
6671  N N   . ILE B 377 ? 0.4919 0.5205 0.2918 -0.1471 0.0358  0.0084  377 ILE B N   
6672  C CA  . ILE B 377 ? 0.4786 0.5139 0.2984 -0.1340 0.0370  0.0131  377 ILE B CA  
6673  C C   . ILE B 377 ? 0.4448 0.4581 0.2550 -0.1368 0.0453  0.0059  377 ILE B C   
6674  O O   . ILE B 377 ? 0.4302 0.4369 0.2531 -0.1195 0.0520  0.0065  377 ILE B O   
6675  C CB  . ILE B 377 ? 0.4454 0.5095 0.2790 -0.1409 0.0257  0.0226  377 ILE B CB  
6676  C CG1 . ILE B 377 ? 0.3846 0.4691 0.2324 -0.1325 0.0194  0.0306  377 ILE B CG1 
6677  C CG2 . ILE B 377 ? 0.3825 0.4503 0.2332 -0.1300 0.0276  0.0268  377 ILE B CG2 
6678  C CD1 . ILE B 377 ? 0.4051 0.5198 0.2640 -0.1421 0.0077  0.0404  377 ILE B CD1 
6679  N N   . ASN B 378 ? 0.5066 0.5075 0.2939 -0.1591 0.0452  -0.0006 378 ASN B N   
6680  C CA  . ASN B 378 ? 0.4831 0.4599 0.2595 -0.1628 0.0540  -0.0078 378 ASN B CA  
6681  C C   . ASN B 378 ? 0.5136 0.4635 0.2838 -0.1491 0.0665  -0.0147 378 ASN B C   
6682  O O   . ASN B 378 ? 0.5314 0.4701 0.3090 -0.1369 0.0743  -0.0160 378 ASN B O   
6683  C CB  . ASN B 378 ? 0.5466 0.5137 0.2972 -0.1921 0.0510  -0.0135 378 ASN B CB  
6684  C CG  . ASN B 378 ? 0.5769 0.5726 0.3374 -0.2043 0.0390  -0.0052 378 ASN B CG  
6685  O OD1 . ASN B 378 ? 0.5344 0.5561 0.3215 -0.1895 0.0335  0.0051  378 ASN B OD1 
6686  N ND2 . ASN B 378 ? 0.5939 0.5847 0.3332 -0.2311 0.0347  -0.0089 378 ASN B ND2 
6687  N N   . ALA B 379 ? 0.5293 0.4711 0.2880 -0.1498 0.0680  -0.0178 379 ALA B N   
6688  C CA  . ALA B 379 ? 0.5213 0.4420 0.2769 -0.1354 0.0787  -0.0222 379 ALA B CA  
6689  C C   . ALA B 379 ? 0.5210 0.4571 0.3048 -0.1098 0.0794  -0.0152 379 ALA B C   
6690  O O   . ALA B 379 ? 0.5825 0.5075 0.3722 -0.0970 0.0870  -0.0165 379 ALA B O   
6691  C CB  . ALA B 379 ? 0.5342 0.4462 0.2729 -0.1409 0.0794  -0.0254 379 ALA B CB  
6692  N N   . LEU B 380 ? 0.4792 0.4410 0.2805 -0.1027 0.0711  -0.0071 380 LEU B N   
6693  C CA  . LEU B 380 ? 0.4534 0.4291 0.2801 -0.0804 0.0710  -0.0001 380 LEU B CA  
6694  C C   . LEU B 380 ? 0.4858 0.4621 0.3253 -0.0733 0.0735  0.0016  380 LEU B C   
6695  O O   . LEU B 380 ? 0.4109 0.3858 0.2614 -0.0601 0.0776  0.0023  380 LEU B O   
6696  C CB  . LEU B 380 ? 0.4394 0.4373 0.2795 -0.0764 0.0626  0.0079  380 LEU B CB  
6697  C CG  . LEU B 380 ? 0.3955 0.4036 0.2563 -0.0594 0.0628  0.0137  380 LEU B CG  
6698  C CD1 . LEU B 380 ? 0.4086 0.4102 0.2688 -0.0506 0.0680  0.0116  380 LEU B CD1 
6699  C CD2 . LEU B 380 ? 0.3472 0.3720 0.2183 -0.0584 0.0553  0.0206  380 LEU B CD2 
6700  N N   . TYR B 381 ? 0.4442 0.4220 0.2797 -0.0859 0.0709  0.0014  381 TYR B N   
6701  C CA  . TYR B 381 ? 0.4363 0.4142 0.2836 -0.0791 0.0738  0.0034  381 TYR B CA  
6702  C C   . TYR B 381 ? 0.5013 0.4546 0.3377 -0.0787 0.0836  -0.0043 381 TYR B C   
6703  O O   . TYR B 381 ? 0.5192 0.4734 0.3701 -0.0639 0.0868  -0.0023 381 TYR B O   
6704  C CB  . TYR B 381 ? 0.3899 0.3767 0.2359 -0.0933 0.0686  0.0059  381 TYR B CB  
6705  C CG  . TYR B 381 ? 0.4578 0.4408 0.3130 -0.0875 0.0732  0.0069  381 TYR B CG  
6706  C CD1 . TYR B 381 ? 0.3990 0.3963 0.2790 -0.0683 0.0723  0.0151  381 TYR B CD1 
6707  C CD2 . TYR B 381 ? 0.4538 0.4165 0.2916 -0.1012 0.0790  -0.0004 381 TYR B CD2 
6708  C CE1 . TYR B 381 ? 0.4425 0.4381 0.3316 -0.0625 0.0760  0.0168  381 TYR B CE1 
6709  C CE2 . TYR B 381 ? 0.4916 0.4504 0.3384 -0.0951 0.0837  0.0007  381 TYR B CE2 
6710  C CZ  . TYR B 381 ? 0.5028 0.4796 0.3761 -0.0756 0.0818  0.0096  381 TYR B CZ  
6711  O OH  . TYR B 381 ? 0.5574 0.5319 0.4402 -0.0695 0.0857  0.0113  381 TYR B OH  
6712  N N   . LEU B 382 ? 0.5289 0.4593 0.3393 -0.0956 0.0882  -0.0130 382 LEU B N   
6713  C CA  . LEU B 382 ? 0.5311 0.4327 0.3291 -0.0951 0.0992  -0.0202 382 LEU B CA  
6714  C C   . LEU B 382 ? 0.6122 0.5125 0.4208 -0.0764 0.1032  -0.0187 382 LEU B C   
6715  O O   . LEU B 382 ? 0.6421 0.5305 0.4551 -0.0674 0.1099  -0.0198 382 LEU B O   
6716  C CB  . LEU B 382 ? 0.6579 0.5324 0.4235 -0.1170 0.1037  -0.0295 382 LEU B CB  
6717  C CG  . LEU B 382 ? 0.6050 0.4771 0.3550 -0.1408 0.0998  -0.0325 382 LEU B CG  
6718  C CD1 . LEU B 382 ? 0.6912 0.5390 0.4082 -0.1635 0.1021  -0.0410 382 LEU B CD1 
6719  C CD2 . LEU B 382 ? 0.6530 0.5141 0.4056 -0.1399 0.1060  -0.0340 382 LEU B CD2 
6720  N N   . GLU B 383 ? 0.6027 0.5167 0.4163 -0.0709 0.0986  -0.0155 383 GLU B N   
6721  C CA  . GLU B 383 ? 0.5908 0.4990 0.4084 -0.0592 0.1037  -0.0155 383 GLU B CA  
6722  C C   . GLU B 383 ? 0.5314 0.4560 0.3727 -0.0447 0.1011  -0.0098 383 GLU B C   
6723  O O   . GLU B 383 ? 0.5629 0.4797 0.4088 -0.0353 0.1063  -0.0097 383 GLU B O   
6724  C CB  . GLU B 383 ? 0.6111 0.5241 0.4218 -0.0612 0.1011  -0.0153 383 GLU B CB  
6725  C CG  . GLU B 383 ? 0.6911 0.5920 0.4988 -0.0527 0.1084  -0.0164 383 GLU B CG  
6726  C CD  . GLU B 383 ? 0.7619 0.6320 0.5462 -0.0594 0.1183  -0.0230 383 GLU B CD  
6727  O OE1 . GLU B 383 ? 0.6929 0.5479 0.4651 -0.0691 0.1210  -0.0273 383 GLU B OE1 
6728  O OE2 . GLU B 383 ? 0.7856 0.6458 0.5627 -0.0551 0.1238  -0.0236 383 GLU B OE2 
6729  N N   . SER B 384 ? 0.5388 0.4853 0.3947 -0.0430 0.0933  -0.0044 384 SER B N   
6730  C CA  . SER B 384 ? 0.4812 0.4437 0.3576 -0.0306 0.0897  0.0009  384 SER B CA  
6731  C C   . SER B 384 ? 0.4358 0.4114 0.3261 -0.0279 0.0855  0.0051  384 SER B C   
6732  O O   . SER B 384 ? 0.4186 0.4036 0.3238 -0.0188 0.0830  0.0080  384 SER B O   
6733  C CB  . SER B 384 ? 0.4551 0.4349 0.3378 -0.0276 0.0838  0.0052  384 SER B CB  
6734  O OG  . SER B 384 ? 0.4395 0.4327 0.3237 -0.0324 0.0775  0.0096  384 SER B OG  
6735  N N   . GLY B 385 ? 0.4350 0.4115 0.3206 -0.0361 0.0842  0.0058  385 GLY B N   
6736  C CA  . GLY B 385 ? 0.4232 0.4145 0.3231 -0.0328 0.0801  0.0117  385 GLY B CA  
6737  C C   . GLY B 385 ? 0.3906 0.4032 0.3024 -0.0287 0.0727  0.0201  385 GLY B C   
6738  O O   . GLY B 385 ? 0.3661 0.3912 0.2914 -0.0233 0.0698  0.0263  385 GLY B O   
6739  N N   . VAL B 386 ? 0.3543 0.3687 0.2610 -0.0302 0.0707  0.0206  386 VAL B N   
6740  C CA  . VAL B 386 ? 0.3249 0.3496 0.2386 -0.0274 0.0659  0.0273  386 VAL B CA  
6741  C C   . VAL B 386 ? 0.3390 0.3653 0.2457 -0.0408 0.0622  0.0277  386 VAL B C   
6742  O O   . VAL B 386 ? 0.3499 0.3698 0.2414 -0.0534 0.0622  0.0229  386 VAL B O   
6743  C CB  . VAL B 386 ? 0.3322 0.3572 0.2425 -0.0254 0.0649  0.0266  386 VAL B CB  
6744  C CG1 . VAL B 386 ? 0.2819 0.3113 0.1955 -0.0267 0.0601  0.0304  386 VAL B CG1 
6745  C CG2 . VAL B 386 ? 0.3464 0.3773 0.2660 -0.0150 0.0658  0.0266  386 VAL B CG2 
6746  N N   . ARG B 387 ? 0.3288 0.3638 0.2458 -0.0398 0.0581  0.0331  387 ARG B N   
6747  C CA  . ARG B 387 ? 0.2960 0.3423 0.2109 -0.0528 0.0511  0.0357  387 ARG B CA  
6748  C C   . ARG B 387 ? 0.2536 0.3141 0.1729 -0.0540 0.0432  0.0396  387 ARG B C   
6749  O O   . ARG B 387 ? 0.2411 0.3076 0.1728 -0.0450 0.0410  0.0429  387 ARG B O   
6750  C CB  . ARG B 387 ? 0.2466 0.2982 0.1721 -0.0521 0.0505  0.0398  387 ARG B CB  
6751  C CG  . ARG B 387 ? 0.2300 0.3033 0.1588 -0.0644 0.0400  0.0458  387 ARG B CG  
6752  C CD  . ARG B 387 ? 0.2790 0.3586 0.2147 -0.0682 0.0392  0.0496  387 ARG B CD  
6753  N NE  . ARG B 387 ? 0.1961 0.2744 0.1480 -0.0527 0.0413  0.0525  387 ARG B NE  
6754  C CZ  . ARG B 387 ? 0.2634 0.3452 0.2237 -0.0521 0.0418  0.0557  387 ARG B CZ  
6755  N NH1 . ARG B 387 ? 0.2459 0.3330 0.2015 -0.0657 0.0407  0.0574  387 ARG B NH1 
6756  N NH2 . ARG B 387 ? 0.2481 0.3330 0.2212 -0.0403 0.0410  0.0578  387 ARG B NH2 
6757  N N   . ALA B 388 ? 0.2471 0.3139 0.1557 -0.0664 0.0383  0.0390  388 ALA B N   
6758  C CA  . ALA B 388 ? 0.2366 0.3206 0.1493 -0.0693 0.0300  0.0440  388 ALA B CA  
6759  C C   . ALA B 388 ? 0.2885 0.3954 0.2014 -0.0858 0.0202  0.0497  388 ALA B C   
6760  O O   . ALA B 388 ? 0.2695 0.3771 0.1780 -0.0958 0.0197  0.0491  388 ALA B O   
6761  C CB  . ALA B 388 ? 0.2744 0.3511 0.1750 -0.0714 0.0315  0.0397  388 ALA B CB  
6762  N N   . VAL B 389 ? 0.2608 0.3876 0.1793 -0.0889 0.0121  0.0560  389 VAL B N   
6763  C CA  . VAL B 389 ? 0.3156 0.4698 0.2387 -0.1028 0.0016  0.0643  389 VAL B CA  
6764  C C   . VAL B 389 ? 0.2976 0.4628 0.2119 -0.1146 -0.0040 0.0652  389 VAL B C   
6765  O O   . VAL B 389 ? 0.2596 0.4166 0.1720 -0.1065 -0.0007 0.0627  389 VAL B O   
6766  C CB  . VAL B 389 ? 0.2354 0.4092 0.1819 -0.0909 -0.0029 0.0748  389 VAL B CB  
6767  C CG1 . VAL B 389 ? 0.2212 0.3995 0.1770 -0.0790 -0.0034 0.0780  389 VAL B CG1 
6768  C CG2 . VAL B 389 ? 0.2576 0.4604 0.2113 -0.1039 -0.0130 0.0846  389 VAL B CG2 
6769  N N   . GLU B 390 ? 0.3677 0.5511 0.2762 -0.1347 -0.0123 0.0687  390 GLU B N   
6770  C CA  . GLU B 390 ? 0.4014 0.5958 0.3005 -0.1487 -0.0177 0.0697  390 GLU B CA  
6771  C C   . GLU B 390 ? 0.3783 0.6060 0.2978 -0.1462 -0.0260 0.0830  390 GLU B C   
6772  O O   . GLU B 390 ? 0.3736 0.6238 0.3097 -0.1461 -0.0317 0.0926  390 GLU B O   
6773  C CB  . GLU B 390 ? 0.4329 0.6269 0.3115 -0.1752 -0.0219 0.0654  390 GLU B CB  
6774  C CG  . GLU B 390 ? 0.5276 0.7382 0.3996 -0.1911 -0.0286 0.0688  390 GLU B CG  
6775  C CD  . GLU B 390 ? 0.6262 0.8320 0.4748 -0.2194 -0.0318 0.0635  390 GLU B CD  
6776  O OE1 . GLU B 390 ? 0.7122 0.8945 0.5452 -0.2261 -0.0269 0.0543  390 GLU B OE1 
6777  O OE2 . GLU B 390 ? 0.6660 0.8901 0.5112 -0.2354 -0.0382 0.0686  390 GLU B OE2 
6778  N N   . ILE B 391 ? 0.3831 0.6136 0.3016 -0.1432 -0.0258 0.0839  391 ILE B N   
6779  C CA  . ILE B 391 ? 0.4797 0.7413 0.4137 -0.1445 -0.0326 0.0960  391 ILE B CA  
6780  C C   . ILE B 391 ? 0.5370 0.8039 0.4542 -0.1637 -0.0362 0.0944  391 ILE B C   
6781  O O   . ILE B 391 ? 0.5839 0.8447 0.4956 -0.1587 -0.0336 0.0925  391 ILE B O   
6782  C CB  . ILE B 391 ? 0.4484 0.7076 0.3963 -0.1226 -0.0282 0.0991  391 ILE B CB  
6783  C CG1 . ILE B 391 ? 0.3638 0.6078 0.3218 -0.1045 -0.0226 0.0971  391 ILE B CG1 
6784  C CG2 . ILE B 391 ? 0.4766 0.7686 0.4430 -0.1218 -0.0337 0.1127  391 ILE B CG2 
6785  C CD1 . ILE B 391 ? 0.3611 0.6229 0.3348 -0.1044 -0.0267 0.1049  391 ILE B CD1 
6786  N N   . GLY B 392 ? 0.5187 0.7951 0.4264 -0.1864 -0.0418 0.0947  392 GLY B N   
6787  C CA  . GLY B 392 ? 0.6152 0.8909 0.5026 -0.2072 -0.0442 0.0914  392 GLY B CA  
6788  C C   . GLY B 392 ? 0.6276 0.9270 0.5135 -0.2330 -0.0523 0.0984  392 GLY B C   
6789  O O   . GLY B 392 ? 0.6118 0.9406 0.5196 -0.2323 -0.0576 0.1112  392 GLY B O   
6790  N N   . SER B 393 ? 0.7295 1.0127 0.5880 -0.2549 -0.0518 0.0900  393 SER B N   
6791  C CA  . SER B 393 ? 0.6912 0.9912 0.5423 -0.2816 -0.0578 0.0962  393 SER B CA  
6792  C C   . SER B 393 ? 0.6598 0.9545 0.5112 -0.2827 -0.0588 0.0966  393 SER B C   
6793  O O   . SER B 393 ? 0.6275 0.9385 0.4787 -0.2940 -0.0636 0.1059  393 SER B O   
6794  C CB  . SER B 393 ? 0.6850 0.9609 0.5018 -0.3033 -0.0552 0.0857  393 SER B CB  
6795  O OG  . SER B 393 ? 0.6993 0.9786 0.5114 -0.2988 -0.0555 0.0864  393 SER B OG  
6796  N N   . PHE B 394 ? 0.5641 0.8371 0.4151 -0.2722 -0.0541 0.0872  394 PHE B N   
6797  C CA  . PHE B 394 ? 0.6354 0.9050 0.4880 -0.2719 -0.0554 0.0881  394 PHE B CA  
6798  C C   . PHE B 394 ? 0.6147 0.9138 0.4988 -0.2534 -0.0602 0.1031  394 PHE B C   
6799  O O   . PHE B 394 ? 0.6445 0.9564 0.5330 -0.2584 -0.0648 0.1112  394 PHE B O   
6800  C CB  . PHE B 394 ? 0.6669 0.9044 0.5083 -0.2666 -0.0483 0.0736  394 PHE B CB  
6801  C CG  . PHE B 394 ? 0.7058 0.9373 0.5453 -0.2673 -0.0490 0.0731  394 PHE B CG  
6802  C CD1 . PHE B 394 ? 0.7127 0.9420 0.5354 -0.2870 -0.0523 0.0739  394 PHE B CD1 
6803  C CD2 . PHE B 394 ? 0.5761 0.8038 0.4294 -0.2492 -0.0463 0.0720  394 PHE B CD2 
6804  C CE1 . PHE B 394 ? 0.6687 0.8925 0.4872 -0.2878 -0.0534 0.0735  394 PHE B CE1 
6805  C CE2 . PHE B 394 ? 0.5902 0.8126 0.4411 -0.2498 -0.0464 0.0721  394 PHE B CE2 
6806  C CZ  . PHE B 394 ? 0.6177 0.8386 0.4509 -0.2695 -0.0502 0.0729  394 PHE B CZ  
6807  N N   . LEU B 395 ? 0.5718 0.8803 0.4772 -0.2321 -0.0584 0.1072  395 LEU B N   
6808  C CA  . LEU B 395 ? 0.5386 0.8716 0.4722 -0.2141 -0.0608 0.1215  395 LEU B CA  
6809  C C   . LEU B 395 ? 0.6613 1.0221 0.6019 -0.2224 -0.0656 0.1348  395 LEU B C   
6810  O O   . LEU B 395 ? 0.6328 1.0122 0.5896 -0.2168 -0.0682 0.1466  395 LEU B O   
6811  C CB  . LEU B 395 ? 0.5634 0.8963 0.5152 -0.1902 -0.0562 0.1221  395 LEU B CB  
6812  C CG  . LEU B 395 ? 0.5205 0.8701 0.4996 -0.1688 -0.0555 0.1346  395 LEU B CG  
6813  C CD1 . LEU B 395 ? 0.5734 0.9094 0.5633 -0.1468 -0.0495 0.1303  395 LEU B CD1 
6814  C CD2 . LEU B 395 ? 0.5745 0.9486 0.5660 -0.1666 -0.0571 0.1467  395 LEU B CD2 
6815  N N   . LEU B 396 ? 0.9217 1.2860 0.8501 -0.2357 -0.0663 0.1336  396 LEU B N   
6816  C CA  . LEU B 396 ? 0.8994 1.2925 0.8350 -0.2426 -0.0702 0.1474  396 LEU B CA  
6817  C C   . LEU B 396 ? 0.9195 1.3239 0.8493 -0.2594 -0.0746 0.1552  396 LEU B C   
6818  O O   . LEU B 396 ? 1.0062 1.4358 0.9537 -0.2541 -0.0768 0.1700  396 LEU B O   
6819  C CB  . LEU B 396 ? 0.9194 1.3120 0.8394 -0.2558 -0.0704 0.1434  396 LEU B CB  
6820  C CG  . LEU B 396 ? 0.9881 1.4125 0.9174 -0.2594 -0.0740 0.1578  396 LEU B CG  
6821  C CD1 . LEU B 396 ? 0.9882 1.4308 0.9473 -0.2342 -0.0721 0.1687  396 LEU B CD1 
6822  C CD2 . LEU B 396 ? 0.9881 1.4101 0.9024 -0.2704 -0.0739 0.1525  396 LEU B CD2 
6823  N N   . GLY B 397 ? 0.7646 1.1817 0.6890 -0.1634 -0.1207 0.0517  397 GLY B N   
6824  C CA  . GLY B 397 ? 0.7001 1.1261 0.6234 -0.1781 -0.1247 0.0471  397 GLY B CA  
6825  C C   . GLY B 397 ? 0.7695 1.1961 0.6816 -0.1835 -0.1339 0.0441  397 GLY B C   
6826  O O   . GLY B 397 ? 0.7316 1.1492 0.6329 -0.1773 -0.1367 0.0450  397 GLY B O   
6827  N N   . ARG B 398 ? 0.7129 1.1504 0.6274 -0.1959 -0.1385 0.0405  398 ARG B N   
6828  C CA  . ARG B 398 ? 0.8019 1.2415 0.7071 -0.2026 -0.1478 0.0374  398 ARG B CA  
6829  C C   . ARG B 398 ? 0.8806 1.3414 0.8041 -0.1966 -0.1549 0.0402  398 ARG B C   
6830  O O   . ARG B 398 ? 0.7972 1.2746 0.7417 -0.1933 -0.1534 0.0420  398 ARG B O   
6831  C CB  . ARG B 398 ? 0.7699 1.2075 0.6663 -0.2200 -0.1498 0.0316  398 ARG B CB  
6832  C CG  . ARG B 398 ? 0.7751 1.1861 0.6477 -0.2266 -0.1461 0.0271  398 ARG B CG  
6833  C CD  . ARG B 398 ? 0.7634 1.1688 0.6242 -0.2439 -0.1505 0.0211  398 ARG B CD  
6834  N NE  . ARG B 398 ? 0.7753 1.1535 0.6155 -0.2498 -0.1466 0.0164  398 ARG B NE  
6835  C CZ  . ARG B 398 ? 0.8082 1.1641 0.6248 -0.2501 -0.1495 0.0112  398 ARG B CZ  
6836  N NH1 . ARG B 398 ? 0.8168 1.1747 0.6264 -0.2460 -0.1560 0.0103  398 ARG B NH1 
6837  N NH2 . ARG B 398 ? 0.8031 1.1332 0.6023 -0.2542 -0.1459 0.0065  398 ARG B NH2 
6838  N N   . ASP B 399 ? 1.0171 1.4761 0.9319 -0.1948 -0.1629 0.0400  399 ASP B N   
6839  C CA  . ASP B 399 ? 1.0286 1.5050 0.9586 -0.1895 -0.1715 0.0421  399 ASP B CA  
6840  C C   . ASP B 399 ? 1.0672 1.5620 1.0089 -0.2006 -0.1760 0.0384  399 ASP B C   
6841  O O   . ASP B 399 ? 1.0844 1.5751 1.0131 -0.2141 -0.1785 0.0339  399 ASP B O   
6842  C CB  . ASP B 399 ? 1.0361 1.5046 0.9507 -0.1874 -0.1794 0.0423  399 ASP B CB  
6843  C CG  . ASP B 399 ? 1.0879 1.5723 1.0166 -0.1824 -0.1897 0.0442  399 ASP B CG  
6844  O OD1 . ASP B 399 ? 1.0843 1.5806 1.0343 -0.1736 -0.1895 0.0470  399 ASP B OD1 
6845  O OD2 . ASP B 399 ? 1.0963 1.5802 1.0142 -0.1871 -0.1984 0.0423  399 ASP B OD2 
6846  N N   . PRO B 400 ? 0.9712 1.4855 0.9370 -0.1951 -0.1773 0.0398  400 PRO B N   
6847  C CA  . PRO B 400 ? 0.9567 1.4903 0.9349 -0.2055 -0.1815 0.0360  400 PRO B CA  
6848  C C   . PRO B 400 ? 1.0103 1.5490 0.9829 -0.2118 -0.1931 0.0335  400 PRO B C   
6849  O O   . PRO B 400 ? 0.9641 1.5144 0.9404 -0.2241 -0.1965 0.0296  400 PRO B O   
6850  C CB  . PRO B 400 ? 0.9012 1.4531 0.9065 -0.1943 -0.1809 0.0377  400 PRO B CB  
6851  C CG  . PRO B 400 ? 0.9030 1.4421 0.9081 -0.1812 -0.1733 0.0421  400 PRO B CG  
6852  C CD  . PRO B 400 ? 0.9796 1.4981 0.9624 -0.1794 -0.1745 0.0442  400 PRO B CD  
6853  N N   . ALA B 401 ? 0.9563 1.4865 0.9196 -0.2043 -0.1995 0.0356  401 ALA B N   
6854  C CA  . ALA B 401 ? 0.8968 1.4320 0.8552 -0.2089 -0.2113 0.0336  401 ALA B CA  
6855  C C   . ALA B 401 ? 0.9429 1.4607 0.8737 -0.2197 -0.2129 0.0305  401 ALA B C   
6856  O O   . ALA B 401 ? 0.8434 1.3648 0.7683 -0.2261 -0.2225 0.0279  401 ALA B O   
6857  C CB  . ALA B 401 ? 0.8630 1.3989 0.8268 -0.1947 -0.2186 0.0376  401 ALA B CB  
6858  N N   . THR B 402 ? 1.0475 1.5459 0.9613 -0.2213 -0.2042 0.0300  402 THR B N   
6859  C CA  . THR B 402 ? 1.0693 1.5489 0.9563 -0.2309 -0.2053 0.0256  402 THR B CA  
6860  C C   . THR B 402 ? 1.1251 1.5932 1.0030 -0.2419 -0.1978 0.0217  402 THR B C   
6861  O O   . THR B 402 ? 1.1138 1.5679 0.9717 -0.2523 -0.2005 0.0165  402 THR B O   
6862  C CB  . THR B 402 ? 1.0710 1.5323 0.9397 -0.2215 -0.2040 0.0275  402 THR B CB  
6863  O OG1 . THR B 402 ? 1.0885 1.5432 0.9618 -0.2119 -0.1939 0.0312  402 THR B OG1 
6864  C CG2 . THR B 402 ? 1.0794 1.5483 0.9519 -0.2131 -0.2129 0.0310  402 THR B CG2 
6865  N N   . GLY B 403 ? 1.0335 1.5055 0.9243 -0.2398 -0.1889 0.0238  403 GLY B N   
6866  C CA  . GLY B 403 ? 1.0624 1.5206 0.9429 -0.2498 -0.1819 0.0205  403 GLY B CA  
6867  C C   . GLY B 403 ? 1.0538 1.4849 0.9113 -0.2465 -0.1772 0.0187  403 GLY B C   
6868  O O   . GLY B 403 ? 1.0388 1.4531 0.8824 -0.2557 -0.1738 0.0144  403 GLY B O   
6869  N N   . GLU B 404 ? 1.0169 1.4425 0.8697 -0.2336 -0.1771 0.0216  404 GLU B N   
6870  C CA  . GLU B 404 ? 0.9934 1.3951 0.8257 -0.2283 -0.1722 0.0198  404 GLU B CA  
6871  C C   . GLU B 404 ? 0.9265 1.3291 0.7696 -0.2139 -0.1646 0.0259  404 GLU B C   
6872  O O   . GLU B 404 ? 0.9018 1.3220 0.7673 -0.2082 -0.1633 0.0310  404 GLU B O   
6873  C CB  . GLU B 404 ? 1.0539 1.4461 0.8665 -0.2268 -0.1791 0.0171  404 GLU B CB  
6874  C CG  . GLU B 404 ? 1.0915 1.4718 0.8848 -0.2402 -0.1848 0.0092  404 GLU B CG  
6875  C CD  . GLU B 404 ? 1.1129 1.4660 0.8842 -0.2426 -0.1795 0.0029  404 GLU B CD  
6876  O OE1 . GLU B 404 ? 0.9817 1.3287 0.7580 -0.2414 -0.1715 0.0038  404 GLU B OE1 
6877  O OE2 . GLU B 404 ? 1.1460 1.4829 0.8946 -0.2451 -0.1837 -0.0033 404 GLU B OE2 
6878  N N   . GLN B 405 ? 0.9139 1.2968 0.7407 -0.2075 -0.1597 0.0248  405 GLN B N   
6879  C CA  . GLN B 405 ? 0.8504 1.2313 0.6856 -0.1944 -0.1521 0.0303  405 GLN B CA  
6880  C C   . GLN B 405 ? 0.8526 1.2474 0.7012 -0.1834 -0.1556 0.0370  405 GLN B C   
6881  O O   . GLN B 405 ? 0.8055 1.1995 0.6445 -0.1817 -0.1619 0.0370  405 GLN B O   
6882  C CB  . GLN B 405 ? 0.8719 1.2289 0.6857 -0.1896 -0.1469 0.0270  405 GLN B CB  
6883  C CG  . GLN B 405 ? 0.7222 1.0756 0.5432 -0.1760 -0.1390 0.0325  405 GLN B CG  
6884  C CD  . GLN B 405 ? 0.7552 1.1129 0.5927 -0.1759 -0.1323 0.0350  405 GLN B CD  
6885  O OE1 . GLN B 405 ? 0.7066 1.0578 0.5399 -0.1856 -0.1304 0.0306  405 GLN B OE1 
6886  N NE2 . GLN B 405 ? 0.6487 1.0162 0.5043 -0.1652 -0.1288 0.0421  405 GLN B NE2 
6887  N N   . LYS B 406 ? 0.7896 1.1960 0.6597 -0.1760 -0.1518 0.0426  406 LYS B N   
6888  C CA  . LYS B 406 ? 0.8314 1.2464 0.7141 -0.1640 -0.1545 0.0490  406 LYS B CA  
6889  C C   . LYS B 406 ? 0.8971 1.2962 0.7688 -0.1537 -0.1495 0.0519  406 LYS B C   
6890  O O   . LYS B 406 ? 0.8344 1.2242 0.7064 -0.1497 -0.1408 0.0526  406 LYS B O   
6891  C CB  . LYS B 406 ? 0.8429 1.2727 0.7510 -0.1589 -0.1518 0.0526  406 LYS B CB  
6892  C CG  . LYS B 406 ? 0.9449 1.3861 0.8687 -0.1489 -0.1581 0.0574  406 LYS B CG  
6893  C CD  . LYS B 406 ? 0.9131 1.3694 0.8613 -0.1453 -0.1561 0.0585  406 LYS B CD  
6894  C CE  . LYS B 406 ? 0.8817 1.3443 0.8454 -0.1326 -0.1617 0.0626  406 LYS B CE  
6895  N NZ  . LYS B 406 ? 0.8031 1.2504 0.7621 -0.1211 -0.1577 0.0677  406 LYS B NZ  
6896  N N   . HIS B 407 ? 0.9726 1.3688 0.8344 -0.1500 -0.1550 0.0534  407 HIS B N   
6897  C CA  . HIS B 407 ? 0.9695 1.3511 0.8188 -0.1417 -0.1505 0.0557  407 HIS B CA  
6898  C C   . HIS B 407 ? 0.9594 1.3414 0.8249 -0.1299 -0.1448 0.0624  407 HIS B C   
6899  O O   . HIS B 407 ? 0.9657 1.3575 0.8467 -0.1241 -0.1492 0.0673  407 HIS B O   
6900  C CB  . HIS B 407 ? 0.9903 1.3711 0.8272 -0.1408 -0.1581 0.0567  407 HIS B CB  
6901  C CG  . HIS B 407 ? 1.0736 1.4426 0.9003 -0.1320 -0.1540 0.0602  407 HIS B CG  
6902  N ND1 . HIS B 407 ? 1.1184 1.4724 0.9245 -0.1324 -0.1485 0.0558  407 HIS B ND1 
6903  C CD2 . HIS B 407 ? 1.0389 1.4086 0.8732 -0.1225 -0.1545 0.0673  407 HIS B CD2 
6904  C CE1 . HIS B 407 ? 1.0733 1.4211 0.8755 -0.1239 -0.1454 0.0604  407 HIS B CE1 
6905  N NE2 . HIS B 407 ? 1.0204 1.3770 0.8393 -0.1184 -0.1491 0.0676  407 HIS B NE2 
6906  N N   . ALA B 408 ? 0.9003 1.2702 0.7619 -0.1260 -0.1355 0.0622  408 ALA B N   
6907  C CA  . ALA B 408 ? 0.9221 1.2896 0.7973 -0.1150 -0.1295 0.0681  408 ALA B CA  
6908  C C   . ALA B 408 ? 0.8867 1.2446 0.7528 -0.1071 -0.1288 0.0719  408 ALA B C   
6909  O O   . ALA B 408 ? 0.8823 1.2301 0.7286 -0.1091 -0.1277 0.0686  408 ALA B O   
6910  C CB  . ALA B 408 ? 0.8160 1.1754 0.6927 -0.1147 -0.1200 0.0661  408 ALA B CB  
6911  N N   . ASP B 409 ? 0.8189 1.1790 0.6987 -0.0982 -0.1295 0.0784  409 ASP B N   
6912  C CA  . ASP B 409 ? 0.8457 1.1968 0.7187 -0.0911 -0.1287 0.0828  409 ASP B CA  
6913  C C   . ASP B 409 ? 0.8497 1.1886 0.7227 -0.0846 -0.1184 0.0839  409 ASP B C   
6914  O O   . ASP B 409 ? 0.8516 1.1827 0.7196 -0.0790 -0.1166 0.0875  409 ASP B O   
6915  C CB  . ASP B 409 ? 0.7778 1.1342 0.6641 -0.0848 -0.1356 0.0887  409 ASP B CB  
6916  C CG  . ASP B 409 ? 0.7413 1.1029 0.6497 -0.0797 -0.1340 0.0904  409 ASP B CG  
6917  O OD1 . ASP B 409 ? 0.7906 1.1626 0.7069 -0.0848 -0.1351 0.0869  409 ASP B OD1 
6918  O OD2 . ASP B 409 ? 0.6345 0.9895 0.5518 -0.0708 -0.1318 0.0948  409 ASP B OD2 
6919  N N   . MET B 410 ? 0.8550 1.1920 0.7331 -0.0857 -0.1118 0.0809  410 MET B N   
6920  C CA  . MET B 410 ? 0.8176 1.1423 0.6952 -0.0799 -0.1024 0.0811  410 MET B CA  
6921  C C   . MET B 410 ? 0.7938 1.1153 0.6677 -0.0854 -0.0978 0.0751  410 MET B C   
6922  O O   . MET B 410 ? 0.8435 1.1729 0.7167 -0.0940 -0.1018 0.0714  410 MET B O   
6923  C CB  . MET B 410 ? 0.8075 1.1315 0.7039 -0.0708 -0.0992 0.0871  410 MET B CB  
6924  C CG  . MET B 410 ? 0.7983 1.1087 0.6923 -0.0634 -0.0916 0.0889  410 MET B CG  
6925  S SD  . MET B 410 ? 0.8675 1.1721 0.7459 -0.0616 -0.0941 0.0913  410 MET B SD  
6926  C CE  . MET B 410 ? 0.7481 1.0636 0.6402 -0.0593 -0.1022 0.0992  410 MET B CE  
6927  N N   . GLU B 411 ? 0.6498 0.9588 0.5211 -0.0806 -0.0898 0.0740  411 GLU B N   
6928  C CA  . GLU B 411 ? 0.6383 0.9396 0.5024 -0.0854 -0.0858 0.0678  411 GLU B CA  
6929  C C   . GLU B 411 ? 0.5612 0.8515 0.4322 -0.0771 -0.0774 0.0695  411 GLU B C   
6930  O O   . GLU B 411 ? 0.5394 0.8151 0.3976 -0.0733 -0.0729 0.0664  411 GLU B O   
6931  C CB  . GLU B 411 ? 0.6401 0.9313 0.4795 -0.0906 -0.0872 0.0604  411 GLU B CB  
6932  C CG  . GLU B 411 ? 0.7437 1.0269 0.5731 -0.0985 -0.0862 0.0527  411 GLU B CG  
6933  C CD  . GLU B 411 ? 0.7475 1.0439 0.5817 -0.1100 -0.0926 0.0511  411 GLU B CD  
6934  O OE1 . GLU B 411 ? 0.7514 1.0602 0.5881 -0.1126 -0.0992 0.0532  411 GLU B OE1 
6935  O OE2 . GLU B 411 ? 0.7034 0.9971 0.5386 -0.1167 -0.0912 0.0476  411 GLU B OE2 
6936  N N   . PHE B 412 ? 0.5000 0.7972 0.3910 -0.0739 -0.0755 0.0740  412 PHE B N   
6937  C CA  . PHE B 412 ? 0.4126 0.7007 0.3132 -0.0656 -0.0682 0.0764  412 PHE B CA  
6938  C C   . PHE B 412 ? 0.4109 0.6922 0.3097 -0.0692 -0.0640 0.0722  412 PHE B C   
6939  O O   . PHE B 412 ? 0.4336 0.7231 0.3333 -0.0782 -0.0666 0.0698  412 PHE B O   
6940  C CB  . PHE B 412 ? 0.3977 0.6944 0.3196 -0.0598 -0.0680 0.0827  412 PHE B CB  
6941  C CG  . PHE B 412 ? 0.4576 0.7535 0.3818 -0.0535 -0.0704 0.0874  412 PHE B CG  
6942  C CD1 . PHE B 412 ? 0.4119 0.6974 0.3238 -0.0504 -0.0687 0.0871  412 PHE B CD1 
6943  C CD2 . PHE B 412 ? 0.4582 0.7625 0.3960 -0.0507 -0.0745 0.0917  412 PHE B CD2 
6944  C CE1 . PHE B 412 ? 0.5409 0.8277 0.4547 -0.0465 -0.0710 0.0922  412 PHE B CE1 
6945  C CE2 . PHE B 412 ? 0.5076 0.8121 0.4467 -0.0464 -0.0772 0.0968  412 PHE B CE2 
6946  C CZ  . PHE B 412 ? 0.5262 0.8240 0.4537 -0.0453 -0.0754 0.0977  412 PHE B CZ  
6947  N N   . MET B 413 ? 0.3229 0.5885 0.2186 -0.0626 -0.0578 0.0711  413 MET B N   
6948  C CA  . MET B 413 ? 0.2754 0.5336 0.1756 -0.0628 -0.0531 0.0696  413 MET B CA  
6949  C C   . MET B 413 ? 0.2446 0.5046 0.1652 -0.0538 -0.0489 0.0755  413 MET B C   
6950  O O   . MET B 413 ? 0.2390 0.4930 0.1624 -0.0455 -0.0468 0.0781  413 MET B O   
6951  C CB  . MET B 413 ? 0.2760 0.5124 0.1577 -0.0609 -0.0492 0.0637  413 MET B CB  
6952  C CG  . MET B 413 ? 0.2618 0.4868 0.1491 -0.0579 -0.0439 0.0634  413 MET B CG  
6953  S SD  . MET B 413 ? 0.4122 0.6086 0.2756 -0.0554 -0.0397 0.0557  413 MET B SD  
6954  C CE  . MET B 413 ? 0.4146 0.6037 0.2738 -0.0439 -0.0366 0.0569  413 MET B CE  
6955  N N   . ARG B 414 ? 0.2288 0.4974 0.1632 -0.0562 -0.0478 0.0773  414 ARG B N   
6956  C CA  . ARG B 414 ? 0.2077 0.4780 0.1609 -0.0480 -0.0439 0.0821  414 ARG B CA  
6957  C C   . ARG B 414 ? 0.1957 0.4525 0.1509 -0.0449 -0.0381 0.0806  414 ARG B C   
6958  O O   . ARG B 414 ? 0.2184 0.4762 0.1711 -0.0520 -0.0378 0.0783  414 ARG B O   
6959  C CB  . ARG B 414 ? 0.2023 0.4911 0.1694 -0.0510 -0.0463 0.0853  414 ARG B CB  
6960  C CG  . ARG B 414 ? 0.1843 0.4714 0.1676 -0.0417 -0.0422 0.0893  414 ARG B CG  
6961  C CD  . ARG B 414 ? 0.1942 0.4966 0.1883 -0.0432 -0.0445 0.0912  414 ARG B CD  
6962  N NE  . ARG B 414 ? 0.1803 0.4900 0.1780 -0.0490 -0.0418 0.0901  414 ARG B NE  
6963  C CZ  . ARG B 414 ? 0.2732 0.5965 0.2789 -0.0510 -0.0433 0.0905  414 ARG B CZ  
6964  N NH1 . ARG B 414 ? 0.2972 0.6274 0.3086 -0.0472 -0.0485 0.0912  414 ARG B NH1 
6965  N NH2 . ARG B 414 ? 0.2368 0.5658 0.2444 -0.0568 -0.0400 0.0895  414 ARG B NH2 
6966  N N   . LEU B 415 ? 0.1854 0.4289 0.1446 -0.0352 -0.0338 0.0816  415 LEU B N   
6967  C CA  . LEU B 415 ? 0.1729 0.4020 0.1358 -0.0305 -0.0285 0.0802  415 LEU B CA  
6968  C C   . LEU B 415 ? 0.1570 0.3936 0.1402 -0.0260 -0.0256 0.0843  415 LEU B C   
6969  O O   . LEU B 415 ? 0.1745 0.4129 0.1671 -0.0195 -0.0230 0.0880  415 LEU B O   
6970  C CB  . LEU B 415 ? 0.1753 0.3846 0.1291 -0.0232 -0.0255 0.0778  415 LEU B CB  
6971  C CG  . LEU B 415 ? 0.1977 0.4002 0.1295 -0.0262 -0.0278 0.0740  415 LEU B CG  
6972  C CD1 . LEU B 415 ? 0.1996 0.3918 0.1265 -0.0190 -0.0247 0.0738  415 LEU B CD1 
6973  C CD2 . LEU B 415 ? 0.2162 0.4081 0.1315 -0.0324 -0.0278 0.0687  415 LEU B CD2 
6974  N N   . THR B 416 ? 0.1627 0.4112 0.1530 -0.0313 -0.0255 0.0854  416 THR B N   
6975  C CA  . THR B 416 ? 0.1420 0.3977 0.1477 -0.0276 -0.0224 0.0888  416 THR B CA  
6976  C C   . THR B 416 ? 0.1292 0.3724 0.1421 -0.0226 -0.0166 0.0879  416 THR B C   
6977  O O   . THR B 416 ? 0.1492 0.3878 0.1581 -0.0265 -0.0165 0.0855  416 THR B O   
6978  C CB  . THR B 416 ? 0.1393 0.4148 0.1477 -0.0356 -0.0248 0.0904  416 THR B CB  
6979  O OG1 . THR B 416 ? 0.1795 0.4639 0.1770 -0.0447 -0.0307 0.0884  416 THR B OG1 
6980  C CG2 . THR B 416 ? 0.1664 0.4475 0.1828 -0.0302 -0.0255 0.0932  416 THR B CG2 
6981  N N   . ILE B 417 ? 0.1436 0.3878 0.1675 -0.0157 -0.0118 0.0917  417 ILE B N   
6982  C CA  . ILE B 417 ? 0.0956 0.3304 0.1275 -0.0103 -0.0058 0.0915  417 ILE B CA  
6983  C C   . ILE B 417 ? 0.1043 0.3370 0.1411 -0.0088 -0.0030 0.0922  417 ILE B C   
6984  O O   . ILE B 417 ? 0.1272 0.3661 0.1662 -0.0066 -0.0021 0.0963  417 ILE B O   
6985  C CB  . ILE B 417 ? 0.0929 0.3238 0.1285 -0.0037 -0.0027 0.0935  417 ILE B CB  
6986  C CG1 . ILE B 417 ? 0.1132 0.3405 0.1374 -0.0043 -0.0072 0.0917  417 ILE B CG1 
6987  C CG2 . ILE B 417 ? 0.1181 0.3310 0.1572 0.0022  0.0014  0.0901  417 ILE B CG2 
6988  C CD1 . ILE B 417 ? 0.1449 0.3566 0.1570 -0.0051 -0.0088 0.0862  417 ILE B CD1 
6989  N N   . ALA B 418 ? 0.1252 0.3464 0.1609 -0.0098 -0.0029 0.0877  418 ALA B N   
6990  C CA  . ALA B 418 ? 0.1050 0.3183 0.1417 -0.0076 -0.0011 0.0866  418 ALA B CA  
6991  C C   . ALA B 418 ? 0.1133 0.3109 0.1528 0.0000  0.0028  0.0859  418 ALA B C   
6992  O O   . ALA B 418 ? 0.1654 0.3540 0.2061 0.0034  0.0042  0.0842  418 ALA B O   
6993  C CB  . ALA B 418 ? 0.1271 0.3328 0.1621 -0.0113 -0.0023 0.0821  418 ALA B CB  
6994  N N   . ARG B 419 ? 0.1661 0.3627 0.2060 0.0023  0.0043  0.0876  419 ARG B N   
6995  C CA  . ARG B 419 ? 0.1315 0.3170 0.1734 0.0077  0.0074  0.0878  419 ARG B CA  
6996  C C   . ARG B 419 ? 0.1171 0.2812 0.1580 0.0093  0.0096  0.0810  419 ARG B C   
6997  O O   . ARG B 419 ? 0.1211 0.2815 0.1602 0.0080  0.0094  0.0791  419 ARG B O   
6998  C CB  . ARG B 419 ? 0.1420 0.3402 0.1855 0.0095  0.0074  0.0940  419 ARG B CB  
6999  C CG  . ARG B 419 ? 0.0916 0.3124 0.1373 0.0083  0.0052  0.1013  419 ARG B CG  
7000  C CD  . ARG B 419 ? 0.1036 0.3441 0.1513 0.0092  0.0041  0.1076  419 ARG B CD  
7001  N NE  . ARG B 419 ? 0.1465 0.3983 0.1962 0.0090  -0.0035 0.1080  419 ARG B NE  
7002  C CZ  . ARG B 419 ? 0.1231 0.3856 0.1709 0.0040  -0.0080 0.1061  419 ARG B CZ  
7003  N NH1 . ARG B 419 ? 0.1306 0.3947 0.1744 -0.0014 -0.0062 0.1037  419 ARG B NH1 
7004  N NH2 . ARG B 419 ? 0.1548 0.4262 0.2042 0.0040  -0.0151 0.1066  419 ARG B NH2 
7005  N N   . ARG B 420 ? 0.1199 0.2718 0.1618 0.0119  0.0115  0.0777  420 ARG B N   
7006  C CA  . ARG B 420 ? 0.1025 0.2357 0.1437 0.0135  0.0135  0.0712  420 ARG B CA  
7007  C C   . ARG B 420 ? 0.1415 0.2696 0.1829 0.0120  0.0120  0.0668  420 ARG B C   
7008  O O   . ARG B 420 ? 0.1352 0.2513 0.1765 0.0126  0.0128  0.0622  420 ARG B O   
7009  C CB  . ARG B 420 ? 0.1072 0.2351 0.1473 0.0143  0.0151  0.0713  420 ARG B CB  
7010  C CG  . ARG B 420 ? 0.1241 0.2619 0.1660 0.0164  0.0156  0.0780  420 ARG B CG  
7011  C CD  . ARG B 420 ? 0.0792 0.2113 0.1208 0.0182  0.0171  0.0781  420 ARG B CD  
7012  N NE  . ARG B 420 ? 0.1369 0.2752 0.1772 0.0179  0.0161  0.0801  420 ARG B NE  
7013  C CZ  . ARG B 420 ? 0.1365 0.2791 0.1779 0.0204  0.0168  0.0837  420 ARG B CZ  
7014  N NH1 . ARG B 420 ? 0.1639 0.3043 0.2076 0.0230  0.0185  0.0856  420 ARG B NH1 
7015  N NH2 . ARG B 420 ? 0.1097 0.2612 0.1500 0.0205  0.0157  0.0859  420 ARG B NH2 
7016  N N   . VAL B 421 ? 0.1533 0.2925 0.1952 0.0100  0.0091  0.0693  421 VAL B N   
7017  C CA  . VAL B 421 ? 0.1014 0.2411 0.1432 0.0080  0.0062  0.0685  421 VAL B CA  
7018  C C   . VAL B 421 ? 0.1366 0.2728 0.1771 0.0107  0.0066  0.0690  421 VAL B C   
7019  O O   . VAL B 421 ? 0.1530 0.2815 0.1927 0.0119  0.0068  0.0680  421 VAL B O   
7020  C CB  . VAL B 421 ? 0.1397 0.2971 0.1799 0.0014  0.0021  0.0722  421 VAL B CB  
7021  C CG1 . VAL B 421 ? 0.1078 0.2693 0.1450 -0.0037 -0.0016 0.0738  421 VAL B CG1 
7022  C CG2 . VAL B 421 ? 0.1255 0.2863 0.1658 -0.0008 0.0026  0.0719  421 VAL B CG2 
7023  N N   . TYR B 422 ? 0.1061 0.2495 0.1459 0.0118  0.0070  0.0713  422 TYR B N   
7024  C CA  . TYR B 422 ? 0.1618 0.3061 0.1993 0.0144  0.0076  0.0727  422 TYR B CA  
7025  C C   . TYR B 422 ? 0.1368 0.2711 0.1746 0.0197  0.0112  0.0701  422 TYR B C   
7026  O O   . TYR B 422 ? 0.1629 0.2978 0.2024 0.0195  0.0121  0.0701  422 TYR B O   
7027  C CB  . TYR B 422 ? 0.1474 0.3073 0.1794 0.0097  0.0041  0.0765  422 TYR B CB  
7028  C CG  . TYR B 422 ? 0.1779 0.3329 0.1968 0.0009  -0.0007 0.0752  422 TYR B CG  
7029  C CD1 . TYR B 422 ? 0.1460 0.2767 0.1474 -0.0022 -0.0010 0.0714  422 TYR B CD1 
7030  C CD2 . TYR B 422 ? 0.0940 0.2677 0.1163 -0.0053 -0.0034 0.0775  422 TYR B CD2 
7031  C CE1 . TYR B 422 ? 0.1593 0.2846 0.1468 -0.0120 -0.0032 0.0699  422 TYR B CE1 
7032  C CE2 . TYR B 422 ? 0.1243 0.2956 0.1349 -0.0146 -0.0069 0.0757  422 TYR B CE2 
7033  C CZ  . TYR B 422 ? 0.1798 0.3266 0.1727 -0.0183 -0.0065 0.0719  422 TYR B CZ  
7034  O OH  . TYR B 422 ? 0.2111 0.3614 0.1939 -0.0302 -0.0085 0.0716  422 TYR B OH  
7035  N N   . THR B 423 ? 0.1375 0.2633 0.1728 0.0238  0.0133  0.0685  423 THR B N   
7036  C CA  . THR B 423 ? 0.1953 0.3122 0.2298 0.0273  0.0161  0.0656  423 THR B CA  
7037  C C   . THR B 423 ? 0.2040 0.3333 0.2369 0.0295  0.0160  0.0697  423 THR B C   
7038  O O   . THR B 423 ? 0.1680 0.3127 0.1995 0.0282  0.0139  0.0741  423 THR B O   
7039  C CB  . THR B 423 ? 0.2252 0.3254 0.2568 0.0303  0.0187  0.0606  423 THR B CB  
7040  O OG1 . THR B 423 ? 0.2093 0.3113 0.2364 0.0344  0.0198  0.0631  423 THR B OG1 
7041  C CG2 . THR B 423 ? 0.1480 0.2392 0.1807 0.0279  0.0183  0.0573  423 THR B CG2 
7042  N N   . ASN B 424 ? 0.1701 0.2947 0.2028 0.0318  0.0180  0.0682  424 ASN B N   
7043  C CA  . ASN B 424 ? 0.2185 0.3553 0.2496 0.0343  0.0180  0.0721  424 ASN B CA  
7044  C C   . ASN B 424 ? 0.2039 0.3405 0.2290 0.0392  0.0193  0.0722  424 ASN B C   
7045  O O   . ASN B 424 ? 0.1843 0.3202 0.1965 0.0376  0.0159  0.0726  424 ASN B O   
7046  C CB  . ASN B 424 ? 0.2058 0.3387 0.2385 0.0353  0.0197  0.0713  424 ASN B CB  
7047  C CG  . ASN B 424 ? 0.2462 0.3849 0.2837 0.0317  0.0188  0.0738  424 ASN B CG  
7048  O OD1 . ASN B 424 ? 0.2023 0.3527 0.2413 0.0290  0.0167  0.0776  424 ASN B OD1 
7049  N ND2 . ASN B 424 ? 0.2578 0.3891 0.2970 0.0314  0.0203  0.0723  424 ASN B ND2 
7050  N N   . ASP B 425 ? 0.2025 0.3229 0.2246 0.0415  0.0213  0.0681  425 ASP B N   
7051  C CA  . ASP B 425 ? 0.2098 0.3096 0.2118 0.0414  0.0193  0.0647  425 ASP B CA  
7052  C C   . ASP B 425 ? 0.2364 0.3271 0.2204 0.0326  0.0136  0.0643  425 ASP B C   
7053  O O   . ASP B 425 ? 0.2315 0.3087 0.1939 0.0294  0.0119  0.0620  425 ASP B O   
7054  C CB  . ASP B 425 ? 0.2943 0.3785 0.2970 0.0453  0.0232  0.0607  425 ASP B CB  
7055  C CG  . ASP B 425 ? 0.2538 0.3372 0.2641 0.0497  0.0276  0.0580  425 ASP B CG  
7056  O OD1 . ASP B 425 ? 0.2848 0.3761 0.2954 0.0513  0.0275  0.0598  425 ASP B OD1 
7057  O OD2 . ASP B 425 ? 0.2750 0.3439 0.2854 0.0470  0.0283  0.0526  425 ASP B OD2 
7058  N N   . HIS B 426 ? 0.2026 0.3015 0.1942 0.0281  0.0116  0.0661  426 HIS B N   
7059  C CA  . HIS B 426 ? 0.1862 0.2812 0.1619 0.0192  0.0070  0.0659  426 HIS B CA  
7060  C C   . HIS B 426 ? 0.1958 0.3040 0.1670 0.0172  0.0046  0.0677  426 HIS B C   
7061  O O   . HIS B 426 ? 0.1926 0.2923 0.1433 0.0112  0.0021  0.0655  426 HIS B O   
7062  C CB  . HIS B 426 ? 0.1964 0.3020 0.1842 0.0154  0.0055  0.0678  426 HIS B CB  
7063  C CG  . HIS B 426 ? 0.1947 0.2848 0.1811 0.0149  0.0069  0.0656  426 HIS B CG  
7064  N ND1 . HIS B 426 ? 0.1556 0.2560 0.1627 0.0187  0.0091  0.0667  426 HIS B ND1 
7065  C CD2 . HIS B 426 ? 0.2075 0.2717 0.1729 0.0103  0.0069  0.0621  426 HIS B CD2 
7066  C CE1 . HIS B 426 ? 0.1839 0.2664 0.1835 0.0169  0.0095  0.0641  426 HIS B CE1 
7067  N NE2 . HIS B 426 ? 0.1998 0.2594 0.1739 0.0113  0.0083  0.0615  426 HIS B NE2 
7068  N N   . MET B 427 ? 0.1937 0.3217 0.1825 0.0216  0.0059  0.0714  427 MET B N   
7069  C CA  . MET B 427 ? 0.2152 0.3554 0.1993 0.0195  0.0034  0.0735  427 MET B CA  
7070  C C   . MET B 427 ? 0.2186 0.3462 0.1835 0.0207  0.0038  0.0705  427 MET B C   
7071  O O   . MET B 427 ? 0.2130 0.3402 0.1617 0.0161  0.0010  0.0693  427 MET B O   
7072  C CB  . MET B 427 ? 0.1767 0.3378 0.1815 0.0230  0.0057  0.0785  427 MET B CB  
7073  C CG  . MET B 427 ? 0.1523 0.3264 0.1744 0.0213  0.0069  0.0815  427 MET B CG  
7074  S SD  . MET B 427 ? 0.1841 0.3671 0.2013 0.0128  0.0015  0.0828  427 MET B SD  
7075  C CE  . MET B 427 ? 0.1440 0.3210 0.1680 0.0117  0.0028  0.0809  427 MET B CE  
7076  N N   . ASP B 428 ? 0.2187 0.3366 0.1848 0.0271  0.0075  0.0688  428 ASP B N   
7077  C CA  . ASP B 428 ? 0.2489 0.3550 0.1965 0.0284  0.0085  0.0656  428 ASP B CA  
7078  C C   . ASP B 428 ? 0.2198 0.3050 0.1406 0.0215  0.0069  0.0604  428 ASP B C   
7079  O O   . ASP B 428 ? 0.2810 0.3622 0.1829 0.0187  0.0062  0.0575  428 ASP B O   
7080  C CB  . ASP B 428 ? 0.2489 0.3486 0.2041 0.0366  0.0130  0.0645  428 ASP B CB  
7081  C CG  . ASP B 428 ? 0.2449 0.3644 0.2211 0.0428  0.0156  0.0687  428 ASP B CG  
7082  O OD1 . ASP B 428 ? 0.2297 0.3654 0.2092 0.0404  0.0136  0.0724  428 ASP B OD1 
7083  O OD2 . ASP B 428 ? 0.2266 0.3448 0.2150 0.0495  0.0200  0.0682  428 ASP B OD2 
7084  N N   . TYR B 429 ? 0.2706 0.3417 0.1882 0.0183  0.0067  0.0587  429 TYR B N   
7085  C CA  . TYR B 429 ? 0.2793 0.3290 0.1697 0.0108  0.0055  0.0537  429 TYR B CA  
7086  C C   . TYR B 429 ? 0.3027 0.3613 0.1834 0.0054  0.0021  0.0534  429 TYR B C   
7087  O O   . TYR B 429 ? 0.3084 0.3544 0.1649 0.0023  0.0016  0.0484  429 TYR B O   
7088  C CB  . TYR B 429 ? 0.2671 0.3029 0.1574 0.0074  0.0056  0.0532  429 TYR B CB  
7089  C CG  . TYR B 429 ? 0.3560 0.3667 0.2163 0.0006  0.0051  0.0480  429 TYR B CG  
7090  C CD1 . TYR B 429 ? 0.3421 0.3620 0.1964 -0.0035 0.0027  0.0482  429 TYR B CD1 
7091  C CD2 . TYR B 429 ? 0.3934 0.3795 0.2362 -0.0022 0.0063  0.0438  429 TYR B CD2 
7092  C CE1 . TYR B 429 ? 0.4360 0.4490 0.2703 -0.0073 0.0019  0.0452  429 TYR B CE1 
7093  C CE2 . TYR B 429 ? 0.4440 0.4177 0.2671 -0.0009 0.0067  0.0398  429 TYR B CE2 
7094  C CZ  . TYR B 429 ? 0.4973 0.4897 0.3149 -0.0020 0.0046  0.0418  429 TYR B CZ  
7095  O OH  . TYR B 429 ? 0.4782 0.4731 0.2834 -0.0105 0.0012  0.0375  429 TYR B OH  
7096  N N   . ILE B 430 ? 0.2717 0.3533 0.1719 0.0043  -0.0004 0.0583  430 ILE B N   
7097  C CA  . ILE B 430 ? 0.2306 0.3246 0.1254 -0.0014 -0.0045 0.0585  430 ILE B CA  
7098  C C   . ILE B 430 ? 0.2503 0.3499 0.1359 0.0000  -0.0050 0.0577  430 ILE B C   
7099  O O   . ILE B 430 ? 0.2713 0.3648 0.1365 -0.0041 -0.0069 0.0533  430 ILE B O   
7100  C CB  . ILE B 430 ? 0.1789 0.2973 0.0983 -0.0029 -0.0070 0.0642  430 ILE B CB  
7101  C CG1 . ILE B 430 ? 0.1998 0.3132 0.1260 -0.0054 -0.0065 0.0642  430 ILE B CG1 
7102  C CG2 . ILE B 430 ? 0.1932 0.3267 0.1090 -0.0088 -0.0116 0.0649  430 ILE B CG2 
7103  C CD1 . ILE B 430 ? 0.1860 0.3201 0.1400 -0.0030 -0.0065 0.0694  430 ILE B CD1 
7104  N N   . ALA B 431 ? 0.2653 0.3778 0.1660 0.0058  -0.0033 0.0616  431 ALA B N   
7105  C CA  . ALA B 431 ? 0.3106 0.4305 0.2036 0.0068  -0.0035 0.0615  431 ALA B CA  
7106  C C   . ALA B 431 ? 0.2724 0.3720 0.1395 0.0070  -0.0010 0.0545  431 ALA B C   
7107  O O   . ALA B 431 ? 0.3238 0.4222 0.1729 0.0038  -0.0026 0.0509  431 ALA B O   
7108  C CB  . ALA B 431 ? 0.2315 0.3670 0.1452 0.0133  -0.0014 0.0670  431 ALA B CB  
7109  N N   . ASP B 432 ? 0.3390 0.4227 0.2040 0.0107  0.0028  0.0520  432 ASP B N   
7110  C CA  . ASP B 432 ? 0.3625 0.4271 0.2035 0.0107  0.0055  0.0448  432 ASP B CA  
7111  C C   . ASP B 432 ? 0.3790 0.4300 0.1949 0.0048  0.0031  0.0387  432 ASP B C   
7112  O O   . ASP B 432 ? 0.4310 0.4787 0.2266 0.0043  0.0035  0.0327  432 ASP B O   
7113  C CB  . ASP B 432 ? 0.4146 0.4662 0.2601 0.0145  0.0090  0.0435  432 ASP B CB  
7114  C CG  . ASP B 432 ? 0.3866 0.4540 0.2547 0.0232  0.0116  0.0484  432 ASP B CG  
7115  O OD1 . ASP B 432 ? 0.4507 0.5347 0.3228 0.0251  0.0115  0.0509  432 ASP B OD1 
7116  O OD2 . ASP B 432 ? 0.4594 0.5224 0.3408 0.0281  0.0135  0.0498  432 ASP B OD2 
7117  N N   . ALA B 433 ? 0.3727 0.4220 0.1915 0.0012  0.0005  0.0401  433 ALA B N   
7118  C CA  . ALA B 433 ? 0.4101 0.4550 0.2091 -0.0038 -0.0027 0.0350  433 ALA B CA  
7119  C C   . ALA B 433 ? 0.4005 0.4618 0.1933 -0.0075 -0.0066 0.0336  433 ALA B C   
7120  O O   . ALA B 433 ? 0.4750 0.5303 0.2458 -0.0094 -0.0082 0.0260  433 ALA B O   
7121  C CB  . ALA B 433 ? 0.3840 0.4318 0.1933 -0.0085 -0.0049 0.0381  433 ALA B CB  
7122  N N   . LEU B 434 ? 0.3886 0.4703 0.2003 -0.0085 -0.0086 0.0401  434 LEU B N   
7123  C CA  . LEU B 434 ? 0.3952 0.4926 0.2013 -0.0127 -0.0126 0.0394  434 LEU B CA  
7124  C C   . LEU B 434 ? 0.4539 0.5488 0.2475 -0.0086 -0.0100 0.0363  434 LEU B C   
7125  O O   . LEU B 434 ? 0.4851 0.5824 0.2615 -0.0116 -0.0124 0.0311  434 LEU B O   
7126  C CB  . LEU B 434 ? 0.3766 0.4958 0.2057 -0.0148 -0.0159 0.0473  434 LEU B CB  
7127  C CG  . LEU B 434 ? 0.4173 0.5534 0.2417 -0.0207 -0.0212 0.0475  434 LEU B CG  
7128  C CD1 . LEU B 434 ? 0.4608 0.5971 0.2723 -0.0298 -0.0256 0.0423  434 LEU B CD1 
7129  C CD2 . LEU B 434 ? 0.3081 0.4642 0.1550 -0.0211 -0.0240 0.0554  434 LEU B CD2 
7130  N N   . ILE B 435 ? 0.4395 0.5311 0.2422 -0.0023 -0.0054 0.0390  435 ILE B N   
7131  C CA  . ILE B 435 ? 0.4665 0.5585 0.2589 0.0009  -0.0022 0.0360  435 ILE B CA  
7132  C C   . ILE B 435 ? 0.5457 0.6216 0.3116 0.0010  -0.0003 0.0256  435 ILE B C   
7133  O O   . ILE B 435 ? 0.4985 0.5771 0.2479 0.0002  -0.0007 0.0202  435 ILE B O   
7134  C CB  . ILE B 435 ? 0.3998 0.4950 0.2099 0.0068  0.0023  0.0407  435 ILE B CB  
7135  C CG1 . ILE B 435 ? 0.3475 0.4670 0.1833 0.0073  -0.0003 0.0504  435 ILE B CG1 
7136  C CG2 . ILE B 435 ? 0.4283 0.5240 0.2272 0.0101  0.0065  0.0365  435 ILE B CG2 
7137  C CD1 . ILE B 435 ? 0.3794 0.5056 0.2374 0.0137  0.0028  0.0557  435 ILE B CD1 
7138  N N   . GLY B 436 ? 0.5301 0.5880 0.2906 0.0017  0.0011  0.0221  436 GLY B N   
7139  C CA  . GLY B 436 ? 0.5613 0.6009 0.2967 0.0020  0.0023  0.0110  436 GLY B CA  
7140  C C   . GLY B 436 ? 0.5742 0.6111 0.2888 -0.0020 -0.0032 0.0034  436 GLY B C   
7141  O O   . GLY B 436 ? 0.7453 0.7658 0.4372 -0.0012 -0.0036 -0.0077 436 GLY B O   
7142  N N   . LEU B 437 ? 0.6234 0.6773 0.3467 -0.0070 -0.0082 0.0083  437 LEU B N   
7143  C CA  . LEU B 437 ? 0.5710 0.6282 0.2792 -0.0129 -0.0144 0.0017  437 LEU B CA  
7144  C C   . LEU B 437 ? 0.6533 0.7243 0.3564 -0.0139 -0.0153 0.0014  437 LEU B C   
7145  O O   . LEU B 437 ? 0.6961 0.7726 0.3893 -0.0198 -0.0209 -0.0028 437 LEU B O   
7146  C CB  . LEU B 437 ? 0.5895 0.6581 0.3110 -0.0214 -0.0199 0.0067  437 LEU B CB  
7147  C CG  . LEU B 437 ? 0.5837 0.6408 0.3073 -0.0241 -0.0206 0.0055  437 LEU B CG  
7148  C CD1 . LEU B 437 ? 0.5686 0.6407 0.3045 -0.0358 -0.0260 0.0099  437 LEU B CD1 
7149  C CD2 . LEU B 437 ? 0.7037 0.7410 0.4034 -0.0234 -0.0222 -0.0074 437 LEU B CD2 
7150  N N   . LYS B 438 ? 0.6396 0.7176 0.3502 -0.0091 -0.0102 0.0059  438 LYS B N   
7151  C CA  . LYS B 438 ? 0.7029 0.7968 0.4113 -0.0106 -0.0112 0.0074  438 LYS B CA  
7152  C C   . LYS B 438 ? 0.7703 0.8566 0.4516 -0.0115 -0.0126 -0.0044 438 LYS B C   
7153  O O   . LYS B 438 ? 0.7558 0.8510 0.4301 -0.0169 -0.0181 -0.0059 438 LYS B O   
7154  C CB  . LYS B 438 ? 0.6460 0.7484 0.3670 -0.0055 -0.0055 0.0136  438 LYS B CB  
7155  C CG  . LYS B 438 ? 0.5997 0.7158 0.3476 -0.0059 -0.0069 0.0257  438 LYS B CG  
7156  C CD  . LYS B 438 ? 0.5755 0.6970 0.3368 -0.0007 -0.0019 0.0309  438 LYS B CD  
7157  C CE  . LYS B 438 ? 0.5739 0.7090 0.3292 -0.0013 -0.0015 0.0318  438 LYS B CE  
7158  N NZ  . LYS B 438 ? 0.5540 0.7001 0.3245 0.0033  0.0030  0.0374  438 LYS B NZ  
7159  N N   . GLU B 439 ? 0.9505 1.0203 0.6168 -0.0066 -0.0081 -0.0136 439 GLU B N   
7160  C CA  . GLU B 439 ? 0.8887 0.9485 0.5288 -0.0068 -0.0096 -0.0267 439 GLU B CA  
7161  C C   . GLU B 439 ? 0.8794 0.9291 0.5074 -0.0116 -0.0179 -0.0336 439 GLU B C   
7162  O O   . GLU B 439 ? 0.8877 0.9346 0.4972 -0.0137 -0.0221 -0.0426 439 GLU B O   
7163  C CB  . GLU B 439 ? 0.9599 1.0037 0.5889 -0.0011 -0.0030 -0.0360 439 GLU B CB  
7164  C CG  . GLU B 439 ? 1.0288 1.0868 0.6709 0.0036  0.0053  -0.0310 439 GLU B CG  
7165  C CD  . GLU B 439 ? 1.0187 1.0784 0.6842 0.0063  0.0090  -0.0216 439 GLU B CD  
7166  O OE1 . GLU B 439 ? 1.0849 1.1306 0.7525 0.0052  0.0070  -0.0216 439 GLU B OE1 
7167  O OE2 . GLU B 439 ? 0.9537 1.0286 0.6353 0.0095  0.0135  -0.0143 439 GLU B OE2 
7168  N N   . LYS B 440 ? 0.8315 0.8778 0.4710 -0.0138 -0.0207 -0.0297 440 LYS B N   
7169  C CA  . LYS B 440 ? 0.8195 0.8605 0.4519 -0.0202 -0.0286 -0.0360 440 LYS B CA  
7170  C C   . LYS B 440 ? 0.8036 0.8648 0.4460 -0.0306 -0.0345 -0.0296 440 LYS B C   
7171  O O   . LYS B 440 ? 0.8782 0.9371 0.5135 -0.0389 -0.0414 -0.0356 440 LYS B O   
7172  C CB  . LYS B 440 ? 0.7842 0.8149 0.4255 -0.0201 -0.0286 -0.0350 440 LYS B CB  
7173  C CG  . LYS B 440 ? 0.8429 0.8632 0.4744 -0.0273 -0.0358 -0.0455 440 LYS B CG  
7174  C CD  . LYS B 440 ? 0.8473 0.8587 0.4893 -0.0294 -0.0349 -0.0435 440 LYS B CD  
7175  C CE  . LYS B 440 ? 0.7958 0.7937 0.4297 -0.0426 -0.0422 -0.0522 440 LYS B CE  
7176  N NZ  . LYS B 440 ? 0.8366 0.8213 0.4790 -0.0478 -0.0412 -0.0490 440 LYS B NZ  
7177  N N   . PHE B 441 ? 0.8049 0.8855 0.4640 -0.0309 -0.0325 -0.0182 441 PHE B N   
7178  C CA  . PHE B 441 ? 0.7370 0.8369 0.4065 -0.0401 -0.0384 -0.0121 441 PHE B CA  
7179  C C   . PHE B 441 ? 0.8707 0.9710 0.5206 -0.0452 -0.0441 -0.0207 441 PHE B C   
7180  O O   . PHE B 441 ? 0.8833 0.9903 0.5344 -0.0551 -0.0510 -0.0211 441 PHE B O   
7181  C CB  . PHE B 441 ? 0.6802 0.7990 0.3693 -0.0379 -0.0359 0.0001  441 PHE B CB  
7182  C CG  . PHE B 441 ? 0.7069 0.8290 0.4197 -0.0353 -0.0327 0.0096  441 PHE B CG  
7183  C CD1 . PHE B 441 ? 0.6297 0.7458 0.3489 -0.0390 -0.0342 0.0093  441 PHE B CD1 
7184  C CD2 . PHE B 441 ? 0.6578 0.7888 0.3864 -0.0297 -0.0286 0.0183  441 PHE B CD2 
7185  C CE1 . PHE B 441 ? 0.6034 0.7223 0.3439 -0.0363 -0.0312 0.0176  441 PHE B CE1 
7186  C CE2 . PHE B 441 ? 0.6391 0.7720 0.3896 -0.0270 -0.0262 0.0261  441 PHE B CE2 
7187  C CZ  . PHE B 441 ? 0.5560 0.6828 0.3123 -0.0298 -0.0273 0.0257  441 PHE B CZ  
7188  N N   . ALA B 442 ? 0.8821 0.9754 0.5139 -0.0390 -0.0412 -0.0276 442 ALA B N   
7189  C CA  . ALA B 442 ? 0.8706 0.9647 0.4834 -0.0429 -0.0463 -0.0356 442 ALA B CA  
7190  C C   . ALA B 442 ? 0.9195 0.9991 0.5184 -0.0485 -0.0532 -0.0470 442 ALA B C   
7191  O O   . ALA B 442 ? 0.9515 1.0363 0.5436 -0.0567 -0.0603 -0.0501 442 ALA B O   
7192  C CB  . ALA B 442 ? 0.8375 0.9259 0.4335 -0.0349 -0.0409 -0.0416 442 ALA B CB  
7193  N N   . THR B 443 ? 0.9370 0.9982 0.5320 -0.0448 -0.0518 -0.0534 443 THR B N   
7194  C CA  . THR B 443 ? 0.9278 0.9737 0.5109 -0.0504 -0.0587 -0.0649 443 THR B CA  
7195  C C   . THR B 443 ? 0.9457 0.9962 0.5449 -0.0629 -0.0628 -0.0588 443 THR B C   
7196  O O   . THR B 443 ? 0.9727 1.0088 0.5649 -0.0700 -0.0680 -0.0668 443 THR B O   
7197  C CB  . THR B 443 ? 0.9685 0.9917 0.5389 -0.0403 -0.0562 -0.0766 443 THR B CB  
7198  O OG1 . THR B 443 ? 0.9417 0.9643 0.5246 -0.0323 -0.0482 -0.0689 443 THR B OG1 
7199  C CG2 . THR B 443 ? 0.8762 0.8900 0.4233 -0.0315 -0.0557 -0.0882 443 THR B CG2 
7200  N N   . LEU B 444 ? 0.9464 1.0161 0.5672 -0.0663 -0.0609 -0.0450 444 LEU B N   
7201  C CA  . LEU B 444 ? 0.9669 1.0436 0.6031 -0.0788 -0.0648 -0.0389 444 LEU B CA  
7202  C C   . LEU B 444 ? 0.9043 0.9892 0.5359 -0.0912 -0.0731 -0.0412 444 LEU B C   
7203  O O   . LEU B 444 ? 0.8563 0.9523 0.4829 -0.0900 -0.0749 -0.0407 444 LEU B O   
7204  C CB  . LEU B 444 ? 0.8925 0.9880 0.5542 -0.0770 -0.0605 -0.0245 444 LEU B CB  
7205  C CG  . LEU B 444 ? 0.7950 0.8832 0.4649 -0.0660 -0.0526 -0.0205 444 LEU B CG  
7206  C CD1 . LEU B 444 ? 0.7130 0.8180 0.4097 -0.0671 -0.0503 -0.0073 444 LEU B CD1 
7207  C CD2 . LEU B 444 ? 0.7930 0.8575 0.4518 -0.0660 -0.0522 -0.0293 444 LEU B CD2 
7208  N N   . LYS B 445 ? 0.9127 0.9917 0.5459 -0.1039 -0.0782 -0.0432 445 LYS B N   
7209  C CA  . LYS B 445 ? 1.0068 1.0912 0.6356 -0.1171 -0.0865 -0.0457 445 LYS B CA  
7210  C C   . LYS B 445 ? 0.9329 1.0389 0.5846 -0.1275 -0.0883 -0.0345 445 LYS B C   
7211  O O   . LYS B 445 ? 0.9309 1.0402 0.5984 -0.1280 -0.0843 -0.0276 445 LYS B O   
7212  C CB  . LYS B 445 ? 1.0519 1.1116 0.6640 -0.1251 -0.0918 -0.0574 445 LYS B CB  
7213  C CG  . LYS B 445 ? 1.1555 1.1944 0.7452 -0.1142 -0.0912 -0.0705 445 LYS B CG  
7214  C CD  . LYS B 445 ? 1.2893 1.3013 0.8656 -0.1215 -0.0965 -0.0815 445 LYS B CD  
7215  C CE  . LYS B 445 ? 1.3246 1.3182 0.8799 -0.1097 -0.0969 -0.0961 445 LYS B CE  
7216  N NZ  . LYS B 445 ? 1.3368 1.3394 0.8794 -0.1067 -0.1004 -0.1012 445 LYS B NZ  
7217  N N   . GLY B 446 ? 0.9639 1.0851 0.6170 -0.1355 -0.0944 -0.0330 446 GLY B N   
7218  C CA  . GLY B 446 ? 0.8977 1.0410 0.5718 -0.1453 -0.0971 -0.0237 446 GLY B CA  
7219  C C   . GLY B 446 ? 1.0417 1.1779 0.7201 -0.1586 -0.0992 -0.0247 446 GLY B C   
7220  O O   . GLY B 446 ? 1.0448 1.1562 0.7082 -0.1611 -0.0996 -0.0328 446 GLY B O   
7221  N N   . LEU B 447 ? 1.0868 1.2443 0.7857 -0.1672 -0.1007 -0.0164 447 LEU B N   
7222  C CA  . LEU B 447 ? 1.0561 1.2105 0.7611 -0.1808 -0.1020 -0.0159 447 LEU B CA  
7223  C C   . LEU B 447 ? 1.0206 1.1882 0.7281 -0.1953 -0.1096 -0.0161 447 LEU B C   
7224  O O   . LEU B 447 ? 0.9527 1.1397 0.6659 -0.1938 -0.1130 -0.0132 447 LEU B O   
7225  C CB  . LEU B 447 ? 0.9902 1.1592 0.7184 -0.1785 -0.0961 -0.0063 447 LEU B CB  
7226  C CG  . LEU B 447 ? 0.9741 1.1292 0.7012 -0.1651 -0.0885 -0.0055 447 LEU B CG  
7227  C CD1 . LEU B 447 ? 0.8382 1.0111 0.5899 -0.1613 -0.0833 0.0047  447 LEU B CD1 
7228  C CD2 . LEU B 447 ? 0.9932 1.1164 0.7019 -0.1690 -0.0880 -0.0136 447 LEU B CD2 
7229  N N   . GLU B 448 ? 0.9039 1.0603 0.6071 -0.2095 -0.1124 -0.0193 448 GLU B N   
7230  C CA  . GLU B 448 ? 0.9568 1.1224 0.6604 -0.2243 -0.1198 -0.0203 448 GLU B CA  
7231  C C   . GLU B 448 ? 0.8691 1.0425 0.5870 -0.2378 -0.1186 -0.0155 448 GLU B C   
7232  O O   . GLU B 448 ? 0.8178 0.9762 0.5347 -0.2390 -0.1141 -0.0152 448 GLU B O   
7233  C CB  . GLU B 448 ? 0.9700 1.1093 0.6478 -0.2294 -0.1260 -0.0312 448 GLU B CB  
7234  C CG  . GLU B 448 ? 0.9829 1.1314 0.6587 -0.2423 -0.1344 -0.0330 448 GLU B CG  
7235  C CD  . GLU B 448 ? 1.1123 1.2333 0.7621 -0.2455 -0.1406 -0.0442 448 GLU B CD  
7236  O OE1 . GLU B 448 ? 1.0936 1.1883 0.7277 -0.2377 -0.1382 -0.0509 448 GLU B OE1 
7237  O OE2 . GLU B 448 ? 1.2232 1.3488 0.8684 -0.2552 -0.1481 -0.0466 448 GLU B OE2 
7238  N N   . PHE B 449 ? 0.8317 1.0290 0.5625 -0.2477 -0.1228 -0.0118 449 PHE B N   
7239  C CA  . PHE B 449 ? 0.8136 1.0234 0.5594 -0.2602 -0.1212 -0.0069 449 PHE B CA  
7240  C C   . PHE B 449 ? 0.8955 1.0792 0.6251 -0.2750 -0.1238 -0.0122 449 PHE B C   
7241  O O   . PHE B 449 ? 0.9185 1.0844 0.6295 -0.2801 -0.1302 -0.0192 449 PHE B O   
7242  C CB  . PHE B 449 ? 0.7880 1.0306 0.5515 -0.2660 -0.1251 -0.0024 449 PHE B CB  
7243  C CG  . PHE B 449 ? 0.6991 0.9695 0.4840 -0.2533 -0.1220 0.0048  449 PHE B CG  
7244  C CD1 . PHE B 449 ? 0.7297 1.0151 0.5342 -0.2504 -0.1155 0.0113  449 PHE B CD1 
7245  C CD2 . PHE B 449 ? 0.6472 0.9275 0.4321 -0.2442 -0.1259 0.0053  449 PHE B CD2 
7246  C CE1 . PHE B 449 ? 0.7476 1.0565 0.5717 -0.2378 -0.1132 0.0178  449 PHE B CE1 
7247  C CE2 . PHE B 449 ? 0.6799 0.9830 0.4840 -0.2325 -0.1237 0.0122  449 PHE B CE2 
7248  C CZ  . PHE B 449 ? 0.7410 1.0580 0.5650 -0.2289 -0.1175 0.0184  449 PHE B CZ  
7249  N N   . GLU B 450 ? 0.8684 1.0494 0.6049 -0.2817 -0.1189 -0.0085 450 GLU B N   
7250  C CA  . GLU B 450 ? 0.8574 1.0208 0.5840 -0.2985 -0.1211 -0.0105 450 GLU B CA  
7251  C C   . GLU B 450 ? 0.8366 1.0284 0.5823 -0.3110 -0.1199 -0.0040 450 GLU B C   
7252  O O   . GLU B 450 ? 0.9935 1.1821 0.7334 -0.3262 -0.1245 -0.0053 450 GLU B O   
7253  C CB  . GLU B 450 ? 0.8924 1.0251 0.6080 -0.2970 -0.1165 -0.0118 450 GLU B CB  
7254  C CG  . GLU B 450 ? 1.0537 1.1556 0.7505 -0.3116 -0.1208 -0.0160 450 GLU B CG  
7255  C CD  . GLU B 450 ? 1.2038 1.2738 0.8897 -0.3091 -0.1168 -0.0169 450 GLU B CD  
7256  O OE1 . GLU B 450 ? 1.1840 1.2636 0.8828 -0.3032 -0.1095 -0.0114 450 GLU B OE1 
7257  O OE2 . GLU B 450 ? 1.2544 1.2893 0.9190 -0.3126 -0.1213 -0.0233 450 GLU B OE2 
7258  N N   . TYR B 451 ? 0.7606 0.9802 0.5288 -0.3042 -0.1138 0.0028  451 TYR B N   
7259  C CA  . TYR B 451 ? 0.8168 1.0696 0.6060 -0.3117 -0.1123 0.0083  451 TYR B CA  
7260  C C   . TYR B 451 ? 0.7541 1.0385 0.5650 -0.2971 -0.1104 0.0128  451 TYR B C   
7261  O O   . TYR B 451 ? 0.7141 0.9968 0.5296 -0.2833 -0.1056 0.0151  451 TYR B O   
7262  C CB  . TYR B 451 ? 0.7656 1.0169 0.5597 -0.3195 -0.1056 0.0122  451 TYR B CB  
7263  C CG  . TYR B 451 ? 0.8074 1.0972 0.6274 -0.3187 -0.1011 0.0181  451 TYR B CG  
7264  C CD1 . TYR B 451 ? 0.8559 1.1680 0.6845 -0.3298 -0.1042 0.0186  451 TYR B CD1 
7265  C CD2 . TYR B 451 ? 0.7785 1.0818 0.6143 -0.3058 -0.0941 0.0226  451 TYR B CD2 
7266  C CE1 . TYR B 451 ? 0.8208 1.1676 0.6729 -0.3271 -0.1002 0.0227  451 TYR B CE1 
7267  C CE2 . TYR B 451 ? 0.7575 1.0945 0.6164 -0.3029 -0.0904 0.0269  451 TYR B CE2 
7268  C CZ  . TYR B 451 ? 0.8327 1.1913 0.6996 -0.3131 -0.0934 0.0265  451 TYR B CZ  
7269  O OH  . TYR B 451 ? 0.7408 1.1318 0.6304 -0.3086 -0.0898 0.0294  451 TYR B OH  
7270  N N   . GLU B 452 ? 0.6756 0.9877 0.4998 -0.2997 -0.1144 0.0141  452 GLU B N   
7271  C CA  . GLU B 452 ? 0.7013 1.0414 0.5455 -0.2856 -0.1141 0.0182  452 GLU B CA  
7272  C C   . GLU B 452 ? 0.6993 1.0722 0.5656 -0.2899 -0.1135 0.0216  452 GLU B C   
7273  O O   . GLU B 452 ? 0.6953 1.0768 0.5611 -0.3017 -0.1189 0.0195  452 GLU B O   
7274  C CB  . GLU B 452 ? 0.7493 1.0877 0.5855 -0.2798 -0.1214 0.0154  452 GLU B CB  
7275  C CG  . GLU B 452 ? 0.7003 1.0620 0.5543 -0.2641 -0.1215 0.0201  452 GLU B CG  
7276  C CD  . GLU B 452 ? 0.7155 1.0742 0.5598 -0.2589 -0.1286 0.0177  452 GLU B CD  
7277  O OE1 . GLU B 452 ? 0.7513 1.0971 0.5788 -0.2691 -0.1346 0.0122  452 GLU B OE1 
7278  O OE2 . GLU B 452 ? 0.7359 1.1042 0.5886 -0.2447 -0.1284 0.0213  452 GLU B OE2 
7279  N N   . PRO B 453 ? 0.6804 1.0721 0.5663 -0.2800 -0.1074 0.0263  453 PRO B N   
7280  C CA  . PRO B 453 ? 0.6997 1.1230 0.6074 -0.2810 -0.1069 0.0283  453 PRO B CA  
7281  C C   . PRO B 453 ? 0.6500 1.0943 0.5717 -0.2697 -0.1126 0.0294  453 PRO B C   
7282  O O   . PRO B 453 ? 0.6126 1.0487 0.5299 -0.2582 -0.1146 0.0303  453 PRO B O   
7283  C CB  . PRO B 453 ? 0.6902 1.1190 0.6097 -0.2733 -0.0979 0.0320  453 PRO B CB  
7284  C CG  . PRO B 453 ? 0.6307 1.0412 0.5432 -0.2605 -0.0956 0.0336  453 PRO B CG  
7285  C CD  . PRO B 453 ? 0.6312 1.0142 0.5195 -0.2673 -0.1005 0.0294  453 PRO B CD  
7286  N N   . PRO B 454 ? 0.6225 1.0931 0.5608 -0.2725 -0.1154 0.0292  454 PRO B N   
7287  C CA  . PRO B 454 ? 0.5745 1.0622 0.5243 -0.2631 -0.1226 0.0296  454 PRO B CA  
7288  C C   . PRO B 454 ? 0.5880 1.0836 0.5528 -0.2432 -0.1203 0.0336  454 PRO B C   
7289  O O   . PRO B 454 ? 0.6890 1.1835 0.6531 -0.2336 -0.1258 0.0348  454 PRO B O   
7290  C CB  . PRO B 454 ? 0.5963 1.1094 0.5608 -0.2720 -0.1257 0.0277  454 PRO B CB  
7291  C CG  . PRO B 454 ? 0.5870 1.0907 0.5401 -0.2899 -0.1220 0.0257  454 PRO B CG  
7292  C CD  . PRO B 454 ? 0.6298 1.1136 0.5742 -0.2862 -0.1136 0.0277  454 PRO B CD  
7293  N N   . VAL B 455 ? 0.5349 1.0371 0.5122 -0.2366 -0.1128 0.0358  455 VAL B N   
7294  C CA  . VAL B 455 ? 0.5064 1.0160 0.4992 -0.2175 -0.1110 0.0394  455 VAL B CA  
7295  C C   . VAL B 455 ? 0.6537 1.1462 0.6406 -0.2112 -0.1025 0.0423  455 VAL B C   
7296  O O   . VAL B 455 ? 0.6007 1.0846 0.5798 -0.2210 -0.0967 0.0413  455 VAL B O   
7297  C CB  . VAL B 455 ? 0.5697 1.1057 0.5868 -0.2127 -0.1110 0.0386  455 VAL B CB  
7298  C CG1 . VAL B 455 ? 0.5620 1.1026 0.5944 -0.1925 -0.1115 0.0416  455 VAL B CG1 
7299  C CG2 . VAL B 455 ? 0.4405 0.9941 0.4633 -0.2219 -0.1191 0.0351  455 VAL B CG2 
7300  N N   . LEU B 456 ? 0.6940 1.1804 0.6841 -0.1952 -0.1020 0.0460  456 LEU B N   
7301  C CA  . LEU B 456 ? 0.6158 1.0878 0.6034 -0.1865 -0.0944 0.0493  456 LEU B CA  
7302  C C   . LEU B 456 ? 0.6046 1.0539 0.5710 -0.1974 -0.0910 0.0478  456 LEU B C   
7303  O O   . LEU B 456 ? 0.6764 1.1175 0.6404 -0.1996 -0.0842 0.0485  456 LEU B O   
7304  C CB  . LEU B 456 ? 0.6749 1.1589 0.6789 -0.1813 -0.0883 0.0501  456 LEU B CB  
7305  C CG  . LEU B 456 ? 0.6389 1.1401 0.6645 -0.1669 -0.0908 0.0509  456 LEU B CG  
7306  C CD1 . LEU B 456 ? 0.5455 1.0567 0.5844 -0.1641 -0.0846 0.0500  456 LEU B CD1 
7307  C CD2 . LEU B 456 ? 0.6569 1.1467 0.6832 -0.1505 -0.0920 0.0553  456 LEU B CD2 
7308  N N   . ARG B 457 ? 0.5343 0.9718 0.4844 -0.2040 -0.0964 0.0452  457 ARG B N   
7309  C CA  . ARG B 457 ? 0.5396 0.9534 0.4682 -0.2157 -0.0950 0.0419  457 ARG B CA  
7310  C C   . ARG B 457 ? 0.5542 0.9486 0.4764 -0.2076 -0.0887 0.0439  457 ARG B C   
7311  O O   . ARG B 457 ? 0.5954 0.9707 0.5039 -0.2164 -0.0857 0.0415  457 ARG B O   
7312  C CB  . ARG B 457 ? 0.6012 1.0042 0.5129 -0.2213 -0.1025 0.0380  457 ARG B CB  
7313  C CG  . ARG B 457 ? 0.5973 0.9949 0.5060 -0.2071 -0.1048 0.0399  457 ARG B CG  
7314  C CD  . ARG B 457 ? 0.5401 0.9288 0.4320 -0.2120 -0.1123 0.0357  457 ARG B CD  
7315  N NE  . ARG B 457 ? 0.5987 0.9779 0.4842 -0.1986 -0.1127 0.0374  457 ARG B NE  
7316  C CZ  . ARG B 457 ? 0.6985 1.0685 0.5684 -0.1986 -0.1182 0.0343  457 ARG B CZ  
7317  N NH1 . ARG B 457 ? 0.7019 1.0706 0.5612 -0.2109 -0.1246 0.0293  457 ARG B NH1 
7318  N NH2 . ARG B 457 ? 0.6225 0.9841 0.4868 -0.1862 -0.1172 0.0363  457 ARG B NH2 
7319  N N   . HIS B 458 ? 0.5270 0.9247 0.4589 -0.1909 -0.0868 0.0484  458 HIS B N   
7320  C CA  . HIS B 458 ? 0.5080 0.8866 0.4334 -0.1824 -0.0814 0.0503  458 HIS B CA  
7321  C C   . HIS B 458 ? 0.4563 0.8318 0.3860 -0.1851 -0.0743 0.0516  458 HIS B C   
7322  O O   . HIS B 458 ? 0.4690 0.8237 0.3882 -0.1839 -0.0706 0.0512  458 HIS B O   
7323  C CB  . HIS B 458 ? 0.5048 0.8875 0.4403 -0.1642 -0.0810 0.0553  458 HIS B CB  
7324  C CG  . HIS B 458 ? 0.4918 0.8949 0.4495 -0.1553 -0.0798 0.0595  458 HIS B CG  
7325  N ND1 . HIS B 458 ? 0.5623 0.9851 0.5307 -0.1573 -0.0852 0.0586  458 HIS B ND1 
7326  C CD2 . HIS B 458 ? 0.5442 0.9490 0.5147 -0.1434 -0.0743 0.0637  458 HIS B CD2 
7327  C CE1 . HIS B 458 ? 0.5334 0.9681 0.5198 -0.1465 -0.0833 0.0615  458 HIS B CE1 
7328  N NE2 . HIS B 458 ? 0.5476 0.9712 0.5351 -0.1381 -0.0766 0.0647  458 HIS B NE2 
7329  N N   . PHE B 459 ? 0.4472 0.8416 0.3910 -0.1883 -0.0724 0.0526  459 PHE B N   
7330  C CA  . PHE B 459 ? 0.4864 0.8776 0.4326 -0.1910 -0.0655 0.0538  459 PHE B CA  
7331  C C   . PHE B 459 ? 0.4725 0.8461 0.4007 -0.2092 -0.0651 0.0497  459 PHE B C   
7332  O O   . PHE B 459 ? 0.4706 0.8274 0.3916 -0.2113 -0.0604 0.0502  459 PHE B O   
7333  C CB  . PHE B 459 ? 0.4062 0.8215 0.3714 -0.1878 -0.0637 0.0550  459 PHE B CB  
7334  C CG  . PHE B 459 ? 0.3908 0.8160 0.3728 -0.1684 -0.0628 0.0590  459 PHE B CG  
7335  C CD1 . PHE B 459 ? 0.3787 0.7926 0.3625 -0.1568 -0.0575 0.0629  459 PHE B CD1 
7336  C CD2 . PHE B 459 ? 0.4824 0.9260 0.4782 -0.1621 -0.0677 0.0586  459 PHE B CD2 
7337  C CE1 . PHE B 459 ? 0.4167 0.8357 0.4145 -0.1393 -0.0569 0.0664  459 PHE B CE1 
7338  C CE2 . PHE B 459 ? 0.4283 0.8762 0.4380 -0.1446 -0.0677 0.0618  459 PHE B CE2 
7339  C CZ  . PHE B 459 ? 0.3487 0.7834 0.3589 -0.1334 -0.0621 0.0656  459 PHE B CZ  
7340  N N   . THR B 460 ? 0.5000 0.8749 0.4201 -0.2225 -0.0704 0.0456  460 THR B N   
7341  C CA  . THR B 460 ? 0.5148 0.8741 0.4194 -0.2406 -0.0702 0.0421  460 THR B CA  
7342  C C   . THR B 460 ? 0.5452 0.8860 0.4300 -0.2514 -0.0768 0.0369  460 THR B C   
7343  O O   . THR B 460 ? 0.5829 0.9086 0.4541 -0.2668 -0.0775 0.0339  460 THR B O   
7344  C CB  . THR B 460 ? 0.5503 0.9315 0.4661 -0.2492 -0.0687 0.0422  460 THR B CB  
7345  O OG1 . THR B 460 ? 0.5393 0.9460 0.4694 -0.2450 -0.0734 0.0420  460 THR B OG1 
7346  C CG2 . THR B 460 ? 0.4682 0.8578 0.3963 -0.2416 -0.0613 0.0455  460 THR B CG2 
7347  N N   . ALA B 461 ? 0.5583 0.8980 0.4398 -0.2437 -0.0819 0.0355  461 ALA B N   
7348  C CA  . ALA B 461 ? 0.5631 0.8835 0.4240 -0.2529 -0.0883 0.0297  461 ALA B CA  
7349  C C   . ALA B 461 ? 0.6256 0.9094 0.4646 -0.2545 -0.0869 0.0258  461 ALA B C   
7350  O O   . ALA B 461 ? 0.6162 0.8903 0.4560 -0.2440 -0.0820 0.0278  461 ALA B O   
7351  C CB  . ALA B 461 ? 0.6649 0.9928 0.5262 -0.2434 -0.0939 0.0289  461 ALA B CB  
7352  N N   . ARG B 462 ? 0.6001 0.8622 0.4193 -0.2668 -0.0916 0.0201  462 ARG B N   
7353  C CA  . ARG B 462 ? 0.6985 0.9223 0.4942 -0.2668 -0.0920 0.0147  462 ARG B CA  
7354  C C   . ARG B 462 ? 0.6932 0.9051 0.4741 -0.2602 -0.0977 0.0089  462 ARG B C   
7355  O O   . ARG B 462 ? 0.7337 0.9613 0.5173 -0.2630 -0.1031 0.0081  462 ARG B O   
7356  C CB  . ARG B 462 ? 0.7202 0.9222 0.5016 -0.2843 -0.0932 0.0120  462 ARG B CB  
7357  C CG  . ARG B 462 ? 0.6754 0.8875 0.4686 -0.2917 -0.0870 0.0176  462 ARG B CG  
7358  C CD  . ARG B 462 ? 0.6427 0.8290 0.4187 -0.3086 -0.0884 0.0156  462 ARG B CD  
7359  N NE  . ARG B 462 ? 0.6637 0.8080 0.4175 -0.3058 -0.0895 0.0108  462 ARG B NE  
7360  C CZ  . ARG B 462 ? 0.6892 0.8159 0.4402 -0.3007 -0.0843 0.0124  462 ARG B CZ  
7361  N NH1 . ARG B 462 ? 0.6578 0.8047 0.4260 -0.2984 -0.0775 0.0188  462 ARG B NH1 
7362  N NH2 . ARG B 462 ? 0.7352 0.8228 0.4654 -0.2970 -0.0862 0.0071  462 ARG B NH2 
7363  N N   . LEU B 463 ? 0.6636 0.8480 0.4285 -0.2506 -0.0964 0.0047  463 LEU B N   
7364  C CA  . LEU B 463 ? 0.7175 0.8907 0.4676 -0.2417 -0.1004 -0.0012 463 LEU B CA  
7365  C C   . LEU B 463 ? 0.8072 0.9406 0.5318 -0.2418 -0.1016 -0.0095 463 LEU B C   
7366  O O   . LEU B 463 ? 0.8292 0.9427 0.5484 -0.2477 -0.0993 -0.0099 463 LEU B O   
7367  C CB  . LEU B 463 ? 0.7666 0.9537 0.5269 -0.2231 -0.0966 0.0028  463 LEU B CB  
7368  C CG  . LEU B 463 ? 0.7424 0.9641 0.5223 -0.2187 -0.0982 0.0088  463 LEU B CG  
7369  C CD1 . LEU B 463 ? 0.6873 0.9356 0.4923 -0.2218 -0.0948 0.0167  463 LEU B CD1 
7370  C CD2 . LEU B 463 ? 0.8023 1.0259 0.5826 -0.2009 -0.0961 0.0105  463 LEU B CD2 
7371  N N   . LYS B 464 ? 0.8869 1.0080 0.5952 -0.2346 -0.1053 -0.0165 464 LYS B N   
7372  C CA  . LYS B 464 ? 0.9130 0.9974 0.5972 -0.2308 -0.1066 -0.0257 464 LYS B CA  
7373  C C   . LYS B 464 ? 0.9557 1.0388 0.6297 -0.2158 -0.1073 -0.0309 464 LYS B C   
7374  O O   . LYS B 464 ? 0.8914 0.9975 0.5721 -0.2139 -0.1096 -0.0285 464 LYS B O   
7375  C CB  . LYS B 464 ? 0.8947 0.9586 0.5636 -0.2468 -0.1136 -0.0316 464 LYS B CB  
7376  C CG  . LYS B 464 ? 1.0054 1.0841 0.6728 -0.2544 -0.1208 -0.0335 464 LYS B CG  
7377  C CD  . LYS B 464 ? 0.9398 0.9968 0.5922 -0.2701 -0.1279 -0.0390 464 LYS B CD  
7378  C CE  . LYS B 464 ? 0.9257 0.9950 0.5745 -0.2761 -0.1355 -0.0418 464 LYS B CE  
7379  N NZ  . LYS B 464 ? 0.9023 0.9485 0.5350 -0.2904 -0.1430 -0.0475 464 LYS B NZ  
7380  N N   . PRO B 465 ? 1.0533 1.1108 0.7114 -0.2046 -0.1051 -0.0377 465 PRO B N   
7381  C CA  . PRO B 465 ? 1.1128 1.1701 0.7602 -0.1902 -0.1049 -0.0431 465 PRO B CA  
7382  C C   . PRO B 465 ? 1.0968 1.1418 0.7248 -0.1951 -0.1129 -0.0530 465 PRO B C   
7383  O O   . PRO B 465 ? 1.0983 1.1232 0.7156 -0.2066 -0.1181 -0.0584 465 PRO B O   
7384  C CB  . PRO B 465 ? 1.0715 1.1067 0.7105 -0.1767 -0.0992 -0.0471 465 PRO B CB  
7385  C CG  . PRO B 465 ? 1.0330 1.0438 0.6672 -0.1872 -0.1004 -0.0490 465 PRO B CG  
7386  C CD  . PRO B 465 ? 1.0368 1.0664 0.6877 -0.2034 -0.1019 -0.0402 465 PRO B CD  
7387  N N   . ILE B 466 ? 1.1671 1.2239 0.7905 -0.1863 -0.1138 -0.0551 466 ILE B N   
7388  C CA  . ILE B 466 ? 1.1019 1.1515 0.7079 -0.1900 -0.1214 -0.0640 466 ILE B CA  
7389  C C   . ILE B 466 ? 1.0987 1.1192 0.6819 -0.1805 -0.1220 -0.0768 466 ILE B C   
7390  O O   . ILE B 466 ? 1.1136 1.1278 0.6949 -0.1665 -0.1155 -0.0783 466 ILE B O   
7391  C CB  . ILE B 466 ? 0.9871 1.0623 0.5975 -0.1854 -0.1226 -0.0602 466 ILE B CB  
7392  C CG1 . ILE B 466 ? 0.9553 1.0601 0.5904 -0.1931 -0.1224 -0.0479 466 ILE B CG1 
7393  C CG2 . ILE B 466 ? 1.0159 1.0842 0.6083 -0.1902 -0.1310 -0.0693 466 ILE B CG2 
7394  C CD1 . ILE B 466 ? 0.9279 1.0576 0.5699 -0.1881 -0.1236 -0.0429 466 ILE B CD1 
7395  N N   . ALA C 2   ? 0.2816 0.7690 0.2818 0.1263  0.0457  -0.0494 2   ALA C N   
7396  C CA  . ALA C 2   ? 0.2622 0.7249 0.2635 0.1256  0.0436  -0.0469 2   ALA C CA  
7397  C C   . ALA C 2   ? 0.3050 0.7623 0.3143 0.1242  0.0385  -0.0555 2   ALA C C   
7398  O O   . ALA C 2   ? 0.2958 0.7616 0.3110 0.1174  0.0432  -0.0565 2   ALA C O   
7399  C CB  . ALA C 2   ? 0.2623 0.7107 0.2625 0.1161  0.0554  -0.0324 2   ALA C CB  
7400  N N   . LYS C 3   ? 0.2466 0.6895 0.2561 0.1303  0.0290  -0.0615 3   LYS C N   
7401  C CA  . LYS C 3   ? 0.2403 0.6778 0.2565 0.1306  0.0226  -0.0702 3   LYS C CA  
7402  C C   . LYS C 3   ? 0.2695 0.6839 0.2889 0.1261  0.0237  -0.0650 3   LYS C C   
7403  O O   . LYS C 3   ? 0.2363 0.6358 0.2515 0.1293  0.0213  -0.0616 3   LYS C O   
7404  C CB  . LYS C 3   ? 0.2776 0.7171 0.2915 0.1417  0.0095  -0.0833 3   LYS C CB  
7405  C CG  . LYS C 3   ? 0.3965 0.8275 0.4163 0.1425  0.0026  -0.0914 3   LYS C CG  
7406  C CD  . LYS C 3   ? 0.4795 0.9058 0.4958 0.1529  -0.0099 -0.1036 3   LYS C CD  
7407  C CE  . LYS C 3   ? 0.5707 0.9870 0.5926 0.1535  -0.0160 -0.1105 3   LYS C CE  
7408  N NZ  . LYS C 3   ? 0.5050 0.9399 0.5325 0.1505  -0.0135 -0.1141 3   LYS C NZ  
7409  N N   . ARG C 4   ? 0.2253 0.6378 0.2522 0.1186  0.0272  -0.0648 4   ARG C N   
7410  C CA  A ARG C 4   ? 0.2277 0.6206 0.2587 0.1141  0.0278  -0.0610 4   ARG C CA  
7411  C CA  B ARG C 4   ? 0.2276 0.6205 0.2586 0.1141  0.0278  -0.0611 4   ARG C CA  
7412  C C   . ARG C 4   ? 0.2356 0.6191 0.2687 0.1212  0.0155  -0.0706 4   ARG C C   
7413  O O   . ARG C 4   ? 0.2257 0.6193 0.2606 0.1254  0.0091  -0.0802 4   ARG C O   
7414  C CB  A ARG C 4   ? 0.2127 0.6082 0.2509 0.1024  0.0368  -0.0571 4   ARG C CB  
7415  C CB  B ARG C 4   ? 0.2128 0.6083 0.2509 0.1024  0.0368  -0.0572 4   ARG C CB  
7416  C CG  A ARG C 4   ? 0.2203 0.6240 0.2568 0.0939  0.0494  -0.0484 4   ARG C CG  
7417  C CG  B ARG C 4   ? 0.2199 0.6219 0.2561 0.0938  0.0496  -0.0477 4   ARG C CG  
7418  C CD  A ARG C 4   ? 0.2195 0.6254 0.2634 0.0821  0.0570  -0.0470 4   ARG C CD  
7419  C CD  B ARG C 4   ? 0.2177 0.6165 0.2609 0.0812  0.0582  -0.0441 4   ARG C CD  
7420  N NE  A ARG C 4   ? 0.2273 0.6325 0.2696 0.0719  0.0702  -0.0367 4   ARG C NE  
7421  N NE  B ARG C 4   ? 0.2227 0.6121 0.2632 0.0720  0.0706  -0.0320 4   ARG C NE  
7422  C CZ  A ARG C 4   ? 0.2369 0.6580 0.2800 0.0667  0.0765  -0.0363 4   ARG C CZ  
7423  C CZ  B ARG C 4   ? 0.2197 0.5949 0.2639 0.0619  0.0777  -0.0264 4   ARG C CZ  
7424  N NH1 A ARG C 4   ? 0.2391 0.6802 0.2850 0.0708  0.0708  -0.0459 4   ARG C NH1 
7425  N NH1 B ARG C 4   ? 0.2105 0.5805 0.2616 0.0597  0.0736  -0.0314 4   ARG C NH1 
7426  N NH2 A ARG C 4   ? 0.2456 0.6619 0.2866 0.0573  0.0886  -0.0261 4   ARG C NH2 
7427  N NH2 B ARG C 4   ? 0.2272 0.5929 0.2681 0.0539  0.0890  -0.0156 4   ARG C NH2 
7428  N N   . ILE C 5   ? 0.2484 0.6117 0.2810 0.1222  0.0123  -0.0677 5   ILE C N   
7429  C CA  . ILE C 5   ? 0.2047 0.5541 0.2394 0.1271  0.0015  -0.0748 5   ILE C CA  
7430  C C   . ILE C 5   ? 0.2334 0.5701 0.2747 0.1198  0.0044  -0.0697 5   ILE C C   
7431  O O   . ILE C 5   ? 0.2401 0.5685 0.2812 0.1146  0.0114  -0.0605 5   ILE C O   
7432  C CB  . ILE C 5   ? 0.2336 0.5691 0.2616 0.1348  -0.0063 -0.0767 5   ILE C CB  
7433  C CG1 . ILE C 5   ? 0.2759 0.6248 0.2976 0.1425  -0.0105 -0.0841 5   ILE C CG1 
7434  C CG2 . ILE C 5   ? 0.2412 0.5572 0.2716 0.1375  -0.0160 -0.0818 5   ILE C CG2 
7435  C CD1 . ILE C 5   ? 0.3020 0.6627 0.3179 0.1424  -0.0035 -0.0776 5   ILE C CD1 
7436  N N   . VAL C 6   ? 0.1891 0.5246 0.2360 0.1198  -0.0012 -0.0757 6   VAL C N   
7437  C CA  . VAL C 6   ? 0.1861 0.5142 0.2400 0.1124  0.0015  -0.0720 6   VAL C CA  
7438  C C   . VAL C 6   ? 0.2148 0.5203 0.2682 0.1137  -0.0032 -0.0682 6   VAL C C   
7439  O O   . VAL C 6   ? 0.2030 0.4965 0.2517 0.1208  -0.0117 -0.0714 6   VAL C O   
7440  C CB  . VAL C 6   ? 0.2308 0.5663 0.2899 0.1129  -0.0037 -0.0797 6   VAL C CB  
7441  C CG1 . VAL C 6   ? 0.2097 0.5319 0.2666 0.1218  -0.0163 -0.0867 6   VAL C CG1 
7442  C CG2 . VAL C 6   ? 0.1833 0.5180 0.2501 0.1036  0.0010  -0.0761 6   VAL C CG2 
7443  N N   . GLU C 7   ? 0.1854 0.4847 0.2436 0.1060  0.0027  -0.0615 7   GLU C N   
7444  C CA  . GLU C 7   ? 0.1931 0.4723 0.2519 0.1062  -0.0016 -0.0576 7   GLU C CA  
7445  C C   . GLU C 7   ? 0.1640 0.4326 0.2245 0.1105  -0.0137 -0.0638 7   GLU C C   
7446  O O   . GLU C 7   ? 0.1760 0.4527 0.2412 0.1089  -0.0154 -0.0681 7   GLU C O   
7447  C CB  . GLU C 7   ? 0.1777 0.4548 0.2418 0.0965  0.0074  -0.0505 7   GLU C CB  
7448  C CG  . GLU C 7   ? 0.1536 0.4319 0.2141 0.0916  0.0197  -0.0421 7   GLU C CG  
7449  C CD  . GLU C 7   ? 0.1901 0.4851 0.2499 0.0861  0.0291  -0.0417 7   GLU C CD  
7450  O OE1 . GLU C 7   ? 0.1854 0.4933 0.2491 0.0853  0.0269  -0.0484 7   GLU C OE1 
7451  O OE2 . GLU C 7   ? 0.2251 0.5195 0.2803 0.0824  0.0387  -0.0342 7   GLU C OE2 
7452  N N   . PRO C 8   ? 0.1872 0.4370 0.2437 0.1152  -0.0220 -0.0639 8   PRO C N   
7453  C CA  . PRO C 8   ? 0.1871 0.4226 0.2449 0.1173  -0.0323 -0.0677 8   PRO C CA  
7454  C C   . PRO C 8   ? 0.2369 0.4606 0.2994 0.1114  -0.0328 -0.0616 8   PRO C C   
7455  O O   . PRO C 8   ? 0.2527 0.4572 0.3141 0.1119  -0.0403 -0.0603 8   PRO C O   
7456  C CB  . PRO C 8   ? 0.1806 0.4013 0.2317 0.1233  -0.0392 -0.0701 8   PRO C CB  
7457  C CG  . PRO C 8   ? 0.2134 0.4335 0.2609 0.1220  -0.0332 -0.0638 8   PRO C CG  
7458  C CD  . PRO C 8   ? 0.2257 0.4668 0.2755 0.1185  -0.0222 -0.0608 8   PRO C CD  
7459  N N   . PHE C 9   ? 0.1750 0.4108 0.2429 0.1048  -0.0242 -0.0578 9   PHE C N   
7460  C CA  . PHE C 9   ? 0.1703 0.3995 0.2435 0.0983  -0.0230 -0.0526 9   PHE C CA  
7461  C C   . PHE C 9   ? 0.1548 0.4033 0.2343 0.0907  -0.0123 -0.0523 9   PHE C C   
7462  O O   . PHE C 9   ? 0.1421 0.4061 0.2210 0.0901  -0.0059 -0.0547 9   PHE C O   
7463  C CB  . PHE C 9   ? 0.1633 0.3779 0.2339 0.0973  -0.0215 -0.0453 9   PHE C CB  
7464  C CG  . PHE C 9   ? 0.1393 0.3599 0.2058 0.0971  -0.0118 -0.0415 9   PHE C CG  
7465  C CD1 . PHE C 9   ? 0.1510 0.3754 0.2169 0.0871  0.0008  -0.0363 9   PHE C CD1 
7466  C CD2 . PHE C 9   ? 0.1678 0.3837 0.2275 0.1039  -0.0150 -0.0422 9   PHE C CD2 
7467  C CE1 . PHE C 9   ? 0.1422 0.3693 0.2028 0.0862  0.0100  -0.0314 9   PHE C CE1 
7468  C CE2 . PHE C 9   ? 0.1689 0.3920 0.2245 0.1044  -0.0063 -0.0381 9   PHE C CE2 
7469  C CZ  . PHE C 9   ? 0.1454 0.3733 0.2011 0.0955  0.0064  -0.0321 9   PHE C CZ  
7470  N N   . ARG C 10  ? 0.1321 0.3745 0.2148 0.0821  -0.0101 -0.0486 10  ARG C N   
7471  C CA  . ARG C 10  ? 0.1308 0.3820 0.2159 0.0705  0.0016  -0.0468 10  ARG C CA  
7472  C C   . ARG C 10  ? 0.1298 0.3614 0.2109 0.0609  0.0080  -0.0382 10  ARG C C   
7473  O O   . ARG C 10  ? 0.1291 0.3423 0.2064 0.0630  0.0026  -0.0341 10  ARG C O   
7474  C CB  . ARG C 10  ? 0.1588 0.4238 0.2512 0.0674  -0.0009 -0.0524 10  ARG C CB  
7475  C CG  . ARG C 10  ? 0.1292 0.3809 0.2225 0.0657  -0.0090 -0.0509 10  ARG C CG  
7476  C CD  . ARG C 10  ? 0.1512 0.4199 0.2514 0.0669  -0.0141 -0.0574 10  ARG C CD  
7477  N NE  . ARG C 10  ? 0.2264 0.4829 0.3268 0.0666  -0.0228 -0.0553 10  ARG C NE  
7478  C CZ  . ARG C 10  ? 0.2857 0.5456 0.3875 0.0710  -0.0317 -0.0589 10  ARG C CZ  
7479  N NH1 . ARG C 10  ? 0.2468 0.5178 0.3480 0.0754  -0.0329 -0.0648 10  ARG C NH1 
7480  N NH2 . ARG C 10  ? 0.2826 0.5302 0.3836 0.0699  -0.0387 -0.0554 10  ARG C NH2 
7481  N N   . ILE C 11  ? 0.1305 0.3663 0.2129 0.0502  0.0198  -0.0357 11  ILE C N   
7482  C CA  . ILE C 11  ? 0.1313 0.3494 0.2101 0.0414  0.0276  -0.0279 11  ILE C CA  
7483  C C   . ILE C 11  ? 0.1277 0.3374 0.2094 0.0345  0.0247  -0.0280 11  ILE C C   
7484  O O   . ILE C 11  ? 0.1260 0.3484 0.2134 0.0305  0.0241  -0.0332 11  ILE C O   
7485  C CB  . ILE C 11  ? 0.1358 0.3606 0.2149 0.0330  0.0418  -0.0251 11  ILE C CB  
7486  C CG1 . ILE C 11  ? 0.1400 0.3738 0.2152 0.0405  0.0443  -0.0242 11  ILE C CG1 
7487  C CG2 . ILE C 11  ? 0.1380 0.3436 0.2143 0.0240  0.0500  -0.0176 11  ILE C CG2 
7488  C CD1 . ILE C 11  ? 0.1454 0.3919 0.2218 0.0335  0.0570  -0.0228 11  ILE C CD1 
7489  N N   . LYS C 12  ? 0.1267 0.3166 0.2045 0.0335  0.0225  -0.0225 12  LYS C N   
7490  C CA  . LYS C 12  ? 0.1239 0.3059 0.2035 0.0266  0.0205  -0.0220 12  LYS C CA  
7491  C C   . LYS C 12  ? 0.1334 0.3035 0.2117 0.0161  0.0312  -0.0170 12  LYS C C   
7492  O O   . LYS C 12  ? 0.1574 0.3269 0.2388 0.0078  0.0330  -0.0185 12  LYS C O   
7493  C CB  . LYS C 12  ? 0.1466 0.3157 0.2235 0.0330  0.0087  -0.0202 12  LYS C CB  
7494  C CG  . LYS C 12  ? 0.1309 0.2986 0.2105 0.0285  0.0032  -0.0214 12  LYS C CG  
7495  C CD  . LYS C 12  ? 0.1727 0.3242 0.2487 0.0324  -0.0059 -0.0174 12  LYS C CD  
7496  C CE  . LYS C 12  ? 0.2107 0.3620 0.2888 0.0282  -0.0117 -0.0178 12  LYS C CE  
7497  N NZ  . LYS C 12  ? 0.2234 0.3839 0.3043 0.0359  -0.0227 -0.0220 12  LYS C NZ  
7498  N N   . MET C 13  ? 0.1294 0.2903 0.2032 0.0167  0.0381  -0.0113 13  MET C N   
7499  C CA  . MET C 13  ? 0.1331 0.2816 0.2057 0.0077  0.0488  -0.0063 13  MET C CA  
7500  C C   . MET C 13  ? 0.1395 0.2883 0.2092 0.0084  0.0584  -0.0018 13  MET C C   
7501  O O   . MET C 13  ? 0.1403 0.2914 0.2060 0.0175  0.0551  0.0000  13  MET C O   
7502  C CB  . MET C 13  ? 0.1314 0.2613 0.2003 0.0084  0.0453  -0.0014 13  MET C CB  
7503  C CG  . MET C 13  ? 0.1353 0.2527 0.2041 -0.0009 0.0554  0.0023  13  MET C CG  
7504  S SD  . MET C 13  ? 0.2667 0.3655 0.3320 -0.0003 0.0510  0.0069  13  MET C SD  
7505  C CE  . MET C 13  ? 0.2578 0.3488 0.3165 0.0104  0.0486  0.0134  13  MET C CE  
7506  N N   . VAL C 14  ? 0.1451 0.2918 0.2167 -0.0014 0.0702  0.0000  14  VAL C N   
7507  C CA  . VAL C 14  ? 0.1655 0.3126 0.2345 -0.0021 0.0804  0.0050  14  VAL C CA  
7508  C C   . VAL C 14  ? 0.1633 0.2899 0.2288 -0.0060 0.0884  0.0129  14  VAL C C   
7509  O O   . VAL C 14  ? 0.1600 0.2752 0.2274 -0.0119 0.0893  0.0125  14  VAL C O   
7510  C CB  . VAL C 14  ? 0.1573 0.3201 0.2318 -0.0104 0.0888  0.0010  14  VAL C CB  
7511  C CG1 . VAL C 14  ? 0.1520 0.3370 0.2298 -0.0048 0.0813  -0.0065 14  VAL C CG1 
7512  C CG2 . VAL C 14  ? 0.1583 0.3169 0.2385 -0.0228 0.0941  -0.0023 14  VAL C CG2 
7513  N N   . GLU C 15  ? 0.1739 0.2969 0.2344 -0.0023 0.0943  0.0199  15  GLU C N   
7514  C CA  . GLU C 15  ? 0.1942 0.2992 0.2515 -0.0054 0.1035  0.0283  15  GLU C CA  
7515  C C   . GLU C 15  ? 0.2225 0.3323 0.2804 -0.0112 0.1157  0.0317  15  GLU C C   
7516  O O   . GLU C 15  ? 0.2166 0.3401 0.2722 -0.0063 0.1159  0.0326  15  GLU C O   
7517  C CB  . GLU C 15  ? 0.2315 0.3274 0.2814 0.0053  0.0989  0.0349  15  GLU C CB  
7518  C CG  . GLU C 15  ? 0.3055 0.3846 0.3512 0.0048  0.1077  0.0445  15  GLU C CG  
7519  C CD  . GLU C 15  ? 0.3853 0.4596 0.4240 0.0162  0.1018  0.0501  15  GLU C CD  
7520  O OE1 . GLU C 15  ? 0.3115 0.3981 0.3479 0.0244  0.0937  0.0474  15  GLU C OE1 
7521  O OE2 . GLU C 15  ? 0.4369 0.4956 0.4728 0.0172  0.1052  0.0565  15  GLU C OE2 
7522  N N   . LYS C 16  ? 0.2388 0.3378 0.2997 -0.0218 0.1253  0.0331  16  LYS C N   
7523  C CA  . LYS C 16  ? 0.2705 0.3724 0.3303 -0.0289 0.1316  0.0345  16  LYS C CA  
7524  C C   . LYS C 16  ? 0.3390 0.4283 0.3905 -0.0245 0.1355  0.0447  16  LYS C C   
7525  O O   . LYS C 16  ? 0.4411 0.5128 0.4888 -0.0204 0.1348  0.0500  16  LYS C O   
7526  C CB  . LYS C 16  ? 0.3917 0.4864 0.4562 -0.0408 0.1340  0.0305  16  LYS C CB  
7527  C CG  . LYS C 16  ? 0.3955 0.5046 0.4679 -0.0446 0.1291  0.0203  16  LYS C CG  
7528  C CD  . LYS C 16  ? 0.3149 0.4189 0.3919 -0.0555 0.1308  0.0156  16  LYS C CD  
7529  C CE  . LYS C 16  ? 0.3299 0.4116 0.4051 -0.0578 0.1310  0.0168  16  LYS C CE  
7530  N NZ  . LYS C 16  ? 0.3083 0.3887 0.3841 -0.0536 0.1246  0.0137  16  LYS C NZ  
7531  N N   . ILE C 17  ? 0.3405 0.4409 0.3893 -0.0246 0.1393  0.0472  17  ILE C N   
7532  C CA  . ILE C 17  ? 0.3243 0.4157 0.3651 -0.0204 0.1430  0.0570  17  ILE C CA  
7533  C C   . ILE C 17  ? 0.3522 0.4482 0.3932 -0.0296 0.1500  0.0585  17  ILE C C   
7534  O O   . ILE C 17  ? 0.3886 0.5012 0.4351 -0.0365 0.1510  0.0520  17  ILE C O   
7535  C CB  . ILE C 17  ? 0.3290 0.4319 0.3643 -0.0074 0.1389  0.0601  17  ILE C CB  
7536  C CG1 . ILE C 17  ? 0.3758 0.5040 0.4137 -0.0071 0.1380  0.0537  17  ILE C CG1 
7537  C CG2 . ILE C 17  ? 0.3591 0.4582 0.3942 0.0020  0.1314  0.0596  17  ILE C CG2 
7538  C CD1 . ILE C 17  ? 0.3684 0.5095 0.4001 0.0053  0.1339  0.0565  17  ILE C CD1 
7539  N N   . ARG C 18  ? 0.4191 0.5012 0.4543 -0.0293 0.1548  0.0677  18  ARG C N   
7540  C CA  . ARG C 18  ? 0.4750 0.5566 0.5106 -0.0389 0.1620  0.0708  18  ARG C CA  
7541  C C   . ARG C 18  ? 0.5091 0.5897 0.5363 -0.0337 0.1656  0.0805  18  ARG C C   
7542  O O   . ARG C 18  ? 0.5123 0.5858 0.5335 -0.0230 0.1629  0.0864  18  ARG C O   
7543  C CB  . ARG C 18  ? 0.4880 0.5478 0.5269 -0.0464 0.1653  0.0720  18  ARG C CB  
7544  C CG  . ARG C 18  ? 0.5648 0.6011 0.5988 -0.0392 0.1652  0.0793  18  ARG C CG  
7545  C CD  . ARG C 18  ? 0.6253 0.6402 0.6630 -0.0458 0.1689  0.0792  18  ARG C CD  
7546  N NE  . ARG C 18  ? 0.6562 0.6641 0.6929 -0.0519 0.1765  0.0854  18  ARG C NE  
7547  C CZ  . ARG C 18  ? 0.6286 0.6236 0.6593 -0.0468 0.1801  0.0956  18  ARG C CZ  
7548  N NH1 . ARG C 18  ? 0.6352 0.6242 0.6605 -0.0351 0.1768  0.1008  18  ARG C NH1 
7549  N NH2 . ARG C 18  ? 0.6146 0.6034 0.6450 -0.0535 0.1872  0.1010  18  ARG C NH2 
7550  N N   . VAL C 19  ? 0.5146 0.6034 0.5414 -0.0415 0.1716  0.0824  19  VAL C N   
7551  C CA  . VAL C 19  ? 0.5257 0.6116 0.5448 -0.0389 0.1763  0.0926  19  VAL C CA  
7552  C C   . VAL C 19  ? 0.5193 0.5817 0.5385 -0.0445 0.1818  0.0999  19  VAL C C   
7553  O O   . VAL C 19  ? 0.5670 0.6276 0.5920 -0.0560 0.1857  0.0973  19  VAL C O   
7554  C CB  . VAL C 19  ? 0.4413 0.5497 0.4596 -0.0442 0.1802  0.0907  19  VAL C CB  
7555  C CG1 . VAL C 19  ? 0.4743 0.5812 0.4833 -0.0391 0.1840  0.1013  19  VAL C CG1 
7556  C CG2 . VAL C 19  ? 0.4875 0.6185 0.5085 -0.0397 0.1751  0.0803  19  VAL C CG2 
7557  N N   . PRO C 20  ? 0.5268 0.5712 0.5405 -0.0364 0.1819  0.1087  20  PRO C N   
7558  C CA  . PRO C 20  ? 0.5745 0.5969 0.5881 -0.0409 0.1879  0.1159  20  PRO C CA  
7559  C C   . PRO C 20  ? 0.6217 0.6504 0.6326 -0.0484 0.1950  0.1219  20  PRO C C   
7560  O O   . PRO C 20  ? 0.6016 0.6473 0.6070 -0.0454 0.1953  0.1245  20  PRO C O   
7561  C CB  . PRO C 20  ? 0.5786 0.5863 0.5862 -0.0280 0.1858  0.1240  20  PRO C CB  
7562  C CG  . PRO C 20  ? 0.5182 0.5362 0.5254 -0.0188 0.1776  0.1185  20  PRO C CG  
7563  C CD  . PRO C 20  ? 0.5007 0.5438 0.5089 -0.0222 0.1762  0.1118  20  PRO C CD  
7564  N N   . SER C 21  ? 0.6248 0.6401 0.6398 -0.0584 0.2008  0.1237  21  SER C N   
7565  C CA  . SER C 21  ? 0.6937 0.7137 0.7066 -0.0668 0.2079  0.1301  21  SER C CA  
7566  C C   . SER C 21  ? 0.6213 0.6370 0.6242 -0.0581 0.2101  0.1424  21  SER C C   
7567  O O   . SER C 21  ? 0.5816 0.5847 0.5806 -0.0466 0.2072  0.1470  21  SER C O   
7568  C CB  . SER C 21  ? 0.6585 0.6609 0.6779 -0.0777 0.2137  0.1309  21  SER C CB  
7569  O OG  . SER C 21  ? 0.6865 0.6616 0.7044 -0.0720 0.2151  0.1366  21  SER C OG  
7570  N N   . ARG C 22  ? 0.6521 0.6803 0.6509 -0.0636 0.2152  0.1475  22  ARG C N   
7571  C CA  . ARG C 22  ? 0.6530 0.6786 0.6420 -0.0560 0.2177  0.1596  22  ARG C CA  
7572  C C   . ARG C 22  ? 0.6942 0.6914 0.6819 -0.0515 0.2200  0.1689  22  ARG C C   
7573  O O   . ARG C 22  ? 0.6424 0.6334 0.6246 -0.0385 0.2170  0.1750  22  ARG C O   
7574  C CB  . ARG C 22  ? 0.6554 0.6952 0.6409 -0.0655 0.2244  0.1640  22  ARG C CB  
7575  C CG  . ARG C 22  ? 0.6833 0.7248 0.6580 -0.0574 0.2267  0.1761  22  ARG C CG  
7576  C CD  . ARG C 22  ? 0.7529 0.8052 0.7228 -0.0416 0.2193  0.1745  22  ARG C CD  
7577  N NE  . ARG C 22  ? 0.7197 0.7754 0.6799 -0.0323 0.2204  0.1858  22  ARG C NE  
7578  C CZ  . ARG C 22  ? 0.7144 0.7921 0.6689 -0.0310 0.2215  0.1866  22  ARG C CZ  
7579  N NH1 . ARG C 22  ? 0.6524 0.7504 0.6100 -0.0385 0.2223  0.1766  22  ARG C NH1 
7580  N NH2 . ARG C 22  ? 0.7177 0.7981 0.6635 -0.0213 0.2217  0.1973  22  ARG C NH2 
7581  N N   . GLU C 23  ? 0.7785 0.7591 0.7720 -0.0617 0.2251  0.1693  23  GLU C N   
7582  C CA  . GLU C 23  ? 0.7751 0.7274 0.7690 -0.0576 0.2275  0.1759  23  GLU C CA  
7583  C C   . GLU C 23  ? 0.7539 0.6978 0.7489 -0.0453 0.2208  0.1719  23  GLU C C   
7584  O O   . GLU C 23  ? 0.7794 0.7102 0.7701 -0.0347 0.2204  0.1797  23  GLU C O   
7585  C CB  . GLU C 23  ? 0.7808 0.7181 0.7831 -0.0707 0.2328  0.1727  23  GLU C CB  
7586  C CG  . GLU C 23  ? 0.8024 0.7096 0.8060 -0.0673 0.2362  0.1782  23  GLU C CG  
7587  C CD  . GLU C 23  ? 0.8134 0.7064 0.8256 -0.0806 0.2417  0.1741  23  GLU C CD  
7588  O OE1 . GLU C 23  ? 0.8118 0.7191 0.8283 -0.0928 0.2435  0.1692  23  GLU C OE1 
7589  O OE2 . GLU C 23  ? 0.8266 0.6952 0.8417 -0.0786 0.2444  0.1754  23  GLU C OE2 
7590  N N   . GLU C 24  ? 0.7108 0.6632 0.7113 -0.0465 0.2153  0.1598  24  GLU C N   
7591  C CA  . GLU C 24  ? 0.6873 0.6333 0.6888 -0.0358 0.2088  0.1557  24  GLU C CA  
7592  C C   . GLU C 24  ? 0.6402 0.5985 0.6342 -0.0223 0.2037  0.1604  24  GLU C C   
7593  O O   . GLU C 24  ? 0.5522 0.5003 0.5439 -0.0111 0.2009  0.1643  24  GLU C O   
7594  C CB  . GLU C 24  ? 0.7215 0.6750 0.7306 -0.0412 0.2044  0.1421  24  GLU C CB  
7595  C CG  . GLU C 24  ? 0.6975 0.6334 0.7148 -0.0498 0.2074  0.1361  24  GLU C CG  
7596  C CD  . GLU C 24  ? 0.6616 0.6080 0.6861 -0.0558 0.2030  0.1228  24  GLU C CD  
7597  O OE1 . GLU C 24  ? 0.6188 0.5875 0.6428 -0.0562 0.1991  0.1184  24  GLU C OE1 
7598  O OE2 . GLU C 24  ? 0.6446 0.5774 0.6753 -0.0597 0.2035  0.1164  24  GLU C OE2 
7599  N N   . ARG C 25  ? 0.6380 0.6193 0.6283 -0.0229 0.2024  0.1594  25  ARG C N   
7600  C CA  . ARG C 25  ? 0.6231 0.6174 0.6062 -0.0099 0.1975  0.1635  25  ARG C CA  
7601  C C   . ARG C 25  ? 0.6657 0.6511 0.6419 -0.0025 0.2008  0.1769  25  ARG C C   
7602  O O   . ARG C 25  ? 0.6239 0.6073 0.5964 0.0103  0.1965  0.1811  25  ARG C O   
7603  C CB  . ARG C 25  ? 0.5940 0.6150 0.5749 -0.0124 0.1963  0.1590  25  ARG C CB  
7604  C CG  . ARG C 25  ? 0.6161 0.6490 0.6038 -0.0176 0.1922  0.1457  25  ARG C CG  
7605  C CD  . ARG C 25  ? 0.5469 0.6072 0.5322 -0.0152 0.1894  0.1408  25  ARG C CD  
7606  N NE  . ARG C 25  ? 0.5896 0.6619 0.5718 -0.0227 0.1958  0.1440  25  ARG C NE  
7607  C CZ  . ARG C 25  ? 0.5977 0.6767 0.5849 -0.0364 0.2004  0.1385  25  ARG C CZ  
7608  N NH1 . ARG C 25  ? 0.5027 0.5779 0.4986 -0.0441 0.1992  0.1298  25  ARG C NH1 
7609  N NH2 . ARG C 25  ? 0.6085 0.6996 0.5922 -0.0426 0.2064  0.1419  25  ARG C NH2 
7610  N N   . GLU C 26  ? 0.6407 0.6213 0.6149 -0.0107 0.2083  0.1839  26  GLU C N   
7611  C CA  . GLU C 26  ? 0.6718 0.6417 0.6397 -0.0046 0.2121  0.1973  26  GLU C CA  
7612  C C   . GLU C 26  ? 0.6575 0.6046 0.6279 0.0029  0.2111  0.1999  26  GLU C C   
7613  O O   . GLU C 26  ? 0.6419 0.5873 0.6076 0.0155  0.2088  0.2072  26  GLU C O   
7614  C CB  . GLU C 26  ? 0.7044 0.6690 0.6713 -0.0168 0.2209  0.2037  26  GLU C CB  
7615  C CG  . GLU C 26  ? 0.7127 0.7010 0.6752 -0.0229 0.2231  0.2040  26  GLU C CG  
7616  C CD  . GLU C 26  ? 0.7411 0.7238 0.7036 -0.0369 0.2320  0.2095  26  GLU C CD  
7617  O OE1 . GLU C 26  ? 0.6944 0.6540 0.6607 -0.0417 0.2361  0.2131  26  GLU C OE1 
7618  O OE2 . GLU C 26  ? 0.7334 0.7351 0.6922 -0.0433 0.2349  0.2100  26  GLU C OE2 
7619  N N   . ALA C 27  ? 0.5983 0.5293 0.5766 -0.0045 0.2128  0.1934  27  ALA C N   
7620  C CA  . ALA C 27  ? 0.6414 0.5509 0.6226 0.0020  0.2127  0.1949  27  ALA C CA  
7621  C C   . ALA C 27  ? 0.6848 0.6000 0.6659 0.0143  0.2045  0.1905  27  ALA C C   
7622  O O   . ALA C 27  ? 0.6464 0.5524 0.6258 0.0250  0.2034  0.1958  27  ALA C O   
7623  C CB  . ALA C 27  ? 0.6052 0.4981 0.5949 -0.0091 0.2163  0.1875  27  ALA C CB  
7624  N N   . ALA C 28  ? 0.6224 0.5537 0.6054 0.0130  0.1989  0.1809  28  ALA C N   
7625  C CA  . ALA C 28  ? 0.6352 0.5718 0.6185 0.0234  0.1910  0.1764  28  ALA C CA  
7626  C C   . ALA C 28  ? 0.5886 0.5373 0.5643 0.0366  0.1874  0.1842  28  ALA C C   
7627  O O   . ALA C 28  ? 0.5889 0.5334 0.5639 0.0474  0.1838  0.1864  28  ALA C O   
7628  C CB  . ALA C 28  ? 0.6004 0.5514 0.5875 0.0183  0.1861  0.1647  28  ALA C CB  
7629  N N   . LEU C 29  ? 0.5966 0.5620 0.5668 0.0359  0.1883  0.1881  29  LEU C N   
7630  C CA  . LEU C 29  ? 0.5828 0.5619 0.5458 0.0484  0.1847  0.1950  29  LEU C CA  
7631  C C   . LEU C 29  ? 0.6745 0.6401 0.6345 0.0558  0.1879  0.2062  29  LEU C C   
7632  O O   . LEU C 29  ? 0.6589 0.6297 0.6158 0.0683  0.1835  0.2098  29  LEU C O   
7633  C CB  . LEU C 29  ? 0.5940 0.5932 0.5518 0.0452  0.1861  0.1970  29  LEU C CB  
7634  C CG  . LEU C 29  ? 0.6427 0.6592 0.5931 0.0582  0.1819  0.2029  29  LEU C CG  
7635  C CD1 . LEU C 29  ? 0.6122 0.6384 0.5638 0.0679  0.1726  0.1958  29  LEU C CD1 
7636  C CD2 . LEU C 29  ? 0.6574 0.6942 0.6026 0.0546  0.1840  0.2044  29  LEU C CD2 
7637  N N   . LYS C 30  ? 0.6328 0.5816 0.5938 0.0482  0.1957  0.2116  30  LYS C N   
7638  C CA  . LYS C 30  ? 0.6571 0.5912 0.6157 0.0550  0.1993  0.2222  30  LYS C CA  
7639  C C   . LYS C 30  ? 0.6499 0.5705 0.6133 0.0619  0.1964  0.2187  30  LYS C C   
7640  O O   . LYS C 30  ? 0.6233 0.5418 0.5841 0.0731  0.1952  0.2252  30  LYS C O   
7641  C CB  . LYS C 30  ? 0.6636 0.5819 0.6226 0.0442  0.2083  0.2283  30  LYS C CB  
7642  C CG  . LYS C 30  ? 0.8358 0.7683 0.7887 0.0385  0.2118  0.2341  30  LYS C CG  
7643  C CD  . LYS C 30  ? 0.9406 0.8601 0.8954 0.0240  0.2203  0.2367  30  LYS C CD  
7644  C CE  . LYS C 30  ? 0.8842 0.8214 0.8329 0.0174  0.2234  0.2411  30  LYS C CE  
7645  N NZ  . LYS C 30  ? 0.8280 0.7546 0.7782 0.0024  0.2319  0.2442  30  LYS C NZ  
7646  N N   . GLU C 31  ? 0.6241 0.5370 0.5947 0.0552  0.1952  0.2080  31  GLU C N   
7647  C CA  . GLU C 31  ? 0.6833 0.5867 0.6584 0.0615  0.1919  0.2033  31  GLU C CA  
7648  C C   . GLU C 31  ? 0.7261 0.6463 0.6985 0.0734  0.1836  0.2018  31  GLU C C   
7649  O O   . GLU C 31  ? 0.6620 0.5783 0.6349 0.0827  0.1814  0.2032  31  GLU C O   
7650  C CB  . GLU C 31  ? 0.6351 0.5299 0.6180 0.0513  0.1920  0.1917  31  GLU C CB  
7651  C CG  . GLU C 31  ? 0.6603 0.5505 0.6478 0.0568  0.1873  0.1847  31  GLU C CG  
7652  C CD  . GLU C 31  ? 0.8986 0.7733 0.8866 0.0642  0.1902  0.1902  31  GLU C CD  
7653  O OE1 . GLU C 31  ? 0.9246 0.7830 0.9139 0.0597  0.1974  0.1946  31  GLU C OE1 
7654  O OE2 . GLU C 31  ? 0.9337 0.8134 0.9211 0.0746  0.1854  0.1901  31  GLU C OE2 
7655  N N   . ALA C 32  ? 0.6932 0.6331 0.6628 0.0730  0.1791  0.1986  32  ALA C N   
7656  C CA  . ALA C 32  ? 0.6901 0.6472 0.6573 0.0835  0.1710  0.1963  32  ALA C CA  
7657  C C   . ALA C 32  ? 0.6872 0.6549 0.6475 0.0947  0.1702  0.2061  32  ALA C C   
7658  O O   . ALA C 32  ? 0.7065 0.6893 0.6646 0.1041  0.1634  0.2046  32  ALA C O   
7659  C CB  . ALA C 32  ? 0.6288 0.6031 0.5956 0.0790  0.1666  0.1887  32  ALA C CB  
7660  N N   . GLY C 33  ? 0.6208 0.5816 0.5776 0.0939  0.1767  0.2160  33  GLY C N   
7661  C CA  . GLY C 33  ? 0.6942 0.6666 0.6442 0.1042  0.1761  0.2256  33  GLY C CA  
7662  C C   . GLY C 33  ? 0.7806 0.7774 0.7252 0.1060  0.1724  0.2253  33  GLY C C   
7663  O O   . GLY C 33  ? 0.7621 0.7745 0.7021 0.1168  0.1684  0.2291  33  GLY C O   
7664  N N   . TYR C 34  ? 0.7114 0.7133 0.6568 0.0958  0.1735  0.2200  34  TYR C N   
7665  C CA  . TYR C 34  ? 0.6894 0.7151 0.6298 0.0965  0.1709  0.2190  34  TYR C CA  
7666  C C   . TYR C 34  ? 0.6862 0.7303 0.6260 0.1064  0.1614  0.2125  34  TYR C C   
7667  O O   . TYR C 34  ? 0.7025 0.7673 0.6368 0.1134  0.1580  0.2143  34  TYR C O   
7668  C CB  . TYR C 34  ? 0.6659 0.6983 0.5990 0.0994  0.1753  0.2307  34  TYR C CB  
7669  C CG  . TYR C 34  ? 0.7652 0.7811 0.6984 0.0882  0.1847  0.2370  34  TYR C CG  
7670  C CD1 . TYR C 34  ? 0.7115 0.7325 0.6447 0.0760  0.1886  0.2338  34  TYR C CD1 
7671  C CD2 . TYR C 34  ? 0.7795 0.7749 0.7131 0.0895  0.1898  0.2456  34  TYR C CD2 
7672  C CE1 . TYR C 34  ? 0.6363 0.6427 0.5699 0.0649  0.1972  0.2392  34  TYR C CE1 
7673  C CE2 . TYR C 34  ? 0.7524 0.7318 0.6861 0.0789  0.1983  0.2512  34  TYR C CE2 
7674  C CZ  . TYR C 34  ? 0.7549 0.7400 0.6886 0.0663  0.2019  0.2480  34  TYR C CZ  
7675  O OH  . TYR C 34  ? 0.8214 0.7914 0.7554 0.0550  0.2103  0.2533  34  TYR C OH  
7676  N N   . ASN C 35  ? 0.6675 0.7045 0.6128 0.1068  0.1571  0.2045  35  ASN C N   
7677  C CA  . ASN C 35  ? 0.7042 0.7568 0.6495 0.1143  0.1480  0.1972  35  ASN C CA  
7678  C C   . ASN C 35  ? 0.7249 0.7728 0.6761 0.1065  0.1456  0.1864  35  ASN C C   
7679  O O   . ASN C 35  ? 0.5860 0.6169 0.5425 0.1038  0.1461  0.1836  35  ASN C O   
7680  C CB  . ASN C 35  ? 0.6230 0.6738 0.5685 0.1253  0.1443  0.1995  35  ASN C CB  
7681  C CG  . ASN C 35  ? 0.5693 0.6360 0.5150 0.1322  0.1350  0.1916  35  ASN C CG  
7682  O OD1 . ASN C 35  ? 0.5901 0.6705 0.5348 0.1305  0.1309  0.1852  35  ASN C OD1 
7683  N ND2 . ASN C 35  ? 0.5294 0.5948 0.4762 0.1401  0.1316  0.1916  35  ASN C ND2 
7684  N N   . PRO C 36  ? 0.6660 0.7293 0.6163 0.1031  0.1428  0.1800  36  PRO C N   
7685  C CA  . PRO C 36  ? 0.5920 0.6514 0.5480 0.0949  0.1412  0.1700  36  PRO C CA  
7686  C C   . PRO C 36  ? 0.5580 0.6136 0.5173 0.0994  0.1345  0.1641  36  PRO C C   
7687  O O   . PRO C 36  ? 0.5290 0.5770 0.4937 0.0921  0.1341  0.1571  36  PRO C O   
7688  C CB  . PRO C 36  ? 0.5705 0.6520 0.5240 0.0935  0.1387  0.1648  36  PRO C CB  
7689  C CG  . PRO C 36  ? 0.5726 0.6633 0.5199 0.0958  0.1428  0.1732  36  PRO C CG  
7690  C CD  . PRO C 36  ? 0.5826 0.6674 0.5271 0.1056  0.1422  0.1816  36  PRO C CD  
7691  N N   . PHE C 37  ? 0.5797 0.6417 0.5363 0.1106  0.1293  0.1663  37  PHE C N   
7692  C CA  . PHE C 37  ? 0.5419 0.5999 0.5017 0.1141  0.1234  0.1610  37  PHE C CA  
7693  C C   . PHE C 37  ? 0.4868 0.5221 0.4520 0.1100  0.1275  0.1622  37  PHE C C   
7694  O O   . PHE C 37  ? 0.4714 0.5010 0.4405 0.1094  0.1239  0.1567  37  PHE C O   
7695  C CB  . PHE C 37  ? 0.5316 0.6037 0.4874 0.1265  0.1170  0.1623  37  PHE C CB  
7696  C CG  . PHE C 37  ? 0.3817 0.4688 0.3365 0.1302  0.1082  0.1540  37  PHE C CG  
7697  C CD1 . PHE C 37  ? 0.3929 0.4725 0.3519 0.1271  0.1046  0.1475  37  PHE C CD1 
7698  C CD2 . PHE C 37  ? 0.4468 0.5560 0.3962 0.1370  0.1035  0.1525  37  PHE C CD2 
7699  C CE1 . PHE C 37  ? 0.3565 0.4492 0.3140 0.1305  0.0964  0.1401  37  PHE C CE1 
7700  C CE2 . PHE C 37  ? 0.4417 0.5644 0.3899 0.1407  0.0952  0.1440  37  PHE C CE2 
7701  C CZ  . PHE C 37  ? 0.3490 0.4629 0.3009 0.1374  0.0916  0.1381  37  PHE C CZ  
7702  N N   . LEU C 38  ? 0.5825 0.6055 0.5477 0.1075  0.1349  0.1692  38  LEU C N   
7703  C CA  . LEU C 38  ? 0.5568 0.5583 0.5271 0.1032  0.1398  0.1700  38  LEU C CA  
7704  C C   . LEU C 38  ? 0.4574 0.4469 0.4322 0.0902  0.1448  0.1658  38  LEU C C   
7705  O O   . LEU C 38  ? 0.4265 0.3982 0.4059 0.0856  0.1489  0.1650  38  LEU C O   
7706  C CB  . LEU C 38  ? 0.5654 0.5596 0.5330 0.1078  0.1453  0.1800  38  LEU C CB  
7707  C CG  . LEU C 38  ? 0.5896 0.5913 0.5543 0.1202  0.1417  0.1840  38  LEU C CG  
7708  C CD1 . LEU C 38  ? 0.5807 0.5734 0.5432 0.1234  0.1483  0.1942  38  LEU C CD1 
7709  C CD2 . LEU C 38  ? 0.4940 0.4911 0.4632 0.1223  0.1373  0.1776  38  LEU C CD2 
7710  N N   . LEU C 39  ? 0.4063 0.4062 0.3800 0.0842  0.1449  0.1627  39  LEU C N   
7711  C CA  . LEU C 39  ? 0.4491 0.4405 0.4276 0.0713  0.1494  0.1575  39  LEU C CA  
7712  C C   . LEU C 39  ? 0.4189 0.4053 0.4033 0.0678  0.1454  0.1484  39  LEU C C   
7713  O O   . LEU C 39  ? 0.3357 0.3328 0.3193 0.0732  0.1384  0.1445  39  LEU C O   
7714  C CB  . LEU C 39  ? 0.4528 0.4601 0.4291 0.0660  0.1502  0.1556  39  LEU C CB  
7715  C CG  . LEU C 39  ? 0.4774 0.4867 0.4495 0.0633  0.1567  0.1633  39  LEU C CG  
7716  C CD1 . LEU C 39  ? 0.4883 0.5168 0.4589 0.0586  0.1564  0.1592  39  LEU C CD1 
7717  C CD2 . LEU C 39  ? 0.5450 0.5341 0.5209 0.0537  0.1646  0.1655  39  LEU C CD2 
7718  N N   . PRO C 40  ? 0.4262 0.3968 0.4164 0.0589  0.1496  0.1447  40  PRO C N   
7719  C CA  . PRO C 40  ? 0.3555 0.3240 0.3513 0.0533  0.1463  0.1352  40  PRO C CA  
7720  C C   . PRO C 40  ? 0.3691 0.3519 0.3658 0.0464  0.1450  0.1290  40  PRO C C   
7721  O O   . PRO C 40  ? 0.3219 0.3119 0.3167 0.0424  0.1487  0.1311  40  PRO C O   
7722  C CB  . PRO C 40  ? 0.3512 0.3003 0.3524 0.0456  0.1521  0.1333  40  PRO C CB  
7723  C CG  . PRO C 40  ? 0.3488 0.2932 0.3477 0.0424  0.1594  0.1401  40  PRO C CG  
7724  C CD  . PRO C 40  ? 0.3741 0.3285 0.3659 0.0532  0.1577  0.1489  40  PRO C CD  
7725  N N   . SER C 41  ? 0.3507 0.3387 0.3508 0.0450  0.1397  0.1213  41  SER C N   
7726  C CA  . SER C 41  ? 0.3094 0.3120 0.3115 0.0390  0.1383  0.1145  41  SER C CA  
7727  C C   . SER C 41  ? 0.3505 0.3485 0.3572 0.0262  0.1446  0.1108  41  SER C C   
7728  O O   . SER C 41  ? 0.3565 0.3687 0.3642 0.0212  0.1452  0.1068  41  SER C O   
7729  C CB  . SER C 41  ? 0.2618 0.2692 0.2674 0.0396  0.1318  0.1071  41  SER C CB  
7730  O OG  . SER C 41  ? 0.3787 0.3723 0.3903 0.0319  0.1334  0.1023  41  SER C OG  
7731  N N   . SER C 42  ? 0.3474 0.3272 0.3573 0.0210  0.1492  0.1114  42  SER C N   
7732  C CA  . SER C 42  ? 0.3199 0.2952 0.3339 0.0089  0.1553  0.1082  42  SER C CA  
7733  C C   . SER C 42  ? 0.3998 0.3808 0.4099 0.0070  0.1605  0.1145  42  SER C C   
7734  O O   . SER C 42  ? 0.4548 0.4386 0.4679 -0.0035 0.1649  0.1114  42  SER C O   
7735  C CB  . SER C 42  ? 0.4060 0.3602 0.4238 0.0053  0.1590  0.1077  42  SER C CB  
7736  O OG  . SER C 42  ? 0.4748 0.4173 0.4886 0.0120  0.1626  0.1171  42  SER C OG  
7737  N N   . ALA C 43  ? 0.3824 0.3666 0.3857 0.0167  0.1600  0.1231  43  ALA C N   
7738  C CA  . ALA C 43  ? 0.3801 0.3705 0.3789 0.0156  0.1649  0.1300  43  ALA C CA  
7739  C C   . ALA C 43  ? 0.4409 0.4553 0.4366 0.0173  0.1620  0.1277  43  ALA C C   
7740  O O   . ALA C 43  ? 0.4717 0.4944 0.4634 0.0160  0.1659  0.1326  43  ALA C O   
7741  C CB  . ALA C 43  ? 0.3890 0.3707 0.3819 0.0254  0.1663  0.1410  43  ALA C CB  
7742  N N   . VAL C 44  ? 0.3996 0.4257 0.3974 0.0201  0.1555  0.1201  44  VAL C N   
7743  C CA  . VAL C 44  ? 0.3578 0.4071 0.3530 0.0246  0.1516  0.1171  44  VAL C CA  
7744  C C   . VAL C 44  ? 0.3925 0.4533 0.3942 0.0157  0.1512  0.1065  44  VAL C C   
7745  O O   . VAL C 44  ? 0.3119 0.3648 0.3198 0.0103  0.1501  0.1004  44  VAL C O   
7746  C CB  . VAL C 44  ? 0.3752 0.4304 0.3670 0.0375  0.1435  0.1173  44  VAL C CB  
7747  C CG1 . VAL C 44  ? 0.3730 0.4528 0.3621 0.0432  0.1389  0.1135  44  VAL C CG1 
7748  C CG2 . VAL C 44  ? 0.3041 0.3487 0.2904 0.0465  0.1437  0.1274  44  VAL C CG2 
7749  N N   . TYR C 45  ? 0.4196 0.5003 0.4202 0.0145  0.1520  0.1039  45  TYR C N   
7750  C CA  . TYR C 45  ? 0.3949 0.4908 0.4020 0.0077  0.1512  0.0934  45  TYR C CA  
7751  C C   . TYR C 45  ? 0.3027 0.4155 0.3102 0.0176  0.1427  0.0872  45  TYR C C   
7752  O O   . TYR C 45  ? 0.3934 0.5044 0.4057 0.0182  0.1380  0.0812  45  TYR C O   
7753  C CB  . TYR C 45  ? 0.3817 0.4900 0.3884 -0.0001 0.1575  0.0932  45  TYR C CB  
7754  C CG  . TYR C 45  ? 0.3803 0.5090 0.3934 -0.0049 0.1563  0.0820  45  TYR C CG  
7755  C CD1 . TYR C 45  ? 0.4052 0.5320 0.4265 -0.0124 0.1554  0.0738  45  TYR C CD1 
7756  C CD2 . TYR C 45  ? 0.4631 0.6135 0.4743 -0.0013 0.1558  0.0793  45  TYR C CD2 
7757  C CE1 . TYR C 45  ? 0.4956 0.6417 0.5234 -0.0161 0.1541  0.0634  45  TYR C CE1 
7758  C CE2 . TYR C 45  ? 0.4232 0.5921 0.4411 -0.0046 0.1544  0.0686  45  TYR C CE2 
7759  C CZ  . TYR C 45  ? 0.4240 0.5903 0.4503 -0.0118 0.1537  0.0607  45  TYR C CZ  
7760  O OH  . TYR C 45  ? 0.4343 0.6185 0.4681 -0.0140 0.1521  0.0502  45  TYR C OH  
7761  N N   . ILE C 46  ? 0.3237 0.4535 0.3260 0.0254  0.1404  0.0882  46  ILE C N   
7762  C CA  . ILE C 46  ? 0.2735 0.4186 0.2748 0.0368  0.1312  0.0830  46  ILE C CA  
7763  C C   . ILE C 46  ? 0.2808 0.4194 0.2744 0.0477  0.1278  0.0909  46  ILE C C   
7764  O O   . ILE C 46  ? 0.3064 0.4448 0.2936 0.0502  0.1311  0.0988  46  ILE C O   
7765  C CB  . ILE C 46  ? 0.3066 0.4764 0.3075 0.0391  0.1295  0.0772  46  ILE C CB  
7766  C CG1 . ILE C 46  ? 0.2541 0.4322 0.2634 0.0289  0.1323  0.0685  46  ILE C CG1 
7767  C CG2 . ILE C 46  ? 0.2418 0.4263 0.2408 0.0520  0.1189  0.0715  46  ILE C CG2 
7768  C CD1 . ILE C 46  ? 0.2819 0.4839 0.2915 0.0307  0.1311  0.0626  46  ILE C CD1 
7769  N N   . ASP C 47  ? 0.2455 0.3795 0.2398 0.0542  0.1212  0.0888  47  ASP C N   
7770  C CA  . ASP C 47  ? 0.2562 0.3839 0.2440 0.0641  0.1177  0.0955  47  ASP C CA  
7771  C C   . ASP C 47  ? 0.2694 0.4171 0.2536 0.0756  0.1089  0.0903  47  ASP C C   
7772  O O   . ASP C 47  ? 0.2567 0.4112 0.2448 0.0786  0.1021  0.0815  47  ASP C O   
7773  C CB  . ASP C 47  ? 0.2449 0.3539 0.2355 0.0634  0.1164  0.0967  47  ASP C CB  
7774  C CG  . ASP C 47  ? 0.3140 0.4109 0.2986 0.0701  0.1166  0.1062  47  ASP C CG  
7775  O OD1 . ASP C 47  ? 0.2946 0.4011 0.2726 0.0777  0.1153  0.1108  47  ASP C OD1 
7776  O OD2 . ASP C 47  ? 0.2842 0.3631 0.2712 0.0679  0.1177  0.1087  47  ASP C OD2 
7777  N N   . LEU C 48  ? 0.2481 0.4052 0.2250 0.0820  0.1087  0.0951  48  LEU C N   
7778  C CA  . LEU C 48  ? 0.2499 0.4258 0.2225 0.0932  0.1002  0.0900  48  LEU C CA  
7779  C C   . LEU C 48  ? 0.2887 0.4607 0.2544 0.1027  0.0970  0.0968  48  LEU C C   
7780  O O   . LEU C 48  ? 0.2805 0.4681 0.2409 0.1117  0.0916  0.0950  48  LEU C O   
7781  C CB  . LEU C 48  ? 0.2505 0.4453 0.2207 0.0934  0.1016  0.0882  48  LEU C CB  
7782  C CG  . LEU C 48  ? 0.2494 0.4495 0.2262 0.0835  0.1057  0.0822  48  LEU C CG  
7783  C CD1 . LEU C 48  ? 0.2587 0.4774 0.2323 0.0842  0.1076  0.0816  48  LEU C CD1 
7784  C CD2 . LEU C 48  ? 0.2334 0.4396 0.2172 0.0846  0.0984  0.0698  48  LEU C CD2 
7785  N N   . LEU C 49  ? 0.2482 0.4003 0.2144 0.1008  0.1000  0.1038  49  LEU C N   
7786  C CA  . LEU C 49  ? 0.2781 0.4265 0.2387 0.1098  0.0968  0.1100  49  LEU C CA  
7787  C C   . LEU C 49  ? 0.2442 0.4050 0.2031 0.1191  0.0866  0.1018  49  LEU C C   
7788  O O   . LEU C 49  ? 0.2532 0.4247 0.2060 0.1283  0.0820  0.1030  49  LEU C O   
7789  C CB  . LEU C 49  ? 0.2644 0.3891 0.2277 0.1056  0.1009  0.1165  49  LEU C CB  
7790  C CG  . LEU C 49  ? 0.3184 0.4366 0.2773 0.1133  0.1000  0.1249  49  LEU C CG  
7791  C CD1 . LEU C 49  ? 0.3478 0.4699 0.3026 0.1149  0.1050  0.1330  49  LEU C CD1 
7792  C CD2 . LEU C 49  ? 0.2876 0.3832 0.2510 0.1088  0.1032  0.1283  49  LEU C CD2 
7793  N N   . THR C 50  ? 0.2425 0.4015 0.2081 0.1162  0.0814  0.0918  50  THR C N   
7794  C CA  . THR C 50  ? 0.2500 0.4126 0.2171 0.1222  0.0682  0.0820  50  THR C CA  
7795  C C   . THR C 50  ? 0.2116 0.3761 0.1868 0.1178  0.0616  0.0695  50  THR C C   
7796  O O   . THR C 50  ? 0.2707 0.4304 0.2511 0.1093  0.0669  0.0688  50  THR C O   
7797  C CB  . THR C 50  ? 0.2135 0.3594 0.1816 0.1227  0.0647  0.0853  50  THR C CB  
7798  O OG1 . THR C 50  ? 0.3368 0.4878 0.3060 0.1284  0.0520  0.0761  50  THR C OG1 
7799  C CG2 . THR C 50  ? 0.2147 0.3425 0.1902 0.1127  0.0672  0.0846  50  THR C CG2 
7800  N N   . ASP C 51  ? 0.1993 0.3709 0.1758 0.1238  0.0497  0.0595  51  ASP C N   
7801  C CA  . ASP C 51  ? 0.1897 0.3594 0.1739 0.1209  0.0413  0.0481  51  ASP C CA  
7802  C C   . ASP C 51  ? 0.2166 0.3704 0.2044 0.1195  0.0335  0.0461  51  ASP C C   
7803  O O   . ASP C 51  ? 0.1988 0.3511 0.1919 0.1193  0.0241  0.0368  51  ASP C O   
7804  C CB  . ASP C 51  ? 0.1974 0.3855 0.1813 0.1284  0.0334  0.0374  51  ASP C CB  
7805  C CG  . ASP C 51  ? 0.2157 0.4080 0.1957 0.1374  0.0244  0.0341  51  ASP C CG  
7806  O OD1 . ASP C 51  ? 0.2551 0.4461 0.2290 0.1403  0.0280  0.0427  51  ASP C OD1 
7807  O OD2 . ASP C 51  ? 0.1870 0.3810 0.1687 0.1395  0.0137  0.0227  51  ASP C OD2 
7808  N N   . SER C 52  ? 0.2091 0.3512 0.1943 0.1186  0.0373  0.0550  52  SER C N   
7809  C CA  . SER C 52  ? 0.2116 0.3414 0.1992 0.1182  0.0302  0.0541  52  SER C CA  
7810  C C   . SER C 52  ? 0.2037 0.3166 0.1962 0.1088  0.0352  0.0578  52  SER C C   
7811  O O   . SER C 52  ? 0.2094 0.3148 0.1997 0.1059  0.0450  0.0669  52  SER C O   
7812  C CB  . SER C 52  ? 0.2101 0.3414 0.1914 0.1250  0.0304  0.0606  52  SER C CB  
7813  O OG  . SER C 52  ? 0.2411 0.3626 0.2251 0.1246  0.0236  0.0594  52  SER C OG  
7814  N N   . GLY C 53  ? 0.1690 0.2756 0.1677 0.1042  0.0283  0.0508  53  GLY C N   
7815  C CA  . GLY C 53  ? 0.1677 0.2595 0.1709 0.0957  0.0313  0.0531  53  GLY C CA  
7816  C C   . GLY C 53  ? 0.1764 0.2666 0.1829 0.0877  0.0396  0.0536  53  GLY C C   
7817  O O   . GLY C 53  ? 0.1794 0.2583 0.1899 0.0802  0.0421  0.0544  53  GLY C O   
7818  N N   . THR C 54  ? 0.1742 0.2762 0.1792 0.0889  0.0440  0.0527  54  THR C N   
7819  C CA  . THR C 54  ? 0.2230 0.3258 0.2314 0.0810  0.0522  0.0528  54  THR C CA  
7820  C C   . THR C 54  ? 0.2004 0.3127 0.2141 0.0795  0.0460  0.0427  54  THR C C   
7821  O O   . THR C 54  ? 0.2051 0.3233 0.2217 0.0741  0.0520  0.0413  54  THR C O   
7822  C CB  . THR C 54  ? 0.1852 0.2957 0.1888 0.0823  0.0626  0.0594  54  THR C CB  
7823  O OG1 . THR C 54  ? 0.1965 0.3235 0.1960 0.0912  0.0578  0.0563  54  THR C OG1 
7824  C CG2 . THR C 54  ? 0.1912 0.2901 0.1902 0.0829  0.0700  0.0704  54  THR C CG2 
7825  N N   . ASN C 55  ? 0.1595 0.2734 0.1749 0.0842  0.0341  0.0358  55  ASN C N   
7826  C CA  . ASN C 55  ? 0.1689 0.2920 0.1890 0.0848  0.0273  0.0265  55  ASN C CA  
7827  C C   . ASN C 55  ? 0.1824 0.2988 0.2088 0.0758  0.0280  0.0244  55  ASN C C   
7828  O O   . ASN C 55  ? 0.2023 0.3053 0.2296 0.0701  0.0299  0.0283  55  ASN C O   
7829  C CB  . ASN C 55  ? 0.1793 0.3033 0.1994 0.0924  0.0144  0.0202  55  ASN C CB  
7830  C CG  . ASN C 55  ? 0.2386 0.3694 0.2524 0.1011  0.0133  0.0218  55  ASN C CG  
7831  O OD1 . ASN C 55  ? 0.2572 0.4029 0.2687 0.1063  0.0147  0.0191  55  ASN C OD1 
7832  N ND2 . ASN C 55  ? 0.1781 0.2995 0.1893 0.1027  0.0108  0.0260  55  ASN C ND2 
7833  N N   . ALA C 56  ? 0.1616 0.2889 0.1922 0.0748  0.0263  0.0177  56  ALA C N   
7834  C CA  . ALA C 56  ? 0.1619 0.2861 0.1986 0.0675  0.0248  0.0142  56  ALA C CA  
7835  C C   . ALA C 56  ? 0.1621 0.2825 0.2013 0.0714  0.0116  0.0087  56  ALA C C   
7836  O O   . ALA C 56  ? 0.1874 0.3159 0.2267 0.0793  0.0038  0.0029  56  ALA C O   
7837  C CB  . ALA C 56  ? 0.1444 0.2836 0.1849 0.0645  0.0295  0.0098  56  ALA C CB  
7838  N N   . MET C 57  ? 0.1400 0.2481 0.1811 0.0658  0.0092  0.0105  57  MET C N   
7839  C CA  . MET C 57  ? 0.1398 0.2423 0.1831 0.0681  -0.0027 0.0068  57  MET C CA  
7840  C C   . MET C 57  ? 0.1543 0.2635 0.2030 0.0656  -0.0066 0.0012  57  MET C C   
7841  O O   . MET C 57  ? 0.1848 0.3016 0.2361 0.0602  0.0005  0.0003  57  MET C O   
7842  C CB  . MET C 57  ? 0.1586 0.2460 0.2010 0.0633  -0.0036 0.0120  57  MET C CB  
7843  C CG  . MET C 57  ? 0.1510 0.2322 0.1886 0.0672  -0.0026 0.0169  57  MET C CG  
7844  S SD  . MET C 57  ? 0.2389 0.3051 0.2765 0.0634  -0.0077 0.0207  57  MET C SD  
7845  C CE  . MET C 57  ? 0.1850 0.2458 0.2242 0.0529  0.0033  0.0250  57  MET C CE  
7846  N N   . SER C 58  ? 0.1539 0.2604 0.2046 0.0698  -0.0181 -0.0026 58  SER C N   
7847  C CA  . SER C 58  ? 0.1280 0.2404 0.1836 0.0689  -0.0231 -0.0075 58  SER C CA  
7848  C C   . SER C 58  ? 0.1412 0.2450 0.1985 0.0602  -0.0231 -0.0041 58  SER C C   
7849  O O   . SER C 58  ? 0.1407 0.2331 0.1954 0.0557  -0.0205 0.0014  58  SER C O   
7850  C CB  . SER C 58  ? 0.1348 0.2475 0.1919 0.0779  -0.0356 -0.0129 58  SER C CB  
7851  O OG  . SER C 58  ? 0.1546 0.2522 0.2104 0.0781  -0.0431 -0.0100 58  SER C OG  
7852  N N   . ASP C 59  ? 0.1614 0.2721 0.2229 0.0582  -0.0263 -0.0077 59  ASP C N   
7853  C CA  . ASP C 59  ? 0.1395 0.2439 0.2023 0.0509  -0.0278 -0.0051 59  ASP C CA  
7854  C C   . ASP C 59  ? 0.1587 0.2495 0.2198 0.0531  -0.0375 -0.0021 59  ASP C C   
7855  O O   . ASP C 59  ? 0.1368 0.2184 0.1965 0.0467  -0.0364 0.0026  59  ASP C O   
7856  C CB  . ASP C 59  ? 0.1251 0.2417 0.1926 0.0496  -0.0304 -0.0098 59  ASP C CB  
7857  C CG  . ASP C 59  ? 0.1932 0.3175 0.2630 0.0597  -0.0396 -0.0154 59  ASP C CG  
7858  O OD1 . ASP C 59  ? 0.2098 0.3322 0.2779 0.0675  -0.0427 -0.0169 59  ASP C OD1 
7859  O OD2 . ASP C 59  ? 0.2132 0.3466 0.2869 0.0601  -0.0439 -0.0188 59  ASP C OD2 
7860  N N   . HIS C 60  ? 0.1818 0.2710 0.2430 0.0620  -0.0467 -0.0050 60  HIS C N   
7861  C CA  . HIS C 60  ? 0.1589 0.2345 0.2188 0.0638  -0.0560 -0.0024 60  HIS C CA  
7862  C C   . HIS C 60  ? 0.1632 0.2293 0.2193 0.0613  -0.0519 0.0025  60  HIS C C   
7863  O O   . HIS C 60  ? 0.1958 0.2513 0.2510 0.0575  -0.0554 0.0068  60  HIS C O   
7864  C CB  . HIS C 60  ? 0.1786 0.2525 0.2387 0.0721  -0.0645 -0.0071 60  HIS C CB  
7865  C CG  . HIS C 60  ? 0.2488 0.3290 0.3113 0.0737  -0.0677 -0.0113 60  HIS C CG  
7866  N ND1 . HIS C 60  ? 0.2592 0.3365 0.3232 0.0700  -0.0721 -0.0090 60  HIS C ND1 
7867  C CD2 . HIS C 60  ? 0.2672 0.3573 0.3306 0.0788  -0.0671 -0.0175 60  HIS C CD2 
7868  C CE1 . HIS C 60  ? 0.2197 0.3045 0.2856 0.0731  -0.0740 -0.0133 60  HIS C CE1 
7869  N NE2 . HIS C 60  ? 0.2253 0.3177 0.2909 0.0784  -0.0712 -0.0188 60  HIS C NE2 
7870  N N   . GLN C 61  ? 0.1678 0.2385 0.2217 0.0636  -0.0446 0.0022  61  GLN C N   
7871  C CA  . GLN C 61  ? 0.1683 0.2312 0.2185 0.0620  -0.0406 0.0071  61  GLN C CA  
7872  C C   . GLN C 61  ? 0.1461 0.2041 0.1960 0.0526  -0.0335 0.0124  61  GLN C C   
7873  O O   . GLN C 61  ? 0.1725 0.2212 0.2209 0.0499  -0.0350 0.0165  61  GLN C O   
7874  C CB  . GLN C 61  ? 0.1471 0.2169 0.1945 0.0668  -0.0340 0.0064  61  GLN C CB  
7875  C CG  . GLN C 61  ? 0.1994 0.2721 0.2460 0.0765  -0.0417 0.0016  61  GLN C CG  
7876  C CD  . GLN C 61  ? 0.1567 0.2389 0.2001 0.0814  -0.0351 0.0010  61  GLN C CD  
7877  O OE1 . GLN C 61  ? 0.1790 0.2721 0.2231 0.0814  -0.0290 -0.0008 61  GLN C OE1 
7878  N NE2 . GLN C 61  ? 0.1838 0.2631 0.2237 0.0853  -0.0361 0.0027  61  GLN C NE2 
7879  N N   . TRP C 62  ? 0.1685 0.2331 0.2200 0.0475  -0.0259 0.0117  62  TRP C N   
7880  C CA  . TRP C 62  ? 0.1765 0.2369 0.2282 0.0385  -0.0190 0.0153  62  TRP C CA  
7881  C C   . TRP C 62  ? 0.1668 0.2223 0.2197 0.0343  -0.0261 0.0165  62  TRP C C   
7882  O O   . TRP C 62  ? 0.1779 0.2266 0.2297 0.0290  -0.0238 0.0204  62  TRP C O   
7883  C CB  . TRP C 62  ? 0.1656 0.2349 0.2194 0.0336  -0.0098 0.0131  62  TRP C CB  
7884  C CG  . TRP C 62  ? 0.2167 0.2871 0.2685 0.0344  0.0002  0.0149  62  TRP C CG  
7885  C CD1 . TRP C 62  ? 0.2252 0.3044 0.2765 0.0397  0.0025  0.0127  62  TRP C CD1 
7886  C CD2 . TRP C 62  ? 0.2640 0.3266 0.3138 0.0301  0.0095  0.0198  62  TRP C CD2 
7887  N NE1 . TRP C 62  ? 0.2328 0.3098 0.2815 0.0385  0.0127  0.0167  62  TRP C NE1 
7888  C CE2 . TRP C 62  ? 0.2858 0.3519 0.3337 0.0330  0.0170  0.0211  62  TRP C CE2 
7889  C CE3 . TRP C 62  ? 0.3156 0.3689 0.3650 0.0244  0.0121  0.0232  62  TRP C CE3 
7890  C CZ2 . TRP C 62  ? 0.3325 0.3916 0.3781 0.0307  0.0269  0.0263  62  TRP C CZ2 
7891  C CZ3 . TRP C 62  ? 0.3355 0.3824 0.3831 0.0225  0.0219  0.0273  62  TRP C CZ3 
7892  C CH2 . TRP C 62  ? 0.3209 0.3700 0.3667 0.0257  0.0291  0.0292  62  TRP C CH2 
7893  N N   . ALA C 63  ? 0.1520 0.2114 0.2072 0.0369  -0.0347 0.0134  63  ALA C N   
7894  C CA  . ALA C 63  ? 0.1734 0.2278 0.2292 0.0336  -0.0422 0.0155  63  ALA C CA  
7895  C C   . ALA C 63  ? 0.1747 0.2175 0.2283 0.0351  -0.0481 0.0194  63  ALA C C   
7896  O O   . ALA C 63  ? 0.1868 0.2241 0.2397 0.0293  -0.0491 0.0236  63  ALA C O   
7897  C CB  . ALA C 63  ? 0.1350 0.1952 0.1935 0.0377  -0.0507 0.0119  63  ALA C CB  
7898  N N   . ALA C 64  ? 0.1702 0.2105 0.2230 0.0425  -0.0520 0.0178  64  ALA C N   
7899  C CA  . ALA C 64  ? 0.1651 0.1956 0.2163 0.0437  -0.0573 0.0207  64  ALA C CA  
7900  C C   . ALA C 64  ? 0.1661 0.1933 0.2152 0.0383  -0.0495 0.0253  64  ALA C C   
7901  O O   . ALA C 64  ? 0.1996 0.2201 0.2482 0.0348  -0.0528 0.0290  64  ALA C O   
7902  C CB  . ALA C 64  ? 0.1599 0.1906 0.2106 0.0526  -0.0614 0.0168  64  ALA C CB  
7903  N N   . MET C 65  ? 0.1615 0.1934 0.2096 0.0376  -0.0392 0.0253  65  MET C N   
7904  C CA  . MET C 65  ? 0.1516 0.1799 0.1980 0.0334  -0.0314 0.0295  65  MET C CA  
7905  C C   . MET C 65  ? 0.1536 0.1802 0.2011 0.0248  -0.0298 0.0318  65  MET C C   
7906  O O   . MET C 65  ? 0.1571 0.1791 0.2037 0.0214  -0.0284 0.0354  65  MET C O   
7907  C CB  . MET C 65  ? 0.1365 0.1690 0.1818 0.0344  -0.0206 0.0293  65  MET C CB  
7908  C CG  . MET C 65  ? 0.2046 0.2396 0.2477 0.0426  -0.0208 0.0283  65  MET C CG  
7909  S SD  . MET C 65  ? 0.2994 0.3385 0.3407 0.0429  -0.0073 0.0300  65  MET C SD  
7910  C CE  . MET C 65  ? 0.1895 0.2203 0.2287 0.0406  -0.0014 0.0361  65  MET C CE  
7911  N N   . ILE C 66  ? 0.1878 0.2196 0.2372 0.0213  -0.0297 0.0295  66  ILE C N   
7912  C CA  . ILE C 66  ? 0.1537 0.1861 0.2037 0.0130  -0.0272 0.0309  66  ILE C CA  
7913  C C   . ILE C 66  ? 0.1892 0.2166 0.2386 0.0106  -0.0354 0.0345  66  ILE C C   
7914  O O   . ILE C 66  ? 0.1608 0.1871 0.2097 0.0045  -0.0326 0.0372  66  ILE C O   
7915  C CB  . ILE C 66  ? 0.1659 0.2072 0.2182 0.0103  -0.0260 0.0271  66  ILE C CB  
7916  C CG1 . ILE C 66  ? 0.2301 0.2758 0.2832 0.0096  -0.0153 0.0243  66  ILE C CG1 
7917  C CG2 . ILE C 66  ? 0.2331 0.2767 0.2858 0.0025  -0.0263 0.0281  66  ILE C CG2 
7918  C CD1 . ILE C 66  ? 0.2558 0.3118 0.3117 0.0075  -0.0140 0.0197  66  ILE C CD1 
7919  N N   . THR C 67  ? 0.1928 0.2170 0.2424 0.0153  -0.0455 0.0346  67  THR C N   
7920  C CA  . THR C 67  ? 0.1920 0.2102 0.2412 0.0128  -0.0536 0.0386  67  THR C CA  
7921  C C   . THR C 67  ? 0.2224 0.2341 0.2708 0.0156  -0.0558 0.0405  67  THR C C   
7922  O O   . THR C 67  ? 0.2224 0.2283 0.2710 0.0147  -0.0638 0.0431  67  THR C O   
7923  C CB  . THR C 67  ? 0.1925 0.2099 0.2430 0.0156  -0.0637 0.0378  67  THR C CB  
7924  O OG1 . THR C 67  ? 0.2383 0.2560 0.2898 0.0240  -0.0665 0.0333  67  THR C OG1 
7925  C CG2 . THR C 67  ? 0.2010 0.2266 0.2523 0.0117  -0.0621 0.0368  67  THR C CG2 
7926  N N   . GLY C 68  ? 0.1975 0.2102 0.2449 0.0186  -0.0487 0.0395  68  GLY C N   
7927  C CA  . GLY C 68  ? 0.1671 0.1759 0.2137 0.0219  -0.0507 0.0408  68  GLY C CA  
7928  C C   . GLY C 68  ? 0.1928 0.1989 0.2392 0.0157  -0.0509 0.0453  68  GLY C C   
7929  O O   . GLY C 68  ? 0.2207 0.2292 0.2670 0.0097  -0.0450 0.0472  68  GLY C O   
7930  N N   . ASP C 69  ? 0.2039 0.2059 0.2507 0.0170  -0.0577 0.0465  69  ASP C N   
7931  C CA  . ASP C 69  ? 0.2180 0.2185 0.2652 0.0111  -0.0591 0.0506  69  ASP C CA  
7932  C C   . ASP C 69  ? 0.2180 0.2213 0.2645 0.0134  -0.0526 0.0512  69  ASP C C   
7933  O O   . ASP C 69  ? 0.2113 0.2143 0.2576 0.0191  -0.0550 0.0496  69  ASP C O   
7934  C CB  . ASP C 69  ? 0.2348 0.2293 0.2820 0.0101  -0.0679 0.0495  69  ASP C CB  
7935  C CG  . ASP C 69  ? 0.2996 0.2933 0.3476 0.0033  -0.0696 0.0537  69  ASP C CG  
7936  O OD1 . ASP C 69  ? 0.3125 0.3111 0.3614 -0.0003 -0.0651 0.0581  69  ASP C OD1 
7937  O OD2 . ASP C 69  ? 0.2496 0.2379 0.2977 0.0015  -0.0753 0.0526  69  ASP C OD2 
7938  N N   . GLU C 70  ? 0.2204 0.2268 0.2665 0.0093  -0.0445 0.0533  70  GLU C N   
7939  C CA  . GLU C 70  ? 0.2073 0.2163 0.2528 0.0121  -0.0374 0.0543  70  GLU C CA  
7940  C C   . GLU C 70  ? 0.2598 0.2703 0.3064 0.0099  -0.0404 0.0568  70  GLU C C   
7941  O O   . GLU C 70  ? 0.2184 0.2322 0.2649 0.0122  -0.0346 0.0580  70  GLU C O   
7942  C CB  . GLU C 70  ? 0.1974 0.2083 0.2425 0.0094  -0.0269 0.0546  70  GLU C CB  
7943  C CG  . GLU C 70  ? 0.2223 0.2328 0.2666 0.0120  -0.0217 0.0518  70  GLU C CG  
7944  C CD  . GLU C 70  ? 0.2292 0.2394 0.2719 0.0205  -0.0204 0.0508  70  GLU C CD  
7945  O OE1 . GLU C 70  ? 0.1975 0.2083 0.2394 0.0248  -0.0208 0.0524  70  GLU C OE1 
7946  O OE2 . GLU C 70  ? 0.2305 0.2414 0.2727 0.0229  -0.0189 0.0483  70  GLU C OE2 
7947  N N   . ALA C 71  ? 0.2330 0.2415 0.2810 0.0059  -0.0494 0.0578  71  ALA C N   
7948  C CA  . ALA C 71  ? 0.2577 0.2684 0.3073 0.0022  -0.0526 0.0603  71  ALA C CA  
7949  C C   . ALA C 71  ? 0.2789 0.2930 0.3288 0.0086  -0.0520 0.0591  71  ALA C C   
7950  O O   . ALA C 71  ? 0.2437 0.2563 0.2927 0.0154  -0.0545 0.0562  71  ALA C O   
7951  C CB  . ALA C 71  ? 0.2486 0.2546 0.2998 -0.0026 -0.0629 0.0614  71  ALA C CB  
7952  N N   . TYR C 72  ? 0.2747 0.2947 0.3258 0.0067  -0.0490 0.0612  72  TYR C N   
7953  C CA  . TYR C 72  ? 0.2676 0.2927 0.3189 0.0130  -0.0482 0.0605  72  TYR C CA  
7954  C C   . TYR C 72  ? 0.2513 0.2756 0.3041 0.0139  -0.0580 0.0583  72  TYR C C   
7955  O O   . TYR C 72  ? 0.2662 0.2927 0.3181 0.0213  -0.0592 0.0556  72  TYR C O   
7956  C CB  . TYR C 72  ? 0.2547 0.2876 0.3076 0.0106  -0.0435 0.0630  72  TYR C CB  
7957  C CG  . TYR C 72  ? 0.2508 0.2901 0.3035 0.0188  -0.0407 0.0626  72  TYR C CG  
7958  C CD1 . TYR C 72  ? 0.3087 0.3477 0.3588 0.0259  -0.0322 0.0632  72  TYR C CD1 
7959  C CD2 . TYR C 72  ? 0.2203 0.2658 0.2751 0.0194  -0.0467 0.0618  72  TYR C CD2 
7960  C CE1 . TYR C 72  ? 0.2874 0.3324 0.3367 0.0341  -0.0298 0.0638  72  TYR C CE1 
7961  C CE2 . TYR C 72  ? 0.2570 0.3101 0.3113 0.0275  -0.0445 0.0615  72  TYR C CE2 
7962  C CZ  . TYR C 72  ? 0.3204 0.3731 0.3716 0.0352  -0.0361 0.0629  72  TYR C CZ  
7963  O OH  . TYR C 72  ? 0.3740 0.4342 0.4241 0.0439  -0.0338 0.0636  72  TYR C OH  
7964  N N   . ALA C 73  ? 0.2332 0.2545 0.2885 0.0062  -0.0651 0.0593  73  ALA C N   
7965  C CA  . ALA C 73  ? 0.2683 0.2869 0.3251 0.0054  -0.0737 0.0562  73  ALA C CA  
7966  C C   . ALA C 73  ? 0.2766 0.2844 0.3328 0.0010  -0.0790 0.0550  73  ALA C C   
7967  O O   . ALA C 73  ? 0.2807 0.2862 0.3376 -0.0060 -0.0793 0.0593  73  ALA C O   
7968  C CB  . ALA C 73  ? 0.2708 0.2964 0.3317 -0.0005 -0.0770 0.0588  73  ALA C CB  
7969  N N   . GLY C 74  ? 0.2775 0.2797 0.3326 0.0055  -0.0830 0.0494  74  GLY C N   
7970  C CA  . GLY C 74  ? 0.3030 0.2945 0.3583 0.0022  -0.0887 0.0482  74  GLY C CA  
7971  C C   . GLY C 74  ? 0.2823 0.2705 0.3348 0.0045  -0.0854 0.0475  74  GLY C C   
7972  O O   . GLY C 74  ? 0.2628 0.2438 0.3156 0.0004  -0.0890 0.0487  74  GLY C O   
7973  N N   . SER C 75  ? 0.2932 0.2866 0.3432 0.0110  -0.0789 0.0460  75  SER C N   
7974  C CA  . SER C 75  ? 0.2569 0.2487 0.3049 0.0132  -0.0759 0.0451  75  SER C CA  
7975  C C   . SER C 75  ? 0.2544 0.2391 0.3021 0.0149  -0.0815 0.0406  75  SER C C   
7976  O O   . SER C 75  ? 0.2853 0.2681 0.3332 0.0189  -0.0853 0.0360  75  SER C O   
7977  C CB  . SER C 75  ? 0.2766 0.2745 0.3225 0.0207  -0.0692 0.0437  75  SER C CB  
7978  O OG  . SER C 75  ? 0.2494 0.2461 0.2942 0.0235  -0.0680 0.0416  75  SER C OG  
7979  N N   . ARG C 76  ? 0.2587 0.2400 0.3062 0.0121  -0.0822 0.0421  76  ARG C N   
7980  C CA  A ARG C 76  ? 0.2894 0.2643 0.3368 0.0143  -0.0871 0.0383  76  ARG C CA  
7981  C CA  B ARG C 76  ? 0.2896 0.2644 0.3370 0.0143  -0.0873 0.0383  76  ARG C CA  
7982  C C   . ARG C 76  ? 0.2546 0.2326 0.3005 0.0231  -0.0857 0.0321  76  ARG C C   
7983  O O   . ARG C 76  ? 0.2997 0.2729 0.3463 0.0262  -0.0907 0.0275  76  ARG C O   
7984  C CB  A ARG C 76  ? 0.2746 0.2488 0.3216 0.0110  -0.0867 0.0413  76  ARG C CB  
7985  C CB  B ARG C 76  ? 0.2745 0.2479 0.3216 0.0109  -0.0873 0.0412  76  ARG C CB  
7986  C CG  A ARG C 76  ? 0.3121 0.2817 0.3589 0.0145  -0.0906 0.0378  76  ARG C CG  
7987  C CG  B ARG C 76  ? 0.2969 0.2725 0.3429 0.0170  -0.0861 0.0372  76  ARG C CG  
7988  C CD  A ARG C 76  ? 0.3261 0.2968 0.3726 0.0107  -0.0904 0.0416  76  ARG C CD  
7989  C CD  B ARG C 76  ? 0.3240 0.3000 0.3700 0.0135  -0.0866 0.0403  76  ARG C CD  
7990  N NE  A ARG C 76  ? 0.3262 0.3060 0.3721 0.0112  -0.0842 0.0428  76  ARG C NE  
7991  N NE  B ARG C 76  ? 0.3365 0.3188 0.3826 0.0087  -0.0818 0.0452  76  ARG C NE  
7992  C CZ  A ARG C 76  ? 0.3229 0.3070 0.3691 0.0055  -0.0808 0.0479  76  ARG C CZ  
7993  C CZ  B ARG C 76  ? 0.3059 0.2954 0.3523 0.0110  -0.0769 0.0450  76  ARG C CZ  
7994  N NH1 A ARG C 76  ? 0.2919 0.2736 0.3384 -0.0013 -0.0825 0.0525  76  ARG C NH1 
7995  N NH1 B ARG C 76  ? 0.2600 0.2524 0.3065 0.0179  -0.0759 0.0403  76  ARG C NH1 
7996  N NH2 A ARG C 76  ? 0.2919 0.2835 0.3387 0.0062  -0.0760 0.0488  76  ARG C NH2 
7997  N NH2 B ARG C 76  ? 0.2787 0.2732 0.3261 0.0059  -0.0732 0.0499  76  ARG C NH2 
7998  N N   . ASN C 77  ? 0.2299 0.2160 0.2744 0.0271  -0.0790 0.0322  77  ASN C N   
7999  C CA  . ASN C 77  ? 0.2623 0.2531 0.3054 0.0351  -0.0770 0.0273  77  ASN C CA  
8000  C C   . ASN C 77  ? 0.2898 0.2822 0.3325 0.0389  -0.0788 0.0239  77  ASN C C   
8001  O O   . ASN C 77  ? 0.2798 0.2745 0.3218 0.0447  -0.0797 0.0188  77  ASN C O   
8002  C CB  . ASN C 77  ? 0.2480 0.2462 0.2903 0.0376  -0.0697 0.0296  77  ASN C CB  
8003  C CG  . ASN C 77  ? 0.2217 0.2192 0.2653 0.0332  -0.0686 0.0329  77  ASN C CG  
8004  O OD1 . ASN C 77  ? 0.2642 0.2625 0.3089 0.0285  -0.0657 0.0379  77  ASN C OD1 
8005  N ND2 . ASN C 77  ? 0.2511 0.2483 0.2951 0.0347  -0.0711 0.0302  77  ASN C ND2 
8006  N N   . TYR C 78  ? 0.2644 0.2570 0.3079 0.0358  -0.0795 0.0264  78  TYR C N   
8007  C CA  . TYR C 78  ? 0.2575 0.2520 0.3012 0.0389  -0.0826 0.0227  78  TYR C CA  
8008  C C   . TYR C 78  ? 0.2513 0.2375 0.2971 0.0389  -0.0909 0.0174  78  TYR C C   
8009  O O   . TYR C 78  ? 0.2386 0.2267 0.2839 0.0444  -0.0931 0.0116  78  TYR C O   
8010  C CB  . TYR C 78  ? 0.2731 0.2696 0.3182 0.0349  -0.0828 0.0265  78  TYR C CB  
8011  C CG  . TYR C 78  ? 0.2778 0.2754 0.3246 0.0364  -0.0884 0.0224  78  TYR C CG  
8012  C CD1 . TYR C 78  ? 0.2410 0.2477 0.2858 0.0434  -0.0860 0.0193  78  TYR C CD1 
8013  C CD2 . TYR C 78  ? 0.2635 0.2530 0.3140 0.0307  -0.0965 0.0217  78  TYR C CD2 
8014  C CE1 . TYR C 78  ? 0.2551 0.2640 0.3016 0.0448  -0.0915 0.0149  78  TYR C CE1 
8015  C CE2 . TYR C 78  ? 0.2133 0.2038 0.2662 0.0319  -0.1024 0.0172  78  TYR C CE2 
8016  C CZ  . TYR C 78  ? 0.2401 0.2408 0.2908 0.0390  -0.0999 0.0133  78  TYR C CZ  
8017  O OH  . TYR C 78  ? 0.3044 0.3076 0.3574 0.0402  -0.1059 0.0081  78  TYR C OH  
8018  N N   . TYR C 79  ? 0.2414 0.2178 0.2893 0.0329  -0.0958 0.0194  79  TYR C N   
8019  C CA  . TYR C 79  ? 0.2999 0.2660 0.3503 0.0330  -0.1045 0.0150  79  TYR C CA  
8020  C C   . TYR C 79  ? 0.2904 0.2562 0.3394 0.0393  -0.1045 0.0096  79  TYR C C   
8021  O O   . TYR C 79  ? 0.3192 0.2807 0.3694 0.0433  -0.1102 0.0031  79  TYR C O   
8022  C CB  . TYR C 79  ? 0.2568 0.2125 0.3098 0.0248  -0.1095 0.0200  79  TYR C CB  
8023  C CG  . TYR C 79  ? 0.2813 0.2381 0.3363 0.0181  -0.1102 0.0251  79  TYR C CG  
8024  C CD1 . TYR C 79  ? 0.2743 0.2286 0.3325 0.0172  -0.1165 0.0226  79  TYR C CD1 
8025  C CD2 . TYR C 79  ? 0.2988 0.2604 0.3529 0.0128  -0.1049 0.0320  79  TYR C CD2 
8026  C CE1 . TYR C 79  ? 0.3404 0.2978 0.4010 0.0110  -0.1172 0.0273  79  TYR C CE1 
8027  C CE2 . TYR C 79  ? 0.3372 0.3014 0.3933 0.0068  -0.1055 0.0366  79  TYR C CE2 
8028  C CZ  . TYR C 79  ? 0.4053 0.3679 0.4648 0.0059  -0.1115 0.0344  79  TYR C CZ  
8029  O OH  . TYR C 79  ? 0.4801 0.4473 0.5421 -0.0003 -0.1123 0.0389  79  TYR C OH  
8030  N N   . ASP C 80  ? 0.3160 0.2869 0.3629 0.0403  -0.0986 0.0119  80  ASP C N   
8031  C CA  . ASP C 80  ? 0.2666 0.2400 0.3126 0.0464  -0.0980 0.0071  80  ASP C CA  
8032  C C   . ASP C 80  ? 0.2933 0.2751 0.3378 0.0533  -0.0956 0.0019  80  ASP C C   
8033  O O   . ASP C 80  ? 0.2938 0.2751 0.3384 0.0586  -0.0988 -0.0048 80  ASP C O   
8034  C CB  . ASP C 80  ? 0.2737 0.2526 0.3186 0.0458  -0.0922 0.0108  80  ASP C CB  
8035  C CG  . ASP C 80  ? 0.3034 0.2753 0.3494 0.0399  -0.0949 0.0152  80  ASP C CG  
8036  O OD1 . ASP C 80  ? 0.3708 0.3326 0.4186 0.0366  -0.1015 0.0155  80  ASP C OD1 
8037  O OD2 . ASP C 80  ? 0.3831 0.3601 0.4285 0.0385  -0.0906 0.0186  80  ASP C OD2 
8038  N N   . LEU C 81  ? 0.2464 0.2365 0.2893 0.0536  -0.0901 0.0048  81  LEU C N   
8039  C CA  . LEU C 81  ? 0.2459 0.2449 0.2870 0.0598  -0.0877 0.0010  81  LEU C CA  
8040  C C   . LEU C 81  ? 0.2835 0.2791 0.3256 0.0618  -0.0947 -0.0053 81  LEU C C   
8041  O O   . LEU C 81  ? 0.2638 0.2628 0.3049 0.0678  -0.0964 -0.0122 81  LEU C O   
8042  C CB  . LEU C 81  ? 0.2663 0.2740 0.3057 0.0597  -0.0804 0.0067  81  LEU C CB  
8043  C CG  . LEU C 81  ? 0.2889 0.3067 0.3259 0.0660  -0.0770 0.0043  81  LEU C CG  
8044  C CD1 . LEU C 81  ? 0.2059 0.2277 0.2417 0.0708  -0.0752 0.0004  81  LEU C CD1 
8045  C CD2 . LEU C 81  ? 0.2208 0.2450 0.2567 0.0656  -0.0700 0.0112  81  LEU C CD2 
8046  N N   . LYS C 82  ? 0.2304 0.2195 0.2749 0.0568  -0.0993 -0.0036 82  LYS C N   
8047  C CA  . LYS C 82  ? 0.2662 0.2506 0.3130 0.0580  -0.1075 -0.0100 82  LYS C CA  
8048  C C   . LYS C 82  ? 0.3227 0.2981 0.3712 0.0613  -0.1144 -0.0173 82  LYS C C   
8049  O O   . LYS C 82  ? 0.3483 0.3248 0.3970 0.0667  -0.1187 -0.0256 82  LYS C O   
8050  C CB  . LYS C 82  ? 0.2665 0.2438 0.3168 0.0507  -0.1122 -0.0060 82  LYS C CB  
8051  C CG  . LYS C 82  ? 0.2767 0.2484 0.3310 0.0508  -0.1218 -0.0124 82  LYS C CG  
8052  C CD  . LYS C 82  ? 0.3158 0.2826 0.3741 0.0426  -0.1258 -0.0072 82  LYS C CD  
8053  C CE  . LYS C 82  ? 0.2994 0.2631 0.3625 0.0423  -0.1351 -0.0135 82  LYS C CE  
8054  N NZ  . LYS C 82  ? 0.4051 0.3535 0.4721 0.0434  -0.1450 -0.0198 82  LYS C NZ  
8055  N N   . ASP C 83  ? 0.2817 0.2486 0.3312 0.0584  -0.1157 -0.0147 83  ASP C N   
8056  C CA  . ASP C 83  ? 0.2867 0.2452 0.3379 0.0620  -0.1221 -0.0212 83  ASP C CA  
8057  C C   . ASP C 83  ? 0.3281 0.2965 0.3763 0.0700  -0.1184 -0.0273 83  ASP C C   
8058  O O   . ASP C 83  ? 0.3778 0.3439 0.4269 0.0756  -0.1240 -0.0363 83  ASP C O   
8059  C CB  . ASP C 83  ? 0.2658 0.2160 0.3181 0.0576  -0.1229 -0.0159 83  ASP C CB  
8060  C CG  . ASP C 83  ? 0.3615 0.3012 0.4167 0.0493  -0.1275 -0.0098 83  ASP C CG  
8061  O OD1 . ASP C 83  ? 0.3609 0.2984 0.4183 0.0469  -0.1312 -0.0103 83  ASP C OD1 
8062  O OD2 . ASP C 83  ? 0.4488 0.3834 0.5043 0.0450  -0.1275 -0.0043 83  ASP C OD2 
8063  N N   . LYS C 84  ? 0.3511 0.3306 0.3963 0.0706  -0.1094 -0.0229 84  LYS C N   
8064  C CA  . LYS C 84  ? 0.3262 0.3158 0.3688 0.0775  -0.1057 -0.0277 84  LYS C CA  
8065  C C   . LYS C 84  ? 0.3298 0.3261 0.3707 0.0831  -0.1070 -0.0347 84  LYS C C   
8066  O O   . LYS C 84  ? 0.3423 0.3411 0.3825 0.0894  -0.1097 -0.0431 84  LYS C O   
8067  C CB  . LYS C 84  ? 0.2885 0.2884 0.3290 0.0764  -0.0962 -0.0209 84  LYS C CB  
8068  C CG  . LYS C 84  ? 0.2703 0.2792 0.3093 0.0820  -0.0929 -0.0247 84  LYS C CG  
8069  C CD  . LYS C 84  ? 0.2711 0.2738 0.3123 0.0831  -0.0975 -0.0282 84  LYS C CD  
8070  C CE  . LYS C 84  ? 0.2931 0.3063 0.3331 0.0890  -0.0945 -0.0327 84  LYS C CE  
8071  N NZ  . LYS C 84  ? 0.3628 0.3711 0.4050 0.0906  -0.0990 -0.0361 84  LYS C NZ  
8072  N N   . ALA C 85  ? 0.2953 0.2955 0.3356 0.0811  -0.1053 -0.0318 85  ALA C N   
8073  C CA  . ALA C 85  ? 0.3179 0.3260 0.3563 0.0865  -0.1066 -0.0383 85  ALA C CA  
8074  C C   . ALA C 85  ? 0.3277 0.3267 0.3693 0.0888  -0.1171 -0.0480 85  ALA C C   
8075  O O   . ALA C 85  ? 0.3273 0.3327 0.3675 0.0952  -0.1194 -0.0568 85  ALA C O   
8076  C CB  . ALA C 85  ? 0.2837 0.2986 0.3208 0.0839  -0.1026 -0.0324 85  ALA C CB  
8077  N N   . LYS C 86  ? 0.3577 0.3419 0.4039 0.0838  -0.1238 -0.0469 86  LYS C N   
8078  C CA  . LYS C 86  ? 0.3711 0.3439 0.4216 0.0863  -0.1348 -0.0563 86  LYS C CA  
8079  C C   . LYS C 86  ? 0.3605 0.3313 0.4106 0.0924  -0.1371 -0.0635 86  LYS C C   
8080  O O   . LYS C 86  ? 0.3780 0.3473 0.4296 0.0985  -0.1437 -0.0746 86  LYS C O   
8081  C CB  . LYS C 86  ? 0.3769 0.3333 0.4328 0.0788  -0.1418 -0.0519 86  LYS C CB  
8082  C CG  . LYS C 86  ? 0.3344 0.2762 0.3961 0.0807  -0.1544 -0.0609 86  LYS C CG  
8083  C CD  . LYS C 86  ? 0.3671 0.3133 0.4310 0.0839  -0.1593 -0.0692 86  LYS C CD  
8084  C CE  . LYS C 86  ? 0.3952 0.3267 0.4661 0.0869  -0.1726 -0.0800 86  LYS C CE  
8085  N NZ  . LYS C 86  ? 0.3709 0.3095 0.4441 0.0912  -0.1769 -0.0902 86  LYS C NZ  
8086  N N   . GLU C 87  ? 0.3284 0.3002 0.3767 0.0911  -0.1318 -0.0579 87  GLU C N   
8087  C CA  . GLU C 87  ? 0.2915 0.2634 0.3395 0.0968  -0.1334 -0.0642 87  GLU C CA  
8088  C C   . GLU C 87  ? 0.3562 0.3435 0.4000 0.1045  -0.1294 -0.0713 87  GLU C C   
8089  O O   . GLU C 87  ? 0.3351 0.3223 0.3794 0.1112  -0.1349 -0.0820 87  GLU C O   
8090  C CB  . GLU C 87  ? 0.3380 0.3098 0.3854 0.0934  -0.1283 -0.0562 87  GLU C CB  
8091  C CG  . GLU C 87  ? 0.3957 0.3720 0.4423 0.0997  -0.1282 -0.0619 87  GLU C CG  
8092  C CD  . GLU C 87  ? 0.4518 0.4334 0.4975 0.0971  -0.1214 -0.0544 87  GLU C CD  
8093  O OE1 . GLU C 87  ? 0.4652 0.4460 0.5109 0.0904  -0.1171 -0.0449 87  GLU C OE1 
8094  O OE2 . GLU C 87  ? 0.5222 0.5093 0.5676 0.1020  -0.1208 -0.0585 87  GLU C OE2 
8095  N N   . LEU C 88  ? 0.3526 0.3536 0.3924 0.1038  -0.1201 -0.0655 88  LEU C N   
8096  C CA  . LEU C 88  ? 0.3452 0.3618 0.3805 0.1106  -0.1154 -0.0704 88  LEU C CA  
8097  C C   . LEU C 88  ? 0.3335 0.3559 0.3674 0.1158  -0.1189 -0.0793 88  LEU C C   
8098  O O   . LEU C 88  ? 0.3887 0.4178 0.4208 0.1231  -0.1211 -0.0893 88  LEU C O   
8099  C CB  . LEU C 88  ? 0.3415 0.3696 0.3735 0.1081  -0.1049 -0.0608 88  LEU C CB  
8100  C CG  . LEU C 88  ? 0.2700 0.2977 0.3030 0.1049  -0.1003 -0.0542 88  LEU C CG  
8101  C CD1 . LEU C 88  ? 0.2774 0.3168 0.3075 0.1036  -0.0908 -0.0465 88  LEU C CD1 
8102  C CD2 . LEU C 88  ? 0.2764 0.3065 0.3097 0.1103  -0.1025 -0.0616 88  LEU C CD2 
8103  N N   . PHE C 89  ? 0.3495 0.3708 0.3840 0.1124  -0.1196 -0.0761 89  PHE C N   
8104  C CA  . PHE C 89  ? 0.3327 0.3626 0.3654 0.1171  -0.1218 -0.0835 89  PHE C CA  
8105  C C   . PHE C 89  ? 0.3662 0.3845 0.4046 0.1170  -0.1326 -0.0914 89  PHE C C   
8106  O O   . PHE C 89  ? 0.3662 0.3915 0.4041 0.1220  -0.1360 -0.1004 89  PHE C O   
8107  C CB  . PHE C 89  ? 0.3227 0.3633 0.3520 0.1143  -0.1143 -0.0746 89  PHE C CB  
8108  C CG  . PHE C 89  ? 0.3130 0.3601 0.3390 0.1120  -0.1045 -0.0643 89  PHE C CG  
8109  C CD1 . PHE C 89  ? 0.3348 0.3942 0.3561 0.1174  -0.0991 -0.0661 89  PHE C CD1 
8110  C CD2 . PHE C 89  ? 0.3289 0.3704 0.3567 0.1047  -0.1008 -0.0533 89  PHE C CD2 
8111  C CE1 . PHE C 89  ? 0.2811 0.3459 0.3003 0.1153  -0.0907 -0.0571 89  PHE C CE1 
8112  C CE2 . PHE C 89  ? 0.3366 0.3835 0.3622 0.1030  -0.0923 -0.0448 89  PHE C CE2 
8113  C CZ  . PHE C 89  ? 0.2623 0.3204 0.2839 0.1083  -0.0875 -0.0467 89  PHE C CZ  
8114  N N   . ASN C 90  ? 0.3604 0.3614 0.4043 0.1115  -0.1383 -0.0885 90  ASN C N   
8115  C CA  . ASN C 90  ? 0.3544 0.3423 0.4050 0.1097  -0.1490 -0.0939 90  ASN C CA  
8116  C C   . ASN C 90  ? 0.3553 0.3487 0.4064 0.1055  -0.1479 -0.0898 90  ASN C C   
8117  O O   . ASN C 90  ? 0.4204 0.4109 0.4761 0.1062  -0.1557 -0.0972 90  ASN C O   
8118  C CB  . ASN C 90  ? 0.3844 0.3703 0.4376 0.1179  -0.1579 -0.1097 90  ASN C CB  
8119  C CG  . ASN C 90  ? 0.3866 0.3536 0.4488 0.1157  -0.1707 -0.1152 90  ASN C CG  
8120  O OD1 . ASN C 90  ? 0.4070 0.3599 0.4729 0.1082  -0.1733 -0.1068 90  ASN C OD1 
8121  N ND2 . ASN C 90  ? 0.4156 0.3821 0.4816 0.1223  -0.1789 -0.1293 90  ASN C ND2 
8122  N N   . TYR C 91  ? 0.3703 0.3723 0.4174 0.1011  -0.1385 -0.0783 91  TYR C N   
8123  C CA  . TYR C 91  ? 0.3223 0.3310 0.3694 0.0970  -0.1366 -0.0733 91  TYR C CA  
8124  C C   . TYR C 91  ? 0.3315 0.3279 0.3831 0.0878  -0.1387 -0.0645 91  TYR C C   
8125  O O   . TYR C 91  ? 0.2835 0.2725 0.3348 0.0843  -0.1359 -0.0575 91  TYR C O   
8126  C CB  . TYR C 91  ? 0.2710 0.2969 0.3111 0.0987  -0.1255 -0.0665 91  TYR C CB  
8127  C CG  . TYR C 91  ? 0.3078 0.3485 0.3432 0.1070  -0.1237 -0.0745 91  TYR C CG  
8128  C CD1 . TYR C 91  ? 0.3183 0.3575 0.3555 0.1131  -0.1310 -0.0878 91  TYR C CD1 
8129  C CD2 . TYR C 91  ? 0.2628 0.3190 0.2920 0.1090  -0.1149 -0.0688 91  TYR C CD2 
8130  C CE1 . TYR C 91  ? 0.3136 0.3679 0.3461 0.1209  -0.1292 -0.0955 91  TYR C CE1 
8131  C CE2 . TYR C 91  ? 0.2856 0.3562 0.3099 0.1166  -0.1132 -0.0757 91  TYR C CE2 
8132  C CZ  . TYR C 91  ? 0.2532 0.3236 0.2789 0.1224  -0.1201 -0.0891 91  TYR C CZ  
8133  O OH  . TYR C 91  ? 0.3113 0.3974 0.3317 0.1301  -0.1182 -0.0962 91  TYR C OH  
8134  N N   . ASP C 92  ? 0.2967 0.2923 0.3523 0.0837  -0.1435 -0.0648 92  ASP C N   
8135  C CA  . ASP C 92  ? 0.2930 0.2758 0.3538 0.0748  -0.1478 -0.0581 92  ASP C CA  
8136  C C   . ASP C 92  ? 0.2981 0.2887 0.3566 0.0689  -0.1399 -0.0464 92  ASP C C   
8137  O O   . ASP C 92  ? 0.3386 0.3195 0.4002 0.0613  -0.1417 -0.0394 92  ASP C O   
8138  C CB  . ASP C 92  ? 0.3639 0.3403 0.4320 0.0722  -0.1587 -0.0652 92  ASP C CB  
8139  C CG  . ASP C 92  ? 0.4086 0.3701 0.4819 0.0759  -0.1691 -0.0753 92  ASP C CG  
8140  O OD1 . ASP C 92  ? 0.4006 0.3522 0.4730 0.0776  -0.1691 -0.0739 92  ASP C OD1 
8141  O OD2 . ASP C 92  ? 0.4621 0.4223 0.5406 0.0770  -0.1771 -0.0848 92  ASP C OD2 
8142  N N   . TYR C 93  ? 0.3229 0.3303 0.3762 0.0722  -0.1318 -0.0441 93  TYR C N   
8143  C CA  . TYR C 93  ? 0.3046 0.3196 0.3562 0.0678  -0.1249 -0.0339 93  TYR C CA  
8144  C C   . TYR C 93  ? 0.3312 0.3553 0.3765 0.0718  -0.1142 -0.0282 93  TYR C C   
8145  O O   . TYR C 93  ? 0.2781 0.3098 0.3195 0.0785  -0.1116 -0.0328 93  TYR C O   
8146  C CB  . TYR C 93  ? 0.2812 0.3082 0.3337 0.0675  -0.1261 -0.0354 93  TYR C CB  
8147  C CG  . TYR C 93  ? 0.3568 0.3767 0.4163 0.0631  -0.1368 -0.0419 93  TYR C CG  
8148  C CD1 . TYR C 93  ? 0.3878 0.3981 0.4527 0.0540  -0.1409 -0.0368 93  TYR C CD1 
8149  C CD2 . TYR C 93  ? 0.3438 0.3665 0.4049 0.0677  -0.1429 -0.0534 93  TYR C CD2 
8150  C CE1 . TYR C 93  ? 0.3667 0.3697 0.4386 0.0488  -0.1508 -0.0421 93  TYR C CE1 
8151  C CE2 . TYR C 93  ? 0.3752 0.3907 0.4435 0.0630  -0.1528 -0.0597 93  TYR C CE2 
8152  C CZ  . TYR C 93  ? 0.3779 0.3832 0.4517 0.0532  -0.1567 -0.0537 93  TYR C CZ  
8153  O OH  . TYR C 93  ? 0.4245 0.4221 0.5059 0.0472  -0.1663 -0.0594 93  TYR C OH  
8154  N N   . ILE C 94  ? 0.2971 0.3205 0.3419 0.0673  -0.1082 -0.0185 94  ILE C N   
8155  C CA  . ILE C 94  ? 0.2842 0.3156 0.3243 0.0701  -0.0983 -0.0124 94  ILE C CA  
8156  C C   . ILE C 94  ? 0.2535 0.2909 0.2937 0.0669  -0.0931 -0.0038 94  ILE C C   
8157  O O   . ILE C 94  ? 0.2344 0.2673 0.2780 0.0610  -0.0961 -0.0009 94  ILE C O   
8158  C CB  . ILE C 94  ? 0.2439 0.2678 0.2834 0.0691  -0.0955 -0.0100 94  ILE C CB  
8159  C CG1 . ILE C 94  ? 0.2919 0.3054 0.3347 0.0615  -0.0973 -0.0047 94  ILE C CG1 
8160  C CG2 . ILE C 94  ? 0.2759 0.2950 0.3154 0.0733  -0.1004 -0.0187 94  ILE C CG2 
8161  C CD1 . ILE C 94  ? 0.2675 0.2799 0.3088 0.0599  -0.0906 0.0015  94  ILE C CD1 
8162  N N   . ILE C 95  ? 0.2060 0.2531 0.2424 0.0710  -0.0855 0.0002  95  ILE C N   
8163  C CA  . ILE C 95  ? 0.1999 0.2511 0.2362 0.0693  -0.0791 0.0090  95  ILE C CA  
8164  C C   . ILE C 95  ? 0.2322 0.2836 0.2654 0.0720  -0.0713 0.0130  95  ILE C C   
8165  O O   . ILE C 95  ? 0.2322 0.2896 0.2615 0.0775  -0.0683 0.0108  95  ILE C O   
8166  C CB  . ILE C 95  ? 0.2640 0.3261 0.2994 0.0719  -0.0782 0.0096  95  ILE C CB  
8167  C CG1 . ILE C 95  ? 0.2480 0.3117 0.2869 0.0693  -0.0866 0.0044  95  ILE C CG1 
8168  C CG2 . ILE C 95  ? 0.2463 0.3106 0.2820 0.0704  -0.0721 0.0181  95  ILE C CG2 
8169  C CD1 . ILE C 95  ? 0.2239 0.2999 0.2611 0.0734  -0.0867 0.0020  95  ILE C CD1 
8170  N N   . PRO C 96  ? 0.2067 0.2521 0.2412 0.0684  -0.0679 0.0183  96  PRO C N   
8171  C CA  . PRO C 96  ? 0.2045 0.2502 0.2368 0.0707  -0.0607 0.0217  96  PRO C CA  
8172  C C   . PRO C 96  ? 0.1795 0.2309 0.2086 0.0739  -0.0547 0.0255  96  PRO C C   
8173  O O   . PRO C 96  ? 0.1846 0.2392 0.2145 0.0733  -0.0556 0.0271  96  PRO C O   
8174  C CB  . PRO C 96  ? 0.2249 0.2632 0.2597 0.0656  -0.0594 0.0261  96  PRO C CB  
8175  C CG  . PRO C 96  ? 0.2046 0.2407 0.2419 0.0608  -0.0640 0.0270  96  PRO C CG  
8176  C CD  . PRO C 96  ? 0.2164 0.2546 0.2540 0.0620  -0.0708 0.0206  96  PRO C CD  
8177  N N   . ALA C 97  ? 0.1827 0.2360 0.2073 0.0779  -0.0482 0.0267  97  ALA C N   
8178  C CA  . ALA C 97  ? 0.1830 0.2409 0.2025 0.0817  -0.0408 0.0309  97  ALA C CA  
8179  C C   . ALA C 97  ? 0.1831 0.2382 0.2000 0.0827  -0.0327 0.0351  97  ALA C C   
8180  O O   . ALA C 97  ? 0.1973 0.2499 0.2154 0.0820  -0.0335 0.0331  97  ALA C O   
8181  C CB  . ALA C 97  ? 0.1557 0.2235 0.1704 0.0878  -0.0409 0.0278  97  ALA C CB  
8182  N N   . HIS C 98  ? 0.1951 0.2508 0.2086 0.0843  -0.0247 0.0411  98  HIS C N   
8183  C CA  . HIS C 98  ? 0.1785 0.2305 0.1906 0.0844  -0.0165 0.0459  98  HIS C CA  
8184  C C   . HIS C 98  ? 0.1888 0.2465 0.1967 0.0894  -0.0130 0.0455  98  HIS C C   
8185  O O   . HIS C 98  ? 0.1966 0.2522 0.2054 0.0889  -0.0092 0.0470  98  HIS C O   
8186  C CB  . HIS C 98  ? 0.1788 0.2283 0.1893 0.0846  -0.0083 0.0528  98  HIS C CB  
8187  C CG  . HIS C 98  ? 0.1984 0.2540 0.2030 0.0905  -0.0026 0.0565  98  HIS C CG  
8188  N ND1 . HIS C 98  ? 0.2440 0.3054 0.2468 0.0930  -0.0051 0.0558  98  HIS C ND1 
8189  C CD2 . HIS C 98  ? 0.2114 0.2682 0.2116 0.0946  0.0058  0.0617  98  HIS C CD2 
8190  C CE1 . HIS C 98  ? 0.2349 0.3012 0.2319 0.0986  0.0012  0.0602  98  HIS C CE1 
8191  N NE2 . HIS C 98  ? 0.2199 0.2833 0.2152 0.0996  0.0080  0.0642  98  HIS C NE2 
8192  N N   . GLN C 99  ? 0.1847 0.2508 0.1883 0.0944  -0.0143 0.0434  99  GLN C N   
8193  C CA  . GLN C 99  ? 0.1925 0.2663 0.1923 0.0993  -0.0129 0.0415  99  GLN C CA  
8194  C C   . GLN C 99  ? 0.1844 0.2676 0.1803 0.1038  -0.0171 0.0371  99  GLN C C   
8195  O O   . GLN C 99  ? 0.1670 0.2503 0.1644 0.1025  -0.0218 0.0351  99  GLN C O   
8196  C CB  . GLN C 99  ? 0.1850 0.2603 0.1806 0.1026  -0.0021 0.0494  99  GLN C CB  
8197  C CG  . GLN C 99  ? 0.2401 0.3178 0.2306 0.1061  0.0043  0.0563  99  GLN C CG  
8198  C CD  . GLN C 99  ? 0.2600 0.3368 0.2476 0.1088  0.0154  0.0653  99  GLN C CD  
8199  O OE1 . GLN C 99  ? 0.2486 0.3167 0.2401 0.1051  0.0202  0.0690  99  GLN C OE1 
8200  N NE2 . GLN C 99  ? 0.2536 0.3397 0.2348 0.1152  0.0197  0.0691  99  GLN C NE2 
8201  N N   . GLY C 100 ? 0.2650 0.1910 0.2061 0.0561  -0.0092 -0.0251 100 GLY C N   
8202  C CA  . GLY C 100 ? 0.2117 0.1538 0.1586 0.0592  -0.0058 -0.0315 100 GLY C CA  
8203  C C   . GLY C 100 ? 0.2729 0.2167 0.2161 0.0592  -0.0060 -0.0322 100 GLY C C   
8204  O O   . GLY C 100 ? 0.2300 0.1820 0.1811 0.0573  -0.0042 -0.0365 100 GLY C O   
8205  N N   . ARG C 101 ? 0.2419 0.1752 0.1696 0.0622  -0.0089 -0.0280 101 ARG C N   
8206  C CA  . ARG C 101 ? 0.2814 0.2182 0.2042 0.0650  -0.0100 -0.0289 101 ARG C CA  
8207  C C   . ARG C 101 ? 0.2223 0.1594 0.1531 0.0619  -0.0101 -0.0280 101 ARG C C   
8208  O O   . ARG C 101 ? 0.2397 0.1848 0.1709 0.0653  -0.0108 -0.0309 101 ARG C O   
8209  C CB  . ARG C 101 ? 0.2711 0.1922 0.1684 0.0705  -0.0132 -0.0244 101 ARG C CB  
8210  C CG  . ARG C 101 ? 0.2563 0.1530 0.1394 0.0682  -0.0173 -0.0159 101 ARG C CG  
8211  C CD  . ARG C 101 ? 0.2932 0.1739 0.1516 0.0644  -0.0213 -0.0071 101 ARG C CD  
8212  N NE  . ARG C 101 ? 0.3179 0.2095 0.1829 0.0525  -0.0200 -0.0024 101 ARG C NE  
8213  C CZ  . ARG C 101 ? 0.3292 0.2145 0.1776 0.0422  -0.0224 0.0069  101 ARG C CZ  
8214  N NH1 . ARG C 101 ? 0.3432 0.2056 0.1629 0.0431  -0.0266 0.0122  101 ARG C NH1 
8215  N NH2 . ARG C 101 ? 0.3209 0.2231 0.1798 0.0306  -0.0207 0.0112  101 ARG C NH2 
8216  N N   . GLY C 102 ? 0.2868 0.2173 0.2231 0.0565  -0.0090 -0.0247 102 GLY C N   
8217  C CA  . GLY C 102 ? 0.2245 0.1582 0.1697 0.0538  -0.0066 -0.0255 102 GLY C CA  
8218  C C   . GLY C 102 ? 0.2416 0.1835 0.2005 0.0500  -0.0026 -0.0322 102 GLY C C   
8219  O O   . GLY C 102 ? 0.2168 0.1632 0.1798 0.0505  -0.0009 -0.0363 102 GLY C O   
8220  N N   . ALA C 103 ? 0.2127 0.1549 0.1756 0.0474  -0.0012 -0.0338 103 ALA C N   
8221  C CA  . ALA C 103 ? 0.2365 0.1814 0.2049 0.0448  0.0017  -0.0400 103 ALA C CA  
8222  C C   . ALA C 103 ? 0.2763 0.2298 0.2421 0.0483  0.0000  -0.0460 103 ALA C C   
8223  O O   . ALA C 103 ? 0.2874 0.2411 0.2547 0.0462  0.0010  -0.0519 103 ALA C O   
8224  C CB  . ALA C 103 ? 0.2429 0.1871 0.2120 0.0448  0.0023  -0.0403 103 ALA C CB  
8225  N N   . GLU C 104 ? 0.2308 0.1909 0.1908 0.0538  -0.0031 -0.0452 104 GLU C N   
8226  C CA  . GLU C 104 ? 0.2389 0.2096 0.1964 0.0577  -0.0056 -0.0508 104 GLU C CA  
8227  C C   . GLU C 104 ? 0.2709 0.2469 0.2294 0.0600  -0.0075 -0.0528 104 GLU C C   
8228  O O   . GLU C 104 ? 0.2632 0.2493 0.2243 0.0608  -0.0095 -0.0604 104 GLU C O   
8229  C CB  . GLU C 104 ? 0.2622 0.2377 0.2106 0.0635  -0.0074 -0.0488 104 GLU C CB  
8230  C CG  . GLU C 104 ? 0.2936 0.2704 0.2415 0.0638  -0.0049 -0.0488 104 GLU C CG  
8231  C CD  . GLU C 104 ? 0.3208 0.3010 0.2574 0.0693  -0.0046 -0.0456 104 GLU C CD  
8232  O OE1 . GLU C 104 ? 0.2926 0.2656 0.2178 0.0717  -0.0067 -0.0416 104 GLU C OE1 
8233  O OE2 . GLU C 104 ? 0.3105 0.2998 0.2462 0.0720  -0.0019 -0.0470 104 GLU C OE2 
8234  N N   . ASN C 105 ? 0.2548 0.2254 0.2102 0.0621  -0.0078 -0.0467 105 ASN C N   
8235  C CA  . ASN C 105 ? 0.2422 0.2210 0.1975 0.0676  -0.0095 -0.0483 105 ASN C CA  
8236  C C   . ASN C 105 ? 0.2698 0.2528 0.2357 0.0636  -0.0061 -0.0546 105 ASN C C   
8237  O O   . ASN C 105 ? 0.2756 0.2761 0.2461 0.0681  -0.0076 -0.0613 105 ASN C O   
8238  C CB  . ASN C 105 ? 0.2508 0.2190 0.1952 0.0720  -0.0108 -0.0394 105 ASN C CB  
8239  C CG  . ASN C 105 ? 0.2858 0.2646 0.2264 0.0814  -0.0131 -0.0402 105 ASN C CG  
8240  O OD1 . ASN C 105 ? 0.2717 0.2691 0.2159 0.0867  -0.0157 -0.0468 105 ASN C OD1 
8241  N ND2 . ASN C 105 ? 0.2787 0.2479 0.2116 0.0841  -0.0125 -0.0338 105 ASN C ND2 
8242  N N   . ILE C 106 ? 0.2711 0.2406 0.2402 0.0556  -0.0018 -0.0535 106 ILE C N   
8243  C CA  . ILE C 106 ? 0.2830 0.2510 0.2571 0.0507  0.0015  -0.0607 106 ILE C CA  
8244  C C   . ILE C 106 ? 0.3014 0.2770 0.2769 0.0470  -0.0016 -0.0722 106 ILE C C   
8245  O O   . ILE C 106 ? 0.3032 0.2947 0.2849 0.0454  -0.0033 -0.0838 106 ILE C O   
8246  C CB  . ILE C 106 ? 0.3020 0.2501 0.2750 0.0433  0.0068  -0.0552 106 ILE C CB  
8247  C CG1 . ILE C 106 ? 0.2872 0.2310 0.2611 0.0451  0.0084  -0.0465 106 ILE C CG1 
8248  C CG2 . ILE C 106 ? 0.3038 0.2427 0.2749 0.0364  0.0097  -0.0632 106 ILE C CG2 
8249  C CD1 . ILE C 106 ? 0.2369 0.1700 0.2147 0.0381  0.0110  -0.0418 106 ILE C CD1 
8250  N N   . LEU C 107 ? 0.2543 0.2220 0.2248 0.0449  -0.0024 -0.0704 107 LEU C N   
8251  C CA  . LEU C 107 ? 0.2900 0.2557 0.2568 0.0400  -0.0049 -0.0795 107 LEU C CA  
8252  C C   . LEU C 107 ? 0.3016 0.2877 0.2701 0.0438  -0.0111 -0.0873 107 LEU C C   
8253  O O   . LEU C 107 ? 0.3035 0.2961 0.2727 0.0375  -0.0151 -0.0984 107 LEU C O   
8254  C CB  . LEU C 107 ? 0.3137 0.2656 0.2735 0.0393  -0.0026 -0.0745 107 LEU C CB  
8255  C CG  . LEU C 107 ? 0.3579 0.2999 0.3082 0.0350  -0.0044 -0.0819 107 LEU C CG  
8256  C CD1 . LEU C 107 ? 0.2978 0.2253 0.2430 0.0245  -0.0037 -0.0878 107 LEU C CD1 
8257  C CD2 . LEU C 107 ? 0.2905 0.2241 0.2359 0.0380  -0.0015 -0.0775 107 LEU C CD2 
8258  N N   . PHE C 108 ? 0.2635 0.2590 0.2308 0.0523  -0.0128 -0.0817 108 PHE C N   
8259  C CA  . PHE C 108 ? 0.3066 0.3167 0.2712 0.0564  -0.0184 -0.0876 108 PHE C CA  
8260  C C   . PHE C 108 ? 0.2549 0.2887 0.2264 0.0572  -0.0233 -0.0974 108 PHE C C   
8261  O O   . PHE C 108 ? 0.2826 0.3258 0.2535 0.0529  -0.0289 -0.1071 108 PHE C O   
8262  C CB  . PHE C 108 ? 0.2832 0.2948 0.2413 0.0644  -0.0186 -0.0791 108 PHE C CB  
8263  C CG  . PHE C 108 ? 0.3497 0.3495 0.3023 0.0635  -0.0152 -0.0742 108 PHE C CG  
8264  C CD1 . PHE C 108 ? 0.3090 0.2961 0.2621 0.0579  -0.0120 -0.0751 108 PHE C CD1 
8265  C CD2 . PHE C 108 ? 0.3175 0.3202 0.2628 0.0691  -0.0152 -0.0694 108 PHE C CD2 
8266  C CE1 . PHE C 108 ? 0.2884 0.2703 0.2374 0.0597  -0.0093 -0.0717 108 PHE C CE1 
8267  C CE2 . PHE C 108 ? 0.3137 0.3122 0.2554 0.0695  -0.0118 -0.0667 108 PHE C CE2 
8268  C CZ  . PHE C 108 ? 0.2996 0.2896 0.2442 0.0657  -0.0092 -0.0681 108 PHE C CZ  
8269  N N   . PRO C 109 ? 0.2696 0.3160 0.2470 0.0626  -0.0219 -0.0957 109 PRO C N   
8270  C CA  . PRO C 109 ? 0.2564 0.3341 0.2456 0.0612  -0.0258 -0.1010 109 PRO C CA  
8271  C C   . PRO C 109 ? 0.2554 0.3389 0.2550 0.0432  -0.0263 -0.1078 109 PRO C C   
8272  O O   . PRO C 109 ? 0.2859 0.3952 0.2943 0.0367  -0.0323 -0.1138 109 PRO C O   
8273  C CB  . PRO C 109 ? 0.2540 0.3387 0.2466 0.0705  -0.0217 -0.0930 109 PRO C CB  
8274  C CG  . PRO C 109 ? 0.2462 0.3034 0.2237 0.0784  -0.0197 -0.0834 109 PRO C CG  
8275  C CD  . PRO C 109 ? 0.2467 0.2814 0.2216 0.0682  -0.0175 -0.0829 109 PRO C CD  
8276  N N   . VAL C 110 ? 0.2735 0.3319 0.2702 0.0342  -0.0208 -0.1069 110 VAL C N   
8277  C CA  . VAL C 110 ? 0.2733 0.3285 0.2735 0.0151  -0.0212 -0.1126 110 VAL C CA  
8278  C C   . VAL C 110 ? 0.2959 0.3417 0.2851 0.0082  -0.0290 -0.1218 110 VAL C C   
8279  O O   . VAL C 110 ? 0.2711 0.3312 0.2652 -0.0065 -0.0347 -0.1281 110 VAL C O   
8280  C CB  . VAL C 110 ? 0.2523 0.2757 0.2457 0.0099  -0.0138 -0.1093 110 VAL C CB  
8281  C CG1 . VAL C 110 ? 0.3059 0.3123 0.2925 -0.0100 -0.0152 -0.1158 110 VAL C CG1 
8282  C CG2 . VAL C 110 ? 0.2242 0.2583 0.2279 0.0141  -0.0067 -0.1011 110 VAL C CG2 
8283  N N   . LEU C 111 ? 0.2815 0.3040 0.2545 0.0185  -0.0296 -0.1227 111 LEU C N   
8284  C CA  . LEU C 111 ? 0.3166 0.3267 0.2761 0.0151  -0.0354 -0.1263 111 LEU C CA  
8285  C C   . LEU C 111 ? 0.3356 0.3754 0.3008 0.0153  -0.0445 -0.1331 111 LEU C C   
8286  O O   . LEU C 111 ? 0.3263 0.3615 0.2842 0.0049  -0.0514 -0.1387 111 LEU C O   
8287  C CB  . LEU C 111 ? 0.3407 0.3306 0.2877 0.0274  -0.0309 -0.1169 111 LEU C CB  
8288  C CG  . LEU C 111 ? 0.2923 0.2561 0.2329 0.0270  -0.0230 -0.1090 111 LEU C CG  
8289  C CD1 . LEU C 111 ? 0.2818 0.2394 0.2160 0.0374  -0.0195 -0.1014 111 LEU C CD1 
8290  C CD2 . LEU C 111 ? 0.3447 0.2836 0.2721 0.0134  -0.0238 -0.1139 111 LEU C CD2 
8291  N N   . LEU C 112 ? 0.2392 0.3067 0.2146 0.0275  -0.0450 -0.1307 112 LEU C N   
8292  C CA  . LEU C 112 ? 0.2795 0.3766 0.2599 0.0298  -0.0539 -0.1352 112 LEU C CA  
8293  C C   . LEU C 112 ? 0.3139 0.4397 0.3125 0.0129  -0.0581 -0.1391 112 LEU C C   
8294  O O   . LEU C 112 ? 0.2998 0.4366 0.2977 0.0029  -0.0679 -0.1472 112 LEU C O   
8295  C CB  . LEU C 112 ? 0.2408 0.3546 0.2229 0.0489  -0.0527 -0.1286 112 LEU C CB  
8296  C CG  . LEU C 112 ? 0.2647 0.4112 0.2515 0.0546  -0.0623 -0.1330 112 LEU C CG  
8297  C CD1 . LEU C 112 ? 0.3174 0.4513 0.2930 0.0518  -0.0678 -0.1363 112 LEU C CD1 
8298  C CD2 . LEU C 112 ? 0.2998 0.4534 0.2811 0.0749  -0.0609 -0.1258 112 LEU C CD2 
8299  N N   . LYS C 113 ? 0.2685 0.4081 0.2830 0.0090  -0.0509 -0.1332 113 LYS C N   
8300  C CA  . LYS C 113 ? 0.2801 0.4519 0.3142 -0.0089 -0.0527 -0.1355 113 LYS C CA  
8301  C C   . LYS C 113 ? 0.3593 0.5106 0.3848 -0.0334 -0.0575 -0.1428 113 LYS C C   
8302  O O   . LYS C 113 ? 0.3401 0.5165 0.3745 -0.0496 -0.0660 -0.1488 113 LYS C O   
8303  C CB  . LYS C 113 ? 0.2744 0.4547 0.3214 -0.0084 -0.0417 -0.1271 113 LYS C CB  
8304  C CG  . LYS C 113 ? 0.3352 0.5550 0.4045 -0.0262 -0.0408 -0.1276 113 LYS C CG  
8305  C CD  . LYS C 113 ? 0.3701 0.6450 0.4578 -0.0153 -0.0466 -0.1285 113 LYS C CD  
8306  C CE  . LYS C 113 ? 0.4126 0.7361 0.5263 -0.0291 -0.0431 -0.1268 113 LYS C CE  
8307  N NZ  . LYS C 113 ? 0.4393 0.8196 0.5704 -0.0120 -0.0481 -0.1271 113 LYS C NZ  
8308  N N   . TYR C 114 ? 0.3407 0.4448 0.3463 -0.0361 -0.0530 -0.1427 114 TYR C N   
8309  C CA  . TYR C 114 ? 0.3611 0.4343 0.3495 -0.0570 -0.0580 -0.1496 114 TYR C CA  
8310  C C   . TYR C 114 ? 0.4495 0.5157 0.4235 -0.0568 -0.0694 -0.1543 114 TYR C C   
8311  O O   . TYR C 114 ? 0.5227 0.5830 0.4907 -0.0765 -0.0770 -0.1569 114 TYR C O   
8312  C CB  . TYR C 114 ? 0.3476 0.3701 0.3141 -0.0524 -0.0508 -0.1472 114 TYR C CB  
8313  C CG  . TYR C 114 ? 0.4517 0.4298 0.3925 -0.0680 -0.0543 -0.1468 114 TYR C CG  
8314  C CD1 . TYR C 114 ? 0.5112 0.4808 0.4533 -0.0890 -0.0515 -0.1455 114 TYR C CD1 
8315  C CD2 . TYR C 114 ? 0.5389 0.4812 0.4506 -0.0606 -0.0602 -0.1467 114 TYR C CD2 
8316  C CE1 . TYR C 114 ? 0.5959 0.5223 0.5136 -0.0989 -0.0568 -0.1447 114 TYR C CE1 
8317  C CE2 . TYR C 114 ? 0.5520 0.4502 0.4373 -0.0690 -0.0674 -0.1475 114 TYR C CE2 
8318  C CZ  . TYR C 114 ? 0.6243 0.5194 0.5189 -0.0859 -0.0658 -0.1481 114 TYR C CZ  
8319  O OH  . TYR C 114 ? 0.7301 0.5956 0.6110 -0.0917 -0.0683 -0.1518 114 TYR C OH  
8320  N N   . LYS C 115 ? 0.3978 0.4621 0.3645 -0.0349 -0.0702 -0.1529 115 LYS C N   
8321  C CA  . LYS C 115 ? 0.4022 0.4583 0.3537 -0.0329 -0.0793 -0.1555 115 LYS C CA  
8322  C C   . LYS C 115 ? 0.5060 0.6061 0.4761 -0.0399 -0.0889 -0.1592 115 LYS C C   
8323  O O   . LYS C 115 ? 0.4902 0.5829 0.4490 -0.0496 -0.0990 -0.1627 115 LYS C O   
8324  C CB  . LYS C 115 ? 0.3875 0.4322 0.3274 -0.0088 -0.0753 -0.1512 115 LYS C CB  
8325  C CG  . LYS C 115 ? 0.4408 0.4663 0.3587 -0.0061 -0.0817 -0.1533 115 LYS C CG  
8326  C CD  . LYS C 115 ? 0.4529 0.4327 0.3437 -0.0133 -0.0795 -0.1534 115 LYS C CD  
8327  C CE  . LYS C 115 ? 0.4947 0.4569 0.3629 -0.0064 -0.0830 -0.1554 115 LYS C CE  
8328  N NZ  . LYS C 115 ? 0.4809 0.4041 0.3244 -0.0090 -0.0782 -0.1557 115 LYS C NZ  
8329  N N   . GLN C 116 ? 0.4240 0.5695 0.4206 -0.0342 -0.0863 -0.1577 116 GLN C N   
8330  C CA  . GLN C 116 ? 0.4719 0.6637 0.4873 -0.0361 -0.0942 -0.1591 116 GLN C CA  
8331  C C   . GLN C 116 ? 0.5269 0.7347 0.5538 -0.0646 -0.0998 -0.1611 116 GLN C C   
8332  O O   . GLN C 116 ? 0.5577 0.8023 0.5991 -0.0682 -0.1074 -0.1620 116 GLN C O   
8333  C CB  . GLN C 116 ? 0.3826 0.6163 0.4196 -0.0191 -0.0891 -0.1551 116 GLN C CB  
8334  C CG  . GLN C 116 ? 0.3271 0.5506 0.3511 0.0090  -0.0873 -0.1518 116 GLN C CG  
8335  C CD  . GLN C 116 ? 0.3227 0.5727 0.3586 0.0267  -0.0817 -0.1463 116 GLN C CD  
8336  O OE1 . GLN C 116 ? 0.3036 0.5714 0.3558 0.0203  -0.0761 -0.1436 116 GLN C OE1 
8337  N NE2 . GLN C 116 ? 0.3300 0.5769 0.3546 0.0494  -0.0821 -0.1425 116 GLN C NE2 
8338  N N   . LYS C 117 ? 0.5640 0.7434 0.5832 -0.0845 -0.0962 -0.1610 117 LYS C N   
8339  C CA  . LYS C 117 ? 0.6880 0.8764 0.7145 -0.1136 -0.1012 -0.1611 117 LYS C CA  
8340  C C   . LYS C 117 ? 0.7562 0.9326 0.7681 -0.1214 -0.1164 -0.1652 117 LYS C C   
8341  O O   . LYS C 117 ? 0.7647 0.8973 0.7466 -0.1124 -0.1217 -0.1680 117 LYS C O   
8342  C CB  . LYS C 117 ? 0.6821 0.8265 0.6926 -0.1305 -0.0948 -0.1593 117 LYS C CB  
8343  C CG  . LYS C 117 ? 0.6707 0.8325 0.6989 -0.1296 -0.0805 -0.1550 117 LYS C CG  
8344  C CD  . LYS C 117 ? 0.6871 0.7908 0.6901 -0.1327 -0.0729 -0.1533 117 LYS C CD  
8345  C CE  . LYS C 117 ? 0.8198 0.8876 0.8045 -0.1578 -0.0771 -0.1521 117 LYS C CE  
8346  N NZ  . LYS C 117 ? 0.7266 0.7407 0.6878 -0.1571 -0.0690 -0.1487 117 LYS C NZ  
8347  N N   . GLU C 118 ? 0.7588 0.9756 0.7917 -0.1377 -0.1233 -0.1651 118 GLU C N   
8348  C CA  . GLU C 118 ? 0.7767 0.9904 0.8005 -0.1459 -0.1395 -0.1694 118 GLU C CA  
8349  C C   . GLU C 118 ? 0.7716 0.9929 0.7890 -0.1202 -0.1447 -0.1718 118 GLU C C   
8350  O O   . GLU C 118 ? 0.8090 0.9994 0.8011 -0.1191 -0.1562 -0.1758 118 GLU C O   
8351  C CB  . GLU C 118 ? 0.9137 1.0637 0.9030 -0.1612 -0.1482 -0.1730 118 GLU C CB  
8352  C CG  . GLU C 118 ? 0.9794 1.1272 0.9754 -0.1915 -0.1484 -0.1718 118 GLU C CG  
8353  C CD  . GLU C 118 ? 1.0654 1.1757 1.0487 -0.1956 -0.1355 -0.1684 118 GLU C CD  
8354  O OE1 . GLU C 118 ? 1.0550 1.1409 1.0252 -0.1746 -0.1279 -0.1677 118 GLU C OE1 
8355  O OE2 . GLU C 118 ? 1.1348 1.2395 1.1199 -0.2198 -0.1327 -0.1659 118 GLU C OE2 
8356  N N   . GLY C 119 ? 0.7535 1.0132 0.7909 -0.0983 -0.1362 -0.1690 119 GLY C N   
8357  C CA  . GLY C 119 ? 0.6985 0.9712 0.7326 -0.0738 -0.1404 -0.1703 119 GLY C CA  
8358  C C   . GLY C 119 ? 0.6995 0.9229 0.7006 -0.0577 -0.1405 -0.1720 119 GLY C C   
8359  O O   . GLY C 119 ? 0.7264 0.9513 0.7182 -0.0432 -0.1465 -0.1737 119 GLY C O   
8360  N N   . LYS C 120 ? 0.6340 0.8141 0.6166 -0.0592 -0.1332 -0.1711 120 LYS C N   
8361  C CA  . LYS C 120 ? 0.5567 0.6955 0.5107 -0.0414 -0.1298 -0.1709 120 LYS C CA  
8362  C C   . LYS C 120 ? 0.5308 0.6836 0.4938 -0.0152 -0.1190 -0.1663 120 LYS C C   
8363  O O   . LYS C 120 ? 0.5055 0.6969 0.4926 -0.0094 -0.1156 -0.1639 120 LYS C O   
8364  C CB  . LYS C 120 ? 0.6251 0.7124 0.5540 -0.0514 -0.1257 -0.1709 120 LYS C CB  
8365  C CG  . LYS C 120 ? 0.7421 0.8063 0.6559 -0.0786 -0.1371 -0.1744 120 LYS C CG  
8366  C CD  . LYS C 120 ? 0.7270 0.7324 0.6070 -0.0841 -0.1326 -0.1737 120 LYS C CD  
8367  C CE  . LYS C 120 ? 0.6581 0.6607 0.5502 -0.0815 -0.1196 -0.1695 120 LYS C CE  
8368  N NZ  . LYS C 120 ? 0.6346 0.6678 0.5562 -0.1006 -0.1205 -0.1691 120 LYS C NZ  
8369  N N   . ALA C 121 ? 0.4709 0.5909 0.4123 0.0008  -0.1135 -0.1639 121 ALA C N   
8370  C CA  . ALA C 121 ? 0.4039 0.5270 0.3480 0.0232  -0.1035 -0.1577 121 ALA C CA  
8371  C C   . ALA C 121 ? 0.4178 0.5763 0.3743 0.0377  -0.1066 -0.1565 121 ALA C C   
8372  O O   . ALA C 121 ? 0.3930 0.5663 0.3593 0.0502  -0.1002 -0.1516 121 ALA C O   
8373  C CB  . ALA C 121 ? 0.4332 0.5544 0.3879 0.0212  -0.0935 -0.1540 121 ALA C CB  
8374  N N   . LYS C 122 ? 0.3476 0.5162 0.3004 0.0369  -0.1168 -0.1607 122 LYS C N   
8375  C CA  . LYS C 122 ? 0.3456 0.5455 0.3075 0.0519  -0.1201 -0.1599 122 LYS C CA  
8376  C C   . LYS C 122 ? 0.3961 0.5789 0.3423 0.0751  -0.1138 -0.1542 122 LYS C C   
8377  O O   . LYS C 122 ? 0.3976 0.5986 0.3485 0.0906  -0.1124 -0.1511 122 LYS C O   
8378  C CB  . LYS C 122 ? 0.3825 0.5966 0.3440 0.0442  -0.1335 -0.1660 122 LYS C CB  
8379  C CG  . LYS C 122 ? 0.4944 0.7506 0.4827 0.0277  -0.1395 -0.1686 122 LYS C CG  
8380  C CD  . LYS C 122 ? 0.4937 0.7843 0.5027 0.0408  -0.1312 -0.1640 122 LYS C CD  
8381  C CE  . LYS C 122 ? 0.4426 0.7701 0.4794 0.0221  -0.1307 -0.1640 122 LYS C CE  
8382  N NZ  . LYS C 122 ? 0.3381 0.6983 0.3886 0.0079  -0.1424 -0.1679 122 LYS C NZ  
8383  N N   . ASN C 123 ? 0.4442 0.5914 0.3702 0.0777  -0.1096 -0.1519 123 ASN C N   
8384  C CA  . ASN C 123 ? 0.3797 0.5092 0.2917 0.0954  -0.1018 -0.1441 123 ASN C CA  
8385  C C   . ASN C 123 ? 0.3874 0.4919 0.2942 0.0917  -0.0918 -0.1390 123 ASN C C   
8386  O O   . ASN C 123 ? 0.3385 0.4189 0.2291 0.0931  -0.0890 -0.1374 123 ASN C O   
8387  C CB  . ASN C 123 ? 0.3876 0.5039 0.2804 0.1039  -0.1065 -0.1453 123 ASN C CB  
8388  C CG  . ASN C 123 ? 0.4166 0.5571 0.3137 0.1090  -0.1167 -0.1504 123 ASN C CG  
8389  O OD1 . ASN C 123 ? 0.4303 0.5775 0.3277 0.0989  -0.1269 -0.1578 123 ASN C OD1 
8390  N ND2 . ASN C 123 ? 0.4061 0.5582 0.3049 0.1246  -0.1145 -0.1461 123 ASN C ND2 
8391  N N   . PRO C 124 ? 0.3409 0.4518 0.2610 0.0879  -0.0860 -0.1360 124 PRO C N   
8392  C CA  . PRO C 124 ? 0.3403 0.4294 0.2580 0.0809  -0.0781 -0.1331 124 PRO C CA  
8393  C C   . PRO C 124 ? 0.3105 0.3816 0.2170 0.0912  -0.0691 -0.1233 124 PRO C C   
8394  O O   . PRO C 124 ? 0.3552 0.4307 0.2586 0.1021  -0.0675 -0.1169 124 PRO C O   
8395  C CB  . PRO C 124 ? 0.3334 0.4381 0.2692 0.0747  -0.0755 -0.1331 124 PRO C CB  
8396  C CG  . PRO C 124 ? 0.3119 0.4418 0.2550 0.0868  -0.0778 -0.1309 124 PRO C CG  
8397  C CD  . PRO C 124 ? 0.3318 0.4705 0.2687 0.0915  -0.0863 -0.1352 124 PRO C CD  
8398  N N   . VAL C 125 ? 0.3421 0.3926 0.2414 0.0870  -0.0635 -0.1215 125 VAL C N   
8399  C CA  . VAL C 125 ? 0.3338 0.3725 0.2252 0.0940  -0.0549 -0.1122 125 VAL C CA  
8400  C C   . VAL C 125 ? 0.3405 0.3667 0.2354 0.0877  -0.0480 -0.1098 125 VAL C C   
8401  O O   . VAL C 125 ? 0.2946 0.3129 0.1909 0.0788  -0.0500 -0.1159 125 VAL C O   
8402  C CB  . VAL C 125 ? 0.3584 0.3877 0.2323 0.1013  -0.0553 -0.1119 125 VAL C CB  
8403  C CG1 . VAL C 125 ? 0.3669 0.4055 0.2352 0.1085  -0.0622 -0.1139 125 VAL C CG1 
8404  C CG2 . VAL C 125 ? 0.4061 0.4202 0.2705 0.0966  -0.0576 -0.1187 125 VAL C CG2 
8405  N N   . PHE C 126 ? 0.2939 0.3174 0.1887 0.0916  -0.0402 -0.1008 126 PHE C N   
8406  C CA  . PHE C 126 ? 0.3306 0.3437 0.2265 0.0888  -0.0334 -0.0975 126 PHE C CA  
8407  C C   . PHE C 126 ? 0.3526 0.3624 0.2364 0.0963  -0.0291 -0.0939 126 PHE C C   
8408  O O   . PHE C 126 ? 0.3227 0.3389 0.2004 0.1021  -0.0278 -0.0894 126 PHE C O   
8409  C CB  . PHE C 126 ? 0.2898 0.3057 0.1966 0.0862  -0.0282 -0.0903 126 PHE C CB  
8410  C CG  . PHE C 126 ? 0.3488 0.3663 0.2676 0.0791  -0.0303 -0.0934 126 PHE C CG  
8411  C CD1 . PHE C 126 ? 0.3300 0.3605 0.2537 0.0796  -0.0360 -0.0973 126 PHE C CD1 
8412  C CD2 . PHE C 126 ? 0.3572 0.3648 0.2818 0.0730  -0.0262 -0.0923 126 PHE C CD2 
8413  C CE1 . PHE C 126 ? 0.3636 0.4000 0.2987 0.0738  -0.0372 -0.1009 126 PHE C CE1 
8414  C CE2 . PHE C 126 ? 0.3404 0.3490 0.2746 0.0664  -0.0271 -0.0950 126 PHE C CE2 
8415  C CZ  . PHE C 126 ? 0.3301 0.3544 0.2700 0.0667  -0.0324 -0.0997 126 PHE C CZ  
8416  N N   . ILE C 127 ? 0.3230 0.3225 0.2017 0.0968  -0.0267 -0.0957 127 ILE C N   
8417  C CA  . ILE C 127 ? 0.3588 0.3580 0.2263 0.1057  -0.0225 -0.0932 127 ILE C CA  
8418  C C   . ILE C 127 ? 0.3934 0.3944 0.2671 0.1063  -0.0157 -0.0881 127 ILE C C   
8419  O O   . ILE C 127 ? 0.4009 0.3928 0.2800 0.1013  -0.0160 -0.0899 127 ILE C O   
8420  C CB  . ILE C 127 ? 0.3945 0.3798 0.2465 0.1094  -0.0272 -0.1005 127 ILE C CB  
8421  C CG1 . ILE C 127 ? 0.4101 0.3953 0.2557 0.1089  -0.0349 -0.1059 127 ILE C CG1 
8422  C CG2 . ILE C 127 ? 0.3345 0.3205 0.1745 0.1209  -0.0224 -0.0978 127 ILE C CG2 
8423  C CD1 . ILE C 127 ? 0.4038 0.3731 0.2311 0.1121  -0.0405 -0.1132 127 ILE C CD1 
8424  N N   . SER C 128 ? 0.3514 0.3649 0.2235 0.1121  -0.0095 -0.0819 128 SER C N   
8425  C CA  . SER C 128 ? 0.3651 0.3859 0.2440 0.1133  -0.0035 -0.0772 128 SER C CA  
8426  C C   . SER C 128 ? 0.3242 0.3577 0.1944 0.1235  0.0022  -0.0742 128 SER C C   
8427  O O   . SER C 128 ? 0.3417 0.3796 0.2020 0.1275  0.0030  -0.0735 128 SER C O   
8428  C CB  . SER C 128 ? 0.2872 0.3162 0.1774 0.1068  -0.0005 -0.0712 128 SER C CB  
8429  O OG  . SER C 128 ? 0.2947 0.3318 0.1920 0.1077  0.0044  -0.0674 128 SER C OG  
8430  N N   . ASN C 129 ? 0.3616 0.4025 0.2352 0.1282  0.0061  -0.0723 129 ASN C N   
8431  C CA  . ASN C 129 ? 0.3453 0.4076 0.2153 0.1368  0.0134  -0.0676 129 ASN C CA  
8432  C C   . ASN C 129 ? 0.3070 0.3863 0.1815 0.1306  0.0192  -0.0605 129 ASN C C   
8433  O O   . ASN C 129 ? 0.3474 0.4382 0.2131 0.1339  0.0241  -0.0570 129 ASN C O   
8434  C CB  . ASN C 129 ? 0.2973 0.3689 0.1720 0.1435  0.0159  -0.0666 129 ASN C CB  
8435  C CG  . ASN C 129 ? 0.3180 0.3904 0.2076 0.1357  0.0157  -0.0646 129 ASN C CG  
8436  O OD1 . ASN C 129 ? 0.3500 0.4075 0.2450 0.1257  0.0119  -0.0660 129 ASN C OD1 
8437  N ND2 . ASN C 129 ? 0.2789 0.3700 0.1750 0.1410  0.0196  -0.0614 129 ASN C ND2 
8438  N N   . PHE C 130 ? 0.3045 0.3823 0.1895 0.1213  0.0186  -0.0581 130 PHE C N   
8439  C CA  . PHE C 130 ? 0.3348 0.4183 0.2178 0.1141  0.0216  -0.0522 130 PHE C CA  
8440  C C   . PHE C 130 ? 0.3514 0.4240 0.2430 0.1058  0.0179  -0.0520 130 PHE C C   
8441  O O   . PHE C 130 ? 0.3077 0.3848 0.2101 0.1041  0.0192  -0.0509 130 PHE C O   
8442  C CB  . PHE C 130 ? 0.3198 0.4304 0.2023 0.1135  0.0316  -0.0437 130 PHE C CB  
8443  C CG  . PHE C 130 ? 0.3319 0.4443 0.1997 0.1078  0.0354  -0.0372 130 PHE C CG  
8444  C CD1 . PHE C 130 ? 0.3654 0.4650 0.2269 0.0985  0.0329  -0.0334 130 PHE C CD1 
8445  C CD2 . PHE C 130 ? 0.3953 0.5185 0.2522 0.1119  0.0410  -0.0344 130 PHE C CD2 
8446  C CE1 . PHE C 130 ? 0.3225 0.4167 0.1648 0.0926  0.0349  -0.0264 130 PHE C CE1 
8447  C CE2 . PHE C 130 ? 0.4213 0.5411 0.2609 0.1052  0.0443  -0.0276 130 PHE C CE2 
8448  C CZ  . PHE C 130 ? 0.3729 0.4766 0.2042 0.0951  0.0408  -0.0234 130 PHE C CZ  
8449  N N   . HIS C 131 ? 0.3363 0.3948 0.2227 0.1019  0.0128  -0.0529 131 HIS C N   
8450  C CA  . HIS C 131 ? 0.3480 0.3956 0.2401 0.0955  0.0092  -0.0520 131 HIS C CA  
8451  C C   . HIS C 131 ? 0.3251 0.3791 0.2106 0.0910  0.0142  -0.0438 131 HIS C C   
8452  O O   . HIS C 131 ? 0.3112 0.3687 0.1811 0.0891  0.0173  -0.0377 131 HIS C O   
8453  C CB  . HIS C 131 ? 0.3245 0.3595 0.2119 0.0946  0.0022  -0.0545 131 HIS C CB  
8454  C CG  . HIS C 131 ? 0.3544 0.3833 0.2482 0.0954  -0.0037 -0.0623 131 HIS C CG  
8455  N ND1 . HIS C 131 ? 0.3248 0.3534 0.2105 0.0998  -0.0069 -0.0664 131 HIS C ND1 
8456  C CD2 . HIS C 131 ? 0.3186 0.3405 0.2235 0.0912  -0.0070 -0.0664 131 HIS C CD2 
8457  C CE1 . HIS C 131 ? 0.3446 0.3669 0.2356 0.0980  -0.0121 -0.0733 131 HIS C CE1 
8458  N NE2 . HIS C 131 ? 0.3252 0.3435 0.2275 0.0923  -0.0118 -0.0732 131 HIS C NE2 
8459  N N   A PHE C 132 ? 0.3441 0.3968 0.2379 0.0877  0.0144  -0.0425 132 PHE C N   
8460  N N   B PHE C 132 ? 0.3440 0.3967 0.2383 0.0878  0.0144  -0.0427 132 PHE C N   
8461  C CA  A PHE C 132 ? 0.3409 0.3943 0.2283 0.0781  0.0163  -0.0315 132 PHE C CA  
8462  C CA  B PHE C 132 ? 0.3403 0.3922 0.2297 0.0784  0.0156  -0.0323 132 PHE C CA  
8463  C C   A PHE C 132 ? 0.3317 0.3599 0.2066 0.0743  0.0095  -0.0285 132 PHE C C   
8464  C C   B PHE C 132 ? 0.3317 0.3608 0.2051 0.0748  0.0098  -0.0286 132 PHE C C   
8465  O O   A PHE C 132 ? 0.3328 0.3503 0.2072 0.0810  0.0047  -0.0366 132 PHE C O   
8466  O O   B PHE C 132 ? 0.3389 0.3588 0.2078 0.0820  0.0054  -0.0360 132 PHE C O   
8467  C CB  A PHE C 132 ? 0.3337 0.3939 0.2380 0.0729  0.0171  -0.0281 132 PHE C CB  
8468  C CB  B PHE C 132 ? 0.3304 0.3800 0.2363 0.0747  0.0142  -0.0316 132 PHE C CB  
8469  C CG  A PHE C 132 ? 0.3509 0.4183 0.2535 0.0584  0.0186  -0.0145 132 PHE C CG  
8470  C CG  B PHE C 132 ? 0.3639 0.4099 0.2687 0.0610  0.0129  -0.0192 132 PHE C CG  
8471  C CD1 A PHE C 132 ? 0.3393 0.4272 0.2345 0.0533  0.0248  -0.0072 132 PHE C CD1 
8472  C CD1 B PHE C 132 ? 0.3572 0.4240 0.2609 0.0520  0.0178  -0.0096 132 PHE C CD1 
8473  C CD2 A PHE C 132 ? 0.3662 0.4187 0.2721 0.0488  0.0135  -0.0085 132 PHE C CD2 
8474  C CD2 B PHE C 132 ? 0.3453 0.3666 0.2482 0.0564  0.0067  -0.0167 132 PHE C CD2 
8475  C CE1 A PHE C 132 ? 0.3442 0.4389 0.2365 0.0362  0.0258  0.0061  132 PHE C CE1 
8476  C CE1 B PHE C 132 ? 0.3805 0.4417 0.2809 0.0363  0.0152  0.0021  132 PHE C CE1 
8477  C CE2 A PHE C 132 ? 0.3889 0.4452 0.2904 0.0328  0.0132  0.0041  132 PHE C CE2 
8478  C CE2 B PHE C 132 ? 0.3631 0.3755 0.2601 0.0435  0.0040  -0.0055 132 PHE C CE2 
8479  C CZ  A PHE C 132 ? 0.3833 0.4614 0.2785 0.0252  0.0193  0.0116  132 PHE C CZ  
8480  C CZ  B PHE C 132 ? 0.3943 0.4254 0.2897 0.0322  0.0076  0.0039  132 PHE C CZ  
8481  N N   A ASP C 133 ? 0.3215 0.3405 0.1848 0.0632  0.0087  -0.0166 133 ASP C N   
8482  N N   B ASP C 133 ? 0.3209 0.3405 0.1845 0.0634  0.0089  -0.0168 133 ASP C N   
8483  C CA  A ASP C 133 ? 0.3653 0.3587 0.2061 0.0627  0.0029  -0.0128 133 ASP C CA  
8484  C CA  B ASP C 133 ? 0.3649 0.3587 0.2062 0.0623  0.0030  -0.0125 133 ASP C CA  
8485  C C   A ASP C 133 ? 0.3674 0.3449 0.2132 0.0695  -0.0036 -0.0190 133 ASP C C   
8486  C C   B ASP C 133 ? 0.3668 0.3453 0.2134 0.0696  -0.0034 -0.0192 133 ASP C C   
8487  O O   A ASP C 133 ? 0.3530 0.3231 0.1906 0.0777  -0.0078 -0.0235 133 ASP C O   
8488  O O   B ASP C 133 ? 0.3516 0.3238 0.1906 0.0780  -0.0074 -0.0242 133 ASP C O   
8489  C CB  A ASP C 133 ? 0.3952 0.3745 0.2183 0.0481  0.0021  0.0014  133 ASP C CB  
8490  C CB  B ASP C 133 ? 0.3951 0.3750 0.2210 0.0473  0.0020  0.0015  133 ASP C CB  
8491  C CG  A ASP C 133 ? 0.4314 0.4039 0.2657 0.0392  -0.0006 0.0061  133 ASP C CG  
8492  C CG  B ASP C 133 ? 0.4297 0.4281 0.2494 0.0374  0.0091  0.0096  133 ASP C CG  
8493  O OD1 A ASP C 133 ? 0.3771 0.3669 0.2365 0.0419  0.0017  0.0005  133 ASP C OD1 
8494  O OD1 B ASP C 133 ? 0.4139 0.4423 0.2549 0.0352  0.0152  0.0091  133 ASP C OD1 
8495  O OD2 A ASP C 133 ? 0.4798 0.4258 0.2940 0.0303  -0.0058 0.0151  133 ASP C OD2 
8496  O OD2 B ASP C 133 ? 0.5208 0.5042 0.3130 0.0325  0.0087  0.0165  133 ASP C OD2 
8497  N N   . THR C 134 ? 0.3456 0.3205 0.2071 0.0663  -0.0042 -0.0190 134 THR C N   
8498  C CA  . THR C 134 ? 0.3217 0.2844 0.1884 0.0725  -0.0087 -0.0245 134 THR C CA  
8499  C C   . THR C 134 ? 0.3327 0.3095 0.2149 0.0801  -0.0081 -0.0367 134 THR C C   
8500  O O   . THR C 134 ? 0.3078 0.2829 0.1964 0.0827  -0.0122 -0.0388 134 THR C O   
8501  C CB  . THR C 134 ? 0.3019 0.2554 0.1788 0.0673  -0.0093 -0.0213 134 THR C CB  
8502  O OG1 . THR C 134 ? 0.2874 0.2574 0.1848 0.0671  -0.0051 -0.0269 134 THR C OG1 
8503  C CG2 . THR C 134 ? 0.3308 0.2703 0.1930 0.0563  -0.0112 -0.0088 134 THR C CG2 
8504  N N   . THR C 135 ? 0.3437 0.3362 0.2376 0.0798  -0.0039 -0.0412 135 THR C N   
8505  C CA  . THR C 135 ? 0.3300 0.3308 0.2396 0.0803  -0.0054 -0.0481 135 THR C CA  
8506  C C   . THR C 135 ? 0.3206 0.3244 0.2232 0.0839  -0.0092 -0.0502 135 THR C C   
8507  O O   . THR C 135 ? 0.3353 0.3404 0.2453 0.0841  -0.0136 -0.0544 135 THR C O   
8508  C CB  . THR C 135 ? 0.3397 0.3512 0.2553 0.0810  -0.0012 -0.0509 135 THR C CB  
8509  O OG1 . THR C 135 ? 0.3207 0.3333 0.2408 0.0799  0.0022  -0.0483 135 THR C OG1 
8510  C CG2 . THR C 135 ? 0.3149 0.3247 0.2402 0.0795  -0.0038 -0.0573 135 THR C CG2 
8511  N N   . ALA C 136 ? 0.3122 0.3185 0.1995 0.0867  -0.0075 -0.0472 136 ALA C N   
8512  C CA  . ALA C 136 ? 0.3356 0.3426 0.2146 0.0912  -0.0115 -0.0487 136 ALA C CA  
8513  C C   . ALA C 136 ? 0.3614 0.3589 0.2345 0.0941  -0.0170 -0.0460 136 ALA C C   
8514  O O   . ALA C 136 ? 0.3436 0.3463 0.2190 0.0991  -0.0222 -0.0500 136 ALA C O   
8515  C CB  . ALA C 136 ? 0.3481 0.3566 0.2098 0.0923  -0.0075 -0.0444 136 ALA C CB  
8516  N N   . ALA C 137 ? 0.3054 0.2891 0.1695 0.0921  -0.0164 -0.0392 137 ALA C N   
8517  C CA  . ALA C 137 ? 0.3437 0.3157 0.2004 0.0972  -0.0216 -0.0359 137 ALA C CA  
8518  C C   . ALA C 137 ? 0.3323 0.3161 0.2077 0.1004  -0.0251 -0.0421 137 ALA C C   
8519  O O   . ALA C 137 ? 0.3085 0.2977 0.1831 0.1083  -0.0300 -0.0440 137 ALA C O   
8520  C CB  . ALA C 137 ? 0.3604 0.3106 0.2026 0.0930  -0.0208 -0.0272 137 ALA C CB  
8521  N N   . HIS C 138 ? 0.3360 0.3252 0.2280 0.0941  -0.0223 -0.0454 138 HIS C N   
8522  C CA  . HIS C 138 ? 0.3114 0.3117 0.2199 0.0934  -0.0244 -0.0509 138 HIS C CA  
8523  C C   . HIS C 138 ? 0.3590 0.3762 0.2751 0.0944  -0.0274 -0.0598 138 HIS C C   
8524  O O   . HIS C 138 ? 0.3460 0.3766 0.2689 0.0979  -0.0315 -0.0652 138 HIS C O   
8525  C CB  . HIS C 138 ? 0.3198 0.3159 0.2413 0.0847  -0.0199 -0.0512 138 HIS C CB  
8526  C CG  . HIS C 138 ? 0.3058 0.2872 0.2224 0.0845  -0.0190 -0.0441 138 HIS C CG  
8527  N ND1 . HIS C 138 ? 0.2804 0.2606 0.1937 0.0899  -0.0218 -0.0419 138 HIS C ND1 
8528  C CD2 . HIS C 138 ? 0.2894 0.2567 0.2019 0.0807  -0.0163 -0.0388 138 HIS C CD2 
8529  C CE1 . HIS C 138 ? 0.2832 0.2462 0.1892 0.0884  -0.0208 -0.0349 138 HIS C CE1 
8530  N NE2 . HIS C 138 ? 0.3018 0.2562 0.2074 0.0825  -0.0180 -0.0331 138 HIS C NE2 
8531  N N   . VAL C 139 ? 0.2727 0.2909 0.1868 0.0921  -0.0258 -0.0621 139 VAL C N   
8532  C CA  . VAL C 139 ? 0.3273 0.3570 0.2431 0.0942  -0.0299 -0.0699 139 VAL C CA  
8533  C C   . VAL C 139 ? 0.3102 0.3462 0.2175 0.1039  -0.0357 -0.0696 139 VAL C C   
8534  O O   . VAL C 139 ? 0.3192 0.3707 0.2337 0.1072  -0.0412 -0.0768 139 VAL C O   
8535  C CB  . VAL C 139 ? 0.3287 0.3549 0.2388 0.0927  -0.0269 -0.0706 139 VAL C CB  
8536  C CG1 . VAL C 139 ? 0.3065 0.3397 0.2119 0.0968  -0.0320 -0.0770 139 VAL C CG1 
8537  C CG2 . VAL C 139 ? 0.2734 0.2950 0.1923 0.0857  -0.0229 -0.0730 139 VAL C CG2 
8538  N N   . GLU C 140 ? 0.3329 0.3569 0.2241 0.1086  -0.0345 -0.0617 140 GLU C N   
8539  C CA  . GLU C 140 ? 0.3501 0.3746 0.2301 0.1192  -0.0395 -0.0606 140 GLU C CA  
8540  C C   . GLU C 140 ? 0.3995 0.4304 0.2843 0.1264  -0.0434 -0.0607 140 GLU C C   
8541  O O   . GLU C 140 ? 0.3992 0.4447 0.2860 0.1360  -0.0489 -0.0656 140 GLU C O   
8542  C CB  . GLU C 140 ? 0.3776 0.3817 0.2359 0.1204  -0.0363 -0.0518 140 GLU C CB  
8543  C CG  . GLU C 140 ? 0.3746 0.3786 0.2267 0.1164  -0.0327 -0.0525 140 GLU C CG  
8544  C CD  . GLU C 140 ? 0.4856 0.4725 0.3167 0.1130  -0.0274 -0.0436 140 GLU C CD  
8545  O OE1 . GLU C 140 ? 0.5143 0.4854 0.3353 0.1110  -0.0266 -0.0366 140 GLU C OE1 
8546  O OE2 . GLU C 140 ? 0.5092 0.4979 0.3324 0.1117  -0.0240 -0.0437 140 GLU C OE2 
8547  N N   . LEU C 141 ? 0.3747 0.3966 0.2612 0.1232  -0.0404 -0.0558 141 LEU C N   
8548  C CA  . LEU C 141 ? 0.3893 0.4175 0.2788 0.1313  -0.0433 -0.0554 141 LEU C CA  
8549  C C   . LEU C 141 ? 0.3482 0.4080 0.2566 0.1322  -0.0469 -0.0664 141 LEU C C   
8550  O O   . LEU C 141 ? 0.3270 0.4039 0.2373 0.1440  -0.0511 -0.0689 141 LEU C O   
8551  C CB  . LEU C 141 ? 0.3830 0.3951 0.2713 0.1252  -0.0392 -0.0488 141 LEU C CB  
8552  C CG  . LEU C 141 ? 0.4284 0.4282 0.3053 0.1348  -0.0411 -0.0419 141 LEU C CG  
8553  C CD1 . LEU C 141 ? 0.4200 0.4099 0.2816 0.1460  -0.0422 -0.0404 141 LEU C CD1 
8554  C CD2 . LEU C 141 ? 0.4287 0.4005 0.2955 0.1274  -0.0370 -0.0338 141 LEU C CD2 
8555  N N   . ASN C 142 ? 0.2990 0.4138 0.2794 0.0220  -0.0141 -0.0554 142 ASN C N   
8556  C CA  . ASN C 142 ? 0.3227 0.4285 0.3039 0.0243  -0.0170 -0.0593 142 ASN C CA  
8557  C C   . ASN C 142 ? 0.3365 0.4491 0.3173 0.0282  -0.0184 -0.0650 142 ASN C C   
8558  O O   . ASN C 142 ? 0.3583 0.4672 0.3415 0.0316  -0.0213 -0.0704 142 ASN C O   
8559  C CB  . ASN C 142 ? 0.2940 0.3963 0.2793 0.0276  -0.0193 -0.0633 142 ASN C CB  
8560  C CG  . ASN C 142 ? 0.3165 0.4075 0.3018 0.0239  -0.0188 -0.0578 142 ASN C CG  
8561  O OD1 . ASN C 142 ? 0.3315 0.4099 0.3161 0.0218  -0.0198 -0.0555 142 ASN C OD1 
8562  N ND2 . ASN C 142 ? 0.2668 0.3627 0.2529 0.0230  -0.0172 -0.0556 142 ASN C ND2 
8563  N N   . GLY C 143 ? 0.2578 0.3802 0.2361 0.0278  -0.0166 -0.0640 143 GLY C N   
8564  C CA  . GLY C 143 ? 0.2935 0.4219 0.2709 0.0312  -0.0178 -0.0688 143 GLY C CA  
8565  C C   . GLY C 143 ? 0.3019 0.4410 0.2820 0.0377  -0.0199 -0.0768 143 GLY C C   
8566  O O   . GLY C 143 ? 0.3278 0.4702 0.3081 0.0412  -0.0218 -0.0820 143 GLY C O   
8567  N N   . CYS C 144 ? 0.2947 0.4397 0.2771 0.0394  -0.0197 -0.0779 144 CYS C N   
8568  C CA  . CYS C 144 ? 0.2479 0.4032 0.2329 0.0455  -0.0217 -0.0854 144 CYS C CA  
8569  C C   . CYS C 144 ? 0.3242 0.4941 0.3075 0.0464  -0.0196 -0.0844 144 CYS C C   
8570  O O   . CYS C 144 ? 0.3173 0.4889 0.2983 0.0421  -0.0167 -0.0779 144 CYS C O   
8571  C CB  . CYS C 144 ? 0.2689 0.4194 0.2584 0.0475  -0.0237 -0.0883 144 CYS C CB  
8572  S SG  . CYS C 144 ? 0.3082 0.4411 0.3005 0.0461  -0.0263 -0.0886 144 CYS C SG  
8573  N N   . LYS C 145 ? 0.2615 0.4418 0.2460 0.0521  -0.0213 -0.0911 145 LYS C N   
8574  C CA  . LYS C 145 ? 0.3056 0.5005 0.2886 0.0540  -0.0197 -0.0912 145 LYS C CA  
8575  C C   . LYS C 145 ? 0.2806 0.4791 0.2668 0.0561  -0.0203 -0.0931 145 LYS C C   
8576  O O   . LYS C 145 ? 0.2766 0.4705 0.2662 0.0592  -0.0230 -0.0983 145 LYS C O   
8577  C CB  . LYS C 145 ? 0.3091 0.5141 0.2908 0.0593  -0.0212 -0.0973 145 LYS C CB  
8578  C CG  . LYS C 145 ? 0.3787 0.5992 0.3582 0.0617  -0.0196 -0.0974 145 LYS C CG  
8579  C CD  . LYS C 145 ? 0.4318 0.6620 0.4099 0.0674  -0.0213 -0.1038 145 LYS C CD  
8580  C CE  . LYS C 145 ? 0.5491 0.7809 0.5230 0.0657  -0.0199 -0.1006 145 LYS C CE  
8581  N NZ  . LYS C 145 ? 0.4231 0.6421 0.3971 0.0627  -0.0206 -0.0992 145 LYS C NZ  
8582  N N   . ALA C 146 ? 0.2449 0.4512 0.2300 0.0542  -0.0177 -0.0888 146 ALA C N   
8583  C CA  . ALA C 146 ? 0.2304 0.4417 0.2181 0.0560  -0.0179 -0.0900 146 ALA C CA  
8584  C C   . ALA C 146 ? 0.2493 0.4757 0.2360 0.0612  -0.0183 -0.0948 146 ALA C C   
8585  O O   . ALA C 146 ? 0.3567 0.5929 0.3405 0.0602  -0.0160 -0.0916 146 ALA C O   
8586  C CB  . ALA C 146 ? 0.2056 0.4164 0.1933 0.0506  -0.0150 -0.0823 146 ALA C CB  
8587  N N   . ILE C 147 ? 0.2683 0.4966 0.2574 0.0668  -0.0212 -0.1023 147 ILE C N   
8588  C CA  . ILE C 147 ? 0.2635 0.5053 0.2516 0.0724  -0.0219 -0.1078 147 ILE C CA  
8589  C C   . ILE C 147 ? 0.2312 0.4788 0.2212 0.0744  -0.0219 -0.1089 147 ILE C C   
8590  O O   . ILE C 147 ? 0.2335 0.4738 0.2270 0.0751  -0.0237 -0.1112 147 ILE C O   
8591  C CB  . ILE C 147 ? 0.2637 0.5040 0.2531 0.0776  -0.0254 -0.1160 147 ILE C CB  
8592  C CG1 . ILE C 147 ? 0.2629 0.4971 0.2505 0.0755  -0.0254 -0.1146 147 ILE C CG1 
8593  C CG2 . ILE C 147 ? 0.3140 0.5685 0.3020 0.0836  -0.0261 -0.1217 147 ILE C CG2 
8594  C CD1 . ILE C 147 ? 0.2957 0.5265 0.2854 0.0797  -0.0291 -0.1222 147 ILE C CD1 
8595  N N   . ASN C 148 ? 0.2974 0.5581 0.2850 0.0751  -0.0198 -0.1072 148 ASN C N   
8596  C CA  . ASN C 148 ? 0.2398 0.5079 0.2286 0.0768  -0.0194 -0.1078 148 ASN C CA  
8597  C C   . ASN C 148 ? 0.2814 0.5610 0.2692 0.0836  -0.0207 -0.1148 148 ASN C C   
8598  O O   . ASN C 148 ? 0.2268 0.5152 0.2113 0.0853  -0.0198 -0.1153 148 ASN C O   
8599  C CB  . ASN C 148 ? 0.2268 0.5012 0.2138 0.0721  -0.0159 -0.0999 148 ASN C CB  
8600  C CG  . ASN C 148 ? 0.2548 0.5184 0.2429 0.0654  -0.0145 -0.0928 148 ASN C CG  
8601  O OD1 . ASN C 148 ? 0.2578 0.5106 0.2489 0.0643  -0.0158 -0.0931 148 ASN C OD1 
8602  N ND2 . ASN C 148 ? 0.2639 0.5302 0.2495 0.0608  -0.0119 -0.0863 148 ASN C ND2 
8603  N N   . ILE C 149 ? 0.2438 0.5232 0.2343 0.0876  -0.0228 -0.1203 149 ILE C N   
8604  C CA  . ILE C 149 ? 0.2546 0.5442 0.2445 0.0943  -0.0243 -0.1275 149 ILE C CA  
8605  C C   . ILE C 149 ? 0.2443 0.5400 0.2353 0.0966  -0.0239 -0.1287 149 ILE C C   
8606  O O   . ILE C 149 ? 0.3080 0.6046 0.3007 0.1018  -0.0263 -0.1358 149 ILE C O   
8607  C CB  . ILE C 149 ? 0.2263 0.5090 0.2185 0.0985  -0.0282 -0.1355 149 ILE C CB  
8608  C CG1 . ILE C 149 ? 0.2718 0.5405 0.2685 0.0970  -0.0303 -0.1365 149 ILE C CG1 
8609  C CG2 . ILE C 149 ? 0.2175 0.4979 0.2079 0.0975  -0.0285 -0.1352 149 ILE C CG2 
8610  C CD1 . ILE C 149 ? 0.2345 0.4973 0.2343 0.1015  -0.0344 -0.1449 149 ILE C CD1 
8611  N N   . VAL C 150 ? 0.2712 0.5713 0.2612 0.0927  -0.0209 -0.1220 150 VAL C N   
8612  C CA  . VAL C 150 ? 0.2625 0.5708 0.2534 0.0950  -0.0204 -0.1230 150 VAL C CA  
8613  C C   . VAL C 150 ? 0.2500 0.5714 0.2387 0.1013  -0.0206 -0.1287 150 VAL C C   
8614  O O   . VAL C 150 ? 0.2939 0.6208 0.2795 0.1026  -0.0199 -0.1292 150 VAL C O   
8615  C CB  . VAL C 150 ? 0.2369 0.5493 0.2268 0.0895  -0.0171 -0.1146 150 VAL C CB  
8616  C CG1 . VAL C 150 ? 0.2602 0.5845 0.2461 0.0888  -0.0142 -0.1111 150 VAL C CG1 
8617  C CG2 . VAL C 150 ? 0.2342 0.5539 0.2270 0.0918  -0.0177 -0.1162 150 VAL C CG2 
8618  N N   . THR C 151 ? 0.2984 0.6272 0.2893 0.1062  -0.0220 -0.1337 151 THR C N   
8619  C CA  . THR C 151 ? 0.2907 0.6327 0.2797 0.1123  -0.0218 -0.1387 151 THR C CA  
8620  C C   . THR C 151 ? 0.2921 0.6448 0.2766 0.1100  -0.0178 -0.1326 151 THR C C   
8621  O O   . THR C 151 ? 0.3010 0.6540 0.2850 0.1045  -0.0151 -0.1251 151 THR C O   
8622  C CB  . THR C 151 ? 0.2560 0.6037 0.2478 0.1169  -0.0233 -0.1435 151 THR C CB  
8623  O OG1 . THR C 151 ? 0.3503 0.7116 0.3399 0.1226  -0.0227 -0.1476 151 THR C OG1 
8624  C CG2 . THR C 151 ? 0.2934 0.6428 0.2863 0.1125  -0.0212 -0.1371 151 THR C CG2 
8625  N N   . GLU C 152 ? 0.2811 0.6422 0.2624 0.1143  -0.0174 -0.1360 152 GLU C N   
8626  C CA  . GLU C 152 ? 0.3298 0.7036 0.3071 0.1135  -0.0139 -0.1314 152 GLU C CA  
8627  C C   . GLU C 152 ? 0.3324 0.7153 0.3100 0.1133  -0.0115 -0.1287 152 GLU C C   
8628  O O   . GLU C 152 ? 0.3163 0.7074 0.2914 0.1106  -0.0082 -0.1228 152 GLU C O   
8629  C CB  . GLU C 152 ? 0.3466 0.7299 0.3209 0.1198  -0.0147 -0.1371 152 GLU C CB  
8630  C CG  . GLU C 152 ? 0.4671 0.8554 0.4428 0.1270  -0.0167 -0.1453 152 GLU C CG  
8631  C CD  . GLU C 152 ? 0.6000 0.9999 0.5725 0.1334  -0.0171 -0.1504 152 GLU C CD  
8632  O OE1 . GLU C 152 ? 0.7297 1.1345 0.6986 0.1324  -0.0157 -0.1474 152 GLU C OE1 
8633  O OE2 . GLU C 152 ? 0.6613 1.0655 0.6347 0.1396  -0.0189 -0.1575 152 GLU C OE2 
8634  N N   . LYS C 153 ? 0.3375 0.7219 0.3188 0.1168  -0.0136 -0.1334 153 LYS C N   
8635  C CA  . LYS C 153 ? 0.3115 0.7060 0.2936 0.1169  -0.0116 -0.1312 153 LYS C CA  
8636  C C   . LYS C 153 ? 0.2940 0.6851 0.2764 0.1090  -0.0091 -0.1220 153 LYS C C   
8637  O O   . LYS C 153 ? 0.3065 0.7070 0.2883 0.1076  -0.0063 -0.1179 153 LYS C O   
8638  C CB  . LYS C 153 ? 0.3243 0.7183 0.3104 0.1216  -0.0145 -0.1377 153 LYS C CB  
8639  C CG  . LYS C 153 ? 0.3587 0.7551 0.3450 0.1295  -0.0174 -0.1473 153 LYS C CG  
8640  C CD  . LYS C 153 ? 0.4582 0.8697 0.4411 0.1339  -0.0153 -0.1488 153 LYS C CD  
8641  C CE  . LYS C 153 ? 0.5825 0.9974 0.5663 0.1422  -0.0184 -0.1587 153 LYS C CE  
8642  N NZ  . LYS C 153 ? 0.5734 0.9868 0.5612 0.1454  -0.0203 -0.1630 153 LYS C NZ  
8643  N N   . ALA C 154 ? 0.3225 0.7004 0.3061 0.1039  -0.0100 -0.1186 154 ALA C N   
8644  C CA  . ALA C 154 ? 0.3074 0.6812 0.2917 0.0964  -0.0079 -0.1101 154 ALA C CA  
8645  C C   . ALA C 154 ? 0.3747 0.7527 0.3550 0.0920  -0.0041 -0.1029 154 ALA C C   
8646  O O   . ALA C 154 ? 0.3800 0.7588 0.3607 0.0865  -0.0019 -0.0960 154 ALA C O   
8647  C CB  . ALA C 154 ? 0.2578 0.6157 0.2442 0.0924  -0.0098 -0.1085 154 ALA C CB  
8648  N N   . PHE C 155 ? 0.3428 0.7262 0.3199 0.0949  -0.0038 -0.1050 155 PHE C N   
8649  C CA  . PHE C 155 ? 0.3635 0.7544 0.3372 0.0920  -0.0009 -0.0993 155 PHE C CA  
8650  C C   . PHE C 155 ? 0.3794 0.7854 0.3512 0.0943  0.0019  -0.0984 155 PHE C C   
8651  O O   . PHE C 155 ? 0.4290 0.8413 0.3984 0.0911  0.0047  -0.0927 155 PHE C O   
8652  C CB  . PHE C 155 ? 0.3866 0.7765 0.3573 0.0943  -0.0018 -0.1018 155 PHE C CB  
8653  C CG  . PHE C 155 ? 0.4399 0.8154 0.4123 0.0914  -0.0040 -0.1018 155 PHE C CG  
8654  C CD1 . PHE C 155 ? 0.4739 0.8407 0.4478 0.0842  -0.0032 -0.0949 155 PHE C CD1 
8655  C CD2 . PHE C 155 ? 0.4150 0.7854 0.3877 0.0959  -0.0070 -0.1088 155 PHE C CD2 
8656  C CE1 . PHE C 155 ? 0.5645 0.9180 0.5399 0.0816  -0.0050 -0.0948 155 PHE C CE1 
8657  C CE2 . PHE C 155 ? 0.4146 0.7716 0.3889 0.0932  -0.0089 -0.1087 155 PHE C CE2 
8658  C CZ  . PHE C 155 ? 0.5289 0.8775 0.5045 0.0861  -0.0078 -0.1016 155 PHE C CZ  
8659  N N   . ASP C 156 ? 0.3665 0.7780 0.3395 0.0996  0.0012  -0.1039 156 ASP C N   
8660  C CA  . ASP C 156 ? 0.3076 0.7335 0.2794 0.1020  0.0039  -0.1033 156 ASP C CA  
8661  C C   . ASP C 156 ? 0.3520 0.7772 0.3267 0.0977  0.0052  -0.0988 156 ASP C C   
8662  O O   . ASP C 156 ? 0.2628 0.6898 0.2407 0.1008  0.0034  -0.1030 156 ASP C O   
8663  C CB  . ASP C 156 ? 0.3063 0.7388 0.2777 0.1103  0.0025  -0.1118 156 ASP C CB  
8664  C CG  . ASP C 156 ? 0.4829 0.9315 0.4521 0.1135  0.0055  -0.1114 156 ASP C CG  
8665  O OD1 . ASP C 156 ? 0.4781 0.9322 0.4468 0.1091  0.0087  -0.1046 156 ASP C OD1 
8666  O OD2 . ASP C 156 ? 0.5580 1.0136 0.5259 0.1205  0.0046  -0.1179 156 ASP C OD2 
8667  N N   . SER C 157 ? 0.3081 0.7345 0.2822 0.0912  0.0077  -0.0908 157 SER C N   
8668  C CA  . SER C 157 ? 0.3985 0.8209 0.3758 0.0858  0.0083  -0.0858 157 SER C CA  
8669  C C   . SER C 157 ? 0.3730 0.8057 0.3521 0.0887  0.0093  -0.0876 157 SER C C   
8670  O O   . SER C 157 ? 0.3293 0.7601 0.3120 0.0883  0.0077  -0.0884 157 SER C O   
8671  C CB  . SER C 157 ? 0.4116 0.8344 0.3877 0.0786  0.0106  -0.0772 157 SER C CB  
8672  O OG  . SER C 157 ? 0.5073 0.9253 0.4864 0.0731  0.0107  -0.0725 157 SER C OG  
8673  N N   . GLU C 158 ? 0.3622 0.8077 0.3391 0.0920  0.0119  -0.0883 158 GLU C N   
8674  C CA  . GLU C 158 ? 0.3744 0.8319 0.3533 0.0948  0.0132  -0.0896 158 GLU C CA  
8675  C C   . GLU C 158 ? 0.3483 0.8117 0.3283 0.1034  0.0108  -0.0988 158 GLU C C   
8676  O O   . GLU C 158 ? 0.3451 0.8172 0.3272 0.1062  0.0113  -0.1006 158 GLU C O   
8677  C CB  . GLU C 158 ? 0.4888 0.9575 0.4652 0.0935  0.0176  -0.0850 158 GLU C CB  
8678  C CG  . GLU C 158 ? 0.5396 1.0060 0.5153 0.0855  0.0195  -0.0764 158 GLU C CG  
8679  C CD  . GLU C 158 ? 0.6304 1.1080 0.6069 0.0828  0.0231  -0.0714 158 GLU C CD  
8680  O OE1 . GLU C 158 ? 0.5537 1.0362 0.5330 0.0847  0.0236  -0.0732 158 GLU C OE1 
8681  O OE2 . GLU C 158 ? 0.6796 1.1608 0.6538 0.0790  0.0256  -0.0657 158 GLU C OE2 
8682  N N   . THR C 159 ? 0.3120 0.7707 0.2907 0.1078  0.0081  -0.1046 159 THR C N   
8683  C CA  . THR C 159 ? 0.3440 0.8070 0.3239 0.1160  0.0055  -0.1137 159 THR C CA  
8684  C C   . THR C 159 ? 0.3367 0.7901 0.3206 0.1164  0.0021  -0.1169 159 THR C C   
8685  O O   . THR C 159 ? 0.3635 0.8042 0.3481 0.1136  -0.0002 -0.1167 159 THR C O   
8686  C CB  . THR C 159 ? 0.3275 0.7893 0.3045 0.1207  0.0039  -0.1189 159 THR C CB  
8687  O OG1 . THR C 159 ? 0.2885 0.7601 0.2614 0.1212  0.0072  -0.1162 159 THR C OG1 
8688  C CG2 . THR C 159 ? 0.2969 0.7611 0.2754 0.1290  0.0007  -0.1286 159 THR C CG2 
8689  N N   . TYR C 160 ? 0.2818 0.7412 0.2685 0.1198  0.0018  -0.1200 160 TYR C N   
8690  C CA  . TYR C 160 ? 0.3317 0.7819 0.3220 0.1205  -0.0013 -0.1231 160 TYR C CA  
8691  C C   . TYR C 160 ? 0.2905 0.7318 0.2812 0.1253  -0.0053 -0.1308 160 TYR C C   
8692  O O   . TYR C 160 ? 0.2648 0.7114 0.2539 0.1311  -0.0060 -0.1364 160 TYR C O   
8693  C CB  . TYR C 160 ? 0.2710 0.7298 0.2640 0.1243  -0.0007 -0.1256 160 TYR C CB  
8694  C CG  . TYR C 160 ? 0.2761 0.7253 0.2728 0.1258  -0.0037 -0.1292 160 TYR C CG  
8695  C CD1 . TYR C 160 ? 0.2735 0.7182 0.2716 0.1326  -0.0070 -0.1378 160 TYR C CD1 
8696  C CD2 . TYR C 160 ? 0.2636 0.7078 0.2626 0.1206  -0.0032 -0.1241 160 TYR C CD2 
8697  C CE1 . TYR C 160 ? 0.2571 0.6920 0.2587 0.1340  -0.0096 -0.1410 160 TYR C CE1 
8698  C CE2 . TYR C 160 ? 0.2482 0.6830 0.2504 0.1222  -0.0058 -0.1273 160 TYR C CE2 
8699  C CZ  . TYR C 160 ? 0.2689 0.6989 0.2724 0.1289  -0.0089 -0.1356 160 TYR C CZ  
8700  O OH  . TYR C 160 ? 0.3028 0.7225 0.3096 0.1306  -0.0113 -0.1387 160 TYR C OH  
8701  N N   . ASP C 161 ? 0.2472 0.6748 0.2402 0.1229  -0.0079 -0.1310 161 ASP C N   
8702  C CA  . ASP C 161 ? 0.2571 0.6752 0.2518 0.1275  -0.0119 -0.1387 161 ASP C CA  
8703  C C   . ASP C 161 ? 0.2737 0.6805 0.2720 0.1258  -0.0139 -0.1387 161 ASP C C   
8704  O O   . ASP C 161 ? 0.2638 0.6670 0.2628 0.1196  -0.0127 -0.1319 161 ASP C O   
8705  C CB  . ASP C 161 ? 0.2792 0.6897 0.2718 0.1262  -0.0132 -0.1391 161 ASP C CB  
8706  C CG  . ASP C 161 ? 0.3249 0.7282 0.3191 0.1319  -0.0172 -0.1480 161 ASP C CG  
8707  O OD1 . ASP C 161 ? 0.4074 0.8183 0.4005 0.1381  -0.0178 -0.1539 161 ASP C OD1 
8708  O OD2 . ASP C 161 ? 0.2741 0.6639 0.2708 0.1302  -0.0198 -0.1490 161 ASP C OD2 
8709  N N   . ASP C 162 ? 0.2485 0.6495 0.2494 0.1314  -0.0171 -0.1463 162 ASP C N   
8710  C CA  . ASP C 162 ? 0.2649 0.6546 0.2694 0.1305  -0.0191 -0.1469 162 ASP C CA  
8711  C C   . ASP C 162 ? 0.2331 0.6083 0.2380 0.1251  -0.0206 -0.1437 162 ASP C C   
8712  O O   . ASP C 162 ? 0.2517 0.6195 0.2584 0.1213  -0.0208 -0.1400 162 ASP C O   
8713  C CB  . ASP C 162 ? 0.2848 0.6707 0.2921 0.1379  -0.0220 -0.1558 162 ASP C CB  
8714  C CG  . ASP C 162 ? 0.3444 0.7413 0.3530 0.1427  -0.0206 -0.1580 162 ASP C CG  
8715  O OD1 . ASP C 162 ? 0.2925 0.6979 0.3006 0.1397  -0.0175 -0.1524 162 ASP C OD1 
8716  O OD2 . ASP C 162 ? 0.3343 0.7312 0.3445 0.1494  -0.0225 -0.1655 162 ASP C OD2 
8717  N N   . TRP C 163 ? 0.2827 0.6536 0.2861 0.1248  -0.0218 -0.1451 163 TRP C N   
8718  C CA  . TRP C 163 ? 0.2257 0.5817 0.2302 0.1209  -0.0238 -0.1438 163 TRP C CA  
8719  C C   . TRP C 163 ? 0.2647 0.6213 0.2661 0.1162  -0.0221 -0.1387 163 TRP C C   
8720  O O   . TRP C 163 ? 0.2702 0.6214 0.2711 0.1173  -0.0237 -0.1417 163 TRP C O   
8721  C CB  . TRP C 163 ? 0.2320 0.5780 0.2391 0.1258  -0.0277 -0.1521 163 TRP C CB  
8722  C CG  . TRP C 163 ? 0.2569 0.6036 0.2668 0.1316  -0.0291 -0.1579 163 TRP C CG  
8723  C CD1 . TRP C 163 ? 0.2683 0.6220 0.2783 0.1385  -0.0299 -0.1648 163 TRP C CD1 
8724  C CD2 . TRP C 163 ? 0.2361 0.5762 0.2490 0.1311  -0.0296 -0.1570 163 TRP C CD2 
8725  N NE1 . TRP C 163 ? 0.3410 0.6925 0.3543 0.1422  -0.0308 -0.1683 163 TRP C NE1 
8726  C CE2 . TRP C 163 ? 0.3067 0.6497 0.3218 0.1379  -0.0306 -0.1636 163 TRP C CE2 
8727  C CE3 . TRP C 163 ? 0.2322 0.5638 0.2463 0.1258  -0.0293 -0.1513 163 TRP C CE3 
8728  C CZ2 . TRP C 163 ? 0.3316 0.6691 0.3501 0.1395  -0.0311 -0.1643 163 TRP C CZ2 
8729  C CZ3 . TRP C 163 ? 0.2840 0.6103 0.3011 0.1275  -0.0299 -0.1523 163 TRP C CZ3 
8730  C CH2 . TRP C 163 ? 0.3078 0.6369 0.3272 0.1342  -0.0307 -0.1586 163 TRP C CH2 
8731  N N   . LYS C 164 ? 0.2145 0.5768 0.2141 0.1107  -0.0189 -0.1307 164 LYS C N   
8732  C CA  . LYS C 164 ? 0.2178 0.5799 0.2144 0.1062  -0.0169 -0.1254 164 LYS C CA  
8733  C C   . LYS C 164 ? 0.2419 0.5892 0.2397 0.1014  -0.0182 -0.1226 164 LYS C C   
8734  O O   . LYS C 164 ? 0.2454 0.5906 0.2408 0.0973  -0.0165 -0.1179 164 LYS C O   
8735  C CB  . LYS C 164 ? 0.2368 0.6083 0.2315 0.1014  -0.0130 -0.1175 164 LYS C CB  
8736  C CG  . LYS C 164 ? 0.2511 0.6379 0.2436 0.1055  -0.0109 -0.1192 164 LYS C CG  
8737  C CD  . LYS C 164 ? 0.2403 0.6349 0.2309 0.1001  -0.0069 -0.1109 164 LYS C CD  
8738  C CE  . LYS C 164 ? 0.2699 0.6791 0.2578 0.1039  -0.0046 -0.1123 164 LYS C CE  
8739  N NZ  . LYS C 164 ? 0.2845 0.6994 0.2701 0.0983  -0.0006 -0.1041 164 LYS C NZ  
8740  N N   . GLY C 165 ? 0.2715 0.6080 0.2726 0.1019  -0.0210 -0.1251 165 GLY C N   
8741  C CA  . GLY C 165 ? 0.2206 0.5426 0.2231 0.0982  -0.0224 -0.1234 165 GLY C CA  
8742  C C   . GLY C 165 ? 0.2485 0.5621 0.2523 0.1024  -0.0257 -0.1308 165 GLY C C   
8743  O O   . GLY C 165 ? 0.2208 0.5216 0.2260 0.0996  -0.0269 -0.1297 165 GLY C O   
8744  N N   . ASP C 166 ? 0.2183 0.5385 0.2217 0.1089  -0.0270 -0.1381 166 ASP C N   
8745  C CA  . ASP C 166 ? 0.2551 0.5675 0.2603 0.1131  -0.0303 -0.1456 166 ASP C CA  
8746  C C   . ASP C 166 ? 0.2836 0.5897 0.2869 0.1102  -0.0301 -0.1439 166 ASP C C   
8747  O O   . ASP C 166 ? 0.2700 0.5818 0.2696 0.1073  -0.0272 -0.1389 166 ASP C O   
8748  C CB  . ASP C 166 ? 0.2272 0.5497 0.2318 0.1204  -0.0313 -0.1531 166 ASP C CB  
8749  C CG  . ASP C 166 ? 0.2791 0.6014 0.2869 0.1248  -0.0330 -0.1580 166 ASP C CG  
8750  O OD1 . ASP C 166 ? 0.2972 0.6117 0.3074 0.1222  -0.0335 -0.1555 166 ASP C OD1 
8751  O OD2 . ASP C 166 ? 0.2890 0.6187 0.2967 0.1309  -0.0339 -0.1643 166 ASP C OD2 
8752  N N   . PHE C 167 ? 0.2647 0.5583 0.2706 0.1111  -0.0332 -0.1480 167 PHE C N   
8753  C CA  . PHE C 167 ? 0.2361 0.5249 0.2405 0.1104  -0.0337 -0.1490 167 PHE C CA  
8754  C C   . PHE C 167 ? 0.2780 0.5782 0.2799 0.1159  -0.0338 -0.1544 167 PHE C C   
8755  O O   . PHE C 167 ? 0.2350 0.5405 0.2384 0.1217  -0.0356 -0.1611 167 PHE C O   
8756  C CB  . PHE C 167 ? 0.2370 0.5109 0.2453 0.1109  -0.0372 -0.1533 167 PHE C CB  
8757  C CG  . PHE C 167 ? 0.2549 0.5155 0.2647 0.1049  -0.0369 -0.1474 167 PHE C CG  
8758  C CD1 . PHE C 167 ? 0.2258 0.4820 0.2384 0.1034  -0.0374 -0.1453 167 PHE C CD1 
8759  C CD2 . PHE C 167 ? 0.2275 0.4795 0.2359 0.1009  -0.0363 -0.1443 167 PHE C CD2 
8760  C CE1 . PHE C 167 ? 0.2387 0.4827 0.2527 0.0982  -0.0372 -0.1400 167 PHE C CE1 
8761  C CE2 . PHE C 167 ? 0.2425 0.4818 0.2521 0.0955  -0.0359 -0.1388 167 PHE C CE2 
8762  C CZ  . PHE C 167 ? 0.2353 0.4708 0.2479 0.0942  -0.0364 -0.1367 167 PHE C CZ  
8763  N N   . ASP C 168 ? 0.2802 0.5833 0.2782 0.1142  -0.0320 -0.1518 168 ASP C N   
8764  C CA  . ASP C 168 ? 0.2956 0.6067 0.2913 0.1195  -0.0327 -0.1575 168 ASP C CA  
8765  C C   . ASP C 168 ? 0.2767 0.5772 0.2754 0.1217  -0.0366 -0.1641 168 ASP C C   
8766  O O   . ASP C 168 ? 0.3097 0.6017 0.3082 0.1185  -0.0369 -0.1621 168 ASP C O   
8767  C CB  . ASP C 168 ? 0.3108 0.6282 0.3015 0.1169  -0.0296 -0.1523 168 ASP C CB  
8768  C CG  . ASP C 168 ? 0.3516 0.6810 0.3397 0.1230  -0.0303 -0.1580 168 ASP C CG  
8769  O OD1 . ASP C 168 ? 0.3169 0.6439 0.3068 0.1277  -0.0337 -0.1657 168 ASP C OD1 
8770  O OD2 . ASP C 168 ? 0.3647 0.7060 0.3489 0.1231  -0.0275 -0.1546 168 ASP C OD2 
8771  N N   . ILE C 169 ? 0.2797 0.5812 0.2816 0.1274  -0.0397 -0.1721 169 ILE C N   
8772  C CA  . ILE C 169 ? 0.2972 0.5880 0.3027 0.1294  -0.0435 -0.1784 169 ILE C CA  
8773  C C   . ILE C 169 ? 0.3157 0.6089 0.3187 0.1309  -0.0441 -0.1810 169 ILE C C   
8774  O O   . ILE C 169 ? 0.3434 0.6277 0.3487 0.1299  -0.0465 -0.1832 169 ILE C O   
8775  C CB  . ILE C 169 ? 0.3663 0.6582 0.3755 0.1354  -0.0465 -0.1866 169 ILE C CB  
8776  C CG1 . ILE C 169 ? 0.3051 0.5950 0.3166 0.1342  -0.0459 -0.1839 169 ILE C CG1 
8777  C CG2 . ILE C 169 ? 0.3742 0.6542 0.3877 0.1370  -0.0504 -0.1929 169 ILE C CG2 
8778  C CD1 . ILE C 169 ? 0.3041 0.5791 0.3185 0.1287  -0.0464 -0.1795 169 ILE C CD1 
8779  N N   . LYS C 170 ? 0.3167 0.6244 0.3156 0.1340  -0.0425 -0.1816 170 LYS C N   
8780  C CA  . LYS C 170 ? 0.3432 0.6565 0.3401 0.1366  -0.0437 -0.1849 170 LYS C CA  
8781  C C   . LYS C 170 ? 0.3382 0.6457 0.3339 0.1311  -0.0425 -0.1790 170 LYS C C   
8782  O O   . LYS C 170 ? 0.3607 0.6638 0.3576 0.1318  -0.0449 -0.1823 170 LYS C O   
8783  C CB  . LYS C 170 ? 0.3729 0.7031 0.3653 0.1408  -0.0417 -0.1856 170 LYS C CB  
8784  C CG  . LYS C 170 ? 0.4259 0.7630 0.4160 0.1445  -0.0432 -0.1898 170 LYS C CG  
8785  C CD  . LYS C 170 ? 0.4793 0.8333 0.4649 0.1489  -0.0412 -0.1904 170 LYS C CD  
8786  C CE  . LYS C 170 ? 0.5700 0.9313 0.5533 0.1532  -0.0428 -0.1948 170 LYS C CE  
8787  N NZ  . LYS C 170 ? 0.5069 0.8650 0.4881 0.1488  -0.0416 -0.1895 170 LYS C NZ  
8788  N N   . LYS C 171 ? 0.3149 0.6221 0.3084 0.1256  -0.0390 -0.1703 171 LYS C N   
8789  C CA  . LYS C 171 ? 0.3037 0.6046 0.2960 0.1201  -0.0377 -0.1642 171 LYS C CA  
8790  C C   . LYS C 171 ? 0.3116 0.5962 0.3083 0.1167  -0.0398 -0.1641 171 LYS C C   
8791  O O   . LYS C 171 ? 0.2866 0.5649 0.2830 0.1136  -0.0398 -0.1617 171 LYS C O   
8792  C CB  . LYS C 171 ? 0.3412 0.6460 0.3304 0.1150  -0.0333 -0.1549 171 LYS C CB  
8793  C CG  . LYS C 171 ? 0.3708 0.6910 0.3551 0.1171  -0.0307 -0.1533 171 LYS C CG  
8794  C CD  . LYS C 171 ? 0.3572 0.6793 0.3392 0.1112  -0.0266 -0.1437 171 LYS C CD  
8795  C CE  . LYS C 171 ? 0.3870 0.7241 0.3644 0.1128  -0.0238 -0.1413 171 LYS C CE  
8796  N NZ  . LYS C 171 ? 0.4386 0.7765 0.4142 0.1064  -0.0200 -0.1318 171 LYS C NZ  
8797  N N   . LEU C 172 ? 0.3118 0.5893 0.3123 0.1173  -0.0413 -0.1664 172 LEU C N   
8798  C CA  . LEU C 172 ? 0.2947 0.5565 0.2996 0.1142  -0.0434 -0.1662 172 LEU C CA  
8799  C C   . LEU C 172 ? 0.3467 0.6040 0.3541 0.1169  -0.0470 -0.1729 172 LEU C C   
8800  O O   . LEU C 172 ? 0.3035 0.5524 0.3119 0.1136  -0.0476 -0.1708 172 LEU C O   
8801  C CB  . LEU C 172 ? 0.2689 0.5246 0.2773 0.1147  -0.0443 -0.1675 172 LEU C CB  
8802  C CG  . LEU C 172 ? 0.2899 0.5291 0.3030 0.1119  -0.0466 -0.1675 172 LEU C CG  
8803  C CD1 . LEU C 172 ? 0.3057 0.5375 0.3176 0.1053  -0.0444 -0.1591 172 LEU C CD1 
8804  C CD2 . LEU C 172 ? 0.2628 0.4974 0.2791 0.1131  -0.0475 -0.1690 172 LEU C CD2 
8805  N N   . LYS C 173 ? 0.3218 0.5852 0.3305 0.1230  -0.0496 -0.1812 173 LYS C N   
8806  C CA  . LYS C 173 ? 0.3241 0.5847 0.3356 0.1260  -0.0532 -0.1881 173 LYS C CA  
8807  C C   . LYS C 173 ? 0.3164 0.5834 0.3242 0.1258  -0.0524 -0.1869 173 LYS C C   
8808  O O   . LYS C 173 ? 0.3427 0.6037 0.3527 0.1252  -0.0545 -0.1891 173 LYS C O   
8809  C CB  . LYS C 173 ? 0.3991 0.6654 0.4125 0.1327  -0.0559 -0.1972 173 LYS C CB  
8810  C CG  . LYS C 173 ? 0.3134 0.5729 0.3306 0.1333  -0.0569 -0.1989 173 LYS C CG  
8811  C CD  . LYS C 173 ? 0.4041 0.6700 0.4227 0.1403  -0.0592 -0.2078 173 LYS C CD  
8812  C CE  . LYS C 173 ? 0.4376 0.6953 0.4602 0.1409  -0.0603 -0.2097 173 LYS C CE  
8813  N NZ  . LYS C 173 ? 0.3742 0.6370 0.3985 0.1477  -0.0625 -0.2183 173 LYS C NZ  
8814  N N   . GLU C 174 ? 0.2983 0.5776 0.3009 0.1263  -0.0493 -0.1833 174 GLU C N   
8815  C CA  . GLU C 174 ? 0.3485 0.6336 0.3471 0.1259  -0.0481 -0.1813 174 GLU C CA  
8816  C C   . GLU C 174 ? 0.3457 0.6201 0.3445 0.1195  -0.0468 -0.1747 174 GLU C C   
8817  O O   . GLU C 174 ? 0.3538 0.6259 0.3525 0.1193  -0.0479 -0.1759 174 GLU C O   
8818  C CB  . GLU C 174 ? 0.3277 0.6270 0.3208 0.1267  -0.0445 -0.1773 174 GLU C CB  
8819  C CG  . GLU C 174 ? 0.4135 0.7262 0.4049 0.1339  -0.0458 -0.1842 174 GLU C CG  
8820  C CD  . GLU C 174 ? 0.4793 0.8053 0.4656 0.1346  -0.0420 -0.1797 174 GLU C CD  
8821  O OE1 . GLU C 174 ? 0.4290 0.7548 0.4153 0.1320  -0.0397 -0.1753 174 GLU C OE1 
8822  O OE2 . GLU C 174 ? 0.6130 0.9500 0.5955 0.1376  -0.0414 -0.1806 174 GLU C OE2 
8823  N N   . ASN C 175 ? 0.2989 0.5666 0.2977 0.1143  -0.0444 -0.1677 175 ASN C N   
8824  C CA  . ASN C 175 ? 0.3299 0.5868 0.3286 0.1081  -0.0430 -0.1612 175 ASN C CA  
8825  C C   . ASN C 175 ? 0.3072 0.5509 0.3111 0.1075  -0.0464 -0.1648 175 ASN C C   
8826  O O   . ASN C 175 ? 0.3554 0.5922 0.3591 0.1044  -0.0464 -0.1623 175 ASN C O   
8827  C CB  . ASN C 175 ? 0.3083 0.5620 0.3059 0.1030  -0.0397 -0.1531 175 ASN C CB  
8828  C CG  . ASN C 175 ? 0.2654 0.5287 0.2577 0.1007  -0.0357 -0.1466 175 ASN C CG  
8829  O OD1 . ASN C 175 ? 0.3376 0.5990 0.3273 0.0975  -0.0342 -0.1422 175 ASN C OD1 
8830  N ND2 . ASN C 175 ? 0.2856 0.5591 0.2762 0.1024  -0.0340 -0.1457 175 ASN C ND2 
8831  N N   . ILE C 176 ? 0.2779 0.5176 0.2864 0.1103  -0.0493 -0.1705 176 ILE C N   
8832  C CA  . ILE C 176 ? 0.3320 0.5599 0.3458 0.1101  -0.0528 -0.1746 176 ILE C CA  
8833  C C   . ILE C 176 ? 0.2979 0.5299 0.3121 0.1135  -0.0553 -0.1806 176 ILE C C   
8834  O O   . ILE C 176 ? 0.2705 0.4939 0.2874 0.1118  -0.0570 -0.1814 176 ILE C O   
8835  C CB  . ILE C 176 ? 0.3034 0.5262 0.3221 0.1125  -0.0554 -0.1795 176 ILE C CB  
8836  C CG1 . ILE C 176 ? 0.3165 0.5341 0.3350 0.1088  -0.0531 -0.1731 176 ILE C CG1 
8837  C CG2 . ILE C 176 ? 0.3237 0.5350 0.3484 0.1125  -0.0592 -0.1842 176 ILE C CG2 
8838  C CD1 . ILE C 176 ? 0.2915 0.5032 0.3147 0.1108  -0.0554 -0.1773 176 ILE C CD1 
8839  N N   . ALA C 177 ? 0.3019 0.5476 0.3133 0.1185  -0.0554 -0.1848 177 ALA C N   
8840  C CA  . ALA C 177 ? 0.3546 0.6055 0.3661 0.1222  -0.0577 -0.1907 177 ALA C CA  
8841  C C   . ALA C 177 ? 0.3692 0.6209 0.3767 0.1190  -0.0555 -0.1853 177 ALA C C   
8842  O O   . ALA C 177 ? 0.4633 0.7111 0.4728 0.1191  -0.0576 -0.1880 177 ALA C O   
8843  C CB  . ALA C 177 ? 0.3171 0.5826 0.3265 0.1287  -0.0584 -0.1965 177 ALA C CB  
8844  N N   . GLN C 178 ? 0.3931 0.6499 0.3952 0.1163  -0.0514 -0.1779 178 GLN C N   
8845  C CA  . GLN C 178 ? 0.3510 0.6092 0.3490 0.1135  -0.0491 -0.1727 178 GLN C CA  
8846  C C   . GLN C 178 ? 0.3657 0.6095 0.3654 0.1075  -0.0487 -0.1677 178 GLN C C   
8847  O O   . GLN C 178 ? 0.3625 0.6032 0.3621 0.1069  -0.0496 -0.1682 178 GLN C O   
8848  C CB  . GLN C 178 ? 0.3921 0.6593 0.3842 0.1118  -0.0448 -0.1659 178 GLN C CB  
8849  C CG  . GLN C 178 ? 0.4903 0.7726 0.4800 0.1175  -0.0447 -0.1699 178 GLN C CG  
8850  C CD  . GLN C 178 ? 0.5865 0.8790 0.5729 0.1216  -0.0453 -0.1731 178 GLN C CD  
8851  O OE1 . GLN C 178 ? 0.7024 0.9997 0.6908 0.1273  -0.0487 -0.1813 178 GLN C OE1 
8852  N NE2 . GLN C 178 ? 0.4860 0.7822 0.4675 0.1189  -0.0422 -0.1666 178 GLN C NE2 
8853  N N   . HIS C 179 ? 0.3538 0.5889 0.3549 0.1033  -0.0473 -0.1628 179 HIS C N   
8854  C CA  . HIS C 179 ? 0.3299 0.5514 0.3319 0.0975  -0.0465 -0.1572 179 HIS C CA  
8855  C C   . HIS C 179 ? 0.3622 0.5729 0.3705 0.0980  -0.0504 -0.1622 179 HIS C C   
8856  O O   . HIS C 179 ? 0.3188 0.5205 0.3279 0.0948  -0.0507 -0.1599 179 HIS C O   
8857  C CB  . HIS C 179 ? 0.3254 0.5423 0.3263 0.0928  -0.0434 -0.1496 179 HIS C CB  
8858  C CG  . HIS C 179 ? 0.2964 0.5228 0.2916 0.0912  -0.0395 -0.1437 179 HIS C CG  
8859  N ND1 . HIS C 179 ? 0.3282 0.5538 0.3193 0.0872  -0.0367 -0.1373 179 HIS C ND1 
8860  C CD2 . HIS C 179 ? 0.3279 0.5651 0.3211 0.0932  -0.0379 -0.1434 179 HIS C CD2 
8861  C CE1 . HIS C 179 ? 0.3302 0.5654 0.3172 0.0866  -0.0336 -0.1331 179 HIS C CE1 
8862  N NE2 . HIS C 179 ? 0.3865 0.6291 0.3748 0.0902  -0.0342 -0.1367 179 HIS C NE2 
8863  N N   . GLY C 180 ? 0.3424 0.5536 0.3551 0.1019  -0.0533 -0.1688 180 GLY C N   
8864  C CA  . GLY C 180 ? 0.3075 0.5076 0.3267 0.1019  -0.0569 -0.1729 180 GLY C CA  
8865  C C   . GLY C 180 ? 0.3684 0.5571 0.3900 0.0979  -0.0562 -0.1682 180 GLY C C   
8866  O O   . GLY C 180 ? 0.3532 0.5382 0.3715 0.0932  -0.0529 -0.1601 180 GLY C O   
8867  N N   . ALA C 181 ? 0.3439 0.5269 0.3713 0.0998  -0.0593 -0.1733 181 ALA C N   
8868  C CA  . ALA C 181 ? 0.3274 0.4994 0.3574 0.0965  -0.0590 -0.1692 181 ALA C CA  
8869  C C   . ALA C 181 ? 0.3503 0.5101 0.3810 0.0910  -0.0583 -0.1631 181 ALA C C   
8870  O O   . ALA C 181 ? 0.3574 0.5092 0.3882 0.0873  -0.0568 -0.1571 181 ALA C O   
8871  C CB  . ALA C 181 ? 0.4066 0.5745 0.4430 0.0997  -0.0627 -0.1761 181 ALA C CB  
8872  N N   . ASP C 182 ? 0.4142 0.5726 0.4452 0.0907  -0.0593 -0.1644 182 ASP C N   
8873  C CA  . ASP C 182 ? 0.3959 0.5432 0.4270 0.0856  -0.0584 -0.1585 182 ASP C CA  
8874  C C   . ASP C 182 ? 0.3226 0.4699 0.3472 0.0812  -0.0540 -0.1493 182 ASP C C   
8875  O O   . ASP C 182 ? 0.3359 0.4726 0.3601 0.0765  -0.0527 -0.1430 182 ASP C O   
8876  C CB  . ASP C 182 ? 0.4337 0.5811 0.4660 0.0865  -0.0603 -0.1621 182 ASP C CB  
8877  C CG  . ASP C 182 ? 0.4942 0.6361 0.5343 0.0887  -0.0647 -0.1691 182 ASP C CG  
8878  O OD1 . ASP C 182 ? 0.5300 0.6657 0.5745 0.0887  -0.0662 -0.1701 182 ASP C OD1 
8879  O OD2 . ASP C 182 ? 0.5592 0.7032 0.6011 0.0904  -0.0667 -0.1738 182 ASP C OD2 
8880  N N   . ASN C 183 ? 0.2954 0.4543 0.3148 0.0825  -0.0515 -0.1484 183 ASN C N   
8881  C CA  . ASN C 183 ? 0.3264 0.4865 0.3398 0.0783  -0.0471 -0.1400 183 ASN C CA  
8882  C C   . ASN C 183 ? 0.3347 0.4957 0.3471 0.0769  -0.0450 -0.1359 183 ASN C C   
8883  O O   . ASN C 183 ? 0.3125 0.4724 0.3207 0.0727  -0.0415 -0.1284 183 ASN C O   
8884  C CB  . ASN C 183 ? 0.2790 0.4515 0.2873 0.0800  -0.0454 -0.1405 183 ASN C CB  
8885  C CG  . ASN C 183 ? 0.2875 0.4582 0.2950 0.0797  -0.0463 -0.1415 183 ASN C CG  
8886  O OD1 . ASN C 183 ? 0.3321 0.4919 0.3401 0.0758  -0.0461 -0.1377 183 ASN C OD1 
8887  N ND2 . ASN C 183 ? 0.3725 0.5542 0.3787 0.0840  -0.0472 -0.1466 183 ASN C ND2 
8888  N N   . ILE C 184 ? 0.2568 0.4199 0.2728 0.0804  -0.0470 -0.1407 184 ILE C N   
8889  C CA  . ILE C 184 ? 0.3074 0.4724 0.3226 0.0796  -0.0452 -0.1375 184 ILE C CA  
8890  C C   . ILE C 184 ? 0.2469 0.3980 0.2652 0.0760  -0.0456 -0.1334 184 ILE C C   
8891  O O   . ILE C 184 ? 0.2798 0.4243 0.3035 0.0777  -0.0489 -0.1376 184 ILE C O   
8892  C CB  . ILE C 184 ? 0.2436 0.4177 0.2608 0.0851  -0.0470 -0.1444 184 ILE C CB  
8893  C CG1 . ILE C 184 ? 0.2774 0.4650 0.2915 0.0889  -0.0468 -0.1484 184 ILE C CG1 
8894  C CG2 . ILE C 184 ? 0.2511 0.4280 0.2673 0.0842  -0.0449 -0.1407 184 ILE C CG2 
8895  C CD1 . ILE C 184 ? 0.3484 0.5453 0.3641 0.0948  -0.0488 -0.1559 184 ILE C CD1 
8896  N N   . VAL C 185 ? 0.2485 0.3948 0.2634 0.0709  -0.0424 -0.1252 185 VAL C N   
8897  C CA  . VAL C 185 ? 0.2922 0.4254 0.3094 0.0674  -0.0426 -0.1207 185 VAL C CA  
8898  C C   . VAL C 185 ? 0.2513 0.3848 0.2715 0.0692  -0.0435 -0.1220 185 VAL C C   
8899  O O   . VAL C 185 ? 0.2670 0.3914 0.2920 0.0695  -0.0461 -0.1234 185 VAL C O   
8900  C CB  . VAL C 185 ? 0.2446 0.3733 0.2569 0.0616  -0.0388 -0.1116 185 VAL C CB  
8901  C CG1 . VAL C 185 ? 0.2457 0.3615 0.2600 0.0583  -0.0390 -0.1068 185 VAL C CG1 
8902  C CG2 . VAL C 185 ? 0.2907 0.4175 0.3002 0.0598  -0.0383 -0.1104 185 VAL C CG2 
8903  N N   . ALA C 186 ? 0.2049 0.3493 0.2225 0.0704  -0.0414 -0.1215 186 ALA C N   
8904  C CA  . ALA C 186 ? 0.2321 0.3780 0.2520 0.0721  -0.0420 -0.1225 186 ALA C CA  
8905  C C   . ALA C 186 ? 0.2641 0.4251 0.2812 0.0749  -0.0403 -0.1244 186 ALA C C   
8906  O O   . ALA C 186 ? 0.2814 0.4507 0.2942 0.0738  -0.0377 -0.1219 186 ALA C O   
8907  C CB  . ALA C 186 ? 0.1799 0.3179 0.1994 0.0677  -0.0400 -0.1150 186 ALA C CB  
8908  N N   . ILE C 187 ? 0.2485 0.4131 0.2681 0.0787  -0.0420 -0.1290 187 ILE C N   
8909  C CA  . ILE C 187 ? 0.2426 0.4205 0.2598 0.0810  -0.0402 -0.1297 187 ILE C CA  
8910  C C   . ILE C 187 ? 0.2514 0.4272 0.2686 0.0783  -0.0384 -0.1241 187 ILE C C   
8911  O O   . ILE C 187 ? 0.2402 0.4068 0.2614 0.0782  -0.0404 -0.1243 187 ILE C O   
8912  C CB  . ILE C 187 ? 0.2763 0.4598 0.2958 0.0872  -0.0431 -0.1384 187 ILE C CB  
8913  C CG1 . ILE C 187 ? 0.2642 0.4515 0.2836 0.0901  -0.0448 -0.1439 187 ILE C CG1 
8914  C CG2 . ILE C 187 ? 0.2263 0.4237 0.2440 0.0899  -0.0415 -0.1390 187 ILE C CG2 
8915  C CD1 . ILE C 187 ? 0.2196 0.4100 0.2419 0.0960  -0.0480 -0.1529 187 ILE C CD1 
8916  N N   . VAL C 188 ? 0.2758 0.4612 0.2894 0.0763  -0.0349 -0.1192 188 VAL C N   
8917  C CA  . VAL C 188 ? 0.2450 0.4323 0.2596 0.0742  -0.0334 -0.1144 188 VAL C CA  
8918  C C   . VAL C 188 ? 0.2375 0.4409 0.2526 0.0786  -0.0336 -0.1179 188 VAL C C   
8919  O O   . VAL C 188 ? 0.2522 0.4671 0.2638 0.0790  -0.0314 -0.1173 188 VAL C O   
8920  C CB  . VAL C 188 ? 0.2493 0.4338 0.2598 0.0675  -0.0292 -0.1050 188 VAL C CB  
8921  C CG1 . VAL C 188 ? 0.2220 0.4102 0.2339 0.0655  -0.0276 -0.1003 188 VAL C CG1 
8922  C CG2 . VAL C 188 ? 0.2185 0.3893 0.2291 0.0642  -0.0297 -0.1026 188 VAL C CG2 
8923  N N   . SER C 189 ? 0.2059 0.4094 0.2248 0.0818  -0.0362 -0.1215 189 SER C N   
8924  C CA  . SER C 189 ? 0.2317 0.4492 0.2507 0.0858  -0.0363 -0.1246 189 SER C CA  
8925  C C   . SER C 189 ? 0.1788 0.4008 0.1974 0.0822  -0.0339 -0.1179 189 SER C C   
8926  O O   . SER C 189 ? 0.2600 0.4743 0.2812 0.0811  -0.0352 -0.1163 189 SER C O   
8927  C CB  . SER C 189 ? 0.2298 0.4440 0.2526 0.0912  -0.0402 -0.1323 189 SER C CB  
8928  O OG  . SER C 189 ? 0.2453 0.4568 0.2688 0.0946  -0.0423 -0.1387 189 SER C OG  
8929  N N   . THR C 190 ? 0.2082 0.4425 0.2235 0.0804  -0.0306 -0.1138 190 THR C N   
8930  C CA  . THR C 190 ? 0.2112 0.4510 0.2262 0.0765  -0.0281 -0.1070 190 THR C CA  
8931  C C   . THR C 190 ? 0.2226 0.4742 0.2380 0.0806  -0.0291 -0.1104 190 THR C C   
8932  O O   . THR C 190 ? 0.2087 0.4719 0.2221 0.0837  -0.0283 -0.1133 190 THR C O   
8933  C CB  . THR C 190 ? 0.1797 0.4250 0.1910 0.0715  -0.0240 -0.1001 190 THR C CB  
8934  O OG1 . THR C 190 ? 0.2115 0.4450 0.2210 0.0683  -0.0231 -0.0980 190 THR C OG1 
8935  C CG2 . THR C 190 ? 0.1953 0.4430 0.2070 0.0661  -0.0215 -0.0922 190 THR C CG2 
8936  N N   . VAL C 191 ? 0.1811 0.4294 0.1987 0.0805  -0.0305 -0.1097 191 VAL C N   
8937  C CA  . VAL C 191 ? 0.1845 0.4409 0.2020 0.0845  -0.0313 -0.1132 191 VAL C CA  
8938  C C   . VAL C 191 ? 0.2047 0.4644 0.2215 0.0804  -0.0298 -0.1066 191 VAL C C   
8939  O O   . VAL C 191 ? 0.1513 0.3982 0.1688 0.0769  -0.0296 -0.1027 191 VAL C O   
8940  C CB  . VAL C 191 ? 0.2334 0.4800 0.2535 0.0897  -0.0350 -0.1206 191 VAL C CB  
8941  C CG1 . VAL C 191 ? 0.2296 0.4752 0.2503 0.0940  -0.0365 -0.1274 191 VAL C CG1 
8942  C CG2 . VAL C 191 ? 0.1749 0.4052 0.1976 0.0871  -0.0370 -0.1186 191 VAL C CG2 
8943  N N   . THR C 192 ? 0.2250 0.4986 0.2395 0.0800  -0.0274 -0.1044 192 THR C N   
8944  C CA  . THR C 192 ? 0.2057 0.4917 0.2181 0.0821  -0.0255 -0.1061 192 THR C CA  
8945  C C   . THR C 192 ? 0.1546 0.4394 0.1660 0.0780  -0.0236 -0.1019 192 THR C C   
8946  O O   . THR C 192 ? 0.1753 0.4504 0.1878 0.0733  -0.0233 -0.0972 192 THR C O   
8947  C CB  . THR C 192 ? 0.1999 0.4999 0.2104 0.0811  -0.0229 -0.1026 192 THR C CB  
8948  O OG1 . THR C 192 ? 0.1693 0.4687 0.1793 0.0740  -0.0211 -0.0939 192 THR C OG1 
8949  C CG2 . THR C 192 ? 0.1951 0.4967 0.2063 0.0856  -0.0238 -0.1068 192 THR C CG2 
8950  N N   . CYS C 193 ? 0.2118 0.5057 0.2208 0.0797  -0.0221 -0.1033 193 CYS C N   
8951  C CA  . CYS C 193 ? 0.1618 0.4535 0.1687 0.0760  -0.0200 -0.0995 193 CYS C CA  
8952  C C   . CYS C 193 ? 0.1943 0.4914 0.1996 0.0696  -0.0166 -0.0906 193 CYS C C   
8953  O O   . CYS C 193 ? 0.2375 0.5466 0.2407 0.0700  -0.0148 -0.0895 193 CYS C O   
8954  C CB  . CYS C 193 ? 0.1593 0.4575 0.1637 0.0807  -0.0200 -0.1049 193 CYS C CB  
8955  S SG  . CYS C 193 ? 0.2591 0.5532 0.2600 0.0764  -0.0175 -0.1003 193 CYS C SG  
8956  N N   . ASN C 194 ? 0.2205 0.5078 0.2270 0.0636  -0.0157 -0.0843 194 ASN C N   
8957  C CA  . ASN C 194 ? 0.2333 0.5235 0.2393 0.0570  -0.0131 -0.0758 194 ASN C CA  
8958  C C   . ASN C 194 ? 0.2362 0.5325 0.2383 0.0549  -0.0103 -0.0727 194 ASN C C   
8959  O O   . ASN C 194 ? 0.2482 0.5548 0.2493 0.0534  -0.0087 -0.0696 194 ASN C O   
8960  C CB  . ASN C 194 ? 0.2297 0.5061 0.2376 0.0512  -0.0125 -0.0701 194 ASN C CB  
8961  C CG  . ASN C 194 ? 0.2674 0.5415 0.2743 0.0442  -0.0099 -0.0614 194 ASN C CG  
8962  O OD1 . ASN C 194 ? 0.3046 0.5906 0.3107 0.0438  -0.0091 -0.0598 194 ASN C OD1 
8963  N ND2 . ASN C 194 ? 0.2555 0.5139 0.2626 0.0386  -0.0085 -0.0559 194 ASN C ND2 
8964  N N   . SER C 195 ? 0.2452 0.5349 0.2450 0.0548  -0.0096 -0.0734 195 SER C N   
8965  C CA  . SER C 195 ? 0.2618 0.5574 0.2580 0.0529  -0.0073 -0.0705 195 SER C CA  
8966  C C   . SER C 195 ? 0.2680 0.5770 0.2617 0.0581  -0.0068 -0.0748 195 SER C C   
8967  O O   . SER C 195 ? 0.2879 0.6059 0.2790 0.0571  -0.0049 -0.0723 195 SER C O   
8968  C CB  . SER C 195 ? 0.2450 0.5333 0.2397 0.0525  -0.0076 -0.0713 195 SER C CB  
8969  O OG  . SER C 195 ? 0.3490 0.6240 0.3459 0.0482  -0.0079 -0.0679 195 SER C OG  
8970  N N   . ALA C 196 ? 0.2989 0.6130 0.2941 0.0644  -0.0089 -0.0818 196 ALA C N   
8971  C CA  . ALA C 196 ? 0.2574 0.5854 0.2508 0.0696  -0.0084 -0.0861 196 ALA C CA  
8972  C C   . ALA C 196 ? 0.2617 0.6004 0.2559 0.0690  -0.0072 -0.0836 196 ALA C C   
8973  O O   . ALA C 196 ? 0.2551 0.6056 0.2483 0.0736  -0.0067 -0.0872 196 ALA C O   
8974  C CB  . ALA C 196 ? 0.1906 0.5191 0.1851 0.0772  -0.0114 -0.0956 196 ALA C CB  
8975  N N   . GLY C 197 ? 0.2211 0.5558 0.2172 0.0633  -0.0067 -0.0774 197 GLY C N   
8976  C CA  . GLY C 197 ? 0.2501 0.5936 0.2470 0.0623  -0.0059 -0.0750 197 GLY C CA  
8977  C C   . GLY C 197 ? 0.2789 0.6199 0.2789 0.0641  -0.0084 -0.0776 197 GLY C C   
8978  O O   . GLY C 197 ? 0.2657 0.6149 0.2660 0.0649  -0.0079 -0.0773 197 GLY C O   
8979  N N   . GLY C 198 ? 0.2272 0.5567 0.2292 0.0648  -0.0109 -0.0801 198 GLY C N   
8980  C CA  . GLY C 198 ? 0.2032 0.5293 0.2076 0.0675  -0.0134 -0.0835 198 GLY C CA  
8981  C C   . GLY C 198 ? 0.1757 0.5078 0.1801 0.0755  -0.0148 -0.0921 198 GLY C C   
8982  O O   . GLY C 198 ? 0.1968 0.5311 0.2022 0.0779  -0.0155 -0.0941 198 GLY C O   
8983  N N   . GLN C 199 ? 0.1643 0.4985 0.1677 0.0796  -0.0151 -0.0971 199 GLN C N   
8984  C CA  . GLN C 199 ? 0.2367 0.5775 0.2399 0.0872  -0.0161 -0.1051 199 GLN C CA  
8985  C C   . GLN C 199 ? 0.1968 0.5268 0.2025 0.0917  -0.0198 -0.1122 199 GLN C C   
8986  O O   . GLN C 199 ? 0.2102 0.5288 0.2167 0.0898  -0.0213 -0.1120 199 GLN C O   
8987  C CB  . GLN C 199 ? 0.2105 0.5588 0.2110 0.0891  -0.0146 -0.1065 199 GLN C CB  
8988  C CG  . GLN C 199 ? 0.2656 0.6246 0.2636 0.0852  -0.0109 -0.1000 199 GLN C CG  
8989  C CD  . GLN C 199 ? 0.1885 0.5582 0.1871 0.0870  -0.0097 -0.1000 199 GLN C CD  
8990  O OE1 . GLN C 199 ? 0.1985 0.5735 0.1979 0.0934  -0.0108 -0.1066 199 GLN C OE1 
8991  N NE2 . GLN C 199 ? 0.1874 0.5598 0.1860 0.0812  -0.0076 -0.0926 199 GLN C NE2 
8992  N N   . PRO C 200 ? 0.1832 0.5157 0.1903 0.0976  -0.0212 -0.1184 200 PRO C N   
8993  C CA  . PRO C 200 ? 0.2156 0.5358 0.2255 0.1013  -0.0247 -0.1245 200 PRO C CA  
8994  C C   . PRO C 200 ? 0.2209 0.5371 0.2311 0.1052  -0.0268 -0.1309 200 PRO C C   
8995  O O   . PRO C 200 ? 0.2513 0.5762 0.2592 0.1071  -0.0257 -0.1324 200 PRO C O   
8996  C CB  . PRO C 200 ? 0.1925 0.5177 0.2039 0.1063  -0.0247 -0.1285 200 PRO C CB  
8997  C CG  . PRO C 200 ? 0.1981 0.5399 0.2072 0.1076  -0.0219 -0.1275 200 PRO C CG  
8998  C CD  . PRO C 200 ? 0.1953 0.5408 0.2019 0.1006  -0.0193 -0.1193 200 PRO C CD  
8999  N N   . VAL C 201 ? 0.2690 0.5710 0.2819 0.1062  -0.0299 -0.1344 201 VAL C N   
9000  C CA  . VAL C 201 ? 0.2315 0.5271 0.2457 0.1101  -0.0326 -0.1412 201 VAL C CA  
9001  C C   . VAL C 201 ? 0.2206 0.5128 0.2378 0.1162  -0.0349 -0.1486 201 VAL C C   
9002  O O   . VAL C 201 ? 0.2067 0.4901 0.2264 0.1158  -0.0360 -0.1481 201 VAL C O   
9003  C CB  . VAL C 201 ? 0.2502 0.5310 0.2657 0.1061  -0.0342 -0.1394 201 VAL C CB  
9004  C CG1 . VAL C 201 ? 0.2410 0.5171 0.2570 0.1093  -0.0364 -0.1455 201 VAL C CG1 
9005  C CG2 . VAL C 201 ? 0.2382 0.5202 0.2514 0.0992  -0.0314 -0.1306 201 VAL C CG2 
9006  N N   . SER C 202 ? 0.2349 0.5333 0.2518 0.1219  -0.0357 -0.1551 202 SER C N   
9007  C CA  . SER C 202 ? 0.2504 0.5461 0.2705 0.1279  -0.0377 -0.1620 202 SER C CA  
9008  C C   . SER C 202 ? 0.2602 0.5381 0.2843 0.1281  -0.0411 -0.1653 202 SER C C   
9009  O O   . SER C 202 ? 0.2789 0.5481 0.3031 0.1248  -0.0423 -0.1641 202 SER C O   
9010  C CB  . SER C 202 ? 0.2405 0.5466 0.2595 0.1339  -0.0379 -0.1684 202 SER C CB  
9011  O OG  . SER C 202 ? 0.2654 0.5653 0.2846 0.1348  -0.0402 -0.1724 202 SER C OG  
9012  N N   . MET C 203 ? 0.2344 0.5062 0.2620 0.1319  -0.0424 -0.1691 203 MET C N   
9013  C CA  . MET C 203 ? 0.2433 0.4980 0.2751 0.1324  -0.0456 -0.1724 203 MET C CA  
9014  C C   . MET C 203 ? 0.3046 0.5573 0.3370 0.1350  -0.0479 -0.1786 203 MET C C   
9015  O O   . MET C 203 ? 0.3447 0.5849 0.3790 0.1326  -0.0499 -0.1789 203 MET C O   
9016  C CB  . MET C 203 ? 0.2427 0.4921 0.2785 0.1365  -0.0462 -0.1753 203 MET C CB  
9017  C CG  . MET C 203 ? 0.2467 0.4768 0.2872 0.1361  -0.0490 -0.1771 203 MET C CG  
9018  S SD  . MET C 203 ? 0.3363 0.5531 0.3777 0.1292  -0.0488 -0.1690 203 MET C SD  
9019  C CE  . MET C 203 ? 0.2561 0.4793 0.2976 0.1305  -0.0461 -0.1654 203 MET C CE  
9020  N N   . SER C 204 ? 0.2771 0.5423 0.3078 0.1399  -0.0474 -0.1833 204 SER C N   
9021  C CA  . SER C 204 ? 0.3203 0.5846 0.3513 0.1428  -0.0496 -0.1894 204 SER C CA  
9022  C C   . SER C 204 ? 0.2819 0.5460 0.3102 0.1383  -0.0493 -0.1861 204 SER C C   
9023  O O   . SER C 204 ? 0.3467 0.6020 0.3767 0.1381  -0.0516 -0.1893 204 SER C O   
9024  C CB  . SER C 204 ? 0.2891 0.5680 0.3183 0.1490  -0.0490 -0.1946 204 SER C CB  
9025  O OG  . SER C 204 ? 0.4436 0.7222 0.4757 0.1535  -0.0492 -0.1978 204 SER C OG  
9026  N N   . ASN C 205 ? 0.2804 0.5537 0.3047 0.1346  -0.0463 -0.1796 205 ASN C N   
9027  C CA  . ASN C 205 ? 0.3011 0.5733 0.3230 0.1299  -0.0455 -0.1754 205 ASN C CA  
9028  C C   . ASN C 205 ? 0.3018 0.5572 0.3264 0.1251  -0.0471 -0.1726 205 ASN C C   
9029  O O   . ASN C 205 ? 0.3150 0.5642 0.3398 0.1233  -0.0481 -0.1730 205 ASN C O   
9030  C CB  . ASN C 205 ? 0.3078 0.5920 0.3254 0.1264  -0.0417 -0.1682 205 ASN C CB  
9031  C CG  . ASN C 205 ? 0.2797 0.5657 0.2941 0.1228  -0.0403 -0.1645 205 ASN C CG  
9032  O OD1 . ASN C 205 ? 0.2748 0.5553 0.2884 0.1169  -0.0389 -0.1578 205 ASN C OD1 
9033  N ND2 . ASN C 205 ? 0.2700 0.5632 0.2824 0.1265  -0.0405 -0.1689 205 ASN C ND2 
9034  N N   . LEU C 206 ? 0.2883 0.5363 0.3152 0.1231  -0.0472 -0.1695 206 LEU C N   
9035  C CA  . LEU C 206 ? 0.2923 0.5240 0.3219 0.1188  -0.0487 -0.1667 206 LEU C CA  
9036  C C   . LEU C 206 ? 0.3002 0.5198 0.3341 0.1214  -0.0521 -0.1731 206 LEU C C   
9037  O O   . LEU C 206 ? 0.2799 0.4883 0.3153 0.1181  -0.0534 -0.1719 206 LEU C O   
9038  C CB  . LEU C 206 ? 0.2893 0.5163 0.3203 0.1166  -0.0481 -0.1623 206 LEU C CB  
9039  C CG  . LEU C 206 ? 0.2694 0.5067 0.2969 0.1133  -0.0448 -0.1554 206 LEU C CG  
9040  C CD1 . LEU C 206 ? 0.2383 0.4710 0.2676 0.1130  -0.0447 -0.1533 206 LEU C CD1 
9041  C CD2 . LEU C 206 ? 0.2249 0.4596 0.2504 0.1071  -0.0434 -0.1486 206 LEU C CD2 
9042  N N   . LYS C 207 ? 0.3382 0.5598 0.3742 0.1271  -0.0534 -0.1796 207 LYS C N   
9043  C CA  . LYS C 207 ? 0.3218 0.5326 0.3622 0.1298  -0.0565 -0.1859 207 LYS C CA  
9044  C C   . LYS C 207 ? 0.3050 0.5177 0.3444 0.1303  -0.0576 -0.1894 207 LYS C C   
9045  O O   . LYS C 207 ? 0.2696 0.4705 0.3117 0.1283  -0.0595 -0.1903 207 LYS C O   
9046  C CB  . LYS C 207 ? 0.3816 0.5959 0.4241 0.1361  -0.0571 -0.1919 207 LYS C CB  
9047  C CG  . LYS C 207 ? 0.4168 0.6191 0.4644 0.1389  -0.0600 -0.1981 207 LYS C CG  
9048  C CD  . LYS C 207 ? 0.4318 0.6395 0.4809 0.1456  -0.0602 -0.2039 207 LYS C CD  
9049  C CE  . LYS C 207 ? 0.4862 0.6794 0.5411 0.1476  -0.0626 -0.2083 207 LYS C CE  
9050  N NZ  . LYS C 207 ? 0.5623 0.7468 0.6191 0.1455  -0.0648 -0.2106 207 LYS C NZ  
9051  N N   . GLU C 208 ? 0.3129 0.5407 0.3483 0.1331  -0.0563 -0.1912 208 GLU C N   
9052  C CA  . GLU C 208 ? 0.3046 0.5351 0.3389 0.1341  -0.0573 -0.1948 208 GLU C CA  
9053  C C   . GLU C 208 ? 0.3299 0.5541 0.3627 0.1281  -0.0565 -0.1890 208 GLU C C   
9054  O O   . GLU C 208 ? 0.3438 0.5610 0.3781 0.1275  -0.0583 -0.1916 208 GLU C O   
9055  C CB  . GLU C 208 ? 0.3009 0.5491 0.3307 0.1381  -0.0556 -0.1969 208 GLU C CB  
9056  C CG  . GLU C 208 ? 0.3513 0.6030 0.3799 0.1402  -0.0568 -0.2014 208 GLU C CG  
9057  C CD  . GLU C 208 ? 0.4272 0.6960 0.4520 0.1453  -0.0557 -0.2046 208 GLU C CD  
9058  O OE1 . GLU C 208 ? 0.4477 0.7260 0.4707 0.1468  -0.0536 -0.2029 208 GLU C OE1 
9059  O OE2 . GLU C 208 ? 0.4910 0.7637 0.5145 0.1477  -0.0567 -0.2087 208 GLU C OE2 
9060  N N   . VAL C 209 ? 0.3490 0.5752 0.3790 0.1235  -0.0538 -0.1812 209 VAL C N   
9061  C CA  . VAL C 209 ? 0.2852 0.5051 0.3137 0.1176  -0.0526 -0.1751 209 VAL C CA  
9062  C C   . VAL C 209 ? 0.3129 0.5152 0.3459 0.1147  -0.0550 -0.1749 209 VAL C C   
9063  O O   . VAL C 209 ? 0.3021 0.4975 0.3353 0.1125  -0.0556 -0.1746 209 VAL C O   
9064  C CB  . VAL C 209 ? 0.3102 0.5354 0.3354 0.1132  -0.0492 -0.1666 209 VAL C CB  
9065  C CG1 . VAL C 209 ? 0.2937 0.5083 0.3183 0.1067  -0.0481 -0.1598 209 VAL C CG1 
9066  C CG2 . VAL C 209 ? 0.2721 0.5139 0.2924 0.1147  -0.0464 -0.1656 209 VAL C CG2 
9067  N N   . TYR C 210 ? 0.2931 0.4877 0.3297 0.1148  -0.0561 -0.1747 210 TYR C N   
9068  C CA  . TYR C 210 ? 0.3086 0.4861 0.3494 0.1118  -0.0580 -0.1737 210 TYR C CA  
9069  C C   . TYR C 210 ? 0.3439 0.5156 0.3883 0.1147  -0.0609 -0.1808 210 TYR C C   
9070  O O   . TYR C 210 ? 0.3490 0.5092 0.3956 0.1115  -0.0620 -0.1798 210 TYR C O   
9071  C CB  . TYR C 210 ? 0.3049 0.4758 0.3486 0.1116  -0.0584 -0.1719 210 TYR C CB  
9072  C CG  . TYR C 210 ? 0.3344 0.4876 0.3822 0.1078  -0.0600 -0.1692 210 TYR C CG  
9073  C CD1 . TYR C 210 ? 0.3066 0.4532 0.3531 0.1019  -0.0589 -0.1620 210 TYR C CD1 
9074  C CD2 . TYR C 210 ? 0.3661 0.5091 0.4189 0.1100  -0.0622 -0.1734 210 TYR C CD2 
9075  C CE1 . TYR C 210 ? 0.3454 0.4761 0.3954 0.0984  -0.0602 -0.1591 210 TYR C CE1 
9076  C CE2 . TYR C 210 ? 0.3185 0.4455 0.3750 0.1063  -0.0633 -0.1703 210 TYR C CE2 
9077  C CZ  . TYR C 210 ? 0.3121 0.4332 0.3671 0.1006  -0.0623 -0.1632 210 TYR C CZ  
9078  O OH  . TYR C 210 ? 0.2885 0.3943 0.3470 0.0969  -0.0633 -0.1598 210 TYR C OH  
9079  N N   . GLU C 211 ? 0.3351 0.5146 0.3800 0.1206  -0.0619 -0.1880 211 GLU C N   
9080  C CA  . GLU C 211 ? 0.3328 0.5083 0.3810 0.1236  -0.0646 -0.1952 211 GLU C CA  
9081  C C   . GLU C 211 ? 0.3377 0.5154 0.3834 0.1219  -0.0645 -0.1952 211 GLU C C   
9082  O O   . GLU C 211 ? 0.3473 0.5164 0.3966 0.1210  -0.0668 -0.1977 211 GLU C O   
9083  C CB  . GLU C 211 ? 0.3319 0.5170 0.3803 0.1305  -0.0654 -0.2026 211 GLU C CB  
9084  C CG  . GLU C 211 ? 0.3812 0.5620 0.4328 0.1329  -0.0658 -0.2039 211 GLU C CG  
9085  C CD  . GLU C 211 ? 0.3763 0.5684 0.4273 0.1398  -0.0660 -0.2105 211 GLU C CD  
9086  O OE1 . GLU C 211 ? 0.4535 0.6564 0.5019 0.1428  -0.0662 -0.2145 211 GLU C OE1 
9087  O OE2 . GLU C 211 ? 0.4168 0.6070 0.4700 0.1424  -0.0659 -0.2116 211 GLU C OE2 
9088  N N   . ILE C 212 ? 0.2962 0.4867 0.3365 0.1220  -0.0622 -0.1928 212 ILE C N   
9089  C CA  . ILE C 212 ? 0.3367 0.5309 0.3746 0.1209  -0.0621 -0.1928 212 ILE C CA  
9090  C C   . ILE C 212 ? 0.3560 0.5396 0.3950 0.1151  -0.0620 -0.1872 212 ILE C C   
9091  O O   . ILE C 212 ? 0.3391 0.5196 0.3801 0.1148  -0.0640 -0.1897 212 ILE C O   
9092  C CB  . ILE C 212 ? 0.3374 0.5470 0.3690 0.1219  -0.0590 -0.1904 212 ILE C CB  
9093  C CG1 . ILE C 212 ? 0.3432 0.5648 0.3741 0.1286  -0.0597 -0.1973 212 ILE C CG1 
9094  C CG2 . ILE C 212 ? 0.2890 0.5022 0.3182 0.1202  -0.0587 -0.1890 212 ILE C CG2 
9095  C CD1 . ILE C 212 ? 0.3371 0.5743 0.3626 0.1297  -0.0566 -0.1943 212 ILE C CD1 
9096  N N   . ALA C 213 ? 0.2966 0.4748 0.3344 0.1106  -0.0598 -0.1795 213 ALA C N   
9097  C CA  . ALA C 213 ? 0.3001 0.4682 0.3387 0.1051  -0.0595 -0.1736 213 ALA C CA  
9098  C C   . ALA C 213 ? 0.3452 0.4995 0.3901 0.1044  -0.0628 -0.1763 213 ALA C C   
9099  O O   . ALA C 213 ? 0.3748 0.5224 0.4213 0.1015  -0.0637 -0.1747 213 ALA C O   
9100  C CB  . ALA C 213 ? 0.2844 0.4504 0.3203 0.1007  -0.0564 -0.1650 213 ALA C CB  
9101  N N   . LYS C 214 ? 0.3590 0.5088 0.4078 0.1070  -0.0645 -0.1803 214 LYS C N   
9102  C CA  . LYS C 214 ? 0.3624 0.4989 0.4176 0.1063  -0.0675 -0.1827 214 LYS C CA  
9103  C C   . LYS C 214 ? 0.4103 0.5483 0.4688 0.1095  -0.0705 -0.1906 214 LYS C C   
9104  O O   . LYS C 214 ? 0.4580 0.5867 0.5210 0.1075  -0.0726 -0.1912 214 LYS C O   
9105  C CB  . LYS C 214 ? 0.3371 0.4676 0.3954 0.1081  -0.0680 -0.1840 214 LYS C CB  
9106  C CG  . LYS C 214 ? 0.3836 0.5074 0.4407 0.1038  -0.0659 -0.1758 214 LYS C CG  
9107  C CD  . LYS C 214 ? 0.4774 0.5893 0.5372 0.0987  -0.0668 -0.1710 214 LYS C CD  
9108  C CE  . LYS C 214 ? 0.4275 0.5370 0.4838 0.0938  -0.0642 -0.1617 214 LYS C CE  
9109  N NZ  . LYS C 214 ? 0.3276 0.4432 0.3793 0.0911  -0.0622 -0.1576 214 LYS C NZ  
9110  N N   . GLN C 215 ? 0.3566 0.5066 0.4130 0.1144  -0.0707 -0.1965 215 GLN C N   
9111  C CA  . GLN C 215 ? 0.4025 0.5549 0.4618 0.1175  -0.0736 -0.2041 215 GLN C CA  
9112  C C   . GLN C 215 ? 0.4068 0.5604 0.4645 0.1146  -0.0735 -0.2017 215 GLN C C   
9113  O O   . GLN C 215 ? 0.4730 0.6254 0.5343 0.1160  -0.0762 -0.2070 215 GLN C O   
9114  C CB  . GLN C 215 ? 0.4760 0.6416 0.5330 0.1236  -0.0739 -0.2109 215 GLN C CB  
9115  C CG  . GLN C 215 ? 0.4248 0.6042 0.4755 0.1245  -0.0720 -0.2097 215 GLN C CG  
9116  C CD  . GLN C 215 ? 0.5074 0.7002 0.5553 0.1305  -0.0718 -0.2151 215 GLN C CD  
9117  O OE1 . GLN C 215 ? 0.5324 0.7253 0.5809 0.1330  -0.0715 -0.2168 215 GLN C OE1 
9118  N NE2 . GLN C 215 ? 0.5490 0.7531 0.5937 0.1330  -0.0718 -0.2178 215 GLN C NE2 
9119  N N   . HIS C 216 ? 0.4242 0.5800 0.4769 0.1108  -0.0704 -0.1939 216 HIS C N   
9120  C CA  . HIS C 216 ? 0.3524 0.5078 0.4035 0.1077  -0.0698 -0.1906 216 HIS C CA  
9121  C C   . HIS C 216 ? 0.3574 0.5001 0.4100 0.1018  -0.0690 -0.1833 216 HIS C C   
9122  O O   . HIS C 216 ? 0.3450 0.4864 0.3957 0.0988  -0.0680 -0.1793 216 HIS C O   
9123  C CB  . HIS C 216 ? 0.3675 0.5353 0.4114 0.1077  -0.0666 -0.1871 216 HIS C CB  
9124  C CG  . HIS C 216 ? 0.3607 0.5420 0.4027 0.1134  -0.0673 -0.1939 216 HIS C CG  
9125  N ND1 . HIS C 216 ? 0.4107 0.6000 0.4509 0.1172  -0.0667 -0.1965 216 HIS C ND1 
9126  C CD2 . HIS C 216 ? 0.3340 0.5225 0.3752 0.1161  -0.0685 -0.1985 216 HIS C CD2 
9127  C CE1 . HIS C 216 ? 0.3643 0.5651 0.4028 0.1219  -0.0675 -0.2024 216 HIS C CE1 
9128  N NE2 . HIS C 216 ? 0.3491 0.5496 0.3881 0.1214  -0.0687 -0.2037 216 HIS C NE2 
9129  N N   . GLY C 217 ? 0.3825 0.5158 0.4382 0.1004  -0.0694 -0.1812 217 GLY C N   
9130  C CA  . GLY C 217 ? 0.3546 0.4761 0.4116 0.0950  -0.0688 -0.1740 217 GLY C CA  
9131  C C   . GLY C 217 ? 0.3531 0.4769 0.4042 0.0911  -0.0650 -0.1653 217 GLY C C   
9132  O O   . GLY C 217 ? 0.3117 0.4288 0.3622 0.0869  -0.0641 -0.1597 217 GLY C O   
9133  N N   . ILE C 218 ? 0.3291 0.4621 0.3756 0.0924  -0.0625 -0.1639 218 ILE C N   
9134  C CA  . ILE C 218 ? 0.3692 0.5060 0.4099 0.0890  -0.0587 -0.1561 218 ILE C CA  
9135  C C   . ILE C 218 ? 0.2988 0.4302 0.3395 0.0867  -0.0573 -0.1508 218 ILE C C   
9136  O O   . ILE C 218 ? 0.2783 0.4121 0.3203 0.0895  -0.0579 -0.1537 218 ILE C O   
9137  C CB  . ILE C 218 ? 0.3149 0.4670 0.3504 0.0917  -0.0566 -0.1577 218 ILE C CB  
9138  C CG1 . ILE C 218 ? 0.2904 0.4478 0.3258 0.0942  -0.0581 -0.1631 218 ILE C CG1 
9139  C CG2 . ILE C 218 ? 0.2581 0.4137 0.2880 0.0877  -0.0524 -0.1493 218 ILE C CG2 
9140  C CD1 . ILE C 218 ? 0.3017 0.4744 0.3323 0.0974  -0.0564 -0.1651 218 ILE C CD1 
9141  N N   . PHE C 219 ? 0.2455 0.3698 0.2848 0.0817  -0.0555 -0.1430 219 PHE C N   
9142  C CA  . PHE C 219 ? 0.2418 0.3611 0.2809 0.0792  -0.0542 -0.1373 219 PHE C CA  
9143  C C   . PHE C 219 ? 0.2260 0.3568 0.2606 0.0800  -0.0511 -0.1354 219 PHE C C   
9144  O O   . PHE C 219 ? 0.2594 0.3999 0.2896 0.0799  -0.0488 -0.1344 219 PHE C O   
9145  C CB  . PHE C 219 ? 0.2350 0.3445 0.2732 0.0739  -0.0528 -0.1295 219 PHE C CB  
9146  C CG  . PHE C 219 ? 0.2873 0.3877 0.3276 0.0715  -0.0529 -0.1247 219 PHE C CG  
9147  C CD1 . PHE C 219 ? 0.2634 0.3527 0.3092 0.0715  -0.0561 -0.1261 219 PHE C CD1 
9148  C CD2 . PHE C 219 ? 0.2477 0.3505 0.2843 0.0692  -0.0499 -0.1186 219 PHE C CD2 
9149  C CE1 . PHE C 219 ? 0.2653 0.3464 0.3130 0.0694  -0.0564 -0.1215 219 PHE C CE1 
9150  C CE2 . PHE C 219 ? 0.2775 0.3720 0.3160 0.0673  -0.0502 -0.1143 219 PHE C CE2 
9151  C CZ  . PHE C 219 ? 0.2835 0.3671 0.3274 0.0674  -0.0535 -0.1157 219 PHE C CZ  
9152  N N   . VAL C 220 ? 0.2484 0.3783 0.2841 0.0807  -0.0511 -0.1347 220 VAL C N   
9153  C CA  . VAL C 220 ? 0.2421 0.3852 0.2752 0.0826  -0.0492 -0.1344 220 VAL C CA  
9154  C C   . VAL C 220 ? 0.2545 0.3943 0.2878 0.0795  -0.0479 -0.1278 220 VAL C C   
9155  O O   . VAL C 220 ? 0.2446 0.3752 0.2817 0.0795  -0.0502 -0.1279 220 VAL C O   
9156  C CB  . VAL C 220 ? 0.2429 0.3938 0.2786 0.0888  -0.0515 -0.1424 220 VAL C CB  
9157  C CG1 . VAL C 220 ? 0.2380 0.4035 0.2710 0.0907  -0.0495 -0.1417 220 VAL C CG1 
9158  C CG2 . VAL C 220 ? 0.2299 0.3844 0.2656 0.0922  -0.0528 -0.1491 220 VAL C CG2 
9159  N N   . VAL C 221 ? 0.2715 0.4184 0.3005 0.0766  -0.0442 -0.1221 221 VAL C N   
9160  C CA  . VAL C 221 ? 0.2404 0.3863 0.2691 0.0737  -0.0425 -0.1158 221 VAL C CA  
9161  C C   . VAL C 221 ? 0.2090 0.3708 0.2371 0.0766  -0.0416 -0.1174 221 VAL C C   
9162  O O   . VAL C 221 ? 0.2579 0.4318 0.2829 0.0777  -0.0397 -0.1184 221 VAL C O   
9163  C CB  . VAL C 221 ? 0.2218 0.3630 0.2460 0.0674  -0.0384 -0.1073 221 VAL C CB  
9164  C CG1 . VAL C 221 ? 0.2243 0.3635 0.2486 0.0645  -0.0366 -0.1010 221 VAL C CG1 
9165  C CG2 . VAL C 221 ? 0.2764 0.4031 0.3003 0.0647  -0.0392 -0.1059 221 VAL C CG2 
9166  N N   . MET C 222 ? 0.2365 0.3980 0.2672 0.0778  -0.0431 -0.1175 222 MET C N   
9167  C CA  . MET C 222 ? 0.2485 0.4243 0.2781 0.0799  -0.0421 -0.1179 222 MET C CA  
9168  C C   . MET C 222 ? 0.2252 0.4038 0.2532 0.0751  -0.0386 -0.1095 222 MET C C   
9169  O O   . MET C 222 ? 0.2520 0.4225 0.2819 0.0732  -0.0393 -0.1061 222 MET C O   
9170  C CB  . MET C 222 ? 0.2075 0.3809 0.2400 0.0839  -0.0453 -0.1228 222 MET C CB  
9171  C CG  . MET C 222 ? 0.2191 0.4074 0.2497 0.0868  -0.0441 -0.1243 222 MET C CG  
9172  S SD  . MET C 222 ? 0.3351 0.5339 0.3650 0.0931  -0.0447 -0.1328 222 MET C SD  
9173  C CE  . MET C 222 ? 0.2516 0.4364 0.2864 0.0973  -0.0485 -0.1394 222 MET C CE  
9174  N N   . ASP C 223 ? 0.1970 0.3862 0.2214 0.0728  -0.0348 -0.1058 223 ASP C N   
9175  C CA  . ASP C 223 ? 0.2192 0.4133 0.2422 0.0682  -0.0310 -0.0980 223 ASP C CA  
9176  C C   . ASP C 223 ? 0.2033 0.4042 0.2257 0.0698  -0.0312 -0.0986 223 ASP C C   
9177  O O   . ASP C 223 ? 0.2015 0.4170 0.2233 0.0733  -0.0317 -0.1024 223 ASP C O   
9178  C CB  . ASP C 223 ? 0.2417 0.4437 0.2604 0.0649  -0.0269 -0.0940 223 ASP C CB  
9179  C CG  . ASP C 223 ? 0.2397 0.4434 0.2568 0.0586  -0.0227 -0.0850 223 ASP C CG  
9180  O OD1 . ASP C 223 ? 0.2687 0.4727 0.2854 0.0573  -0.0217 -0.0822 223 ASP C OD1 
9181  O OD2 . ASP C 223 ? 0.2397 0.4385 0.2528 0.0536  -0.0196 -0.0797 223 ASP C OD2 
9182  N N   . SER C 224 ? 0.1903 0.3812 0.2126 0.0674  -0.0307 -0.0948 224 SER C N   
9183  C CA  . SER C 224 ? 0.1703 0.3642 0.1924 0.0701  -0.0323 -0.0972 224 SER C CA  
9184  C C   . SER C 224 ? 0.2217 0.4193 0.2406 0.0655  -0.0283 -0.0897 224 SER C C   
9185  O O   . SER C 224 ? 0.2354 0.4308 0.2533 0.0665  -0.0293 -0.0901 224 SER C O   
9186  C CB  . SER C 224 ? 0.1846 0.3635 0.2094 0.0720  -0.0363 -0.1003 224 SER C CB  
9187  O OG  . SER C 224 ? 0.2364 0.4123 0.2649 0.0761  -0.0405 -0.1074 224 SER C OG  
9188  N N   . ALA C 225 ? 0.1816 0.3845 0.1987 0.0604  -0.0240 -0.0830 225 ALA C N   
9189  C CA  . ALA C 225 ? 0.2129 0.4179 0.2277 0.0554  -0.0205 -0.0754 225 ALA C CA  
9190  C C   . ALA C 225 ? 0.1834 0.4008 0.1965 0.0585  -0.0215 -0.0783 225 ALA C C   
9191  O O   . ALA C 225 ? 0.1940 0.4089 0.2050 0.0568  -0.0208 -0.0752 225 ALA C O   
9192  C CB  . ALA C 225 ? 0.2496 0.4591 0.2630 0.0496  -0.0165 -0.0686 225 ALA C CB  
9193  N N   . ARG C 226 ? 0.1777 0.4089 0.1911 0.0634  -0.0230 -0.0843 226 ARG C N   
9194  C CA  . ARG C 226 ? 0.1658 0.4103 0.1780 0.0668  -0.0234 -0.0871 226 ARG C CA  
9195  C C   . ARG C 226 ? 0.1811 0.4291 0.1954 0.0751  -0.0277 -0.0974 226 ARG C C   
9196  O O   . ARG C 226 ? 0.1756 0.4385 0.1899 0.0795  -0.0285 -0.1019 226 ARG C O   
9197  C CB  . ARG C 226 ? 0.1663 0.4262 0.1770 0.0647  -0.0207 -0.0838 226 ARG C CB  
9198  C CG  . ARG C 226 ? 0.2079 0.4628 0.2173 0.0563  -0.0170 -0.0737 226 ARG C CG  
9199  C CD  . ARG C 226 ? 0.2336 0.5028 0.2418 0.0537  -0.0147 -0.0701 226 ARG C CD  
9200  N NE  . ARG C 226 ? 0.1755 0.4377 0.1831 0.0456  -0.0118 -0.0608 226 ARG C NE  
9201  C CZ  . ARG C 226 ? 0.2471 0.5023 0.2552 0.0419  -0.0105 -0.0576 226 ARG C CZ  
9202  N NH1 . ARG C 226 ? 0.2299 0.4849 0.2388 0.0455  -0.0118 -0.0627 226 ARG C NH1 
9203  N NH2 . ARG C 226 ? 0.1653 0.4130 0.1728 0.0347  -0.0081 -0.0494 226 ARG C NH2 
9204  N N   . PHE C 227 ? 0.1700 0.4042 0.1865 0.0773  -0.0308 -0.1012 227 PHE C N   
9205  C CA  . PHE C 227 ? 0.1956 0.4288 0.2150 0.0845  -0.0345 -0.1103 227 PHE C CA  
9206  C C   . PHE C 227 ? 0.1981 0.4355 0.2182 0.0886  -0.0331 -0.1125 227 PHE C C   
9207  O O   . PHE C 227 ? 0.2035 0.4441 0.2260 0.0943  -0.0338 -0.1187 227 PHE C O   
9208  C CB  . PHE C 227 ? 0.1875 0.4025 0.2100 0.0849  -0.0376 -0.1125 227 PHE C CB  
9209  C CG  . PHE C 227 ? 0.2087 0.4119 0.2314 0.0836  -0.0377 -0.1098 227 PHE C CG  
9210  C CD1 . PHE C 227 ? 0.2204 0.4185 0.2400 0.0776  -0.0355 -0.1022 227 PHE C CD1 
9211  C CD2 . PHE C 227 ? 0.2119 0.4067 0.2387 0.0883  -0.0386 -0.1136 227 PHE C CD2 
9212  C CE1 . PHE C 227 ? 0.2749 0.4623 0.2943 0.0768  -0.0357 -0.1001 227 PHE C CE1 
9213  C CE2 . PHE C 227 ? 0.2520 0.4353 0.2805 0.0873  -0.0381 -0.1101 227 PHE C CE2 
9214  C CZ  . PHE C 227 ? 0.2524 0.4319 0.2775 0.0816  -0.0366 -0.1032 227 PHE C CZ  
9215  N N   . CYS C 228 ? 0.1941 0.4315 0.2129 0.0859  -0.0310 -0.1073 228 CYS C N   
9216  C CA  . CYS C 228 ? 0.2075 0.4489 0.2286 0.0897  -0.0294 -0.1083 228 CYS C CA  
9217  C C   . CYS C 228 ? 0.1874 0.4474 0.2071 0.0912  -0.0271 -0.1088 228 CYS C C   
9218  O O   . CYS C 228 ? 0.2063 0.4716 0.2287 0.0966  -0.0268 -0.1131 228 CYS C O   
9219  C CB  . CYS C 228 ? 0.1663 0.4020 0.1874 0.0861  -0.0274 -0.1018 228 CYS C CB  
9220  S SG  . CYS C 228 ? 0.2586 0.4716 0.2833 0.0857  -0.0297 -0.1011 228 CYS C SG  
9221  N N   . GLU C 229 ? 0.2043 0.4740 0.2199 0.0862  -0.0255 -0.1041 229 GLU C N   
9222  C CA  . GLU C 229 ? 0.2068 0.4935 0.2213 0.0875  -0.0235 -0.1044 229 GLU C CA  
9223  C C   . GLU C 229 ? 0.2053 0.4952 0.2211 0.0930  -0.0251 -0.1118 229 GLU C C   
9224  O O   . GLU C 229 ? 0.2729 0.5738 0.2891 0.0972  -0.0240 -0.1151 229 GLU C O   
9225  C CB  . GLU C 229 ? 0.1911 0.4857 0.2021 0.0806  -0.0216 -0.0971 229 GLU C CB  
9226  C CG  . GLU C 229 ? 0.2366 0.5298 0.2458 0.0752  -0.0197 -0.0897 229 GLU C CG  
9227  C CD  . GLU C 229 ? 0.2184 0.5133 0.2251 0.0671  -0.0178 -0.0813 229 GLU C CD  
9228  O OE1 . GLU C 229 ? 0.2435 0.5422 0.2503 0.0657  -0.0173 -0.0805 229 GLU C OE1 
9229  O OE2 . GLU C 229 ? 0.2146 0.5037 0.2200 0.0619  -0.0157 -0.0746 229 GLU C OE2 
9230  N N   . ASN C 230 ? 0.2146 0.4945 0.2310 0.0932  -0.0277 -0.1145 230 ASN C N   
9231  C CA  . ASN C 230 ? 0.1812 0.4621 0.1989 0.0985  -0.0294 -0.1218 230 ASN C CA  
9232  C C   . ASN C 230 ? 0.2171 0.4933 0.2384 0.1050  -0.0308 -0.1283 230 ASN C C   
9233  O O   . ASN C 230 ? 0.2556 0.5394 0.2776 0.1103  -0.0309 -0.1337 230 ASN C O   
9234  C CB  . ASN C 230 ? 0.1781 0.4484 0.1964 0.0968  -0.0317 -0.1228 230 ASN C CB  
9235  C CG  . ASN C 230 ? 0.2646 0.5402 0.2826 0.1002  -0.0323 -0.1279 230 ASN C CG  
9236  O OD1 . ASN C 230 ? 0.2392 0.5247 0.2547 0.0982  -0.0303 -0.1251 230 ASN C OD1 
9237  N ND2 . ASN C 230 ? 0.2213 0.4899 0.2420 0.1055  -0.0349 -0.1352 230 ASN C ND2 
9238  N N   . ALA C 231 ? 0.2228 0.4864 0.2467 0.1048  -0.0318 -0.1275 231 ALA C N   
9239  C CA  . ALA C 231 ? 0.2194 0.4776 0.2477 0.1108  -0.0329 -0.1326 231 ALA C CA  
9240  C C   . ALA C 231 ? 0.2217 0.4933 0.2504 0.1139  -0.0304 -0.1325 231 ALA C C   
9241  O O   . ALA C 231 ? 0.2755 0.5495 0.3069 0.1199  -0.0310 -0.1382 231 ALA C O   
9242  C CB  . ALA C 231 ? 0.2269 0.4682 0.2584 0.1094  -0.0342 -0.1304 231 ALA C CB  
9243  N N   . TYR C 232 ? 0.2197 0.5002 0.2461 0.1097  -0.0275 -0.1261 232 TYR C N   
9244  C CA  . TYR C 232 ? 0.2032 0.4973 0.2302 0.1122  -0.0250 -0.1258 232 TYR C CA  
9245  C C   . TYR C 232 ? 0.2558 0.5637 0.2810 0.1156  -0.0245 -0.1301 232 TYR C C   
9246  O O   . TYR C 232 ? 0.2256 0.5402 0.2529 0.1213  -0.0242 -0.1344 232 TYR C O   
9247  C CB  . TYR C 232 ? 0.1800 0.4806 0.2048 0.1062  -0.0220 -0.1177 232 TYR C CB  
9248  C CG  . TYR C 232 ? 0.2458 0.5614 0.2715 0.1082  -0.0193 -0.1168 232 TYR C CG  
9249  C CD1 . TYR C 232 ? 0.2464 0.5774 0.2692 0.1079  -0.0176 -0.1168 232 TYR C CD1 
9250  C CD2 . TYR C 232 ? 0.2314 0.5457 0.2612 0.1103  -0.0185 -0.1159 232 TYR C CD2 
9251  C CE1 . TYR C 232 ? 0.2215 0.5662 0.2454 0.1096  -0.0152 -0.1160 232 TYR C CE1 
9252  C CE2 . TYR C 232 ? 0.1972 0.5256 0.2282 0.1121  -0.0162 -0.1153 232 TYR C CE2 
9253  C CZ  . TYR C 232 ? 0.2266 0.5700 0.2545 0.1117  -0.0145 -0.1154 232 TYR C CZ  
9254  O OH  . TYR C 232 ? 0.2882 0.6457 0.3174 0.1133  -0.0121 -0.1147 232 TYR C OH  
9255  N N   . PHE C 233 ? 0.2350 0.5473 0.2565 0.1123  -0.0244 -0.1286 233 PHE C N   
9256  C CA  . PHE C 233 ? 0.2486 0.5733 0.2683 0.1154  -0.0238 -0.1322 233 PHE C CA  
9257  C C   . PHE C 233 ? 0.2783 0.5983 0.3003 0.1222  -0.0265 -0.1408 233 PHE C C   
9258  O O   . PHE C 233 ? 0.2480 0.5785 0.2697 0.1270  -0.0260 -0.1451 233 PHE C O   
9259  C CB  . PHE C 233 ? 0.2199 0.5478 0.2358 0.1104  -0.0232 -0.1284 233 PHE C CB  
9260  C CG  . PHE C 233 ? 0.2530 0.5906 0.2664 0.1045  -0.0200 -0.1204 233 PHE C CG  
9261  C CD1 . PHE C 233 ? 0.2117 0.5634 0.2249 0.1059  -0.0173 -0.1193 233 PHE C CD1 
9262  C CD2 . PHE C 233 ? 0.2164 0.5490 0.2281 0.0975  -0.0197 -0.1139 233 PHE C CD2 
9263  C CE1 . PHE C 233 ? 0.2728 0.6326 0.2841 0.1000  -0.0145 -0.1118 233 PHE C CE1 
9264  C CE2 . PHE C 233 ? 0.1904 0.5309 0.2001 0.0918  -0.0169 -0.1063 233 PHE C CE2 
9265  C CZ  . PHE C 233 ? 0.2203 0.5741 0.2298 0.0929  -0.0143 -0.1053 233 PHE C CZ  
9266  N N   . ILE C 234 ? 0.2461 0.5501 0.2703 0.1226  -0.0294 -0.1434 234 ILE C N   
9267  C CA  . ILE C 234 ? 0.2740 0.5723 0.3010 0.1288  -0.0321 -0.1515 234 ILE C CA  
9268  C C   . ILE C 234 ? 0.2642 0.5650 0.2945 0.1344  -0.0316 -0.1546 234 ILE C C   
9269  O O   . ILE C 234 ? 0.2391 0.5463 0.2701 0.1402  -0.0321 -0.1605 234 ILE C O   
9270  C CB  . ILE C 234 ? 0.2438 0.5236 0.2730 0.1274  -0.0352 -0.1529 234 ILE C CB  
9271  C CG1 . ILE C 234 ? 0.2482 0.5272 0.2746 0.1240  -0.0361 -0.1523 234 ILE C CG1 
9272  C CG2 . ILE C 234 ? 0.2805 0.5520 0.3139 0.1336  -0.0377 -0.1603 234 ILE C CG2 
9273  C CD1 . ILE C 234 ? 0.2486 0.5099 0.2774 0.1220  -0.0390 -0.1531 234 ILE C CD1 
9274  N N   . LYS C 235 ? 0.2398 0.5364 0.2723 0.1329  -0.0306 -0.1505 235 LYS C N   
9275  C CA  . LYS C 235 ? 0.2757 0.5747 0.3119 0.1381  -0.0300 -0.1527 235 LYS C CA  
9276  C C   . LYS C 235 ? 0.3038 0.6219 0.3382 0.1403  -0.0273 -0.1528 235 LYS C C   
9277  O O   . LYS C 235 ? 0.2900 0.6130 0.3267 0.1464  -0.0274 -0.1575 235 LYS C O   
9278  C CB  . LYS C 235 ? 0.2523 0.5423 0.2915 0.1357  -0.0293 -0.1476 235 LYS C CB  
9279  C CG  . LYS C 235 ? 0.3069 0.5988 0.3504 0.1410  -0.0287 -0.1494 235 LYS C CG  
9280  C CD  . LYS C 235 ? 0.2590 0.5410 0.3060 0.1390  -0.0283 -0.1442 235 LYS C CD  
9281  C CE  . LYS C 235 ? 0.2872 0.5734 0.3386 0.1445  -0.0275 -0.1457 235 LYS C CE  
9282  N NZ  . LYS C 235 ? 0.3543 0.6266 0.4103 0.1442  -0.0281 -0.1424 235 LYS C NZ  
9283  N N   . ALA C 236 ? 0.2825 0.6113 0.3130 0.1353  -0.0249 -0.1474 236 ALA C N   
9284  C CA  . ALA C 236 ? 0.2557 0.6026 0.2848 0.1369  -0.0221 -0.1469 236 ALA C CA  
9285  C C   . ALA C 236 ? 0.3468 0.7015 0.3742 0.1419  -0.0229 -0.1532 236 ALA C C   
9286  O O   . ALA C 236 ? 0.3973 0.7626 0.4257 0.1470  -0.0220 -0.1565 236 ALA C O   
9287  C CB  . ALA C 236 ? 0.2244 0.5797 0.2500 0.1299  -0.0193 -0.1390 236 ALA C CB  
9288  N N   . ARG C 237 ? 0.2890 0.6389 0.3142 0.1407  -0.0247 -0.1550 237 ARG C N   
9289  C CA  . ARG C 237 ? 0.2508 0.6099 0.2736 0.1442  -0.0250 -0.1596 237 ARG C CA  
9290  C C   . ARG C 237 ? 0.3068 0.6570 0.3314 0.1496  -0.0284 -0.1677 237 ARG C C   
9291  O O   . ARG C 237 ? 0.3917 0.7498 0.4147 0.1534  -0.0288 -0.1723 237 ARG C O   
9292  C CB  . ARG C 237 ? 0.2919 0.6551 0.3104 0.1386  -0.0238 -0.1550 237 ARG C CB  
9293  C CG  . ARG C 237 ? 0.3111 0.6829 0.3277 0.1328  -0.0204 -0.1467 237 ARG C CG  
9294  C CD  . ARG C 237 ? 0.2592 0.6337 0.2720 0.1271  -0.0193 -0.1417 237 ARG C CD  
9295  N NE  . ARG C 237 ? 0.2911 0.6733 0.3027 0.1214  -0.0160 -0.1336 237 ARG C NE  
9296  C CZ  . ARG C 237 ? 0.2769 0.6607 0.2856 0.1152  -0.0145 -0.1273 237 ARG C CZ  
9297  N NH1 . ARG C 237 ? 0.2430 0.6215 0.2499 0.1139  -0.0157 -0.1279 237 ARG C NH1 
9298  N NH2 . ARG C 237 ? 0.2636 0.6542 0.2717 0.1101  -0.0116 -0.1202 237 ARG C NH2 
9299  N N   . ASP C 238 ? 0.3119 0.6461 0.3400 0.1499  -0.0309 -0.1695 238 ASP C N   
9300  C CA  . ASP C 238 ? 0.3401 0.6652 0.3705 0.1547  -0.0342 -0.1771 238 ASP C CA  
9301  C C   . ASP C 238 ? 0.3544 0.6765 0.3891 0.1605  -0.0348 -0.1811 238 ASP C C   
9302  O O   . ASP C 238 ? 0.3267 0.6388 0.3646 0.1592  -0.0349 -0.1785 238 ASP C O   
9303  C CB  . ASP C 238 ? 0.3051 0.6130 0.3366 0.1509  -0.0367 -0.1765 238 ASP C CB  
9304  C CG  . ASP C 238 ? 0.3714 0.6706 0.4051 0.1551  -0.0400 -0.1842 238 ASP C CG  
9305  O OD1 . ASP C 238 ? 0.4143 0.7173 0.4497 0.1613  -0.0407 -0.1900 238 ASP C OD1 
9306  O OD2 . ASP C 238 ? 0.3765 0.6647 0.4104 0.1520  -0.0420 -0.1842 238 ASP C OD2 
9307  N N   . PRO C 239 ? 0.3074 0.6376 0.3423 0.1669  -0.0352 -0.1873 239 PRO C N   
9308  C CA  . PRO C 239 ? 0.3973 0.7248 0.4364 0.1728  -0.0357 -0.1911 239 PRO C CA  
9309  C C   . PRO C 239 ? 0.3480 0.6560 0.3917 0.1733  -0.0385 -0.1933 239 PRO C C   
9310  O O   . PRO C 239 ? 0.4303 0.7329 0.4779 0.1759  -0.0383 -0.1932 239 PRO C O   
9311  C CB  . PRO C 239 ? 0.3821 0.7205 0.4201 0.1793  -0.0362 -0.1980 239 PRO C CB  
9312  C CG  . PRO C 239 ? 0.4232 0.7747 0.4560 0.1765  -0.0346 -0.1957 239 PRO C CG  
9313  C CD  . PRO C 239 ? 0.3057 0.6482 0.3370 0.1693  -0.0350 -0.1907 239 PRO C CD  
9314  N N   . LYS C 240 ? 0.3574 0.6546 0.4008 0.1710  -0.0408 -0.1949 240 LYS C N   
9315  C CA  . LYS C 240 ? 0.3506 0.6288 0.3986 0.1709  -0.0434 -0.1966 240 LYS C CA  
9316  C C   . LYS C 240 ? 0.3741 0.6428 0.4243 0.1669  -0.0424 -0.1900 240 LYS C C   
9317  O O   . LYS C 240 ? 0.4047 0.6601 0.4595 0.1685  -0.0435 -0.1907 240 LYS C O   
9318  C CB  . LYS C 240 ? 0.3433 0.6133 0.3901 0.1680  -0.0458 -0.1985 240 LYS C CB  
9319  C CG  . LYS C 240 ? 0.4096 0.6594 0.4605 0.1655  -0.0480 -0.1980 240 LYS C CG  
9320  C CD  . LYS C 240 ? 0.5337 0.7746 0.5894 0.1711  -0.0499 -0.2041 240 LYS C CD  
9321  C CE  . LYS C 240 ? 0.5396 0.7614 0.5987 0.1684  -0.0524 -0.2046 240 LYS C CE  
9322  N NZ  . LYS C 240 ? 0.4594 0.6810 0.5159 0.1649  -0.0538 -0.2055 240 LYS C NZ  
9323  N N   . TYR C 241 ? 0.4032 0.6783 0.4503 0.1618  -0.0401 -0.1833 241 TYR C N   
9324  C CA  . TYR C 241 ? 0.3473 0.6143 0.3962 0.1575  -0.0391 -0.1767 241 TYR C CA  
9325  C C   . TYR C 241 ? 0.3728 0.6514 0.4218 0.1583  -0.0361 -0.1728 241 TYR C C   
9326  O O   . TYR C 241 ? 0.3591 0.6358 0.4081 0.1538  -0.0346 -0.1663 241 TYR C O   
9327  C CB  . TYR C 241 ? 0.3686 0.6318 0.4143 0.1503  -0.0391 -0.1716 241 TYR C CB  
9328  C CG  . TYR C 241 ? 0.3135 0.5625 0.3603 0.1491  -0.0422 -0.1745 241 TYR C CG  
9329  C CD1 . TYR C 241 ? 0.3414 0.5725 0.3921 0.1474  -0.0437 -0.1730 241 TYR C CD1 
9330  C CD2 . TYR C 241 ? 0.2961 0.5495 0.3405 0.1497  -0.0434 -0.1788 241 TYR C CD2 
9331  C CE1 . TYR C 241 ? 0.3446 0.5627 0.3967 0.1461  -0.0464 -0.1755 241 TYR C CE1 
9332  C CE2 . TYR C 241 ? 0.3063 0.5469 0.3522 0.1486  -0.0462 -0.1815 241 TYR C CE2 
9333  C CZ  . TYR C 241 ? 0.3218 0.5449 0.3717 0.1466  -0.0477 -0.1798 241 TYR C CZ  
9334  O OH  . TYR C 241 ? 0.3637 0.5739 0.4153 0.1450  -0.0503 -0.1821 241 TYR C OH  
9335  N N   . LYS C 242 ? 0.3894 0.6797 0.4387 0.1640  -0.0353 -0.1769 242 LYS C N   
9336  C CA  . LYS C 242 ? 0.3649 0.6680 0.4144 0.1649  -0.0324 -0.1735 242 LYS C CA  
9337  C C   . LYS C 242 ? 0.3397 0.6331 0.3937 0.1646  -0.0321 -0.1697 242 LYS C C   
9338  O O   . LYS C 242 ? 0.3574 0.6569 0.4112 0.1616  -0.0297 -0.1638 242 LYS C O   
9339  C CB  . LYS C 242 ? 0.3789 0.6945 0.4285 0.1718  -0.0321 -0.1793 242 LYS C CB  
9340  C CG  . LYS C 242 ? 0.4268 0.7558 0.4772 0.1735  -0.0293 -0.1767 242 LYS C CG  
9341  C CD  . LYS C 242 ? 0.4458 0.7856 0.4966 0.1809  -0.0293 -0.1831 242 LYS C CD  
9342  C CE  . LYS C 242 ? 0.5575 0.9101 0.6098 0.1828  -0.0267 -0.1805 242 LYS C CE  
9343  N NZ  . LYS C 242 ? 0.5411 0.8837 0.5980 0.1825  -0.0266 -0.1770 242 LYS C NZ  
9344  N N   . ASN C 243 ? 0.3108 0.5891 0.3690 0.1676  -0.0342 -0.1725 243 ASN C N   
9345  C CA  . ASN C 243 ? 0.3566 0.6252 0.4194 0.1680  -0.0340 -0.1689 243 ASN C CA  
9346  C C   . ASN C 243 ? 0.3639 0.6138 0.4283 0.1635  -0.0355 -0.1655 243 ASN C C   
9347  O O   . ASN C 243 ? 0.4031 0.6411 0.4718 0.1646  -0.0359 -0.1636 243 ASN C O   
9348  C CB  . ASN C 243 ? 0.5228 0.7893 0.5897 0.1755  -0.0348 -0.1741 243 ASN C CB  
9349  C CG  . ASN C 243 ? 0.4913 0.7747 0.5583 0.1794  -0.0326 -0.1745 243 ASN C CG  
9350  O OD1 . ASN C 243 ? 0.5673 0.8599 0.6335 0.1846  -0.0328 -0.1802 243 ASN C OD1 
9351  N ND2 . ASN C 243 ? 0.5555 0.8429 0.6235 0.1769  -0.0305 -0.1682 243 ASN C ND2 
9352  N N   . ALA C 244 ? 0.3400 0.5872 0.4009 0.1584  -0.0362 -0.1644 244 ALA C N   
9353  C CA  . ALA C 244 ? 0.3317 0.5624 0.3936 0.1535  -0.0375 -0.1606 244 ALA C CA  
9354  C C   . ALA C 244 ? 0.3284 0.5609 0.3889 0.1479  -0.0355 -0.1525 244 ALA C C   
9355  O O   . ALA C 244 ? 0.3258 0.5731 0.3831 0.1461  -0.0333 -0.1501 244 ALA C O   
9356  C CB  . ALA C 244 ? 0.2903 0.5172 0.3492 0.1508  -0.0395 -0.1634 244 ALA C CB  
9357  N N   . THR C 245 ? 0.3004 0.5176 0.3636 0.1451  -0.0362 -0.1481 245 THR C N   
9358  C CA  . THR C 245 ? 0.2970 0.5141 0.3588 0.1392  -0.0347 -0.1404 245 THR C CA  
9359  C C   . THR C 245 ? 0.2737 0.4919 0.3304 0.1335  -0.0350 -0.1391 245 THR C C   
9360  O O   . THR C 245 ? 0.3238 0.5386 0.3791 0.1339  -0.0370 -0.1436 245 THR C O   
9361  C CB  . THR C 245 ? 0.2909 0.4911 0.3569 0.1379  -0.0354 -0.1359 245 THR C CB  
9362  O OG1 . THR C 245 ? 0.2877 0.4725 0.3540 0.1357  -0.0378 -0.1370 245 THR C OG1 
9363  C CG2 . THR C 245 ? 0.2863 0.4838 0.3574 0.1439  -0.0353 -0.1377 245 THR C CG2 
9364  N N   . ILE C 246 ? 0.2937 0.5171 0.3475 0.1283  -0.0331 -0.1328 246 ILE C N   
9365  C CA  . ILE C 246 ? 0.2533 0.4776 0.3021 0.1226  -0.0332 -0.1307 246 ILE C CA  
9366  C C   . ILE C 246 ? 0.2685 0.4749 0.3184 0.1203  -0.0359 -0.1309 246 ILE C C   
9367  O O   . ILE C 246 ? 0.3098 0.5151 0.3568 0.1185  -0.0373 -0.1332 246 ILE C O   
9368  C CB  . ILE C 246 ? 0.2421 0.4736 0.2881 0.1171  -0.0305 -0.1232 246 ILE C CB  
9369  C CG1 . ILE C 246 ? 0.2333 0.4844 0.2773 0.1184  -0.0278 -0.1234 246 ILE C CG1 
9370  C CG2 . ILE C 246 ? 0.2188 0.4472 0.2601 0.1108  -0.0308 -0.1202 246 ILE C CG2 
9371  C CD1 . ILE C 246 ? 0.2034 0.4655 0.2434 0.1193  -0.0280 -0.1278 246 ILE C CD1 
9372  N N   . LYS C 247 ? 0.2672 0.4592 0.3214 0.1203  -0.0366 -0.1280 247 LYS C N   
9373  C CA  . LYS C 247 ? 0.2679 0.4421 0.3235 0.1180  -0.0391 -0.1277 247 LYS C CA  
9374  C C   . LYS C 247 ? 0.2970 0.4663 0.3545 0.1218  -0.0416 -0.1350 247 LYS C C   
9375  O O   . LYS C 247 ? 0.3240 0.4842 0.3808 0.1192  -0.0436 -0.1362 247 LYS C O   
9376  C CB  . LYS C 247 ? 0.2308 0.3912 0.2909 0.1173  -0.0391 -0.1225 247 LYS C CB  
9377  C CG  . LYS C 247 ? 0.2504 0.4107 0.3088 0.1120  -0.0374 -0.1145 247 LYS C CG  
9378  C CD  . LYS C 247 ? 0.2717 0.4188 0.3349 0.1119  -0.0374 -0.1093 247 LYS C CD  
9379  C CE  . LYS C 247 ? 0.3654 0.5119 0.4272 0.1065  -0.0357 -0.1011 247 LYS C CE  
9380  N NZ  . LYS C 247 ? 0.4173 0.5498 0.4836 0.1060  -0.0359 -0.0956 247 LYS C NZ  
9381  N N   . GLU C 248 ? 0.2926 0.4676 0.3526 0.1279  -0.0414 -0.1399 248 GLU C N   
9382  C CA  . GLU C 248 ? 0.3027 0.4744 0.3641 0.1317  -0.0435 -0.1472 248 GLU C CA  
9383  C C   . GLU C 248 ? 0.2918 0.4739 0.3486 0.1307  -0.0441 -0.1508 248 GLU C C   
9384  O O   . GLU C 248 ? 0.3578 0.5340 0.4151 0.1311  -0.0463 -0.1552 248 GLU C O   
9385  C CB  . GLU C 248 ? 0.2755 0.4523 0.3400 0.1386  -0.0429 -0.1515 248 GLU C CB  
9386  C CG  . GLU C 248 ? 0.3476 0.5115 0.4176 0.1406  -0.0429 -0.1491 248 GLU C CG  
9387  C CD  . GLU C 248 ? 0.4163 0.5875 0.4890 0.1474  -0.0419 -0.1525 248 GLU C CD  
9388  O OE1 . GLU C 248 ? 0.3745 0.5621 0.4447 0.1500  -0.0409 -0.1556 248 GLU C OE1 
9389  O OE2 . GLU C 248 ? 0.4605 0.6210 0.5378 0.1500  -0.0421 -0.1518 248 GLU C OE2 
9390  N N   . VAL C 249 ? 0.2942 0.4920 0.3466 0.1292  -0.0419 -0.1488 249 VAL C N   
9391  C CA  . VAL C 249 ? 0.2840 0.4921 0.3319 0.1279  -0.0421 -0.1512 249 VAL C CA  
9392  C C   . VAL C 249 ? 0.2855 0.4848 0.3313 0.1218  -0.0434 -0.1479 249 VAL C C   
9393  O O   . VAL C 249 ? 0.2671 0.4656 0.3119 0.1213  -0.0451 -0.1512 249 VAL C O   
9394  C CB  . VAL C 249 ? 0.2457 0.4728 0.2896 0.1276  -0.0391 -0.1490 249 VAL C CB  
9395  C CG1 . VAL C 249 ? 0.2110 0.4479 0.2501 0.1254  -0.0390 -0.1498 249 VAL C CG1 
9396  C CG2 . VAL C 249 ? 0.2952 0.5316 0.3412 0.1340  -0.0381 -0.1529 249 VAL C CG2 
9397  N N   . ILE C 250 ? 0.2767 0.4695 0.3223 0.1173  -0.0426 -0.1413 250 ILE C N   
9398  C CA  . ILE C 250 ? 0.2633 0.4468 0.3072 0.1115  -0.0438 -0.1378 250 ILE C CA  
9399  C C   . ILE C 250 ? 0.2931 0.4606 0.3408 0.1121  -0.0469 -0.1411 250 ILE C C   
9400  O O   . ILE C 250 ? 0.2890 0.4538 0.3355 0.1098  -0.0485 -0.1424 250 ILE C O   
9401  C CB  . ILE C 250 ? 0.2258 0.4040 0.2690 0.1071  -0.0424 -0.1303 250 ILE C CB  
9402  C CG1 . ILE C 250 ? 0.2143 0.4088 0.2531 0.1051  -0.0392 -0.1264 250 ILE C CG1 
9403  C CG2 . ILE C 250 ? 0.2239 0.3888 0.2664 0.1018  -0.0442 -0.1270 250 ILE C CG2 
9404  C CD1 . ILE C 250 ? 0.2725 0.4637 0.3115 0.1019  -0.0372 -0.1193 250 ILE C CD1 
9405  N N   . PHE C 251 ? 0.3027 0.4596 0.3553 0.1151  -0.0475 -0.1421 251 PHE C N   
9406  C CA  . PHE C 251 ? 0.2878 0.4287 0.3444 0.1151  -0.0501 -0.1442 251 PHE C CA  
9407  C C   . PHE C 251 ? 0.3137 0.4583 0.3702 0.1175  -0.0517 -0.1511 251 PHE C C   
9408  O O   . PHE C 251 ? 0.3153 0.4502 0.3730 0.1152  -0.0537 -0.1520 251 PHE C O   
9409  C CB  . PHE C 251 ? 0.3301 0.4616 0.3919 0.1185  -0.0498 -0.1441 251 PHE C CB  
9410  C CG  . PHE C 251 ? 0.3474 0.4608 0.4134 0.1173  -0.0517 -0.1439 251 PHE C CG  
9411  C CD1 . PHE C 251 ? 0.3411 0.4413 0.4082 0.1125  -0.0518 -0.1372 251 PHE C CD1 
9412  C CD2 . PHE C 251 ? 0.3583 0.4680 0.4272 0.1207  -0.0532 -0.1502 251 PHE C CD2 
9413  C CE1 . PHE C 251 ? 0.3304 0.4145 0.4012 0.1109  -0.0531 -0.1364 251 PHE C CE1 
9414  C CE2 . PHE C 251 ? 0.3332 0.4265 0.4059 0.1192  -0.0546 -0.1496 251 PHE C CE2 
9415  C CZ  . PHE C 251 ? 0.3340 0.4147 0.4076 0.1142  -0.0543 -0.1425 251 PHE C CZ  
9416  N N   . ASP C 252 ? 0.3273 0.4863 0.3823 0.1222  -0.0508 -0.1558 252 ASP C N   
9417  C CA  . ASP C 252 ? 0.2852 0.4489 0.3398 0.1246  -0.0523 -0.1623 252 ASP C CA  
9418  C C   . ASP C 252 ? 0.3154 0.4855 0.3656 0.1205  -0.0524 -0.1607 252 ASP C C   
9419  O O   . ASP C 252 ? 0.2809 0.4472 0.3316 0.1200  -0.0541 -0.1637 252 ASP C O   
9420  C CB  . ASP C 252 ? 0.3138 0.4913 0.3678 0.1309  -0.0513 -0.1675 252 ASP C CB  
9421  C CG  . ASP C 252 ? 0.3404 0.5101 0.3995 0.1360  -0.0521 -0.1716 252 ASP C CG  
9422  O OD1 . ASP C 252 ? 0.3491 0.5029 0.4121 0.1344  -0.0531 -0.1697 252 ASP C OD1 
9423  O OD2 . ASP C 252 ? 0.4365 0.6160 0.4957 0.1415  -0.0517 -0.1766 252 ASP C OD2 
9424  N N   . MET C 253 ? 0.3207 0.5006 0.3668 0.1175  -0.0502 -0.1556 253 MET C N   
9425  C CA  . MET C 253 ? 0.2918 0.4786 0.3337 0.1136  -0.0497 -0.1533 253 MET C CA  
9426  C C   . MET C 253 ? 0.2808 0.4537 0.3242 0.1093  -0.0517 -0.1514 253 MET C C   
9427  O O   . MET C 253 ? 0.2930 0.4679 0.3353 0.1084  -0.0524 -0.1530 253 MET C O   
9428  C CB  . MET C 253 ? 0.2941 0.4906 0.3320 0.1101  -0.0470 -0.1468 253 MET C CB  
9429  C CG  . MET C 253 ? 0.2247 0.4402 0.2594 0.1126  -0.0445 -0.1476 253 MET C CG  
9430  S SD  . MET C 253 ? 0.2595 0.4841 0.2907 0.1083  -0.0411 -0.1395 253 MET C SD  
9431  C CE  . MET C 253 ? 0.2520 0.4731 0.2805 0.1011  -0.0411 -0.1334 253 MET C CE  
9432  N N   . TYR C 254 ? 0.2480 0.4066 0.2941 0.1068  -0.0526 -0.1479 254 TYR C N   
9433  C CA  . TYR C 254 ? 0.2851 0.4306 0.3323 0.1020  -0.0541 -0.1447 254 TYR C CA  
9434  C C   . TYR C 254 ? 0.3294 0.4629 0.3811 0.1034  -0.0565 -0.1491 254 TYR C C   
9435  O O   . TYR C 254 ? 0.3444 0.4665 0.3976 0.0994  -0.0577 -0.1464 254 TYR C O   
9436  C CB  . TYR C 254 ? 0.2672 0.4038 0.3147 0.0980  -0.0537 -0.1380 254 TYR C CB  
9437  C CG  . TYR C 254 ? 0.2881 0.4365 0.3307 0.0951  -0.0514 -0.1332 254 TYR C CG  
9438  C CD1 . TYR C 254 ? 0.2541 0.4150 0.2944 0.0974  -0.0492 -0.1329 254 TYR C CD1 
9439  C CD2 . TYR C 254 ? 0.3112 0.4594 0.3516 0.0902  -0.0512 -0.1286 254 TYR C CD2 
9440  C CE1 . TYR C 254 ? 0.2469 0.4193 0.2827 0.0943  -0.0468 -0.1282 254 TYR C CE1 
9441  C CE2 . TYR C 254 ? 0.2187 0.3782 0.2550 0.0874  -0.0489 -0.1239 254 TYR C CE2 
9442  C CZ  . TYR C 254 ? 0.2624 0.4341 0.2963 0.0892  -0.0467 -0.1237 254 TYR C CZ  
9443  O OH  . TYR C 254 ? 0.2547 0.4378 0.2846 0.0858  -0.0442 -0.1184 254 TYR C OH  
9444  N N   . LYS C 255 ? 0.3233 0.4597 0.3772 0.1089  -0.0571 -0.1556 255 LYS C N   
9445  C CA  . LYS C 255 ? 0.3103 0.4396 0.3674 0.1105  -0.0591 -0.1608 255 LYS C CA  
9446  C C   . LYS C 255 ? 0.3322 0.4693 0.3867 0.1098  -0.0594 -0.1630 255 LYS C C   
9447  O O   . LYS C 255 ? 0.3268 0.4578 0.3836 0.1102  -0.0611 -0.1667 255 LYS C O   
9448  C CB  . LYS C 255 ? 0.3410 0.4727 0.4008 0.1169  -0.0594 -0.1674 255 LYS C CB  
9449  C CG  . LYS C 255 ? 0.3231 0.4490 0.3857 0.1188  -0.0586 -0.1656 255 LYS C CG  
9450  C CD  . LYS C 255 ? 0.3098 0.4390 0.3749 0.1256  -0.0588 -0.1724 255 LYS C CD  
9451  C CE  . LYS C 255 ? 0.3118 0.4343 0.3803 0.1279  -0.0577 -0.1705 255 LYS C CE  
9452  N NZ  . LYS C 255 ? 0.4771 0.5815 0.5492 0.1241  -0.0583 -0.1658 255 LYS C NZ  
9453  N N   . TYR C 256 ? 0.3216 0.4719 0.3713 0.1087  -0.0576 -0.1606 256 TYR C N   
9454  C CA  . TYR C 256 ? 0.3167 0.4760 0.3635 0.1087  -0.0572 -0.1623 256 TYR C CA  
9455  C C   . TYR C 256 ? 0.3378 0.4965 0.3817 0.1028  -0.0558 -0.1554 256 TYR C C   
9456  O O   . TYR C 256 ? 0.3354 0.5052 0.3753 0.1022  -0.0539 -0.1541 256 TYR C O   
9457  C CB  . TYR C 256 ? 0.3464 0.5231 0.3900 0.1131  -0.0557 -0.1658 256 TYR C CB  
9458  C CG  . TYR C 256 ? 0.3659 0.5431 0.4124 0.1190  -0.0567 -0.1719 256 TYR C CG  
9459  C CD1 . TYR C 256 ? 0.3818 0.5521 0.4318 0.1221  -0.0590 -0.1783 256 TYR C CD1 
9460  C CD2 . TYR C 256 ? 0.2731 0.4573 0.3188 0.1214  -0.0551 -0.1712 256 TYR C CD2 
9461  C CE1 . TYR C 256 ? 0.3629 0.5331 0.4157 0.1275  -0.0597 -0.1837 256 TYR C CE1 
9462  C CE2 . TYR C 256 ? 0.3266 0.5109 0.3751 0.1270  -0.0557 -0.1765 256 TYR C CE2 
9463  C CZ  . TYR C 256 ? 0.3185 0.4956 0.3705 0.1300  -0.0580 -0.1827 256 TYR C CZ  
9464  O OH  . TYR C 256 ? 0.4092 0.5861 0.4642 0.1356  -0.0585 -0.1878 256 TYR C OH  
9465  N N   . ALA C 257 ? 0.3115 0.4567 0.3573 0.0986  -0.0564 -0.1505 257 ALA C N   
9466  C CA  . ALA C 257 ? 0.2811 0.4226 0.3250 0.0930  -0.0552 -0.1440 257 ALA C CA  
9467  C C   . ALA C 257 ? 0.2680 0.3918 0.3156 0.0897  -0.0570 -0.1414 257 ALA C C   
9468  O O   . ALA C 257 ? 0.3174 0.4326 0.3687 0.0912  -0.0587 -0.1433 257 ALA C O   
9469  C CB  . ALA C 257 ? 0.2745 0.4238 0.3150 0.0904  -0.0526 -0.1377 257 ALA C CB  
9470  N N   . ASP C 258 ? 0.2992 0.4173 0.3456 0.0851  -0.0562 -0.1365 258 ASP C N   
9471  C CA  . ASP C 258 ? 0.2905 0.3923 0.3398 0.0814  -0.0574 -0.1329 258 ASP C CA  
9472  C C   . ASP C 258 ? 0.2781 0.3745 0.3264 0.0769  -0.0563 -0.1247 258 ASP C C   
9473  O O   . ASP C 258 ? 0.2800 0.3630 0.3308 0.0740  -0.0574 -0.1212 258 ASP C O   
9474  C CB  . ASP C 258 ? 0.2833 0.3811 0.3317 0.0792  -0.0571 -0.1327 258 ASP C CB  
9475  C CG  . ASP C 258 ? 0.2862 0.3883 0.3361 0.0835  -0.0586 -0.1410 258 ASP C CG  
9476  O OD1 . ASP C 258 ? 0.2929 0.3903 0.3470 0.0863  -0.0608 -0.1457 258 ASP C OD1 
9477  O OD2 . ASP C 258 ? 0.2743 0.3850 0.3213 0.0844  -0.0578 -0.1430 258 ASP C OD2 
9478  N N   . ALA C 259 ? 0.3029 0.4095 0.3475 0.0763  -0.0539 -0.1215 259 ALA C N   
9479  C CA  . ALA C 259 ? 0.2214 0.3244 0.2646 0.0722  -0.0524 -0.1138 259 ALA C CA  
9480  C C   . ALA C 259 ? 0.1837 0.3020 0.2238 0.0733  -0.0499 -0.1127 259 ALA C C   
9481  O O   . ALA C 259 ? 0.2008 0.3316 0.2391 0.0763  -0.0490 -0.1170 259 ALA C O   
9482  C CB  . ALA C 259 ? 0.2106 0.3053 0.2516 0.0673  -0.0503 -0.1077 259 ALA C CB  
9483  N N   . LEU C 260 ? 0.2481 0.3655 0.2876 0.0706  -0.0486 -0.1067 260 LEU C N   
9484  C CA  . LEU C 260 ? 0.2315 0.3632 0.2680 0.0705  -0.0453 -0.1043 260 LEU C CA  
9485  C C   . LEU C 260 ? 0.2300 0.3552 0.2625 0.0644  -0.0403 -0.0949 260 LEU C C   
9486  O O   . LEU C 260 ? 0.2572 0.3677 0.2901 0.0613  -0.0405 -0.0904 260 LEU C O   
9487  C CB  . LEU C 260 ? 0.2180 0.3543 0.2541 0.0729  -0.0464 -0.1064 260 LEU C CB  
9488  C CG  . LEU C 260 ? 0.2379 0.3615 0.2744 0.0711  -0.0476 -0.1032 260 LEU C CG  
9489  C CD1 . LEU C 260 ? 0.2259 0.3483 0.2577 0.0661  -0.0425 -0.0946 260 LEU C CD1 
9490  C CD2 . LEU C 260 ? 0.2442 0.3719 0.2826 0.0762  -0.0512 -0.1099 260 LEU C CD2 
9491  N N   . THR C 261 ? 0.2171 0.3537 0.2458 0.0625  -0.0358 -0.0919 261 THR C N   
9492  C CA  . THR C 261 ? 0.1949 0.3290 0.2195 0.0568  -0.0306 -0.0833 261 THR C CA  
9493  C C   . THR C 261 ? 0.2026 0.3481 0.2253 0.0568  -0.0283 -0.0818 261 THR C C   
9494  O O   . THR C 261 ? 0.1917 0.3520 0.2143 0.0595  -0.0286 -0.0855 261 THR C O   
9495  C CB  . THR C 261 ? 0.2201 0.3552 0.2403 0.0527  -0.0272 -0.0795 261 THR C CB  
9496  O OG1 . THR C 261 ? 0.2278 0.3781 0.2475 0.0554  -0.0271 -0.0836 261 THR C OG1 
9497  C CG2 . THR C 261 ? 0.2456 0.3645 0.2642 0.0507  -0.0287 -0.0792 261 THR C CG2 
9498  N N   . MET C 262 ? 0.1924 0.3315 0.2135 0.0538  -0.0262 -0.0765 262 MET C N   
9499  C CA  . MET C 262 ? 0.2324 0.3814 0.2522 0.0536  -0.0243 -0.0749 262 MET C CA  
9500  C C   . MET C 262 ? 0.2056 0.3524 0.2216 0.0471  -0.0189 -0.0660 262 MET C C   
9501  O O   . MET C 262 ? 0.2208 0.3541 0.2354 0.0442  -0.0182 -0.0621 262 MET C O   
9502  C CB  . MET C 262 ? 0.1955 0.3396 0.2173 0.0572  -0.0281 -0.0783 262 MET C CB  
9503  C CG  . MET C 262 ? 0.2750 0.4289 0.2943 0.0565  -0.0270 -0.0763 262 MET C CG  
9504  S SD  . MET C 262 ? 0.2964 0.4409 0.3121 0.0604  -0.0309 -0.0824 262 MET C SD  
9505  C CE  . MET C 262 ? 0.2769 0.4263 0.2989 0.0678  -0.0370 -0.0928 262 MET C CE  
9506  N N   . SER C 263 ? 0.1868 0.3465 0.2011 0.0446  -0.0159 -0.0627 263 SER C N   
9507  C CA  . SER C 263 ? 0.1960 0.3546 0.2074 0.0385  -0.0118 -0.0546 263 SER C CA  
9508  C C   . SER C 263 ? 0.1863 0.3474 0.1972 0.0410  -0.0119 -0.0558 263 SER C C   
9509  O O   . SER C 263 ? 0.1837 0.3577 0.1961 0.0442  -0.0127 -0.0590 263 SER C O   
9510  C CB  . SER C 263 ? 0.1783 0.3478 0.1887 0.0343  -0.0092 -0.0501 263 SER C CB  
9511  O OG  . SER C 263 ? 0.2187 0.3853 0.2272 0.0283  -0.0062 -0.0422 263 SER C OG  
9512  N N   . ALA C 264 ? 0.2330 0.3821 0.2418 0.0396  -0.0120 -0.0536 264 ALA C N   
9513  C CA  . ALA C 264 ? 0.1969 0.3481 0.2039 0.0417  -0.0129 -0.0548 264 ALA C CA  
9514  C C   . ALA C 264 ? 0.1844 0.3443 0.1889 0.0370  -0.0093 -0.0482 264 ALA C C   
9515  O O   . ALA C 264 ? 0.1772 0.3419 0.1808 0.0388  -0.0101 -0.0487 264 ALA C O   
9516  C CB  . ALA C 264 ? 0.2095 0.3463 0.2171 0.0422  -0.0151 -0.0544 264 ALA C CB  
9517  N N   . LYS C 265 ? 0.1996 0.3614 0.2041 0.0312  -0.0061 -0.0419 265 LYS C N   
9518  C CA  . LYS C 265 ? 0.1402 0.3074 0.1432 0.0261  -0.0032 -0.0353 265 LYS C CA  
9519  C C   . LYS C 265 ? 0.1847 0.3670 0.1865 0.0289  -0.0031 -0.0389 265 LYS C C   
9520  O O   . LYS C 265 ? 0.1617 0.3484 0.1606 0.0251  -0.0016 -0.0343 265 LYS C O   
9521  C CB  . LYS C 265 ? 0.1964 0.3576 0.2007 0.0191  -0.0012 -0.0281 265 LYS C CB  
9522  C CG  . LYS C 265 ? 0.1648 0.3096 0.1680 0.0156  -0.0013 -0.0243 265 LYS C CG  
9523  C CD  . LYS C 265 ? 0.1810 0.3214 0.1847 0.0100  -0.0001 -0.0194 265 LYS C CD  
9524  C CE  . LYS C 265 ? 0.1789 0.3203 0.1831 0.0047  0.0013  -0.0133 265 LYS C CE  
9525  N NZ  . LYS C 265 ? 0.1914 0.3288 0.1962 -0.0001 0.0016  -0.0096 265 LYS C NZ  
9526  N N   . LYS C 266 ? 0.1393 0.3274 0.1399 0.0351  -0.0060 -0.0472 266 LYS C N   
9527  C CA  . LYS C 266 ? 0.1647 0.3708 0.1663 0.0376  -0.0114 -0.0503 266 LYS C CA  
9528  C C   . LYS C 266 ? 0.1481 0.3592 0.1498 0.0441  -0.0124 -0.0566 266 LYS C C   
9529  O O   . LYS C 266 ? 0.1865 0.3975 0.1876 0.0430  -0.0108 -0.0534 266 LYS C O   
9530  C CB  . LYS C 266 ? 0.1856 0.4017 0.1932 0.0411  -0.0130 -0.0548 266 LYS C CB  
9531  C CG  . LYS C 266 ? 0.1709 0.3883 0.1802 0.0359  -0.0100 -0.0493 266 LYS C CG  
9532  C CD  . LYS C 266 ? 0.2323 0.4349 0.2428 0.0331  -0.0082 -0.0468 266 LYS C CD  
9533  C CE  . LYS C 266 ? 0.2595 0.4595 0.2687 0.0266  -0.0057 -0.0402 266 LYS C CE  
9534  N NZ  . LYS C 266 ? 0.3244 0.5287 0.3333 0.0277  -0.0061 -0.0430 266 LYS C NZ  
9535  N N   . ASP C 267 ? 0.2118 0.4277 0.2162 0.0512  -0.0159 -0.0653 267 ASP C N   
9536  C CA  . ASP C 267 ? 0.2166 0.4392 0.2226 0.0579  -0.0181 -0.0717 267 ASP C CA  
9537  C C   . ASP C 267 ? 0.2088 0.4202 0.2153 0.0587  -0.0185 -0.0711 267 ASP C C   
9538  O O   . ASP C 267 ? 0.2459 0.4619 0.2551 0.0611  -0.0182 -0.0709 267 ASP C O   
9539  C CB  . ASP C 267 ? 0.2312 0.4582 0.2400 0.0651  -0.0222 -0.0813 267 ASP C CB  
9540  C CG  . ASP C 267 ? 0.2480 0.4928 0.2569 0.0671  -0.0220 -0.0837 267 ASP C CG  
9541  O OD1 . ASP C 267 ? 0.2373 0.4899 0.2445 0.0622  -0.0189 -0.0775 267 ASP C OD1 
9542  O OD2 . ASP C 267 ? 0.2717 0.5226 0.2827 0.0737  -0.0251 -0.0919 267 ASP C OD2 
9543  N N   . PRO C 268 ? 0.1518 0.3466 0.1585 0.0567  -0.0188 -0.0694 268 PRO C N   
9544  C CA  . PRO C 268 ? 0.1466 0.3295 0.1572 0.0571  -0.0193 -0.0668 268 PRO C CA  
9545  C C   . PRO C 268 ? 0.2063 0.3894 0.2169 0.0514  -0.0158 -0.0573 268 PRO C C   
9546  O O   . PRO C 268 ? 0.2136 0.3847 0.2294 0.0499  -0.0164 -0.0522 268 PRO C O   
9547  C CB  . PRO C 268 ? 0.1965 0.3628 0.2071 0.0559  -0.0208 -0.0672 268 PRO C CB  
9548  C CG  . PRO C 268 ? 0.1617 0.3312 0.1712 0.0578  -0.0225 -0.0730 268 PRO C CG  
9549  C CD  . PRO C 268 ? 0.1793 0.3640 0.1864 0.0552  -0.0195 -0.0701 268 PRO C CD  
9550  N N   . LEU C 269 ? 0.1813 0.3775 0.1859 0.0478  -0.0127 -0.0546 269 LEU C N   
9551  C CA  . LEU C 269 ? 0.1698 0.3692 0.1745 0.0432  -0.0101 -0.0469 269 LEU C CA  
9552  C C   . LEU C 269 ? 0.1327 0.3171 0.1376 0.0367  -0.0083 -0.0385 269 LEU C C   
9553  O O   . LEU C 269 ? 0.1650 0.3433 0.1744 0.0348  -0.0086 -0.0332 269 LEU C O   
9554  C CB  . LEU C 269 ? 0.1820 0.3845 0.1944 0.0475  -0.0115 -0.0479 269 LEU C CB  
9555  C CG  . LEU C 269 ? 0.1403 0.3579 0.1540 0.0534  -0.0125 -0.0548 269 LEU C CG  
9556  C CD1 . LEU C 269 ? 0.1398 0.3544 0.1622 0.0591  -0.0142 -0.0571 269 LEU C CD1 
9557  C CD2 . LEU C 269 ? 0.1773 0.4100 0.1868 0.0500  -0.0101 -0.0516 269 LEU C CD2 
9558  N N   . LEU C 270 ? 0.1540 0.3317 0.1552 0.0330  -0.0065 -0.0367 270 LEU C N   
9559  C CA  . LEU C 270 ? 0.1649 0.3273 0.1668 0.0270  -0.0053 -0.0290 270 LEU C CA  
9560  C C   . LEU C 270 ? 0.1991 0.3589 0.1988 0.0194  -0.0020 -0.0218 270 LEU C C   
9561  O O   . LEU C 270 ? 0.2108 0.3777 0.2097 0.0186  -0.0012 -0.0226 270 LEU C O   
9562  C CB  . LEU C 270 ? 0.1766 0.3241 0.1815 0.0281  -0.0080 -0.0307 270 LEU C CB  
9563  C CG  . LEU C 270 ? 0.1666 0.3077 0.1771 0.0343  -0.0131 -0.0361 270 LEU C CG  
9564  C CD1 . LEU C 270 ? 0.1742 0.3004 0.1856 0.0340  -0.0154 -0.0370 270 LEU C CD1 
9565  C CD2 . LEU C 270 ? 0.1313 0.2660 0.1475 0.0337  -0.0149 -0.0312 270 LEU C CD2 
9566  N N   . ASN C 271 ? 0.1596 0.3068 0.1592 0.0140  -0.0009 -0.0148 271 ASN C N   
9567  C CA  . ASN C 271 ? 0.1515 0.2913 0.1505 0.0072  0.0010  -0.0085 271 ASN C CA  
9568  C C   . ASN C 271 ? 0.1643 0.2952 0.1641 0.0053  0.0011  -0.0079 271 ASN C C   
9569  O O   . ASN C 271 ? 0.1554 0.2815 0.1558 0.0009  0.0022  -0.0045 271 ASN C O   
9570  C CB  . ASN C 271 ? 0.1336 0.2668 0.1321 0.0029  0.0015  -0.0021 271 ASN C CB  
9571  C CG  . ASN C 271 ? 0.1800 0.3233 0.1780 0.0045  0.0012  -0.0023 271 ASN C CG  
9572  O OD1 . ASN C 271 ? 0.1579 0.3020 0.1566 0.0056  0.0006  -0.0010 271 ASN C OD1 
9573  N ND2 . ASN C 271 ? 0.1406 0.2925 0.1374 0.0047  0.0014  -0.0036 271 ASN C ND2 
9574  N N   . ILE C 272 ? 0.1388 0.2674 0.1391 0.0089  -0.0003 -0.0117 272 ILE C N   
9575  C CA  . ILE C 272 ? 0.1829 0.3043 0.1835 0.0078  -0.0005 -0.0120 272 ILE C CA  
9576  C C   . ILE C 272 ? 0.1598 0.2757 0.1615 0.0140  -0.0050 -0.0186 272 ILE C C   
9577  O O   . ILE C 272 ? 0.1958 0.3102 0.1994 0.0176  -0.0081 -0.0209 272 ILE C O   
9578  C CB  . ILE C 272 ? 0.1688 0.2778 0.1690 0.0018  0.0002  -0.0048 272 ILE C CB  
9579  C CG1 . ILE C 272 ? 0.1237 0.2258 0.1239 -0.0003 0.0002  -0.0044 272 ILE C CG1 
9580  C CG2 . ILE C 272 ? 0.1346 0.2343 0.1351 0.0031  -0.0029 -0.0037 272 ILE C CG2 
9581  C CD1 . ILE C 272 ? 0.1399 0.2455 0.1408 -0.0021 0.0010  -0.0047 272 ILE C CD1 
9582  N N   . GLY C 273 ? 0.1599 0.2707 0.1616 0.0148  -0.0063 -0.0214 273 GLY C N   
9583  C CA  . GLY C 273 ? 0.1661 0.2672 0.1694 0.0195  -0.0112 -0.0267 273 GLY C CA  
9584  C C   . GLY C 273 ? 0.1399 0.2479 0.1441 0.0241  -0.0113 -0.0340 273 GLY C C   
9585  O O   . GLY C 273 ? 0.2088 0.3345 0.2138 0.0260  -0.0080 -0.0370 273 GLY C O   
9586  N N   . GLY C 274 ? 0.1845 0.2820 0.1899 0.0269  -0.0149 -0.0380 274 GLY C N   
9587  C CA  . GLY C 274 ? 0.1487 0.2532 0.1566 0.0326  -0.0157 -0.0464 274 GLY C CA  
9588  C C   . GLY C 274 ? 0.1672 0.2602 0.1784 0.0376  -0.0203 -0.0522 274 GLY C C   
9589  O O   . GLY C 274 ? 0.1750 0.2545 0.1862 0.0358  -0.0225 -0.0490 274 GLY C O   
9590  N N   . LEU C 275 ? 0.1783 0.2759 0.1935 0.0430  -0.0223 -0.0596 275 LEU C N   
9591  C CA  . LEU C 275 ? 0.1771 0.2634 0.1964 0.0467  -0.0275 -0.0643 275 LEU C CA  
9592  C C   . LEU C 275 ? 0.1902 0.2792 0.2128 0.0489  -0.0299 -0.0685 275 LEU C C   
9593  O O   . LEU C 275 ? 0.1784 0.2818 0.2010 0.0506  -0.0291 -0.0716 275 LEU C O   
9594  C CB  . LEU C 275 ? 0.1611 0.2508 0.1817 0.0511  -0.0299 -0.0696 275 LEU C CB  
9595  C CG  . LEU C 275 ? 0.1922 0.2690 0.2153 0.0533  -0.0353 -0.0744 275 LEU C CG  
9596  C CD1 . LEU C 275 ? 0.1811 0.2405 0.2039 0.0494  -0.0369 -0.0691 275 LEU C CD1 
9597  C CD2 . LEU C 275 ? 0.1766 0.2642 0.2018 0.0576  -0.0412 -0.0811 275 LEU C CD2 
9598  N N   . VAL C 276 ? 0.1912 0.2666 0.2163 0.0485  -0.0331 -0.0681 276 VAL C N   
9599  C CA  . VAL C 276 ? 0.2230 0.2993 0.2520 0.0511  -0.0369 -0.0732 276 VAL C CA  
9600  C C   . VAL C 276 ? 0.1780 0.2486 0.2121 0.0538  -0.0426 -0.0773 276 VAL C C   
9601  O O   . VAL C 276 ? 0.1983 0.2573 0.2329 0.0515  -0.0438 -0.0733 276 VAL C O   
9602  C CB  . VAL C 276 ? 0.2603 0.3268 0.2882 0.0477  -0.0361 -0.0691 276 VAL C CB  
9603  C CG1 . VAL C 276 ? 0.2267 0.2948 0.2585 0.0505  -0.0398 -0.0749 276 VAL C CG1 
9604  C CG2 . VAL C 276 ? 0.1866 0.2550 0.2061 0.0418  -0.0304 -0.0632 276 VAL C CG2 
9605  N N   . ALA C 277 ? 0.2016 0.2807 0.2390 0.0584  -0.0462 -0.0855 277 ALA C N   
9606  C CA  . ALA C 277 ? 0.2459 0.3198 0.2884 0.0611  -0.0518 -0.0907 277 ALA C CA  
9607  C C   . ALA C 277 ? 0.2481 0.3248 0.2947 0.0640  -0.0547 -0.0970 277 ALA C C   
9608  O O   . ALA C 277 ? 0.2738 0.3615 0.3186 0.0661  -0.0529 -0.1006 277 ALA C O   
9609  C CB  . ALA C 277 ? 0.2287 0.3104 0.2714 0.0650  -0.0535 -0.0959 277 ALA C CB  
9610  N N   . ILE C 278 ? 0.2816 0.3450 0.3310 0.0625  -0.0566 -0.0967 278 ILE C N   
9611  C CA  A ILE C 278 ? 0.2718 0.3324 0.3228 0.0635  -0.0570 -0.1010 278 ILE C CA  
9612  C CA  B ILE C 278 ? 0.2717 0.3325 0.3227 0.0636  -0.0570 -0.1010 278 ILE C CA  
9613  C C   . ILE C 278 ? 0.2962 0.3514 0.3512 0.0663  -0.0590 -0.1060 278 ILE C C   
9614  O O   . ILE C 278 ? 0.2984 0.3435 0.3553 0.0646  -0.0596 -0.1026 278 ILE C O   
9615  C CB  A ILE C 278 ? 0.2925 0.3424 0.3431 0.0588  -0.0561 -0.0952 278 ILE C CB  
9616  C CB  B ILE C 278 ? 0.2923 0.3428 0.3427 0.0589  -0.0560 -0.0953 278 ILE C CB  
9617  C CG1 A ILE C 278 ? 0.2766 0.3307 0.3225 0.0564  -0.0528 -0.0903 278 ILE C CG1 
9618  C CG1 B ILE C 278 ? 0.2761 0.3313 0.3216 0.0565  -0.0525 -0.0903 278 ILE C CG1 
9619  C CG2 A ILE C 278 ? 0.3139 0.3622 0.3680 0.0608  -0.0583 -0.1014 278 ILE C CG2 
9620  C CG2 B ILE C 278 ? 0.3137 0.3629 0.3673 0.0609  -0.0580 -0.1014 278 ILE C CG2 
9621  C CD1 A ILE C 278 ? 0.2658 0.3127 0.3105 0.0525  -0.0516 -0.0817 278 ILE C CD1 
9622  C CD1 B ILE C 278 ? 0.2852 0.3328 0.3306 0.0535  -0.0524 -0.0863 278 ILE C CD1 
9623  N N   . ARG C 279 ? 0.2992 0.3606 0.3551 0.0706  -0.0594 -0.1135 279 ARG C N   
9624  C CA  . ARG C 279 ? 0.2987 0.3561 0.3583 0.0742  -0.0606 -0.1186 279 ARG C CA  
9625  C C   . ARG C 279 ? 0.3548 0.3975 0.4186 0.0718  -0.0616 -0.1165 279 ARG C C   
9626  O O   . ARG C 279 ? 0.3772 0.4120 0.4436 0.0716  -0.0619 -0.1145 279 ARG C O   
9627  C CB  . ARG C 279 ? 0.2831 0.3502 0.3428 0.0791  -0.0609 -0.1269 279 ARG C CB  
9628  C CG  . ARG C 279 ? 0.3520 0.4173 0.4154 0.0838  -0.0616 -0.1327 279 ARG C CG  
9629  C CD  . ARG C 279 ? 0.3553 0.4329 0.4177 0.0886  -0.0619 -0.1403 279 ARG C CD  
9630  N NE  . ARG C 279 ? 0.4083 0.4851 0.4739 0.0937  -0.0625 -0.1464 279 ARG C NE  
9631  C CZ  . ARG C 279 ? 0.4827 0.5701 0.5478 0.0987  -0.0627 -0.1534 279 ARG C CZ  
9632  N NH1 . ARG C 279 ? 0.3873 0.4873 0.4485 0.0991  -0.0623 -0.1550 279 ARG C NH1 
9633  N NH2 . ARG C 279 ? 0.4966 0.5819 0.5651 0.1033  -0.0633 -0.1586 279 ARG C NH2 
9634  N N   . ASP C 280 ? 0.3310 0.3718 0.3969 0.0707  -0.0632 -0.1182 280 ASP C N   
9635  C CA  . ASP C 280 ? 0.3782 0.4079 0.4498 0.0692  -0.0655 -0.1178 280 ASP C CA  
9636  C C   . ASP C 280 ? 0.3543 0.3817 0.4268 0.0661  -0.0665 -0.1159 280 ASP C C   
9637  O O   . ASP C 280 ? 0.3861 0.4048 0.4633 0.0644  -0.0682 -0.1147 280 ASP C O   
9638  C CB  . ASP C 280 ? 0.3915 0.4193 0.4678 0.0737  -0.0668 -0.1255 280 ASP C CB  
9639  C CG  . ASP C 280 ? 0.4126 0.4501 0.4878 0.0776  -0.0670 -0.1330 280 ASP C CG  
9640  O OD1 . ASP C 280 ? 0.4125 0.4541 0.4862 0.0761  -0.0673 -0.1332 280 ASP C OD1 
9641  O OD2 . ASP C 280 ? 0.4705 0.5115 0.5466 0.0822  -0.0669 -0.1388 280 ASP C OD2 
9642  N N   . ASN C 281 ? 0.3078 0.3426 0.3760 0.0654  -0.0653 -0.1153 281 ASN C N   
9643  C CA  . ASN C 281 ? 0.3665 0.3991 0.4353 0.0629  -0.0658 -0.1133 281 ASN C CA  
9644  C C   . ASN C 281 ? 0.3585 0.3840 0.4265 0.0583  -0.0654 -0.1043 281 ASN C C   
9645  O O   . ASN C 281 ? 0.3578 0.3862 0.4210 0.0564  -0.0631 -0.0989 281 ASN C O   
9646  C CB  . ASN C 281 ? 0.3735 0.4161 0.4376 0.0639  -0.0640 -0.1152 281 ASN C CB  
9647  C CG  . ASN C 281 ? 0.3377 0.3783 0.4027 0.0624  -0.0646 -0.1152 281 ASN C CG  
9648  O OD1 . ASN C 281 ? 0.3391 0.3721 0.4052 0.0590  -0.0650 -0.1097 281 ASN C OD1 
9649  N ND2 . ASN C 281 ? 0.3542 0.4021 0.4185 0.0652  -0.0648 -0.1215 281 ASN C ND2 
9650  N N   . GLU C 282 ? 0.3614 0.3778 0.4344 0.0564  -0.0673 -0.1025 282 GLU C N   
9651  C CA  . GLU C 282 ? 0.3677 0.3778 0.4404 0.0522  -0.0672 -0.0939 282 GLU C CA  
9652  C C   . GLU C 282 ? 0.3405 0.3508 0.4105 0.0497  -0.0663 -0.0896 282 GLU C C   
9653  O O   . GLU C 282 ? 0.3245 0.3320 0.3917 0.0467  -0.0653 -0.0818 282 GLU C O   
9654  C CB  . GLU C 282 ? 0.3777 0.3788 0.4565 0.0511  -0.0693 -0.0934 282 GLU C CB  
9655  C CG  . GLU C 282 ? 0.4551 0.4507 0.5334 0.0471  -0.0693 -0.0848 282 GLU C CG  
9656  C CD  . GLU C 282 ? 0.4998 0.4874 0.5842 0.0460  -0.0709 -0.0843 282 GLU C CD  
9657  O OE1 . GLU C 282 ? 0.6113 0.5969 0.7007 0.0478  -0.0721 -0.0900 282 GLU C OE1 
9658  O OE2 . GLU C 282 ? 0.4414 0.4250 0.5258 0.0434  -0.0708 -0.0784 282 GLU C OE2 
9659  N N   . GLU C 283 ? 0.3152 0.3284 0.3856 0.0512  -0.0665 -0.0944 283 GLU C N   
9660  C CA  . GLU C 283 ? 0.3575 0.3708 0.4245 0.0492  -0.0651 -0.0908 283 GLU C CA  
9661  C C   . GLU C 283 ? 0.3284 0.3474 0.3880 0.0488  -0.0616 -0.0875 283 GLU C C   
9662  O O   . GLU C 283 ? 0.3312 0.3472 0.3867 0.0460  -0.0596 -0.0805 283 GLU C O   
9663  C CB  . GLU C 283 ? 0.3779 0.3935 0.4473 0.0511  -0.0662 -0.0975 283 GLU C CB  
9664  C CG  . GLU C 283 ? 0.3901 0.4061 0.4554 0.0493  -0.0646 -0.0944 283 GLU C CG  
9665  C CD  . GLU C 283 ? 0.4827 0.5017 0.5502 0.0512  -0.0659 -0.1015 283 GLU C CD  
9666  O OE1 . GLU C 283 ? 0.5037 0.5261 0.5753 0.0544  -0.0677 -0.1091 283 GLU C OE1 
9667  O OE2 . GLU C 283 ? 0.5280 0.5461 0.5932 0.0497  -0.0650 -0.0994 283 GLU C OE2 
9668  N N   . ILE C 284 ? 0.2844 0.3116 0.3420 0.0517  -0.0605 -0.0926 284 ILE C N   
9669  C CA  . ILE C 284 ? 0.3316 0.3650 0.3824 0.0511  -0.0567 -0.0897 284 ILE C CA  
9670  C C   . ILE C 284 ? 0.2413 0.2711 0.2904 0.0490  -0.0554 -0.0826 284 ILE C C   
9671  O O   . ILE C 284 ? 0.2057 0.2355 0.2493 0.0466  -0.0520 -0.0770 284 ILE C O   
9672  C CB  . ILE C 284 ? 0.3154 0.3598 0.3650 0.0548  -0.0561 -0.0968 284 ILE C CB  
9673  C CG1 . ILE C 284 ? 0.3414 0.3901 0.3911 0.0566  -0.0567 -0.1026 284 ILE C CG1 
9674  C CG2 . ILE C 284 ? 0.3224 0.3739 0.3658 0.0541  -0.0522 -0.0936 284 ILE C CG2 
9675  C CD1 . ILE C 284 ? 0.3908 0.4510 0.4392 0.0604  -0.0564 -0.1095 284 ILE C CD1 
9676  N N   . PHE C 285 ? 0.2712 0.2973 0.3248 0.0494  -0.0580 -0.0827 285 PHE C N   
9677  C CA  . PHE C 285 ? 0.2898 0.3123 0.3423 0.0473  -0.0574 -0.0759 285 PHE C CA  
9678  C C   . PHE C 285 ? 0.2766 0.2914 0.3279 0.0437  -0.0571 -0.0678 285 PHE C C   
9679  O O   . PHE C 285 ? 0.2323 0.2442 0.2771 0.0407  -0.0530 -0.0609 285 PHE C O   
9680  C CB  . PHE C 285 ? 0.3514 0.3709 0.4085 0.0481  -0.0603 -0.0782 285 PHE C CB  
9681  C CG  . PHE C 285 ? 0.3207 0.3352 0.3776 0.0453  -0.0607 -0.0712 285 PHE C CG  
9682  C CD1 . PHE C 285 ? 0.2890 0.3047 0.3391 0.0436  -0.0564 -0.0666 285 PHE C CD1 
9683  C CD2 . PHE C 285 ? 0.3482 0.3549 0.4091 0.0431  -0.0633 -0.0687 285 PHE C CD2 
9684  C CE1 . PHE C 285 ? 0.3313 0.3404 0.3785 0.0397  -0.0547 -0.0597 285 PHE C CE1 
9685  C CE2 . PHE C 285 ? 0.2958 0.2967 0.3537 0.0394  -0.0618 -0.0618 285 PHE C CE2 
9686  C CZ  . PHE C 285 ? 0.2929 0.2949 0.3438 0.0376  -0.0574 -0.0573 285 PHE C CZ  
9687  N N   . THR C 286 ? 0.3260 0.3356 0.3811 0.0429  -0.0596 -0.0681 286 THR C N   
9688  C CA  . THR C 286 ? 0.2961 0.2985 0.3489 0.0392  -0.0588 -0.0603 286 THR C CA  
9689  C C   . THR C 286 ? 0.3009 0.3037 0.3467 0.0381  -0.0550 -0.0569 286 THR C C   
9690  O O   . THR C 286 ? 0.2677 0.2648 0.3069 0.0341  -0.0516 -0.0487 286 THR C O   
9691  C CB  . THR C 286 ? 0.2956 0.2949 0.3550 0.0394  -0.0626 -0.0628 286 THR C CB  
9692  O OG1 . THR C 286 ? 0.3509 0.3483 0.4163 0.0399  -0.0654 -0.0659 286 THR C OG1 
9693  C CG2 . THR C 286 ? 0.3201 0.3127 0.3757 0.0354  -0.0612 -0.0545 286 THR C CG2 
9694  N N   . LEU C 287 ? 0.3204 0.3289 0.3654 0.0401  -0.0542 -0.0629 287 LEU C N   
9695  C CA  . LEU C 287 ? 0.3001 0.3094 0.3376 0.0383  -0.0502 -0.0606 287 LEU C CA  
9696  C C   . LEU C 287 ? 0.2740 0.2856 0.3054 0.0368  -0.0461 -0.0572 287 LEU C C   
9697  O O   . LEU C 287 ? 0.2705 0.2786 0.2952 0.0334  -0.0427 -0.0515 287 LEU C O   
9698  C CB  . LEU C 287 ? 0.3065 0.3226 0.3439 0.0402  -0.0502 -0.0682 287 LEU C CB  
9699  C CG  . LEU C 287 ? 0.2990 0.3125 0.3413 0.0410  -0.0534 -0.0716 287 LEU C CG  
9700  C CD1 . LEU C 287 ? 0.3190 0.3405 0.3618 0.0437  -0.0537 -0.0800 287 LEU C CD1 
9701  C CD2 . LEU C 287 ? 0.3169 0.3237 0.3560 0.0379  -0.0524 -0.0653 287 LEU C CD2 
9702  N N   . ALA C 288 ? 0.2090 0.2266 0.2422 0.0391  -0.0462 -0.0606 288 ALA C N   
9703  C CA  . ALA C 288 ? 0.2829 0.3034 0.3105 0.0375  -0.0421 -0.0576 288 ALA C CA  
9704  C C   . ALA C 288 ? 0.2305 0.2422 0.2568 0.0350  -0.0414 -0.0496 288 ALA C C   
9705  O O   . ALA C 288 ? 0.2555 0.2657 0.2749 0.0314  -0.0373 -0.0450 288 ALA C O   
9706  C CB  . ALA C 288 ? 0.2231 0.2534 0.2532 0.0409  -0.0426 -0.0635 288 ALA C CB  
9707  N N   . ARG C 289 ? 0.2047 0.2097 0.2346 0.0341  -0.0440 -0.0469 289 ARG C N   
9708  C CA  . ARG C 289 ? 0.2439 0.2400 0.2693 0.0292  -0.0415 -0.0377 289 ARG C CA  
9709  C C   . ARG C 289 ? 0.2844 0.2748 0.3044 0.0258  -0.0392 -0.0316 289 ARG C C   
9710  O O   . ARG C 289 ? 0.2479 0.2342 0.2622 0.0221  -0.0355 -0.0250 289 ARG C O   
9711  C CB  . ARG C 289 ? 0.2530 0.2458 0.2826 0.0279  -0.0440 -0.0363 289 ARG C CB  
9712  C CG  . ARG C 289 ? 0.2296 0.2253 0.2626 0.0294  -0.0455 -0.0394 289 ARG C CG  
9713  C CD  . ARG C 289 ? 0.3106 0.3022 0.3473 0.0275  -0.0482 -0.0378 289 ARG C CD  
9714  N NE  . ARG C 289 ? 0.3104 0.3021 0.3471 0.0267  -0.0480 -0.0369 289 ARG C NE  
9715  C CZ  . ARG C 289 ? 0.3857 0.3741 0.4254 0.0250  -0.0501 -0.0358 289 ARG C CZ  
9716  N NH1 . ARG C 289 ? 0.3749 0.3602 0.4182 0.0241  -0.0525 -0.0352 289 ARG C NH1 
9717  N NH2 . ARG C 289 ? 0.3687 0.3570 0.4082 0.0244  -0.0500 -0.0356 289 ARG C NH2 
9718  N N   . GLN C 290 ? 0.2714 0.2617 0.2930 0.0270  -0.0413 -0.0338 290 GLN C N   
9719  C CA  . GLN C 290 ? 0.3042 0.2891 0.3202 0.0238  -0.0392 -0.0280 290 GLN C CA  
9720  C C   . GLN C 290 ? 0.2496 0.2358 0.2605 0.0238  -0.0369 -0.0278 290 GLN C C   
9721  O O   . GLN C 290 ? 0.2316 0.2118 0.2362 0.0197  -0.0341 -0.0209 290 GLN C O   
9722  C CB  . GLN C 290 ? 0.3281 0.3133 0.3476 0.0256  -0.0424 -0.0312 290 GLN C CB  
9723  C CG  . GLN C 290 ? 0.3982 0.3818 0.4229 0.0253  -0.0452 -0.0313 290 GLN C CG  
9724  C CD  . GLN C 290 ? 0.4282 0.4131 0.4587 0.0280  -0.0494 -0.0368 290 GLN C CD  
9725  O OE1 . GLN C 290 ? 0.4147 0.4025 0.4452 0.0303  -0.0500 -0.0407 290 GLN C OE1 
9726  N NE2 . GLN C 290 ? 0.4960 0.4794 0.5320 0.0277  -0.0523 -0.0375 290 GLN C NE2 
9727  N N   . ARG C 291 ? 0.2913 0.2867 0.3012 0.0241  -0.0351 -0.0342 291 ARG C N   
9728  C CA  . ARG C 291 ? 0.2692 0.2690 0.2713 0.0194  -0.0305 -0.0326 291 ARG C CA  
9729  C C   . ARG C 291 ? 0.2727 0.2719 0.2724 0.0169  -0.0283 -0.0286 291 ARG C C   
9730  O O   . ARG C 291 ? 0.2692 0.2684 0.2628 0.0113  -0.0249 -0.0236 291 ARG C O   
9731  C CB  . ARG C 291 ? 0.2263 0.2382 0.2281 0.0211  -0.0299 -0.0397 291 ARG C CB  
9732  C CG  . ARG C 291 ? 0.2664 0.2852 0.2612 0.0166  -0.0259 -0.0375 291 ARG C CG  
9733  C CD  . ARG C 291 ? 0.2406 0.2691 0.2342 0.0179  -0.0254 -0.0422 291 ARG C CD  
9734  N NE  . ARG C 291 ? 0.2740 0.3091 0.2621 0.0139  -0.0219 -0.0389 291 ARG C NE  
9735  C CZ  . ARG C 291 ? 0.3018 0.3345 0.2850 0.0095  -0.0201 -0.0346 291 ARG C CZ  
9736  N NH1 . ARG C 291 ? 0.2722 0.2965 0.2544 0.0084  -0.0211 -0.0333 291 ARG C NH1 
9737  N NH2 . ARG C 291 ? 0.2620 0.3017 0.2424 0.0066  -0.0172 -0.0317 291 ARG C NH2 
9738  N N   . CYS C 292 ? 0.2406 0.2396 0.2458 0.0207  -0.0304 -0.0305 292 CYS C N   
9739  C CA  . CYS C 292 ? 0.2310 0.2296 0.2342 0.0185  -0.0285 -0.0272 292 CYS C CA  
9740  C C   . CYS C 292 ? 0.2459 0.2338 0.2453 0.0143  -0.0269 -0.0186 292 CYS C C   
9741  O O   . CYS C 292 ? 0.2320 0.2220 0.2268 0.0092  -0.0237 -0.0148 292 CYS C O   
9742  C CB  . CYS C 292 ? 0.2224 0.2209 0.2329 0.0240  -0.0315 -0.0306 292 CYS C CB  
9743  S SG  . CYS C 292 ? 0.2573 0.2544 0.2656 0.0217  -0.0294 -0.0272 292 CYS C SG  
9744  N N   . VAL C 293 ? 0.2802 0.2595 0.2807 0.0146  -0.0280 -0.0143 293 VAL C N   
9745  C CA  . VAL C 293 ? 0.2787 0.2557 0.2756 0.0080  -0.0218 -0.0057 293 VAL C CA  
9746  C C   . VAL C 293 ? 0.2705 0.2464 0.2627 0.0041  -0.0187 -0.0021 293 VAL C C   
9747  O O   . VAL C 293 ? 0.2671 0.2485 0.2579 0.0000  -0.0162 0.0000  293 VAL C O   
9748  C CB  . VAL C 293 ? 0.2773 0.2517 0.2749 0.0063  -0.0218 -0.0060 293 VAL C CB  
9749  C CG1 . VAL C 293 ? 0.3031 0.2772 0.2982 0.0024  -0.0198 -0.0021 293 VAL C CG1 
9750  C CG2 . VAL C 293 ? 0.3217 0.3029 0.3238 0.0078  -0.0271 -0.0081 293 VAL C CG2 
9751  N N   . PRO C 294 ? 0.2726 0.2458 0.2618 0.0043  -0.0207 -0.0029 294 PRO C N   
9752  C CA  . PRO C 294 ? 0.2558 0.2301 0.2414 -0.0011 -0.0162 0.0012  294 PRO C CA  
9753  C C   . PRO C 294 ? 0.2734 0.2557 0.2569 -0.0043 -0.0156 -0.0006 294 PRO C C   
9754  O O   . PRO C 294 ? 0.2566 0.2370 0.2389 -0.0098 -0.0118 0.0049  294 PRO C O   
9755  C CB  . PRO C 294 ? 0.2845 0.2555 0.2673 -0.0004 -0.0182 0.0004  294 PRO C CB  
9756  C CG  . PRO C 294 ? 0.2637 0.2400 0.2501 0.0049  -0.0225 -0.0075 294 PRO C CG  
9757  C CD  . PRO C 294 ? 0.2652 0.2377 0.2563 0.0088  -0.0250 -0.0072 294 PRO C CD  
9758  N N   . MET C 295 ? 0.2685 0.2655 0.2533 -0.0026 -0.0167 -0.0080 295 MET C N   
9759  C CA  . MET C 295 ? 0.2348 0.2412 0.2160 -0.0071 -0.0154 -0.0076 295 MET C CA  
9760  C C   . MET C 295 ? 0.2507 0.2541 0.2324 -0.0058 -0.0168 -0.0059 295 MET C C   
9761  O O   . MET C 295 ? 0.2462 0.2582 0.2297 -0.0055 -0.0139 -0.0055 295 MET C O   
9762  C CB  . MET C 295 ? 0.2474 0.2601 0.2287 -0.0016 -0.0179 -0.0152 295 MET C CB  
9763  C CG  . MET C 295 ? 0.2633 0.2754 0.2428 -0.0014 -0.0180 -0.0169 295 MET C CG  
9764  S SD  . MET C 295 ? 0.3214 0.3343 0.2972 -0.0049 -0.0155 -0.0125 295 MET C SD  
9765  C CE  . MET C 295 ? 0.3120 0.3209 0.2851 -0.0050 -0.0166 -0.0141 295 MET C CE  
9766  N N   . GLU C 296 ? 0.2095 0.2172 0.1953 -0.0035 -0.0174 -0.0088 296 GLU C N   
9767  C CA  . GLU C 296 ? 0.2031 0.2134 0.1900 -0.0035 -0.0178 -0.0078 296 GLU C CA  
9768  C C   . GLU C 296 ? 0.2339 0.2362 0.2244 -0.0020 -0.0169 -0.0051 296 GLU C C   
9769  O O   . GLU C 296 ? 0.2262 0.2291 0.2171 -0.0039 -0.0150 -0.0018 296 GLU C O   
9770  C CB  . GLU C 296 ? 0.2455 0.2619 0.2364 0.0038  -0.0199 -0.0156 296 GLU C CB  
9771  C CG  . GLU C 296 ? 0.2092 0.2376 0.1997 0.0063  -0.0189 -0.0206 296 GLU C CG  
9772  C CD  . GLU C 296 ? 0.2410 0.2814 0.2309 0.0047  -0.0158 -0.0189 296 GLU C CD  
9773  O OE1 . GLU C 296 ? 0.2843 0.3263 0.2755 0.0044  -0.0156 -0.0171 296 GLU C OE1 
9774  O OE2 . GLU C 296 ? 0.3650 0.4145 0.3542 0.0038  -0.0133 -0.0194 296 GLU C OE2 
9775  N N   . GLY C 297 ? 0.2051 0.1918 0.1975 0.0020  -0.0196 -0.0051 297 GLY C N   
9776  C CA  . GLY C 297 ? 0.2181 0.1963 0.2125 0.0013  -0.0176 -0.0007 297 GLY C CA  
9777  C C   . GLY C 297 ? 0.2320 0.2106 0.2298 0.0040  -0.0178 -0.0038 297 GLY C C   
9778  O O   . GLY C 297 ? 0.2559 0.2348 0.2556 0.0084  -0.0216 -0.0070 297 GLY C O   
9779  N N   . PHE C 298 ? 0.2192 0.2022 0.2181 0.0025  -0.0202 -0.0025 298 PHE C N   
9780  C CA  . PHE C 298 ? 0.2499 0.2265 0.2518 0.0047  -0.0214 -0.0049 298 PHE C CA  
9781  C C   . PHE C 298 ? 0.2470 0.2315 0.2528 0.0079  -0.0257 -0.0088 298 PHE C C   
9782  O O   . PHE C 298 ? 0.2676 0.2541 0.2735 0.0090  -0.0248 -0.0102 298 PHE C O   
9783  C CB  . PHE C 298 ? 0.2844 0.2606 0.2873 0.0027  -0.0216 -0.0029 298 PHE C CB  
9784  C CG  . PHE C 298 ? 0.3148 0.2894 0.3209 0.0041  -0.0244 -0.0046 298 PHE C CG  
9785  C CD1 . PHE C 298 ? 0.3480 0.3288 0.3548 0.0041  -0.0279 -0.0046 298 PHE C CD1 
9786  C CD2 . PHE C 298 ? 0.3227 0.3047 0.3330 0.0046  -0.0286 -0.0055 298 PHE C CD2 
9787  C CE1 . PHE C 298 ? 0.3578 0.3382 0.3686 0.0051  -0.0309 -0.0061 298 PHE C CE1 
9788  C CE2 . PHE C 298 ? 0.3054 0.2871 0.3198 0.0056  -0.0316 -0.0070 298 PHE C CE2 
9789  C CZ  . PHE C 298 ? 0.2848 0.2657 0.2996 0.0058  -0.0328 -0.0073 298 PHE C CZ  
9790  N N   . VAL C 299 ? 0.2671 0.2445 0.2756 0.0108  -0.0260 -0.0127 299 VAL C N   
9791  C CA  . VAL C 299 ? 0.2698 0.2499 0.2862 0.0186  -0.0384 -0.0229 299 VAL C CA  
9792  C C   . VAL C 299 ? 0.2787 0.2602 0.2927 0.0158  -0.0285 -0.0202 299 VAL C C   
9793  O O   . VAL C 299 ? 0.2246 0.2164 0.2451 0.0211  -0.0319 -0.0229 299 VAL C O   
9794  C CB  . VAL C 299 ? 0.2790 0.2586 0.2944 0.0163  -0.0306 -0.0209 299 VAL C CB  
9795  C CG1 . VAL C 299 ? 0.2996 0.2850 0.3158 0.0170  -0.0321 -0.0167 299 VAL C CG1 
9796  C CG2 . VAL C 299 ? 0.2647 0.2513 0.2843 0.0135  -0.0360 -0.0176 299 VAL C CG2 
9797  N N   . THR C 300 ? 0.2570 0.2447 0.2717 0.0120  -0.0311 -0.0152 300 THR C N   
9798  C CA  . THR C 300 ? 0.2748 0.2546 0.2900 0.0139  -0.0287 -0.0181 300 THR C CA  
9799  C C   . THR C 300 ? 0.2617 0.2431 0.2736 0.0122  -0.0268 -0.0173 300 THR C C   
9800  O O   . THR C 300 ? 0.2631 0.2453 0.2774 0.0132  -0.0297 -0.0192 300 THR C O   
9801  C CB  . THR C 300 ? 0.3089 0.2849 0.3329 0.0150  -0.0415 -0.0199 300 THR C CB  
9802  O OG1 . THR C 300 ? 0.2712 0.2555 0.2875 0.0076  -0.0310 -0.0099 300 THR C OG1 
9803  C CG2 . THR C 300 ? 0.3023 0.2779 0.3232 0.0131  -0.0329 -0.0179 300 THR C CG2 
9804  N N   . TYR C 301 ? 0.2147 0.1966 0.2245 0.0124  -0.0256 -0.0151 301 TYR C N   
9805  C CA  . TYR C 301 ? 0.2312 0.2157 0.2407 0.0144  -0.0279 -0.0171 301 TYR C CA  
9806  C C   . TYR C 301 ? 0.2200 0.2162 0.2272 0.0148  -0.0267 -0.0178 301 TYR C C   
9807  O O   . TYR C 301 ? 0.2168 0.2278 0.2232 0.0140  -0.0256 -0.0176 301 TYR C O   
9808  C CB  . TYR C 301 ? 0.2521 0.2325 0.2595 0.0082  -0.0252 -0.0096 301 TYR C CB  
9809  C CG  . TYR C 301 ? 0.2350 0.2150 0.2385 0.0033  -0.0198 -0.0037 301 TYR C CG  
9810  C CD1 . TYR C 301 ? 0.2322 0.2116 0.2331 0.0016  -0.0210 -0.0016 301 TYR C CD1 
9811  C CD2 . TYR C 301 ? 0.2499 0.2348 0.2536 0.0015  -0.0204 -0.0016 301 TYR C CD2 
9812  C CE1 . TYR C 301 ? 0.2203 0.2029 0.2188 -0.0020 -0.0146 0.0021  301 TYR C CE1 
9813  C CE2 . TYR C 301 ? 0.2582 0.2434 0.2594 -0.0007 -0.0185 0.0007  301 TYR C CE2 
9814  C CZ  . TYR C 301 ? 0.2388 0.2211 0.2376 -0.0023 -0.0147 0.0022  301 TYR C CZ  
9815  O OH  . TYR C 301 ? 0.2652 0.2526 0.2621 -0.0037 -0.0145 0.0034  301 TYR C OH  
9816  N N   . GLY C 302 ? 0.2321 0.2240 0.2378 0.0146  -0.0264 -0.0174 302 GLY C N   
9817  C CA  . GLY C 302 ? 0.2297 0.2341 0.2326 0.0134  -0.0249 -0.0189 302 GLY C CA  
9818  C C   . GLY C 302 ? 0.2264 0.2413 0.2247 0.0069  -0.0220 -0.0135 302 GLY C C   
9819  O O   . GLY C 302 ? 0.2390 0.2650 0.2361 0.0078  -0.0210 -0.0163 302 GLY C O   
9820  N N   . GLY C 303 ? 0.2049 0.2162 0.2014 0.0016  -0.0201 -0.0065 303 GLY C N   
9821  C CA  . GLY C 303 ? 0.2077 0.2205 0.2012 -0.0034 -0.0190 -0.0014 303 GLY C CA  
9822  C C   . GLY C 303 ? 0.2023 0.2231 0.1980 -0.0013 -0.0191 -0.0022 303 GLY C C   
9823  O O   . GLY C 303 ? 0.1981 0.2299 0.1933 -0.0031 -0.0138 -0.0006 303 GLY C O   
9824  N N   . LEU C 304 ? 0.1668 0.1892 0.1660 0.0003  -0.0209 -0.0027 304 LEU C N   
9825  C CA  . LEU C 304 ? 0.2015 0.2302 0.2033 0.0021  -0.0210 -0.0026 304 LEU C CA  
9826  C C   . LEU C 304 ? 0.2183 0.2393 0.2223 -0.0008 -0.0208 0.0028  304 LEU C C   
9827  O O   . LEU C 304 ? 0.1989 0.2140 0.2033 0.0022  -0.0201 0.0001  304 LEU C O   
9828  C CB  . LEU C 304 ? 0.2288 0.2666 0.2340 0.0086  -0.0219 -0.0096 304 LEU C CB  
9829  C CG  . LEU C 304 ? 0.2107 0.2612 0.2146 0.0119  -0.0201 -0.0156 304 LEU C CG  
9830  C CD1 . LEU C 304 ? 0.2235 0.2783 0.2313 0.0189  -0.0222 -0.0233 304 LEU C CD1 
9831  C CD2 . LEU C 304 ? 0.1626 0.2260 0.1650 0.0099  -0.0160 -0.0132 304 LEU C CD2 
9832  N N   . ALA C 305 ? 0.2102 0.2334 0.2147 0.0015  -0.0206 0.0015  305 ALA C N   
9833  C CA  . ALA C 305 ? 0.2009 0.2230 0.2069 0.0028  -0.0192 0.0024  305 ALA C CA  
9834  C C   . ALA C 305 ? 0.2328 0.2611 0.2439 0.0040  -0.0209 0.0042  305 ALA C C   
9835  O O   . ALA C 305 ? 0.1915 0.2235 0.2053 0.0073  -0.0240 0.0001  305 ALA C O   
9836  C CB  . ALA C 305 ? 0.2297 0.2562 0.2360 -0.0020 -0.0157 0.0084  305 ALA C CB  
9837  N N   . GLY C 306 ? 0.1926 0.2085 0.2051 0.0056  -0.0219 0.0028  306 GLY C N   
9838  C CA  . GLY C 306 ? 0.1818 0.1961 0.1989 0.0102  -0.0250 -0.0006 306 GLY C CA  
9839  C C   . GLY C 306 ? 0.1891 0.2184 0.2104 0.0125  -0.0253 0.0011  306 GLY C C   
9840  O O   . GLY C 306 ? 0.2098 0.2421 0.2347 0.0179  -0.0272 -0.0042 306 GLY C O   
9841  N N   . ARG C 307 ? 0.1673 0.2023 0.1886 0.0081  -0.0236 0.0071  307 ARG C N   
9842  C CA  . ARG C 307 ? 0.1521 0.1938 0.1782 0.0108  -0.0259 0.0052  307 ARG C CA  
9843  C C   . ARG C 307 ? 0.1880 0.2414 0.2121 0.0144  -0.0246 -0.0008 307 ARG C C   
9844  O O   . ARG C 307 ? 0.1702 0.2336 0.1972 0.0188  -0.0243 -0.0041 307 ARG C O   
9845  C CB  . ARG C 307 ? 0.1395 0.1812 0.1619 0.0087  -0.0240 0.0059  307 ARG C CB  
9846  C CG  . ARG C 307 ? 0.1515 0.1945 0.1664 0.0040  -0.0187 0.0082  307 ARG C CG  
9847  C CD  . ARG C 307 ? 0.1614 0.2108 0.1736 -0.0009 -0.0131 0.0142  307 ARG C CD  
9848  N NE  . ARG C 307 ? 0.2637 0.3134 0.2717 -0.0077 -0.0076 0.0191  307 ARG C NE  
9849  C CZ  . ARG C 307 ? 0.2077 0.2443 0.2154 -0.0120 -0.0058 0.0214  307 ARG C CZ  
9850  N NH1 . ARG C 307 ? 0.1727 0.1989 0.1825 -0.0119 -0.0073 0.0212  307 ARG C NH1 
9851  N NH2 . ARG C 307 ? 0.1754 0.2043 0.1804 -0.0118 -0.0039 0.0175  307 ARG C NH2 
9852  N N   . ASP C 308 ? 0.2007 0.2535 0.2201 0.0127  -0.0234 -0.0023 308 ASP C N   
9853  C CA  . ASP C 308 ? 0.1631 0.2281 0.1805 0.0158  -0.0217 -0.0080 308 ASP C CA  
9854  C C   . ASP C 308 ? 0.1559 0.2203 0.1761 0.0216  -0.0240 -0.0147 308 ASP C C   
9855  O O   . ASP C 308 ? 0.1722 0.2475 0.1933 0.0260  -0.0235 -0.0202 308 ASP C O   
9856  C CB  . ASP C 308 ? 0.1770 0.2432 0.1883 0.0117  -0.0186 -0.0068 308 ASP C CB  
9857  C CG  . ASP C 308 ? 0.2004 0.2725 0.2085 0.0072  -0.0140 -0.0018 308 ASP C CG  
9858  O OD1 . ASP C 308 ? 0.2175 0.3015 0.2261 0.0085  -0.0122 -0.0022 308 ASP C OD1 
9859  O OD2 . ASP C 308 ? 0.2399 0.3052 0.2451 0.0022  -0.0117 0.0029  308 ASP C OD2 
9860  N N   . MET C 309 ? 0.1662 0.2179 0.1873 0.0220  -0.0262 -0.0151 309 MET C N   
9861  C CA  . MET C 309 ? 0.1484 0.1976 0.1725 0.0281  -0.0285 -0.0225 309 MET C CA  
9862  C C   . MET C 309 ? 0.1486 0.2022 0.1782 0.0325  -0.0293 -0.0235 309 MET C C   
9863  O O   . MET C 309 ? 0.1653 0.2244 0.1975 0.0379  -0.0302 -0.0299 309 MET C O   
9864  C CB  . MET C 309 ? 0.1569 0.1897 0.1802 0.0273  -0.0304 -0.0233 309 MET C CB  
9865  C CG  . MET C 309 ? 0.1907 0.2192 0.2096 0.0251  -0.0298 -0.0246 309 MET C CG  
9866  S SD  . MET C 309 ? 0.2891 0.2966 0.3074 0.0243  -0.0324 -0.0270 309 MET C SD  
9867  C CE  . MET C 309 ? 0.2158 0.2144 0.2329 0.0182  -0.0310 -0.0183 309 MET C CE  
9868  N N   . ALA C 310 ? 0.1766 0.2283 0.2081 0.0301  -0.0289 -0.0173 310 ALA C N   
9869  C CA  . ALA C 310 ? 0.1864 0.2429 0.2231 0.0342  -0.0294 -0.0176 310 ALA C CA  
9870  C C   . ALA C 310 ? 0.1729 0.2454 0.2104 0.0362  -0.0277 -0.0200 310 ALA C C   
9871  O O   . ALA C 310 ? 0.1721 0.2506 0.2135 0.0417  -0.0282 -0.0242 310 ALA C O   
9872  C CB  . ALA C 310 ? 0.1877 0.2393 0.2257 0.0309  -0.0291 -0.0104 310 ALA C CB  
9873  N N   . ALA C 311 ? 0.1584 0.2375 0.1916 0.0318  -0.0255 -0.0174 311 ALA C N   
9874  C CA  . ALA C 311 ? 0.1642 0.2589 0.1964 0.0334  -0.0233 -0.0201 311 ALA C CA  
9875  C C   . ALA C 311 ? 0.1508 0.2521 0.1821 0.0381  -0.0235 -0.0281 311 ALA C C   
9876  O O   . ALA C 311 ? 0.2038 0.3188 0.2361 0.0429  -0.0228 -0.0332 311 ALA C O   
9877  C CB  . ALA C 311 ? 0.1297 0.2295 0.1561 0.0275  -0.0202 -0.0158 311 ALA C CB  
9878  N N   . MET C 312 ? 0.1333 0.2273 0.1620 0.0382  -0.0247 -0.0311 312 MET C N   
9879  C CA  . MET C 312 ? 0.1139 0.2158 0.1406 0.0440  -0.0255 -0.0413 312 MET C CA  
9880  C C   . MET C 312 ? 0.1488 0.2495 0.1809 0.0511  -0.0285 -0.0479 312 MET C C   
9881  O O   . MET C 312 ? 0.1807 0.2928 0.2128 0.0564  -0.0289 -0.0555 312 MET C O   
9882  C CB  . MET C 312 ? 0.1038 0.1970 0.1267 0.0419  -0.0261 -0.0429 312 MET C CB  
9883  C CG  . MET C 312 ? 0.1503 0.2524 0.1703 0.0472  -0.0267 -0.0537 312 MET C CG  
9884  S SD  . MET C 312 ? 0.2336 0.3246 0.2504 0.0455  -0.0272 -0.0558 312 MET C SD  
9885  C CE  . MET C 312 ? 0.1844 0.2720 0.1978 0.0354  -0.0228 -0.0425 312 MET C CE  
9886  N N   . VAL C 313 ? 0.1708 0.2574 0.2072 0.0509  -0.0305 -0.0445 313 VAL C N   
9887  C CA  . VAL C 313 ? 0.1868 0.2706 0.2285 0.0569  -0.0327 -0.0493 313 VAL C CA  
9888  C C   . VAL C 313 ? 0.1970 0.2941 0.2417 0.0606  -0.0312 -0.0501 313 VAL C C   
9889  O O   . VAL C 313 ? 0.2077 0.3104 0.2548 0.0666  -0.0322 -0.0569 313 VAL C O   
9890  C CB  . VAL C 313 ? 0.2145 0.2817 0.2593 0.0548  -0.0338 -0.0436 313 VAL C CB  
9891  C CG1 . VAL C 313 ? 0.2517 0.3159 0.3019 0.0605  -0.0352 -0.0472 313 VAL C CG1 
9892  C CG2 . VAL C 313 ? 0.2151 0.2694 0.2565 0.0512  -0.0354 -0.0436 313 VAL C CG2 
9893  N N   . GLN C 314 ? 0.2144 0.3166 0.2593 0.0568  -0.0288 -0.0430 314 GLN C N   
9894  C CA  . GLN C 314 ? 0.2368 0.3518 0.2845 0.0598  -0.0274 -0.0435 314 GLN C CA  
9895  C C   . GLN C 314 ? 0.2131 0.3452 0.2565 0.0614  -0.0257 -0.0490 314 GLN C C   
9896  O O   . GLN C 314 ? 0.2004 0.3431 0.2459 0.0666  -0.0255 -0.0539 314 GLN C O   
9897  C CB  . GLN C 314 ? 0.1579 0.2719 0.2071 0.0547  -0.0258 -0.0345 314 GLN C CB  
9898  C CG  . GLN C 314 ? 0.1719 0.2993 0.2237 0.0572  -0.0244 -0.0351 314 GLN C CG  
9899  C CD  . GLN C 314 ? 0.2193 0.3448 0.2772 0.0635  -0.0257 -0.0378 314 GLN C CD  
9900  O OE1 . GLN C 314 ? 0.2723 0.3844 0.3329 0.0644  -0.0273 -0.0365 314 GLN C OE1 
9901  N NE2 . GLN C 314 ? 0.1953 0.3341 0.2550 0.0677  -0.0247 -0.0413 314 GLN C NE2 
9902  N N   . GLY C 315 ? 0.2165 0.3518 0.2538 0.0568  -0.0242 -0.0478 315 GLY C N   
9903  C CA  . GLY C 315 ? 0.1690 0.3210 0.2013 0.0577  -0.0221 -0.0523 315 GLY C CA  
9904  C C   . GLY C 315 ? 0.1822 0.3385 0.2141 0.0639  -0.0242 -0.0621 315 GLY C C   
9905  O O   . GLY C 315 ? 0.2192 0.3902 0.2497 0.0670  -0.0233 -0.0666 315 GLY C O   
9906  N N   . LEU C 316 ? 0.1701 0.3133 0.2032 0.0655  -0.0272 -0.0654 316 LEU C N   
9907  C CA  . LEU C 316 ? 0.1811 0.3265 0.2147 0.0711  -0.0298 -0.0747 316 LEU C CA  
9908  C C   . LEU C 316 ? 0.2252 0.3764 0.2643 0.0771  -0.0302 -0.0780 316 LEU C C   
9909  O O   . LEU C 316 ? 0.2126 0.3743 0.2512 0.0813  -0.0305 -0.0846 316 LEU C O   
9910  C CB  . LEU C 316 ? 0.1941 0.3223 0.2292 0.0712  -0.0332 -0.0767 316 LEU C CB  
9911  C CG  . LEU C 316 ? 0.1873 0.3128 0.2163 0.0672  -0.0336 -0.0775 316 LEU C CG  
9912  C CD1 . LEU C 316 ? 0.1706 0.2770 0.2017 0.0658  -0.0368 -0.0772 316 LEU C CD1 
9913  C CD2 . LEU C 316 ? 0.1515 0.2902 0.1769 0.0700  -0.0345 -0.0854 316 LEU C CD2 
9914  N N   . GLU C 317 ? 0.2288 0.3732 0.2731 0.0775  -0.0300 -0.0733 317 GLU C N   
9915  C CA  . GLU C 317 ? 0.2431 0.3930 0.2924 0.0831  -0.0299 -0.0758 317 GLU C CA  
9916  C C   . GLU C 317 ? 0.2243 0.3929 0.2717 0.0833  -0.0271 -0.0757 317 GLU C C   
9917  O O   . GLU C 317 ? 0.2152 0.3944 0.2630 0.0881  -0.0270 -0.0816 317 GLU C O   
9918  C CB  . GLU C 317 ? 0.2300 0.3682 0.2848 0.0829  -0.0303 -0.0700 317 GLU C CB  
9919  C CG  . GLU C 317 ? 0.2335 0.3766 0.2936 0.0886  -0.0300 -0.0719 317 GLU C CG  
9920  C CD  . GLU C 317 ? 0.3213 0.4622 0.3832 0.0948  -0.0319 -0.0800 317 GLU C CD  
9921  O OE1 . GLU C 317 ? 0.3208 0.4525 0.3814 0.0943  -0.0339 -0.0831 317 GLU C OE1 
9922  O OE2 . GLU C 317 ? 0.4136 0.5622 0.4785 0.1000  -0.0313 -0.0832 317 GLU C OE2 
9923  N N   . GLU C 318 ? 0.1959 0.3685 0.2411 0.0778  -0.0247 -0.0687 318 GLU C N   
9924  C CA  . GLU C 318 ? 0.1803 0.3698 0.2241 0.0772  -0.0220 -0.0676 318 GLU C CA  
9925  C C   . GLU C 318 ? 0.1666 0.3700 0.2050 0.0782  -0.0212 -0.0730 318 GLU C C   
9926  O O   . GLU C 318 ? 0.2301 0.4477 0.2687 0.0807  -0.0198 -0.0753 318 GLU C O   
9927  C CB  . GLU C 318 ? 0.1521 0.3412 0.1939 0.0701  -0.0198 -0.0589 318 GLU C CB  
9928  C CG  . GLU C 318 ? 0.1912 0.3681 0.2384 0.0688  -0.0206 -0.0529 318 GLU C CG  
9929  C CD  . GLU C 318 ? 0.2021 0.3816 0.2482 0.0624  -0.0184 -0.0451 318 GLU C CD  
9930  O OE1 . GLU C 318 ? 0.1896 0.3812 0.2307 0.0595  -0.0160 -0.0446 318 GLU C OE1 
9931  O OE2 . GLU C 318 ? 0.1659 0.3351 0.2158 0.0603  -0.0192 -0.0395 318 GLU C OE2 
9932  N N   . GLY C 319 ? 0.1758 0.3755 0.2094 0.0762  -0.0221 -0.0751 319 GLY C N   
9933  C CA  . GLY C 319 ? 0.1530 0.3655 0.1812 0.0767  -0.0216 -0.0796 319 GLY C CA  
9934  C C   . GLY C 319 ? 0.1991 0.4166 0.2300 0.0838  -0.0236 -0.0880 319 GLY C C   
9935  O O   . GLY C 319 ? 0.2084 0.4390 0.2361 0.0848  -0.0231 -0.0914 319 GLY C O   
9936  N N   . THR C 320 ? 0.2168 0.4238 0.2537 0.0885  -0.0257 -0.0909 320 THR C N   
9937  C CA  . THR C 320 ? 0.2299 0.4401 0.2696 0.0953  -0.0274 -0.0986 320 THR C CA  
9938  C C   . THR C 320 ? 0.2189 0.4395 0.2622 0.0994  -0.0258 -0.0993 320 THR C C   
9939  O O   . THR C 320 ? 0.2109 0.4365 0.2559 0.1051  -0.0266 -0.1055 320 THR C O   
9940  C CB  . THR C 320 ? 0.2396 0.4324 0.2837 0.0982  -0.0305 -0.1016 320 THR C CB  
9941  O OG1 . THR C 320 ? 0.2276 0.4117 0.2768 0.0987  -0.0303 -0.0972 320 THR C OG1 
9942  C CG2 . THR C 320 ? 0.2213 0.4025 0.2625 0.0939  -0.0324 -0.1008 320 THR C CG2 
9943  N N   . GLU C 321 ? 0.2674 0.4912 0.3119 0.0968  -0.0236 -0.0930 321 GLU C N   
9944  C CA  . GLU C 321 ? 0.1989 0.4311 0.2476 0.1008  -0.0225 -0.0934 321 GLU C CA  
9945  C C   . GLU C 321 ? 0.2434 0.4944 0.2893 0.1025  -0.0208 -0.0968 321 GLU C C   
9946  O O   . GLU C 321 ? 0.2614 0.5220 0.3025 0.0977  -0.0189 -0.0937 321 GLU C O   
9947  C CB  . GLU C 321 ? 0.2083 0.4390 0.2591 0.0969  -0.0208 -0.0856 321 GLU C CB  
9948  C CG  . GLU C 321 ? 0.2243 0.4364 0.2776 0.0949  -0.0225 -0.0818 321 GLU C CG  
9949  C CD  . GLU C 321 ? 0.3086 0.5175 0.3658 0.0927  -0.0216 -0.0749 321 GLU C CD  
9950  O OE1 . GLU C 321 ? 0.3946 0.6159 0.4515 0.0912  -0.0194 -0.0724 321 GLU C OE1 
9951  O OE2 . GLU C 321 ? 0.3493 0.5433 0.4099 0.0925  -0.0231 -0.0720 321 GLU C OE2 
9952  N N   . GLU C 322 ? 0.2281 0.4838 0.2769 0.1092  -0.0215 -0.1028 322 GLU C N   
9953  C CA  . GLU C 322 ? 0.2637 0.5360 0.3099 0.1116  -0.0203 -0.1069 322 GLU C CA  
9954  C C   . GLU C 322 ? 0.1979 0.4849 0.2433 0.1087  -0.0172 -0.1022 322 GLU C C   
9955  O O   . GLU C 322 ? 0.2020 0.5021 0.2433 0.1068  -0.0157 -0.1022 322 GLU C O   
9956  C CB  . GLU C 322 ? 0.2089 0.4820 0.2589 0.1196  -0.0217 -0.1140 322 GLU C CB  
9957  C CG  . GLU C 322 ? 0.2786 0.5690 0.3267 0.1227  -0.0205 -0.1181 322 GLU C CG  
9958  C CD  . GLU C 322 ? 0.3368 0.6259 0.3875 0.1304  -0.0223 -0.1260 322 GLU C CD  
9959  O OE1 . GLU C 322 ? 0.3072 0.5814 0.3607 0.1327  -0.0248 -0.1285 322 GLU C OE1 
9960  O OE2 . GLU C 322 ? 0.3974 0.7004 0.4475 0.1341  -0.0213 -0.1294 322 GLU C OE2 
9961  N N   . GLU C 323 ? 0.1958 0.4806 0.2452 0.1081  -0.0164 -0.0978 323 GLU C N   
9962  C CA  . GLU C 323 ? 0.2184 0.5169 0.2677 0.1054  -0.0137 -0.0937 323 GLU C CA  
9963  C C   . GLU C 323 ? 0.2204 0.5209 0.2645 0.0972  -0.0120 -0.0874 323 GLU C C   
9964  O O   . GLU C 323 ? 0.2597 0.5740 0.3013 0.0945  -0.0098 -0.0854 323 GLU C O   
9965  C CB  . GLU C 323 ? 0.2264 0.5217 0.2816 0.1071  -0.0135 -0.0909 323 GLU C CB  
9966  C CG  . GLU C 323 ? 0.3502 0.6292 0.4074 0.1037  -0.0146 -0.0857 323 GLU C CG  
9967  C CD  . GLU C 323 ? 0.4937 0.7568 0.5539 0.1081  -0.0175 -0.0892 323 GLU C CD  
9968  O OE1 . GLU C 323 ? 0.3645 0.6275 0.4237 0.1124  -0.0188 -0.0957 323 GLU C OE1 
9969  O OE2 . GLU C 323 ? 0.4772 0.7277 0.5409 0.1070  -0.0184 -0.0851 323 GLU C OE2 
9970  N N   . TYR C 324 ? 0.1635 0.4503 0.2061 0.0931  -0.0130 -0.0842 324 TYR C N   
9971  C CA  . TYR C 324 ? 0.1731 0.4609 0.2100 0.0855  -0.0116 -0.0786 324 TYR C CA  
9972  C C   . TYR C 324 ? 0.1864 0.4824 0.2177 0.0850  -0.0116 -0.0818 324 TYR C C   
9973  O O   . TYR C 324 ? 0.1957 0.5017 0.2229 0.0802  -0.0098 -0.0782 324 TYR C O   
9974  C CB  . TYR C 324 ? 0.2057 0.4764 0.2423 0.0816  -0.0128 -0.0746 324 TYR C CB  
9975  C CG  . TYR C 324 ? 0.1832 0.4525 0.2127 0.0758  -0.0124 -0.0722 324 TYR C CG  
9976  C CD1 . TYR C 324 ? 0.1251 0.3995 0.1504 0.0688  -0.0101 -0.0656 324 TYR C CD1 
9977  C CD2 . TYR C 324 ? 0.2145 0.4776 0.2416 0.0774  -0.0145 -0.0767 324 TYR C CD2 
9978  C CE1 . TYR C 324 ? 0.1474 0.4207 0.1659 0.0636  -0.0099 -0.0633 324 TYR C CE1 
9979  C CE2 . TYR C 324 ? 0.1596 0.4222 0.1803 0.0723  -0.0143 -0.0747 324 TYR C CE2 
9980  C CZ  . TYR C 324 ? 0.1467 0.4144 0.1629 0.0655  -0.0120 -0.0678 324 TYR C CZ  
9981  O OH  . TYR C 324 ? 0.2068 0.4736 0.2165 0.0604  -0.0121 -0.0656 324 TYR C OH  
9982  N N   . LEU C 325 ? 0.1567 0.4482 0.1880 0.0896  -0.0139 -0.0884 325 LEU C N   
9983  C CA  . LEU C 325 ? 0.1791 0.4779 0.2057 0.0893  -0.0143 -0.0914 325 LEU C CA  
9984  C C   . LEU C 325 ? 0.1878 0.5044 0.2139 0.0912  -0.0124 -0.0928 325 LEU C C   
9985  O O   . LEU C 325 ? 0.1683 0.4940 0.1902 0.0880  -0.0114 -0.0912 325 LEU C O   
9986  C CB  . LEU C 325 ? 0.1757 0.4658 0.2034 0.0944  -0.0173 -0.0986 325 LEU C CB  
9987  C CG  . LEU C 325 ? 0.1778 0.4509 0.2047 0.0918  -0.0194 -0.0975 325 LEU C CG  
9988  C CD1 . LEU C 325 ? 0.1875 0.4505 0.2178 0.0977  -0.0225 -0.1046 325 LEU C CD1 
9989  C CD2 . LEU C 325 ? 0.1962 0.4714 0.2170 0.0861  -0.0193 -0.0948 325 LEU C CD2 
9990  N N   . HIS C 326 ? 0.2001 0.5218 0.2309 0.0966  -0.0120 -0.0957 326 HIS C N   
9991  C CA  . HIS C 326 ? 0.1975 0.5363 0.2284 0.0987  -0.0101 -0.0971 326 HIS C CA  
9992  C C   . HIS C 326 ? 0.2077 0.5556 0.2364 0.0920  -0.0073 -0.0898 326 HIS C C   
9993  O O   . HIS C 326 ? 0.1926 0.5527 0.2185 0.0904  -0.0059 -0.0891 326 HIS C O   
9994  C CB  . HIS C 326 ? 0.1814 0.5223 0.2180 0.1054  -0.0102 -0.1009 326 HIS C CB  
9995  C CG  . HIS C 326 ? 0.1881 0.5465 0.2254 0.1077  -0.0081 -0.1021 326 HIS C CG  
9996  N ND1 . HIS C 326 ? 0.2783 0.6467 0.3132 0.1109  -0.0080 -0.1066 326 HIS C ND1 
9997  C CD2 . HIS C 326 ? 0.2334 0.6009 0.2736 0.1074  -0.0061 -0.0993 326 HIS C CD2 
9998  C CE1 . HIS C 326 ? 0.3429 0.7260 0.3792 0.1124  -0.0058 -0.1064 326 HIS C CE1 
9999  N NE2 . HIS C 326 ? 0.2480 0.6308 0.2875 0.1103  -0.0047 -0.1021 326 HIS C NE2 
10000 N N   . TYR C 327 ? 0.1620 0.5036 0.1922 0.0878  -0.0066 -0.0841 327 TYR C N   
10001 C CA  A TYR C 327 ? 0.1665 0.5147 0.1947 0.0808  -0.0043 -0.0769 327 TYR C CA  
10002 C CA  B TYR C 327 ? 0.1668 0.5150 0.1949 0.0808  -0.0043 -0.0769 327 TYR C CA  
10003 C C   . TYR C 327 ? 0.1567 0.5031 0.1788 0.0745  -0.0043 -0.0732 327 TYR C C   
10004 O O   . TYR C 327 ? 0.1948 0.5516 0.2144 0.0707  -0.0027 -0.0699 327 TYR C O   
10005 C CB  A TYR C 327 ? 0.1894 0.5294 0.2208 0.0780  -0.0039 -0.0719 327 TYR C CB  
10006 C CB  B TYR C 327 ? 0.1893 0.5293 0.2206 0.0780  -0.0039 -0.0719 327 TYR C CB  
10007 C CG  A TYR C 327 ? 0.1834 0.5184 0.2107 0.0693  -0.0030 -0.0642 327 TYR C CG  
10008 C CG  B TYR C 327 ? 0.1816 0.5224 0.2098 0.0695  -0.0023 -0.0640 327 TYR C CG  
10009 C CD1 A TYR C 327 ? 0.1768 0.5215 0.2029 0.0642  -0.0009 -0.0591 327 TYR C CD1 
10010 C CD1 B TYR C 327 ? 0.1681 0.5212 0.1973 0.0671  -0.0001 -0.0609 327 TYR C CD1 
10011 C CD2 A TYR C 327 ? 0.1782 0.4983 0.2030 0.0662  -0.0044 -0.0619 327 TYR C CD2 
10012 C CD2 B TYR C 327 ? 0.1792 0.5079 0.2034 0.0639  -0.0030 -0.0596 327 TYR C CD2 
10013 C CE1 A TYR C 327 ? 0.1776 0.5168 0.1999 0.0563  -0.0004 -0.0521 327 TYR C CE1 
10014 C CE1 B TYR C 327 ? 0.1671 0.5198 0.1935 0.0593  0.0011  -0.0537 327 TYR C CE1 
10015 C CE2 A TYR C 327 ? 0.1727 0.4877 0.1934 0.0584  -0.0036 -0.0549 327 TYR C CE2 
10016 C CE2 B TYR C 327 ? 0.1737 0.5020 0.1946 0.0562  -0.0017 -0.0524 327 TYR C CE2 
10017 C CZ  A TYR C 327 ? 0.1750 0.4992 0.1943 0.0535  -0.0018 -0.0500 327 TYR C CZ  
10018 C CZ  B TYR C 327 ? 0.1821 0.5222 0.2042 0.0539  0.0002  -0.0495 327 TYR C CZ  
10019 O OH  A TYR C 327 ? 0.1448 0.4627 0.1598 0.0459  -0.0014 -0.0430 327 TYR C OH  
10020 O OH  B TYR C 327 ? 0.1795 0.5182 0.1986 0.0463  0.0011  -0.0425 327 TYR C OH  
10021 N N   . ARG C 328 ? 0.1601 0.4930 0.1800 0.0733  -0.0062 -0.0734 328 ARG C N   
10022 C CA  . ARG C 328 ? 0.1553 0.4855 0.1697 0.0671  -0.0066 -0.0694 328 ARG C CA  
10023 C C   . ARG C 328 ? 0.1789 0.5200 0.1911 0.0685  -0.0067 -0.0723 328 ARG C C   
10024 O O   . ARG C 328 ? 0.1652 0.5122 0.1747 0.0632  -0.0057 -0.0676 328 ARG C O   
10025 C CB  . ARG C 328 ? 0.1424 0.4562 0.1553 0.0665  -0.0087 -0.0700 328 ARG C CB  
10026 C CG  . ARG C 328 ? 0.1658 0.4747 0.1732 0.0597  -0.0094 -0.0652 328 ARG C CG  
10027 C CD  . ARG C 328 ? 0.1393 0.4546 0.1451 0.0610  -0.0108 -0.0687 328 ARG C CD  
10028 N NE  . ARG C 328 ? 0.1612 0.4667 0.1646 0.0561  -0.0118 -0.0653 328 ARG C NE  
10029 C CZ  . ARG C 328 ? 0.1359 0.4365 0.1382 0.0484  -0.0096 -0.0571 328 ARG C CZ  
10030 N NH1 . ARG C 328 ? 0.1236 0.4311 0.1253 0.0446  -0.0079 -0.0520 328 ARG C NH1 
10031 N NH2 . ARG C 328 ? 0.1243 0.4127 0.1266 0.0444  -0.0093 -0.0540 328 ARG C NH2 
10032 N N   . ILE C 329 ? 0.1562 0.4992 0.1703 0.0755  -0.0079 -0.0798 329 ILE C N   
10033 C CA  . ILE C 329 ? 0.1574 0.5096 0.1697 0.0772  -0.0080 -0.0828 329 ILE C CA  
10034 C C   . ILE C 329 ? 0.1634 0.5316 0.1766 0.0780  -0.0053 -0.0819 329 ILE C C   
10035 O O   . ILE C 329 ? 0.1682 0.5449 0.1793 0.0761  -0.0042 -0.0803 329 ILE C O   
10036 C CB  . ILE C 329 ? 0.1756 0.5233 0.1894 0.0844  -0.0104 -0.0912 329 ILE C CB  
10037 C CG1 . ILE C 329 ? 0.1777 0.5090 0.1908 0.0830  -0.0130 -0.0916 329 ILE C CG1 
10038 C CG2 . ILE C 329 ? 0.1930 0.5502 0.2051 0.0867  -0.0103 -0.0944 329 ILE C CG2 
10039 C CD1 . ILE C 329 ? 0.2017 0.5269 0.2165 0.0893  -0.0157 -0.0996 329 ILE C CD1 
10040 N N   . GLY C 330 ? 0.1998 0.5720 0.2165 0.0807  -0.0042 -0.0826 330 GLY C N   
10041 C CA  . GLY C 330 ? 0.1820 0.5694 0.1999 0.0809  -0.0015 -0.0813 330 GLY C CA  
10042 C C   . GLY C 330 ? 0.1785 0.5695 0.1946 0.0728  0.0005  -0.0731 330 GLY C C   
10043 O O   . GLY C 330 ? 0.1997 0.6030 0.2155 0.0717  0.0027  -0.0715 330 GLY C O   
10044 N N   . GLN C 331 ? 0.1576 0.5376 0.1725 0.0671  -0.0001 -0.0678 331 GLN C N   
10045 C CA  . GLN C 331 ? 0.1526 0.5341 0.1654 0.0591  0.0013  -0.0600 331 GLN C CA  
10046 C C   . GLN C 331 ? 0.1519 0.5354 0.1614 0.0562  0.0011  -0.0584 331 GLN C C   
10047 O O   . GLN C 331 ? 0.1735 0.5651 0.1825 0.0524  0.0031  -0.0543 331 GLN C O   
10048 C CB  . GLN C 331 ? 0.1627 0.5308 0.1746 0.0539  0.0003  -0.0549 331 GLN C CB  
10049 C CG  . GLN C 331 ? 0.1695 0.5374 0.1791 0.0456  0.0013  -0.0470 331 GLN C CG  
10050 C CD  . GLN C 331 ? 0.1692 0.5236 0.1773 0.0406  0.0003  -0.0419 331 GLN C CD  
10051 O OE1 . GLN C 331 ? 0.1372 0.4798 0.1426 0.0394  -0.0016 -0.0416 331 GLN C OE1 
10052 N NE2 . GLN C 331 ? 0.1398 0.4956 0.1499 0.0377  0.0018  -0.0380 331 GLN C NE2 
10053 N N   . VAL C 332 ? 0.1500 0.5260 0.1578 0.0579  -0.0011 -0.0615 332 VAL C N   
10054 C CA  . VAL C 332 ? 0.1552 0.5336 0.1609 0.0563  -0.0011 -0.0607 332 VAL C CA  
10055 C C   . VAL C 332 ? 0.1935 0.5863 0.1998 0.0606  0.0010  -0.0642 332 VAL C C   
10056 O O   . VAL C 332 ? 0.1808 0.5798 0.1859 0.0577  0.0028  -0.0608 332 VAL C O   
10057 C CB  . VAL C 332 ? 0.1528 0.5210 0.1576 0.0583  -0.0039 -0.0644 332 VAL C CB  
10058 C CG1 . VAL C 332 ? 0.1490 0.5204 0.1525 0.0577  -0.0036 -0.0643 332 VAL C CG1 
10059 C CG2 . VAL C 332 ? 0.1722 0.5261 0.1759 0.0533  -0.0058 -0.0602 332 VAL C CG2 
10060 N N   . LYS C 333 ? 0.1672 0.5651 0.1756 0.0679  0.0008  -0.0709 333 LYS C N   
10061 C CA  . LYS C 333 ? 0.1770 0.5888 0.1859 0.0725  0.0027  -0.0743 333 LYS C CA  
10062 C C   . LYS C 333 ? 0.1787 0.6011 0.1886 0.0689  0.0059  -0.0692 333 LYS C C   
10063 O O   . LYS C 333 ? 0.2147 0.6469 0.2236 0.0687  0.0081  -0.0682 333 LYS C O   
10064 C CB  . LYS C 333 ? 0.1842 0.5980 0.1954 0.0810  0.0016  -0.0824 333 LYS C CB  
10065 C CG  . LYS C 333 ? 0.2428 0.6687 0.2537 0.0869  0.0027  -0.0874 333 LYS C CG  
10066 C CD  . LYS C 333 ? 0.2708 0.6986 0.2846 0.0952  0.0015  -0.0951 333 LYS C CD  
10067 C CE  . LYS C 333 ? 0.3255 0.7663 0.3388 0.1010  0.0026  -0.0999 333 LYS C CE  
10068 N NZ  . LYS C 333 ? 0.2237 0.6787 0.2376 0.0990  0.0062  -0.0959 333 LYS C NZ  
10069 N N   . TYR C 334 ? 0.1746 0.5944 0.1865 0.0659  0.0063  -0.0658 334 TYR C N   
10070 C CA  . TYR C 334 ? 0.1763 0.6055 0.1897 0.0623  0.0092  -0.0610 334 TYR C CA  
10071 C C   . TYR C 334 ? 0.1736 0.6031 0.1845 0.0553  0.0106  -0.0546 334 TYR C C   
10072 O O   . TYR C 334 ? 0.1808 0.6212 0.1921 0.0547  0.0134  -0.0530 334 TYR C O   
10073 C CB  . TYR C 334 ? 0.1715 0.5958 0.1876 0.0599  0.0089  -0.0583 334 TYR C CB  
10074 C CG  . TYR C 334 ? 0.1723 0.6046 0.1903 0.0553  0.0116  -0.0530 334 TYR C CG  
10075 C CD1 . TYR C 334 ? 0.2062 0.6523 0.2274 0.0590  0.0139  -0.0553 334 TYR C CD1 
10076 C CD2 . TYR C 334 ? 0.2136 0.6392 0.2303 0.0474  0.0118  -0.0459 334 TYR C CD2 
10077 C CE1 . TYR C 334 ? 0.1812 0.6348 0.2047 0.0547  0.0164  -0.0507 334 TYR C CE1 
10078 C CE2 . TYR C 334 ? 0.1669 0.5992 0.1857 0.0431  0.0142  -0.0414 334 TYR C CE2 
10079 C CZ  . TYR C 334 ? 0.1747 0.6210 0.1969 0.0468  0.0165  -0.0438 334 TYR C CZ  
10080 O OH  . TYR C 334 ? 0.1781 0.6312 0.2029 0.0425  0.0190  -0.0395 334 TYR C OH  
10081 N N   . LEU C 335 ? 0.1654 0.5825 0.1741 0.0503  0.0088  -0.0508 335 LEU C N   
10082 C CA  . LEU C 335 ? 0.1631 0.5788 0.1697 0.0440  0.0099  -0.0449 335 LEU C CA  
10083 C C   . LEU C 335 ? 0.1822 0.6050 0.1871 0.0471  0.0113  -0.0474 335 LEU C C   
10084 O O   . LEU C 335 ? 0.1734 0.6023 0.1777 0.0443  0.0140  -0.0439 335 LEU C O   
10085 C CB  . LEU C 335 ? 0.1532 0.5536 0.1580 0.0388  0.0073  -0.0411 335 LEU C CB  
10086 C CG  . LEU C 335 ? 0.1506 0.5472 0.1536 0.0327  0.0081  -0.0354 335 LEU C CG  
10087 C CD1 . LEU C 335 ? 0.1815 0.5838 0.1854 0.0280  0.0109  -0.0301 335 LEU C CD1 
10088 C CD2 . LEU C 335 ? 0.1406 0.5219 0.1425 0.0281  0.0052  -0.0321 335 LEU C CD2 
10089 N N   . GLY C 336 ? 0.1769 0.5987 0.1811 0.0531  0.0096  -0.0538 336 GLY C N   
10090 C CA  . GLY C 336 ? 0.1855 0.6138 0.1879 0.0566  0.0108  -0.0567 336 GLY C CA  
10091 C C   . GLY C 336 ? 0.2093 0.6530 0.2126 0.0604  0.0138  -0.0587 336 GLY C C   
10092 O O   . GLY C 336 ? 0.2433 0.6938 0.2448 0.0604  0.0162  -0.0575 336 GLY C O   
10093 N N   . ASP C 337 ? 0.1919 0.6413 0.1981 0.0639  0.0138  -0.0616 337 ASP C N   
10094 C CA  . ASP C 337 ? 0.2336 0.6980 0.2412 0.0675  0.0166  -0.0634 337 ASP C CA  
10095 C C   . ASP C 337 ? 0.2295 0.6995 0.2378 0.0613  0.0200  -0.0564 337 ASP C C   
10096 O O   . ASP C 337 ? 0.2217 0.7026 0.2295 0.0623  0.0229  -0.0560 337 ASP C O   
10097 C CB  . ASP C 337 ? 0.2039 0.6719 0.2151 0.0730  0.0157  -0.0684 337 ASP C CB  
10098 C CG  . ASP C 337 ? 0.2365 0.7031 0.2472 0.0810  0.0133  -0.0766 337 ASP C CG  
10099 O OD1 . ASP C 337 ? 0.2916 0.7598 0.2996 0.0835  0.0132  -0.0791 337 ASP C OD1 
10100 O OD2 . ASP C 337 ? 0.2119 0.6753 0.2251 0.0850  0.0115  -0.0807 337 ASP C OD2 
10101 N N   . ARG C 338 ? 0.2462 0.7084 0.2556 0.0547  0.0195  -0.0509 338 ARG C N   
10102 C CA  . ARG C 338 ? 0.2045 0.6701 0.2145 0.0484  0.0224  -0.0442 338 ARG C CA  
10103 C C   . ARG C 338 ? 0.2170 0.6825 0.2238 0.0457  0.0242  -0.0411 338 ARG C C   
10104 O O   . ARG C 338 ? 0.2261 0.7016 0.2331 0.0439  0.0274  -0.0383 338 ARG C O   
10105 C CB  . ARG C 338 ? 0.1899 0.6445 0.2008 0.0417  0.0209  -0.0390 338 ARG C CB  
10106 C CG  . ARG C 338 ? 0.2020 0.6570 0.2165 0.0432  0.0199  -0.0405 338 ARG C CG  
10107 C CD  . ARG C 338 ? 0.2067 0.6737 0.2248 0.0426  0.0230  -0.0390 338 ARG C CD  
10108 N NE  . ARG C 338 ? 0.2514 0.7232 0.2688 0.0379  0.0261  -0.0341 338 ARG C NE  
10109 C CZ  . ARG C 338 ? 0.2362 0.7047 0.2531 0.0306  0.0261  -0.0279 338 ARG C CZ  
10110 N NH1 . ARG C 338 ? 0.1793 0.6366 0.1964 0.0268  0.0236  -0.0254 338 ARG C NH1 
10111 N NH2 . ARG C 338 ? 0.2715 0.7479 0.2876 0.0273  0.0287  -0.0243 338 ARG C NH2 
10112 N N   . LEU C 339 ? 0.2158 0.6716 0.2196 0.0456  0.0221  -0.0418 339 LEU C N   
10113 C CA  . LEU C 339 ? 0.2432 0.7002 0.2438 0.0434  0.0234  -0.0390 339 LEU C CA  
10114 C C   . LEU C 339 ? 0.2608 0.7293 0.2599 0.0496  0.0257  -0.0433 339 LEU C C   
10115 O O   . LEU C 339 ? 0.2416 0.7194 0.2394 0.0483  0.0286  -0.0405 339 LEU C O   
10116 C CB  . LEU C 339 ? 0.2375 0.6807 0.2359 0.0414  0.0204  -0.0385 339 LEU C CB  
10117 C CG  . LEU C 339 ? 0.2479 0.6793 0.2472 0.0348  0.0180  -0.0337 339 LEU C CG  
10118 C CD1 . LEU C 339 ? 0.2036 0.6225 0.2011 0.0331  0.0153  -0.0332 339 LEU C CD1 
10119 C CD2 . LEU C 339 ? 0.2119 0.6479 0.2116 0.0284  0.0199  -0.0271 339 LEU C CD2 
10120 N N   . ARG C 340 ? 0.2175 0.6866 0.2166 0.0565  0.0241  -0.0502 340 ARG C N   
10121 C CA  . ARG C 340 ? 0.2378 0.7183 0.2354 0.0630  0.0258  -0.0548 340 ARG C CA  
10122 C C   . ARG C 340 ? 0.2667 0.7613 0.2661 0.0635  0.0295  -0.0534 340 ARG C C   
10123 O O   . ARG C 340 ? 0.2624 0.7660 0.2597 0.0645  0.0325  -0.0525 340 ARG C O   
10124 C CB  . ARG C 340 ? 0.2346 0.7157 0.2327 0.0707  0.0227  -0.0631 340 ARG C CB  
10125 C CG  . ARG C 340 ? 0.2864 0.7555 0.2824 0.0715  0.0195  -0.0655 340 ARG C CG  
10126 C CD  . ARG C 340 ? 0.3222 0.7917 0.3191 0.0793  0.0166  -0.0739 340 ARG C CD  
10127 N NE  . ARG C 340 ? 0.3269 0.8100 0.3236 0.0861  0.0182  -0.0788 340 ARG C NE  
10128 C CZ  . ARG C 340 ? 0.3744 0.8617 0.3682 0.0904  0.0185  -0.0823 340 ARG C CZ  
10129 N NH1 . ARG C 340 ? 0.3916 0.8708 0.3824 0.0887  0.0177  -0.0813 340 ARG C NH1 
10130 N NH2 . ARG C 340 ? 0.3567 0.8566 0.3506 0.0968  0.0198  -0.0868 340 ARG C NH2 
10131 N N   . GLU C 341 ? 0.2346 0.7326 0.2379 0.0629  0.0295  -0.0532 341 GLU C N   
10132 C CA  . GLU C 341 ? 0.2556 0.7675 0.2614 0.0635  0.0331  -0.0521 341 GLU C CA  
10133 C C   . GLU C 341 ? 0.3211 0.8365 0.3260 0.0571  0.0363  -0.0451 341 GLU C C   
10134 O O   . GLU C 341 ? 0.3181 0.8468 0.3240 0.0580  0.0398  -0.0442 341 GLU C O   
10135 C CB  . GLU C 341 ? 0.2284 0.7421 0.2388 0.0636  0.0322  -0.0529 341 GLU C CB  
10136 C CG  . GLU C 341 ? 0.3239 0.8387 0.3356 0.0713  0.0293  -0.0606 341 GLU C CG  
10137 C CD  . GLU C 341 ? 0.3427 0.8561 0.3587 0.0710  0.0281  -0.0610 341 GLU C CD  
10138 O OE1 . GLU C 341 ? 0.4018 0.9211 0.4208 0.0675  0.0305  -0.0572 341 GLU C OE1 
10139 O OE2 . GLU C 341 ? 0.2889 0.7948 0.3054 0.0743  0.0248  -0.0652 341 GLU C OE2 
10140 N N   . ALA C 342 ? 0.2711 0.7764 0.2741 0.0509  0.0351  -0.0402 342 ALA C N   
10141 C CA  . ALA C 342 ? 0.3094 0.8184 0.3111 0.0451  0.0377  -0.0338 342 ALA C CA  
10142 C C   . ALA C 342 ? 0.3078 0.8171 0.3048 0.0462  0.0385  -0.0335 342 ALA C C   
10143 O O   . ALA C 342 ? 0.3027 0.8123 0.2980 0.0413  0.0403  -0.0281 342 ALA C O   
10144 C CB  . ALA C 342 ? 0.2901 0.7886 0.2927 0.0373  0.0360  -0.0282 342 ALA C CB  
10145 N N   . GLY C 343 ? 0.2755 0.7843 0.2704 0.0527  0.0372  -0.0394 343 GLY C N   
10146 C CA  . GLY C 343 ? 0.3021 0.8123 0.2926 0.0546  0.0381  -0.0397 343 GLY C CA  
10147 C C   . GLY C 343 ? 0.3711 0.8677 0.3590 0.0511  0.0354  -0.0377 343 GLY C C   
10148 O O   . GLY C 343 ? 0.3432 0.8407 0.3276 0.0511  0.0366  -0.0362 343 GLY C O   
10149 N N   . ILE C 344 ? 0.3399 0.8244 0.3297 0.0483  0.0321  -0.0375 344 ILE C N   
10150 C CA  . ILE C 344 ? 0.3160 0.7872 0.3040 0.0451  0.0293  -0.0358 344 ILE C CA  
10151 C C   . ILE C 344 ? 0.3319 0.7984 0.3185 0.0513  0.0269  -0.0425 344 ILE C C   
10152 O O   . ILE C 344 ? 0.2904 0.7552 0.2791 0.0552  0.0251  -0.0473 344 ILE C O   
10153 C CB  . ILE C 344 ? 0.3246 0.7848 0.3153 0.0392  0.0269  -0.0323 344 ILE C CB  
10154 C CG1 . ILE C 344 ? 0.3230 0.7884 0.3154 0.0335  0.0291  -0.0264 344 ILE C CG1 
10155 C CG2 . ILE C 344 ? 0.2544 0.7018 0.2434 0.0357  0.0243  -0.0302 344 ILE C CG2 
10156 C CD1 . ILE C 344 ? 0.3633 0.8326 0.3532 0.0298  0.0318  -0.0213 344 ILE C CD1 
10157 N N   . PRO C 345 ? 0.3046 0.7686 0.2878 0.0524  0.0266  -0.0430 345 PRO C N   
10158 C CA  . PRO C 345 ? 0.3514 0.8101 0.3335 0.0580  0.0241  -0.0495 345 PRO C CA  
10159 C C   . PRO C 345 ? 0.3672 0.8110 0.3512 0.0554  0.0204  -0.0497 345 PRO C C   
10160 O O   . PRO C 345 ? 0.3462 0.7820 0.3306 0.0490  0.0197  -0.0444 345 PRO C O   
10161 C CB  . PRO C 345 ? 0.4135 0.8742 0.3914 0.0589  0.0252  -0.0488 345 PRO C CB  
10162 C CG  . PRO C 345 ? 0.4137 0.8736 0.3909 0.0517  0.0271  -0.0410 345 PRO C CG  
10163 C CD  . PRO C 345 ? 0.4598 0.9260 0.4399 0.0489  0.0289  -0.0379 345 PRO C CD  
10164 N N   . ILE C 346 ? 0.2924 0.7323 0.2777 0.0604  0.0181  -0.0560 346 ILE C N   
10165 C CA  . ILE C 346 ? 0.2955 0.7212 0.2827 0.0589  0.0147  -0.0571 346 ILE C CA  
10166 C C   . ILE C 346 ? 0.2795 0.7019 0.2661 0.0656  0.0126  -0.0647 346 ILE C C   
10167 O O   . ILE C 346 ? 0.2873 0.7198 0.2729 0.0719  0.0132  -0.0699 346 ILE C O   
10168 C CB  . ILE C 346 ? 0.3014 0.7244 0.2921 0.0570  0.0139  -0.0560 346 ILE C CB  
10169 C CG1 . ILE C 346 ? 0.2416 0.6739 0.2341 0.0645  0.0129  -0.0633 346 ILE C CG1 
10170 C CG2 . ILE C 346 ? 0.2654 0.6942 0.2570 0.0513  0.0162  -0.0493 346 ILE C CG2 
10171 C CD1 . ILE C 346 ? 0.2669 0.6989 0.2627 0.0636  0.0118  -0.0630 346 ILE C CD1 
10172 N N   . GLN C 347 ? 0.2566 0.6666 0.2440 0.0645  0.0096  -0.0658 347 GLN C N   
10173 C CA  . GLN C 347 ? 0.3047 0.7127 0.2927 0.0710  0.0067  -0.0737 347 GLN C CA  
10174 C C   . GLN C 347 ? 0.2870 0.7024 0.2776 0.0762  0.0055  -0.0789 347 GLN C C   
10175 O O   . GLN C 347 ? 0.3277 0.7404 0.3209 0.0739  0.0047  -0.0771 347 GLN C O   
10176 C CB  . GLN C 347 ? 0.2279 0.6209 0.2171 0.0684  0.0039  -0.0734 347 GLN C CB  
10177 C CG  . GLN C 347 ? 0.2728 0.6620 0.2637 0.0746  0.0004  -0.0816 347 GLN C CG  
10178 C CD  . GLN C 347 ? 0.3587 0.7479 0.3472 0.0794  -0.0002 -0.0869 347 GLN C CD  
10179 O OE1 . GLN C 347 ? 0.3653 0.7644 0.3513 0.0825  0.0016  -0.0884 347 GLN C OE1 
10180 N NE2 . GLN C 347 ? 0.3532 0.7311 0.3426 0.0801  -0.0029 -0.0899 347 GLN C NE2 
10181 N N   . TYR C 348 ? 0.2075 0.6321 0.1973 0.0833  0.0056  -0.0852 348 TYR C N   
10182 C CA  . TYR C 348 ? 0.2499 0.6822 0.2419 0.0888  0.0049  -0.0904 348 TYR C CA  
10183 C C   . TYR C 348 ? 0.2723 0.7005 0.2650 0.0958  0.0015  -0.0992 348 TYR C C   
10184 O O   . TYR C 348 ? 0.3079 0.7358 0.2983 0.0987  0.0010  -0.1025 348 TYR C O   
10185 C CB  . TYR C 348 ? 0.2899 0.7375 0.2807 0.0913  0.0082  -0.0902 348 TYR C CB  
10186 C CG  . TYR C 348 ? 0.3290 0.7859 0.3222 0.0970  0.0081  -0.0951 348 TYR C CG  
10187 C CD1 . TYR C 348 ? 0.2901 0.7461 0.2865 0.0951  0.0079  -0.0934 348 TYR C CD1 
10188 C CD2 . TYR C 348 ? 0.3085 0.7750 0.3007 0.1044  0.0083  -0.1014 348 TYR C CD2 
10189 C CE1 . TYR C 348 ? 0.3319 0.7961 0.3307 0.1004  0.0080  -0.0979 348 TYR C CE1 
10190 C CE2 . TYR C 348 ? 0.2992 0.7739 0.2938 0.1097  0.0082  -0.1059 348 TYR C CE2 
10191 C CZ  . TYR C 348 ? 0.3324 0.8059 0.3303 0.1078  0.0082  -0.1041 348 TYR C CZ  
10192 O OH  . TYR C 348 ? 0.4099 0.8913 0.4104 0.1133  0.0082  -0.1086 348 TYR C OH  
10193 N N   . PRO C 349 ? 0.2430 0.6669 0.2386 0.0985  -0.0009 -0.1032 349 PRO C N   
10194 C CA  . PRO C 349 ? 0.2294 0.6520 0.2277 0.0956  -0.0007 -0.1001 349 PRO C CA  
10195 C C   . PRO C 349 ? 0.2316 0.6423 0.2303 0.0882  -0.0014 -0.0939 349 PRO C C   
10196 O O   . PRO C 349 ? 0.2179 0.6203 0.2153 0.0860  -0.0025 -0.0929 349 PRO C O   
10197 C CB  . PRO C 349 ? 0.2193 0.6387 0.2202 0.1024  -0.0035 -0.1080 349 PRO C CB  
10198 C CG  . PRO C 349 ? 0.2157 0.6267 0.2157 0.1053  -0.0063 -0.1131 349 PRO C CG  
10199 C CD  . PRO C 349 ? 0.2369 0.6547 0.2335 0.1047  -0.0044 -0.1115 349 PRO C CD  
10200 N N   . THR C 350 ? 0.1969 0.6065 0.1973 0.0843  -0.0008 -0.0895 350 THR C N   
10201 C CA  . THR C 350 ? 0.1919 0.5900 0.1926 0.0775  -0.0018 -0.0837 350 THR C CA  
10202 C C   . THR C 350 ? 0.2456 0.6311 0.2477 0.0798  -0.0053 -0.0881 350 THR C C   
10203 O O   . THR C 350 ? 0.1867 0.5720 0.1904 0.0858  -0.0068 -0.0945 350 THR C O   
10204 C CB  . THR C 350 ? 0.1791 0.5793 0.1810 0.0728  -0.0003 -0.0780 350 THR C CB  
10205 O OG1 . THR C 350 ? 0.1920 0.5951 0.1963 0.0777  -0.0009 -0.0825 350 THR C OG1 
10206 C CG2 . THR C 350 ? 0.1960 0.6070 0.1969 0.0695  0.0033  -0.0728 350 THR C CG2 
10207 N N   . GLY C 351 ? 0.1697 0.5442 0.1714 0.0750  -0.0065 -0.0846 351 GLY C N   
10208 C CA  . GLY C 351 ? 0.1924 0.5538 0.1955 0.0761  -0.0097 -0.0876 351 GLY C CA  
10209 C C   . GLY C 351 ? 0.2188 0.5750 0.2234 0.0740  -0.0104 -0.0852 351 GLY C C   
10210 O O   . GLY C 351 ? 0.2499 0.6130 0.2546 0.0727  -0.0085 -0.0824 351 GLY C O   
10211 N N   . GLY C 352 ? 0.1692 0.5124 0.1748 0.0736  -0.0129 -0.0864 352 GLY C N   
10212 C CA  . GLY C 352 ? 0.1628 0.4994 0.1691 0.0729  -0.0137 -0.0853 352 GLY C CA  
10213 C C   . GLY C 352 ? 0.2084 0.5410 0.2136 0.0651  -0.0129 -0.0768 352 GLY C C   
10214 O O   . GLY C 352 ? 0.2226 0.5504 0.2278 0.0645  -0.0128 -0.0754 352 GLY C O   
10215 N N   . HIS C 353 ? 0.1498 0.4831 0.1542 0.0593  -0.0121 -0.0709 353 HIS C N   
10216 C CA  . HIS C 353 ? 0.1709 0.4928 0.1747 0.0513  -0.0101 -0.0623 353 HIS C CA  
10217 C C   . HIS C 353 ? 0.1928 0.5204 0.1959 0.0453  -0.0080 -0.0554 353 HIS C C   
10218 O O   . HIS C 353 ? 0.1417 0.4602 0.1444 0.0388  -0.0066 -0.0484 353 HIS C O   
10219 C CB  . HIS C 353 ? 0.1261 0.4291 0.1305 0.0487  -0.0105 -0.0607 353 HIS C CB  
10220 C CG  . HIS C 353 ? 0.1602 0.4619 0.1651 0.0475  -0.0102 -0.0604 353 HIS C CG  
10221 N ND1 . HIS C 353 ? 0.1415 0.4528 0.1470 0.0534  -0.0117 -0.0672 353 HIS C ND1 
10222 C CD2 . HIS C 353 ? 0.1659 0.4577 0.1710 0.0413  -0.0086 -0.0544 353 HIS C CD2 
10223 C CE1 . HIS C 353 ? 0.1833 0.4911 0.1889 0.0509  -0.0109 -0.0652 353 HIS C CE1 
10224 N NE2 . HIS C 353 ? 0.1496 0.4458 0.1550 0.0436  -0.0090 -0.0575 353 HIS C NE2 
10225 N N   . ALA C 354 ? 0.1885 0.5307 0.1915 0.0475  -0.0078 -0.0573 354 ALA C N   
10226 C CA  . ALA C 354 ? 0.2185 0.5641 0.2208 0.0419  -0.0056 -0.0510 354 ALA C CA  
10227 C C   . ALA C 354 ? 0.1923 0.5506 0.1933 0.0455  -0.0031 -0.0536 354 ALA C C   
10228 O O   . ALA C 354 ? 0.2515 0.6144 0.2523 0.0521  -0.0035 -0.0605 354 ALA C O   
10229 C CB  . ALA C 354 ? 0.1924 0.5263 0.1950 0.0378  -0.0055 -0.0478 354 ALA C CB  
10230 N N   . VAL C 355 ? 0.1596 0.5230 0.1596 0.0410  -0.0006 -0.0482 355 VAL C N   
10231 C CA  . VAL C 355 ? 0.1925 0.5675 0.1911 0.0433  0.0023  -0.0492 355 VAL C CA  
10232 C C   . VAL C 355 ? 0.2229 0.5929 0.2196 0.0396  0.0036  -0.0455 355 VAL C C   
10233 O O   . VAL C 355 ? 0.1855 0.5490 0.1826 0.0332  0.0032  -0.0395 355 VAL C O   
10234 C CB  . VAL C 355 ? 0.1779 0.5622 0.1768 0.0413  0.0046  -0.0459 355 VAL C CB  
10235 C CG1 . VAL C 355 ? 0.1603 0.5559 0.1575 0.0429  0.0079  -0.0460 355 VAL C CG1 
10236 C CG2 . VAL C 355 ? 0.1531 0.5421 0.1537 0.0456  0.0038  -0.0499 355 VAL C CG2 
10237 N N   . PHE C 356 ? 0.1969 0.5718 0.1916 0.0439  0.0047  -0.0493 356 PHE C N   
10238 C CA  . PHE C 356 ? 0.2645 0.6389 0.2572 0.0418  0.0056  -0.0469 356 PHE C CA  
10239 C C   . PHE C 356 ? 0.2673 0.6554 0.2577 0.0425  0.0087  -0.0456 356 PHE C C   
10240 O O   . PHE C 356 ? 0.2780 0.6749 0.2673 0.0483  0.0098  -0.0504 356 PHE C O   
10241 C CB  . PHE C 356 ? 0.3282 0.6969 0.3199 0.0462  0.0042  -0.0524 356 PHE C CB  
10242 C CG  . PHE C 356 ? 0.2917 0.6462 0.2857 0.0450  0.0016  -0.0531 356 PHE C CG  
10243 C CD1 . PHE C 356 ? 0.2807 0.6342 0.2771 0.0481  -0.0007 -0.0571 356 PHE C CD1 
10244 C CD2 . PHE C 356 ? 0.3733 0.7189 0.3673 0.0412  0.0009  -0.0502 356 PHE C CD2 
10245 C CE1 . PHE C 356 ? 0.2967 0.6389 0.2954 0.0473  -0.0032 -0.0578 356 PHE C CE1 
10246 C CE2 . PHE C 356 ? 0.3272 0.6599 0.3236 0.0400  -0.0012 -0.0507 356 PHE C CE2 
10247 C CZ  . PHE C 356 ? 0.3441 0.6743 0.3428 0.0430  -0.0032 -0.0543 356 PHE C CZ  
10248 N N   . VAL C 357 ? 0.3119 0.7015 0.3015 0.0367  0.0100  -0.0392 357 VAL C N   
10249 C CA  . VAL C 357 ? 0.3611 0.7630 0.3487 0.0364  0.0133  -0.0368 357 VAL C CA  
10250 C C   . VAL C 357 ? 0.5020 0.9043 0.4864 0.0367  0.0143  -0.0362 357 VAL C C   
10251 O O   . VAL C 357 ? 0.5268 0.9195 0.5111 0.0331  0.0130  -0.0337 357 VAL C O   
10252 C CB  . VAL C 357 ? 0.3357 0.7390 0.3246 0.0297  0.0142  -0.0300 357 VAL C CB  
10253 C CG1 . VAL C 357 ? 0.3199 0.7357 0.3068 0.0294  0.0178  -0.0276 357 VAL C CG1 
10254 C CG2 . VAL C 357 ? 0.2956 0.6975 0.2875 0.0293  0.0130  -0.0305 357 VAL C CG2 
10255 N N   . ASP C 358 ? 0.4568 0.8703 0.4384 0.0411  0.0167  -0.0385 358 ASP C N   
10256 C CA  A ASP C 358 ? 0.5627 0.9781 0.5406 0.0417  0.0181  -0.0377 358 ASP C CA  
10257 C CA  B ASP C 358 ? 0.5626 0.9781 0.5405 0.0417  0.0181  -0.0377 358 ASP C CA  
10258 C C   . ASP C 358 ? 0.5879 1.0081 0.5645 0.0364  0.0208  -0.0308 358 ASP C C   
10259 O O   . ASP C 358 ? 0.5812 1.0124 0.5575 0.0371  0.0235  -0.0298 358 ASP C O   
10260 C CB  A ASP C 358 ? 0.5554 0.9801 0.5307 0.0494  0.0191  -0.0438 358 ASP C CB  
10261 C CB  B ASP C 358 ? 0.5558 0.9808 0.5311 0.0494  0.0192  -0.0437 358 ASP C CB  
10262 C CG  A ASP C 358 ? 0.6296 1.0567 0.6006 0.0505  0.0205  -0.0430 358 ASP C CG  
10263 C CG  B ASP C 358 ? 0.6281 1.0566 0.5990 0.0505  0.0209  -0.0428 358 ASP C CG  
10264 O OD1 A ASP C 358 ? 0.6569 1.0742 0.6273 0.0484  0.0190  -0.0421 358 ASP C OD1 
10265 O OD1 B ASP C 358 ? 0.6524 1.0728 0.6225 0.0462  0.0204  -0.0390 358 ASP C OD1 
10266 O OD2 A ASP C 358 ? 0.6383 1.0771 0.6067 0.0536  0.0233  -0.0434 358 ASP C OD2 
10267 O OD2 B ASP C 358 ? 0.6333 1.0727 0.6017 0.0557  0.0228  -0.0457 358 ASP C OD2 
10268 N N   . CYS C 359 ? 0.6199 1.0619 0.4432 0.1838  0.1253  0.0551  359 CYS C N   
10269 C CA  . CYS C 359 ? 0.6600 1.0853 0.4727 0.1957  0.1278  0.0701  359 CYS C CA  
10270 C C   . CYS C 359 ? 0.7640 1.1888 0.5493 0.2072  0.1273  0.0745  359 CYS C C   
10271 O O   . CYS C 359 ? 0.7129 1.1189 0.4881 0.2157  0.1316  0.0868  359 CYS C O   
10272 C CB  . CYS C 359 ? 0.6550 1.0905 0.4760 0.2036  0.1200  0.0751  359 CYS C CB  
10273 S SG  . CYS C 359 ? 0.5304 0.9581 0.3811 0.1911  0.1217  0.0746  359 CYS C SG  
10274 N N   . LYS C 360 ? 0.9112 1.3553 0.6841 0.2071  0.1221  0.0648  360 LYS C N   
10275 C CA  . LYS C 360 ? 0.9277 1.3705 0.6737 0.2166  0.1213  0.0688  360 LYS C CA  
10276 C C   . LYS C 360 ? 0.9392 1.3516 0.6744 0.2140  0.1341  0.0749  360 LYS C C   
10277 O O   . LYS C 360 ? 0.9722 1.3759 0.6865 0.2235  0.1350  0.0826  360 LYS C O   
10278 C CB  . LYS C 360 ? 0.9370 1.4036 0.6720 0.2133  0.1143  0.0561  360 LYS C CB  
10279 C CG  . LYS C 360 ? 0.9369 1.4351 0.6712 0.2223  0.0998  0.0539  360 LYS C CG  
10280 C CD  . LYS C 360 ? 0.9603 1.4797 0.6813 0.2181  0.0931  0.0423  360 LYS C CD  
10281 C CE  . LYS C 360 ? 0.9591 1.5124 0.6828 0.2258  0.0782  0.0396  360 LYS C CE  
10282 N NZ  . LYS C 360 ? 0.9881 1.5627 0.7014 0.2192  0.0711  0.0273  360 LYS C NZ  
10283 N N   . LYS C 361 ? 0.7634 1.1598 0.5132 0.2014  0.1441  0.0719  361 LYS C N   
10284 C CA  . LYS C 361 ? 0.8093 1.1778 0.5516 0.1980  0.1569  0.0773  361 LYS C CA  
10285 C C   . LYS C 361 ? 0.7816 1.1273 0.5320 0.2019  0.1622  0.0913  361 LYS C C   
10286 O O   . LYS C 361 ? 0.6760 1.0001 0.4144 0.2049  0.1702  0.0992  361 LYS C O   
10287 C CB  . LYS C 361 ? 0.7751 1.1378 0.5297 0.1824  0.1659  0.0672  361 LYS C CB  
10288 C CG  . LYS C 361 ? 0.7159 1.0994 0.4628 0.1769  0.1613  0.0525  361 LYS C CG  
10289 C CD  . LYS C 361 ? 0.7410 1.1180 0.5028 0.1614  0.1706  0.0424  361 LYS C CD  
10290 C CE  . LYS C 361 ? 0.7864 1.1344 0.5457 0.1570  0.1861  0.0479  361 LYS C CE  
10291 N NZ  . LYS C 361 ? 0.7846 1.1261 0.5596 0.1424  0.1962  0.0384  361 LYS C NZ  
10292 N N   . LEU C 362 ? 0.6910 1.0408 0.4608 0.2016  0.1580  0.0942  362 LEU C N   
10293 C CA  . LEU C 362 ? 0.7878 1.1159 0.5653 0.2042  0.1623  0.1071  362 LEU C CA  
10294 C C   . LEU C 362 ? 0.8226 1.1482 0.5833 0.2201  0.1579  0.1176  362 LEU C C   
10295 O O   . LEU C 362 ? 0.8106 1.1130 0.5673 0.2238  0.1638  0.1285  362 LEU C O   
10296 C CB  . LEU C 362 ? 0.7367 1.0689 0.5400 0.1967  0.1596  0.1061  362 LEU C CB  
10297 C CG  . LEU C 362 ? 0.6250 0.9580 0.4493 0.1805  0.1640  0.0970  362 LEU C CG  
10298 C CD1 . LEU C 362 ? 0.5399 0.8780 0.3879 0.1739  0.1596  0.0964  362 LEU C CD1 
10299 C CD2 . LEU C 362 ? 0.5211 0.8290 0.3487 0.1732  0.1764  0.1017  362 LEU C CD2 
10300 N N   . VAL C 363 ? 0.8584 1.2073 0.6100 0.2296  0.1475  0.1145  363 VAL C N   
10301 C CA  . VAL C 363 ? 0.7978 1.1463 0.5347 0.2455  0.1430  0.1244  363 VAL C CA  
10302 C C   . VAL C 363 ? 0.7750 1.1400 0.4898 0.2532  0.1371  0.1205  363 VAL C C   
10303 O O   . VAL C 363 ? 0.7835 1.1726 0.4957 0.2615  0.1268  0.1185  363 VAL C O   
10304 C CB  . VAL C 363 ? 0.7594 1.1198 0.5093 0.2511  0.1358  0.1270  363 VAL C CB  
10305 C CG1 . VAL C 363 ? 0.8364 1.1734 0.6015 0.2458  0.1424  0.1347  363 VAL C CG1 
10306 C CG2 . VAL C 363 ? 0.7154 1.1036 0.4788 0.2442  0.1283  0.1145  363 VAL C CG2 
10307 N N   . PRO C 364 ? 0.7971 1.1501 0.4956 0.2505  0.1433  0.1195  364 PRO C N   
10308 C CA  . PRO C 364 ? 0.8322 1.2000 0.5080 0.2564  0.1375  0.1158  364 PRO C CA  
10309 C C   . PRO C 364 ? 0.8766 1.2481 0.5389 0.2731  0.1311  0.1259  364 PRO C C   
10310 O O   . PRO C 364 ? 0.8549 1.2482 0.5049 0.2794  0.1218  0.1228  364 PRO C O   
10311 C CB  . PRO C 364 ? 0.6968 1.0436 0.3585 0.2493  0.1482  0.1146  364 PRO C CB  
10312 C CG  . PRO C 364 ? 0.8053 1.1340 0.4872 0.2372  0.1585  0.1138  364 PRO C CG  
10313 C CD  . PRO C 364 ? 0.7364 1.0619 0.4362 0.2415  0.1561  0.1218  364 PRO C CD  
10314 N N   . GLN C 365 ? 0.8922 1.2431 0.5574 0.2800  0.1357  0.1378  365 GLN C N   
10315 C CA  . GLN C 365 ? 0.8716 1.2229 0.5260 0.2961  0.1313  0.1481  365 GLN C CA  
10316 C C   . GLN C 365 ? 0.8330 1.2105 0.4975 0.3045  0.1208  0.1476  365 GLN C C   
10317 O O   . GLN C 365 ? 0.9437 1.3246 0.6010 0.3185  0.1170  0.1558  365 GLN C O   
10318 C CB  . GLN C 365 ? 0.8557 1.1762 0.5126 0.2995  0.1402  0.1598  365 GLN C CB  
10319 C CG  . GLN C 365 ? 0.8809 1.1969 0.5598 0.2984  0.1409  0.1634  365 GLN C CG  
10320 C CD  . GLN C 365 ? 0.8175 1.1282 0.5153 0.2822  0.1457  0.1569  365 GLN C CD  
10321 O OE1 . GLN C 365 ? 0.7787 1.0841 0.4744 0.2720  0.1508  0.1511  365 GLN C OE1 
10322 N NE2 . GLN C 365 ? 0.8225 1.1341 0.5392 0.2796  0.1445  0.1580  365 GLN C NE2 
10323 N N   . ILE C 366 ? 0.8910 1.2870 0.5727 0.2964  0.1166  0.1383  366 ILE C N   
10324 C CA  . ILE C 366 ? 0.8792 1.3015 0.5722 0.3030  0.1069  0.1366  366 ILE C CA  
10325 C C   . ILE C 366 ? 0.9135 1.3672 0.6034 0.2992  0.0974  0.1245  366 ILE C C   
10326 O O   . ILE C 366 ? 0.9300 1.3879 0.6272 0.2853  0.0988  0.1135  366 ILE C O   
10327 C CB  . ILE C 366 ? 0.7787 1.1967 0.4953 0.2960  0.1094  0.1356  366 ILE C CB  
10328 C CG1 . ILE C 366 ? 0.7469 1.1304 0.4661 0.2955  0.1198  0.1462  366 ILE C CG1 
10329 C CG2 . ILE C 366 ? 0.8145 1.2560 0.5412 0.3050  0.1009  0.1361  366 ILE C CG2 
10330 C CD1 . ILE C 366 ? 0.7488 1.1259 0.4895 0.2886  0.1220  0.1467  366 ILE C CD1 
10331 N N   . PRO C 367 ? 0.9804 1.4561 0.6604 0.3104  0.0880  0.1259  367 PRO C N   
10332 C CA  . PRO C 367 ? 0.9950 1.5024 0.6739 0.3058  0.0779  0.1140  367 PRO C CA  
10333 C C   . PRO C 367 ? 0.9294 1.4585 0.6317 0.3006  0.0727  0.1058  367 PRO C C   
10334 O O   . PRO C 367 ? 0.8801 1.4019 0.5978 0.3027  0.0757  0.1103  367 PRO C O   
10335 C CB  . PRO C 367 ? 0.9838 1.5073 0.6486 0.3205  0.0694  0.1206  367 PRO C CB  
10336 C CG  . PRO C 367 ? 0.9693 1.4770 0.6372 0.3340  0.0737  0.1346  367 PRO C CG  
10337 C CD  . PRO C 367 ? 0.9929 1.4653 0.6629 0.3272  0.0864  0.1385  367 PRO C CD  
10338 N N   . GLY C 368 ? 0.8420 1.3974 0.5462 0.2930  0.0647  0.0931  368 GLY C N   
10339 C CA  . GLY C 368 ? 0.7740 1.3507 0.5004 0.2864  0.0596  0.0834  368 GLY C CA  
10340 C C   . GLY C 368 ? 0.7687 1.3651 0.5059 0.2993  0.0525  0.0889  368 GLY C C   
10341 O O   . GLY C 368 ? 0.7167 1.3160 0.4728 0.2969  0.0531  0.0872  368 GLY C O   
10342 N N   . ASP C 369 ? 0.8039 1.4133 0.5294 0.3128  0.0460  0.0957  369 ASP C N   
10343 C CA  . ASP C 369 ? 0.7545 1.3834 0.4905 0.3258  0.0399  0.1012  369 ASP C CA  
10344 C C   . ASP C 369 ? 0.7488 1.3544 0.4907 0.3345  0.0484  0.1134  369 ASP C C   
10345 O O   . ASP C 369 ? 0.7684 1.3868 0.5218 0.3435  0.0456  0.1171  369 ASP C O   
10346 C CB  . ASP C 369 ? 0.7682 1.4138 0.4902 0.3376  0.0320  0.1065  369 ASP C CB  
10347 C CG  . ASP C 369 ? 0.8219 1.4409 0.5234 0.3458  0.0383  0.1188  369 ASP C CG  
10348 O OD1 . ASP C 369 ? 0.8658 1.4551 0.5617 0.3396  0.0482  0.1205  369 ASP C OD1 
10349 O OD2 . ASP C 369 ? 0.9479 1.5756 0.6396 0.3581  0.0335  0.1267  369 ASP C OD2 
10350 N N   . GLN C 370 ? 0.8400 1.4111 0.5744 0.3317  0.0589  0.1197  370 GLN C N   
10351 C CA  . GLN C 370 ? 0.8253 1.3706 0.5653 0.3372  0.0677  0.1306  370 GLN C CA  
10352 C C   . GLN C 370 ? 0.7767 1.3052 0.5314 0.3223  0.0744  0.1256  370 GLN C C   
10353 O O   . GLN C 370 ? 0.6893 1.1889 0.4461 0.3222  0.0833  0.1340  370 GLN C O   
10354 C CB  . GLN C 370 ? 0.8564 1.3736 0.5784 0.3452  0.0748  0.1426  370 GLN C CB  
10355 C CG  . GLN C 370 ? 0.9030 1.4331 0.6129 0.3616  0.0694  0.1503  370 GLN C CG  
10356 C CD  . GLN C 370 ? 0.9189 1.4696 0.6419 0.3726  0.0647  0.1534  370 GLN C CD  
10357 O OE1 . GLN C 370 ? 0.8799 1.4160 0.6120 0.3767  0.0710  0.1598  370 GLN C OE1 
10358 N NE2 . GLN C 370 ? 0.9240 1.5081 0.6478 0.3768  0.0539  0.1488  370 GLN C NE2 
10359 N N   . PHE C 371 ? 0.7325 1.2778 0.4978 0.3090  0.0703  0.1120  371 PHE C N   
10360 C CA  . PHE C 371 ? 0.7404 1.2766 0.5239 0.2945  0.0746  0.1058  371 PHE C CA  
10361 C C   . PHE C 371 ? 0.6987 1.1992 0.4797 0.2851  0.0858  0.1098  371 PHE C C   
10362 O O   . PHE C 371 ? 0.6446 1.1215 0.4318 0.2846  0.0927  0.1179  371 PHE C O   
10363 C CB  . PHE C 371 ? 0.7065 1.2450 0.5040 0.2999  0.0743  0.1104  371 PHE C CB  
10364 C CG  . PHE C 371 ? 0.6678 1.2369 0.4647 0.3143  0.0653  0.1115  371 PHE C CG  
10365 C CD1 . PHE C 371 ? 0.6348 1.2385 0.4347 0.3121  0.0550  0.1000  371 PHE C CD1 
10366 C CD2 . PHE C 371 ? 0.7469 1.3098 0.5408 0.3298  0.0675  0.1240  371 PHE C CD2 
10367 C CE1 . PHE C 371 ? 0.6281 1.2607 0.4292 0.3249  0.0466  0.1014  371 PHE C CE1 
10368 C CE2 . PHE C 371 ? 0.6912 1.2824 0.4860 0.3434  0.0599  0.1256  371 PHE C CE2 
10369 C CZ  . PHE C 371 ? 0.5917 1.2181 0.3907 0.3408  0.0492  0.1144  371 PHE C CZ  
10370 N N   . PRO C 372 ? 0.7082 1.2036 0.4805 0.2768  0.0883  0.1042  372 PRO C N   
10371 C CA  . PRO C 372 ? 0.6933 1.1563 0.4657 0.2672  0.0995  0.1076  372 PRO C CA  
10372 C C   . PRO C 372 ? 0.5998 1.0559 0.3943 0.2518  0.1032  0.1017  372 PRO C C   
10373 O O   . PRO C 372 ? 0.5624 0.9921 0.3633 0.2474  0.1111  0.1091  372 PRO C O   
10374 C CB  . PRO C 372 ? 0.6776 1.1411 0.4345 0.2629  0.1008  0.1018  372 PRO C CB  
10375 C CG  . PRO C 372 ? 0.7205 1.2181 0.4781 0.2618  0.0902  0.0901  372 PRO C CG  
10376 C CD  . PRO C 372 ? 0.6866 1.2046 0.4489 0.2747  0.0816  0.0942  372 PRO C CD  
10377 N N   . ALA C 373 ? 0.5115 0.9905 0.3183 0.2427  0.0973  0.0885  373 ALA C N   
10378 C CA  . ALA C 373 ? 0.5634 1.0364 0.3924 0.2274  0.1003  0.0824  373 ALA C CA  
10379 C C   . ALA C 373 ? 0.5708 1.0353 0.4118 0.2297  0.1008  0.0897  373 ALA C C   
10380 O O   . ALA C 373 ? 0.5966 1.0391 0.4495 0.2197  0.1075  0.0931  373 ALA C O   
10381 C CB  . ALA C 373 ? 0.5616 1.0622 0.4014 0.2182  0.0929  0.0665  373 ALA C CB  
10382 N N   . GLN C 374 ? 0.5504 1.0319 0.3884 0.2424  0.0941  0.0926  374 GLN C N   
10383 C CA  . GLN C 374 ? 0.4649 0.9371 0.3125 0.2450  0.0955  0.0995  374 GLN C CA  
10384 C C   . GLN C 374 ? 0.5429 0.9815 0.3823 0.2492  0.1046  0.1139  374 GLN C C   
10385 O O   . GLN C 374 ? 0.5532 0.9735 0.4028 0.2435  0.1090  0.1187  374 GLN C O   
10386 C CB  . GLN C 374 ? 0.5567 1.0543 0.4020 0.2593  0.0875  0.1002  374 GLN C CB  
10387 C CG  . GLN C 374 ? 0.4587 0.9480 0.3146 0.2610  0.0893  0.1056  374 GLN C CG  
10388 C CD  . GLN C 374 ? 0.5117 0.9979 0.3891 0.2428  0.0897  0.0965  374 GLN C CD  
10389 O OE1 . GLN C 374 ? 0.4560 0.9665 0.3451 0.2365  0.0826  0.0841  374 GLN C OE1 
10390 N NE2 . GLN C 374 ? 0.4255 0.8815 0.3085 0.2334  0.0977  0.1025  374 GLN C NE2 
10391 N N   . ALA C 375 ? 0.5508 0.9805 0.3717 0.2583  0.1073  0.1207  375 ALA C N   
10392 C CA  . ALA C 375 ? 0.5117 0.9087 0.3250 0.2613  0.1160  0.1334  375 ALA C CA  
10393 C C   . ALA C 375 ? 0.5832 0.9571 0.4065 0.2448  0.1238  0.1328  375 ALA C C   
10394 O O   . ALA C 375 ? 0.6716 1.0191 0.4974 0.2423  0.1303  0.1418  375 ALA C O   
10395 C CB  . ALA C 375 ? 0.6274 1.0209 0.4191 0.2742  0.1167  0.1397  375 ALA C CB  
10396 N N   . VAL C 376 ? 0.5311 0.9144 0.3609 0.2333  0.1233  0.1223  376 VAL C N   
10397 C CA  . VAL C 376 ? 0.5220 0.8865 0.3653 0.2172  0.1304  0.1212  376 VAL C CA  
10398 C C   . VAL C 376 ? 0.5083 0.8713 0.3722 0.2070  0.1294  0.1195  376 VAL C C   
10399 O O   . VAL C 376 ? 0.5279 0.8678 0.4006 0.1984  0.1355  0.1258  376 VAL C O   
10400 C CB  . VAL C 376 ? 0.5226 0.8976 0.3675 0.2082  0.1309  0.1101  376 VAL C CB  
10401 C CG1 . VAL C 376 ? 0.5351 0.8953 0.3987 0.1911  0.1375  0.1079  376 VAL C CG1 
10402 C CG2 . VAL C 376 ? 0.5901 0.9591 0.4136 0.2160  0.1343  0.1132  376 VAL C CG2 
10403 N N   . ILE C 377 ? 0.4948 0.8825 0.3665 0.2075  0.1214  0.1110  377 ILE C N   
10404 C CA  . ILE C 377 ? 0.4664 0.8539 0.3575 0.1970  0.1199  0.1079  377 ILE C CA  
10405 C C   . ILE C 377 ? 0.4801 0.8468 0.3691 0.2015  0.1236  0.1199  377 ILE C C   
10406 O O   . ILE C 377 ? 0.4728 0.8227 0.3746 0.1896  0.1274  0.1225  377 ILE C O   
10407 C CB  . ILE C 377 ? 0.4310 0.8499 0.3294 0.1980  0.1102  0.0960  377 ILE C CB  
10408 C CG1 . ILE C 377 ? 0.4401 0.8760 0.3431 0.1896  0.1072  0.0830  377 ILE C CG1 
10409 C CG2 . ILE C 377 ? 0.3975 0.8148 0.3141 0.1887  0.1086  0.0935  377 ILE C CG2 
10410 C CD1 . ILE C 377 ? 0.3898 0.8562 0.3015 0.1884  0.0974  0.0701  377 ILE C CD1 
10411 N N   . ASN C 378 ? 0.4425 0.8095 0.3152 0.2183  0.1229  0.1276  378 ASN C N   
10412 C CA  . ASN C 378 ? 0.4546 0.8000 0.3240 0.2231  0.1273  0.1389  378 ASN C CA  
10413 C C   . ASN C 378 ? 0.5689 0.8820 0.4355 0.2170  0.1358  0.1481  378 ASN C C   
10414 O O   . ASN C 378 ? 0.5353 0.8275 0.4082 0.2100  0.1399  0.1539  378 ASN C O   
10415 C CB  . ASN C 378 ? 0.5235 0.8773 0.3769 0.2432  0.1248  0.1449  378 ASN C CB  
10416 C CG  . ASN C 378 ? 0.6253 1.0102 0.4838 0.2493  0.1165  0.1372  378 ASN C CG  
10417 O OD1 . ASN C 378 ? 0.6152 1.0180 0.4874 0.2387  0.1117  0.1255  378 ASN C OD1 
10418 N ND2 . ASN C 378 ? 0.6517 1.0432 0.5002 0.2663  0.1150  0.1436  378 ASN C ND2 
10419 N N   . ALA C 379 ? 0.5744 0.8830 0.4317 0.2189  0.1385  0.1493  379 ALA C N   
10420 C CA  . ALA C 379 ? 0.5827 0.8626 0.4397 0.2119  0.1464  0.1568  379 ALA C CA  
10421 C C   . ALA C 379 ? 0.5512 0.8243 0.4284 0.1926  0.1487  0.1531  379 ALA C C   
10422 O O   . ALA C 379 ? 0.5194 0.7697 0.4032 0.1843  0.1531  0.1598  379 ALA C O   
10423 C CB  . ALA C 379 ? 0.4874 0.7656 0.3306 0.2177  0.1491  0.1576  379 ALA C CB  
10424 N N   . LEU C 380 ? 0.5012 0.7942 0.3889 0.1848  0.1453  0.1421  380 LEU C N   
10425 C CA  . LEU C 380 ? 0.5365 0.8259 0.4456 0.1666  0.1465  0.1378  380 LEU C CA  
10426 C C   . LEU C 380 ? 0.4933 0.7754 0.4125 0.1605  0.1450  0.1405  380 LEU C C   
10427 O O   . LEU C 380 ? 0.4256 0.6900 0.3570 0.1472  0.1483  0.1445  380 LEU C O   
10428 C CB  . LEU C 380 ? 0.4955 0.8100 0.4143 0.1607  0.1418  0.1240  380 LEU C CB  
10429 C CG  . LEU C 380 ? 0.4375 0.7506 0.3801 0.1421  0.1420  0.1183  380 LEU C CG  
10430 C CD1 . LEU C 380 ? 0.4586 0.7497 0.4073 0.1330  0.1497  0.1248  380 LEU C CD1 
10431 C CD2 . LEU C 380 ? 0.3784 0.7164 0.3301 0.1372  0.1367  0.1036  380 LEU C CD2 
10432 N N   . TYR C 381 ? 0.4801 0.7753 0.3941 0.1698  0.1402  0.1386  381 TYR C N   
10433 C CA  . TYR C 381 ? 0.4293 0.7169 0.3512 0.1642  0.1397  0.1407  381 TYR C CA  
10434 C C   . TYR C 381 ? 0.5378 0.7946 0.4526 0.1645  0.1458  0.1533  381 TYR C C   
10435 O O   . TYR C 381 ? 0.5066 0.7468 0.4321 0.1508  0.1478  0.1559  381 TYR C O   
10436 C CB  . TYR C 381 ? 0.4364 0.7444 0.3540 0.1756  0.1340  0.1363  381 TYR C CB  
10437 C CG  . TYR C 381 ? 0.4810 0.7769 0.4037 0.1710  0.1354  0.1397  381 TYR C CG  
10438 C CD1 . TYR C 381 ? 0.4240 0.7223 0.3648 0.1548  0.1335  0.1332  381 TYR C CD1 
10439 C CD2 . TYR C 381 ? 0.4844 0.7642 0.3937 0.1820  0.1390  0.1495  381 TYR C CD2 
10440 C CE1 . TYR C 381 ? 0.4206 0.7061 0.3649 0.1493  0.1353  0.1360  381 TYR C CE1 
10441 C CE2 . TYR C 381 ? 0.5045 0.7707 0.4174 0.1768  0.1413  0.1523  381 TYR C CE2 
10442 C CZ  . TYR C 381 ? 0.4766 0.7457 0.4064 0.1603  0.1395  0.1455  381 TYR C CZ  
10443 O OH  . TYR C 381 ? 0.5098 0.7643 0.4418 0.1541  0.1420  0.1479  381 TYR C OH  
10444 N N   . LEU C 382 ? 0.5599 0.8084 0.4569 0.1793  0.1482  0.1606  382 LEU C N   
10445 C CA  . LEU C 382 ? 0.5575 0.7763 0.4476 0.1798  0.1537  0.1711  382 LEU C CA  
10446 C C   . LEU C 382 ? 0.5797 0.7783 0.4787 0.1651  0.1578  0.1744  382 LEU C C   
10447 O O   . LEU C 382 ? 0.5569 0.7327 0.4592 0.1566  0.1604  0.1796  382 LEU C O   
10448 C CB  . LEU C 382 ? 0.6381 0.8529 0.5086 0.1984  0.1555  0.1773  382 LEU C CB  
10449 C CG  . LEU C 382 ? 0.5862 0.8152 0.4465 0.2151  0.1524  0.1776  382 LEU C CG  
10450 C CD1 . LEU C 382 ? 0.5959 0.8146 0.4384 0.2313  0.1553  0.1855  382 LEU C CD1 
10451 C CD2 . LEU C 382 ? 0.6158 0.8364 0.4819 0.2109  0.1531  0.1788  382 LEU C CD2 
10452 N N   . GLU C 383 ? 0.5659 0.7725 0.4692 0.1615  0.1583  0.1709  383 GLU C N   
10453 C CA  . GLU C 383 ? 0.5999 0.7888 0.5127 0.1488  0.1624  0.1743  383 GLU C CA  
10454 C C   . GLU C 383 ? 0.6377 0.8275 0.5720 0.1300  0.1603  0.1702  383 GLU C C   
10455 O O   . GLU C 383 ? 0.6897 0.8620 0.6338 0.1179  0.1624  0.1741  383 GLU C O   
10456 C CB  . GLU C 383 ? 0.6638 0.8587 0.5720 0.1529  0.1651  0.1727  383 GLU C CB  
10457 C CG  . GLU C 383 ? 0.7013 0.8745 0.6138 0.1453  0.1707  0.1787  383 GLU C CG  
10458 C CD  . GLU C 383 ? 0.7838 0.9348 0.6831 0.1525  0.1739  0.1874  383 GLU C CD  
10459 O OE1 . GLU C 383 ? 0.8229 0.9766 0.7067 0.1667  0.1729  0.1890  383 GLU C OE1 
10460 O OE2 . GLU C 383 ? 0.8525 0.9840 0.7580 0.1440  0.1772  0.1921  383 GLU C OE2 
10461 N N   . SER C 384 ? 0.5077 0.7179 0.4502 0.1271  0.1556  0.1621  384 SER C N   
10462 C CA  . SER C 384 ? 0.5561 0.7697 0.5200 0.1093  0.1532  0.1568  384 SER C CA  
10463 C C   . SER C 384 ? 0.4653 0.6868 0.4368 0.1035  0.1486  0.1520  384 SER C C   
10464 O O   . SER C 384 ? 0.4734 0.6898 0.4614 0.0872  0.1466  0.1500  384 SER C O   
10465 C CB  . SER C 384 ? 0.4611 0.6940 0.4336 0.1070  0.1523  0.1480  384 SER C CB  
10466 O OG  . SER C 384 ? 0.4224 0.6801 0.3873 0.1181  0.1484  0.1397  384 SER C OG  
10467 N N   . GLY C 385 ? 0.4675 0.7010 0.4281 0.1159  0.1465  0.1498  385 GLY C N   
10468 C CA  . GLY C 385 ? 0.4060 0.6507 0.3751 0.1107  0.1423  0.1434  385 GLY C CA  
10469 C C   . GLY C 385 ? 0.3987 0.6706 0.3810 0.1065  0.1369  0.1304  385 GLY C C   
10470 O O   . GLY C 385 ? 0.3677 0.6507 0.3583 0.1020  0.1328  0.1235  385 GLY C O   
10471 N N   . VAL C 386 ? 0.3838 0.6652 0.3682 0.1073  0.1370  0.1263  386 VAL C N   
10472 C CA  . VAL C 386 ? 0.3102 0.6160 0.3058 0.1033  0.1317  0.1128  386 VAL C CA  
10473 C C   . VAL C 386 ? 0.3344 0.6634 0.3183 0.1189  0.1269  0.1065  386 VAL C C   
10474 O O   . VAL C 386 ? 0.3672 0.6961 0.3330 0.1340  0.1286  0.1119  386 VAL C O   
10475 C CB  . VAL C 386 ? 0.3391 0.6440 0.3394 0.0988  0.1346  0.1109  386 VAL C CB  
10476 C CG1 . VAL C 386 ? 0.3001 0.6291 0.3086 0.0964  0.1295  0.0963  386 VAL C CG1 
10477 C CG2 . VAL C 386 ? 0.3302 0.6140 0.3455 0.0827  0.1381  0.1166  386 VAL C CG2 
10478 N N   . ARG C 387 ? 0.3051 0.6539 0.2993 0.1150  0.1201  0.0949  387 ARG C N   
10479 C CA  . ARG C 387 ? 0.3113 0.6846 0.2973 0.1282  0.1138  0.0878  387 ARG C CA  
10480 C C   . ARG C 387 ? 0.3052 0.6995 0.2970 0.1249  0.1087  0.0749  387 ARG C C   
10481 O O   . ARG C 387 ? 0.2876 0.6859 0.2964 0.1107  0.1058  0.0657  387 ARG C O   
10482 C CB  . ARG C 387 ? 0.3027 0.6827 0.2954 0.1270  0.1096  0.0839  387 ARG C CB  
10483 C CG  . ARG C 387 ? 0.3229 0.7311 0.3123 0.1378  0.1016  0.0746  387 ARG C CG  
10484 C CD  . ARG C 387 ? 0.3315 0.7417 0.3218 0.1425  0.1000  0.0754  387 ARG C CD  
10485 N NE  . ARG C 387 ? 0.2857 0.6936 0.2939 0.1264  0.0978  0.0680  387 ARG C NE  
10486 C CZ  . ARG C 387 ? 0.2831 0.6924 0.2950 0.1272  0.0967  0.0665  387 ARG C CZ  
10487 N NH1 . ARG C 387 ? 0.2982 0.7114 0.2983 0.1436  0.0977  0.0721  387 ARG C NH1 
10488 N NH2 . ARG C 387 ? 0.2659 0.6716 0.2935 0.1113  0.0948  0.0595  387 ARG C NH2 
10489 N N   . ALA C 388 ? 0.3211 0.7274 0.2977 0.1377  0.1077  0.0742  388 ALA C N   
10490 C CA  . ALA C 388 ? 0.3197 0.7473 0.2976 0.1363  0.1028  0.0619  388 ALA C CA  
10491 C C   . ALA C 388 ? 0.3280 0.7827 0.2986 0.1483  0.0942  0.0557  388 ALA C C   
10492 O O   . ALA C 388 ? 0.3313 0.7873 0.2961 0.1585  0.0928  0.0616  388 ALA C O   
10493 C CB  . ALA C 388 ? 0.3345 0.7556 0.3005 0.1400  0.1085  0.0654  388 ALA C CB  
10494 N N   . VAL C 389 ? 0.3246 0.8011 0.2958 0.1468  0.0885  0.0438  389 VAL C N   
10495 C CA  . VAL C 389 ? 0.3299 0.8354 0.2953 0.1570  0.0794  0.0370  389 VAL C CA  
10496 C C   . VAL C 389 ? 0.3482 0.8671 0.2966 0.1660  0.0787  0.0356  389 VAL C C   
10497 O O   . VAL C 389 ? 0.3498 0.8620 0.2974 0.1583  0.0828  0.0320  389 VAL C O   
10498 C CB  . VAL C 389 ? 0.3112 0.8331 0.2939 0.1451  0.0714  0.0225  389 VAL C CB  
10499 C CG1 . VAL C 389 ? 0.3036 0.8262 0.2940 0.1313  0.0719  0.0121  389 VAL C CG1 
10500 C CG2 . VAL C 389 ? 0.3162 0.8686 0.2944 0.1558  0.0619  0.0166  389 VAL C CG2 
10501 N N   . GLU C 390 ? 0.3635 0.8999 0.2977 0.1825  0.0740  0.0390  390 GLU C N   
10502 C CA  . GLU C 390 ? 0.4218 0.9692 0.3366 0.1926  0.0732  0.0398  390 GLU C CA  
10503 C C   . GLU C 390 ? 0.3826 0.9623 0.2992 0.1901  0.0639  0.0254  390 GLU C C   
10504 O O   . GLU C 390 ? 0.4014 1.0045 0.3247 0.1937  0.0557  0.0204  390 GLU C O   
10505 C CB  . GLU C 390 ? 0.4380 0.9862 0.3357 0.2121  0.0731  0.0526  390 GLU C CB  
10506 C CG  . GLU C 390 ? 0.4297 0.9785 0.3049 0.2221  0.0744  0.0572  390 GLU C CG  
10507 C CD  . GLU C 390 ? 0.5360 1.1194 0.4023 0.2311  0.0643  0.0508  390 GLU C CD  
10508 O OE1 . GLU C 390 ? 0.4578 1.0664 0.3364 0.2297  0.0564  0.0422  390 GLU C OE1 
10509 O OE2 . GLU C 390 ? 0.5281 1.1130 0.3753 0.2392  0.0641  0.0545  390 GLU C OE2 
10510 N N   . ILE C 391 ? 0.4876 1.0681 0.3982 0.1835  0.0657  0.0188  391 ILE C N   
10511 C CA  . ILE C 391 ? 0.5798 1.1897 0.4880 0.1813  0.0576  0.0056  391 ILE C CA  
10512 C C   . ILE C 391 ? 0.6036 1.2196 0.4874 0.1927  0.0572  0.0098  391 ILE C C   
10513 O O   . ILE C 391 ? 0.6050 1.2072 0.4790 0.1874  0.0633  0.0087  391 ILE C O   
10514 C CB  . ILE C 391 ? 0.5587 1.1641 0.4795 0.1627  0.0597  -0.0071 391 ILE C CB  
10515 C CG1 . ILE C 391 ? 0.3535 0.9490 0.2978 0.1508  0.0599  -0.0100 391 ILE C CG1 
10516 C CG2 . ILE C 391 ? 0.4641 1.0991 0.3815 0.1596  0.0515  -0.0211 391 ILE C CG2 
10517 C CD1 . ILE C 391 ? 0.3526 0.9673 0.3059 0.1553  0.0509  -0.0122 391 ILE C CD1 
10518 N N   . GLY C 392 ? 0.4978 1.1333 0.3718 0.2082  0.0502  0.0151  392 GLY C N   
10519 C CA  . GLY C 392 ? 0.5242 1.1637 0.3749 0.2193  0.0490  0.0206  392 GLY C CA  
10520 C C   . GLY C 392 ? 0.5857 1.2497 0.4298 0.2361  0.0401  0.0262  392 GLY C C   
10521 O O   . GLY C 392 ? 0.5319 1.2222 0.3890 0.2369  0.0321  0.0199  392 GLY C O   
10522 N N   . SER C 393 ? 0.6263 1.2810 0.4510 0.2495  0.0418  0.0384  393 SER C N   
10523 C CA  . SER C 393 ? 0.5349 1.2115 0.3521 0.2660  0.0337  0.0450  393 SER C CA  
10524 C C   . SER C 393 ? 0.4948 1.1777 0.3257 0.2751  0.0326  0.0510  393 SER C C   
10525 O O   . SER C 393 ? 0.4984 1.2079 0.3318 0.2855  0.0244  0.0519  393 SER C O   
10526 C CB  . SER C 393 ? 0.6161 1.2754 0.4106 0.2774  0.0373  0.0577  393 SER C CB  
10527 O OG  . SER C 393 ? 0.5558 1.2155 0.3350 0.2708  0.0363  0.0517  393 SER C OG  
10528 N N   . PHE C 394 ? 0.4800 1.1376 0.3201 0.2708  0.0411  0.0556  394 PHE C N   
10529 C CA  . PHE C 394 ? 0.4685 1.1294 0.3215 0.2770  0.0411  0.0601  394 PHE C CA  
10530 C C   . PHE C 394 ? 0.5362 1.2228 0.4094 0.2672  0.0343  0.0458  394 PHE C C   
10531 O O   . PHE C 394 ? 0.4978 1.2035 0.3792 0.2755  0.0300  0.0468  394 PHE C O   
10532 C CB  . PHE C 394 ? 0.4600 1.0826 0.3165 0.2731  0.0524  0.0691  394 PHE C CB  
10533 C CG  . PHE C 394 ? 0.5686 1.1864 0.4316 0.2826  0.0546  0.0781  394 PHE C CG  
10534 C CD1 . PHE C 394 ? 0.5691 1.1998 0.4222 0.3023  0.0519  0.0880  394 PHE C CD1 
10535 C CD2 . PHE C 394 ? 0.4747 1.0727 0.3539 0.2713  0.0598  0.0770  394 PHE C CD2 
10536 C CE1 . PHE C 394 ? 0.4703 1.0950 0.3289 0.3112  0.0554  0.0963  394 PHE C CE1 
10537 C CE2 . PHE C 394 ? 0.5864 1.1767 0.4708 0.2786  0.0626  0.0847  394 PHE C CE2 
10538 C CZ  . PHE C 394 ? 0.4987 1.1022 0.3728 0.2990  0.0610  0.0943  394 PHE C CZ  
10539 N N   . LEU C 395 ? 0.4658 1.1526 0.3475 0.2495  0.0338  0.0325  395 LEU C N   
10540 C CA  . LEU C 395 ? 0.4535 1.1645 0.3539 0.2391  0.0266  0.0179  395 LEU C CA  
10541 C C   . LEU C 395 ? 0.4955 1.2450 0.3917 0.2434  0.0158  0.0097  395 LEU C C   
10542 O O   . LEU C 395 ? 0.4660 1.2436 0.3753 0.2437  0.0083  0.0022  395 LEU C O   
10543 C CB  . LEU C 395 ? 0.5028 1.1965 0.4150 0.2180  0.0305  0.0074  395 LEU C CB  
10544 C CG  . LEU C 395 ? 0.5071 1.2221 0.4377 0.2046  0.0230  -0.0090 395 LEU C CG  
10545 C CD1 . LEU C 395 ? 0.5777 1.2660 0.5255 0.1869  0.0280  -0.0133 395 LEU C CD1 
10546 C CD2 . LEU C 395 ? 0.5289 1.2656 0.4541 0.1985  0.0177  -0.0211 395 LEU C CD2 
10547 N N   . LEU C 396 ? 0.6162 1.3658 0.4949 0.2454  0.0148  0.0107  396 LEU C N   
10548 C CA  . LEU C 396 ? 0.6187 1.3997 0.4943 0.2459  0.0048  0.0024  396 LEU C CA  
10549 C C   . LEU C 396 ? 0.6186 1.4241 0.4973 0.2613  -0.0022 0.0083  396 LEU C C   
10550 O O   . LEU C 396 ? 0.6466 1.4788 0.5398 0.2580  -0.0089 -0.0012 396 LEU C O   
10551 C CB  . LEU C 396 ? 0.6706 1.4408 0.5244 0.2453  0.0063  0.0046  396 LEU C CB  
10552 C CG  . LEU C 396 ? 0.7458 1.5417 0.5946 0.2405  -0.0026 -0.0055 396 LEU C CG  
10553 C CD1 . LEU C 396 ? 0.7260 1.5370 0.5925 0.2236  -0.0057 -0.0230 396 LEU C CD1 
10554 C CD2 . LEU C 396 ? 0.7890 1.5684 0.6141 0.2385  0.0006  -0.0030 396 LEU C CD2 
10555 N N   . GLY C 397 ? 0.5323 1.3261 0.3986 0.2775  0.0006  0.0241  397 GLY C N   
10556 C CA  . GLY C 397 ? 0.4819 1.2916 0.3518 0.2923  -0.0036 0.0317  397 GLY C CA  
10557 C C   . GLY C 397 ? 0.6112 1.4310 0.4661 0.3013  -0.0092 0.0373  397 GLY C C   
10558 O O   . GLY C 397 ? 0.6115 1.4245 0.4505 0.2974  -0.0096 0.0365  397 GLY C O   
10559 N N   . ARG C 398 ? 0.5532 1.3873 0.4128 0.3129  -0.0132 0.0434  398 ARG C N   
10560 C CA  . ARG C 398 ? 0.6239 1.4714 0.4720 0.3212  -0.0200 0.0489  398 ARG C CA  
10561 C C   . ARG C 398 ? 0.5605 1.4377 0.4166 0.3107  -0.0299 0.0355  398 ARG C C   
10562 O O   . ARG C 398 ? 0.5442 1.4337 0.4182 0.3023  -0.0314 0.0249  398 ARG C O   
10563 C CB  . ARG C 398 ? 0.6289 1.4749 0.4779 0.3386  -0.0190 0.0633  398 ARG C CB  
10564 C CG  . ARG C 398 ? 0.6751 1.4909 0.5118 0.3507  -0.0093 0.0787  398 ARG C CG  
10565 C CD  . ARG C 398 ? 0.6242 1.4376 0.4621 0.3674  -0.0076 0.0925  398 ARG C CD  
10566 N NE  . ARG C 398 ? 0.7341 1.5162 0.5612 0.3777  0.0029  0.1064  398 ARG C NE  
10567 C CZ  . ARG C 398 ? 0.8052 1.5733 0.6138 0.3864  0.0051  0.1170  398 ARG C CZ  
10568 N NH1 . ARG C 398 ? 0.6918 1.4746 0.4896 0.3867  -0.0028 0.1163  398 ARG C NH1 
10569 N NH2 . ARG C 398 ? 0.8421 1.5793 0.6424 0.3941  0.0157  0.1286  398 ARG C NH2 
10570 N N   . LYS C 406 ? 0.6595 1.4745 0.4598 0.3016  -0.0168 0.0425  406 LYS C N   
10571 C CA  . LYS C 406 ? 0.7097 1.5290 0.5070 0.2841  -0.0187 0.0279  406 LYS C CA  
10572 C C   . LYS C 406 ? 0.7677 1.5547 0.5492 0.2781  -0.0090 0.0294  406 LYS C C   
10573 O O   . LYS C 406 ? 0.7300 1.4935 0.5155 0.2794  0.0001  0.0346  406 LYS C O   
10574 C CB  . LYS C 406 ? 0.7017 1.5363 0.5226 0.2719  -0.0203 0.0136  406 LYS C CB  
10575 C CG  . LYS C 406 ? 0.7316 1.5802 0.5532 0.2547  -0.0250 -0.0026 406 LYS C CG  
10576 C CD  . LYS C 406 ? 0.7073 1.5875 0.5331 0.2554  -0.0361 -0.0068 406 LYS C CD  
10577 C CE  . LYS C 406 ? 0.5818 1.4763 0.4141 0.2370  -0.0399 -0.0243 406 LYS C CE  
10578 N NZ  . LYS C 406 ? 0.5565 1.4506 0.4114 0.2271  -0.0357 -0.0348 406 LYS C NZ  
10579 N N   . HIS C 407 ? 0.7561 1.5403 0.5192 0.2707  -0.0104 0.0251  407 HIS C N   
10580 C CA  . HIS C 407 ? 0.8599 1.6129 0.6069 0.2639  -0.0004 0.0257  407 HIS C CA  
10581 C C   . HIS C 407 ? 0.8524 1.5969 0.6129 0.2476  0.0057  0.0132  407 HIS C C   
10582 O O   . HIS C 407 ? 0.8418 1.6032 0.6092 0.2349  0.0011  -0.0008 407 HIS C O   
10583 C CB  . HIS C 407 ? 0.7797 1.5327 0.5022 0.2598  -0.0035 0.0237  407 HIS C CB  
10584 C CG  . HIS C 407 ? 0.9065 1.6290 0.6128 0.2503  0.0073  0.0217  407 HIS C CG  
10585 N ND1 . HIS C 407 ? 0.9452 1.6636 0.6546 0.2329  0.0113  0.0075  407 HIS C ND1 
10586 C CD2 . HIS C 407 ? 0.9696 1.6632 0.6571 0.2555  0.0159  0.0319  407 HIS C CD2 
10587 C CE1 . HIS C 407 ? 1.0056 1.6939 0.6989 0.2282  0.0223  0.0094  407 HIS C CE1 
10588 N NE2 . HIS C 407 ? 0.9941 1.6670 0.6738 0.2415  0.0251  0.0239  407 HIS C NE2 
10589 N N   . ALA C 408 ? 0.8388 1.5560 0.6038 0.2474  0.0164  0.0185  408 ALA C N   
10590 C CA  . ALA C 408 ? 0.8861 1.5907 0.6640 0.2319  0.0236  0.0085  408 ALA C CA  
10591 C C   . ALA C 408 ? 1.0051 1.6848 0.7658 0.2223  0.0326  0.0060  408 ALA C C   
10592 O O   . ALA C 408 ? 0.9753 1.6323 0.7190 0.2293  0.0391  0.0168  408 ALA C O   
10593 C CB  . ALA C 408 ? 0.7074 1.3946 0.5009 0.2348  0.0306  0.0156  408 ALA C CB  
10594 N N   . ASP C 409 ? 1.2018 1.8850 0.9670 0.2063  0.0336  -0.0085 409 ASP C N   
10595 C CA  . ASP C 409 ? 1.2171 1.8765 0.9675 0.1959  0.0436  -0.0123 409 ASP C CA  
10596 C C   . ASP C 409 ? 1.2037 1.8309 0.9622 0.1918  0.0573  -0.0076 409 ASP C C   
10597 O O   . ASP C 409 ? 1.2253 1.8284 0.9706 0.1864  0.0677  -0.0071 409 ASP C O   
10598 C CB  . ASP C 409 ? 1.2267 1.8993 0.9802 0.1799  0.0410  -0.0294 409 ASP C CB  
10599 C CG  . ASP C 409 ? 1.2388 1.9355 0.9767 0.1811  0.0299  -0.0337 409 ASP C CG  
10600 O OD1 . ASP C 409 ? 1.2557 1.9594 0.9812 0.1947  0.0240  -0.0231 409 ASP C OD1 
10601 O OD2 . ASP C 409 ? 1.2411 1.9488 0.9796 0.1681  0.0273  -0.0473 409 ASP C OD2 
10602 N N   . MET C 410 ? 0.9826 1.6083 0.7625 0.1937  0.0580  -0.0039 410 MET C N   
10603 C CA  . MET C 410 ? 0.8648 1.4607 0.6552 0.1886  0.0702  0.0010  410 MET C CA  
10604 C C   . MET C 410 ? 0.7453 1.3377 0.5475 0.1988  0.0692  0.0124  410 MET C C   
10605 O O   . MET C 410 ? 0.7090 1.3246 0.5208 0.2045  0.0597  0.0114  410 MET C O   
10606 C CB  . MET C 410 ? 0.9069 1.5008 0.7166 0.1713  0.0741  -0.0119 410 MET C CB  
10607 C CG  . MET C 410 ? 0.8742 1.4930 0.7060 0.1677  0.0644  -0.0201 410 MET C CG  
10608 S SD  . MET C 410 ? 0.8696 1.5005 0.7135 0.1487  0.0629  -0.0398 410 MET C SD  
10609 C CE  . MET C 410 ? 0.7712 1.4171 0.5879 0.1501  0.0579  -0.0457 410 MET C CE  
10610 N N   . GLU C 411 ? 0.7450 1.3074 0.5461 0.2007  0.0796  0.0235  411 GLU C N   
10611 C CA  . GLU C 411 ? 0.7713 1.3232 0.5831 0.2079  0.0811  0.0347  411 GLU C CA  
10612 C C   . GLU C 411 ? 0.7837 1.3144 0.6153 0.1942  0.0900  0.0332  411 GLU C C   
10613 O O   . GLU C 411 ? 0.6422 1.1452 0.4706 0.1916  0.1005  0.0403  411 GLU C O   
10614 C CB  . GLU C 411 ? 0.6419 1.1762 0.4354 0.2221  0.0850  0.0502  411 GLU C CB  
10615 C CG  . GLU C 411 ? 0.6554 1.2091 0.4295 0.2355  0.0763  0.0529  411 GLU C CG  
10616 C CD  . GLU C 411 ? 0.6298 1.2101 0.4124 0.2457  0.0656  0.0540  411 GLU C CD  
10617 O OE1 . GLU C 411 ? 0.5671 1.1426 0.3650 0.2473  0.0670  0.0584  411 GLU C OE1 
10618 O OE2 . GLU C 411 ? 0.7034 1.3091 0.4773 0.2517  0.0561  0.0507  411 GLU C OE2 
10619 N N   . PHE C 412 ? 0.8660 1.4948 0.8319 0.1897  0.0308  0.1096  412 PHE C N   
10620 C CA  . PHE C 412 ? 0.8418 1.4464 0.8093 0.1784  0.0268  0.0967  412 PHE C CA  
10621 C C   . PHE C 412 ? 0.8290 1.4076 0.7993 0.1771  0.0302  0.1058  412 PHE C C   
10622 O O   . PHE C 412 ? 0.8347 1.4106 0.8054 0.1825  0.0349  0.1174  412 PHE C O   
10623 C CB  . PHE C 412 ? 0.8542 1.4543 0.8210 0.1687  0.0197  0.0724  412 PHE C CB  
10624 C CG  . PHE C 412 ? 0.9083 1.5234 0.8751 0.1650  0.0154  0.0593  412 PHE C CG  
10625 C CD1 . PHE C 412 ? 0.8412 1.4822 0.8064 0.1723  0.0174  0.0679  412 PHE C CD1 
10626 C CD2 . PHE C 412 ? 0.8738 1.4774 0.8428 0.1543  0.0098  0.0389  412 PHE C CD2 
10627 C CE1 . PHE C 412 ? 0.8432 1.4993 0.8086 0.1685  0.0136  0.0554  412 PHE C CE1 
10628 C CE2 . PHE C 412 ? 0.8695 1.4865 0.8395 0.1506  0.0065  0.0273  412 PHE C CE2 
10629 C CZ  . PHE C 412 ? 0.9179 1.5615 0.8860 0.1575  0.0083  0.0350  412 PHE C CZ  
10630 N N   . MET C 413 ? 0.5167 1.0770 0.4879 0.1697  0.0278  0.1007  413 MET C N   
10631 C CA  . MET C 413 ? 0.3321 0.8672 0.3039 0.1658  0.0290  0.1039  413 MET C CA  
10632 C C   . MET C 413 ? 0.2911 0.8119 0.2612 0.1538  0.0221  0.0824  413 MET C C   
10633 O O   . MET C 413 ? 0.2433 0.7658 0.2136 0.1490  0.0196  0.0741  413 MET C O   
10634 C CB  . MET C 413 ? 0.3215 0.8439 0.2961 0.1676  0.0387  0.1203  413 MET C CB  
10635 C CG  . MET C 413 ? 0.2614 0.7511 0.2440 0.1580  0.0449  0.1154  413 MET C CG  
10636 S SD  . MET C 413 ? 0.3405 0.8117 0.3337 0.1583  0.0598  0.1323  413 MET C SD  
10637 C CE  . MET C 413 ? 0.3687 0.8446 0.3514 0.1543  0.0578  0.1268  413 MET C CE  
10638 N N   . ARG C 414 ? 0.2832 0.7911 0.2524 0.1491  0.0197  0.0736  414 ARG C N   
10639 C CA  . ARG C 414 ? 0.2266 0.7203 0.1960 0.1381  0.0140  0.0540  414 ARG C CA  
10640 C C   . ARG C 414 ? 0.2279 0.6922 0.2063 0.1306  0.0210  0.0535  414 ARG C C   
10641 O O   . ARG C 414 ? 0.2190 0.6712 0.2066 0.1313  0.0263  0.0593  414 ARG C O   
10642 C CB  . ARG C 414 ? 0.2238 0.7151 0.1916 0.1347  0.0099  0.0410  414 ARG C CB  
10643 C CG  . ARG C 414 ? 0.2403 0.7164 0.2103 0.1237  0.0047  0.0219  414 ARG C CG  
10644 C CD  . ARG C 414 ? 0.2087 0.6821 0.1782 0.1206  0.0016  0.0096  414 ARG C CD  
10645 N NE  . ARG C 414 ? 0.2580 0.7223 0.2301 0.1214  0.0035  0.0127  414 ARG C NE  
10646 C CZ  . ARG C 414 ? 0.3580 0.8140 0.3332 0.1167  0.0009  0.0010  414 ARG C CZ  
10647 N NH1 . ARG C 414 ? 0.3294 0.7864 0.3027 0.1117  -0.0034 -0.0138 414 ARG C NH1 
10648 N NH2 . ARG C 414 ? 0.2760 0.7173 0.2636 0.1157  0.0038  0.0040  414 ARG C NH2 
10649 N N   . LEU C 415 ? 0.2140 0.6673 0.1926 0.1233  0.0210  0.0459  415 LEU C N   
10650 C CA  . LEU C 415 ? 0.2061 0.6334 0.1930 0.1150  0.0260  0.0416  415 LEU C CA  
10651 C C   . LEU C 415 ? 0.1944 0.6127 0.1807 0.1069  0.0190  0.0241  415 LEU C C   
10652 O O   . LEU C 415 ? 0.1901 0.6087 0.1730 0.1022  0.0143  0.0142  415 LEU C O   
10653 C CB  . LEU C 415 ? 0.2087 0.6301 0.1958 0.1125  0.0308  0.0447  415 LEU C CB  
10654 C CG  . LEU C 415 ? 0.2225 0.6546 0.2085 0.1206  0.0376  0.0622  415 LEU C CG  
10655 C CD1 . LEU C 415 ? 0.2255 0.6547 0.2089 0.1172  0.0403  0.0615  415 LEU C CD1 
10656 C CD2 . LEU C 415 ? 0.2270 0.6485 0.2247 0.1238  0.0475  0.0756  415 LEU C CD2 
10657 N N   . THR C 416 ? 0.1899 0.6004 0.1811 0.1056  0.0185  0.0208  416 THR C N   
10658 C CA  . THR C 416 ? 0.1805 0.5827 0.1714 0.0987  0.0127  0.0056  416 THR C CA  
10659 C C   . THR C 416 ? 0.1722 0.5518 0.1704 0.0906  0.0158  0.0005  416 THR C C   
10660 O O   . THR C 416 ? 0.1728 0.5417 0.1800 0.0903  0.0220  0.0064  416 THR C O   
10661 C CB  . THR C 416 ? 0.1999 0.6054 0.1925 0.1009  0.0106  0.0037  416 THR C CB  
10662 O OG1 . THR C 416 ? 0.2148 0.6373 0.2056 0.1106  0.0124  0.0162  416 THR C OG1 
10663 C CG2 . THR C 416 ? 0.1770 0.5886 0.1634 0.0977  0.0027  -0.0105 416 THR C CG2 
10664 N N   . ILE C 417 ? 0.1659 0.5393 0.1615 0.0843  0.0116  -0.0105 417 ILE C N   
10665 C CA  . ILE C 417 ? 0.1594 0.5146 0.1597 0.0774  0.0139  -0.0149 417 ILE C CA  
10666 C C   . ILE C 417 ? 0.1685 0.5136 0.1713 0.0723  0.0107  -0.0246 417 ILE C C   
10667 O O   . ILE C 417 ? 0.1540 0.5025 0.1533 0.0704  0.0052  -0.0329 417 ILE C O   
10668 C CB  . ILE C 417 ? 0.1696 0.5250 0.1665 0.0747  0.0123  -0.0186 417 ILE C CB  
10669 C CG1 . ILE C 417 ? 0.1786 0.5470 0.1720 0.0801  0.0148  -0.0097 417 ILE C CG1 
10670 C CG2 . ILE C 417 ? 0.1531 0.4918 0.1550 0.0688  0.0152  -0.0216 417 ILE C CG2 
10671 C CD1 . ILE C 417 ? 0.1725 0.5382 0.1707 0.0836  0.0229  0.0025  417 ILE C CD1 
10672 N N   . ALA C 418 ? 0.1551 0.4880 0.1652 0.0698  0.0146  -0.0237 418 ALA C N   
10673 C CA  . ALA C 418 ? 0.1444 0.4667 0.1567 0.0644  0.0123  -0.0324 418 ALA C CA  
10674 C C   . ALA C 418 ? 0.1441 0.4594 0.1540 0.0592  0.0099  -0.0390 418 ALA C C   
10675 O O   . ALA C 418 ? 0.1761 0.4910 0.1850 0.0589  0.0112  -0.0368 418 ALA C O   
10676 C CB  . ALA C 418 ? 0.1412 0.4533 0.1629 0.0624  0.0173  -0.0303 418 ALA C CB  
10677 N N   . ARG C 419 ? 0.1565 0.4663 0.1663 0.0554  0.0066  -0.0468 419 ARG C N   
10678 C CA  . ARG C 419 ? 0.1302 0.4347 0.1390 0.0515  0.0043  -0.0523 419 ARG C CA  
10679 C C   . ARG C 419 ? 0.1412 0.4344 0.1532 0.0477  0.0069  -0.0525 419 ARG C C   
10680 O O   . ARG C 419 ? 0.1258 0.4129 0.1410 0.0456  0.0083  -0.0537 419 ARG C O   
10681 C CB  . ARG C 419 ? 0.1365 0.4414 0.1454 0.0495  0.0005  -0.0598 419 ARG C CB  
10682 C CG  . ARG C 419 ? 0.1312 0.4494 0.1378 0.0527  -0.0028 -0.0617 419 ARG C CG  
10683 C CD  . ARG C 419 ? 0.1297 0.4485 0.1387 0.0507  -0.0054 -0.0693 419 ARG C CD  
10684 N NE  . ARG C 419 ? 0.1480 0.4823 0.1555 0.0540  -0.0087 -0.0718 419 ARG C NE  
10685 C CZ  . ARG C 419 ? 0.1376 0.4822 0.1424 0.0585  -0.0092 -0.0685 419 ARG C CZ  
10686 N NH1 . ARG C 419 ? 0.1382 0.4775 0.1429 0.0601  -0.0059 -0.0626 419 ARG C NH1 
10687 N NH2 . ARG C 419 ? 0.1614 0.5210 0.1646 0.0615  -0.0120 -0.0708 419 ARG C NH2 
10688 N N   . ARG C 420 ? 0.1267 0.4183 0.1382 0.0468  0.0075  -0.0518 420 ARG C N   
10689 C CA  . ARG C 420 ? 0.1404 0.4242 0.1544 0.0433  0.0089  -0.0530 420 ARG C CA  
10690 C C   . ARG C 420 ? 0.1358 0.4160 0.1549 0.0426  0.0136  -0.0497 420 ARG C C   
10691 O O   . ARG C 420 ? 0.1423 0.4171 0.1643 0.0393  0.0147  -0.0521 420 ARG C O   
10692 C CB  . ARG C 420 ? 0.1258 0.4044 0.1398 0.0402  0.0065  -0.0585 420 ARG C CB  
10693 C CG  . ARG C 420 ? 0.1374 0.4185 0.1496 0.0406  0.0033  -0.0623 420 ARG C CG  
10694 C CD  . ARG C 420 ? 0.1181 0.3935 0.1315 0.0379  0.0026  -0.0663 420 ARG C CD  
10695 N NE  . ARG C 420 ? 0.1590 0.4310 0.1736 0.0362  0.0030  -0.0680 420 ARG C NE  
10696 C CZ  . ARG C 420 ? 0.1519 0.4198 0.1675 0.0343  0.0030  -0.0714 420 ARG C CZ  
10697 N NH1 . ARG C 420 ? 0.1175 0.3843 0.1333 0.0342  0.0028  -0.0732 420 ARG C NH1 
10698 N NH2 . ARG C 420 ? 0.1164 0.3814 0.1333 0.0326  0.0039  -0.0729 420 ARG C NH2 
10699 N N   . VAL C 421 ? 0.1523 0.4367 0.1737 0.0459  0.0169  -0.0441 421 VAL C N   
10700 C CA  . VAL C 421 ? 0.1296 0.4107 0.1594 0.0455  0.0226  -0.0407 421 VAL C CA  
10701 C C   . VAL C 421 ? 0.1451 0.4268 0.1790 0.0462  0.0273  -0.0362 421 VAL C C   
10702 O O   . VAL C 421 ? 0.1417 0.4185 0.1834 0.0432  0.0314  -0.0371 421 VAL C O   
10703 C CB  . VAL C 421 ? 0.1323 0.4175 0.1647 0.0492  0.0243  -0.0365 421 VAL C CB  
10704 C CG1 . VAL C 421 ? 0.1572 0.4396 0.2014 0.0494  0.0314  -0.0319 421 VAL C CG1 
10705 C CG2 . VAL C 421 ? 0.1293 0.4125 0.1595 0.0475  0.0205  -0.0421 421 VAL C CG2 
10706 N N   . TYR C 422 ? 0.1361 0.4247 0.1657 0.0498  0.0271  -0.0319 422 TYR C N   
10707 C CA  . TYR C 422 ? 0.1439 0.4337 0.1776 0.0509  0.0325  -0.0268 422 TYR C CA  
10708 C C   . TYR C 422 ? 0.1504 0.4412 0.1789 0.0496  0.0297  -0.0300 422 TYR C C   
10709 O O   . TYR C 422 ? 0.1496 0.4436 0.1706 0.0499  0.0239  -0.0336 422 TYR C O   
10710 C CB  . TYR C 422 ? 0.1468 0.4451 0.1803 0.0568  0.0358  -0.0176 422 TYR C CB  
10711 C CG  . TYR C 422 ? 0.1827 0.4807 0.2236 0.0590  0.0393  -0.0134 422 TYR C CG  
10712 C CD1 . TYR C 422 ? 0.1489 0.4404 0.2034 0.0571  0.0466  -0.0114 422 TYR C CD1 
10713 C CD2 . TYR C 422 ? 0.1491 0.4538 0.1852 0.0627  0.0355  -0.0121 422 TYR C CD2 
10714 C CE1 . TYR C 422 ? 0.1503 0.4412 0.2140 0.0591  0.0502  -0.0078 422 TYR C CE1 
10715 C CE2 . TYR C 422 ? 0.1505 0.4551 0.1946 0.0649  0.0386  -0.0083 422 TYR C CE2 
10716 C CZ  . TYR C 422 ? 0.1511 0.4485 0.2093 0.0632  0.0461  -0.0058 422 TYR C CZ  
10717 O OH  . TYR C 422 ? 0.1525 0.4498 0.2211 0.0655  0.0495  -0.0022 422 TYR C OH  
10718 N N   . THR C 423 ? 0.1406 0.4289 0.1751 0.0479  0.0342  -0.0291 423 THR C N   
10719 C CA  . THR C 423 ? 0.1403 0.4298 0.1719 0.0468  0.0325  -0.0318 423 THR C CA  
10720 C C   . THR C 423 ? 0.1555 0.4522 0.1841 0.0505  0.0350  -0.0259 423 THR C C   
10721 O O   . THR C 423 ? 0.1515 0.4526 0.1807 0.0542  0.0387  -0.0187 423 THR C O   
10722 C CB  . THR C 423 ? 0.1658 0.4502 0.2058 0.0430  0.0360  -0.0349 423 THR C CB  
10723 O OG1 . THR C 423 ? 0.1494 0.4335 0.1983 0.0438  0.0443  -0.0293 423 THR C OG1 
10724 C CG2 . THR C 423 ? 0.1345 0.4136 0.1778 0.0395  0.0342  -0.0402 423 THR C CG2 
10725 N N   . ASN C 424 ? 0.1465 0.4453 0.1720 0.0497  0.0332  -0.0287 424 ASN C N   
10726 C CA  . ASN C 424 ? 0.2256 0.5316 0.2485 0.0526  0.0361  -0.0237 424 ASN C CA  
10727 C C   . ASN C 424 ? 0.1984 0.5026 0.2297 0.0530  0.0452  -0.0173 424 ASN C C   
10728 O O   . ASN C 424 ? 0.1795 0.4899 0.2090 0.0566  0.0493  -0.0099 424 ASN C O   
10729 C CB  . ASN C 424 ? 0.1863 0.4944 0.2061 0.0511  0.0328  -0.0291 424 ASN C CB  
10730 C CG  . ASN C 424 ? 0.2600 0.5713 0.2734 0.0512  0.0253  -0.0346 424 ASN C CG  
10731 O OD1 . ASN C 424 ? 0.2399 0.5572 0.2488 0.0539  0.0229  -0.0329 424 ASN C OD1 
10732 N ND2 . ASN C 424 ? 0.2707 0.5788 0.2850 0.0486  0.0219  -0.0412 424 ASN C ND2 
10733 N N   . ASP C 425 ? 0.1556 0.4519 0.1967 0.0495  0.0488  -0.0200 425 ASP C N   
10734 C CA  . ASP C 425 ? 0.1829 0.4769 0.2352 0.0495  0.0586  -0.0144 425 ASP C CA  
10735 C C   . ASP C 425 ? 0.1652 0.4607 0.2203 0.0532  0.0626  -0.0062 425 ASP C C   
10736 O O   . ASP C 425 ? 0.1730 0.4702 0.2339 0.0558  0.0708  0.0023  425 ASP C O   
10737 C CB  . ASP C 425 ? 0.1570 0.4436 0.2210 0.0444  0.0612  -0.0209 425 ASP C CB  
10738 C CG  . ASP C 425 ? 0.2004 0.4872 0.2643 0.0417  0.0594  -0.0268 425 ASP C CG  
10739 O OD1 . ASP C 425 ? 0.2144 0.5057 0.2734 0.0435  0.0599  -0.0245 425 ASP C OD1 
10740 O OD2 . ASP C 425 ? 0.2309 0.5143 0.2998 0.0379  0.0574  -0.0339 425 ASP C OD2 
10741 N N   . HIS C 426 ? 0.1609 0.4561 0.2125 0.0539  0.0575  -0.0079 426 HIS C N   
10742 C CA  . HIS C 426 ? 0.1653 0.4640 0.2183 0.0585  0.0603  0.0003  426 HIS C CA  
10743 C C   . HIS C 426 ? 0.1723 0.4825 0.2147 0.0645  0.0589  0.0081  426 HIS C C   
10744 O O   . HIS C 426 ? 0.1804 0.4954 0.2257 0.0696  0.0647  0.0189  426 HIS C O   
10745 C CB  . HIS C 426 ? 0.1591 0.4556 0.2105 0.0576  0.0546  -0.0044 426 HIS C CB  
10746 C CG  . HIS C 426 ? 0.1544 0.4415 0.2175 0.0526  0.0574  -0.0101 426 HIS C CG  
10747 N ND1 . HIS C 426 ? 0.1503 0.4329 0.2101 0.0482  0.0512  -0.0194 426 HIS C ND1 
10748 C CD2 . HIS C 426 ? 0.1567 0.4390 0.2354 0.0511  0.0660  -0.0080 426 HIS C CD2 
10749 C CE1 . HIS C 426 ? 0.1454 0.4218 0.2168 0.0444  0.0552  -0.0230 426 HIS C CE1 
10750 N NE2 . HIS C 426 ? 0.1507 0.4265 0.2346 0.0457  0.0643  -0.0169 426 HIS C NE2 
10751 N N   . MET C 427 ? 0.1802 0.4956 0.2111 0.0643  0.0514  0.0030  427 MET C N   
10752 C CA  . MET C 427 ? 0.1863 0.5144 0.2072 0.0694  0.0497  0.0086  427 MET C CA  
10753 C C   . MET C 427 ? 0.1864 0.5168 0.2103 0.0714  0.0580  0.0170  427 MET C C   
10754 O O   . MET C 427 ? 0.1971 0.5375 0.2170 0.0774  0.0608  0.0274  427 MET C O   
10755 C CB  . MET C 427 ? 0.1728 0.5050 0.1848 0.0674  0.0414  -0.0005 427 MET C CB  
10756 C CG  . MET C 427 ? 0.1649 0.4951 0.1741 0.0656  0.0337  -0.0086 427 MET C CG  
10757 S SD  . MET C 427 ? 0.1723 0.5119 0.1778 0.0710  0.0311  -0.0039 427 MET C SD  
10758 C CE  . MET C 427 ? 0.1616 0.4876 0.1766 0.0679  0.0337  -0.0054 427 MET C CE  
10759 N N   . ASP C 428 ? 0.1846 0.5067 0.2155 0.0666  0.0621  0.0128  428 ASP C N   
10760 C CA  . ASP C 428 ? 0.1936 0.5165 0.2288 0.0675  0.0709  0.0199  428 ASP C CA  
10761 C C   . ASP C 428 ? 0.2014 0.5228 0.2460 0.0711  0.0804  0.0316  428 ASP C C   
10762 O O   . ASP C 428 ? 0.2213 0.5490 0.2639 0.0759  0.0862  0.0430  428 ASP C O   
10763 C CB  . ASP C 428 ? 0.2195 0.5336 0.2629 0.0613  0.0737  0.0117  428 ASP C CB  
10764 C CG  . ASP C 428 ? 0.1863 0.5039 0.2213 0.0594  0.0672  0.0040  428 ASP C CG  
10765 O OD1 . ASP C 428 ? 0.2250 0.5524 0.2490 0.0627  0.0630  0.0060  428 ASP C OD1 
10766 O OD2 . ASP C 428 ? 0.1863 0.4977 0.2266 0.0547  0.0665  -0.0041 428 ASP C OD2 
10767 N N   . TYR C 429 ? 0.1962 0.5091 0.2520 0.0688  0.0824  0.0294  429 TYR C N   
10768 C CA  . TYR C 429 ? 0.2034 0.5138 0.2710 0.0721  0.0915  0.0401  429 TYR C CA  
10769 C C   . TYR C 429 ? 0.2116 0.5335 0.2702 0.0807  0.0902  0.0527  429 TYR C C   
10770 O O   . TYR C 429 ? 0.2273 0.5519 0.2900 0.0860  0.0984  0.0666  429 TYR C O   
10771 C CB  . TYR C 429 ? 0.1952 0.4963 0.2755 0.0679  0.0920  0.0332  429 TYR C CB  
10772 C CG  . TYR C 429 ? 0.3092 0.6064 0.4051 0.0706  0.1016  0.0429  429 TYR C CG  
10773 C CD1 . TYR C 429 ? 0.2959 0.5987 0.3893 0.0775  0.1005  0.0526  429 TYR C CD1 
10774 C CD2 . TYR C 429 ? 0.3162 0.6041 0.4309 0.0663  0.1121  0.0416  429 TYR C CD2 
10775 C CE1 . TYR C 429 ? 0.3499 0.6480 0.4593 0.0804  0.1096  0.0622  429 TYR C CE1 
10776 C CE2 . TYR C 429 ? 0.3296 0.6124 0.4606 0.0684  0.1213  0.0500  429 TYR C CE2 
10777 C CZ  . TYR C 429 ? 0.3660 0.6531 0.4944 0.0756  0.1202  0.0609  429 TYR C CZ  
10778 O OH  . TYR C 429 ? 0.3922 0.6728 0.5384 0.0781  0.1297  0.0700  429 TYR C OH  
10779 N N   . ILE C 430 ? 0.2060 0.5352 0.2530 0.0825  0.0799  0.0483  430 ILE C N   
10780 C CA  . ILE C 430 ? 0.2133 0.5565 0.2514 0.0910  0.0774  0.0587  430 ILE C CA  
10781 C C   . ILE C 430 ? 0.2369 0.5917 0.2648 0.0956  0.0789  0.0671  430 ILE C C   
10782 O O   . ILE C 430 ? 0.2716 0.6340 0.2994 0.1030  0.0845  0.0823  430 ILE C O   
10783 C CB  . ILE C 430 ? 0.2047 0.5539 0.2330 0.0907  0.0658  0.0494  430 ILE C CB  
10784 C CG1 . ILE C 430 ? 0.1948 0.5321 0.2329 0.0861  0.0648  0.0416  430 ILE C CG1 
10785 C CG2 . ILE C 430 ? 0.2125 0.5790 0.2319 0.0997  0.0627  0.0590  430 ILE C CG2 
10786 C CD1 . ILE C 430 ? 0.1853 0.5239 0.2147 0.0831  0.0542  0.0294  430 ILE C CD1 
10787 N N   . ALA C 431 ? 0.2213 0.5777 0.2412 0.0914  0.0742  0.0577  431 ALA C N   
10788 C CA  . ALA C 431 ? 0.2391 0.6069 0.2496 0.0949  0.0753  0.0637  431 ALA C CA  
10789 C C   . ALA C 431 ? 0.2590 0.6221 0.2777 0.0968  0.0878  0.0764  431 ALA C C   
10790 O O   . ALA C 431 ? 0.3170 0.6907 0.3308 0.1041  0.0916  0.0905  431 ALA C O   
10791 C CB  . ALA C 431 ? 0.2253 0.5927 0.2300 0.0889  0.0693  0.0501  431 ALA C CB  
10792 N N   . ASP C 432 ? 0.2455 0.5931 0.2774 0.0904  0.0946  0.0717  432 ASP C N   
10793 C CA  . ASP C 432 ? 0.2513 0.5926 0.2934 0.0909  0.1073  0.0819  432 ASP C CA  
10794 C C   . ASP C 432 ? 0.3390 0.6806 0.3886 0.0981  0.1150  0.0989  432 ASP C C   
10795 O O   . ASP C 432 ? 0.3427 0.6853 0.3944 0.1025  0.1242  0.1129  432 ASP C O   
10796 C CB  . ASP C 432 ? 0.2653 0.5913 0.3228 0.0822  0.1124  0.0711  432 ASP C CB  
10797 C CG  . ASP C 432 ? 0.3270 0.6530 0.3787 0.0762  0.1069  0.0575  432 ASP C CG  
10798 O OD1 . ASP C 432 ? 0.3924 0.7287 0.4302 0.0786  0.1024  0.0583  432 ASP C OD1 
10799 O OD2 . ASP C 432 ? 0.4050 0.7212 0.4665 0.0694  0.1072  0.0460  432 ASP C OD2 
10800 N N   . ALA C 433 ? 0.2926 0.6327 0.3468 0.0997  0.1118  0.0985  433 ALA C N   
10801 C CA  . ALA C 433 ? 0.2903 0.6309 0.3528 0.1074  0.1189  0.1152  433 ALA C CA  
10802 C C   . ALA C 433 ? 0.3214 0.6805 0.3691 0.1179  0.1168  0.1302  433 ALA C C   
10803 O O   . ALA C 433 ? 0.4273 0.7875 0.4791 0.1244  0.1262  0.1479  433 ALA C O   
10804 C CB  . ALA C 433 ? 0.2872 0.6235 0.3577 0.1065  0.1150  0.1098  433 ALA C CB  
10805 N N   . LEU C 434 ? 0.2905 0.6647 0.3215 0.1196  0.1045  0.1232  434 LEU C N   
10806 C CA  . LEU C 434 ? 0.3077 0.7028 0.3245 0.1293  0.1009  0.1350  434 LEU C CA  
10807 C C   . LEU C 434 ? 0.3907 0.7902 0.4013 0.1306  0.1060  0.1420  434 LEU C C   
10808 O O   . LEU C 434 ? 0.4406 0.8514 0.4470 0.1396  0.1100  0.1591  434 LEU C O   
10809 C CB  . LEU C 434 ? 0.2909 0.7008 0.2939 0.1290  0.0865  0.1221  434 LEU C CB  
10810 C CG  . LEU C 434 ? 0.2865 0.7219 0.2757 0.1384  0.0801  0.1297  434 LEU C CG  
10811 C CD1 . LEU C 434 ? 0.4093 0.8532 0.4025 0.1493  0.0843  0.1483  434 LEU C CD1 
10812 C CD2 . LEU C 434 ? 0.2746 0.7218 0.2547 0.1356  0.0664  0.1128  434 LEU C CD2 
10813 N N   . ILE C 435 ? 0.3519 0.7428 0.3622 0.1218  0.1060  0.1292  435 ILE C N   
10814 C CA  . ILE C 435 ? 0.4052 0.7996 0.4101 0.1219  0.1110  0.1339  435 ILE C CA  
10815 C C   . ILE C 435 ? 0.5008 0.8846 0.5179 0.1249  0.1259  0.1508  435 ILE C C   
10816 O O   . ILE C 435 ? 0.5070 0.8997 0.5186 0.1317  0.1308  0.1657  435 ILE C O   
10817 C CB  . ILE C 435 ? 0.3544 0.7412 0.3585 0.1116  0.1079  0.1155  435 ILE C CB  
10818 C CG1 . ILE C 435 ? 0.3148 0.7138 0.3065 0.1099  0.0939  0.1012  435 ILE C CG1 
10819 C CG2 . ILE C 435 ? 0.3517 0.7376 0.3548 0.1103  0.1160  0.1200  435 ILE C CG2 
10820 C CD1 . ILE C 435 ? 0.3182 0.7066 0.3126 0.1000  0.0897  0.0826  435 ILE C CD1 
10821 N N   . GLY C 436 ? 0.4593 0.8242 0.4946 0.1198  0.1335  0.1484  436 GLY C N   
10822 C CA  . GLY C 436 ? 0.4805 0.8325 0.5316 0.1210  0.1486  0.1619  436 GLY C CA  
10823 C C   . GLY C 436 ? 0.5259 0.8847 0.5774 0.1329  0.1545  0.1854  436 GLY C C   
10824 O O   . GLY C 436 ? 0.6397 0.9906 0.7004 0.1356  0.1670  0.1995  436 GLY C O   
10825 N N   . LEU C 437 ? 0.5320 0.9056 0.5744 0.1404  0.1459  0.1902  437 LEU C N   
10826 C CA  . LEU C 437 ? 0.5375 0.9214 0.5792 0.1532  0.1498  0.2129  437 LEU C CA  
10827 C C   . LEU C 437 ? 0.6237 1.0279 0.6474 0.1607  0.1467  0.2225  437 LEU C C   
10828 O O   . LEU C 437 ? 0.6500 1.0681 0.6704 0.1723  0.1471  0.2403  437 LEU C O   
10829 C CB  . LEU C 437 ? 0.5085 0.9019 0.5491 0.1583  0.1416  0.2129  437 LEU C CB  
10830 C CG  . LEU C 437 ? 0.5133 0.8897 0.5720 0.1526  0.1437  0.2045  437 LEU C CG  
10831 C CD1 . LEU C 437 ? 0.4500 0.8399 0.5036 0.1581  0.1339  0.2034  437 LEU C CD1 
10832 C CD2 . LEU C 437 ? 0.5591 0.9167 0.6414 0.1541  0.1595  0.2187  437 LEU C CD2 
10833 N N   . LYS C 438 ? 0.6002 1.0075 0.6135 0.1543  0.1435  0.2109  438 LYS C N   
10834 C CA  . LYS C 438 ? 0.6162 1.0452 0.6124 0.1602  0.1385  0.2161  438 LYS C CA  
10835 C C   . LYS C 438 ? 0.6923 1.1233 0.6915 0.1698  0.1499  0.2402  438 LYS C C   
10836 O O   . LYS C 438 ? 0.7281 1.1811 0.7161 0.1792  0.1456  0.2504  438 LYS C O   
10837 C CB  . LYS C 438 ? 0.5880 1.0169 0.5757 0.1507  0.1348  0.1987  438 LYS C CB  
10838 C CG  . LYS C 438 ? 0.5495 0.9925 0.5252 0.1471  0.1192  0.1796  438 LYS C CG  
10839 C CD  . LYS C 438 ? 0.5560 0.9887 0.5316 0.1350  0.1169  0.1592  438 LYS C CD  
10840 C CE  . LYS C 438 ? 0.5392 0.9759 0.5084 0.1331  0.1213  0.1598  438 LYS C CE  
10841 N NZ  . LYS C 438 ? 0.5143 0.9409 0.4851 0.1218  0.1194  0.1403  438 LYS C NZ  
10842 N N   . GLU C 439 ? 0.7467 1.0325 0.8391 -0.1184 0.3880  0.2077  439 GLU C N   
10843 C CA  . GLU C 439 ? 0.7625 1.0232 0.8487 -0.1391 0.4012  0.2225  439 GLU C CA  
10844 C C   . GLU C 439 ? 0.7733 0.9990 0.8587 -0.1404 0.3942  0.2432  439 GLU C C   
10845 O O   . GLU C 439 ? 0.8171 1.0118 0.8857 -0.1544 0.4026  0.2599  439 GLU C O   
10846 C CB  . GLU C 439 ? 0.7774 1.0673 0.9100 -0.1542 0.4209  0.2055  439 GLU C CB  
10847 C CG  . GLU C 439 ? 0.8113 1.1342 0.9412 -0.1554 0.4298  0.1884  439 GLU C CG  
10848 C CD  . GLU C 439 ? 0.9547 1.2543 1.0302 -0.1634 0.4325  0.2029  439 GLU C CD  
10849 O OE1 . GLU C 439 ? 0.9972 1.2689 1.0559 -0.1793 0.4409  0.2205  439 GLU C OE1 
10850 O OE2 . GLU C 439 ? 0.9056 1.2140 0.9549 -0.1536 0.4259  0.1958  439 GLU C OE2 
10851 N N   . LYS C 440 ? 0.7559 0.9858 0.8587 -0.1256 0.3791  0.2427  440 LYS C N   
10852 C CA  . LYS C 440 ? 0.7490 0.9461 0.8476 -0.1241 0.3695  0.2628  440 LYS C CA  
10853 C C   . LYS C 440 ? 0.7683 0.9429 0.8153 -0.1102 0.3497  0.2782  440 LYS C C   
10854 O O   . LYS C 440 ? 0.8799 1.0267 0.9165 -0.1072 0.3399  0.2963  440 LYS C O   
10855 C CB  . LYS C 440 ? 0.7425 0.9598 0.8966 -0.1184 0.3645  0.2521  440 LYS C CB  
10856 C CG  . LYS C 440 ? 0.8123 1.0530 1.0228 -0.1333 0.3822  0.2325  440 LYS C CG  
10857 C CD  . LYS C 440 ? 0.8302 1.0979 1.0907 -0.1245 0.3666  0.2096  440 LYS C CD  
10858 C CE  . LYS C 440 ? 0.9018 1.2009 1.2208 -0.1393 0.3842  0.1851  440 LYS C CE  
10859 N NZ  . LYS C 440 ? 0.9161 1.2472 1.2821 -0.1295 0.3666  0.1591  440 LYS C NZ  
10860 N N   . PHE C 441 ? 0.7952 0.9818 0.8113 -0.1019 0.3436  0.2692  441 PHE C N   
10861 C CA  . PHE C 441 ? 0.7797 0.9487 0.7496 -0.0901 0.3249  0.2777  441 PHE C CA  
10862 C C   . PHE C 441 ? 0.8885 1.0216 0.8188 -0.0971 0.3237  0.2994  441 PHE C C   
10863 O O   . PHE C 441 ? 0.9009 1.0161 0.8062 -0.0877 0.3072  0.3112  441 PHE C O   
10864 C CB  . PHE C 441 ? 0.7340 0.9188 0.6798 -0.0839 0.3226  0.2609  441 PHE C CB  
10865 C CG  . PHE C 441 ? 0.7150 0.9258 0.6820 -0.0684 0.3145  0.2433  441 PHE C CG  
10866 C CD1 . PHE C 441 ? 0.7202 0.9337 0.7067 -0.0575 0.3018  0.2460  441 PHE C CD1 
10867 C CD2 . PHE C 441 ? 0.6758 0.9072 0.6418 -0.0641 0.3197  0.2240  441 PHE C CD2 
10868 C CE1 . PHE C 441 ? 0.6736 0.9101 0.6761 -0.0426 0.2946  0.2298  441 PHE C CE1 
10869 C CE2 . PHE C 441 ? 0.6793 0.9308 0.6606 -0.0476 0.3121  0.2085  441 PHE C CE2 
10870 C CZ  . PHE C 441 ? 0.6114 0.8654 0.6098 -0.0369 0.2997  0.2113  441 PHE C CZ  
10871 N N   . ALA C 442 ? 0.9563 1.0798 0.8797 -0.1132 0.3409  0.3043  442 ALA C N   
10872 C CA  . ALA C 442 ? 0.9752 1.0651 0.8567 -0.1191 0.3408  0.3248  442 ALA C CA  
10873 C C   . ALA C 442 ? 1.0177 1.0786 0.9121 -0.1222 0.3427  0.3445  442 ALA C C   
10874 O O   . ALA C 442 ? 1.0541 1.0844 0.9119 -0.1212 0.3379  0.3640  442 ALA C O   
10875 C CB  . ALA C 442 ? 0.9981 1.0896 0.8625 -0.1356 0.3586  0.3221  442 ALA C CB  
10876 N N   . THR C 443 ? 0.9876 1.0570 0.9334 -0.1254 0.3496  0.3389  443 THR C N   
10877 C CA  . THR C 443 ? 0.9245 0.9640 0.8878 -0.1298 0.3534  0.3547  443 THR C CA  
10878 C C   . THR C 443 ? 0.9175 0.9513 0.8933 -0.1141 0.3338  0.3613  443 THR C C   
10879 O O   . THR C 443 ? 0.9283 0.9369 0.9225 -0.1163 0.3354  0.3732  443 THR C O   
10880 C CB  . THR C 443 ? 0.9073 0.9579 0.9240 -0.1466 0.3752  0.3419  443 THR C CB  
10881 O OG1 . THR C 443 ? 0.9368 1.0242 1.0024 -0.1406 0.3710  0.3213  443 THR C OG1 
10882 C CG2 . THR C 443 ? 0.9309 0.9939 0.9393 -0.1624 0.3944  0.3328  443 THR C CG2 
10883 N N   . LEU C 444 ? 0.9351 0.9907 0.9019 -0.0992 0.3159  0.3531  444 LEU C N   
10884 C CA  . LEU C 444 ? 0.9175 0.9716 0.8965 -0.0852 0.2969  0.3580  444 LEU C CA  
10885 C C   . LEU C 444 ? 0.9421 0.9762 0.8691 -0.0725 0.2779  0.3730  444 LEU C C   
10886 O O   . LEU C 444 ? 0.9277 0.9631 0.8122 -0.0715 0.2757  0.3713  444 LEU C O   
10887 C CB  . LEU C 444 ? 0.8853 0.9781 0.8923 -0.0769 0.2889  0.3365  444 LEU C CB  
10888 C CG  . LEU C 444 ? 0.8648 0.9806 0.8430 -0.0697 0.2843  0.3221  444 LEU C CG  
10889 C CD1 . LEU C 444 ? 0.8406 0.9519 0.7846 -0.0549 0.2619  0.3251  444 LEU C CD1 
10890 C CD2 . LEU C 444 ? 0.6923 0.8447 0.7102 -0.0680 0.2888  0.2976  444 LEU C CD2 
10891 N N   . LYS C 445 ? 0.8996 0.9171 0.8330 -0.0632 0.2640  0.3858  445 LYS C N   
10892 C CA  . LYS C 445 ? 0.9621 0.9594 0.8513 -0.0505 0.2462  0.4013  445 LYS C CA  
10893 C C   . LYS C 445 ? 0.9725 0.9912 0.8575 -0.0355 0.2238  0.3925  445 LYS C C   
10894 O O   . LYS C 445 ? 0.9259 0.9645 0.8478 -0.0339 0.2171  0.3735  445 LYS C O   
10895 C CB  . LYS C 445 ? 1.0586 1.0181 0.9541 -0.0492 0.2463  0.4228  445 LYS C CB  
10896 C CG  . LYS C 445 ? 1.1174 1.0536 0.9634 -0.0357 0.2308  0.4408  445 LYS C CG  
10897 C CD  . LYS C 445 ? 1.0681 1.0021 0.8654 -0.0402 0.2372  0.4428  445 LYS C CD  
10898 C CE  . LYS C 445 ? 1.1203 1.0390 0.8696 -0.0251 0.2201  0.4579  445 LYS C CE  
10899 N NZ  . LYS C 445 ? 1.1701 1.0905 0.8732 -0.0299 0.2255  0.4581  445 LYS C NZ  
10900 N N   . GLY C 446 ? 0.9448 0.9593 0.7847 -0.0250 0.2086  0.3973  446 GLY C N   
10901 C CA  . GLY C 446 ? 0.9649 0.9979 0.7964 -0.0118 0.1878  0.3880  446 GLY C CA  
10902 C C   . GLY C 446 ? 0.9673 0.9890 0.8231 -0.0023 0.1702  0.3925  446 GLY C C   
10903 O O   . GLY C 446 ? 0.9039 0.9006 0.7811 -0.0049 0.1745  0.4053  446 GLY C O   
10904 N N   . LEU C 447 ? 0.9071 0.9458 0.7604 0.0080  0.1490  0.3756  447 LEU C N   
10905 C CA  . LEU C 447 ? 0.9049 0.9377 0.7833 0.0171  0.1280  0.3693  447 LEU C CA  
10906 C C   . LEU C 447 ? 0.9391 0.9696 0.7807 0.0318  0.1091  0.3787  447 LEU C C   
10907 O O   . LEU C 447 ? 0.9420 0.9871 0.7429 0.0351  0.1082  0.3789  447 LEU C O   
10908 C CB  . LEU C 447 ? 0.9043 0.9606 0.8145 0.0171  0.1183  0.3387  447 LEU C CB  
10909 C CG  . LEU C 447 ? 0.9154 0.9805 0.8676 0.0062  0.1322  0.3248  447 LEU C CG  
10910 C CD1 . LEU C 447 ? 0.7656 0.8567 0.7277 0.0088  0.1258  0.2973  447 LEU C CD1 
10911 C CD2 . LEU C 447 ? 0.8493 0.8991 0.8469 0.0032  0.1304  0.3265  447 LEU C CD2 
10912 N N   . GLU C 448 ? 0.9948 1.0090 0.8523 0.0410  0.0942  0.3852  448 GLU C N   
10913 C CA  . GLU C 448 ? 0.9659 0.9828 0.7983 0.0575  0.0720  0.3887  448 GLU C CA  
10914 C C   . GLU C 448 ? 0.8399 0.8654 0.7097 0.0628  0.0520  0.3666  448 GLU C C   
10915 O O   . GLU C 448 ? 0.7825 0.8125 0.6931 0.0539  0.0557  0.3495  448 GLU C O   
10916 C CB  . GLU C 448 ? 0.8594 0.8456 0.6683 0.0673  0.0727  0.4214  448 GLU C CB  
10917 C CG  . GLU C 448 ? 0.8943 0.8466 0.7402 0.0644  0.0797  0.4339  448 GLU C CG  
10918 C CD  . GLU C 448 ? 1.0497 0.9657 0.8652 0.0742  0.0851  0.4692  448 GLU C CD  
10919 O OE1 . GLU C 448 ? 1.1005 1.0214 0.8671 0.0844  0.0792  0.4790  448 GLU C OE1 
10920 O OE2 . GLU C 448 ? 1.0769 0.9591 0.9175 0.0710  0.0952  0.4824  448 GLU C OE2 
10921 N N   . PHE C 449 ? 0.7927 0.8228 0.6481 0.0778  0.0306  0.3661  449 PHE C N   
10922 C CA  . PHE C 449 ? 0.8122 0.8551 0.6979 0.0829  0.0108  0.3423  449 PHE C CA  
10923 C C   . PHE C 449 ? 0.8510 0.8688 0.7697 0.0894  0.0027  0.3521  449 PHE C C   
10924 O O   . PHE C 449 ? 0.8106 0.8060 0.7114 0.1007  0.0001  0.3771  449 PHE C O   
10925 C CB  . PHE C 449 ? 0.8009 0.8687 0.6565 0.0945  -0.0081 0.3300  449 PHE C CB  
10926 C CG  . PHE C 449 ? 0.7374 0.8326 0.5721 0.0863  -0.0018 0.3097  449 PHE C CG  
10927 C CD1 . PHE C 449 ? 0.7738 0.8832 0.6335 0.0782  -0.0020 0.2816  449 PHE C CD1 
10928 C CD2 . PHE C 449 ? 0.7804 0.8860 0.5689 0.0873  0.0051  0.3185  449 PHE C CD2 
10929 C CE1 . PHE C 449 ? 0.7942 0.9237 0.6331 0.0714  0.0059  0.2637  449 PHE C CE1 
10930 C CE2 . PHE C 449 ? 0.7079 0.8366 0.4780 0.0792  0.0126  0.2989  449 PHE C CE2 
10931 C CZ  . PHE C 449 ? 0.7612 0.9000 0.5563 0.0714  0.0136  0.2719  449 PHE C CZ  
10932 N N   . GLU C 450 ? 0.8699 0.8909 0.8357 0.0829  -0.0005 0.3323  450 GLU C N   
10933 C CA  . GLU C 450 ? 0.8511 0.8578 0.8515 0.0902  -0.0139 0.3310  450 GLU C CA  
10934 C C   . GLU C 450 ? 0.8489 0.8794 0.8541 0.0995  -0.0379 0.3071  450 GLU C C   
10935 O O   . GLU C 450 ? 0.9013 0.9234 0.9158 0.1124  -0.0540 0.3103  450 GLU C O   
10936 C CB  . GLU C 450 ? 0.8361 0.8340 0.8879 0.0764  -0.0023 0.3222  450 GLU C CB  
10937 C CG  . GLU C 450 ? 0.8385 0.8306 0.9339 0.0807  -0.0167 0.3102  450 GLU C CG  
10938 C CD  . GLU C 450 ? 0.8856 0.8834 1.0317 0.0660  -0.0076 0.2918  450 GLU C CD  
10939 O OE1 . GLU C 450 ? 0.9101 0.9056 1.0616 0.0534  0.0129  0.2961  450 GLU C OE1 
10940 O OE2 . GLU C 450 ? 0.7919 0.7989 0.9725 0.0672  -0.0210 0.2715  450 GLU C OE2 
10941 N N   . TYR C 451 ? 0.7780 0.8369 0.7752 0.0934  -0.0393 0.2832  451 TYR C N   
10942 C CA  . TYR C 451 ? 0.7330 0.8157 0.7332 0.0989  -0.0584 0.2571  451 TYR C CA  
10943 C C   . TYR C 451 ? 0.7521 0.8592 0.7184 0.0939  -0.0535 0.2424  451 TYR C C   
10944 O O   . TYR C 451 ? 0.7726 0.8823 0.7384 0.0822  -0.0369 0.2379  451 TYR C O   
10945 C CB  . TYR C 451 ? 0.6816 0.7675 0.7307 0.0924  -0.0631 0.2348  451 TYR C CB  
10946 C CG  . TYR C 451 ? 0.7125 0.8235 0.7648 0.0933  -0.0773 0.2040  451 TYR C CG  
10947 C CD1 . TYR C 451 ? 0.7607 0.8803 0.8113 0.1053  -0.0978 0.1964  451 TYR C CD1 
10948 C CD2 . TYR C 451 ? 0.7737 0.8990 0.8305 0.0825  -0.0695 0.1821  451 TYR C CD2 
10949 C CE1 . TYR C 451 ? 0.7482 0.8912 0.8028 0.1042  -0.1090 0.1662  451 TYR C CE1 
10950 C CE2 . TYR C 451 ? 0.7483 0.8927 0.8060 0.0821  -0.0797 0.1540  451 TYR C CE2 
10951 C CZ  . TYR C 451 ? 0.7738 0.9273 0.8311 0.0917  -0.0989 0.1454  451 TYR C CZ  
10952 O OH  . TYR C 451 ? 0.8090 0.9816 0.8678 0.0893  -0.1072 0.1156  451 TYR C OH  
10953 N N   . GLU C 452 ? 0.7040 0.8300 0.6427 0.1029  -0.0672 0.2338  452 GLU C N   
10954 C CA  . GLU C 452 ? 0.6472 0.7961 0.5545 0.0968  -0.0609 0.2171  452 GLU C CA  
10955 C C   . GLU C 452 ? 0.6281 0.8019 0.5346 0.1004  -0.0773 0.1880  452 GLU C C   
10956 O O   . GLU C 452 ? 0.6689 0.8521 0.5678 0.1134  -0.0947 0.1891  452 GLU C O   
10957 C CB  . GLU C 452 ? 0.6273 0.7784 0.4891 0.1006  -0.0537 0.2372  452 GLU C CB  
10958 C CG  . GLU C 452 ? 0.6625 0.8364 0.4922 0.0929  -0.0444 0.2196  452 GLU C CG  
10959 C CD  . GLU C 452 ? 0.7635 0.9414 0.5489 0.0958  -0.0364 0.2388  452 GLU C CD  
10960 O OE1 . GLU C 452 ? 0.7401 0.9009 0.5178 0.1042  -0.0375 0.2676  452 GLU C OE1 
10961 O OE2 . GLU C 452 ? 0.7191 0.9162 0.4767 0.0894  -0.0279 0.2250  452 GLU C OE2 
10962 N N   . PRO C 453 ? 0.5934 0.7781 0.5070 0.0898  -0.0715 0.1614  453 PRO C N   
10963 C CA  . PRO C 453 ? 0.7190 0.9267 0.6301 0.0905  -0.0836 0.1313  453 PRO C CA  
10964 C C   . PRO C 453 ? 0.7942 1.0238 0.6624 0.0899  -0.0799 0.1231  453 PRO C C   
10965 O O   . PRO C 453 ? 0.5887 0.8148 0.4292 0.0870  -0.0657 0.1386  453 PRO C O   
10966 C CB  . PRO C 453 ? 0.7304 0.9351 0.6623 0.0785  -0.0742 0.1092  453 PRO C CB  
10967 C CG  . PRO C 453 ? 0.6515 0.8345 0.6069 0.0752  -0.0636 0.1279  453 PRO C CG  
10968 C CD  . PRO C 453 ? 0.6725 0.8467 0.6041 0.0782  -0.0553 0.1568  453 PRO C CD  
10969 N N   . PRO C 454 ? 0.9777 1.2322 0.8402 0.0918  -0.0917 0.0969  454 PRO C N   
10970 C CA  . PRO C 454 ? 0.9494 1.2295 0.7724 0.0914  -0.0892 0.0870  454 PRO C CA  
10971 C C   . PRO C 454 ? 0.9385 1.2198 0.7403 0.0758  -0.0661 0.0719  454 PRO C C   
10972 O O   . PRO C 454 ? 1.0061 1.2985 0.7739 0.0740  -0.0568 0.0761  454 PRO C O   
10973 C CB  . PRO C 454 ? 0.9342 1.2421 0.7650 0.0971  -0.1086 0.0594  454 PRO C CB  
10974 C CG  . PRO C 454 ? 0.9532 1.2474 0.8236 0.1059  -0.1248 0.0659  454 PRO C CG  
10975 C CD  . PRO C 454 ? 0.9324 1.1957 0.8247 0.0964  -0.1103 0.0773  454 PRO C CD  
10976 N N   . VAL C 455 ? 0.7042 0.9743 0.5235 0.0651  -0.0561 0.0542  455 VAL C N   
10977 C CA  . VAL C 455 ? 0.6821 0.9498 0.4805 0.0520  -0.0333 0.0388  455 VAL C CA  
10978 C C   . VAL C 455 ? 0.6164 0.8572 0.4333 0.0472  -0.0199 0.0469  455 VAL C C   
10979 O O   . VAL C 455 ? 0.6468 0.8774 0.4970 0.0499  -0.0290 0.0477  455 VAL C O   
10980 C CB  . VAL C 455 ? 0.6523 0.9374 0.4445 0.0437  -0.0320 0.0006  455 VAL C CB  
10981 C CG1 . VAL C 455 ? 0.5821 0.9006 0.3511 0.0468  -0.0412 -0.0113 455 VAL C CG1 
10982 C CG2 . VAL C 455 ? 0.6061 0.8878 0.4331 0.0446  -0.0452 -0.0144 455 VAL C CG2 
10983 N N   . LEU C 456 ? 0.6395 0.8714 0.4351 0.0407  0.0018  0.0514  456 LEU C N   
10984 C CA  . LEU C 456 ? 0.6253 0.8359 0.4334 0.0377  0.0164  0.0586  456 LEU C CA  
10985 C C   . LEU C 456 ? 0.5957 0.7950 0.4362 0.0443  0.0070  0.0825  456 LEU C C   
10986 O O   . LEU C 456 ? 0.6130 0.8031 0.4833 0.0448  0.0041  0.0788  456 LEU C O   
10987 C CB  . LEU C 456 ? 0.6538 0.8574 0.4690 0.0324  0.0229  0.0325  456 LEU C CB  
10988 C CG  . LEU C 456 ? 0.6523 0.8566 0.4346 0.0234  0.0421  0.0098  456 LEU C CG  
10989 C CD1 . LEU C 456 ? 0.6265 0.8527 0.3948 0.0194  0.0343  -0.0124 456 LEU C CD1 
10990 C CD2 . LEU C 456 ? 0.6075 0.7935 0.3947 0.0203  0.0546  -0.0057 456 LEU C CD2 
10991 N N   . ARG C 457 ? 0.6548 0.8548 0.4878 0.0489  0.0035  0.1069  457 ARG C N   
10992 C CA  . ARG C 457 ? 0.6030 0.7910 0.4648 0.0545  -0.0048 0.1297  457 ARG C CA  
10993 C C   . ARG C 457 ? 0.6126 0.7865 0.4929 0.0504  0.0097  0.1390  457 ARG C C   
10994 O O   . ARG C 457 ? 0.6211 0.7860 0.5351 0.0524  0.0038  0.1484  457 ARG C O   
10995 C CB  . ARG C 457 ? 0.6110 0.7999 0.4532 0.0605  -0.0089 0.1543  457 ARG C CB  
10996 C CG  . ARG C 457 ? 0.5951 0.7841 0.4050 0.0554  0.0102  0.1659  457 ARG C CG  
10997 C CD  . ARG C 457 ? 0.5843 0.7775 0.3671 0.0619  0.0057  0.1872  457 ARG C CD  
10998 N NE  . ARG C 457 ? 0.6031 0.7953 0.3577 0.0559  0.0253  0.1990  457 ARG C NE  
10999 C CZ  . ARG C 457 ? 0.7307 0.9281 0.4536 0.0594  0.0266  0.2164  457 ARG C CZ  
11000 N NH1 . ARG C 457 ? 0.6834 0.8875 0.3959 0.0709  0.0089  0.2253  457 ARG C NH1 
11001 N NH2 . ARG C 457 ? 0.7397 0.9363 0.4399 0.0523  0.0461  0.2251  457 ARG C NH2 
11002 N N   . HIS C 458 ? 0.7253 0.8989 0.5855 0.0450  0.0288  0.1350  458 HIS C N   
11003 C CA  . HIS C 458 ? 0.7255 0.8904 0.6008 0.0428  0.0431  0.1438  458 HIS C CA  
11004 C C   . HIS C 458 ? 0.6139 0.7757 0.5250 0.0440  0.0387  0.1315  458 HIS C C   
11005 O O   . HIS C 458 ? 0.5486 0.7073 0.4821 0.0437  0.0459  0.1388  458 HIS C O   
11006 C CB  . HIS C 458 ? 0.7153 0.8815 0.5596 0.0387  0.0639  0.1391  458 HIS C CB  
11007 C CG  . HIS C 458 ? 0.7442 0.9125 0.5704 0.0369  0.0685  0.1137  458 HIS C CG  
11008 N ND1 . HIS C 458 ? 0.7360 0.9130 0.5441 0.0353  0.0603  0.0994  458 HIS C ND1 
11009 C CD2 . HIS C 458 ? 0.6837 0.8456 0.5059 0.0365  0.0820  0.0998  458 HIS C CD2 
11010 C CE1 . HIS C 458 ? 0.6899 0.8641 0.4844 0.0319  0.0701  0.0770  458 HIS C CE1 
11011 N NE2 . HIS C 458 ? 0.6934 0.8562 0.4944 0.0334  0.0835  0.0782  458 HIS C NE2 
11012 N N   . PHE C 459 ? 0.5527 0.7178 0.4701 0.0452  0.0273  0.1118  459 PHE C N   
11013 C CA  . PHE C 459 ? 0.5323 0.6960 0.4822 0.0466  0.0219  0.0993  459 PHE C CA  
11014 C C   . PHE C 459 ? 0.5916 0.7541 0.5812 0.0488  0.0070  0.1089  459 PHE C C   
11015 O O   . PHE C 459 ? 0.4763 0.6388 0.4980 0.0491  0.0072  0.1069  459 PHE C O   
11016 C CB  . PHE C 459 ? 0.4681 0.6345 0.4087 0.0457  0.0166  0.0741  459 PHE C CB  
11017 C CG  . PHE C 459 ? 0.4604 0.6231 0.3658 0.0429  0.0342  0.0613  459 PHE C CG  
11018 C CD1 . PHE C 459 ? 0.5065 0.6628 0.4047 0.0445  0.0515  0.0657  459 PHE C CD1 
11019 C CD2 . PHE C 459 ? 0.5639 0.7300 0.4446 0.0389  0.0343  0.0431  459 PHE C CD2 
11020 C CE1 . PHE C 459 ? 0.4967 0.6457 0.3617 0.0430  0.0691  0.0541  459 PHE C CE1 
11021 C CE2 . PHE C 459 ? 0.5369 0.6961 0.3854 0.0351  0.0531  0.0300  459 PHE C CE2 
11022 C CZ  . PHE C 459 ? 0.5102 0.6589 0.3501 0.0376  0.0708  0.0365  459 PHE C CZ  
11023 N N   . THR C 460 ? 0.5913 0.7534 0.5792 0.0511  -0.0056 0.1185  460 THR C N   
11024 C CA  . THR C 460 ? 0.5288 0.6871 0.5530 0.0542  -0.0208 0.1239  460 THR C CA  
11025 C C   . THR C 460 ? 0.5987 0.7479 0.6198 0.0578  -0.0244 0.1493  460 THR C C   
11026 O O   . THR C 460 ? 0.5959 0.7381 0.6457 0.0612  -0.0358 0.1553  460 THR C O   
11027 C CB  . THR C 460 ? 0.5054 0.6712 0.5377 0.0567  -0.0380 0.1031  460 THR C CB  
11028 O OG1 . THR C 460 ? 0.4802 0.6544 0.4765 0.0580  -0.0406 0.0972  460 THR C OG1 
11029 C CG2 . THR C 460 ? 0.4148 0.5848 0.4602 0.0534  -0.0355 0.0798  460 THR C CG2 
11030 N N   . ALA C 461 ? 0.5768 0.7245 0.5632 0.0576  -0.0146 0.1646  461 ALA C N   
11031 C CA  . ALA C 461 ? 0.6068 0.7427 0.5871 0.0618  -0.0163 0.1910  461 ALA C CA  
11032 C C   . ALA C 461 ? 0.6973 0.8184 0.7082 0.0572  -0.0060 0.2060  461 ALA C C   
11033 O O   . ALA C 461 ? 0.6668 0.7909 0.6857 0.0502  0.0088  0.2025  461 ALA C O   
11034 C CB  . ALA C 461 ? 0.6193 0.7588 0.5535 0.0620  -0.0069 0.2031  461 ALA C CB  
11035 N N   . ARG C 462 ? 0.7279 0.8336 0.7569 0.0615  -0.0132 0.2216  462 ARG C N   
11036 C CA  . ARG C 462 ? 0.7127 0.8023 0.7725 0.0557  -0.0021 0.2351  462 ARG C CA  
11037 C C   . ARG C 462 ? 0.7253 0.7981 0.7578 0.0555  0.0106  0.2639  462 ARG C C   
11038 O O   . ARG C 462 ? 0.7517 0.8126 0.7631 0.0648  0.0023  0.2805  462 ARG C O   
11039 C CB  . ARG C 462 ? 0.7051 0.7844 0.8052 0.0591  -0.0149 0.2325  462 ARG C CB  
11040 C CG  . ARG C 462 ? 0.5790 0.6755 0.7080 0.0581  -0.0264 0.2035  462 ARG C CG  
11041 C CD  . ARG C 462 ? 0.5697 0.6565 0.7442 0.0589  -0.0353 0.2004  462 ARG C CD  
11042 N NE  . ARG C 462 ? 0.5548 0.6270 0.7563 0.0508  -0.0198 0.2130  462 ARG C NE  
11043 C CZ  . ARG C 462 ? 0.5755 0.6592 0.8086 0.0412  -0.0099 0.1999  462 ARG C CZ  
11044 N NH1 . ARG C 462 ? 0.5464 0.6534 0.7864 0.0402  -0.0143 0.1759  462 ARG C NH1 
11045 N NH2 . ARG C 462 ? 0.5781 0.6499 0.8355 0.0329  0.0055  0.2104  462 ARG C NH2 
11046 N N   . LEU C 463 ? 0.7537 0.8262 0.7850 0.0458  0.0307  0.2694  463 LEU C N   
11047 C CA  . LEU C 463 ? 0.7641 0.8222 0.7671 0.0433  0.0459  0.2948  463 LEU C CA  
11048 C C   . LEU C 463 ? 0.7753 0.8101 0.8079 0.0366  0.0585  0.3104  463 LEU C C   
11049 O O   . LEU C 463 ? 0.7155 0.7484 0.7929 0.0329  0.0562  0.2996  463 LEU C O   
11050 C CB  . LEU C 463 ? 0.8148 0.8882 0.7949 0.0361  0.0621  0.2901  463 LEU C CB  
11051 C CG  . LEU C 463 ? 0.7652 0.8598 0.7174 0.0403  0.0545  0.2720  463 LEU C CG  
11052 C CD1 . LEU C 463 ? 0.8045 0.9101 0.7351 0.0334  0.0732  0.2692  463 LEU C CD1 
11053 C CD2 . LEU C 463 ? 0.6662 0.7603 0.5833 0.0503  0.0404  0.2798  463 LEU C CD2 
11054 N N   . LYS C 464 ? 0.8851 0.9017 0.8915 0.0341  0.0734  0.3354  464 LYS C N   
11055 C CA  . LYS C 464 ? 0.8920 0.8817 0.9210 0.0263  0.0892  0.3520  464 LYS C CA  
11056 C C   . LYS C 464 ? 0.9007 0.8814 0.8979 0.0187  0.1116  0.3715  464 LYS C C   
11057 O O   . LYS C 464 ? 0.9427 0.9264 0.8925 0.0254  0.1091  0.3826  464 LYS C O   
11058 C CB  . LYS C 464 ? 0.9092 0.8697 0.9397 0.0372  0.0782  0.3691  464 LYS C CB  
11059 C CG  . LYS C 464 ? 1.0254 0.9535 1.0849 0.0285  0.0954  0.3834  464 LYS C CG  
11060 C CD  . LYS C 464 ? 1.0956 0.9908 1.1512 0.0421  0.0849  0.4023  464 LYS C CD  
11061 C CE  . LYS C 464 ? 1.1979 1.0558 1.2815 0.0322  0.1057  0.4164  464 LYS C CE  
11062 N NZ  . LYS C 464 ? 1.2260 1.0454 1.3004 0.0474  0.0985  0.4388  464 LYS C NZ  
11063 N N   . PRO C 465 ? 0.9123 0.8855 0.9344 0.0041  0.1338  0.3735  465 PRO C N   
11064 C CA  . PRO C 465 ? 1.0081 0.9695 1.0005 -0.0044 0.1569  0.3932  465 PRO C CA  
11065 C C   . PRO C 465 ? 1.0071 0.9315 0.9637 0.0032  0.1592  0.4259  465 PRO C C   
11066 O O   . PRO C 465 ? 0.9408 0.8445 0.9038 0.0139  0.1459  0.4343  465 PRO C O   
11067 C CB  . PRO C 465 ? 0.9058 0.8671 0.9433 -0.0220 0.1788  0.3844  465 PRO C CB  
11068 C CG  . PRO C 465 ? 0.8201 0.8102 0.9021 -0.0216 0.1657  0.3536  465 PRO C CG  
11069 C CD  . PRO C 465 ? 0.8136 0.7984 0.8923 -0.0065 0.1392  0.3521  465 PRO C CD  
11070 N N   . ILE C 466 ? 0.9840 0.9003 0.9012 -0.0014 0.1765  0.4446  466 ILE C N   
11071 C CA  . ILE C 466 ? 1.1430 1.0251 1.0174 0.0071  0.1795  0.4758  466 ILE C CA  
11072 C C   . ILE C 466 ? 1.2026 1.0523 1.0848 -0.0085 0.2058  0.4855  466 ILE C C   
11073 O O   . ILE C 466 ? 1.2536 1.1076 1.1180 -0.0211 0.2225  0.4825  466 ILE C O   
11074 C CB  . ILE C 466 ? 1.1399 1.0378 0.9574 0.0141  0.1709  0.4743  466 ILE C CB  
11075 C CG1 . ILE C 466 ? 1.1073 1.0414 0.9202 0.0256  0.1487  0.4589  466 ILE C CG1 
11076 C CG2 . ILE C 466 ? 1.1786 1.0458 0.9532 0.0258  0.1647  0.4949  466 ILE C CG2 
11077 C CD1 . ILE C 466 ? 1.0483 1.0005 0.8101 0.0311  0.1408  0.4530  466 ILE C CD1 
11078 N N   . ALA D 2   ? 0.3039 0.7515 0.2688 -0.0548 0.0061  -0.0328 2   ALA D N   
11079 C CA  . ALA D 2   ? 0.2841 0.7132 0.2501 -0.0502 0.0038  -0.0326 2   ALA D CA  
11080 C C   . ALA D 2   ? 0.2710 0.6770 0.2306 -0.0412 0.0005  -0.0270 2   ALA D C   
11081 O O   . ALA D 2   ? 0.2662 0.6686 0.2189 -0.0420 0.0008  -0.0211 2   ALA D O   
11082 C CB  . ALA D 2   ? 0.2341 0.6567 0.1968 -0.0617 0.0064  -0.0293 2   ALA D CB  
11083 N N   . LYS D 3   ? 0.2004 0.5905 0.1619 -0.0330 -0.0026 -0.0291 3   LYS D N   
11084 C CA  . LYS D 3   ? 0.2448 0.6126 0.2006 -0.0248 -0.0063 -0.0255 3   LYS D CA  
11085 C C   . LYS D 3   ? 0.2815 0.6281 0.2345 -0.0258 -0.0081 -0.0207 3   LYS D C   
11086 O O   . LYS D 3   ? 0.2774 0.6196 0.2346 -0.0242 -0.0088 -0.0244 3   LYS D O   
11087 C CB  . LYS D 3   ? 0.2653 0.6300 0.2240 -0.0134 -0.0089 -0.0322 3   LYS D CB  
11088 C CG  . LYS D 3   ? 0.3240 0.6664 0.2759 -0.0068 -0.0126 -0.0294 3   LYS D CG  
11089 C CD  . LYS D 3   ? 0.3598 0.7009 0.3124 0.0030  -0.0148 -0.0360 3   LYS D CD  
11090 C CE  . LYS D 3   ? 0.4227 0.7508 0.3779 0.0089  -0.0171 -0.0392 3   LYS D CE  
11091 N NZ  . LYS D 3   ? 0.5534 0.8755 0.5066 0.0184  -0.0198 -0.0442 3   LYS D NZ  
11092 N N   . ARG D 4   ? 0.2383 0.5725 0.1842 -0.0278 -0.0088 -0.0124 4   ARG D N   
11093 C CA  A ARG D 4   ? 0.2369 0.5511 0.1801 -0.0277 -0.0109 -0.0074 4   ARG D CA  
11094 C CA  B ARG D 4   ? 0.2370 0.5511 0.1802 -0.0277 -0.0109 -0.0075 4   ARG D CA  
11095 C C   . ARG D 4   ? 0.2573 0.5524 0.1998 -0.0180 -0.0154 -0.0093 4   ARG D C   
11096 O O   . ARG D 4   ? 0.2516 0.5440 0.1910 -0.0137 -0.0170 -0.0094 4   ARG D O   
11097 C CB  A ARG D 4   ? 0.2663 0.5758 0.2022 -0.0334 -0.0095 0.0031  4   ARG D CB  
11098 C CB  B ARG D 4   ? 0.2661 0.5757 0.2021 -0.0334 -0.0095 0.0030  4   ARG D CB  
11099 C CG  A ARG D 4   ? 0.2345 0.5602 0.1676 -0.0432 -0.0043 0.0066  4   ARG D CG  
11100 C CG  B ARG D 4   ? 0.2430 0.5632 0.1770 -0.0444 -0.0044 0.0063  4   ARG D CG  
11101 C CD  A ARG D 4   ? 0.2498 0.5660 0.1746 -0.0462 -0.0026 0.0188  4   ARG D CD  
11102 C CD  B ARG D 4   ? 0.2511 0.5668 0.1768 -0.0487 -0.0016 0.0178  4   ARG D CD  
11103 N NE  A ARG D 4   ? 0.2656 0.5918 0.1857 -0.0547 0.0035  0.0240  4   ARG D NE  
11104 N NE  B ARG D 4   ? 0.2543 0.5672 0.1758 -0.0586 0.0045  0.0235  4   ARG D NE  
11105 C CZ  A ARG D 4   ? 0.2484 0.5705 0.1650 -0.0638 0.0100  0.0295  4   ARG D CZ  
11106 C CZ  B ARG D 4   ? 0.2265 0.5224 0.1436 -0.0598 0.0060  0.0321  4   ARG D CZ  
11107 N NH1 A ARG D 4   ? 0.2596 0.5703 0.1766 -0.0660 0.0108  0.0300  4   ARG D NH1 
11108 N NH1 B ARG D 4   ? 0.2379 0.5205 0.1545 -0.0519 0.0005  0.0359  4   ARG D NH1 
11109 N NH2 A ARG D 4   ? 0.2429 0.5702 0.1557 -0.0710 0.0168  0.0347  4   ARG D NH2 
11110 N NH2 B ARG D 4   ? 0.2336 0.5244 0.1479 -0.0694 0.0142  0.0368  4   ARG D NH2 
11111 N N   . ILE D 5   ? 0.2872 0.5690 0.2319 -0.0155 -0.0175 -0.0109 5   ILE D N   
11112 C CA  . ILE D 5   ? 0.2655 0.5273 0.2088 -0.0078 -0.0217 -0.0123 5   ILE D CA  
11113 C C   . ILE D 5   ? 0.2490 0.4932 0.1892 -0.0092 -0.0236 -0.0058 5   ILE D C   
11114 O O   . ILE D 5   ? 0.2653 0.5090 0.2073 -0.0132 -0.0226 -0.0039 5   ILE D O   
11115 C CB  . ILE D 5   ? 0.2878 0.5485 0.2359 -0.0027 -0.0227 -0.0195 5   ILE D CB  
11116 C CG1 . ILE D 5   ? 0.2932 0.5727 0.2445 0.0000  -0.0208 -0.0257 5   ILE D CG1 
11117 C CG2 . ILE D 5   ? 0.2187 0.4572 0.1640 0.0036  -0.0269 -0.0198 5   ILE D CG2 
11118 C CD1 . ILE D 5   ? 0.2420 0.5276 0.1993 0.0042  -0.0206 -0.0322 5   ILE D CD1 
11119 N N   . VAL D 6   ? 0.2377 0.4686 0.1736 -0.0061 -0.0264 -0.0027 6   VAL D N   
11120 C CA  . VAL D 6   ? 0.3012 0.5183 0.2345 -0.0073 -0.0281 0.0041  6   VAL D CA  
11121 C C   . VAL D 6   ? 0.2457 0.4475 0.1813 -0.0049 -0.0305 0.0021  6   VAL D C   
11122 O O   . VAL D 6   ? 0.2271 0.4244 0.1646 -0.0009 -0.0320 -0.0038 6   VAL D O   
11123 C CB  . VAL D 6   ? 0.2934 0.5033 0.2220 -0.0051 -0.0303 0.0069  6   VAL D CB  
11124 C CG1 . VAL D 6   ? 0.2425 0.4405 0.1698 0.0002  -0.0338 0.0009  6   VAL D CG1 
11125 C CG2 . VAL D 6   ? 0.2295 0.4298 0.1563 -0.0065 -0.0313 0.0148  6   VAL D CG2 
11126 N N   . GLU D 7   ? 0.2563 0.4509 0.1915 -0.0072 -0.0307 0.0078  7   GLU D N   
11127 C CA  . GLU D 7   ? 0.2546 0.4352 0.1918 -0.0054 -0.0328 0.0066  7   GLU D CA  
11128 C C   . GLU D 7   ? 0.2591 0.4229 0.1942 -0.0007 -0.0368 0.0050  7   GLU D C   
11129 O O   . GLU D 7   ? 0.2988 0.4583 0.2305 -0.0003 -0.0381 0.0083  7   GLU D O   
11130 C CB  . GLU D 7   ? 0.2677 0.4456 0.2045 -0.0088 -0.0320 0.0136  7   GLU D CB  
11131 C CG  . GLU D 7   ? 0.1991 0.3909 0.1367 -0.0151 -0.0283 0.0154  7   GLU D CG  
11132 C CD  . GLU D 7   ? 0.2627 0.4700 0.1974 -0.0196 -0.0249 0.0190  7   GLU D CD  
11133 O OE1 . GLU D 7   ? 0.2732 0.4808 0.2055 -0.0174 -0.0256 0.0215  7   GLU D OE1 
11134 O OE2 . GLU D 7   ? 0.2832 0.5025 0.2174 -0.0262 -0.0213 0.0193  7   GLU D OE2 
11135 N N   . PRO D 8   ? 0.2054 0.3600 0.1420 0.0023  -0.0388 0.0003  8   PRO D N   
11136 C CA  . PRO D 8   ? 0.2128 0.3573 0.1475 0.0053  -0.0420 -0.0002 8   PRO D CA  
11137 C C   . PRO D 8   ? 0.1947 0.3281 0.1300 0.0044  -0.0434 0.0039  8   PRO D C   
11138 O O   . PRO D 8   ? 0.2151 0.3403 0.1507 0.0063  -0.0455 0.0025  8   PRO D O   
11139 C CB  . PRO D 8   ? 0.2015 0.3472 0.1378 0.0090  -0.0425 -0.0063 8   PRO D CB  
11140 C CG  . PRO D 8   ? 0.2097 0.3609 0.1503 0.0074  -0.0403 -0.0076 8   PRO D CG  
11141 C CD  . PRO D 8   ? 0.2244 0.3850 0.1649 0.0031  -0.0376 -0.0047 8   PRO D CD  
11142 N N   . PHE D 9   ? 0.2025 0.3359 0.1376 0.0017  -0.0421 0.0092  9   PHE D N   
11143 C CA  . PHE D 9   ? 0.1909 0.3155 0.1268 0.0011  -0.0429 0.0136  9   PHE D CA  
11144 C C   . PHE D 9   ? 0.1924 0.3232 0.1272 -0.0011 -0.0409 0.0206  9   PHE D C   
11145 O O   . PHE D 9   ? 0.2366 0.3793 0.1701 -0.0027 -0.0389 0.0220  9   PHE D O   
11146 C CB  . PHE D 9   ? 0.1721 0.2931 0.1110 0.0006  -0.0424 0.0119  9   PHE D CB  
11147 C CG  . PHE D 9   ? 0.2124 0.3487 0.1533 -0.0024 -0.0390 0.0110  9   PHE D CG  
11148 C CD1 . PHE D 9   ? 0.2147 0.3607 0.1552 -0.0064 -0.0362 0.0169  9   PHE D CD1 
11149 C CD2 . PHE D 9   ? 0.2009 0.3431 0.1438 -0.0018 -0.0383 0.0047  9   PHE D CD2 
11150 C CE1 . PHE D 9   ? 0.2012 0.3621 0.1425 -0.0111 -0.0330 0.0159  9   PHE D CE1 
11151 C CE2 . PHE D 9   ? 0.1987 0.3570 0.1438 -0.0055 -0.0350 0.0030  9   PHE D CE2 
11152 C CZ  . PHE D 9   ? 0.1839 0.3515 0.1279 -0.0109 -0.0324 0.0082  9   PHE D CZ  
11153 N N   . ARG D 10  ? 0.2022 0.3278 0.1379 -0.0013 -0.0411 0.0257  10  ARG D N   
11154 C CA  . ARG D 10  ? 0.1758 0.3092 0.1110 -0.0032 -0.0386 0.0343  10  ARG D CA  
11155 C C   . ARG D 10  ? 0.2079 0.3392 0.1452 -0.0043 -0.0373 0.0384  10  ARG D C   
11156 O O   . ARG D 10  ? 0.1552 0.2790 0.0945 -0.0033 -0.0387 0.0341  10  ARG D O   
11157 C CB  . ARG D 10  ? 0.2006 0.3311 0.1342 -0.0016 -0.0399 0.0384  10  ARG D CB  
11158 C CG  . ARG D 10  ? 0.1880 0.3062 0.1227 0.0006  -0.0426 0.0378  10  ARG D CG  
11159 C CD  . ARG D 10  ? 0.2397 0.3614 0.1732 0.0012  -0.0440 0.0403  10  ARG D CD  
11160 N NE  . ARG D 10  ? 0.2657 0.3829 0.2015 0.0021  -0.0458 0.0409  10  ARG D NE  
11161 C CZ  . ARG D 10  ? 0.2956 0.4152 0.2305 0.0021  -0.0480 0.0400  10  ARG D CZ  
11162 N NH1 . ARG D 10  ? 0.3095 0.4355 0.2411 0.0015  -0.0487 0.0382  10  ARG D NH1 
11163 N NH2 . ARG D 10  ? 0.3270 0.4429 0.2640 0.0025  -0.0494 0.0408  10  ARG D NH2 
11164 N N   . ILE D 11  ? 0.1896 0.3273 0.1259 -0.0064 -0.0343 0.0475  11  ILE D N   
11165 C CA  . ILE D 11  ? 0.1655 0.3022 0.1022 -0.0083 -0.0322 0.0526  11  ILE D CA  
11166 C C   . ILE D 11  ? 0.1647 0.2911 0.1038 -0.0047 -0.0335 0.0565  11  ILE D C   
11167 O O   . ILE D 11  ? 0.1895 0.3141 0.1288 -0.0023 -0.0340 0.0608  11  ILE D O   
11168 C CB  . ILE D 11  ? 0.2070 0.3513 0.1397 -0.0123 -0.0272 0.0623  11  ILE D CB  
11169 C CG1 . ILE D 11  ? 0.1757 0.3321 0.1059 -0.0168 -0.0256 0.0572  11  ILE D CG1 
11170 C CG2 . ILE D 11  ? 0.1787 0.3182 0.1098 -0.0148 -0.0235 0.0690  11  ILE D CG2 
11171 C CD1 . ILE D 11  ? 0.1872 0.3494 0.1120 -0.0216 -0.0195 0.0666  11  ILE D CD1 
11172 N N   . LYS D 12  ? 0.2000 0.3208 0.1411 -0.0044 -0.0342 0.0543  12  LYS D N   
11173 C CA  . LYS D 12  ? 0.2352 0.3476 0.1788 -0.0013 -0.0348 0.0583  12  LYS D CA  
11174 C C   . LYS D 12  ? 0.2155 0.3271 0.1591 -0.0021 -0.0311 0.0673  12  LYS D C   
11175 O O   . LYS D 12  ? 0.2033 0.3095 0.1490 0.0011  -0.0300 0.0740  12  LYS D O   
11176 C CB  . LYS D 12  ? 0.2383 0.3422 0.1841 0.0005  -0.0383 0.0495  12  LYS D CB  
11177 C CG  . LYS D 12  ? 0.2758 0.3724 0.2238 0.0034  -0.0396 0.0518  12  LYS D CG  
11178 C CD  . LYS D 12  ? 0.3231 0.4103 0.2714 0.0046  -0.0429 0.0434  12  LYS D CD  
11179 C CE  . LYS D 12  ? 0.3695 0.4516 0.3195 0.0066  -0.0439 0.0455  12  LYS D CE  
11180 N NZ  . LYS D 12  ? 0.2837 0.3648 0.2345 0.0062  -0.0465 0.0404  12  LYS D NZ  
11181 N N   . MET D 13  ? 0.1819 0.2980 0.1222 -0.0067 -0.0286 0.0675  13  MET D N   
11182 C CA  . MET D 13  ? 0.1748 0.2865 0.1124 -0.0088 -0.0228 0.0774  13  MET D CA  
11183 C C   . MET D 13  ? 0.1828 0.2940 0.1199 -0.0158 -0.0153 0.0747  13  MET D C   
11184 O O   . MET D 13  ? 0.2030 0.3236 0.1388 -0.0198 -0.0174 0.0651  13  MET D O   
11185 C CB  . MET D 13  ? 0.1724 0.2780 0.1136 -0.0086 -0.0236 0.0719  13  MET D CB  
11186 C CG  . MET D 13  ? 0.1803 0.2697 0.1264 -0.0095 -0.0141 0.0755  13  MET D CG  
11187 S SD  . MET D 13  ? 0.3809 0.4640 0.3316 -0.0100 -0.0145 0.0662  13  MET D SD  
11188 C CE  . MET D 13  ? 0.2092 0.3003 0.1583 -0.0026 -0.0252 0.0701  13  MET D CE  
11189 N N   . VAL D 14  ? 0.1966 0.2957 0.1351 -0.0172 -0.0060 0.0828  14  VAL D N   
11190 C CA  . VAL D 14  ? 0.2073 0.3029 0.1459 -0.0247 0.0027  0.0810  14  VAL D CA  
11191 C C   . VAL D 14  ? 0.2201 0.2989 0.1638 -0.0290 0.0117  0.0777  14  VAL D C   
11192 O O   . VAL D 14  ? 0.2180 0.2857 0.1646 -0.0247 0.0128  0.0807  14  VAL D O   
11193 C CB  . VAL D 14  ? 0.2193 0.3141 0.1539 -0.0236 0.0071  0.0936  14  VAL D CB  
11194 C CG1 . VAL D 14  ? 0.2160 0.3286 0.1451 -0.0200 -0.0017 0.0955  14  VAL D CG1 
11195 C CG2 . VAL D 14  ? 0.2296 0.3104 0.1655 -0.0174 0.0115  0.1066  14  VAL D CG2 
11196 N N   . GLU D 15  ? 0.2238 0.3011 0.1683 -0.0380 0.0186  0.0711  15  GLU D N   
11197 C CA  . GLU D 15  ? 0.2625 0.3237 0.2111 -0.0444 0.0286  0.0668  15  GLU D CA  
11198 C C   . GLU D 15  ? 0.2834 0.3374 0.2304 -0.0515 0.0390  0.0712  15  GLU D C   
11199 O O   . GLU D 15  ? 0.2866 0.3542 0.2313 -0.0564 0.0380  0.0680  15  GLU D O   
11200 C CB  . GLU D 15  ? 0.2360 0.3051 0.1877 -0.0503 0.0261  0.0509  15  GLU D CB  
11201 C CG  . GLU D 15  ? 0.3338 0.3893 0.2892 -0.0590 0.0363  0.0438  15  GLU D CG  
11202 C CD  . GLU D 15  ? 0.4061 0.4742 0.3640 -0.0651 0.0330  0.0279  15  GLU D CD  
11203 O OE1 . GLU D 15  ? 0.3444 0.4321 0.3010 -0.0666 0.0269  0.0222  15  GLU D OE1 
11204 O OE2 . GLU D 15  ? 0.5233 0.5827 0.4843 -0.0680 0.0365  0.0212  15  GLU D OE2 
11205 N N   . LYS D 16  ? 0.3294 0.3620 0.2773 -0.0516 0.0492  0.0792  16  LYS D N   
11206 C CA  . LYS D 16  ? 0.3492 0.3719 0.2947 -0.0578 0.0599  0.0855  16  LYS D CA  
11207 C C   . LYS D 16  ? 0.3666 0.3914 0.3142 -0.0715 0.0659  0.0722  16  LYS D C   
11208 O O   . LYS D 16  ? 0.3622 0.3852 0.3137 -0.0762 0.0664  0.0601  16  LYS D O   
11209 C CB  . LYS D 16  ? 0.4228 0.4195 0.3688 -0.0539 0.0700  0.0969  16  LYS D CB  
11210 C CG  . LYS D 16  ? 0.4075 0.3891 0.3507 -0.0602 0.0828  0.1046  16  LYS D CG  
11211 C CD  . LYS D 16  ? 0.4624 0.4177 0.4057 -0.0534 0.0919  0.1173  16  LYS D CD  
11212 C CE  . LYS D 16  ? 0.5618 0.5012 0.5010 -0.0576 0.1043  0.1281  16  LYS D CE  
11213 N NZ  . LYS D 16  ? 0.6358 0.5518 0.5742 -0.0477 0.1119  0.1434  16  LYS D NZ  
11214 N N   . ILE D 17  ? 0.3690 0.3996 0.3137 -0.0782 0.0702  0.0742  17  ILE D N   
11215 C CA  . ILE D 17  ? 0.3498 0.3810 0.2965 -0.0924 0.0781  0.0634  17  ILE D CA  
11216 C C   . ILE D 17  ? 0.4063 0.4230 0.3496 -0.0979 0.0901  0.0737  17  ILE D C   
11217 O O   . ILE D 17  ? 0.4782 0.4942 0.4168 -0.0909 0.0895  0.0879  17  ILE D O   
11218 C CB  . ILE D 17  ? 0.3785 0.4383 0.3259 -0.0970 0.0702  0.0513  17  ILE D CB  
11219 C CG1 . ILE D 17  ? 0.4088 0.4844 0.3512 -0.0930 0.0655  0.0593  17  ILE D CG1 
11220 C CG2 . ILE D 17  ? 0.4005 0.4727 0.3509 -0.0917 0.0592  0.0411  17  ILE D CG2 
11221 C CD1 . ILE D 17  ? 0.3685 0.4716 0.3115 -0.0971 0.0591  0.0477  17  ILE D CD1 
11222 N N   . ARG D 18  ? 0.4729 0.4782 0.4182 -0.1109 0.1013  0.0666  18  ARG D N   
11223 C CA  . ARG D 18  ? 0.5233 0.5103 0.4654 -0.1178 0.1147  0.0757  18  ARG D CA  
11224 C C   . ARG D 18  ? 0.5236 0.5189 0.4676 -0.1348 0.1212  0.0632  18  ARG D C   
11225 O O   . ARG D 18  ? 0.5100 0.5148 0.4588 -0.1420 0.1191  0.0473  18  ARG D O   
11226 C CB  . ARG D 18  ? 0.5792 0.5323 0.5216 -0.1156 0.1253  0.0825  18  ARG D CB  
11227 C CG  . ARG D 18  ? 0.6708 0.6007 0.6087 -0.1201 0.1396  0.0950  18  ARG D CG  
11228 C CD  . ARG D 18  ? 0.7142 0.6100 0.6536 -0.1229 0.1524  0.0951  18  ARG D CD  
11229 N NE  . ARG D 18  ? 0.7419 0.6381 0.6861 -0.1358 0.1552  0.0757  18  ARG D NE  
11230 C CZ  . ARG D 18  ? 0.8504 0.7247 0.7960 -0.1466 0.1674  0.0694  18  ARG D CZ  
11231 N NH1 . ARG D 18  ? 0.8786 0.7297 0.8222 -0.1442 0.1755  0.0803  18  ARG D NH1 
11232 N NH2 . ARG D 18  ? 0.8424 0.7216 0.7923 -0.1582 0.1684  0.0508  18  ARG D NH2 
11233 N N   . VAL D 19  ? 0.5397 0.5332 0.4798 -0.1414 0.1290  0.0705  19  VAL D N   
11234 C CA  . VAL D 19  ? 0.5956 0.5949 0.5374 -0.1589 0.1373  0.0601  19  VAL D CA  
11235 C C   . VAL D 19  ? 0.6640 0.6299 0.6059 -0.1659 0.1521  0.0637  19  VAL D C   
11236 O O   . VAL D 19  ? 0.6574 0.6052 0.5955 -0.1597 0.1574  0.0797  19  VAL D O   
11237 C CB  . VAL D 19  ? 0.5592 0.5807 0.4975 -0.1618 0.1356  0.0642  19  VAL D CB  
11238 C CG1 . VAL D 19  ? 0.5898 0.6022 0.5211 -0.1509 0.1362  0.0843  19  VAL D CG1 
11239 C CG2 . VAL D 19  ? 0.5664 0.5884 0.5083 -0.1756 0.1437  0.0560  19  VAL D CG2 
11240 N N   . PRO D 20  ? 0.6856 0.6436 0.6326 -0.1757 0.1567  0.0492  20  PRO D N   
11241 C CA  . PRO D 20  ? 0.7548 0.6813 0.7023 -0.1806 0.1687  0.0510  20  PRO D CA  
11242 C C   . PRO D 20  ? 0.8073 0.7339 0.7535 -0.1884 0.1748  0.0548  20  PRO D C   
11243 O O   . PRO D 20  ? 0.7736 0.7262 0.7212 -0.1956 0.1712  0.0475  20  PRO D O   
11244 C CB  . PRO D 20  ? 0.7388 0.6645 0.6912 -0.1906 0.1702  0.0314  20  PRO D CB  
11245 C CG  . PRO D 20  ? 0.6541 0.6168 0.6096 -0.1941 0.1594  0.0188  20  PRO D CG  
11246 C CD  . PRO D 20  ? 0.5792 0.5565 0.5312 -0.1817 0.1506  0.0307  20  PRO D CD  
11247 N N   . SER D 21  ? 0.8529 0.7505 0.7963 -0.1862 0.1840  0.0667  21  SER D N   
11248 C CA  . SER D 21  ? 0.9105 0.8039 0.8525 -0.1946 0.1914  0.0706  21  SER D CA  
11249 C C   . SER D 21  ? 0.9013 0.8028 0.8473 -0.2114 0.1949  0.0513  21  SER D C   
11250 O O   . SER D 21  ? 0.8484 0.7463 0.7975 -0.2164 0.1952  0.0367  21  SER D O   
11251 C CB  . SER D 21  ? 0.9752 0.8331 0.9136 -0.1900 0.2010  0.0841  21  SER D CB  
11252 O OG  . SER D 21  ? 0.9833 0.8334 0.9186 -0.1734 0.1968  0.0997  21  SER D OG  
11253 N N   . ARG D 22  ? 0.9598 0.8739 0.9056 -0.2201 0.1974  0.0510  22  ARG D N   
11254 C CA  . ARG D 22  ? 0.9292 0.8561 0.8786 -0.2357 0.1994  0.0325  22  ARG D CA  
11255 C C   . ARG D 22  ? 0.9639 0.8620 0.9133 -0.2445 0.2096  0.0242  22  ARG D C   
11256 O O   . ARG D 22  ? 0.9148 0.8217 0.8672 -0.2549 0.2094  0.0059  22  ARG D O   
11257 C CB  . ARG D 22  ? 0.9915 0.9346 0.9403 -0.2432 0.2014  0.0349  22  ARG D CB  
11258 C CG  . ARG D 22  ? 0.9460 0.9106 0.8986 -0.2579 0.2007  0.0148  22  ARG D CG  
11259 C CD  . ARG D 22  ? 0.9676 0.9452 0.9197 -0.2667 0.2044  0.0164  22  ARG D CD  
11260 N NE  . ARG D 22  ? 1.0058 1.0023 0.9612 -0.2808 0.2041  -0.0031 22  ARG D NE  
11261 C CZ  . ARG D 22  ? 1.0493 1.0822 1.0076 -0.2821 0.1948  -0.0136 22  ARG D CZ  
11262 N NH1 . ARG D 22  ? 1.0426 1.0968 1.0009 -0.2708 0.1853  -0.0073 22  ARG D NH1 
11263 N NH2 . ARG D 22  ? 1.0538 1.1026 1.0146 -0.2947 0.1951  -0.0310 22  ARG D NH2 
11264 N N   . GLU D 23  ? 1.2404 1.1049 1.1861 -0.2399 0.2183  0.0372  23  GLU D N   
11265 C CA  . GLU D 23  ? 1.2679 1.1023 1.2128 -0.2458 0.2279  0.0294  23  GLU D CA  
11266 C C   . GLU D 23  ? 1.2564 1.0915 1.2040 -0.2425 0.2233  0.0174  23  GLU D C   
11267 O O   . GLU D 23  ? 1.2879 1.1234 1.2373 -0.2532 0.2260  -0.0003 23  GLU D O   
11268 C CB  . GLU D 23  ? 1.2975 1.0965 1.2376 -0.2377 0.2366  0.0470  23  GLU D CB  
11269 C CG  . GLU D 23  ? 1.3199 1.1146 1.2568 -0.2423 0.2428  0.0586  23  GLU D CG  
11270 C CD  . GLU D 23  ? 1.3021 1.1191 1.2379 -0.2331 0.2350  0.0740  23  GLU D CD  
11271 O OE1 . GLU D 23  ? 1.2699 1.1033 1.2070 -0.2224 0.2249  0.0764  23  GLU D OE1 
11272 O OE2 . GLU D 23  ? 1.3159 1.1341 1.2493 -0.2368 0.2390  0.0836  23  GLU D OE2 
11273 N N   . GLU D 24  ? 0.9988 0.8356 0.9464 -0.2278 0.2162  0.0267  24  GLU D N   
11274 C CA  . GLU D 24  ? 0.9248 0.7664 0.8754 -0.2244 0.2106  0.0159  24  GLU D CA  
11275 C C   . GLU D 24  ? 0.8893 0.7677 0.8440 -0.2323 0.2015  -0.0005 24  GLU D C   
11276 O O   . GLU D 24  ? 0.8605 0.7436 0.8177 -0.2381 0.2004  -0.0167 24  GLU D O   
11277 C CB  . GLU D 24  ? 0.9105 0.7485 0.8600 -0.2069 0.2045  0.0304  24  GLU D CB  
11278 C CG  . GLU D 24  ? 0.9790 0.7853 0.9243 -0.1960 0.2114  0.0486  24  GLU D CG  
11279 C CD  . GLU D 24  ? 0.9194 0.7286 0.8634 -0.1785 0.2038  0.0636  24  GLU D CD  
11280 O OE1 . GLU D 24  ? 0.8653 0.7023 0.8106 -0.1757 0.1936  0.0623  24  GLU D OE1 
11281 O OE2 . GLU D 24  ? 0.9016 0.6860 0.8430 -0.1672 0.2079  0.0764  24  GLU D OE2 
11282 N N   . ARG D 25  ? 0.9045 0.8102 0.8597 -0.2320 0.1948  0.0036  25  ARG D N   
11283 C CA  . ARG D 25  ? 0.8304 0.7733 0.7893 -0.2368 0.1849  -0.0105 25  ARG D CA  
11284 C C   . ARG D 25  ? 0.8925 0.8432 0.8533 -0.2526 0.1888  -0.0287 25  ARG D C   
11285 O O   . ARG D 25  ? 0.7449 0.7169 0.7088 -0.2565 0.1824  -0.0443 25  ARG D O   
11286 C CB  . ARG D 25  ? 0.7712 0.7389 0.7293 -0.2323 0.1783  -0.0014 25  ARG D CB  
11287 C CG  . ARG D 25  ? 0.8061 0.8115 0.7674 -0.2303 0.1656  -0.0112 25  ARG D CG  
11288 C CD  . ARG D 25  ? 0.7616 0.7839 0.7205 -0.2201 0.1587  0.0018  25  ARG D CD  
11289 N NE  . ARG D 25  ? 0.8301 0.8596 0.7873 -0.2251 0.1623  0.0069  25  ARG D NE  
11290 C CZ  . ARG D 25  ? 0.7945 0.8074 0.7474 -0.2208 0.1681  0.0238  25  ARG D CZ  
11291 N NH1 . ARG D 25  ? 0.8382 0.8265 0.7877 -0.2107 0.1707  0.0379  25  ARG D NH1 
11292 N NH2 . ARG D 25  ? 0.7781 0.8006 0.7300 -0.2262 0.1712  0.0270  25  ARG D NH2 
11293 N N   . GLU D 26  ? 0.9094 0.8438 0.8680 -0.2617 0.1991  -0.0268 26  GLU D N   
11294 C CA  . GLU D 26  ? 0.8916 0.8337 0.8511 -0.2774 0.2034  -0.0438 26  GLU D CA  
11295 C C   . GLU D 26  ? 0.8622 0.7820 0.8208 -0.2828 0.2102  -0.0553 26  GLU D C   
11296 O O   . GLU D 26  ? 0.8624 0.7974 0.8223 -0.2930 0.2093  -0.0731 26  GLU D O   
11297 C CB  . GLU D 26  ? 0.9814 0.9154 0.9385 -0.2858 0.2121  -0.0374 26  GLU D CB  
11298 C CG  . GLU D 26  ? 1.0799 1.0320 1.0380 -0.3018 0.2143  -0.0536 26  GLU D CG  
11299 C CD  . GLU D 26  ? 1.2138 1.1567 1.1695 -0.3099 0.2233  -0.0460 26  GLU D CD  
11300 O OE1 . GLU D 26  ? 1.1496 1.0753 1.1030 -0.3020 0.2266  -0.0275 26  GLU D OE1 
11301 O OE2 . GLU D 26  ? 1.3276 1.2811 1.2834 -0.3241 0.2271  -0.0583 26  GLU D OE2 
11302 N N   . ALA D 27  ? 0.8837 0.7687 0.8399 -0.2756 0.2170  -0.0454 27  ALA D N   
11303 C CA  . ALA D 27  ? 0.9134 0.7777 0.8687 -0.2786 0.2230  -0.0563 27  ALA D CA  
11304 C C   . ALA D 27  ? 0.8525 0.7382 0.8112 -0.2749 0.2130  -0.0677 27  ALA D C   
11305 O O   . ALA D 27  ? 0.8319 0.7202 0.7907 -0.2827 0.2147  -0.0843 27  ALA D O   
11306 C CB  . ALA D 27  ? 0.8654 0.6897 0.8175 -0.2688 0.2314  -0.0420 27  ALA D CB  
11307 N N   . ALA D 28  ? 0.8558 0.7578 0.8166 -0.2630 0.2024  -0.0591 28  ALA D N   
11308 C CA  . ALA D 28  ? 0.8233 0.7473 0.7874 -0.2589 0.1921  -0.0688 28  ALA D CA  
11309 C C   . ALA D 28  ? 0.8269 0.7874 0.7933 -0.2684 0.1853  -0.0855 28  ALA D C   
11310 O O   . ALA D 28  ? 0.8091 0.7835 0.7771 -0.2698 0.1805  -0.0989 28  ALA D O   
11311 C CB  . ALA D 28  ? 0.7561 0.6894 0.7214 -0.2444 0.1828  -0.0550 28  ALA D CB  
11312 N N   . LEU D 29  ? 0.8022 0.7797 0.7687 -0.2743 0.1847  -0.0846 29  LEU D N   
11313 C CA  . LEU D 29  ? 0.8062 0.8187 0.7744 -0.2826 0.1785  -0.1002 29  LEU D CA  
11314 C C   . LEU D 29  ? 0.8537 0.8592 0.8199 -0.2965 0.1870  -0.1157 29  LEU D C   
11315 O O   . LEU D 29  ? 0.8184 0.8490 0.7854 -0.3011 0.1820  -0.1310 29  LEU D O   
11316 C CB  . LEU D 29  ? 0.7764 0.8097 0.7451 -0.2844 0.1756  -0.0947 29  LEU D CB  
11317 C CG  . LEU D 29  ? 0.7439 0.8170 0.7145 -0.2903 0.1679  -0.1090 29  LEU D CG  
11318 C CD1 . LEU D 29  ? 0.5947 0.6921 0.5677 -0.2821 0.1560  -0.1167 29  LEU D CD1 
11319 C CD2 . LEU D 29  ? 0.7432 0.8356 0.7144 -0.2893 0.1645  -0.1015 29  LEU D CD2 
11320 N N   . LYS D 30  ? 0.8291 0.8013 0.7921 -0.3028 0.2001  -0.1119 30  LYS D N   
11321 C CA  . LYS D 30  ? 0.8805 0.8426 0.8409 -0.3159 0.2093  -0.1267 30  LYS D CA  
11322 C C   . LYS D 30  ? 0.8649 0.8270 0.8254 -0.3133 0.2071  -0.1378 30  LYS D C   
11323 O O   . LYS D 30  ? 0.8971 0.8817 0.8575 -0.3207 0.2047  -0.1541 30  LYS D O   
11324 C CB  . LYS D 30  ? 0.9221 0.8438 0.8786 -0.3205 0.2239  -0.1188 30  LYS D CB  
11325 C CG  . LYS D 30  ? 0.9922 0.9150 0.9477 -0.3274 0.2283  -0.1116 30  LYS D CG  
11326 C CD  . LYS D 30  ? 0.9941 0.8762 0.9454 -0.3320 0.2431  -0.1041 30  LYS D CD  
11327 C CE  . LYS D 30  ? 1.0901 0.9742 1.0403 -0.3384 0.2472  -0.0957 30  LYS D CE  
11328 N NZ  . LYS D 30  ? 1.1119 0.9570 1.0576 -0.3436 0.2619  -0.0888 30  LYS D NZ  
11329 N N   . GLU D 31  ? 0.8465 0.7853 0.8073 -0.3022 0.2076  -0.1288 31  GLU D N   
11330 C CA  . GLU D 31  ? 0.8348 0.7730 0.7959 -0.2992 0.2058  -0.1385 31  GLU D CA  
11331 C C   . GLU D 31  ? 0.7680 0.7461 0.7324 -0.2950 0.1915  -0.1461 31  GLU D C   
11332 O O   . GLU D 31  ? 0.7350 0.7244 0.6993 -0.2969 0.1895  -0.1591 31  GLU D O   
11333 C CB  . GLU D 31  ? 0.7839 0.6902 0.7448 -0.2871 0.2088  -0.1259 31  GLU D CB  
11334 C CG  . GLU D 31  ? 0.7889 0.6879 0.7495 -0.2851 0.2099  -0.1359 31  GLU D CG  
11335 C CD  . GLU D 31  ? 0.9829 0.8427 0.9421 -0.2760 0.2178  -0.1250 31  GLU D CD  
11336 O OE1 . GLU D 31  ? 1.0109 0.8527 0.9695 -0.2687 0.2201  -0.1079 31  GLU D OE1 
11337 O OE2 . GLU D 31  ? 0.9964 0.8441 0.9546 -0.2755 0.2219  -0.1331 31  GLU D OE2 
11338 N N   . ALA D 32  ? 0.7919 0.7924 0.7590 -0.2887 0.1817  -0.1379 32  ALA D N   
11339 C CA  . ALA D 32  ? 0.7745 0.8136 0.7444 -0.2836 0.1680  -0.1442 32  ALA D CA  
11340 C C   . ALA D 32  ? 0.8288 0.8976 0.7977 -0.2938 0.1664  -0.1598 32  ALA D C   
11341 O O   . ALA D 32  ? 0.8159 0.9161 0.7861 -0.2895 0.1563  -0.1670 32  ALA D O   
11342 C CB  . ALA D 32  ? 0.6273 0.6810 0.5997 -0.2739 0.1589  -0.1309 32  ALA D CB  
11343 N N   . GLY D 33  ? 0.8390 0.8990 0.8053 -0.3066 0.1764  -0.1645 33  GLY D N   
11344 C CA  . GLY D 33  ? 0.8352 0.9243 0.8003 -0.3168 0.1756  -0.1786 33  GLY D CA  
11345 C C   . GLY D 33  ? 0.8362 0.9608 0.8035 -0.3129 0.1650  -0.1767 33  GLY D C   
11346 O O   . GLY D 33  ? 0.8842 1.0417 0.8512 -0.3145 0.1592  -0.1878 33  GLY D O   
11347 N N   . TYR D 34  ? 0.7656 0.8848 0.7347 -0.3069 0.1626  -0.1625 34  TYR D N   
11348 C CA  . TYR D 34  ? 0.7522 0.9025 0.7230 -0.3039 0.1542  -0.1600 34  TYR D CA  
11349 C C   . TYR D 34  ? 0.7607 0.9454 0.7331 -0.2936 0.1408  -0.1654 34  TYR D C   
11350 O O   . TYR D 34  ? 0.7919 1.0090 0.7643 -0.2941 0.1351  -0.1716 34  TYR D O   
11351 C CB  . TYR D 34  ? 0.8075 0.9687 0.7764 -0.3179 0.1604  -0.1680 34  TYR D CB  
11352 C CG  . TYR D 34  ? 0.8387 0.9649 0.8057 -0.3277 0.1740  -0.1621 34  TYR D CG  
11353 C CD1 . TYR D 34  ? 0.8237 0.9400 0.7913 -0.3260 0.1763  -0.1479 34  TYR D CD1 
11354 C CD2 . TYR D 34  ? 0.8636 0.9662 0.8276 -0.3379 0.1851  -0.1701 34  TYR D CD2 
11355 C CE1 . TYR D 34  ? 0.7458 0.8295 0.7111 -0.3338 0.1890  -0.1412 34  TYR D CE1 
11356 C CE2 . TYR D 34  ? 0.8527 0.9216 0.8143 -0.3458 0.1979  -0.1642 34  TYR D CE2 
11357 C CZ  . TYR D 34  ? 0.8240 0.8836 0.7864 -0.3435 0.1997  -0.1493 34  TYR D CZ  
11358 O OH  . TYR D 34  ? 0.9094 0.9353 0.8689 -0.3505 0.2126  -0.1423 34  TYR D OH  
11359 N N   . ASN D 35  ? 0.7314 0.9085 0.7050 -0.2837 0.1362  -0.1626 35  ASN D N   
11360 C CA  . ASN D 35  ? 0.6741 0.8794 0.6491 -0.2715 0.1234  -0.1644 35  ASN D CA  
11361 C C   . ASN D 35  ? 0.6516 0.8427 0.6290 -0.2591 0.1183  -0.1511 35  ASN D C   
11362 O O   . ASN D 35  ? 0.6305 0.7958 0.6079 -0.2579 0.1225  -0.1486 35  ASN D O   
11363 C CB  . ASN D 35  ? 0.6523 0.8681 0.6259 -0.2728 0.1230  -0.1771 35  ASN D CB  
11364 C CG  . ASN D 35  ? 0.6617 0.9071 0.6365 -0.2592 0.1107  -0.1778 35  ASN D CG  
11365 O OD1 . ASN D 35  ? 0.6633 0.9262 0.6393 -0.2501 0.1023  -0.1715 35  ASN D OD1 
11366 N ND2 . ASN D 35  ? 0.6820 0.9327 0.6565 -0.2570 0.1101  -0.1849 35  ASN D ND2 
11367 N N   . PRO D 36  ? 0.6884 0.8952 0.6674 -0.2497 0.1099  -0.1426 36  PRO D N   
11368 C CA  . PRO D 36  ? 0.5855 0.7781 0.5664 -0.2389 0.1062  -0.1291 36  PRO D CA  
11369 C C   . PRO D 36  ? 0.5140 0.7064 0.4959 -0.2305 0.1002  -0.1311 36  PRO D C   
11370 O O   . PRO D 36  ? 0.5246 0.6957 0.5076 -0.2252 0.1013  -0.1217 36  PRO D O   
11371 C CB  . PRO D 36  ? 0.4983 0.7149 0.4801 -0.2310 0.0977  -0.1227 36  PRO D CB  
11372 C CG  . PRO D 36  ? 0.4495 0.6830 0.4300 -0.2401 0.1004  -0.1300 36  PRO D CG  
11373 C CD  . PRO D 36  ? 0.6126 0.8501 0.5915 -0.2486 0.1041  -0.1445 36  PRO D CD  
11374 N N   . PHE D 37  ? 0.5398 0.7554 0.5209 -0.2285 0.0946  -0.1423 37  PHE D N   
11375 C CA  . PHE D 37  ? 0.4980 0.7141 0.4798 -0.2200 0.0891  -0.1439 37  PHE D CA  
11376 C C   . PHE D 37  ? 0.4727 0.6573 0.4543 -0.2260 0.0980  -0.1452 37  PHE D C   
11377 O O   . PHE D 37  ? 0.4505 0.6275 0.4332 -0.2187 0.0944  -0.1427 37  PHE D O   
11378 C CB  . PHE D 37  ? 0.5116 0.7578 0.4924 -0.2167 0.0840  -0.1543 37  PHE D CB  
11379 C CG  . PHE D 37  ? 0.4155 0.6863 0.3976 -0.2010 0.0722  -0.1495 37  PHE D CG  
11380 C CD1 . PHE D 37  ? 0.4459 0.7129 0.4298 -0.1893 0.0655  -0.1443 37  PHE D CD1 
11381 C CD2 . PHE D 37  ? 0.4476 0.7443 0.4294 -0.1973 0.0683  -0.1497 37  PHE D CD2 
11382 C CE1 . PHE D 37  ? 0.4394 0.7257 0.4253 -0.1737 0.0556  -0.1384 37  PHE D CE1 
11383 C CE2 . PHE D 37  ? 0.4524 0.7689 0.4363 -0.1815 0.0592  -0.1442 37  PHE D CE2 
11384 C CZ  . PHE D 37  ? 0.4751 0.7852 0.4616 -0.1695 0.0529  -0.1380 37  PHE D CZ  
11385 N N   . LEU D 38  ? 0.5493 0.7148 0.5291 -0.2385 0.1098  -0.1490 38  LEU D N   
11386 C CA  . LEU D 38  ? 0.5550 0.6884 0.5337 -0.2438 0.1198  -0.1506 38  LEU D CA  
11387 C C   . LEU D 38  ? 0.5500 0.6493 0.5291 -0.2429 0.1271  -0.1366 38  LEU D C   
11388 O O   . LEU D 38  ? 0.4981 0.5669 0.4757 -0.2465 0.1370  -0.1364 38  LEU D O   
11389 C CB  . LEU D 38  ? 0.6442 0.7749 0.6200 -0.2575 0.1296  -0.1632 38  LEU D CB  
11390 C CG  . LEU D 38  ? 0.6588 0.8195 0.6336 -0.2591 0.1257  -0.1770 38  LEU D CG  
11391 C CD1 . LEU D 38  ? 0.7172 0.8729 0.6890 -0.2740 0.1369  -0.1886 38  LEU D CD1 
11392 C CD2 . LEU D 38  ? 0.6427 0.8048 0.6185 -0.2507 0.1209  -0.1788 38  LEU D CD2 
11393 N N   . LEU D 39  ? 0.4852 0.5892 0.4656 -0.2372 0.1231  -0.1244 39  LEU D N   
11394 C CA  . LEU D 39  ? 0.4370 0.5117 0.4168 -0.2334 0.1294  -0.1085 39  LEU D CA  
11395 C C   . LEU D 39  ? 0.4664 0.5328 0.4476 -0.2221 0.1248  -0.1007 39  LEU D C   
11396 O O   . LEU D 39  ? 0.4013 0.4925 0.3849 -0.2148 0.1133  -0.1027 39  LEU D O   
11397 C CB  . LEU D 39  ? 0.4768 0.5627 0.4565 -0.2311 0.1269  -0.0983 39  LEU D CB  
11398 C CG  . LEU D 39  ? 0.6049 0.6892 0.5828 -0.2417 0.1343  -0.0998 39  LEU D CG  
11399 C CD1 . LEU D 39  ? 0.5414 0.6509 0.5200 -0.2378 0.1272  -0.0940 39  LEU D CD1 
11400 C CD2 . LEU D 39  ? 0.6131 0.6585 0.5882 -0.2448 0.1474  -0.0896 39  LEU D CD2 
11401 N N   . PRO D 40  ? 0.4710 0.5031 0.4506 -0.2198 0.1336  -0.0915 40  PRO D N   
11402 C CA  . PRO D 40  ? 0.4306 0.4543 0.4105 -0.2068 0.1289  -0.0812 40  PRO D CA  
11403 C C   . PRO D 40  ? 0.3883 0.4180 0.3659 -0.1941 0.1217  -0.0653 40  PRO D C   
11404 O O   . PRO D 40  ? 0.4165 0.4459 0.3929 -0.1994 0.1266  -0.0594 40  PRO D O   
11405 C CB  . PRO D 40  ? 0.3996 0.3830 0.3773 -0.2074 0.1416  -0.0765 40  PRO D CB  
11406 C CG  . PRO D 40  ? 0.4514 0.4196 0.4267 -0.2167 0.1521  -0.0755 40  PRO D CG  
11407 C CD  . PRO D 40  ? 0.4557 0.4543 0.4323 -0.2264 0.1475  -0.0888 40  PRO D CD  
11408 N N   . SER D 41  ? 0.3415 0.3775 0.3183 -0.1777 0.1099  -0.0586 41  SER D N   
11409 C CA  . SER D 41  ? 0.3727 0.4168 0.3471 -0.1656 0.1019  -0.0450 41  SER D CA  
11410 C C   . SER D 41  ? 0.4005 0.4175 0.3716 -0.1627 0.1108  -0.0291 41  SER D C   
11411 O O   . SER D 41  ? 0.4176 0.4416 0.3862 -0.1582 0.1078  -0.0189 41  SER D O   
11412 C CB  . SER D 41  ? 0.3061 0.3590 0.2801 -0.1497 0.0887  -0.0412 41  SER D CB  
11413 O OG  . SER D 41  ? 0.3142 0.3417 0.2874 -0.1428 0.0922  -0.0353 41  SER D OG  
11414 N N   . SER D 42  ? 0.4242 0.4103 0.3946 -0.1648 0.1217  -0.0266 42  SER D N   
11415 C CA  . SER D 42  ? 0.4260 0.3847 0.3929 -0.1619 0.1313  -0.0111 42  SER D CA  
11416 C C   . SER D 42  ? 0.4757 0.4354 0.4410 -0.1740 0.1396  -0.0094 42  SER D C   
11417 O O   . SER D 42  ? 0.5613 0.5053 0.5228 -0.1701 0.1451  0.0055  42  SER D O   
11418 C CB  . SER D 42  ? 0.4104 0.3358 0.3773 -0.1634 0.1430  -0.0114 42  SER D CB  
11419 O OG  . SER D 42  ? 0.4507 0.3726 0.4194 -0.1809 0.1522  -0.0272 42  SER D OG  
11420 N N   . ALA D 43  ? 0.4418 0.4204 0.4099 -0.1887 0.1408  -0.0241 43  ALA D N   
11421 C CA  . ALA D 43  ? 0.4658 0.4476 0.4329 -0.2003 0.1478  -0.0241 43  ALA D CA  
11422 C C   . ALA D 43  ? 0.4909 0.5063 0.4582 -0.1988 0.1384  -0.0230 43  ALA D C   
11423 O O   . ALA D 43  ? 0.4849 0.5073 0.4518 -0.2053 0.1410  -0.0236 43  ALA D O   
11424 C CB  . ALA D 43  ? 0.5489 0.5305 0.5185 -0.2138 0.1529  -0.0412 43  ALA D CB  
11425 N N   . VAL D 44  ? 0.4515 0.4863 0.4192 -0.1852 0.1242  -0.0214 44  VAL D N   
11426 C CA  . VAL D 44  ? 0.4633 0.5305 0.4312 -0.1816 0.1139  -0.0221 44  VAL D CA  
11427 C C   . VAL D 44  ? 0.4210 0.4846 0.3842 -0.1663 0.1078  -0.0053 44  VAL D C   
11428 O O   . VAL D 44  ? 0.4313 0.4809 0.3931 -0.1541 0.1038  0.0024  44  VAL D O   
11429 C CB  . VAL D 44  ? 0.3777 0.4725 0.3494 -0.1785 0.1019  -0.0355 44  VAL D CB  
11430 C CG1 . VAL D 44  ? 0.3437 0.4684 0.3148 -0.1714 0.0909  -0.0344 44  VAL D CG1 
11431 C CG2 . VAL D 44  ? 0.4294 0.5337 0.4057 -0.1951 0.1077  -0.0527 44  VAL D CG2 
11432 N N   . TYR D 45  ? 0.4105 0.4878 0.3712 -0.1675 0.1074  0.0002  45  TYR D N   
11433 C CA  . TYR D 45  ? 0.3910 0.4712 0.3470 -0.1538 0.1004  0.0144  45  TYR D CA  
11434 C C   . TYR D 45  ? 0.3760 0.4824 0.3330 -0.1435 0.0851  0.0088  45  TYR D C   
11435 O O   . TYR D 45  ? 0.4379 0.5396 0.3951 -0.1328 0.0777  0.0102  45  TYR D O   
11436 C CB  . TYR D 45  ? 0.4301 0.5151 0.3825 -0.1593 0.1063  0.0221  45  TYR D CB  
11437 C CG  . TYR D 45  ? 0.4544 0.5459 0.4013 -0.1461 0.0989  0.0356  45  TYR D CG  
11438 C CD1 . TYR D 45  ? 0.4076 0.4828 0.3517 -0.1330 0.0954  0.0476  45  TYR D CD1 
11439 C CD2 . TYR D 45  ? 0.4583 0.5735 0.4029 -0.1472 0.0956  0.0360  45  TYR D CD2 
11440 C CE1 . TYR D 45  ? 0.4824 0.5652 0.4213 -0.1218 0.0885  0.0592  45  TYR D CE1 
11441 C CE2 . TYR D 45  ? 0.3973 0.5190 0.3363 -0.1357 0.0890  0.0474  45  TYR D CE2 
11442 C CZ  . TYR D 45  ? 0.4815 0.5872 0.4177 -0.1234 0.0853  0.0588  45  TYR D CZ  
11443 O OH  . TYR D 45  ? 0.4908 0.6045 0.4214 -0.1127 0.0785  0.0696  45  TYR D OH  
11444 N N   . ILE D 46  ? 0.3769 0.5108 0.3346 -0.1466 0.0808  0.0025  46  ILE D N   
11445 C CA  . ILE D 46  ? 0.2710 0.4301 0.2298 -0.1380 0.0675  -0.0046 46  ILE D CA  
11446 C C   . ILE D 46  ? 0.2912 0.4651 0.2559 -0.1461 0.0667  -0.0212 46  ILE D C   
11447 O O   . ILE D 46  ? 0.2874 0.4691 0.2550 -0.1597 0.0743  -0.0288 46  ILE D O   
11448 C CB  . ILE D 46  ? 0.3388 0.5200 0.2946 -0.1351 0.0631  -0.0019 46  ILE D CB  
11449 C CG1 . ILE D 46  ? 0.2754 0.4440 0.2248 -0.1261 0.0625  0.0144  46  ILE D CG1 
11450 C CG2 . ILE D 46  ? 0.2846 0.4914 0.2418 -0.1270 0.0506  -0.0108 46  ILE D CG2 
11451 C CD1 . ILE D 46  ? 0.3102 0.4988 0.2556 -0.1239 0.0594  0.0177  46  ILE D CD1 
11452 N N   . ASP D 47  ? 0.3090 0.4873 0.2752 -0.1381 0.0578  -0.0266 47  ASP D N   
11453 C CA  . ASP D 47  ? 0.3125 0.5038 0.2838 -0.1444 0.0565  -0.0414 47  ASP D CA  
11454 C C   . ASP D 47  ? 0.2725 0.4958 0.2450 -0.1386 0.0458  -0.0489 47  ASP D C   
11455 O O   . ASP D 47  ? 0.2492 0.4765 0.2195 -0.1254 0.0355  -0.0463 47  ASP D O   
11456 C CB  . ASP D 47  ? 0.2501 0.4240 0.2219 -0.1397 0.0548  -0.0423 47  ASP D CB  
11457 C CG  . ASP D 47  ? 0.2985 0.4774 0.2750 -0.1507 0.0588  -0.0566 47  ASP D CG  
11458 O OD1 . ASP D 47  ? 0.2911 0.4906 0.2708 -0.1612 0.0611  -0.0667 47  ASP D OD1 
11459 O OD2 . ASP D 47  ? 0.2948 0.4578 0.2716 -0.1492 0.0597  -0.0581 47  ASP D OD2 
11460 N N   . LEU D 48  ? 0.2305 0.4764 0.2064 -0.1485 0.0487  -0.0581 48  LEU D N   
11461 C CA  . LEU D 48  ? 0.2835 0.5619 0.2614 -0.1435 0.0398  -0.0661 48  LEU D CA  
11462 C C   . LEU D 48  ? 0.2946 0.5909 0.2779 -0.1495 0.0383  -0.0805 48  LEU D C   
11463 O O   . LEU D 48  ? 0.2939 0.6128 0.2761 -0.1458 0.0335  -0.0877 48  LEU D O   
11464 C CB  . LEU D 48  ? 0.2231 0.5192 0.2011 -0.1487 0.0432  -0.0656 48  LEU D CB  
11465 C CG  . LEU D 48  ? 0.2235 0.5053 0.1955 -0.1434 0.0448  -0.0515 48  LEU D CG  
11466 C CD1 . LEU D 48  ? 0.2257 0.5288 0.1977 -0.1479 0.0474  -0.0522 48  LEU D CD1 
11467 C CD2 . LEU D 48  ? 0.2501 0.5264 0.2174 -0.1264 0.0340  -0.0445 48  LEU D CD2 
11468 N N   . LEU D 49  ? 0.2447 0.5241 0.2293 -0.1545 0.0420  -0.0837 49  LEU D N   
11469 C CA  . LEU D 49  ? 0.2551 0.5443 0.2401 -0.1574 0.0410  -0.0963 49  LEU D CA  
11470 C C   . LEU D 49  ? 0.2476 0.5523 0.2312 -0.1406 0.0312  -0.0974 49  LEU D C   
11471 O O   . LEU D 49  ? 0.2605 0.5816 0.2456 -0.1380 0.0320  -0.1037 49  LEU D O   
11472 C CB  . LEU D 49  ? 0.2537 0.5201 0.2402 -0.1653 0.0476  -0.0988 49  LEU D CB  
11473 C CG  . LEU D 49  ? 0.3065 0.5779 0.2918 -0.1692 0.0493  -0.1112 49  LEU D CG  
11474 C CD1 . LEU D 49  ? 0.4222 0.7045 0.4061 -0.1794 0.0554  -0.1190 49  LEU D CD1 
11475 C CD2 . LEU D 49  ? 0.2919 0.5385 0.2784 -0.1761 0.0557  -0.1128 49  LEU D CD2 
11476 N N   . THR D 50  ? 0.2205 0.5179 0.2033 -0.1279 0.0235  -0.0890 50  THR D N   
11477 C CA  . THR D 50  ? 0.1805 0.4824 0.1660 -0.1100 0.0166  -0.0860 50  THR D CA  
11478 C C   . THR D 50  ? 0.2038 0.4946 0.1866 -0.0970 0.0092  -0.0755 50  THR D C   
11479 O O   . THR D 50  ? 0.2438 0.5229 0.2210 -0.1015 0.0086  -0.0707 50  THR D O   
11480 C CB  . THR D 50  ? 0.2457 0.5400 0.2330 -0.1086 0.0164  -0.0897 50  THR D CB  
11481 O OG1 . THR D 50  ? 0.2785 0.5779 0.2698 -0.0928 0.0106  -0.0868 50  THR D OG1 
11482 C CG2 . THR D 50  ? 0.1955 0.4677 0.1786 -0.1102 0.0147  -0.0858 50  THR D CG2 
11483 N N   . ASP D 51  ? 0.1985 0.4918 0.1848 -0.0814 0.0039  -0.0720 51  ASP D N   
11484 C CA  . ASP D 51  ? 0.1542 0.4322 0.1380 -0.0679 -0.0027 -0.0631 51  ASP D CA  
11485 C C   . ASP D 51  ? 0.1952 0.4593 0.1792 -0.0606 -0.0064 -0.0616 51  ASP D C   
11486 O O   . ASP D 51  ? 0.1825 0.4342 0.1651 -0.0486 -0.0116 -0.0555 51  ASP D O   
11487 C CB  . ASP D 51  ? 0.1682 0.4535 0.1546 -0.0567 -0.0054 -0.0607 51  ASP D CB  
11488 C CG  . ASP D 51  ? 0.1586 0.4541 0.1504 -0.0500 -0.0058 -0.0651 51  ASP D CG  
11489 O OD1 . ASP D 51  ? 0.2058 0.5136 0.2006 -0.0574 -0.0019 -0.0719 51  ASP D OD1 
11490 O OD2 . ASP D 51  ? 0.1598 0.4508 0.1520 -0.0379 -0.0097 -0.0619 51  ASP D OD2 
11491 N N   . SER D 52  ? 0.1874 0.4525 0.1725 -0.0684 -0.0032 -0.0675 52  SER D N   
11492 C CA  . SER D 52  ? 0.1643 0.4203 0.1502 -0.0621 -0.0060 -0.0672 52  SER D CA  
11493 C C   . SER D 52  ? 0.1909 0.4300 0.1720 -0.0662 -0.0065 -0.0648 52  SER D C   
11494 O O   . SER D 52  ? 0.2208 0.4594 0.2006 -0.0793 -0.0013 -0.0703 52  SER D O   
11495 C CB  . SER D 52  ? 0.1902 0.4602 0.1806 -0.0673 -0.0021 -0.0757 52  SER D CB  
11496 O OG  . SER D 52  ? 0.2350 0.4981 0.2259 -0.0606 -0.0050 -0.0749 52  SER D OG  
11497 N N   . GLY D 53  ? 0.1676 0.3920 0.1461 -0.0556 -0.0120 -0.0573 53  GLY D N   
11498 C CA  . GLY D 53  ? 0.1732 0.3833 0.1477 -0.0576 -0.0129 -0.0550 53  GLY D CA  
11499 C C   . GLY D 53  ? 0.1841 0.3883 0.1526 -0.0651 -0.0117 -0.0518 53  GLY D C   
11500 O O   . GLY D 53  ? 0.1838 0.3768 0.1483 -0.0684 -0.0114 -0.0505 53  GLY D O   
11501 N N   . THR D 54  ? 0.1654 0.3767 0.1326 -0.0677 -0.0107 -0.0499 54  THR D N   
11502 C CA  . THR D 54  ? 0.2040 0.4038 0.1672 -0.0721 -0.0068 -0.0427 54  THR D CA  
11503 C C   . THR D 54  ? 0.1893 0.3876 0.1480 -0.0622 -0.0132 -0.0332 54  THR D C   
11504 O O   . THR D 54  ? 0.2266 0.4146 0.1838 -0.0629 -0.0092 -0.0248 54  THR D O   
11505 C CB  . THR D 54  ? 0.2522 0.4578 0.2181 -0.0835 0.0017  -0.0463 54  THR D CB  
11506 O OG1 . THR D 54  ? 0.2380 0.4687 0.2042 -0.0827 -0.0028 -0.0519 54  THR D OG1 
11507 C CG2 . THR D 54  ? 0.2243 0.4276 0.1944 -0.0950 0.0095  -0.0554 54  THR D CG2 
11508 N N   . ASN D 55  ? 0.1682 0.3656 0.1295 -0.0500 -0.0191 -0.0318 55  ASN D N   
11509 C CA  . ASN D 55  ? 0.1763 0.3667 0.1363 -0.0403 -0.0229 -0.0241 55  ASN D CA  
11510 C C   . ASN D 55  ? 0.2094 0.3864 0.1642 -0.0376 -0.0256 -0.0154 55  ASN D C   
11511 O O   . ASN D 55  ? 0.2066 0.3781 0.1595 -0.0400 -0.0257 -0.0150 55  ASN D O   
11512 C CB  . ASN D 55  ? 0.1875 0.3726 0.1519 -0.0294 -0.0259 -0.0254 55  ASN D CB  
11513 C CG  . ASN D 55  ? 0.1853 0.3846 0.1547 -0.0310 -0.0234 -0.0330 55  ASN D CG  
11514 O OD1 . ASN D 55  ? 0.1611 0.3733 0.1320 -0.0335 -0.0212 -0.0353 55  ASN D OD1 
11515 N ND2 . ASN D 55  ? 0.1455 0.3439 0.1176 -0.0294 -0.0236 -0.0367 55  ASN D ND2 
11516 N N   . ALA D 56  ? 0.1954 0.3678 0.1480 -0.0325 -0.0274 -0.0083 56  ALA D N   
11517 C CA  . ALA D 56  ? 0.1437 0.3037 0.0929 -0.0281 -0.0299 0.0008  56  ALA D CA  
11518 C C   . ALA D 56  ? 0.1636 0.3094 0.1161 -0.0184 -0.0337 0.0004  56  ALA D C   
11519 O O   . ALA D 56  ? 0.1986 0.3424 0.1526 -0.0139 -0.0348 -0.0021 56  ALA D O   
11520 C CB  . ALA D 56  ? 0.1463 0.3084 0.0911 -0.0287 -0.0291 0.0087  56  ALA D CB  
11521 N N   . MET D 57  ? 0.1798 0.3154 0.1322 -0.0160 -0.0354 0.0029  57  MET D N   
11522 C CA  . MET D 57  ? 0.1559 0.2766 0.1095 -0.0091 -0.0386 0.0026  57  MET D CA  
11523 C C   . MET D 57  ? 0.1436 0.2546 0.0953 -0.0056 -0.0404 0.0085  57  MET D C   
11524 O O   . MET D 57  ? 0.1741 0.2895 0.1240 -0.0074 -0.0392 0.0142  57  MET D O   
11525 C CB  . MET D 57  ? 0.1814 0.2968 0.1359 -0.0088 -0.0393 0.0020  57  MET D CB  
11526 C CG  . MET D 57  ? 0.1754 0.2990 0.1322 -0.0117 -0.0377 -0.0052 57  MET D CG  
11527 S SD  . MET D 57  ? 0.2080 0.3239 0.1654 -0.0103 -0.0389 -0.0060 57  MET D SD  
11528 C CE  . MET D 57  ? 0.2210 0.3392 0.1755 -0.0143 -0.0380 0.0002  57  MET D CE  
11529 N N   . SER D 58  ? 0.1314 0.2292 0.0829 -0.0014 -0.0432 0.0073  58  SER D N   
11530 C CA  . SER D 58  ? 0.1552 0.2436 0.1047 0.0009  -0.0450 0.0110  58  SER D CA  
11531 C C   . SER D 58  ? 0.1940 0.2750 0.1439 0.0019  -0.0458 0.0148  58  SER D C   
11532 O O   . SER D 58  ? 0.1967 0.2777 0.1480 0.0013  -0.0454 0.0143  58  SER D O   
11533 C CB  . SER D 58  ? 0.1547 0.2417 0.1038 0.0032  -0.0467 0.0081  58  SER D CB  
11534 O OG  . SER D 58  ? 0.1756 0.2582 0.1256 0.0045  -0.0479 0.0063  58  SER D OG  
11535 N N   . ASP D 59  ? 0.1741 0.2515 0.1230 0.0031  -0.0466 0.0186  59  ASP D N   
11536 C CA  . ASP D 59  ? 0.1483 0.2206 0.0984 0.0043  -0.0471 0.0219  59  ASP D CA  
11537 C C   . ASP D 59  ? 0.1932 0.2612 0.1439 0.0052  -0.0489 0.0186  59  ASP D C   
11538 O O   . ASP D 59  ? 0.2029 0.2676 0.1549 0.0056  -0.0488 0.0194  59  ASP D O   
11539 C CB  . ASP D 59  ? 0.2112 0.2844 0.1609 0.0051  -0.0474 0.0262  59  ASP D CB  
11540 C CG  . ASP D 59  ? 0.2211 0.2959 0.1689 0.0052  -0.0491 0.0236  59  ASP D CG  
11541 O OD1 . ASP D 59  ? 0.2694 0.3442 0.2162 0.0053  -0.0499 0.0189  59  ASP D OD1 
11542 O OD2 . ASP D 59  ? 0.3178 0.3945 0.2650 0.0054  -0.0495 0.0264  59  ASP D OD2 
11543 N N   . HIS D 60  ? 0.1956 0.2637 0.1451 0.0057  -0.0503 0.0151  60  HIS D N   
11544 C CA  . HIS D 60  ? 0.1937 0.2571 0.1427 0.0065  -0.0520 0.0128  60  HIS D CA  
11545 C C   . HIS D 60  ? 0.2217 0.2862 0.1724 0.0060  -0.0510 0.0106  60  HIS D C   
11546 O O   . HIS D 60  ? 0.2121 0.2726 0.1630 0.0064  -0.0518 0.0104  60  HIS D O   
11547 C CB  . HIS D 60  ? 0.2049 0.2683 0.1515 0.0073  -0.0537 0.0101  60  HIS D CB  
11548 C CG  . HIS D 60  ? 0.2609 0.3213 0.2048 0.0075  -0.0556 0.0116  60  HIS D CG  
11549 N ND1 . HIS D 60  ? 0.3831 0.4480 0.3258 0.0073  -0.0552 0.0119  60  HIS D ND1 
11550 C CD2 . HIS D 60  ? 0.2583 0.3128 0.2004 0.0076  -0.0579 0.0127  60  HIS D CD2 
11551 C CE1 . HIS D 60  ? 0.3312 0.3931 0.2713 0.0073  -0.0573 0.0130  60  HIS D CE1 
11552 N NE2 . HIS D 60  ? 0.3364 0.3919 0.2761 0.0075  -0.0590 0.0133  60  HIS D NE2 
11553 N N   . GLN D 61  ? 0.2023 0.2728 0.1540 0.0048  -0.0492 0.0088  61  GLN D N   
11554 C CA  . GLN D 61  ? 0.1980 0.2709 0.1511 0.0038  -0.0482 0.0060  61  GLN D CA  
11555 C C   . GLN D 61  ? 0.2361 0.3054 0.1898 0.0030  -0.0478 0.0083  61  GLN D C   
11556 O O   . GLN D 61  ? 0.2365 0.3044 0.1908 0.0030  -0.0480 0.0070  61  GLN D O   
11557 C CB  . GLN D 61  ? 0.2012 0.2825 0.1550 0.0021  -0.0464 0.0028  61  GLN D CB  
11558 C CG  . GLN D 61  ? 0.2488 0.3359 0.2030 0.0037  -0.0464 -0.0008 61  GLN D CG  
11559 C CD  . GLN D 61  ? 0.2066 0.3039 0.1620 0.0019  -0.0443 -0.0043 61  GLN D CD  
11560 O OE1 . GLN D 61  ? 0.2003 0.2997 0.1549 0.0003  -0.0436 -0.0030 61  GLN D OE1 
11561 N NE2 . GLN D 61  ? 0.2073 0.3119 0.1649 0.0018  -0.0432 -0.0086 61  GLN D NE2 
11562 N N   . TRP D 62  ? 0.2015 0.2727 0.1550 0.0025  -0.0467 0.0124  62  TRP D N   
11563 C CA  . TRP D 62  ? 0.2325 0.3063 0.1870 0.0020  -0.0456 0.0165  62  TRP D CA  
11564 C C   . TRP D 62  ? 0.1978 0.2608 0.1526 0.0046  -0.0473 0.0174  62  TRP D C   
11565 O O   . TRP D 62  ? 0.1823 0.2460 0.1381 0.0045  -0.0469 0.0179  62  TRP D O   
11566 C CB  . TRP D 62  ? 0.1790 0.2594 0.1334 0.0011  -0.0437 0.0235  62  TRP D CB  
11567 C CG  . TRP D 62  ? 0.2764 0.3695 0.2295 -0.0032 -0.0415 0.0240  62  TRP D CG  
11568 C CD1 . TRP D 62  ? 0.2680 0.3674 0.2200 -0.0053 -0.0407 0.0221  62  TRP D CD1 
11569 C CD2 . TRP D 62  ? 0.3318 0.4334 0.2832 -0.0074 -0.0395 0.0263  62  TRP D CD2 
11570 N NE1 . TRP D 62  ? 0.3348 0.4461 0.2843 -0.0113 -0.0382 0.0225  62  TRP D NE1 
11571 C CE2 . TRP D 62  ? 0.3722 0.4824 0.3214 -0.0130 -0.0367 0.0244  62  TRP D CE2 
11572 C CE3 . TRP D 62  ? 0.3782 0.4778 0.3299 -0.0074 -0.0385 0.0287  62  TRP D CE3 
11573 C CZ2 . TRP D 62  ? 0.4457 0.5484 0.3988 -0.0185 -0.0277 0.0213  62  TRP D CZ2 
11574 C CZ3 . TRP D 62  ? 0.4013 0.4935 0.3569 -0.0121 -0.0295 0.0253  62  TRP D CZ3 
11575 C CH2 . TRP D 62  ? 0.3897 0.4829 0.3459 -0.0178 -0.0242 0.0216  62  TRP D CH2 
11576 N N   . ALA D 63  ? 0.1963 0.2555 0.1505 0.0059  -0.0487 0.0181  63  ALA D N   
11577 C CA  . ALA D 63  ? 0.2081 0.2636 0.1627 0.0070  -0.0498 0.0192  63  ALA D CA  
11578 C C   . ALA D 63  ? 0.1986 0.2521 0.1528 0.0069  -0.0508 0.0158  63  ALA D C   
11579 O O   . ALA D 63  ? 0.2342 0.2854 0.1890 0.0074  -0.0510 0.0167  63  ALA D O   
11580 C CB  . ALA D 63  ? 0.1653 0.2202 0.1187 0.0075  -0.0513 0.0199  63  ALA D CB  
11581 N N   . ALA D 64  ? 0.2307 0.2862 0.1840 0.0063  -0.0511 0.0123  64  ALA D N   
11582 C CA  . ALA D 64  ? 0.2330 0.2882 0.1860 0.0063  -0.0517 0.0098  64  ALA D CA  
11583 C C   . ALA D 64  ? 0.2192 0.2766 0.1735 0.0053  -0.0502 0.0088  64  ALA D C   
11584 O O   . ALA D 64  ? 0.2405 0.2965 0.1946 0.0055  -0.0505 0.0084  64  ALA D O   
11585 C CB  . ALA D 64  ? 0.1974 0.2569 0.1497 0.0065  -0.0517 0.0066  64  ALA D CB  
11586 N N   A MET D 65  ? 0.1848 0.2455 0.1397 0.0039  -0.0488 0.0082  65  MET D N   
11587 N N   B MET D 65  ? 0.1724 0.2330 0.1273 0.0039  -0.0488 0.0082  65  MET D N   
11588 C CA  A MET D 65  ? 0.2094 0.2763 0.1651 0.0023  -0.0471 0.0069  65  MET D CA  
11589 C CA  B MET D 65  ? 0.2224 0.2893 0.1782 0.0023  -0.0472 0.0069  65  MET D CA  
11590 C C   A MET D 65  ? 0.2175 0.2824 0.1737 0.0033  -0.0470 0.0109  65  MET D C   
11591 C C   B MET D 65  ? 0.2236 0.2884 0.1798 0.0033  -0.0471 0.0109  65  MET D C   
11592 O O   A MET D 65  ? 0.2267 0.2948 0.1831 0.0027  -0.0465 0.0095  65  MET D O   
11593 O O   B MET D 65  ? 0.2196 0.2875 0.1760 0.0027  -0.0465 0.0095  65  MET D O   
11594 C CB  A MET D 65  ? 0.2162 0.2959 0.1724 -0.0006 -0.0448 0.0066  65  MET D CB  
11595 C CB  B MET D 65  ? 0.2226 0.3021 0.1787 -0.0006 -0.0448 0.0066  65  MET D CB  
11596 C CG  A MET D 65  ? 0.2174 0.3034 0.1738 -0.0025 -0.0440 0.0012  65  MET D CG  
11597 C CG  B MET D 65  ? 0.2180 0.3026 0.1743 -0.0020 -0.0442 0.0019  65  MET D CG  
11598 S SD  A MET D 65  ? 0.1975 0.3009 0.1540 -0.0093 -0.0404 -0.0039 65  MET D SD  
11599 S SD  B MET D 65  ? 0.1947 0.2943 0.1506 -0.0073 -0.0414 0.0016  65  MET D SD  
11600 C CE  A MET D 65  ? 0.2353 0.3426 0.1892 -0.0118 -0.0396 0.0040  65  MET D CE  
11601 C CE  B MET D 65  ? 0.2168 0.3256 0.1715 -0.0128 -0.0391 -0.0017 65  MET D CE  
11602 N N   . ILE D 66  ? 0.2373 0.2981 0.1941 0.0049  -0.0474 0.0156  66  ILE D N   
11603 C CA  . ILE D 66  ? 0.2519 0.3127 0.2101 0.0062  -0.0467 0.0203  66  ILE D CA  
11604 C C   . ILE D 66  ? 0.2082 0.2612 0.1658 0.0073  -0.0482 0.0183  66  ILE D C   
11605 O O   . ILE D 66  ? 0.2350 0.2911 0.1938 0.0075  -0.0473 0.0203  66  ILE D O   
11606 C CB  . ILE D 66  ? 0.2367 0.2963 0.1960 0.0075  -0.0462 0.0257  66  ILE D CB  
11607 C CG1 . ILE D 66  ? 0.3064 0.3753 0.2663 0.0064  -0.0439 0.0308  66  ILE D CG1 
11608 C CG2 . ILE D 66  ? 0.2155 0.2732 0.1768 0.0092  -0.0457 0.0298  66  ILE D CG2 
11609 C CD1 . ILE D 66  ? 0.4038 0.4799 0.3648 0.0064  -0.0418 0.0365  66  ILE D CD1 
11610 N N   . THR D 67  ? 0.1953 0.2453 0.1516 0.0074  -0.0498 0.0163  67  THR D N   
11611 C CA  . THR D 67  ? 0.2238 0.2717 0.1792 0.0078  -0.0509 0.0160  67  THR D CA  
11612 C C   . THR D 67  ? 0.2184 0.2676 0.1724 0.0069  -0.0512 0.0125  67  THR D C   
11613 O O   . THR D 67  ? 0.2342 0.2814 0.1865 0.0073  -0.0524 0.0124  67  THR D O   
11614 C CB  . THR D 67  ? 0.2320 0.2768 0.1860 0.0085  -0.0525 0.0169  67  THR D CB  
11615 O OG1 . THR D 67  ? 0.2722 0.3166 0.2246 0.0083  -0.0536 0.0151  67  THR D OG1 
11616 C CG2 . THR D 67  ? 0.2261 0.2722 0.1821 0.0090  -0.0517 0.0207  67  THR D CG2 
11617 N N   . GLY D 68  ? 0.2157 0.2691 0.1701 0.0056  -0.0501 0.0097  68  GLY D N   
11618 C CA  . GLY D 68  ? 0.1832 0.2409 0.1368 0.0049  -0.0497 0.0060  68  GLY D CA  
11619 C C   . GLY D 68  ? 0.2279 0.2861 0.1810 0.0048  -0.0494 0.0057  68  GLY D C   
11620 O O   . GLY D 68  ? 0.2567 0.3140 0.2103 0.0045  -0.0487 0.0069  68  GLY D O   
11621 N N   . ASP D 69  ? 0.1936 0.2539 0.1452 0.0054  -0.0499 0.0043  69  ASP D N   
11622 C CA  . ASP D 69  ? 0.1701 0.2317 0.1206 0.0055  -0.0496 0.0041  69  ASP D CA  
11623 C C   . ASP D 69  ? 0.2356 0.3050 0.1863 0.0040  -0.0477 -0.0008 69  ASP D C   
11624 O O   . ASP D 69  ? 0.2204 0.2960 0.1712 0.0043  -0.0473 -0.0039 69  ASP D O   
11625 C CB  . ASP D 69  ? 0.2377 0.2972 0.1856 0.0071  -0.0514 0.0054  69  ASP D CB  
11626 C CG  . ASP D 69  ? 0.2882 0.3491 0.2343 0.0074  -0.0513 0.0057  69  ASP D CG  
11627 O OD1 . ASP D 69  ? 0.2452 0.3088 0.1921 0.0062  -0.0498 0.0047  69  ASP D OD1 
11628 O OD2 . ASP D 69  ? 0.2681 0.3275 0.2113 0.0087  -0.0530 0.0069  69  ASP D OD2 
11629 N N   . GLU D 70  ? 0.2573 0.3293 0.2083 0.0026  -0.0463 -0.0018 70  GLU D N   
11630 C CA  . GLU D 70  ? 0.2412 0.3263 0.1926 0.0004  -0.0436 -0.0079 70  GLU D CA  
11631 C C   . GLU D 70  ? 0.2281 0.3170 0.1778 0.0007  -0.0432 -0.0101 70  GLU D C   
11632 O O   . GLU D 70  ? 0.2170 0.3172 0.1669 -0.0017 -0.0407 -0.0162 70  GLU D O   
11633 C CB  . GLU D 70  ? 0.2255 0.3186 0.1774 -0.0016 -0.0414 -0.0092 70  GLU D CB  
11634 C CG  . GLU D 70  ? 0.1887 0.2816 0.1419 -0.0024 -0.0414 -0.0075 70  GLU D CG  
11635 C CD  . GLU D 70  ? 0.2285 0.3267 0.1825 -0.0050 -0.0403 -0.0130 70  GLU D CD  
11636 O OE1 . GLU D 70  ? 0.1911 0.2958 0.1453 -0.0071 -0.0387 -0.0193 70  GLU D OE1 
11637 O OE2 . GLU D 70  ? 0.2157 0.3123 0.1705 -0.0052 -0.0408 -0.0111 70  GLU D OE2 
11638 N N   . ALA D 71  ? 0.2581 0.3383 0.2058 0.0028  -0.0455 -0.0060 71  ALA D N   
11639 C CA  . ALA D 71  ? 0.2631 0.3485 0.2089 0.0034  -0.0452 -0.0072 71  ALA D CA  
11640 C C   . ALA D 71  ? 0.2426 0.3390 0.1890 0.0028  -0.0439 -0.0128 71  ALA D C   
11641 O O   . ALA D 71  ? 0.2590 0.3587 0.2068 0.0036  -0.0441 -0.0141 71  ALA D O   
11642 C CB  . ALA D 71  ? 0.2447 0.3257 0.1885 0.0062  -0.0475 -0.0025 71  ALA D CB  
11643 N N   . TYR D 72  ? 0.2349 0.3391 0.1802 0.0016  -0.0422 -0.0164 72  TYR D N   
11644 C CA  . TYR D 72  ? 0.2343 0.3506 0.1808 0.0004  -0.0407 -0.0224 72  TYR D CA  
11645 C C   . TYR D 72  ? 0.2667 0.3878 0.2127 0.0043  -0.0425 -0.0205 72  TYR D C   
11646 O O   . TYR D 72  ? 0.2851 0.4160 0.2332 0.0046  -0.0419 -0.0241 72  TYR D O   
11647 C CB  . TYR D 72  ? 0.2564 0.3841 0.2023 -0.0020 -0.0380 -0.0276 72  TYR D CB  
11648 C CG  . TYR D 72  ? 0.2179 0.3600 0.1660 -0.0048 -0.0357 -0.0353 72  TYR D CG  
11649 C CD1 . TYR D 72  ? 0.2456 0.3950 0.1966 -0.0101 -0.0323 -0.0427 72  TYR D CD1 
11650 C CD2 . TYR D 72  ? 0.2480 0.3971 0.1953 -0.0027 -0.0367 -0.0355 72  TYR D CD2 
11651 C CE1 . TYR D 72  ? 0.2014 0.3643 0.1550 -0.0139 -0.0298 -0.0504 72  TYR D CE1 
11652 C CE2 . TYR D 72  ? 0.2704 0.4347 0.2204 -0.0055 -0.0346 -0.0425 72  TYR D CE2 
11653 C CZ  . TYR D 72  ? 0.2598 0.4309 0.2133 -0.0114 -0.0311 -0.0500 72  TYR D CZ  
11654 O OH  . TYR D 72  ? 0.3968 0.5835 0.3534 -0.0151 -0.0287 -0.0574 72  TYR D OH  
11655 N N   . ALA D 73  ? 0.2398 0.3551 0.1829 0.0074  -0.0446 -0.0151 73  ALA D N   
11656 C CA  . ALA D 73  ? 0.2576 0.3764 0.1988 0.0115  -0.0465 -0.0131 73  ALA D CA  
11657 C C   . ALA D 73  ? 0.2363 0.3423 0.1752 0.0137  -0.0490 -0.0070 73  ALA D C   
11658 O O   . ALA D 73  ? 0.2968 0.3937 0.2341 0.0126  -0.0497 -0.0034 73  ALA D O   
11659 C CB  . ALA D 73  ? 0.2293 0.3555 0.1676 0.0125  -0.0465 -0.0133 73  ALA D CB  
11660 N N   . GLY D 74  ? 0.2107 0.3165 0.1494 0.0166  -0.0504 -0.0062 74  GLY D N   
11661 C CA  . GLY D 74  ? 0.2692 0.3631 0.2050 0.0182  -0.0530 -0.0012 74  GLY D CA  
11662 C C   . GLY D 74  ? 0.2493 0.3337 0.1871 0.0159  -0.0531 0.0004  74  GLY D C   
11663 O O   . GLY D 74  ? 0.2757 0.3495 0.2111 0.0155  -0.0551 0.0046  74  GLY D O   
11664 N N   . SER D 75  ? 0.2409 0.3290 0.1827 0.0141  -0.0512 -0.0029 75  SER D N   
11665 C CA  . SER D 75  ? 0.2396 0.3197 0.1830 0.0122  -0.0514 -0.0013 75  SER D CA  
11666 C C   . SER D 75  ? 0.2409 0.3141 0.1825 0.0140  -0.0536 0.0017  75  SER D C   
11667 O O   . SER D 75  ? 0.2594 0.3365 0.1999 0.0170  -0.0544 0.0008  75  SER D O   
11668 C CB  . SER D 75  ? 0.2423 0.3284 0.1895 0.0104  -0.0492 -0.0053 75  SER D CB  
11669 O OG  . SER D 75  ? 0.2458 0.3252 0.1941 0.0096  -0.0497 -0.0034 75  SER D OG  
11670 N N   . ARG D 76  ? 0.1997 0.1894 0.2711 -0.0217 -0.0488 -0.0349 76  ARG D N   
11671 C CA  A ARG D 76  ? 0.2371 0.2266 0.3051 -0.0221 -0.0556 -0.0357 76  ARG D CA  
11672 C CA  B ARG D 76  ? 0.2372 0.2265 0.3051 -0.0222 -0.0556 -0.0357 76  ARG D CA  
11673 C C   . ARG D 76  ? 0.2199 0.2037 0.2739 -0.0172 -0.0605 -0.0324 76  ARG D C   
11674 O O   . ARG D 76  ? 0.2217 0.2001 0.2675 -0.0187 -0.0633 -0.0336 76  ARG D O   
11675 C CB  A ARG D 76  ? 0.2519 0.2546 0.3355 -0.0205 -0.0607 -0.0388 76  ARG D CB  
11676 C CB  B ARG D 76  ? 0.2521 0.2544 0.3354 -0.0208 -0.0606 -0.0389 76  ARG D CB  
11677 C CG  A ARG D 76  ? 0.2546 0.2600 0.3379 -0.0226 -0.0672 -0.0427 76  ARG D CG  
11678 C CG  B ARG D 76  ? 0.2612 0.2704 0.3599 -0.0265 -0.0558 -0.0432 76  ARG D CG  
11679 C CD  A ARG D 76  ? 0.2396 0.2610 0.3377 -0.0204 -0.0735 -0.0456 76  ARG D CD  
11680 C CD  B ARG D 76  ? 0.2531 0.2759 0.3672 -0.0255 -0.0621 -0.0469 76  ARG D CD  
11681 N NE  A ARG D 76  ? 0.2391 0.2670 0.3339 -0.0126 -0.0797 -0.0409 76  ARG D NE  
11682 N NE  B ARG D 76  ? 0.2661 0.2970 0.3849 -0.0173 -0.0680 -0.0437 76  ARG D NE  
11683 C CZ  A ARG D 76  ? 0.2256 0.2596 0.3303 -0.0074 -0.0797 -0.0364 76  ARG D CZ  
11684 C CZ  B ARG D 76  ? 0.2426 0.2812 0.3770 -0.0137 -0.0662 -0.0428 76  ARG D CZ  
11685 N NH1 A ARG D 76  ? 0.2331 0.2691 0.3527 -0.0089 -0.0737 -0.0380 76  ARG D NH1 
11686 N NH1 B ARG D 76  ? 0.1978 0.2386 0.3441 -0.0177 -0.0581 -0.0467 76  ARG D NH1 
11687 N NH2 A ARG D 76  ? 0.2031 0.2417 0.3038 -0.0007 -0.0854 -0.0299 76  ARG D NH2 
11688 N NH2 B ARG D 76  ? 0.2353 0.2803 0.3743 -0.0059 -0.0723 -0.0376 76  ARG D NH2 
11689 N N   . ASN D 77  ? 0.2236 0.2085 0.2763 -0.0114 -0.0612 -0.0285 77  ASN D N   
11690 C CA  . ASN D 77  ? 0.2043 0.1861 0.2448 -0.0068 -0.0654 -0.0248 77  ASN D CA  
11691 C C   . ASN D 77  ? 0.2329 0.2031 0.2597 -0.0083 -0.0618 -0.0233 77  ASN D C   
11692 O O   . ASN D 77  ? 0.2268 0.1940 0.2431 -0.0060 -0.0650 -0.0221 77  ASN D O   
11693 C CB  . ASN D 77  ? 0.2101 0.1972 0.2564 -0.0007 -0.0670 -0.0196 77  ASN D CB  
11694 C CG  . ASN D 77  ? 0.2030 0.2027 0.2657 0.0014  -0.0708 -0.0199 77  ASN D CG  
11695 O OD1 . ASN D 77  ? 0.1814 0.1837 0.2588 0.0020  -0.0671 -0.0202 77  ASN D OD1 
11696 N ND2 . ASN D 77  ? 0.1646 0.1735 0.2261 0.0023  -0.0782 -0.0206 77  ASN D ND2 
11697 N N   . TYR D 78  ? 0.1645 0.1296 0.1911 -0.0121 -0.0553 -0.0237 78  TYR D N   
11698 C CA  . TYR D 78  ? 0.1759 0.1317 0.1898 -0.0140 -0.0529 -0.0220 78  TYR D CA  
11699 C C   . TYR D 78  ? 0.2216 0.1725 0.2309 -0.0168 -0.0557 -0.0231 78  TYR D C   
11700 O O   . TYR D 78  ? 0.2333 0.1780 0.2334 -0.0152 -0.0576 -0.0218 78  TYR D O   
11701 C CB  . TYR D 78  ? 0.1732 0.1278 0.1871 -0.0185 -0.0459 -0.0223 78  TYR D CB  
11702 C CG  . TYR D 78  ? 0.1935 0.1408 0.1954 -0.0218 -0.0444 -0.0197 78  TYR D CG  
11703 C CD1 . TYR D 78  ? 0.2066 0.1495 0.1990 -0.0193 -0.0445 -0.0174 78  TYR D CD1 
11704 C CD2 . TYR D 78  ? 0.2239 0.1689 0.2254 -0.0275 -0.0431 -0.0187 78  TYR D CD2 
11705 C CE1 . TYR D 78  ? 0.2282 0.1657 0.2108 -0.0219 -0.0440 -0.0142 78  TYR D CE1 
11706 C CE2 . TYR D 78  ? 0.2555 0.1941 0.2473 -0.0301 -0.0425 -0.0143 78  TYR D CE2 
11707 C CZ  . TYR D 78  ? 0.2682 0.2036 0.2506 -0.0270 -0.0433 -0.0122 78  TYR D CZ  
11708 O OH  . TYR D 78  ? 0.2893 0.2197 0.2634 -0.0292 -0.0436 -0.0071 78  TYR D OH  
11709 N N   . TYR D 79  ? 0.2182 0.1716 0.2360 -0.0212 -0.0557 -0.0260 79  TYR D N   
11710 C CA  . TYR D 79  ? 0.1882 0.1358 0.2055 -0.0242 -0.0580 -0.0276 79  TYR D CA  
11711 C C   . TYR D 79  ? 0.2855 0.2356 0.3014 -0.0201 -0.0645 -0.0315 79  TYR D C   
11712 O O   . TYR D 79  ? 0.2642 0.2081 0.2764 -0.0201 -0.0658 -0.0329 79  TYR D O   
11713 C CB  . TYR D 79  ? 0.2606 0.2109 0.2895 -0.0305 -0.0560 -0.0298 79  TYR D CB  
11714 C CG  . TYR D 79  ? 0.2734 0.2233 0.3022 -0.0356 -0.0488 -0.0261 79  TYR D CG  
11715 C CD1 . TYR D 79  ? 0.3152 0.2567 0.3361 -0.0393 -0.0460 -0.0207 79  TYR D CD1 
11716 C CD2 . TYR D 79  ? 0.2839 0.2433 0.3208 -0.0367 -0.0448 -0.0280 79  TYR D CD2 
11717 C CE1 . TYR D 79  ? 0.2643 0.2083 0.2829 -0.0446 -0.0394 -0.0170 79  TYR D CE1 
11718 C CE2 . TYR D 79  ? 0.2608 0.2222 0.2967 -0.0419 -0.0374 -0.0262 79  TYR D CE2 
11719 C CZ  . TYR D 79  ? 0.2907 0.2451 0.3161 -0.0461 -0.0348 -0.0205 79  TYR D CZ  
11720 O OH  . TYR D 79  ? 0.3542 0.3134 0.3767 -0.0518 -0.0277 -0.0185 79  TYR D OH  
11721 N N   . ASP D 80  ? 0.2092 0.1699 0.2286 -0.0164 -0.0679 -0.0330 80  ASP D N   
11722 C CA  . ASP D 80  ? 0.2598 0.2262 0.2752 -0.0126 -0.0739 -0.0363 80  ASP D CA  
11723 C C   . ASP D 80  ? 0.2372 0.1983 0.2398 -0.0087 -0.0737 -0.0332 80  ASP D C   
11724 O O   . ASP D 80  ? 0.2486 0.2096 0.2464 -0.0073 -0.0737 -0.0359 80  ASP D O   
11725 C CB  . ASP D 80  ? 0.2110 0.1914 0.2319 -0.0093 -0.0779 -0.0357 80  ASP D CB  
11726 C CG  . ASP D 80  ? 0.2914 0.2802 0.3260 -0.0129 -0.0800 -0.0409 80  ASP D CG  
11727 O OD1 . ASP D 80  ? 0.3408 0.3251 0.3790 -0.0177 -0.0777 -0.0453 80  ASP D OD1 
11728 O OD2 . ASP D 80  ? 0.2583 0.2586 0.3010 -0.0105 -0.0826 -0.0393 80  ASP D OD2 
11729 N N   . LEU D 81  ? 0.2189 0.1774 0.2176 -0.0066 -0.0702 -0.0271 81  LEU D N   
11730 C CA  . LEU D 81  ? 0.2192 0.1737 0.2073 -0.0032 -0.0697 -0.0241 81  LEU D CA  
11731 C C   . LEU D 81  ? 0.2818 0.2258 0.2653 -0.0053 -0.0681 -0.0253 81  LEU D C   
11732 O O   . LEU D 81  ? 0.2592 0.2022 0.2367 -0.0026 -0.0684 -0.0258 81  LEU D O   
11733 C CB  . LEU D 81  ? 0.2327 0.1865 0.2206 -0.0014 -0.0660 -0.0183 81  LEU D CB  
11734 C CG  . LEU D 81  ? 0.2430 0.1936 0.2221 0.0016  -0.0649 -0.0148 81  LEU D CG  
11735 C CD1 . LEU D 81  ? 0.2634 0.2215 0.2374 0.0053  -0.0691 -0.0146 81  LEU D CD1 
11736 C CD2 . LEU D 81  ? 0.2300 0.1799 0.2128 0.0025  -0.0610 -0.0106 81  LEU D CD2 
11737 N N   . LYS D 82  ? 0.2636 0.2016 0.2512 -0.0099 -0.0652 -0.0246 82  LYS D N   
11738 C CA  . LYS D 82  ? 0.2586 0.1871 0.2440 -0.0118 -0.0641 -0.0235 82  LYS D CA  
11739 C C   . LYS D 82  ? 0.2977 0.2267 0.2876 -0.0109 -0.0657 -0.0284 82  LYS D C   
11740 O O   . LYS D 82  ? 0.3009 0.2255 0.2884 -0.0087 -0.0659 -0.0288 82  LYS D O   
11741 C CB  . LYS D 82  ? 0.2485 0.1729 0.2375 -0.0176 -0.0605 -0.0201 82  LYS D CB  
11742 C CG  . LYS D 82  ? 0.2584 0.1732 0.2455 -0.0199 -0.0599 -0.0159 82  LYS D CG  
11743 C CD  . LYS D 82  ? 0.2709 0.1850 0.2604 -0.0263 -0.0557 -0.0111 82  LYS D CD  
11744 C CE  . LYS D 82  ? 0.3814 0.2864 0.3756 -0.0299 -0.0564 -0.0070 82  LYS D CE  
11745 N NZ  . LYS D 82  ? 0.4344 0.3328 0.4223 -0.0274 -0.0578 -0.0015 82  LYS D NZ  
11746 N N   . ASP D 83  ? 0.2411 0.1763 0.2389 -0.0127 -0.0669 -0.0332 83  ASP D N   
11747 C CA  . ASP D 83  ? 0.2988 0.2360 0.3020 -0.0125 -0.0680 -0.0399 83  ASP D CA  
11748 C C   . ASP D 83  ? 0.2869 0.2311 0.2832 -0.0076 -0.0697 -0.0435 83  ASP D C   
11749 O O   . ASP D 83  ? 0.2882 0.2312 0.2864 -0.0066 -0.0695 -0.0486 83  ASP D O   
11750 C CB  . ASP D 83  ? 0.2441 0.1889 0.2567 -0.0158 -0.0691 -0.0449 83  ASP D CB  
11751 C CG  . ASP D 83  ? 0.3220 0.2610 0.3431 -0.0217 -0.0665 -0.0422 83  ASP D CG  
11752 O OD1 . ASP D 83  ? 0.3453 0.2744 0.3642 -0.0237 -0.0640 -0.0360 83  ASP D OD1 
11753 O OD2 . ASP D 83  ? 0.3415 0.2871 0.3715 -0.0249 -0.0671 -0.0460 83  ASP D OD2 
11754 N N   . LYS D 84  ? 0.2660 0.2180 0.2553 -0.0047 -0.0710 -0.0408 84  LYS D N   
11755 C CA  . LYS D 84  ? 0.2613 0.2220 0.2432 -0.0009 -0.0719 -0.0429 84  LYS D CA  
11756 C C   . LYS D 84  ? 0.2999 0.2540 0.2761 0.0017  -0.0699 -0.0411 84  LYS D C   
11757 O O   . LYS D 84  ? 0.2957 0.2545 0.2695 0.0036  -0.0696 -0.0460 84  LYS D O   
11758 C CB  . LYS D 84  ? 0.2241 0.1947 0.2015 0.0013  -0.0739 -0.0380 84  LYS D CB  
11759 C CG  . LYS D 84  ? 0.2504 0.2342 0.2207 0.0039  -0.0748 -0.0391 84  LYS D CG  
11760 C CD  . LYS D 84  ? 0.2669 0.2610 0.2403 0.0018  -0.0767 -0.0475 84  LYS D CD  
11761 C CE  . LYS D 84  ? 0.3289 0.3383 0.2934 0.0031  -0.0775 -0.0481 84  LYS D CE  
11762 N NZ  . LYS D 84  ? 0.3486 0.3687 0.3150 0.0003  -0.0795 -0.0571 84  LYS D NZ  
11763 N N   . ALA D 85  ? 0.2670 0.2114 0.2411 0.0015  -0.0685 -0.0348 85  ALA D N   
11764 C CA  . ALA D 85  ? 0.2471 0.1856 0.2170 0.0037  -0.0672 -0.0331 85  ALA D CA  
11765 C C   . ALA D 85  ? 0.3123 0.2439 0.2891 0.0031  -0.0674 -0.0375 85  ALA D C   
11766 O O   . ALA D 85  ? 0.3012 0.2324 0.2774 0.0059  -0.0673 -0.0404 85  ALA D O   
11767 C CB  . ALA D 85  ? 0.2225 0.1539 0.1887 0.0028  -0.0660 -0.0258 85  ALA D CB  
11768 N N   . LYS D 86  ? 0.2809 0.2074 0.2661 -0.0006 -0.0675 -0.0380 86  LYS D N   
11769 C CA  . LYS D 86  ? 0.2555 0.1755 0.2505 -0.0013 -0.0675 -0.0417 86  LYS D CA  
11770 C C   . LYS D 86  ? 0.2713 0.1995 0.2700 0.0003  -0.0677 -0.0521 86  LYS D C   
11771 O O   . LYS D 86  ? 0.3215 0.2464 0.3261 0.0020  -0.0673 -0.0566 86  LYS D O   
11772 C CB  . LYS D 86  ? 0.2980 0.2116 0.3017 -0.0064 -0.0668 -0.0392 86  LYS D CB  
11773 C CG  . LYS D 86  ? 0.3508 0.2563 0.3668 -0.0074 -0.0664 -0.0411 86  LYS D CG  
11774 C CD  . LYS D 86  ? 0.3498 0.2473 0.3651 -0.0045 -0.0669 -0.0358 86  LYS D CD  
11775 C CE  . LYS D 86  ? 0.3260 0.2148 0.3561 -0.0055 -0.0664 -0.0353 86  LYS D CE  
11776 N NZ  . LYS D 86  ? 0.3384 0.2212 0.3692 -0.0020 -0.0675 -0.0298 86  LYS D NZ  
11777 N N   . GLU D 87  ? 0.3062 0.2460 0.3018 -0.0004 -0.0683 -0.0561 87  GLU D N   
11778 C CA  . GLU D 87  ? 0.3129 0.2631 0.3098 0.0002  -0.0685 -0.0662 87  GLU D CA  
11779 C C   . GLU D 87  ? 0.3426 0.2990 0.3310 0.0042  -0.0677 -0.0679 87  GLU D C   
11780 O O   . GLU D 87  ? 0.3810 0.3399 0.3733 0.0053  -0.0667 -0.0762 87  GLU D O   
11781 C CB  . GLU D 87  ? 0.3038 0.2665 0.2986 -0.0018 -0.0702 -0.0686 87  GLU D CB  
11782 C CG  . GLU D 87  ? 0.3983 0.3758 0.3881 -0.0010 -0.0707 -0.0766 87  GLU D CG  
11783 C CD  . GLU D 87  ? 0.4207 0.4129 0.4054 -0.0023 -0.0734 -0.0758 87  GLU D CD  
11784 O OE1 . GLU D 87  ? 0.4354 0.4261 0.4231 -0.0037 -0.0749 -0.0707 87  GLU D OE1 
11785 O OE2 . GLU D 87  ? 0.5051 0.5110 0.4831 -0.0020 -0.0743 -0.0801 87  GLU D OE2 
11786 N N   . LEU D 88  ? 0.3435 0.3029 0.3214 0.0062  -0.0677 -0.0605 88  LEU D N   
11787 C CA  . LEU D 88  ? 0.3185 0.2863 0.2877 0.0091  -0.0666 -0.0615 88  LEU D CA  
11788 C C   . LEU D 88  ? 0.3344 0.2935 0.3059 0.0119  -0.0654 -0.0618 88  LEU D C   
11789 O O   . LEU D 88  ? 0.3236 0.2882 0.2957 0.0137  -0.0640 -0.0689 88  LEU D O   
11790 C CB  . LEU D 88  ? 0.2938 0.2677 0.2530 0.0099  -0.0667 -0.0524 88  LEU D CB  
11791 C CG  . LEU D 88  ? 0.3176 0.3054 0.2728 0.0086  -0.0684 -0.0515 88  LEU D CG  
11792 C CD1 . LEU D 88  ? 0.2640 0.2561 0.2116 0.0102  -0.0682 -0.0412 88  LEU D CD1 
11793 C CD2 . LEU D 88  ? 0.3355 0.3365 0.2880 0.0078  -0.0684 -0.0604 88  LEU D CD2 
11794 N N   . PHE D 89  ? 0.3286 0.2752 0.3016 0.0120  -0.0659 -0.0543 89  PHE D N   
11795 C CA  . PHE D 89  ? 0.3203 0.2595 0.2944 0.0146  -0.0657 -0.0525 89  PHE D CA  
11796 C C   . PHE D 89  ? 0.3442 0.2708 0.3303 0.0142  -0.0669 -0.0526 89  PHE D C   
11797 O O   . PHE D 89  ? 0.3156 0.2368 0.3052 0.0168  -0.0673 -0.0518 89  PHE D O   
11798 C CB  . PHE D 89  ? 0.2933 0.2292 0.2588 0.0148  -0.0657 -0.0427 89  PHE D CB  
11799 C CG  . PHE D 89  ? 0.2928 0.2388 0.2497 0.0144  -0.0644 -0.0391 89  PHE D CG  
11800 C CD1 . PHE D 89  ? 0.3177 0.2753 0.2687 0.0163  -0.0630 -0.0414 89  PHE D CD1 
11801 C CD2 . PHE D 89  ? 0.2577 0.2018 0.2134 0.0121  -0.0646 -0.0329 89  PHE D CD2 
11802 C CE1 . PHE D 89  ? 0.3062 0.2728 0.2505 0.0158  -0.0622 -0.0359 89  PHE D CE1 
11803 C CE2 . PHE D 89  ? 0.2234 0.1757 0.1741 0.0123  -0.0638 -0.0289 89  PHE D CE2 
11804 C CZ  . PHE D 89  ? 0.2733 0.2367 0.2185 0.0142  -0.0629 -0.0295 89  PHE D CZ  
11805 N N   . ASN D 90  ? 0.2821 0.2046 0.2757 0.0108  -0.0672 -0.0527 90  ASN D N   
11806 C CA  . ASN D 90  ? 0.3091 0.2197 0.3146 0.0093  -0.0678 -0.0497 90  ASN D CA  
11807 C C   . ASN D 90  ? 0.3236 0.2253 0.3248 0.0084  -0.0690 -0.0380 90  ASN D C   
11808 O O   . ASN D 90  ? 0.3604 0.2537 0.3695 0.0087  -0.0698 -0.0332 90  ASN D O   
11809 C CB  . ASN D 90  ? 0.3667 0.2754 0.3840 0.0124  -0.0673 -0.0565 90  ASN D CB  
11810 C CG  . ASN D 90  ? 0.3740 0.2728 0.4071 0.0102  -0.0672 -0.0549 90  ASN D CG  
11811 O OD1 . ASN D 90  ? 0.3105 0.2058 0.3455 0.0059  -0.0671 -0.0509 90  ASN D OD1 
11812 N ND2 . ASN D 90  ? 0.3372 0.2322 0.3828 0.0131  -0.0670 -0.0579 90  ASN D ND2 
11813 N N   . TYR D 91  ? 0.3059 0.2102 0.2952 0.0072  -0.0689 -0.0329 91  TYR D N   
11814 C CA  . TYR D 91  ? 0.2742 0.1721 0.2580 0.0055  -0.0696 -0.0232 91  TYR D CA  
11815 C C   . TYR D 91  ? 0.3096 0.2042 0.2944 0.0001  -0.0688 -0.0182 91  TYR D C   
11816 O O   . TYR D 91  ? 0.2736 0.1737 0.2583 -0.0019 -0.0677 -0.0215 91  TYR D O   
11817 C CB  . TYR D 91  ? 0.2821 0.1850 0.2538 0.0070  -0.0692 -0.0217 91  TYR D CB  
11818 C CG  . TYR D 91  ? 0.2974 0.2037 0.2677 0.0117  -0.0692 -0.0244 91  TYR D CG  
11819 C CD1 . TYR D 91  ? 0.3061 0.2101 0.2857 0.0148  -0.0704 -0.0302 91  TYR D CD1 
11820 C CD2 . TYR D 91  ? 0.2586 0.1714 0.2206 0.0128  -0.0673 -0.0215 91  TYR D CD2 
11821 C CE1 . TYR D 91  ? 0.2857 0.1939 0.2651 0.0191  -0.0700 -0.0336 91  TYR D CE1 
11822 C CE2 . TYR D 91  ? 0.2548 0.1720 0.2165 0.0165  -0.0668 -0.0237 91  TYR D CE2 
11823 C CZ  . TYR D 91  ? 0.2995 0.2151 0.2695 0.0197  -0.0680 -0.0298 91  TYR D CZ  
11824 O OH  . TYR D 91  ? 0.2776 0.1990 0.2482 0.0234  -0.0668 -0.0327 91  TYR D OH  
11825 N N   . ASP D 92  ? 0.3115 0.1986 0.2977 -0.0025 -0.0693 -0.0096 92  ASP D N   
11826 C CA  . ASP D 92  ? 0.3098 0.1938 0.2985 -0.0085 -0.0680 -0.0045 92  ASP D CA  
11827 C C   . ASP D 92  ? 0.3222 0.2117 0.3005 -0.0119 -0.0656 -0.0010 92  ASP D C   
11828 O O   . ASP D 92  ? 0.3093 0.1996 0.2899 -0.0169 -0.0636 0.0006  92  ASP D O   
11829 C CB  . ASP D 92  ? 0.3272 0.2040 0.3221 -0.0102 -0.0686 0.0050  92  ASP D CB  
11830 C CG  . ASP D 92  ? 0.4020 0.2754 0.4125 -0.0080 -0.0688 0.0012  92  ASP D CG  
11831 O OD1 . ASP D 92  ? 0.4652 0.3413 0.4820 -0.0077 -0.0679 -0.0085 92  ASP D OD1 
11832 O OD2 . ASP D 92  ? 0.4004 0.2694 0.4176 -0.0067 -0.0698 0.0077  92  ASP D OD2 
11833 N N   . TYR D 93  ? 0.2969 0.1924 0.2660 -0.0094 -0.0647 -0.0005 93  TYR D N   
11834 C CA  . TYR D 93  ? 0.2903 0.1924 0.2521 -0.0125 -0.0613 0.0023  93  TYR D CA  
11835 C C   . TYR D 93  ? 0.2901 0.1988 0.2483 -0.0093 -0.0601 -0.0028 93  TYR D C   
11836 O O   . TYR D 93  ? 0.2867 0.1961 0.2431 -0.0049 -0.0615 -0.0049 93  TYR D O   
11837 C CB  . TYR D 93  ? 0.2930 0.1961 0.2484 -0.0139 -0.0610 0.0096  93  TYR D CB  
11838 C CG  . TYR D 93  ? 0.3167 0.2139 0.2757 -0.0166 -0.0628 0.0178  93  TYR D CG  
11839 C CD1 . TYR D 93  ? 0.3189 0.2155 0.2798 -0.0226 -0.0606 0.0219  93  TYR D CD1 
11840 C CD2 . TYR D 93  ? 0.3284 0.2209 0.2901 -0.0132 -0.0666 0.0222  93  TYR D CD2 
11841 C CE1 . TYR D 93  ? 0.3548 0.2457 0.3198 -0.0256 -0.0621 0.0315  93  TYR D CE1 
11842 C CE2 . TYR D 93  ? 0.3582 0.2446 0.3252 -0.0154 -0.0687 0.0318  93  TYR D CE2 
11843 C CZ  . TYR D 93  ? 0.3865 0.2718 0.3549 -0.0218 -0.0664 0.0370  93  TYR D CZ  
11844 O OH  . TYR D 93  ? 0.3592 0.2384 0.3336 -0.0245 -0.0682 0.0484  93  TYR D OH  
11845 N N   . ILE D 94  ? 0.2656 0.1793 0.2239 -0.0117 -0.0572 -0.0042 94  ILE D N   
11846 C CA  . ILE D 94  ? 0.2529 0.1722 0.2103 -0.0089 -0.0560 -0.0071 94  ILE D CA  
11847 C C   . ILE D 94  ? 0.2064 0.1302 0.1629 -0.0119 -0.0516 -0.0065 94  ILE D C   
11848 O O   . ILE D 94  ? 0.2350 0.1601 0.1922 -0.0167 -0.0491 -0.0056 94  ILE D O   
11849 C CB  . ILE D 94  ? 0.2413 0.1638 0.2040 -0.0071 -0.0576 -0.0110 94  ILE D CB  
11850 C CG1 . ILE D 94  ? 0.2662 0.1909 0.2353 -0.0112 -0.0559 -0.0119 94  ILE D CG1 
11851 C CG2 . ILE D 94  ? 0.2623 0.1824 0.2259 -0.0047 -0.0614 -0.0141 94  ILE D CG2 
11852 C CD1 . ILE D 94  ? 0.2332 0.1648 0.2080 -0.0092 -0.0564 -0.0144 94  ILE D CD1 
11853 N N   . ILE D 95  ? 0.2200 0.1467 0.1758 -0.0095 -0.0503 -0.0076 95  ILE D N   
11854 C CA  . ILE D 95  ? 0.2427 0.1739 0.2014 -0.0116 -0.0458 -0.0096 95  ILE D CA  
11855 C C   . ILE D 95  ? 0.2220 0.1548 0.1868 -0.0074 -0.0458 -0.0105 95  ILE D C   
11856 O O   . ILE D 95  ? 0.2071 0.1390 0.1694 -0.0044 -0.0470 -0.0090 95  ILE D O   
11857 C CB  . ILE D 95  ? 0.2272 0.1604 0.1804 -0.0138 -0.0439 -0.0096 95  ILE D CB  
11858 C CG1 . ILE D 95  ? 0.2397 0.1720 0.1857 -0.0170 -0.0455 -0.0058 95  ILE D CG1 
11859 C CG2 . ILE D 95  ? 0.1998 0.1386 0.1577 -0.0170 -0.0385 -0.0143 95  ILE D CG2 
11860 C CD1 . ILE D 95  ? 0.2125 0.1496 0.1524 -0.0192 -0.0446 -0.0056 95  ILE D CD1 
11861 N N   . PRO D 96  ? 0.1861 0.1217 0.1596 -0.0071 -0.0447 -0.0119 96  PRO D N   
11862 C CA  . PRO D 96  ? 0.1560 0.0933 0.1364 -0.0030 -0.0451 -0.0103 96  PRO D CA  
11863 C C   . PRO D 96  ? 0.1811 0.1182 0.1657 -0.0034 -0.0409 -0.0115 96  PRO D C   
11864 O O   . PRO D 96  ? 0.1816 0.1196 0.1654 -0.0073 -0.0373 -0.0156 96  PRO D O   
11865 C CB  . PRO D 96  ? 0.1811 0.1224 0.1719 -0.0027 -0.0452 -0.0114 96  PRO D CB  
11866 C CG  . PRO D 96  ? 0.2435 0.1856 0.2346 -0.0079 -0.0421 -0.0152 96  PRO D CG  
11867 C CD  . PRO D 96  ? 0.2192 0.1574 0.1980 -0.0106 -0.0428 -0.0142 96  PRO D CD  
11868 N N   . ALA D 97  ? 0.1899 0.1267 0.1785 0.0002  -0.0415 -0.0080 97  ALA D N   
11869 C CA  . ALA D 97  ? 0.2019 0.1375 0.1979 -0.0001 -0.0376 -0.0090 97  ALA D CA  
11870 C C   . ALA D 97  ? 0.1889 0.1249 0.1979 0.0038  -0.0378 -0.0041 97  ALA D C   
11871 O O   . ALA D 97  ? 0.2247 0.1633 0.2329 0.0069  -0.0419 0.0010  97  ALA D O   
11872 C CB  . ALA D 97  ? 0.2205 0.1546 0.2082 -0.0002 -0.0380 -0.0077 97  ALA D CB  
11873 N N   . HIS D 98  ? 0.1976 0.1317 0.2198 0.0034  -0.0335 -0.0058 98  HIS D N   
11874 C CA  . HIS D 98  ? 0.1872 0.1210 0.2251 0.0074  -0.0338 0.0003  98  HIS D CA  
11875 C C   . HIS D 98  ? 0.1851 0.1187 0.2189 0.0104  -0.0366 0.0104  98  HIS D C   
11876 O O   . HIS D 98  ? 0.1845 0.1206 0.2250 0.0142  -0.0394 0.0189  98  HIS D O   
11877 C CB  . HIS D 98  ? 0.1917 0.1226 0.2492 0.0063  -0.0280 -0.0050 98  HIS D CB  
11878 C CG  . HIS D 98  ? 0.2240 0.1510 0.2848 0.0046  -0.0247 -0.0058 98  HIS D CG  
11879 N ND1 . HIS D 98  ? 0.2221 0.1497 0.2755 -0.0002 -0.0217 -0.0147 98  HIS D ND1 
11880 C CD2 . HIS D 98  ? 0.2219 0.1452 0.2936 0.0067  -0.0239 0.0016  98  HIS D CD2 
11881 C CE1 . HIS D 98  ? 0.2367 0.1614 0.2969 -0.0010 -0.0193 -0.0141 98  HIS D CE1 
11882 N NE2 . HIS D 98  ? 0.2251 0.1464 0.2967 0.0029  -0.0202 -0.0040 98  HIS D NE2 
11883 N N   . GLN D 99  ? 0.1936 0.1261 0.2167 0.0087  -0.0359 0.0100  99  GLN D N   
11884 C CA  . GLN D 99  ? 0.1906 0.1255 0.2061 0.0109  -0.0382 0.0186  99  GLN D CA  
11885 C C   . GLN D 99  ? 0.1949 0.1295 0.1984 0.0085  -0.0373 0.0146  99  GLN D C   
11886 O O   . GLN D 99  ? 0.1950 0.1282 0.1940 0.0056  -0.0363 0.0066  99  GLN D O   
11887 C CB  . GLN D 99  ? 0.1626 0.0961 0.1927 0.0128  -0.0364 0.0277  99  GLN D CB  
11888 C CG  . GLN D 99  ? 0.1672 0.0948 0.2100 0.0102  -0.0309 0.0246  99  GLN D CG  
11889 C CD  . GLN D 99  ? 0.2012 0.1261 0.2619 0.0123  -0.0293 0.0353  99  GLN D CD  
11890 O OE1 . GLN D 99  ? 0.2109 0.1357 0.2844 0.0152  -0.0305 0.0397  99  GLN D OE1 
11891 N NE2 . GLN D 99  ? 0.2413 0.1650 0.3041 0.0109  -0.0267 0.0403  99  GLN D NE2 
11892 N N   . GLY D 100 ? 0.1976 0.1349 0.1961 0.0097  -0.0377 0.0207  100 GLY D N   
11893 C CA  . GLY D 100 ? 0.1517 0.0906 0.1390 0.0084  -0.0377 0.0171  100 GLY D CA  
11894 C C   . GLY D 100 ? 0.1957 0.1314 0.1875 0.0049  -0.0343 0.0105  100 GLY D C   
11895 O O   . GLY D 100 ? 0.1985 0.1347 0.1822 0.0033  -0.0355 0.0046  100 GLY D O   
11896 N N   . ARG D 101 ? 0.1701 0.1030 0.1757 0.0033  -0.0303 0.0114  101 ARG D N   
11897 C CA  . ARG D 101 ? 0.1797 0.1117 0.1901 -0.0007 -0.0272 0.0034  101 ARG D CA  
11898 C C   . ARG D 101 ? 0.1773 0.1088 0.1876 -0.0031 -0.0269 -0.0056 101 ARG D C   
11899 O O   . ARG D 101 ? 0.1962 0.1302 0.2038 -0.0066 -0.0261 -0.0129 101 ARG D O   
11900 C CB  . ARG D 101 ? 0.1807 0.1097 0.2083 -0.0022 -0.0226 0.0054  101 ARG D CB  
11901 C CG  . ARG D 101 ? 0.1849 0.1090 0.2295 -0.0016 -0.0203 0.0059  101 ARG D CG  
11902 C CD  . ARG D 101 ? 0.2093 0.1296 0.2711 -0.0017 -0.0168 0.0131  101 ARG D CD  
11903 N NE  . ARG D 101 ? 0.2496 0.1726 0.3049 0.0016  -0.0191 0.0270  101 ARG D NE  
11904 C CZ  . ARG D 101 ? 0.2393 0.1602 0.3070 0.0022  -0.0169 0.0380  101 ARG D CZ  
11905 N NH1 . ARG D 101 ? 0.2262 0.1405 0.3157 -0.0003 -0.0121 0.0366  101 ARG D NH1 
11906 N NH2 . ARG D 101 ? 0.2573 0.1835 0.3161 0.0050  -0.0195 0.0508  101 ARG D NH2 
11907 N N   . GLY D 102 ? 0.1585 0.0886 0.1715 -0.0016 -0.0277 -0.0051 102 GLY D N   
11908 C CA  . GLY D 102 ? 0.2000 0.1316 0.2101 -0.0043 -0.0273 -0.0129 102 GLY D CA  
11909 C C   . GLY D 102 ? 0.1988 0.1330 0.1917 -0.0049 -0.0310 -0.0135 102 GLY D C   
11910 O O   . GLY D 102 ? 0.2047 0.1419 0.1925 -0.0086 -0.0305 -0.0193 102 GLY D O   
11911 N N   . ALA D 103 ? 0.1774 0.1112 0.1622 -0.0016 -0.0349 -0.0074 103 ALA D N   
11912 C CA  . ALA D 103 ? 0.1884 0.1233 0.1604 -0.0016 -0.0385 -0.0078 103 ALA D CA  
11913 C C   . ALA D 103 ? 0.2549 0.1921 0.2231 -0.0032 -0.0386 -0.0098 103 ALA D C   
11914 O O   . ALA D 103 ? 0.2486 0.1874 0.2097 -0.0049 -0.0406 -0.0116 103 ALA D O   
11915 C CB  . ALA D 103 ? 0.1997 0.1346 0.1664 0.0024  -0.0420 -0.0030 103 ALA D CB  
11916 N N   . GLU D 104 ? 0.2285 0.1666 0.2024 -0.0028 -0.0365 -0.0087 104 GLU D N   
11917 C CA  . GLU D 104 ? 0.2256 0.1674 0.1983 -0.0046 -0.0365 -0.0113 104 GLU D CA  
11918 C C   . GLU D 104 ? 0.2535 0.1986 0.2283 -0.0094 -0.0349 -0.0183 104 GLU D C   
11919 O O   . GLU D 104 ? 0.2613 0.2113 0.2299 -0.0111 -0.0372 -0.0204 104 GLU D O   
11920 C CB  . GLU D 104 ? 0.2285 0.1712 0.2089 -0.0039 -0.0338 -0.0087 104 GLU D CB  
11921 C CG  . GLU D 104 ? 0.2516 0.1950 0.2273 0.0002  -0.0352 -0.0023 104 GLU D CG  
11922 C CD  . GLU D 104 ? 0.2914 0.2357 0.2752 0.0004  -0.0316 0.0030  104 GLU D CD  
11923 O OE1 . GLU D 104 ? 0.2616 0.2035 0.2574 -0.0021 -0.0280 0.0027  104 GLU D OE1 
11924 O OE2 . GLU D 104 ? 0.3070 0.2551 0.2859 0.0029  -0.0321 0.0076  104 GLU D OE2 
11925 N N   . ASN D 105 ? 0.2264 0.1701 0.2105 -0.0115 -0.0309 -0.0222 105 ASN D N   
11926 C CA  . ASN D 105 ? 0.2204 0.1693 0.2065 -0.0166 -0.0286 -0.0310 105 ASN D CA  
11927 C C   . ASN D 105 ? 0.2391 0.1917 0.2126 -0.0183 -0.0313 -0.0314 105 ASN D C   
11928 O O   . ASN D 105 ? 0.2665 0.2269 0.2345 -0.0224 -0.0318 -0.0359 105 ASN D O   
11929 C CB  . ASN D 105 ? 0.2258 0.1720 0.2270 -0.0179 -0.0233 -0.0360 105 ASN D CB  
11930 C CG  . ASN D 105 ? 0.2523 0.2054 0.2589 -0.0237 -0.0197 -0.0479 105 ASN D CG  
11931 O OD1 . ASN D 105 ? 0.2268 0.1862 0.2309 -0.0268 -0.0204 -0.0521 105 ASN D OD1 
11932 N ND2 . ASN D 105 ? 0.2696 0.2232 0.2844 -0.0255 -0.0156 -0.0544 105 ASN D ND2 
11933 N N   . ILE D 106 ? 0.2403 0.1883 0.2094 -0.0156 -0.0331 -0.0262 106 ILE D N   
11934 C CA  . ILE D 106 ? 0.2704 0.2208 0.2289 -0.0174 -0.0354 -0.0248 106 ILE D CA  
11935 C C   . ILE D 106 ? 0.2993 0.2523 0.2484 -0.0170 -0.0402 -0.0209 106 ILE D C   
11936 O O   . ILE D 106 ? 0.3112 0.2711 0.2533 -0.0207 -0.0415 -0.0216 106 ILE D O   
11937 C CB  . ILE D 106 ? 0.2693 0.2139 0.2274 -0.0147 -0.0367 -0.0204 106 ILE D CB  
11938 C CG1 . ILE D 106 ? 0.2007 0.1457 0.1679 -0.0161 -0.0323 -0.0246 106 ILE D CG1 
11939 C CG2 . ILE D 106 ? 0.2682 0.2131 0.2161 -0.0159 -0.0401 -0.0164 106 ILE D CG2 
11940 C CD1 . ILE D 106 ? 0.2071 0.1478 0.1762 -0.0131 -0.0340 -0.0206 106 ILE D CD1 
11941 N N   . LEU D 107 ? 0.2674 0.2163 0.2166 -0.0124 -0.0430 -0.0164 107 LEU D N   
11942 C CA  . LEU D 107 ? 0.2736 0.2230 0.2163 -0.0105 -0.0480 -0.0118 107 LEU D CA  
11943 C C   . LEU D 107 ? 0.2540 0.2102 0.1969 -0.0111 -0.0497 -0.0131 107 LEU D C   
11944 O O   . LEU D 107 ? 0.2777 0.2381 0.2154 -0.0117 -0.0538 -0.0101 107 LEU D O   
11945 C CB  . LEU D 107 ? 0.2609 0.2040 0.2046 -0.0053 -0.0500 -0.0082 107 LEU D CB  
11946 C CG  . LEU D 107 ? 0.2592 0.2011 0.1997 -0.0027 -0.0549 -0.0044 107 LEU D CG  
11947 C CD1 . LEU D 107 ? 0.2239 0.1648 0.1600 -0.0053 -0.0567 -0.0011 107 LEU D CD1 
11948 C CD2 . LEU D 107 ? 0.2300 0.1674 0.1728 0.0022  -0.0559 -0.0039 107 LEU D CD2 
11949 N N   . PHE D 108 ? 0.2586 0.2164 0.2085 -0.0109 -0.0470 -0.0165 108 PHE D N   
11950 C CA  . PHE D 108 ? 0.2217 0.1866 0.1733 -0.0111 -0.0491 -0.0176 108 PHE D CA  
11951 C C   . PHE D 108 ? 0.2213 0.1964 0.1696 -0.0163 -0.0503 -0.0216 108 PHE D C   
11952 O O   . PHE D 108 ? 0.2340 0.2159 0.1791 -0.0159 -0.0550 -0.0192 108 PHE D O   
11953 C CB  . PHE D 108 ? 0.2544 0.2192 0.2156 -0.0107 -0.0453 -0.0201 108 PHE D CB  
11954 C CG  . PHE D 108 ? 0.2936 0.2532 0.2562 -0.0057 -0.0450 -0.0155 108 PHE D CG  
11955 C CD1 . PHE D 108 ? 0.2459 0.2008 0.2025 -0.0020 -0.0478 -0.0116 108 PHE D CD1 
11956 C CD2 . PHE D 108 ? 0.2911 0.2515 0.2613 -0.0053 -0.0416 -0.0154 108 PHE D CD2 
11957 C CE1 . PHE D 108 ? 0.2914 0.2440 0.2486 0.0020  -0.0473 -0.0091 108 PHE D CE1 
11958 C CE2 . PHE D 108 ? 0.3225 0.2810 0.2923 -0.0013 -0.0409 -0.0112 108 PHE D CE2 
11959 C CZ  . PHE D 108 ? 0.2823 0.2377 0.2450 0.0023  -0.0439 -0.0088 108 PHE D CZ  
11960 N N   . PRO D 109 ? 0.2440 0.2220 0.1934 -0.0212 -0.0463 -0.0279 109 PRO D N   
11961 C CA  . PRO D 109 ? 0.2874 0.2781 0.2312 -0.0267 -0.0476 -0.0324 109 PRO D CA  
11962 C C   . PRO D 109 ? 0.2749 0.2698 0.2087 -0.0259 -0.0512 -0.0245 109 PRO D C   
11963 O O   . PRO D 109 ? 0.2949 0.3020 0.2254 -0.0270 -0.0536 -0.0237 109 PRO D O   
11964 C CB  . PRO D 109 ? 0.2949 0.2866 0.2432 -0.0313 -0.0412 -0.0415 109 PRO D CB  
11965 C CG  . PRO D 109 ? 0.2361 0.2168 0.1970 -0.0281 -0.0370 -0.0422 109 PRO D CG  
11966 C CD  . PRO D 109 ? 0.2362 0.2080 0.1938 -0.0220 -0.0403 -0.0322 109 PRO D CD  
11967 N N   . VAL D 110 ? 0.2390 0.2239 0.1695 -0.0234 -0.0517 -0.0182 110 VAL D N   
11968 C CA  . VAL D 110 ? 0.2686 0.2556 0.1924 -0.0229 -0.0546 -0.0096 110 VAL D CA  
11969 C C   . VAL D 110 ? 0.2711 0.2589 0.1972 -0.0181 -0.0595 -0.0027 110 VAL D C   
11970 O O   . VAL D 110 ? 0.2971 0.2931 0.2198 -0.0185 -0.0625 0.0027  110 VAL D O   
11971 C CB  . VAL D 110 ? 0.3128 0.2883 0.2347 -0.0221 -0.0539 -0.0059 110 VAL D CB  
11972 C CG1 . VAL D 110 ? 0.2955 0.2693 0.2136 -0.0209 -0.0578 0.0044  110 VAL D CG1 
11973 C CG2 . VAL D 110 ? 0.2897 0.2678 0.2088 -0.0278 -0.0493 -0.0122 110 VAL D CG2 
11974 N N   . LEU D 111 ? 0.2760 0.2560 0.2085 -0.0134 -0.0604 -0.0028 111 LEU D N   
11975 C CA  . LEU D 111 ? 0.2637 0.2441 0.2005 -0.0086 -0.0646 0.0022  111 LEU D CA  
11976 C C   . LEU D 111 ? 0.2468 0.2415 0.1849 -0.0100 -0.0670 0.0008  111 LEU D C   
11977 O O   . LEU D 111 ? 0.2416 0.2416 0.1808 -0.0077 -0.0711 0.0069  111 LEU D O   
11978 C CB  . LEU D 111 ? 0.2079 0.1795 0.1508 -0.0038 -0.0643 0.0003  111 LEU D CB  
11979 C CG  . LEU D 111 ? 0.2429 0.2025 0.1854 -0.0016 -0.0627 0.0012  111 LEU D CG  
11980 C CD1 . LEU D 111 ? 0.2423 0.1975 0.1890 0.0025  -0.0619 -0.0020 111 LEU D CD1 
11981 C CD2 . LEU D 111 ? 0.2434 0.1981 0.1863 0.0004  -0.0657 0.0075  111 LEU D CD2 
11982 N N   . LEU D 112 ? 0.2213 0.2224 0.1604 -0.0138 -0.0646 -0.0076 112 LEU D N   
11983 C CA  . LEU D 112 ? 0.2352 0.2516 0.1758 -0.0160 -0.0668 -0.0110 112 LEU D CA  
11984 C C   . LEU D 112 ? 0.2853 0.3123 0.2184 -0.0177 -0.0688 -0.0076 112 LEU D C   
11985 O O   . LEU D 112 ? 0.3050 0.3407 0.2384 -0.0154 -0.0736 -0.0031 112 LEU D O   
11986 C CB  . LEU D 112 ? 0.2371 0.2570 0.1818 -0.0210 -0.0631 -0.0224 112 LEU D CB  
11987 C CG  . LEU D 112 ? 0.3016 0.3361 0.2496 -0.0234 -0.0655 -0.0288 112 LEU D CG  
11988 C CD1 . LEU D 112 ? 0.2848 0.3255 0.2388 -0.0200 -0.0702 -0.0248 112 LEU D CD1 
11989 C CD2 . LEU D 112 ? 0.2336 0.2660 0.1882 -0.0292 -0.0605 -0.0393 112 LEU D CD2 
11990 N N   . LYS D 113 ? 0.3113 0.3371 0.2376 -0.0215 -0.0653 -0.0095 113 LYS D N   
11991 C CA  . LYS D 113 ? 0.2967 0.3311 0.2142 -0.0240 -0.0667 -0.0055 113 LYS D CA  
11992 C C   . LYS D 113 ? 0.3342 0.3661 0.2500 -0.0200 -0.0712 0.0078  113 LYS D C   
11993 O O   . LYS D 113 ? 0.3881 0.4293 0.3000 -0.0200 -0.0751 0.0133  113 LYS D O   
11994 C CB  . LYS D 113 ? 0.2939 0.3267 0.2055 -0.0291 -0.0613 -0.0094 113 LYS D CB  
11995 C CG  . LYS D 113 ? 0.4451 0.4889 0.3468 -0.0334 -0.0614 -0.0056 113 LYS D CG  
11996 C CD  . LYS D 113 ? 0.5121 0.5705 0.4125 -0.0370 -0.0618 -0.0126 113 LYS D CD  
11997 C CE  . LYS D 113 ? 0.4182 0.4900 0.3078 -0.0418 -0.0617 -0.0083 113 LYS D CE  
11998 N NZ  . LYS D 113 ? 0.5161 0.6040 0.4044 -0.0457 -0.0622 -0.0155 113 LYS D NZ  
11999 N N   . TYR D 114 ? 0.3059 0.3240 0.2256 -0.0168 -0.0709 0.0130  114 TYR D N   
12000 C CA  . TYR D 114 ? 0.3449 0.3572 0.2669 -0.0129 -0.0748 0.0246  114 TYR D CA  
12001 C C   . TYR D 114 ? 0.3797 0.3975 0.3092 -0.0079 -0.0799 0.0278  114 TYR D C   
12002 O O   . TYR D 114 ? 0.3567 0.3786 0.2860 -0.0060 -0.0840 0.0367  114 TYR D O   
12003 C CB  . TYR D 114 ? 0.3050 0.3002 0.2314 -0.0107 -0.0732 0.0260  114 TYR D CB  
12004 C CG  . TYR D 114 ? 0.3508 0.3369 0.2825 -0.0069 -0.0766 0.0358  114 TYR D CG  
12005 C CD1 . TYR D 114 ? 0.4168 0.4021 0.3442 -0.0095 -0.0773 0.0445  114 TYR D CD1 
12006 C CD2 . TYR D 114 ? 0.3801 0.3580 0.3224 -0.0009 -0.0787 0.0358  114 TYR D CD2 
12007 C CE1 . TYR D 114 ? 0.4166 0.3925 0.3516 -0.0063 -0.0801 0.0533  114 TYR D CE1 
12008 C CE2 . TYR D 114 ? 0.3962 0.3653 0.3462 0.0025  -0.0815 0.0431  114 TYR D CE2 
12009 C CZ  . TYR D 114 ? 0.4003 0.3678 0.3472 -0.0001 -0.0821 0.0519  114 TYR D CZ  
12010 O OH  . TYR D 114 ? 0.4458 0.4036 0.4029 0.0031  -0.0846 0.0588  114 TYR D OH  
12011 N N   . LYS D 115 ? 0.2799 0.2979 0.2164 -0.0058 -0.0796 0.0211  115 LYS D N   
12012 C CA  . LYS D 115 ? 0.2985 0.3230 0.2434 -0.0014 -0.0843 0.0232  115 LYS D CA  
12013 C C   . LYS D 115 ? 0.3686 0.4103 0.3095 -0.0029 -0.0879 0.0228  115 LYS D C   
12014 O O   . LYS D 115 ? 0.3451 0.3929 0.2912 0.0011  -0.0932 0.0285  115 LYS D O   
12015 C CB  . LYS D 115 ? 0.3001 0.3219 0.2527 -0.0002 -0.0829 0.0153  115 LYS D CB  
12016 C CG  . LYS D 115 ? 0.2994 0.3259 0.2631 0.0050  -0.0874 0.0171  115 LYS D CG  
12017 C CD  . LYS D 115 ? 0.3617 0.3742 0.3332 0.0111  -0.0885 0.0218  115 LYS D CD  
12018 C CE  . LYS D 115 ? 0.3261 0.3434 0.3110 0.0169  -0.0928 0.0225  115 LYS D CE  
12019 N NZ  . LYS D 115 ? 0.3532 0.3576 0.3471 0.0230  -0.0938 0.0262  115 LYS D NZ  
12020 N N   . GLN D 116 ? 0.3734 0.4220 0.3061 -0.0085 -0.0854 0.0153  116 GLN D N   
12021 C CA  . GLN D 116 ? 0.3899 0.4524 0.3184 -0.0109 -0.0891 0.0127  116 GLN D CA  
12022 C C   . GLN D 116 ? 0.4520 0.5190 0.3707 -0.0128 -0.0915 0.0222  116 GLN D C   
12023 O O   . GLN D 116 ? 0.5244 0.6041 0.4374 -0.0165 -0.0939 0.0206  116 GLN D O   
12024 C CB  . GLN D 116 ? 0.3555 0.4217 0.2818 -0.0174 -0.0851 -0.0004 116 GLN D CB  
12025 C CG  . GLN D 116 ? 0.3584 0.4221 0.2956 -0.0165 -0.0841 -0.0089 116 GLN D CG  
12026 C CD  . GLN D 116 ? 0.3699 0.4372 0.3082 -0.0238 -0.0804 -0.0206 116 GLN D CD  
12027 O OE1 . GLN D 116 ? 0.3135 0.3796 0.2467 -0.0284 -0.0749 -0.0253 116 GLN D OE1 
12028 N NE2 . GLN D 116 ? 0.3447 0.4183 0.2919 -0.0252 -0.0823 -0.0256 116 GLN D NE2 
12029 N N   . LYS D 117 ? 0.4394 0.4971 0.3566 -0.0111 -0.0907 0.0321  117 LYS D N   
12030 C CA  . LYS D 117 ? 0.5008 0.5627 0.4118 -0.0120 -0.0939 0.0440  117 LYS D CA  
12031 C C   . LYS D 117 ? 0.5836 0.6528 0.5006 -0.0071 -0.1014 0.0506  117 LYS D C   
12032 O O   . LYS D 117 ? 0.5699 0.6369 0.4982 -0.0015 -0.1036 0.0484  117 LYS D O   
12033 C CB  . LYS D 117 ? 0.4841 0.5322 0.3963 -0.0110 -0.0921 0.0536  117 LYS D CB  
12034 C CG  . LYS D 117 ? 0.5293 0.5731 0.4336 -0.0169 -0.0858 0.0496  117 LYS D CG  
12035 C CD  . LYS D 117 ? 0.5971 0.6311 0.5009 -0.0177 -0.0852 0.0611  117 LYS D CD  
12036 C CE  . LYS D 117 ? 0.5546 0.5721 0.4714 -0.0115 -0.0865 0.0649  117 LYS D CE  
12037 N NZ  . LYS D 117 ? 0.4696 0.4761 0.3878 -0.0129 -0.0858 0.0748  117 LYS D NZ  
12038 N N   . GLU D 118 ? 0.7148 0.7940 0.6244 -0.0095 -0.1051 0.0589  118 GLU D N   
12039 C CA  . GLU D 118 ? 0.8002 0.8886 0.7143 -0.0057 -0.1130 0.0663  118 GLU D CA  
12040 C C   . GLU D 118 ? 0.7976 0.8972 0.7158 -0.0052 -0.1160 0.0555  118 GLU D C   
12041 O O   . GLU D 118 ? 0.8122 0.9188 0.7374 -0.0008 -0.1229 0.0599  118 GLU D O   
12042 C CB  . GLU D 118 ? 0.8332 0.9102 0.7607 0.0023  -0.1161 0.0768  118 GLU D CB  
12043 C CG  . GLU D 118 ? 0.9370 1.0031 0.8630 0.0015  -0.1146 0.0894  118 GLU D CG  
12044 C CD  . GLU D 118 ? 1.0677 1.1230 1.0094 0.0090  -0.1183 0.0995  118 GLU D CD  
12045 O OE1 . GLU D 118 ? 1.0662 1.1259 1.0184 0.0148  -0.1230 0.0989  118 GLU D OE1 
12046 O OE2 . GLU D 118 ? 0.9641 1.0064 0.9090 0.0088  -0.1163 0.1074  118 GLU D OE2 
12047 N N   . GLY D 119 ? 0.7524 0.8535 0.6680 -0.0098 -0.1112 0.0416  119 GLY D N   
12048 C CA  . GLY D 119 ? 0.6875 0.7993 0.6074 -0.0115 -0.1136 0.0311  119 GLY D CA  
12049 C C   . GLY D 119 ? 0.6722 0.7799 0.6071 -0.0053 -0.1159 0.0270  119 GLY D C   
12050 O O   . GLY D 119 ? 0.7135 0.8314 0.6545 -0.0058 -0.1201 0.0217  119 GLY D O   
12051 N N   . LYS D 120 ? 0.5278 0.6226 0.4697 0.0000  -0.1128 0.0294  120 LYS D N   
12052 C CA  . LYS D 120 ? 0.4653 0.5589 0.4217 0.0050  -0.1131 0.0247  120 LYS D CA  
12053 C C   . LYS D 120 ? 0.4074 0.4957 0.3644 0.0009  -0.1065 0.0128  120 LYS D C   
12054 O O   . LYS D 120 ? 0.4144 0.5003 0.3619 -0.0057 -0.1026 0.0072  120 LYS D O   
12055 C CB  . LYS D 120 ? 0.4955 0.5803 0.4610 0.0121  -0.1131 0.0351  120 LYS D CB  
12056 C CG  . LYS D 120 ? 0.5219 0.5907 0.4825 0.0108  -0.1074 0.0390  120 LYS D CG  
12057 C CD  . LYS D 120 ? 0.5466 0.6029 0.5194 0.0169  -0.1079 0.0469  120 LYS D CD  
12058 C CE  . LYS D 120 ? 0.5774 0.6164 0.5465 0.0151  -0.1026 0.0482  120 LYS D CE  
12059 N NZ  . LYS D 120 ? 0.6722 0.6968 0.6539 0.0207  -0.1034 0.0537  120 LYS D NZ  
12060 N N   . ALA D 121 ? 0.3954 0.4834 0.3647 0.0039  -0.1046 0.0097  121 ALA D N   
12061 C CA  . ALA D 121 ? 0.2852 0.3694 0.2568 -0.0005 -0.0981 0.0004  121 ALA D CA  
12062 C C   . ALA D 121 ? 0.2807 0.3647 0.2508 -0.0078 -0.0998 -0.0101 121 ALA D C   
12063 O O   . ALA D 121 ? 0.3081 0.3860 0.2740 -0.0142 -0.0943 -0.0163 121 ALA D O   
12064 C CB  . ALA D 121 ? 0.3352 0.4043 0.2987 -0.0027 -0.0921 0.0024  121 ALA D CB  
12065 N N   . LYS D 122 ? 0.2937 0.3890 0.2686 -0.0095 -0.1061 -0.0099 122 LYS D N   
12066 C CA  . LYS D 122 ? 0.2800 0.3859 0.2562 -0.0181 -0.1037 -0.0187 122 LYS D CA  
12067 C C   . LYS D 122 ? 0.2516 0.3578 0.2397 -0.0216 -0.0977 -0.0270 122 LYS D C   
12068 O O   . LYS D 122 ? 0.2458 0.3572 0.2360 -0.0277 -0.0925 -0.0372 122 LYS D O   
12069 C CB  . LYS D 122 ? 0.3440 0.4654 0.3233 -0.0176 -0.1112 -0.0166 122 LYS D CB  
12070 C CG  . LYS D 122 ? 0.3870 0.5130 0.3536 -0.0158 -0.1156 -0.0092 122 LYS D CG  
12071 C CD  . LYS D 122 ? 0.4621 0.5925 0.4165 -0.0236 -0.1100 -0.0156 122 LYS D CD  
12072 C CE  . LYS D 122 ? 0.4853 0.6256 0.4273 -0.0239 -0.1141 -0.0081 122 LYS D CE  
12073 N NZ  . LYS D 122 ? 0.6337 0.7753 0.5634 -0.0305 -0.1072 -0.0128 122 LYS D NZ  
12074 N N   . ASN D 123 ? 0.2463 0.3490 0.2436 -0.0173 -0.0974 -0.0237 123 ASN D N   
12075 C CA  . ASN D 123 ? 0.2217 0.3252 0.2312 -0.0181 -0.0909 -0.0327 123 ASN D CA  
12076 C C   . ASN D 123 ? 0.2649 0.3537 0.2728 -0.0133 -0.0870 -0.0307 123 ASN D C   
12077 O O   . ASN D 123 ? 0.2189 0.3050 0.2357 -0.0067 -0.0879 -0.0291 123 ASN D O   
12078 C CB  . ASN D 123 ? 0.2453 0.3614 0.2706 -0.0151 -0.0940 -0.0338 123 ASN D CB  
12079 C CG  . ASN D 123 ? 0.3412 0.4718 0.3678 -0.0187 -0.0993 -0.0346 123 ASN D CG  
12080 O OD1 . ASN D 123 ? 0.2831 0.4219 0.3143 -0.0147 -0.1069 -0.0275 123 ASN D OD1 
12081 N ND2 . ASN D 123 ? 0.2863 0.4201 0.3099 -0.0259 -0.0955 -0.0435 123 ASN D ND2 
12082 N N   . PRO D 124 ? 0.3035 0.3815 0.3006 -0.0162 -0.0830 -0.0315 124 PRO D N   
12083 C CA  . PRO D 124 ? 0.2251 0.2870 0.2175 -0.0109 -0.0813 -0.0271 124 PRO D CA  
12084 C C   . PRO D 124 ? 0.2272 0.2792 0.2281 -0.0096 -0.0734 -0.0304 124 PRO D C   
12085 O O   . PRO D 124 ? 0.2633 0.3166 0.2705 -0.0146 -0.0676 -0.0375 124 PRO D O   
12086 C CB  . PRO D 124 ? 0.1922 0.2485 0.1718 -0.0158 -0.0781 -0.0271 124 PRO D CB  
12087 C CG  . PRO D 124 ? 0.2716 0.3359 0.2538 -0.0235 -0.0751 -0.0366 124 PRO D CG  
12088 C CD  . PRO D 124 ? 0.2410 0.3195 0.2305 -0.0235 -0.0799 -0.0368 124 PRO D CD  
12089 N N   . VAL D 125 ? 0.1825 0.2251 0.1841 -0.0030 -0.0727 -0.0250 125 VAL D N   
12090 C CA  . VAL D 125 ? 0.1834 0.2183 0.1905 -0.0016 -0.0652 -0.0265 125 VAL D CA  
12091 C C   . VAL D 125 ? 0.2375 0.2582 0.2365 0.0027  -0.0637 -0.0216 125 VAL D C   
12092 O O   . VAL D 125 ? 0.2004 0.2174 0.1937 0.0060  -0.0688 -0.0169 125 VAL D O   
12093 C CB  . VAL D 125 ? 0.2386 0.2826 0.2587 0.0016  -0.0648 -0.0280 125 VAL D CB  
12094 C CG1 . VAL D 125 ? 0.2529 0.3122 0.2825 -0.0032 -0.0665 -0.0336 125 VAL D CG1 
12095 C CG2 . VAL D 125 ? 0.2119 0.2566 0.2340 0.0092  -0.0707 -0.0235 125 VAL D CG2 
12096 N N   . PHE D 126 ? 0.1986 0.2123 0.1979 0.0021  -0.0567 -0.0224 126 PHE D N   
12097 C CA  . PHE D 126 ? 0.1993 0.2026 0.1930 0.0061  -0.0545 -0.0192 126 PHE D CA  
12098 C C   . PHE D 126 ? 0.2124 0.2200 0.2132 0.0091  -0.0505 -0.0203 126 PHE D C   
12099 O O   . PHE D 126 ? 0.2026 0.2166 0.2108 0.0060  -0.0461 -0.0223 126 PHE D O   
12100 C CB  . PHE D 126 ? 0.2579 0.2522 0.2459 0.0028  -0.0499 -0.0184 126 PHE D CB  
12101 C CG  . PHE D 126 ? 0.2660 0.2551 0.2458 0.0007  -0.0527 -0.0176 126 PHE D CG  
12102 C CD1 . PHE D 126 ? 0.2548 0.2505 0.2342 -0.0035 -0.0555 -0.0203 126 PHE D CD1 
12103 C CD2 . PHE D 126 ? 0.2624 0.2417 0.2349 0.0022  -0.0522 -0.0148 126 PHE D CD2 
12104 C CE1 . PHE D 126 ? 0.1960 0.1889 0.1672 -0.0061 -0.0571 -0.0198 126 PHE D CE1 
12105 C CE2 . PHE D 126 ? 0.2544 0.2299 0.2203 -0.0002 -0.0539 -0.0142 126 PHE D CE2 
12106 C CZ  . PHE D 126 ? 0.1717 0.1542 0.1366 -0.0044 -0.0560 -0.0166 126 PHE D CZ  
12107 N N   . ILE D 127 ? 0.1647 0.1696 0.1642 0.0146  -0.0515 -0.0196 127 ILE D N   
12108 C CA  . ILE D 127 ? 0.1838 0.1945 0.1886 0.0172  -0.0468 -0.0219 127 ILE D CA  
12109 C C   . ILE D 127 ? 0.2227 0.2266 0.2188 0.0185  -0.0435 -0.0207 127 ILE D C   
12110 O O   . ILE D 127 ? 0.2270 0.2229 0.2172 0.0209  -0.0469 -0.0201 127 ILE D O   
12111 C CB  . ILE D 127 ? 0.1667 0.1841 0.1810 0.0228  -0.0505 -0.0248 127 ILE D CB  
12112 C CG1 . ILE D 127 ? 0.1802 0.2065 0.2034 0.0216  -0.0549 -0.0251 127 ILE D CG1 
12113 C CG2 . ILE D 127 ? 0.2040 0.2294 0.2239 0.0251  -0.0444 -0.0289 127 ILE D CG2 
12114 C CD1 . ILE D 127 ? 0.2058 0.2380 0.2401 0.0279  -0.0600 -0.0264 127 ILE D CD1 
12115 N N   . SER D 128 ? 0.1942 0.2026 0.1900 0.0167  -0.0369 -0.0201 128 SER D N   
12116 C CA  . SER D 128 ? 0.1791 0.1849 0.1661 0.0176  -0.0339 -0.0185 128 SER D CA  
12117 C C   . SER D 128 ? 0.1776 0.1953 0.1670 0.0182  -0.0280 -0.0204 128 SER D C   
12118 O O   . SER D 128 ? 0.1947 0.2210 0.1926 0.0163  -0.0246 -0.0209 128 SER D O   
12119 C CB  . SER D 128 ? 0.1751 0.1741 0.1565 0.0134  -0.0319 -0.0127 128 SER D CB  
12120 O OG  . SER D 128 ? 0.2375 0.2353 0.2103 0.0146  -0.0304 -0.0104 128 SER D OG  
12121 N N   . ASN D 129 ? 0.1837 0.2033 0.1658 0.0205  -0.0266 -0.0221 129 ASN D N   
12122 C CA  . ASN D 129 ? 0.2862 0.3188 0.2668 0.0196  -0.0199 -0.0223 129 ASN D CA  
12123 C C   . ASN D 129 ? 0.2570 0.2910 0.2370 0.0142  -0.0151 -0.0132 129 ASN D C   
12124 O O   . ASN D 129 ? 0.2502 0.2943 0.2364 0.0116  -0.0095 -0.0119 129 ASN D O   
12125 C CB  . ASN D 129 ? 0.1943 0.2303 0.1650 0.0220  -0.0195 -0.0258 129 ASN D CB  
12126 C CG  . ASN D 129 ? 0.2414 0.2683 0.2015 0.0207  -0.0222 -0.0200 129 ASN D CG  
12127 O OD1 . ASN D 129 ? 0.2271 0.2414 0.1878 0.0202  -0.0266 -0.0170 129 ASN D OD1 
12128 N ND2 . ASN D 129 ? 0.2270 0.2621 0.1774 0.0202  -0.0198 -0.0186 129 ASN D ND2 
12129 N N   . PHE D 130 ? 0.2303 0.2536 0.2054 0.0122  -0.0171 -0.0067 130 PHE D N   
12130 C CA  . PHE D 130 ? 0.2829 0.3035 0.2629 0.0072  -0.0137 0.0013  130 PHE D CA  
12131 C C   . PHE D 130 ? 0.2754 0.2824 0.2535 0.0065  -0.0176 0.0044  130 PHE D C   
12132 O O   . PHE D 130 ? 0.2790 0.2823 0.2484 0.0081  -0.0196 0.0071  130 PHE D O   
12133 C CB  . PHE D 130 ? 0.2430 0.2723 0.2193 0.0048  -0.0075 0.0095  130 PHE D CB  
12134 C CG  . PHE D 130 ? 0.2799 0.3125 0.2676 -0.0002 -0.0017 0.0151  130 PHE D CG  
12135 C CD1 . PHE D 130 ? 0.2476 0.2695 0.2442 -0.0037 -0.0018 0.0196  130 PHE D CD1 
12136 C CD2 . PHE D 130 ? 0.3351 0.3820 0.3264 -0.0019 0.0043  0.0148  130 PHE D CD2 
12137 C CE1 . PHE D 130 ? 0.2978 0.3221 0.3076 -0.0089 0.0037  0.0238  130 PHE D CE1 
12138 C CE2 . PHE D 130 ? 0.3607 0.4106 0.3644 -0.0072 0.0100  0.0201  130 PHE D CE2 
12139 C CZ  . PHE D 130 ? 0.2975 0.3354 0.3109 -0.0108 0.0095  0.0246  130 PHE D CZ  
12140 N N   . HIS D 131 ? 0.2465 0.2476 0.2331 0.0038  -0.0187 0.0029  131 HIS D N   
12141 C CA  . HIS D 131 ? 0.2615 0.2515 0.2485 0.0022  -0.0208 0.0050  131 HIS D CA  
12142 C C   . HIS D 131 ? 0.2561 0.2435 0.2460 -0.0002 -0.0166 0.0141  131 HIS D C   
12143 O O   . HIS D 131 ? 0.3056 0.2968 0.3044 -0.0035 -0.0115 0.0184  131 HIS D O   
12144 C CB  . HIS D 131 ? 0.2755 0.2632 0.2718 -0.0010 -0.0219 0.0000  131 HIS D CB  
12145 C CG  . HIS D 131 ? 0.2928 0.2818 0.2862 0.0012  -0.0275 -0.0067 131 HIS D CG  
12146 N ND1 . HIS D 131 ? 0.2639 0.2618 0.2628 0.0018  -0.0282 -0.0107 131 HIS D ND1 
12147 C CD2 . HIS D 131 ? 0.2886 0.2718 0.2757 0.0027  -0.0326 -0.0088 131 HIS D CD2 
12148 C CE1 . HIS D 131 ? 0.2730 0.2701 0.2690 0.0041  -0.0342 -0.0143 131 HIS D CE1 
12149 N NE2 . HIS D 131 ? 0.2912 0.2794 0.2796 0.0044  -0.0367 -0.0129 131 HIS D NE2 
12150 N N   . PHE D 132 ? 0.2306 0.2115 0.2150 0.0013  -0.0189 0.0177  132 PHE D N   
12151 C CA  A PHE D 132 ? 0.3033 0.2802 0.2938 -0.0005 -0.0161 0.0270  132 PHE D CA  
12152 C CA  B PHE D 132 ? 0.3030 0.2804 0.2940 -0.0007 -0.0157 0.0272  132 PHE D CA  
12153 C C   . PHE D 132 ? 0.2668 0.2359 0.2722 -0.0044 -0.0142 0.0247  132 PHE D C   
12154 O O   . PHE D 132 ? 0.2927 0.2598 0.2999 -0.0054 -0.0162 0.0156  132 PHE D O   
12155 C CB  A PHE D 132 ? 0.3201 0.2932 0.3027 0.0025  -0.0198 0.0303  132 PHE D CB  
12156 C CB  B PHE D 132 ? 0.3200 0.2950 0.3029 0.0022  -0.0188 0.0323  132 PHE D CB  
12157 C CG  A PHE D 132 ? 0.3162 0.2852 0.3066 0.0017  -0.0180 0.0408  132 PHE D CG  
12158 C CG  B PHE D 132 ? 0.3291 0.3045 0.3173 0.0013  -0.0159 0.0451  132 PHE D CG  
12159 C CD1 A PHE D 132 ? 0.3309 0.3069 0.3210 0.0012  -0.0150 0.0523  132 PHE D CD1 
12160 C CD1 B PHE D 132 ? 0.3364 0.3208 0.3250 -0.0004 -0.0114 0.0532  132 PHE D CD1 
12161 C CD2 A PHE D 132 ? 0.2978 0.2568 0.2970 0.0013  -0.0192 0.0396  132 PHE D CD2 
12162 C CD2 B PHE D 132 ? 0.3269 0.2945 0.3211 0.0021  -0.0177 0.0499  132 PHE D CD2 
12163 C CE1 A PHE D 132 ? 0.3480 0.3201 0.3473 0.0008  -0.0139 0.0640  132 PHE D CE1 
12164 C CE1 B PHE D 132 ? 0.3429 0.3281 0.3370 -0.0014 -0.0091 0.0674  132 PHE D CE1 
12165 C CE2 A PHE D 132 ? 0.3227 0.2776 0.3326 0.0013  -0.0177 0.0494  132 PHE D CE2 
12166 C CE2 B PHE D 132 ? 0.3586 0.3264 0.3598 0.0018  -0.0157 0.0634  132 PHE D CE2 
12167 C CZ  A PHE D 132 ? 0.3720 0.3329 0.3824 0.0012  -0.0154 0.0624  132 PHE D CZ  
12168 C CZ  B PHE D 132 ? 0.3490 0.3254 0.3499 -0.0001 -0.0116 0.0730  132 PHE D CZ  
12169 N N   . ASP D 133 ? 0.2785 0.2435 0.2953 -0.0065 -0.0104 0.0331  133 ASP D N   
12170 C CA  A ASP D 133 ? 0.2899 0.2482 0.3246 -0.0108 -0.0073 0.0298  133 ASP D CA  
12171 C CA  B ASP D 133 ? 0.2903 0.2488 0.3249 -0.0108 -0.0073 0.0296  133 ASP D CA  
12172 C C   . ASP D 133 ? 0.2923 0.2440 0.3281 -0.0108 -0.0104 0.0200  133 ASP D C   
12173 O O   . ASP D 133 ? 0.2480 0.2000 0.2900 -0.0141 -0.0101 0.0102  133 ASP D O   
12174 C CB  A ASP D 133 ? 0.3071 0.2604 0.3560 -0.0123 -0.0031 0.0417  133 ASP D CB  
12175 C CB  B ASP D 133 ? 0.3069 0.2608 0.3563 -0.0126 -0.0028 0.0414  133 ASP D CB  
12176 C CG  A ASP D 133 ? 0.3238 0.2855 0.3698 -0.0128 0.0004  0.0536  133 ASP D CG  
12177 C CG  B ASP D 133 ? 0.3244 0.2712 0.3747 -0.0095 -0.0051 0.0476  133 ASP D CG  
12178 O OD1 A ASP D 133 ? 0.3820 0.3539 0.4133 -0.0112 -0.0008 0.0515  133 ASP D OD1 
12179 O OD1 B ASP D 133 ? 0.3245 0.2747 0.3590 -0.0054 -0.0095 0.0493  133 ASP D OD1 
12180 O OD2 A ASP D 133 ? 0.3981 0.3568 0.4576 -0.0150 0.0045  0.0650  133 ASP D OD2 
12181 O OD2 B ASP D 133 ? 0.3704 0.3086 0.4390 -0.0111 -0.0026 0.0501  133 ASP D OD2 
12182 N N   . THR D 134 ? 0.2482 0.1955 0.2780 -0.0076 -0.0135 0.0222  134 THR D N   
12183 C CA  . THR D 134 ? 0.2393 0.1818 0.2699 -0.0081 -0.0156 0.0129  134 THR D CA  
12184 C C   . THR D 134 ? 0.2292 0.1766 0.2469 -0.0080 -0.0194 0.0043  134 THR D C   
12185 O O   . THR D 134 ? 0.2530 0.2004 0.2730 -0.0107 -0.0200 -0.0047 134 THR D O   
12186 C CB  . THR D 134 ? 0.2911 0.2291 0.3188 -0.0048 -0.0179 0.0170  134 THR D CB  
12187 O OG1 . THR D 134 ? 0.2399 0.1820 0.2499 -0.0012 -0.0225 0.0182  134 THR D OG1 
12188 C CG2 . THR D 134 ? 0.3137 0.2484 0.3531 -0.0036 -0.0155 0.0288  134 THR D CG2 
12189 N N   . THR D 135 ? 0.2736 0.2260 0.2785 -0.0049 -0.0221 0.0070  135 THR D N   
12190 C CA  . THR D 135 ? 0.2773 0.2338 0.2728 -0.0040 -0.0261 0.0005  135 THR D CA  
12191 C C   . THR D 135 ? 0.2595 0.2211 0.2620 -0.0075 -0.0250 -0.0054 135 THR D C   
12192 O O   . THR D 135 ? 0.2146 0.1778 0.2156 -0.0093 -0.0276 -0.0121 135 THR D O   
12193 C CB  . THR D 135 ? 0.3108 0.2719 0.2957 0.0001  -0.0281 0.0036  135 THR D CB  
12194 O OG1 . THR D 135 ? 0.2713 0.2298 0.2510 0.0026  -0.0289 0.0090  135 THR D OG1 
12195 C CG2 . THR D 135 ? 0.2522 0.2149 0.2295 0.0020  -0.0329 -0.0018 135 THR D CG2 
12196 N N   . ALA D 136 ? 0.2323 0.1980 0.2427 -0.0090 -0.0212 -0.0026 136 ALA D N   
12197 C CA  . ALA D 136 ? 0.2614 0.2331 0.2811 -0.0128 -0.0200 -0.0086 136 ALA D CA  
12198 C C   . ALA D 136 ? 0.2899 0.2584 0.3199 -0.0177 -0.0186 -0.0155 136 ALA D C   
12199 O O   . ALA D 136 ? 0.2988 0.2735 0.3309 -0.0206 -0.0205 -0.0237 136 ALA D O   
12200 C CB  . ALA D 136 ? 0.2894 0.2656 0.3179 -0.0143 -0.0149 -0.0036 136 ALA D CB  
12201 N N   . ALA D 137 ? 0.2494 0.2095 0.2871 -0.0185 -0.0153 -0.0127 137 ALA D N   
12202 C CA  . ALA D 137 ? 0.2938 0.2512 0.3438 -0.0231 -0.0131 -0.0213 137 ALA D CA  
12203 C C   . ALA D 137 ? 0.2724 0.2330 0.3119 -0.0236 -0.0173 -0.0299 137 ALA D C   
12204 O O   . ALA D 137 ? 0.2842 0.2505 0.3288 -0.0282 -0.0172 -0.0402 137 ALA D O   
12205 C CB  . ALA D 137 ? 0.2408 0.1880 0.3028 -0.0227 -0.0092 -0.0163 137 ALA D CB  
12206 N N   . HIS D 138 ? 0.2859 0.2443 0.3109 -0.0194 -0.0211 -0.0257 138 HIS D N   
12207 C CA  . HIS D 138 ? 0.2760 0.2378 0.2907 -0.0203 -0.0248 -0.0318 138 HIS D CA  
12208 C C   . HIS D 138 ? 0.2989 0.2706 0.3059 -0.0210 -0.0293 -0.0346 138 HIS D C   
12209 O O   . HIS D 138 ? 0.2586 0.2374 0.2624 -0.0244 -0.0314 -0.0416 138 HIS D O   
12210 C CB  . HIS D 138 ? 0.2460 0.2024 0.2495 -0.0161 -0.0273 -0.0261 138 HIS D CB  
12211 C CG  . HIS D 138 ? 0.2694 0.2186 0.2806 -0.0161 -0.0239 -0.0258 138 HIS D CG  
12212 N ND1 . HIS D 138 ? 0.2216 0.1716 0.2369 -0.0195 -0.0221 -0.0341 138 HIS D ND1 
12213 C CD2 . HIS D 138 ? 0.2136 0.1563 0.2307 -0.0131 -0.0221 -0.0184 138 HIS D CD2 
12214 C CE1 . HIS D 138 ? 0.2540 0.1973 0.2791 -0.0181 -0.0191 -0.0322 138 HIS D CE1 
12215 N NE2 . HIS D 138 ? 0.2174 0.1561 0.2437 -0.0141 -0.0196 -0.0218 138 HIS D NE2 
12216 N N   . VAL D 139 ? 0.2947 0.2686 0.2992 -0.0176 -0.0310 -0.0292 139 VAL D N   
12217 C CA  . VAL D 139 ? 0.3042 0.2880 0.3054 -0.0176 -0.0354 -0.0314 139 VAL D CA  
12218 C C   . VAL D 139 ? 0.2498 0.2423 0.2612 -0.0235 -0.0342 -0.0401 139 VAL D C   
12219 O O   . VAL D 139 ? 0.2528 0.2547 0.2597 -0.0259 -0.0384 -0.0452 139 VAL D O   
12220 C CB  . VAL D 139 ? 0.2683 0.2537 0.2698 -0.0133 -0.0358 -0.0259 139 VAL D CB  
12221 C CG1 . VAL D 139 ? 0.2775 0.2744 0.2816 -0.0136 -0.0395 -0.0290 139 VAL D CG1 
12222 C CG2 . VAL D 139 ? 0.2290 0.2087 0.2194 -0.0077 -0.0384 -0.0200 139 VAL D CG2 
12223 N N   . GLU D 140 ? 0.2861 0.2761 0.3119 -0.0265 -0.0284 -0.0419 140 GLU D N   
12224 C CA  . GLU D 140 ? 0.2367 0.2348 0.2753 -0.0327 -0.0267 -0.0516 140 GLU D CA  
12225 C C   . GLU D 140 ? 0.2787 0.2782 0.3192 -0.0376 -0.0257 -0.0617 140 GLU D C   
12226 O O   . GLU D 140 ? 0.3093 0.3210 0.3517 -0.0424 -0.0277 -0.0715 140 GLU D O   
12227 C CB  . GLU D 140 ? 0.2736 0.2675 0.3291 -0.0346 -0.0202 -0.0494 140 GLU D CB  
12228 C CG  . GLU D 140 ? 0.3211 0.3173 0.3745 -0.0306 -0.0204 -0.0408 140 GLU D CG  
12229 C CD  . GLU D 140 ? 0.4096 0.4016 0.4777 -0.0326 -0.0134 -0.0355 140 GLU D CD  
12230 O OE1 . GLU D 140 ? 0.4226 0.4057 0.5018 -0.0353 -0.0087 -0.0353 140 GLU D OE1 
12231 O OE2 . GLU D 140 ? 0.3740 0.3718 0.4434 -0.0314 -0.0123 -0.0311 140 GLU D OE2 
12232 N N   . LEU D 141 ? 0.2508 0.2400 0.2912 -0.0367 -0.0226 -0.0605 141 LEU D N   
12233 C CA  . LEU D 141 ? 0.2631 0.2549 0.3057 -0.0413 -0.0209 -0.0715 141 LEU D CA  
12234 C C   . LEU D 141 ? 0.2901 0.2934 0.3148 -0.0418 -0.0264 -0.0734 141 LEU D C   
12235 O O   . LEU D 141 ? 0.2970 0.3076 0.3200 -0.0445 -0.0246 -0.0793 141 LEU D O   
12236 C CB  . LEU D 141 ? 0.2930 0.2724 0.3382 -0.0389 -0.0172 -0.0683 141 LEU D CB  
12237 C CG  . LEU D 141 ? 0.3982 0.3664 0.4640 -0.0389 -0.0109 -0.0665 141 LEU D CG  
12238 C CD1 . LEU D 141 ? 0.3617 0.3192 0.4261 -0.0343 -0.0097 -0.0591 141 LEU D CD1 
12239 C CD2 . LEU D 141 ? 0.4180 0.3914 0.4966 -0.0422 -0.0056 -0.0754 141 LEU D CD2 
12240 N N   . ASN D 142 ? 0.3020 0.2646 0.3118 0.0147  -0.0505 -0.0181 142 ASN D N   
12241 C CA  . ASN D 142 ? 0.3082 0.2674 0.3158 0.0173  -0.0505 -0.0184 142 ASN D CA  
12242 C C   . ASN D 142 ? 0.3190 0.2789 0.3303 0.0183  -0.0522 -0.0201 142 ASN D C   
12243 O O   . ASN D 142 ? 0.3424 0.3030 0.3529 0.0195  -0.0518 -0.0208 142 ASN D O   
12244 C CB  . ASN D 142 ? 0.2993 0.2616 0.3075 0.0182  -0.0488 -0.0197 142 ASN D CB  
12245 C CG  . ASN D 142 ? 0.3425 0.3032 0.3461 0.0174  -0.0472 -0.0177 142 ASN D CG  
12246 O OD1 . ASN D 142 ? 0.3594 0.3175 0.3576 0.0171  -0.0464 -0.0157 142 ASN D OD1 
12247 N ND2 . ASN D 142 ? 0.2607 0.2262 0.2660 0.0158  -0.0462 -0.0183 142 ASN D ND2 
12248 N N   . GLY D 143 ? 0.2908 0.2514 0.3059 0.0172  -0.0541 -0.0208 143 GLY D N   
12249 C CA  . GLY D 143 ? 0.3086 0.2698 0.3274 0.0180  -0.0560 -0.0227 143 GLY D CA  
12250 C C   . GLY D 143 ? 0.3281 0.2975 0.3520 0.0179  -0.0547 -0.0265 143 GLY D C   
12251 O O   . GLY D 143 ? 0.3795 0.3478 0.4057 0.0201  -0.0566 -0.0284 143 GLY D O   
12252 N N   . CYS D 144 ? 0.2622 0.2401 0.2877 0.0159  -0.0519 -0.0277 144 CYS D N   
12253 C CA  . CYS D 144 ? 0.2718 0.2587 0.3019 0.0162  -0.0509 -0.0314 144 CYS D CA  
12254 C C   . CYS D 144 ? 0.2935 0.2934 0.3284 0.0121  -0.0498 -0.0319 144 CYS D C   
12255 O O   . CYS D 144 ? 0.2773 0.2799 0.3122 0.0088  -0.0497 -0.0288 144 CYS D O   
12256 C CB  . CYS D 144 ? 0.2655 0.2536 0.2940 0.0178  -0.0490 -0.0324 144 CYS D CB  
12257 S SG  . CYS D 144 ? 0.3037 0.2797 0.3275 0.0218  -0.0506 -0.0303 144 CYS D SG  
12258 N N   . LYS D 145 ? 0.2802 0.2892 0.3198 0.0126  -0.0494 -0.0354 145 LYS D N   
12259 C CA  . LYS D 145 ? 0.2633 0.2872 0.3082 0.0091  -0.0484 -0.0357 145 LYS D CA  
12260 C C   . LYS D 145 ? 0.2438 0.2763 0.2885 0.0094  -0.0458 -0.0368 145 LYS D C   
12261 O O   . LYS D 145 ? 0.2449 0.2739 0.2880 0.0128  -0.0453 -0.0399 145 LYS D O   
12262 C CB  . LYS D 145 ? 0.2937 0.3232 0.3445 0.0099  -0.0498 -0.0392 145 LYS D CB  
12263 C CG  . LYS D 145 ? 0.3074 0.3299 0.3594 0.0095  -0.0526 -0.0385 145 LYS D CG  
12264 C CD  . LYS D 145 ? 0.3854 0.4152 0.4440 0.0101  -0.0540 -0.0423 145 LYS D CD  
12265 C CE  . LYS D 145 ? 0.4826 0.5069 0.5431 0.0091  -0.0570 -0.0413 145 LYS D CE  
12266 N NZ  . LYS D 145 ? 0.4312 0.4545 0.4911 0.0045  -0.0573 -0.0365 145 LYS D NZ  
12267 N N   . ALA D 146 ? 0.2292 0.2730 0.2759 0.0058  -0.0446 -0.0341 146 ALA D N   
12268 C CA  . ALA D 146 ? 0.2500 0.3031 0.2967 0.0061  -0.0422 -0.0350 146 ALA D CA  
12269 C C   . ALA D 146 ? 0.2424 0.3099 0.2954 0.0060  -0.0415 -0.0380 146 ALA D C   
12270 O O   . ALA D 146 ? 0.3304 0.4080 0.3883 0.0025  -0.0415 -0.0352 146 ALA D O   
12271 C CB  . ALA D 146 ? 0.2304 0.2869 0.2751 0.0032  -0.0414 -0.0300 146 ALA D CB  
12272 N N   . ILE D 147 ? 0.2604 0.3294 0.3138 0.0099  -0.0409 -0.0437 147 ILE D N   
12273 C CA  . ILE D 147 ? 0.1966 0.2792 0.2557 0.0110  -0.0400 -0.0481 147 ILE D CA  
12274 C C   . ILE D 147 ? 0.1827 0.2757 0.2407 0.0122  -0.0373 -0.0503 147 ILE D C   
12275 O O   . ILE D 147 ? 0.1957 0.2827 0.2497 0.0151  -0.0370 -0.0529 147 ILE D O   
12276 C CB  . ILE D 147 ? 0.2131 0.2906 0.2739 0.0155  -0.0417 -0.0543 147 ILE D CB  
12277 C CG1 . ILE D 147 ? 0.2164 0.2838 0.2778 0.0147  -0.0445 -0.0523 147 ILE D CG1 
12278 C CG2 . ILE D 147 ? 0.2095 0.3022 0.2760 0.0170  -0.0407 -0.0595 147 ILE D CG2 
12279 C CD1 . ILE D 147 ? 0.2093 0.2697 0.2720 0.0196  -0.0467 -0.0578 147 ILE D CD1 
12280 N N   . ASN D 148 ? 0.2016 0.3105 0.2631 0.0099  -0.0352 -0.0490 148 ASN D N   
12281 C CA  . ASN D 148 ? 0.2071 0.3280 0.2668 0.0111  -0.0323 -0.0512 148 ASN D CA  
12282 C C   . ASN D 148 ? 0.2383 0.3730 0.3019 0.0139  -0.0310 -0.0579 148 ASN D C   
12283 O O   . ASN D 148 ? 0.2792 0.4230 0.3484 0.0120  -0.0307 -0.0572 148 ASN D O   
12284 C CB  . ASN D 148 ? 0.2230 0.3535 0.2827 0.0069  -0.0303 -0.0447 148 ASN D CB  
12285 C CG  . ASN D 148 ? 0.2291 0.3470 0.2856 0.0044  -0.0319 -0.0385 148 ASN D CG  
12286 O OD1 . ASN D 148 ? 0.2118 0.3179 0.2632 0.0063  -0.0328 -0.0391 148 ASN D OD1 
12287 N ND2 . ASN D 148 ? 0.2330 0.3537 0.2928 0.0001  -0.0325 -0.0324 148 ASN D ND2 
12288 N N   . ILE D 149 ? 0.2355 0.3722 0.2963 0.0183  -0.0303 -0.0646 149 ILE D N   
12289 C CA  . ILE D 149 ? 0.2210 0.3703 0.2848 0.0218  -0.0295 -0.0723 149 ILE D CA  
12290 C C   . ILE D 149 ? 0.2365 0.3986 0.2966 0.0239  -0.0268 -0.0763 149 ILE D C   
12291 O O   . ILE D 149 ? 0.2269 0.3910 0.2864 0.0290  -0.0273 -0.0846 149 ILE D O   
12292 C CB  . ILE D 149 ? 0.2164 0.3545 0.2815 0.0266  -0.0325 -0.0789 149 ILE D CB  
12293 C CG1 . ILE D 149 ? 0.2348 0.3586 0.2957 0.0293  -0.0338 -0.0802 149 ILE D CG1 
12294 C CG2 . ILE D 149 ? 0.1726 0.3011 0.2412 0.0248  -0.0350 -0.0757 149 ILE D CG2 
12295 C CD1 . ILE D 149 ? 0.2006 0.3157 0.2634 0.0349  -0.0366 -0.0872 149 ILE D CD1 
12296 N N   . VAL D 150 ? 0.2141 0.3857 0.2718 0.0204  -0.0241 -0.0706 150 VAL D N   
12297 C CA  . VAL D 150 ? 0.2424 0.4270 0.2956 0.0225  -0.0216 -0.0741 150 VAL D CA  
12298 C C   . VAL D 150 ? 0.2420 0.4448 0.2969 0.0250  -0.0201 -0.0808 150 VAL D C   
12299 O O   . VAL D 150 ? 0.2015 0.4107 0.2617 0.0235  -0.0199 -0.0802 150 VAL D O   
12300 C CB  . VAL D 150 ? 0.2254 0.4167 0.2753 0.0182  -0.0192 -0.0659 150 VAL D CB  
12301 C CG1 . VAL D 150 ? 0.2276 0.4354 0.2808 0.0142  -0.0166 -0.0609 150 VAL D CG1 
12302 C CG2 . VAL D 150 ? 0.1963 0.3950 0.2400 0.0208  -0.0176 -0.0691 150 VAL D CG2 
12303 N N   . THR D 151 ? 0.2904 0.5022 0.3411 0.0291  -0.0192 -0.0876 151 THR D N   
12304 C CA  . THR D 151 ? 0.3208 0.5502 0.3719 0.0321  -0.0182 -0.0951 151 THR D CA  
12305 C C   . THR D 151 ? 0.2835 0.5322 0.3353 0.0277  -0.0148 -0.0889 151 THR D C   
12306 O O   . THR D 151 ? 0.2164 0.4694 0.2654 0.0236  -0.0126 -0.0808 151 THR D O   
12307 C CB  . THR D 151 ? 0.2170 0.4524 0.2625 0.0374  -0.0183 -0.1038 151 THR D CB  
12308 O OG1 . THR D 151 ? 0.3086 0.5643 0.3529 0.0396  -0.0176 -0.1101 151 THR D OG1 
12309 C CG2 . THR D 151 ? 0.2636 0.5014 0.3035 0.0356  -0.0162 -0.0986 151 THR D CG2 
12310 N N   . GLU D 152 ? 0.2565 0.5171 0.3128 0.0284  -0.0144 -0.0924 152 GLU D N   
12311 C CA  . GLU D 152 ? 0.3400 0.6199 0.3986 0.0242  -0.0108 -0.0863 152 GLU D CA  
12312 C C   . GLU D 152 ? 0.2877 0.5844 0.3387 0.0241  -0.0082 -0.0851 152 GLU D C   
12313 O O   . GLU D 152 ? 0.2957 0.6053 0.3473 0.0194  -0.0048 -0.0766 152 GLU D O   
12314 C CB  . GLU D 152 ? 0.3550 0.6460 0.4198 0.0260  -0.0108 -0.0918 152 GLU D CB  
12315 C CG  . GLU D 152 ? 0.4559 0.7311 0.5270 0.0279  -0.0144 -0.0956 152 GLU D CG  
12316 C CD  . GLU D 152 ? 0.5531 0.8134 0.6289 0.0228  -0.0151 -0.0864 152 GLU D CD  
12317 O OE1 . GLU D 152 ? 0.5051 0.7737 0.5865 0.0175  -0.0127 -0.0789 152 GLU D OE1 
12318 O OE2 . GLU D 152 ? 0.4804 0.7207 0.5542 0.0240  -0.0181 -0.0866 152 GLU D OE2 
12319 N N   . LYS D 153 ? 0.2510 0.5478 0.2951 0.0292  -0.0100 -0.0931 153 LYS D N   
12320 C CA  . LYS D 153 ? 0.2841 0.5967 0.3203 0.0295  -0.0086 -0.0923 153 LYS D CA  
12321 C C   . LYS D 153 ? 0.2756 0.5859 0.3089 0.0244  -0.0063 -0.0808 153 LYS D C   
12322 O O   . LYS D 153 ? 0.2620 0.5885 0.2910 0.0224  -0.0042 -0.0756 153 LYS D O   
12323 C CB  . LYS D 153 ? 0.2471 0.5570 0.2770 0.0358  -0.0118 -0.1033 153 LYS D CB  
12324 C CG  . LYS D 153 ? 0.3132 0.6234 0.3477 0.0410  -0.0148 -0.1135 153 LYS D CG  
12325 C CD  . LYS D 153 ? 0.4130 0.7090 0.4490 0.0459  -0.0178 -0.1185 153 LYS D CD  
12326 C CE  . LYS D 153 ? 0.4443 0.7162 0.4816 0.0453  -0.0181 -0.1156 153 LYS D CE  
12327 N NZ  . LYS D 153 ? 0.3709 0.6313 0.4099 0.0492  -0.0202 -0.1188 153 LYS D NZ  
12328 N N   . ALA D 154 ? 0.3087 0.5991 0.3444 0.0223  -0.0071 -0.0763 154 ALA D N   
12329 C CA  . ALA D 154 ? 0.3070 0.5940 0.3402 0.0178  -0.0057 -0.0658 154 ALA D CA  
12330 C C   . ALA D 154 ? 0.3320 0.6306 0.3687 0.0117  -0.0026 -0.0553 154 ALA D C   
12331 O O   . ALA D 154 ? 0.2663 0.5684 0.2995 0.0081  -0.0010 -0.0464 154 ALA D O   
12332 C CB  . ALA D 154 ? 0.2641 0.5271 0.3003 0.0169  -0.0080 -0.0635 154 ALA D CB  
12333 N N   . PHE D 155 ? 0.2798 0.5840 0.3236 0.0104  -0.0017 -0.0559 155 PHE D N   
12334 C CA  . PHE D 155 ? 0.3399 0.6533 0.3890 0.0041  0.0015  -0.0460 155 PHE D CA  
12335 C C   . PHE D 155 ? 0.3714 0.7081 0.4169 0.0032  0.0050  -0.0433 155 PHE D C   
12336 O O   . PHE D 155 ? 0.3151 0.6600 0.3634 -0.0026 0.0083  -0.0334 155 PHE D O   
12337 C CB  . PHE D 155 ? 0.3152 0.6243 0.3745 0.0030  0.0008  -0.0480 155 PHE D CB  
12338 C CG  . PHE D 155 ? 0.3380 0.6241 0.4010 0.0038  -0.0032 -0.0499 155 PHE D CG  
12339 C CD1 . PHE D 155 ? 0.4305 0.7022 0.4915 0.0013  -0.0046 -0.0437 155 PHE D CD1 
12340 C CD2 . PHE D 155 ? 0.3960 0.6752 0.4642 0.0072  -0.0058 -0.0577 155 PHE D CD2 
12341 C CE1 . PHE D 155 ? 0.4325 0.6832 0.4964 0.0021  -0.0086 -0.0451 155 PHE D CE1 
12342 C CE2 . PHE D 155 ? 0.4164 0.6745 0.4873 0.0080  -0.0098 -0.0587 155 PHE D CE2 
12343 C CZ  . PHE D 155 ? 0.3309 0.5748 0.3994 0.0053  -0.0111 -0.0524 155 PHE D CZ  
12344 N N   . ASP D 156 ? 0.3129 0.6601 0.3526 0.0086  0.0042  -0.0518 156 ASP D N   
12345 C CA  . ASP D 156 ? 0.2960 0.6656 0.3317 0.0087  0.0067  -0.0499 156 ASP D CA  
12346 C C   . ASP D 156 ? 0.3079 0.6786 0.3345 0.0094  0.0057  -0.0465 156 ASP D C   
12347 O O   . ASP D 156 ? 0.3208 0.6926 0.3418 0.0148  0.0025  -0.0549 156 ASP D O   
12348 C CB  . ASP D 156 ? 0.3216 0.7025 0.3573 0.0146  0.0053  -0.0617 156 ASP D CB  
12349 C CG  . ASP D 156 ? 0.4717 0.8769 0.5055 0.0144  0.0082  -0.0593 156 ASP D CG  
12350 O OD1 . ASP D 156 ? 0.4757 0.8885 0.5061 0.0105  0.0109  -0.0492 156 ASP D OD1 
12351 O OD2 . ASP D 156 ? 0.5248 0.9413 0.5607 0.0183  0.0078  -0.0677 156 ASP D OD2 
12352 N N   . SER D 157 ? 0.3568 0.7269 0.3826 0.0038  0.0080  -0.0341 157 SER D N   
12353 C CA  . SER D 157 ? 0.3923 0.7598 0.4107 0.0043  0.0065  -0.0300 157 SER D CA  
12354 C C   . SER D 157 ? 0.3979 0.7826 0.4102 0.0087  0.0052  -0.0341 157 SER D C   
12355 O O   . SER D 157 ? 0.4204 0.8019 0.4283 0.0132  0.0013  -0.0406 157 SER D O   
12356 C CB  . SER D 157 ? 0.4150 0.7811 0.4341 -0.0025 0.0092  -0.0154 157 SER D CB  
12357 O OG  . SER D 157 ? 0.5013 0.8512 0.5269 -0.0065 0.0093  -0.0118 157 SER D OG  
12358 N N   . GLU D 158 ? 0.3406 0.7437 0.3537 0.0073  0.0084  -0.0304 158 GLU D N   
12359 C CA  . GLU D 158 ? 0.3613 0.7811 0.3698 0.0110  0.0075  -0.0318 158 GLU D CA  
12360 C C   . GLU D 158 ? 0.3440 0.7718 0.3526 0.0180  0.0040  -0.0460 158 GLU D C   
12361 O O   . GLU D 158 ? 0.3388 0.7800 0.3451 0.0219  0.0025  -0.0488 158 GLU D O   
12362 C CB  . GLU D 158 ? 0.4851 0.9211 0.4937 0.0068  0.0127  -0.0216 158 GLU D CB  
12363 C CG  . GLU D 158 ? 0.5333 0.9613 0.5420 -0.0005 0.0157  -0.0070 158 GLU D CG  
12364 C CD  . GLU D 158 ? 0.6493 1.0923 0.6560 -0.0041 0.0201  0.0036  158 GLU D CD  
12365 O OE1 . GLU D 158 ? 0.6380 1.0959 0.6406 -0.0001 0.0201  0.0010  158 GLU D OE1 
12366 O OE2 . GLU D 158 ? 0.6443 1.0839 0.6537 -0.0110 0.0235  0.0146  158 GLU D OE2 
12367 N N   . THR D 159 ? 0.3668 0.7864 0.3788 0.0199  0.0026  -0.0550 159 THR D N   
12368 C CA  . THR D 159 ? 0.3607 0.7865 0.3731 0.0267  -0.0014 -0.0686 159 THR D CA  
12369 C C   . THR D 159 ? 0.2982 0.7060 0.3096 0.0307  -0.0060 -0.0759 159 THR D C   
12370 O O   . THR D 159 ? 0.3507 0.7372 0.3629 0.0294  -0.0062 -0.0765 159 THR D O   
12371 C CB  . THR D 159 ? 0.3222 0.7471 0.3401 0.0271  -0.0001 -0.0744 159 THR D CB  
12372 O OG1 . THR D 159 ? 0.2709 0.7114 0.2919 0.0233  0.0054  -0.0670 159 THR D OG1 
12373 C CG2 . THR D 159 ? 0.2851 0.7157 0.3035 0.0344  -0.0048 -0.0887 159 THR D CG2 
12374 N N   . TYR D 160 ? 0.2365 0.6486 0.2484 0.0354  -0.0078 -0.0802 160 TYR D N   
12375 C CA  . TYR D 160 ? 0.2900 0.6814 0.3038 0.0388  -0.0103 -0.0854 160 TYR D CA  
12376 C C   . TYR D 160 ? 0.3261 0.7007 0.3432 0.0414  -0.0124 -0.0946 160 TYR D C   
12377 O O   . TYR D 160 ? 0.3319 0.7158 0.3512 0.0435  -0.0131 -0.1008 160 TYR D O   
12378 C CB  . TYR D 160 ? 0.2896 0.6926 0.3051 0.0441  -0.0120 -0.0897 160 TYR D CB  
12379 C CG  . TYR D 160 ? 0.2807 0.6654 0.3004 0.0476  -0.0145 -0.0950 160 TYR D CG  
12380 C CD1 . TYR D 160 ? 0.2868 0.6625 0.3118 0.0521  -0.0176 -0.1050 160 TYR D CD1 
12381 C CD2 . TYR D 160 ? 0.2804 0.6579 0.3000 0.0468  -0.0133 -0.0897 160 TYR D CD2 
12382 C CE1 . TYR D 160 ? 0.2611 0.6217 0.2919 0.0555  -0.0188 -0.1090 160 TYR D CE1 
12383 C CE2 . TYR D 160 ? 0.2864 0.6490 0.3104 0.0502  -0.0141 -0.0946 160 TYR D CE2 
12384 C CZ  . TYR D 160 ? 0.2706 0.6248 0.2999 0.0545  -0.0165 -0.1041 160 TYR D CZ  
12385 O OH  . TYR D 160 ? 0.3163 0.6557 0.3480 0.0577  -0.0174 -0.1089 160 TYR D OH  
12386 N N   . ASP D 161 ? 0.2688 0.6191 0.2861 0.0413  -0.0134 -0.0952 161 ASP D N   
12387 C CA  . ASP D 161 ? 0.2474 0.5799 0.2679 0.0447  -0.0157 -0.1039 161 ASP D CA  
12388 C C   . ASP D 161 ? 0.2558 0.5676 0.2749 0.0462  -0.0144 -0.1043 161 ASP D C   
12389 O O   . ASP D 161 ? 0.2185 0.5269 0.2370 0.0438  -0.0107 -0.0970 161 ASP D O   
12390 C CB  . ASP D 161 ? 0.3061 0.6295 0.3283 0.0426  -0.0142 -0.1041 161 ASP D CB  
12391 C CG  . ASP D 161 ? 0.3692 0.6776 0.3964 0.0469  -0.0170 -0.1130 161 ASP D CG  
12392 O OD1 . ASP D 161 ? 0.3306 0.6490 0.3606 0.0502  -0.0194 -0.1200 161 ASP D OD1 
12393 O OD2 . ASP D 161 ? 0.3387 0.6266 0.3682 0.0472  -0.0168 -0.1128 161 ASP D OD2 
12394 N N   . ASP D 162 ? 0.2532 0.5591 0.2837 0.0526  -0.0142 -0.1118 162 ASP D N   
12395 C CA  . ASP D 162 ? 0.2699 0.5635 0.3053 0.0542  -0.0166 -0.1122 162 ASP D CA  
12396 C C   . ASP D 162 ? 0.2438 0.5166 0.2771 0.0506  -0.0164 -0.1083 162 ASP D C   
12397 O O   . ASP D 162 ? 0.2094 0.4737 0.2421 0.0497  -0.0167 -0.1054 162 ASP D O   
12398 C CB  . ASP D 162 ? 0.2796 0.5697 0.3220 0.0600  -0.0212 -0.1214 162 ASP D CB  
12399 C CG  . ASP D 162 ? 0.3123 0.6198 0.3566 0.0640  -0.0233 -0.1255 162 ASP D CG  
12400 O OD1 . ASP D 162 ? 0.3323 0.6514 0.3725 0.0625  -0.0215 -0.1210 162 ASP D OD1 
12401 O OD2 . ASP D 162 ? 0.3169 0.6260 0.3661 0.0690  -0.0272 -0.1336 162 ASP D OD2 
12402 N N   . TRP D 163 ? 0.2161 0.4817 0.2489 0.0488  -0.0164 -0.1083 163 TRP D N   
12403 C CA  . TRP D 163 ? 0.2619 0.5080 0.2965 0.0469  -0.0174 -0.1062 163 TRP D CA  
12404 C C   . TRP D 163 ? 0.2276 0.4740 0.2594 0.0425  -0.0156 -0.1015 163 TRP D C   
12405 O O   . TRP D 163 ? 0.2464 0.4845 0.2814 0.0429  -0.0170 -0.1040 163 TRP D O   
12406 C CB  . TRP D 163 ? 0.2052 0.4385 0.2463 0.0510  -0.0212 -0.1130 163 TRP D CB  
12407 C CG  . TRP D 163 ? 0.2007 0.4369 0.2459 0.0558  -0.0239 -0.1188 163 TRP D CG  
12408 C CD1 . TRP D 163 ? 0.2206 0.4659 0.2698 0.0603  -0.0259 -0.1256 163 TRP D CD1 
12409 C CD2 . TRP D 163 ? 0.2554 0.4865 0.3017 0.0569  -0.0254 -0.1188 163 TRP D CD2 
12410 N NE1 . TRP D 163 ? 0.2539 0.5001 0.3067 0.0641  -0.0289 -0.1299 163 TRP D NE1 
12411 C CE2 . TRP D 163 ? 0.2602 0.4975 0.3110 0.0619  -0.0286 -0.1260 163 TRP D CE2 
12412 C CE3 . TRP D 163 ? 0.2615 0.4838 0.3053 0.0541  -0.0247 -0.1138 163 TRP D CE3 
12413 C CZ2 . TRP D 163 ? 0.2241 0.4589 0.2766 0.0642  -0.0310 -0.1286 163 TRP D CZ2 
12414 C CZ3 . TRP D 163 ? 0.2159 0.4360 0.2615 0.0563  -0.0268 -0.1163 163 TRP D CZ3 
12415 C CH2 . TRP D 163 ? 0.2759 0.5021 0.3258 0.0612  -0.0299 -0.1237 163 TRP D CH2 
12416 N N   . LYS D 164 ? 0.2019 0.4581 0.2285 0.0384  -0.0128 -0.0941 164 LYS D N   
12417 C CA  . LYS D 164 ? 0.2077 0.4667 0.2328 0.0341  -0.0112 -0.0894 164 LYS D CA  
12418 C C   . LYS D 164 ? 0.2201 0.4595 0.2479 0.0318  -0.0122 -0.0854 164 LYS D C   
12419 O O   . LYS D 164 ? 0.1939 0.4305 0.2239 0.0272  -0.0122 -0.0783 164 LYS D O   
12420 C CB  . LYS D 164 ? 0.2169 0.4924 0.2365 0.0298  -0.0085 -0.0810 164 LYS D CB  
12421 C CG  . LYS D 164 ? 0.2610 0.5577 0.2791 0.0303  -0.0081 -0.0825 164 LYS D CG  
12422 C CD  . LYS D 164 ? 0.2953 0.6077 0.3086 0.0260  -0.0060 -0.0726 164 LYS D CD  
12423 C CE  . LYS D 164 ? 0.2611 0.5971 0.2738 0.0260  -0.0058 -0.0732 164 LYS D CE  
12424 N NZ  . LYS D 164 ? 0.2427 0.5945 0.2519 0.0213  -0.0039 -0.0620 164 LYS D NZ  
12425 N N   . GLY D 165 ? 0.1966 0.4200 0.2264 0.0340  -0.0142 -0.0874 165 GLY D N   
12426 C CA  . GLY D 165 ? 0.1859 0.3879 0.2186 0.0313  -0.0167 -0.0822 165 GLY D CA  
12427 C C   . GLY D 165 ? 0.2011 0.3902 0.2389 0.0343  -0.0196 -0.0880 165 GLY D C   
12428 O O   . GLY D 165 ? 0.2221 0.3939 0.2618 0.0323  -0.0218 -0.0839 165 GLY D O   
12429 N N   . ASP D 166 ? 0.1725 0.3702 0.2123 0.0394  -0.0197 -0.0976 166 ASP D N   
12430 C CA  . ASP D 166 ? 0.2113 0.3980 0.2565 0.0432  -0.0228 -0.1035 166 ASP D CA  
12431 C C   . ASP D 166 ? 0.2240 0.4015 0.2713 0.0399  -0.0240 -0.0993 166 ASP D C   
12432 O O   . ASP D 166 ? 0.2188 0.4039 0.2652 0.0357  -0.0224 -0.0939 166 ASP D O   
12433 C CB  . ASP D 166 ? 0.2407 0.4374 0.2881 0.0468  -0.0241 -0.1103 166 ASP D CB  
12434 C CG  . ASP D 166 ? 0.2109 0.4079 0.2597 0.0501  -0.0257 -0.1134 166 ASP D CG  
12435 O OD1 . ASP D 166 ? 0.2414 0.4309 0.2897 0.0495  -0.0259 -0.1106 166 ASP D OD1 
12436 O OD2 . ASP D 166 ? 0.3385 0.5441 0.3893 0.0536  -0.0269 -0.1192 166 ASP D OD2 
12437 N N   . PHE D 167 ? 0.2228 0.3843 0.2740 0.0422  -0.0272 -0.1012 167 PHE D N   
12438 C CA  . PHE D 167 ? 0.2350 0.3893 0.2892 0.0411  -0.0289 -0.1000 167 PHE D CA  
12439 C C   . PHE D 167 ? 0.2420 0.4102 0.2984 0.0442  -0.0287 -0.1077 167 PHE D C   
12440 O O   . PHE D 167 ? 0.2161 0.3914 0.2732 0.0484  -0.0292 -0.1147 167 PHE D O   
12441 C CB  . PHE D 167 ? 0.1590 0.2945 0.2164 0.0438  -0.0326 -0.1010 167 PHE D CB  
12442 C CG  . PHE D 167 ? 0.1956 0.3156 0.2505 0.0399  -0.0334 -0.0925 167 PHE D CG  
12443 C CD1 . PHE D 167 ? 0.1811 0.2988 0.2334 0.0391  -0.0329 -0.0902 167 PHE D CD1 
12444 C CD2 . PHE D 167 ? 0.1795 0.2873 0.2348 0.0375  -0.0350 -0.0874 167 PHE D CD2 
12445 C CE1 . PHE D 167 ? 0.2046 0.3087 0.2543 0.0356  -0.0338 -0.0829 167 PHE D CE1 
12446 C CE2 . PHE D 167 ? 0.1531 0.2474 0.2055 0.0343  -0.0358 -0.0803 167 PHE D CE2 
12447 C CZ  . PHE D 167 ? 0.1716 0.2643 0.2212 0.0333  -0.0351 -0.0782 167 PHE D CZ  
12448 N N   . ASP D 168 ? 0.1989 0.3698 0.2576 0.0410  -0.0286 -0.1043 168 ASP D N   
12449 C CA  . ASP D 168 ? 0.2806 0.4610 0.3426 0.0437  -0.0294 -0.1113 168 ASP D CA  
12450 C C   . ASP D 168 ? 0.2219 0.3868 0.2874 0.0485  -0.0333 -0.1166 168 ASP D C   
12451 O O   . ASP D 168 ? 0.1972 0.3495 0.2650 0.0466  -0.0352 -0.1120 168 ASP D O   
12452 C CB  . ASP D 168 ? 0.2974 0.4856 0.3628 0.0385  -0.0281 -0.1047 168 ASP D CB  
12453 C CG  . ASP D 168 ? 0.3150 0.5169 0.3847 0.0407  -0.0283 -0.1110 168 ASP D CG  
12454 O OD1 . ASP D 168 ? 0.2862 0.4851 0.3567 0.0465  -0.0311 -0.1204 168 ASP D OD1 
12455 O OD2 . ASP D 168 ? 0.3245 0.5403 0.3972 0.0367  -0.0259 -0.1063 168 ASP D OD2 
12456 N N   . ILE D 169 ? 0.2156 0.3795 0.2823 0.0531  -0.0355 -0.1223 169 ILE D N   
12457 C CA  . ILE D 169 ? 0.2567 0.4038 0.3271 0.0561  -0.0401 -0.1228 169 ILE D CA  
12458 C C   . ILE D 169 ? 0.3245 0.4707 0.3983 0.0571  -0.0420 -0.1256 169 ILE D C   
12459 O O   . ILE D 169 ? 0.3051 0.4358 0.3809 0.0575  -0.0449 -0.1228 169 ILE D O   
12460 C CB  . ILE D 169 ? 0.2701 0.4183 0.3421 0.0602  -0.0425 -0.1272 169 ILE D CB  
12461 C CG1 . ILE D 169 ? 0.2345 0.3807 0.3044 0.0594  -0.0414 -0.1242 169 ILE D CG1 
12462 C CG2 . ILE D 169 ? 0.2972 0.4314 0.3734 0.0634  -0.0474 -0.1280 169 ILE D CG2 
12463 C CD1 . ILE D 169 ? 0.2176 0.3457 0.2879 0.0581  -0.0433 -0.1180 169 ILE D CD1 
12464 N N   . LYS D 170 ? 0.2766 0.4403 0.3512 0.0574  -0.0405 -0.1308 170 LYS D N   
12465 C CA  . LYS D 170 ? 0.3131 0.4781 0.3918 0.0584  -0.0423 -0.1342 170 LYS D CA  
12466 C C   . LYS D 170 ? 0.2745 0.4294 0.3544 0.0542  -0.0420 -0.1265 170 LYS D C   
12467 O O   . LYS D 170 ? 0.2821 0.4252 0.3648 0.0557  -0.0452 -0.1268 170 LYS D O   
12468 C CB  . LYS D 170 ? 0.2521 0.4409 0.3316 0.0585  -0.0401 -0.1402 170 LYS D CB  
12469 C CG  . LYS D 170 ? 0.3524 0.5456 0.4382 0.0585  -0.0417 -0.1415 170 LYS D CG  
12470 C CD  . LYS D 170 ? 0.3363 0.5545 0.4243 0.0578  -0.0392 -0.1442 170 LYS D CD  
12471 C CE  . LYS D 170 ? 0.3631 0.5877 0.4583 0.0597  -0.0412 -0.1483 170 LYS D CE  
12472 N NZ  . LYS D 170 ? 0.3907 0.6131 0.4923 0.0544  -0.0401 -0.1391 170 LYS D NZ  
12473 N N   . LYS D 171 ? 0.2783 0.4365 0.3560 0.0480  -0.0387 -0.1173 171 LYS D N   
12474 C CA  . LYS D 171 ? 0.2788 0.4270 0.3577 0.0429  -0.0391 -0.1077 171 LYS D CA  
12475 C C   . LYS D 171 ? 0.2779 0.4046 0.3540 0.0440  -0.0416 -0.1050 171 LYS D C   
12476 O O   . LYS D 171 ? 0.2395 0.3551 0.3165 0.0421  -0.0435 -0.1002 171 LYS D O   
12477 C CB  . LYS D 171 ? 0.3035 0.4608 0.3811 0.0364  -0.0355 -0.0990 171 LYS D CB  
12478 C CG  . LYS D 171 ? 0.2833 0.4621 0.3650 0.0341  -0.0327 -0.0989 171 LYS D CG  
12479 C CD  . LYS D 171 ? 0.2589 0.4448 0.3398 0.0278  -0.0295 -0.0894 171 LYS D CD  
12480 C CE  . LYS D 171 ? 0.3649 0.5728 0.4506 0.0252  -0.0262 -0.0882 171 LYS D CE  
12481 N NZ  . LYS D 171 ? 0.4616 0.6755 0.5472 0.0190  -0.0233 -0.0784 171 LYS D NZ  
12482 N N   . LEU D 172 ? 0.2549 0.3763 0.3281 0.0471  -0.0416 -0.1075 172 LEU D N   
12483 C CA  . LEU D 172 ? 0.2631 0.3656 0.3352 0.0486  -0.0441 -0.1046 172 LEU D CA  
12484 C C   . LEU D 172 ? 0.3410 0.4336 0.4165 0.0526  -0.0483 -0.1075 172 LEU D C   
12485 O O   . LEU D 172 ? 0.2797 0.3590 0.3547 0.0517  -0.0503 -0.1027 172 LEU D O   
12486 C CB  . LEU D 172 ? 0.2059 0.3066 0.2763 0.0508  -0.0438 -0.1057 172 LEU D CB  
12487 C CG  . LEU D 172 ? 0.2937 0.3765 0.3632 0.0506  -0.0467 -0.0998 172 LEU D CG  
12488 C CD1 . LEU D 172 ? 0.2085 0.2829 0.2746 0.0465  -0.0456 -0.0926 172 LEU D CD1 
12489 C CD2 . LEU D 172 ? 0.2397 0.3221 0.3087 0.0517  -0.0473 -0.1001 172 LEU D CD2 
12490 N N   . LYS D 173 ? 0.2468 0.3461 0.3248 0.0558  -0.0499 -0.1136 173 LYS D N   
12491 C CA  . LYS D 173 ? 0.3042 0.3951 0.3848 0.0585  -0.0542 -0.1148 173 LYS D CA  
12492 C C   . LYS D 173 ? 0.3147 0.4059 0.3976 0.0578  -0.0548 -0.1155 173 LYS D C   
12493 O O   . LYS D 173 ? 0.3324 0.4109 0.4154 0.0581  -0.0579 -0.1121 173 LYS D O   
12494 C CB  . LYS D 173 ? 0.3095 0.4089 0.3924 0.0624  -0.0559 -0.1221 173 LYS D CB  
12495 C CG  . LYS D 173 ? 0.2383 0.3351 0.3204 0.0641  -0.0568 -0.1217 173 LYS D CG  
12496 C CD  . LYS D 173 ? 0.3359 0.4434 0.4205 0.0682  -0.0583 -0.1298 173 LYS D CD  
12497 C CE  . LYS D 173 ? 0.4652 0.5697 0.5508 0.0706  -0.0601 -0.1297 173 LYS D CE  
12498 N NZ  . LYS D 173 ? 0.4732 0.5878 0.5618 0.0753  -0.0621 -0.1378 173 LYS D NZ  
12499 N N   . GLU D 174 ? 0.2857 0.3926 0.3707 0.0566  -0.0518 -0.1197 174 GLU D N   
12500 C CA  . GLU D 174 ? 0.2400 0.3486 0.3281 0.0533  -0.0526 -0.1160 174 GLU D CA  
12501 C C   . GLU D 174 ? 0.3214 0.4151 0.4068 0.0495  -0.0532 -0.1068 174 GLU D C   
12502 O O   . GLU D 174 ? 0.3005 0.3850 0.3874 0.0503  -0.0562 -0.1059 174 GLU D O   
12503 C CB  . GLU D 174 ? 0.2937 0.4225 0.3847 0.0486  -0.0490 -0.1140 174 GLU D CB  
12504 C CG  . GLU D 174 ? 0.3350 0.4808 0.4292 0.0523  -0.0486 -0.1232 174 GLU D CG  
12505 C CD  . GLU D 174 ? 0.4362 0.6033 0.5323 0.0478  -0.0441 -0.1203 174 GLU D CD  
12506 O OE1 . GLU D 174 ? 0.3934 0.5618 0.4890 0.0418  -0.0415 -0.1110 174 GLU D OE1 
12507 O OE2 . GLU D 174 ? 0.4859 0.6689 0.5840 0.0506  -0.0433 -0.1273 174 GLU D OE2 
12508 N N   . ASN D 175 ? 0.2405 0.3319 0.3216 0.0455  -0.0506 -0.1002 175 ASN D N   
12509 C CA  . ASN D 175 ? 0.3076 0.3860 0.3854 0.0418  -0.0511 -0.0918 175 ASN D CA  
12510 C C   . ASN D 175 ? 0.2695 0.3301 0.3454 0.0461  -0.0545 -0.0920 175 ASN D C   
12511 O O   . ASN D 175 ? 0.2609 0.3108 0.3354 0.0451  -0.0563 -0.0875 175 ASN D O   
12512 C CB  . ASN D 175 ? 0.2307 0.3113 0.3041 0.0370  -0.0479 -0.0854 175 ASN D CB  
12513 C CG  . ASN D 175 ? 0.2586 0.3511 0.3340 0.0311  -0.0457 -0.0804 175 ASN D CG  
12514 O OD1 . ASN D 175 ? 0.3296 0.4169 0.4051 0.0275  -0.0467 -0.0747 175 ASN D OD1 
12515 N ND2 . ASN D 175 ? 0.2705 0.3797 0.3479 0.0303  -0.0430 -0.0824 175 ASN D ND2 
12516 N N   . ILE D 176 ? 0.2628 0.3206 0.3386 0.0506  -0.0554 -0.0958 176 ILE D N   
12517 C CA  . ILE D 176 ? 0.2610 0.3044 0.3339 0.0512  -0.0587 -0.0906 176 ILE D CA  
12518 C C   . ILE D 176 ? 0.3040 0.3438 0.3790 0.0532  -0.0622 -0.0924 176 ILE D C   
12519 O O   . ILE D 176 ? 0.2669 0.2953 0.3390 0.0525  -0.0646 -0.0871 176 ILE D O   
12520 C CB  . ILE D 176 ? 0.2811 0.3245 0.3533 0.0528  -0.0594 -0.0915 176 ILE D CB  
12521 C CG1 . ILE D 176 ? 0.2648 0.3100 0.3345 0.0506  -0.0563 -0.0889 176 ILE D CG1 
12522 C CG2 . ILE D 176 ? 0.2906 0.3217 0.3610 0.0538  -0.0635 -0.0873 176 ILE D CG2 
12523 C CD1 . ILE D 176 ? 0.3155 0.3604 0.3852 0.0521  -0.0573 -0.0897 176 ILE D CD1 
12524 N N   . ALA D 177 ? 0.2899 0.3405 0.3698 0.0556  -0.0626 -0.1000 177 ALA D N   
12525 C CA  . ALA D 177 ? 0.3054 0.3539 0.3880 0.0578  -0.0661 -0.1028 177 ALA D CA  
12526 C C   . ALA D 177 ? 0.3114 0.3575 0.3952 0.0559  -0.0662 -0.1007 177 ALA D C   
12527 O O   . ALA D 177 ? 0.2926 0.3287 0.3749 0.0562  -0.0693 -0.0976 177 ALA D O   
12528 C CB  . ALA D 177 ? 0.2776 0.3401 0.3654 0.0609  -0.0664 -0.1123 177 ALA D CB  
12529 N N   . GLN D 178 ? 0.2656 0.3213 0.3512 0.0528  -0.0629 -0.1010 178 GLN D N   
12530 C CA  . GLN D 178 ? 0.3076 0.3637 0.3941 0.0480  -0.0631 -0.0956 178 GLN D CA  
12531 C C   . GLN D 178 ? 0.3268 0.3665 0.4079 0.0470  -0.0643 -0.0887 178 GLN D C   
12532 O O   . GLN D 178 ? 0.2599 0.2917 0.3413 0.0479  -0.0673 -0.0876 178 GLN D O   
12533 C CB  . GLN D 178 ? 0.3342 0.4058 0.4224 0.0416  -0.0591 -0.0918 178 GLN D CB  
12534 C CG  . GLN D 178 ? 0.3837 0.4543 0.4727 0.0360  -0.0593 -0.0848 178 GLN D CG  
12535 C CD  . GLN D 178 ? 0.5737 0.6614 0.6669 0.0301  -0.0562 -0.0813 178 GLN D CD  
12536 O OE1 . GLN D 178 ? 0.5630 0.6495 0.6540 0.0249  -0.0548 -0.0744 178 GLN D OE1 
12537 N NE2 . GLN D 178 ? 0.6812 0.7851 0.7807 0.0311  -0.0551 -0.0861 178 GLN D NE2 
12538 N N   . HIS D 179 ? 0.2908 0.3257 0.3669 0.0454  -0.0621 -0.0842 179 HIS D N   
12539 C CA  . HIS D 179 ? 0.2832 0.3045 0.3541 0.0442  -0.0630 -0.0774 179 HIS D CA  
12540 C C   . HIS D 179 ? 0.3442 0.3546 0.4105 0.0462  -0.0654 -0.0742 179 HIS D C   
12541 O O   . HIS D 179 ? 0.3115 0.3123 0.3730 0.0449  -0.0668 -0.0685 179 HIS D O   
12542 C CB  . HIS D 179 ? 0.2619 0.2848 0.3283 0.0395  -0.0593 -0.0720 179 HIS D CB  
12543 C CG  . HIS D 179 ? 0.2947 0.3291 0.3624 0.0335  -0.0567 -0.0694 179 HIS D CG  
12544 N ND1 . HIS D 179 ? 0.2229 0.2543 0.2896 0.0296  -0.0572 -0.0645 179 HIS D ND1 
12545 C CD2 . HIS D 179 ? 0.3009 0.3503 0.3714 0.0309  -0.0539 -0.0707 179 HIS D CD2 
12546 C CE1 . HIS D 179 ? 0.2975 0.3414 0.3671 0.0246  -0.0551 -0.0625 179 HIS D CE1 
12547 N NE2 . HIS D 179 ? 0.3183 0.3736 0.3901 0.0253  -0.0530 -0.0658 179 HIS D NE2 
12548 N N   . GLY D 180 ? 0.2572 0.2701 0.3240 0.0483  -0.0658 -0.0769 180 GLY D N   
12549 C CA  . GLY D 180 ? 0.2348 0.2390 0.2974 0.0490  -0.0681 -0.0730 180 GLY D CA  
12550 C C   . GLY D 180 ? 0.2590 0.2600 0.3173 0.0470  -0.0665 -0.0683 180 GLY D C   
12551 O O   . GLY D 180 ? 0.2664 0.2662 0.3222 0.0443  -0.0640 -0.0647 180 GLY D O   
12552 N N   . ALA D 181 ? 0.3091 0.3087 0.3672 0.0485  -0.0683 -0.0685 181 ALA D N   
12553 C CA  . ALA D 181 ? 0.3056 0.3024 0.3604 0.0467  -0.0674 -0.0648 181 ALA D CA  
12554 C C   . ALA D 181 ? 0.3522 0.3406 0.4006 0.0436  -0.0672 -0.0577 181 ALA D C   
12555 O O   . ALA D 181 ? 0.3235 0.3109 0.3693 0.0414  -0.0651 -0.0548 181 ALA D O   
12556 C CB  . ALA D 181 ? 0.2723 0.2678 0.3283 0.0489  -0.0710 -0.0665 181 ALA D CB  
12557 N N   . ASP D 182 ? 0.2977 0.2806 0.3433 0.0435  -0.0694 -0.0552 182 ASP D N   
12558 C CA  . ASP D 182 ? 0.3437 0.3194 0.3824 0.0408  -0.0695 -0.0491 182 ASP D CA  
12559 C C   . ASP D 182 ? 0.3354 0.3118 0.3726 0.0384  -0.0659 -0.0467 182 ASP D C   
12560 O O   . ASP D 182 ? 0.3344 0.3061 0.3659 0.0360  -0.0651 -0.0420 182 ASP D O   
12561 C CB  . ASP D 182 ? 0.3796 0.3501 0.4155 0.0416  -0.0731 -0.0478 182 ASP D CB  
12562 C CG  . ASP D 182 ? 0.5187 0.4858 0.5536 0.0432  -0.0776 -0.0487 182 ASP D CG  
12563 O OD1 . ASP D 182 ? 0.5484 0.5164 0.5846 0.0434  -0.0780 -0.0497 182 ASP D OD1 
12564 O OD2 . ASP D 182 ? 0.5803 0.5434 0.6130 0.0442  -0.0813 -0.0485 182 ASP D OD2 
12565 N N   . ASN D 183 ? 0.2697 0.2519 0.3117 0.0390  -0.0641 -0.0504 183 ASN D N   
12566 C CA  . ASN D 183 ? 0.2536 0.2364 0.2948 0.0368  -0.0616 -0.0486 183 ASN D CA  
12567 C C   . ASN D 183 ? 0.2753 0.2629 0.3178 0.0358  -0.0588 -0.0495 183 ASN D C   
12568 O O   . ASN D 183 ? 0.2374 0.2250 0.2788 0.0340  -0.0571 -0.0477 183 ASN D O   
12569 C CB  . ASN D 183 ? 0.2596 0.2460 0.3057 0.0376  -0.0623 -0.0523 183 ASN D CB  
12570 C CG  . ASN D 183 ? 0.3152 0.2957 0.3588 0.0378  -0.0648 -0.0501 183 ASN D CG  
12571 O OD1 . ASN D 183 ? 0.2745 0.2486 0.3118 0.0360  -0.0648 -0.0449 183 ASN D OD1 
12572 N ND2 . ASN D 183 ? 0.3240 0.3071 0.3725 0.0401  -0.0671 -0.0547 183 ASN D ND2 
12573 N N   . ILE D 184 ? 0.2476 0.2393 0.2925 0.0372  -0.0585 -0.0525 184 ILE D N   
12574 C CA  . ILE D 184 ? 0.2279 0.2256 0.2745 0.0368  -0.0559 -0.0543 184 ILE D CA  
12575 C C   . ILE D 184 ? 0.2134 0.2054 0.2551 0.0349  -0.0554 -0.0494 184 ILE D C   
12576 O O   . ILE D 184 ? 0.2077 0.1973 0.2487 0.0355  -0.0570 -0.0490 184 ILE D O   
12577 C CB  . ILE D 184 ? 0.2147 0.2208 0.2663 0.0394  -0.0558 -0.0607 184 ILE D CB  
12578 C CG1 . ILE D 184 ? 0.1899 0.2029 0.2465 0.0411  -0.0562 -0.0661 184 ILE D CG1 
12579 C CG2 . ILE D 184 ? 0.2035 0.2169 0.2563 0.0390  -0.0530 -0.0629 184 ILE D CG2 
12580 C CD1 . ILE D 184 ? 0.3016 0.3241 0.3625 0.0438  -0.0560 -0.0729 184 ILE D CD1 
12581 N N   . VAL D 185 ? 0.1973 0.1873 0.2360 0.0327  -0.0537 -0.0461 185 VAL D N   
12582 C CA  . VAL D 185 ? 0.1930 0.1778 0.2268 0.0308  -0.0532 -0.0416 185 VAL D CA  
12583 C C   . VAL D 185 ? 0.1936 0.1826 0.2299 0.0315  -0.0525 -0.0441 185 VAL D C   
12584 O O   . VAL D 185 ? 0.2106 0.1957 0.2450 0.0311  -0.0537 -0.0423 185 VAL D O   
12585 C CB  . VAL D 185 ? 0.1960 0.1784 0.2264 0.0286  -0.0517 -0.0381 185 VAL D CB  
12586 C CG1 . VAL D 185 ? 0.2188 0.1970 0.2446 0.0269  -0.0511 -0.0343 185 VAL D CG1 
12587 C CG2 . VAL D 185 ? 0.2124 0.1902 0.2402 0.0280  -0.0527 -0.0357 185 VAL D CG2 
12588 N N   . ALA D 186 ? 0.1730 0.1711 0.2115 0.0306  -0.0498 -0.0477 186 ALA D N   
12589 C CA  . ALA D 186 ? 0.1804 0.1840 0.2200 0.0302  -0.0485 -0.0500 186 ALA D CA  
12590 C C   . ALA D 186 ? 0.1658 0.1812 0.2080 0.0299  -0.0463 -0.0542 186 ALA D C   
12591 O O   . ALA D 186 ? 0.1778 0.1972 0.2198 0.0282  -0.0451 -0.0539 186 ALA D O   
12592 C CB  . ALA D 186 ? 0.1884 0.1901 0.2236 0.0268  -0.0466 -0.0461 186 ALA D CB  
12593 N N   . ILE D 187 ? 0.1562 0.1775 0.2008 0.0315  -0.0461 -0.0583 187 ILE D N   
12594 C CA  . ILE D 187 ? 0.1775 0.2117 0.2235 0.0311  -0.0437 -0.0620 187 ILE D CA  
12595 C C   . ILE D 187 ? 0.1735 0.2112 0.2160 0.0279  -0.0414 -0.0594 187 ILE D C   
12596 O O   . ILE D 187 ? 0.2316 0.2650 0.2736 0.0282  -0.0422 -0.0590 187 ILE D O   
12597 C CB  . ILE D 187 ? 0.2031 0.2428 0.2544 0.0360  -0.0453 -0.0691 187 ILE D CB  
12598 C CG1 . ILE D 187 ? 0.2032 0.2410 0.2583 0.0393  -0.0476 -0.0721 187 ILE D CG1 
12599 C CG2 . ILE D 187 ? 0.1553 0.2092 0.2072 0.0358  -0.0426 -0.0731 187 ILE D CG2 
12600 C CD1 . ILE D 187 ? 0.2380 0.2794 0.2986 0.0445  -0.0501 -0.0787 187 ILE D CD1 
12601 N N   . VAL D 188 ? 0.1692 0.2149 0.2098 0.0248  -0.0390 -0.0573 188 VAL D N   
12602 C CA  . VAL D 188 ? 0.1606 0.2107 0.1981 0.0221  -0.0371 -0.0544 188 VAL D CA  
12603 C C   . VAL D 188 ? 0.1869 0.2509 0.2262 0.0234  -0.0356 -0.0588 188 VAL D C   
12604 O O   . VAL D 188 ? 0.1920 0.2658 0.2323 0.0230  -0.0344 -0.0597 188 VAL D O   
12605 C CB  . VAL D 188 ? 0.1645 0.2144 0.1989 0.0182  -0.0361 -0.0483 188 VAL D CB  
12606 C CG1 . VAL D 188 ? 0.1714 0.2257 0.2032 0.0161  -0.0346 -0.0454 188 VAL D CG1 
12607 C CG2 . VAL D 188 ? 0.1861 0.2232 0.2188 0.0176  -0.0375 -0.0449 188 VAL D CG2 
12608 N N   . SER D 189 ? 0.1598 0.2252 0.1994 0.0250  -0.0358 -0.0616 189 SER D N   
12609 C CA  . SER D 189 ? 0.2146 0.2933 0.2549 0.0266  -0.0342 -0.0660 189 SER D CA  
12610 C C   . SER D 189 ? 0.2141 0.2978 0.2506 0.0235  -0.0324 -0.0615 189 SER D C   
12611 O O   . SER D 189 ? 0.2254 0.3035 0.2603 0.0225  -0.0329 -0.0596 189 SER D O   
12612 C CB  . SER D 189 ? 0.1673 0.2453 0.2109 0.0306  -0.0360 -0.0720 189 SER D CB  
12613 O OG  . SER D 189 ? 0.1959 0.2705 0.2438 0.0341  -0.0382 -0.0762 189 SER D OG  
12614 N N   . THR D 190 ? 0.1326 0.2275 0.1679 0.0221  -0.0303 -0.0598 190 THR D N   
12615 C CA  . THR D 190 ? 0.1089 0.2093 0.1408 0.0195  -0.0287 -0.0551 190 THR D CA  
12616 C C   . THR D 190 ? 0.1113 0.2247 0.1427 0.0218  -0.0273 -0.0596 190 THR D C   
12617 O O   . THR D 190 ? 0.1687 0.2943 0.2012 0.0238  -0.0259 -0.0639 190 THR D O   
12618 C CB  . THR D 190 ? 0.1346 0.2400 0.1658 0.0167  -0.0277 -0.0499 190 THR D CB  
12619 O OG1 . THR D 190 ? 0.1713 0.2652 0.2037 0.0153  -0.0294 -0.0472 190 THR D OG1 
12620 C CG2 . THR D 190 ? 0.1489 0.2570 0.1769 0.0143  -0.0267 -0.0440 190 THR D CG2 
12621 N N   . VAL D 191 ? 0.1523 0.2638 0.1820 0.0217  -0.0276 -0.0590 191 VAL D N   
12622 C CA  . VAL D 191 ? 0.1716 0.2945 0.2009 0.0241  -0.0266 -0.0634 191 VAL D CA  
12623 C C   . VAL D 191 ? 0.1740 0.3003 0.1995 0.0220  -0.0256 -0.0583 191 VAL D C   
12624 O O   . VAL D 191 ? 0.1796 0.2956 0.2042 0.0199  -0.0268 -0.0542 191 VAL D O   
12625 C CB  . VAL D 191 ? 0.1578 0.2751 0.1903 0.0270  -0.0289 -0.0693 191 VAL D CB  
12626 C CG1 . VAL D 191 ? 0.1354 0.2516 0.1720 0.0302  -0.0300 -0.0750 191 VAL D CG1 
12627 C CG2 . VAL D 191 ? 0.1496 0.2520 0.1820 0.0246  -0.0310 -0.0655 191 VAL D CG2 
12628 N N   . THR D 192 ? 0.1924 0.3339 0.2155 0.0225  -0.0233 -0.0581 192 THR D N   
12629 C CA  . THR D 192 ? 0.2075 0.3627 0.2310 0.0239  -0.0213 -0.0609 192 THR D CA  
12630 C C   . THR D 192 ? 0.1658 0.3177 0.1897 0.0210  -0.0210 -0.0559 192 THR D C   
12631 O O   . THR D 192 ? 0.1278 0.2683 0.1512 0.0182  -0.0222 -0.0501 192 THR D O   
12632 C CB  . THR D 192 ? 0.1779 0.3512 0.1979 0.0245  -0.0186 -0.0600 192 THR D CB  
12633 O OG1 . THR D 192 ? 0.1689 0.3408 0.1857 0.0212  -0.0181 -0.0515 192 THR D OG1 
12634 C CG2 . THR D 192 ? 0.1586 0.3375 0.1790 0.0279  -0.0191 -0.0657 192 THR D CG2 
12635 N N   . CYS D 193 ? 0.1619 0.3247 0.1870 0.0217  -0.0196 -0.0584 193 CYS D N   
12636 C CA  . CYS D 193 ? 0.1955 0.3565 0.2222 0.0187  -0.0197 -0.0539 193 CYS D CA  
12637 C C   . CYS D 193 ? 0.2074 0.3771 0.2313 0.0153  -0.0179 -0.0458 193 CYS D C   
12638 O O   . CYS D 193 ? 0.2210 0.4083 0.2432 0.0152  -0.0153 -0.0453 193 CYS D O   
12639 C CB  . CYS D 193 ? 0.1507 0.3209 0.1804 0.0205  -0.0189 -0.0595 193 CYS D CB  
12640 S SG  . CYS D 193 ? 0.2040 0.3693 0.2378 0.0170  -0.0199 -0.0548 193 CYS D SG  
12641 N N   . ASN D 194 ? 0.2237 0.3819 0.2469 0.0127  -0.0193 -0.0394 194 ASN D N   
12642 C CA  . ASN D 194 ? 0.2589 0.4240 0.2793 0.0100  -0.0180 -0.0313 194 ASN D CA  
12643 C C   . ASN D 194 ? 0.2516 0.4284 0.2742 0.0072  -0.0166 -0.0275 194 ASN D C   
12644 O O   . ASN D 194 ? 0.2741 0.4675 0.2942 0.0061  -0.0140 -0.0240 194 ASN D O   
12645 C CB  . ASN D 194 ? 0.2570 0.4065 0.2770 0.0083  -0.0203 -0.0260 194 ASN D CB  
12646 C CG  . ASN D 194 ? 0.2424 0.3974 0.2589 0.0065  -0.0194 -0.0181 194 ASN D CG  
12647 O OD1 . ASN D 194 ? 0.2863 0.4568 0.3003 0.0064  -0.0171 -0.0161 194 ASN D OD1 
12648 N ND2 . ASN D 194 ? 0.2842 0.4271 0.3003 0.0054  -0.0213 -0.0134 194 ASN D ND2 
12649 N N   . SER D 195 ? 0.2513 0.4205 0.2787 0.0059  -0.0181 -0.0278 195 SER D N   
12650 C CA  . SER D 195 ? 0.2531 0.4317 0.2841 0.0023  -0.0170 -0.0231 195 SER D CA  
12651 C C   . SER D 195 ? 0.2782 0.4759 0.3099 0.0030  -0.0141 -0.0266 195 SER D C   
12652 O O   . SER D 195 ? 0.3800 0.5906 0.4136 -0.0005 -0.0121 -0.0210 195 SER D O   
12653 C CB  . SER D 195 ? 0.2832 0.4483 0.3198 0.0011  -0.0198 -0.0235 195 SER D CB  
12654 O OG  . SER D 195 ? 0.3614 0.5095 0.3966 0.0008  -0.0226 -0.0207 195 SER D OG  
12655 N N   . ALA D 196 ? 0.2952 0.4956 0.3254 0.0074  -0.0138 -0.0354 196 ALA D N   
12656 C CA  . ALA D 196 ? 0.2973 0.5173 0.3266 0.0088  -0.0111 -0.0395 196 ALA D CA  
12657 C C   . ALA D 196 ? 0.2614 0.4970 0.2841 0.0095  -0.0086 -0.0375 196 ALA D C   
12658 O O   . ALA D 196 ? 0.2672 0.5204 0.2875 0.0112  -0.0065 -0.0412 196 ALA D O   
12659 C CB  . ALA D 196 ? 0.2165 0.4333 0.2471 0.0138  -0.0122 -0.0505 196 ALA D CB  
12660 N N   . GLY D 197 ? 0.2742 0.5043 0.2935 0.0084  -0.0090 -0.0318 197 GLY D N   
12661 C CA  . GLY D 197 ? 0.2910 0.5355 0.3042 0.0091  -0.0067 -0.0291 197 GLY D CA  
12662 C C   . GLY D 197 ? 0.2681 0.5061 0.2789 0.0134  -0.0076 -0.0349 197 GLY D C   
12663 O O   . GLY D 197 ? 0.3183 0.5703 0.3255 0.0157  -0.0056 -0.0367 197 GLY D O   
12664 N N   . GLY D 198 ? 0.2007 0.4182 0.2141 0.0142  -0.0105 -0.0375 198 GLY D N   
12665 C CA  . GLY D 198 ? 0.2135 0.4239 0.2260 0.0175  -0.0117 -0.0427 198 GLY D CA  
12666 C C   . GLY D 198 ? 0.1954 0.4141 0.2092 0.0221  -0.0111 -0.0528 198 GLY D C   
12667 O O   . GLY D 198 ? 0.1951 0.4181 0.2080 0.0250  -0.0110 -0.0565 198 GLY D O   
12668 N N   . GLN D 199 ? 0.1536 0.3746 0.1702 0.0230  -0.0110 -0.0577 199 GLN D N   
12669 C CA  . GLN D 199 ? 0.1654 0.3969 0.1833 0.0277  -0.0103 -0.0675 199 GLN D CA  
12670 C C   . GLN D 199 ? 0.1790 0.3943 0.2015 0.0309  -0.0134 -0.0746 199 GLN D C   
12671 O O   . GLN D 199 ? 0.1814 0.3792 0.2063 0.0290  -0.0158 -0.0724 199 GLN D O   
12672 C CB  . GLN D 199 ? 0.1779 0.4211 0.1959 0.0270  -0.0089 -0.0689 199 GLN D CB  
12673 C CG  . GLN D 199 ? 0.1884 0.4497 0.2017 0.0235  -0.0061 -0.0614 199 GLN D CG  
12674 C CD  . GLN D 199 ? 0.2067 0.4827 0.2173 0.0256  -0.0051 -0.0618 199 GLN D CD  
12675 O OE1 . GLN D 199 ? 0.2475 0.5277 0.2601 0.0296  -0.0062 -0.0693 199 GLN D OE1 
12676 N NE2 . GLN D 199 ? 0.2376 0.5206 0.2449 0.0229  -0.0037 -0.0531 199 GLN D NE2 
12677 N N   . PRO D 200 ? 0.1838 0.4053 0.2083 0.0358  -0.0137 -0.0825 200 PRO D N   
12678 C CA  . PRO D 200 ? 0.1760 0.3819 0.2052 0.0385  -0.0172 -0.0876 200 PRO D CA  
12679 C C   . PRO D 200 ? 0.1808 0.3805 0.2146 0.0407  -0.0188 -0.0931 200 PRO D C   
12680 O O   . PRO D 200 ? 0.1771 0.3867 0.2111 0.0415  -0.0179 -0.0956 200 PRO D O   
12681 C CB  . PRO D 200 ? 0.1855 0.4018 0.2162 0.0427  -0.0177 -0.0934 200 PRO D CB  
12682 C CG  . PRO D 200 ? 0.1603 0.3954 0.1883 0.0426  -0.0155 -0.0926 200 PRO D CG  
12683 C CD  . PRO D 200 ? 0.1771 0.4163 0.2001 0.0378  -0.0125 -0.0842 200 PRO D CD  
12684 N N   . VAL D 201 ? 0.1838 0.3648 0.2209 0.0407  -0.0221 -0.0931 201 VAL D N   
12685 C CA  . VAL D 201 ? 0.2021 0.3755 0.2445 0.0438  -0.0245 -0.0986 201 VAL D CA  
12686 C C   . VAL D 201 ? 0.2635 0.4365 0.3106 0.0485  -0.0274 -0.1054 201 VAL D C   
12687 O O   . VAL D 201 ? 0.2369 0.4035 0.2842 0.0482  -0.0289 -0.1044 201 VAL D O   
12688 C CB  . VAL D 201 ? 0.2238 0.3768 0.2667 0.0404  -0.0268 -0.0930 201 VAL D CB  
12689 C CG1 . VAL D 201 ? 0.1994 0.3462 0.2476 0.0438  -0.0291 -0.0981 201 VAL D CG1 
12690 C CG2 . VAL D 201 ? 0.1814 0.3333 0.2201 0.0350  -0.0250 -0.0846 201 VAL D CG2 
12691 N N   . SER D 202 ? 0.1906 0.3689 0.2409 0.0517  -0.0290 -0.1108 202 SER D N   
12692 C CA  . SER D 202 ? 0.1737 0.3527 0.2284 0.0559  -0.0325 -0.1168 202 SER D CA  
12693 C C   . SER D 202 ? 0.1438 0.3051 0.2033 0.0571  -0.0367 -0.1175 202 SER D C   
12694 O O   . SER D 202 ? 0.1884 0.3377 0.2484 0.0554  -0.0372 -0.1142 202 SER D O   
12695 C CB  . SER D 202 ? 0.2353 0.4255 0.2924 0.0594  -0.0334 -0.1225 202 SER D CB  
12696 O OG  . SER D 202 ? 0.2021 0.3836 0.2624 0.0601  -0.0353 -0.1236 202 SER D OG  
12697 N N   . MET D 203 ? 0.1555 0.3158 0.2187 0.0602  -0.0401 -0.1219 203 MET D N   
12698 C CA  . MET D 203 ? 0.1942 0.3389 0.2622 0.0613  -0.0447 -0.1226 203 MET D CA  
12699 C C   . MET D 203 ? 0.2386 0.3774 0.3102 0.0634  -0.0476 -0.1244 203 MET D C   
12700 O O   . MET D 203 ? 0.2374 0.3619 0.3110 0.0626  -0.0501 -0.1217 203 MET D O   
12701 C CB  . MET D 203 ? 0.1859 0.3323 0.2575 0.0645  -0.0481 -0.1278 203 MET D CB  
12702 C CG  . MET D 203 ? 0.2519 0.3806 0.3262 0.0635  -0.0529 -0.1264 203 MET D CG  
12703 S SD  . MET D 203 ? 0.2965 0.4102 0.3637 0.0552  -0.0510 -0.1158 203 MET D SD  
12704 C CE  . MET D 203 ? 0.2379 0.3593 0.3015 0.0535  -0.0499 -0.1164 203 MET D CE  
12705 N N   . SER D 204 ? 0.2059 0.3563 0.2784 0.0660  -0.0475 -0.1289 204 SER D N   
12706 C CA  . SER D 204 ? 0.2221 0.3678 0.2983 0.0683  -0.0505 -0.1312 204 SER D CA  
12707 C C   . SER D 204 ? 0.2120 0.3533 0.2856 0.0652  -0.0478 -0.1264 204 SER D C   
12708 O O   . SER D 204 ? 0.2797 0.4118 0.3561 0.0661  -0.0506 -0.1262 204 SER D O   
12709 C CB  . SER D 204 ? 0.3036 0.4640 0.3823 0.0726  -0.0517 -0.1383 204 SER D CB  
12710 O OG  . SER D 204 ? 0.4050 0.5803 0.4794 0.0711  -0.0467 -0.1378 204 SER D OG  
12711 N N   . ASN D 205 ? 0.2029 0.3507 0.2713 0.0616  -0.0427 -0.1226 205 ASN D N   
12712 C CA  . ASN D 205 ? 0.2153 0.3576 0.2813 0.0584  -0.0406 -0.1181 205 ASN D CA  
12713 C C   . ASN D 205 ? 0.2274 0.3522 0.2936 0.0563  -0.0423 -0.1127 205 ASN D C   
12714 O O   . ASN D 205 ? 0.2113 0.3261 0.2789 0.0560  -0.0440 -0.1107 205 ASN D O   
12715 C CB  . ASN D 205 ? 0.2458 0.4004 0.3062 0.0551  -0.0355 -0.1155 205 ASN D CB  
12716 C CG  . ASN D 205 ? 0.2413 0.3946 0.3000 0.0525  -0.0337 -0.1128 205 ASN D CG  
12717 O OD1 . ASN D 205 ? 0.1949 0.3428 0.2511 0.0491  -0.0319 -0.1075 205 ASN D OD1 
12718 N ND2 . ASN D 205 ? 0.2215 0.3808 0.2821 0.0542  -0.0343 -0.1169 205 ASN D ND2 
12719 N N   . LEU D 206 ? 0.1388 0.2603 0.2037 0.0549  -0.0419 -0.1103 206 LEU D N   
12720 C CA  . LEU D 206 ? 0.1781 0.2839 0.2433 0.0531  -0.0437 -0.1055 206 LEU D CA  
12721 C C   . LEU D 206 ? 0.2600 0.3546 0.3298 0.0555  -0.0490 -0.1068 206 LEU D C   
12722 O O   . LEU D 206 ? 0.2137 0.2964 0.2835 0.0543  -0.0507 -0.1027 206 LEU D O   
12723 C CB  . LEU D 206 ? 0.1648 0.2686 0.2265 0.0499  -0.0431 -0.1023 206 LEU D CB  
12724 C CG  . LEU D 206 ? 0.2303 0.3425 0.2858 0.0460  -0.0387 -0.0984 206 LEU D CG  
12725 C CD1 . LEU D 206 ? 0.2272 0.3388 0.2803 0.0440  -0.0389 -0.0967 206 LEU D CD1 
12726 C CD2 . LEU D 206 ? 0.2356 0.3401 0.2869 0.0412  -0.0370 -0.0908 206 LEU D CD2 
12727 N N   . LYS D 207 ? 0.2760 0.3748 0.3496 0.0591  -0.0522 -0.1125 207 LYS D N   
12728 C CA  . LYS D 207 ? 0.2655 0.3550 0.3436 0.0618  -0.0579 -0.1143 207 LYS D CA  
12729 C C   . LYS D 207 ? 0.2456 0.3322 0.3243 0.0625  -0.0588 -0.1137 207 LYS D C   
12730 O O   . LYS D 207 ? 0.2385 0.3127 0.3178 0.0619  -0.0619 -0.1102 207 LYS D O   
12731 C CB  . LYS D 207 ? 0.3099 0.4071 0.3920 0.0661  -0.0610 -0.1216 207 LYS D CB  
12732 C CG  . LYS D 207 ? 0.3450 0.4327 0.4322 0.0691  -0.0679 -0.1241 207 LYS D CG  
12733 C CD  . LYS D 207 ? 0.3475 0.4427 0.4384 0.0729  -0.0709 -0.1313 207 LYS D CD  
12734 C CE  . LYS D 207 ? 0.3908 0.4753 0.4869 0.0756  -0.0784 -0.1336 207 LYS D CE  
12735 N NZ  . LYS D 207 ? 0.4429 0.5236 0.5412 0.0781  -0.0824 -0.1351 207 LYS D NZ  
12736 N N   . GLU D 208 ? 0.2313 0.3298 0.3097 0.0636  -0.0563 -0.1171 208 GLU D N   
12737 C CA  . GLU D 208 ? 0.2738 0.3706 0.3534 0.0647  -0.0575 -0.1177 208 GLU D CA  
12738 C C   . GLU D 208 ? 0.2801 0.3678 0.3566 0.0610  -0.0556 -0.1112 208 GLU D C   
12739 O O   . GLU D 208 ? 0.3033 0.3824 0.3810 0.0615  -0.0584 -0.1095 208 GLU D O   
12740 C CB  . GLU D 208 ? 0.2129 0.3258 0.2928 0.0666  -0.0550 -0.1232 208 GLU D CB  
12741 C CG  . GLU D 208 ? 0.2974 0.4098 0.3796 0.0685  -0.0567 -0.1253 208 GLU D CG  
12742 C CD  . GLU D 208 ? 0.2858 0.4151 0.3687 0.0708  -0.0548 -0.1318 208 GLU D CD  
12743 O OE1 . GLU D 208 ? 0.2756 0.4173 0.3574 0.0714  -0.0526 -0.1347 208 GLU D OE1 
12744 O OE2 . GLU D 208 ? 0.3723 0.5029 0.4565 0.0721  -0.0554 -0.1342 208 GLU D OE2 
12745 N N   . VAL D 209 ? 0.2465 0.3361 0.3189 0.0575  -0.0513 -0.1075 209 VAL D N   
12746 C CA  . VAL D 209 ? 0.2607 0.3416 0.3304 0.0543  -0.0500 -0.1015 209 VAL D CA  
12747 C C   . VAL D 209 ? 0.2934 0.3587 0.3634 0.0536  -0.0536 -0.0967 209 VAL D C   
12748 O O   . VAL D 209 ? 0.2756 0.3319 0.3450 0.0528  -0.0553 -0.0932 209 VAL D O   
12749 C CB  . VAL D 209 ? 0.2489 0.3359 0.3145 0.0510  -0.0451 -0.0989 209 VAL D CB  
12750 C CG1 . VAL D 209 ? 0.1906 0.2662 0.2538 0.0480  -0.0448 -0.0925 209 VAL D CG1 
12751 C CG2 . VAL D 209 ? 0.1908 0.2928 0.2554 0.0509  -0.0418 -0.1025 209 VAL D CG2 
12752 N N   . TYR D 210 ? 0.2836 0.3460 0.3542 0.0537  -0.0552 -0.0966 210 TYR D N   
12753 C CA  . TYR D 210 ? 0.2384 0.2871 0.3090 0.0528  -0.0589 -0.0923 210 TYR D CA  
12754 C C   . TYR D 210 ? 0.2658 0.3084 0.3393 0.0554  -0.0641 -0.0936 210 TYR D C   
12755 O O   . TYR D 210 ? 0.3348 0.3667 0.4066 0.0542  -0.0665 -0.0889 210 TYR D O   
12756 C CB  . TYR D 210 ? 0.2205 0.2685 0.2921 0.0527  -0.0598 -0.0929 210 TYR D CB  
12757 C CG  . TYR D 210 ? 0.2831 0.3168 0.3521 0.0494  -0.0627 -0.0872 210 TYR D CG  
12758 C CD1 . TYR D 210 ? 0.2408 0.2673 0.3042 0.0447  -0.0603 -0.0800 210 TYR D CD1 
12759 C CD2 . TYR D 210 ? 0.2658 0.2936 0.3378 0.0510  -0.0680 -0.0890 210 TYR D CD2 
12760 C CE1 . TYR D 210 ? 0.2539 0.2687 0.3147 0.0419  -0.0628 -0.0752 210 TYR D CE1 
12761 C CE2 . TYR D 210 ? 0.2836 0.2989 0.3526 0.0476  -0.0704 -0.0839 210 TYR D CE2 
12762 C CZ  . TYR D 210 ? 0.3243 0.3336 0.3877 0.0431  -0.0676 -0.0771 210 TYR D CZ  
12763 O OH  . TYR D 210 ? 0.3252 0.3234 0.3858 0.0399  -0.0700 -0.0725 210 TYR D OH  
12764 N N   . GLU D 211 ? 0.2839 0.3333 0.3612 0.0591  -0.0663 -0.1000 211 GLU D N   
12765 C CA  . GLU D 211 ? 0.2934 0.3373 0.3735 0.0619  -0.0720 -0.1017 211 GLU D CA  
12766 C C   . GLU D 211 ? 0.3206 0.3624 0.3994 0.0616  -0.0716 -0.0997 211 GLU D C   
12767 O O   . GLU D 211 ? 0.3528 0.3852 0.4314 0.0619  -0.0757 -0.0972 211 GLU D O   
12768 C CB  . GLU D 211 ? 0.2589 0.3119 0.3436 0.0663  -0.0744 -0.1097 211 GLU D CB  
12769 C CG  . GLU D 211 ? 0.3516 0.4040 0.4385 0.0674  -0.0769 -0.1122 211 GLU D CG  
12770 C CD  . GLU D 211 ? 0.4041 0.4687 0.4948 0.0715  -0.0778 -0.1203 211 GLU D CD  
12771 O OE1 . GLU D 211 ? 0.4941 0.5678 0.5858 0.0737  -0.0769 -0.1242 211 GLU D OE1 
12772 O OE2 . GLU D 211 ? 0.4542 0.5197 0.5469 0.0726  -0.0797 -0.1231 211 GLU D OE2 
12773 N N   . ILE D 212 ? 0.2558 0.3064 0.3337 0.0609  -0.0668 -0.1008 212 ILE D N   
12774 C CA  . ILE D 212 ? 0.3148 0.3635 0.3918 0.0605  -0.0664 -0.0993 212 ILE D CA  
12775 C C   . ILE D 212 ? 0.3222 0.3590 0.3951 0.0570  -0.0663 -0.0917 212 ILE D C   
12776 O O   . ILE D 212 ? 0.3769 0.4065 0.4493 0.0572  -0.0692 -0.0893 212 ILE D O   
12777 C CB  . ILE D 212 ? 0.3335 0.3947 0.4104 0.0602  -0.0615 -0.1028 212 ILE D CB  
12778 C CG1 . ILE D 212 ? 0.2634 0.3366 0.3441 0.0642  -0.0623 -0.1108 212 ILE D CG1 
12779 C CG2 . ILE D 212 ? 0.2999 0.3580 0.3755 0.0589  -0.0606 -0.1006 212 ILE D CG2 
12780 C CD1 . ILE D 212 ? 0.2394 0.3275 0.3191 0.0637  -0.0574 -0.1148 212 ILE D CD1 
12781 N N   . ALA D 213 ? 0.3009 0.3361 0.3709 0.0539  -0.0633 -0.0878 213 ALA D N   
12782 C CA  . ALA D 213 ? 0.3089 0.3337 0.3747 0.0507  -0.0632 -0.0807 213 ALA D CA  
12783 C C   . ALA D 213 ? 0.2923 0.3063 0.3573 0.0508  -0.0682 -0.0777 213 ALA D C   
12784 O O   . ALA D 213 ? 0.2990 0.3048 0.3609 0.0496  -0.0699 -0.0732 213 ALA D O   
12785 C CB  . ALA D 213 ? 0.3052 0.3315 0.3683 0.0478  -0.0592 -0.0780 213 ALA D CB  
12786 N N   . LYS D 214 ? 0.2972 0.3113 0.3647 0.0523  -0.0708 -0.0803 214 LYS D N   
12787 C CA  . LYS D 214 ? 0.3269 0.3308 0.3939 0.0524  -0.0762 -0.0782 214 LYS D CA  
12788 C C   . LYS D 214 ? 0.3498 0.3497 0.4173 0.0545  -0.0807 -0.0791 214 LYS D C   
12789 O O   . LYS D 214 ? 0.3469 0.3372 0.4111 0.0532  -0.0839 -0.0748 214 LYS D O   
12790 C CB  . LYS D 214 ? 0.3317 0.3373 0.4025 0.0541  -0.0787 -0.0823 214 LYS D CB  
12791 C CG  . LYS D 214 ? 0.4460 0.4410 0.5162 0.0531  -0.0835 -0.0793 214 LYS D CG  
12792 C CD  . LYS D 214 ? 0.4916 0.4885 0.5666 0.0552  -0.0866 -0.0844 214 LYS D CD  
12793 C CE  . LYS D 214 ? 0.4547 0.4392 0.5262 0.0513  -0.0897 -0.0809 214 LYS D CE  
12794 N NZ  . LYS D 214 ? 0.5222 0.5075 0.5970 0.0519  -0.0920 -0.0858 214 LYS D NZ  
12795 N N   . GLN D 215 ? 0.3860 0.3937 0.4574 0.0578  -0.0811 -0.0848 215 GLN D N   
12796 C CA  . GLN D 215 ? 0.3601 0.3652 0.4325 0.0602  -0.0854 -0.0864 215 GLN D CA  
12797 C C   . GLN D 215 ? 0.3696 0.3698 0.4379 0.0580  -0.0842 -0.0814 215 GLN D C   
12798 O O   . GLN D 215 ? 0.3461 0.3395 0.4129 0.0587  -0.0887 -0.0801 215 GLN D O   
12799 C CB  . GLN D 215 ? 0.4093 0.4258 0.4868 0.0640  -0.0850 -0.0937 215 GLN D CB  
12800 C CG  . GLN D 215 ? 0.4385 0.4555 0.5170 0.0659  -0.0869 -0.0952 215 GLN D CG  
12801 C CD  . GLN D 215 ? 0.5483 0.5784 0.6308 0.0684  -0.0839 -0.1015 215 GLN D CD  
12802 O OE1 . GLN D 215 ? 0.4831 0.5221 0.5667 0.0682  -0.0799 -0.1042 215 GLN D OE1 
12803 N NE2 . GLN D 215 ? 0.5398 0.5714 0.6242 0.0706  -0.0861 -0.1039 215 GLN D NE2 
12804 N N   . HIS D 216 ? 0.3663 0.3699 0.4326 0.0555  -0.0786 -0.0788 216 HIS D N   
12805 C CA  . HIS D 216 ? 0.3308 0.3299 0.3933 0.0535  -0.0775 -0.0743 216 HIS D CA  
12806 C C   . HIS D 216 ? 0.3818 0.3723 0.4385 0.0498  -0.0770 -0.0674 216 HIS D C   
12807 O O   . HIS D 216 ? 0.3801 0.3670 0.4331 0.0480  -0.0758 -0.0634 216 HIS D O   
12808 C CB  . HIS D 216 ? 0.3217 0.3289 0.3855 0.0531  -0.0724 -0.0761 216 HIS D CB  
12809 C CG  . HIS D 216 ? 0.3581 0.3738 0.4270 0.0566  -0.0729 -0.0829 216 HIS D CG  
12810 N ND1 . HIS D 216 ? 0.3985 0.4241 0.4712 0.0587  -0.0716 -0.0889 216 HIS D ND1 
12811 C CD2 . HIS D 216 ? 0.3546 0.3710 0.4253 0.0586  -0.0746 -0.0852 216 HIS D CD2 
12812 C CE1 . HIS D 216 ? 0.3760 0.4082 0.4524 0.0617  -0.0723 -0.0946 216 HIS D CE1 
12813 N NE2 . HIS D 216 ? 0.4275 0.4541 0.5031 0.0617  -0.0742 -0.0926 216 HIS D NE2 
12814 N N   . GLY D 217 ? 0.3426 0.3299 0.3987 0.0489  -0.0780 -0.0663 217 GLY D N   
12815 C CA  . GLY D 217 ? 0.3142 0.2941 0.3651 0.0456  -0.0777 -0.0605 217 GLY D CA  
12816 C C   . GLY D 217 ? 0.3295 0.3123 0.3781 0.0430  -0.0721 -0.0576 217 GLY D C   
12817 O O   . GLY D 217 ? 0.3643 0.3414 0.4078 0.0405  -0.0716 -0.0525 217 GLY D O   
12818 N N   . ILE D 218 ? 0.3136 0.3053 0.3655 0.0436  -0.0682 -0.0610 218 ILE D N   
12819 C CA  . ILE D 218 ? 0.2937 0.2884 0.3438 0.0414  -0.0634 -0.0590 218 ILE D CA  
12820 C C   . ILE D 218 ? 0.2775 0.2732 0.3274 0.0401  -0.0620 -0.0585 218 ILE D C   
12821 O O   . ILE D 218 ? 0.2625 0.2629 0.3162 0.0418  -0.0626 -0.0627 218 ILE D O   
12822 C CB  . ILE D 218 ? 0.2844 0.2887 0.3379 0.0427  -0.0606 -0.0636 218 ILE D CB  
12823 C CG1 . ILE D 218 ? 0.2654 0.2685 0.3196 0.0440  -0.0623 -0.0643 218 ILE D CG1 
12824 C CG2 . ILE D 218 ? 0.2021 0.2096 0.2539 0.0405  -0.0564 -0.0621 218 ILE D CG2 
12825 C CD1 . ILE D 218 ? 0.2812 0.2941 0.3393 0.0455  -0.0602 -0.0698 218 ILE D CD1 
12826 N N   . PHE D 219 ? 0.2620 0.2537 0.3079 0.0374  -0.0602 -0.0537 219 PHE D N   
12827 C CA  . PHE D 219 ? 0.2246 0.2169 0.2690 0.0350  -0.0582 -0.0526 219 PHE D CA  
12828 C C   . PHE D 219 ? 0.1889 0.1913 0.2343 0.0342  -0.0538 -0.0558 219 PHE D C   
12829 O O   . PHE D 219 ? 0.2141 0.2210 0.2598 0.0344  -0.0518 -0.0567 219 PHE D O   
12830 C CB  . PHE D 219 ? 0.1872 0.1728 0.2256 0.0316  -0.0571 -0.0465 219 PHE D CB  
12831 C CG  . PHE D 219 ? 0.2199 0.2040 0.2556 0.0281  -0.0555 -0.0446 219 PHE D CG  
12832 C CD1 . PHE D 219 ? 0.2521 0.2418 0.2864 0.0256  -0.0514 -0.0444 219 PHE D CD1 
12833 C CD2 . PHE D 219 ? 0.2224 0.1996 0.2566 0.0270  -0.0583 -0.0429 219 PHE D CD2 
12834 C CE1 . PHE D 219 ? 0.1833 0.1722 0.2155 0.0226  -0.0504 -0.0428 219 PHE D CE1 
12835 C CE2 . PHE D 219 ? 0.2522 0.2280 0.2844 0.0236  -0.0569 -0.0415 219 PHE D CE2 
12836 C CZ  . PHE D 219 ? 0.2472 0.2292 0.2788 0.0216  -0.0530 -0.0416 219 PHE D CZ  
12837 N N   . VAL D 220 ? 0.2016 0.2078 0.2471 0.0329  -0.0526 -0.0573 220 VAL D N   
12838 C CA  . VAL D 220 ? 0.2043 0.2212 0.2499 0.0320  -0.0490 -0.0600 220 VAL D CA  
12839 C C   . VAL D 220 ? 0.2326 0.2498 0.2741 0.0278  -0.0466 -0.0565 220 VAL D C   
12840 O O   . VAL D 220 ? 0.2038 0.2176 0.2451 0.0268  -0.0479 -0.0561 220 VAL D O   
12841 C CB  . VAL D 220 ? 0.1678 0.1921 0.2183 0.0354  -0.0503 -0.0666 220 VAL D CB  
12842 C CG1 . VAL D 220 ? 0.1842 0.2209 0.2340 0.0347  -0.0466 -0.0692 220 VAL D CG1 
12843 C CG2 . VAL D 220 ? 0.1852 0.2090 0.2407 0.0402  -0.0536 -0.0705 220 VAL D CG2 
12844 N N   . VAL D 221 ? 0.2077 0.2296 0.2461 0.0253  -0.0435 -0.0542 221 VAL D N   
12845 C CA  . VAL D 221 ? 0.1684 0.1927 0.2035 0.0219  -0.0414 -0.0510 221 VAL D CA  
12846 C C   . VAL D 221 ? 0.1689 0.2054 0.2045 0.0218  -0.0394 -0.0537 221 VAL D C   
12847 O O   . VAL D 221 ? 0.1920 0.2352 0.2283 0.0226  -0.0383 -0.0552 221 VAL D O   
12848 C CB  . VAL D 221 ? 0.1844 0.2047 0.2155 0.0193  -0.0402 -0.0458 221 VAL D CB  
12849 C CG1 . VAL D 221 ? 0.1448 0.1678 0.1732 0.0164  -0.0386 -0.0427 221 VAL D CG1 
12850 C CG2 . VAL D 221 ? 0.1999 0.2089 0.2302 0.0201  -0.0423 -0.0435 221 VAL D CG2 
12851 N N   . MET D 222 ? 0.2212 0.2610 0.2564 0.0209  -0.0391 -0.0541 222 MET D N   
12852 C CA  . MET D 222 ? 0.1982 0.2498 0.2331 0.0209  -0.0373 -0.0560 222 MET D CA  
12853 C C   . MET D 222 ? 0.1955 0.2495 0.2265 0.0176  -0.0354 -0.0505 222 MET D C   
12854 O O   . MET D 222 ? 0.2075 0.2579 0.2370 0.0157  -0.0356 -0.0477 222 MET D O   
12855 C CB  . MET D 222 ? 0.1594 0.2133 0.1963 0.0221  -0.0385 -0.0599 222 MET D CB  
12856 C CG  . MET D 222 ? 0.1882 0.2551 0.2252 0.0235  -0.0370 -0.0634 222 MET D CG  
12857 S SD  . MET D 222 ? 0.2772 0.3508 0.3188 0.0286  -0.0379 -0.0713 222 MET D SD  
12858 C CE  . MET D 222 ? 0.1949 0.2633 0.2404 0.0307  -0.0415 -0.0757 222 MET D CE  
12859 N N   . ASP D 223 ? 0.1778 0.2383 0.2077 0.0170  -0.0338 -0.0489 223 ASP D N   
12860 C CA  . ASP D 223 ? 0.1467 0.2117 0.1738 0.0145  -0.0324 -0.0440 223 ASP D CA  
12861 C C   . ASP D 223 ? 0.1933 0.2681 0.2200 0.0153  -0.0314 -0.0460 223 ASP D C   
12862 O O   . ASP D 223 ? 0.1895 0.2743 0.2172 0.0171  -0.0305 -0.0498 223 ASP D O   
12863 C CB  . ASP D 223 ? 0.1861 0.2558 0.2129 0.0136  -0.0315 -0.0416 223 ASP D CB  
12864 C CG  . ASP D 223 ? 0.2016 0.2746 0.2260 0.0113  -0.0307 -0.0357 223 ASP D CG  
12865 O OD1 . ASP D 223 ? 0.2401 0.3185 0.2630 0.0113  -0.0298 -0.0349 223 ASP D OD1 
12866 O OD2 . ASP D 223 ? 0.2178 0.2879 0.2420 0.0098  -0.0311 -0.0320 223 ASP D OD2 
12867 N N   . SER D 224 ? 0.1841 0.2569 0.2096 0.0140  -0.0317 -0.0438 224 SER D N   
12868 C CA  . SER D 224 ? 0.2023 0.2815 0.2282 0.0150  -0.0318 -0.0468 224 SER D CA  
12869 C C   . SER D 224 ? 0.1754 0.2621 0.1987 0.0140  -0.0305 -0.0433 224 SER D C   
12870 O O   . SER D 224 ? 0.2016 0.2917 0.2250 0.0144  -0.0309 -0.0447 224 SER D O   
12871 C CB  . SER D 224 ? 0.1423 0.2133 0.1700 0.0146  -0.0338 -0.0482 224 SER D CB  
12872 O OG  . SER D 224 ? 0.1841 0.2476 0.2140 0.0157  -0.0352 -0.0508 224 SER D OG  
12873 N N   . ALA D 225 ? 0.1802 0.2693 0.2015 0.0129  -0.0293 -0.0385 225 ALA D N   
12874 C CA  . ALA D 225 ? 0.1502 0.2462 0.1690 0.0124  -0.0282 -0.0346 225 ALA D CA  
12875 C C   . ALA D 225 ? 0.2184 0.3264 0.2364 0.0142  -0.0272 -0.0382 225 ALA D C   
12876 O O   . ALA D 225 ? 0.2089 0.3204 0.2257 0.0143  -0.0273 -0.0371 225 ALA D O   
12877 C CB  . ALA D 225 ? 0.1761 0.2747 0.1933 0.0114  -0.0272 -0.0296 225 ALA D CB  
12878 N N   . ARG D 226 ? 0.1740 0.2892 0.1928 0.0160  -0.0264 -0.0427 226 ARG D N   
12879 C CA  . ARG D 226 ? 0.1795 0.3076 0.1972 0.0181  -0.0254 -0.0464 226 ARG D CA  
12880 C C   . ARG D 226 ? 0.1773 0.3058 0.1982 0.0207  -0.0265 -0.0543 226 ARG D C   
12881 O O   . ARG D 226 ? 0.1901 0.3300 0.2111 0.0233  -0.0254 -0.0589 226 ARG D O   
12882 C CB  . ARG D 226 ? 0.1570 0.2983 0.1724 0.0183  -0.0229 -0.0444 226 ARG D CB  
12883 C CG  . ARG D 226 ? 0.1460 0.2872 0.1586 0.0160  -0.0222 -0.0362 226 ARG D CG  
12884 C CD  . ARG D 226 ? 0.1954 0.3500 0.2058 0.0155  -0.0199 -0.0329 226 ARG D CD  
12885 N NE  . ARG D 226 ? 0.2051 0.3573 0.2137 0.0132  -0.0199 -0.0246 226 ARG D NE  
12886 C CZ  . ARG D 226 ? 0.2370 0.3809 0.2471 0.0111  -0.0207 -0.0210 226 ARG D CZ  
12887 N NH1 . ARG D 226 ? 0.1692 0.3065 0.1826 0.0110  -0.0216 -0.0246 226 ARG D NH1 
12888 N NH2 . ARG D 226 ? 0.2050 0.3469 0.2134 0.0095  -0.0210 -0.0136 226 ARG D NH2 
12889 N N   . PHE D 227 ? 0.1627 0.2795 0.1861 0.0202  -0.0289 -0.0557 227 PHE D N   
12890 C CA  . PHE D 227 ? 0.1610 0.2760 0.1881 0.0227  -0.0306 -0.0627 227 PHE D CA  
12891 C C   . PHE D 227 ? 0.1860 0.3104 0.2135 0.0250  -0.0311 -0.0677 227 PHE D C   
12892 O O   . PHE D 227 ? 0.1741 0.3018 0.2045 0.0282  -0.0322 -0.0744 227 PHE D O   
12893 C CB  . PHE D 227 ? 0.1497 0.2501 0.1791 0.0210  -0.0331 -0.0619 227 PHE D CB  
12894 C CG  . PHE D 227 ? 0.1853 0.2827 0.2147 0.0191  -0.0345 -0.0601 227 PHE D CG  
12895 C CD1 . PHE D 227 ? 0.2173 0.3148 0.2440 0.0167  -0.0335 -0.0541 227 PHE D CD1 
12896 C CD2 . PHE D 227 ? 0.1572 0.2518 0.1898 0.0197  -0.0371 -0.0646 227 PHE D CD2 
12897 C CE1 . PHE D 227 ? 0.2082 0.3041 0.2356 0.0151  -0.0348 -0.0529 227 PHE D CE1 
12898 C CE2 . PHE D 227 ? 0.1826 0.2753 0.2157 0.0176  -0.0386 -0.0631 227 PHE D CE2 
12899 C CZ  . PHE D 227 ? 0.2246 0.3183 0.2553 0.0153  -0.0374 -0.0573 227 PHE D CZ  
12900 N N   . CYS D 228 ? 0.1903 0.3191 0.2153 0.0239  -0.0308 -0.0648 228 CYS D N   
12901 C CA  . CYS D 228 ? 0.1800 0.3182 0.2051 0.0262  -0.0315 -0.0695 228 CYS D CA  
12902 C C   . CYS D 228 ? 0.2232 0.3774 0.2462 0.0291  -0.0290 -0.0719 228 CYS D C   
12903 O O   . CYS D 228 ? 0.2413 0.4042 0.2660 0.0325  -0.0297 -0.0784 228 CYS D O   
12904 C CB  . CYS D 228 ? 0.1699 0.3078 0.1932 0.0242  -0.0322 -0.0656 228 CYS D CB  
12905 S SG  . CYS D 228 ? 0.2491 0.3722 0.2759 0.0211  -0.0353 -0.0643 228 CYS D SG  
12906 N N   . GLU D 229 ? 0.2535 0.4127 0.2733 0.0278  -0.0262 -0.0666 229 GLU D N   
12907 C CA  . GLU D 229 ? 0.1915 0.3674 0.2095 0.0301  -0.0236 -0.0683 229 GLU D CA  
12908 C C   . GLU D 229 ? 0.1839 0.3625 0.2056 0.0328  -0.0234 -0.0747 229 GLU D C   
12909 O O   . GLU D 229 ? 0.2312 0.4248 0.2535 0.0363  -0.0222 -0.0797 229 GLU D O   
12910 C CB  . GLU D 229 ? 0.1696 0.3499 0.1837 0.0275  -0.0210 -0.0603 229 GLU D CB  
12911 C CG  . GLU D 229 ? 0.1988 0.3802 0.2096 0.0261  -0.0211 -0.0548 229 GLU D CG  
12912 C CD  . GLU D 229 ? 0.2272 0.4091 0.2348 0.0233  -0.0195 -0.0460 229 GLU D CD  
12913 O OE1 . GLU D 229 ? 0.2487 0.4315 0.2566 0.0221  -0.0181 -0.0441 229 GLU D OE1 
12914 O OE2 . GLU D 229 ? 0.2269 0.4083 0.2321 0.0225  -0.0198 -0.0411 229 GLU D OE2 
12915 N N   . ASN D 230 ? 0.2088 0.3738 0.2332 0.0317  -0.0249 -0.0748 230 ASN D N   
12916 C CA  . ASN D 230 ? 0.2141 0.3803 0.2427 0.0349  -0.0255 -0.0815 230 ASN D CA  
12917 C C   . ASN D 230 ? 0.2423 0.4090 0.2749 0.0387  -0.0282 -0.0892 230 ASN D C   
12918 O O   . ASN D 230 ? 0.2282 0.4061 0.2637 0.0431  -0.0280 -0.0960 230 ASN D O   
12919 C CB  . ASN D 230 ? 0.1865 0.3375 0.2172 0.0330  -0.0268 -0.0793 230 ASN D CB  
12920 C CG  . ASN D 230 ? 0.2212 0.3763 0.2551 0.0359  -0.0264 -0.0844 230 ASN D CG  
12921 O OD1 . ASN D 230 ? 0.2047 0.3676 0.2370 0.0351  -0.0240 -0.0826 230 ASN D OD1 
12922 N ND2 . ASN D 230 ? 0.1681 0.3187 0.2071 0.0394  -0.0291 -0.0908 230 ASN D ND2 
12923 N N   . ALA D 231 ? 0.2108 0.3665 0.2440 0.0371  -0.0309 -0.0882 231 ALA D N   
12924 C CA  . ALA D 231 ? 0.2071 0.3621 0.2443 0.0401  -0.0342 -0.0951 231 ALA D CA  
12925 C C   . ALA D 231 ? 0.2435 0.4156 0.2801 0.0437  -0.0335 -0.0999 231 ALA D C   
12926 O O   . ALA D 231 ? 0.2830 0.4605 0.3237 0.0482  -0.0355 -0.1075 231 ALA D O   
12927 C CB  . ALA D 231 ? 0.1957 0.3377 0.2332 0.0368  -0.0370 -0.0923 231 ALA D CB  
12928 N N   . TYR D 232 ? 0.2387 0.4198 0.2702 0.0422  -0.0309 -0.0954 232 TYR D N   
12929 C CA  . TYR D 232 ? 0.2226 0.4212 0.2529 0.0456  -0.0300 -0.0992 232 TYR D CA  
12930 C C   . TYR D 232 ? 0.1997 0.4136 0.2322 0.0498  -0.0281 -0.1043 232 TYR D C   
12931 O O   . TYR D 232 ? 0.2387 0.4638 0.2740 0.0545  -0.0293 -0.1114 232 TYR D O   
12932 C CB  . TYR D 232 ? 0.2158 0.4211 0.2402 0.0430  -0.0276 -0.0921 232 TYR D CB  
12933 C CG  . TYR D 232 ? 0.2628 0.4870 0.2853 0.0464  -0.0266 -0.0949 232 TYR D CG  
12934 C CD1 . TYR D 232 ? 0.2541 0.4963 0.2756 0.0485  -0.0233 -0.0949 232 TYR D CD1 
12935 C CD2 . TYR D 232 ? 0.2244 0.4492 0.2464 0.0474  -0.0292 -0.0974 232 TYR D CD2 
12936 C CE1 . TYR D 232 ? 0.2640 0.5245 0.2841 0.0516  -0.0226 -0.0970 232 TYR D CE1 
12937 C CE2 . TYR D 232 ? 0.2273 0.4693 0.2474 0.0507  -0.0287 -0.0999 232 TYR D CE2 
12938 C CZ  . TYR D 232 ? 0.2589 0.5187 0.2780 0.0529  -0.0254 -0.0995 232 TYR D CZ  
12939 O OH  . TYR D 232 ? 0.3323 0.6099 0.3495 0.0563  -0.0250 -0.1016 232 TYR D OH  
12940 N N   . PHE D 233 ? 0.2652 0.4805 0.2968 0.0483  -0.0252 -0.1008 233 PHE D N   
12941 C CA  . PHE D 233 ? 0.2468 0.4784 0.2809 0.0520  -0.0230 -0.1053 233 PHE D CA  
12942 C C   . PHE D 233 ? 0.2279 0.4556 0.2686 0.0562  -0.0264 -0.1136 233 PHE D C   
12943 O O   . PHE D 233 ? 0.1972 0.4366 0.2393 0.0595  -0.0273 -0.1184 233 PHE D O   
12944 C CB  . PHE D 233 ? 0.2218 0.4529 0.2531 0.0484  -0.0199 -0.0993 233 PHE D CB  
12945 C CG  . PHE D 233 ? 0.2205 0.4622 0.2458 0.0452  -0.0165 -0.0915 233 PHE D CG  
12946 C CD1 . PHE D 233 ? 0.2171 0.4769 0.2403 0.0464  -0.0153 -0.0910 233 PHE D CD1 
12947 C CD2 . PHE D 233 ? 0.2384 0.4691 0.2598 0.0401  -0.0157 -0.0829 233 PHE D CD2 
12948 C CE1 . PHE D 233 ? 0.2648 0.5346 0.2831 0.0434  -0.0126 -0.0828 233 PHE D CE1 
12949 C CE2 . PHE D 233 ? 0.2523 0.4925 0.2688 0.0373  -0.0131 -0.0751 233 PHE D CE2 
12950 C CZ  . PHE D 233 ? 0.2258 0.4872 0.2412 0.0393  -0.0110 -0.0753 233 PHE D CZ  
12951 N N   . ILE D 234 ? 0.2315 0.4406 0.2751 0.0553  -0.0293 -0.1140 234 ILE D N   
12952 C CA  . ILE D 234 ? 0.2414 0.4463 0.2921 0.0598  -0.0331 -0.1218 234 ILE D CA  
12953 C C   . ILE D 234 ? 0.3004 0.5123 0.3535 0.0637  -0.0361 -0.1283 234 ILE D C   
12954 O O   . ILE D 234 ? 0.2982 0.5180 0.3552 0.0683  -0.0383 -0.1350 234 ILE D O   
12955 C CB  . ILE D 234 ? 0.2732 0.4555 0.3254 0.0568  -0.0361 -0.1189 234 ILE D CB  
12956 C CG1 . ILE D 234 ? 0.1940 0.3711 0.2454 0.0546  -0.0339 -0.1147 234 ILE D CG1 
12957 C CG2 . ILE D 234 ? 0.2540 0.4307 0.3130 0.0611  -0.0412 -0.1260 234 ILE D CG2 
12958 C CD1 . ILE D 234 ? 0.2043 0.3601 0.2558 0.0509  -0.0362 -0.1098 234 ILE D CD1 
12959 N N   . LYS D 235 ? 0.2386 0.4456 0.2880 0.0610  -0.0370 -0.1254 235 LYS D N   
12960 C CA  . LYS D 235 ? 0.2836 0.4973 0.3345 0.0645  -0.0401 -0.1316 235 LYS D CA  
12961 C C   . LYS D 235 ? 0.2852 0.5227 0.3355 0.0688  -0.0377 -0.1351 235 LYS D C   
12962 O O   . LYS D 235 ? 0.2818 0.5286 0.3357 0.0740  -0.0405 -0.1429 235 LYS D O   
12963 C CB  . LYS D 235 ? 0.3073 0.5121 0.3542 0.0604  -0.0414 -0.1276 235 LYS D CB  
12964 C CG  . LYS D 235 ? 0.3186 0.5284 0.3672 0.0637  -0.0451 -0.1343 235 LYS D CG  
12965 C CD  . LYS D 235 ? 0.2614 0.4648 0.3060 0.0595  -0.0462 -0.1303 235 LYS D CD  
12966 C CE  . LYS D 235 ? 0.3650 0.5755 0.4107 0.0629  -0.0497 -0.1372 235 LYS D CE  
12967 N NZ  . LYS D 235 ? 0.4329 0.6343 0.4848 0.0653  -0.0550 -0.1442 235 LYS D NZ  
12968 N N   . ALA D 236 ? 0.2977 0.5459 0.3435 0.0666  -0.0328 -0.1293 236 ALA D N   
12969 C CA  . ALA D 236 ? 0.2702 0.5392 0.3132 0.0686  -0.0310 -0.1299 236 ALA D CA  
12970 C C   . ALA D 236 ? 0.3095 0.5864 0.3544 0.0707  -0.0313 -0.1331 236 ALA D C   
12971 O O   . ALA D 236 ? 0.2716 0.5659 0.3160 0.0739  -0.0316 -0.1364 236 ALA D O   
12972 C CB  . ALA D 236 ? 0.2848 0.5605 0.3212 0.0642  -0.0265 -0.1206 236 ALA D CB  
12973 N N   . ARG D 237 ? 0.2953 0.5608 0.3424 0.0692  -0.0316 -0.1324 237 ARG D N   
12974 C CA  . ARG D 237 ? 0.3086 0.5820 0.3570 0.0706  -0.0315 -0.1345 237 ARG D CA  
12975 C C   . ARG D 237 ? 0.2864 0.5500 0.3413 0.0739  -0.0357 -0.1412 237 ARG D C   
12976 O O   . ARG D 237 ? 0.2930 0.5656 0.3498 0.0765  -0.0365 -0.1450 237 ARG D O   
12977 C CB  . ARG D 237 ? 0.2602 0.5329 0.3045 0.0654  -0.0273 -0.1267 237 ARG D CB  
12978 C CG  . ARG D 237 ? 0.1899 0.4721 0.2280 0.0619  -0.0235 -0.1190 237 ARG D CG  
12979 C CD  . ARG D 237 ? 0.1977 0.4805 0.2322 0.0570  -0.0199 -0.1117 237 ARG D CD  
12980 N NE  . ARG D 237 ? 0.1778 0.4698 0.2068 0.0537  -0.0169 -0.1037 237 ARG D NE  
12981 C CZ  . ARG D 237 ? 0.2573 0.5480 0.2824 0.0488  -0.0139 -0.0958 237 ARG D CZ  
12982 N NH1 . ARG D 237 ? 0.1520 0.4327 0.1776 0.0467  -0.0134 -0.0952 237 ARG D NH1 
12983 N NH2 . ARG D 237 ? 0.2317 0.5317 0.2526 0.0462  -0.0117 -0.0883 237 ARG D NH2 
12984 N N   . ASP D 238 ? 0.2977 0.5439 0.3560 0.0741  -0.0386 -0.1425 238 ASP D N   
12985 C CA  . ASP D 238 ? 0.3080 0.5448 0.3727 0.0774  -0.0432 -0.1483 238 ASP D CA  
12986 C C   . ASP D 238 ? 0.3373 0.5770 0.4064 0.0827  -0.0480 -0.1564 238 ASP D C   
12987 O O   . ASP D 238 ? 0.2460 0.4782 0.3160 0.0824  -0.0494 -0.1565 238 ASP D O   
12988 C CB  . ASP D 238 ? 0.3012 0.5172 0.3675 0.0744  -0.0441 -0.1443 238 ASP D CB  
12989 C CG  . ASP D 238 ? 0.3700 0.5765 0.4424 0.0775  -0.0487 -0.1488 238 ASP D CG  
12990 O OD1 . ASP D 238 ? 0.3838 0.5955 0.4606 0.0826  -0.0529 -0.1563 238 ASP D OD1 
12991 O OD2 . ASP D 238 ? 0.3382 0.5321 0.4109 0.0749  -0.0484 -0.1447 238 ASP D OD2 
12992 N N   . PRO D 239 ? 0.3000 0.5507 0.3722 0.0879  -0.0508 -0.1636 239 PRO D N   
12993 C CA  . PRO D 239 ? 0.3072 0.5619 0.3837 0.0934  -0.0558 -0.1721 239 PRO D CA  
12994 C C   . PRO D 239 ? 0.3406 0.5769 0.4226 0.0943  -0.0608 -0.1745 239 PRO D C   
12995 O O   . PRO D 239 ? 0.3163 0.5528 0.4008 0.0970  -0.0639 -0.1791 239 PRO D O   
12996 C CB  . PRO D 239 ? 0.3441 0.6116 0.4233 0.0986  -0.0583 -0.1790 239 PRO D CB  
12997 C CG  . PRO D 239 ? 0.2673 0.5432 0.3423 0.0952  -0.0534 -0.1736 239 PRO D CG  
12998 C CD  . PRO D 239 ? 0.3218 0.5819 0.3944 0.0890  -0.0501 -0.1649 239 PRO D CD  
12999 N N   . LYS D 240 ? 0.3184 0.5393 0.4028 0.0924  -0.0619 -0.1716 240 LYS D N   
13000 C CA  . LYS D 240 ? 0.2950 0.4985 0.3847 0.0928  -0.0668 -0.1728 240 LYS D CA  
13001 C C   . LYS D 240 ? 0.3293 0.5239 0.4152 0.0879  -0.0655 -0.1680 240 LYS D C   
13002 O O   . LYS D 240 ? 0.3122 0.4920 0.3988 0.0862  -0.0700 -0.1684 240 LYS D O   
13003 C CB  . LYS D 240 ? 0.3457 0.5347 0.4368 0.0905  -0.0674 -0.1685 240 LYS D CB  
13004 C CG  . LYS D 240 ? 0.4037 0.5747 0.5004 0.0909  -0.0730 -0.1690 240 LYS D CG  
13005 C CD  . LYS D 240 ? 0.4688 0.6261 0.5656 0.0880  -0.0731 -0.1634 240 LYS D CD  
13006 C CE  . LYS D 240 ? 0.4630 0.6004 0.5623 0.0864  -0.0787 -0.1619 240 LYS D CE  
13007 N NZ  . LYS D 240 ? 0.5733 0.6998 0.6742 0.0854  -0.0796 -0.1576 240 LYS D NZ  
13008 N N   . TYR D 241 ? 0.2966 0.4979 0.3761 0.0841  -0.0597 -0.1621 241 TYR D N   
13009 C CA  . TYR D 241 ? 0.3475 0.5379 0.4210 0.0775  -0.0583 -0.1552 241 TYR D CA  
13010 C C   . TYR D 241 ? 0.3631 0.5664 0.4319 0.0774  -0.0563 -0.1557 241 TYR D C   
13011 O O   . TYR D 241 ? 0.3387 0.5355 0.4025 0.0722  -0.0549 -0.1498 241 TYR D O   
13012 C CB  . TYR D 241 ? 0.2802 0.4629 0.3498 0.0720  -0.0538 -0.1461 241 TYR D CB  
13013 C CG  . TYR D 241 ? 0.2918 0.4570 0.3645 0.0703  -0.0563 -0.1437 241 TYR D CG  
13014 C CD1 . TYR D 241 ? 0.3067 0.4543 0.3792 0.0663  -0.0596 -0.1406 241 TYR D CD1 
13015 C CD2 . TYR D 241 ? 0.3026 0.4698 0.3785 0.0727  -0.0553 -0.1443 241 TYR D CD2 
13016 C CE1 . TYR D 241 ? 0.2649 0.3974 0.3398 0.0647  -0.0619 -0.1378 241 TYR D CE1 
13017 C CE2 . TYR D 241 ? 0.2719 0.4232 0.3503 0.0714  -0.0579 -0.1418 241 TYR D CE2 
13018 C CZ  . TYR D 241 ? 0.2863 0.4204 0.3640 0.0674  -0.0612 -0.1384 241 TYR D CZ  
13019 O OH  . TYR D 241 ? 0.2775 0.3967 0.3573 0.0661  -0.0638 -0.1354 241 TYR D OH  
13020 N N   . LYS D 242 ? 0.3613 0.5836 0.4318 0.0833  -0.0564 -0.1624 242 LYS D N   
13021 C CA  . LYS D 242 ? 0.3610 0.5970 0.4267 0.0836  -0.0546 -0.1626 242 LYS D CA  
13022 C C   . LYS D 242 ? 0.3319 0.5583 0.3964 0.0821  -0.0588 -0.1644 242 LYS D C   
13023 O O   . LYS D 242 ? 0.3689 0.6009 0.4281 0.0802  -0.0572 -0.1619 242 LYS D O   
13024 C CB  . LYS D 242 ? 0.4398 0.6988 0.5081 0.0906  -0.0545 -0.1698 242 LYS D CB  
13025 C CG  . LYS D 242 ? 0.4922 0.7691 0.5546 0.0907  -0.0511 -0.1680 242 LYS D CG  
13026 C CD  . LYS D 242 ? 0.5474 0.8472 0.6113 0.0965  -0.0510 -0.1736 242 LYS D CD  
13027 C CE  . LYS D 242 ? 0.5807 0.8841 0.6506 0.1037  -0.0571 -0.1849 242 LYS D CE  
13028 N NZ  . LYS D 242 ? 0.6133 0.9379 0.6820 0.1084  -0.0574 -0.1896 242 LYS D NZ  
13029 N N   . ASN D 243 ? 0.3062 0.5184 0.3754 0.0827  -0.0643 -0.1684 243 ASN D N   
13030 C CA  . ASN D 243 ? 0.3251 0.5277 0.3941 0.0807  -0.0688 -0.1703 243 ASN D CA  
13031 C C   . ASN D 243 ? 0.3931 0.5757 0.4612 0.0734  -0.0694 -0.1629 243 ASN D C   
13032 O O   . ASN D 243 ? 0.4160 0.5892 0.4851 0.0711  -0.0736 -0.1642 243 ASN D O   
13033 C CB  . ASN D 243 ? 0.4917 0.6932 0.5668 0.0864  -0.0753 -0.1802 243 ASN D CB  
13034 C CG  . ASN D 243 ? 0.6077 0.8076 0.6822 0.0863  -0.0798 -0.1847 243 ASN D CG  
13035 O OD1 . ASN D 243 ? 0.6195 0.8344 0.6918 0.0900  -0.0797 -0.1892 243 ASN D OD1 
13036 N ND2 . ASN D 243 ? 0.5987 0.7810 0.6753 0.0820  -0.0840 -0.1835 243 ASN D ND2 
13037 N N   . ALA D 244 ? 0.3773 0.5540 0.4437 0.0697  -0.0655 -0.1555 244 ALA D N   
13038 C CA  . ALA D 244 ? 0.3722 0.5312 0.4379 0.0631  -0.0661 -0.1484 244 ALA D CA  
13039 C C   . ALA D 244 ? 0.3817 0.5420 0.4413 0.0579  -0.0621 -0.1407 244 ALA D C   
13040 O O   . ALA D 244 ? 0.3595 0.5326 0.4150 0.0589  -0.0578 -0.1387 244 ALA D O   
13041 C CB  . ALA D 244 ? 0.3675 0.5174 0.4353 0.0624  -0.0651 -0.1450 244 ALA D CB  
13042 N N   . THR D 245 ? 0.3407 0.4884 0.4000 0.0524  -0.0639 -0.1362 245 THR D N   
13043 C CA  . THR D 245 ? 0.3186 0.4666 0.3730 0.0474  -0.0608 -0.1286 245 THR D CA  
13044 C C   . THR D 245 ? 0.3273 0.4714 0.3791 0.0451  -0.0564 -0.1213 245 THR D C   
13045 O O   . THR D 245 ? 0.2907 0.4290 0.3450 0.0462  -0.0564 -0.1217 245 THR D O   
13046 C CB  . THR D 245 ? 0.3929 0.5298 0.4486 0.0422  -0.0641 -0.1260 245 THR D CB  
13047 O OG1 . THR D 245 ? 0.3010 0.4232 0.3595 0.0390  -0.0654 -0.1227 245 THR D OG1 
13048 C CG2 . THR D 245 ? 0.3843 0.5233 0.4433 0.0443  -0.0692 -0.1337 245 THR D CG2 
13049 N N   . ILE D 246 ? 0.2607 0.4082 0.3077 0.0420  -0.0530 -0.1148 246 ILE D N   
13050 C CA  . ILE D 246 ? 0.2918 0.4357 0.3361 0.0396  -0.0491 -0.1079 246 ILE D CA  
13051 C C   . ILE D 246 ? 0.2615 0.3890 0.3082 0.0356  -0.0508 -0.1040 246 ILE D C   
13052 O O   . ILE D 246 ? 0.2555 0.3776 0.3025 0.0355  -0.0494 -0.1017 246 ILE D O   
13053 C CB  . ILE D 246 ? 0.3003 0.4510 0.3391 0.0373  -0.0458 -0.1016 246 ILE D CB  
13054 C CG1 . ILE D 246 ? 0.2589 0.4271 0.2951 0.0415  -0.0437 -0.1050 246 ILE D CG1 
13055 C CG2 . ILE D 246 ? 0.2409 0.3859 0.2773 0.0343  -0.0425 -0.0942 246 ILE D CG2 
13056 C CD1 . ILE D 246 ? 0.2359 0.4117 0.2722 0.0446  -0.0409 -0.1067 246 ILE D CD1 
13057 N N   . LYS D 247 ? 0.2406 0.3606 0.2891 0.0324  -0.0539 -0.1032 247 LYS D N   
13058 C CA  . LYS D 247 ? 0.2939 0.3997 0.3447 0.0286  -0.0556 -0.0996 247 LYS D CA  
13059 C C   . LYS D 247 ? 0.3029 0.4021 0.3577 0.0313  -0.0580 -0.1040 247 LYS D C   
13060 O O   . LYS D 247 ? 0.3105 0.3999 0.3659 0.0296  -0.0578 -0.1004 247 LYS D O   
13061 C CB  . LYS D 247 ? 0.2918 0.3929 0.3446 0.0246  -0.0587 -0.0988 247 LYS D CB  
13062 C CG  . LYS D 247 ? 0.2534 0.3581 0.3030 0.0212  -0.0565 -0.0926 247 LYS D CG  
13063 C CD  . LYS D 247 ? 0.3515 0.4528 0.4043 0.0171  -0.0598 -0.0921 247 LYS D CD  
13064 C CE  . LYS D 247 ? 0.3273 0.4312 0.3779 0.0139  -0.0577 -0.0854 247 LYS D CE  
13065 N NZ  . LYS D 247 ? 0.3526 0.4561 0.4070 0.0103  -0.0610 -0.0855 247 LYS D NZ  
13066 N N   . GLU D 248 ? 0.2811 0.3858 0.3387 0.0359  -0.0605 -0.1118 248 GLU D N   
13067 C CA  . GLU D 248 ? 0.2714 0.3712 0.3333 0.0394  -0.0631 -0.1163 248 GLU D CA  
13068 C C   . GLU D 248 ? 0.2973 0.4003 0.3582 0.0420  -0.0597 -0.1150 248 GLU D C   
13069 O O   . GLU D 248 ? 0.3014 0.3958 0.3647 0.0425  -0.0610 -0.1144 248 GLU D O   
13070 C CB  . GLU D 248 ? 0.4016 0.5086 0.4669 0.0444  -0.0666 -0.1254 248 GLU D CB  
13071 C CG  . GLU D 248 ? 0.4799 0.5816 0.5475 0.0422  -0.0713 -0.1280 248 GLU D CG  
13072 C CD  . GLU D 248 ? 0.5231 0.6341 0.5931 0.0475  -0.0744 -0.1370 248 GLU D CD  
13073 O OE1 . GLU D 248 ? 0.4524 0.5775 0.5196 0.0505  -0.0715 -0.1390 248 GLU D OE1 
13074 O OE2 . GLU D 248 ? 0.5192 0.6238 0.5938 0.0487  -0.0798 -0.1422 248 GLU D OE2 
13075 N N   . VAL D 249 ? 0.2686 0.3843 0.3261 0.0436  -0.0556 -0.1146 249 VAL D N   
13076 C CA  . VAL D 249 ? 0.2538 0.3737 0.3103 0.0453  -0.0521 -0.1131 249 VAL D CA  
13077 C C   . VAL D 249 ? 0.2277 0.3362 0.2818 0.0406  -0.0504 -0.1050 249 VAL D C   
13078 O O   . VAL D 249 ? 0.2454 0.3493 0.3009 0.0416  -0.0502 -0.1042 249 VAL D O   
13079 C CB  . VAL D 249 ? 0.2416 0.3781 0.2944 0.0471  -0.0481 -0.1136 249 VAL D CB  
13080 C CG1 . VAL D 249 ? 0.2683 0.4094 0.3202 0.0481  -0.0445 -0.1117 249 VAL D CG1 
13081 C CG2 . VAL D 249 ? 0.2603 0.4092 0.3156 0.0524  -0.0499 -0.1220 249 VAL D CG2 
13082 N N   . ILE D 250 ? 0.2121 0.3165 0.2628 0.0358  -0.0495 -0.0992 250 ILE D N   
13083 C CA  . ILE D 250 ? 0.2218 0.3163 0.2703 0.0315  -0.0481 -0.0917 250 ILE D CA  
13084 C C   . ILE D 250 ? 0.2323 0.3133 0.2842 0.0307  -0.0514 -0.0916 250 ILE D C   
13085 O O   . ILE D 250 ? 0.2293 0.3040 0.2811 0.0304  -0.0507 -0.0887 250 ILE D O   
13086 C CB  . ILE D 250 ? 0.2352 0.3294 0.2805 0.0271  -0.0470 -0.0862 250 ILE D CB  
13087 C CG1 . ILE D 250 ? 0.2426 0.3496 0.2839 0.0280  -0.0437 -0.0851 250 ILE D CG1 
13088 C CG2 . ILE D 250 ? 0.1970 0.2807 0.2407 0.0231  -0.0462 -0.0792 250 ILE D CG2 
13089 C CD1 . ILE D 250 ? 0.2219 0.3297 0.2605 0.0245  -0.0431 -0.0801 250 ILE D CD1 
13090 N N   . PHE D 251 ? 0.2500 0.3267 0.3051 0.0303  -0.0553 -0.0948 251 PHE D N   
13091 C CA  . PHE D 251 ? 0.2477 0.3115 0.3058 0.0292  -0.0588 -0.0944 251 PHE D CA  
13092 C C   . PHE D 251 ? 0.2732 0.3350 0.3341 0.0336  -0.0599 -0.0973 251 PHE D C   
13093 O O   . PHE D 251 ? 0.2735 0.3254 0.3347 0.0325  -0.0609 -0.0941 251 PHE D O   
13094 C CB  . PHE D 251 ? 0.2547 0.3159 0.3162 0.0284  -0.0632 -0.0984 251 PHE D CB  
13095 C CG  . PHE D 251 ? 0.3356 0.3833 0.3993 0.0251  -0.0665 -0.0961 251 PHE D CG  
13096 C CD1 . PHE D 251 ? 0.3633 0.4059 0.4253 0.0193  -0.0658 -0.0903 251 PHE D CD1 
13097 C CD2 . PHE D 251 ? 0.3712 0.4120 0.4387 0.0278  -0.0706 -0.0997 251 PHE D CD2 
13098 C CE1 . PHE D 251 ? 0.3547 0.3858 0.4187 0.0160  -0.0687 -0.0882 251 PHE D CE1 
13099 C CE2 . PHE D 251 ? 0.4041 0.4324 0.4732 0.0246  -0.0738 -0.0973 251 PHE D CE2 
13100 C CZ  . PHE D 251 ? 0.4042 0.4277 0.4714 0.0185  -0.0727 -0.0915 251 PHE D CZ  
13101 N N   . ASP D 252 ? 0.2563 0.3283 0.3192 0.0388  -0.0600 -0.1036 252 ASP D N   
13102 C CA  . ASP D 252 ? 0.2411 0.3137 0.3074 0.0435  -0.0610 -0.1069 252 ASP D CA  
13103 C C   . ASP D 252 ? 0.1962 0.2698 0.2597 0.0428  -0.0570 -0.1023 252 ASP D C   
13104 O O   . ASP D 252 ? 0.2262 0.2932 0.2915 0.0440  -0.0583 -0.1013 252 ASP D O   
13105 C CB  . ASP D 252 ? 0.2857 0.3712 0.3553 0.0495  -0.0619 -0.1153 252 ASP D CB  
13106 C CG  . ASP D 252 ? 0.2968 0.3793 0.3708 0.0517  -0.0674 -0.1212 252 ASP D CG  
13107 O OD1 . ASP D 252 ? 0.3102 0.3799 0.3847 0.0483  -0.0706 -0.1186 252 ASP D OD1 
13108 O OD2 . ASP D 252 ? 0.3856 0.4787 0.4625 0.0568  -0.0687 -0.1285 252 ASP D OD2 
13109 N N   . MET D 253 ? 0.2370 0.3189 0.2961 0.0410  -0.0525 -0.0995 253 MET D N   
13110 C CA  . MET D 253 ? 0.2119 0.2946 0.2680 0.0398  -0.0489 -0.0951 253 MET D CA  
13111 C C   . MET D 253 ? 0.2291 0.2977 0.2843 0.0366  -0.0498 -0.0891 253 MET D C   
13112 O O   . MET D 253 ? 0.2310 0.2970 0.2865 0.0375  -0.0492 -0.0878 253 MET D O   
13113 C CB  . MET D 253 ? 0.2009 0.2917 0.2517 0.0369  -0.0448 -0.0913 253 MET D CB  
13114 C CG  . MET D 253 ? 0.2406 0.3479 0.2910 0.0401  -0.0422 -0.0955 253 MET D CG  
13115 S SD  . MET D 253 ? 0.2129 0.3290 0.2569 0.0367  -0.0386 -0.0907 253 MET D SD  
13116 C CE  . MET D 253 ? 0.1892 0.2978 0.2294 0.0323  -0.0362 -0.0819 253 MET D CE  
13117 N N   . TYR D 254 ? 0.2179 0.2780 0.2720 0.0329  -0.0513 -0.0858 254 TYR D N   
13118 C CA  . TYR D 254 ? 0.2014 0.2499 0.2537 0.0295  -0.0516 -0.0797 254 TYR D CA  
13119 C C   . TYR D 254 ? 0.2233 0.2617 0.2791 0.0310  -0.0559 -0.0810 254 TYR D C   
13120 O O   . TYR D 254 ? 0.2396 0.2682 0.2938 0.0285  -0.0565 -0.0763 254 TYR D O   
13121 C CB  . TYR D 254 ? 0.2203 0.2664 0.2695 0.0246  -0.0506 -0.0751 254 TYR D CB  
13122 C CG  . TYR D 254 ? 0.2080 0.2618 0.2531 0.0232  -0.0466 -0.0718 254 TYR D CG  
13123 C CD1 . TYR D 254 ? 0.1934 0.2590 0.2378 0.0246  -0.0450 -0.0746 254 TYR D CD1 
13124 C CD2 . TYR D 254 ? 0.2062 0.2560 0.2482 0.0209  -0.0445 -0.0660 254 TYR D CD2 
13125 C CE1 . TYR D 254 ? 0.1651 0.2378 0.2057 0.0234  -0.0417 -0.0712 254 TYR D CE1 
13126 C CE2 . TYR D 254 ? 0.1821 0.2386 0.2206 0.0197  -0.0414 -0.0629 254 TYR D CE2 
13127 C CZ  . TYR D 254 ? 0.2180 0.2858 0.2558 0.0209  -0.0400 -0.0652 254 TYR D CZ  
13128 O OH  . TYR D 254 ? 0.2100 0.2842 0.2443 0.0196  -0.0373 -0.0615 254 TYR D OH  
13129 N N   . LYS D 255 ? 0.2352 0.2760 0.2955 0.0351  -0.0590 -0.0874 255 LYS D N   
13130 C CA  . LYS D 255 ? 0.2787 0.3114 0.3425 0.0377  -0.0633 -0.0888 255 LYS D CA  
13131 C C   . LYS D 255 ? 0.2459 0.2797 0.3100 0.0403  -0.0621 -0.0878 255 LYS D C   
13132 O O   . LYS D 255 ? 0.2549 0.2809 0.3208 0.0417  -0.0653 -0.0870 255 LYS D O   
13133 C CB  . LYS D 255 ? 0.2291 0.2654 0.2982 0.0422  -0.0673 -0.0963 255 LYS D CB  
13134 C CG  . LYS D 255 ? 0.2291 0.2647 0.2986 0.0400  -0.0692 -0.0983 255 LYS D CG  
13135 C CD  . LYS D 255 ? 0.3509 0.3927 0.4255 0.0453  -0.0727 -0.1067 255 LYS D CD  
13136 C CE  . LYS D 255 ? 0.3399 0.3776 0.4158 0.0433  -0.0763 -0.1090 255 LYS D CE  
13137 N NZ  . LYS D 255 ? 0.4444 0.4673 0.5210 0.0402  -0.0803 -0.1058 255 LYS D NZ  
13138 N N   . TYR D 256 ? 0.2224 0.2655 0.2846 0.0407  -0.0577 -0.0878 256 TYR D N   
13139 C CA  . TYR D 256 ? 0.2132 0.2594 0.2763 0.0432  -0.0565 -0.0881 256 TYR D CA  
13140 C C   . TYR D 256 ? 0.2385 0.2807 0.2965 0.0391  -0.0531 -0.0812 256 TYR D C   
13141 O O   . TYR D 256 ? 0.2128 0.2606 0.2698 0.0397  -0.0504 -0.0812 256 TYR D O   
13142 C CB  . TYR D 256 ? 0.2535 0.3146 0.3189 0.0470  -0.0544 -0.0943 256 TYR D CB  
13143 C CG  . TYR D 256 ? 0.2803 0.3456 0.3508 0.0513  -0.0581 -0.1014 256 TYR D CG  
13144 C CD1 . TYR D 256 ? 0.2792 0.3367 0.3544 0.0541  -0.0636 -0.1035 256 TYR D CD1 
13145 C CD2 . TYR D 256 ? 0.2691 0.3458 0.3397 0.0524  -0.0567 -0.1057 256 TYR D CD2 
13146 C CE1 . TYR D 256 ? 0.2891 0.3497 0.3690 0.0580  -0.0677 -0.1099 256 TYR D CE1 
13147 C CE2 . TYR D 256 ? 0.3216 0.4019 0.3970 0.0565  -0.0605 -0.1125 256 TYR D CE2 
13148 C CZ  . TYR D 256 ? 0.3017 0.3736 0.3819 0.0593  -0.0661 -0.1146 256 TYR D CZ  
13149 O OH  . TYR D 256 ? 0.3921 0.4669 0.4770 0.0634  -0.0706 -0.1215 256 TYR D OH  
13150 N N   . ALA D 257 ? 0.1770 0.2098 0.2316 0.0350  -0.0534 -0.0758 257 ALA D N   
13151 C CA  . ALA D 257 ? 0.1640 0.1916 0.2143 0.0316  -0.0512 -0.0694 257 ALA D CA  
13152 C C   . ALA D 257 ? 0.2312 0.2469 0.2802 0.0292  -0.0538 -0.0655 257 ALA D C   
13153 O O   . ALA D 257 ? 0.2251 0.2376 0.2759 0.0289  -0.0565 -0.0671 257 ALA D O   
13154 C CB  . ALA D 257 ? 0.1893 0.2232 0.2354 0.0282  -0.0472 -0.0667 257 ALA D CB  
13155 N N   . ASP D 258 ? 0.2083 0.2176 0.2541 0.0276  -0.0531 -0.0605 258 ASP D N   
13156 C CA  . ASP D 258 ? 0.2028 0.2017 0.2466 0.0252  -0.0552 -0.0564 258 ASP D CA  
13157 C C   . ASP D 258 ? 0.2321 0.2302 0.2719 0.0209  -0.0525 -0.0522 258 ASP D C   
13158 O O   . ASP D 258 ? 0.2413 0.2322 0.2797 0.0185  -0.0540 -0.0494 258 ASP D O   
13159 C CB  . ASP D 258 ? 0.2232 0.2155 0.2660 0.0268  -0.0569 -0.0538 258 ASP D CB  
13160 C CG  . ASP D 258 ? 0.2362 0.2296 0.2835 0.0314  -0.0602 -0.0579 258 ASP D CG  
13161 O OD1 . ASP D 258 ? 0.2875 0.2789 0.3377 0.0326  -0.0636 -0.0608 258 ASP D OD1 
13162 O OD2 . ASP D 258 ? 0.2141 0.2106 0.2625 0.0338  -0.0596 -0.0587 258 ASP D OD2 
13163 N N   . ALA D 259 ? 0.2204 0.2261 0.2585 0.0200  -0.0490 -0.0517 259 ALA D N   
13164 C CA  . ALA D 259 ? 0.1944 0.2010 0.2291 0.0166  -0.0466 -0.0478 259 ALA D CA  
13165 C C   . ALA D 259 ? 0.1834 0.2006 0.2174 0.0165  -0.0436 -0.0487 259 ALA D C   
13166 O O   . ALA D 259 ? 0.1576 0.1806 0.1933 0.0189  -0.0432 -0.0519 259 ALA D O   
13167 C CB  . ALA D 259 ? 0.2040 0.2035 0.2355 0.0159  -0.0464 -0.0433 259 ALA D CB  
13168 N N   . LEU D 260 ? 0.1841 0.2044 0.2157 0.0138  -0.0419 -0.0457 260 LEU D N   
13169 C CA  . LEU D 260 ? 0.1856 0.2156 0.2158 0.0134  -0.0394 -0.0452 260 LEU D CA  
13170 C C   . LEU D 260 ? 0.1849 0.2143 0.2119 0.0113  -0.0380 -0.0400 260 LEU D C   
13171 O O   . LEU D 260 ? 0.1710 0.1948 0.1972 0.0098  -0.0387 -0.0377 260 LEU D O   
13172 C CB  . LEU D 260 ? 0.1834 0.2212 0.2149 0.0132  -0.0394 -0.0478 260 LEU D CB  
13173 C CG  . LEU D 260 ? 0.1670 0.2042 0.1988 0.0107  -0.0401 -0.0462 260 LEU D CG  
13174 C CD1 . LEU D 260 ? 0.1631 0.2052 0.1924 0.0090  -0.0382 -0.0419 260 LEU D CD1 
13175 C CD2 . LEU D 260 ? 0.1917 0.2333 0.2263 0.0113  -0.0415 -0.0506 260 LEU D CD2 
13176 N N   . THR D 261 ? 0.1755 0.2107 0.2009 0.0113  -0.0363 -0.0385 261 THR D N   
13177 C CA  . THR D 261 ? 0.1724 0.2094 0.1952 0.0097  -0.0351 -0.0338 261 THR D CA  
13178 C C   . THR D 261 ? 0.1858 0.2335 0.2085 0.0095  -0.0339 -0.0335 261 THR D C   
13179 O O   . THR D 261 ? 0.2423 0.2964 0.2657 0.0106  -0.0332 -0.0359 261 THR D O   
13180 C CB  . THR D 261 ? 0.1554 0.1892 0.1766 0.0098  -0.0348 -0.0314 261 THR D CB  
13181 O OG1 . THR D 261 ? 0.2346 0.2741 0.2569 0.0106  -0.0343 -0.0333 261 THR D OG1 
13182 C CG2 . THR D 261 ? 0.2006 0.2234 0.2214 0.0106  -0.0362 -0.0316 261 THR D CG2 
13183 N N   . MET D 262 ? 0.1473 0.1976 0.1693 0.0084  -0.0336 -0.0309 262 MET D N   
13184 C CA  . MET D 262 ? 0.1835 0.2434 0.2053 0.0086  -0.0328 -0.0307 262 MET D CA  
13185 C C   . MET D 262 ? 0.1737 0.2360 0.1936 0.0081  -0.0321 -0.0255 262 MET D C   
13186 O O   . MET D 262 ? 0.1868 0.2447 0.2065 0.0075  -0.0326 -0.0229 262 MET D O   
13187 C CB  . MET D 262 ? 0.1662 0.2280 0.1899 0.0085  -0.0337 -0.0337 262 MET D CB  
13188 C CG  . MET D 262 ? 0.2200 0.2916 0.2433 0.0090  -0.0329 -0.0337 262 MET D CG  
13189 S SD  . MET D 262 ? 0.2767 0.3498 0.3028 0.0086  -0.0346 -0.0373 262 MET D SD  
13190 C CE  . MET D 262 ? 0.2583 0.3281 0.2866 0.0100  -0.0359 -0.0436 262 MET D CE  
13191 N N   . SER D 263 ? 0.1634 0.2332 0.1820 0.0087  -0.0310 -0.0241 263 SER D N   
13192 C CA  . SER D 263 ? 0.1498 0.2236 0.1667 0.0088  -0.0305 -0.0197 263 SER D CA  
13193 C C   . SER D 263 ? 0.1612 0.2424 0.1784 0.0095  -0.0301 -0.0215 263 SER D C   
13194 O O   . SER D 263 ? 0.1598 0.2487 0.1765 0.0103  -0.0294 -0.0241 263 SER D O   
13195 C CB  . SER D 263 ? 0.1853 0.2636 0.2005 0.0090  -0.0297 -0.0166 263 SER D CB  
13196 O OG  . SER D 263 ? 0.1965 0.2795 0.2096 0.0096  -0.0291 -0.0125 263 SER D OG  
13197 N N   . ALA D 264 ? 0.1351 0.2149 0.1533 0.0092  -0.0308 -0.0204 264 ALA D N   
13198 C CA  . ALA D 264 ? 0.1322 0.2191 0.1510 0.0097  -0.0308 -0.0219 264 ALA D CA  
13199 C C   . ALA D 264 ? 0.1525 0.2471 0.1685 0.0110  -0.0297 -0.0185 264 ALA D C   
13200 O O   . ALA D 264 ? 0.1914 0.2926 0.2073 0.0117  -0.0299 -0.0196 264 ALA D O   
13201 C CB  . ALA D 264 ? 0.1891 0.2730 0.2107 0.0088  -0.0320 -0.0217 264 ALA D CB  
13202 N N   . LYS D 265 ? 0.1574 0.2513 0.1710 0.0113  -0.0290 -0.0144 265 LYS D N   
13203 C CA  . LYS D 265 ? 0.1392 0.2404 0.1497 0.0124  -0.0280 -0.0105 265 LYS D CA  
13204 C C   . LYS D 265 ? 0.1288 0.2399 0.1376 0.0128  -0.0269 -0.0126 265 LYS D C   
13205 O O   . LYS D 265 ? 0.1477 0.2664 0.1536 0.0136  -0.0260 -0.0091 265 LYS D O   
13206 C CB  . LYS D 265 ? 0.1305 0.2271 0.1392 0.0123  -0.0279 -0.0050 265 LYS D CB  
13207 C CG  . LYS D 265 ? 0.1293 0.2167 0.1393 0.0126  -0.0289 -0.0032 265 LYS D CG  
13208 C CD  . LYS D 265 ? 0.2184 0.2998 0.2266 0.0127  -0.0293 0.0011  265 LYS D CD  
13209 C CE  . LYS D 265 ? 0.1865 0.2714 0.1914 0.0139  -0.0289 0.0068  265 LYS D CE  
13210 N NZ  . LYS D 265 ? 0.1863 0.2629 0.1896 0.0141  -0.0299 0.0111  265 LYS D NZ  
13211 N N   . LYS D 266 ? 0.1647 0.2762 0.1753 0.0126  -0.0269 -0.0180 266 LYS D N   
13212 C CA  . LYS D 266 ? 0.1612 0.2832 0.1705 0.0135  -0.0257 -0.0212 266 LYS D CA  
13213 C C   . LYS D 266 ? 0.1560 0.2819 0.1665 0.0147  -0.0265 -0.0267 266 LYS D C   
13214 O O   . LYS D 266 ? 0.1990 0.3291 0.2086 0.0154  -0.0269 -0.0258 266 LYS D O   
13215 C CB  . LYS D 266 ? 0.1940 0.3148 0.2046 0.0131  -0.0252 -0.0237 266 LYS D CB  
13216 C CG  . LYS D 266 ? 0.1594 0.2812 0.1687 0.0120  -0.0244 -0.0188 266 LYS D CG  
13217 C CD  . LYS D 266 ? 0.1935 0.3049 0.2029 0.0109  -0.0255 -0.0137 266 LYS D CD  
13218 C CE  . LYS D 266 ? 0.2600 0.3680 0.2699 0.0096  -0.0258 -0.0109 266 LYS D CE  
13219 N NZ  . LYS D 266 ? 0.2955 0.3922 0.3057 0.0092  -0.0273 -0.0074 266 LYS D NZ  
13220 N N   . ASP D 267 ? 0.1823 0.3067 0.1951 0.0151  -0.0270 -0.0326 267 ASP D N   
13221 C CA  . ASP D 267 ? 0.1912 0.3201 0.2053 0.0165  -0.0280 -0.0383 267 ASP D CA  
13222 C C   . ASP D 267 ? 0.1846 0.3088 0.2008 0.0156  -0.0300 -0.0385 267 ASP D C   
13223 O O   . ASP D 267 ? 0.1971 0.3276 0.2136 0.0168  -0.0310 -0.0418 267 ASP D O   
13224 C CB  . ASP D 267 ? 0.2190 0.3457 0.2357 0.0174  -0.0285 -0.0445 267 ASP D CB  
13225 C CG  . ASP D 267 ? 0.2200 0.3578 0.2352 0.0194  -0.0266 -0.0470 267 ASP D CG  
13226 O OD1 . ASP D 267 ? 0.2685 0.4144 0.2805 0.0192  -0.0246 -0.0427 267 ASP D OD1 
13227 O OD2 . ASP D 267 ? 0.2545 0.3937 0.2719 0.0212  -0.0270 -0.0531 267 ASP D OD2 
13228 N N   . PRO D 268 ? 0.1691 0.2835 0.1872 0.0137  -0.0309 -0.0355 268 PRO D N   
13229 C CA  . PRO D 268 ? 0.1800 0.2927 0.2004 0.0127  -0.0326 -0.0351 268 PRO D CA  
13230 C C   . PRO D 268 ? 0.1491 0.2682 0.1675 0.0135  -0.0321 -0.0312 268 PRO D C   
13231 O O   . PRO D 268 ? 0.1484 0.2669 0.1692 0.0128  -0.0335 -0.0306 268 PRO D O   
13232 C CB  . PRO D 268 ? 0.1714 0.2734 0.1940 0.0107  -0.0332 -0.0327 268 PRO D CB  
13233 C CG  . PRO D 268 ? 0.1299 0.2272 0.1525 0.0108  -0.0329 -0.0350 268 PRO D CG  
13234 C CD  . PRO D 268 ? 0.1752 0.2797 0.1944 0.0124  -0.0310 -0.0345 268 PRO D CD  
13235 N N   . LEU D 269 ? 0.1611 0.2863 0.1754 0.0148  -0.0304 -0.0281 269 LEU D N   
13236 C CA  . LEU D 269 ? 0.1340 0.2668 0.1460 0.0162  -0.0301 -0.0249 269 LEU D CA  
13237 C C   . LEU D 269 ? 0.1446 0.2726 0.1573 0.0158  -0.0305 -0.0198 269 LEU D C   
13238 O O   . LEU D 269 ? 0.1822 0.3143 0.1952 0.0166  -0.0313 -0.0187 269 LEU D O   
13239 C CB  . LEU D 269 ? 0.1623 0.3022 0.1751 0.0172  -0.0316 -0.0294 269 LEU D CB  
13240 C CG  . LEU D 269 ? 0.1681 0.3160 0.1794 0.0187  -0.0313 -0.0346 269 LEU D CG  
13241 C CD1 . LEU D 269 ? 0.2181 0.3690 0.2322 0.0193  -0.0337 -0.0403 269 LEU D CD1 
13242 C CD2 . LEU D 269 ? 0.1559 0.3144 0.1624 0.0206  -0.0295 -0.0313 269 LEU D CD2 
13243 N N   . LEU D 270 ? 0.1866 0.3064 0.1996 0.0148  -0.0299 -0.0168 270 LEU D N   
13244 C CA  . LEU D 270 ? 0.1506 0.2659 0.1646 0.0150  -0.0302 -0.0125 270 LEU D CA  
13245 C C   . LEU D 270 ? 0.1383 0.2529 0.1486 0.0160  -0.0291 -0.0067 270 LEU D C   
13246 O O   . LEU D 270 ? 0.1751 0.2920 0.1826 0.0160  -0.0281 -0.0056 270 LEU D O   
13247 C CB  . LEU D 270 ? 0.1198 0.2262 0.1373 0.0133  -0.0308 -0.0136 270 LEU D CB  
13248 C CG  . LEU D 270 ? 0.1807 0.2860 0.2024 0.0117  -0.0322 -0.0185 270 LEU D CG  
13249 C CD1 . LEU D 270 ? 0.1843 0.2814 0.2089 0.0102  -0.0326 -0.0179 270 LEU D CD1 
13250 C CD2 . LEU D 270 ? 0.1453 0.2573 0.1692 0.0121  -0.0334 -0.0195 270 LEU D CD2 
13251 N N   . ASN D 271 ? 0.1281 0.2396 0.1386 0.0171  -0.0293 -0.0028 271 ASN D N   
13252 C CA  . ASN D 271 ? 0.1473 0.2555 0.1548 0.0182  -0.0288 0.0029  271 ASN D CA  
13253 C C   . ASN D 271 ? 0.1703 0.2685 0.1786 0.0177  -0.0289 0.0041  271 ASN D C   
13254 O O   . ASN D 271 ? 0.1679 0.2617 0.1737 0.0184  -0.0289 0.0085  271 ASN D O   
13255 C CB  . ASN D 271 ? 0.1521 0.2630 0.1586 0.0206  -0.0293 0.0066  271 ASN D CB  
13256 C CG  . ASN D 271 ? 0.1819 0.3026 0.1878 0.0214  -0.0297 0.0050  271 ASN D CG  
13257 O OD1 . ASN D 271 ? 0.1582 0.2821 0.1669 0.0222  -0.0306 0.0033  271 ASN D OD1 
13258 N ND2 . ASN D 271 ? 0.1679 0.2944 0.1706 0.0212  -0.0291 0.0053  271 ASN D ND2 
13259 N N   . ILE D 272 ? 0.1520 0.2466 0.1639 0.0164  -0.0293 0.0005  272 ILE D N   
13260 C CA  . ILE D 272 ? 0.1375 0.2233 0.1500 0.0160  -0.0295 0.0010  272 ILE D CA  
13261 C C   . ILE D 272 ? 0.1604 0.2448 0.1766 0.0140  -0.0301 -0.0038 272 ILE D C   
13262 O O   . ILE D 272 ? 0.1532 0.2427 0.1718 0.0133  -0.0304 -0.0067 272 ILE D O   
13263 C CB  . ILE D 272 ? 0.1196 0.2017 0.1318 0.0183  -0.0295 0.0047  272 ILE D CB  
13264 C CG1 . ILE D 272 ? 0.1748 0.2476 0.1862 0.0185  -0.0297 0.0059  272 ILE D CG1 
13265 C CG2 . ILE D 272 ? 0.1549 0.2414 0.1711 0.0186  -0.0295 0.0030  272 ILE D CG2 
13266 C CD1 . ILE D 272 ? 0.1713 0.2389 0.1791 0.0182  -0.0301 0.0084  272 ILE D CD1 
13267 N N   . GLY D 273 ? 0.1507 0.2280 0.1672 0.0130  -0.0305 -0.0047 273 GLY D N   
13268 C CA  . GLY D 273 ? 0.1392 0.2139 0.1589 0.0112  -0.0313 -0.0086 273 GLY D CA  
13269 C C   . GLY D 273 ? 0.1592 0.2297 0.1783 0.0098  -0.0316 -0.0114 273 GLY D C   
13270 O O   . GLY D 273 ? 0.1712 0.2438 0.1885 0.0099  -0.0311 -0.0116 273 GLY D O   
13271 N N   . GLY D 274 ? 0.1651 0.2300 0.1860 0.0085  -0.0325 -0.0136 274 GLY D N   
13272 C CA  . GLY D 274 ? 0.1499 0.2097 0.1703 0.0076  -0.0329 -0.0165 274 GLY D CA  
13273 C C   . GLY D 274 ? 0.1475 0.2030 0.1705 0.0063  -0.0341 -0.0195 274 GLY D C   
13274 O O   . GLY D 274 ? 0.1233 0.1801 0.1487 0.0057  -0.0347 -0.0191 274 GLY D O   
13275 N N   . LEU D 275 ? 0.1227 0.1732 0.1455 0.0059  -0.0346 -0.0226 275 LEU D N   
13276 C CA  . LEU D 275 ? 0.1384 0.1840 0.1635 0.0047  -0.0360 -0.0257 275 LEU D CA  
13277 C C   . LEU D 275 ? 0.1402 0.1776 0.1641 0.0053  -0.0365 -0.0276 275 LEU D C   
13278 O O   . LEU D 275 ? 0.1661 0.2048 0.1889 0.0064  -0.0357 -0.0286 275 LEU D O   
13279 C CB  . LEU D 275 ? 0.1483 0.1990 0.1761 0.0041  -0.0366 -0.0291 275 LEU D CB  
13280 C CG  . LEU D 275 ? 0.1287 0.1747 0.1597 0.0025  -0.0387 -0.0322 275 LEU D CG  
13281 C CD1 . LEU D 275 ? 0.1653 0.2115 0.1989 0.0005  -0.0395 -0.0300 275 LEU D CD1 
13282 C CD2 . LEU D 275 ? 0.1221 0.1726 0.1552 0.0026  -0.0396 -0.0363 275 LEU D CD2 
13283 N N   . VAL D 276 ? 0.1402 0.1696 0.1648 0.0048  -0.0380 -0.0281 276 VAL D N   
13284 C CA  . VAL D 276 ? 0.1892 0.2102 0.2137 0.0055  -0.0392 -0.0305 276 VAL D CA  
13285 C C   . VAL D 276 ? 0.1799 0.1990 0.2077 0.0042  -0.0410 -0.0333 276 VAL D C   
13286 O O   . VAL D 276 ? 0.1870 0.2068 0.2168 0.0020  -0.0419 -0.0324 276 VAL D O   
13287 C CB  . VAL D 276 ? 0.1707 0.1819 0.1925 0.0062  -0.0401 -0.0283 276 VAL D CB  
13288 C CG1 . VAL D 276 ? 0.1752 0.1779 0.1971 0.0073  -0.0416 -0.0303 276 VAL D CG1 
13289 C CG2 . VAL D 276 ? 0.1669 0.1793 0.1856 0.0074  -0.0388 -0.0258 276 VAL D CG2 
13290 N N   . ALA D 277 ? 0.1683 0.1856 0.1973 0.0055  -0.0418 -0.0366 277 ALA D N   
13291 C CA  . ALA D 277 ? 0.1856 0.1995 0.2178 0.0046  -0.0441 -0.0393 277 ALA D CA  
13292 C C   . ALA D 277 ? 0.2265 0.2327 0.2588 0.0069  -0.0457 -0.0410 277 ALA D C   
13293 O O   . ALA D 277 ? 0.2214 0.2295 0.2530 0.0095  -0.0448 -0.0422 277 ALA D O   
13294 C CB  . ALA D 277 ? 0.1733 0.1955 0.2079 0.0045  -0.0442 -0.0424 277 ALA D CB  
13295 N N   . ILE D 278 ? 0.1921 0.1899 0.2256 0.0058  -0.0483 -0.0409 278 ILE D N   
13296 C CA  . ILE D 278 ? 0.1767 0.1666 0.2101 0.0080  -0.0505 -0.0415 278 ILE D CA  
13297 C C   . ILE D 278 ? 0.2264 0.2136 0.2635 0.0075  -0.0535 -0.0445 278 ILE D C   
13298 O O   . ILE D 278 ? 0.2210 0.2065 0.2595 0.0041  -0.0546 -0.0440 278 ILE D O   
13299 C CB  . ILE D 278 ? 0.1928 0.1733 0.2229 0.0073  -0.0513 -0.0374 278 ILE D CB  
13300 C CG1 . ILE D 278 ? 0.1759 0.1587 0.2025 0.0083  -0.0488 -0.0349 278 ILE D CG1 
13301 C CG2 . ILE D 278 ? 0.2666 0.2393 0.2965 0.0095  -0.0542 -0.0376 278 ILE D CG2 
13302 C CD1 . ILE D 278 ? 0.2531 0.2269 0.2755 0.0077  -0.0497 -0.0310 278 ILE D CD1 
13303 N N   . ARG D 279 ? 0.1892 0.1761 0.2282 0.0109  -0.0552 -0.0478 279 ARG D N   
13304 C CA  . ARG D 279 ? 0.2546 0.2397 0.2973 0.0110  -0.0584 -0.0514 279 ARG D CA  
13305 C C   . ARG D 279 ? 0.2957 0.2698 0.3382 0.0082  -0.0615 -0.0490 279 ARG D C   
13306 O O   . ARG D 279 ? 0.3359 0.3087 0.3804 0.0045  -0.0625 -0.0491 279 ARG D O   
13307 C CB  . ARG D 279 ? 0.2583 0.2454 0.3036 0.0157  -0.0602 -0.0557 279 ARG D CB  
13308 C CG  . ARG D 279 ? 0.3263 0.3122 0.3757 0.0161  -0.0638 -0.0601 279 ARG D CG  
13309 C CD  . ARG D 279 ? 0.4299 0.4151 0.4823 0.0211  -0.0670 -0.0641 279 ARG D CD  
13310 N NE  . ARG D 279 ? 0.4743 0.4702 0.5283 0.0250  -0.0649 -0.0679 279 ARG D NE  
13311 C CZ  . ARG D 279 ? 0.4493 0.4478 0.5067 0.0299  -0.0671 -0.0723 279 ARG D CZ  
13312 N NH1 . ARG D 279 ? 0.4822 0.4735 0.5421 0.0319  -0.0720 -0.0736 279 ARG D NH1 
13313 N NH2 . ARG D 279 ? 0.3681 0.3771 0.4267 0.0329  -0.0646 -0.0757 279 ARG D NH2 
13314 N N   . ASP D 280 ? 0.2833 0.2497 0.3235 0.0096  -0.0631 -0.0466 280 ASP D N   
13315 C CA  . ASP D 280 ? 0.3101 0.2656 0.3494 0.0070  -0.0661 -0.0440 280 ASP D CA  
13316 C C   . ASP D 280 ? 0.3388 0.2868 0.3730 0.0074  -0.0665 -0.0396 280 ASP D C   
13317 O O   . ASP D 280 ? 0.3535 0.2919 0.3861 0.0058  -0.0694 -0.0375 280 ASP D O   
13318 C CB  . ASP D 280 ? 0.3835 0.3353 0.4263 0.0086  -0.0705 -0.0477 280 ASP D CB  
13319 C CG  . ASP D 280 ? 0.4141 0.3679 0.4578 0.0143  -0.0721 -0.0503 280 ASP D CG  
13320 O OD1 . ASP D 280 ? 0.3656 0.3202 0.4063 0.0162  -0.0707 -0.0480 280 ASP D OD1 
13321 O OD2 . ASP D 280 ? 0.4103 0.3652 0.4580 0.0168  -0.0752 -0.0549 280 ASP D OD2 
13322 N N   . ASN D 281 ? 0.3050 0.2566 0.3362 0.0094  -0.0639 -0.0380 281 ASN D N   
13323 C CA  . ASN D 281 ? 0.3069 0.2519 0.3328 0.0099  -0.0646 -0.0340 281 ASN D CA  
13324 C C   . ASN D 281 ? 0.3213 0.2625 0.3433 0.0060  -0.0626 -0.0298 281 ASN D C   
13325 O O   . ASN D 281 ? 0.2777 0.2237 0.2984 0.0061  -0.0597 -0.0288 281 ASN D O   
13326 C CB  . ASN D 281 ? 0.3146 0.2651 0.3398 0.0139  -0.0633 -0.0345 281 ASN D CB  
13327 C CG  . ASN D 281 ? 0.3652 0.3093 0.3856 0.0153  -0.0653 -0.0315 281 ASN D CG  
13328 O OD1 . ASN D 281 ? 0.3279 0.2648 0.3430 0.0129  -0.0655 -0.0278 281 ASN D OD1 
13329 N ND2 . ASN D 281 ? 0.3488 0.2958 0.3709 0.0192  -0.0669 -0.0333 281 ASN D ND2 
13330 N N   . GLU D 282 ? 0.3317 0.2638 0.3522 0.0026  -0.0644 -0.0273 282 GLU D N   
13331 C CA  . GLU D 282 ? 0.3272 0.2549 0.3443 -0.0013 -0.0626 -0.0232 282 GLU D CA  
13332 C C   . GLU D 282 ? 0.3053 0.2303 0.3152 0.0006  -0.0613 -0.0200 282 GLU D C   
13333 O O   . GLU D 282 ? 0.2957 0.2214 0.3032 -0.0008 -0.0589 -0.0179 282 GLU D O   
13334 C CB  . GLU D 282 ? 0.3427 0.2602 0.3592 -0.0056 -0.0645 -0.0204 282 GLU D CB  
13335 C CG  . GLU D 282 ? 0.4264 0.3391 0.4399 -0.0101 -0.0623 -0.0153 282 GLU D CG  
13336 C CD  . GLU D 282 ? 0.4920 0.3930 0.5030 -0.0141 -0.0634 -0.0107 282 GLU D CD  
13337 O OE1 . GLU D 282 ? 0.5425 0.4420 0.5591 -0.0176 -0.0650 -0.0114 282 GLU D OE1 
13338 O OE2 . GLU D 282 ? 0.5092 0.4024 0.5123 -0.0137 -0.0625 -0.0063 282 GLU D OE2 
13339 N N   . GLU D 283 ? 0.3365 0.2586 0.3430 0.0038  -0.0632 -0.0199 283 GLU D N   
13340 C CA  . GLU D 283 ? 0.2873 0.2069 0.2867 0.0054  -0.0623 -0.0172 283 GLU D CA  
13341 C C   . GLU D 283 ? 0.3214 0.2495 0.3216 0.0075  -0.0598 -0.0182 283 GLU D C   
13342 O O   . GLU D 283 ? 0.2946 0.2210 0.2898 0.0070  -0.0578 -0.0158 283 GLU D O   
13343 C CB  . GLU D 283 ? 0.2857 0.2020 0.2824 0.0081  -0.0654 -0.0176 283 GLU D CB  
13344 C CG  . GLU D 283 ? 0.3804 0.2954 0.3701 0.0099  -0.0649 -0.0157 283 GLU D CG  
13345 C CD  . GLU D 283 ? 0.4216 0.3346 0.4097 0.0126  -0.0685 -0.0167 283 GLU D CD  
13346 O OE1 . GLU D 283 ? 0.4834 0.3949 0.4753 0.0131  -0.0716 -0.0185 283 GLU D OE1 
13347 O OE2 . GLU D 283 ? 0.3959 0.3088 0.3790 0.0141  -0.0687 -0.0159 283 GLU D OE2 
13348 N N   . ILE D 284 ? 0.2510 0.1876 0.2571 0.0099  -0.0596 -0.0217 284 ILE D N   
13349 C CA  . ILE D 284 ? 0.2446 0.1890 0.2521 0.0114  -0.0569 -0.0225 284 ILE D CA  
13350 C C   . ILE D 284 ? 0.2602 0.2071 0.2686 0.0087  -0.0546 -0.0221 284 ILE D C   
13351 O O   . ILE D 284 ? 0.2379 0.1870 0.2441 0.0091  -0.0528 -0.0210 284 ILE D O   
13352 C CB  . ILE D 284 ? 0.2727 0.2249 0.2863 0.0142  -0.0568 -0.0263 284 ILE D CB  
13353 C CG1 . ILE D 284 ? 0.2528 0.2035 0.2656 0.0173  -0.0592 -0.0263 284 ILE D CG1 
13354 C CG2 . ILE D 284 ? 0.2525 0.2129 0.2681 0.0146  -0.0534 -0.0274 284 ILE D CG2 
13355 C CD1 . ILE D 284 ? 0.3668 0.3243 0.3857 0.0202  -0.0594 -0.0303 284 ILE D CD1 
13356 N N   . PHE D 285 ? 0.2352 0.1818 0.2471 0.0057  -0.0551 -0.0231 285 PHE D N   
13357 C CA  . PHE D 285 ? 0.2340 0.1837 0.2476 0.0025  -0.0536 -0.0228 285 PHE D CA  
13358 C C   . PHE D 285 ? 0.2505 0.1923 0.2580 0.0008  -0.0533 -0.0187 285 PHE D C   
13359 O O   . PHE D 285 ? 0.2381 0.1830 0.2446 0.0005  -0.0520 -0.0180 285 PHE D O   
13360 C CB  . PHE D 285 ? 0.2547 0.2053 0.2737 -0.0008 -0.0548 -0.0244 285 PHE D CB  
13361 C CG  . PHE D 285 ? 0.2725 0.2267 0.2945 -0.0050 -0.0540 -0.0236 285 PHE D CG  
13362 C CD1 . PHE D 285 ? 0.2156 0.1807 0.2398 -0.0045 -0.0522 -0.0249 285 PHE D CD1 
13363 C CD2 . PHE D 285 ? 0.2990 0.2466 0.3224 -0.0098 -0.0552 -0.0210 285 PHE D CD2 
13364 C CE1 . PHE D 285 ? 0.2137 0.1849 0.2421 -0.0083 -0.0520 -0.0240 285 PHE D CE1 
13365 C CE2 . PHE D 285 ? 0.2943 0.2473 0.3226 -0.0144 -0.0547 -0.0198 285 PHE D CE2 
13366 C CZ  . PHE D 285 ? 0.2252 0.1910 0.2564 -0.0134 -0.0533 -0.0215 285 PHE D CZ  
13367 N N   . THR D 286 ? 0.2732 0.2046 0.2761 -0.0002 -0.0544 -0.0157 286 THR D N   
13368 C CA  . THR D 286 ? 0.2933 0.2160 0.2888 -0.0013 -0.0530 -0.0111 286 THR D CA  
13369 C C   . THR D 286 ? 0.2761 0.2001 0.2659 0.0028  -0.0515 -0.0107 286 THR D C   
13370 O O   . THR D 286 ? 0.2494 0.1710 0.2354 0.0031  -0.0494 -0.0083 286 THR D O   
13371 C CB  . THR D 286 ? 0.3343 0.2467 0.3247 -0.0023 -0.0537 -0.0077 286 THR D CB  
13372 O OG1 . THR D 286 ? 0.3521 0.2629 0.3484 -0.0064 -0.0552 -0.0078 286 THR D OG1 
13373 C CG2 . THR D 286 ? 0.3448 0.2487 0.3265 -0.0028 -0.0510 -0.0019 286 THR D CG2 
13374 N N   . LEU D 287 ? 0.2523 0.1799 0.2417 0.0059  -0.0525 -0.0125 287 LEU D N   
13375 C CA  . LEU D 287 ? 0.2532 0.1825 0.2380 0.0088  -0.0515 -0.0120 287 LEU D CA  
13376 C C   . LEU D 287 ? 0.2229 0.1592 0.2110 0.0096  -0.0502 -0.0134 287 LEU D C   
13377 O O   . LEU D 287 ? 0.2563 0.1914 0.2397 0.0110  -0.0487 -0.0119 287 LEU D O   
13378 C CB  . LEU D 287 ? 0.2880 0.2200 0.2734 0.0111  -0.0534 -0.0134 287 LEU D CB  
13379 C CG  . LEU D 287 ? 0.2867 0.2120 0.2671 0.0113  -0.0553 -0.0123 287 LEU D CG  
13380 C CD1 . LEU D 287 ? 0.2849 0.2148 0.2689 0.0137  -0.0579 -0.0144 287 LEU D CD1 
13381 C CD2 . LEU D 287 ? 0.2387 0.1582 0.2098 0.0116  -0.0537 -0.0099 287 LEU D CD2 
13382 N N   . ALA D 288 ? 0.2120 0.1561 0.2079 0.0089  -0.0504 -0.0163 288 ALA D N   
13383 C CA  . ALA D 288 ? 0.2245 0.1767 0.2234 0.0093  -0.0490 -0.0177 288 ALA D CA  
13384 C C   . ALA D 288 ? 0.2433 0.1959 0.2404 0.0075  -0.0477 -0.0157 288 ALA D C   
13385 O O   . ALA D 288 ? 0.2065 0.1643 0.2021 0.0092  -0.0450 -0.0137 288 ALA D O   
13386 C CB  . ALA D 288 ? 0.2224 0.1848 0.2289 0.0089  -0.0481 -0.0210 288 ALA D CB  
13387 N N   . ARG D 289 ? 0.2268 0.1775 0.2252 0.0046  -0.0467 -0.0138 289 ARG D N   
13388 C CA  . ARG D 289 ? 0.2523 0.2081 0.2503 0.0036  -0.0420 -0.0091 289 ARG D CA  
13389 C C   . ARG D 289 ? 0.2848 0.2345 0.2739 0.0066  -0.0392 -0.0050 289 ARG D C   
13390 O O   . ARG D 289 ? 0.2344 0.1903 0.2226 0.0080  -0.0355 -0.0024 289 ARG D O   
13391 C CB  . ARG D 289 ? 0.2570 0.2110 0.2581 -0.0006 -0.0417 -0.0074 289 ARG D CB  
13392 C CG  . ARG D 289 ? 0.2063 0.1699 0.2169 -0.0037 -0.0430 -0.0107 289 ARG D CG  
13393 C CD  . ARG D 289 ? 0.2645 0.2266 0.2782 -0.0083 -0.0419 -0.0077 289 ARG D CD  
13394 N NE  . ARG D 289 ? 0.2597 0.2339 0.2825 -0.0113 -0.0416 -0.0092 289 ARG D NE  
13395 C CZ  . ARG D 289 ? 0.2831 0.2595 0.3106 -0.0158 -0.0401 -0.0065 289 ARG D CZ  
13396 N NH1 . ARG D 289 ? 0.2775 0.2452 0.3010 -0.0180 -0.0383 -0.0014 289 ARG D NH1 
13397 N NH2 . ARG D 289 ? 0.2588 0.2468 0.2952 -0.0184 -0.0405 -0.0087 289 ARG D NH2 
13398 N N   . GLN D 290 ? 0.2365 0.1740 0.2189 0.0079  -0.0413 -0.0046 290 GLN D N   
13399 C CA  . GLN D 290 ? 0.2464 0.1775 0.2196 0.0112  -0.0393 -0.0015 290 GLN D CA  
13400 C C   . GLN D 290 ? 0.2467 0.1805 0.2186 0.0146  -0.0396 -0.0030 290 GLN D C   
13401 O O   . GLN D 290 ? 0.2772 0.2094 0.2433 0.0175  -0.0372 -0.0006 290 GLN D O   
13402 C CB  . GLN D 290 ? 0.2412 0.1586 0.2073 0.0119  -0.0422 -0.0010 290 GLN D CB  
13403 C CG  . GLN D 290 ? 0.3056 0.2191 0.2721 0.0082  -0.0416 0.0018  290 GLN D CG  
13404 C CD  . GLN D 290 ? 0.3638 0.2691 0.3253 0.0080  -0.0437 0.0018  290 GLN D CD  
13405 O OE1 . GLN D 290 ? 0.3751 0.2824 0.3344 0.0100  -0.0447 -0.0009 290 GLN D OE1 
13406 N NE2 . GLN D 290 ? 0.3851 0.2837 0.3456 0.0049  -0.0438 0.0052  290 GLN D NE2 
13407 N N   . ARG D 291 ? 0.2222 0.1603 0.1995 0.0144  -0.0424 -0.0069 291 ARG D N   
13408 C CA  . ARG D 291 ? 0.2061 0.1481 0.1835 0.0167  -0.0423 -0.0075 291 ARG D CA  
13409 C C   . ARG D 291 ? 0.2257 0.1796 0.2077 0.0163  -0.0392 -0.0061 291 ARG D C   
13410 O O   . ARG D 291 ? 0.2395 0.1951 0.2194 0.0187  -0.0379 -0.0045 291 ARG D O   
13411 C CB  . ARG D 291 ? 0.2219 0.1664 0.2031 0.0159  -0.0456 -0.0117 291 ARG D CB  
13412 C CG  . ARG D 291 ? 0.2745 0.2237 0.2567 0.0168  -0.0449 -0.0120 291 ARG D CG  
13413 C CD  . ARG D 291 ? 0.2695 0.2201 0.2529 0.0161  -0.0456 -0.0136 291 ARG D CD  
13414 N NE  . ARG D 291 ? 0.2233 0.1749 0.2069 0.0162  -0.0445 -0.0138 291 ARG D NE  
13415 C CZ  . ARG D 291 ? 0.2641 0.2129 0.2431 0.0162  -0.0443 -0.0129 291 ARG D CZ  
13416 N NH1 . ARG D 291 ? 0.3117 0.2565 0.2850 0.0165  -0.0446 -0.0123 291 ARG D NH1 
13417 N NH2 . ARG D 291 ? 0.2265 0.1759 0.2065 0.0161  -0.0442 -0.0129 291 ARG D NH2 
13418 N N   . CYS D 292 ? 0.2100 0.1719 0.1983 0.0135  -0.0384 -0.0067 292 CYS D N   
13419 C CA  . CYS D 292 ? 0.2215 0.1954 0.2144 0.0132  -0.0359 -0.0056 292 CYS D CA  
13420 C C   . CYS D 292 ? 0.2388 0.2133 0.2279 0.0154  -0.0320 -0.0015 292 CYS D C   
13421 O O   . CYS D 292 ? 0.2363 0.2169 0.2260 0.0175  -0.0306 -0.0002 292 CYS D O   
13422 C CB  . CYS D 292 ? 0.2289 0.2103 0.2291 0.0097  -0.0363 -0.0074 292 CYS D CB  
13423 S SG  . CYS D 292 ? 0.2447 0.2416 0.2509 0.0094  -0.0336 -0.0061 292 CYS D SG  
13424 N N   . VAL D 293 ? 0.2607 0.2290 0.2456 0.0153  -0.0303 0.0007  293 VAL D N   
13425 C CA  . VAL D 293 ? 0.2619 0.2325 0.2436 0.0174  -0.0260 0.0044  293 VAL D CA  
13426 C C   . VAL D 293 ? 0.2430 0.2106 0.2191 0.0223  -0.0257 0.0051  293 VAL D C   
13427 O O   . VAL D 293 ? 0.2635 0.2386 0.2414 0.0244  -0.0235 0.0064  293 VAL D O   
13428 C CB  . VAL D 293 ? 0.3345 0.2988 0.3118 0.0163  -0.0241 0.0068  293 VAL D CB  
13429 C CG1 . VAL D 293 ? 0.2799 0.2454 0.2518 0.0198  -0.0197 0.0102  293 VAL D CG1 
13430 C CG2 . VAL D 293 ? 0.2598 0.2296 0.2445 0.0111  -0.0238 0.0070  293 VAL D CG2 
13431 N N   . PRO D 294 ? 0.2568 0.2136 0.2265 0.0243  -0.0281 0.0041  294 PRO D N   
13432 C CA  . PRO D 294 ? 0.2372 0.1904 0.2020 0.0287  -0.0281 0.0046  294 PRO D CA  
13433 C C   . PRO D 294 ? 0.2984 0.2569 0.2680 0.0286  -0.0298 0.0036  294 PRO D C   
13434 O O   . PRO D 294 ? 0.2565 0.2162 0.2251 0.0304  -0.0280 0.0044  294 PRO D O   
13435 C CB  . PRO D 294 ? 0.3056 0.2490 0.2647 0.0283  -0.0290 0.0028  294 PRO D CB  
13436 C CG  . PRO D 294 ? 0.2921 0.2330 0.2537 0.0250  -0.0319 0.0009  294 PRO D CG  
13437 C CD  . PRO D 294 ? 0.2786 0.2250 0.2446 0.0231  -0.0310 0.0026  294 PRO D CD  
13438 N N   . MET D 295 ? 0.2731 0.2358 0.2485 0.0254  -0.0322 0.0017  295 MET D N   
13439 C CA  . MET D 295 ? 0.2833 0.2509 0.2625 0.0247  -0.0333 0.0009  295 MET D CA  
13440 C C   . MET D 295 ? 0.2673 0.2471 0.2519 0.0245  -0.0323 0.0022  295 MET D C   
13441 O O   . MET D 295 ? 0.2437 0.2268 0.2291 0.0256  -0.0323 0.0035  295 MET D O   
13442 C CB  . MET D 295 ? 0.2578 0.2245 0.2399 0.0217  -0.0362 -0.0024 295 MET D CB  
13443 C CG  . MET D 295 ? 0.2320 0.1890 0.2098 0.0209  -0.0367 -0.0043 295 MET D CG  
13444 S SD  . MET D 295 ? 0.3431 0.2971 0.3179 0.0215  -0.0353 -0.0035 295 MET D SD  
13445 C CE  . MET D 295 ? 0.3165 0.2624 0.2860 0.0206  -0.0366 -0.0061 295 MET D CE  
13446 N N   . GLU D 296 ? 0.2437 0.2306 0.2326 0.0224  -0.0308 0.0017  296 GLU D N   
13447 C CA  . GLU D 296 ? 0.2210 0.2208 0.2161 0.0213  -0.0301 0.0017  296 GLU D CA  
13448 C C   . GLU D 296 ? 0.1867 0.1927 0.1837 0.0220  -0.0270 0.0037  296 GLU D C   
13449 O O   . GLU D 296 ? 0.2292 0.2429 0.2281 0.0240  -0.0259 0.0054  296 GLU D O   
13450 C CB  . GLU D 296 ? 0.2282 0.2330 0.2288 0.0175  -0.0322 -0.0019 296 GLU D CB  
13451 C CG  . GLU D 296 ? 0.2293 0.2320 0.2298 0.0170  -0.0350 -0.0041 296 GLU D CG  
13452 C CD  . GLU D 296 ? 0.2727 0.2837 0.2747 0.0177  -0.0351 -0.0030 296 GLU D CD  
13453 O OE1 . GLU D 296 ? 0.2858 0.3067 0.2909 0.0178  -0.0341 -0.0021 296 GLU D OE1 
13454 O OE2 . GLU D 296 ? 0.3329 0.3406 0.3332 0.0177  -0.0358 -0.0026 296 GLU D OE2 
13455 N N   . GLY D 297 ? 0.1920 0.1950 0.1885 0.0205  -0.0255 0.0038  297 GLY D N   
13456 C CA  . GLY D 297 ? 0.1834 0.1941 0.1833 0.0201  -0.0224 0.0056  297 GLY D CA  
13457 C C   . GLY D 297 ? 0.2094 0.2177 0.2112 0.0159  -0.0222 0.0050  297 GLY D C   
13458 O O   . GLY D 297 ? 0.2199 0.2197 0.2197 0.0141  -0.0246 0.0032  297 GLY D O   
13459 N N   . PHE D 298 ? 0.2272 0.2431 0.2333 0.0144  -0.0193 0.0068  298 PHE D N   
13460 C CA  . PHE D 298 ? 0.2359 0.2498 0.2447 0.0097  -0.0191 0.0069  298 PHE D CA  
13461 C C   . PHE D 298 ? 0.1961 0.2122 0.2112 0.0058  -0.0230 0.0030  298 PHE D C   
13462 O O   . PHE D 298 ? 0.2225 0.2464 0.2416 0.0064  -0.0249 0.0007  298 PHE D O   
13463 C CB  . PHE D 298 ? 0.2606 0.2838 0.2740 0.0083  -0.0150 0.0098  298 PHE D CB  
13464 C CG  . PHE D 298 ? 0.2623 0.2829 0.2786 0.0028  -0.0146 0.0109  298 PHE D CG  
13465 C CD1 . PHE D 298 ? 0.2920 0.3003 0.3009 0.0023  -0.0140 0.0129  298 PHE D CD1 
13466 C CD2 . PHE D 298 ? 0.2194 0.2492 0.2457 -0.0021 -0.0153 0.0100  298 PHE D CD2 
13467 C CE1 . PHE D 298 ? 0.2887 0.2935 0.2999 -0.0031 -0.0139 0.0146  298 PHE D CE1 
13468 C CE2 . PHE D 298 ? 0.1971 0.2234 0.2265 -0.0077 -0.0153 0.0113  298 PHE D CE2 
13469 C CZ  . PHE D 298 ? 0.2439 0.2574 0.2656 -0.0083 -0.0145 0.0139  298 PHE D CZ  
13470 N N   . VAL D 299 ? 0.2081 0.2173 0.2240 0.0019  -0.0245 0.0023  299 VAL D N   
13471 C CA  . VAL D 299 ? 0.1897 0.1974 0.2096 -0.0007 -0.0291 -0.0022 299 VAL D CA  
13472 C C   . VAL D 299 ? 0.2207 0.2407 0.2501 -0.0035 -0.0304 -0.0048 299 VAL D C   
13473 O O   . VAL D 299 ? 0.2019 0.2226 0.2346 -0.0047 -0.0344 -0.0095 299 VAL D O   
13474 C CB  . VAL D 299 ? 0.2116 0.2070 0.2294 -0.0037 -0.0310 -0.0023 299 VAL D CB  
13475 C CG1 . VAL D 299 ? 0.2015 0.1847 0.2094 -0.0004 -0.0305 -0.0004 299 VAL D CG1 
13476 C CG2 . VAL D 299 ? 0.2020 0.1992 0.2239 -0.0082 -0.0288 0.0009  299 VAL D CG2 
13477 N N   . THR D 300 ? 0.1721 0.2024 0.2061 -0.0043 -0.0275 -0.0024 300 THR D N   
13478 C CA  . THR D 300 ? 0.1781 0.2207 0.2214 -0.0069 -0.0291 -0.0050 300 THR D CA  
13479 C C   . THR D 300 ? 0.1804 0.2347 0.2247 -0.0031 -0.0286 -0.0054 300 THR D C   
13480 O O   . THR D 300 ? 0.2010 0.2671 0.2527 -0.0046 -0.0296 -0.0070 300 THR D O   
13481 C CB  . THR D 300 ? 0.1946 0.2420 0.2444 -0.0114 -0.0270 -0.0025 300 THR D CB  
13482 O OG1 . THR D 300 ? 0.1835 0.2366 0.2320 -0.0090 -0.0220 0.0021  300 THR D OG1 
13483 C CG2 . THR D 300 ? 0.1875 0.2224 0.2358 -0.0155 -0.0277 -0.0013 300 THR D CG2 
13484 N N   . TYR D 301 ? 0.2032 0.2542 0.2406 0.0016  -0.0276 -0.0039 301 TYR D N   
13485 C CA  . TYR D 301 ? 0.1497 0.2096 0.1873 0.0050  -0.0282 -0.0044 301 TYR D CA  
13486 C C   . TYR D 301 ? 0.1520 0.2050 0.1827 0.0080  -0.0294 -0.0048 301 TYR D C   
13487 O O   . TYR D 301 ? 0.2061 0.2656 0.2375 0.0093  -0.0312 -0.0064 301 TYR D O   
13488 C CB  . TYR D 301 ? 0.1566 0.2246 0.1950 0.0080  -0.0249 -0.0007 301 TYR D CB  
13489 C CG  . TYR D 301 ? 0.1669 0.2265 0.1979 0.0118  -0.0217 0.0031  301 TYR D CG  
13490 C CD1 . TYR D 301 ? 0.1734 0.2284 0.1980 0.0162  -0.0222 0.0040  301 TYR D CD1 
13491 C CD2 . TYR D 301 ? 0.1968 0.2532 0.2269 0.0110  -0.0184 0.0056  301 TYR D CD2 
13492 C CE1 . TYR D 301 ? 0.1643 0.2109 0.1820 0.0198  -0.0200 0.0067  301 TYR D CE1 
13493 C CE2 . TYR D 301 ? 0.2019 0.2508 0.2243 0.0150  -0.0158 0.0084  301 TYR D CE2 
13494 C CZ  . TYR D 301 ? 0.2327 0.2764 0.2490 0.0196  -0.0169 0.0085  301 TYR D CZ  
13495 O OH  . TYR D 301 ? 0.2208 0.2564 0.2294 0.0238  -0.0149 0.0105  301 TYR D OH  
13496 N N   . GLY D 302 ? 0.1593 0.2000 0.1836 0.0091  -0.0287 -0.0035 302 GLY D N   
13497 C CA  . GLY D 302 ? 0.1527 0.1863 0.1720 0.0107  -0.0306 -0.0046 302 GLY D CA  
13498 C C   . GLY D 302 ? 0.1840 0.2213 0.2007 0.0143  -0.0302 -0.0027 302 GLY D C   
13499 O O   . GLY D 302 ? 0.2137 0.2516 0.2295 0.0145  -0.0322 -0.0042 302 GLY D O   
13500 N N   . GLY D 303 ? 0.1698 0.2099 0.1854 0.0171  -0.0277 0.0008  303 GLY D N   
13501 C CA  . GLY D 303 ? 0.1694 0.2122 0.1826 0.0206  -0.0277 0.0030  303 GLY D CA  
13502 C C   . GLY D 303 ? 0.1480 0.2042 0.1660 0.0206  -0.0287 0.0027  303 GLY D C   
13503 O O   . GLY D 303 ? 0.1539 0.2118 0.1696 0.0229  -0.0292 0.0047  303 GLY D O   
13504 N N   . LEU D 304 ? 0.1553 0.2203 0.1796 0.0179  -0.0292 0.0002  304 LEU D N   
13505 C CA  . LEU D 304 ? 0.1675 0.2436 0.1958 0.0174  -0.0297 -0.0005 304 LEU D CA  
13506 C C   . LEU D 304 ? 0.1540 0.2392 0.1874 0.0184  -0.0283 0.0008  304 LEU D C   
13507 O O   . LEU D 304 ? 0.1852 0.2696 0.2215 0.0167  -0.0270 0.0007  304 LEU D O   
13508 C CB  . LEU D 304 ? 0.1407 0.2183 0.1721 0.0132  -0.0313 -0.0049 304 LEU D CB  
13509 C CG  . LEU D 304 ? 0.1917 0.2629 0.2191 0.0121  -0.0320 -0.0065 304 LEU D CG  
13510 C CD1 . LEU D 304 ? 0.1204 0.1924 0.1508 0.0087  -0.0333 -0.0109 304 LEU D CD1 
13511 C CD2 . LEU D 304 ? 0.1971 0.2700 0.2209 0.0138  -0.0311 -0.0042 304 LEU D CD2 
13512 N N   . ALA D 305 ? 0.1746 0.2648 0.2081 0.0200  -0.0275 0.0022  305 ALA D N   
13513 C CA  . ALA D 305 ? 0.1740 0.2741 0.2137 0.0199  -0.0267 0.0022  305 ALA D CA  
13514 C C   . ALA D 305 ? 0.1669 0.2714 0.2128 0.0149  -0.0282 -0.0018 305 ALA D C   
13515 O O   . ALA D 305 ? 0.1331 0.2336 0.1775 0.0125  -0.0300 -0.0046 305 ALA D O   
13516 C CB  . ALA D 305 ? 0.1703 0.2742 0.2084 0.0226  -0.0263 0.0038  305 ALA D CB  
13517 N N   . GLY D 306 ? 0.1738 0.2865 0.2272 0.0134  -0.0275 -0.0019 306 GLY D N   
13518 C CA  . GLY D 306 ? 0.1403 0.2563 0.2000 0.0084  -0.0295 -0.0056 306 GLY D CA  
13519 C C   . GLY D 306 ? 0.1590 0.2763 0.2173 0.0082  -0.0312 -0.0078 306 GLY D C   
13520 O O   . GLY D 306 ? 0.1655 0.2808 0.2252 0.0051  -0.0334 -0.0112 306 GLY D O   
13521 N N   . ARG D 307 ? 0.1316 0.2522 0.1869 0.0119  -0.0304 -0.0057 307 ARG D N   
13522 C CA  . ARG D 307 ? 0.1477 0.2708 0.2010 0.0122  -0.0320 -0.0074 307 ARG D CA  
13523 C C   . ARG D 307 ? 0.1351 0.2513 0.1822 0.0117  -0.0327 -0.0089 307 ARG D C   
13524 O O   . ARG D 307 ? 0.1471 0.2652 0.1938 0.0105  -0.0343 -0.0118 307 ARG D O   
13525 C CB  . ARG D 307 ? 0.1430 0.2704 0.1936 0.0164  -0.0311 -0.0044 307 ARG D CB  
13526 C CG  . ARG D 307 ? 0.1793 0.3007 0.2233 0.0200  -0.0296 -0.0007 307 ARG D CG  
13527 C CD  . ARG D 307 ? 0.1383 0.2629 0.1793 0.0240  -0.0294 0.0021  307 ARG D CD  
13528 N NE  . ARG D 307 ? 0.1571 0.2748 0.1928 0.0274  -0.0282 0.0058  307 ARG D NE  
13529 C CZ  . ARG D 307 ? 0.1568 0.2742 0.1932 0.0306  -0.0267 0.0082  307 ARG D CZ  
13530 N NH1 . ARG D 307 ? 0.1574 0.2827 0.2000 0.0310  -0.0259 0.0076  307 ARG D NH1 
13531 N NH2 . ARG D 307 ? 0.1593 0.2684 0.1902 0.0335  -0.0260 0.0111  307 ARG D NH2 
13532 N N   . ASP D 308 ? 0.1741 0.2830 0.2167 0.0126  -0.0317 -0.0073 308 ASP D N   
13533 C CA  . ASP D 308 ? 0.1628 0.2663 0.2004 0.0120  -0.0322 -0.0087 308 ASP D CA  
13534 C C   . ASP D 308 ? 0.1426 0.2425 0.1826 0.0086  -0.0336 -0.0126 308 ASP D C   
13535 O O   . ASP D 308 ? 0.1347 0.2338 0.1725 0.0079  -0.0343 -0.0153 308 ASP D O   
13536 C CB  . ASP D 308 ? 0.1714 0.2684 0.2036 0.0142  -0.0310 -0.0054 308 ASP D CB  
13537 C CG  . ASP D 308 ? 0.2069 0.3061 0.2355 0.0175  -0.0301 -0.0016 308 ASP D CG  
13538 O OD1 . ASP D 308 ? 0.2705 0.3732 0.2967 0.0179  -0.0304 -0.0018 308 ASP D OD1 
13539 O OD2 . ASP D 308 ? 0.2186 0.3165 0.2468 0.0200  -0.0291 0.0015  308 ASP D OD2 
13540 N N   . MET D 309 ? 0.1153 0.2135 0.1598 0.0066  -0.0340 -0.0131 309 MET D N   
13541 C CA  . MET D 309 ? 0.1493 0.2443 0.1967 0.0030  -0.0359 -0.0169 309 MET D CA  
13542 C C   . MET D 309 ? 0.1415 0.2421 0.1925 0.0015  -0.0375 -0.0198 309 MET D C   
13543 O O   . MET D 309 ? 0.1375 0.2354 0.1879 0.0000  -0.0391 -0.0234 309 MET D O   
13544 C CB  . MET D 309 ? 0.1307 0.2236 0.1828 0.0008  -0.0362 -0.0166 309 MET D CB  
13545 C CG  . MET D 309 ? 0.1298 0.2151 0.1777 0.0020  -0.0356 -0.0152 309 MET D CG  
13546 S SD  . MET D 309 ? 0.1567 0.2407 0.2105 -0.0008 -0.0364 -0.0155 309 MET D SD  
13547 C CE  . MET D 309 ? 0.1242 0.2205 0.1836 0.0001  -0.0338 -0.0117 309 MET D CE  
13548 N N   . ALA D 310 ? 0.1100 0.2184 0.1644 0.0022  -0.0374 -0.0185 310 ALA D N   
13549 C CA  . ALA D 310 ? 0.0874 0.2017 0.1452 0.0010  -0.0393 -0.0213 310 ALA D CA  
13550 C C   . ALA D 310 ? 0.1103 0.2257 0.1621 0.0032  -0.0395 -0.0231 310 ALA D C   
13551 O O   . ALA D 310 ? 0.1328 0.2497 0.1854 0.0021  -0.0415 -0.0269 310 ALA D O   
13552 C CB  . ALA D 310 ? 0.0851 0.2081 0.1481 0.0016  -0.0390 -0.0193 310 ALA D CB  
13553 N N   . ALA D 311 ? 0.1297 0.2449 0.1756 0.0064  -0.0376 -0.0202 311 ALA D N   
13554 C CA  . ALA D 311 ? 0.1356 0.2527 0.1760 0.0082  -0.0375 -0.0214 311 ALA D CA  
13555 C C   . ALA D 311 ? 0.1399 0.2514 0.1778 0.0073  -0.0376 -0.0245 311 ALA D C   
13556 O O   . ALA D 311 ? 0.1491 0.2637 0.1849 0.0079  -0.0382 -0.0277 311 ALA D O   
13557 C CB  . ALA D 311 ? 0.1293 0.2474 0.1646 0.0113  -0.0355 -0.0170 311 ALA D CB  
13558 N N   . MET D 312 ? 0.1042 0.2081 0.1424 0.0060  -0.0371 -0.0238 312 MET D N   
13559 C CA  . MET D 312 ? 0.1248 0.2231 0.1611 0.0054  -0.0372 -0.0267 312 MET D CA  
13560 C C   . MET D 312 ? 0.1492 0.2475 0.1889 0.0035  -0.0395 -0.0316 312 MET D C   
13561 O O   . MET D 312 ? 0.1567 0.2549 0.1944 0.0044  -0.0399 -0.0353 312 MET D O   
13562 C CB  . MET D 312 ? 0.1147 0.2049 0.1507 0.0046  -0.0366 -0.0247 312 MET D CB  
13563 C CG  . MET D 312 ? 0.1049 0.1893 0.1380 0.0047  -0.0364 -0.0269 312 MET D CG  
13564 S SD  . MET D 312 ? 0.1802 0.2554 0.2123 0.0041  -0.0358 -0.0244 312 MET D SD  
13565 C CE  . MET D 312 ? 0.2230 0.3007 0.2525 0.0063  -0.0341 -0.0188 312 MET D CE  
13566 N N   . VAL D 313 ? 0.1270 0.2257 0.1723 0.0010  -0.0412 -0.0319 313 VAL D N   
13567 C CA  . VAL D 313 ? 0.1676 0.2658 0.2166 -0.0011 -0.0439 -0.0365 313 VAL D CA  
13568 C C   . VAL D 313 ? 0.1733 0.2784 0.2209 0.0007  -0.0448 -0.0399 313 VAL D C   
13569 O O   . VAL D 313 ? 0.2070 0.3110 0.2542 0.0011  -0.0462 -0.0446 313 VAL D O   
13570 C CB  . VAL D 313 ? 0.2041 0.3035 0.2602 -0.0046 -0.0456 -0.0355 313 VAL D CB  
13571 C CG1 . VAL D 313 ? 0.1398 0.2395 0.1999 -0.0070 -0.0488 -0.0402 313 VAL D CG1 
13572 C CG2 . VAL D 313 ? 0.1982 0.2908 0.2556 -0.0066 -0.0449 -0.0331 313 VAL D CG2 
13573 N N   . GLN D 314 ? 0.1710 0.2837 0.2179 0.0024  -0.0442 -0.0378 314 GLN D N   
13574 C CA  . GLN D 314 ? 0.1661 0.2862 0.2112 0.0044  -0.0451 -0.0409 314 GLN D CA  
13575 C C   . GLN D 314 ? 0.1905 0.3116 0.2292 0.0073  -0.0432 -0.0420 314 GLN D C   
13576 O O   . GLN D 314 ? 0.2247 0.3494 0.2622 0.0086  -0.0442 -0.0467 314 GLN D O   
13577 C CB  . GLN D 314 ? 0.1413 0.2692 0.1872 0.0054  -0.0451 -0.0381 314 GLN D CB  
13578 C CG  . GLN D 314 ? 0.1539 0.2903 0.1975 0.0077  -0.0462 -0.0411 314 GLN D CG  
13579 C CD  . GLN D 314 ? 0.1661 0.3041 0.2139 0.0061  -0.0497 -0.0468 314 GLN D CD  
13580 O OE1 . GLN D 314 ? 0.2001 0.3343 0.2538 0.0027  -0.0515 -0.0475 314 GLN D OE1 
13581 N NE2 . GLN D 314 ? 0.2039 0.3477 0.2487 0.0084  -0.0506 -0.0509 314 GLN D NE2 
13582 N N   . GLY D 315 ? 0.1711 0.2897 0.2060 0.0083  -0.0406 -0.0378 315 GLY D N   
13583 C CA  . GLY D 315 ? 0.1626 0.2834 0.1922 0.0107  -0.0387 -0.0382 315 GLY D CA  
13584 C C   . GLY D 315 ? 0.1903 0.3067 0.2201 0.0106  -0.0388 -0.0424 315 GLY D C   
13585 O O   . GLY D 315 ? 0.1665 0.2876 0.1933 0.0127  -0.0379 -0.0450 315 GLY D O   
13586 N N   . LEU D 316 ? 0.1843 0.2922 0.2174 0.0084  -0.0400 -0.0431 316 LEU D N   
13587 C CA  . LEU D 316 ? 0.2191 0.3224 0.2527 0.0087  -0.0406 -0.0475 316 LEU D CA  
13588 C C   . LEU D 316 ? 0.2177 0.3258 0.2530 0.0098  -0.0427 -0.0538 316 LEU D C   
13589 O O   . LEU D 316 ? 0.2722 0.3814 0.3065 0.0120  -0.0425 -0.0580 316 LEU D O   
13590 C CB  . LEU D 316 ? 0.2113 0.3045 0.2481 0.0061  -0.0417 -0.0467 316 LEU D CB  
13591 C CG  . LEU D 316 ? 0.1632 0.2505 0.1979 0.0057  -0.0398 -0.0423 316 LEU D CG  
13592 C CD1 . LEU D 316 ? 0.1469 0.2264 0.1846 0.0030  -0.0410 -0.0407 316 LEU D CD1 
13593 C CD2 . LEU D 316 ? 0.1780 0.2631 0.2101 0.0077  -0.0386 -0.0442 316 LEU D CD2 
13594 N N   . GLU D 317 ? 0.1870 0.2987 0.2251 0.0087  -0.0448 -0.0547 317 GLU D N   
13595 C CA  . GLU D 317 ? 0.2246 0.3412 0.2642 0.0099  -0.0473 -0.0609 317 GLU D CA  
13596 C C   . GLU D 317 ? 0.2400 0.3673 0.2753 0.0135  -0.0459 -0.0625 317 GLU D C   
13597 O O   . GLU D 317 ? 0.2256 0.3567 0.2601 0.0162  -0.0463 -0.0679 317 GLU D O   
13598 C CB  . GLU D 317 ? 0.2170 0.3344 0.2615 0.0072  -0.0503 -0.0612 317 GLU D CB  
13599 C CG  . GLU D 317 ? 0.2646 0.3876 0.3108 0.0084  -0.0534 -0.0676 317 GLU D CG  
13600 C CD  . GLU D 317 ? 0.2814 0.3986 0.3300 0.0087  -0.0556 -0.0734 317 GLU D CD  
13601 O OE1 . GLU D 317 ? 0.2781 0.3861 0.3282 0.0068  -0.0554 -0.0720 317 GLU D OE1 
13602 O OE2 . GLU D 317 ? 0.3298 0.4517 0.3788 0.0110  -0.0577 -0.0795 317 GLU D OE2 
13603 N N   . GLU D 318 ? 0.1929 0.3257 0.2255 0.0139  -0.0443 -0.0578 318 GLU D N   
13604 C CA  . GLU D 318 ? 0.1881 0.3318 0.2161 0.0171  -0.0430 -0.0586 318 GLU D CA  
13605 C C   . GLU D 318 ? 0.1690 0.3150 0.1934 0.0193  -0.0402 -0.0593 318 GLU D C   
13606 O O   . GLU D 318 ? 0.1994 0.3552 0.2210 0.0222  -0.0396 -0.0623 318 GLU D O   
13607 C CB  . GLU D 318 ? 0.2215 0.3691 0.2471 0.0170  -0.0418 -0.0525 318 GLU D CB  
13608 C CG  . GLU D 318 ? 0.2098 0.3575 0.2395 0.0153  -0.0443 -0.0518 318 GLU D CG  
13609 C CD  . GLU D 318 ? 0.1964 0.3498 0.2237 0.0163  -0.0434 -0.0466 318 GLU D CD  
13610 O OE1 . GLU D 318 ? 0.2092 0.3668 0.2311 0.0185  -0.0410 -0.0439 318 GLU D OE1 
13611 O OE2 . GLU D 318 ? 0.1887 0.3426 0.2196 0.0151  -0.0451 -0.0452 318 GLU D OE2 
13612 N N   . GLY D 319 ? 0.1913 0.3295 0.2156 0.0180  -0.0386 -0.0564 319 GLY D N   
13613 C CA  . GLY D 319 ? 0.1695 0.3102 0.1911 0.0198  -0.0362 -0.0570 319 GLY D CA  
13614 C C   . GLY D 319 ? 0.1691 0.3104 0.1929 0.0217  -0.0372 -0.0641 319 GLY D C   
13615 O O   . GLY D 319 ? 0.1540 0.3009 0.1761 0.0239  -0.0352 -0.0657 319 GLY D O   
13616 N N   . THR D 320 ? 0.1923 0.3286 0.2202 0.0212  -0.0403 -0.0685 320 THR D N   
13617 C CA  . THR D 320 ? 0.2235 0.3608 0.2540 0.0237  -0.0418 -0.0759 320 THR D CA  
13618 C C   . THR D 320 ? 0.2049 0.3537 0.2347 0.0269  -0.0430 -0.0814 320 THR D C   
13619 O O   . THR D 320 ? 0.2070 0.3590 0.2388 0.0299  -0.0441 -0.0880 320 THR D O   
13620 C CB  . THR D 320 ? 0.2245 0.3501 0.2599 0.0216  -0.0451 -0.0780 320 THR D CB  
13621 O OG1 . THR D 320 ? 0.2523 0.3782 0.2900 0.0198  -0.0480 -0.0789 320 THR D OG1 
13622 C CG2 . THR D 320 ? 0.1913 0.3059 0.2271 0.0185  -0.0442 -0.0723 320 THR D CG2 
13623 N N   . GLU D 321 ? 0.1869 0.3425 0.2143 0.0266  -0.0429 -0.0790 321 GLU D N   
13624 C CA  . GLU D 321 ? 0.2489 0.4150 0.2758 0.0294  -0.0446 -0.0844 321 GLU D CA  
13625 C C   . GLU D 321 ? 0.2802 0.4591 0.3039 0.0336  -0.0420 -0.0871 321 GLU D C   
13626 O O   . GLU D 321 ? 0.2767 0.4615 0.2962 0.0338  -0.0386 -0.0821 321 GLU D O   
13627 C CB  . GLU D 321 ? 0.2026 0.3727 0.2279 0.0281  -0.0454 -0.0807 321 GLU D CB  
13628 C CG  . GLU D 321 ? 0.2480 0.4084 0.2780 0.0243  -0.0486 -0.0798 321 GLU D CG  
13629 C CD  . GLU D 321 ? 0.2924 0.4571 0.3220 0.0231  -0.0497 -0.0764 321 GLU D CD  
13630 O OE1 . GLU D 321 ? 0.3308 0.5053 0.3558 0.0254  -0.0482 -0.0746 321 GLU D OE1 
13631 O OE2 . GLU D 321 ? 0.2984 0.4569 0.3324 0.0198  -0.0521 -0.0753 321 GLU D OE2 
13632 N N   . GLU D 322 ? 0.2302 0.4830 0.2094 0.0542  0.0061  -0.0022 322 GLU D N   
13633 C CA  . GLU D 322 ? 0.2216 0.4848 0.2016 0.0526  0.0065  -0.0034 322 GLU D CA  
13634 C C   . GLU D 322 ? 0.1944 0.4596 0.1754 0.0456  0.0066  -0.0039 322 GLU D C   
13635 O O   . GLU D 322 ? 0.1961 0.4721 0.1797 0.0428  0.0058  -0.0041 322 GLU D O   
13636 C CB  . GLU D 322 ? 0.2536 0.5126 0.2288 0.0562  0.0101  -0.0046 322 GLU D CB  
13637 C CG  . GLU D 322 ? 0.2671 0.5362 0.2428 0.0549  0.0109  -0.0057 322 GLU D CG  
13638 C CD  . GLU D 322 ? 0.3907 0.6556 0.3617 0.0598  0.0152  -0.0066 322 GLU D CD  
13639 O OE1 . GLU D 322 ? 0.3851 0.6405 0.3527 0.0647  0.0175  -0.0062 322 GLU D OE1 
13640 O OE2 . GLU D 322 ? 0.4546 0.7261 0.4253 0.0591  0.0167  -0.0075 322 GLU D OE2 
13641 N N   . GLU D 323 ? 0.2596 0.5162 0.2387 0.0429  0.0076  -0.0040 323 GLU D N   
13642 C CA  . GLU D 323 ? 0.2861 0.5452 0.2656 0.0372  0.0077  -0.0039 323 GLU D CA  
13643 C C   . GLU D 323 ? 0.2402 0.5025 0.2228 0.0339  0.0061  -0.0021 323 GLU D C   
13644 O O   . GLU D 323 ? 0.2095 0.4766 0.1922 0.0297  0.0064  -0.0018 323 GLU D O   
13645 C CB  . GLU D 323 ? 0.2943 0.5460 0.2710 0.0354  0.0088  -0.0044 323 GLU D CB  
13646 C CG  . GLU D 323 ? 0.3650 0.6096 0.3421 0.0362  0.0079  -0.0029 323 GLU D CG  
13647 C CD  . GLU D 323 ? 0.4655 0.7025 0.4403 0.0409  0.0088  -0.0037 323 GLU D CD  
13648 O OE1 . GLU D 323 ? 0.3767 0.6141 0.3500 0.0447  0.0100  -0.0046 323 GLU D OE1 
13649 O OE2 . GLU D 323 ? 0.3954 0.6260 0.3695 0.0410  0.0087  -0.0030 323 GLU D OE2 
13650 N N   . TYR D 324 ? 0.2515 0.5103 0.2355 0.0357  0.0049  -0.0008 324 TYR D N   
13651 C CA  . TYR D 324 ? 0.2171 0.4780 0.2027 0.0326  0.0043  0.0006  324 TYR D CA  
13652 C C   . TYR D 324 ? 0.1854 0.4595 0.1734 0.0317  0.0036  -0.0006 324 TYR D C   
13653 O O   . TYR D 324 ? 0.2038 0.4826 0.1914 0.0267  0.0041  -0.0005 324 TYR D O   
13654 C CB  . TYR D 324 ? 0.2415 0.4954 0.2278 0.0351  0.0035  0.0019  324 TYR D CB  
13655 C CG  . TYR D 324 ? 0.1910 0.4504 0.1790 0.0338  0.0029  0.0021  324 TYR D CG  
13656 C CD1 . TYR D 324 ? 0.2095 0.4671 0.1949 0.0283  0.0040  0.0031  324 TYR D CD1 
13657 C CD2 . TYR D 324 ? 0.1647 0.4315 0.1558 0.0379  0.0015  0.0012  324 TYR D CD2 
13658 C CE1 . TYR D 324 ? 0.1940 0.4563 0.1794 0.0259  0.0039  0.0026  324 TYR D CE1 
13659 C CE2 . TYR D 324 ? 0.1365 0.4103 0.1290 0.0360  0.0010  0.0007  324 TYR D CE2 
13660 C CZ  . TYR D 324 ? 0.1616 0.4328 0.1511 0.0295  0.0024  0.0011  324 TYR D CZ  
13661 O OH  . TYR D 324 ? 0.2126 0.4899 0.2019 0.0264  0.0024  0.0000  324 TYR D OH  
13662 N N   . LEU D 325 ? 0.1733 0.4537 0.1630 0.0367  0.0024  -0.0016 325 LEU D N   
13663 C CA  . LEU D 325 ? 0.2023 0.4980 0.1948 0.0364  0.0013  -0.0027 325 LEU D CA  
13664 C C   . LEU D 325 ? 0.2068 0.5101 0.1986 0.0324  0.0023  -0.0037 325 LEU D C   
13665 O O   . LEU D 325 ? 0.1524 0.4666 0.1457 0.0280  0.0020  -0.0044 325 LEU D O   
13666 C CB  . LEU D 325 ? 0.1766 0.4772 0.1698 0.0438  -0.0001 -0.0029 325 LEU D CB  
13667 C CG  . LEU D 325 ? 0.1746 0.4681 0.1677 0.0471  -0.0006 -0.0021 325 LEU D CG  
13668 C CD1 . LEU D 325 ? 0.1498 0.4400 0.1403 0.0550  -0.0007 -0.0015 325 LEU D CD1 
13669 C CD2 . LEU D 325 ? 0.1850 0.4868 0.1799 0.0433  -0.0010 -0.0032 325 LEU D CD2 
13670 N N   . HIS D 326 ? 0.2462 0.5440 0.2354 0.0336  0.0037  -0.0039 326 HIS D N   
13671 C CA  . HIS D 326 ? 0.2202 0.5243 0.2085 0.0302  0.0049  -0.0047 326 HIS D CA  
13672 C C   . HIS D 326 ? 0.2023 0.5058 0.1900 0.0233  0.0056  -0.0038 326 HIS D C   
13673 O O   . HIS D 326 ? 0.1734 0.4867 0.1617 0.0192  0.0060  -0.0043 326 HIS D O   
13674 C CB  . HIS D 326 ? 0.1868 0.4833 0.1718 0.0324  0.0069  -0.0054 326 HIS D CB  
13675 C CG  . HIS D 326 ? 0.2691 0.5698 0.2529 0.0286  0.0083  -0.0060 326 HIS D CG  
13676 N ND1 . HIS D 326 ? 0.2925 0.6048 0.2772 0.0290  0.0086  -0.0068 326 HIS D ND1 
13677 C CD2 . HIS D 326 ? 0.2567 0.5522 0.2384 0.0248  0.0095  -0.0056 326 HIS D CD2 
13678 C CE1 . HIS D 326 ? 0.2924 0.6058 0.2756 0.0255  0.0101  -0.0070 326 HIS D CE1 
13679 N NE2 . HIS D 326 ? 0.2523 0.5558 0.2337 0.0230  0.0106  -0.0063 326 HIS D NE2 
13680 N N   . TYR D 327 ? 0.2044 0.4960 0.1903 0.0219  0.0061  -0.0023 327 TYR D N   
13681 C CA  A TYR D 327 ? 0.1921 0.4804 0.1756 0.0163  0.0074  -0.0007 327 TYR D CA  
13682 C CA  B TYR D 327 ? 0.1921 0.4805 0.1756 0.0163  0.0074  -0.0007 327 TYR D CA  
13683 C C   . TYR D 327 ? 0.1928 0.4868 0.1768 0.0128  0.0072  -0.0008 327 TYR D C   
13684 O O   . TYR D 327 ? 0.2030 0.5008 0.1849 0.0074  0.0087  -0.0007 327 TYR D O   
13685 C CB  A TYR D 327 ? 0.2018 0.4765 0.1827 0.0168  0.0078  0.0014  327 TYR D CB  
13686 C CB  B TYR D 327 ? 0.2016 0.4763 0.1825 0.0168  0.0078  0.0014  327 TYR D CB  
13687 C CG  A TYR D 327 ? 0.2003 0.4688 0.1782 0.0135  0.0086  0.0035  327 TYR D CG  
13688 C CG  B TYR D 327 ? 0.2030 0.4718 0.1799 0.0124  0.0092  0.0037  327 TYR D CG  
13689 C CD1 A TYR D 327 ? 0.1949 0.4612 0.1683 0.0089  0.0108  0.0052  327 TYR D CD1 
13690 C CD1 B TYR D 327 ? 0.1994 0.4666 0.1726 0.0091  0.0111  0.0053  327 TYR D CD1 
13691 C CD2 A TYR D 327 ? 0.1945 0.4582 0.1729 0.0153  0.0078  0.0039  327 TYR D CD2 
13692 C CD2 B TYR D 327 ? 0.1892 0.4532 0.1650 0.0120  0.0091  0.0046  327 TYR D CD2 
13693 C CE1 A TYR D 327 ? 0.2020 0.4602 0.1705 0.0062  0.0124  0.0073  327 TYR D CE1 
13694 C CE1 B TYR D 327 ? 0.2032 0.4631 0.1711 0.0058  0.0131  0.0079  327 TYR D CE1 
13695 C CE2 A TYR D 327 ? 0.2111 0.4676 0.1851 0.0124  0.0091  0.0057  327 TYR D CE2 
13696 C CE2 B TYR D 327 ? 0.1863 0.4426 0.1563 0.0082  0.0112  0.0068  327 TYR D CE2 
13697 C CZ  A TYR D 327 ? 0.1839 0.4370 0.1525 0.0078  0.0115  0.0074  327 TYR D CZ  
13698 C CZ  B TYR D 327 ? 0.2067 0.4605 0.1725 0.0053  0.0134  0.0086  327 TYR D CZ  
13699 O OH  A TYR D 327 ? 0.1534 0.3969 0.1155 0.0051  0.0135  0.0093  327 TYR D OH  
13700 O OH  B TYR D 327 ? 0.2031 0.4474 0.1616 0.0022  0.0163  0.0113  327 TYR D OH  
13701 N N   . ARG D 328 ? 0.1790 0.4731 0.1652 0.0156  0.0058  -0.0013 328 ARG D N   
13702 C CA  . ARG D 328 ? 0.1525 0.4516 0.1387 0.0120  0.0058  -0.0019 328 ARG D CA  
13703 C C   . ARG D 328 ? 0.1644 0.4805 0.1528 0.0084  0.0055  -0.0042 328 ARG D C   
13704 O O   . ARG D 328 ? 0.1561 0.4751 0.1417 0.0015  0.0073  -0.0046 328 ARG D O   
13705 C CB  . ARG D 328 ? 0.1751 0.4730 0.1639 0.0168  0.0040  -0.0022 328 ARG D CB  
13706 C CG  . ARG D 328 ? 0.1628 0.4627 0.1506 0.0132  0.0043  -0.0029 328 ARG D CG  
13707 C CD  . ARG D 328 ? 0.1498 0.4697 0.1415 0.0104  0.0032  -0.0060 328 ARG D CD  
13708 N NE  . ARG D 328 ? 0.1363 0.4599 0.1278 0.0077  0.0030  -0.0075 328 ARG D NE  
13709 C CZ  . ARG D 328 ? 0.1331 0.4511 0.1186 0.0001  0.0053  -0.0079 328 ARG D CZ  
13710 N NH1 . ARG D 328 ? 0.1342 0.4413 0.1132 -0.0048 0.0082  -0.0062 328 ARG D NH1 
13711 N NH2 . ARG D 328 ? 0.1500 0.4734 0.1353 -0.0026 0.0052  -0.0102 328 ARG D NH2 
13712 N N   . ILE D 329 ? 0.1840 0.5112 0.1765 0.0132  0.0035  -0.0056 329 ILE D N   
13713 C CA  . ILE D 329 ? 0.1901 0.5356 0.1851 0.0108  0.0027  -0.0077 329 ILE D CA  
13714 C C   . ILE D 329 ? 0.1898 0.5369 0.1824 0.0063  0.0047  -0.0075 329 ILE D C   
13715 O O   . ILE D 329 ? 0.2025 0.5616 0.1953 0.0005  0.0052  -0.0090 329 ILE D O   
13716 C CB  . ILE D 329 ? 0.2322 0.5869 0.2305 0.0189  0.0002  -0.0083 329 ILE D CB  
13717 C CG1 . ILE D 329 ? 0.2369 0.5869 0.2360 0.0229  -0.0008 -0.0082 329 ILE D CG1 
13718 C CG2 . ILE D 329 ? 0.2448 0.6176 0.2444 0.0175  -0.0006 -0.0101 329 ILE D CG2 
13719 C CD1 . ILE D 329 ? 0.1714 0.5181 0.1694 0.0320  -0.0013 -0.0077 329 ILE D CD1 
13720 N N   . GLY D 330 ? 0.2027 0.5383 0.1930 0.0084  0.0060  -0.0059 330 GLY D N   
13721 C CA  . GLY D 330 ? 0.1712 0.5073 0.1590 0.0043  0.0081  -0.0054 330 GLY D CA  
13722 C C   . GLY D 330 ? 0.1723 0.5037 0.1561 -0.0032 0.0106  -0.0044 330 GLY D C   
13723 O O   . GLY D 330 ? 0.1990 0.5365 0.1813 -0.0082 0.0125  -0.0047 330 GLY D O   
13724 N N   . GLN D 331 ? 0.2052 0.5244 0.1862 -0.0039 0.0112  -0.0029 331 GLN D N   
13725 C CA  . GLN D 331 ? 0.1628 0.4750 0.1378 -0.0106 0.0144  -0.0016 331 GLN D CA  
13726 C C   . GLN D 331 ? 0.1814 0.5063 0.1571 -0.0172 0.0151  -0.0043 331 GLN D C   
13727 O O   . GLN D 331 ? 0.2175 0.5430 0.1892 -0.0240 0.0185  -0.0042 331 GLN D O   
13728 C CB  . GLN D 331 ? 0.1602 0.4563 0.1312 -0.0091 0.0150  0.0007  331 GLN D CB  
13729 C CG  . GLN D 331 ? 0.2013 0.4897 0.1648 -0.0157 0.0188  0.0017  331 GLN D CG  
13730 C CD  . GLN D 331 ? 0.2156 0.4864 0.1735 -0.0135 0.0198  0.0046  331 GLN D CD  
13731 O OE1 . GLN D 331 ? 0.1905 0.4595 0.1488 -0.0127 0.0186  0.0036  331 GLN D OE1 
13732 N NE2 . GLN D 331 ? 0.2090 0.4673 0.1616 -0.0122 0.0220  0.0082  331 GLN D NE2 
13733 N N   . VAL D 332 ? 0.1687 0.5042 0.1492 -0.0155 0.0122  -0.0069 332 VAL D N   
13734 C CA  . VAL D 332 ? 0.1752 0.5270 0.1574 -0.0221 0.0121  -0.0103 332 VAL D CA  
13735 C C   . VAL D 332 ? 0.1894 0.5555 0.1737 -0.0245 0.0123  -0.0116 332 VAL D C   
13736 O O   . VAL D 332 ? 0.1816 0.5546 0.1638 -0.0330 0.0148  -0.0133 332 VAL D O   
13737 C CB  . VAL D 332 ? 0.1433 0.5060 0.1311 -0.0180 0.0083  -0.0126 332 VAL D CB  
13738 C CG1 . VAL D 332 ? 0.2436 0.6280 0.2342 -0.0243 0.0074  -0.0167 332 VAL D CG1 
13739 C CG2 . VAL D 332 ? 0.1730 0.5216 0.1579 -0.0170 0.0088  -0.0115 332 VAL D CG2 
13740 N N   . LYS D 333 ? 0.1902 0.5600 0.1780 -0.0172 0.0101  -0.0108 333 LYS D N   
13741 C CA  . LYS D 333 ? 0.1899 0.5724 0.1792 -0.0182 0.0103  -0.0117 333 LYS D CA  
13742 C C   . LYS D 333 ? 0.1895 0.5640 0.1740 -0.0237 0.0145  -0.0100 333 LYS D C   
13743 O O   . LYS D 333 ? 0.2336 0.6189 0.2181 -0.0290 0.0161  -0.0111 333 LYS D O   
13744 C CB  . LYS D 333 ? 0.2454 0.6291 0.2374 -0.0087 0.0080  -0.0109 333 LYS D CB  
13745 C CG  . LYS D 333 ? 0.2560 0.6529 0.2491 -0.0082 0.0081  -0.0116 333 LYS D CG  
13746 C CD  . LYS D 333 ? 0.1889 0.5819 0.1825 0.0008  0.0074  -0.0105 333 LYS D CD  
13747 C CE  . LYS D 333 ? 0.2426 0.6493 0.2370 0.0021  0.0077  -0.0110 333 LYS D CE  
13748 N NZ  . LYS D 333 ? 0.2386 0.6455 0.2311 -0.0047 0.0107  -0.0106 333 LYS D NZ  
13749 N N   . TYR D 334 ? 0.1935 0.5496 0.1737 -0.0223 0.0165  -0.0070 334 TYR D N   
13750 C CA  . TYR D 334 ? 0.2212 0.5687 0.1961 -0.0265 0.0208  -0.0046 334 TYR D CA  
13751 C C   . TYR D 334 ? 0.2019 0.5501 0.1728 -0.0361 0.0248  -0.0054 334 TYR D C   
13752 O O   . TYR D 334 ? 0.2086 0.5607 0.1778 -0.0412 0.0282  -0.0052 334 TYR D O   
13753 C CB  . TYR D 334 ? 0.1706 0.4992 0.1413 -0.0224 0.0217  -0.0011 334 TYR D CB  
13754 C CG  . TYR D 334 ? 0.2250 0.5432 0.1891 -0.0258 0.0264  0.0021  334 TYR D CG  
13755 C CD1 . TYR D 334 ? 0.2066 0.5270 0.1706 -0.0244 0.0275  0.0032  334 TYR D CD1 
13756 C CD2 . TYR D 334 ? 0.2281 0.5337 0.1853 -0.0300 0.0305  0.0042  334 TYR D CD2 
13757 C CE1 . TYR D 334 ? 0.2032 0.5147 0.1610 -0.0267 0.0321  0.0065  334 TYR D CE1 
13758 C CE2 . TYR D 334 ? 0.2378 0.5328 0.1881 -0.0320 0.0357  0.0078  334 TYR D CE2 
13759 C CZ  . TYR D 334 ? 0.2563 0.5548 0.2073 -0.0302 0.0363  0.0090  334 TYR D CZ  
13760 O OH  . TYR D 334 ? 0.2078 0.4965 0.1520 -0.0314 0.0417  0.0129  334 TYR D OH  
13761 N N   . LEU D 335 ? 0.2119 0.5558 0.1809 -0.0390 0.0250  -0.0064 335 LEU D N   
13762 C CA  . LEU D 335 ? 0.1984 0.5424 0.1629 -0.0492 0.0295  -0.0080 335 LEU D CA  
13763 C C   . LEU D 335 ? 0.2470 0.6127 0.2161 -0.0554 0.0288  -0.0122 335 LEU D C   
13764 O O   . LEU D 335 ? 0.2054 0.5726 0.1715 -0.0637 0.0337  -0.0128 335 LEU D O   
13765 C CB  . LEU D 335 ? 0.1881 0.5252 0.1500 -0.0509 0.0293  -0.0091 335 LEU D CB  
13766 C CG  . LEU D 335 ? 0.2003 0.5381 0.1573 -0.0625 0.0340  -0.0120 335 LEU D CG  
13767 C CD1 . LEU D 335 ? 0.2142 0.5384 0.1633 -0.0681 0.0416  -0.0090 335 LEU D CD1 
13768 C CD2 . LEU D 335 ? 0.2011 0.5291 0.1542 -0.0631 0.0340  -0.0127 335 LEU D CD2 
13769 N N   . GLY D 336 ? 0.2174 0.6002 0.1937 -0.0510 0.0232  -0.0149 336 GLY D N   
13770 C CA  . GLY D 336 ? 0.2357 0.6411 0.2161 -0.0557 0.0219  -0.0187 336 GLY D CA  
13771 C C   . GLY D 336 ? 0.2291 0.6382 0.2096 -0.0560 0.0240  -0.0172 336 GLY D C   
13772 O O   . GLY D 336 ? 0.2601 0.6801 0.2404 -0.0642 0.0265  -0.0194 336 GLY D O   
13773 N N   . ASP D 337 ? 0.2771 0.6774 0.2578 -0.0475 0.0232  -0.0137 337 ASP D N   
13774 C CA  . ASP D 337 ? 0.2460 0.6496 0.2267 -0.0471 0.0252  -0.0122 337 ASP D CA  
13775 C C   . ASP D 337 ? 0.2472 0.6401 0.2222 -0.0547 0.0317  -0.0102 337 ASP D C   
13776 O O   . ASP D 337 ? 0.2865 0.6878 0.2618 -0.0594 0.0345  -0.0106 337 ASP D O   
13777 C CB  . ASP D 337 ? 0.2271 0.6230 0.2086 -0.0369 0.0231  -0.0095 337 ASP D CB  
13778 C CG  . ASP D 337 ? 0.2761 0.6837 0.2627 -0.0292 0.0182  -0.0111 337 ASP D CG  
13779 O OD1 . ASP D 337 ? 0.2612 0.6864 0.2509 -0.0312 0.0163  -0.0137 337 ASP D OD1 
13780 O OD2 . ASP D 337 ? 0.2241 0.6232 0.2111 -0.0213 0.0166  -0.0096 337 ASP D OD2 
13781 N N   . ARG D 338 ? 0.2537 0.6274 0.2230 -0.0555 0.0348  -0.0077 338 ARG D N   
13782 C CA  . ARG D 338 ? 0.2460 0.6080 0.2087 -0.0625 0.0421  -0.0054 338 ARG D CA  
13783 C C   . ARG D 338 ? 0.2846 0.6578 0.2476 -0.0740 0.0453  -0.0093 338 ARG D C   
13784 O O   . ARG D 338 ? 0.3174 0.6905 0.2783 -0.0801 0.0508  -0.0084 338 ARG D O   
13785 C CB  . ARG D 338 ? 0.2742 0.6143 0.2297 -0.0613 0.0450  -0.0022 338 ARG D CB  
13786 C CG  . ARG D 338 ? 0.2743 0.6015 0.2280 -0.0516 0.0432  0.0020  338 ARG D CG  
13787 C CD  . ARG D 338 ? 0.3304 0.6510 0.2803 -0.0505 0.0477  0.0060  338 ARG D CD  
13788 N NE  . ARG D 338 ? 0.3347 0.6530 0.2802 -0.0589 0.0551  0.0068  338 ARG D NE  
13789 C CZ  . ARG D 338 ? 0.3644 0.6657 0.3015 -0.0624 0.0620  0.0099  338 ARG D CZ  
13790 N NH1 . ARG D 338 ? 0.3763 0.6615 0.3080 -0.0579 0.0622  0.0127  338 ARG D NH1 
13791 N NH2 . ARG D 338 ? 0.3918 0.6915 0.3255 -0.0703 0.0694  0.0105  338 ARG D NH2 
13792 N N   . LEU D 339 ? 0.3062 0.6898 0.2720 -0.0775 0.0420  -0.0138 339 LEU D N   
13793 C CA  . LEU D 339 ? 0.2935 0.6887 0.2595 -0.0897 0.0448  -0.0185 339 LEU D CA  
13794 C C   . LEU D 339 ? 0.3240 0.7416 0.2957 -0.0917 0.0430  -0.0211 339 LEU D C   
13795 O O   . LEU D 339 ? 0.3747 0.7959 0.3452 -0.1009 0.0482  -0.0222 339 LEU D O   
13796 C CB  . LEU D 339 ? 0.2642 0.6653 0.2311 -0.0926 0.0414  -0.0230 339 LEU D CB  
13797 C CG  . LEU D 339 ? 0.2734 0.6516 0.2330 -0.0935 0.0450  -0.0209 339 LEU D CG  
13798 C CD1 . LEU D 339 ? 0.2417 0.6264 0.2030 -0.0946 0.0409  -0.0251 339 LEU D CD1 
13799 C CD2 . LEU D 339 ? 0.2838 0.6477 0.2355 -0.1043 0.0545  -0.0202 339 LEU D CD2 
13800 N N   . ARG D 340 ? 0.2601 0.6924 0.2377 -0.0829 0.0361  -0.0217 340 ARG D N   
13801 C CA  . ARG D 340 ? 0.2949 0.7490 0.2769 -0.0845 0.0344  -0.0239 340 ARG D CA  
13802 C C   . ARG D 340 ? 0.3525 0.8026 0.3341 -0.0817 0.0376  -0.0201 340 ARG D C   
13803 O O   . ARG D 340 ? 0.3577 0.8217 0.3413 -0.0865 0.0393  -0.0214 340 ARG D O   
13804 C CB  . ARG D 340 ? 0.2719 0.7432 0.2590 -0.0757 0.0269  -0.0256 340 ARG D CB  
13805 C CG  . ARG D 340 ? 0.3117 0.7766 0.3005 -0.0624 0.0237  -0.0217 340 ARG D CG  
13806 C CD  . ARG D 340 ? 0.3610 0.8394 0.3537 -0.0540 0.0173  -0.0231 340 ARG D CD  
13807 N NE  . ARG D 340 ? 0.3064 0.8087 0.3016 -0.0546 0.0153  -0.0253 340 ARG D NE  
13808 C CZ  . ARG D 340 ? 0.3473 0.8570 0.3441 -0.0469 0.0141  -0.0233 340 ARG D CZ  
13809 N NH1 . ARG D 340 ? 0.3163 0.8119 0.3128 -0.0389 0.0149  -0.0197 340 ARG D NH1 
13810 N NH2 . ARG D 340 ? 0.3996 0.9318 0.3980 -0.0474 0.0124  -0.0251 340 ARG D NH2 
13811 N N   . GLU D 341 ? 0.2766 0.7086 0.2556 -0.0743 0.0386  -0.0154 341 GLU D N   
13812 C CA  . GLU D 341 ? 0.2816 0.7084 0.2589 -0.0732 0.0426  -0.0119 341 GLU D CA  
13813 C C   . GLU D 341 ? 0.3602 0.7808 0.3335 -0.0841 0.0506  -0.0114 341 GLU D C   
13814 O O   . GLU D 341 ? 0.3329 0.7547 0.3059 -0.0853 0.0544  -0.0093 341 GLU D O   
13815 C CB  . GLU D 341 ? 0.3190 0.7278 0.2933 -0.0641 0.0424  -0.0074 341 GLU D CB  
13816 C CG  . GLU D 341 ? 0.3368 0.7500 0.3148 -0.0532 0.0361  -0.0075 341 GLU D CG  
13817 C CD  . GLU D 341 ? 0.3224 0.7171 0.2971 -0.0462 0.0357  -0.0042 341 GLU D CD  
13818 O OE1 . GLU D 341 ? 0.4179 0.7989 0.3875 -0.0479 0.0403  -0.0009 341 GLU D OE1 
13819 O OE2 . GLU D 341 ? 0.2979 0.6919 0.2750 -0.0388 0.0311  -0.0047 341 GLU D OE2 
13820 N N   . ALA D 342 ? 0.3000 0.7133 0.2699 -0.0922 0.0536  -0.0132 342 ALA D N   
13821 C CA  . ALA D 342 ? 0.3196 0.7256 0.2852 -0.1036 0.0621  -0.0133 342 ALA D CA  
13822 C C   . ALA D 342 ? 0.4051 0.8308 0.3743 -0.1152 0.0623  -0.0195 342 ALA D C   
13823 O O   . ALA D 342 ? 0.4531 0.8734 0.4190 -0.1267 0.0696  -0.0208 342 ALA D O   
13824 C CB  . ALA D 342 ? 0.2989 0.6816 0.2568 -0.1059 0.0669  -0.0112 342 ALA D CB  
13825 N N   . GLY D 343 ? 0.3187 0.7667 0.2941 -0.1124 0.0548  -0.0234 343 GLY D N   
13826 C CA  . GLY D 343 ? 0.3569 0.8269 0.3356 -0.1224 0.0543  -0.0294 343 GLY D CA  
13827 C C   . GLY D 343 ? 0.4322 0.9052 0.4094 -0.1311 0.0535  -0.0352 343 GLY D C   
13828 O O   . GLY D 343 ? 0.4324 0.9182 0.4100 -0.1433 0.0557  -0.0407 343 GLY D O   
13829 N N   . ILE D 344 ? 0.3947 0.8563 0.3699 -0.1255 0.0506  -0.0343 344 ILE D N   
13830 C CA  . ILE D 344 ? 0.3609 0.8253 0.3344 -0.1325 0.0493  -0.0398 344 ILE D CA  
13831 C C   . ILE D 344 ? 0.3978 0.8835 0.3767 -0.1243 0.0399  -0.0423 344 ILE D C   
13832 O O   . ILE D 344 ? 0.4150 0.8969 0.3962 -0.1108 0.0352  -0.0381 344 ILE D O   
13833 C CB  . ILE D 344 ? 0.3833 0.8209 0.3505 -0.1314 0.0529  -0.0368 344 ILE D CB  
13834 C CG1 . ILE D 344 ? 0.3813 0.7984 0.3415 -0.1410 0.0634  -0.0348 344 ILE D CG1 
13835 C CG2 . ILE D 344 ? 0.3791 0.8213 0.3456 -0.1353 0.0497  -0.0421 344 ILE D CG2 
13836 C CD1 . ILE D 344 ? 0.4903 0.8797 0.4423 -0.1398 0.0681  -0.0312 344 ILE D CD1 
13837 N N   . PRO D 345 ? 0.4619 0.9697 0.4423 -0.1316 0.0372  -0.0490 345 PRO D N   
13838 C CA  . PRO D 345 ? 0.4350 0.9642 0.4194 -0.1224 0.0287  -0.0505 345 PRO D CA  
13839 C C   . PRO D 345 ? 0.4599 0.9812 0.4438 -0.1160 0.0247  -0.0503 345 PRO D C   
13840 O O   . PRO D 345 ? 0.4615 0.9731 0.4419 -0.1242 0.0275  -0.0533 345 PRO D O   
13841 C CB  . PRO D 345 ? 0.4700 1.0242 0.4539 -0.1337 0.0283  -0.0579 345 PRO D CB  
13842 C CG  . PRO D 345 ? 0.5134 1.0548 0.4929 -0.1503 0.0361  -0.0618 345 PRO D CG  
13843 C CD  . PRO D 345 ? 0.4085 0.9234 0.3863 -0.1487 0.0424  -0.0553 345 PRO D CD  
13844 N N   . ILE D 346 ? 0.3497 0.8745 0.3372 -0.1012 0.0187  -0.0467 346 ILE D N   
13845 C CA  . ILE D 346 ? 0.4326 0.9513 0.4211 -0.0932 0.0146  -0.0458 346 ILE D CA  
13846 C C   . ILE D 346 ? 0.3309 0.8703 0.3225 -0.0825 0.0074  -0.0461 346 ILE D C   
13847 O O   . ILE D 346 ? 0.3001 0.8525 0.2928 -0.0781 0.0062  -0.0449 346 ILE D O   
13848 C CB  . ILE D 346 ? 0.3271 0.8194 0.3154 -0.0842 0.0160  -0.0394 346 ILE D CB  
13849 C CG1 . ILE D 346 ? 0.2843 0.7766 0.2751 -0.0735 0.0145  -0.0348 346 ILE D CG1 
13850 C CG2 . ILE D 346 ? 0.3505 0.8208 0.3332 -0.0933 0.0235  -0.0382 346 ILE D CG2 
13851 C CD1 . ILE D 346 ? 0.2778 0.7478 0.2683 -0.0638 0.0147  -0.0294 346 ILE D CD1 
13852 N N   . GLN D 347 ? 0.2355 0.7698 0.2286 -0.0766 0.0058  -0.0461 347 GLN D N   
13853 C CA  . GLN D 347 ? 0.2463 0.7834 0.2423 -0.0620 0.0033  -0.0433 347 GLN D CA  
13854 C C   . GLN D 347 ? 0.2903 0.8157 0.2881 -0.0498 0.0022  -0.0373 347 GLN D C   
13855 O O   . GLN D 347 ? 0.2991 0.8064 0.2975 -0.0449 0.0019  -0.0344 347 GLN D O   
13856 C CB  . GLN D 347 ? 0.3453 0.8756 0.3423 -0.0581 0.0025  -0.0440 347 GLN D CB  
13857 C CG  . GLN D 347 ? 0.2859 0.8131 0.2852 -0.0419 0.0001  -0.0400 347 GLN D CG  
13858 C CD  . GLN D 347 ? 0.3814 0.9290 0.3802 -0.0388 -0.0008 -0.0415 347 GLN D CD  
13859 O OE1 . GLN D 347 ? 0.3130 0.8745 0.3112 -0.0399 -0.0006 -0.0416 347 GLN D OE1 
13860 N NE2 . GLN D 347 ? 0.2619 0.8120 0.2607 -0.0346 -0.0018 -0.0425 347 GLN D NE2 
13861 N N   . TYR D 348 ? 0.1878 0.7237 0.1860 -0.0455 0.0017  -0.0357 348 TYR D N   
13862 C CA  . TYR D 348 ? 0.2683 0.7940 0.2677 -0.0349 0.0010  -0.0308 348 TYR D CA  
13863 C C   . TYR D 348 ? 0.2604 0.7868 0.2608 -0.0211 -0.0006 -0.0282 348 TYR D C   
13864 O O   . TYR D 348 ? 0.2709 0.8140 0.2711 -0.0198 -0.0011 -0.0295 348 TYR D O   
13865 C CB  . TYR D 348 ? 0.2213 0.7568 0.2202 -0.0387 0.0018  -0.0304 348 TYR D CB  
13866 C CG  . TYR D 348 ? 0.2924 0.8171 0.2919 -0.0299 0.0015  -0.0260 348 TYR D CG  
13867 C CD1 . TYR D 348 ? 0.3313 0.8323 0.3304 -0.0295 0.0039  -0.0237 348 TYR D CD1 
13868 C CD2 . TYR D 348 ? 0.3383 0.8719 0.3385 -0.0218 0.0009  -0.0238 348 TYR D CD2 
13869 C CE1 . TYR D 348 ? 0.3060 0.7936 0.3049 -0.0218 0.0053  -0.0201 348 TYR D CE1 
13870 C CE2 . TYR D 348 ? 0.2807 0.8001 0.2811 -0.0142 0.0026  -0.0202 348 TYR D CE2 
13871 C CZ  . TYR D 348 ? 0.3367 0.8334 0.3363 -0.0147 0.0047  -0.0187 348 TYR D CZ  
13872 O OH  . TYR D 348 ? 0.3195 0.8028 0.3185 -0.0079 0.0064  -0.0159 348 TYR D OH  
13873 N N   . PRO D 349 ? 0.1834 0.6927 0.1843 -0.0111 -0.0012 -0.0247 349 PRO D N   
13874 C CA  . PRO D 349 ? 0.1926 0.6827 0.1936 -0.0113 -0.0006 -0.0229 349 PRO D CA  
13875 C C   . PRO D 349 ? 0.2245 0.7048 0.2255 -0.0160 -0.0005 -0.0245 349 PRO D C   
13876 O O   . PRO D 349 ? 0.2298 0.7158 0.2311 -0.0167 -0.0010 -0.0266 349 PRO D O   
13877 C CB  . PRO D 349 ? 0.2563 0.7356 0.2574 0.0018  -0.0013 -0.0193 349 PRO D CB  
13878 C CG  . PRO D 349 ? 0.2359 0.7229 0.2367 0.0086  -0.0022 -0.0193 349 PRO D CG  
13879 C CD  . PRO D 349 ? 0.2253 0.7343 0.2262 0.0018  -0.0022 -0.0220 349 PRO D CD  
13880 N N   . THR D 350 ? 0.1945 0.6610 0.1952 -0.0191 0.0003  -0.0233 350 THR D N   
13881 C CA  . THR D 350 ? 0.2038 0.6606 0.2043 -0.0227 0.0006  -0.0241 350 THR D CA  
13882 C C   . THR D 350 ? 0.2312 0.6774 0.2328 -0.0120 -0.0005 -0.0224 350 THR D C   
13883 O O   . THR D 350 ? 0.2415 0.6809 0.2432 -0.0021 -0.0011 -0.0196 350 THR D O   
13884 C CB  . THR D 350 ? 0.1827 0.6234 0.1810 -0.0266 0.0028  -0.0221 350 THR D CB  
13885 O OG1 . THR D 350 ? 0.1972 0.6252 0.1954 -0.0177 0.0030  -0.0185 350 THR D OG1 
13886 C CG2 . THR D 350 ? 0.1898 0.6319 0.1846 -0.0377 0.0069  -0.0234 350 THR D CG2 
13887 N N   . GLY D 351 ? 0.1562 0.6013 0.1581 -0.0147 -0.0006 -0.0242 351 GLY D N   
13888 C CA  . GLY D 351 ? 0.2042 0.6389 0.2069 -0.0056 -0.0015 -0.0226 351 GLY D CA  
13889 C C   . GLY D 351 ? 0.1954 0.6108 0.1977 -0.0019 -0.0011 -0.0196 351 GLY D C   
13890 O O   . GLY D 351 ? 0.2017 0.6116 0.2032 -0.0044 -0.0004 -0.0181 351 GLY D O   
13891 N N   . GLY D 352 ? 0.1461 0.5516 0.1488 0.0041  -0.0016 -0.0185 352 GLY D N   
13892 C CA  . GLY D 352 ? 0.1318 0.5192 0.1338 0.0084  -0.0013 -0.0156 352 GLY D CA  
13893 C C   . GLY D 352 ? 0.2048 0.5871 0.2061 0.0011  -0.0004 -0.0157 352 GLY D C   
13894 O O   . GLY D 352 ? 0.2032 0.5729 0.2031 0.0024  0.0002  -0.0131 352 GLY D O   
13895 N N   . HIS D 353 ? 0.1703 0.5619 0.1716 -0.0068 0.0001  -0.0187 353 HIS D N   
13896 C CA  . HIS D 353 ? 0.1889 0.5683 0.1861 -0.0122 0.0021  -0.0184 353 HIS D CA  
13897 C C   . HIS D 353 ? 0.1889 0.5683 0.1799 -0.0249 0.0055  -0.0207 353 HIS D C   
13898 O O   . HIS D 353 ? 0.1630 0.5238 0.1458 -0.0291 0.0088  -0.0195 353 HIS D O   
13899 C CB  . HIS D 353 ? 0.1424 0.5240 0.1419 -0.0095 0.0010  -0.0196 353 HIS D CB  
13900 C CG  . HIS D 353 ? 0.1672 0.5675 0.1687 -0.0152 0.0007  -0.0243 353 HIS D CG  
13901 N ND1 . HIS D 353 ? 0.1518 0.5634 0.1549 -0.0128 -0.0001 -0.0257 353 HIS D ND1 
13902 C CD2 . HIS D 353 ? 0.1587 0.5667 0.1593 -0.0237 0.0016  -0.0281 353 HIS D CD2 
13903 C CE1 . HIS D 353 ? 0.1898 0.6160 0.1936 -0.0192 0.0003  -0.0300 353 HIS D CE1 
13904 N NE2 . HIS D 353 ? 0.2023 0.6264 0.2046 -0.0264 0.0014  -0.0320 353 HIS D NE2 
13905 N N   . ALA D 354 ? 0.1519 0.5503 0.1452 -0.0310 0.0051  -0.0238 354 ALA D N   
13906 C CA  . ALA D 354 ? 0.1807 0.5805 0.1682 -0.0443 0.0089  -0.0269 354 ALA D CA  
13907 C C   . ALA D 354 ? 0.2671 0.6826 0.2566 -0.0484 0.0087  -0.0285 354 ALA D C   
13908 O O   . ALA D 354 ? 0.2274 0.6597 0.2232 -0.0421 0.0045  -0.0288 354 ALA D O   
13909 C CB  . ALA D 354 ? 0.1626 0.5743 0.1505 -0.0519 0.0088  -0.0321 354 ALA D CB  
13910 N N   . VAL D 355 ? 0.1785 0.5869 0.1614 -0.0584 0.0136  -0.0291 355 VAL D N   
13911 C CA  . VAL D 355 ? 0.2411 0.6651 0.2249 -0.0653 0.0144  -0.0316 355 VAL D CA  
13912 C C   . VAL D 355 ? 0.2661 0.7064 0.2492 -0.0778 0.0152  -0.0383 355 VAL D C   
13913 O O   . VAL D 355 ? 0.2471 0.6761 0.2243 -0.0859 0.0191  -0.0402 355 VAL D O   
13914 C CB  . VAL D 355 ? 0.1962 0.6031 0.1736 -0.0689 0.0201  -0.0282 355 VAL D CB  
13915 C CG1 . VAL D 355 ? 0.1932 0.6157 0.1718 -0.0760 0.0215  -0.0307 355 VAL D CG1 
13916 C CG2 . VAL D 355 ? 0.1782 0.5706 0.1562 -0.0571 0.0189  -0.0225 355 VAL D CG2 
13917 N N   . PHE D 356 ? 0.2492 0.7159 0.2371 -0.0793 0.0113  -0.0421 356 PHE D N   
13918 C CA  . PHE D 356 ? 0.3386 0.8250 0.3257 -0.0916 0.0112  -0.0495 356 PHE D CA  
13919 C C   . PHE D 356 ? 0.3619 0.8548 0.3458 -0.1019 0.0150  -0.0518 356 PHE D C   
13920 O O   . PHE D 356 ? 0.4099 0.9180 0.3966 -0.0974 0.0121  -0.0512 356 PHE D O   
13921 C CB  . PHE D 356 ? 0.3857 0.8878 0.3777 -0.0831 0.0072  -0.0508 356 PHE D CB  
13922 C CG  . PHE D 356 ? 0.3630 0.8559 0.3575 -0.0750 0.0060  -0.0493 356 PHE D CG  
13923 C CD1 . PHE D 356 ? 0.3275 0.8049 0.3245 -0.0618 0.0044  -0.0432 356 PHE D CD1 
13924 C CD2 . PHE D 356 ? 0.3944 0.8948 0.3887 -0.0809 0.0067  -0.0542 356 PHE D CD2 
13925 C CE1 . PHE D 356 ? 0.3358 0.8049 0.3348 -0.0545 0.0035  -0.0419 356 PHE D CE1 
13926 C CE2 . PHE D 356 ? 0.3461 0.8391 0.3432 -0.0732 0.0058  -0.0527 356 PHE D CE2 
13927 C CZ  . PHE D 356 ? 0.2688 0.7460 0.2681 -0.0599 0.0042  -0.0464 356 PHE D CZ  
13928 N N   . VAL D 357 ? 0.4198 0.8999 0.3973 -0.1153 0.0221  -0.0542 357 VAL D N   
13929 C CA  . VAL D 357 ? 0.4525 0.9382 0.4274 -0.1265 0.0268  -0.0568 357 VAL D CA  
13930 C C   . VAL D 357 ? 0.6712 1.1854 0.6467 -0.1359 0.0240  -0.0652 357 VAL D C   
13931 O O   . VAL D 357 ? 0.6733 1.1929 0.6467 -0.1429 0.0235  -0.0709 357 VAL D O   
13932 C CB  . VAL D 357 ? 0.4750 0.9347 0.4418 -0.1374 0.0363  -0.0561 357 VAL D CB  
13933 C CG1 . VAL D 357 ? 0.5356 1.0003 0.5006 -0.1493 0.0419  -0.0587 357 VAL D CG1 
13934 C CG2 . VAL D 357 ? 0.4417 0.8744 0.4057 -0.1266 0.0386  -0.0474 357 VAL D CG2 
13935 N N   . ASP D 358 ? 0.8406 1.3733 0.8181 -0.1358 0.0225  -0.0660 358 ASP D N   
13936 C CA  . ASP D 358 ? 0.9603 1.5225 0.9369 -0.1412 0.0192  -0.0729 358 ASP D CA  
13937 C C   . ASP D 358 ? 1.0653 1.6290 1.0364 -0.1612 0.0256  -0.0810 358 ASP D C   
13938 O O   . ASP D 358 ? 1.0644 1.6049 1.0323 -0.1705 0.0328  -0.0809 358 ASP D O   
13939 C CB  . ASP D 358 ? 0.9264 1.5058 0.9058 -0.1340 0.0165  -0.0703 358 ASP D CB  
13940 C CG  . ASP D 358 ? 1.0178 1.6197 0.9986 -0.1295 0.0141  -0.0727 358 ASP D CG  
13941 O OD1 . ASP D 358 ? 1.0192 1.6236 0.9994 -0.1314 0.0145  -0.0764 358 ASP D OD1 
13942 O OD2 . ASP D 358 ? 1.0352 1.6515 1.0181 -0.1234 0.0127  -0.0704 358 ASP D OD2 
13943 N N   . CYS D 359 ? 1.1418 1.7324 1.1105 -0.1674 0.0238  -0.0878 359 CYS D N   
13944 C CA  . CYS D 359 ? 1.0911 1.6862 1.0539 -0.1868 0.0296  -0.0970 359 CYS D CA  
13945 C C   . CYS D 359 ? 1.0658 1.6427 1.0284 -0.1986 0.0383  -0.0962 359 CYS D C   
13946 O O   . CYS D 359 ? 1.0468 1.6186 1.0135 -0.1921 0.0391  -0.0896 359 CYS D O   
13947 C CB  . CYS D 359 ? 1.0520 1.6776 1.0144 -0.1883 0.0280  -0.1020 359 CYS D CB  
13948 S SG  . CYS D 359 ? 1.1976 1.8429 1.1621 -0.1880 0.0275  -0.1002 359 CYS D SG  
13949 N N   . LYS D 360 ? 0.9000 1.4656 0.8565 -0.2160 0.0455  -0.1029 360 LYS D N   
13950 C CA  . LYS D 360 ? 0.8443 1.3843 0.7982 -0.2267 0.0555  -0.1012 360 LYS D CA  
13951 C C   . LYS D 360 ? 0.8287 1.3827 0.7852 -0.2330 0.0581  -0.1023 360 LYS D C   
13952 O O   . LYS D 360 ? 0.7959 1.3585 0.7490 -0.2490 0.0628  -0.1104 360 LYS D O   
13953 C CB  . LYS D 360 ? 0.7863 1.3087 0.7318 -0.2434 0.0630  -0.1083 360 LYS D CB  
13954 C CG  . LYS D 360 ? 0.8560 1.3596 0.7990 -0.2364 0.0616  -0.1054 360 LYS D CG  
13955 C CD  . LYS D 360 ? 0.6932 1.1764 0.6394 -0.2200 0.0610  -0.0932 360 LYS D CD  
13956 C CE  . LYS D 360 ? 0.6266 1.1060 0.5747 -0.2062 0.0545  -0.0893 360 LYS D CE  
13957 N NZ  . LYS D 360 ? 0.5292 0.9746 0.4731 -0.1989 0.0596  -0.0804 360 LYS D NZ  
13958 N N   . LYS D 361 ? 0.7807 1.3369 0.7432 -0.2198 0.0553  -0.0941 361 LYS D N   
13959 C CA  . LYS D 361 ? 0.7750 1.3360 0.7403 -0.2238 0.0593  -0.0924 361 LYS D CA  
13960 C C   . LYS D 361 ? 0.8019 1.3308 0.7643 -0.2287 0.0692  -0.0874 361 LYS D C   
13961 O O   . LYS D 361 ? 0.7484 1.2766 0.7134 -0.2289 0.0729  -0.0837 361 LYS D O   
13962 C CB  . LYS D 361 ? 0.6861 1.2641 0.6582 -0.2069 0.0519  -0.0860 361 LYS D CB  
13963 C CG  . LYS D 361 ? 0.6168 1.2254 0.5900 -0.2002 0.0431  -0.0897 361 LYS D CG  
13964 C CD  . LYS D 361 ? 0.6727 1.2879 0.6507 -0.1800 0.0358  -0.0820 361 LYS D CD  
13965 C CE  . LYS D 361 ? 0.7054 1.3275 0.6877 -0.1765 0.0371  -0.0775 361 LYS D CE  
13966 N NZ  . LYS D 361 ? 0.7398 1.3646 0.7257 -0.1573 0.0310  -0.0701 361 LYS D NZ  
13967 N N   . LEU D 362 ? 0.7744 1.2764 0.7306 -0.2316 0.0738  -0.0868 362 LEU D N   
13968 C CA  . LEU D 362 ? 0.8464 1.3154 0.7967 -0.2364 0.0846  -0.0820 362 LEU D CA  
13969 C C   . LEU D 362 ? 0.8982 1.3524 0.8398 -0.2556 0.0936  -0.0897 362 LEU D C   
13970 O O   . LEU D 362 ? 0.8433 1.2679 0.7781 -0.2605 0.1039  -0.0861 362 LEU D O   
13971 C CB  . LEU D 362 ? 0.7972 1.2420 0.7451 -0.2218 0.0840  -0.0730 362 LEU D CB  
13972 C CG  . LEU D 362 ? 0.7019 1.1507 0.6559 -0.2031 0.0779  -0.0641 362 LEU D CG  
13973 C CD1 . LEU D 362 ? 0.6159 1.0420 0.5664 -0.1905 0.0770  -0.0572 362 LEU D CD1 
13974 C CD2 . LEU D 362 ? 0.8455 1.2894 0.8008 -0.2028 0.0836  -0.0589 362 LEU D CD2 
13975 N N   . VAL D 363 ? 1.1645 1.6371 1.1051 -0.2658 0.0905  -0.1001 363 VAL D N   
13976 C CA  . VAL D 363 ? 1.2084 1.6691 1.1403 -0.2859 0.0991  -0.1092 363 VAL D CA  
13977 C C   . VAL D 363 ? 1.1927 1.6875 1.1270 -0.2970 0.0954  -0.1201 363 VAL D C   
13978 O O   . VAL D 363 ? 1.1937 1.7032 1.1255 -0.3007 0.0909  -0.1278 363 VAL D O   
13979 C CB  . VAL D 363 ? 1.1921 1.6328 1.1161 -0.2874 0.1006  -0.1113 363 VAL D CB  
13980 C CG1 . VAL D 363 ? 1.2552 1.6748 1.1683 -0.3076 0.1120  -0.1192 363 VAL D CG1 
13981 C CG2 . VAL D 363 ? 1.1767 1.5899 1.0990 -0.2722 0.1018  -0.0995 363 VAL D CG2 
13982 N N   . PRO D 364 ? 0.9505 1.4593 0.8889 -0.3018 0.0973  -0.1207 364 PRO D N   
13983 C CA  . PRO D 364 ? 0.8774 1.4217 0.8179 -0.3101 0.0932  -0.1300 364 PRO D CA  
13984 C C   . PRO D 364 ? 0.8369 1.3780 0.7687 -0.3315 0.1003  -0.1423 364 PRO D C   
13985 O O   . PRO D 364 ? 0.7568 1.3264 0.6878 -0.3366 0.0958  -0.1509 364 PRO D O   
13986 C CB  . PRO D 364 ? 0.8869 1.4421 0.8340 -0.3088 0.0946  -0.1257 364 PRO D CB  
13987 C CG  . PRO D 364 ? 0.8970 1.4161 0.8415 -0.3099 0.1045  -0.1184 364 PRO D CG  
13988 C CD  . PRO D 364 ? 0.9341 1.4287 0.8752 -0.2988 0.1033  -0.1124 364 PRO D CD  
13989 N N   . GLN D 365 ? 0.8700 1.3767 0.7941 -0.3437 0.1119  -0.1432 365 GLN D N   
13990 C CA  . GLN D 365 ? 0.8128 1.3125 0.7274 -0.3653 0.1203  -0.1553 365 GLN D CA  
13991 C C   . GLN D 365 ? 0.8814 1.3800 0.7887 -0.3687 0.1181  -0.1627 365 GLN D C   
13992 O O   . GLN D 365 ? 0.8471 1.3460 0.7463 -0.3862 0.1237  -0.1742 365 GLN D O   
13993 C CB  . GLN D 365 ? 0.8060 1.2648 0.7130 -0.3755 0.1344  -0.1530 365 GLN D CB  
13994 C CG  . GLN D 365 ? 0.8388 1.2590 0.7385 -0.3689 0.1389  -0.1463 365 GLN D CG  
13995 C CD  . GLN D 365 ? 0.8916 1.3048 0.7982 -0.3472 0.1342  -0.1317 365 GLN D CD  
13996 O OE1 . GLN D 365 ? 0.8194 1.2576 0.7366 -0.3361 0.1264  -0.1268 365 GLN D OE1 
13997 N NE2 . GLN D 365 ? 0.9099 1.2880 0.8094 -0.3409 0.1396  -0.1244 365 GLN D NE2 
13998 N N   . ILE D 366 ? 0.8837 1.3810 0.7935 -0.3527 0.1104  -0.1566 366 ILE D N   
13999 C CA  . ILE D 366 ? 0.9657 1.4606 0.8690 -0.3544 0.1083  -0.1623 366 ILE D CA  
14000 C C   . ILE D 366 ? 1.0172 1.5540 0.9262 -0.3448 0.0964  -0.1651 366 ILE D C   
14001 O O   . ILE D 366 ? 0.9883 1.5389 0.9061 -0.3263 0.0874  -0.1564 366 ILE D O   
14002 C CB  . ILE D 366 ? 0.9729 1.4359 0.8741 -0.3430 0.1089  -0.1533 366 ILE D CB  
14003 C CG1 . ILE D 366 ? 0.9248 1.3441 0.8168 -0.3524 0.1227  -0.1506 366 ILE D CG1 
14004 C CG2 . ILE D 366 ? 0.9168 1.3825 0.8132 -0.3424 0.1049  -0.1585 366 ILE D CG2 
14005 C CD1 . ILE D 366 ? 0.9261 1.3118 0.8130 -0.3421 0.1252  -0.1419 366 ILE D CD1 
14006 N N   . PRO D 367 ? 1.2233 1.7805 1.1268 -0.3559 0.0969  -0.1765 367 PRO D N   
14007 C CA  . PRO D 367 ? 1.2170 1.8137 1.1245 -0.3450 0.0872  -0.1780 367 PRO D CA  
14008 C C   . PRO D 367 ? 1.2323 1.8261 1.1388 -0.3314 0.0812  -0.1746 367 PRO D C   
14009 O O   . PRO D 367 ? 1.2267 1.7902 1.1325 -0.3268 0.0821  -0.1689 367 PRO D O   
14010 C CB  . PRO D 367 ? 1.1829 1.7989 1.0840 -0.3630 0.0925  -0.1909 367 PRO D CB  
14011 C CG  . PRO D 367 ? 1.1922 1.7718 1.0830 -0.3814 0.1037  -0.1973 367 PRO D CG  
14012 C CD  . PRO D 367 ? 1.2307 1.7761 1.1237 -0.3788 0.1076  -0.1883 367 PRO D CD  
14013 N N   . GLY D 368 ? 0.8752 1.5893 1.0867 -0.2283 0.0194  -0.2961 368 GLY D N   
14014 C CA  . GLY D 368 ? 0.7851 1.4910 0.9796 -0.2126 0.0087  -0.2872 368 GLY D CA  
14015 C C   . GLY D 368 ? 0.7572 1.4484 0.9449 -0.2185 0.0091  -0.2875 368 GLY D C   
14016 O O   . GLY D 368 ? 0.7919 1.4653 0.9624 -0.2149 0.0090  -0.2740 368 GLY D O   
14017 N N   . ASP D 369 ? 0.7669 1.4657 0.9686 -0.2273 0.0095  -0.3037 369 ASP D N   
14018 C CA  . ASP D 369 ? 0.7811 1.4674 0.9776 -0.2318 0.0089  -0.3064 369 ASP D CA  
14019 C C   . ASP D 369 ? 0.7670 1.4316 0.9632 -0.2489 0.0215  -0.3007 369 ASP D C   
14020 O O   . ASP D 369 ? 0.7366 1.3889 0.9302 -0.2540 0.0220  -0.3038 369 ASP D O   
14021 C CB  . ASP D 369 ? 0.7827 1.4847 0.9946 -0.2338 0.0036  -0.3264 369 ASP D CB  
14022 C CG  . ASP D 369 ? 0.8387 1.5326 1.0406 -0.2302 -0.0027 -0.3293 369 ASP D CG  
14023 O OD1 . ASP D 369 ? 0.6817 1.3606 0.8639 -0.2232 -0.0048 -0.3157 369 ASP D OD1 
14024 O OD2 . ASP D 369 ? 0.8474 1.5502 1.0612 -0.2342 -0.0055 -0.3455 369 ASP D OD2 
14025 N N   . GLN D 370 ? 0.7757 1.4341 0.9744 -0.2576 0.0313  -0.2924 370 GLN D N   
14026 C CA  . GLN D 370 ? 0.7883 1.4207 0.9822 -0.2708 0.0418  -0.2813 370 GLN D CA  
14027 C C   . GLN D 370 ? 0.7276 1.3443 0.9006 -0.2620 0.0410  -0.2620 370 GLN D C   
14028 O O   . GLN D 370 ? 0.7305 1.3236 0.8978 -0.2712 0.0489  -0.2506 370 GLN D O   
14029 C CB  . GLN D 370 ? 0.8194 1.4505 1.0276 -0.2869 0.0536  -0.2816 370 GLN D CB  
14030 C CG  . GLN D 370 ? 0.8248 1.4634 1.0550 -0.3005 0.0575  -0.2990 370 GLN D CG  
14031 C CD  . GLN D 370 ? 0.8032 1.4201 1.0356 -0.3107 0.0606  -0.3010 370 GLN D CD  
14032 O OE1 . GLN D 370 ? 0.7475 1.3657 0.9760 -0.3036 0.0528  -0.3083 370 GLN D OE1 
14033 N NE2 . GLN D 370 ? 0.7489 1.3451 0.9875 -0.3271 0.0719  -0.2942 370 GLN D NE2 
14034 N N   . PHE D 371 ? 0.7578 1.3856 0.9198 -0.2441 0.0311  -0.2576 371 PHE D N   
14035 C CA  . PHE D 371 ? 0.7550 1.3704 0.8972 -0.2326 0.0279  -0.2406 371 PHE D CA  
14036 C C   . PHE D 371 ? 0.7113 1.3157 0.8490 -0.2367 0.0358  -0.2262 371 PHE D C   
14037 O O   . PHE D 371 ? 0.6813 1.2626 0.8110 -0.2437 0.0421  -0.2149 371 PHE D O   
14038 C CB  . PHE D 371 ? 0.7446 1.3412 0.8761 -0.2343 0.0275  -0.2375 371 PHE D CB  
14039 C CG  . PHE D 371 ? 0.7019 1.3077 0.8381 -0.2326 0.0209  -0.2525 371 PHE D CG  
14040 C CD1 . PHE D 371 ? 0.6504 1.2700 0.7799 -0.2162 0.0090  -0.2546 371 PHE D CD1 
14041 C CD2 . PHE D 371 ? 0.7097 1.3090 0.8574 -0.2470 0.0262  -0.2642 371 PHE D CD2 
14042 C CE1 . PHE D 371 ? 0.7044 1.3319 0.8369 -0.2142 0.0024  -0.2677 371 PHE D CE1 
14043 C CE2 . PHE D 371 ? 0.7809 1.3894 0.9329 -0.2448 0.0198  -0.2787 371 PHE D CE2 
14044 C CZ  . PHE D 371 ? 0.7992 1.4223 0.9429 -0.2284 0.0078  -0.2805 371 PHE D CZ  
14045 N N   . PRO D 372 ? 0.7194 1.3391 0.8619 -0.2317 0.0353  -0.2261 372 PRO D N   
14046 C CA  . PRO D 372 ? 0.7391 1.3493 0.8781 -0.2368 0.0433  -0.2137 372 PRO D CA  
14047 C C   . PRO D 372 ? 0.5847 1.1791 0.7048 -0.2262 0.0408  -0.1957 372 PRO D C   
14048 O O   . PRO D 372 ? 0.6239 1.1987 0.7380 -0.2337 0.0484  -0.1832 372 PRO D O   
14049 C CB  . PRO D 372 ? 0.7207 1.3548 0.8703 -0.2323 0.0417  -0.2216 372 PRO D CB  
14050 C CG  . PRO D 372 ? 0.6994 1.3502 0.8502 -0.2164 0.0293  -0.2302 372 PRO D CG  
14051 C CD  . PRO D 372 ? 0.7247 1.3693 0.8748 -0.2196 0.0265  -0.2364 372 PRO D CD  
14052 N N   . ALA D 373 ? 0.6306 1.2315 0.7416 -0.2085 0.0303  -0.1931 373 ALA D N   
14053 C CA  . ALA D 373 ? 0.6190 1.2050 0.7129 -0.1979 0.0277  -0.1761 373 ALA D CA  
14054 C C   . ALA D 373 ? 0.5825 1.1452 0.6681 -0.2061 0.0319  -0.1696 373 ALA D C   
14055 O O   . ALA D 373 ? 0.5366 1.0811 0.6120 -0.2058 0.0352  -0.1550 373 ALA D O   
14056 C CB  . ALA D 373 ? 0.5888 1.1839 0.6761 -0.1777 0.0159  -0.1745 373 ALA D CB  
14057 N N   . GLN D 374 ? 0.5334 1.0957 0.6241 -0.2133 0.0317  -0.1808 374 GLN D N   
14058 C CA  . GLN D 374 ? 0.5223 1.0619 0.6068 -0.2213 0.0358  -0.1767 374 GLN D CA  
14059 C C   . GLN D 374 ? 0.5832 1.1016 0.6722 -0.2371 0.0474  -0.1697 374 GLN D C   
14060 O O   . GLN D 374 ? 0.6004 1.0950 0.6801 -0.2387 0.0511  -0.1569 374 GLN D O   
14061 C CB  . GLN D 374 ? 0.6467 1.1911 0.7374 -0.2258 0.0331  -0.1923 374 GLN D CB  
14062 C CG  . GLN D 374 ? 0.5747 1.0975 0.6573 -0.2301 0.0349  -0.1896 374 GLN D CG  
14063 C CD  . GLN D 374 ? 0.5393 1.0540 0.6041 -0.2170 0.0304  -0.1752 374 GLN D CD  
14064 O OE1 . GLN D 374 ? 0.5235 1.0515 0.5804 -0.2017 0.0214  -0.1739 374 GLN D OE1 
14065 N NE2 . GLN D 374 ? 0.4518 0.9427 0.5110 -0.2224 0.0366  -0.1632 374 GLN D NE2 
14066 N N   . ALA D 375 ? 0.5856 1.1108 0.6890 -0.2488 0.0535  -0.1774 375 ALA D N   
14067 C CA  . ALA D 375 ? 0.5162 1.0198 0.6238 -0.2637 0.0649  -0.1692 375 ALA D CA  
14068 C C   . ALA D 375 ? 0.5441 1.0363 0.6403 -0.2581 0.0674  -0.1509 375 ALA D C   
14069 O O   . ALA D 375 ? 0.5906 1.0553 0.6823 -0.2654 0.0747  -0.1382 375 ALA D O   
14070 C CB  . ALA D 375 ? 0.6151 1.1318 0.7401 -0.2759 0.0706  -0.1807 375 ALA D CB  
14071 N N   . VAL D 376 ? 0.5744 1.0858 0.6660 -0.2443 0.0609  -0.1493 376 VAL D N   
14072 C CA  . VAL D 376 ? 0.5704 1.0718 0.6502 -0.2358 0.0609  -0.1325 376 VAL D CA  
14073 C C   . VAL D 376 ? 0.5320 1.0125 0.5982 -0.2287 0.0581  -0.1209 376 VAL D C   
14074 O O   . VAL D 376 ? 0.4818 0.9373 0.5408 -0.2305 0.0633  -0.1060 376 VAL D O   
14075 C CB  . VAL D 376 ? 0.5394 1.0662 0.6185 -0.2211 0.0531  -0.1352 376 VAL D CB  
14076 C CG1 . VAL D 376 ? 0.4436 0.9600 0.5110 -0.2110 0.0521  -0.1187 376 VAL D CG1 
14077 C CG2 . VAL D 376 ? 0.5426 1.0897 0.6362 -0.2288 0.0568  -0.1474 376 VAL D CG2 
14078 N N   . ILE D 377 ? 0.5353 1.0253 0.5978 -0.2201 0.0499  -0.1274 377 ILE D N   
14079 C CA  . ILE D 377 ? 0.5298 1.0031 0.5799 -0.2131 0.0471  -0.1179 377 ILE D CA  
14080 C C   . ILE D 377 ? 0.5210 0.9645 0.5720 -0.2268 0.0559  -0.1140 377 ILE D C   
14081 O O   . ILE D 377 ? 0.5280 0.9479 0.5699 -0.2240 0.0583  -0.1001 377 ILE D O   
14082 C CB  . ILE D 377 ? 0.4395 0.9294 0.4858 -0.2030 0.0374  -0.1271 377 ILE D CB  
14083 C CG1 . ILE D 377 ? 0.3892 0.9009 0.4328 -0.1864 0.0288  -0.1264 377 ILE D CG1 
14084 C CG2 . ILE D 377 ? 0.4681 0.9412 0.5028 -0.1987 0.0357  -0.1195 377 ILE D CG2 
14085 C CD1 . ILE D 377 ? 0.4426 0.9687 0.4839 -0.1753 0.0198  -0.1341 377 ILE D CD1 
14086 N N   . ASN D 378 ? 0.4531 0.8954 0.5159 -0.2412 0.0608  -0.1260 378 ASN D N   
14087 C CA  . ASN D 378 ? 0.5430 0.9549 0.6080 -0.2538 0.0685  -0.1232 378 ASN D CA  
14088 C C   . ASN D 378 ? 0.6513 1.0382 0.7146 -0.2603 0.0774  -0.1075 378 ASN D C   
14089 O O   . ASN D 378 ? 0.6473 1.0036 0.7041 -0.2618 0.0813  -0.0960 378 ASN D O   
14090 C CB  . ASN D 378 ? 0.5304 0.9479 0.6097 -0.2663 0.0703  -0.1407 378 ASN D CB  
14091 C CG  . ASN D 378 ? 0.5318 0.9693 0.6105 -0.2592 0.0614  -0.1555 378 ASN D CG  
14092 O OD1 . ASN D 378 ? 0.5827 1.0355 0.6512 -0.2448 0.0533  -0.1532 378 ASN D OD1 
14093 N ND2 . ASN D 378 ? 0.5150 0.9516 0.6042 -0.2685 0.0623  -0.1703 378 ASN D ND2 
14094 N N   . ALA D 379 ? 0.6146 1.0133 0.6834 -0.2638 0.0806  -0.1068 379 ALA D N   
14095 C CA  . ALA D 379 ? 0.5751 0.9520 0.6396 -0.2681 0.0883  -0.0908 379 ALA D CA  
14096 C C   . ALA D 379 ? 0.5469 0.9146 0.5966 -0.2530 0.0848  -0.0751 379 ALA D C   
14097 O O   . ALA D 379 ? 0.5658 0.9032 0.6077 -0.2538 0.0895  -0.0601 379 ALA D O   
14098 C CB  . ALA D 379 ? 0.6233 1.0187 0.6966 -0.2747 0.0923  -0.0949 379 ALA D CB  
14099 N N   . LEU D 380 ? 0.5461 0.9385 0.5919 -0.2385 0.0759  -0.0782 380 LEU D N   
14100 C CA  . LEU D 380 ? 0.5218 0.9061 0.5549 -0.2227 0.0711  -0.0644 380 LEU D CA  
14101 C C   . LEU D 380 ? 0.5488 0.9059 0.5741 -0.2209 0.0719  -0.0572 380 LEU D C   
14102 O O   . LEU D 380 ? 0.5596 0.8930 0.5755 -0.2142 0.0735  -0.0419 380 LEU D O   
14103 C CB  . LEU D 380 ? 0.3817 0.7968 0.4135 -0.2077 0.0602  -0.0705 380 LEU D CB  
14104 C CG  . LEU D 380 ? 0.4213 0.8310 0.4416 -0.1899 0.0535  -0.0577 380 LEU D CG  
14105 C CD1 . LEU D 380 ? 0.3970 0.7897 0.4133 -0.1873 0.0578  -0.0433 380 LEU D CD1 
14106 C CD2 . LEU D 380 ? 0.4274 0.8679 0.4477 -0.1763 0.0424  -0.0647 380 LEU D CD2 
14107 N N   . TYR D 381 ? 0.5259 0.8861 0.5554 -0.2265 0.0706  -0.0690 381 TYR D N   
14108 C CA  . TYR D 381 ? 0.5278 0.8622 0.5515 -0.2266 0.0722  -0.0646 381 TYR D CA  
14109 C C   . TYR D 381 ? 0.6470 0.9456 0.6724 -0.2392 0.0814  -0.0571 381 TYR D C   
14110 O O   . TYR D 381 ? 0.6248 0.8942 0.6417 -0.2352 0.0835  -0.0447 381 TYR D O   
14111 C CB  . TYR D 381 ? 0.5733 0.9220 0.6016 -0.2295 0.0681  -0.0811 381 TYR D CB  
14112 C CG  . TYR D 381 ? 0.6118 0.9330 0.6370 -0.2331 0.0711  -0.0800 381 TYR D CG  
14113 C CD1 . TYR D 381 ? 0.5176 0.8258 0.5311 -0.2214 0.0696  -0.0687 381 TYR D CD1 
14114 C CD2 . TYR D 381 ? 0.6012 0.9081 0.6361 -0.2476 0.0754  -0.0907 381 TYR D CD2 
14115 C CE1 . TYR D 381 ? 0.4657 0.7482 0.4771 -0.2246 0.0728  -0.0689 381 TYR D CE1 
14116 C CE2 . TYR D 381 ? 0.6489 0.9294 0.6823 -0.2506 0.0775  -0.0914 381 TYR D CE2 
14117 C CZ  . TYR D 381 ? 0.5724 0.8411 0.5941 -0.2394 0.0764  -0.0809 381 TYR D CZ  
14118 O OH  . TYR D 381 ? 0.5703 0.8067 0.5883 -0.2370 0.0769  -0.0823 381 TYR D OH  
14119 N N   . LEU D 382 ? 0.9776 1.2769 1.0141 -0.2538 0.0865  -0.0643 382 LEU D N   
14120 C CA  . LEU D 382 ? 1.0018 1.2663 1.0405 -0.2660 0.0942  -0.0567 382 LEU D CA  
14121 C C   . LEU D 382 ? 1.0078 1.2538 1.0369 -0.2618 0.0978  -0.0376 382 LEU D C   
14122 O O   . LEU D 382 ? 1.0498 1.2608 1.0746 -0.2655 0.1016  -0.0262 382 LEU D O   
14123 C CB  . LEU D 382 ? 1.0233 1.2941 1.0771 -0.2822 0.0984  -0.0685 382 LEU D CB  
14124 C CG  . LEU D 382 ? 1.0320 1.3086 1.0964 -0.2886 0.0959  -0.0869 382 LEU D CG  
14125 C CD1 . LEU D 382 ? 1.0555 1.3259 1.1353 -0.3053 0.1012  -0.0946 382 LEU D CD1 
14126 C CD2 . LEU D 382 ? 1.0309 1.2814 1.0895 -0.2853 0.0943  -0.0847 382 LEU D CD2 
14127 N N   . GLU D 383 ? 0.6962 0.9647 0.7221 -0.2535 0.0957  -0.0344 383 GLU D N   
14128 C CA  . GLU D 383 ? 0.6363 0.8900 0.6536 -0.2490 0.0988  -0.0179 383 GLU D CA  
14129 C C   . GLU D 383 ? 0.6505 0.8900 0.6547 -0.2320 0.0944  -0.0053 383 GLU D C   
14130 O O   . GLU D 383 ? 0.6580 0.8744 0.6540 -0.2285 0.0971  0.0093  383 GLU D O   
14131 C CB  . GLU D 383 ? 0.7518 1.0352 0.7730 -0.2482 0.0989  -0.0214 383 GLU D CB  
14132 C CG  . GLU D 383 ? 0.7917 1.0747 0.8216 -0.2655 0.1071  -0.0240 383 GLU D CG  
14133 C CD  . GLU D 383 ? 0.8195 1.0664 0.8424 -0.2717 0.1140  -0.0075 383 GLU D CD  
14134 O OE1 . GLU D 383 ? 0.8896 1.1282 0.9016 -0.2624 0.1140  0.0056  383 GLU D OE1 
14135 O OE2 . GLU D 383 ? 0.8163 1.0425 0.8447 -0.2852 0.1185  -0.0077 383 GLU D OE2 
14136 N N   . SER D 384 ? 0.6331 0.8853 0.6352 -0.2211 0.0875  -0.0107 384 SER D N   
14137 C CA  . SER D 384 ? 0.5202 0.7630 0.5113 -0.2031 0.0826  0.0006  384 SER D CA  
14138 C C   . SER D 384 ? 0.5356 0.7717 0.5230 -0.1970 0.0791  -0.0021 384 SER D C   
14139 O O   . SER D 384 ? 0.4640 0.6811 0.4423 -0.1845 0.0772  0.0089  384 SER D O   
14140 C CB  . SER D 384 ? 0.4670 0.7394 0.4579 -0.1899 0.0758  -0.0002 384 SER D CB  
14141 O OG  . SER D 384 ? 0.4959 0.8019 0.4942 -0.1909 0.0705  -0.0153 384 SER D OG  
14142 N N   . GLY D 385 ? 0.4873 0.7385 0.4815 -0.2049 0.0781  -0.0168 385 GLY D N   
14143 C CA  . GLY D 385 ? 0.4811 0.7313 0.4714 -0.1988 0.0749  -0.0209 385 GLY D CA  
14144 C C   . GLY D 385 ? 0.4375 0.7177 0.4241 -0.1837 0.0660  -0.0237 385 GLY D C   
14145 O O   . GLY D 385 ? 0.4078 0.6863 0.3883 -0.1757 0.0632  -0.0240 385 GLY D O   
14146 N N   . VAL D 386 ? 0.4278 0.7346 0.4181 -0.1796 0.0612  -0.0260 386 VAL D N   
14147 C CA  . VAL D 386 ? 0.3536 0.6885 0.3416 -0.1651 0.0510  -0.0285 386 VAL D CA  
14148 C C   . VAL D 386 ? 0.3303 0.6946 0.3248 -0.1722 0.0474  -0.0461 386 VAL D C   
14149 O O   . VAL D 386 ? 0.4236 0.8018 0.4275 -0.1832 0.0492  -0.0566 386 VAL D O   
14150 C CB  . VAL D 386 ? 0.3492 0.6976 0.3389 -0.1567 0.0466  -0.0234 386 VAL D CB  
14151 C CG1 . VAL D 386 ? 0.2550 0.6361 0.2453 -0.1449 0.0351  -0.0294 386 VAL D CG1 
14152 C CG2 . VAL D 386 ? 0.3814 0.7029 0.3642 -0.1457 0.0477  -0.0067 386 VAL D CG2 
14153 N N   . ARG D 387 ? 0.3606 0.7341 0.3497 -0.1652 0.0421  -0.0496 387 ARG D N   
14154 C CA  . ARG D 387 ? 0.3138 0.7162 0.3075 -0.1693 0.0365  -0.0662 387 ARG D CA  
14155 C C   . ARG D 387 ? 0.2363 0.6672 0.2275 -0.1552 0.0252  -0.0667 387 ARG D C   
14156 O O   . ARG D 387 ? 0.2449 0.6774 0.2273 -0.1404 0.0190  -0.0572 387 ARG D O   
14157 C CB  . ARG D 387 ? 0.2558 0.6466 0.2410 -0.1675 0.0354  -0.0707 387 ARG D CB  
14158 C CG  . ARG D 387 ? 0.3277 0.7455 0.3124 -0.1669 0.0260  -0.0866 387 ARG D CG  
14159 C CD  . ARG D 387 ? 0.3342 0.7349 0.3116 -0.1700 0.0273  -0.0958 387 ARG D CD  
14160 N NE  . ARG D 387 ? 0.2914 0.6734 0.2515 -0.1557 0.0253  -0.0861 387 ARG D NE  
14161 C CZ  . ARG D 387 ? 0.3298 0.6979 0.2814 -0.1556 0.0263  -0.0931 387 ARG D CZ  
14162 N NH1 . ARG D 387 ? 0.3396 0.7096 0.2981 -0.1683 0.0285  -0.1100 387 ARG D NH1 
14163 N NH2 . ARG D 387 ? 0.3001 0.6533 0.2369 -0.1428 0.0253  -0.0839 387 ARG D NH2 
14164 N N   . ALA D 388 ? 0.2743 0.7240 0.2728 -0.1587 0.0235  -0.0773 388 ALA D N   
14165 C CA  . ALA D 388 ? 0.3316 0.8032 0.3290 -0.1446 0.0156  -0.0796 388 ALA D CA  
14166 C C   . ALA D 388 ? 0.3374 0.8221 0.3382 -0.1454 0.0120  -0.0937 388 ALA D C   
14167 O O   . ALA D 388 ? 0.3692 0.8496 0.3721 -0.1579 0.0149  -0.1036 388 ALA D O   
14168 C CB  . ALA D 388 ? 0.2782 0.7588 0.2831 -0.1452 0.0170  -0.0804 388 ALA D CB  
14169 N N   . VAL D 389 ? 0.2825 0.7799 0.2853 -0.1312 0.0053  -0.0943 389 VAL D N   
14170 C CA  . VAL D 389 ? 0.3840 0.8913 0.3898 -0.1288 -0.0003 -0.1055 389 VAL D CA  
14171 C C   . VAL D 389 ? 0.4249 0.9508 0.4430 -0.1294 -0.0021 -0.1158 389 VAL D C   
14172 O O   . VAL D 389 ? 0.4078 0.9381 0.4297 -0.1235 -0.0021 -0.1110 389 VAL D O   
14173 C CB  . VAL D 389 ? 0.3575 0.8571 0.3553 -0.1112 -0.0084 -0.0964 389 VAL D CB  
14174 C CG1 . VAL D 389 ? 0.2882 0.7872 0.2885 -0.0953 -0.0129 -0.0863 389 VAL D CG1 
14175 C CG2 . VAL D 389 ? 0.4679 0.9742 0.4652 -0.1104 -0.0147 -0.1075 389 VAL D CG2 
14176 N N   . GLU D 390 ? 0.4205 0.9571 0.4455 -0.1366 -0.0036 -0.1307 390 GLU D N   
14177 C CA  . GLU D 390 ? 0.5384 1.0933 0.5768 -0.1381 -0.0054 -0.1423 390 GLU D CA  
14178 C C   . GLU D 390 ? 0.4884 1.0506 0.5273 -0.1222 -0.0167 -0.1432 390 GLU D C   
14179 O O   . GLU D 390 ? 0.5316 1.0873 0.5620 -0.1157 -0.0228 -0.1414 390 GLU D O   
14180 C CB  . GLU D 390 ? 0.5111 1.0732 0.5596 -0.1551 -0.0007 -0.1589 390 GLU D CB  
14181 C CG  . GLU D 390 ? 0.5761 1.1575 0.6403 -0.1576 -0.0015 -0.1711 390 GLU D CG  
14182 C CD  . GLU D 390 ? 0.6500 1.2385 0.7259 -0.1724 0.0021  -0.1880 390 GLU D CD  
14183 O OE1 . GLU D 390 ? 0.6855 1.2606 0.7596 -0.1852 0.0088  -0.1891 390 GLU D OE1 
14184 O OE2 . GLU D 390 ? 0.7232 1.3290 0.8110 -0.1712 -0.0021 -0.2003 390 GLU D OE2 
14185 N N   . ILE D 391 ? 0.5336 1.1072 0.5821 -0.1163 -0.0197 -0.1459 391 ILE D N   
14186 C CA  . ILE D 391 ? 0.6318 1.2118 0.6837 -0.1034 -0.0311 -0.1491 391 ILE D CA  
14187 C C   . ILE D 391 ? 0.6609 1.2617 0.7296 -0.1099 -0.0309 -0.1652 391 ILE D C   
14188 O O   . ILE D 391 ? 0.6830 1.2910 0.7599 -0.1060 -0.0309 -0.1655 391 ILE D O   
14189 C CB  . ILE D 391 ? 0.5489 1.1174 0.5958 -0.0867 -0.0368 -0.1346 391 ILE D CB  
14190 C CG1 . ILE D 391 ? 0.4399 0.9872 0.4715 -0.0814 -0.0360 -0.1193 391 ILE D CG1 
14191 C CG2 . ILE D 391 ? 0.5821 1.1533 0.6324 -0.0745 -0.0499 -0.1377 391 ILE D CG2 
14192 C CD1 . ILE D 391 ? 0.4947 1.0265 0.5219 -0.0659 -0.0406 -0.1049 391 ILE D CD1 
14193 N N   . GLY D 392 ? 0.5920 1.2025 0.6668 -0.1202 -0.0304 -0.1793 392 GLY D N   
14194 C CA  . GLY D 392 ? 0.6282 1.2581 0.7205 -0.1281 -0.0290 -0.1957 392 GLY D CA  
14195 C C   . GLY D 392 ? 0.6148 1.2536 0.7129 -0.1346 -0.0322 -0.2107 392 GLY D C   
14196 O O   . GLY D 392 ? 0.6050 1.2404 0.6951 -0.1256 -0.0420 -0.2100 392 GLY D O   
14197 N N   . SER D 393 ? 0.6111 1.2598 0.7226 -0.1504 -0.0240 -0.2243 393 SER D N   
14198 C CA  . SER D 393 ? 0.6600 1.3183 0.7801 -0.1571 -0.0265 -0.2406 393 SER D CA  
14199 C C   . SER D 393 ? 0.6756 1.3206 0.7844 -0.1623 -0.0250 -0.2398 393 SER D C   
14200 O O   . SER D 393 ? 0.6457 1.2965 0.7571 -0.1636 -0.0300 -0.2514 393 SER D O   
14201 C CB  . SER D 393 ? 0.6849 1.3557 0.8245 -0.1730 -0.0174 -0.2550 393 SER D CB  
14202 O OG  . SER D 393 ? 0.5716 1.2581 0.7235 -0.1683 -0.0196 -0.2597 393 SER D OG  
14203 N N   . PHE D 394 ? 0.6091 1.2366 0.7058 -0.1654 -0.0184 -0.2271 394 PHE D N   
14204 C CA  . PHE D 394 ? 0.6574 1.2710 0.7430 -0.1696 -0.0169 -0.2261 394 PHE D CA  
14205 C C   . PHE D 394 ? 0.6190 1.2243 0.6864 -0.1540 -0.0263 -0.2151 394 PHE D C   
14206 O O   . PHE D 394 ? 0.6066 1.2043 0.6646 -0.1553 -0.0276 -0.2173 394 PHE D O   
14207 C CB  . PHE D 394 ? 0.6915 1.2883 0.7741 -0.1819 -0.0051 -0.2187 394 PHE D CB  
14208 C CG  . PHE D 394 ? 0.6832 1.2647 0.7580 -0.1890 -0.0020 -0.2206 394 PHE D CG  
14209 C CD1 . PHE D 394 ? 0.7178 1.3032 0.8007 -0.1974 -0.0019 -0.2368 394 PHE D CD1 
14210 C CD2 . PHE D 394 ? 0.6661 1.2289 0.7266 -0.1875 0.0010  -0.2069 394 PHE D CD2 
14211 C CE1 . PHE D 394 ? 0.6621 1.2326 0.7387 -0.2037 0.0011  -0.2397 394 PHE D CE1 
14212 C CE2 . PHE D 394 ? 0.7035 1.2516 0.7577 -0.1940 0.0040  -0.2099 394 PHE D CE2 
14213 C CZ  . PHE D 394 ? 0.6776 1.2292 0.7399 -0.2020 0.0042  -0.2265 394 PHE D CZ  
14214 N N   . LEU D 395 ? 0.6116 1.2165 0.6740 -0.1395 -0.0328 -0.2033 395 LEU D N   
14215 C CA  . LEU D 395 ? 0.5720 1.1672 0.6185 -0.1244 -0.0428 -0.1925 395 LEU D CA  
14216 C C   . LEU D 395 ? 0.6288 1.2346 0.6776 -0.1161 -0.0554 -0.2005 395 LEU D C   
14217 O O   . LEU D 395 ? 0.5765 1.1764 0.6127 -0.1108 -0.0627 -0.1996 395 LEU D O   
14218 C CB  . LEU D 395 ? 0.5499 1.1344 0.5900 -0.1129 -0.0438 -0.1747 395 LEU D CB  
14219 C CG  . LEU D 395 ? 0.5121 1.0852 0.5390 -0.0963 -0.0554 -0.1631 395 LEU D CG  
14220 C CD1 . LEU D 395 ? 0.5147 1.0746 0.5249 -0.0962 -0.0562 -0.1589 395 LEU D CD1 
14221 C CD2 . LEU D 395 ? 0.4953 1.0571 0.5197 -0.0856 -0.0558 -0.1471 395 LEU D CD2 
14222 N N   . LEU D 396 ? 0.6229 1.2441 0.6874 -0.1152 -0.0582 -0.2087 396 LEU D N   
14223 C CA  . LEU D 396 ? 0.6079 1.2380 0.6750 -0.1062 -0.0716 -0.2155 396 LEU D CA  
14224 C C   . LEU D 396 ? 0.5937 1.2306 0.6600 -0.1122 -0.0748 -0.2295 396 LEU D C   
14225 O O   . LEU D 396 ? 0.5751 1.2070 0.6285 -0.1039 -0.0857 -0.2274 396 LEU D O   
14226 C CB  . LEU D 396 ? 0.6270 1.2736 0.7135 -0.1061 -0.0724 -0.2240 396 LEU D CB  
14227 C CG  . LEU D 396 ? 0.7024 1.3566 0.7930 -0.0950 -0.0874 -0.2289 396 LEU D CG  
14228 C CD1 . LEU D 396 ? 0.7770 1.4124 0.8483 -0.0807 -0.0991 -0.2131 396 LEU D CD1 
14229 C CD2 . LEU D 396 ? 0.6522 1.3192 0.7606 -0.0932 -0.0870 -0.2337 396 LEU D CD2 
14230 N N   . GLY D 397 ? 0.6313 1.2783 0.7109 -0.1268 -0.0656 -0.2438 397 GLY D N   
14231 C CA  . GLY D 397 ? 0.6130 1.2652 0.6932 -0.1334 -0.0671 -0.2578 397 GLY D CA  
14232 C C   . GLY D 397 ? 0.7246 1.3944 0.8165 -0.1305 -0.0771 -0.2728 397 GLY D C   
14233 O O   . GLY D 397 ? 0.6731 1.3538 0.7774 -0.1262 -0.0811 -0.2755 397 GLY D O   
14234 N N   . ARG D 398 ? 0.7006 1.3732 0.7886 -0.1330 -0.0812 -0.2834 398 ARG D N   
14235 C CA  . ARG D 398 ? 0.7110 1.4001 0.8091 -0.1311 -0.0911 -0.2991 398 ARG D CA  
14236 C C   . ARG D 398 ? 0.6504 1.3368 0.7355 -0.1151 -0.1076 -0.2911 398 ARG D C   
14237 O O   . ARG D 398 ? 0.6219 1.2938 0.6844 -0.1079 -0.1137 -0.2797 398 ARG D O   
14238 C CB  . ARG D 398 ? 0.6257 1.3176 0.7232 -0.1392 -0.0897 -0.3133 398 ARG D CB  
14239 C CG  . ARG D 398 ? 0.6569 1.3471 0.7669 -0.1558 -0.0741 -0.3211 398 ARG D CG  
14240 C CD  . ARG D 398 ? 0.6648 1.3710 0.8021 -0.1657 -0.0685 -0.3357 398 ARG D CD  
14241 N NE  . ARG D 398 ? 0.6797 1.3787 0.8273 -0.1813 -0.0530 -0.3373 398 ARG D NE  
14242 C CZ  . ARG D 398 ? 0.6524 1.3465 0.8054 -0.1934 -0.0462 -0.3476 398 ARG D CZ  
14243 N NH1 . ARG D 398 ? 0.6096 1.3067 0.7584 -0.1915 -0.0526 -0.3581 398 ARG D NH1 
14244 N NH2 . ARG D 398 ? 0.6762 1.3605 0.8387 -0.2077 -0.0328 -0.3471 398 ARG D NH2 
14245 N N   . GLN D 405 ? 0.7671 1.5056 0.9373 -0.1509 -0.0781 -0.3364 405 GLN D N   
14246 C CA  . GLN D 405 ? 0.8059 1.5351 0.9708 -0.1482 -0.0722 -0.3202 405 GLN D CA  
14247 C C   . GLN D 405 ? 0.8293 1.5621 0.9930 -0.1329 -0.0836 -0.3135 405 GLN D C   
14248 O O   . GLN D 405 ? 0.8939 1.6422 1.0756 -0.1329 -0.0845 -0.3231 405 GLN D O   
14249 C CB  . GLN D 405 ? 0.7558 1.4903 0.9379 -0.1633 -0.0568 -0.3256 405 GLN D CB  
14250 C CG  . GLN D 405 ? 0.7986 1.5256 0.9762 -0.1610 -0.0505 -0.3104 405 GLN D CG  
14251 C CD  . GLN D 405 ? 0.7909 1.4962 0.9471 -0.1589 -0.0471 -0.2923 405 GLN D CD  
14252 O OE1 . GLN D 405 ? 0.7195 1.4148 0.8743 -0.1715 -0.0354 -0.2899 405 GLN D OE1 
14253 N NE2 . GLN D 405 ? 0.7626 1.4589 0.9025 -0.1433 -0.0574 -0.2792 405 GLN D NE2 
14254 N N   . LYS D 406 ? 0.7415 1.4587 0.8843 -0.1202 -0.0924 -0.2973 406 LYS D N   
14255 C CA  . LYS D 406 ? 0.7705 1.4851 0.9108 -0.1060 -0.1027 -0.2878 406 LYS D CA  
14256 C C   . LYS D 406 ? 0.8301 1.5484 0.9820 -0.1086 -0.0927 -0.2843 406 LYS D C   
14257 O O   . LYS D 406 ? 0.8266 1.5385 0.9764 -0.1176 -0.0794 -0.2787 406 LYS D O   
14258 C CB  . LYS D 406 ? 0.7084 1.4008 0.8233 -0.0947 -0.1105 -0.2687 406 LYS D CB  
14259 C CG  . LYS D 406 ? 0.7025 1.3881 0.8118 -0.0795 -0.1254 -0.2594 406 LYS D CG  
14260 C CD  . LYS D 406 ? 0.6451 1.3089 0.7283 -0.0711 -0.1341 -0.2439 406 LYS D CD  
14261 C CE  . LYS D 406 ? 0.6155 1.2661 0.6915 -0.0572 -0.1474 -0.2307 406 LYS D CE  
14262 N NZ  . LYS D 406 ? 0.6328 1.2742 0.7114 -0.0542 -0.1398 -0.2182 406 LYS D NZ  
14263 N N   . HIS D 407 ? 0.7977 1.5262 0.9618 -0.1013 -0.0995 -0.2884 407 HIS D N   
14264 C CA  . HIS D 407 ? 0.6965 1.4337 0.8749 -0.1051 -0.0898 -0.2900 407 HIS D CA  
14265 C C   . HIS D 407 ? 0.7598 1.4797 0.9248 -0.1030 -0.0825 -0.2713 407 HIS D C   
14266 O O   . HIS D 407 ? 0.7863 1.4907 0.9377 -0.0901 -0.0909 -0.2565 407 HIS D O   
14267 C CB  . HIS D 407 ? 0.6884 1.4371 0.8799 -0.0950 -0.1004 -0.2963 407 HIS D CB  
14268 C CG  . HIS D 407 ? 0.7719 1.5296 0.9765 -0.0976 -0.0913 -0.2981 407 HIS D CG  
14269 N ND1 . HIS D 407 ? 0.7911 1.5397 0.9912 -0.0864 -0.0951 -0.2859 407 HIS D ND1 
14270 C CD2 . HIS D 407 ? 0.7264 1.5007 0.9481 -0.1106 -0.0784 -0.3108 407 HIS D CD2 
14271 C CE1 . HIS D 407 ? 0.7027 1.4632 0.9160 -0.0919 -0.0850 -0.2916 407 HIS D CE1 
14272 N NE2 . HIS D 407 ? 0.7264 1.5025 0.9523 -0.1069 -0.0747 -0.3063 407 HIS D NE2 
14273 N N   . ALA D 408 ? 0.7730 1.4944 0.9419 -0.1162 -0.0669 -0.2719 408 ALA D N   
14274 C CA  . ALA D 408 ? 0.7793 1.4852 0.9360 -0.1160 -0.0588 -0.2553 408 ALA D CA  
14275 C C   . ALA D 408 ? 0.7909 1.5023 0.9555 -0.1103 -0.0578 -0.2529 408 ALA D C   
14276 O O   . ALA D 408 ? 0.7021 1.4237 0.8773 -0.1206 -0.0468 -0.2591 408 ALA D O   
14277 C CB  . ALA D 408 ? 0.6923 1.3953 0.8484 -0.1334 -0.0438 -0.2566 408 ALA D CB  
14278 N N   . ASP D 409 ? 0.8996 1.6025 1.0584 -0.0940 -0.0694 -0.2436 409 ASP D N   
14279 C CA  . ASP D 409 ? 0.8893 1.5962 1.0560 -0.0872 -0.0698 -0.2419 409 ASP D CA  
14280 C C   . ASP D 409 ? 0.8829 1.5805 1.0419 -0.0909 -0.0577 -0.2302 409 ASP D C   
14281 O O   . ASP D 409 ? 0.8693 1.5760 1.0372 -0.0923 -0.0524 -0.2336 409 ASP D O   
14282 C CB  . ASP D 409 ? 0.8966 1.5923 1.0584 -0.0696 -0.0858 -0.2337 409 ASP D CB  
14283 C CG  . ASP D 409 ? 0.9032 1.5742 1.0438 -0.0624 -0.0914 -0.2163 409 ASP D CG  
14284 O OD1 . ASP D 409 ? 0.9135 1.5799 1.0445 -0.0702 -0.0855 -0.2144 409 ASP D OD1 
14285 O OD2 . ASP D 409 ? 0.8981 1.5538 1.0321 -0.0494 -0.1017 -0.2050 409 ASP D OD2 
14286 N N   . MET D 410 ? 0.8143 1.4945 0.9569 -0.0929 -0.0534 -0.2171 410 MET D N   
14287 C CA  A MET D 410 ? 0.7497 1.4191 0.8832 -0.0959 -0.0432 -0.2048 410 MET D CA  
14288 C CA  B MET D 410 ? 0.7494 1.4193 0.8833 -0.0963 -0.0430 -0.2053 410 MET D CA  
14289 C C   . MET D 410 ? 0.7249 1.3873 0.8497 -0.1096 -0.0334 -0.2022 410 MET D C   
14290 O O   . MET D 410 ? 0.7400 1.3961 0.8579 -0.1099 -0.0373 -0.2019 410 MET D O   
14291 C CB  A MET D 410 ? 0.7041 1.3529 0.8247 -0.0800 -0.0500 -0.1872 410 MET D CB  
14292 C CB  B MET D 410 ? 0.7035 1.3538 0.8254 -0.0803 -0.0495 -0.1880 410 MET D CB  
14293 C CG  A MET D 410 ? 0.6710 1.3216 0.7996 -0.0672 -0.0584 -0.1874 410 MET D CG  
14294 C CG  B MET D 410 ? 0.6639 1.3001 0.7762 -0.0693 -0.0622 -0.1811 410 MET D CG  
14295 S SD  A MET D 410 ? 0.5373 1.1994 0.6749 -0.0717 -0.0478 -0.1910 410 MET D SD  
14296 S SD  B MET D 410 ? 0.6274 1.2464 0.7363 -0.0502 -0.0741 -0.1683 410 MET D SD  
14297 C CE  A MET D 410 ? 0.4453 1.1008 0.5881 -0.0532 -0.0606 -0.1873 410 MET D CE  
14298 C CE  B MET D 410 ? 0.6348 1.2761 0.7651 -0.0485 -0.0792 -0.1848 410 MET D CE  
14299 N N   . GLU D 411 ? 0.6860 1.3482 0.8107 -0.1213 -0.0212 -0.2003 411 GLU D N   
14300 C CA  . GLU D 411 ? 0.7542 1.4053 0.8701 -0.1347 -0.0120 -0.1957 411 GLU D CA  
14301 C C   . GLU D 411 ? 0.7815 1.4143 0.8821 -0.1297 -0.0088 -0.1775 411 GLU D C   
14302 O O   . GLU D 411 ? 0.7481 1.3764 0.8465 -0.1401 0.0007  -0.1734 411 GLU D O   
14303 C CB  . GLU D 411 ? 0.7383 1.3989 0.8657 -0.1542 -0.0008 -0.2067 411 GLU D CB  
14304 C CG  . GLU D 411 ? 0.7522 1.4282 0.8946 -0.1617 -0.0023 -0.2250 411 GLU D CG  
14305 C CD  . GLU D 411 ? 0.7102 1.3777 0.8467 -0.1651 -0.0047 -0.2266 411 GLU D CD  
14306 O OE1 . GLU D 411 ? 0.6970 1.3477 0.8230 -0.1727 0.0016  -0.2180 411 GLU D OE1 
14307 O OE2 . GLU D 411 ? 0.7297 1.4069 0.8722 -0.1601 -0.0131 -0.2369 411 GLU D OE2 
14308 N N   . PHE D 412 ? 0.8138 1.4346 0.9043 -0.1138 -0.0171 -0.1662 412 PHE D N   
14309 C CA  . PHE D 412 ? 0.7555 1.3585 0.8326 -0.1071 -0.0150 -0.1490 412 PHE D CA  
14310 C C   . PHE D 412 ? 0.6885 1.2787 0.7551 -0.1186 -0.0073 -0.1427 412 PHE D C   
14311 O O   . PHE D 412 ? 0.7157 1.3068 0.7830 -0.1282 -0.0060 -0.1499 412 PHE D O   
14312 C CB  . PHE D 412 ? 0.7424 1.3326 0.8124 -0.0886 -0.0257 -0.1388 412 PHE D CB  
14313 C CG  . PHE D 412 ? 0.7558 1.3471 0.8319 -0.0752 -0.0320 -0.1372 412 PHE D CG  
14314 C CD1 . PHE D 412 ? 0.7354 1.3390 0.8206 -0.0789 -0.0270 -0.1431 412 PHE D CD1 
14315 C CD2 . PHE D 412 ? 0.7550 1.3328 0.8273 -0.0598 -0.0431 -0.1296 412 PHE D CD2 
14316 C CE1 . PHE D 412 ? 0.7071 1.3112 0.7985 -0.0668 -0.0330 -0.1427 412 PHE D CE1 
14317 C CE2 . PHE D 412 ? 0.7454 1.3210 0.8240 -0.0484 -0.0496 -0.1284 412 PHE D CE2 
14318 C CZ  . PHE D 412 ? 0.7202 1.3097 0.8089 -0.0516 -0.0445 -0.1354 412 PHE D CZ  
14319 N N   . MET D 413 ? 0.4930 1.0705 0.5504 -0.1177 -0.0025 -0.1297 413 MET D N   
14320 C CA  . MET D 413 ? 0.4421 1.0020 0.4871 -0.1226 0.0015  -0.1193 413 MET D CA  
14321 C C   . MET D 413 ? 0.3511 0.8966 0.3858 -0.1061 -0.0022 -0.1032 413 MET D C   
14322 O O   . MET D 413 ? 0.3382 0.8827 0.3731 -0.0989 -0.0020 -0.0975 413 MET D O   
14323 C CB  . MET D 413 ? 0.4011 0.9547 0.4457 -0.1393 0.0112  -0.1179 413 MET D CB  
14324 C CG  . MET D 413 ? 0.2799 0.8121 0.3123 -0.1427 0.0141  -0.1059 413 MET D CG  
14325 S SD  . MET D 413 ? 0.3801 0.8947 0.4139 -0.1616 0.0248  -0.1007 413 MET D SD  
14326 C CE  . MET D 413 ? 0.3591 0.8760 0.3921 -0.1539 0.0248  -0.0922 413 MET D CE  
14327 N N   . ARG D 414 ? 0.3428 0.8763 0.3693 -0.1003 -0.0054 -0.0964 414 ARG D N   
14328 C CA  . ARG D 414 ? 0.2882 0.8054 0.3073 -0.0843 -0.0090 -0.0814 414 ARG D CA  
14329 C C   . ARG D 414 ? 0.2553 0.7579 0.2646 -0.0886 -0.0028 -0.0699 414 ARG D C   
14330 O O   . ARG D 414 ? 0.2159 0.7133 0.2202 -0.0977 -0.0003 -0.0707 414 ARG D O   
14331 C CB  . ARG D 414 ? 0.2554 0.7657 0.2719 -0.0744 -0.0174 -0.0801 414 ARG D CB  
14332 C CG  . ARG D 414 ? 0.2170 0.7078 0.2287 -0.0576 -0.0222 -0.0661 414 ARG D CG  
14333 C CD  . ARG D 414 ? 0.2571 0.7381 0.2636 -0.0500 -0.0309 -0.0647 414 ARG D CD  
14334 N NE  . ARG D 414 ? 0.2889 0.7615 0.2863 -0.0552 -0.0281 -0.0615 414 ARG D NE  
14335 C CZ  . ARG D 414 ? 0.3903 0.8495 0.3790 -0.0488 -0.0340 -0.0571 414 ARG D CZ  
14336 N NH1 . ARG D 414 ? 0.3339 0.7856 0.3212 -0.0378 -0.0435 -0.0547 414 ARG D NH1 
14337 N NH2 . ARG D 414 ? 0.3181 0.7700 0.2986 -0.0542 -0.0306 -0.0554 414 ARG D NH2 
14338 N N   . LEU D 415 ? 0.2211 0.7164 0.2276 -0.0821 -0.0008 -0.0600 415 LEU D N   
14339 C CA  . LEU D 415 ? 0.2223 0.7014 0.2193 -0.0824 0.0032  -0.0470 415 LEU D CA  
14340 C C   . LEU D 415 ? 0.2045 0.6677 0.2016 -0.0646 -0.0004 -0.0354 415 LEU D C   
14341 O O   . LEU D 415 ? 0.1740 0.6297 0.1731 -0.0523 -0.0018 -0.0292 415 LEU D O   
14342 C CB  . LEU D 415 ? 0.1995 0.6770 0.1930 -0.0857 0.0058  -0.0433 415 LEU D CB  
14343 C CG  . LEU D 415 ? 0.1997 0.6899 0.2004 -0.1016 0.0083  -0.0550 415 LEU D CG  
14344 C CD1 . LEU D 415 ? 0.1979 0.6848 0.1987 -0.1015 0.0093  -0.0497 415 LEU D CD1 
14345 C CD2 . LEU D 415 ? 0.2240 0.7074 0.2261 -0.1196 0.0127  -0.0589 415 LEU D CD2 
14346 N N   . THR D 416 ? 0.1756 0.6305 0.1705 -0.0641 -0.0025 -0.0336 416 THR D N   
14347 C CA  . THR D 416 ? 0.1694 0.6047 0.1634 -0.0489 -0.0076 -0.0244 416 THR D CA  
14348 C C   . THR D 416 ? 0.1595 0.5764 0.1523 -0.0452 -0.0039 -0.0117 416 THR D C   
14349 O O   . THR D 416 ? 0.1851 0.6013 0.1762 -0.0555 -0.0008 -0.0109 416 THR D O   
14350 C CB  . THR D 416 ? 0.1807 0.6146 0.1704 -0.0501 -0.0128 -0.0297 416 THR D CB  
14351 O OG1 . THR D 416 ? 0.1992 0.6538 0.1910 -0.0623 -0.0126 -0.0439 416 THR D OG1 
14352 C CG2 . THR D 416 ? 0.1844 0.6066 0.1731 -0.0361 -0.0211 -0.0267 416 THR D CG2 
14353 N N   . ILE D 417 ? 0.1601 0.5595 0.1549 -0.0311 -0.0054 -0.0030 417 ILE D N   
14354 C CA  . ILE D 417 ? 0.1690 0.5501 0.1661 -0.0258 -0.0021 0.0080  417 ILE D CA  
14355 C C   . ILE D 417 ? 0.1371 0.4928 0.1310 -0.0159 -0.0060 0.0135  417 ILE D C   
14356 O O   . ILE D 417 ? 0.1907 0.5352 0.1830 -0.0066 -0.0100 0.0140  417 ILE D O   
14357 C CB  . ILE D 417 ? 0.1717 0.5459 0.1713 -0.0182 -0.0003 0.0117  417 ILE D CB  
14358 C CG1 . ILE D 417 ? 0.1886 0.5830 0.1869 -0.0264 0.0004  0.0037  417 ILE D CG1 
14359 C CG2 . ILE D 417 ? 0.1938 0.5408 0.1954 -0.0143 0.0002  0.0208  417 ILE D CG2 
14360 C CD1 . ILE D 417 ? 0.2296 0.6274 0.2253 -0.0411 0.0016  0.0019  417 ILE D CD1 
14361 N N   . ALA D 418 ? 0.1649 0.5090 0.1565 -0.0188 -0.0055 0.0170  418 ALA D N   
14362 C CA  . ALA D 418 ? 0.1708 0.4894 0.1578 -0.0100 -0.0077 0.0220  418 ALA D CA  
14363 C C   . ALA D 418 ? 0.1723 0.4707 0.1648 0.0010  -0.0058 0.0288  418 ALA D C   
14364 O O   . ALA D 418 ? 0.1815 0.4823 0.1808 0.0016  -0.0022 0.0313  418 ALA D O   
14365 C CB  . ALA D 418 ? 0.1826 0.4896 0.1625 -0.0155 -0.0072 0.0227  418 ALA D CB  
14366 N N   . ARG D 419 ? 0.1612 0.4469 0.1512 0.0086  -0.0074 0.0317  419 ARG D N   
14367 C CA  . ARG D 419 ? 0.1638 0.4431 0.1595 0.0179  -0.0040 0.0371  419 ARG D CA  
14368 C C   . ARG D 419 ? 0.1620 0.4241 0.1614 0.0204  -0.0002 0.0418  419 ARG D C   
14369 O O   . ARG D 419 ? 0.1458 0.3963 0.1408 0.0196  -0.0018 0.0426  419 ARG D O   
14370 C CB  . ARG D 419 ? 0.1349 0.4128 0.1267 0.0238  -0.0073 0.0385  419 ARG D CB  
14371 C CG  . ARG D 419 ? 0.1333 0.4260 0.1216 0.0231  -0.0131 0.0338  419 ARG D CG  
14372 C CD  . ARG D 419 ? 0.1467 0.4364 0.1287 0.0264  -0.0191 0.0354  419 ARG D CD  
14373 N NE  . ARG D 419 ? 0.1640 0.4674 0.1436 0.0260  -0.0264 0.0303  419 ARG D NE  
14374 C CZ  . ARG D 419 ? 0.1672 0.4822 0.1438 0.0194  -0.0295 0.0238  419 ARG D CZ  
14375 N NH1 . ARG D 419 ? 0.1643 0.4776 0.1380 0.0120  -0.0266 0.0217  419 ARG D NH1 
14376 N NH2 . ARG D 419 ? 0.1787 0.5065 0.1554 0.0199  -0.0362 0.0184  419 ARG D NH2 
14377 N N   . ARG D 420 ? 0.1367 0.3950 0.1422 0.0237  0.0041  0.0441  420 ARG D N   
14378 C CA  . ARG D 420 ? 0.1140 0.3480 0.1211 0.0274  0.0060  0.0472  420 ARG D CA  
14379 C C   . ARG D 420 ? 0.1324 0.3626 0.1403 0.0228  0.0048  0.0481  420 ARG D C   
14380 O O   . ARG D 420 ? 0.1353 0.3495 0.1434 0.0264  0.0060  0.0505  420 ARG D O   
14381 C CB  . ARG D 420 ? 0.1563 0.3803 0.1627 0.0341  0.0079  0.0495  420 ARG D CB  
14382 C CG  . ARG D 420 ? 0.1465 0.3783 0.1511 0.0387  0.0086  0.0498  420 ARG D CG  
14383 C CD  . ARG D 420 ? 0.1172 0.3371 0.1210 0.0443  0.0106  0.0524  420 ARG D CD  
14384 N NE  . ARG D 420 ? 0.1373 0.3583 0.1406 0.0440  0.0095  0.0539  420 ARG D NE  
14385 C CZ  . ARG D 420 ? 0.1563 0.3710 0.1572 0.0473  0.0090  0.0561  420 ARG D CZ  
14386 N NH1 . ARG D 420 ? 0.1430 0.3545 0.1437 0.0517  0.0106  0.0577  420 ARG D NH1 
14387 N NH2 . ARG D 420 ? 0.1302 0.3413 0.1273 0.0456  0.0060  0.0567  420 ARG D NH2 
14388 N N   . VAL D 421 ? 0.1474 0.3860 0.1512 0.0139  0.0016  0.0453  421 VAL D N   
14389 C CA  . VAL D 421 ? 0.1187 0.3463 0.1115 0.0067  -0.0001 0.0452  421 VAL D CA  
14390 C C   . VAL D 421 ? 0.1371 0.3654 0.1303 0.0025  0.0007  0.0477  421 VAL D C   
14391 O O   . VAL D 421 ? 0.1673 0.3710 0.1520 0.0021  0.0031  0.0506  421 VAL D O   
14392 C CB  . VAL D 421 ? 0.1502 0.3946 0.1334 -0.0030 -0.0016 0.0399  421 VAL D CB  
14393 C CG1 . VAL D 421 ? 0.1671 0.4043 0.1366 -0.0141 0.0015  0.0381  421 VAL D CG1 
14394 C CG2 . VAL D 421 ? 0.1481 0.3837 0.1256 0.0009  -0.0027 0.0385  421 VAL D CG2 
14395 N N   . TYR D 422 ? 0.1152 0.3700 0.1166 -0.0013 -0.0003 0.0463  422 TYR D N   
14396 C CA  . TYR D 422 ? 0.1391 0.3958 0.1378 -0.0076 -0.0001 0.0483  422 TYR D CA  
14397 C C   . TYR D 422 ? 0.2019 0.4596 0.2126 0.0008  0.0001  0.0504  422 TYR D C   
14398 O O   . TYR D 422 ? 0.1545 0.4052 0.1663 0.0070  0.0018  0.0465  422 TYR D O   
14399 C CB  . TYR D 422 ? 0.1333 0.4170 0.1276 -0.0220 -0.0008 0.0426  422 TYR D CB  
14400 C CG  . TYR D 422 ? 0.1437 0.4237 0.1246 -0.0326 0.0023  0.0372  422 TYR D CG  
14401 C CD1 . TYR D 422 ? 0.1882 0.4412 0.1552 -0.0405 0.0103  0.0383  422 TYR D CD1 
14402 C CD2 . TYR D 422 ? 0.1663 0.4702 0.1506 -0.0349 -0.0006 0.0304  422 TYR D CD2 
14403 C CE1 . TYR D 422 ? 0.1746 0.4269 0.1324 -0.0510 0.0149  0.0318  422 TYR D CE1 
14404 C CE2 . TYR D 422 ? 0.1751 0.4775 0.1474 -0.0449 0.0021  0.0237  422 TYR D CE2 
14405 C CZ  . TYR D 422 ? 0.2067 0.4843 0.1661 -0.0533 0.0101  0.0238  422 TYR D CZ  
14406 O OH  . TYR D 422 ? 0.2475 0.5256 0.1977 -0.0641 0.0146  0.0154  422 TYR D OH  
14407 N N   . THR D 423 ? 0.1857 0.4344 0.1942 -0.0003 0.0005  0.0549  423 THR D N   
14408 C CA  . THR D 423 ? 0.1913 0.4333 0.2056 0.0063  0.0013  0.0556  423 THR D CA  
14409 C C   . THR D 423 ? 0.1761 0.4416 0.1892 -0.0012 -0.0007 0.0533  423 THR D C   
14410 O O   . THR D 423 ? 0.1529 0.4425 0.1620 -0.0131 -0.0026 0.0510  423 THR D O   
14411 C CB  . THR D 423 ? 0.1876 0.4077 0.1997 0.0097  0.0033  0.0614  423 THR D CB  
14412 O OG1 . THR D 423 ? 0.1984 0.4084 0.1936 -0.0020 0.0066  0.0636  423 THR D OG1 
14413 C CG2 . THR D 423 ? 0.1723 0.3652 0.1791 0.0142  0.0054  0.0620  423 THR D CG2 
14414 N N   . ASN D 424 ? 0.1525 0.4112 0.1681 0.0042  0.0001  0.0519  424 ASN D N   
14415 C CA  . ASN D 424 ? 0.1610 0.4430 0.1747 -0.0025 -0.0021 0.0495  424 ASN D CA  
14416 C C   . ASN D 424 ? 0.1485 0.4495 0.1581 -0.0148 -0.0028 0.0555  424 ASN D C   
14417 O O   . ASN D 424 ? 0.2075 0.5249 0.2108 -0.0264 -0.0011 0.0510  424 ASN D O   
14418 C CB  . ASN D 424 ? 0.2255 0.4974 0.2433 0.0055  -0.0003 0.0466  424 ASN D CB  
14419 C CG  . ASN D 424 ? 0.2488 0.5064 0.2593 0.0113  0.0073  0.0412  424 ASN D CG  
14420 O OD1 . ASN D 424 ? 0.2325 0.5027 0.2383 0.0090  0.0067  0.0377  424 ASN D OD1 
14421 N ND2 . ASN D 424 ? 0.2376 0.4759 0.2449 0.0189  0.0092  0.0415  424 ASN D ND2 
14422 N N   . ASP D 425 ? 0.1623 0.4271 0.1635 -0.0138 0.0037  0.0609  425 ASP D N   
14423 C CA  . ASP D 425 ? 0.1676 0.4104 0.1529 -0.0272 0.0140  0.0627  425 ASP D CA  
14424 C C   . ASP D 425 ? 0.2231 0.4680 0.2019 -0.0405 0.0188  0.0584  425 ASP D C   
14425 O O   . ASP D 425 ? 0.2159 0.4601 0.1890 -0.0551 0.0269  0.0569  425 ASP D O   
14426 C CB  . ASP D 425 ? 0.1956 0.3994 0.1729 -0.0217 0.0184  0.0689  425 ASP D CB  
14427 C CG  . ASP D 425 ? 0.2311 0.4327 0.2133 -0.0126 0.0161  0.0718  425 ASP D CG  
14428 O OD1 . ASP D 425 ? 0.2598 0.4896 0.2506 -0.0117 0.0123  0.0700  425 ASP D OD1 
14429 O OD2 . ASP D 425 ? 0.2917 0.4653 0.2691 -0.0067 0.0177  0.0752  425 ASP D OD2 
14430 N N   . HIS D 426 ? 0.1594 0.4079 0.1406 -0.0363 0.0144  0.0560  426 HIS D N   
14431 C CA  . HIS D 426 ? 0.1969 0.4561 0.1742 -0.0490 0.0175  0.0496  426 HIS D CA  
14432 C C   . HIS D 426 ? 0.2207 0.5173 0.2040 -0.0568 0.0142  0.0414  426 HIS D C   
14433 O O   . HIS D 426 ? 0.2275 0.5312 0.2082 -0.0723 0.0206  0.0352  426 HIS D O   
14434 C CB  . HIS D 426 ? 0.2176 0.4752 0.1954 -0.0422 0.0130  0.0482  426 HIS D CB  
14435 C CG  . HIS D 426 ? 0.2071 0.4281 0.1764 -0.0382 0.0179  0.0534  426 HIS D CG  
14436 N ND1 . HIS D 426 ? 0.1970 0.4051 0.1699 -0.0238 0.0133  0.0562  426 HIS D ND1 
14437 C CD2 . HIS D 426 ? 0.2091 0.4046 0.1681 -0.0474 0.0273  0.0555  426 HIS D CD2 
14438 C CE1 . HIS D 426 ? 0.1961 0.3727 0.1591 -0.0238 0.0190  0.0591  426 HIS D CE1 
14439 N NE2 . HIS D 426 ? 0.2296 0.3985 0.1844 -0.0377 0.0274  0.0594  426 HIS D NE2 
14440 N N   . MET D 427 ? 0.1551 0.4763 0.1476 -0.0463 0.0042  0.0403  427 MET D N   
14441 C CA  . MET D 427 ? 0.1967 0.5522 0.1913 -0.0522 0.0002  0.0314  427 MET D CA  
14442 C C   . MET D 427 ? 0.1961 0.5492 0.1883 -0.0645 0.0095  0.0296  427 MET D C   
14443 O O   . MET D 427 ? 0.2140 0.5839 0.2065 -0.0776 0.0135  0.0204  427 MET D O   
14444 C CB  . MET D 427 ? 0.1373 0.4918 0.1364 -0.0355 -0.0050 0.0305  427 MET D CB  
14445 C CG  . MET D 427 ? 0.1598 0.4953 0.1643 -0.0228 -0.0058 0.0307  427 MET D CG  
14446 S SD  . MET D 427 ? 0.2008 0.5533 0.2055 -0.0303 -0.0051 0.0228  427 MET D SD  
14447 C CE  . MET D 427 ? 0.1647 0.5050 0.1668 -0.0338 -0.0042 0.0296  427 MET D CE  
14448 N N   . ASP D 428 ? 0.1853 0.5180 0.1761 -0.0607 0.0135  0.0379  428 ASP D N   
14449 C CA  . ASP D 428 ? 0.2166 0.5456 0.2047 -0.0725 0.0231  0.0379  428 ASP D CA  
14450 C C   . ASP D 428 ? 0.2429 0.5579 0.2261 -0.0897 0.0343  0.0363  428 ASP D C   
14451 O O   . ASP D 428 ? 0.2717 0.5992 0.2569 -0.1036 0.0404  0.0304  428 ASP D O   
14452 C CB  . ASP D 428 ? 0.1855 0.4912 0.1699 -0.0648 0.0255  0.0477  428 ASP D CB  
14453 C CG  . ASP D 428 ? 0.2129 0.5387 0.2046 -0.0523 0.0163  0.0473  428 ASP D CG  
14454 O OD1 . ASP D 428 ? 0.2395 0.5969 0.2359 -0.0529 0.0104  0.0390  428 ASP D OD1 
14455 O OD2 . ASP D 428 ? 0.2510 0.5608 0.2428 -0.0417 0.0148  0.0543  428 ASP D OD2 
14456 N N   . TYR D 429 ? 0.2457 0.5349 0.2231 -0.0893 0.0370  0.0411  429 TYR D N   
14457 C CA  . TYR D 429 ? 0.2824 0.5591 0.2564 -0.1057 0.0465  0.0392  429 TYR D CA  
14458 C C   . TYR D 429 ? 0.3138 0.6206 0.2948 -0.1165 0.0453  0.0260  429 TYR D C   
14459 O O   . TYR D 429 ? 0.3523 0.6626 0.3358 -0.1327 0.0530  0.0210  429 TYR D O   
14460 C CB  . TYR D 429 ? 0.3020 0.5493 0.2692 -0.1021 0.0480  0.0449  429 TYR D CB  
14461 C CG  . TYR D 429 ? 0.3518 0.5860 0.3168 -0.1190 0.0567  0.0424  429 TYR D CG  
14462 C CD1 . TYR D 429 ? 0.3731 0.6246 0.3424 -0.1270 0.0556  0.0318  429 TYR D CD1 
14463 C CD2 . TYR D 429 ? 0.3566 0.5613 0.3160 -0.1272 0.0652  0.0503  429 TYR D CD2 
14464 C CE1 . TYR D 429 ? 0.4253 0.6653 0.3950 -0.1433 0.0630  0.0279  429 TYR D CE1 
14465 C CE2 . TYR D 429 ? 0.3592 0.5511 0.3190 -0.1433 0.0719  0.0479  429 TYR D CE2 
14466 C CZ  . TYR D 429 ? 0.4550 0.6646 0.4207 -0.1516 0.0709  0.0361  429 TYR D CZ  
14467 O OH  . TYR D 429 ? 0.4703 0.6671 0.4385 -0.1682 0.0771  0.0317  429 TYR D OH  
14468 N N   . ILE D 430 ? 0.2575 0.5861 0.2420 -0.1076 0.0355  0.0201  430 ILE D N   
14469 C CA  . ILE D 430 ? 0.3029 0.6619 0.2931 -0.1159 0.0330  0.0063  430 ILE D CA  
14470 C C   . ILE D 430 ? 0.2906 0.6713 0.2869 -0.1227 0.0348  -0.0007 430 ILE D C   
14471 O O   . ILE D 430 ? 0.3215 0.7122 0.3225 -0.1375 0.0408  -0.0100 430 ILE D O   
14472 C CB  . ILE D 430 ? 0.2195 0.5979 0.2098 -0.1027 0.0209  0.0028  430 ILE D CB  
14473 C CG1 . ILE D 430 ? 0.2194 0.5780 0.2044 -0.0981 0.0204  0.0080  430 ILE D CG1 
14474 C CG2 . ILE D 430 ? 0.2859 0.6962 0.2798 -0.1091 0.0179  -0.0122 430 ILE D CG2 
14475 C CD1 . ILE D 430 ? 0.1962 0.5680 0.1816 -0.0823 0.0084  0.0093  430 ILE D CD1 
14476 N N   . ALA D 431 ? 0.3028 0.6910 0.2998 -0.1120 0.0299  0.0030  431 ALA D N   
14477 C CA  . ALA D 431 ? 0.2782 0.6886 0.2806 -0.1174 0.0316  -0.0046 431 ALA D CA  
14478 C C   . ALA D 431 ? 0.3295 0.7271 0.3324 -0.1341 0.0446  -0.0029 431 ALA D C   
14479 O O   . ALA D 431 ? 0.3684 0.7827 0.3776 -0.1469 0.0494  -0.0132 431 ALA D O   
14480 C CB  . ALA D 431 ? 0.2662 0.6837 0.2680 -0.1028 0.0244  -0.0003 431 ALA D CB  
14481 N N   . ASP D 432 ? 0.3179 0.6846 0.3137 -0.1338 0.0505  0.0102  432 ASP D N   
14482 C CA  . ASP D 432 ? 0.3642 0.7164 0.3578 -0.1486 0.0627  0.0140  432 ASP D CA  
14483 C C   . ASP D 432 ? 0.3859 0.7340 0.3825 -0.1654 0.0695  0.0080  432 ASP D C   
14484 O O   . ASP D 432 ? 0.4649 0.8179 0.4654 -0.1803 0.0776  0.0041  432 ASP D O   
14485 C CB  . ASP D 432 ? 0.4179 0.7351 0.4010 -0.1432 0.0667  0.0293  432 ASP D CB  
14486 C CG  . ASP D 432 ? 0.3732 0.6941 0.3546 -0.1271 0.0601  0.0342  432 ASP D CG  
14487 O OD1 . ASP D 432 ? 0.3487 0.6992 0.3369 -0.1243 0.0554  0.0266  432 ASP D OD1 
14488 O OD2 . ASP D 432 ? 0.4639 0.7581 0.4377 -0.1172 0.0595  0.0448  432 ASP D OD2 
14489 N N   . ALA D 433 ? 0.3915 0.7311 0.3869 -0.1636 0.0665  0.0067  433 ALA D N   
14490 C CA  . ALA D 433 ? 0.3920 0.7303 0.3920 -0.1793 0.0718  -0.0012 433 ALA D CA  
14491 C C   . ALA D 433 ? 0.4261 0.7983 0.4373 -0.1877 0.0712  -0.0170 433 ALA D C   
14492 O O   . ALA D 433 ? 0.4927 0.8654 0.5096 -0.2037 0.0794  -0.0219 433 ALA D O   
14493 C CB  . ALA D 433 ? 0.3653 0.6956 0.3627 -0.1743 0.0672  -0.0025 433 ALA D CB  
14494 N N   . LEU D 434 ? 0.3932 0.7930 0.4077 -0.1765 0.0613  -0.0252 434 LEU D N   
14495 C CA  . LEU D 434 ? 0.3513 0.7827 0.3761 -0.1823 0.0597  -0.0415 434 LEU D CA  
14496 C C   . LEU D 434 ? 0.4444 0.8869 0.4742 -0.1894 0.0656  -0.0437 434 LEU D C   
14497 O O   . LEU D 434 ? 0.4856 0.9421 0.5247 -0.2024 0.0709  -0.0548 434 LEU D O   
14498 C CB  . LEU D 434 ? 0.3646 0.8196 0.3894 -0.1668 0.0472  -0.0484 434 LEU D CB  
14499 C CG  . LEU D 434 ? 0.3958 0.8809 0.4303 -0.1705 0.0447  -0.0663 434 LEU D CG  
14500 C CD1 . LEU D 434 ? 0.4222 0.9042 0.4630 -0.1863 0.0509  -0.0750 434 LEU D CD1 
14501 C CD2 . LEU D 434 ? 0.3834 0.8847 0.4146 -0.1535 0.0330  -0.0708 434 LEU D CD2 
14502 N N   . ILE D 435 ? 0.4161 0.8532 0.4405 -0.1811 0.0650  -0.0338 435 ILE D N   
14503 C CA  . ILE D 435 ? 0.4236 0.8713 0.4516 -0.1882 0.0713  -0.0355 435 ILE D CA  
14504 C C   . ILE D 435 ? 0.5576 0.9863 0.5854 -0.2067 0.0844  -0.0309 435 ILE D C   
14505 O O   . ILE D 435 ? 0.5576 1.0010 0.5935 -0.2198 0.0910  -0.0394 435 ILE D O   
14506 C CB  . ILE D 435 ? 0.3231 0.7670 0.3446 -0.1753 0.0679  -0.0255 435 ILE D CB  
14507 C CG1 . ILE D 435 ? 0.3582 0.8226 0.3811 -0.1576 0.0545  -0.0311 435 ILE D CG1 
14508 C CG2 . ILE D 435 ? 0.3884 0.8423 0.4124 -0.1842 0.0757  -0.0269 435 ILE D CG2 
14509 C CD1 . ILE D 435 ? 0.3190 0.7748 0.3356 -0.1424 0.0491  -0.0202 435 ILE D CD1 
14510 N N   . GLY D 436 ? 0.5065 0.9015 0.5252 -0.2078 0.0882  -0.0175 436 GLY D N   
14511 C CA  . GLY D 436 ? 0.5237 0.8960 0.5408 -0.2244 0.0997  -0.0113 436 GLY D CA  
14512 C C   . GLY D 436 ? 0.5975 0.9784 0.6256 -0.2401 0.1038  -0.0237 436 GLY D C   
14513 O O   . GLY D 436 ? 0.6781 1.0447 0.7076 -0.2556 0.1134  -0.0204 436 GLY D O   
14514 N N   . LEU D 437 ? 0.5880 0.9912 0.6240 -0.2361 0.0964  -0.0377 437 LEU D N   
14515 C CA  . LEU D 437 ? 0.6608 1.0763 0.7090 -0.2496 0.0993  -0.0520 437 LEU D CA  
14516 C C   . LEU D 437 ? 0.7211 1.1643 0.7803 -0.2579 0.1032  -0.0636 437 LEU D C   
14517 O O   . LEU D 437 ? 0.7657 1.2220 0.8370 -0.2686 0.1055  -0.0771 437 LEU D O   
14518 C CB  . LEU D 437 ? 0.5461 0.9753 0.5975 -0.2415 0.0897  -0.0632 437 LEU D CB  
14519 C CG  . LEU D 437 ? 0.5229 0.9271 0.5674 -0.2388 0.0877  -0.0568 437 LEU D CG  
14520 C CD1 . LEU D 437 ? 0.5013 0.9249 0.5496 -0.2322 0.0788  -0.0699 437 LEU D CD1 
14521 C CD2 . LEU D 437 ? 0.5816 0.9594 0.6285 -0.2555 0.0972  -0.0535 437 LEU D CD2 
14522 N N   . LYS D 438 ? 0.6945 1.1473 0.7506 -0.2533 0.1041  -0.0596 438 LYS D N   
14523 C CA  . LYS D 438 ? 0.8039 1.2807 0.8700 -0.2630 0.1097  -0.0696 438 LYS D CA  
14524 C C   . LYS D 438 ? 0.8298 1.2897 0.8966 -0.2820 0.1231  -0.0630 438 LYS D C   
14525 O O   . LYS D 438 ? 0.8635 1.3403 0.9370 -0.2914 0.1296  -0.0687 438 LYS D O   
14526 C CB  . LYS D 438 ? 0.7331 1.2271 0.7958 -0.2517 0.1058  -0.0687 438 LYS D CB  
14527 C CG  . LYS D 438 ? 0.7399 1.2560 0.8048 -0.2340 0.0924  -0.0780 438 LYS D CG  
14528 C CD  . LYS D 438 ? 0.7653 1.3152 0.8399 -0.2325 0.0907  -0.0923 438 LYS D CD  
14529 C CE  . LYS D 438 ? 0.6630 1.2286 0.7359 -0.2121 0.0773  -0.0966 438 LYS D CE  
14530 N NZ  . LYS D 438 ? 0.5756 1.1260 0.6364 -0.2001 0.0738  -0.0813 438 LYS D NZ  
14531 N N   . GLU D 439 ? 0.9145 1.3410 0.9746 -0.2877 0.1271  -0.0510 439 GLU D N   
14532 C CA  . GLU D 439 ? 1.0013 1.4085 1.0624 -0.3059 0.1388  -0.0441 439 GLU D CA  
14533 C C   . GLU D 439 ? 1.0165 1.4283 1.0926 -0.3196 0.1413  -0.0570 439 GLU D C   
14534 O O   . GLU D 439 ? 1.0114 1.4321 1.0974 -0.3347 0.1495  -0.0626 439 GLU D O   
14535 C CB  . GLU D 439 ? 1.0416 1.4081 1.0880 -0.3042 0.1410  -0.0241 439 GLU D CB  
14536 C CG  . GLU D 439 ? 1.1554 1.4969 1.2015 -0.3222 0.1518  -0.0146 439 GLU D CG  
14537 C CD  . GLU D 439 ? 1.1680 1.5149 1.2098 -0.3296 0.1604  -0.0080 439 GLU D CD  
14538 O OE1 . GLU D 439 ? 1.1300 1.4978 1.1682 -0.3197 0.1578  -0.0101 439 GLU D OE1 
14539 O OE2 . GLU D 439 ? 1.2459 1.5761 1.2882 -0.3454 0.1695  -0.0007 439 GLU D OE2 
14540 N N   . LYS D 440 ? 0.9786 1.3853 1.0569 -0.3144 0.1344  -0.0624 440 LYS D N   
14541 C CA  . LYS D 440 ? 0.9570 1.3677 1.0497 -0.3256 0.1355  -0.0758 440 LYS D CA  
14542 C C   . LYS D 440 ? 0.8544 1.2980 0.9567 -0.3172 0.1265  -0.0952 440 LYS D C   
14543 O O   . LYS D 440 ? 0.8545 1.3001 0.9661 -0.3214 0.1241  -0.1064 440 LYS D O   
14544 C CB  . LYS D 440 ? 0.9700 1.3466 1.0585 -0.3285 0.1353  -0.0678 440 LYS D CB  
14545 C CG  . LYS D 440 ? 1.0309 1.3712 1.1088 -0.3350 0.1426  -0.0477 440 LYS D CG  
14546 C CD  . LYS D 440 ? 1.0476 1.3889 1.1325 -0.3522 0.1532  -0.0459 440 LYS D CD  
14547 C CE  . LYS D 440 ? 1.0465 1.3518 1.1192 -0.3577 0.1596  -0.0247 440 LYS D CE  
14548 N NZ  . LYS D 440 ? 0.9532 1.2632 1.0294 -0.3726 0.1699  -0.0211 440 LYS D NZ  
14549 N N   . PHE D 441 ? 0.8014 1.2703 0.9018 -0.3050 0.1208  -0.0995 441 PHE D N   
14550 C CA  . PHE D 441 ? 0.7212 1.2203 0.8298 -0.2956 0.1113  -0.1171 441 PHE D CA  
14551 C C   . PHE D 441 ? 0.8061 1.3246 0.9331 -0.3083 0.1150  -0.1349 441 PHE D C   
14552 O O   . PHE D 441 ? 0.8105 1.3425 0.9457 -0.3052 0.1086  -0.1490 441 PHE D O   
14553 C CB  . PHE D 441 ? 0.7477 1.2690 0.8522 -0.2809 0.1048  -0.1182 441 PHE D CB  
14554 C CG  . PHE D 441 ? 0.8628 1.4020 0.9744 -0.2885 0.1116  -0.1227 441 PHE D CG  
14555 C CD1 . PHE D 441 ? 0.8214 1.3909 0.9487 -0.2922 0.1111  -0.1418 441 PHE D CD1 
14556 C CD2 . PHE D 441 ? 0.8425 1.3688 0.9450 -0.2915 0.1185  -0.1083 441 PHE D CD2 
14557 C CE1 . PHE D 441 ? 0.7410 1.3279 0.8753 -0.2997 0.1179  -0.1469 441 PHE D CE1 
14558 C CE2 . PHE D 441 ? 0.8828 1.4269 0.9913 -0.2990 0.1253  -0.1129 441 PHE D CE2 
14559 C CZ  . PHE D 441 ? 0.9025 1.4773 1.0271 -0.3035 0.1252  -0.1324 441 PHE D CZ  
14560 N N   . ALA D 442 ? 0.8781 1.3985 1.0120 -0.3227 0.1254  -0.1344 442 ALA D N   
14561 C CA  . ALA D 442 ? 0.8141 1.3539 0.9670 -0.3354 0.1298  -0.1514 442 ALA D CA  
14562 C C   . ALA D 442 ? 0.8277 1.3475 0.9881 -0.3485 0.1339  -0.1526 442 ALA D C   
14563 O O   . ALA D 442 ? 0.7971 1.3308 0.9710 -0.3504 0.1303  -0.1691 442 ALA D O   
14564 C CB  . ALA D 442 ? 0.7771 1.3270 0.9346 -0.3464 0.1399  -0.1504 442 ALA D CB  
14565 N N   . THR D 443 ? 0.8722 1.3585 1.0243 -0.3570 0.1408  -0.1356 443 THR D N   
14566 C CA  . THR D 443 ? 0.9070 1.3703 1.0661 -0.3690 0.1441  -0.1354 443 THR D CA  
14567 C C   . THR D 443 ? 0.9186 1.3717 1.0716 -0.3576 0.1345  -0.1368 443 THR D C   
14568 O O   . THR D 443 ? 1.0051 1.4283 1.1464 -0.3554 0.1343  -0.1227 443 THR D O   
14569 C CB  . THR D 443 ? 1.0114 1.4413 1.1636 -0.3811 0.1538  -0.1160 443 THR D CB  
14570 O OG1 . THR D 443 ? 1.0502 1.4916 1.2041 -0.3894 0.1624  -0.1130 443 THR D OG1 
14571 C CG2 . THR D 443 ? 0.9951 1.4042 1.1593 -0.3959 0.1576  -0.1182 443 THR D CG2 
14572 N N   . LEU D 444 ? 0.8967 1.3759 1.0576 -0.3498 0.1262  -0.1546 444 LEU D N   
14573 C CA  . LEU D 444 ? 0.8425 1.3184 0.9974 -0.3381 0.1165  -0.1582 444 LEU D CA  
14574 C C   . LEU D 444 ? 0.8449 1.3365 1.0161 -0.3422 0.1129  -0.1787 444 LEU D C   
14575 O O   . LEU D 444 ? 0.7843 1.3055 0.9668 -0.3410 0.1107  -0.1936 444 LEU D O   
14576 C CB  . LEU D 444 ? 0.8225 1.3155 0.9654 -0.3188 0.1073  -0.1567 444 LEU D CB  
14577 C CG  . LEU D 444 ? 0.8135 1.2876 0.9401 -0.3068 0.1012  -0.1454 444 LEU D CG  
14578 C CD1 . LEU D 444 ? 0.7349 1.1747 0.8499 -0.3110 0.1082  -0.1245 444 LEU D CD1 
14579 C CD2 . LEU D 444 ? 0.7124 1.2072 0.8302 -0.2879 0.0911  -0.1461 444 LEU D CD2 
14580 N N   . LYS D 445 ? 0.8593 1.3310 1.0321 -0.3463 0.1120  -0.1800 445 LYS D N   
14581 C CA  . LYS D 445 ? 0.8594 1.3432 1.0477 -0.3503 0.1084  -0.1995 445 LYS D CA  
14582 C C   . LYS D 445 ? 0.8301 1.3341 1.0129 -0.3339 0.0964  -0.2102 445 LYS D C   
14583 O O   . LYS D 445 ? 0.8544 1.3518 1.0207 -0.3216 0.0911  -0.2008 445 LYS D O   
14584 C CB  . LYS D 445 ? 0.9541 1.4076 1.1475 -0.3616 0.1120  -0.1975 445 LYS D CB  
14585 C CG  . LYS D 445 ? 1.0716 1.5054 1.2742 -0.3795 0.1230  -0.1892 445 LYS D CG  
14586 C CD  . LYS D 445 ? 1.0843 1.4839 1.2905 -0.3883 0.1248  -0.1850 445 LYS D CD  
14587 C CE  . LYS D 445 ? 1.1227 1.5028 1.3394 -0.4063 0.1347  -0.1767 445 LYS D CE  
14588 N NZ  . LYS D 445 ? 1.0938 1.4367 1.3132 -0.4138 0.1354  -0.1701 445 LYS D NZ  
14589 N N   . GLY D 446 ? 0.7764 1.3052 0.9733 -0.3336 0.0919  -0.2297 446 GLY D N   
14590 C CA  . GLY D 446 ? 0.7418 1.2886 0.9344 -0.3189 0.0803  -0.2406 446 GLY D CA  
14591 C C   . GLY D 446 ? 0.7589 1.2892 0.9493 -0.3197 0.0772  -0.2445 446 GLY D C   
14592 O O   . GLY D 446 ? 0.7744 1.2805 0.9705 -0.3324 0.0837  -0.2419 446 GLY D O   
14593 N N   . LEU D 447 ? 0.7376 1.2807 0.9196 -0.3055 0.0667  -0.2509 447 LEU D N   
14594 C CA  . LEU D 447 ? 0.7143 1.2444 0.8912 -0.3038 0.0628  -0.2550 447 LEU D CA  
14595 C C   . LEU D 447 ? 0.7249 1.2777 0.9100 -0.2985 0.0544  -0.2748 447 LEU D C   
14596 O O   . LEU D 447 ? 0.7204 1.2993 0.9106 -0.2916 0.0492  -0.2827 447 LEU D O   
14597 C CB  . LEU D 447 ? 0.7252 1.2452 0.8803 -0.2911 0.0582  -0.2415 447 LEU D CB  
14598 C CG  . LEU D 447 ? 0.7637 1.2544 0.9089 -0.2954 0.0655  -0.2220 447 LEU D CG  
14599 C CD1 . LEU D 447 ? 0.7201 1.2128 0.8654 -0.2977 0.0712  -0.2102 447 LEU D CD1 
14600 C CD2 . LEU D 447 ? 0.6719 1.1547 0.7978 -0.2827 0.0598  -0.2125 447 LEU D CD2 
14601 N N   . GLU D 448 ? 0.7234 1.2653 0.9101 -0.3015 0.0528  -0.2830 448 GLU D N   
14602 C CA  . GLU D 448 ? 0.7964 1.3570 0.9910 -0.2975 0.0453  -0.3021 448 GLU D CA  
14603 C C   . GLU D 448 ? 0.8728 1.4244 1.0536 -0.2898 0.0394  -0.3037 448 GLU D C   
14604 O O   . GLU D 448 ? 0.8086 1.3357 0.9802 -0.2925 0.0434  -0.2937 448 GLU D O   
14605 C CB  . GLU D 448 ? 0.6306 1.1903 0.8489 -0.3129 0.0508  -0.3159 448 GLU D CB  
14606 C CG  . GLU D 448 ? 0.6327 1.2140 0.8617 -0.3091 0.0431  -0.3368 448 GLU D CG  
14607 C CD  . GLU D 448 ? 0.6897 1.2692 0.9433 -0.3246 0.0488  -0.3500 448 GLU D CD  
14608 O OE1 . GLU D 448 ? 0.6888 1.2592 0.9528 -0.3372 0.0582  -0.3435 448 GLU D OE1 
14609 O OE2 . GLU D 448 ? 0.6437 1.2306 0.9060 -0.3241 0.0439  -0.3666 448 GLU D OE2 
14610 N N   . PHE D 449 ? 0.8263 1.3978 1.0055 -0.2799 0.0299  -0.3163 449 PHE D N   
14611 C CA  . PHE D 449 ? 0.8420 1.4082 1.0076 -0.2721 0.0240  -0.3195 449 PHE D CA  
14612 C C   . PHE D 449 ? 0.8969 1.4453 1.0737 -0.2842 0.0290  -0.3299 449 PHE D C   
14613 O O   . PHE D 449 ? 0.9287 1.4858 1.1236 -0.2910 0.0289  -0.3456 449 PHE D O   
14614 C CB  . PHE D 449 ? 0.8180 1.4092 0.9793 -0.2587 0.0123  -0.3294 449 PHE D CB  
14615 C CG  . PHE D 449 ? 0.8226 1.4247 0.9677 -0.2431 0.0051  -0.3167 449 PHE D CG  
14616 C CD1 . PHE D 449 ? 0.9120 1.5025 1.0354 -0.2338 0.0027  -0.3029 449 PHE D CD1 
14617 C CD2 . PHE D 449 ? 0.8214 1.4443 0.9739 -0.2374 0.0004  -0.3187 449 PHE D CD2 
14618 C CE1 . PHE D 449 ? 0.8473 1.4456 0.9569 -0.2191 -0.0043 -0.2903 449 PHE D CE1 
14619 C CE2 . PHE D 449 ? 0.7740 1.4044 0.9132 -0.2223 -0.0070 -0.3069 449 PHE D CE2 
14620 C CZ  . PHE D 449 ? 0.8029 1.4203 0.9207 -0.2131 -0.0093 -0.2921 449 PHE D CZ  
14621 N N   . GLU D 450 ? 0.9342 1.4571 1.1016 -0.2865 0.0331  -0.3215 450 GLU D N   
14622 C CA  . GLU D 450 ? 0.9059 1.4113 1.0810 -0.2940 0.0356  -0.3318 450 GLU D CA  
14623 C C   . GLU D 450 ? 0.8921 1.4052 1.0537 -0.2827 0.0278  -0.3405 450 GLU D C   
14624 O O   . GLU D 450 ? 0.9213 1.4341 1.0924 -0.2860 0.0266  -0.3563 450 GLU D O   
14625 C CB  . GLU D 450 ? 0.8938 1.3652 1.0676 -0.3023 0.0438  -0.3189 450 GLU D CB  
14626 C CG  . GLU D 450 ? 1.0546 1.5042 1.2422 -0.3120 0.0472  -0.3290 450 GLU D CG  
14627 C CD  . GLU D 450 ? 1.1337 1.5470 1.3197 -0.3186 0.0541  -0.3151 450 GLU D CD  
14628 O OE1 . GLU D 450 ? 1.1153 1.5212 1.2849 -0.3130 0.0552  -0.2990 450 GLU D OE1 
14629 O OE2 . GLU D 450 ? 1.1799 1.5715 1.3817 -0.3288 0.0579  -0.3199 450 GLU D OE2 
14630 N N   . TYR D 451 ? 0.8644 1.3841 1.0039 -0.2694 0.0226  -0.3301 451 TYR D N   
14631 C CA  . TYR D 451 ? 0.8661 1.3960 0.9899 -0.2573 0.0146  -0.3359 451 TYR D CA  
14632 C C   . TYR D 451 ? 0.8312 1.3788 0.9387 -0.2430 0.0069  -0.3245 451 TYR D C   
14633 O O   . TYR D 451 ? 0.8475 1.3868 0.9426 -0.2386 0.0084  -0.3078 451 TYR D O   
14634 C CB  . TYR D 451 ? 0.8349 1.3425 0.9467 -0.2567 0.0177  -0.3327 451 TYR D CB  
14635 C CG  . TYR D 451 ? 0.8711 1.3868 0.9593 -0.2422 0.0106  -0.3293 451 TYR D CG  
14636 C CD1 . TYR D 451 ? 0.8528 1.3827 0.9380 -0.2369 0.0044  -0.3430 451 TYR D CD1 
14637 C CD2 . TYR D 451 ? 0.9105 1.4186 0.9791 -0.2339 0.0103  -0.3115 451 TYR D CD2 
14638 C CE1 . TYR D 451 ? 0.9110 1.4464 0.9734 -0.2242 -0.0018 -0.3380 451 TYR D CE1 
14639 C CE2 . TYR D 451 ? 0.8870 1.4003 0.9340 -0.2209 0.0043  -0.3066 451 TYR D CE2 
14640 C CZ  . TYR D 451 ? 0.9242 1.4506 0.9677 -0.2164 -0.0016 -0.3193 451 TYR D CZ  
14641 O OH  . TYR D 451 ? 0.8861 1.4157 0.9072 -0.2042 -0.0073 -0.3127 451 TYR D OH  
14642 N N   . GLU D 452 ? 0.8007 1.3711 0.9089 -0.2355 -0.0019 -0.3333 452 GLU D N   
14643 C CA  . GLU D 452 ? 0.7176 1.3023 0.8119 -0.2210 -0.0106 -0.3225 452 GLU D CA  
14644 C C   . GLU D 452 ? 0.6973 1.2866 0.7726 -0.2089 -0.0194 -0.3233 452 GLU D C   
14645 O O   . GLU D 452 ? 0.7433 1.3414 0.8230 -0.2099 -0.0232 -0.3388 452 GLU D O   
14646 C CB  . GLU D 452 ? 0.7196 1.3255 0.8292 -0.2203 -0.0149 -0.3293 452 GLU D CB  
14647 C CG  . GLU D 452 ? 0.7274 1.3452 0.8247 -0.2048 -0.0245 -0.3178 452 GLU D CG  
14648 C CD  . GLU D 452 ? 0.7610 1.3982 0.8751 -0.2043 -0.0281 -0.3244 452 GLU D CD  
14649 O OE1 . GLU D 452 ? 0.8714 1.5164 1.0053 -0.2147 -0.0248 -0.3403 452 GLU D OE1 
14650 O OE2 . GLU D 452 ? 0.7615 1.4053 0.8696 -0.1933 -0.0341 -0.3140 452 GLU D OE2 
14651 N N   . PRO D 453 ? 0.7079 1.2908 0.7619 -0.1977 -0.0228 -0.3067 453 PRO D N   
14652 C CA  . PRO D 453 ? 0.7253 1.3112 0.7595 -0.1862 -0.0315 -0.3051 453 PRO D CA  
14653 C C   . PRO D 453 ? 0.7144 1.3182 0.7469 -0.1758 -0.0434 -0.3054 453 PRO D C   
14654 O O   . PRO D 453 ? 0.6921 1.3034 0.7337 -0.1736 -0.0453 -0.3003 453 PRO D O   
14655 C CB  . PRO D 453 ? 0.6620 1.2316 0.6764 -0.1790 -0.0297 -0.2853 453 PRO D CB  
14656 C CG  . PRO D 453 ? 0.7144 1.2718 0.7390 -0.1882 -0.0195 -0.2793 453 PRO D CG  
14657 C CD  . PRO D 453 ? 0.6446 1.2146 0.6913 -0.1959 -0.0182 -0.2883 453 PRO D CD  
14658 N N   . PRO D 454 ? 0.6961 1.3064 0.7168 -0.1692 -0.0520 -0.3113 454 PRO D N   
14659 C CA  . PRO D 454 ? 0.6662 1.2913 0.6847 -0.1594 -0.0649 -0.3120 454 PRO D CA  
14660 C C   . PRO D 454 ? 0.5909 1.2117 0.5989 -0.1477 -0.0708 -0.2923 454 PRO D C   
14661 O O   . PRO D 454 ? 0.6503 1.2825 0.6663 -0.1426 -0.0785 -0.2932 454 PRO D O   
14662 C CB  . PRO D 454 ? 0.6896 1.3163 0.6909 -0.1546 -0.0720 -0.3181 454 PRO D CB  
14663 C CG  . PRO D 454 ? 0.7196 1.3399 0.7254 -0.1652 -0.0619 -0.3295 454 PRO D CG  
14664 C CD  . PRO D 454 ? 0.7242 1.3288 0.7340 -0.1710 -0.0505 -0.3190 454 PRO D CD  
14665 N N   . VAL D 455 ? 0.6296 1.2337 0.6209 -0.1430 -0.0677 -0.2751 455 VAL D N   
14666 C CA  . VAL D 455 ? 0.6374 1.2347 0.6187 -0.1314 -0.0733 -0.2559 455 VAL D CA  
14667 C C   . VAL D 455 ? 0.6625 1.2446 0.6418 -0.1335 -0.0632 -0.2421 455 VAL D C   
14668 O O   . VAL D 455 ? 0.6652 1.2386 0.6437 -0.1419 -0.0537 -0.2451 455 VAL D O   
14669 C CB  . VAL D 455 ? 0.6112 1.2015 0.5678 -0.1193 -0.0846 -0.2462 455 VAL D CB  
14670 C CG1 . VAL D 455 ? 0.5619 1.1663 0.5181 -0.1171 -0.0958 -0.2596 455 VAL D CG1 
14671 C CG2 . VAL D 455 ? 0.5759 1.1515 0.5141 -0.1205 -0.0788 -0.2410 455 VAL D CG2 
14672 N N   . LEU D 456 ? 0.6609 1.2393 0.6400 -0.1255 -0.0657 -0.2273 456 LEU D N   
14673 C CA  . LEU D 456 ? 0.6542 1.2180 0.6296 -0.1247 -0.0581 -0.2118 456 LEU D CA  
14674 C C   . LEU D 456 ? 0.6340 1.1969 0.6237 -0.1392 -0.0453 -0.2190 456 LEU D C   
14675 O O   . LEU D 456 ? 0.6498 1.1981 0.6332 -0.1430 -0.0375 -0.2127 456 LEU D O   
14676 C CB  . LEU D 456 ? 0.7453 1.2917 0.6983 -0.1184 -0.0587 -0.1998 456 LEU D CB  
14677 C CG  . LEU D 456 ? 0.7228 1.2645 0.6590 -0.1047 -0.0710 -0.1893 456 LEU D CG  
14678 C CD1 . LEU D 456 ? 0.6181 1.1461 0.5324 -0.1022 -0.0708 -0.1840 456 LEU D CD1 
14679 C CD2 . LEU D 456 ? 0.6563 1.1902 0.5936 -0.0948 -0.0742 -0.1723 456 LEU D CD2 
14680 N N   . ARG D 457 ? 0.6760 1.2532 0.6854 -0.1476 -0.0432 -0.2322 457 ARG D N   
14681 C CA  . ARG D 457 ? 0.6716 1.2464 0.6951 -0.1636 -0.0317 -0.2422 457 ARG D CA  
14682 C C   . ARG D 457 ? 0.6148 1.1765 0.6381 -0.1672 -0.0231 -0.2291 457 ARG D C   
14683 O O   . ARG D 457 ? 0.5922 1.1414 0.6180 -0.1786 -0.0141 -0.2320 457 ARG D O   
14684 C CB  . ARG D 457 ? 0.6546 1.2467 0.6997 -0.1714 -0.0315 -0.2578 457 ARG D CB  
14685 C CG  . ARG D 457 ? 0.6349 1.2381 0.6884 -0.1653 -0.0351 -0.2522 457 ARG D CG  
14686 C CD  . ARG D 457 ? 0.5794 1.2010 0.6537 -0.1719 -0.0359 -0.2691 457 ARG D CD  
14687 N NE  . ARG D 457 ? 0.6987 1.3286 0.7839 -0.1702 -0.0349 -0.2648 457 ARG D NE  
14688 C CZ  . ARG D 457 ? 0.7250 1.3713 0.8293 -0.1750 -0.0349 -0.2773 457 ARG D CZ  
14689 N NH1 . ARG D 457 ? 0.6284 1.2849 0.7441 -0.1816 -0.0363 -0.2950 457 ARG D NH1 
14690 N NH2 . ARG D 457 ? 0.6524 1.3053 0.7650 -0.1730 -0.0332 -0.2726 457 ARG D NH2 
14691 N N   . HIS D 458 ? 0.6098 1.1725 0.6303 -0.1573 -0.0263 -0.2148 458 HIS D N   
14692 C CA  . HIS D 458 ? 0.6003 1.1519 0.6206 -0.1600 -0.0187 -0.2022 458 HIS D CA  
14693 C C   . HIS D 458 ? 0.5675 1.0991 0.5725 -0.1595 -0.0149 -0.1930 458 HIS D C   
14694 O O   . HIS D 458 ? 0.5635 1.0832 0.5692 -0.1661 -0.0073 -0.1864 458 HIS D O   
14695 C CB  . HIS D 458 ? 0.5970 1.1534 0.6170 -0.1474 -0.0238 -0.1892 458 HIS D CB  
14696 C CG  . HIS D 458 ? 0.5316 1.0813 0.5360 -0.1307 -0.0332 -0.1768 458 HIS D CG  
14697 N ND1 . HIS D 458 ? 0.5963 1.1508 0.5944 -0.1241 -0.0427 -0.1821 458 HIS D ND1 
14698 C CD2 . HIS D 458 ? 0.5620 1.0986 0.5561 -0.1198 -0.0346 -0.1591 458 HIS D CD2 
14699 C CE1 . HIS D 458 ? 0.6158 1.1589 0.5995 -0.1106 -0.0494 -0.1677 458 HIS D CE1 
14700 N NE2 . HIS D 458 ? 0.5954 1.1274 0.5774 -0.1076 -0.0445 -0.1538 458 HIS D NE2 
14701 N N   . PHE D 459 ? 0.5710 1.0979 0.5622 -0.1523 -0.0200 -0.1926 459 PHE D N   
14702 C CA  . PHE D 459 ? 0.6025 1.1105 0.5802 -0.1528 -0.0157 -0.1865 459 PHE D CA  
14703 C C   . PHE D 459 ? 0.6771 1.1780 0.6614 -0.1684 -0.0074 -0.2013 459 PHE D C   
14704 O O   . PHE D 459 ? 0.6101 1.0937 0.5918 -0.1744 -0.0002 -0.1973 459 PHE D O   
14705 C CB  . PHE D 459 ? 0.5025 1.0071 0.4630 -0.1406 -0.0231 -0.1814 459 PHE D CB  
14706 C CG  . PHE D 459 ? 0.4764 0.9784 0.4288 -0.1251 -0.0305 -0.1638 459 PHE D CG  
14707 C CD1 . PHE D 459 ? 0.4992 0.9928 0.4532 -0.1211 -0.0276 -0.1493 459 PHE D CD1 
14708 C CD2 . PHE D 459 ? 0.5240 1.0301 0.4673 -0.1148 -0.0408 -0.1620 459 PHE D CD2 
14709 C CE1 . PHE D 459 ? 0.5082 0.9971 0.4569 -0.1066 -0.0343 -0.1339 459 PHE D CE1 
14710 C CE2 . PHE D 459 ? 0.4557 0.9555 0.3925 -0.1012 -0.0479 -0.1464 459 PHE D CE2 
14711 C CZ  . PHE D 459 ? 0.5142 1.0051 0.4546 -0.0969 -0.0445 -0.1326 459 PHE D CZ  
14712 N N   . THR D 460 ? 0.6808 1.1929 0.6748 -0.1751 -0.0084 -0.2189 460 THR D N   
14713 C CA  . THR D 460 ? 0.6823 1.1851 0.6819 -0.1875 -0.0020 -0.2337 460 THR D CA  
14714 C C   . THR D 460 ? 0.7288 1.2393 0.7503 -0.2009 0.0015  -0.2501 460 THR D C   
14715 O O   . THR D 460 ? 0.7827 1.2859 0.8113 -0.2100 0.0056  -0.2640 460 THR D O   
14716 C CB  . THR D 460 ? 0.6906 1.1946 0.6773 -0.1812 -0.0064 -0.2400 460 THR D CB  
14717 O OG1 . THR D 460 ? 0.6281 1.1497 0.6105 -0.1710 -0.0166 -0.2395 460 THR D OG1 
14718 C CG2 . THR D 460 ? 0.6800 1.1669 0.6478 -0.1739 -0.0049 -0.2271 460 THR D CG2 
14719 N N   . ALA D 461 ? 0.6800 1.2038 0.7136 -0.2022 0.0004  -0.2494 461 ALA D N   
14720 C CA  . ALA D 461 ? 0.6711 1.2005 0.7263 -0.2154 0.0045  -0.2641 461 ALA D CA  
14721 C C   . ALA D 461 ? 0.7963 1.3049 0.8618 -0.2300 0.0153  -0.2617 461 ALA D C   
14722 O O   . ALA D 461 ? 0.8104 1.3087 0.8709 -0.2297 0.0188  -0.2468 461 ALA D O   
14723 C CB  . ALA D 461 ? 0.7397 1.2901 0.8051 -0.2120 0.0003  -0.2647 461 ALA D CB  
14724 N N   . ARG D 462 ? 0.7844 1.2851 0.8650 -0.2424 0.0202  -0.2758 462 ARG D N   
14725 C CA  . ARG D 462 ? 0.8228 1.2999 0.9160 -0.2570 0.0300  -0.2733 462 ARG D CA  
14726 C C   . ARG D 462 ? 0.8454 1.3315 0.9579 -0.2664 0.0334  -0.2770 462 ARG D C   
14727 O O   . ARG D 462 ? 0.9238 1.4215 1.0504 -0.2709 0.0320  -0.2925 462 ARG D O   
14728 C CB  . ARG D 462 ? 0.8016 1.2599 0.9008 -0.2643 0.0333  -0.2850 462 ARG D CB  
14729 C CG  . ARG D 462 ? 0.7777 1.2235 0.8588 -0.2565 0.0319  -0.2815 462 ARG D CG  
14730 C CD  . ARG D 462 ? 0.8206 1.2412 0.9110 -0.2652 0.0372  -0.2906 462 ARG D CD  
14731 N NE  . ARG D 462 ? 0.7928 1.1869 0.8962 -0.2771 0.0451  -0.2822 462 ARG D NE  
14732 C CZ  . ARG D 462 ? 0.7924 1.1617 0.8888 -0.2775 0.0493  -0.2684 462 ARG D CZ  
14733 N NH1 . ARG D 462 ? 0.7250 1.0929 0.8022 -0.2671 0.0467  -0.2626 462 ARG D NH1 
14734 N NH2 . ARG D 462 ? 0.7348 1.0791 0.8434 -0.2881 0.0560  -0.2595 462 ARG D NH2 
14735 N N   . LEU D 463 ? 0.8933 1.3744 1.0065 -0.2692 0.0381  -0.2628 463 LEU D N   
14736 C CA  . LEU D 463 ? 0.9016 1.3909 1.0314 -0.2779 0.0424  -0.2645 463 LEU D CA  
14737 C C   . LEU D 463 ? 0.9242 1.3861 1.0673 -0.2943 0.0525  -0.2615 463 LEU D C   
14738 O O   . LEU D 463 ? 0.9001 1.3361 1.0403 -0.2980 0.0556  -0.2584 463 LEU D O   
14739 C CB  . LEU D 463 ? 0.8639 1.3656 0.9868 -0.2705 0.0413  -0.2512 463 LEU D CB  
14740 C CG  . LEU D 463 ? 0.8831 1.4106 0.9954 -0.2535 0.0305  -0.2525 463 LEU D CG  
14741 C CD1 . LEU D 463 ? 0.8889 1.4305 1.0024 -0.2485 0.0301  -0.2440 463 LEU D CD1 
14742 C CD2 . LEU D 463 ? 0.8759 1.4217 0.9964 -0.2517 0.0243  -0.2709 463 LEU D CD2 
14743 N N   . LYS D 464 ? 0.9096 1.3764 1.0676 -0.3038 0.0576  -0.2620 464 LYS D N   
14744 C CA  . LYS D 464 ? 0.9083 1.3503 1.0804 -0.3197 0.0669  -0.2587 464 LYS D CA  
14745 C C   . LYS D 464 ? 0.8467 1.2992 1.0288 -0.3268 0.0723  -0.2545 464 LYS D C   
14746 O O   . LYS D 464 ? 0.8118 1.2929 1.0016 -0.3241 0.0687  -0.2660 464 LYS D O   
14747 C CB  . LYS D 464 ? 0.9046 1.3415 1.0923 -0.3274 0.0663  -0.2761 464 LYS D CB  
14748 C CG  . LYS D 464 ? 0.9097 1.3128 1.1092 -0.3417 0.0740  -0.2710 464 LYS D CG  
14749 C CD  . LYS D 464 ? 0.9384 1.3109 1.1247 -0.3388 0.0752  -0.2585 464 LYS D CD  
14750 C CE  . LYS D 464 ? 1.0004 1.3377 1.1998 -0.3513 0.0805  -0.2556 464 LYS D CE  
14751 N NZ  . LYS D 464 ? 1.0373 1.3771 1.2532 -0.3556 0.0775  -0.2758 464 LYS D NZ  
14752 N N   . PRO D 465 ? 0.8291 1.2594 1.0112 -0.3355 0.0807  -0.2384 465 PRO D N   
14753 C CA  . PRO D 465 ? 0.7966 1.2361 0.9867 -0.3427 0.0868  -0.2335 465 PRO D CA  
14754 C C   . PRO D 465 ? 0.8391 1.2850 1.0518 -0.3561 0.0905  -0.2473 465 PRO D C   
14755 O O   . PRO D 465 ? 0.8205 1.2491 1.0434 -0.3641 0.0915  -0.2536 465 PRO D O   
14756 C CB  . PRO D 465 ? 0.7900 1.1981 0.9718 -0.3483 0.0946  -0.2118 465 PRO D CB  
14757 C CG  . PRO D 465 ? 0.8077 1.1855 0.9876 -0.3505 0.0942  -0.2101 465 PRO D CG  
14758 C CD  . PRO D 465 ? 0.7952 1.1891 0.9692 -0.3386 0.0849  -0.2237 465 PRO D CD  
# 
