data_9EWU
# 
_entry.id   9EWU 
# 
_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   9EWU         pdb_00009ewu 10.2210/pdb9ewu/pdb 
WWPDB D_1292137714 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2025-02-05 
2 'Structure model' 1 1 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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            citation 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume' 
2 2 'Structure model' '_citation.year'           
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9EWU 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-04 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              florian.nachon@def.gouv.fr 
_pdbx_contact_author.name_first         Florian 
_pdbx_contact_author.name_last          NACHON 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0293-2429 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Panek, D.'       1 ? 
'Pasieka, A.'     2 ? 
'Malawska, B.'    3 ? 
'Nachon, F.'      4 ? 
'Brazzolotto, X.' 5 ? 
# 
_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                   GE 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Angew.Chem.Int.Ed.Engl. 
_citation.journal_id_ASTM           ACIEAY 
_citation.journal_id_CSD            0179 
_citation.journal_id_ISSN           1521-3773 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            64 
_citation.language                  ? 
_citation.page_first                e202420510 
_citation.page_last                 e202420510 
_citation.title                     
;Multifunctional, Fluorene-Based Modulator of Cholinergic and GABAergic Neurotransmission as a Novel Drug Candidate for Palliative Treatment of Alzheimer's Disease.
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1002/anie.202420510 
_citation.pdbx_database_id_PubMed   39523866 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Panek, D.'            1  0000-0002-3211-7188 
primary 'Pasieka, A.'          2  0000-0002-5426-9123 
primary 'Jonczyk, J.'          3  0000-0002-9731-908X 
primary 'Gawlinska, M.'        4  ?                   
primary 'Zareba, P.'           5  0000-0002-5037-6183 
primary 'Siwek, A.'            6  0000-0001-5321-9266 
primary 'Wolak, M.'            7  0000-0002-3161-0878 
primary 'Mordyl, B.'           8  0000-0001-7906-0353 
primary 'Gluch-Lutwin, M.'     9  0000-0003-1632-6569 
primary 'Latacz, G.'           10 0000-0001-9247-2598 
primary 'Brazzolotto, X.'      11 0000-0001-9219-1032 
primary 'Chantegreil, F.'      12 0000-0001-5982-8265 
primary 'Nachon, F.'           13 0000-0003-0293-2429 
primary 'Zdarova Karasova, J.' 14 0000-0003-0891-9591 
primary 'Pejchal, J.'          15 0000-0003-2228-7922 
primary 'Mzik, M.'             16 0000-0003-4649-7828 
primary 'Sestak, V.'           17 0000-0002-4688-2577 
primary 'Prchal, L.'           18 0000-0001-9698-4478 
primary 'Odvarkova, J.'        19 0009-0009-0628-9865 
primary 'Soukup, O.'           20 0000-0001-6376-8701 
primary 'Korabecny, J.'        21 0000-0001-6977-7596 
primary 'Sorf, A.'             22 0000-0001-7829-3980 
primary 'Hamsikova, M.'        23 ?                   
primary 'Zemanova, L.'         24 0000-0002-2732-5935 
primary 'Muckova, L.'          25 0000-0001-6693-6061 
primary 'Vanova, N.'           26 0000-0002-1827-9308 
primary 'Dryja, P.'            27 ?                   
primary 'Salat, K.'            28 0000-0003-0614-5393 
primary 'Hofner, G.'           29 0000-0002-7957-4503 
primary 'Wanner, K.'           30 0000-0003-4399-1425 
primary 'Wieckowska, A.'       31 ?                   
primary 'Malawska, B.'         32 0000-0003-4637-5820 
# 
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 Cholinesterase 59713.512 1  3.1.1.8 
;N17Q, N455Q, N481Q, N486Q mutations compared to mature wild type sequence to avoid too much N-glycozylation. Numeration on the maturated enzyme (devoid of the signal peptide)
;
? ? 
2  branched    man 'alpha-L-fucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose' 367.349   1  ?       ? ? ? 
3  branched    man 
'2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose' 570.542   3  
?       ? ? ? 
4  non-polymer syn 2-acetamido-2-deoxy-beta-D-glucopyranose 221.208   2  ?       ? ? ? 
5  non-polymer syn '2-(N-MORPHOLINO)-ETHANESULFONIC ACID' 195.237   1  ?       ? ? ? 
6  non-polymer syn 'SULFATE ION' 96.063    3  ?       ? ? ? 
7  non-polymer syn GLYCEROL 92.094    1  ?       ? ? ? 
8  non-polymer syn 'N-acetyl-alpha-neuraminic acid' 309.270   1  ?       ? ? ? 
9  non-polymer syn '(2~{R},3~{S})-1-(cyclopropylmethylamino)-3-(9~{H}-fluoren-9-ylamino)-4-phenyl-butan-2-ol' 398.540   1  ?       
? ? ? 
10 water       nat water 18.015    87 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Acylcholine acylhydrolase,Butyrylcholine esterase,Choline esterase II,Pseudocholinesterase' 
# 
_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       
;EDDIIIATKNGKVRGMQLTVFGGTVTAFLGIPYAQPPLGRLRFKKPQSLTKWSDIWNATKYANSCCQNIDQSFPGFHGSE
MWNPNTDLSEDCLYLNVWIPAPKPKNATVLIWIYGGGFQTGTSSLHVYDGKFLARVERVIVVSMNYRVGALGFLALPGNP
EAPGNMGLFDQQLALQWVQKNIAAFGGNPKSVTLFGESAGAASVSLHLLSPGSHSLFTRAILQSGSFNAPWAVTSLYEAR
NRTLNLAKLTGCSRENETEIIKCLRNKDPQEILLNEAFVVPYGTPLSVNFGPTVDGDFLTDMPDILLELGQFKKTQILVG
VNKDEGTAFLVYGAPGFSKDNNSIITRKEFQEGLKIFFPGVSEFGKESILFHYTDWVDDQRPENYREALGDVVGDYNFIC
PALEFTKKFSEWGNNAFFYYFEHRSSKLPWPEWMGVMHGYEIEFVFGLPLERRDQYTKAEEILSRSIVKRWANFAKYGNP
QETQNQSTSWPVFKSTEQKYLTLNTESTRIMTKLRAQQCRFWTSFFPKV
;
_entity_poly.pdbx_seq_one_letter_code_can   
;EDDIIIATKNGKVRGMQLTVFGGTVTAFLGIPYAQPPLGRLRFKKPQSLTKWSDIWNATKYANSCCQNIDQSFPGFHGSE
MWNPNTDLSEDCLYLNVWIPAPKPKNATVLIWIYGGGFQTGTSSLHVYDGKFLARVERVIVVSMNYRVGALGFLALPGNP
EAPGNMGLFDQQLALQWVQKNIAAFGGNPKSVTLFGESAGAASVSLHLLSPGSHSLFTRAILQSGSFNAPWAVTSLYEAR
NRTLNLAKLTGCSRENETEIIKCLRNKDPQEILLNEAFVVPYGTPLSVNFGPTVDGDFLTDMPDILLELGQFKKTQILVG
VNKDEGTAFLVYGAPGFSKDNNSIITRKEFQEGLKIFFPGVSEFGKESILFHYTDWVDDQRPENYREALGDVVGDYNFIC
PALEFTKKFSEWGNNAFFYYFEHRSSKLPWPEWMGVMHGYEIEFVFGLPLERRDQYTKAEEILSRSIVKRWANFAKYGNP
QETQNQSTSWPVFKSTEQKYLTLNTESTRIMTKLRAQQCRFWTSFFPKV
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
4  2-acetamido-2-deoxy-beta-D-glucopyranose                                                   NAG   
5  '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                                                     MES   
6  'SULFATE ION'                                                                              SO4   
7  GLYCEROL                                                                                   GOL   
8  'N-acetyl-alpha-neuraminic acid'                                                           SIA   
9  '(2~{R},3~{S})-1-(cyclopropylmethylamino)-3-(9~{H}-fluoren-9-ylamino)-4-phenyl-butan-2-ol' A1H77 
10 water                                                                                      HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLU n 
1 2   ASP n 
1 3   ASP n 
1 4   ILE n 
1 5   ILE n 
1 6   ILE n 
1 7   ALA n 
1 8   THR n 
1 9   LYS n 
1 10  ASN n 
1 11  GLY n 
1 12  LYS n 
1 13  VAL n 
1 14  ARG n 
1 15  GLY n 
1 16  MET n 
1 17  GLN n 
1 18  LEU n 
1 19  THR n 
1 20  VAL n 
1 21  PHE n 
1 22  GLY n 
1 23  GLY n 
1 24  THR n 
1 25  VAL n 
1 26  THR n 
1 27  ALA n 
1 28  PHE n 
1 29  LEU n 
1 30  GLY n 
1 31  ILE n 
1 32  PRO n 
1 33  TYR n 
1 34  ALA n 
1 35  GLN n 
1 36  PRO n 
1 37  PRO n 
1 38  LEU n 
1 39  GLY n 
1 40  ARG n 
1 41  LEU n 
1 42  ARG n 
1 43  PHE n 
1 44  LYS n 
1 45  LYS n 
1 46  PRO n 
1 47  GLN n 
1 48  SER n 
1 49  LEU n 
1 50  THR n 
1 51  LYS n 
1 52  TRP n 
1 53  SER n 
1 54  ASP n 
1 55  ILE n 
1 56  TRP n 
1 57  ASN n 
1 58  ALA n 
1 59  THR n 
1 60  LYS n 
1 61  TYR n 
1 62  ALA n 
1 63  ASN n 
1 64  SER n 
1 65  CYS n 
1 66  CYS n 
1 67  GLN n 
1 68  ASN n 
1 69  ILE n 
1 70  ASP n 
1 71  GLN n 
1 72  SER n 
1 73  PHE n 
1 74  PRO n 
1 75  GLY n 
1 76  PHE n 
1 77  HIS n 
1 78  GLY n 
1 79  SER n 
1 80  GLU n 
1 81  MET n 
1 82  TRP n 
1 83  ASN n 
1 84  PRO n 
1 85  ASN n 
1 86  THR n 
1 87  ASP n 
1 88  LEU n 
1 89  SER n 
1 90  GLU n 
1 91  ASP n 
1 92  CYS n 
1 93  LEU n 
1 94  TYR n 
1 95  LEU n 
1 96  ASN n 
1 97  VAL n 
1 98  TRP n 
1 99  ILE n 
1 100 PRO n 
1 101 ALA n 
1 102 PRO n 
1 103 LYS n 
1 104 PRO n 
1 105 LYS n 
1 106 ASN n 
1 107 ALA n 
1 108 THR n 
1 109 VAL n 
1 110 LEU n 
1 111 ILE n 
1 112 TRP n 
1 113 ILE n 
1 114 TYR n 
1 115 GLY n 
1 116 GLY n 
1 117 GLY n 
1 118 PHE n 
1 119 GLN n 
1 120 THR n 
1 121 GLY n 
1 122 THR n 
1 123 SER n 
1 124 SER n 
1 125 LEU n 
1 126 HIS n 
1 127 VAL n 
1 128 TYR n 
1 129 ASP n 
1 130 GLY n 
1 131 LYS n 
1 132 PHE n 
1 133 LEU n 
1 134 ALA n 
1 135 ARG n 
1 136 VAL n 
1 137 GLU n 
1 138 ARG n 
1 139 VAL n 
1 140 ILE n 
1 141 VAL n 
1 142 VAL n 
1 143 SER n 
1 144 MET n 
1 145 ASN n 
1 146 TYR n 
1 147 ARG n 
1 148 VAL n 
1 149 GLY n 
1 150 ALA n 
1 151 LEU n 
1 152 GLY n 
1 153 PHE n 
1 154 LEU n 
1 155 ALA n 
1 156 LEU n 
1 157 PRO n 
1 158 GLY n 
1 159 ASN n 
1 160 PRO n 
1 161 GLU n 
1 162 ALA n 
1 163 PRO n 
1 164 GLY n 
1 165 ASN n 
1 166 MET n 
1 167 GLY n 
1 168 LEU n 
1 169 PHE n 
1 170 ASP n 
1 171 GLN n 
1 172 GLN n 
1 173 LEU n 
1 174 ALA n 
1 175 LEU n 
1 176 GLN n 
1 177 TRP n 
1 178 VAL n 
1 179 GLN n 
1 180 LYS n 
1 181 ASN n 
1 182 ILE n 
1 183 ALA n 
1 184 ALA n 
1 185 PHE n 
1 186 GLY n 
1 187 GLY n 
1 188 ASN n 
1 189 PRO n 
1 190 LYS n 
1 191 SER n 
1 192 VAL n 
1 193 THR n 
1 194 LEU n 
1 195 PHE n 
1 196 GLY n 
1 197 GLU n 
1 198 SER n 
1 199 ALA n 
1 200 GLY n 
1 201 ALA n 
1 202 ALA n 
1 203 SER n 
1 204 VAL n 
1 205 SER n 
1 206 LEU n 
1 207 HIS n 
1 208 LEU n 
1 209 LEU n 
1 210 SER n 
1 211 PRO n 
1 212 GLY n 
1 213 SER n 
1 214 HIS n 
1 215 SER n 
1 216 LEU n 
1 217 PHE n 
1 218 THR n 
1 219 ARG n 
1 220 ALA n 
1 221 ILE n 
1 222 LEU n 
1 223 GLN n 
1 224 SER n 
1 225 GLY n 
1 226 SER n 
1 227 PHE n 
1 228 ASN n 
1 229 ALA n 
1 230 PRO n 
1 231 TRP n 
1 232 ALA n 
1 233 VAL n 
1 234 THR n 
1 235 SER n 
1 236 LEU n 
1 237 TYR n 
1 238 GLU n 
1 239 ALA n 
1 240 ARG n 
1 241 ASN n 
1 242 ARG n 
1 243 THR n 
1 244 LEU n 
1 245 ASN n 
1 246 LEU n 
1 247 ALA n 
1 248 LYS n 
1 249 LEU n 
1 250 THR n 
1 251 GLY n 
1 252 CYS n 
1 253 SER n 
1 254 ARG n 
1 255 GLU n 
1 256 ASN n 
1 257 GLU n 
1 258 THR n 
1 259 GLU n 
1 260 ILE n 
1 261 ILE n 
1 262 LYS n 
1 263 CYS n 
1 264 LEU n 
1 265 ARG n 
1 266 ASN n 
1 267 LYS n 
1 268 ASP n 
1 269 PRO n 
1 270 GLN n 
1 271 GLU n 
1 272 ILE n 
1 273 LEU n 
1 274 LEU n 
1 275 ASN n 
1 276 GLU n 
1 277 ALA n 
1 278 PHE n 
1 279 VAL n 
1 280 VAL n 
1 281 PRO n 
1 282 TYR n 
1 283 GLY n 
1 284 THR n 
1 285 PRO n 
1 286 LEU n 
1 287 SER n 
1 288 VAL n 
1 289 ASN n 
1 290 PHE n 
1 291 GLY n 
1 292 PRO n 
1 293 THR n 
1 294 VAL n 
1 295 ASP n 
1 296 GLY n 
1 297 ASP n 
1 298 PHE n 
1 299 LEU n 
1 300 THR n 
1 301 ASP n 
1 302 MET n 
1 303 PRO n 
1 304 ASP n 
1 305 ILE n 
1 306 LEU n 
1 307 LEU n 
1 308 GLU n 
1 309 LEU n 
1 310 GLY n 
1 311 GLN n 
1 312 PHE n 
1 313 LYS n 
1 314 LYS n 
1 315 THR n 
1 316 GLN n 
1 317 ILE n 
1 318 LEU n 
1 319 VAL n 
1 320 GLY n 
1 321 VAL n 
1 322 ASN n 
1 323 LYS n 
1 324 ASP n 
1 325 GLU n 
1 326 GLY n 
1 327 THR n 
1 328 ALA n 
1 329 PHE n 
1 330 LEU n 
1 331 VAL n 
1 332 TYR n 
1 333 GLY n 
1 334 ALA n 
1 335 PRO n 
1 336 GLY n 
1 337 PHE n 
1 338 SER n 
1 339 LYS n 
1 340 ASP n 
1 341 ASN n 
1 342 ASN n 
1 343 SER n 
1 344 ILE n 
1 345 ILE n 
1 346 THR n 
1 347 ARG n 
1 348 LYS n 
1 349 GLU n 
1 350 PHE n 
1 351 GLN n 
1 352 GLU n 
1 353 GLY n 
1 354 LEU n 
1 355 LYS n 
1 356 ILE n 
1 357 PHE n 
1 358 PHE n 
1 359 PRO n 
1 360 GLY n 
1 361 VAL n 
1 362 SER n 
1 363 GLU n 
1 364 PHE n 
1 365 GLY n 
1 366 LYS n 
1 367 GLU n 
1 368 SER n 
1 369 ILE n 
1 370 LEU n 
1 371 PHE n 
1 372 HIS n 
1 373 TYR n 
1 374 THR n 
1 375 ASP n 
1 376 TRP n 
1 377 VAL n 
1 378 ASP n 
1 379 ASP n 
1 380 GLN n 
1 381 ARG n 
1 382 PRO n 
1 383 GLU n 
1 384 ASN n 
1 385 TYR n 
1 386 ARG n 
1 387 GLU n 
1 388 ALA n 
1 389 LEU n 
1 390 GLY n 
1 391 ASP n 
1 392 VAL n 
1 393 VAL n 
1 394 GLY n 
1 395 ASP n 
1 396 TYR n 
1 397 ASN n 
1 398 PHE n 
1 399 ILE n 
1 400 CYS n 
1 401 PRO n 
1 402 ALA n 
1 403 LEU n 
1 404 GLU n 
1 405 PHE n 
1 406 THR n 
1 407 LYS n 
1 408 LYS n 
1 409 PHE n 
1 410 SER n 
1 411 GLU n 
1 412 TRP n 
1 413 GLY n 
1 414 ASN n 
1 415 ASN n 
1 416 ALA n 
1 417 PHE n 
1 418 PHE n 
1 419 TYR n 
1 420 TYR n 
1 421 PHE n 
1 422 GLU n 
1 423 HIS n 
1 424 ARG n 
1 425 SER n 
1 426 SER n 
1 427 LYS n 
1 428 LEU n 
1 429 PRO n 
1 430 TRP n 
1 431 PRO n 
1 432 GLU n 
1 433 TRP n 
1 434 MET n 
1 435 GLY n 
1 436 VAL n 
1 437 MET n 
1 438 HIS n 
1 439 GLY n 
1 440 TYR n 
1 441 GLU n 
1 442 ILE n 
1 443 GLU n 
1 444 PHE n 
1 445 VAL n 
1 446 PHE n 
1 447 GLY n 
1 448 LEU n 
1 449 PRO n 
1 450 LEU n 
1 451 GLU n 
1 452 ARG n 
1 453 ARG n 
1 454 ASP n 
1 455 GLN n 
1 456 TYR n 
1 457 THR n 
1 458 LYS n 
1 459 ALA n 
1 460 GLU n 
1 461 GLU n 
1 462 ILE n 
1 463 LEU n 
1 464 SER n 
1 465 ARG n 
1 466 SER n 
1 467 ILE n 
1 468 VAL n 
1 469 LYS n 
1 470 ARG n 
1 471 TRP n 
1 472 ALA n 
1 473 ASN n 
1 474 PHE n 
1 475 ALA n 
1 476 LYS n 
1 477 TYR n 
1 478 GLY n 
1 479 ASN n 
1 480 PRO n 
1 481 GLN n 
1 482 GLU n 
1 483 THR n 
1 484 GLN n 
1 485 ASN n 
1 486 GLN n 
1 487 SER n 
1 488 THR n 
1 489 SER n 
1 490 TRP n 
1 491 PRO n 
1 492 VAL n 
1 493 PHE n 
1 494 LYS n 
1 495 SER n 
1 496 THR n 
1 497 GLU n 
1 498 GLN n 
1 499 LYS n 
1 500 TYR n 
1 501 LEU n 
1 502 THR n 
1 503 LEU n 
1 504 ASN n 
1 505 THR n 
1 506 GLU n 
1 507 SER n 
1 508 THR n 
1 509 ARG n 
1 510 ILE n 
1 511 MET n 
1 512 THR n 
1 513 LYS n 
1 514 LEU n 
1 515 ARG n 
1 516 ALA n 
1 517 GLN n 
1 518 GLN n 
1 519 CYS n 
1 520 ARG n 
1 521 PHE n 
1 522 TRP n 
1 523 THR n 
1 524 SER n 
1 525 PHE n 
1 526 PHE n 
1 527 PRO n 
1 528 LYS n 
1 529 VAL 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                   529 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'BCHE, CHE1' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Cricetulus griseus' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     10029 
_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_
_pdbx_entity_branch.entity_id 
_pdbx_entity_branch.type 
2 oligosaccharide 
3 oligosaccharide 
# 
loop_
_pdbx_entity_branch_descriptor.ordinal 
_pdbx_entity_branch_descriptor.entity_id 
_pdbx_entity_branch_descriptor.descriptor 
_pdbx_entity_branch_descriptor.type 
_pdbx_entity_branch_descriptor.program 
_pdbx_entity_branch_descriptor.program_version 
1 2 LFucpa1-6DGlcpNAcb1-                                                         'Glycam Condensed Sequence' GMML       1.0   
2 2 'WURCS=2.0/2,2,1/[a2122h-1b_1-5_2*NCC/3=O][a1221m-1a_1-5]/1-2/a6-b1'         WURCS                       PDB2Glycan 1.1.0 
3 2 '[]{[(4+1)][b-D-GlcpNAc]{[(6+1)][a-L-Fucp]{}}}'                              LINUCS                      PDB-CARE   ?     
4 3 'DGlcpNAcb1-4[LFucpa1-6]DGlcpNAcb1-'                                         'Glycam Condensed Sequence' GMML       1.0   
5 3 'WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1221m-1a_1-5]/1-1-2/a4-b1_a6-c1' WURCS                       PDB2Glycan 1.1.0 
6 3 '[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}[(6+1)][a-L-Fucp]{}}}'        LINUCS                      PDB-CARE   ?     
# 
loop_
_pdbx_entity_branch_link.link_id 
_pdbx_entity_branch_link.entity_id 
_pdbx_entity_branch_link.entity_branch_list_num_1 
_pdbx_entity_branch_link.comp_id_1 
_pdbx_entity_branch_link.atom_id_1 
_pdbx_entity_branch_link.leaving_atom_id_1 
_pdbx_entity_branch_link.entity_branch_list_num_2 
_pdbx_entity_branch_link.comp_id_2 
_pdbx_entity_branch_link.atom_id_2 
_pdbx_entity_branch_link.leaving_atom_id_2 
_pdbx_entity_branch_link.value_order 
_pdbx_entity_branch_link.details 
1 2 2 FUC C1 O1 1 NAG O6 HO6 sing ? 
2 3 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
3 3 3 FUC C1 O1 1 NAG O6 HO6 sing ? 
# 
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 
A1H77 non-polymer                   . '(2~{R},3~{S})-1-(cyclopropylmethylamino)-3-(9~{H}-fluoren-9-ylamino)-4-phenyl-butan-2-ol' ? 
'C27 H30 N2 O'   398.540 
ALA   'L-peptide linking'           y ALANINE                                                                                    ? 
'C3 H7 N O2'     89.093  
ARG   'L-peptide linking'           y ARGININE                                                                                   ? 
'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking'           y ASPARAGINE                                                                                 ? 
'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking'           y 'ASPARTIC ACID'                                                                            ? 
'C4 H7 N O4'     133.103 
CYS   'L-peptide linking'           y CYSTEINE                                                                                   ? 
'C3 H7 N O2 S'   121.158 
FUC   'L-saccharide, alpha linking' . alpha-L-fucopyranose                                                                       
'alpha-L-fucose; 6-deoxy-alpha-L-galactopyranose; L-fucose; fucose' 'C6 H12 O5'      164.156 
GLN   'L-peptide linking'           y GLUTAMINE                                                                                  ? 
'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking'           y 'GLUTAMIC ACID'                                                                            ? 
'C5 H9 N O4'     147.129 
GLY   'peptide linking'             y GLYCINE                                                                                    ? 
'C2 H5 N O2'     75.067  
GOL   non-polymer                   . GLYCEROL                                                                                   
'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
HIS   'L-peptide linking'           y HISTIDINE                                                                                  ? 
'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer                   . WATER                                                                                      ? 
'H2 O'           18.015  
ILE   'L-peptide linking'           y ISOLEUCINE                                                                                 ? 
'C6 H13 N O2'    131.173 
LEU   'L-peptide linking'           y LEUCINE                                                                                    ? 
'C6 H13 N O2'    131.173 
LYS   'L-peptide linking'           y LYSINE                                                                                     ? 
'C6 H15 N2 O2 1' 147.195 
MES   non-polymer                   . '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                                                     ? 
'C6 H13 N O4 S'  195.237 
MET   'L-peptide linking'           y METHIONINE                                                                                 ? 
'C5 H11 N O2 S'  149.211 
NAG   'D-saccharide, beta linking'  . 2-acetamido-2-deoxy-beta-D-glucopyranose                                                   
;N-acetyl-beta-D-glucosamine; 2-acetamido-2-deoxy-beta-D-glucose; 2-acetamido-2-deoxy-D-glucose; 2-acetamido-2-deoxy-glucose; N-ACETYL-D-GLUCOSAMINE
;
'C8 H15 N O6'    221.208 
PHE   'L-peptide linking'           y PHENYLALANINE                                                                              ? 
'C9 H11 N O2'    165.189 
PRO   'L-peptide linking'           y PROLINE                                                                                    ? 
'C5 H9 N O2'     115.130 
SER   'L-peptide linking'           y SERINE                                                                                     ? 
'C3 H7 N O3'     105.093 
SIA   'D-saccharide, alpha linking' . 'N-acetyl-alpha-neuraminic acid'                                                           
'N-acetylneuraminic acid; sialic acid; alpha-sialic acid; O-SIALIC ACID' 'C11 H19 N O9'   309.270 
SO4   non-polymer                   . 'SULFATE ION'                                                                              ? 
'O4 S -2'        96.063  
THR   'L-peptide linking'           y THREONINE                                                                                  ? 
'C4 H9 N O3'     119.119 
TRP   'L-peptide linking'           y TRYPTOPHAN                                                                                 ? 
'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking'           y TYROSINE                                                                                   ? 
'C9 H11 N O3'    181.189 
VAL   'L-peptide linking'           y VALINE                                                                                     ? 
'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
FUC 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 LFucpa                         
FUC 'COMMON NAME'                         GMML     1.0 a-L-fucopyranose               
FUC 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 a-L-Fucp                       
FUC 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Fuc                            
NAG 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpNAcb                      
NAG 'COMMON NAME'                         GMML     1.0 N-acetyl-b-D-glucopyranosamine 
NAG 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-GlcpNAc                    
NAG 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 GlcNAc                         
SIA 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DNeup5Aca                      
SIA 'COMMON NAME'                         GMML     1.0 'N-acetyl-a-D-neuraminic acid' 
SIA 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 a-D-Neup5Ac                    
SIA 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Neu5Ac                         
# 
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   GLU 1   1   ?   ?   ?   A . n 
A 1 2   ASP 2   2   ?   ?   ?   A . n 
A 1 3   ASP 3   3   ?   ?   ?   A . n 
A 1 4   ILE 4   4   4   ILE ILE A . n 
A 1 5   ILE 5   5   5   ILE ILE A . n 
A 1 6   ILE 6   6   6   ILE ILE A . n 
A 1 7   ALA 7   7   7   ALA ALA A . n 
A 1 8   THR 8   8   8   THR THR A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  ASN 10  10  10  ASN ASN A . n 
A 1 11  GLY 11  11  11  GLY GLY A . n 
A 1 12  LYS 12  12  12  LYS LYS A . n 
A 1 13  VAL 13  13  13  VAL VAL A . n 
A 1 14  ARG 14  14  14  ARG ARG A . n 
A 1 15  GLY 15  15  15  GLY GLY A . n 
A 1 16  MET 16  16  16  MET MET A . n 
A 1 17  GLN 17  17  17  GLN GLN A . n 
A 1 18  LEU 18  18  18  LEU LEU A . n 
A 1 19  THR 19  19  19  THR THR A . n 
A 1 20  VAL 20  20  20  VAL VAL A . n 
A 1 21  PHE 21  21  21  PHE PHE A . n 
A 1 22  GLY 22  22  22  GLY GLY A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  THR 24  24  24  THR THR A . n 
A 1 25  VAL 25  25  25  VAL VAL A . n 
A 1 26  THR 26  26  26  THR THR A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  PHE 28  28  28  PHE PHE A . n 
A 1 29  LEU 29  29  29  LEU LEU A . n 
A 1 30  GLY 30  30  30  GLY GLY A . n 
A 1 31  ILE 31  31  31  ILE ILE A . n 
A 1 32  PRO 32  32  32  PRO PRO A . n 
A 1 33  TYR 33  33  33  TYR TYR A . n 
A 1 34  ALA 34  34  34  ALA ALA A . n 
A 1 35  GLN 35  35  35  GLN GLN A . n 
A 1 36  PRO 36  36  36  PRO PRO A . n 
A 1 37  PRO 37  37  37  PRO PRO A . n 
A 1 38  LEU 38  38  38  LEU LEU A . n 
A 1 39  GLY 39  39  39  GLY GLY A . n 
A 1 40  ARG 40  40  40  ARG ARG A . n 
A 1 41  LEU 41  41  41  LEU LEU A . n 
A 1 42  ARG 42  42  42  ARG ARG A . n 
A 1 43  PHE 43  43  43  PHE PHE A . n 
A 1 44  LYS 44  44  44  LYS LYS A . n 
A 1 45  LYS 45  45  45  LYS LYS A . n 
A 1 46  PRO 46  46  46  PRO PRO A . n 
A 1 47  GLN 47  47  47  GLN GLN A . n 
A 1 48  SER 48  48  48  SER SER 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  LYS 51  51  51  LYS LYS A . n 
A 1 52  TRP 52  52  52  TRP TRP A . n 
A 1 53  SER 53  53  53  SER SER A . n 
A 1 54  ASP 54  54  54  ASP ASP A . n 
A 1 55  ILE 55  55  55  ILE ILE A . n 
A 1 56  TRP 56  56  56  TRP TRP A . n 
A 1 57  ASN 57  57  57  ASN ASN A . n 
A 1 58  ALA 58  58  58  ALA ALA A . n 
A 1 59  THR 59  59  59  THR THR A . n 
A 1 60  LYS 60  60  60  LYS LYS A . n 
A 1 61  TYR 61  61  61  TYR TYR A . n 
A 1 62  ALA 62  62  62  ALA ALA A . n 
A 1 63  ASN 63  63  63  ASN ASN A . n 
A 1 64  SER 64  64  64  SER SER A . n 
A 1 65  CYS 65  65  65  CYS CYS A . n 
A 1 66  CYS 66  66  66  CYS CYS A . n 
A 1 67  GLN 67  67  67  GLN GLN A . n 
A 1 68  ASN 68  68  68  ASN ASN A . n 
A 1 69  ILE 69  69  69  ILE ILE A . n 
A 1 70  ASP 70  70  70  ASP ASP A . n 
A 1 71  GLN 71  71  71  GLN GLN A . n 
A 1 72  SER 72  72  72  SER SER A . n 
A 1 73  PHE 73  73  73  PHE PHE A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  GLY 75  75  75  GLY GLY A . n 
A 1 76  PHE 76  76  76  PHE PHE A . n 
A 1 77  HIS 77  77  77  HIS HIS A . n 
A 1 78  GLY 78  78  78  GLY GLY A . n 
A 1 79  SER 79  79  79  SER SER A . n 
A 1 80  GLU 80  80  80  GLU GLU A . n 
A 1 81  MET 81  81  81  MET MET A . n 
A 1 82  TRP 82  82  82  TRP TRP A . n 
A 1 83  ASN 83  83  83  ASN ASN A . n 
A 1 84  PRO 84  84  84  PRO PRO A . n 
A 1 85  ASN 85  85  85  ASN ASN A . n 
A 1 86  THR 86  86  86  THR THR A . n 
A 1 87  ASP 87  87  87  ASP ASP A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  SER 89  89  89  SER SER A . n 
A 1 90  GLU 90  90  90  GLU GLU A . n 
A 1 91  ASP 91  91  91  ASP ASP A . n 
A 1 92  CYS 92  92  92  CYS CYS A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  TYR 94  94  94  TYR TYR A . n 
A 1 95  LEU 95  95  95  LEU LEU A . n 
A 1 96  ASN 96  96  96  ASN ASN A . n 
A 1 97  VAL 97  97  97  VAL VAL A . n 
A 1 98  TRP 98  98  98  TRP TRP A . n 
A 1 99  ILE 99  99  99  ILE ILE A . n 
A 1 100 PRO 100 100 100 PRO PRO A . n 
A 1 101 ALA 101 101 101 ALA ALA A . n 
A 1 102 PRO 102 102 102 PRO PRO A . n 
A 1 103 LYS 103 103 103 LYS LYS A . n 
A 1 104 PRO 104 104 104 PRO PRO A . n 
A 1 105 LYS 105 105 105 LYS LYS A . n 
A 1 106 ASN 106 106 106 ASN ASN A . n 
A 1 107 ALA 107 107 107 ALA ALA A . n 
A 1 108 THR 108 108 108 THR THR A . n 
A 1 109 VAL 109 109 109 VAL VAL A . n 
A 1 110 LEU 110 110 110 LEU LEU A . n 
A 1 111 ILE 111 111 111 ILE ILE A . n 
A 1 112 TRP 112 112 112 TRP TRP A . n 
A 1 113 ILE 113 113 113 ILE ILE A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 GLY 115 115 115 GLY GLY A . n 
A 1 116 GLY 116 116 116 GLY GLY A . n 
A 1 117 GLY 117 117 117 GLY GLY A . n 
A 1 118 PHE 118 118 118 PHE PHE A . n 
A 1 119 GLN 119 119 119 GLN GLN A . n 
A 1 120 THR 120 120 120 THR THR A . n 
A 1 121 GLY 121 121 121 GLY GLY A . n 
A 1 122 THR 122 122 122 THR THR A . n 
A 1 123 SER 123 123 123 SER SER A . n 
A 1 124 SER 124 124 124 SER SER A . n 
A 1 125 LEU 125 125 125 LEU LEU A . n 
A 1 126 HIS 126 126 126 HIS HIS A . n 
A 1 127 VAL 127 127 127 VAL VAL A . n 
A 1 128 TYR 128 128 128 TYR TYR A . n 
A 1 129 ASP 129 129 129 ASP ASP A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 LYS 131 131 131 LYS LYS A . n 
A 1 132 PHE 132 132 132 PHE PHE A . n 
A 1 133 LEU 133 133 133 LEU LEU A . n 
A 1 134 ALA 134 134 134 ALA ALA A . n 
A 1 135 ARG 135 135 135 ARG ARG A . n 
A 1 136 VAL 136 136 136 VAL VAL A . n 
A 1 137 GLU 137 137 137 GLU GLU A . n 
A 1 138 ARG 138 138 138 ARG ARG A . n 
A 1 139 VAL 139 139 139 VAL VAL A . n 
A 1 140 ILE 140 140 140 ILE ILE A . n 
A 1 141 VAL 141 141 141 VAL VAL A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 SER 143 143 143 SER SER A . n 
A 1 144 MET 144 144 144 MET MET A . n 
A 1 145 ASN 145 145 145 ASN ASN A . n 
A 1 146 TYR 146 146 146 TYR TYR A . n 
A 1 147 ARG 147 147 147 ARG ARG A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 GLY 149 149 149 GLY GLY A . n 
A 1 150 ALA 150 150 150 ALA ALA A . n 
A 1 151 LEU 151 151 151 LEU LEU A . n 
A 1 152 GLY 152 152 152 GLY GLY A . n 
A 1 153 PHE 153 153 153 PHE PHE A . n 
A 1 154 LEU 154 154 154 LEU LEU A . n 
A 1 155 ALA 155 155 155 ALA ALA A . n 
A 1 156 LEU 156 156 156 LEU LEU A . n 
A 1 157 PRO 157 157 157 PRO PRO A . n 
A 1 158 GLY 158 158 158 GLY GLY A . n 
A 1 159 ASN 159 159 159 ASN ASN A . n 
A 1 160 PRO 160 160 160 PRO PRO A . n 
A 1 161 GLU 161 161 161 GLU GLU A . n 
A 1 162 ALA 162 162 162 ALA ALA A . n 
A 1 163 PRO 163 163 163 PRO PRO A . n 
A 1 164 GLY 164 164 164 GLY GLY A . n 
A 1 165 ASN 165 165 165 ASN ASN A . n 
A 1 166 MET 166 166 166 MET MET A . n 
A 1 167 GLY 167 167 167 GLY GLY A . n 
A 1 168 LEU 168 168 168 LEU LEU A . n 
A 1 169 PHE 169 169 169 PHE PHE A . n 
A 1 170 ASP 170 170 170 ASP ASP A . n 
A 1 171 GLN 171 171 171 GLN GLN A . n 
A 1 172 GLN 172 172 172 GLN GLN A . n 
A 1 173 LEU 173 173 173 LEU LEU A . n 
A 1 174 ALA 174 174 174 ALA ALA A . n 
A 1 175 LEU 175 175 175 LEU LEU A . n 
A 1 176 GLN 176 176 176 GLN GLN A . n 
A 1 177 TRP 177 177 177 TRP TRP A . n 
A 1 178 VAL 178 178 178 VAL VAL A . n 
A 1 179 GLN 179 179 179 GLN GLN A . n 
A 1 180 LYS 180 180 180 LYS LYS A . n 
A 1 181 ASN 181 181 181 ASN ASN A . n 
A 1 182 ILE 182 182 182 ILE ILE A . n 
A 1 183 ALA 183 183 183 ALA ALA A . n 
A 1 184 ALA 184 184 184 ALA ALA A . n 
A 1 185 PHE 185 185 185 PHE PHE A . n 
A 1 186 GLY 186 186 186 GLY GLY A . n 
A 1 187 GLY 187 187 187 GLY GLY A . n 
A 1 188 ASN 188 188 188 ASN ASN A . n 
A 1 189 PRO 189 189 189 PRO PRO A . n 
A 1 190 LYS 190 190 190 LYS LYS A . n 
A 1 191 SER 191 191 191 SER SER A . n 
A 1 192 VAL 192 192 192 VAL VAL A . n 
A 1 193 THR 193 193 193 THR THR A . n 
A 1 194 LEU 194 194 194 LEU LEU A . n 
A 1 195 PHE 195 195 195 PHE PHE A . n 
A 1 196 GLY 196 196 196 GLY GLY A . n 
A 1 197 GLU 197 197 197 GLU GLU A . n 
A 1 198 SER 198 198 198 SER SER A . n 
A 1 199 ALA 199 199 199 ALA ALA A . n 
A 1 200 GLY 200 200 200 GLY GLY A . n 
A 1 201 ALA 201 201 201 ALA ALA A . n 
A 1 202 ALA 202 202 202 ALA ALA A . n 
A 1 203 SER 203 203 203 SER SER A . n 
A 1 204 VAL 204 204 204 VAL VAL A . n 
A 1 205 SER 205 205 205 SER SER A . n 
A 1 206 LEU 206 206 206 LEU LEU A . n 
A 1 207 HIS 207 207 207 HIS HIS A . n 
A 1 208 LEU 208 208 208 LEU LEU A . n 
A 1 209 LEU 209 209 209 LEU LEU A . n 
A 1 210 SER 210 210 210 SER SER A . n 
A 1 211 PRO 211 211 211 PRO PRO A . n 
A 1 212 GLY 212 212 212 GLY GLY A . n 
A 1 213 SER 213 213 213 SER SER A . n 
A 1 214 HIS 214 214 214 HIS HIS A . n 
A 1 215 SER 215 215 215 SER SER A . n 
A 1 216 LEU 216 216 216 LEU LEU A . n 
A 1 217 PHE 217 217 217 PHE PHE A . n 
A 1 218 THR 218 218 218 THR THR A . n 
A 1 219 ARG 219 219 219 ARG ARG A . n 
A 1 220 ALA 220 220 220 ALA ALA A . n 
A 1 221 ILE 221 221 221 ILE ILE A . n 
A 1 222 LEU 222 222 222 LEU LEU A . n 
A 1 223 GLN 223 223 223 GLN GLN A . n 
A 1 224 SER 224 224 224 SER SER A . n 
A 1 225 GLY 225 225 225 GLY GLY A . n 
A 1 226 SER 226 226 226 SER SER A . n 
A 1 227 PHE 227 227 227 PHE PHE A . n 
A 1 228 ASN 228 228 228 ASN ASN A . n 
A 1 229 ALA 229 229 229 ALA ALA A . n 
A 1 230 PRO 230 230 230 PRO PRO A . n 
A 1 231 TRP 231 231 231 TRP TRP A . n 
A 1 232 ALA 232 232 232 ALA ALA A . n 
A 1 233 VAL 233 233 233 VAL VAL A . n 
A 1 234 THR 234 234 234 THR THR A . n 
A 1 235 SER 235 235 235 SER SER A . n 
A 1 236 LEU 236 236 236 LEU LEU A . n 
A 1 237 TYR 237 237 237 TYR TYR A . n 
A 1 238 GLU 238 238 238 GLU GLU A . n 
A 1 239 ALA 239 239 239 ALA ALA A . n 
A 1 240 ARG 240 240 240 ARG ARG A . n 
A 1 241 ASN 241 241 241 ASN ASN A . n 
A 1 242 ARG 242 242 242 ARG ARG A . n 
A 1 243 THR 243 243 243 THR THR A . n 
A 1 244 LEU 244 244 244 LEU LEU A . n 
A 1 245 ASN 245 245 245 ASN ASN A . n 
A 1 246 LEU 246 246 246 LEU LEU A . n 
A 1 247 ALA 247 247 247 ALA ALA A . n 
A 1 248 LYS 248 248 248 LYS LYS A . n 
A 1 249 LEU 249 249 249 LEU LEU A . n 
A 1 250 THR 250 250 250 THR THR A . n 
A 1 251 GLY 251 251 251 GLY GLY A . n 
A 1 252 CYS 252 252 252 CYS CYS A . n 
A 1 253 SER 253 253 253 SER SER A . n 
A 1 254 ARG 254 254 254 ARG ARG A . n 
A 1 255 GLU 255 255 255 GLU GLU A . n 
A 1 256 ASN 256 256 256 ASN ASN A . n 
A 1 257 GLU 257 257 257 GLU GLU A . n 
A 1 258 THR 258 258 258 THR THR A . n 
A 1 259 GLU 259 259 259 GLU GLU A . n 
A 1 260 ILE 260 260 260 ILE ILE A . n 
A 1 261 ILE 261 261 261 ILE ILE A . n 
A 1 262 LYS 262 262 262 LYS LYS A . n 
A 1 263 CYS 263 263 263 CYS CYS A . n 
A 1 264 LEU 264 264 264 LEU LEU A . n 
A 1 265 ARG 265 265 265 ARG ARG A . n 
A 1 266 ASN 266 266 266 ASN ASN A . n 
A 1 267 LYS 267 267 267 LYS LYS A . n 
A 1 268 ASP 268 268 268 ASP ASP A . n 
A 1 269 PRO 269 269 269 PRO PRO A . n 
A 1 270 GLN 270 270 270 GLN GLN A . n 
A 1 271 GLU 271 271 271 GLU GLU A . n 
A 1 272 ILE 272 272 272 ILE ILE A . n 
A 1 273 LEU 273 273 273 LEU LEU A . n 
A 1 274 LEU 274 274 274 LEU LEU A . n 
A 1 275 ASN 275 275 275 ASN ASN A . n 
A 1 276 GLU 276 276 276 GLU GLU A . n 
A 1 277 ALA 277 277 277 ALA ALA A . n 
A 1 278 PHE 278 278 278 PHE PHE A . n 
A 1 279 VAL 279 279 279 VAL VAL A . n 
A 1 280 VAL 280 280 280 VAL VAL A . n 
A 1 281 PRO 281 281 281 PRO PRO A . n 
A 1 282 TYR 282 282 282 TYR TYR A . n 
A 1 283 GLY 283 283 283 GLY GLY A . n 
A 1 284 THR 284 284 284 THR THR A . n 
A 1 285 PRO 285 285 285 PRO PRO A . n 
A 1 286 LEU 286 286 286 LEU LEU A . n 
A 1 287 SER 287 287 287 SER SER A . n 
A 1 288 VAL 288 288 288 VAL VAL A . n 
A 1 289 ASN 289 289 289 ASN ASN A . n 
A 1 290 PHE 290 290 290 PHE PHE A . n 
A 1 291 GLY 291 291 291 GLY GLY A . n 
A 1 292 PRO 292 292 292 PRO PRO A . n 
A 1 293 THR 293 293 293 THR THR A . n 
A 1 294 VAL 294 294 294 VAL VAL A . n 
A 1 295 ASP 295 295 295 ASP ASP A . n 
A 1 296 GLY 296 296 296 GLY GLY A . n 
A 1 297 ASP 297 297 297 ASP ASP A . n 
A 1 298 PHE 298 298 298 PHE PHE A . n 
A 1 299 LEU 299 299 299 LEU LEU A . n 
A 1 300 THR 300 300 300 THR THR A . n 
A 1 301 ASP 301 301 301 ASP ASP A . n 
A 1 302 MET 302 302 302 MET MET A . n 
A 1 303 PRO 303 303 303 PRO PRO A . n 
A 1 304 ASP 304 304 304 ASP ASP A . n 
A 1 305 ILE 305 305 305 ILE ILE A . n 
A 1 306 LEU 306 306 306 LEU LEU A . n 
A 1 307 LEU 307 307 307 LEU LEU A . n 
A 1 308 GLU 308 308 308 GLU GLU A . n 
A 1 309 LEU 309 309 309 LEU LEU A . n 
A 1 310 GLY 310 310 310 GLY GLY A . n 
A 1 311 GLN 311 311 311 GLN GLN A . n 
A 1 312 PHE 312 312 312 PHE PHE A . n 
A 1 313 LYS 313 313 313 LYS LYS A . n 
A 1 314 LYS 314 314 314 LYS LYS A . n 
A 1 315 THR 315 315 315 THR THR A . n 
A 1 316 GLN 316 316 316 GLN GLN A . n 
A 1 317 ILE 317 317 317 ILE ILE A . n 
A 1 318 LEU 318 318 318 LEU LEU A . n 
A 1 319 VAL 319 319 319 VAL VAL A . n 
A 1 320 GLY 320 320 320 GLY GLY A . n 
A 1 321 VAL 321 321 321 VAL VAL A . n 
A 1 322 ASN 322 322 322 ASN ASN A . n 
A 1 323 LYS 323 323 323 LYS LYS A . n 
A 1 324 ASP 324 324 324 ASP ASP A . n 
A 1 325 GLU 325 325 325 GLU GLU A . n 
A 1 326 GLY 326 326 326 GLY GLY A . n 
A 1 327 THR 327 327 327 THR THR A . n 
A 1 328 ALA 328 328 328 ALA ALA A . n 
A 1 329 PHE 329 329 329 PHE PHE A . n 
A 1 330 LEU 330 330 330 LEU LEU A . n 
A 1 331 VAL 331 331 331 VAL VAL A . n 
A 1 332 TYR 332 332 332 TYR TYR A . n 
A 1 333 GLY 333 333 333 GLY GLY A . n 
A 1 334 ALA 334 334 334 ALA ALA A . n 
A 1 335 PRO 335 335 335 PRO PRO A . n 
A 1 336 GLY 336 336 336 GLY GLY A . n 
A 1 337 PHE 337 337 337 PHE PHE A . n 
A 1 338 SER 338 338 338 SER SER A . n 
A 1 339 LYS 339 339 339 LYS LYS A . n 
A 1 340 ASP 340 340 340 ASP ASP A . n 
A 1 341 ASN 341 341 341 ASN ASN A . n 
A 1 342 ASN 342 342 342 ASN ASN A . n 
A 1 343 SER 343 343 343 SER SER A . n 
A 1 344 ILE 344 344 344 ILE ILE A . n 
A 1 345 ILE 345 345 345 ILE ILE A . n 
A 1 346 THR 346 346 346 THR THR A . n 
A 1 347 ARG 347 347 347 ARG ARG A . n 
A 1 348 LYS 348 348 348 LYS LYS A . n 
A 1 349 GLU 349 349 349 GLU GLU A . n 
A 1 350 PHE 350 350 350 PHE PHE A . n 
A 1 351 GLN 351 351 351 GLN GLN A . n 
A 1 352 GLU 352 352 352 GLU GLU A . n 
A 1 353 GLY 353 353 353 GLY GLY A . n 
A 1 354 LEU 354 354 354 LEU LEU A . n 
A 1 355 LYS 355 355 355 LYS LYS A . n 
A 1 356 ILE 356 356 356 ILE ILE A . n 
A 1 357 PHE 357 357 357 PHE PHE A . n 
A 1 358 PHE 358 358 358 PHE PHE A . n 
A 1 359 PRO 359 359 359 PRO PRO A . n 
A 1 360 GLY 360 360 360 GLY GLY A . n 
A 1 361 VAL 361 361 361 VAL VAL A . n 
A 1 362 SER 362 362 362 SER SER A . n 
A 1 363 GLU 363 363 363 GLU GLU A . n 
A 1 364 PHE 364 364 364 PHE PHE A . n 
A 1 365 GLY 365 365 365 GLY GLY A . n 
A 1 366 LYS 366 366 366 LYS LYS A . n 
A 1 367 GLU 367 367 367 GLU GLU A . n 
A 1 368 SER 368 368 368 SER SER A . n 
A 1 369 ILE 369 369 369 ILE ILE A . n 
A 1 370 LEU 370 370 370 LEU LEU A . n 
A 1 371 PHE 371 371 371 PHE PHE A . n 
A 1 372 HIS 372 372 372 HIS HIS A . n 
A 1 373 TYR 373 373 373 TYR TYR A . n 
A 1 374 THR 374 374 374 THR THR A . n 
A 1 375 ASP 375 375 375 ASP ASP A . n 
A 1 376 TRP 376 376 376 TRP TRP A . n 
A 1 377 VAL 377 377 377 VAL VAL A . n 
A 1 378 ASP 378 378 378 ASP ASP A . n 
A 1 379 ASP 379 379 379 ASP ASP A . n 
A 1 380 GLN 380 380 380 GLN GLN A . n 
A 1 381 ARG 381 381 381 ARG ARG A . n 
A 1 382 PRO 382 382 382 PRO PRO A . n 
A 1 383 GLU 383 383 383 GLU GLU A . n 
A 1 384 ASN 384 384 384 ASN ASN A . n 
A 1 385 TYR 385 385 385 TYR TYR A . n 
A 1 386 ARG 386 386 386 ARG ARG A . n 
A 1 387 GLU 387 387 387 GLU GLU A . n 
A 1 388 ALA 388 388 388 ALA ALA A . n 
A 1 389 LEU 389 389 389 LEU LEU A . n 
A 1 390 GLY 390 390 390 GLY GLY A . n 
A 1 391 ASP 391 391 391 ASP ASP A . n 
A 1 392 VAL 392 392 392 VAL VAL A . n 
A 1 393 VAL 393 393 393 VAL VAL A . n 
A 1 394 GLY 394 394 394 GLY GLY A . n 
A 1 395 ASP 395 395 395 ASP ASP A . n 
A 1 396 TYR 396 396 396 TYR TYR A . n 
A 1 397 ASN 397 397 397 ASN ASN A . n 
A 1 398 PHE 398 398 398 PHE PHE A . n 
A 1 399 ILE 399 399 399 ILE ILE A . n 
A 1 400 CYS 400 400 400 CYS CYS A . n 
A 1 401 PRO 401 401 401 PRO PRO A . n 
A 1 402 ALA 402 402 402 ALA ALA A . n 
A 1 403 LEU 403 403 403 LEU LEU A . n 
A 1 404 GLU 404 404 404 GLU GLU A . n 
A 1 405 PHE 405 405 405 PHE PHE A . n 
A 1 406 THR 406 406 406 THR THR A . n 
A 1 407 LYS 407 407 407 LYS LYS A . n 
A 1 408 LYS 408 408 408 LYS LYS A . n 
A 1 409 PHE 409 409 409 PHE PHE A . n 
A 1 410 SER 410 410 410 SER SER A . n 
A 1 411 GLU 411 411 411 GLU GLU A . n 
A 1 412 TRP 412 412 412 TRP TRP A . n 
A 1 413 GLY 413 413 413 GLY GLY A . n 
A 1 414 ASN 414 414 414 ASN ASN A . n 
A 1 415 ASN 415 415 415 ASN ASN A . n 
A 1 416 ALA 416 416 416 ALA ALA A . n 
A 1 417 PHE 417 417 417 PHE PHE A . n 
A 1 418 PHE 418 418 418 PHE PHE A . n 
A 1 419 TYR 419 419 419 TYR TYR A . n 
A 1 420 TYR 420 420 420 TYR TYR A . n 
A 1 421 PHE 421 421 421 PHE PHE A . n 
A 1 422 GLU 422 422 422 GLU GLU A . n 
A 1 423 HIS 423 423 423 HIS HIS A . n 
A 1 424 ARG 424 424 424 ARG ARG A . n 
A 1 425 SER 425 425 425 SER SER A . n 
A 1 426 SER 426 426 426 SER SER A . n 
A 1 427 LYS 427 427 427 LYS LYS A . n 
A 1 428 LEU 428 428 428 LEU LEU A . n 
A 1 429 PRO 429 429 429 PRO PRO A . n 
A 1 430 TRP 430 430 430 TRP TRP A . n 
A 1 431 PRO 431 431 431 PRO PRO A . n 
A 1 432 GLU 432 432 432 GLU GLU A . n 
A 1 433 TRP 433 433 433 TRP TRP A . n 
A 1 434 MET 434 434 434 MET MET A . n 
A 1 435 GLY 435 435 435 GLY GLY A . n 
A 1 436 VAL 436 436 436 VAL VAL A . n 
A 1 437 MET 437 437 437 MET MET A . n 
A 1 438 HIS 438 438 438 HIS HIS A . n 
A 1 439 GLY 439 439 439 GLY GLY A . n 
A 1 440 TYR 440 440 440 TYR TYR A . n 
A 1 441 GLU 441 441 441 GLU GLU A . n 
A 1 442 ILE 442 442 442 ILE ILE A . n 
A 1 443 GLU 443 443 443 GLU GLU A . n 
A 1 444 PHE 444 444 444 PHE PHE A . n 
A 1 445 VAL 445 445 445 VAL VAL A . n 
A 1 446 PHE 446 446 446 PHE PHE A . n 
A 1 447 GLY 447 447 447 GLY GLY A . n 
A 1 448 LEU 448 448 448 LEU LEU A . n 
A 1 449 PRO 449 449 449 PRO PRO A . n 
A 1 450 LEU 450 450 450 LEU LEU A . n 
A 1 451 GLU 451 451 451 GLU GLU A . n 
A 1 452 ARG 452 452 452 ARG ARG A . n 
A 1 453 ARG 453 453 453 ARG ARG A . n 
A 1 454 ASP 454 454 454 ASP ASP A . n 
A 1 455 GLN 455 455 455 GLN GLN A . n 
A 1 456 TYR 456 456 456 TYR TYR A . n 
A 1 457 THR 457 457 457 THR THR A . n 
A 1 458 LYS 458 458 458 LYS LYS A . n 
A 1 459 ALA 459 459 459 ALA ALA A . n 
A 1 460 GLU 460 460 460 GLU GLU A . n 
A 1 461 GLU 461 461 461 GLU GLU A . n 
A 1 462 ILE 462 462 462 ILE ILE A . n 
A 1 463 LEU 463 463 463 LEU LEU A . n 
A 1 464 SER 464 464 464 SER SER A . n 
A 1 465 ARG 465 465 465 ARG ARG A . n 
A 1 466 SER 466 466 466 SER SER A . n 
A 1 467 ILE 467 467 467 ILE ILE A . n 
A 1 468 VAL 468 468 468 VAL VAL A . n 
A 1 469 LYS 469 469 469 LYS LYS A . n 
A 1 470 ARG 470 470 470 ARG ARG A . n 
A 1 471 TRP 471 471 471 TRP TRP A . n 
A 1 472 ALA 472 472 472 ALA ALA A . n 
A 1 473 ASN 473 473 473 ASN ASN A . n 
A 1 474 PHE 474 474 474 PHE PHE A . n 
A 1 475 ALA 475 475 475 ALA ALA A . n 
A 1 476 LYS 476 476 476 LYS LYS A . n 
A 1 477 TYR 477 477 477 TYR TYR A . n 
A 1 478 GLY 478 478 478 GLY GLY A . n 
A 1 479 ASN 479 479 479 ASN ASN A . n 
A 1 480 PRO 480 480 480 PRO PRO A . n 
A 1 481 GLN 481 481 481 GLN GLN A . n 
A 1 482 GLU 482 482 482 GLU GLU A . n 
A 1 483 THR 483 483 483 THR THR A . n 
A 1 484 GLN 484 484 484 GLN GLN A . n 
A 1 485 ASN 485 485 485 ASN ASN A . n 
A 1 486 GLN 486 486 486 GLN GLN A . n 
A 1 487 SER 487 487 487 SER SER A . n 
A 1 488 THR 488 488 488 THR THR A . n 
A 1 489 SER 489 489 489 SER SER A . n 
A 1 490 TRP 490 490 490 TRP TRP A . n 
A 1 491 PRO 491 491 491 PRO PRO A . n 
A 1 492 VAL 492 492 492 VAL VAL A . n 
A 1 493 PHE 493 493 493 PHE PHE A . n 
A 1 494 LYS 494 494 494 LYS LYS A . n 
A 1 495 SER 495 495 495 SER SER A . n 
A 1 496 THR 496 496 496 THR THR A . n 
A 1 497 GLU 497 497 497 GLU GLU A . n 
A 1 498 GLN 498 498 498 GLN GLN A . n 
A 1 499 LYS 499 499 499 LYS LYS A . n 
A 1 500 TYR 500 500 500 TYR TYR A . n 
A 1 501 LEU 501 501 501 LEU LEU A . n 
A 1 502 THR 502 502 502 THR THR A . n 
A 1 503 LEU 503 503 503 LEU LEU A . n 
A 1 504 ASN 504 504 504 ASN ASN A . n 
A 1 505 THR 505 505 505 THR THR A . n 
A 1 506 GLU 506 506 506 GLU GLU A . n 
A 1 507 SER 507 507 507 SER SER A . n 
A 1 508 THR 508 508 508 THR THR A . n 
A 1 509 ARG 509 509 509 ARG ARG A . n 
A 1 510 ILE 510 510 510 ILE ILE A . n 
A 1 511 MET 511 511 511 MET MET A . n 
A 1 512 THR 512 512 512 THR THR A . n 
A 1 513 LYS 513 513 513 LYS LYS A . n 
A 1 514 LEU 514 514 514 LEU LEU A . n 
A 1 515 ARG 515 515 515 ARG ARG A . n 
A 1 516 ALA 516 516 516 ALA ALA A . n 
A 1 517 GLN 517 517 517 GLN GLN A . n 
A 1 518 GLN 518 518 518 GLN GLN A . n 
A 1 519 CYS 519 519 519 CYS CYS A . n 
A 1 520 ARG 520 520 520 ARG ARG A . n 
A 1 521 PHE 521 521 521 PHE PHE A . n 
A 1 522 TRP 522 522 522 TRP TRP A . n 
A 1 523 THR 523 523 523 THR THR A . n 
A 1 524 SER 524 524 524 SER SER A . n 
A 1 525 PHE 525 525 525 PHE PHE A . n 
A 1 526 PHE 526 526 526 PHE PHE A . n 
A 1 527 PRO 527 527 527 PRO PRO A . n 
A 1 528 LYS 528 528 528 LYS LYS A . n 
A 1 529 VAL 529 529 529 VAL VAL A . n 
# 
loop_
_pdbx_branch_scheme.asym_id 
_pdbx_branch_scheme.entity_id 
_pdbx_branch_scheme.mon_id 
_pdbx_branch_scheme.num 
_pdbx_branch_scheme.pdb_asym_id 
_pdbx_branch_scheme.pdb_mon_id 
_pdbx_branch_scheme.pdb_seq_num 
_pdbx_branch_scheme.auth_asym_id 
_pdbx_branch_scheme.auth_mon_id 
_pdbx_branch_scheme.auth_seq_num 
_pdbx_branch_scheme.hetero 
B 2 NAG 1 B NAG 1 A NAG 601 n 
B 2 FUC 2 B FUC 2 A FUC 602 n 
C 3 NAG 1 C NAG 1 A NAG 603 n 
C 3 NAG 2 C NAG 2 A NAG 904 n 
C 3 FUC 3 C FUC 3 A FUC 903 n 
D 3 NAG 1 D NAG 1 A NAG 605 n 
D 3 NAG 2 D NAG 2 A NAG 604 n 
D 3 FUC 3 D FUC 3 A FUC 606 n 
E 3 NAG 1 E NAG 1 A NAG 607 n 
E 3 NAG 2 E NAG 2 A NAG 608 n 
E 3 FUC 3 E FUC 3 A FUC 609 n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1H77 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1H77 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
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 
F 4  NAG   1  601 610 NAG   NAG A . 
G 4  NAG   1  602 611 NAG   NAG A . 
H 5  MES   1  603 619 MES   MES A . 
I 6  SO4   1  604 620 SO4   SO4 A . 
J 6  SO4   1  605 621 SO4   SO4 A . 
K 6  SO4   1  606 622 SO4   SO4 A . 
L 7  GOL   1  607 701 GOL   GOL A . 
M 8  SIA   1  608 901 SIA   SIA A . 
N 9  A1H77 1  609 905 A1H77 XT3 A . 
O 10 HOH   1  701 61  HOH   HOH A . 
O 10 HOH   2  702 52  HOH   HOH A . 
O 10 HOH   3  703 63  HOH   HOH A . 
O 10 HOH   4  704 42  HOH   HOH A . 
O 10 HOH   5  705 25  HOH   HOH A . 
O 10 HOH   6  706 15  HOH   HOH A . 
O 10 HOH   7  707 9   HOH   HOH A . 
O 10 HOH   8  708 45  HOH   HOH A . 
O 10 HOH   9  709 12  HOH   HOH A . 
O 10 HOH   10 710 22  HOH   HOH A . 
O 10 HOH   11 711 62  HOH   HOH A . 
O 10 HOH   12 712 85  HOH   HOH A . 
O 10 HOH   13 713 91  HOH   HOH A . 
O 10 HOH   14 714 84  HOH   HOH A . 
O 10 HOH   15 715 32  HOH   HOH A . 
O 10 HOH   16 716 39  HOH   HOH A . 
O 10 HOH   17 717 14  HOH   HOH A . 
O 10 HOH   18 718 92  HOH   HOH A . 
O 10 HOH   19 719 48  HOH   HOH A . 
O 10 HOH   20 720 29  HOH   HOH A . 
O 10 HOH   21 721 36  HOH   HOH A . 
O 10 HOH   22 722 74  HOH   HOH A . 
O 10 HOH   23 723 17  HOH   HOH A . 
O 10 HOH   24 724 46  HOH   HOH A . 
O 10 HOH   25 725 20  HOH   HOH A . 
O 10 HOH   26 726 23  HOH   HOH A . 
O 10 HOH   27 727 89  HOH   HOH A . 
O 10 HOH   28 728 80  HOH   HOH A . 
O 10 HOH   29 729 35  HOH   HOH A . 
O 10 HOH   30 730 54  HOH   HOH A . 
O 10 HOH   31 731 4   HOH   HOH A . 
O 10 HOH   32 732 31  HOH   HOH A . 
O 10 HOH   33 733 38  HOH   HOH A . 
O 10 HOH   34 734 57  HOH   HOH A . 
O 10 HOH   35 735 77  HOH   HOH A . 
O 10 HOH   36 736 49  HOH   HOH A . 
O 10 HOH   37 737 30  HOH   HOH A . 
O 10 HOH   38 738 60  HOH   HOH A . 
O 10 HOH   39 739 34  HOH   HOH A . 
O 10 HOH   40 740 72  HOH   HOH A . 
O 10 HOH   41 741 64  HOH   HOH A . 
O 10 HOH   42 742 18  HOH   HOH A . 
O 10 HOH   43 743 43  HOH   HOH A . 
O 10 HOH   44 744 3   HOH   HOH A . 
O 10 HOH   45 745 21  HOH   HOH A . 
O 10 HOH   46 746 27  HOH   HOH A . 
O 10 HOH   47 747 2   HOH   HOH A . 
O 10 HOH   48 748 1   HOH   HOH A . 
O 10 HOH   49 749 16  HOH   HOH A . 
O 10 HOH   50 750 28  HOH   HOH A . 
O 10 HOH   51 751 65  HOH   HOH A . 
O 10 HOH   52 752 11  HOH   HOH A . 
O 10 HOH   53 753 5   HOH   HOH A . 
O 10 HOH   54 754 50  HOH   HOH A . 
O 10 HOH   55 755 67  HOH   HOH A . 
O 10 HOH   56 756 6   HOH   HOH A . 
O 10 HOH   57 757 33  HOH   HOH A . 
O 10 HOH   58 758 90  HOH   HOH A . 
O 10 HOH   59 759 19  HOH   HOH A . 
O 10 HOH   60 760 81  HOH   HOH A . 
O 10 HOH   61 761 76  HOH   HOH A . 
O 10 HOH   62 762 73  HOH   HOH A . 
O 10 HOH   63 763 58  HOH   HOH A . 
O 10 HOH   64 764 47  HOH   HOH A . 
O 10 HOH   65 765 51  HOH   HOH A . 
O 10 HOH   66 766 53  HOH   HOH A . 
O 10 HOH   67 767 26  HOH   HOH A . 
O 10 HOH   68 768 44  HOH   HOH A . 
O 10 HOH   69 769 24  HOH   HOH A . 
O 10 HOH   70 770 94  HOH   HOH A . 
O 10 HOH   71 771 7   HOH   HOH A . 
O 10 HOH   72 772 78  HOH   HOH A . 
O 10 HOH   73 773 79  HOH   HOH A . 
O 10 HOH   74 774 8   HOH   HOH A . 
O 10 HOH   75 775 88  HOH   HOH A . 
O 10 HOH   76 776 93  HOH   HOH A . 
O 10 HOH   77 777 13  HOH   HOH A . 
O 10 HOH   78 778 66  HOH   HOH A . 
O 10 HOH   79 779 59  HOH   HOH A . 
O 10 HOH   80 780 75  HOH   HOH A . 
O 10 HOH   81 781 40  HOH   HOH A . 
O 10 HOH   82 782 82  HOH   HOH A . 
O 10 HOH   83 783 83  HOH   HOH A . 
O 10 HOH   84 784 87  HOH   HOH A . 
O 10 HOH   85 785 97  HOH   HOH A . 
O 10 HOH   86 786 10  HOH   HOH A . 
O 10 HOH   87 787 96  HOH   HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 A GLN 486 ? CG  ? A GLN 486 CG  
2 1 Y 1 A GLN 486 ? CD  ? A GLN 486 CD  
3 1 Y 1 A GLN 486 ? OE1 ? A GLN 486 OE1 
4 1 Y 1 A GLN 486 ? NE2 ? A GLN 486 NE2 
# 
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 
? 'data collection' ? ? ? ? ? ? ? ? ? ? ? MxCuBE ? ? ? .           1 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           2 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .           3 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .           4 
? 'model building'  ? ? ? ? ? ? ? ? ? ? ? Coot   ? ? ? 1.20.1_4487 5 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.20.1_4487 6 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9EWU 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     154.600 
_cell.length_a_esd                 ? 
_cell.length_b                     154.600 
_cell.length_b_esd                 ? 
_cell.length_c                     128.520 
_cell.length_c_esd                 ? 
_cell.volume                       3071777.083 
_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                         9EWU 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                97 
_symmetry.space_group_name_Hall            'I 4 2' 
_symmetry.space_group_name_H-M             'I 4 2 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9EWU 
_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             3.22 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          61.74 
_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    'Ammonium sulfate' 
_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         2020-07-04 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97856 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SOLEIL BEAMLINE PROXIMA 1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97856 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'PROXIMA 1' 
_diffrn_source.pdbx_synchrotron_site       SOLEIL 
# 
_reflns.B_iso_Wilson_estimate                          61.90 
_reflns.entry_id                                       9EWU 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.45 
_reflns.d_resolution_low                               38.91 
_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                                     28852 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.91 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                26.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          14.88 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.2032 
_reflns.pdbx_Rpim_I_all                                0.03961 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   1 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.1993 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.45 
_reflns_shell.d_res_low                                     2.538 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.85 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2854 
_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                               27.9 
_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                               2.643 
_reflns_shell.pdbx_Rpim_I_all                               0.4987 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.656 
_reflns_shell.pdbx_CC_star                                  0.89 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          100.00 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  2.596 
_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                               71.70 
_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                                 9EWU 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.45 
_refine.ls_d_res_low                             38.91 
_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                     28846 
_refine.ls_number_reflns_R_free                  1154 
_refine.ls_number_reflns_R_work                  27692 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.95 
_refine.ls_percent_reflns_R_free                 4.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1905 
_refine.ls_R_factor_R_free                       0.2439 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1884 
_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                          1.36 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 27.2877 
_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                            0.3193 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.45 
_refine_hist.d_res_low                        38.91 
_refine_hist.number_atoms_solvent             87 
_refine_hist.number_atoms_total               4528 
_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        4191 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         250 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0090  ? 4628 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.0168  ? 6296 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0904  ? 705  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0080  ? 780  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 15.1027 ? 692  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.45 2.56  . . 142 3397 100.00 . . . . 0.2853 . . . . . . . . . . . 0.3408 
'X-RAY DIFFRACTION' 2.56 2.70  . . 143 3420 99.94  . . . . 0.2693 . . . . . . . . . . . 0.3436 
'X-RAY DIFFRACTION' 2.70 2.87  . . 142 3410 100.00 . . . . 0.2397 . . . . . . . . . . . 0.2820 
'X-RAY DIFFRACTION' 2.87 3.09  . . 143 3439 99.97  . . . . 0.2118 . . . . . . . . . . . 0.3063 
'X-RAY DIFFRACTION' 3.09 3.40  . . 142 3418 99.92  . . . . 0.2094 . . . . . . . . . . . 0.2639 
'X-RAY DIFFRACTION' 3.40 3.89  . . 146 3484 100.00 . . . . 0.1718 . . . . . . . . . . . 0.2232 
'X-RAY DIFFRACTION' 3.89 4.90  . . 145 3479 99.97  . . . . 0.1557 . . . . . . . . . . . 0.2135 
'X-RAY DIFFRACTION' 4.90 38.91 . . 151 3645 99.79  . . . . 0.1802 . . . . . . . . . . . 0.2284 
# 
_struct.entry_id                     9EWU 
_struct.title                        
;Crystal structure of human butyrylcholinesterase in complex with (2R,3S)-1-[(cyclopropylmethyl)amino]-3-[(9H-fluoren-9-yl)amino]-4-phenylbutan-2-ol
;
_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        9EWU 
_struct_keywords.text            'Butyrylcholinesterase, Inhibitor, Complex, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1  ? 
B N N 2  ? 
C N N 3  ? 
D N N 3  ? 
E N N 3  ? 
F N N 4  ? 
G N N 4  ? 
H N N 5  ? 
I N N 6  ? 
J N N 6  ? 
K N N 6  ? 
L N N 7  ? 
M N N 8  ? 
N N N 9  ? 
O N N 10 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CHLE_HUMAN 
_struct_ref.pdbx_db_accession          P06276 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;EDDIIIATKNGKVRGMNLTVFGGTVTAFLGIPYAQPPLGRLRFKKPQSLTKWSDIWNATKYANSCCQNIDQSFPGFHGSE
MWNPNTDLSEDCLYLNVWIPAPKPKNATVLIWIYGGGFQTGTSSLHVYDGKFLARVERVIVVSMNYRVGALGFLALPGNP
EAPGNMGLFDQQLALQWVQKNIAAFGGNPKSVTLFGESAGAASVSLHLLSPGSHSLFTRAILQSGSFNAPWAVTSLYEAR
NRTLNLAKLTGCSRENETEIIKCLRNKDPQEILLNEAFVVPYGTPLSVNFGPTVDGDFLTDMPDILLELGQFKKTQILVG
VNKDEGTAFLVYGAPGFSKDNNSIITRKEFQEGLKIFFPGVSEFGKESILFHYTDWVDDQRPENYREALGDVVGDYNFIC
PALEFTKKFSEWGNNAFFYYFEHRSSKLPWPEWMGVMHGYEIEFVFGLPLERRDNYTKAEEILSRSIVKRWANFAKYGNP
NETQNNSTSWPVFKSTEQKYLTLNTESTRIMTKLRAQQCRFWTSFFPKV
;
_struct_ref.pdbx_align_begin           29 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9EWU 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 529 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P06276 
_struct_ref_seq.db_align_beg                  29 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  557 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       529 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9EWU GLN A 17  ? UNP P06276 ASN 45  'engineered mutation' 17  1 
1 9EWU GLN A 455 ? UNP P06276 ASN 483 'engineered mutation' 455 2 
1 9EWU GLN A 481 ? UNP P06276 ASN 509 'engineered mutation' 481 3 
1 9EWU GLN A 486 ? UNP P06276 ASN 514 'engineered mutation' 486 4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O 
# 
_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 LEU A 38  ? ARG A 42  ? LEU A 38  ARG A 42  5 ? 5  
HELX_P HELX_P2  AA2 PHE A 76  ? MET A 81  ? PHE A 76  MET A 81  1 ? 6  
HELX_P HELX_P3  AA3 LEU A 125 ? ASP A 129 ? LEU A 125 ASP A 129 5 ? 5  
HELX_P HELX_P4  AA4 GLY A 130 ? ARG A 138 ? GLY A 130 ARG A 138 1 ? 9  
HELX_P HELX_P5  AA5 VAL A 148 ? LEU A 154 ? VAL A 148 LEU A 154 1 ? 7  
HELX_P HELX_P6  AA6 ASN A 165 ? ILE A 182 ? ASN A 165 ILE A 182 1 ? 18 
HELX_P HELX_P7  AA7 ALA A 183 ? PHE A 185 ? ALA A 183 PHE A 185 5 ? 3  
HELX_P HELX_P8  AA8 SER A 198 ? SER A 210 ? SER A 198 SER A 210 1 ? 13 
HELX_P HELX_P9  AA9 PRO A 211 ? PHE A 217 ? PRO A 211 PHE A 217 5 ? 7  
HELX_P HELX_P10 AB1 SER A 235 ? THR A 250 ? SER A 235 THR A 250 1 ? 16 
HELX_P HELX_P11 AB2 ASN A 256 ? ASN A 266 ? ASN A 256 ASN A 266 1 ? 11 
HELX_P HELX_P12 AB3 ASP A 268 ? ALA A 277 ? ASP A 268 ALA A 277 1 ? 10 
HELX_P HELX_P13 AB4 PHE A 278 ? VAL A 280 ? PHE A 278 VAL A 280 5 ? 3  
HELX_P HELX_P14 AB5 MET A 302 ? LEU A 309 ? MET A 302 LEU A 309 1 ? 8  
HELX_P HELX_P15 AB6 GLY A 326 ? VAL A 331 ? GLY A 326 VAL A 331 1 ? 6  
HELX_P HELX_P16 AB7 THR A 346 ? PHE A 358 ? THR A 346 PHE A 358 1 ? 13 
HELX_P HELX_P17 AB8 SER A 362 ? THR A 374 ? SER A 362 THR A 374 1 ? 13 
HELX_P HELX_P18 AB9 GLU A 383 ? PHE A 398 ? GLU A 383 PHE A 398 1 ? 16 
HELX_P HELX_P19 AC1 PHE A 398 ? GLU A 411 ? PHE A 398 GLU A 411 1 ? 14 
HELX_P HELX_P20 AC2 PRO A 431 ? GLY A 435 ? PRO A 431 GLY A 435 5 ? 5  
HELX_P HELX_P21 AC3 GLU A 441 ? GLY A 447 ? GLU A 441 GLY A 447 1 ? 7  
HELX_P HELX_P22 AC4 LEU A 448 ? GLU A 451 ? LEU A 448 GLU A 451 5 ? 4  
HELX_P HELX_P23 AC5 THR A 457 ? GLY A 478 ? THR A 457 GLY A 478 1 ? 22 
HELX_P HELX_P24 AC6 ARG A 515 ? SER A 524 ? ARG A 515 SER A 524 1 ? 10 
HELX_P HELX_P25 AC7 PHE A 525 ? VAL A 529 ? PHE A 525 VAL A 529 5 ? 5  
# 
_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 
disulf1  disulf ?    ? A CYS 65  SG  ? ? ? 1_555 A CYS 92  SG ? ? A CYS 65  A CYS 92  1_555 ? ? ? ? ? ? ? 2.054 ? ?               
disulf2  disulf ?    ? A CYS 252 SG  ? ? ? 1_555 A CYS 263 SG ? ? A CYS 252 A CYS 263 1_555 ? ? ? ? ? ? ? 2.031 ? ?               
disulf3  disulf ?    ? A CYS 400 SG  ? ? ? 1_555 A CYS 519 SG ? ? A CYS 400 A CYS 519 1_555 ? ? ? ? ? ? ? 2.054 ? ?               
covale1  covale one  ? A ASN 57  ND2 ? ? ? 1_555 B NAG .   C1 ? ? A ASN 57  B NAG 1   1_555 ? ? ? ? ? ? ? 1.444 ? N-Glycosylation 
covale2  covale one  ? A ASN 106 ND2 ? ? ? 1_555 C NAG .   C1 ? ? A ASN 106 C NAG 1   1_555 ? ? ? ? ? ? ? 1.460 ? N-Glycosylation 
covale3  covale one  ? A ASN 241 ND2 ? ? ? 1_555 E NAG .   C1 ? ? A ASN 241 E NAG 1   1_555 ? ? ? ? ? ? ? 1.460 ? N-Glycosylation 
covale4  covale one  ? A ASN 256 ND2 ? ? ? 1_555 F NAG .   C1 ? ? A ASN 256 A NAG 601 1_555 ? ? ? ? ? ? ? 1.445 ? N-Glycosylation 
covale5  covale one  ? A ASN 341 ND2 ? ? ? 1_555 D NAG .   C1 ? ? A ASN 341 D NAG 1   1_555 ? ? ? ? ? ? ? 1.446 ? N-Glycosylation 
covale6  covale one  ? A ASN 485 ND2 ? ? ? 1_555 G NAG .   C1 ? ? A ASN 485 A NAG 602 1_555 ? ? ? ? ? ? ? 1.460 ? N-Glycosylation 
covale7  covale both ? B NAG .   O6  ? ? ? 1_555 B FUC .   C1 ? ? B NAG 1   B FUC 2   1_555 ? ? ? ? ? ? ? 1.432 ? ?               
covale8  covale both ? C NAG .   O4  ? ? ? 1_555 C NAG .   C1 ? ? C NAG 1   C NAG 2   1_555 ? ? ? ? ? ? ? 1.439 ? ?               
covale9  covale both ? C NAG .   O6  ? ? ? 1_555 C FUC .   C1 ? ? C NAG 1   C FUC 3   1_555 ? ? ? ? ? ? ? 1.454 ? ?               
covale10 covale both ? D NAG .   O4  ? ? ? 1_555 D NAG .   C1 ? ? D NAG 1   D NAG 2   1_555 ? ? ? ? ? ? ? 1.442 ? ?               
covale11 covale both ? D NAG .   O6  ? ? ? 1_555 D FUC .   C1 ? ? D NAG 1   D FUC 3   1_555 ? ? ? ? ? ? ? 1.447 ? ?               
covale12 covale both ? E NAG .   O4  ? ? ? 1_555 E NAG .   C1 ? ? E NAG 1   E NAG 2   1_555 ? ? ? ? ? ? ? 1.452 ? ?               
covale13 covale both ? E NAG .   O6  ? ? ? 1_555 E FUC .   C1 ? ? E NAG 1   E FUC 3   1_555 ? ? ? ? ? ? ? 1.458 ? ?               
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 NAG B .   ? ASN A 57  ? NAG B 1   ? 1_555 ASN A 57  ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
2 NAG C .   ? ASN A 106 ? NAG C 1   ? 1_555 ASN A 106 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
3 NAG D .   ? ASN A 341 ? NAG D 1   ? 1_555 ASN A 341 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
4 NAG E .   ? ASN A 241 ? NAG E 1   ? 1_555 ASN A 241 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
5 NAG F .   ? ASN A 256 ? NAG A 601 ? 1_555 ASN A 256 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
6 NAG G .   ? ASN A 485 ? NAG A 602 ? 1_555 ASN A 485 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
7 CYS A 65  ? CYS A 92  ? CYS A 65  ? 1_555 CYS A 92  ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
8 CYS A 252 ? CYS A 263 ? CYS A 252 ? 1_555 CYS A 263 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
9 CYS A 400 ? CYS A 519 ? CYS A 400 ? 1_555 CYS A 519 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          ALA 
_struct_mon_prot_cis.label_seq_id           101 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           ALA 
_struct_mon_prot_cis.auth_seq_id            101 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    102 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     102 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       0.75 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3  ? 
AA2 ? 11 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1  2  ? anti-parallel 
AA1 2  3  ? parallel      
AA2 1  2  ? anti-parallel 
AA2 2  3  ? anti-parallel 
AA2 3  4  ? anti-parallel 
AA2 4  5  ? parallel      
AA2 5  6  ? parallel      
AA2 6  7  ? parallel      
AA2 7  8  ? parallel      
AA2 8  9  ? parallel      
AA2 9  10 ? parallel      
AA2 10 11 ? 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  ILE A 5   ? THR A 8   ? ILE A 5   THR A 8   
AA1 2  GLY A 11  ? ARG A 14  ? GLY A 11  ARG A 14  
AA1 3  ILE A 55  ? ASN A 57  ? ILE A 55  ASN A 57  
AA2 1  MET A 16  ? THR A 19  ? MET A 16  THR A 19  
AA2 2  THR A 24  ? PRO A 32  ? THR A 24  PRO A 32  
AA2 3  TYR A 94  ? ALA A 101 ? TYR A 94  ALA A 101 
AA2 4  ILE A 140 ? MET A 144 ? ILE A 140 MET A 144 
AA2 5  ALA A 107 ? ILE A 113 ? ALA A 107 ILE A 113 
AA2 6  GLY A 187 ? GLU A 197 ? GLY A 187 GLU A 197 
AA2 7  ARG A 219 ? GLN A 223 ? ARG A 219 GLN A 223 
AA2 8  ILE A 317 ? ASN A 322 ? ILE A 317 ASN A 322 
AA2 9  ALA A 416 ? PHE A 421 ? ALA A 416 PHE A 421 
AA2 10 LYS A 499 ? LEU A 503 ? LYS A 499 LEU A 503 
AA2 11 ILE A 510 ? THR A 512 ? ILE A 510 THR A 512 
# 
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 ILE A 6   ? N ILE A 6   O VAL A 13  ? O VAL A 13  
AA1 2  3  N ARG A 14  ? N ARG A 14  O TRP A 56  ? O TRP A 56  
AA2 1  2  N LEU A 18  ? N LEU A 18  O VAL A 25  ? O VAL A 25  
AA2 2  3  N ILE A 31  ? N ILE A 31  O LEU A 95  ? O LEU A 95  
AA2 3  4  N ASN A 96  ? N ASN A 96  O SER A 143 ? O SER A 143 
AA2 4  5  O ILE A 140 ? O ILE A 140 N LEU A 110 ? N LEU A 110 
AA2 5  6  N VAL A 109 ? N VAL A 109 O SER A 191 ? O SER A 191 
AA2 6  7  N GLY A 196 ? N GLY A 196 O GLN A 223 ? O GLN A 223 
AA2 7  8  N LEU A 222 ? N LEU A 222 O LEU A 318 ? O LEU A 318 
AA2 8  9  N VAL A 319 ? N VAL A 319 O PHE A 417 ? O PHE A 417 
AA2 9  10 N PHE A 418 ? N PHE A 418 O LEU A 501 ? O LEU A 501 
AA2 10 11 N TYR A 500 ? N TYR A 500 O MET A 511 ? O MET A 511 
# 
_pdbx_entry_details.entry_id                   9EWU 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
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 PHE A 21  ? ? 47.87   70.64   
2  1 PHE A 43  ? ? 80.56   -17.42  
3  1 ALA A 58  ? ? -102.77 66.12   
4  1 LYS A 103 ? ? -38.82  130.19  
5  1 LYS A 105 ? ? -93.45  -64.02  
6  1 PHE A 118 ? ? 58.21   10.44   
7  1 ALA A 162 ? ? -156.25 74.65   
8  1 SER A 198 ? ? 64.44   -124.88 
9  1 ARG A 254 ? ? -127.89 -164.07 
10 1 ASN A 256 ? ? -57.51  108.69  
11 1 ASP A 297 ? ? -130.13 -71.23  
12 1 PHE A 398 ? ? -140.21 -57.57  
13 1 ASP A 454 ? ? -66.11  -176.90 
14 1 ASN A 485 ? ? -88.21  47.08   
15 1 GLN A 486 ? ? 39.86   49.76   
16 1 SER A 524 ? ? -95.53  -61.24  
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1  x,y,z                
2  -y,x,z               
3  y,-x,z               
4  x,-y,-z              
5  -x,y,-z              
6  -x,-y,z              
7  y,x,-z               
8  -y,-x,-z             
9  x+1/2,y+1/2,z+1/2    
10 -y+1/2,x+1/2,z+1/2   
11 y+1/2,-x+1/2,z+1/2   
12 x+1/2,-y+1/2,-z+1/2  
13 -x+1/2,y+1/2,-z+1/2  
14 -x+1/2,-y+1/2,z+1/2  
15 y+1/2,x+1/2,-z+1/2   
16 -y+1/2,-x+1/2,-z+1/2 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         16.7309431458 
_pdbx_refine_tls.origin_y         32.1738923623 
_pdbx_refine_tls.origin_z         39.1470476625 
_pdbx_refine_tls.T[1][1]          0.417124517994 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0383212429458 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          0.0267953043104 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.405648713244 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.0420623596442 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.515973523391 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          1.37373565317 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          0.17298208913 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.235935844444 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          1.68768013494 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          0.0608224799266 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          2.10534521872 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0171123496568 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.00969888952953 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.157220921502 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.117688961162 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.0689256924903 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          0.0127062679505 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.130808669063 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.0503382107998 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.0595826822382 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   A 
_pdbx_refine_tls_group.beg_label_seq_id    1 
_pdbx_refine_tls_group.beg_auth_asym_id    A 
_pdbx_refine_tls_group.beg_auth_seq_id     4 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   A 
_pdbx_refine_tls_group.end_label_seq_id    526 
_pdbx_refine_tls_group.end_auth_asym_id    A 
_pdbx_refine_tls_group.end_auth_seq_id     529 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   
;chain 'A' and (resid 4 through 529 )
;
# 
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 GLU 1 ? A GLU 1 
2 1 Y 1 A ASP 2 ? A ASP 2 
3 1 Y 1 A ASP 3 ? A ASP 3 
# 
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 
A1H77 C02  C N R 1   
A1H77 C03  C N N 2   
A1H77 C05  C N N 3   
A1H77 C06  C N N 4   
A1H77 C07  C N N 5   
A1H77 C08  C N N 6   
A1H77 C09  C N R 7   
A1H77 C10  C N N 8   
A1H77 C11  C Y N 9   
A1H77 C12  C Y N 10  
A1H77 C13  C Y N 11  
A1H77 C14  C Y N 12  
A1H77 C15  C Y N 13  
A1H77 C16  C Y N 14  
A1H77 C18  C N R 15  
A1H77 C19  C Y N 16  
A1H77 C20  C Y N 17  
A1H77 C21  C Y N 18  
A1H77 C22  C Y N 19  
A1H77 C23  C Y N 20  
A1H77 C24  C Y N 21  
A1H77 C25  C Y N 22  
A1H77 C26  C Y N 23  
A1H77 C27  C Y N 24  
A1H77 C28  C Y N 25  
A1H77 C29  C Y N 26  
A1H77 C30  C Y N 27  
A1H77 N04  N N N 28  
A1H77 N17  N N N 29  
A1H77 O01  O N N 30  
A1H77 H021 H N N 31  
A1H77 H031 H N N 32  
A1H77 H032 H N N 33  
A1H77 H051 H N N 34  
A1H77 H052 H N N 35  
A1H77 H061 H N N 36  
A1H77 H072 H N N 37  
A1H77 H071 H N N 38  
A1H77 H082 H N N 39  
A1H77 H081 H N N 40  
A1H77 H091 H N N 41  
A1H77 H101 H N N 42  
A1H77 H102 H N N 43  
A1H77 H121 H N N 44  
A1H77 H131 H N N 45  
A1H77 H141 H N N 46  
A1H77 H151 H N N 47  
A1H77 H161 H N N 48  
A1H77 H181 H N N 49  
A1H77 H201 H N N 50  
A1H77 H211 H N N 51  
A1H77 H221 H N N 52  
A1H77 H231 H N N 53  
A1H77 H271 H N N 54  
A1H77 H281 H N N 55  
A1H77 H291 H N N 56  
A1H77 H301 H N N 57  
A1H77 H1   H N N 58  
A1H77 H171 H N N 59  
A1H77 H011 H N N 60  
ALA   N    N N N 61  
ALA   CA   C N S 62  
ALA   C    C N N 63  
ALA   O    O N N 64  
ALA   CB   C N N 65  
ALA   OXT  O N N 66  
ALA   H    H N N 67  
ALA   H2   H N N 68  
ALA   HA   H N N 69  
ALA   HB1  H N N 70  
ALA   HB2  H N N 71  
ALA   HB3  H N N 72  
ALA   HXT  H N N 73  
ARG   N    N N N 74  
ARG   CA   C N S 75  
ARG   C    C N N 76  
ARG   O    O N N 77  
ARG   CB   C N N 78  
ARG   CG   C N N 79  
ARG   CD   C N N 80  
ARG   NE   N N N 81  
ARG   CZ   C N N 82  
ARG   NH1  N N N 83  
ARG   NH2  N N N 84  
ARG   OXT  O N N 85  
ARG   H    H N N 86  
ARG   H2   H N N 87  
ARG   HA   H N N 88  
ARG   HB2  H N N 89  
ARG   HB3  H N N 90  
ARG   HG2  H N N 91  
ARG   HG3  H N N 92  
ARG   HD2  H N N 93  
ARG   HD3  H N N 94  
ARG   HE   H N N 95  
ARG   HH11 H N N 96  
ARG   HH12 H N N 97  
ARG   HH21 H N N 98  
ARG   HH22 H N N 99  
ARG   HXT  H N N 100 
ASN   N    N N N 101 
ASN   CA   C N S 102 
ASN   C    C N N 103 
ASN   O    O N N 104 
ASN   CB   C N N 105 
ASN   CG   C N N 106 
ASN   OD1  O N N 107 
ASN   ND2  N N N 108 
ASN   OXT  O N N 109 
ASN   H    H N N 110 
ASN   H2   H N N 111 
ASN   HA   H N N 112 
ASN   HB2  H N N 113 
ASN   HB3  H N N 114 
ASN   HD21 H N N 115 
ASN   HD22 H N N 116 
ASN   HXT  H N N 117 
ASP   N    N N N 118 
ASP   CA   C N S 119 
ASP   C    C N N 120 
ASP   O    O N N 121 
ASP   CB   C N N 122 
ASP   CG   C N N 123 
ASP   OD1  O N N 124 
ASP   OD2  O N N 125 
ASP   OXT  O N N 126 
ASP   H    H N N 127 
ASP   H2   H N N 128 
ASP   HA   H N N 129 
ASP   HB2  H N N 130 
ASP   HB3  H N N 131 
ASP   HD2  H N N 132 
ASP   HXT  H N N 133 
CYS   N    N N N 134 
CYS   CA   C N R 135 
CYS   C    C N N 136 
CYS   O    O N N 137 
CYS   CB   C N N 138 
CYS   SG   S N N 139 
CYS   OXT  O N N 140 
CYS   H    H N N 141 
CYS   H2   H N N 142 
CYS   HA   H N N 143 
CYS   HB2  H N N 144 
CYS   HB3  H N N 145 
CYS   HG   H N N 146 
CYS   HXT  H N N 147 
FUC   C1   C N R 148 
FUC   C2   C N S 149 
FUC   C3   C N R 150 
FUC   C4   C N S 151 
FUC   C5   C N S 152 
FUC   C6   C N N 153 
FUC   O1   O N N 154 
FUC   O2   O N N 155 
FUC   O3   O N N 156 
FUC   O4   O N N 157 
FUC   O5   O N N 158 
FUC   H1   H N N 159 
FUC   H2   H N N 160 
FUC   H3   H N N 161 
FUC   H4   H N N 162 
FUC   H5   H N N 163 
FUC   H61  H N N 164 
FUC   H62  H N N 165 
FUC   H63  H N N 166 
FUC   HO1  H N N 167 
FUC   HO2  H N N 168 
FUC   HO3  H N N 169 
FUC   HO4  H N N 170 
GLN   N    N N N 171 
GLN   CA   C N S 172 
GLN   C    C N N 173 
GLN   O    O N N 174 
GLN   CB   C N N 175 
GLN   CG   C N N 176 
GLN   CD   C N N 177 
GLN   OE1  O N N 178 
GLN   NE2  N N N 179 
GLN   OXT  O N N 180 
GLN   H    H N N 181 
GLN   H2   H N N 182 
GLN   HA   H N N 183 
GLN   HB2  H N N 184 
GLN   HB3  H N N 185 
GLN   HG2  H N N 186 
GLN   HG3  H N N 187 
GLN   HE21 H N N 188 
GLN   HE22 H N N 189 
GLN   HXT  H N N 190 
GLU   N    N N N 191 
GLU   CA   C N S 192 
GLU   C    C N N 193 
GLU   O    O N N 194 
GLU   CB   C N N 195 
GLU   CG   C N N 196 
GLU   CD   C N N 197 
GLU   OE1  O N N 198 
GLU   OE2  O N N 199 
GLU   OXT  O N N 200 
GLU   H    H N N 201 
GLU   H2   H N N 202 
GLU   HA   H N N 203 
GLU   HB2  H N N 204 
GLU   HB3  H N N 205 
GLU   HG2  H N N 206 
GLU   HG3  H N N 207 
GLU   HE2  H N N 208 
GLU   HXT  H N N 209 
GLY   N    N N N 210 
GLY   CA   C N N 211 
GLY   C    C N N 212 
GLY   O    O N N 213 
GLY   OXT  O N N 214 
GLY   H    H N N 215 
GLY   H2   H N N 216 
GLY   HA2  H N N 217 
GLY   HA3  H N N 218 
GLY   HXT  H N N 219 
GOL   C1   C N N 220 
GOL   O1   O N N 221 
GOL   C2   C N N 222 
GOL   O2   O N N 223 
GOL   C3   C N N 224 
GOL   O3   O N N 225 
GOL   H11  H N N 226 
GOL   H12  H N N 227 
GOL   HO1  H N N 228 
GOL   H2   H N N 229 
GOL   HO2  H N N 230 
GOL   H31  H N N 231 
GOL   H32  H N N 232 
GOL   HO3  H N N 233 
HIS   N    N N N 234 
HIS   CA   C N S 235 
HIS   C    C N N 236 
HIS   O    O N N 237 
HIS   CB   C N N 238 
HIS   CG   C Y N 239 
HIS   ND1  N Y N 240 
HIS   CD2  C Y N 241 
HIS   CE1  C Y N 242 
HIS   NE2  N Y N 243 
HIS   OXT  O N N 244 
HIS   H    H N N 245 
HIS   H2   H N N 246 
HIS   HA   H N N 247 
HIS   HB2  H N N 248 
HIS   HB3  H N N 249 
HIS   HD1  H N N 250 
HIS   HD2  H N N 251 
HIS   HE1  H N N 252 
HIS   HE2  H N N 253 
HIS   HXT  H N N 254 
HOH   O    O N N 255 
HOH   H1   H N N 256 
HOH   H2   H N N 257 
ILE   N    N N N 258 
ILE   CA   C N S 259 
ILE   C    C N N 260 
ILE   O    O N N 261 
ILE   CB   C N S 262 
ILE   CG1  C N N 263 
ILE   CG2  C N N 264 
ILE   CD1  C N N 265 
ILE   OXT  O N N 266 
ILE   H    H N N 267 
ILE   H2   H N N 268 
ILE   HA   H N N 269 
ILE   HB   H N N 270 
ILE   HG12 H N N 271 
ILE   HG13 H N N 272 
ILE   HG21 H N N 273 
ILE   HG22 H N N 274 
ILE   HG23 H N N 275 
ILE   HD11 H N N 276 
ILE   HD12 H N N 277 
ILE   HD13 H N N 278 
ILE   HXT  H N N 279 
LEU   N    N N N 280 
LEU   CA   C N S 281 
LEU   C    C N N 282 
LEU   O    O N N 283 
LEU   CB   C N N 284 
LEU   CG   C N N 285 
LEU   CD1  C N N 286 
LEU   CD2  C N N 287 
LEU   OXT  O N N 288 
LEU   H    H N N 289 
LEU   H2   H N N 290 
LEU   HA   H N N 291 
LEU   HB2  H N N 292 
LEU   HB3  H N N 293 
LEU   HG   H N N 294 
LEU   HD11 H N N 295 
LEU   HD12 H N N 296 
LEU   HD13 H N N 297 
LEU   HD21 H N N 298 
LEU   HD22 H N N 299 
LEU   HD23 H N N 300 
LEU   HXT  H N N 301 
LYS   N    N N N 302 
LYS   CA   C N S 303 
LYS   C    C N N 304 
LYS   O    O N N 305 
LYS   CB   C N N 306 
LYS   CG   C N N 307 
LYS   CD   C N N 308 
LYS   CE   C N N 309 
LYS   NZ   N N N 310 
LYS   OXT  O N N 311 
LYS   H    H N N 312 
LYS   H2   H N N 313 
LYS   HA   H N N 314 
LYS   HB2  H N N 315 
LYS   HB3  H N N 316 
LYS   HG2  H N N 317 
LYS   HG3  H N N 318 
LYS   HD2  H N N 319 
LYS   HD3  H N N 320 
LYS   HE2  H N N 321 
LYS   HE3  H N N 322 
LYS   HZ1  H N N 323 
LYS   HZ2  H N N 324 
LYS   HZ3  H N N 325 
LYS   HXT  H N N 326 
MES   O1   O N N 327 
MES   C2   C N N 328 
MES   C3   C N N 329 
MES   N4   N N N 330 
MES   C5   C N N 331 
MES   C6   C N N 332 
MES   C7   C N N 333 
MES   C8   C N N 334 
MES   S    S N N 335 
MES   O1S  O N N 336 
MES   O2S  O N N 337 
MES   O3S  O N N 338 
MES   H21  H N N 339 
MES   H22  H N N 340 
MES   H31  H N N 341 
MES   H32  H N N 342 
MES   HN4  H N N 343 
MES   H51  H N N 344 
MES   H52  H N N 345 
MES   H61  H N N 346 
MES   H62  H N N 347 
MES   H71  H N N 348 
MES   H72  H N N 349 
MES   H81  H N N 350 
MES   H82  H N N 351 
MET   N    N N N 352 
MET   CA   C N S 353 
MET   C    C N N 354 
MET   O    O N N 355 
MET   CB   C N N 356 
MET   CG   C N N 357 
MET   SD   S N N 358 
MET   CE   C N N 359 
MET   OXT  O N N 360 
MET   H    H N N 361 
MET   H2   H N N 362 
MET   HA   H N N 363 
MET   HB2  H N N 364 
MET   HB3  H N N 365 
MET   HG2  H N N 366 
MET   HG3  H N N 367 
MET   HE1  H N N 368 
MET   HE2  H N N 369 
MET   HE3  H N N 370 
MET   HXT  H N N 371 
NAG   C1   C N R 372 
NAG   C2   C N R 373 
NAG   C3   C N R 374 
NAG   C4   C N S 375 
NAG   C5   C N R 376 
NAG   C6   C N N 377 
NAG   C7   C N N 378 
NAG   C8   C N N 379 
NAG   N2   N N N 380 
NAG   O1   O N N 381 
NAG   O3   O N N 382 
NAG   O4   O N N 383 
NAG   O5   O N N 384 
NAG   O6   O N N 385 
NAG   O7   O N N 386 
NAG   H1   H N N 387 
NAG   H2   H N N 388 
NAG   H3   H N N 389 
NAG   H4   H N N 390 
NAG   H5   H N N 391 
NAG   H61  H N N 392 
NAG   H62  H N N 393 
NAG   H81  H N N 394 
NAG   H82  H N N 395 
NAG   H83  H N N 396 
NAG   HN2  H N N 397 
NAG   HO1  H N N 398 
NAG   HO3  H N N 399 
NAG   HO4  H N N 400 
NAG   HO6  H N N 401 
PHE   N    N N N 402 
PHE   CA   C N S 403 
PHE   C    C N N 404 
PHE   O    O N N 405 
PHE   CB   C N N 406 
PHE   CG   C Y N 407 
PHE   CD1  C Y N 408 
PHE   CD2  C Y N 409 
PHE   CE1  C Y N 410 
PHE   CE2  C Y N 411 
PHE   CZ   C Y N 412 
PHE   OXT  O N N 413 
PHE   H    H N N 414 
PHE   H2   H N N 415 
PHE   HA   H N N 416 
PHE   HB2  H N N 417 
PHE   HB3  H N N 418 
PHE   HD1  H N N 419 
PHE   HD2  H N N 420 
PHE   HE1  H N N 421 
PHE   HE2  H N N 422 
PHE   HZ   H N N 423 
PHE   HXT  H N N 424 
PRO   N    N N N 425 
PRO   CA   C N S 426 
PRO   C    C N N 427 
PRO   O    O N N 428 
PRO   CB   C N N 429 
PRO   CG   C N N 430 
PRO   CD   C N N 431 
PRO   OXT  O N N 432 
PRO   H    H N N 433 
PRO   HA   H N N 434 
PRO   HB2  H N N 435 
PRO   HB3  H N N 436 
PRO   HG2  H N N 437 
PRO   HG3  H N N 438 
PRO   HD2  H N N 439 
PRO   HD3  H N N 440 
PRO   HXT  H N N 441 
SER   N    N N N 442 
SER   CA   C N S 443 
SER   C    C N N 444 
SER   O    O N N 445 
SER   CB   C N N 446 
SER   OG   O N N 447 
SER   OXT  O N N 448 
SER   H    H N N 449 
SER   H2   H N N 450 
SER   HA   H N N 451 
SER   HB2  H N N 452 
SER   HB3  H N N 453 
SER   HG   H N N 454 
SER   HXT  H N N 455 
SIA   C1   C N N 456 
SIA   C2   C N R 457 
SIA   C3   C N N 458 
SIA   C4   C N S 459 
SIA   C5   C N R 460 
SIA   C6   C N R 461 
SIA   C7   C N R 462 
SIA   C8   C N R 463 
SIA   C9   C N N 464 
SIA   C10  C N N 465 
SIA   C11  C N N 466 
SIA   N5   N N N 467 
SIA   O1A  O N N 468 
SIA   O1B  O N N 469 
SIA   O2   O N N 470 
SIA   O4   O N N 471 
SIA   O6   O N N 472 
SIA   O7   O N N 473 
SIA   O8   O N N 474 
SIA   O9   O N N 475 
SIA   O10  O N N 476 
SIA   H32  H N N 477 
SIA   H31  H N N 478 
SIA   H4   H N N 479 
SIA   H5   H N N 480 
SIA   H6   H N N 481 
SIA   H7   H N N 482 
SIA   H8   H N N 483 
SIA   H92  H N N 484 
SIA   H91  H N N 485 
SIA   H111 H N N 486 
SIA   H113 H N N 487 
SIA   H112 H N N 488 
SIA   HN5  H N N 489 
SIA   HO1B H N N 490 
SIA   HO2  H N N 491 
SIA   HO4  H N N 492 
SIA   HO7  H N N 493 
SIA   HO8  H N N 494 
SIA   HO9  H N N 495 
SO4   S    S N N 496 
SO4   O1   O N N 497 
SO4   O2   O N N 498 
SO4   O3   O N N 499 
SO4   O4   O N N 500 
THR   N    N N N 501 
THR   CA   C N S 502 
THR   C    C N N 503 
THR   O    O N N 504 
THR   CB   C N R 505 
THR   OG1  O N N 506 
THR   CG2  C N N 507 
THR   OXT  O N N 508 
THR   H    H N N 509 
THR   H2   H N N 510 
THR   HA   H N N 511 
THR   HB   H N N 512 
THR   HG1  H N N 513 
THR   HG21 H N N 514 
THR   HG22 H N N 515 
THR   HG23 H N N 516 
THR   HXT  H N N 517 
TRP   N    N N N 518 
TRP   CA   C N S 519 
TRP   C    C N N 520 
TRP   O    O N N 521 
TRP   CB   C N N 522 
TRP   CG   C Y N 523 
TRP   CD1  C Y N 524 
TRP   CD2  C Y N 525 
TRP   NE1  N Y N 526 
TRP   CE2  C Y N 527 
TRP   CE3  C Y N 528 
TRP   CZ2  C Y N 529 
TRP   CZ3  C Y N 530 
TRP   CH2  C Y N 531 
TRP   OXT  O N N 532 
TRP   H    H N N 533 
TRP   H2   H N N 534 
TRP   HA   H N N 535 
TRP   HB2  H N N 536 
TRP   HB3  H N N 537 
TRP   HD1  H N N 538 
TRP   HE1  H N N 539 
TRP   HE3  H N N 540 
TRP   HZ2  H N N 541 
TRP   HZ3  H N N 542 
TRP   HH2  H N N 543 
TRP   HXT  H N N 544 
TYR   N    N N N 545 
TYR   CA   C N S 546 
TYR   C    C N N 547 
TYR   O    O N N 548 
TYR   CB   C N N 549 
TYR   CG   C Y N 550 
TYR   CD1  C Y N 551 
TYR   CD2  C Y N 552 
TYR   CE1  C Y N 553 
TYR   CE2  C Y N 554 
TYR   CZ   C Y N 555 
TYR   OH   O N N 556 
TYR   OXT  O N N 557 
TYR   H    H N N 558 
TYR   H2   H N N 559 
TYR   HA   H N N 560 
TYR   HB2  H N N 561 
TYR   HB3  H N N 562 
TYR   HD1  H N N 563 
TYR   HD2  H N N 564 
TYR   HE1  H N N 565 
TYR   HE2  H N N 566 
TYR   HH   H N N 567 
TYR   HXT  H N N 568 
VAL   N    N N N 569 
VAL   CA   C N S 570 
VAL   C    C N N 571 
VAL   O    O N N 572 
VAL   CB   C N N 573 
VAL   CG1  C N N 574 
VAL   CG2  C N N 575 
VAL   OXT  O N N 576 
VAL   H    H N N 577 
VAL   H2   H N N 578 
VAL   HA   H N N 579 
VAL   HB   H N N 580 
VAL   HG11 H N N 581 
VAL   HG12 H N N 582 
VAL   HG13 H N N 583 
VAL   HG21 H N N 584 
VAL   HG22 H N N 585 
VAL   HG23 H N N 586 
VAL   HXT  H N N 587 
# 
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 
A1H77 C02 O01  sing N N 1   
A1H77 N04 C03  sing N N 2   
A1H77 C05 N04  sing N N 3   
A1H77 C06 C05  sing N N 4   
A1H77 C07 C06  sing N N 5   
A1H77 C08 C07  sing N N 6   
A1H77 C03 C02  sing N N 7   
A1H77 C09 C02  sing N N 8   
A1H77 C11 C10  sing N N 9   
A1H77 C12 C11  doub Y N 10  
A1H77 C13 C12  sing Y N 11  
A1H77 C14 C13  doub Y N 12  
A1H77 C15 C14  sing Y N 13  
A1H77 C16 C15  doub Y N 14  
A1H77 C10 C09  sing N N 15  
A1H77 N17 C09  sing N N 16  
A1H77 C18 N17  sing N N 17  
A1H77 C19 C18  sing N N 18  
A1H77 C20 C19  doub Y N 19  
A1H77 C21 C20  sing Y N 20  
A1H77 C22 C21  doub Y N 21  
A1H77 C23 C22  sing Y N 22  
A1H77 C24 C23  doub Y N 23  
A1H77 C25 C24  sing N N 24  
A1H77 C26 C25  doub Y N 25  
A1H77 C27 C26  sing Y N 26  
A1H77 C28 C27  doub Y N 27  
A1H77 C29 C28  sing Y N 28  
A1H77 C30 C29  doub Y N 29  
A1H77 C06 C08  sing N N 30  
A1H77 C11 C16  sing Y N 31  
A1H77 C18 C26  sing N N 32  
A1H77 C19 C24  sing Y N 33  
A1H77 C25 C30  sing Y N 34  
A1H77 C02 H021 sing N N 35  
A1H77 C03 H031 sing N N 36  
A1H77 C03 H032 sing N N 37  
A1H77 C05 H051 sing N N 38  
A1H77 C05 H052 sing N N 39  
A1H77 C06 H061 sing N N 40  
A1H77 C07 H072 sing N N 41  
A1H77 C07 H071 sing N N 42  
A1H77 C08 H082 sing N N 43  
A1H77 C08 H081 sing N N 44  
A1H77 C09 H091 sing N N 45  
A1H77 C10 H101 sing N N 46  
A1H77 C10 H102 sing N N 47  
A1H77 C12 H121 sing N N 48  
A1H77 C13 H131 sing N N 49  
A1H77 C14 H141 sing N N 50  
A1H77 C15 H151 sing N N 51  
A1H77 C16 H161 sing N N 52  
A1H77 C18 H181 sing N N 53  
A1H77 C20 H201 sing N N 54  
A1H77 C21 H211 sing N N 55  
A1H77 C22 H221 sing N N 56  
A1H77 C23 H231 sing N N 57  
A1H77 C27 H271 sing N N 58  
A1H77 C28 H281 sing N N 59  
A1H77 C29 H291 sing N N 60  
A1H77 C30 H301 sing N N 61  
A1H77 N04 H1   sing N N 62  
A1H77 N17 H171 sing N N 63  
A1H77 O01 H011 sing N N 64  
ALA   N   CA   sing N N 65  
ALA   N   H    sing N N 66  
ALA   N   H2   sing N N 67  
ALA   CA  C    sing N N 68  
ALA   CA  CB   sing N N 69  
ALA   CA  HA   sing N N 70  
ALA   C   O    doub N N 71  
ALA   C   OXT  sing N N 72  
ALA   CB  HB1  sing N N 73  
ALA   CB  HB2  sing N N 74  
ALA   CB  HB3  sing N N 75  
ALA   OXT HXT  sing N N 76  
ARG   N   CA   sing N N 77  
ARG   N   H    sing N N 78  
ARG   N   H2   sing N N 79  
ARG   CA  C    sing N N 80  
ARG   CA  CB   sing N N 81  
ARG   CA  HA   sing N N 82  
ARG   C   O    doub N N 83  
ARG   C   OXT  sing N N 84  
ARG   CB  CG   sing N N 85  
ARG   CB  HB2  sing N N 86  
ARG   CB  HB3  sing N N 87  
ARG   CG  CD   sing N N 88  
ARG   CG  HG2  sing N N 89  
ARG   CG  HG3  sing N N 90  
ARG   CD  NE   sing N N 91  
ARG   CD  HD2  sing N N 92  
ARG   CD  HD3  sing N N 93  
ARG   NE  CZ   sing N N 94  
ARG   NE  HE   sing N N 95  
ARG   CZ  NH1  sing N N 96  
ARG   CZ  NH2  doub N N 97  
ARG   NH1 HH11 sing N N 98  
ARG   NH1 HH12 sing N N 99  
ARG   NH2 HH21 sing N N 100 
ARG   NH2 HH22 sing N N 101 
ARG   OXT HXT  sing N N 102 
ASN   N   CA   sing N N 103 
ASN   N   H    sing N N 104 
ASN   N   H2   sing N N 105 
ASN   CA  C    sing N N 106 
ASN   CA  CB   sing N N 107 
ASN   CA  HA   sing N N 108 
ASN   C   O    doub N N 109 
ASN   C   OXT  sing N N 110 
ASN   CB  CG   sing N N 111 
ASN   CB  HB2  sing N N 112 
ASN   CB  HB3  sing N N 113 
ASN   CG  OD1  doub N N 114 
ASN   CG  ND2  sing N N 115 
ASN   ND2 HD21 sing N N 116 
ASN   ND2 HD22 sing N N 117 
ASN   OXT HXT  sing N N 118 
ASP   N   CA   sing N N 119 
ASP   N   H    sing N N 120 
ASP   N   H2   sing N N 121 
ASP   CA  C    sing N N 122 
ASP   CA  CB   sing N N 123 
ASP   CA  HA   sing N N 124 
ASP   C   O    doub N N 125 
ASP   C   OXT  sing N N 126 
ASP   CB  CG   sing N N 127 
ASP   CB  HB2  sing N N 128 
ASP   CB  HB3  sing N N 129 
ASP   CG  OD1  doub N N 130 
ASP   CG  OD2  sing N N 131 
ASP   OD2 HD2  sing N N 132 
ASP   OXT HXT  sing N N 133 
CYS   N   CA   sing N N 134 
CYS   N   H    sing N N 135 
CYS   N   H2   sing N N 136 
CYS   CA  C    sing N N 137 
CYS   CA  CB   sing N N 138 
CYS   CA  HA   sing N N 139 
CYS   C   O    doub N N 140 
CYS   C   OXT  sing N N 141 
CYS   CB  SG   sing N N 142 
CYS   CB  HB2  sing N N 143 
CYS   CB  HB3  sing N N 144 
CYS   SG  HG   sing N N 145 
CYS   OXT HXT  sing N N 146 
FUC   C1  C2   sing N N 147 
FUC   C1  O1   sing N N 148 
FUC   C1  O5   sing N N 149 
FUC   C1  H1   sing N N 150 
FUC   C2  C3   sing N N 151 
FUC   C2  O2   sing N N 152 
FUC   C2  H2   sing N N 153 
FUC   C3  C4   sing N N 154 
FUC   C3  O3   sing N N 155 
FUC   C3  H3   sing N N 156 
FUC   C4  C5   sing N N 157 
FUC   C4  O4   sing N N 158 
FUC   C4  H4   sing N N 159 
FUC   C5  C6   sing N N 160 
FUC   C5  O5   sing N N 161 
FUC   C5  H5   sing N N 162 
FUC   C6  H61  sing N N 163 
FUC   C6  H62  sing N N 164 
FUC   C6  H63  sing N N 165 
FUC   O1  HO1  sing N N 166 
FUC   O2  HO2  sing N N 167 
FUC   O3  HO3  sing N N 168 
FUC   O4  HO4  sing N N 169 
GLN   N   CA   sing N N 170 
GLN   N   H    sing N N 171 
GLN   N   H2   sing N N 172 
GLN   CA  C    sing N N 173 
GLN   CA  CB   sing N N 174 
GLN   CA  HA   sing N N 175 
GLN   C   O    doub N N 176 
GLN   C   OXT  sing N N 177 
GLN   CB  CG   sing N N 178 
GLN   CB  HB2  sing N N 179 
GLN   CB  HB3  sing N N 180 
GLN   CG  CD   sing N N 181 
GLN   CG  HG2  sing N N 182 
GLN   CG  HG3  sing N N 183 
GLN   CD  OE1  doub N N 184 
GLN   CD  NE2  sing N N 185 
GLN   NE2 HE21 sing N N 186 
GLN   NE2 HE22 sing N N 187 
GLN   OXT HXT  sing N N 188 
GLU   N   CA   sing N N 189 
GLU   N   H    sing N N 190 
GLU   N   H2   sing N N 191 
GLU   CA  C    sing N N 192 
GLU   CA  CB   sing N N 193 
GLU   CA  HA   sing N N 194 
GLU   C   O    doub N N 195 
GLU   C   OXT  sing N N 196 
GLU   CB  CG   sing N N 197 
GLU   CB  HB2  sing N N 198 
GLU   CB  HB3  sing N N 199 
GLU   CG  CD   sing N N 200 
GLU   CG  HG2  sing N N 201 
GLU   CG  HG3  sing N N 202 
GLU   CD  OE1  doub N N 203 
GLU   CD  OE2  sing N N 204 
GLU   OE2 HE2  sing N N 205 
GLU   OXT HXT  sing N N 206 
GLY   N   CA   sing N N 207 
GLY   N   H    sing N N 208 
GLY   N   H2   sing N N 209 
GLY   CA  C    sing N N 210 
GLY   CA  HA2  sing N N 211 
GLY   CA  HA3  sing N N 212 
GLY   C   O    doub N N 213 
GLY   C   OXT  sing N N 214 
GLY   OXT HXT  sing N N 215 
GOL   C1  O1   sing N N 216 
GOL   C1  C2   sing N N 217 
GOL   C1  H11  sing N N 218 
GOL   C1  H12  sing N N 219 
GOL   O1  HO1  sing N N 220 
GOL   C2  O2   sing N N 221 
GOL   C2  C3   sing N N 222 
GOL   C2  H2   sing N N 223 
GOL   O2  HO2  sing N N 224 
GOL   C3  O3   sing N N 225 
GOL   C3  H31  sing N N 226 
GOL   C3  H32  sing N N 227 
GOL   O3  HO3  sing N N 228 
HIS   N   CA   sing N N 229 
HIS   N   H    sing N N 230 
HIS   N   H2   sing N N 231 
HIS   CA  C    sing N N 232 
HIS   CA  CB   sing N N 233 
HIS   CA  HA   sing N N 234 
HIS   C   O    doub N N 235 
HIS   C   OXT  sing N N 236 
HIS   CB  CG   sing N N 237 
HIS   CB  HB2  sing N N 238 
HIS   CB  HB3  sing N N 239 
HIS   CG  ND1  sing Y N 240 
HIS   CG  CD2  doub Y N 241 
HIS   ND1 CE1  doub Y N 242 
HIS   ND1 HD1  sing N N 243 
HIS   CD2 NE2  sing Y N 244 
HIS   CD2 HD2  sing N N 245 
HIS   CE1 NE2  sing Y N 246 
HIS   CE1 HE1  sing N N 247 
HIS   NE2 HE2  sing N N 248 
HIS   OXT HXT  sing N N 249 
HOH   O   H1   sing N N 250 
HOH   O   H2   sing N N 251 
ILE   N   CA   sing N N 252 
ILE   N   H    sing N N 253 
ILE   N   H2   sing N N 254 
ILE   CA  C    sing N N 255 
ILE   CA  CB   sing N N 256 
ILE   CA  HA   sing N N 257 
ILE   C   O    doub N N 258 
ILE   C   OXT  sing N N 259 
ILE   CB  CG1  sing N N 260 
ILE   CB  CG2  sing N N 261 
ILE   CB  HB   sing N N 262 
ILE   CG1 CD1  sing N N 263 
ILE   CG1 HG12 sing N N 264 
ILE   CG1 HG13 sing N N 265 
ILE   CG2 HG21 sing N N 266 
ILE   CG2 HG22 sing N N 267 
ILE   CG2 HG23 sing N N 268 
ILE   CD1 HD11 sing N N 269 
ILE   CD1 HD12 sing N N 270 
ILE   CD1 HD13 sing N N 271 
ILE   OXT HXT  sing N N 272 
LEU   N   CA   sing N N 273 
LEU   N   H    sing N N 274 
LEU   N   H2   sing N N 275 
LEU   CA  C    sing N N 276 
LEU   CA  CB   sing N N 277 
LEU   CA  HA   sing N N 278 
LEU   C   O    doub N N 279 
LEU   C   OXT  sing N N 280 
LEU   CB  CG   sing N N 281 
LEU   CB  HB2  sing N N 282 
LEU   CB  HB3  sing N N 283 
LEU   CG  CD1  sing N N 284 
LEU   CG  CD2  sing N N 285 
LEU   CG  HG   sing N N 286 
LEU   CD1 HD11 sing N N 287 
LEU   CD1 HD12 sing N N 288 
LEU   CD1 HD13 sing N N 289 
LEU   CD2 HD21 sing N N 290 
LEU   CD2 HD22 sing N N 291 
LEU   CD2 HD23 sing N N 292 
LEU   OXT HXT  sing N N 293 
LYS   N   CA   sing N N 294 
LYS   N   H    sing N N 295 
LYS   N   H2   sing N N 296 
LYS   CA  C    sing N N 297 
LYS   CA  CB   sing N N 298 
LYS   CA  HA   sing N N 299 
LYS   C   O    doub N N 300 
LYS   C   OXT  sing N N 301 
LYS   CB  CG   sing N N 302 
LYS   CB  HB2  sing N N 303 
LYS   CB  HB3  sing N N 304 
LYS   CG  CD   sing N N 305 
LYS   CG  HG2  sing N N 306 
LYS   CG  HG3  sing N N 307 
LYS   CD  CE   sing N N 308 
LYS   CD  HD2  sing N N 309 
LYS   CD  HD3  sing N N 310 
LYS   CE  NZ   sing N N 311 
LYS   CE  HE2  sing N N 312 
LYS   CE  HE3  sing N N 313 
LYS   NZ  HZ1  sing N N 314 
LYS   NZ  HZ2  sing N N 315 
LYS   NZ  HZ3  sing N N 316 
LYS   OXT HXT  sing N N 317 
MES   O1  C2   sing N N 318 
MES   O1  C6   sing N N 319 
MES   C2  C3   sing N N 320 
MES   C2  H21  sing N N 321 
MES   C2  H22  sing N N 322 
MES   C3  N4   sing N N 323 
MES   C3  H31  sing N N 324 
MES   C3  H32  sing N N 325 
MES   N4  C5   sing N N 326 
MES   N4  C7   sing N N 327 
MES   N4  HN4  sing N N 328 
MES   C5  C6   sing N N 329 
MES   C5  H51  sing N N 330 
MES   C5  H52  sing N N 331 
MES   C6  H61  sing N N 332 
MES   C6  H62  sing N N 333 
MES   C7  C8   sing N N 334 
MES   C7  H71  sing N N 335 
MES   C7  H72  sing N N 336 
MES   C8  S    sing N N 337 
MES   C8  H81  sing N N 338 
MES   C8  H82  sing N N 339 
MES   S   O1S  doub N N 340 
MES   S   O2S  doub N N 341 
MES   S   O3S  sing N N 342 
MET   N   CA   sing N N 343 
MET   N   H    sing N N 344 
MET   N   H2   sing N N 345 
MET   CA  C    sing N N 346 
MET   CA  CB   sing N N 347 
MET   CA  HA   sing N N 348 
MET   C   O    doub N N 349 
MET   C   OXT  sing N N 350 
MET   CB  CG   sing N N 351 
MET   CB  HB2  sing N N 352 
MET   CB  HB3  sing N N 353 
MET   CG  SD   sing N N 354 
MET   CG  HG2  sing N N 355 
MET   CG  HG3  sing N N 356 
MET   SD  CE   sing N N 357 
MET   CE  HE1  sing N N 358 
MET   CE  HE2  sing N N 359 
MET   CE  HE3  sing N N 360 
MET   OXT HXT  sing N N 361 
NAG   C1  C2   sing N N 362 
NAG   C1  O1   sing N N 363 
NAG   C1  O5   sing N N 364 
NAG   C1  H1   sing N N 365 
NAG   C2  C3   sing N N 366 
NAG   C2  N2   sing N N 367 
NAG   C2  H2   sing N N 368 
NAG   C3  C4   sing N N 369 
NAG   C3  O3   sing N N 370 
NAG   C3  H3   sing N N 371 
NAG   C4  C5   sing N N 372 
NAG   C4  O4   sing N N 373 
NAG   C4  H4   sing N N 374 
NAG   C5  C6   sing N N 375 
NAG   C5  O5   sing N N 376 
NAG   C5  H5   sing N N 377 
NAG   C6  O6   sing N N 378 
NAG   C6  H61  sing N N 379 
NAG   C6  H62  sing N N 380 
NAG   C7  C8   sing N N 381 
NAG   C7  N2   sing N N 382 
NAG   C7  O7   doub N N 383 
NAG   C8  H81  sing N N 384 
NAG   C8  H82  sing N N 385 
NAG   C8  H83  sing N N 386 
NAG   N2  HN2  sing N N 387 
NAG   O1  HO1  sing N N 388 
NAG   O3  HO3  sing N N 389 
NAG   O4  HO4  sing N N 390 
NAG   O6  HO6  sing N N 391 
PHE   N   CA   sing N N 392 
PHE   N   H    sing N N 393 
PHE   N   H2   sing N N 394 
PHE   CA  C    sing N N 395 
PHE   CA  CB   sing N N 396 
PHE   CA  HA   sing N N 397 
PHE   C   O    doub N N 398 
PHE   C   OXT  sing N N 399 
PHE   CB  CG   sing N N 400 
PHE   CB  HB2  sing N N 401 
PHE   CB  HB3  sing N N 402 
PHE   CG  CD1  doub Y N 403 
PHE   CG  CD2  sing Y N 404 
PHE   CD1 CE1  sing Y N 405 
PHE   CD1 HD1  sing N N 406 
PHE   CD2 CE2  doub Y N 407 
PHE   CD2 HD2  sing N N 408 
PHE   CE1 CZ   doub Y N 409 
PHE   CE1 HE1  sing N N 410 
PHE   CE2 CZ   sing Y N 411 
PHE   CE2 HE2  sing N N 412 
PHE   CZ  HZ   sing N N 413 
PHE   OXT HXT  sing N N 414 
PRO   N   CA   sing N N 415 
PRO   N   CD   sing N N 416 
PRO   N   H    sing N N 417 
PRO   CA  C    sing N N 418 
PRO   CA  CB   sing N N 419 
PRO   CA  HA   sing N N 420 
PRO   C   O    doub N N 421 
PRO   C   OXT  sing N N 422 
PRO   CB  CG   sing N N 423 
PRO   CB  HB2  sing N N 424 
PRO   CB  HB3  sing N N 425 
PRO   CG  CD   sing N N 426 
PRO   CG  HG2  sing N N 427 
PRO   CG  HG3  sing N N 428 
PRO   CD  HD2  sing N N 429 
PRO   CD  HD3  sing N N 430 
PRO   OXT HXT  sing N N 431 
SER   N   CA   sing N N 432 
SER   N   H    sing N N 433 
SER   N   H2   sing N N 434 
SER   CA  C    sing N N 435 
SER   CA  CB   sing N N 436 
SER   CA  HA   sing N N 437 
SER   C   O    doub N N 438 
SER   C   OXT  sing N N 439 
SER   CB  OG   sing N N 440 
SER   CB  HB2  sing N N 441 
SER   CB  HB3  sing N N 442 
SER   OG  HG   sing N N 443 
SER   OXT HXT  sing N N 444 
SIA   C1  C2   sing N N 445 
SIA   C1  O1A  doub N N 446 
SIA   C1  O1B  sing N N 447 
SIA   C2  C3   sing N N 448 
SIA   C2  O2   sing N N 449 
SIA   C2  O6   sing N N 450 
SIA   C3  C4   sing N N 451 
SIA   C3  H32  sing N N 452 
SIA   C3  H31  sing N N 453 
SIA   C4  C5   sing N N 454 
SIA   C4  O4   sing N N 455 
SIA   C4  H4   sing N N 456 
SIA   C5  C6   sing N N 457 
SIA   C5  N5   sing N N 458 
SIA   C5  H5   sing N N 459 
SIA   C6  C7   sing N N 460 
SIA   C6  O6   sing N N 461 
SIA   C6  H6   sing N N 462 
SIA   C7  C8   sing N N 463 
SIA   C7  O7   sing N N 464 
SIA   C7  H7   sing N N 465 
SIA   C8  C9   sing N N 466 
SIA   C8  O8   sing N N 467 
SIA   C8  H8   sing N N 468 
SIA   C9  O9   sing N N 469 
SIA   C9  H92  sing N N 470 
SIA   C9  H91  sing N N 471 
SIA   C10 C11  sing N N 472 
SIA   C10 N5   sing N N 473 
SIA   C10 O10  doub N N 474 
SIA   C11 H111 sing N N 475 
SIA   C11 H113 sing N N 476 
SIA   C11 H112 sing N N 477 
SIA   N5  HN5  sing N N 478 
SIA   O1B HO1B sing N N 479 
SIA   O2  HO2  sing N N 480 
SIA   O4  HO4  sing N N 481 
SIA   O7  HO7  sing N N 482 
SIA   O8  HO8  sing N N 483 
SIA   O9  HO9  sing N N 484 
SO4   S   O1   doub N N 485 
SO4   S   O2   doub N N 486 
SO4   S   O3   sing N N 487 
SO4   S   O4   sing N N 488 
THR   N   CA   sing N N 489 
THR   N   H    sing N N 490 
THR   N   H2   sing N N 491 
THR   CA  C    sing N N 492 
THR   CA  CB   sing N N 493 
THR   CA  HA   sing N N 494 
THR   C   O    doub N N 495 
THR   C   OXT  sing N N 496 
THR   CB  OG1  sing N N 497 
THR   CB  CG2  sing N N 498 
THR   CB  HB   sing N N 499 
THR   OG1 HG1  sing N N 500 
THR   CG2 HG21 sing N N 501 
THR   CG2 HG22 sing N N 502 
THR   CG2 HG23 sing N N 503 
THR   OXT HXT  sing N N 504 
TRP   N   CA   sing N N 505 
TRP   N   H    sing N N 506 
TRP   N   H2   sing N N 507 
TRP   CA  C    sing N N 508 
TRP   CA  CB   sing N N 509 
TRP   CA  HA   sing N N 510 
TRP   C   O    doub N N 511 
TRP   C   OXT  sing N N 512 
TRP   CB  CG   sing N N 513 
TRP   CB  HB2  sing N N 514 
TRP   CB  HB3  sing N N 515 
TRP   CG  CD1  doub Y N 516 
TRP   CG  CD2  sing Y N 517 
TRP   CD1 NE1  sing Y N 518 
TRP   CD1 HD1  sing N N 519 
TRP   CD2 CE2  doub Y N 520 
TRP   CD2 CE3  sing Y N 521 
TRP   NE1 CE2  sing Y N 522 
TRP   NE1 HE1  sing N N 523 
TRP   CE2 CZ2  sing Y N 524 
TRP   CE3 CZ3  doub Y N 525 
TRP   CE3 HE3  sing N N 526 
TRP   CZ2 CH2  doub Y N 527 
TRP   CZ2 HZ2  sing N N 528 
TRP   CZ3 CH2  sing Y N 529 
TRP   CZ3 HZ3  sing N N 530 
TRP   CH2 HH2  sing N N 531 
TRP   OXT HXT  sing N N 532 
TYR   N   CA   sing N N 533 
TYR   N   H    sing N N 534 
TYR   N   H2   sing N N 535 
TYR   CA  C    sing N N 536 
TYR   CA  CB   sing N N 537 
TYR   CA  HA   sing N N 538 
TYR   C   O    doub N N 539 
TYR   C   OXT  sing N N 540 
TYR   CB  CG   sing N N 541 
TYR   CB  HB2  sing N N 542 
TYR   CB  HB3  sing N N 543 
TYR   CG  CD1  doub Y N 544 
TYR   CG  CD2  sing Y N 545 
TYR   CD1 CE1  sing Y N 546 
TYR   CD1 HD1  sing N N 547 
TYR   CD2 CE2  doub Y N 548 
TYR   CD2 HD2  sing N N 549 
TYR   CE1 CZ   doub Y N 550 
TYR   CE1 HE1  sing N N 551 
TYR   CE2 CZ   sing Y N 552 
TYR   CE2 HE2  sing N N 553 
TYR   CZ  OH   sing N N 554 
TYR   OH  HH   sing N N 555 
TYR   OXT HXT  sing N N 556 
VAL   N   CA   sing N N 557 
VAL   N   H    sing N N 558 
VAL   N   H2   sing N N 559 
VAL   CA  C    sing N N 560 
VAL   CA  CB   sing N N 561 
VAL   CA  HA   sing N N 562 
VAL   C   O    doub N N 563 
VAL   C   OXT  sing N N 564 
VAL   CB  CG1  sing N N 565 
VAL   CB  CG2  sing N N 566 
VAL   CB  HB   sing N N 567 
VAL   CG1 HG11 sing N N 568 
VAL   CG1 HG12 sing N N 569 
VAL   CG1 HG13 sing N N 570 
VAL   CG2 HG21 sing N N 571 
VAL   CG2 HG22 sing N N 572 
VAL   CG2 HG23 sing N N 573 
VAL   OXT HXT  sing N N 574 
# 
_pdbx_audit_support.funding_organization   'French Ministry of Armed Forces' 
_pdbx_audit_support.country                France 
_pdbx_audit_support.grant_number           NBC-5-C-2316 
_pdbx_audit_support.ordinal                1 
# 
loop_
_pdbx_entity_branch_list.entity_id 
_pdbx_entity_branch_list.comp_id 
_pdbx_entity_branch_list.num 
_pdbx_entity_branch_list.hetero 
2 NAG 1 n 
2 FUC 2 n 
3 NAG 1 n 
3 NAG 2 n 
3 FUC 3 n 
# 
_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   1p0i 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'I 4 2 2' 
_space_group.name_Hall        'I 4 2' 
_space_group.IT_number        97 
_space_group.crystal_system   tetragonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    9EWU 
_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]   0.006468 
_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]   0.006468 
_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]   0.007781 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . ILE   A 1  4   ? 34.63349  18.52530 15.49218 1.000 81.04105  ? 4   ILE   A N   1 
ATOM   2    C CA  . ILE   A 1  4   ? 33.52073  17.57801 15.58250 1.000 97.59140  ? 4   ILE   A CA  1 
ATOM   3    C C   . ILE   A 1  4   ? 32.19174  18.23154 15.19358 1.000 91.45491  ? 4   ILE   A C   1 
ATOM   4    O O   . ILE   A 1  4   ? 31.79138  19.24026 15.76399 1.000 85.83702  ? 4   ILE   A O   1 
ATOM   5    C CB  . ILE   A 1  4   ? 33.42876  16.95295 16.99866 1.000 100.65189 ? 4   ILE   A CB  1 
ATOM   6    C CG1 . ILE   A 1  4   ? 34.83514  16.64369 17.53411 1.000 106.90939 ? 4   ILE   A CG1 1 
ATOM   7    C CG2 . ILE   A 1  4   ? 32.52320  15.70505 16.99707 1.000 97.41684  ? 4   ILE   A CG2 1 
ATOM   8    C CD1 . ILE   A 1  4   ? 34.86867  15.71760 18.74646 1.000 95.52148  ? 4   ILE   A CD1 1 
ATOM   9    N N   . ILE   A 1  5   ? 31.50472  17.63614 14.22242 1.000 85.99733  ? 5   ILE   A N   1 
ATOM   10   C CA  . ILE   A 1  5   ? 30.25358  18.16148 13.69141 1.000 78.52383  ? 5   ILE   A CA  1 
ATOM   11   C C   . ILE   A 1  5   ? 29.12786  17.21053 14.07592 1.000 83.52511  ? 5   ILE   A C   1 
ATOM   12   O O   . ILE   A 1  5   ? 29.28328  15.98281 14.01326 1.000 86.71054  ? 5   ILE   A O   1 
ATOM   13   C CB  . ILE   A 1  5   ? 30.34187  18.33816 12.16356 1.000 75.32512  ? 5   ILE   A CB  1 
ATOM   14   C CG1 . ILE   A 1  5   ? 30.96409  19.68450 11.82751 1.000 81.23761  ? 5   ILE   A CG1 1 
ATOM   15   C CG2 . ILE   A 1  5   ? 28.98035  18.24556 11.50807 1.000 73.84456  ? 5   ILE   A CG2 1 
ATOM   16   C CD1 . ILE   A 1  5   ? 31.66135  19.66750 10.49740 1.000 85.70289  ? 5   ILE   A CD1 1 
ATOM   17   N N   . ILE   A 1  6   ? 27.99401  17.77242 14.47975 1.000 72.07935  ? 6   ILE   A N   1 
ATOM   18   C CA  . ILE   A 1  6   ? 26.84719  16.98099 14.90251 1.000 77.13124  ? 6   ILE   A CA  1 
ATOM   19   C C   . ILE   A 1  6   ? 25.65198  17.38446 14.05486 1.000 77.48064  ? 6   ILE   A C   1 
ATOM   20   O O   . ILE   A 1  6   ? 25.33283  18.57422 13.95306 1.000 80.61083  ? 6   ILE   A O   1 
ATOM   21   C CB  . ILE   A 1  6   ? 26.53888  17.17729 16.39883 1.000 77.34968  ? 6   ILE   A CB  1 
ATOM   22   C CG1 . ILE   A 1  6   ? 27.70079  16.68278 17.26558 1.000 75.61954  ? 6   ILE   A CG1 1 
ATOM   23   C CG2 . ILE   A 1  6   ? 25.24740  16.46011 16.76627 1.000 72.16135  ? 6   ILE   A CG2 1 
ATOM   24   C CD1 . ILE   A 1  6   ? 27.70030  15.20630 17.50055 1.000 71.83569  ? 6   ILE   A CD1 1 
ATOM   25   N N   . ALA   A 1  7   ? 24.99037  16.39769 13.46050 1.000 76.48891  ? 7   ALA   A N   1 
ATOM   26   C CA  . ALA   A 1  7   ? 23.75034  16.63364 12.73747 1.000 73.75283  ? 7   ALA   A CA  1 
ATOM   27   C C   . ALA   A 1  7   ? 22.60483  16.78061 13.72702 1.000 76.57658  ? 7   ALA   A C   1 
ATOM   28   O O   . ALA   A 1  7   ? 22.38598  15.90158 14.55973 1.000 76.90518  ? 7   ALA   A O   1 
ATOM   29   C CB  . ALA   A 1  7   ? 23.46089  15.47864 11.77991 1.000 68.34887  ? 7   ALA   A CB  1 
ATOM   30   N N   . THR   A 1  8   ? 21.88026  17.88970 13.64627 1.000 80.01511  ? 8   THR   A N   1 
ATOM   31   C CA  . THR   A 1  8   ? 20.65666  18.08308 14.41086 1.000 77.89492  ? 8   THR   A CA  1 
ATOM   32   C C   . THR   A 1  8   ? 19.46360  17.97359 13.47231 1.000 82.35452  ? 8   THR   A C   1 
ATOM   33   O O   . THR   A 1  8   ? 19.61304  17.74763 12.26799 1.000 82.54811  ? 8   THR   A O   1 
ATOM   34   C CB  . THR   A 1  8   ? 20.66386  19.42776 15.14458 1.000 76.50830  ? 8   THR   A CB  1 
ATOM   35   O OG1 . THR   A 1  8   ? 20.20644  20.47167 14.26382 1.000 77.01175  ? 8   THR   A OG1 1 
ATOM   36   C CG2 . THR   A 1  8   ? 22.05524  19.73267 15.66631 1.000 72.09292  ? 8   THR   A CG2 1 
ATOM   37   N N   . LYS   A 1  9   ? 18.26405  18.14456 14.03183 1.000 78.10378  ? 9   LYS   A N   1 
ATOM   38   C CA  . LYS   A 1  9   ? 17.07350  17.96531 13.21551 1.000 82.22350  ? 9   LYS   A CA  1 
ATOM   39   C C   . LYS   A 1  9   ? 16.92145  19.05399 12.15817 1.000 85.72225  ? 9   LYS   A C   1 
ATOM   40   O O   . LYS   A 1  9   ? 16.25127  18.81592 11.14927 1.000 88.92222  ? 9   LYS   A O   1 
ATOM   41   C CB  . LYS   A 1  9   ? 15.83549  17.87886 14.10808 1.000 83.48968  ? 9   LYS   A CB  1 
ATOM   42   C CG  . LYS   A 1  9   ? 15.76215  16.55735 14.87739 1.000 86.96394  ? 9   LYS   A CG  1 
ATOM   43   C CD  . LYS   A 1  9   ? 14.33983  16.13225 15.18002 1.000 90.11864  ? 9   LYS   A CD  1 
ATOM   44   C CE  . LYS   A 1  9   ? 14.31402  14.73782 15.80733 1.000 93.34926  ? 9   LYS   A CE  1 
ATOM   45   N NZ  . LYS   A 1  9   ? 15.32953  13.83440 15.18350 1.000 98.41598  ? 9   LYS   A NZ  1 
ATOM   46   N N   . ASN   A 1  10  ? 17.56107  20.21553 12.33347 1.000 85.76812  ? 10  ASN   A N   1 
ATOM   47   C CA  . ASN   A 1  10  ? 17.49791  21.29764 11.35208 1.000 91.51798  ? 10  ASN   A CA  1 
ATOM   48   C C   . ASN   A 1  10  ? 18.82204  21.58675 10.65510 1.000 90.05253  ? 10  ASN   A C   1 
ATOM   49   O O   . ASN   A 1  10  ? 18.88677  22.53597 9.86731  1.000 92.25559  ? 10  ASN   A O   1 
ATOM   50   C CB  . ASN   A 1  10  ? 17.00488  22.59316 12.00557 1.000 95.53604  ? 10  ASN   A CB  1 
ATOM   51   C CG  . ASN   A 1  10  ? 15.72346  22.40255 12.77088 1.000 94.19454  ? 10  ASN   A CG  1 
ATOM   52   O OD1 . ASN   A 1  10  ? 15.70753  21.76154 13.82173 1.000 90.12436  ? 10  ASN   A OD1 1 
ATOM   53   N ND2 . ASN   A 1  10  ? 14.63031  22.94227 12.24025 1.000 101.62947 ? 10  ASN   A ND2 1 
ATOM   54   N N   . GLY   A 1  11  ? 19.87357  20.83418 10.92621 1.000 86.19935  ? 11  GLY   A N   1 
ATOM   55   C CA  . GLY   A 1  11  ? 21.11344  21.03041 10.19965 1.000 86.29687  ? 11  GLY   A CA  1 
ATOM   56   C C   . GLY   A 1  11  ? 22.32076  20.70361 11.05229 1.000 82.98610  ? 11  GLY   A C   1 
ATOM   57   O O   . GLY   A 1  11  ? 22.22561  20.44915 12.25029 1.000 80.25781  ? 11  GLY   A O   1 
ATOM   58   N N   . LYS   A 1  12  ? 23.47838  20.72140 10.39707 1.000 80.18998  ? 12  LYS   A N   1 
ATOM   59   C CA  . LYS   A 1  12  ? 24.73806  20.46865 11.08137 1.000 82.72368  ? 12  LYS   A CA  1 
ATOM   60   C C   . LYS   A 1  12  ? 25.19773  21.69507 11.86486 1.000 80.03534  ? 12  LYS   A C   1 
ATOM   61   O O   . LYS   A 1  12  ? 25.06726  22.83795 11.41133 1.000 81.10321  ? 12  LYS   A O   1 
ATOM   62   C CB  . LYS   A 1  12  ? 25.82697  20.05247 10.08703 1.000 87.78168  ? 12  LYS   A CB  1 
ATOM   63   C CG  . LYS   A 1  12  ? 25.40515  19.03439 9.01935  1.000 85.40664  ? 12  LYS   A CG  1 
ATOM   64   C CD  . LYS   A 1  12  ? 26.64725  18.35758 8.41065  1.000 90.72255  ? 12  LYS   A CD  1 
ATOM   65   C CE  . LYS   A 1  12  ? 26.50463  16.83578 8.22295  1.000 88.37715  ? 12  LYS   A CE  1 
ATOM   66   N NZ  . LYS   A 1  12  ? 26.03354  16.46787 6.84884  1.000 89.84915  ? 12  LYS   A NZ  1 
ATOM   67   N N   . VAL   A 1  13  ? 25.73083  21.44550 13.05452 1.000 76.97544  ? 13  VAL   A N   1 
ATOM   68   C CA  . VAL   A 1  13  ? 26.35454  22.46996 13.87667 1.000 78.32118  ? 13  VAL   A CA  1 
ATOM   69   C C   . VAL   A 1  13  ? 27.79054  22.04376 14.14876 1.000 77.34668  ? 13  VAL   A C   1 
ATOM   70   O O   . VAL   A 1  13  ? 28.07187  20.85618 14.34397 1.000 79.69152  ? 13  VAL   A O   1 
ATOM   71   C CB  . VAL   A 1  13  ? 25.58202  22.70966 15.19520 1.000 74.71753  ? 13  VAL   A CB  1 
ATOM   72   C CG1 . VAL   A 1  13  ? 24.12556  23.09470 14.90644 1.000 71.49482  ? 13  VAL   A CG1 1 
ATOM   73   C CG2 . VAL   A 1  13  ? 25.64846  21.49724 16.08905 1.000 70.67372  ? 13  VAL   A CG2 1 
ATOM   74   N N   . ARG   A 1  14  ? 28.69991  23.01473 14.13587 1.000 79.68771  ? 14  ARG   A N   1 
ATOM   75   C CA  . ARG   A 1  14  ? 30.11383  22.79057 14.41312 1.000 78.00077  ? 14  ARG   A CA  1 
ATOM   76   C C   . ARG   A 1  14  ? 30.44486  23.27318 15.82027 1.000 74.25880  ? 14  ARG   A C   1 
ATOM   77   O O   . ARG   A 1  14  ? 30.08721  24.39495 16.19898 1.000 72.27402  ? 14  ARG   A O   1 
ATOM   78   C CB  . ARG   A 1  14  ? 30.98723  23.51817 13.39102 1.000 78.25029  ? 14  ARG   A CB  1 
ATOM   79   C CG  . ARG   A 1  14  ? 32.47214  23.57853 13.74491 1.000 81.63392  ? 14  ARG   A CG  1 
ATOM   80   C CD  . ARG   A 1  14  ? 33.25195  24.33421 12.66316 1.000 88.87651  ? 14  ARG   A CD  1 
ATOM   81   N NE  . ARG   A 1  14  ? 33.49854  23.47278 11.51498 1.000 95.28698  ? 14  ARG   A NE  1 
ATOM   82   C CZ  . ARG   A 1  14  ? 32.97630  23.65708 10.30993 1.000 94.75364  ? 14  ARG   A CZ  1 
ATOM   83   N NH1 . ARG   A 1  14  ? 32.23829  24.72073 10.02930 1.000 91.91889  ? 14  ARG   A NH1 1 
ATOM   84   N NH2 . ARG   A 1  14  ? 33.19522  22.74672 9.36416  1.000 98.32752  ? 14  ARG   A NH2 1 
ATOM   85   N N   . GLY   A 1  15  ? 31.13305  22.42668 16.58640 1.000 73.20784  ? 15  GLY   A N   1 
ATOM   86   C CA  . GLY   A 1  15  ? 31.55766  22.76060 17.92596 1.000 68.99043  ? 15  GLY   A CA  1 
ATOM   87   C C   . GLY   A 1  15  ? 33.03023  23.13711 18.00155 1.000 78.07520  ? 15  GLY   A C   1 
ATOM   88   O O   . GLY   A 1  15  ? 33.73722  23.27087 16.99858 1.000 74.94702  ? 15  GLY   A O   1 
ATOM   89   N N   . MET   A 1  16  ? 33.48820  23.31979 19.23383 1.000 76.52153  ? 16  MET   A N   1 
ATOM   90   C CA  . MET   A 1  16  ? 34.88082  23.61122 19.52783 1.000 79.02287  ? 16  MET   A CA  1 
ATOM   91   C C   . MET   A 1  16  ? 35.30697  22.75230 20.71316 1.000 79.20697  ? 16  MET   A C   1 
ATOM   92   O O   . MET   A 1  16  ? 34.47466  22.29424 21.50323 1.000 81.55001  ? 16  MET   A O   1 
ATOM   93   C CB  . MET   A 1  16  ? 35.08550  25.10917 19.82474 1.000 77.68724  ? 16  MET   A CB  1 
ATOM   94   C CG  . MET   A 1  16  ? 34.70589  25.50919 21.23478 1.000 76.63021  ? 16  MET   A CG  1 
ATOM   95   S SD  . MET   A 1  16  ? 34.43548  27.27258 21.38110 1.000 92.70545  ? 16  MET   A SD  1 
ATOM   96   C CE  . MET   A 1  16  ? 36.03911  27.81253 21.97819 1.000 91.04617  ? 16  MET   A CE  1 
ATOM   97   N N   . GLN   A 1  17  ? 36.61150  22.53304 20.83853 1.000 77.50106  ? 17  GLN   A N   1 
ATOM   98   C CA  . GLN   A 1  17  ? 37.14995  21.63002 21.84759 1.000 79.53474  ? 17  GLN   A CA  1 
ATOM   99   C C   . GLN   A 1  17  ? 37.84966  22.41830 22.94076 1.000 77.19634  ? 17  GLN   A C   1 
ATOM   100  O O   . GLN   A 1  17  ? 38.74207  23.22274 22.65961 1.000 76.89808  ? 17  GLN   A O   1 
ATOM   101  C CB  . GLN   A 1  17  ? 38.10694  20.61778 21.21837 1.000 83.88142  ? 17  GLN   A CB  1 
ATOM   102  C CG  . GLN   A 1  17  ? 37.42062  19.30908 20.83761 1.000 93.63308  ? 17  GLN   A CG  1 
ATOM   103  C CD  . GLN   A 1  17  ? 38.38033  18.31156 20.21881 1.000 106.41851 ? 17  GLN   A CD  1 
ATOM   104  O OE1 . GLN   A 1  17  ? 39.59537  18.52798 20.20567 1.000 106.69349 ? 17  GLN   A OE1 1 
ATOM   105  N NE2 . GLN   A 1  17  ? 37.83868  17.21351 19.69236 1.000 111.63252 ? 17  GLN   A NE2 1 
ATOM   106  N N   . LEU   A 1  18  ? 37.45269  22.17478 24.18248 1.000 73.30683  ? 18  LEU   A N   1 
ATOM   107  C CA  . LEU   A 1  18  ? 38.02107  22.86094 25.33046 1.000 72.36310  ? 18  LEU   A CA  1 
ATOM   108  C C   . LEU   A 1  18  ? 38.97169  21.92859 26.07022 1.000 75.77241  ? 18  LEU   A C   1 
ATOM   109  O O   . LEU   A 1  18  ? 38.77459  20.71332 26.09229 1.000 78.75493  ? 18  LEU   A O   1 
ATOM   110  C CB  . LEU   A 1  18  ? 36.91359  23.34117 26.27152 1.000 70.11801  ? 18  LEU   A CB  1 
ATOM   111  C CG  . LEU   A 1  18  ? 35.74521  24.12091 25.63666 1.000 80.71694  ? 18  LEU   A CG  1 
ATOM   112  C CD1 . LEU   A 1  18  ? 34.79753  24.73934 26.68622 1.000 70.41958  ? 18  LEU   A CD1 1 
ATOM   113  C CD2 . LEU   A 1  18  ? 36.25965  25.20421 24.66588 1.000 76.93806  ? 18  LEU   A CD2 1 
ATOM   114  N N   . THR   A 1  19  ? 40.01501  22.50421 26.66539 1.000 72.01757  ? 19  THR   A N   1 
ATOM   115  C CA  . THR   A 1  19  ? 40.91357  21.77599 27.55652 1.000 75.58682  ? 19  THR   A CA  1 
ATOM   116  C C   . THR   A 1  19  ? 40.51894  22.07343 28.99924 1.000 75.32827  ? 19  THR   A C   1 
ATOM   117  O O   . THR   A 1  19  ? 40.59711  23.22312 29.43569 1.000 76.56313  ? 19  THR   A O   1 
ATOM   118  C CB  . THR   A 1  19  ? 42.37040  22.16827 27.30771 1.000 78.89133  ? 19  THR   A CB  1 
ATOM   119  O OG1 . THR   A 1  19  ? 42.56795  22.42145 25.91187 1.000 89.62764  ? 19  THR   A OG1 1 
ATOM   120  C CG2 . THR   A 1  19  ? 43.31861  21.07732 27.76604 1.000 78.03428  ? 19  THR   A CG2 1 
ATOM   121  N N   . VAL   A 1  20  ? 40.07826  21.04547 29.72478 1.000 76.52415  ? 20  VAL   A N   1 
ATOM   122  C CA  . VAL   A 1  20  ? 39.63138  21.16964 31.11318 1.000 77.81828  ? 20  VAL   A CA  1 
ATOM   123  C C   . VAL   A 1  20  ? 40.27663  20.06260 31.92381 1.000 78.89522  ? 20  VAL   A C   1 
ATOM   124  O O   . VAL   A 1  20  ? 39.98562  18.88142 31.69559 1.000 80.24050  ? 20  VAL   A O   1 
ATOM   125  C CB  . VAL   A 1  20  ? 38.09646  21.08544 31.26794 1.000 76.16907  ? 20  VAL   A CB  1 
ATOM   126  C CG1 . VAL   A 1  20  ? 37.66707  21.66528 32.61259 1.000 69.67688  ? 20  VAL   A CG1 1 
ATOM   127  C CG2 . VAL   A 1  20  ? 37.38066  21.77879 30.12355 1.000 65.85706  ? 20  VAL   A CG2 1 
ATOM   128  N N   . PHE   A 1  21  ? 41.12536  20.44126 32.87922 1.000 81.81504  ? 21  PHE   A N   1 
ATOM   129  C CA  . PHE   A 1  21  ? 41.75644  19.51161 33.81438 1.000 76.60573  ? 21  PHE   A CA  1 
ATOM   130  C C   . PHE   A 1  21  ? 42.34613  18.30787 33.07977 1.000 73.07898  ? 21  PHE   A C   1 
ATOM   131  O O   . PHE   A 1  21  ? 41.83627  17.19664 33.16964 1.000 74.27423  ? 21  PHE   A O   1 
ATOM   132  C CB  . PHE   A 1  21  ? 40.75549  19.02005 34.86589 1.000 76.22452  ? 21  PHE   A CB  1 
ATOM   133  C CG  . PHE   A 1  21  ? 40.03212  20.11240 35.60188 1.000 73.42861  ? 21  PHE   A CG  1 
ATOM   134  C CD1 . PHE   A 1  21  ? 40.66140  21.30188 35.92357 1.000 79.09080  ? 21  PHE   A CD1 1 
ATOM   135  C CD2 . PHE   A 1  21  ? 38.71844  19.92947 36.00275 1.000 77.19174  ? 21  PHE   A CD2 1 
ATOM   136  C CE1 . PHE   A 1  21  ? 39.98254  22.30411 36.61947 1.000 75.84916  ? 21  PHE   A CE1 1 
ATOM   137  C CE2 . PHE   A 1  21  ? 38.03038  20.93353 36.69708 1.000 78.38884  ? 21  PHE   A CE2 1 
ATOM   138  C CZ  . PHE   A 1  21  ? 38.67738  22.12113 37.00647 1.000 74.57105  ? 21  PHE   A CZ  1 
ATOM   139  N N   . GLY   A 1  22  ? 43.42598  18.55901 32.34218 1.000 80.46553  ? 22  GLY   A N   1 
ATOM   140  C CA  . GLY   A 1  22  ? 44.06031  17.50746 31.56307 1.000 75.70673  ? 22  GLY   A CA  1 
ATOM   141  C C   . GLY   A 1  22  ? 43.10073  16.58422 30.82681 1.000 78.83977  ? 22  GLY   A C   1 
ATOM   142  O O   . GLY   A 1  22  ? 43.34697  15.37908 30.70931 1.000 85.74035  ? 22  GLY   A O   1 
ATOM   143  N N   . GLY   A 1  23  ? 41.98556  17.13823 30.35489 1.000 79.08245  ? 23  GLY   A N   1 
ATOM   144  C CA  . GLY   A 1  23  ? 40.96217  16.39670 29.63985 1.000 75.88098  ? 23  GLY   A CA  1 
ATOM   145  C C   . GLY   A 1  23  ? 40.26029  17.31961 28.66284 1.000 82.96003  ? 23  GLY   A C   1 
ATOM   146  O O   . GLY   A 1  23  ? 40.73613  18.43423 28.43708 1.000 88.96767  ? 23  GLY   A O   1 
ATOM   147  N N   . THR   A 1  24  ? 39.12624  16.90643 28.09825 1.000 80.35441  ? 24  THR   A N   1 
ATOM   148  C CA  . THR   A 1  24  ? 38.50504  17.64868 27.00736 1.000 72.09240  ? 24  THR   A CA  1 
ATOM   149  C C   . THR   A 1  24  ? 36.99205  17.68734 27.17192 1.000 75.28406  ? 24  THR   A C   1 
ATOM   150  O O   . THR   A 1  24  ? 36.36677  16.66394 27.46433 1.000 71.88662  ? 24  THR   A O   1 
ATOM   151  C CB  . THR   A 1  24  ? 38.87057  17.02420 25.65229 1.000 75.21003  ? 24  THR   A CB  1 
ATOM   152  O OG1 . THR   A 1  24  ? 40.29457  17.05131 25.48422 1.000 79.41654  ? 24  THR   A OG1 1 
ATOM   153  C CG2 . THR   A 1  24  ? 38.21428  17.77309 24.50431 1.000 74.96172  ? 24  THR   A CG2 1 
ATOM   154  N N   . VAL   A 1  25  ? 36.40855  18.87221 26.98850 1.000 71.32263  ? 25  VAL   A N   1 
ATOM   155  C CA  . VAL   A 1  25  ? 34.96519  19.03466 26.87340 1.000 74.81703  ? 25  VAL   A CA  1 
ATOM   156  C C   . VAL   A 1  25  ? 34.68924  19.62040 25.49789 1.000 72.60744  ? 25  VAL   A C   1 
ATOM   157  O O   . VAL   A 1  25  ? 35.46944  20.43751 25.00543 1.000 72.80038  ? 25  VAL   A O   1 
ATOM   158  C CB  . VAL   A 1  25  ? 34.38830  19.92492 27.99696 1.000 63.52999  ? 25  VAL   A CB  1 
ATOM   159  C CG1 . VAL   A 1  25  ? 32.93002  20.22866 27.73732 1.000 67.57120  ? 25  VAL   A CG1 1 
ATOM   160  C CG2 . VAL   A 1  25  ? 34.53610  19.23245 29.33705 1.000 63.66851  ? 25  VAL   A CG2 1 
ATOM   161  N N   . THR   A 1  26  ? 33.61957  19.16093 24.85468 1.000 73.00288  ? 26  THR   A N   1 
ATOM   162  C CA  . THR   A 1  26  ? 33.21075  19.68380 23.55770 1.000 74.25259  ? 26  THR   A CA  1 
ATOM   163  C C   . THR   A 1  26  ? 32.06439  20.66510 23.78549 1.000 68.17447  ? 26  THR   A C   1 
ATOM   164  O O   . THR   A 1  26  ? 31.03761  20.29667 24.35778 1.000 60.26618  ? 26  THR   A O   1 
ATOM   165  C CB  . THR   A 1  26  ? 32.79000  18.55573 22.61313 1.000 70.98287  ? 26  THR   A CB  1 
ATOM   166  O OG1 . THR   A 1  26  ? 33.85669  17.61102 22.48950 1.000 77.62005  ? 26  THR   A OG1 1 
ATOM   167  C CG2 . THR   A 1  26  ? 32.47104  19.10613 21.24205 1.000 68.69707  ? 26  THR   A CG2 1 
ATOM   168  N N   . ALA   A 1  27  ? 32.24974  21.91462 23.36166 1.000 69.42139  ? 27  ALA   A N   1 
ATOM   169  C CA  . ALA   A 1  27  ? 31.28145  22.97053 23.62173 1.000 65.54453  ? 27  ALA   A CA  1 
ATOM   170  C C   . ALA   A 1  27  ? 30.63093  23.40725 22.31913 1.000 65.10318  ? 27  ALA   A C   1 
ATOM   171  O O   . ALA   A 1  27  ? 31.30794  23.57307 21.29920 1.000 68.95214  ? 27  ALA   A O   1 
ATOM   172  C CB  . ALA   A 1  27  ? 31.92625  24.16500 24.32297 1.000 62.20400  ? 27  ALA   A CB  1 
ATOM   173  N N   . PHE   A 1  28  ? 29.31425  23.53008 22.35162 1.000 59.77286  ? 28  PHE   A N   1 
ATOM   174  C CA  . PHE   A 1  28  ? 28.52060  24.07543 21.25770 1.000 68.76889  ? 28  PHE   A CA  1 
ATOM   175  C C   . PHE   A 1  28  ? 27.90046  25.35010 21.81611 1.000 68.24105  ? 28  PHE   A C   1 
ATOM   176  O O   . PHE   A 1  28  ? 26.97179  25.28556 22.62945 1.000 66.10728  ? 28  PHE   A O   1 
ATOM   177  C CB  . PHE   A 1  28  ? 27.45969  23.08059 20.78439 1.000 66.87048  ? 28  PHE   A CB  1 
ATOM   178  C CG  . PHE   A 1  28  ? 28.03800  21.85428 20.13928 1.000 67.45982  ? 28  PHE   A CG  1 
ATOM   179  C CD1 . PHE   A 1  28  ? 28.43786  20.76628 20.91606 1.000 68.56977  ? 28  PHE   A CD1 1 
ATOM   180  C CD2 . PHE   A 1  28  ? 28.20032  21.79323 18.76327 1.000 64.50754  ? 28  PHE   A CD2 1 
ATOM   181  C CE1 . PHE   A 1  28  ? 28.98974  19.62898 20.32809 1.000 72.03883  ? 28  PHE   A CE1 1 
ATOM   182  C CE2 . PHE   A 1  28  ? 28.74908  20.66488 18.16267 1.000 72.11489  ? 28  PHE   A CE2 1 
ATOM   183  C CZ  . PHE   A 1  28  ? 29.14835  19.57542 18.94628 1.000 70.80470  ? 28  PHE   A CZ  1 
ATOM   184  N N   . LEU   A 1  29  ? 28.43427  26.50005 21.41853 1.000 62.60852  ? 29  LEU   A N   1 
ATOM   185  C CA  . LEU   A 1  29  ? 27.98436  27.77761 21.94541 1.000 66.08159  ? 29  LEU   A CA  1 
ATOM   186  C C   . LEU   A 1  29  ? 27.16070  28.50082 20.88382 1.000 66.04729  ? 29  LEU   A C   1 
ATOM   187  O O   . LEU   A 1  29  ? 27.61962  28.69534 19.75319 1.000 63.77792  ? 29  LEU   A O   1 
ATOM   188  C CB  . LEU   A 1  29  ? 29.17787  28.62608 22.39753 1.000 65.74914  ? 29  LEU   A CB  1 
ATOM   189  C CG  . LEU   A 1  29  ? 30.13739  28.01307 23.43948 1.000 62.57145  ? 29  LEU   A CG  1 
ATOM   190  C CD1 . LEU   A 1  29  ? 31.17137  29.01780 23.84182 1.000 60.44744  ? 29  LEU   A CD1 1 
ATOM   191  C CD2 . LEU   A 1  29  ? 29.41114  27.50644 24.67789 1.000 63.86602  ? 29  LEU   A CD2 1 
ATOM   192  N N   . GLY   A 1  30  ? 25.94210  28.88214 21.24589 1.000 62.62476  ? 30  GLY   A N   1 
ATOM   193  C CA  . GLY   A 1  30  ? 25.10114  29.66227 20.36115 1.000 59.04347  ? 30  GLY   A CA  1 
ATOM   194  C C   . GLY   A 1  30  ? 24.42776  28.86276 19.26718 1.000 64.74609  ? 30  GLY   A C   1 
ATOM   195  O O   . GLY   A 1  30  ? 24.61445  29.15517 18.08207 1.000 66.59776  ? 30  GLY   A O   1 
ATOM   196  N N   . ILE   A 1  31  ? 23.66265  27.83797 19.64174 1.000 66.63117  ? 31  ILE   A N   1 
ATOM   197  C CA  . ILE   A 1  31  ? 22.81402  27.14133 18.67792 1.000 64.75178  ? 31  ILE   A CA  1 
ATOM   198  C C   . ILE   A 1  31  ? 21.47466  27.86713 18.67748 1.000 65.20620  ? 31  ILE   A C   1 
ATOM   199  O O   . ILE   A 1  31  ? 20.90289  28.08848 19.75373 1.000 66.17321  ? 31  ILE   A O   1 
ATOM   200  C CB  . ILE   A 1  31  ? 22.61841  25.65203 19.01452 1.000 67.66536  ? 31  ILE   A CB  1 
ATOM   201  C CG1 . ILE   A 1  31  ? 23.93403  24.89865 19.19951 1.000 66.92038  ? 31  ILE   A CG1 1 
ATOM   202  C CG2 . ILE   A 1  31  ? 21.81530  24.96402 17.92071 1.000 68.10180  ? 31  ILE   A CG2 1 
ATOM   203  C CD1 . ILE   A 1  31  ? 23.70007  23.44515 19.62663 1.000 60.31846  ? 31  ILE   A CD1 1 
ATOM   204  N N   . PRO   A 1  32  ? 20.93158  28.24647 17.52449 1.000 66.73019  ? 32  PRO   A N   1 
ATOM   205  C CA  . PRO   A 1  32  ? 19.60452  28.86495 17.52392 1.000 66.20755  ? 32  PRO   A CA  1 
ATOM   206  C C   . PRO   A 1  32  ? 18.53588  27.81872 17.77217 1.000 66.54716  ? 32  PRO   A C   1 
ATOM   207  O O   . PRO   A 1  32  ? 18.63129  26.69095 17.29113 1.000 64.31760  ? 32  PRO   A O   1 
ATOM   208  C CB  . PRO   A 1  32  ? 19.48897  29.45376 16.11597 1.000 68.70803  ? 32  PRO   A CB  1 
ATOM   209  C CG  . PRO   A 1  32  ? 20.32225  28.52689 15.27517 1.000 69.50196  ? 32  PRO   A CG  1 
ATOM   210  C CD  . PRO   A 1  32  ? 21.47706  28.10850 16.15982 1.000 71.18462  ? 32  PRO   A CD  1 
ATOM   211  N N   . TYR   A 1  33  ? 17.50048  28.20152 18.51913 1.000 68.41520  ? 33  TYR   A N   1 
ATOM   212  C CA  . TYR   A 1  33  ? 16.38867  27.29235 18.75161 1.000 64.71120  ? 33  TYR   A CA  1 
ATOM   213  C C   . TYR   A 1  33  ? 15.03993  27.90086 18.38813 1.000 68.32723  ? 33  TYR   A C   1 
ATOM   214  O O   . TYR   A 1  33  ? 14.00786  27.32555 18.74423 1.000 65.21932  ? 33  TYR   A O   1 
ATOM   215  C CB  . TYR   A 1  33  ? 16.36790  26.80420 20.20531 1.000 57.67772  ? 33  TYR   A CB  1 
ATOM   216  C CG  . TYR   A 1  33  ? 16.02873  27.83749 21.27951 1.000 62.58873  ? 33  TYR   A CG  1 
ATOM   217  C CD1 . TYR   A 1  33  ? 17.02531  28.61233 21.87192 1.000 58.25545  ? 33  TYR   A CD1 1 
ATOM   218  C CD2 . TYR   A 1  33  ? 14.71760  28.00228 21.73266 1.000 61.03089  ? 33  TYR   A CD2 1 
ATOM   219  C CE1 . TYR   A 1  33  ? 16.72411  29.52591 22.86947 1.000 56.30877  ? 33  TYR   A CE1 1 
ATOM   220  C CE2 . TYR   A 1  33  ? 14.40120  28.92778 22.72255 1.000 56.50015  ? 33  TYR   A CE2 1 
ATOM   221  C CZ  . TYR   A 1  33  ? 15.41085  29.67701 23.29398 1.000 57.61906  ? 33  TYR   A CZ  1 
ATOM   222  O OH  . TYR   A 1  33  ? 15.10748  30.57875 24.28401 1.000 51.78081  ? 33  TYR   A OH  1 
ATOM   223  N N   . ALA   A 1  34  ? 15.01181  29.02578 17.67672 1.000 66.66921  ? 34  ALA   A N   1 
ATOM   224  C CA  . ALA   A 1  34  ? 13.74101  29.61077 17.26352 1.000 69.97095  ? 34  ALA   A CA  1 
ATOM   225  C C   . ALA   A 1  34  ? 14.00403  30.68713 16.21867 1.000 70.71995  ? 34  ALA   A C   1 
ATOM   226  O O   . ALA   A 1  34  ? 15.11129  31.22624 16.12557 1.000 70.26822  ? 34  ALA   A O   1 
ATOM   227  C CB  . ALA   A 1  34  ? 12.98214  30.18760 18.47252 1.000 61.19089  ? 34  ALA   A CB  1 
ATOM   228  N N   . GLN   A 1  35  ? 12.97880  30.99945 15.43614 1.000 71.34935  ? 35  GLN   A N   1 
ATOM   229  C CA  . GLN   A 1  35  ? 13.06825  32.18449 14.59751 1.000 72.56709  ? 35  GLN   A CA  1 
ATOM   230  C C   . GLN   A 1  35  ? 13.35432  33.40011 15.46517 1.000 69.85529  ? 35  GLN   A C   1 
ATOM   231  O O   . GLN   A 1  35  ? 12.72499  33.56412 16.51920 1.000 70.30809  ? 35  GLN   A O   1 
ATOM   232  C CB  . GLN   A 1  35  ? 11.79464  32.44414 13.80225 1.000 70.38219  ? 35  GLN   A CB  1 
ATOM   233  C CG  . GLN   A 1  35  ? 11.85809  31.99911 12.36004 1.000 81.59356  ? 35  GLN   A CG  1 
ATOM   234  C CD  . GLN   A 1  35  ? 10.48265  31.70954 11.81344 1.000 92.19747  ? 35  GLN   A CD  1 
ATOM   235  O OE1 . GLN   A 1  35  ? 9.97672   30.57905 11.87583 1.000 90.84506  ? 35  GLN   A OE1 1 
ATOM   236  N NE2 . GLN   A 1  35  ? 9.83756   32.75827 11.31128 1.000 86.18059  ? 35  GLN   A NE2 1 
ATOM   237  N N   . PRO   A 1  36  ? 14.28160  34.25978 15.07102 1.000 70.82777  ? 36  PRO   A N   1 
ATOM   238  C CA  . PRO   A 1  36  ? 14.47834  35.51828 15.78075 1.000 68.26467  ? 36  PRO   A CA  1 
ATOM   239  C C   . PRO   A 1  36  ? 13.15937  36.24996 15.94577 1.000 67.61877  ? 36  PRO   A C   1 
ATOM   240  O O   . PRO   A 1  36  ? 12.40525  36.42394 14.97481 1.000 70.09055  ? 36  PRO   A O   1 
ATOM   241  C CB  . PRO   A 1  36  ? 15.44263  36.28432 14.86468 1.000 64.41329  ? 36  PRO   A CB  1 
ATOM   242  C CG  . PRO   A 1  36  ? 16.19984  35.21935 14.16595 1.000 60.55155  ? 36  PRO   A CG  1 
ATOM   243  C CD  . PRO   A 1  36  ? 15.23260  34.08399 13.95980 1.000 66.14066  ? 36  PRO   A CD  1 
ATOM   244  N N   . PRO   A 1  37  ? 12.81372  36.65032 17.16255 1.000 68.38783  ? 37  PRO   A N   1 
ATOM   245  C CA  . PRO   A 1  37  ? 11.49086  37.26794 17.37991 1.000 65.44939  ? 37  PRO   A CA  1 
ATOM   246  C C   . PRO   A 1  37  ? 11.49741  38.75410 17.05131 1.000 65.06795  ? 37  PRO   A C   1 
ATOM   247  O O   . PRO   A 1  37  ? 11.28559  39.60222 17.91399 1.000 67.87962  ? 37  PRO   A O   1 
ATOM   248  C CB  . PRO   A 1  37  ? 11.24051  36.98770 18.87155 1.000 65.39726  ? 37  PRO   A CB  1 
ATOM   249  C CG  . PRO   A 1  37  ? 12.62898  36.97985 19.49349 1.000 66.01922  ? 37  PRO   A CG  1 
ATOM   250  C CD  . PRO   A 1  37  ? 13.57837  36.48439 18.41655 1.000 65.12057  ? 37  PRO   A CD  1 
ATOM   251  N N   . LEU   A 1  38  ? 11.77401  39.07592 15.78561 1.000 69.70183  ? 38  LEU   A N   1 
ATOM   252  C CA  . LEU   A 1  38  ? 11.89342  40.44749 15.30624 1.000 66.68784  ? 38  LEU   A CA  1 
ATOM   253  C C   . LEU   A 1  38  ? 10.72388  40.84555 14.41736 1.000 72.59131  ? 38  LEU   A C   1 
ATOM   254  O O   . LEU   A 1  38  ? 10.00970  40.00112 13.86836 1.000 74.38021  ? 38  LEU   A O   1 
ATOM   255  C CB  . LEU   A 1  38  ? 13.18192  40.66644 14.50709 1.000 66.19313  ? 38  LEU   A CB  1 
ATOM   256  C CG  . LEU   A 1  38  ? 14.48799  39.96626 14.83655 1.000 74.28696  ? 38  LEU   A CG  1 
ATOM   257  C CD1 . LEU   A 1  38  ? 15.40492  40.07268 13.63723 1.000 74.84094  ? 38  LEU   A CD1 1 
ATOM   258  C CD2 . LEU   A 1  38  ? 15.13701  40.68332 16.01402 1.000 67.11580  ? 38  LEU   A CD2 1 
ATOM   259  N N   . GLY   A 1  39  ? 10.56928  42.16139 14.25265 1.000 71.93837  ? 39  GLY   A N   1 
ATOM   260  C CA  . GLY   A 1  39  ? 9.53881   42.68872 13.36616 1.000 71.15358  ? 39  GLY   A CA  1 
ATOM   261  C C   . GLY   A 1  39  ? 8.15409   42.38729 13.91251 1.000 80.54970  ? 39  GLY   A C   1 
ATOM   262  O O   . GLY   A 1  39  ? 7.85167   42.63786 15.08706 1.000 76.89271  ? 39  GLY   A O   1 
ATOM   263  N N   . ARG   A 1  40  ? 7.29353   41.83271 13.05534 1.000 80.03571  ? 40  ARG   A N   1 
ATOM   264  C CA  . ARG   A 1  40  ? 5.95927   41.41053 13.47637 1.000 78.88912  ? 40  ARG   A CA  1 
ATOM   265  C C   . ARG   A 1  40  ? 5.99059   40.29055 14.51776 1.000 78.96634  ? 40  ARG   A C   1 
ATOM   266  O O   . ARG   A 1  40  ? 4.98105   40.08101 15.19562 1.000 79.39277  ? 40  ARG   A O   1 
ATOM   267  C CB  . ARG   A 1  40  ? 5.13472   40.99362 12.24303 1.000 82.79710  ? 40  ARG   A CB  1 
ATOM   268  C CG  . ARG   A 1  40  ? 5.51734   39.64886 11.60804 1.000 85.78361  ? 40  ARG   A CG  1 
ATOM   269  C CD  . ARG   A 1  40  ? 6.78376   39.73202 10.71179 1.000 94.52467  ? 40  ARG   A CD  1 
ATOM   270  N NE  . ARG   A 1  40  ? 6.76835   40.74920 9.65438  1.000 100.41290 ? 40  ARG   A NE  1 
ATOM   271  C CZ  . ARG   A 1  40  ? 7.74520   41.62253 9.41195  1.000 93.79875  ? 40  ARG   A CZ  1 
ATOM   272  N NH1 . ARG   A 1  40  ? 8.79868   41.72796 10.20419 1.000 85.86949  ? 40  ARG   A NH1 1 
ATOM   273  N NH2 . ARG   A 1  40  ? 7.67058   42.39924 8.33424  1.000 96.41650  ? 40  ARG   A NH2 1 
ATOM   274  N N   . LEU   A 1  41  ? 7.12783   39.60342 14.69312 1.000 76.01160  ? 41  LEU   A N   1 
ATOM   275  C CA  . LEU   A 1  41  ? 7.24935   38.52253 15.66354 1.000 69.73265  ? 41  LEU   A CA  1 
ATOM   276  C C   . LEU   A 1  41  ? 7.53964   39.00696 17.08066 1.000 71.33205  ? 41  LEU   A C   1 
ATOM   277  O O   . LEU   A 1  41  ? 7.44680   38.20568 18.02749 1.000 61.80365  ? 41  LEU   A O   1 
ATOM   278  C CB  . LEU   A 1  41  ? 8.34067   37.54341 15.21432 1.000 67.41820  ? 41  LEU   A CB  1 
ATOM   279  C CG  . LEU   A 1  41  ? 7.92935   36.21960 14.53962 1.000 73.61713  ? 41  LEU   A CG  1 
ATOM   280  C CD1 . LEU   A 1  41  ? 6.65073   36.36733 13.70340 1.000 76.61827  ? 41  LEU   A CD1 1 
ATOM   281  C CD2 . LEU   A 1  41  ? 9.06335   35.64065 13.68141 1.000 71.29007  ? 41  LEU   A CD2 1 
ATOM   282  N N   . ARG   A 1  42  ? 7.89314   40.27953 17.25788 1.000 67.29124  ? 42  ARG   A N   1 
ATOM   283  C CA  . ARG   A 1  42  ? 8.14971   40.78656 18.60096 1.000 70.24238  ? 42  ARG   A CA  1 
ATOM   284  C C   . ARG   A 1  42  ? 6.88184   40.70098 19.44638 1.000 70.65324  ? 42  ARG   A C   1 
ATOM   285  O O   . ARG   A 1  42  ? 5.79333   41.06647 18.98406 1.000 70.85981  ? 42  ARG   A O   1 
ATOM   286  C CB  . ARG   A 1  42  ? 8.65489   42.23428 18.53789 1.000 71.86787  ? 42  ARG   A CB  1 
ATOM   287  C CG  . ARG   A 1  42  ? 8.71833   42.95332 19.89933 1.000 70.06829  ? 42  ARG   A CG  1 
ATOM   288  C CD  . ARG   A 1  42  ? 8.85908   44.48086 19.75649 1.000 68.99412  ? 42  ARG   A CD  1 
ATOM   289  N NE  . ARG   A 1  42  ? 10.20292  44.86400 19.34649 1.000 71.79782  ? 42  ARG   A NE  1 
ATOM   290  C CZ  . ARG   A 1  42  ? 10.56578  46.07796 18.95148 1.000 69.90369  ? 42  ARG   A CZ  1 
ATOM   291  N NH1 . ARG   A 1  42  ? 9.71119   47.08811 18.93335 1.000 77.17620  ? 42  ARG   A NH1 1 
ATOM   292  N NH2 . ARG   A 1  42  ? 11.81669  46.28004 18.54916 1.000 69.40072  ? 42  ARG   A NH2 1 
ATOM   293  N N   . PHE   A 1  43  ? 7.04291   40.21858 20.68848 1.000 62.72406  ? 43  PHE   A N   1 
ATOM   294  C CA  . PHE   A 1  43  ? 5.99018   40.00739 21.68889 1.000 65.55226  ? 43  PHE   A CA  1 
ATOM   295  C C   . PHE   A 1  43  ? 5.21413   38.71032 21.46712 1.000 68.82599  ? 43  PHE   A C   1 
ATOM   296  O O   . PHE   A 1  43  ? 4.50346   38.25398 22.36860 1.000 70.85066  ? 43  PHE   A O   1 
ATOM   297  C CB  . PHE   A 1  43  ? 4.97725   41.15437 21.72653 1.000 73.10813  ? 43  PHE   A CB  1 
ATOM   298  C CG  . PHE   A 1  43  ? 5.55257   42.48773 22.09386 1.000 70.29455  ? 43  PHE   A CG  1 
ATOM   299  C CD1 . PHE   A 1  43  ? 6.23206   42.66691 23.28198 1.000 66.14422  ? 43  PHE   A CD1 1 
ATOM   300  C CD2 . PHE   A 1  43  ? 5.36053   43.57720 21.25610 1.000 73.14762  ? 43  PHE   A CD2 1 
ATOM   301  C CE1 . PHE   A 1  43  ? 6.72879   43.89686 23.61886 1.000 66.06973  ? 43  PHE   A CE1 1 
ATOM   302  C CE2 . PHE   A 1  43  ? 5.85113   44.81531 21.58847 1.000 69.48048  ? 43  PHE   A CE2 1 
ATOM   303  C CZ  . PHE   A 1  43  ? 6.53307   44.97750 22.76769 1.000 66.36571  ? 43  PHE   A CZ  1 
ATOM   304  N N   . LYS   A 1  44  ? 5.30148   38.12677 20.27331 1.000 65.87193  ? 44  LYS   A N   1 
ATOM   305  C CA  . LYS   A 1  44  ? 4.62213   36.86406 20.03310 1.000 64.78275  ? 44  LYS   A CA  1 
ATOM   306  C C   . LYS   A 1  44  ? 5.39557   35.71794 20.66706 1.000 62.61927  ? 44  LYS   A C   1 
ATOM   307  O O   . LYS   A 1  44  ? 6.55096   35.85601 21.07376 1.000 63.34037  ? 44  LYS   A O   1 
ATOM   308  C CB  . LYS   A 1  44  ? 4.47416   36.58128 18.54271 1.000 65.58474  ? 44  LYS   A CB  1 
ATOM   309  C CG  . LYS   A 1  44  ? 4.03382   37.76202 17.70518 1.000 72.54504  ? 44  LYS   A CG  1 
ATOM   310  C CD  . LYS   A 1  44  ? 2.68343   37.51512 17.10587 1.000 80.54966  ? 44  LYS   A CD  1 
ATOM   311  C CE  . LYS   A 1  44  ? 2.78430   36.44787 16.03191 1.000 86.27949  ? 44  LYS   A CE  1 
ATOM   312  N NZ  . LYS   A 1  44  ? 1.47941   36.21909 15.34545 1.000 88.08802  ? 44  LYS   A NZ  1 
ATOM   313  N N   . LYS   A 1  45  ? 4.74351   34.55770 20.70415 1.000 65.96656  ? 45  LYS   A N   1 
ATOM   314  C CA  . LYS   A 1  45  ? 5.37693   33.33899 21.16990 1.000 65.61142  ? 45  LYS   A CA  1 
ATOM   315  C C   . LYS   A 1  45  ? 6.53892   32.96807 20.24318 1.000 66.60843  ? 45  LYS   A C   1 
ATOM   316  O O   . LYS   A 1  45  ? 6.55522   33.36106 19.06879 1.000 69.41209  ? 45  LYS   A O   1 
ATOM   317  C CB  . LYS   A 1  45  ? 4.35523   32.20186 21.22669 1.000 59.04874  ? 45  LYS   A CB  1 
ATOM   318  C CG  . LYS   A 1  45  ? 3.42502   32.25219 22.43454 1.000 64.47561  ? 45  LYS   A CG  1 
ATOM   319  C CD  . LYS   A 1  45  ? 2.25203   31.28713 22.28310 1.000 64.51386  ? 45  LYS   A CD  1 
ATOM   320  C CE  . LYS   A 1  45  ? 2.50199   29.98515 23.02180 1.000 67.49573  ? 45  LYS   A CE  1 
ATOM   321  N NZ  . LYS   A 1  45  ? 1.22593   29.32931 23.43325 1.000 67.36276  ? 45  LYS   A NZ  1 
ATOM   322  N N   . PRO   A 1  46  ? 7.52775   32.22635 20.74817 1.000 56.83862  ? 46  PRO   A N   1 
ATOM   323  C CA  . PRO   A 1  46  ? 8.64097   31.80573 19.88891 1.000 60.96541  ? 46  PRO   A CA  1 
ATOM   324  C C   . PRO   A 1  46  ? 8.13812   30.89667 18.78246 1.000 63.68916  ? 46  PRO   A C   1 
ATOM   325  O O   . PRO   A 1  46  ? 7.27616   30.05281 19.00848 1.000 69.69777  ? 46  PRO   A O   1 
ATOM   326  C CB  . PRO   A 1  46  ? 9.57997   31.05853 20.85073 1.000 60.59929  ? 46  PRO   A CB  1 
ATOM   327  C CG  . PRO   A 1  46  ? 8.71309   30.64214 22.01102 1.000 57.05479  ? 46  PRO   A CG  1 
ATOM   328  C CD  . PRO   A 1  46  ? 7.66561   31.73063 22.13059 1.000 63.19787  ? 46  PRO   A CD  1 
ATOM   329  N N   . GLN   A 1  47  ? 8.68627   31.07109 17.58204 1.000 68.89797  ? 47  GLN   A N   1 
ATOM   330  C CA  . GLN   A 1  47  ? 8.29510   30.30568 16.40404 1.000 71.39253  ? 47  GLN   A CA  1 
ATOM   331  C C   . GLN   A 1  47  ? 9.40491   29.34026 16.00509 1.000 72.74755  ? 47  GLN   A C   1 
ATOM   332  O O   . GLN   A 1  47  ? 10.57880  29.54429 16.32698 1.000 68.60637  ? 47  GLN   A O   1 
ATOM   333  C CB  . GLN   A 1  47  ? 7.96047   31.23352 15.23012 1.000 70.13805  ? 47  GLN   A CB  1 
ATOM   334  C CG  . GLN   A 1  47  ? 7.11981   32.41537 15.64241 1.000 70.97601  ? 47  GLN   A CG  1 
ATOM   335  C CD  . GLN   A 1  47  ? 5.64367   32.11651 15.55867 1.000 82.69616  ? 47  GLN   A CD  1 
ATOM   336  O OE1 . GLN   A 1  47  ? 5.17477   31.59359 14.54502 1.000 91.60263  ? 47  GLN   A OE1 1 
ATOM   337  N NE2 . GLN   A 1  47  ? 4.89689   32.43447 16.62612 1.000 76.15336  ? 47  GLN   A NE2 1 
ATOM   338  N N   . SER   A 1  48  ? 9.01289   28.28076 15.29375 1.000 86.78755  ? 48  SER   A N   1 
ATOM   339  C CA  . SER   A 1  48  ? 9.90348   27.15767 15.00531 1.000 88.73300  ? 48  SER   A CA  1 
ATOM   340  C C   . SER   A 1  48  ? 10.88106  27.51870 13.89295 1.000 83.54618  ? 48  SER   A C   1 
ATOM   341  O O   . SER   A 1  48  ? 10.59440  28.35281 13.03285 1.000 86.00702  ? 48  SER   A O   1 
ATOM   342  C CB  . SER   A 1  48  ? 9.10269   25.90348 14.62462 1.000 83.89794  ? 48  SER   A CB  1 
ATOM   343  O OG  . SER   A 1  48  ? 8.28204   26.12263 13.48858 1.000 90.83522  ? 48  SER   A OG  1 
ATOM   344  N N   . LEU   A 1  49  ? 12.05125  26.88879 13.92045 1.000 84.54169  ? 49  LEU   A N   1 
ATOM   345  C CA  . LEU   A 1  49  ? 13.12464  27.24937 13.00438 1.000 91.42119  ? 49  LEU   A CA  1 
ATOM   346  C C   . LEU   A 1  49  ? 13.01352  26.51027 11.67705 1.000 100.18494 ? 49  LEU   A C   1 
ATOM   347  O O   . LEU   A 1  49  ? 12.65839  25.32699 11.63032 1.000 100.80702 ? 49  LEU   A O   1 
ATOM   348  C CB  . LEU   A 1  49  ? 14.48437  26.96307 13.63110 1.000 83.64906  ? 49  LEU   A CB  1 
ATOM   349  C CG  . LEU   A 1  49  ? 15.19081  28.22471 14.09074 1.000 83.90826  ? 49  LEU   A CG  1 
ATOM   350  C CD1 . LEU   A 1  49  ? 16.30701  27.85085 15.03843 1.000 77.49739  ? 49  LEU   A CD1 1 
ATOM   351  C CD2 . LEU   A 1  49  ? 15.71273  28.99642 12.88307 1.000 82.85392  ? 49  LEU   A CD2 1 
ATOM   352  N N   . THR   A 1  50  ? 13.32101  27.22178 10.59758 1.000 104.30310 ? 50  THR   A N   1 
ATOM   353  C CA  . THR   A 1  50  ? 13.45529  26.58997 9.29631  1.000 109.16045 ? 50  THR   A CA  1 
ATOM   354  C C   . THR   A 1  50  ? 14.81284  25.90714 9.19199  1.000 110.30776 ? 50  THR   A C   1 
ATOM   355  O O   . THR   A 1  50  ? 15.80852  26.36684 9.75996  1.000 105.58267 ? 50  THR   A O   1 
ATOM   356  C CB  . THR   A 1  50  ? 13.29534  27.61516 8.16663  1.000 114.18604 ? 50  THR   A CB  1 
ATOM   357  O OG1 . THR   A 1  50  ? 13.89135  28.86938 8.54541  1.000 107.93136 ? 50  THR   A OG1 1 
ATOM   358  C CG2 . THR   A 1  50  ? 11.82425  27.81786 7.83646  1.000 114.12674 ? 50  THR   A CG2 1 
ATOM   359  N N   . LYS   A 1  51  ? 14.84084  24.79415 8.46412  1.000 109.41146 ? 51  LYS   A N   1 
ATOM   360  C CA  . LYS   A 1  51  ? 16.08650  24.07222 8.24450  1.000 106.20524 ? 51  LYS   A CA  1 
ATOM   361  C C   . LYS   A 1  51  ? 17.12078  24.96607 7.56756  1.000 105.02130 ? 51  LYS   A C   1 
ATOM   362  O O   . LYS   A 1  51  ? 16.78970  25.79723 6.71686  1.000 106.53578 ? 51  LYS   A O   1 
ATOM   363  C CB  . LYS   A 1  51  ? 15.83177  22.83512 7.37968  1.000 111.27444 ? 51  LYS   A CB  1 
ATOM   364  C CG  . LYS   A 1  51  ? 15.19290  21.66313 8.11339  1.000 116.75047 ? 51  LYS   A CG  1 
ATOM   365  C CD  . LYS   A 1  51  ? 14.98556  20.46988 7.18079  1.000 121.33850 ? 51  LYS   A CD  1 
ATOM   366  C CE  . LYS   A 1  51  ? 16.27787  19.68895 6.96711  1.000 120.76448 ? 51  LYS   A CE  1 
ATOM   367  N NZ  . LYS   A 1  51  ? 16.74903  19.01147 8.21446  1.000 115.62020 ? 51  LYS   A NZ  1 
ATOM   368  N N   . TRP   A 1  52  ? 18.37963  24.80796 7.96259  1.000 99.69552  ? 52  TRP   A N   1 
ATOM   369  C CA  . TRP   A 1  52  ? 19.49105  25.34296 7.19478  1.000 96.45062  ? 52  TRP   A CA  1 
ATOM   370  C C   . TRP   A 1  52  ? 20.31988  24.19113 6.64541  1.000 99.94033  ? 52  TRP   A C   1 
ATOM   371  O O   . TRP   A 1  52  ? 20.29933  23.06902 7.16474  1.000 94.80894  ? 52  TRP   A O   1 
ATOM   372  C CB  . TRP   A 1  52  ? 20.37608  26.27193 8.02832  1.000 92.19455  ? 52  TRP   A CB  1 
ATOM   373  C CG  . TRP   A 1  52  ? 21.13204  25.55059 9.06368  1.000 92.99982  ? 52  TRP   A CG  1 
ATOM   374  C CD1 . TRP   A 1  52  ? 22.34299  24.93687 8.92285  1.000 94.66661  ? 52  TRP   A CD1 1 
ATOM   375  C CD2 . TRP   A 1  52  ? 20.72969  25.34571 10.41561 1.000 87.08524  ? 52  TRP   A CD2 1 
ATOM   376  N NE1 . TRP   A 1  52  ? 22.72069  24.36166 10.11153 1.000 90.98564  ? 52  TRP   A NE1 1 
ATOM   377  C CE2 . TRP   A 1  52  ? 21.74732  24.60117 11.04554 1.000 85.59440  ? 52  TRP   A CE2 1 
ATOM   378  C CE3 . TRP   A 1  52  ? 19.60627  25.72157 11.15883 1.000 87.50919  ? 52  TRP   A CE3 1 
ATOM   379  C CZ2 . TRP   A 1  52  ? 21.67581  24.22430 12.38488 1.000 85.85674  ? 52  TRP   A CZ2 1 
ATOM   380  C CZ3 . TRP   A 1  52  ? 19.53984  25.35555 12.49176 1.000 86.79288  ? 52  TRP   A CZ3 1 
ATOM   381  C CH2 . TRP   A 1  52  ? 20.56577  24.60995 13.09034 1.000 83.97696  ? 52  TRP   A CH2 1 
ATOM   382  N N   . SER   A 1  53  ? 21.06250  24.49158 5.58415  1.000 100.70506 ? 53  SER   A N   1 
ATOM   383  C CA  . SER   A 1  53  ? 21.79518  23.48128 4.84165  1.000 100.72905 ? 53  SER   A CA  1 
ATOM   384  C C   . SER   A 1  53  ? 23.29880  23.55433 5.03748  1.000 100.24429 ? 53  SER   A C   1 
ATOM   385  O O   . SER   A 1  53  ? 23.99847  22.61328 4.65300  1.000 101.16865 ? 53  SER   A O   1 
ATOM   386  C CB  . SER   A 1  53  ? 21.47732  23.59906 3.34440  1.000 106.52357 ? 53  SER   A CB  1 
ATOM   387  O OG  . SER   A 1  53  ? 20.11957  23.27949 3.09704  1.000 108.75663 ? 53  SER   A OG  1 
ATOM   388  N N   . ASP   A 1  54  ? 23.81284  24.63684 5.60372  1.000 108.88170 ? 54  ASP   A N   1 
ATOM   389  C CA  . ASP   A 1  54  ? 25.24623  24.78351 5.80211  1.000 109.79881 ? 54  ASP   A CA  1 
ATOM   390  C C   . ASP   A 1  54  ? 25.63175  24.12791 7.12784  1.000 108.54672 ? 54  ASP   A C   1 
ATOM   391  O O   . ASP   A 1  54  ? 24.86456  23.34519 7.69138  1.000 103.70907 ? 54  ASP   A O   1 
ATOM   392  C CB  . ASP   A 1  54  ? 25.62520  26.26897 5.66497  1.000 113.76145 ? 54  ASP   A CB  1 
ATOM   393  C CG  . ASP   A 1  54  ? 25.31354  27.10710 6.91877  1.000 122.72427 ? 54  ASP   A CG  1 
ATOM   394  O OD1 . ASP   A 1  54  ? 25.66488  26.73471 8.06415  1.000 127.66546 ? 54  ASP   A OD1 1 
ATOM   395  O OD2 . ASP   A 1  54  ? 24.66828  28.16177 6.74014  1.000 124.71293 ? 54  ASP   A OD2 1 
ATOM   396  N N   . ILE   A 1  55  ? 26.82395  24.42352 7.62784  1.000 101.73511 ? 55  ILE   A N   1 
ATOM   397  C CA  . ILE   A 1  55  ? 27.26010  23.98928 8.94880  1.000 95.82696  ? 55  ILE   A CA  1 
ATOM   398  C C   . ILE   A 1  55  ? 27.23163  25.20738 9.86028  1.000 91.39700  ? 55  ILE   A C   1 
ATOM   399  O O   . ILE   A 1  55  ? 28.07549  26.09990 9.72925  1.000 93.36852  ? 55  ILE   A O   1 
ATOM   400  C CB  . ILE   A 1  55  ? 28.65928  23.36401 8.91324  1.000 93.52347  ? 55  ILE   A CB  1 
ATOM   401  C CG1 . ILE   A 1  55  ? 28.73821  22.33795 7.77317  1.000 89.93223  ? 55  ILE   A CG1 1 
ATOM   402  C CG2 . ILE   A 1  55  ? 28.99659  22.76335 10.28574 1.000 87.35411  ? 55  ILE   A CG2 1 
ATOM   403  C CD1 . ILE   A 1  55  ? 29.83444  21.32265 7.91007  1.000 74.56484  ? 55  ILE   A CD1 1 
ATOM   404  N N   . TRP   A 1  56  ? 26.26537  25.26147 10.77935 1.000 81.99192  ? 56  TRP   A N   1 
ATOM   405  C CA  . TRP   A 1  56  ? 26.17416  26.39986 11.68719 1.000 80.91467  ? 56  TRP   A CA  1 
ATOM   406  C C   . TRP   A 1  56  ? 27.35464  26.41326 12.64633 1.000 79.84612  ? 56  TRP   A C   1 
ATOM   407  O O   . TRP   A 1  56  ? 27.60308  25.42950 13.34725 1.000 82.26763  ? 56  TRP   A O   1 
ATOM   408  C CB  . TRP   A 1  56  ? 24.87542  26.36500 12.48541 1.000 79.95875  ? 56  TRP   A CB  1 
ATOM   409  C CG  . TRP   A 1  56  ? 24.77005  27.54136 13.40018 1.000 79.09756  ? 56  TRP   A CG  1 
ATOM   410  C CD1 . TRP   A 1  56  ? 25.42563  27.73013 14.58940 1.000 77.11542  ? 56  TRP   A CD1 1 
ATOM   411  C CD2 . TRP   A 1  56  ? 23.98208  28.71359 13.18759 1.000 78.70031  ? 56  TRP   A CD2 1 
ATOM   412  N NE1 . TRP   A 1  56  ? 25.08577  28.94971 15.12972 1.000 78.87614  ? 56  TRP   A NE1 1 
ATOM   413  C CE2 . TRP   A 1  56  ? 24.19981  29.57205 14.29023 1.000 77.59995  ? 56  TRP   A CE2 1 
ATOM   414  C CE3 . TRP   A 1  56  ? 23.10123  29.11599 12.17886 1.000 80.57429  ? 56  TRP   A CE3 1 
ATOM   415  C CZ2 . TRP   A 1  56  ? 23.57084  30.80872 14.40842 1.000 77.62567  ? 56  TRP   A CZ2 1 
ATOM   416  C CZ3 . TRP   A 1  56  ? 22.47614  30.34585 12.29504 1.000 84.57298  ? 56  TRP   A CZ3 1 
ATOM   417  C CH2 . TRP   A 1  56  ? 22.71108  31.17768 13.40581 1.000 81.34892  ? 56  TRP   A CH2 1 
ATOM   418  N N   . ASN   A 1  57  ? 28.05545  27.54171 12.71431 1.000 75.19740  ? 57  ASN   A N   1 
ATOM   419  C CA  . ASN   A 1  57  ? 29.26339  27.64892 13.53301 1.000 81.09440  ? 57  ASN   A CA  1 
ATOM   420  C C   . ASN   A 1  57  ? 28.86847  28.07070 14.94450 1.000 77.64638  ? 57  ASN   A C   1 
ATOM   421  O O   . ASN   A 1  57  ? 28.64968  29.24935 15.22270 1.000 79.39695  ? 57  ASN   A O   1 
ATOM   422  C CB  . ASN   A 1  57  ? 30.25897  28.61241 12.89698 1.000 85.08432  ? 57  ASN   A CB  1 
ATOM   423  C CG  . ASN   A 1  57  ? 31.07680  27.95037 11.79503 1.000 92.81721  ? 57  ASN   A CG  1 
ATOM   424  O OD1 . ASN   A 1  57  ? 31.07830  26.72234 11.66945 1.000 90.95802  ? 57  ASN   A OD1 1 
ATOM   425  N ND2 . ASN   A 1  57  ? 31.77145  28.75401 10.99189 1.000 95.81367  ? 57  ASN   A ND2 1 
ATOM   426  N N   . ALA   A 1  58  ? 28.78670  27.09145 15.83800 1.000 73.39799  ? 58  ALA   A N   1 
ATOM   427  C CA  . ALA   A 1  58  ? 28.39055  27.31475 17.22287 1.000 69.63543  ? 58  ALA   A CA  1 
ATOM   428  C C   . ALA   A 1  58  ? 29.62622  27.29038 18.11945 1.000 71.29550  ? 58  ALA   A C   1 
ATOM   429  O O   . ALA   A 1  58  ? 29.80354  26.41830 18.96951 1.000 72.50804  ? 58  ALA   A O   1 
ATOM   430  C CB  . ALA   A 1  58  ? 27.37301  26.26404 17.65535 1.000 70.46699  ? 58  ALA   A CB  1 
ATOM   431  N N   . THR   A 1  59  ? 30.48275  28.29166 17.91254 1.000 71.33077  ? 59  THR   A N   1 
ATOM   432  C CA  . THR   A 1  59  ? 31.80805  28.34066 18.51489 1.000 70.63885  ? 59  THR   A CA  1 
ATOM   433  C C   . THR   A 1  59  ? 32.02877  29.56950 19.39200 1.000 68.23409  ? 59  THR   A C   1 
ATOM   434  O O   . THR   A 1  59  ? 33.15053  29.78627 19.87412 1.000 68.42499  ? 59  THR   A O   1 
ATOM   435  C CB  . THR   A 1  59  ? 32.87033  28.30321 17.41108 1.000 75.76298  ? 59  THR   A CB  1 
ATOM   436  O OG1 . THR   A 1  59  ? 32.53562  29.28698 16.42723 1.000 76.20744  ? 59  THR   A OG1 1 
ATOM   437  C CG2 . THR   A 1  59  ? 32.88911  26.92231 16.74147 1.000 72.48439  ? 59  THR   A CG2 1 
ATOM   438  N N   . LYS   A 1  60  ? 31.00563  30.39653 19.58203 1.000 70.43948  ? 60  LYS   A N   1 
ATOM   439  C CA  . LYS   A 1  60  ? 31.06073  31.50908 20.51840 1.000 72.02537  ? 60  LYS   A CA  1 
ATOM   440  C C   . LYS   A 1  60  ? 29.64851  31.74329 21.01637 1.000 65.32496  ? 60  LYS   A C   1 
ATOM   441  O O   . LYS   A 1  60  ? 28.67375  31.36928 20.36486 1.000 61.54073  ? 60  LYS   A O   1 
ATOM   442  C CB  . LYS   A 1  60  ? 31.65740  32.79450 19.90101 1.000 66.20748  ? 60  LYS   A CB  1 
ATOM   443  C CG  . LYS   A 1  60  ? 30.76269  33.52292 18.89776 1.000 73.02890  ? 60  LYS   A CG  1 
ATOM   444  C CD  . LYS   A 1  60  ? 31.56180  34.53954 18.03438 1.000 77.49056  ? 60  LYS   A CD  1 
ATOM   445  C CE  . LYS   A 1  60  ? 30.81453  35.87686 17.89632 1.000 87.97705  ? 60  LYS   A CE  1 
ATOM   446  N NZ  . LYS   A 1  60  ? 31.68553  37.09161 17.88413 1.000 86.76159  ? 60  LYS   A NZ  1 
ATOM   447  N N   . TYR   A 1  61  ? 29.55619  32.32205 22.20437 1.000 65.54638  ? 61  TYR   A N   1 
ATOM   448  C CA  . TYR   A 1  61  ? 28.27099  32.72791 22.73822 1.000 60.62508  ? 61  TYR   A CA  1 
ATOM   449  C C   . TYR   A 1  61  ? 27.56539  33.66739 21.76636 1.000 57.95972  ? 61  TYR   A C   1 
ATOM   450  O O   . TYR   A 1  61  ? 28.19841  34.47071 21.08304 1.000 68.53031  ? 61  TYR   A O   1 
ATOM   451  C CB  . TYR   A 1  61  ? 28.47507  33.42677 24.07123 1.000 60.38872  ? 61  TYR   A CB  1 
ATOM   452  C CG  . TYR   A 1  61  ? 28.91663  32.54940 25.20874 1.000 60.71764  ? 61  TYR   A CG  1 
ATOM   453  C CD1 . TYR   A 1  61  ? 28.05455  31.62293 25.76933 1.000 61.26581  ? 61  TYR   A CD1 1 
ATOM   454  C CD2 . TYR   A 1  61  ? 30.17415  32.69924 25.77559 1.000 58.77288  ? 61  TYR   A CD2 1 
ATOM   455  C CE1 . TYR   A 1  61  ? 28.44435  30.83979 26.84095 1.000 63.55899  ? 61  TYR   A CE1 1 
ATOM   456  C CE2 . TYR   A 1  61  ? 30.57738  31.92275 26.84994 1.000 52.38717  ? 61  TYR   A CE2 1 
ATOM   457  C CZ  . TYR   A 1  61  ? 29.70490  31.00129 27.38709 1.000 64.01973  ? 61  TYR   A CZ  1 
ATOM   458  O OH  . TYR   A 1  61  ? 30.10874  30.21980 28.45742 1.000 64.72904  ? 61  TYR   A OH  1 
ATOM   459  N N   . ALA   A 1  62  ? 26.24379  33.56239 21.70571 1.000 61.47494  ? 62  ALA   A N   1 
ATOM   460  C CA  . ALA   A 1  62  ? 25.44722  34.42944 20.84749 1.000 67.69873  ? 62  ALA   A CA  1 
ATOM   461  C C   . ALA   A 1  62  ? 25.06703  35.72018 21.58358 1.000 64.26600  ? 62  ALA   A C   1 
ATOM   462  O O   . ALA   A 1  62  ? 25.46453  35.95106 22.72824 1.000 63.26559  ? 62  ALA   A O   1 
ATOM   463  C CB  . ALA   A 1  62  ? 24.20469  33.69007 20.35035 1.000 57.37691  ? 62  ALA   A CB  1 
ATOM   464  N N   . ASN   A 1  63  ? 24.30315  36.57728 20.89681 1.000 64.30695  ? 63  ASN   A N   1 
ATOM   465  C CA  . ASN   A 1  63  ? 23.74508  37.79101 21.49284 1.000 63.36902  ? 63  ASN   A CA  1 
ATOM   466  C C   . ASN   A 1  63  ? 22.93855  37.48084 22.75278 1.000 62.11931  ? 63  ASN   A C   1 
ATOM   467  O O   . ASN   A 1  63  ? 22.19516  36.49878 22.80423 1.000 55.46782  ? 63  ASN   A O   1 
ATOM   468  C CB  . ASN   A 1  63  ? 22.82028  38.49723 20.49644 1.000 61.15924  ? 63  ASN   A CB  1 
ATOM   469  C CG  . ASN   A 1  63  ? 23.52589  38.92243 19.20263 1.000 68.75353  ? 63  ASN   A CG  1 
ATOM   470  O OD1 . ASN   A 1  63  ? 24.65978  39.40200 19.21143 1.000 66.72171  ? 63  ASN   A OD1 1 
ATOM   471  N ND2 . ASN   A 1  63  ? 22.83249  38.76256 18.08420 1.000 70.49949  ? 63  ASN   A ND2 1 
ATOM   472  N N   . SER   A 1  64  ? 23.07576  38.33284 23.76986 1.000 57.68627  ? 64  SER   A N   1 
ATOM   473  C CA  . SER   A 1  64  ? 22.14406  38.31827 24.88816 1.000 58.12463  ? 64  SER   A CA  1 
ATOM   474  C C   . SER   A 1  64  ? 20.89542  39.12042 24.52278 1.000 58.57512  ? 64  SER   A C   1 
ATOM   475  O O   . SER   A 1  64  ? 20.94457  40.02359 23.68186 1.000 63.23133  ? 64  SER   A O   1 
ATOM   476  C CB  . SER   A 1  64  ? 22.79119  38.90246 26.14540 1.000 57.20397  ? 64  SER   A CB  1 
ATOM   477  O OG  . SER   A 1  64  ? 23.92370  38.15094 26.53221 1.000 57.81535  ? 64  SER   A OG  1 
ATOM   478  N N   . CYS   A 1  65  ? 19.77092  38.78156 25.15563 1.000 52.04683  ? 65  CYS   A N   1 
ATOM   479  C CA  . CYS   A 1  65  ? 18.52016  39.50078 24.92665 1.000 55.91953  ? 65  CYS   A CA  1 
ATOM   480  C C   . CYS   A 1  65  ? 18.58684  40.92546 25.48324 1.000 61.56888  ? 65  CYS   A C   1 
ATOM   481  O O   . CYS   A 1  65  ? 19.27071  41.20230 26.47966 1.000 57.92184  ? 65  CYS   A O   1 
ATOM   482  C CB  . CYS   A 1  65  ? 17.33386  38.74616 25.55474 1.000 53.36139  ? 65  CYS   A CB  1 
ATOM   483  S SG  . CYS   A 1  65  ? 17.04822  37.04270 24.87089 1.000 58.12793  ? 65  CYS   A SG  1 
ATOM   484  N N   . CYS   A 1  66  ? 17.87277  41.83522 24.80993 1.000 55.80360  ? 66  CYS   A N   1 
ATOM   485  C CA  . CYS   A 1  66  ? 17.78526  43.22135 25.25174 1.000 59.19511  ? 66  CYS   A CA  1 
ATOM   486  C C   . CYS   A 1  66  ? 17.34122  43.32064 26.70634 1.000 58.92395  ? 66  CYS   A C   1 
ATOM   487  O O   . CYS   A 1  66  ? 16.46810  42.57981 27.16575 1.000 63.23021  ? 66  CYS   A O   1 
ATOM   488  C CB  . CYS   A 1  66  ? 16.81552  43.99389 24.36104 1.000 61.81947  ? 66  CYS   A CB  1 
ATOM   489  S SG  . CYS   A 1  66  ? 17.27690  44.02066 22.60209 1.000 69.31377  ? 66  CYS   A SG  1 
ATOM   490  N N   . GLN   A 1  67  ? 17.95127  44.24867 27.42980 1.000 61.50024  ? 67  GLN   A N   1 
ATOM   491  C CA  . GLN   A 1  67  ? 17.70988  44.39450 28.85743 1.000 63.31264  ? 67  GLN   A CA  1 
ATOM   492  C C   . GLN   A 1  67  ? 18.41640  45.65216 29.35610 1.000 60.47968  ? 67  GLN   A C   1 
ATOM   493  O O   . GLN   A 1  67  ? 19.40376  46.10483 28.77537 1.000 61.16344  ? 67  GLN   A O   1 
ATOM   494  C CB  . GLN   A 1  67  ? 18.20341  43.17196 29.63301 1.000 58.21217  ? 67  GLN   A CB  1 
ATOM   495  C CG  . GLN   A 1  67  ? 19.71161  42.96744 29.49641 1.000 58.33649  ? 67  GLN   A CG  1 
ATOM   496  C CD  . GLN   A 1  67  ? 20.12595  41.58524 29.91676 1.000 61.97471  ? 67  GLN   A CD  1 
ATOM   497  O OE1 . GLN   A 1  67  ? 20.43236  41.35162 31.08543 1.000 60.06605  ? 67  GLN   A OE1 1 
ATOM   498  N NE2 . GLN   A 1  67  ? 20.11660  40.64297 28.96916 1.000 63.09627  ? 67  GLN   A NE2 1 
ATOM   499  N N   . ASN   A 1  68  ? 17.88979  46.20085 30.44121 1.000 58.08873  ? 68  ASN   A N   1 
ATOM   500  C CA  . ASN   A 1  68  ? 18.55448  47.27297 31.14962 1.000 61.95021  ? 68  ASN   A CA  1 
ATOM   501  C C   . ASN   A 1  68  ? 19.74814  46.73349 31.92442 1.000 61.71918  ? 68  ASN   A C   1 
ATOM   502  O O   . ASN   A 1  68  ? 19.80094  45.56412 32.30484 1.000 64.85052  ? 68  ASN   A O   1 
ATOM   503  C CB  . ASN   A 1  68  ? 17.56656  47.96858 32.08308 1.000 60.99877  ? 68  ASN   A CB  1 
ATOM   504  C CG  . ASN   A 1  68  ? 16.61987  48.91018 31.32391 1.000 71.82004  ? 68  ASN   A CG  1 
ATOM   505  O OD1 . ASN   A 1  68  ? 17.05691  49.80779 30.60181 1.000 71.58009  ? 68  ASN   A OD1 1 
ATOM   506  N ND2 . ASN   A 1  68  ? 15.32469  48.69275 31.47446 1.000 73.30296  ? 68  ASN   A ND2 1 
ATOM   507  N N   . ILE   A 1  69  ? 20.73372  47.58690 32.12068 1.000 66.30163  ? 69  ILE   A N   1 
ATOM   508  C CA  . ILE   A 1  69  ? 21.96841  47.21428 32.79673 1.000 70.28330  ? 69  ILE   A CA  1 
ATOM   509  C C   . ILE   A 1  69  ? 21.99080  47.87021 34.16552 1.000 69.43781  ? 69  ILE   A C   1 
ATOM   510  O O   . ILE   A 1  69  ? 21.62761  49.04339 34.31350 1.000 66.67383  ? 69  ILE   A O   1 
ATOM   511  C CB  . ILE   A 1  69  ? 23.21105  47.62066 31.97930 1.000 73.46541  ? 69  ILE   A CB  1 
ATOM   512  C CG1 . ILE   A 1  69  ? 23.00043  47.30215 30.50077 1.000 68.60237  ? 69  ILE   A CG1 1 
ATOM   513  C CG2 . ILE   A 1  69  ? 24.45041  46.95587 32.52866 1.000 72.29050  ? 69  ILE   A CG2 1 
ATOM   514  C CD1 . ILE   A 1  69  ? 23.00876  45.84308 30.21787 1.000 64.46336  ? 69  ILE   A CD1 1 
ATOM   515  N N   . ASP   A 1  70  ? 22.43667  47.11592 35.16060 1.000 71.41031  ? 70  ASP   A N   1 
ATOM   516  C CA  . ASP   A 1  70  ? 22.61365  47.66457 36.49899 1.000 79.90422  ? 70  ASP   A CA  1 
ATOM   517  C C   . ASP   A 1  70  ? 23.81659  48.62281 36.49428 1.000 73.70405  ? 70  ASP   A C   1 
ATOM   518  O O   . ASP   A 1  70  ? 24.94516  48.21046 36.21014 1.000 72.21996  ? 70  ASP   A O   1 
ATOM   519  C CB  . ASP   A 1  70  ? 22.75681  46.49670 37.49335 1.000 75.95696  ? 70  ASP   A CB  1 
ATOM   520  C CG  . ASP   A 1  70  ? 23.43141  46.87878 38.81911 1.000 76.26828  ? 70  ASP   A CG  1 
ATOM   521  O OD1 . ASP   A 1  70  ? 23.32001  48.05054 39.28097 1.000 82.11486  ? 70  ASP   A OD1 1 
ATOM   522  O OD2 . ASP   A 1  70  ? 23.97519  45.95737 39.46282 1.000 68.51467  ? 70  ASP   A OD2 1 
ATOM   523  N N   . GLN   A 1  71  ? 23.56587  49.90951 36.76778 1.000 72.20284  ? 71  GLN   A N   1 
ATOM   524  C CA  . GLN   A 1  71  ? 24.59317  50.94679 36.72530 1.000 74.02077  ? 71  GLN   A CA  1 
ATOM   525  C C   . GLN   A 1  71  ? 24.90845  51.54252 38.08462 1.000 68.76495  ? 71  GLN   A C   1 
ATOM   526  O O   . GLN   A 1  71  ? 25.56309  52.58294 38.15633 1.000 63.83173  ? 71  GLN   A O   1 
ATOM   527  C CB  . GLN   A 1  71  ? 24.18175  52.07214 35.78639 1.000 74.06953  ? 71  GLN   A CB  1 
ATOM   528  C CG  . GLN   A 1  71  ? 24.44199  51.75235 34.34992 1.000 84.22902  ? 71  GLN   A CG  1 
ATOM   529  C CD  . GLN   A 1  71  ? 23.50697  52.50517 33.46403 1.000 85.58116  ? 71  GLN   A CD  1 
ATOM   530  O OE1 . GLN   A 1  71  ? 22.74243  51.92366 32.69335 1.000 87.45713  ? 71  GLN   A OE1 1 
ATOM   531  N NE2 . GLN   A 1  71  ? 23.54216  53.82265 33.57952 1.000 86.70570  ? 71  GLN   A NE2 1 
ATOM   532  N N   . SER   A 1  72  ? 24.49316  50.88770 39.15967 1.000 75.27707  ? 72  SER   A N   1 
ATOM   533  C CA  . SER   A 1  72  ? 24.67844  51.44248 40.49379 1.000 71.46901  ? 72  SER   A CA  1 
ATOM   534  C C   . SER   A 1  72  ? 26.13643  51.40896 40.93790 1.000 66.40345  ? 72  SER   A C   1 
ATOM   535  O O   . SER   A 1  72  ? 26.55180  52.24186 41.74429 1.000 72.92688  ? 72  SER   A O   1 
ATOM   536  C CB  . SER   A 1  72  ? 23.80428  50.66655 41.47800 1.000 71.51339  ? 72  SER   A CB  1 
ATOM   537  O OG  . SER   A 1  72  ? 22.45705  50.65760 41.04291 1.000 72.65891  ? 72  SER   A OG  1 
ATOM   538  N N   . PHE   A 1  73  ? 26.92881  50.45520 40.45864 1.000 72.77572  ? 73  PHE   A N   1 
ATOM   539  C CA  . PHE   A 1  73  ? 28.32814  50.33243 40.87451 1.000 67.07510  ? 73  PHE   A CA  1 
ATOM   540  C C   . PHE   A 1  73  ? 29.22255  50.13813 39.66028 1.000 66.58816  ? 73  PHE   A C   1 
ATOM   541  O O   . PHE   A 1  73  ? 29.82548  49.07278 39.47952 1.000 70.29772  ? 73  PHE   A O   1 
ATOM   542  C CB  . PHE   A 1  73  ? 28.49056  49.17885 41.86355 1.000 71.59237  ? 73  PHE   A CB  1 
ATOM   543  C CG  . PHE   A 1  73  ? 27.60076  49.29650 43.05704 1.000 69.70234  ? 73  PHE   A CG  1 
ATOM   544  C CD1 . PHE   A 1  73  ? 27.94285  50.12491 44.11556 1.000 67.41910  ? 73  PHE   A CD1 1 
ATOM   545  C CD2 . PHE   A 1  73  ? 26.41252  48.60951 43.11122 1.000 63.82922  ? 73  PHE   A CD2 1 
ATOM   546  C CE1 . PHE   A 1  73  ? 27.12376  50.24768 45.21260 1.000 63.29546  ? 73  PHE   A CE1 1 
ATOM   547  C CE2 . PHE   A 1  73  ? 25.58422  48.72333 44.21203 1.000 67.02496  ? 73  PHE   A CE2 1 
ATOM   548  C CZ  . PHE   A 1  73  ? 25.93517  49.53624 45.26046 1.000 64.18494  ? 73  PHE   A CZ  1 
ATOM   549  N N   . PRO   A 1  74  ? 29.34087  51.16018 38.81045 1.000 66.77422  ? 74  PRO   A N   1 
ATOM   550  C CA  . PRO   A 1  74  ? 30.25907  51.07672 37.66543 1.000 69.77757  ? 74  PRO   A CA  1 
ATOM   551  C C   . PRO   A 1  74  ? 31.65481  50.61947 38.08039 1.000 68.72114  ? 74  PRO   A C   1 
ATOM   552  O O   . PRO   A 1  74  ? 32.26756  51.17364 39.00562 1.000 69.14318  ? 74  PRO   A O   1 
ATOM   553  C CB  . PRO   A 1  74  ? 30.28552  52.52132 37.13000 1.000 68.34886  ? 74  PRO   A CB  1 
ATOM   554  C CG  . PRO   A 1  74  ? 29.06156  53.13037 37.63972 1.000 70.98400  ? 74  PRO   A CG  1 
ATOM   555  C CD  . PRO   A 1  74  ? 28.81373  52.52403 38.97922 1.000 64.58482  ? 74  PRO   A CD  1 
ATOM   556  N N   . GLY   A 1  75  ? 32.15946  49.61097 37.37389 1.000 67.93190  ? 75  GLY   A N   1 
ATOM   557  C CA  . GLY   A 1  75  ? 33.52473  49.15210 37.52661 1.000 68.75579  ? 75  GLY   A CA  1 
ATOM   558  C C   . GLY   A 1  75  ? 33.75998  48.20816 38.68018 1.000 67.31686  ? 75  GLY   A C   1 
ATOM   559  O O   . GLY   A 1  75  ? 34.90748  47.81309 38.90583 1.000 71.69424  ? 75  GLY   A O   1 
ATOM   560  N N   . PHE   A 1  76  ? 32.71876  47.86459 39.42914 1.000 68.75738  ? 76  PHE   A N   1 
ATOM   561  C CA  . PHE   A 1  76  ? 32.79829  46.99595 40.59595 1.000 67.60078  ? 76  PHE   A CA  1 
ATOM   562  C C   . PHE   A 1  76  ? 32.42395  45.58174 40.17824 1.000 70.33488  ? 76  PHE   A C   1 
ATOM   563  O O   . PHE   A 1  76  ? 31.32767  45.35668 39.64660 1.000 65.36459  ? 76  PHE   A O   1 
ATOM   564  C CB  . PHE   A 1  76  ? 31.86108  47.49794 41.69476 1.000 67.37274  ? 76  PHE   A CB  1 
ATOM   565  C CG  . PHE   A 1  76  ? 31.81054  46.62216 42.90728 1.000 63.45843  ? 76  PHE   A CG  1 
ATOM   566  C CD1 . PHE   A 1  76  ? 32.94724  46.41415 43.67754 1.000 72.04517  ? 76  PHE   A CD1 1 
ATOM   567  C CD2 . PHE   A 1  76  ? 30.62215  46.02745 43.30356 1.000 66.42358  ? 76  PHE   A CD2 1 
ATOM   568  C CE1 . PHE   A 1  76  ? 32.89427  45.60486 44.81136 1.000 67.04833  ? 76  PHE   A CE1 1 
ATOM   569  C CE2 . PHE   A 1  76  ? 30.56086  45.22475 44.43633 1.000 62.73726  ? 76  PHE   A CE2 1 
ATOM   570  C CZ  . PHE   A 1  76  ? 31.70346  45.02012 45.18879 1.000 65.50401  ? 76  PHE   A CZ  1 
ATOM   571  N N   . HIS   A 1  77  ? 33.32749  44.62751 40.43292 1.000 66.61815  ? 77  HIS   A N   1 
ATOM   572  C CA  . HIS   A 1  77  ? 33.10099  43.27220 39.93416 1.000 67.46703  ? 77  HIS   A CA  1 
ATOM   573  C C   . HIS   A 1  77  ? 31.89928  42.61830 40.59333 1.000 63.14152  ? 77  HIS   A C   1 
ATOM   574  O O   . HIS   A 1  77  ? 31.29267  41.71758 40.00164 1.000 63.20100  ? 77  HIS   A O   1 
ATOM   575  C CB  . HIS   A 1  77  ? 34.34013  42.39320 40.12646 1.000 63.04243  ? 77  HIS   A CB  1 
ATOM   576  C CG  . HIS   A 1  77  ? 34.22608  41.05490 39.46715 1.000 67.96882  ? 77  HIS   A CG  1 
ATOM   577  N ND1 . HIS   A 1  77  ? 34.25460  39.86964 40.17263 1.000 71.36486  ? 77  HIS   A ND1 1 
ATOM   578  C CD2 . HIS   A 1  77  ? 34.07207  40.71322 38.16447 1.000 68.56840  ? 77  HIS   A CD2 1 
ATOM   579  C CE1 . HIS   A 1  77  ? 34.12653  38.85583 39.33326 1.000 72.14933  ? 77  HIS   A CE1 1 
ATOM   580  N NE2 . HIS   A 1  77  ? 34.01589  39.34018 38.10814 1.000 68.95864  ? 77  HIS   A NE2 1 
ATOM   581  N N   . GLY   A 1  78  ? 31.54583  43.04400 41.81138 1.000 62.95466  ? 78  GLY   A N   1 
ATOM   582  C CA  . GLY   A 1  78  ? 30.41577  42.42465 42.50459 1.000 58.29274  ? 78  GLY   A CA  1 
ATOM   583  C C   . GLY   A 1  78  ? 29.09830  42.64190 41.78875 1.000 61.81124  ? 78  GLY   A C   1 
ATOM   584  O O   . GLY   A 1  78  ? 28.21131  41.78742 41.82866 1.000 59.75072  ? 78  GLY   A O   1 
ATOM   585  N N   . SER   A 1  79  ? 28.94140  43.79195 41.13356 1.000 63.15104  ? 79  SER   A N   1 
ATOM   586  C CA  . SER   A 1  79  ? 27.71897  43.96761 40.36604 1.000 63.84154  ? 79  SER   A CA  1 
ATOM   587  C C   . SER   A 1  79  ? 27.92251  43.58555 38.91694 1.000 56.36711  ? 79  SER   A C   1 
ATOM   588  O O   . SER   A 1  79  ? 27.05670  42.94664 38.31198 1.000 59.65065  ? 79  SER   A O   1 
ATOM   589  C CB  . SER   A 1  79  ? 27.21958  45.41056 40.44717 1.000 54.11891  ? 79  SER   A CB  1 
ATOM   590  O OG  . SER   A 1  79  ? 28.22137  46.28420 39.99722 1.000 75.54090  ? 79  SER   A OG  1 
ATOM   591  N N   . GLU   A 1  80  ? 29.06257  43.93483 38.36040 1.000 54.35551  ? 80  GLU   A N   1 
ATOM   592  C CA  . GLU   A 1  80  ? 29.22257  43.79254 36.92666 1.000 61.51061  ? 80  GLU   A CA  1 
ATOM   593  C C   . GLU   A 1  80  ? 29.44977  42.35407 36.47712 1.000 65.62008  ? 80  GLU   A C   1 
ATOM   594  O O   . GLU   A 1  80  ? 29.28829  42.08519 35.28249 1.000 66.10285  ? 80  GLU   A O   1 
ATOM   595  C CB  . GLU   A 1  80  ? 30.33604  44.72961 36.45628 1.000 64.32111  ? 80  GLU   A CB  1 
ATOM   596  C CG  . GLU   A 1  80  ? 29.94883  46.18494 36.76758 1.000 67.93835  ? 80  GLU   A CG  1 
ATOM   597  C CD  . GLU   A 1  80  ? 30.79351  47.20641 36.05286 1.000 73.64039  ? 80  GLU   A CD  1 
ATOM   598  O OE1 . GLU   A 1  80  ? 32.01479  46.99515 35.96581 1.000 76.81171  ? 80  GLU   A OE1 1 
ATOM   599  O OE2 . GLU   A 1  80  ? 30.25133  48.25035 35.62082 1.000 78.69103  ? 80  GLU   A OE2 1 
ATOM   600  N N   . MET   A 1  81  ? 29.73076  41.40816 37.39465 1.000 62.67579  ? 81  MET   A N   1 
ATOM   601  C CA  . MET   A 1  81  ? 29.78524  40.00118 36.99350 1.000 54.82167  ? 81  MET   A CA  1 
ATOM   602  C C   . MET   A 1  81  ? 28.42609  39.48113 36.52076 1.000 59.38850  ? 81  MET   A C   1 
ATOM   603  O O   . MET   A 1  81  ? 28.36859  38.37280 35.96868 1.000 57.85126  ? 81  MET   A O   1 
ATOM   604  C CB  . MET   A 1  81  ? 30.19483  39.04045 38.11957 1.000 59.30539  ? 81  MET   A CB  1 
ATOM   605  C CG  . MET   A 1  81  ? 29.41207  39.22379 39.42033 1.000 63.78953  ? 81  MET   A CG  1 
ATOM   606  S SD  . MET   A 1  81  ? 30.08247  38.38647 40.88194 1.000 67.26113  ? 81  MET   A SD  1 
ATOM   607  C CE  . MET   A 1  81  ? 29.93023  36.66822 40.36726 1.000 64.98180  ? 81  MET   A CE  1 
ATOM   608  N N   . TRP   A 1  82  ? 27.32440  40.20569 36.79319 1.000 51.11855  ? 82  TRP   A N   1 
ATOM   609  C CA  . TRP   A 1  82  ? 25.97584  39.79749 36.37883 1.000 59.80651  ? 82  TRP   A CA  1 
ATOM   610  C C   . TRP   A 1  82  ? 25.48181  40.50666 35.12350 1.000 56.29875  ? 82  TRP   A C   1 
ATOM   611  O O   . TRP   A 1  82  ? 24.48931  40.06894 34.54068 1.000 60.41552  ? 82  TRP   A O   1 
ATOM   612  C CB  . TRP   A 1  82  ? 24.96997  40.01898 37.52693 1.000 53.35869  ? 82  TRP   A CB  1 
ATOM   613  C CG  . TRP   A 1  82  ? 25.43230  39.45233 38.83617 1.000 61.72102  ? 82  TRP   A CG  1 
ATOM   614  C CD1 . TRP   A 1  82  ? 25.99021  40.13687 39.87196 1.000 56.56408  ? 82  TRP   A CD1 1 
ATOM   615  C CD2 . TRP   A 1  82  ? 25.40130  38.05920 39.24278 1.000 59.78085  ? 82  TRP   A CD2 1 
ATOM   616  N NE1 . TRP   A 1  82  ? 26.29716  39.26777 40.90966 1.000 59.75163  ? 82  TRP   A NE1 1 
ATOM   617  C CE2 . TRP   A 1  82  ? 25.94373  37.99090 40.54761 1.000 58.04645  ? 82  TRP   A CE2 1 
ATOM   618  C CE3 . TRP   A 1  82  ? 24.94454  36.88053 38.64014 1.000 56.22274  ? 82  TRP   A CE3 1 
ATOM   619  C CZ2 . TRP   A 1  82  ? 26.05265  36.78175 41.25453 1.000 60.27991  ? 82  TRP   A CZ2 1 
ATOM   620  C CZ3 . TRP   A 1  82  ? 25.03687  35.67157 39.35322 1.000 59.55492  ? 82  TRP   A CZ3 1 
ATOM   621  C CH2 . TRP   A 1  82  ? 25.59431  35.63593 40.64220 1.000 60.24866  ? 82  TRP   A CH2 1 
ATOM   622  N N   . ASN   A 1  83  ? 26.15096  41.57210 34.69726 1.000 58.55162  ? 83  ASN   A N   1 
ATOM   623  C CA  . ASN   A 1  83  ? 25.75921  42.29370 33.50206 1.000 59.12394  ? 83  ASN   A CA  1 
ATOM   624  C C   . ASN   A 1  83  ? 26.07669  41.47129 32.25433 1.000 60.34088  ? 83  ASN   A C   1 
ATOM   625  O O   . ASN   A 1  83  ? 26.96600  40.61753 32.27688 1.000 65.25326  ? 83  ASN   A O   1 
ATOM   626  C CB  . ASN   A 1  83  ? 26.48204  43.64043 33.46291 1.000 61.91511  ? 83  ASN   A CB  1 
ATOM   627  C CG  . ASN   A 1  83  ? 25.94795  44.61345 34.49947 1.000 65.55299  ? 83  ASN   A CG  1 
ATOM   628  O OD1 . ASN   A 1  83  ? 24.79315  44.51469 34.91945 1.000 67.14914  ? 83  ASN   A OD1 1 
ATOM   629  N ND2 . ASN   A 1  83  ? 26.78150  45.57178 34.90591 1.000 67.15957  ? 83  ASN   A ND2 1 
ATOM   630  N N   . PRO   A 1  84  ? 25.36325  41.70291 31.15208 1.000 60.96689  ? 84  PRO   A N   1 
ATOM   631  C CA  . PRO   A 1  84  ? 25.56040  40.86374 29.96157 1.000 66.62279  ? 84  PRO   A CA  1 
ATOM   632  C C   . PRO   A 1  84  ? 26.95511  41.04529 29.39461 1.000 55.50787  ? 84  PRO   A C   1 
ATOM   633  O O   . PRO   A 1  84  ? 27.51390  42.13710 29.42685 1.000 65.02007  ? 84  PRO   A O   1 
ATOM   634  C CB  . PRO   A 1  84  ? 24.49571  41.37057 28.97572 1.000 61.22418  ? 84  PRO   A CB  1 
ATOM   635  C CG  . PRO   A 1  84  ? 23.58836  42.20164 29.76589 1.000 66.28968  ? 84  PRO   A CG  1 
ATOM   636  C CD  . PRO   A 1  84  ? 24.38085  42.76119 30.90547 1.000 59.42113  ? 84  PRO   A CD  1 
ATOM   637  N N   . ASN   A 1  85  ? 27.51012  39.95955 28.85735 1.000 62.69527  ? 85  ASN   A N   1 
ATOM   638  C CA  . ASN   A 1  85  ? 28.86152  39.96882 28.29831 1.000 65.36245  ? 85  ASN   A CA  1 
ATOM   639  C C   . ASN   A 1  85  ? 28.87181  39.54467 26.83682 1.000 66.23668  ? 85  ASN   A C   1 
ATOM   640  O O   . ASN   A 1  85  ? 29.88686  39.05999 26.34209 1.000 66.86418  ? 85  ASN   A O   1 
ATOM   641  C CB  . ASN   A 1  85  ? 29.80085  39.07293 29.11901 1.000 55.16196  ? 85  ASN   A CB  1 
ATOM   642  C CG  . ASN   A 1  85  ? 29.38626  37.60591 29.10377 1.000 62.10254  ? 85  ASN   A CG  1 
ATOM   643  O OD1 . ASN   A 1  85  ? 28.21992  37.25435 28.83234 1.000 61.27864  ? 85  ASN   A OD1 1 
ATOM   644  N ND2 . ASN   A 1  85  ? 30.35030  36.73474 29.38880 1.000 58.31794  ? 85  ASN   A ND2 1 
ATOM   645  N N   . THR   A 1  86  ? 27.73773  39.65059 26.15729 1.000 68.57383  ? 86  THR   A N   1 
ATOM   646  C CA  . THR   A 1  86  ? 27.69327  39.66127 24.70760 1.000 65.96281  ? 86  THR   A CA  1 
ATOM   647  C C   . THR   A 1  86  ? 26.78516  40.80702 24.30463 1.000 64.18201  ? 86  THR   A C   1 
ATOM   648  O O   . THR   A 1  86  ? 26.10239  41.39692 25.14672 1.000 67.67708  ? 86  THR   A O   1 
ATOM   649  C CB  . THR   A 1  86  ? 27.19858  38.32717 24.12820 1.000 63.60096  ? 86  THR   A CB  1 
ATOM   650  O OG1 . THR   A 1  86  ? 25.85193  38.07330 24.55321 1.000 62.54485  ? 86  THR   A OG1 1 
ATOM   651  C CG2 . THR   A 1  86  ? 28.08099  37.19834 24.59422 1.000 64.36715  ? 86  THR   A CG2 1 
ATOM   652  N N   . ASP   A 1  87  ? 26.78079  41.12358 23.01035 1.000 62.61929  ? 87  ASP   A N   1 
ATOM   653  C CA  . ASP   A 1  87  ? 25.90475  42.17611 22.50740 1.000 65.90156  ? 87  ASP   A CA  1 
ATOM   654  C C   . ASP   A 1  87  ? 24.46320  41.91738 22.90311 1.000 65.19843  ? 87  ASP   A C   1 
ATOM   655  O O   . ASP   A 1  87  ? 23.98807  40.77663 22.87392 1.000 61.87680  ? 87  ASP   A O   1 
ATOM   656  C CB  . ASP   A 1  87  ? 25.98039  42.27632 20.98515 1.000 66.04230  ? 87  ASP   A CB  1 
ATOM   657  C CG  . ASP   A 1  87  ? 27.35768  42.60884 20.50224 1.000 69.74535  ? 87  ASP   A CG  1 
ATOM   658  O OD1 . ASP   A 1  87  ? 28.29826  41.86121 20.82952 1.000 83.31672  ? 87  ASP   A OD1 1 
ATOM   659  O OD2 . ASP   A 1  87  ? 27.51033  43.62918 19.82321 1.000 75.28418  ? 87  ASP   A OD2 1 
ATOM   660  N N   . LEU   A 1  88  ? 23.78248  42.99166 23.29260 1.000 64.82519  ? 88  LEU   A N   1 
ATOM   661  C CA  . LEU   A 1  88  ? 22.33871  42.95716 23.44696 1.000 61.98041  ? 88  LEU   A CA  1 
ATOM   662  C C   . LEU   A 1  88  ? 21.70613  43.03493 22.07293 1.000 65.72837  ? 88  LEU   A C   1 
ATOM   663  O O   . LEU   A 1  88  ? 22.14834  43.79882 21.20646 1.000 58.58188  ? 88  LEU   A O   1 
ATOM   664  C CB  . LEU   A 1  88  ? 21.83448  44.11032 24.30956 1.000 57.35918  ? 88  LEU   A CB  1 
ATOM   665  C CG  . LEU   A 1  88  ? 22.48570  44.21223 25.67730 1.000 61.85274  ? 88  LEU   A CG  1 
ATOM   666  C CD1 . LEU   A 1  88  ? 21.69070  45.13080 26.58024 1.000 58.69531  ? 88  LEU   A CD1 1 
ATOM   667  C CD2 . LEU   A 1  88  ? 22.62243  42.82532 26.26002 1.000 52.71313  ? 88  LEU   A CD2 1 
ATOM   668  N N   . SER   A 1  89  ? 20.67368  42.22771 21.87539 1.000 63.21516  ? 89  SER   A N   1 
ATOM   669  C CA  . SER   A 1  89  ? 20.00191  42.18063 20.59377 1.000 61.95600  ? 89  SER   A CA  1 
ATOM   670  C C   . SER   A 1  89  ? 18.67934  41.47500 20.80685 1.000 63.38238  ? 89  SER   A C   1 
ATOM   671  O O   . SER   A 1  89  ? 18.57642  40.58358 21.64803 1.000 63.43376  ? 89  SER   A O   1 
ATOM   672  C CB  . SER   A 1  89  ? 20.85144  41.45262 19.54765 1.000 63.93892  ? 89  SER   A CB  1 
ATOM   673  O OG  . SER   A 1  89  ? 20.06704  41.09390 18.42788 1.000 69.01893  ? 89  SER   A OG  1 
ATOM   674  N N   . GLU   A 1  90  ? 17.65912  41.90903 20.06715 1.000 66.99512  ? 90  GLU   A N   1 
ATOM   675  C CA  . GLU   A 1  90  ? 16.41048  41.15609 20.04406 1.000 62.73981  ? 90  GLU   A CA  1 
ATOM   676  C C   . GLU   A 1  90  ? 16.62915  39.76484 19.46587 1.000 62.84050  ? 90  GLU   A C   1 
ATOM   677  O O   . GLU   A 1  90  ? 15.92872  38.81244 19.83793 1.000 65.26536  ? 90  GLU   A O   1 
ATOM   678  C CB  . GLU   A 1  90  ? 15.35837  41.89800 19.22612 1.000 62.90958  ? 90  GLU   A CB  1 
ATOM   679  C CG  . GLU   A 1  90  ? 14.67811  43.04223 19.92060 1.000 63.08775  ? 90  GLU   A CG  1 
ATOM   680  C CD  . GLU   A 1  90  ? 13.42409  43.46989 19.18003 1.000 71.55663  ? 90  GLU   A CD  1 
ATOM   681  O OE1 . GLU   A 1  90  ? 13.52669  44.27029 18.21038 1.000 73.59799  ? 90  GLU   A OE1 1 
ATOM   682  O OE2 . GLU   A 1  90  ? 12.33395  42.97804 19.55620 1.000 70.85673  ? 90  GLU   A OE2 1 
ATOM   683  N N   . ASP   A 1  91  ? 17.59759  39.62306 18.56598 1.000 61.79403  ? 91  ASP   A N   1 
ATOM   684  C CA  . ASP   A 1  91  ? 17.93590  38.31883 18.00735 1.000 63.71265  ? 91  ASP   A CA  1 
ATOM   685  C C   . ASP   A 1  91  ? 18.78110  37.57896 19.04224 1.000 62.06389  ? 91  ASP   A C   1 
ATOM   686  O O   . ASP   A 1  91  ? 20.00774  37.60917 19.01274 1.000 64.19945  ? 91  ASP   A O   1 
ATOM   687  C CB  . ASP   A 1  91  ? 18.64954  38.48672 16.67276 1.000 58.67962  ? 91  ASP   A CB  1 
ATOM   688  C CG  . ASP   A 1  91  ? 19.08687  37.15869 16.06288 1.000 66.49289  ? 91  ASP   A CG  1 
ATOM   689  O OD1 . ASP   A 1  91  ? 18.76149  36.08118 16.60825 1.000 59.97278  ? 91  ASP   A OD1 1 
ATOM   690  O OD2 . ASP   A 1  91  ? 19.75954  37.19574 15.01368 1.000 66.24981  ? 91  ASP   A OD2 1 
ATOM   691  N N   . CYS   A 1  92  ? 18.11769  36.88983 19.97430 1.000 61.25381  ? 92  CYS   A N   1 
ATOM   692  C CA  . CYS   A 1  92  ? 18.85388  36.33011 21.09876 1.000 60.02870  ? 92  CYS   A CA  1 
ATOM   693  C C   . CYS   A 1  92  ? 18.43777  34.91143 21.46488 1.000 58.76732  ? 92  CYS   A C   1 
ATOM   694  O O   . CYS   A 1  92  ? 18.88188  34.40291 22.50534 1.000 60.54638  ? 92  CYS   A O   1 
ATOM   695  C CB  . CYS   A 1  92  ? 18.70170  37.24117 22.31603 1.000 55.96552  ? 92  CYS   A CB  1 
ATOM   696  S SG  . CYS   A 1  92  ? 17.00142  37.41195 22.85066 1.000 61.28760  ? 92  CYS   A SG  1 
ATOM   697  N N   . LEU   A 1  93  ? 17.63880  34.23541 20.64148 1.000 59.38550  ? 93  LEU   A N   1 
ATOM   698  C CA  . LEU   A 1  93  ? 17.07727  32.93990 21.03001 1.000 52.55429  ? 93  LEU   A CA  1 
ATOM   699  C C   . LEU   A 1  93  ? 18.04166  31.83373 20.61293 1.000 60.41508  ? 93  LEU   A C   1 
ATOM   700  O O   . LEU   A 1  93  ? 17.90124  31.17812 19.57546 1.000 60.48958  ? 93  LEU   A O   1 
ATOM   701  C CB  . LEU   A 1  93  ? 15.68715  32.78093 20.43721 1.000 55.38906  ? 93  LEU   A CB  1 
ATOM   702  C CG  . LEU   A 1  93  ? 14.72826  33.81603 21.04636 1.000 63.92703  ? 93  LEU   A CG  1 
ATOM   703  C CD1 . LEU   A 1  93  ? 13.27484  33.63267 20.55520 1.000 61.80524  ? 93  LEU   A CD1 1 
ATOM   704  C CD2 . LEU   A 1  93  ? 14.81364  33.72381 22.57156 1.000 61.03623  ? 93  LEU   A CD2 1 
ATOM   705  N N   . TYR   A 1  94  ? 19.05110  31.62813 21.45762 1.000 61.63976  ? 94  TYR   A N   1 
ATOM   706  C CA  . TYR   A 1  94  ? 20.08042  30.62231 21.22323 1.000 57.07932  ? 94  TYR   A CA  1 
ATOM   707  C C   . TYR   A 1  94  ? 20.32745  29.85829 22.51522 1.000 60.66643  ? 94  TYR   A C   1 
ATOM   708  O O   . TYR   A 1  94  ? 19.90147  30.27506 23.59776 1.000 60.60617  ? 94  TYR   A O   1 
ATOM   709  C CB  . TYR   A 1  94  ? 21.38404  31.24938 20.71403 1.000 58.71445  ? 94  TYR   A CB  1 
ATOM   710  C CG  . TYR   A 1  94  ? 21.19770  32.12369 19.48771 1.000 62.26836  ? 94  TYR   A CG  1 
ATOM   711  C CD1 . TYR   A 1  94  ? 20.68153  33.41357 19.60178 1.000 56.94244  ? 94  TYR   A CD1 1 
ATOM   712  C CD2 . TYR   A 1  94  ? 21.54076  31.66343 18.21759 1.000 58.47738  ? 94  TYR   A CD2 1 
ATOM   713  C CE1 . TYR   A 1  94  ? 20.50302  34.20985 18.49976 1.000 60.80945  ? 94  TYR   A CE1 1 
ATOM   714  C CE2 . TYR   A 1  94  ? 21.37123  32.46436 17.09769 1.000 57.79033  ? 94  TYR   A CE2 1 
ATOM   715  C CZ  . TYR   A 1  94  ? 20.85000  33.73158 17.24910 1.000 63.48823  ? 94  TYR   A CZ  1 
ATOM   716  O OH  . TYR   A 1  94  ? 20.66268  34.53044 16.15576 1.000 60.69543  ? 94  TYR   A OH  1 
ATOM   717  N N   . LEU   A 1  95  ? 21.02990  28.73224 22.39775 1.000 58.53990  ? 95  LEU   A N   1 
ATOM   718  C CA  . LEU   A 1  95  ? 21.37337  27.91904 23.55461 1.000 59.13023  ? 95  LEU   A CA  1 
ATOM   719  C C   . LEU   A 1  95  ? 22.77929  27.32066 23.39610 1.000 61.07359  ? 95  LEU   A C   1 
ATOM   720  O O   . LEU   A 1  95  ? 23.38127  27.34059 22.31431 1.000 56.57474  ? 95  LEU   A O   1 
ATOM   721  C CB  . LEU   A 1  95  ? 20.32488  26.82247 23.77985 1.000 55.36659  ? 95  LEU   A CB  1 
ATOM   722  C CG  . LEU   A 1  95  ? 20.00914  25.91547 22.58004 1.000 62.02658  ? 95  LEU   A CG  1 
ATOM   723  C CD1 . LEU   A 1  95  ? 21.07111  24.82259 22.35289 1.000 59.25048  ? 95  LEU   A CD1 1 
ATOM   724  C CD2 . LEU   A 1  95  ? 18.61135  25.25905 22.75650 1.000 58.73661  ? 95  LEU   A CD2 1 
ATOM   725  N N   . ASN   A 1  96  ? 23.29187  26.76098 24.49800 1.000 58.00781  ? 96  ASN   A N   1 
ATOM   726  C CA  . ASN   A 1  96  ? 24.63208  26.18584 24.56210 1.000 59.77064  ? 96  ASN   A CA  1 
ATOM   727  C C   . ASN   A 1  96  ? 24.58498  24.73623 25.04552 1.000 59.23310  ? 96  ASN   A C   1 
ATOM   728  O O   . ASN   A 1  96  ? 23.70094  24.34177 25.81437 1.000 58.91724  ? 96  ASN   A O   1 
ATOM   729  C CB  . ASN   A 1  96  ? 25.53862  27.01478 25.49518 1.000 60.04022  ? 96  ASN   A CB  1 
ATOM   730  C CG  . ASN   A 1  96  ? 25.30672  28.52212 25.35388 1.000 64.00924  ? 96  ASN   A CG  1 
ATOM   731  O OD1 . ASN   A 1  96  ? 25.66100  29.14261 24.33701 1.000 60.33237  ? 96  ASN   A OD1 1 
ATOM   732  N ND2 . ASN   A 1  96  ? 24.67908  29.10836 26.36834 1.000 58.12938  ? 96  ASN   A ND2 1 
ATOM   733  N N   . VAL   A 1  97  ? 25.53909  23.93567 24.58160 1.000 61.08852  ? 97  VAL   A N   1 
ATOM   734  C CA  . VAL   A 1  97  ? 25.62741  22.52513 24.94935 1.000 60.06217  ? 97  VAL   A CA  1 
ATOM   735  C C   . VAL   A 1  97  ? 27.08368  22.20374 25.27204 1.000 63.60879  ? 97  VAL   A C   1 
ATOM   736  O O   . VAL   A 1  97  ? 27.98649  22.50615 24.47764 1.000 60.77906  ? 97  VAL   A O   1 
ATOM   737  C CB  . VAL   A 1  97  ? 25.09523  21.59860 23.83138 1.000 56.81187  ? 97  VAL   A CB  1 
ATOM   738  C CG1 . VAL   A 1  97  ? 25.08617  20.16409 24.30447 1.000 60.34460  ? 97  VAL   A CG1 1 
ATOM   739  C CG2 . VAL   A 1  97  ? 23.66577  22.01144 23.38046 1.000 58.67957  ? 97  VAL   A CG2 1 
ATOM   740  N N   . TRP   A 1  98  ? 27.31731  21.61769 26.44234 1.000 59.61380  ? 98  TRP   A N   1 
ATOM   741  C CA  . TRP   A 1  98  ? 28.63944  21.12100 26.82243 1.000 60.34786  ? 98  TRP   A CA  1 
ATOM   742  C C   . TRP   A 1  98  ? 28.53935  19.61002 26.91588 1.000 63.38930  ? 98  TRP   A C   1 
ATOM   743  O O   . TRP   A 1  98  ? 27.77652  19.09099 27.74312 1.000 65.01781  ? 98  TRP   A O   1 
ATOM   744  C CB  . TRP   A 1  98  ? 29.10615  21.68128 28.16892 1.000 60.21829  ? 98  TRP   A CB  1 
ATOM   745  C CG  . TRP   A 1  98  ? 29.50425  23.13632 28.19608 1.000 63.35841  ? 98  TRP   A CG  1 
ATOM   746  C CD1 . TRP   A 1  98  ? 30.76605  23.63634 28.02687 1.000 66.00815  ? 98  TRP   A CD1 1 
ATOM   747  C CD2 . TRP   A 1  98  ? 28.65736  24.27247 28.45967 1.000 61.13153  ? 98  TRP   A CD2 1 
ATOM   748  N NE1 . TRP   A 1  98  ? 30.75579  25.00338 28.14479 1.000 63.72525  ? 98  TRP   A NE1 1 
ATOM   749  C CE2 . TRP   A 1  98  ? 29.47828  25.42274 28.41026 1.000 61.19398  ? 98  TRP   A CE2 1 
ATOM   750  C CE3 . TRP   A 1  98  ? 27.29095  24.43174 28.71379 1.000 59.20693  ? 98  TRP   A CE3 1 
ATOM   751  C CZ2 . TRP   A 1  98  ? 28.97839  26.71743 28.61248 1.000 56.31874  ? 98  TRP   A CZ2 1 
ATOM   752  C CZ3 . TRP   A 1  98  ? 26.79087  25.73665 28.91992 1.000 60.61688  ? 98  TRP   A CZ3 1 
ATOM   753  C CH2 . TRP   A 1  98  ? 27.63742  26.85099 28.86423 1.000 60.93001  ? 98  TRP   A CH2 1 
ATOM   754  N N   . ILE   A 1  99  ? 29.27258  18.90457 26.06050 1.000 60.49957  ? 99  ILE   A N   1 
ATOM   755  C CA  . ILE   A 1  99  ? 29.23164  17.44629 26.11265 1.000 67.57208  ? 99  ILE   A CA  1 
ATOM   756  C C   . ILE   A 1  99  ? 30.62182  16.93295 26.47852 1.000 73.67287  ? 99  ILE   A C   1 
ATOM   757  O O   . ILE   A 1  99  ? 31.64849  17.53313 26.09938 1.000 68.65533  ? 99  ILE   A O   1 
ATOM   758  C CB  . ILE   A 1  99  ? 28.70017  16.82924 24.80179 1.000 66.57652  ? 99  ILE   A CB  1 
ATOM   759  C CG1 . ILE   A 1  99  ? 29.73197  16.88560 23.67624 1.000 72.22130  ? 99  ILE   A CG1 1 
ATOM   760  C CG2 . ILE   A 1  99  ? 27.42085  17.53792 24.34853 1.000 62.15179  ? 99  ILE   A CG2 1 
ATOM   761  C CD1 . ILE   A 1  99  ? 29.57079  15.76271 22.65279 1.000 70.33951  ? 99  ILE   A CD1 1 
ATOM   762  N N   . PRO   A 1  100 ? 30.69544  15.86011 27.25975 1.000 73.88220  ? 100 PRO   A N   1 
ATOM   763  C CA  . PRO   A 1  100 ? 31.99627  15.29745 27.62181 1.000 70.24095  ? 100 PRO   A CA  1 
ATOM   764  C C   . PRO   A 1  100 ? 32.69597  14.69540 26.41482 1.000 71.74720  ? 100 PRO   A C   1 
ATOM   765  O O   . PRO   A 1  100 ? 32.07816  14.29692 25.42710 1.000 70.03909  ? 100 PRO   A O   1 
ATOM   766  C CB  . PRO   A 1  100 ? 31.64632  14.22043 28.65719 1.000 71.85465  ? 100 PRO   A CB  1 
ATOM   767  C CG  . PRO   A 1  100 ? 30.25272  14.56888 29.14260 1.000 67.67300  ? 100 PRO   A CG  1 
ATOM   768  C CD  . PRO   A 1  100 ? 29.57773  15.21964 27.97977 1.000 67.07040  ? 100 PRO   A CD  1 
ATOM   769  N N   . ALA   A 1  101 ? 34.01792  14.66321 26.49830 1.000 72.13416  ? 101 ALA   A N   1 
ATOM   770  C CA  . ALA   A 1  101 ? 34.82837  13.97951 25.52264 1.000 75.12664  ? 101 ALA   A CA  1 
ATOM   771  C C   . ALA   A 1  101 ? 35.60962  12.88319 26.23259 1.000 78.44365  ? 101 ALA   A C   1 
ATOM   772  O O   . ALA   A 1  101 ? 36.24034  13.15148 27.26370 1.000 80.29959  ? 101 ALA   A O   1 
ATOM   773  C CB  . ALA   A 1  101 ? 35.78812  14.94594 24.81173 1.000 75.46522  ? 101 ALA   A CB  1 
ATOM   774  N N   . PRO   A 1  102 ? 35.58327  11.64040 25.73968 1.000 79.88120  ? 102 PRO   A N   1 
ATOM   775  C CA  . PRO   A 1  102 ? 34.86352  11.21635 24.53215 1.000 79.86924  ? 102 PRO   A CA  1 
ATOM   776  C C   . PRO   A 1  102 ? 33.35147  11.24609 24.68261 1.000 74.89916  ? 102 PRO   A C   1 
ATOM   777  O O   . PRO   A 1  102 ? 32.84022  11.04871 25.78510 1.000 76.41093  ? 102 PRO   A O   1 
ATOM   778  C CB  . PRO   A 1  102 ? 35.34791  9.77757  24.31651 1.000 74.66706  ? 102 PRO   A CB  1 
ATOM   779  C CG  . PRO   A 1  102 ? 36.59554  9.65115  25.15469 1.000 80.00055  ? 102 PRO   A CG  1 
ATOM   780  C CD  . PRO   A 1  102 ? 36.37258  10.54539 26.32393 1.000 80.82088  ? 102 PRO   A CD  1 
ATOM   781  N N   . LYS   A 1  103 ? 32.66930  11.50800 23.56440 1.000 73.67307  ? 103 LYS   A N   1 
ATOM   782  C CA  . LYS   A 1  103 ? 31.22393  11.60478 23.43470 1.000 70.75670  ? 103 LYS   A CA  1 
ATOM   783  C C   . LYS   A 1  103 ? 30.56634  10.54021 24.30066 1.000 75.79787  ? 103 LYS   A C   1 
ATOM   784  O O   . LYS   A 1  103 ? 30.96309  9.37039  24.25603 1.000 68.92487  ? 103 LYS   A O   1 
ATOM   785  C CB  . LYS   A 1  103 ? 30.81898  11.45433 21.96626 1.000 74.76405  ? 103 LYS   A CB  1 
ATOM   786  C CG  . LYS   A 1  103 ? 29.32321  11.42837 21.70141 1.000 78.62299  ? 103 LYS   A CG  1 
ATOM   787  C CD  . LYS   A 1  103 ? 29.03724  11.49625 20.19467 1.000 85.20550  ? 103 LYS   A CD  1 
ATOM   788  C CE  . LYS   A 1  103 ? 27.58601  11.13412 19.86525 1.000 88.23874  ? 103 LYS   A CE  1 
ATOM   789  N NZ  . LYS   A 1  103 ? 27.25486  9.68020  20.12561 1.000 88.74927  ? 103 LYS   A NZ  1 
ATOM   790  N N   . PRO   A 1  104 ? 29.59272  10.90586 25.12161 1.000 76.79880  ? 104 PRO   A N   1 
ATOM   791  C CA  . PRO   A 1  104 ? 28.97875  9.93101  26.02035 1.000 71.87854  ? 104 PRO   A CA  1 
ATOM   792  C C   . PRO   A 1  104 ? 27.98391  9.05759  25.27175 1.000 72.51360  ? 104 PRO   A C   1 
ATOM   793  O O   . PRO   A 1  104 ? 27.68290  9.26267  24.09308 1.000 68.09424  ? 104 PRO   A O   1 
ATOM   794  C CB  . PRO   A 1  104 ? 28.28894  10.80732 27.07365 1.000 65.61348  ? 104 PRO   A CB  1 
ATOM   795  C CG  . PRO   A 1  104 ? 27.95598  12.05033 26.35059 1.000 67.37317  ? 104 PRO   A CG  1 
ATOM   796  C CD  . PRO   A 1  104 ? 29.00612  12.24587 25.27161 1.000 68.18084  ? 104 PRO   A CD  1 
ATOM   797  N N   . LYS   A 1  105 ? 27.48706  8.05013  25.98496 1.000 73.11655  ? 105 LYS   A N   1 
ATOM   798  C CA  . LYS   A 1  105 ? 26.53106  7.12540  25.39785 1.000 71.42408  ? 105 LYS   A CA  1 
ATOM   799  C C   . LYS   A 1  105 ? 25.09719  7.56918  25.68325 1.000 80.79560  ? 105 LYS   A C   1 
ATOM   800  O O   . LYS   A 1  105 ? 24.35844  7.91301  24.75578 1.000 86.70315  ? 105 LYS   A O   1 
ATOM   801  C CB  . LYS   A 1  105 ? 26.80504  5.70909  25.90625 1.000 76.01480  ? 105 LYS   A CB  1 
ATOM   802  C CG  . LYS   A 1  105 ? 27.97893  5.03176  25.21527 1.000 74.49237  ? 105 LYS   A CG  1 
ATOM   803  C CD  . LYS   A 1  105 ? 27.69134  4.89844  23.73719 1.000 77.33593  ? 105 LYS   A CD  1 
ATOM   804  C CE  . LYS   A 1  105 ? 28.91663  4.49114  22.95195 1.000 83.80169  ? 105 LYS   A CE  1 
ATOM   805  N NZ  . LYS   A 1  105 ? 29.36769  3.15317  23.38774 1.000 80.91876  ? 105 LYS   A NZ  1 
ATOM   806  N N   . ASN   A 1  106 ? 24.68547  7.59102  26.96484 1.000 77.50235  ? 106 ASN   A N   1 
ATOM   807  C CA  . ASN   A 1  106 ? 23.35508  8.10144  27.31441 1.000 74.23441  ? 106 ASN   A CA  1 
ATOM   808  C C   . ASN   A 1  106 ? 23.43186  8.90323  28.61569 1.000 68.71050  ? 106 ASN   A C   1 
ATOM   809  O O   . ASN   A 1  106 ? 22.96346  8.49451  29.67504 1.000 71.84749  ? 106 ASN   A O   1 
ATOM   810  C CB  . ASN   A 1  106 ? 22.29452  6.99102  27.38490 1.000 82.14581  ? 106 ASN   A CB  1 
ATOM   811  C CG  . ASN   A 1  106 ? 21.09105  7.36375  26.55872 1.000 88.20731  ? 106 ASN   A CG  1 
ATOM   812  O OD1 . ASN   A 1  106 ? 21.17720  8.38842  25.89027 1.000 89.77914  ? 106 ASN   A OD1 1 
ATOM   813  N ND2 . ASN   A 1  106 ? 19.98160  6.62755  26.56884 1.000 103.49437 ? 106 ASN   A ND2 1 
ATOM   814  N N   . ALA   A 1  107 ? 23.98881  10.10792 28.50077 1.000 67.54067  ? 107 ALA   A N   1 
ATOM   815  C CA  . ALA   A 1  107 ? 24.30899  10.94328 29.65073 1.000 63.46424  ? 107 ALA   A CA  1 
ATOM   816  C C   . ALA   A 1  107 ? 23.10431  11.72509 30.14907 1.000 63.64604  ? 107 ALA   A C   1 
ATOM   817  O O   . ALA   A 1  107 ? 22.32880  12.28612 29.36197 1.000 60.84218  ? 107 ALA   A O   1 
ATOM   818  C CB  . ALA   A 1  107 ? 25.43124  11.91977 29.29082 1.000 54.78625  ? 107 ALA   A CB  1 
ATOM   819  N N   . THR   A 1  108 ? 22.96533  11.77291 31.46995 1.000 60.73260  ? 108 THR   A N   1 
ATOM   820  C CA  . THR   A 1  108 ? 21.99271  12.67102 32.07915 1.000 56.20793  ? 108 THR   A CA  1 
ATOM   821  C C   . THR   A 1  108 ? 22.26941  14.09635 31.64031 1.000 62.83799  ? 108 THR   A C   1 
ATOM   822  O O   . THR   A 1  108 ? 23.43293  14.52717 31.57537 1.000 61.53029  ? 108 THR   A O   1 
ATOM   823  C CB  . THR   A 1  108 ? 22.06296  12.58503 33.59873 1.000 56.53216  ? 108 THR   A CB  1 
ATOM   824  O OG1 . THR   A 1  108 ? 21.52185  11.33380 34.01402 1.000 56.57993  ? 108 THR   A OG1 1 
ATOM   825  C CG2 . THR   A 1  108 ? 21.26976  13.71103 34.25093 1.000 60.14359  ? 108 THR   A CG2 1 
ATOM   826  N N   . VAL   A 1  109 ? 21.18746  14.83454 31.36225 1.000 55.98356  ? 109 VAL   A N   1 
ATOM   827  C CA  . VAL   A 1  109 ? 21.26046  16.21307 30.89968 1.000 59.61186  ? 109 VAL   A CA  1 
ATOM   828  C C   . VAL   A 1  109 ? 20.87414  17.15478 32.03135 1.000 58.10021  ? 109 VAL   A C   1 
ATOM   829  O O   . VAL   A 1  109 ? 19.93510  16.89333 32.78767 1.000 56.40423  ? 109 VAL   A O   1 
ATOM   830  C CB  . VAL   A 1  109 ? 20.35137  16.43118 29.67375 1.000 60.33409  ? 109 VAL   A CB  1 
ATOM   831  C CG1 . VAL   A 1  109 ? 20.49849  17.84519 29.16501 1.000 54.10173  ? 109 VAL   A CG1 1 
ATOM   832  C CG2 . VAL   A 1  109 ? 20.69009  15.41652 28.57668 1.000 59.01724  ? 109 VAL   A CG2 1 
ATOM   833  N N   A LEU   A 1  110 ? 21.60097  18.25687 32.15068 0.518 56.80293  ? 110 LEU   A N   1 
ATOM   834  N N   B LEU   A 1  110 ? 21.60801  18.25423 32.14414 0.482 56.72580  ? 110 LEU   A N   1 
ATOM   835  C CA  A LEU   A 1  110 ? 21.26151  19.30694 33.09951 0.518 56.31091  ? 110 LEU   A CA  1 
ATOM   836  C CA  B LEU   A 1  110 ? 21.30315  19.32320 33.08124 0.482 54.24388  ? 110 LEU   A CA  1 
ATOM   837  C C   A LEU   A 1  110 ? 21.03728  20.60135 32.33283 0.518 57.21666  ? 110 LEU   A C   1 
ATOM   838  C C   B LEU   A 1  110 ? 21.02085  20.58592 32.28203 0.482 56.93507  ? 110 LEU   A C   1 
ATOM   839  O O   A LEU   A 1  110 ? 21.91689  21.04696 31.58608 0.518 55.73057  ? 110 LEU   A O   1 
ATOM   840  O O   B LEU   A 1  110 ? 21.84481  20.99451 31.45514 0.482 55.81008  ? 110 LEU   A O   1 
ATOM   841  C CB  A LEU   A 1  110 ? 22.35397  19.47600 34.15164 0.518 56.26336  ? 110 LEU   A CB  1 
ATOM   842  C CB  B LEU   A 1  110 ? 22.46613  19.56094 34.04737 0.482 56.15388  ? 110 LEU   A CB  1 
ATOM   843  C CG  A LEU   A 1  110 ? 22.02301  18.69495 35.42301 0.518 58.39714  ? 110 LEU   A CG  1 
ATOM   844  C CG  B LEU   A 1  110 ? 22.53985  18.71381 35.31647 0.482 58.35201  ? 110 LEU   A CG  1 
ATOM   845  C CD1 A LEU   A 1  110 ? 23.25270  17.97287 35.96078 0.518 56.77980  ? 110 LEU   A CD1 1 
ATOM   846  C CD1 B LEU   A 1  110 ? 22.43719  17.22906 34.99882 0.482 54.78500  ? 110 LEU   A CD1 1 
ATOM   847  C CD2 A LEU   A 1  110 ? 21.40048  19.61651 36.46780 0.518 50.80637  ? 110 LEU   A CD2 1 
ATOM   848  C CD2 B LEU   A 1  110 ? 23.83332  19.01170 36.04873 0.482 56.28024  ? 110 LEU   A CD2 1 
ATOM   849  N N   . ILE   A 1  111 ? 19.86437  21.19966 32.52256 1.000 57.91655  ? 111 ILE   A N   1 
ATOM   850  C CA  . ILE   A 1  111 ? 19.45306  22.39636 31.80034 1.000 58.75847  ? 111 ILE   A CA  1 
ATOM   851  C C   . ILE   A 1  111 ? 19.33534  23.56097 32.77445 1.000 53.42399  ? 111 ILE   A C   1 
ATOM   852  O O   . ILE   A 1  111 ? 18.52148  23.51930 33.70968 1.000 57.38032  ? 111 ILE   A O   1 
ATOM   853  C CB  . ILE   A 1  111 ? 18.13653  22.17715 31.05676 1.000 56.26723  ? 111 ILE   A CB  1 
ATOM   854  C CG1 . ILE   A 1  111 ? 18.31636  21.06004 30.02475 1.000 50.54900  ? 111 ILE   A CG1 1 
ATOM   855  C CG2 . ILE   A 1  111 ? 17.68315  23.50211 30.44480 1.000 45.54764  ? 111 ILE   A CG2 1 
ATOM   856  C CD1 . ILE   A 1  111 ? 17.06050  20.71691 29.24670 1.000 50.31455  ? 111 ILE   A CD1 1 
ATOM   857  N N   . TRP   A 1  112 ? 20.13121  24.60433 32.53610 1.000 50.06741  ? 112 TRP   A N   1 
ATOM   858  C CA  . TRP   A 1  112 ? 20.22011  25.77165 33.40576 1.000 52.57827  ? 112 TRP   A CA  1 
ATOM   859  C C   . TRP   A 1  112 ? 19.30390  26.89011 32.93209 1.000 51.96197  ? 112 TRP   A C   1 
ATOM   860  O O   . TRP   A 1  112 ? 19.31146  27.23814 31.74691 1.000 51.17328  ? 112 TRP   A O   1 
ATOM   861  C CB  . TRP   A 1  112 ? 21.64801  26.29577 33.44005 1.000 54.82073  ? 112 TRP   A CB  1 
ATOM   862  C CG  . TRP   A 1  112 ? 21.81745  27.59367 34.23045 1.000 52.19019  ? 112 TRP   A CG  1 
ATOM   863  C CD1 . TRP   A 1  112 ? 22.08911  28.82312 33.73267 1.000 52.44187  ? 112 TRP   A CD1 1 
ATOM   864  C CD2 . TRP   A 1  112 ? 21.76580  27.73808 35.66276 1.000 51.14247  ? 112 TRP   A CD2 1 
ATOM   865  N NE1 . TRP   A 1  112 ? 22.21568  29.73384 34.76240 1.000 55.25296  ? 112 TRP   A NE1 1 
ATOM   866  C CE2 . TRP   A 1  112 ? 22.02302  29.08641 35.95523 1.000 49.51430  ? 112 TRP   A CE2 1 
ATOM   867  C CE3 . TRP   A 1  112 ? 21.53272  26.84489 36.72506 1.000 51.84825  ? 112 TRP   A CE3 1 
ATOM   868  C CZ2 . TRP   A 1  112 ? 22.04441  29.57803 37.25723 1.000 48.69879  ? 112 TRP   A CZ2 1 
ATOM   869  C CZ3 . TRP   A 1  112 ? 21.56004  27.33298 38.02194 1.000 52.37070  ? 112 TRP   A CZ3 1 
ATOM   870  C CH2 . TRP   A 1  112 ? 21.81476  28.69485 38.27550 1.000 49.00045  ? 112 TRP   A CH2 1 
ATOM   871  N N   . ILE   A 1  113 ? 18.55851  27.48143 33.86670 1.000 55.20613  ? 113 ILE   A N   1 
ATOM   872  C CA  . ILE   A 1  113 ? 17.69625  28.63997 33.59810 1.000 53.41506  ? 113 ILE   A CA  1 
ATOM   873  C C   . ILE   A 1  113 ? 18.15565  29.76533 34.51817 1.000 54.82543  ? 113 ILE   A C   1 
ATOM   874  O O   . ILE   A 1  113 ? 18.01082  29.66029 35.74449 1.000 55.65968  ? 113 ILE   A O   1 
ATOM   875  C CB  . ILE   A 1  113 ? 16.21407  28.30977 33.81547 1.000 54.10035  ? 113 ILE   A CB  1 
ATOM   876  C CG1 . ILE   A 1  113 ? 15.76557  27.18928 32.86539 1.000 44.64590  ? 113 ILE   A CG1 1 
ATOM   877  C CG2 . ILE   A 1  113 ? 15.32643  29.56864 33.64192 1.000 46.15229  ? 113 ILE   A CG2 1 
ATOM   878  C CD1 . ILE   A 1  113 ? 14.31366  26.70624 33.13269 1.000 48.07567  ? 113 ILE   A CD1 1 
ATOM   879  N N   . TYR   A 1  114 ? 18.72942  30.83133 33.94094 1.000 52.13795  ? 114 TYR   A N   1 
ATOM   880  C CA  . TYR   A 1  114 ? 19.30774  31.91150 34.73961 1.000 50.96264  ? 114 TYR   A CA  1 
ATOM   881  C C   . TYR   A 1  114 ? 18.22166  32.81979 35.32451 1.000 56.86809  ? 114 TYR   A C   1 
ATOM   882  O O   . TYR   A 1  114 ? 17.07998  32.87473 34.84070 1.000 53.80982  ? 114 TYR   A O   1 
ATOM   883  C CB  . TYR   A 1  114 ? 20.28378  32.76643 33.91135 1.000 56.08348  ? 114 TYR   A CB  1 
ATOM   884  C CG  . TYR   A 1  114 ? 19.69377  33.38274 32.63794 1.000 55.40413  ? 114 TYR   A CG  1 
ATOM   885  C CD1 . TYR   A 1  114 ? 18.78303  34.44824 32.69155 1.000 48.80776  ? 114 TYR   A CD1 1 
ATOM   886  C CD2 . TYR   A 1  114 ? 20.07087  32.90887 31.37983 1.000 57.73025  ? 114 TYR   A CD2 1 
ATOM   887  C CE1 . TYR   A 1  114 ? 18.25463  35.00178 31.52030 1.000 56.04203  ? 114 TYR   A CE1 1 
ATOM   888  C CE2 . TYR   A 1  114 ? 19.54880  33.46209 30.19962 1.000 53.02381  ? 114 TYR   A CE2 1 
ATOM   889  C CZ  . TYR   A 1  114 ? 18.64612  34.49326 30.27512 1.000 53.54168  ? 114 TYR   A CZ  1 
ATOM   890  O OH  . TYR   A 1  114 ? 18.13614  34.99840 29.10443 1.000 54.43853  ? 114 TYR   A OH  1 
ATOM   891  N N   . GLY   A 1  115 ? 18.61157  33.56539 36.36223 1.000 52.05179  ? 115 GLY   A N   1 
ATOM   892  C CA  . GLY   A 1  115 ? 17.75781  34.54604 36.98454 1.000 54.54046  ? 115 GLY   A CA  1 
ATOM   893  C C   . GLY   A 1  115 ? 18.17650  35.96150 36.63717 1.000 58.17919  ? 115 GLY   A C   1 
ATOM   894  O O   . GLY   A 1  115 ? 18.98221  36.20185 35.73918 1.000 55.58252  ? 115 GLY   A O   1 
ATOM   895  N N   . GLY   A 1  116 ? 17.61701  36.90548 37.38371 1.000 58.10874  ? 116 GLY   A N   1 
ATOM   896  C CA  . GLY   A 1  116 ? 17.76007  38.30709 37.06224 1.000 60.06889  ? 116 GLY   A CA  1 
ATOM   897  C C   . GLY   A 1  116 ? 16.43682  39.04552 37.08640 1.000 65.86438  ? 116 GLY   A C   1 
ATOM   898  O O   . GLY   A 1  116 ? 16.23402  39.99486 36.31864 1.000 67.21648  ? 116 GLY   A O   1 
ATOM   899  N N   . GLY   A 1  117 ? 15.52417  38.61569 37.95831 1.000 62.14760  ? 117 GLY   A N   1 
ATOM   900  C CA  . GLY   A 1  117 ? 14.25589  39.30993 38.13620 1.000 65.02582  ? 117 GLY   A CA  1 
ATOM   901  C C   . GLY   A 1  117 ? 13.28647  39.25565 36.96322 1.000 62.40994  ? 117 GLY   A C   1 
ATOM   902  O O   . GLY   A 1  117 ? 12.36762  40.07571 36.91090 1.000 60.87837  ? 117 GLY   A O   1 
ATOM   903  N N   . PHE   A 1  118 ? 13.45316  38.30709 36.02645 1.000 51.38901  ? 118 PHE   A N   1 
ATOM   904  C CA  . PHE   A 1  118 ? 12.74740  38.27669 34.74176 1.000 58.22702  ? 118 PHE   A CA  1 
ATOM   905  C C   . PHE   A 1  118 ? 12.97993  39.53489 33.90117 1.000 56.84557  ? 118 PHE   A C   1 
ATOM   906  O O   . PHE   A 1  118 ? 12.28556  39.73997 32.90160 1.000 52.28567  ? 118 PHE   A O   1 
ATOM   907  C CB  . PHE   A 1  118 ? 11.22916  38.05787 34.90889 1.000 52.64215  ? 118 PHE   A CB  1 
ATOM   908  C CG  . PHE   A 1  118 ? 10.87683  36.76146 35.57021 1.000 53.18504  ? 118 PHE   A CG  1 
ATOM   909  C CD1 . PHE   A 1  118 ? 10.99531  35.56146 34.88338 1.000 49.62933  ? 118 PHE   A CD1 1 
ATOM   910  C CD2 . PHE   A 1  118 ? 10.45206  36.74118 36.89386 1.000 53.53074  ? 118 PHE   A CD2 1 
ATOM   911  C CE1 . PHE   A 1  118 ? 10.68400  34.35367 35.50947 1.000 51.12508  ? 118 PHE   A CE1 1 
ATOM   912  C CE2 . PHE   A 1  118 ? 10.14393  35.56274 37.51950 1.000 50.57907  ? 118 PHE   A CE2 1 
ATOM   913  C CZ  . PHE   A 1  118 ? 10.24758  34.35168 36.82351 1.000 48.30158  ? 118 PHE   A CZ  1 
ATOM   914  N N   . GLN   A 1  119 ? 13.92168  40.39428 34.28885 1.000 52.48358  ? 119 GLN   A N   1 
ATOM   915  C CA  . GLN   A 1  119 ? 14.23566  41.57297 33.49383 1.000 60.57868  ? 119 GLN   A CA  1 
ATOM   916  C C   . GLN   A 1  119 ? 15.65307  41.56289 32.95073 1.000 60.59206  ? 119 GLN   A C   1 
ATOM   917  O O   . GLN   A 1  119 ? 15.94489  42.33138 32.03498 1.000 59.68731  ? 119 GLN   A O   1 
ATOM   918  C CB  . GLN   A 1  119 ? 14.04505  42.86823 34.30792 1.000 51.61922  ? 119 GLN   A CB  1 
ATOM   919  C CG  . GLN   A 1  119 ? 12.90829  42.86026 35.31767 1.000 62.20349  ? 119 GLN   A CG  1 
ATOM   920  C CD  . GLN   A 1  119 ? 11.53103  42.73960 34.66272 1.000 64.84777  ? 119 GLN   A CD  1 
ATOM   921  O OE1 . GLN   A 1  119 ? 11.12796  43.59483 33.87121 1.000 66.67638  ? 119 GLN   A OE1 1 
ATOM   922  N NE2 . GLN   A 1  119 ? 10.81074  41.66940 34.98653 1.000 57.96750  ? 119 GLN   A NE2 1 
ATOM   923  N N   . THR   A 1  120 ? 16.54499  40.73838 33.50360 1.000 60.00012  ? 120 THR   A N   1 
ATOM   924  C CA  . THR   A 1  120 ? 17.95196  40.73799 33.10707 1.000 63.69705  ? 120 THR   A CA  1 
ATOM   925  C C   . THR   A 1  120 ? 18.44225  39.29299 33.06455 1.000 59.53886  ? 120 THR   A C   1 
ATOM   926  O O   . THR   A 1  120 ? 17.70040  38.35266 33.37480 1.000 55.36965  ? 120 THR   A O   1 
ATOM   927  C CB  . THR   A 1  120 ? 18.84137  41.59159 34.05246 1.000 59.96084  ? 120 THR   A CB  1 
ATOM   928  O OG1 . THR   A 1  120 ? 18.96695  40.94354 35.32873 1.000 65.64388  ? 120 THR   A OG1 1 
ATOM   929  C CG2 . THR   A 1  120 ? 18.29720  43.00759 34.25325 1.000 50.58455  ? 120 THR   A CG2 1 
ATOM   930  N N   . GLY   A 1  121 ? 19.71170  39.12407 32.68136 1.000 57.12490  ? 121 GLY   A N   1 
ATOM   931  C CA  . GLY   A 1  121 ? 20.33926  37.82060 32.71239 1.000 55.89726  ? 121 GLY   A CA  1 
ATOM   932  C C   . GLY   A 1  121 ? 20.81278  37.34489 31.35326 1.000 58.53111  ? 121 GLY   A C   1 
ATOM   933  O O   . GLY   A 1  121 ? 20.36433  37.83716 30.30649 1.000 54.67142  ? 121 GLY   A O   1 
ATOM   934  N N   . THR   A 1  122 ? 21.74325  36.39784 31.36166 1.000 54.69690  ? 122 THR   A N   1 
ATOM   935  C CA  . THR   A 1  122 ? 22.18397  35.76829 30.12391 1.000 61.08455  ? 122 THR   A CA  1 
ATOM   936  C C   . THR   A 1  122 ? 22.96255  34.51068 30.47026 1.000 58.64019  ? 122 THR   A C   1 
ATOM   937  O O   . THR   A 1  122 ? 23.60136  34.43110 31.52451 1.000 57.79647  ? 122 THR   A O   1 
ATOM   938  C CB  . THR   A 1  122 ? 23.04142  36.70152 29.26007 1.000 54.01761  ? 122 THR   A CB  1 
ATOM   939  O OG1 . THR   A 1  122 ? 23.33546  36.05132 28.01876 1.000 58.68999  ? 122 THR   A OG1 1 
ATOM   940  C CG2 . THR   A 1  122 ? 24.34653  37.08509 29.96010 1.000 51.44600  ? 122 THR   A CG2 1 
ATOM   941  N N   . SER   A 1  123 ? 22.90435  33.53220 29.56972 1.000 56.77949  ? 123 SER   A N   1 
ATOM   942  C CA  . SER   A 1  123 ? 23.54328  32.24925 29.82529 1.000 55.76187  ? 123 SER   A CA  1 
ATOM   943  C C   . SER   A 1  123 ? 25.04514  32.28780 29.60122 1.000 59.60521  ? 123 SER   A C   1 
ATOM   944  O O   . SER   A 1  123 ? 25.73229  31.33687 29.98311 1.000 59.84577  ? 123 SER   A O   1 
ATOM   945  C CB  . SER   A 1  123 ? 22.93310  31.16567 28.94145 1.000 52.75185  ? 123 SER   A CB  1 
ATOM   946  O OG  . SER   A 1  123 ? 23.04026  31.50375 27.57581 1.000 55.18814  ? 123 SER   A OG  1 
ATOM   947  N N   . SER   A 1  124 ? 25.56828  33.34679 28.98347 1.000 56.49165  ? 124 SER   A N   1 
ATOM   948  C CA  . SER   A 1  124 ? 26.98875  33.38757 28.67913 1.000 56.05501  ? 124 SER   A CA  1 
ATOM   949  C C   . SER   A 1  124 ? 27.83501  33.80194 29.87834 1.000 59.19783  ? 124 SER   A C   1 
ATOM   950  O O   . SER   A 1  124 ? 29.05471  33.89169 29.74492 1.000 61.63690  ? 124 SER   A O   1 
ATOM   951  C CB  . SER   A 1  124 ? 27.25183  34.33269 27.49485 1.000 60.86959  ? 124 SER   A CB  1 
ATOM   952  O OG  . SER   A 1  124 ? 26.52299  35.54211 27.56951 1.000 56.37231  ? 124 SER   A OG  1 
ATOM   953  N N   . LEU   A 1  125 ? 27.23188  34.04616 31.03973 1.000 60.67117  ? 125 LEU   A N   1 
ATOM   954  C CA  . LEU   A 1  125 ? 27.99151  34.53170 32.18602 1.000 54.65070  ? 125 LEU   A CA  1 
ATOM   955  C C   . LEU   A 1  125 ? 29.03895  33.51099 32.62884 1.000 54.38960  ? 125 LEU   A C   1 
ATOM   956  O O   . LEU   A 1  125 ? 28.83773  32.29344 32.55567 1.000 59.58026  ? 125 LEU   A O   1 
ATOM   957  C CB  . LEU   A 1  125 ? 27.05636  34.85772 33.35017 1.000 56.06503  ? 125 LEU   A CB  1 
ATOM   958  C CG  . LEU   A 1  125 ? 26.05459  36.00919 33.21226 1.000 57.92617  ? 125 LEU   A CG  1 
ATOM   959  C CD1 . LEU   A 1  125 ? 25.35093  36.25900 34.54893 1.000 52.20977  ? 125 LEU   A CD1 1 
ATOM   960  C CD2 . LEU   A 1  125 ? 26.73691  37.28248 32.70674 1.000 58.82703  ? 125 LEU   A CD2 1 
ATOM   961  N N   . HIS   A 1  126 ? 30.16287  34.04373 33.10754 1.000 55.11430  ? 126 HIS   A N   1 
ATOM   962  C CA  . HIS   A 1  126 ? 31.30140  33.24402 33.54598 1.000 55.92714  ? 126 HIS   A CA  1 
ATOM   963  C C   . HIS   A 1  126 ? 30.90230  32.23215 34.62102 1.000 64.11969  ? 126 HIS   A C   1 
ATOM   964  O O   . HIS   A 1  126 ? 31.40542  31.09963 34.63554 1.000 57.05584  ? 126 HIS   A O   1 
ATOM   965  C CB  . HIS   A 1  126 ? 32.39569  34.19501 34.05548 1.000 66.78232  ? 126 HIS   A CB  1 
ATOM   966  C CG  . HIS   A 1  126 ? 33.58166  33.51994 34.67723 1.000 72.39119  ? 126 HIS   A CG  1 
ATOM   967  N ND1 . HIS   A 1  126 ? 33.98517  33.77834 35.97152 1.000 77.33671  ? 126 HIS   A ND1 1 
ATOM   968  C CD2 . HIS   A 1  126 ? 34.49281  32.65460 34.16776 1.000 73.87126  ? 126 HIS   A CD2 1 
ATOM   969  C CE1 . HIS   A 1  126 ? 35.07028  33.07486 36.24488 1.000 77.12539  ? 126 HIS   A CE1 1 
ATOM   970  N NE2 . HIS   A 1  126 ? 35.39878  32.38365 35.16747 1.000 74.94557  ? 126 HIS   A NE2 1 
ATOM   971  N N   . VAL   A 1  127 ? 30.00535  32.61917 35.53767 1.000 55.11761  ? 127 VAL   A N   1 
ATOM   972  C CA  . VAL   A 1  127 ? 29.60191  31.70382 36.60114 1.000 59.93859  ? 127 VAL   A CA  1 
ATOM   973  C C   . VAL   A 1  127 ? 28.58279  30.67148 36.13885 1.000 60.89442  ? 127 VAL   A C   1 
ATOM   974  O O   . VAL   A 1  127 ? 28.14294  29.84604 36.94677 1.000 52.46096  ? 127 VAL   A O   1 
ATOM   975  C CB  . VAL   A 1  127 ? 29.08514  32.50563 37.81653 1.000 60.96383  ? 127 VAL   A CB  1 
ATOM   976  C CG1 . VAL   A 1  127 ? 30.19157  33.41878 38.32433 1.000 52.58346  ? 127 VAL   A CG1 1 
ATOM   977  C CG2 . VAL   A 1  127 ? 27.80469  33.30650 37.48832 1.000 47.29242  ? 127 VAL   A CG2 1 
ATOM   978  N N   . TYR   A 1  128 ? 28.20165  30.67790 34.86213 1.000 60.79355  ? 128 TYR   A N   1 
ATOM   979  C CA  . TYR   A 1  128 ? 27.31165  29.65871 34.31707 1.000 58.35080  ? 128 TYR   A CA  1 
ATOM   980  C C   . TYR   A 1  128 ? 28.03065  28.71492 33.36832 1.000 61.10146  ? 128 TYR   A C   1 
ATOM   981  O O   . TYR   A 1  128 ? 27.36582  27.98186 32.63113 1.000 60.57280  ? 128 TYR   A O   1 
ATOM   982  C CB  . TYR   A 1  128 ? 26.13422  30.29759 33.58086 1.000 59.62365  ? 128 TYR   A CB  1 
ATOM   983  C CG  . TYR   A 1  128 ? 25.27369  31.25458 34.38615 1.000 59.38918  ? 128 TYR   A CG  1 
ATOM   984  C CD1 . TYR   A 1  128 ? 25.15320  31.13283 35.77712 1.000 54.22294  ? 128 TYR   A CD1 1 
ATOM   985  C CD2 . TYR   A 1  128 ? 24.57563  32.27929 33.74640 1.000 51.87266  ? 128 TYR   A CD2 1 
ATOM   986  C CE1 . TYR   A 1  128 ? 24.34830  32.00820 36.49682 1.000 49.12678  ? 128 TYR   A CE1 1 
ATOM   987  C CE2 . TYR   A 1  128 ? 23.78106  33.14980 34.44847 1.000 50.04228  ? 128 TYR   A CE2 1 
ATOM   988  C CZ  . TYR   A 1  128 ? 23.67541  33.02551 35.81681 1.000 52.88512  ? 128 TYR   A CZ  1 
ATOM   989  O OH  . TYR   A 1  128 ? 22.86620  33.91364 36.48722 1.000 54.80732  ? 128 TYR   A OH  1 
ATOM   990  N N   . ASP   A 1  129 ? 29.36479  28.74602 33.33888 1.000 54.17813  ? 129 ASP   A N   1 
ATOM   991  C CA  . ASP   A 1  129 ? 30.14102  27.90494 32.43510 1.000 56.51574  ? 129 ASP   A CA  1 
ATOM   992  C C   . ASP   A 1  129 ? 29.95011  26.44225 32.80791 1.000 60.30899  ? 129 ASP   A C   1 
ATOM   993  O O   . ASP   A 1  129 ? 30.41852  25.99915 33.85956 1.000 58.37834  ? 129 ASP   A O   1 
ATOM   994  C CB  . ASP   A 1  129 ? 31.61333  28.28875 32.49925 1.000 56.97252  ? 129 ASP   A CB  1 
ATOM   995  C CG  . ASP   A 1  129 ? 32.39438  27.82343 31.28499 1.000 62.42470  ? 129 ASP   A CG  1 
ATOM   996  O OD1 . ASP   A 1  129 ? 31.98334  26.83271 30.63052 1.000 65.74385  ? 129 ASP   A OD1 1 
ATOM   997  O OD2 . ASP   A 1  129 ? 33.43142  28.44104 30.99114 1.000 66.08952  ? 129 ASP   A OD2 1 
ATOM   998  N N   . GLY   A 1  130 ? 29.27767  25.68397 31.93922 1.000 58.29204  ? 130 GLY   A N   1 
ATOM   999  C CA  . GLY   A 1  130 ? 29.01435  24.29025 32.19239 1.000 55.61582  ? 130 GLY   A CA  1 
ATOM   1000 C C   . GLY   A 1  130 ? 30.13668  23.31669 31.87886 1.000 64.97918  ? 130 GLY   A C   1 
ATOM   1001 O O   . GLY   A 1  130 ? 29.92864  22.10656 32.00810 1.000 63.32777  ? 130 GLY   A O   1 
ATOM   1002 N N   . LYS   A 1  131 ? 31.32415  23.79225 31.48534 1.000 58.35702  ? 131 LYS   A N   1 
ATOM   1003 C CA  . LYS   A 1  131 ? 32.37718  22.87009 31.08183 1.000 62.19591  ? 131 LYS   A CA  1 
ATOM   1004 C C   . LYS   A 1  131 ? 32.90886  22.05990 32.26357 1.000 66.14381  ? 131 LYS   A C   1 
ATOM   1005 O O   . LYS   A 1  131 ? 33.34187  20.91652 32.08086 1.000 65.97346  ? 131 LYS   A O   1 
ATOM   1006 C CB  . LYS   A 1  131 ? 33.52031  23.63180 30.40540 1.000 62.95399  ? 131 LYS   A CB  1 
ATOM   1007 C CG  . LYS   A 1  131 ? 34.32479  24.49847 31.35064 1.000 65.47880  ? 131 LYS   A CG  1 
ATOM   1008 C CD  . LYS   A 1  131 ? 35.15936  25.52153 30.59482 1.000 72.42324  ? 131 LYS   A CD  1 
ATOM   1009 C CE  . LYS   A 1  131 ? 36.30384  26.02671 31.45263 1.000 67.76226  ? 131 LYS   A CE  1 
ATOM   1010 N NZ  . LYS   A 1  131 ? 37.03922  27.14236 30.80200 1.000 71.44192  ? 131 LYS   A NZ  1 
ATOM   1011 N N   . PHE   A 1  132 ? 32.89165  22.61621 33.47699 1.000 61.14189  ? 132 PHE   A N   1 
ATOM   1012 C CA  . PHE   A 1  132 ? 33.41359  21.85696 34.60577 1.000 59.22673  ? 132 PHE   A CA  1 
ATOM   1013 C C   . PHE   A 1  132 ? 32.49333  20.68809 34.92773 1.000 63.10153  ? 132 PHE   A C   1 
ATOM   1014 O O   . PHE   A 1  132 ? 32.96014  19.57651 35.18978 1.000 62.13338  ? 132 PHE   A O   1 
ATOM   1015 C CB  . PHE   A 1  132 ? 33.59174  22.77393 35.81961 1.000 66.76397  ? 132 PHE   A CB  1 
ATOM   1016 C CG  . PHE   A 1  132 ? 34.57270  23.90175 35.58982 1.000 67.52181  ? 132 PHE   A CG  1 
ATOM   1017 C CD1 . PHE   A 1  132 ? 34.16565  25.22610 35.71059 1.000 67.44509  ? 132 PHE   A CD1 1 
ATOM   1018 C CD2 . PHE   A 1  132 ? 35.88476  23.63861 35.22901 1.000 60.13273  ? 132 PHE   A CD2 1 
ATOM   1019 C CE1 . PHE   A 1  132 ? 35.04997  26.26950 35.48012 1.000 68.57352  ? 132 PHE   A CE1 1 
ATOM   1020 C CE2 . PHE   A 1  132 ? 36.78034  24.67641 34.99587 1.000 71.52145  ? 132 PHE   A CE2 1 
ATOM   1021 C CZ  . PHE   A 1  132 ? 36.36372  25.99915 35.12251 1.000 69.49980  ? 132 PHE   A CZ  1 
ATOM   1022 N N   . LEU   A 1  133 ? 31.17828  20.91973 34.87733 1.000 62.78397  ? 133 LEU   A N   1 
ATOM   1023 C CA  . LEU   A 1  133 ? 30.20522  19.86690 35.14675 1.000 60.61970  ? 133 LEU   A CA  1 
ATOM   1024 C C   . LEU   A 1  133 ? 30.31676  18.73317 34.13425 1.000 64.73864  ? 133 LEU   A C   1 
ATOM   1025 O O   . LEU   A 1  133 ? 30.28932  17.55048 34.50130 1.000 66.05191  ? 133 LEU   A O   1 
ATOM   1026 C CB  . LEU   A 1  133 ? 28.80083  20.46800 35.14177 1.000 58.13064  ? 133 LEU   A CB  1 
ATOM   1027 C CG  . LEU   A 1  133 ? 28.44604  21.17924 36.45265 1.000 59.35391  ? 133 LEU   A CG  1 
ATOM   1028 C CD1 . LEU   A 1  133 ? 27.23195  22.09032 36.30623 1.000 59.16450  ? 133 LEU   A CD1 1 
ATOM   1029 C CD2 . LEU   A 1  133 ? 28.17791  20.11956 37.51035 1.000 62.88721  ? 133 LEU   A CD2 1 
ATOM   1030 N N   . ALA   A 1  134 ? 30.44985  19.07581 32.85516 1.000 64.81339  ? 134 ALA   A N   1 
ATOM   1031 C CA  . ALA   A 1  134 ? 30.63023  18.06047 31.82859 1.000 64.73285  ? 134 ALA   A CA  1 
ATOM   1032 C C   . ALA   A 1  134 ? 31.88727  17.23259 32.10323 1.000 66.48467  ? 134 ALA   A C   1 
ATOM   1033 O O   . ALA   A 1  134 ? 31.85010  15.99327 32.10398 1.000 58.80033  ? 134 ALA   A O   1 
ATOM   1034 C CB  . ALA   A 1  134 ? 30.68941  18.74115 30.45564 1.000 59.57207  ? 134 ALA   A CB  1 
ATOM   1035 N N   . ARG   A 1  135 ? 32.99960  17.91496 32.39023 1.000 65.75912  ? 135 ARG   A N   1 
ATOM   1036 C CA  . ARG   A 1  135 ? 34.27586  17.24848 32.63083 1.000 63.88716  ? 135 ARG   A CA  1 
ATOM   1037 C C   . ARG   A 1  135 ? 34.23354  16.34974 33.86578 1.000 65.33907  ? 135 ARG   A C   1 
ATOM   1038 O O   . ARG   A 1  135 ? 34.60298  15.17105 33.80933 1.000 70.00913  ? 135 ARG   A O   1 
ATOM   1039 C CB  . ARG   A 1  135 ? 35.36544  18.30351 32.79260 1.000 64.76079  ? 135 ARG   A CB  1 
ATOM   1040 C CG  . ARG   A 1  135 ? 36.71331  17.74115 33.21883 1.000 73.38572  ? 135 ARG   A CG  1 
ATOM   1041 C CD  . ARG   A 1  135 ? 37.29073  16.85677 32.14185 1.000 66.08283  ? 135 ARG   A CD  1 
ATOM   1042 N NE  . ARG   A 1  135 ? 38.61987  16.37030 32.49017 1.000 81.75126  ? 135 ARG   A NE  1 
ATOM   1043 C CZ  . ARG   A 1  135 ? 38.89728  15.13515 32.89006 1.000 82.45418  ? 135 ARG   A CZ  1 
ATOM   1044 N NH1 . ARG   A 1  135 ? 37.94473  14.22638 33.04901 1.000 77.17801  ? 135 ARG   A NH1 1 
ATOM   1045 N NH2 . ARG   A 1  135 ? 40.16266  14.80493 33.13606 1.000 79.35367  ? 135 ARG   A NH2 1 
ATOM   1046 N N   . VAL   A 1  136 ? 33.81789  16.90600 35.00143 1.000 65.86309  ? 136 VAL   A N   1 
ATOM   1047 C CA  . VAL   A 1  136 ? 33.96425  16.22667 36.28225 1.000 61.15304  ? 136 VAL   A CA  1 
ATOM   1048 C C   . VAL   A 1  136 ? 32.92097  15.12394 36.44725 1.000 64.63668  ? 136 VAL   A C   1 
ATOM   1049 O O   . VAL   A 1  136 ? 33.22916  14.03893 36.95040 1.000 60.92628  ? 136 VAL   A O   1 
ATOM   1050 C CB  . VAL   A 1  136 ? 33.89030  17.26452 37.42186 1.000 66.33172  ? 136 VAL   A CB  1 
ATOM   1051 C CG1 . VAL   A 1  136 ? 33.77252  16.59010 38.78293 1.000 63.47124  ? 136 VAL   A CG1 1 
ATOM   1052 C CG2 . VAL   A 1  136 ? 35.11171  18.15864 37.38166 1.000 63.84421  ? 136 VAL   A CG2 1 
ATOM   1053 N N   . GLU   A 1  137 ? 31.66651  15.37943 36.05864 1.000 65.56195  ? 137 GLU   A N   1 
ATOM   1054 C CA  . GLU   A 1  137 ? 30.58609  14.44605 36.35363 1.000 64.15889  ? 137 GLU   A CA  1 
ATOM   1055 C C   . GLU   A 1  137 ? 30.03158  13.72844 35.12632 1.000 62.74610  ? 137 GLU   A C   1 
ATOM   1056 O O   . GLU   A 1  137 ? 29.15413  12.86848 35.27718 1.000 54.66430  ? 137 GLU   A O   1 
ATOM   1057 C CB  . GLU   A 1  137 ? 29.45059  15.16867 37.09423 1.000 60.92523  ? 137 GLU   A CB  1 
ATOM   1058 C CG  . GLU   A 1  137 ? 29.80517  15.51827 38.53312 1.000 57.28008  ? 137 GLU   A CG  1 
ATOM   1059 C CD  . GLU   A 1  137 ? 30.06053  14.28335 39.42597 1.000 67.22478  ? 137 GLU   A CD  1 
ATOM   1060 O OE1 . GLU   A 1  137 ? 29.49529  13.18894 39.17423 1.000 67.70440  ? 137 GLU   A OE1 1 
ATOM   1061 O OE2 . GLU   A 1  137 ? 30.83041  14.41377 40.39842 1.000 63.64246  ? 137 GLU   A OE2 1 
ATOM   1062 N N   . ARG   A 1  138 ? 30.51002  14.05539 33.92398 1.000 63.20214  ? 138 ARG   A N   1 
ATOM   1063 C CA  . ARG   A 1  138 ? 30.10013  13.39699 32.68271 1.000 61.55698  ? 138 ARG   A CA  1 
ATOM   1064 C C   . ARG   A 1  138 ? 28.61780  13.61091 32.37043 1.000 61.78097  ? 138 ARG   A C   1 
ATOM   1065 O O   . ARG   A 1  138 ? 28.01288  12.82734 31.64104 1.000 63.05441  ? 138 ARG   A O   1 
ATOM   1066 C CB  . ARG   A 1  138 ? 30.42471  11.89979 32.70819 1.000 66.13072  ? 138 ARG   A CB  1 
ATOM   1067 C CG  . ARG   A 1  138 ? 31.92590  11.53605 32.69935 1.000 76.58557  ? 138 ARG   A CG  1 
ATOM   1068 C CD  . ARG   A 1  138 ? 32.60659  11.98711 31.41515 1.000 87.36395  ? 138 ARG   A CD  1 
ATOM   1069 N NE  . ARG   A 1  138 ? 32.33635  11.09204 30.29260 1.000 96.70609  ? 138 ARG   A NE  1 
ATOM   1070 C CZ  . ARG   A 1  138 ? 33.15127  10.90137 29.26316 1.000 91.09577  ? 138 ARG   A CZ  1 
ATOM   1071 N NH1 . ARG   A 1  138 ? 34.34302  11.48325 29.20445 1.000 82.67185  ? 138 ARG   A NH1 1 
ATOM   1072 N NH2 . ARG   A 1  138 ? 32.74921  10.12881 28.25594 1.000 88.00949  ? 138 ARG   A NH2 1 
ATOM   1073 N N   . VAL   A 1  139 ? 28.01377  14.66470 32.90316 1.000 57.04474  ? 139 VAL   A N   1 
ATOM   1074 C CA  . VAL   A 1  139 ? 26.68943  15.09751 32.47352 1.000 62.04477  ? 139 VAL   A CA  1 
ATOM   1075 C C   . VAL   A 1  139 ? 26.81539  16.00556 31.25433 1.000 59.23756  ? 139 VAL   A C   1 
ATOM   1076 O O   . VAL   A 1  139 ? 27.86122  16.60265 30.99465 1.000 56.85745  ? 139 VAL   A O   1 
ATOM   1077 C CB  . VAL   A 1  139 ? 25.95015  15.82156 33.60836 1.000 62.14877  ? 139 VAL   A CB  1 
ATOM   1078 C CG1 . VAL   A 1  139 ? 25.46115  14.82013 34.63751 1.000 53.74894  ? 139 VAL   A CG1 1 
ATOM   1079 C CG2 . VAL   A 1  139 ? 26.87674  16.88371 34.22090 1.000 56.79624  ? 139 VAL   A CG2 1 
ATOM   1080 N N   . ILE   A 1  140 ? 25.72800  16.13059 30.50556 1.000 60.31322  ? 140 ILE   A N   1 
ATOM   1081 C CA  . ILE   A 1  140 ? 25.63082  17.15621 29.47646 1.000 59.26802  ? 140 ILE   A CA  1 
ATOM   1082 C C   . ILE   A 1  140 ? 24.91933  18.35786 30.06889 1.000 55.38469  ? 140 ILE   A C   1 
ATOM   1083 O O   . ILE   A 1  140 ? 23.87066  18.20846 30.70540 1.000 63.15583  ? 140 ILE   A O   1 
ATOM   1084 C CB  . ILE   A 1  140 ? 24.88745  16.63292 28.24324 1.000 58.26882  ? 140 ILE   A CB  1 
ATOM   1085 C CG1 . ILE   A 1  140 ? 25.83335  15.78538 27.41597 1.000 58.81389  ? 140 ILE   A CG1 1 
ATOM   1086 C CG2 . ILE   A 1  140 ? 24.30401  17.80123 27.42028 1.000 57.57646  ? 140 ILE   A CG2 1 
ATOM   1087 C CD1 . ILE   A 1  140 ? 25.13572  14.68658 26.70455 1.000 61.97240  ? 140 ILE   A CD1 1 
ATOM   1088 N N   . VAL   A 1  141 ? 25.48095  19.54465 29.85421 1.000 58.71892  ? 141 VAL   A N   1 
ATOM   1089 C CA  . VAL   A 1  141 ? 24.93703  20.79939 30.36902 1.000 60.46052  ? 141 VAL   A CA  1 
ATOM   1090 C C   . VAL   A 1  141 ? 24.39145  21.62452 29.20485 1.000 55.65879  ? 141 VAL   A C   1 
ATOM   1091 O O   . VAL   A 1  141 ? 25.05933  21.80233 28.18091 1.000 57.90423  ? 141 VAL   A O   1 
ATOM   1092 C CB  . VAL   A 1  141 ? 25.99839  21.59022 31.16128 1.000 62.87167  ? 141 VAL   A CB  1 
ATOM   1093 C CG1 . VAL   A 1  141 ? 25.39823  22.87434 31.75737 1.000 51.40286  ? 141 VAL   A CG1 1 
ATOM   1094 C CG2 . VAL   A 1  141 ? 26.62180  20.70850 32.26093 1.000 59.64978  ? 141 VAL   A CG2 1 
ATOM   1095 N N   . VAL   A 1  142 ? 23.18044  22.12485 29.36659 1.000 54.79215  ? 142 VAL   A N   1 
ATOM   1096 C CA  . VAL   A 1  142 ? 22.53425  22.97927 28.38633 1.000 57.40016  ? 142 VAL   A CA  1 
ATOM   1097 C C   . VAL   A 1  142 ? 22.03726  24.22308 29.10641 1.000 60.51787  ? 142 VAL   A C   1 
ATOM   1098 O O   . VAL   A 1  142 ? 21.55439  24.12586 30.24278 1.000 57.79220  ? 142 VAL   A O   1 
ATOM   1099 C CB  . VAL   A 1  142 ? 21.35935  22.26596 27.68740 1.000 58.96350  ? 142 VAL   A CB  1 
ATOM   1100 C CG1 . VAL   A 1  142 ? 20.74928  23.18162 26.63604 1.000 57.96308  ? 142 VAL   A CG1 1 
ATOM   1101 C CG2 . VAL   A 1  142 ? 21.80070  20.93218 27.07853 1.000 59.15303  ? 142 VAL   A CG2 1 
ATOM   1102 N N   . SER   A 1  143 ? 22.16872  25.39219 28.44950 1.000 54.58371  ? 143 SER   A N   1 
ATOM   1103 C CA  . SER   A 1  143 ? 21.59117  26.64741 28.92136 1.000 52.71814  ? 143 SER   A CA  1 
ATOM   1104 C C   . SER   A 1  143 ? 21.09093  27.45812 27.72874 1.000 57.11420  ? 143 SER   A C   1 
ATOM   1105 O O   . SER   A 1  143 ? 21.64432  27.37114 26.62811 1.000 56.72441  ? 143 SER   A O   1 
ATOM   1106 C CB  . SER   A 1  143 ? 22.60389  27.47239 29.72033 1.000 53.00156  ? 143 SER   A CB  1 
ATOM   1107 O OG  . SER   A 1  143 ? 23.70010  27.87376 28.89811 1.000 57.15669  ? 143 SER   A OG  1 
ATOM   1108 N N   . MET   A 1  144 ? 20.03943  28.25192 27.94926 1.000 55.10147  ? 144 MET   A N   1 
ATOM   1109 C CA  . MET   A 1  144 ? 19.42947  29.03607 26.87998 1.000 56.11235  ? 144 MET   A CA  1 
ATOM   1110 C C   . MET   A 1  144 ? 19.23143  30.49053 27.29706 1.000 58.82638  ? 144 MET   A C   1 
ATOM   1111 O O   . MET   A 1  144 ? 19.02892  30.79845 28.47950 1.000 52.80633  ? 144 MET   A O   1 
ATOM   1112 C CB  . MET   A 1  144 ? 18.05637  28.44231 26.41046 1.000 52.99179  ? 144 MET   A CB  1 
ATOM   1113 C CG  . MET   A 1  144 ? 16.79849  28.77063 27.22288 1.000 49.72892  ? 144 MET   A CG  1 
ATOM   1114 S SD  . MET   A 1  144 ? 16.89027  28.53726 29.02795 1.000 53.54459  ? 144 MET   A SD  1 
ATOM   1115 C CE  . MET   A 1  144 ? 16.33733  26.85977 29.15975 1.000 42.40202  ? 144 MET   A CE  1 
ATOM   1116 N N   . ASN   A 1  145 ? 19.28368  31.38518 26.30104 1.000 55.68335  ? 145 ASN   A N   1 
ATOM   1117 C CA  . ASN   A 1  145 ? 18.80421  32.74760 26.48761 1.000 55.48048  ? 145 ASN   A CA  1 
ATOM   1118 C C   . ASN   A 1  145 ? 17.29094  32.80690 26.25956 1.000 58.44727  ? 145 ASN   A C   1 
ATOM   1119 O O   . ASN   A 1  145 ? 16.75171  32.18569 25.33604 1.000 58.67197  ? 145 ASN   A O   1 
ATOM   1120 C CB  . ASN   A 1  145 ? 19.52287  33.70508 25.53196 1.000 56.92341  ? 145 ASN   A CB  1 
ATOM   1121 C CG  . ASN   A 1  145 ? 20.97262  33.93564 25.91322 1.000 57.36644  ? 145 ASN   A CG  1 
ATOM   1122 O OD1 . ASN   A 1  145 ? 21.41279  33.53281 26.98946 1.000 55.91208  ? 145 ASN   A OD1 1 
ATOM   1123 N ND2 . ASN   A 1  145 ? 21.73471  34.57315 25.01600 1.000 54.69920  ? 145 ASN   A ND2 1 
ATOM   1124 N N   . TYR   A 1  146 ? 16.59812  33.54234 27.11369 1.000 55.59862  ? 146 TYR   A N   1 
ATOM   1125 C CA  . TYR   A 1  146 ? 15.16773  33.75335 26.92949 1.000 55.91973  ? 146 TYR   A CA  1 
ATOM   1126 C C   . TYR   A 1  146 ? 14.87205  35.22976 27.10571 1.000 50.87878  ? 146 TYR   A C   1 
ATOM   1127 O O   . TYR   A 1  146 ? 15.59459  35.93337 27.81319 1.000 55.04231  ? 146 TYR   A O   1 
ATOM   1128 C CB  . TYR   A 1  146 ? 14.33429  32.92243 27.90598 1.000 54.31091  ? 146 TYR   A CB  1 
ATOM   1129 C CG  . TYR   A 1  146 ? 14.60601  33.24097 29.36122 1.000 55.12706  ? 146 TYR   A CG  1 
ATOM   1130 C CD1 . TYR   A 1  146 ? 13.88907  34.24175 30.01771 1.000 49.06724  ? 146 TYR   A CD1 1 
ATOM   1131 C CD2 . TYR   A 1  146 ? 15.59412  32.55177 30.07937 1.000 51.39837  ? 146 TYR   A CD2 1 
ATOM   1132 C CE1 . TYR   A 1  146 ? 14.13898  34.53818 31.34382 1.000 53.14087  ? 146 TYR   A CE1 1 
ATOM   1133 C CE2 . TYR   A 1  146 ? 15.85043  32.84356 31.42073 1.000 50.99406  ? 146 TYR   A CE2 1 
ATOM   1134 C CZ  . TYR   A 1  146 ? 15.11102  33.84295 32.04248 1.000 54.28232  ? 146 TYR   A CZ  1 
ATOM   1135 O OH  . TYR   A 1  146 ? 15.33649  34.15374 33.36146 1.000 56.14538  ? 146 TYR   A OH  1 
ATOM   1136 N N   . ARG   A 1  147 ? 13.80911  35.69092 26.45398 1.000 55.59942  ? 147 ARG   A N   1 
ATOM   1137 C CA  . ARG   A 1  147 ? 13.46991  37.10768 26.48352 1.000 53.43418  ? 147 ARG   A CA  1 
ATOM   1138 C C   . ARG   A 1  147 ? 13.03934  37.55055 27.87871 1.000 56.19807  ? 147 ARG   A C   1 
ATOM   1139 O O   . ARG   A 1  147 ? 12.33991  36.82644 28.59575 1.000 55.31290  ? 147 ARG   A O   1 
ATOM   1140 C CB  . ARG   A 1  147 ? 12.37129  37.40585 25.46902 1.000 56.11001  ? 147 ARG   A CB  1 
ATOM   1141 C CG  . ARG   A 1  147 ? 12.86903  37.46921 24.03954 1.000 60.97211  ? 147 ARG   A CG  1 
ATOM   1142 C CD  . ARG   A 1  147 ? 11.70471  37.58819 23.06287 1.000 60.03232  ? 147 ARG   A CD  1 
ATOM   1143 N NE  . ARG   A 1  147 ? 11.07492  36.28784 22.87705 1.000 58.10404  ? 147 ARG   A NE  1 
ATOM   1144 C CZ  . ARG   A 1  147 ? 9.84118   36.08467 22.42249 1.000 64.47133  ? 147 ARG   A CZ  1 
ATOM   1145 N NH1 . ARG   A 1  147 ? 9.05754   37.09297 22.04793 1.000 58.24593  ? 147 ARG   A NH1 1 
ATOM   1146 N NH2 . ARG   A 1  147 ? 9.38432   34.83396 22.32766 1.000 59.31217  ? 147 ARG   A NH2 1 
ATOM   1147 N N   . VAL   A 1  148 ? 13.45068  38.76316 28.25469 1.000 52.37484  ? 148 VAL   A N   1 
ATOM   1148 C CA  . VAL   A 1  148 ? 13.19957  39.31143 29.57989 1.000 53.98301  ? 148 VAL   A CA  1 
ATOM   1149 C C   . VAL   A 1  148 ? 12.57144  40.69471 29.45888 1.000 59.57422  ? 148 VAL   A C   1 
ATOM   1150 O O   . VAL   A 1  148 ? 12.52107  41.30291 28.38203 1.000 55.38239  ? 148 VAL   A O   1 
ATOM   1151 C CB  . VAL   A 1  148 ? 14.48534  39.39377 30.42735 1.000 60.68010  ? 148 VAL   A CB  1 
ATOM   1152 C CG1 . VAL   A 1  148 ? 15.00094  37.99926 30.76671 1.000 47.85898  ? 148 VAL   A CG1 1 
ATOM   1153 C CG2 . VAL   A 1  148 ? 15.54061  40.22554 29.69921 1.000 48.86354  ? 148 VAL   A CG2 1 
ATOM   1154 N N   . GLY   A 1  149 ? 12.10660  41.19705 30.60181 1.000 56.01574  ? 149 GLY   A N   1 
ATOM   1155 C CA  . GLY   A 1  149 ? 11.48917  42.49980 30.58222 1.000 55.82708  ? 149 GLY   A CA  1 
ATOM   1156 C C   . GLY   A 1  149 ? 10.22584  42.46878 29.74244 1.000 60.21939  ? 149 GLY   A C   1 
ATOM   1157 O O   . GLY   A 1  149 ? 9.64813   41.41501 29.46792 1.000 60.78831  ? 149 GLY   A O   1 
ATOM   1158 N N   . ALA   A 1  150 ? 9.78799   43.66138 29.33388 1.000 59.93718  ? 150 ALA   A N   1 
ATOM   1159 C CA  . ALA   A 1  150 ? 8.55324   43.74630 28.56389 1.000 62.00937  ? 150 ALA   A CA  1 
ATOM   1160 C C   . ALA   A 1  150 ? 8.63026   42.89187 27.30258 1.000 64.01325  ? 150 ALA   A C   1 
ATOM   1161 O O   . ALA   A 1  150 ? 7.63848   42.26656 26.91142 1.000 61.29777  ? 150 ALA   A O   1 
ATOM   1162 C CB  . ALA   A 1  150 ? 8.24486   45.19838 28.20816 1.000 64.46300  ? 150 ALA   A CB  1 
ATOM   1163 N N   . LEU   A 1  151 ? 9.80547   42.83618 26.66047 1.000 62.89918  ? 151 LEU   A N   1 
ATOM   1164 C CA  . LEU   A 1  151 ? 9.93106   42.08558 25.41214 1.000 60.42760  ? 151 LEU   A CA  1 
ATOM   1165 C C   . LEU   A 1  151 ? 9.65596   40.60349 25.62120 1.000 61.68950  ? 151 LEU   A C   1 
ATOM   1166 O O   . LEU   A 1  151 ? 9.28831   39.90474 24.66699 1.000 60.88196  ? 151 LEU   A O   1 
ATOM   1167 C CB  . LEU   A 1  151 ? 11.32679  42.30419 24.79508 1.000 59.50017  ? 151 LEU   A CB  1 
ATOM   1168 C CG  . LEU   A 1  151 ? 11.62474  43.71041 24.20538 1.000 63.24526  ? 151 LEU   A CG  1 
ATOM   1169 C CD1 . LEU   A 1  151 ? 13.09683  43.87055 23.83140 1.000 62.45523  ? 151 LEU   A CD1 1 
ATOM   1170 C CD2 . LEU   A 1  151 ? 10.74580  44.09561 22.99731 1.000 60.28537  ? 151 LEU   A CD2 1 
ATOM   1171 N N   . GLY   A 1  152 ? 9.79358   40.12052 26.85238 1.000 59.43320  ? 152 GLY   A N   1 
ATOM   1172 C CA  . GLY   A 1  152 ? 9.53538   38.73600 27.15134 1.000 57.18765  ? 152 GLY   A CA  1 
ATOM   1173 C C   . GLY   A 1  152 ? 8.27996   38.46899 27.96123 1.000 61.07251  ? 152 GLY   A C   1 
ATOM   1174 O O   . GLY   A 1  152 ? 7.85458   37.31060 28.04525 1.000 58.14264  ? 152 GLY   A O   1 
ATOM   1175 N N   . PHE   A 1  153 ? 7.67626   39.50604 28.57380 1.000 59.72626  ? 153 PHE   A N   1 
ATOM   1176 C CA  . PHE   A 1  153 ? 6.54314   39.26851 29.46695 1.000 60.68866  ? 153 PHE   A CA  1 
ATOM   1177 C C   . PHE   A 1  153 ? 5.46814   40.34118 29.40966 1.000 64.18166  ? 153 PHE   A C   1 
ATOM   1178 O O   . PHE   A 1  153 ? 4.55957   40.32631 30.25962 1.000 67.29460  ? 153 PHE   A O   1 
ATOM   1179 C CB  . PHE   A 1  153 ? 7.01913   39.10763 30.91711 1.000 56.21274  ? 153 PHE   A CB  1 
ATOM   1180 C CG  . PHE   A 1  153 ? 7.88131   37.90375 31.12290 1.000 55.34290  ? 153 PHE   A CG  1 
ATOM   1181 C CD1 . PHE   A 1  153 ? 7.32191   36.68737 31.46661 1.000 53.46206  ? 153 PHE   A CD1 1 
ATOM   1182 C CD2 . PHE   A 1  153 ? 9.25889   37.97691 30.92382 1.000 56.16811  ? 153 PHE   A CD2 1 
ATOM   1183 C CE1 . PHE   A 1  153 ? 8.11832   35.55747 31.64700 1.000 57.40734  ? 153 PHE   A CE1 1 
ATOM   1184 C CE2 . PHE   A 1  153 ? 10.07937  36.84858 31.08898 1.000 52.78112  ? 153 PHE   A CE2 1 
ATOM   1185 C CZ  . PHE   A 1  153 ? 9.50717   35.63745 31.45770 1.000 55.11439  ? 153 PHE   A CZ  1 
ATOM   1186 N N   . LEU   A 1  154 ? 5.52557   41.26480 28.45805 1.000 58.85804  ? 154 LEU   A N   1 
ATOM   1187 C CA  . LEU   A 1  154 ? 4.40085   42.16875 28.27516 1.000 67.74756  ? 154 LEU   A CA  1 
ATOM   1188 C C   . LEU   A 1  154 ? 3.12302   41.35689 28.05226 1.000 70.66206  ? 154 LEU   A C   1 
ATOM   1189 O O   . LEU   A 1  154 ? 3.13894   40.32721 27.37144 1.000 66.35390  ? 154 LEU   A O   1 
ATOM   1190 C CB  . LEU   A 1  154 ? 4.66233   43.09040 27.09457 1.000 68.89500  ? 154 LEU   A CB  1 
ATOM   1191 C CG  . LEU   A 1  154 ? 3.59616   44.13369 26.80971 1.000 68.66852  ? 154 LEU   A CG  1 
ATOM   1192 C CD1 . LEU   A 1  154 ? 4.06653   45.43863 27.40904 1.000 71.41747  ? 154 LEU   A CD1 1 
ATOM   1193 C CD2 . LEU   A 1  154 ? 3.39216   44.28680 25.31787 1.000 69.86382  ? 154 LEU   A CD2 1 
ATOM   1194 N N   . ALA   A 1  155 ? 2.01439   41.79658 28.64897 1.000 66.42377  ? 155 ALA   A N   1 
ATOM   1195 C CA  . ALA   A 1  155 ? 0.81565   40.95990 28.68951 1.000 74.35948  ? 155 ALA   A CA  1 
ATOM   1196 C C   . ALA   A 1  155 ? -0.44769  41.76250 28.38410 1.000 79.56723  ? 155 ALA   A C   1 
ATOM   1197 O O   . ALA   A 1  155 ? -0.73540  42.76591 29.05202 1.000 72.46061  ? 155 ALA   A O   1 
ATOM   1198 C CB  . ALA   A 1  155 ? 0.68752   40.25767 30.05171 1.000 65.26208  ? 155 ALA   A CB  1 
ATOM   1199 N N   . LEU   A 1  156 ? -1.18891  41.31260 27.36084 1.000 75.08811  ? 156 LEU   A N   1 
ATOM   1200 C CA  . LEU   A 1  156 ? -2.60904  41.62237 27.15338 1.000 82.93288  ? 156 LEU   A CA  1 
ATOM   1201 C C   . LEU   A 1  156 ? -3.37468  40.30158 27.15961 1.000 86.11089  ? 156 LEU   A C   1 
ATOM   1202 O O   . LEU   A 1  156 ? -3.48946  39.63930 26.11446 1.000 80.23582  ? 156 LEU   A O   1 
ATOM   1203 C CB  . LEU   A 1  156 ? -2.83970  42.36859 25.84265 1.000 84.24349  ? 156 LEU   A CB  1 
ATOM   1204 C CG  . LEU   A 1  156 ? -2.47926  43.83908 25.65508 1.000 86.04001  ? 156 LEU   A CG  1 
ATOM   1205 C CD1 . LEU   A 1  156 ? -2.97100  44.27318 24.29168 1.000 87.98782  ? 156 LEU   A CD1 1 
ATOM   1206 C CD2 . LEU   A 1  156 ? -3.11703  44.72202 26.74017 1.000 79.79035  ? 156 LEU   A CD2 1 
ATOM   1207 N N   . PRO   A 1  157 ? -3.91833  39.88097 28.30421 1.000 89.70745  ? 157 PRO   A N   1 
ATOM   1208 C CA  . PRO   A 1  157 ? -4.38069  38.48676 28.43510 1.000 88.91109  ? 157 PRO   A CA  1 
ATOM   1209 C C   . PRO   A 1  157 ? -5.39160  38.11001 27.35621 1.000 86.68108  ? 157 PRO   A C   1 
ATOM   1210 O O   . PRO   A 1  157 ? -6.33380  38.85474 27.06819 1.000 87.27174  ? 157 PRO   A O   1 
ATOM   1211 C CB  . PRO   A 1  157 ? -4.99368  38.43453 29.84160 1.000 94.82359  ? 157 PRO   A CB  1 
ATOM   1212 C CG  . PRO   A 1  157 ? -4.56901  39.70819 30.54423 1.000 90.01039  ? 157 PRO   A CG  1 
ATOM   1213 C CD  . PRO   A 1  157 ? -4.16057  40.69837 29.50863 1.000 84.60544  ? 157 PRO   A CD  1 
ATOM   1214 N N   . GLY   A 1  158 ? -5.14878  36.95997 26.71980 1.000 81.61781  ? 158 GLY   A N   1 
ATOM   1215 C CA  . GLY   A 1  158 ? -5.95317  36.48071 25.61972 1.000 84.84606  ? 158 GLY   A CA  1 
ATOM   1216 C C   . GLY   A 1  158 ? -5.53855  36.96379 24.24231 1.000 89.11901  ? 158 GLY   A C   1 
ATOM   1217 O O   . GLY   A 1  158 ? -5.89197  36.32177 23.24661 1.000 89.91355  ? 158 GLY   A O   1 
ATOM   1218 N N   . ASN   A 1  159 ? -4.81872  38.08191 24.14918 1.000 90.85694  ? 159 ASN   A N   1 
ATOM   1219 C CA  . ASN   A 1  159 ? -4.39127  38.62186 22.86031 1.000 82.42732  ? 159 ASN   A CA  1 
ATOM   1220 C C   . ASN   A 1  159 ? -3.09282  37.95789 22.42458 1.000 85.17854  ? 159 ASN   A C   1 
ATOM   1221 O O   . ASN   A 1  159 ? -2.05955  38.15850 23.08201 1.000 83.99251  ? 159 ASN   A O   1 
ATOM   1222 C CB  . ASN   A 1  159 ? -4.17909  40.11692 22.95484 1.000 80.45859  ? 159 ASN   A CB  1 
ATOM   1223 C CG  . ASN   A 1  159 ? -4.17960  40.78423 21.60453 1.000 83.21546  ? 159 ASN   A CG  1 
ATOM   1224 O OD1 . ASN   A 1  159 ? -3.64651  40.24263 20.63116 1.000 78.41132  ? 159 ASN   A OD1 1 
ATOM   1225 N ND2 . ASN   A 1  159 ? -4.78535  41.96469 21.53086 1.000 83.09541  ? 159 ASN   A ND2 1 
ATOM   1226 N N   . PRO   A 1  160 ? -3.07536  37.19996 21.32207 1.000 87.67492  ? 160 PRO   A N   1 
ATOM   1227 C CA  . PRO   A 1  160 ? -1.83502  36.49002 20.93854 1.000 80.01117  ? 160 PRO   A CA  1 
ATOM   1228 C C   . PRO   A 1  160 ? -0.73045  37.41833 20.44037 1.000 80.57742  ? 160 PRO   A C   1 
ATOM   1229 O O   . PRO   A 1  160 ? 0.42053   36.98064 20.32859 1.000 79.66780  ? 160 PRO   A O   1 
ATOM   1230 C CB  . PRO   A 1  160 ? -2.29200  35.52634 19.82431 1.000 71.77582  ? 160 PRO   A CB  1 
ATOM   1231 C CG  . PRO   A 1  160 ? -3.79279  35.75067 19.65385 1.000 78.85371  ? 160 PRO   A CG  1 
ATOM   1232 C CD  . PRO   A 1  160 ? -4.14347  37.05344 20.31793 1.000 78.46685  ? 160 PRO   A CD  1 
ATOM   1233 N N   . GLU   A 1  161 ? -1.04494  38.67850 20.12446 1.000 84.16026  ? 161 GLU   A N   1 
ATOM   1234 C CA  . GLU   A 1  161 ? -0.00880  39.62721 19.74090 1.000 82.70557  ? 161 GLU   A CA  1 
ATOM   1235 C C   . GLU   A 1  161 ? 0.93449   39.92064 20.90389 1.000 79.15353  ? 161 GLU   A C   1 
ATOM   1236 O O   . GLU   A 1  161 ? 2.09971   40.25975 20.68720 1.000 76.79825  ? 161 GLU   A O   1 
ATOM   1237 C CB  . GLU   A 1  161 ? -0.64738  40.91781 19.23428 1.000 80.04447  ? 161 GLU   A CB  1 
ATOM   1238 C CG  . GLU   A 1  161 ? -1.37346  40.80506 17.87967 1.000 85.00231  ? 161 GLU   A CG  1 
ATOM   1239 C CD  . GLU   A 1  161 ? -0.62542  39.96614 16.84294 1.000 91.35297  ? 161 GLU   A CD  1 
ATOM   1240 O OE1 . GLU   A 1  161 ? 0.63071   39.95076 16.84817 1.000 90.77796  ? 161 GLU   A OE1 1 
ATOM   1241 O OE2 . GLU   A 1  161 ? -1.29850  39.32941 16.00356 1.000 94.58802  ? 161 GLU   A OE2 1 
ATOM   1242 N N   . ALA   A 1  162 ? 0.44648   39.79440 22.12707 1.000 77.74992  ? 162 ALA   A N   1 
ATOM   1243 C CA  . ALA   A 1  162 ? 1.23799   39.93213 23.33586 1.000 78.41238  ? 162 ALA   A CA  1 
ATOM   1244 C C   . ALA   A 1  162 ? 0.51702   39.16227 24.43324 1.000 77.55764  ? 162 ALA   A C   1 
ATOM   1245 O O   . ALA   A 1  162 ? -0.13776  39.76946 25.29610 1.000 77.40533  ? 162 ALA   A O   1 
ATOM   1246 C CB  . ALA   A 1  162 ? 1.42326   41.40597 23.70951 1.000 72.71104  ? 162 ALA   A CB  1 
ATOM   1247 N N   . PRO   A 1  163 ? 0.57418   37.81910 24.41531 1.000 75.65320  ? 163 PRO   A N   1 
ATOM   1248 C CA  . PRO   A 1  163 ? -0.23009  37.04192 25.36540 1.000 73.35963  ? 163 PRO   A CA  1 
ATOM   1249 C C   . PRO   A 1  163 ? 0.40681   36.92390 26.73700 1.000 71.61200  ? 163 PRO   A C   1 
ATOM   1250 O O   . PRO   A 1  163 ? -0.29753  36.60127 27.70374 1.000 68.97068  ? 163 PRO   A O   1 
ATOM   1251 C CB  . PRO   A 1  163 ? -0.33848  35.67271 24.67872 1.000 65.80393  ? 163 PRO   A CB  1 
ATOM   1252 C CG  . PRO   A 1  163 ? 0.94900   35.54932 23.90211 1.000 69.67569  ? 163 PRO   A CG  1 
ATOM   1253 C CD  . PRO   A 1  163 ? 1.37452   36.95635 23.51995 1.000 77.60652  ? 163 PRO   A CD  1 
ATOM   1254 N N   . GLY   A 1  164 ? 1.69937   37.19804 26.85516 1.000 66.61899  ? 164 GLY   A N   1 
ATOM   1255 C CA  . GLY   A 1  164 ? 2.39812   37.05182 28.10896 1.000 59.03167  ? 164 GLY   A CA  1 
ATOM   1256 C C   . GLY   A 1  164 ? 3.16981   35.75093 28.14544 1.000 60.39062  ? 164 GLY   A C   1 
ATOM   1257 O O   . GLY   A 1  164 ? 2.94671   34.84056 27.34973 1.000 66.46902  ? 164 GLY   A O   1 
ATOM   1258 N N   . ASN   A 1  165 ? 4.12883   35.67904 29.06872 1.000 57.65879  ? 165 ASN   A N   1 
ATOM   1259 C CA  . ASN   A 1  165 ? 4.91065   34.47420 29.33776 1.000 52.69550  ? 165 ASN   A CA  1 
ATOM   1260 C C   . ASN   A 1  165 ? 5.78309   34.02719 28.15892 1.000 54.69813  ? 165 ASN   A C   1 
ATOM   1261 O O   . ASN   A 1  165 ? 6.31945   32.90730 28.17333 1.000 58.69855  ? 165 ASN   A O   1 
ATOM   1262 C CB  . ASN   A 1  165 ? 3.99201   33.32616 29.78991 1.000 58.87771  ? 165 ASN   A CB  1 
ATOM   1263 C CG  . ASN   A 1  165 ? 3.41199   33.56667 31.17584 1.000 59.24604  ? 165 ASN   A CG  1 
ATOM   1264 O OD1 . ASN   A 1  165 ? 3.85611   34.45940 31.90233 1.000 59.77307  ? 165 ASN   A OD1 1 
ATOM   1265 N ND2 . ASN   A 1  165 ? 2.43133   32.76499 31.55121 1.000 57.62457  ? 165 ASN   A ND2 1 
ATOM   1266 N N   . MET   A 1  166 ? 5.95447   34.88312 27.15438 1.000 50.61851  ? 166 MET   A N   1 
ATOM   1267 C CA  . MET   A 1  166 ? 6.82503   34.60714 26.01365 1.000 57.67901  ? 166 MET   A CA  1 
ATOM   1268 C C   . MET   A 1  166 ? 8.19665   34.05965 26.43297 1.000 54.59638  ? 166 MET   A C   1 
ATOM   1269 O O   . MET   A 1  166 ? 8.68054   33.06335 25.87850 1.000 55.85650  ? 166 MET   A O   1 
ATOM   1270 C CB  . MET   A 1  166 ? 6.99497   35.90089 25.21137 1.000 62.44120  ? 166 MET   A CB  1 
ATOM   1271 C CG  . MET   A 1  166 ? 5.69921   36.39326 24.61494 1.000 60.86168  ? 166 MET   A CG  1 
ATOM   1272 S SD  . MET   A 1  166 ? 4.77757   37.55570 25.68831 1.000 64.17707  ? 166 MET   A SD  1 
ATOM   1273 C CE  . MET   A 1  166 ? 5.71389   39.09596 25.60667 1.000 62.18576  ? 166 MET   A CE  1 
ATOM   1274 N N   . GLY   A 1  167 ? 8.85401   34.72248 27.38806 1.000 52.13476  ? 167 GLY   A N   1 
ATOM   1275 C CA  . GLY   A 1  167 ? 10.14446  34.23895 27.86354 1.000 53.97796  ? 167 GLY   A CA  1 
ATOM   1276 C C   . GLY   A 1  167 ? 10.07773  32.84670 28.46630 1.000 54.98892  ? 167 GLY   A C   1 
ATOM   1277 O O   . GLY   A 1  167 ? 11.00532  32.04636 28.31067 1.000 53.15992  ? 167 GLY   A O   1 
ATOM   1278 N N   . LEU   A 1  168 ? 8.98003   32.53499 29.16498 1.000 55.59472  ? 168 LEU   A N   1 
ATOM   1279 C CA  . LEU   A 1  168 ? 8.77283   31.16174 29.61993 1.000 54.37617  ? 168 LEU   A CA  1 
ATOM   1280 C C   . LEU   A 1  168 ? 8.58244   30.22180 28.43588 1.000 58.15502  ? 168 LEU   A C   1 
ATOM   1281 O O   . LEU   A 1  168 ? 9.11764   29.10154 28.42840 1.000 54.63904  ? 168 LEU   A O   1 
ATOM   1282 C CB  . LEU   A 1  168 ? 7.57689   31.09052 30.56523 1.000 54.46828  ? 168 LEU   A CB  1 
ATOM   1283 C CG  . LEU   A 1  168 ? 7.80280   31.73757 31.92956 1.000 53.76668  ? 168 LEU   A CG  1 
ATOM   1284 C CD1 . LEU   A 1  168 ? 6.48364   31.92846 32.66179 1.000 51.51524  ? 168 LEU   A CD1 1 
ATOM   1285 C CD2 . LEU   A 1  168 ? 8.75708   30.90243 32.73417 1.000 47.23022  ? 168 LEU   A CD2 1 
ATOM   1286 N N   . PHE   A 1  169 ? 7.83468   30.66069 27.41096 1.000 51.65506  ? 169 PHE   A N   1 
ATOM   1287 C CA  . PHE   A 1  169 ? 7.72180   29.80710 26.23185 1.000 55.24562  ? 169 PHE   A CA  1 
ATOM   1288 C C   . PHE   A 1  169 ? 9.06358   29.69040 25.50320 1.000 56.31824  ? 169 PHE   A C   1 
ATOM   1289 O O   . PHE   A 1  169 ? 9.35624   28.64132 24.91596 1.000 51.68727  ? 169 PHE   A O   1 
ATOM   1290 C CB  . PHE   A 1  169 ? 6.61947   30.32246 25.32003 1.000 54.38600  ? 169 PHE   A CB  1 
ATOM   1291 C CG  . PHE   A 1  169 ? 5.23227   29.87064 25.72755 1.000 59.38697  ? 169 PHE   A CG  1 
ATOM   1292 C CD1 . PHE   A 1  169 ? 4.90297   28.51719 25.74047 1.000 61.44213  ? 169 PHE   A CD1 1 
ATOM   1293 C CD2 . PHE   A 1  169 ? 4.26556   30.79566 26.10969 1.000 56.94960  ? 169 PHE   A CD2 1 
ATOM   1294 C CE1 . PHE   A 1  169 ? 3.62571   28.09297 26.11339 1.000 54.56698  ? 169 PHE   A CE1 1 
ATOM   1295 C CE2 . PHE   A 1  169 ? 2.99368   30.38889 26.49102 1.000 60.14775  ? 169 PHE   A CE2 1 
ATOM   1296 C CZ  . PHE   A 1  169 ? 2.67317   29.03724 26.49114 1.000 63.22454  ? 169 PHE   A CZ  1 
ATOM   1297 N N   . ASP   A 1  170 ? 9.89960   30.73627 25.55208 1.000 54.07077  ? 170 ASP   A N   1 
ATOM   1298 C CA  . ASP   A 1  170 ? 11.26579  30.60627 25.05246 1.000 58.62898  ? 170 ASP   A CA  1 
ATOM   1299 C C   . ASP   A 1  170 ? 11.98722  29.44334 25.73979 1.000 60.91077  ? 170 ASP   A C   1 
ATOM   1300 O O   . ASP   A 1  170 ? 12.46382  28.51017 25.07937 1.000 56.42258  ? 170 ASP   A O   1 
ATOM   1301 C CB  . ASP   A 1  170 ? 12.02802  31.91080 25.26697 1.000 53.92756  ? 170 ASP   A CB  1 
ATOM   1302 C CG  . ASP   A 1  170 ? 11.58594  33.00890 24.32331 1.000 59.04075  ? 170 ASP   A CG  1 
ATOM   1303 O OD1 . ASP   A 1  170 ? 10.86843  32.71256 23.34906 1.000 57.22461  ? 170 ASP   A OD1 1 
ATOM   1304 O OD2 . ASP   A 1  170 ? 11.94977  34.17768 24.56360 1.000 57.96876  ? 170 ASP   A OD2 1 
ATOM   1305 N N   . GLN   A 1  171 ? 12.05619  29.47812 27.07788 1.000 55.49870  ? 171 GLN   A N   1 
ATOM   1306 C CA  . GLN   A 1  171 ? 12.58968  28.34599 27.83072 1.000 55.98475  ? 171 GLN   A CA  1 
ATOM   1307 C C   . GLN   A 1  171 ? 11.98690  27.03124 27.35483 1.000 55.00832  ? 171 GLN   A C   1 
ATOM   1308 O O   . GLN   A 1  171 ? 12.69890  26.03796 27.16948 1.000 57.75031  ? 171 GLN   A O   1 
ATOM   1309 C CB  . GLN   A 1  171 ? 12.32727  28.53061 29.32233 1.000 50.79305  ? 171 GLN   A CB  1 
ATOM   1310 C CG  . GLN   A 1  171 ? 12.88716  29.81366 29.91830 1.000 46.43644  ? 171 GLN   A CG  1 
ATOM   1311 C CD  . GLN   A 1  171 ? 12.39182  30.04367 31.34763 1.000 52.62024  ? 171 GLN   A CD  1 
ATOM   1312 O OE1 . GLN   A 1  171 ? 11.86137  29.12418 32.00325 1.000 52.04204  ? 171 GLN   A OE1 1 
ATOM   1313 N NE2 . GLN   A 1  171 ? 12.54264  31.28347 31.83265 1.000 46.25721  ? 171 GLN   A NE2 1 
ATOM   1314 N N   . GLN   A 1  172 ? 10.67387  27.00889 27.13964 1.000 54.48746  ? 172 GLN   A N   1 
ATOM   1315 C CA  . GLN   A 1  172 ? 10.00939  25.74366 26.84883 1.000 54.70200  ? 172 GLN   A CA  1 
ATOM   1316 C C   . GLN   A 1  172 ? 10.40600  25.21109 25.47795 1.000 59.61608  ? 172 GLN   A C   1 
ATOM   1317 O O   . GLN   A 1  172 ? 10.68745  24.01422 25.32116 1.000 54.23351  ? 172 GLN   A O   1 
ATOM   1318 C CB  . GLN   A 1  172 ? 8.49785   25.90031 26.93672 1.000 56.72112  ? 172 GLN   A CB  1 
ATOM   1319 C CG  . GLN   A 1  172 ? 7.77379   24.58136 27.05937 1.000 52.96806  ? 172 GLN   A CG  1 
ATOM   1320 C CD  . GLN   A 1  172 ? 6.29038   24.75320 26.96782 1.000 57.28066  ? 172 GLN   A CD  1 
ATOM   1321 O OE1 . GLN   A 1  172 ? 5.77661   25.25483 25.96574 1.000 59.01130  ? 172 GLN   A OE1 1 
ATOM   1322 N NE2 . GLN   A 1  172 ? 5.58390   24.35747 28.01700 1.000 58.91049  ? 172 GLN   A NE2 1 
ATOM   1323 N N   . LEU   A 1  173 ? 10.42484  26.08380 24.46786 1.000 60.93246  ? 173 LEU   A N   1 
ATOM   1324 C CA  . LEU   A 1  173 ? 10.92404  25.67366 23.16008 1.000 56.64784  ? 173 LEU   A CA  1 
ATOM   1325 C C   . LEU   A 1  173 ? 12.32917  25.10105 23.26928 1.000 58.72000  ? 173 LEU   A C   1 
ATOM   1326 O O   . LEU   A 1  173 ? 12.68091  24.13520 22.57667 1.000 61.35813  ? 173 LEU   A O   1 
ATOM   1327 C CB  . LEU   A 1  173 ? 10.90902  26.85672 22.19913 1.000 60.61432  ? 173 LEU   A CB  1 
ATOM   1328 C CG  . LEU   A 1  173 ? 10.47431  26.44661 20.79680 1.000 66.28734  ? 173 LEU   A CG  1 
ATOM   1329 C CD1 . LEU   A 1  173 ? 8.97684   26.18822 20.78076 1.000 62.39065  ? 173 LEU   A CD1 1 
ATOM   1330 C CD2 . LEU   A 1  173 ? 10.85779  27.51750 19.79672 1.000 58.97557  ? 173 LEU   A CD2 1 
ATOM   1331 N N   . ALA   A 1  174 ? 13.14375  25.66646 24.15268 1.000 53.94823  ? 174 ALA   A N   1 
ATOM   1332 C CA  . ALA   A 1  174 ? 14.48588  25.12827 24.33268 1.000 55.39877  ? 174 ALA   A CA  1 
ATOM   1333 C C   . ALA   A 1  174 ? 14.45329  23.73652 24.95927 1.000 60.83319  ? 174 ALA   A C   1 
ATOM   1334 O O   . ALA   A 1  174 ? 15.20072  22.84730 24.53175 1.000 62.90123  ? 174 ALA   A O   1 
ATOM   1335 C CB  . ALA   A 1  174 ? 15.32837  26.08724 25.16879 1.000 55.05846  ? 174 ALA   A CB  1 
ATOM   1336 N N   . LEU   A 1  175 ? 13.59926  23.52009 25.97080 1.000 57.42028  ? 175 LEU   A N   1 
ATOM   1337 C CA  . LEU   A 1  175 ? 13.42977  22.16416 26.49566 1.000 59.42885  ? 175 LEU   A CA  1 
ATOM   1338 C C   . LEU   A 1  175 ? 13.01871  21.20011 25.38067 1.000 62.25921  ? 175 LEU   A C   1 
ATOM   1339 O O   . LEU   A 1  175 ? 13.47471  20.04924 25.33618 1.000 58.19838  ? 175 LEU   A O   1 
ATOM   1340 C CB  . LEU   A 1  175 ? 12.39145  22.14858 27.62176 1.000 55.02901  ? 175 LEU   A CB  1 
ATOM   1341 C CG  . LEU   A 1  175 ? 12.61821  23.02195 28.86116 1.000 62.94096  ? 175 LEU   A CG  1 
ATOM   1342 C CD1 . LEU   A 1  175 ? 11.75794  22.55880 30.05924 1.000 56.37383  ? 175 LEU   A CD1 1 
ATOM   1343 C CD2 . LEU   A 1  175 ? 14.10809  23.09203 29.22522 1.000 60.70994  ? 175 LEU   A CD2 1 
ATOM   1344 N N   . GLN   A 1  176 ? 12.14928  21.65827 24.47404 1.000 61.29775  ? 176 GLN   A N   1 
ATOM   1345 C CA  . GLN   A 1  176 ? 11.72299  20.82857 23.35397 1.000 60.23585  ? 176 GLN   A CA  1 
ATOM   1346 C C   . GLN   A 1  176 ? 12.89901  20.46172 22.45635 1.000 65.39567  ? 176 GLN   A C   1 
ATOM   1347 O O   . GLN   A 1  176 ? 13.00236  19.31536 21.99168 1.000 63.47344  ? 176 GLN   A O   1 
ATOM   1348 C CB  . GLN   A 1  176 ? 10.64191  21.54990 22.55568 1.000 64.27689  ? 176 GLN   A CB  1 
ATOM   1349 C CG  . GLN   A 1  176 ? 9.29865   20.92690 22.71905 1.000 79.17731  ? 176 GLN   A CG  1 
ATOM   1350 C CD  . GLN   A 1  176 ? 9.14156   19.74053 21.77232 1.000 94.75007  ? 176 GLN   A CD  1 
ATOM   1351 O OE1 . GLN   A 1  176 ? 9.67255   19.75007 20.65485 1.000 99.95279  ? 176 GLN   A OE1 1 
ATOM   1352 N NE2 . GLN   A 1  176 ? 8.47057   18.68488 22.23954 1.000 87.05324  ? 176 GLN   A NE2 1 
ATOM   1353 N N   . TRP   A 1  177 ? 13.79762  21.42621 22.21334 1.000 63.79686  ? 177 TRP   A N   1 
ATOM   1354 C CA  . TRP   A 1  177 ? 14.97621  21.18364 21.38391 1.000 61.16160  ? 177 TRP   A CA  1 
ATOM   1355 C C   . TRP   A 1  177 ? 15.83094  20.07849 21.98086 1.000 61.42226  ? 177 TRP   A C   1 
ATOM   1356 O O   . TRP   A 1  177 ? 16.42958  19.27318 21.25340 1.000 64.54167  ? 177 TRP   A O   1 
ATOM   1357 C CB  . TRP   A 1  177 ? 15.79698  22.47948 21.24360 1.000 64.45469  ? 177 TRP   A CB  1 
ATOM   1358 C CG  . TRP   A 1  177 ? 17.03455  22.35374 20.35622 1.000 68.03765  ? 177 TRP   A CG  1 
ATOM   1359 C CD1 . TRP   A 1  177 ? 17.13427  22.71386 19.04055 1.000 64.48907  ? 177 TRP   A CD1 1 
ATOM   1360 C CD2 . TRP   A 1  177 ? 18.32214  21.82546 20.72006 1.000 64.06704  ? 177 TRP   A CD2 1 
ATOM   1361 N NE1 . TRP   A 1  177 ? 18.39105  22.44456 18.56536 1.000 63.06101  ? 177 TRP   A NE1 1 
ATOM   1362 C CE2 . TRP   A 1  177 ? 19.14314  21.89754 19.56937 1.000 66.05756  ? 177 TRP   A CE2 1 
ATOM   1363 C CE3 . TRP   A 1  177 ? 18.85884  21.29298 21.89798 1.000 64.80860  ? 177 TRP   A CE3 1 
ATOM   1364 C CZ2 . TRP   A 1  177 ? 20.46997  21.44773 19.55909 1.000 60.30391  ? 177 TRP   A CZ2 1 
ATOM   1365 C CZ3 . TRP   A 1  177 ? 20.18449  20.84869 21.88995 1.000 63.33093  ? 177 TRP   A CZ3 1 
ATOM   1366 C CH2 . TRP   A 1  177 ? 20.97039  20.93394 20.72908 1.000 70.13776  ? 177 TRP   A CH2 1 
ATOM   1367 N N   . VAL   A 1  178 ? 15.91155  20.03598 23.30972 1.000 58.01515  ? 178 VAL   A N   1 
ATOM   1368 C CA  . VAL   A 1  178 ? 16.69268  18.99718 23.96153 1.000 61.50432  ? 178 VAL   A CA  1 
ATOM   1369 C C   . VAL   A 1  178 ? 16.02500  17.64043 23.76230 1.000 63.49134  ? 178 VAL   A C   1 
ATOM   1370 O O   . VAL   A 1  178 ? 16.70103  16.63530 23.51651 1.000 65.12197  ? 178 VAL   A O   1 
ATOM   1371 C CB  . VAL   A 1  178 ? 16.90309  19.34454 25.44908 1.000 61.17329  ? 178 VAL   A CB  1 
ATOM   1372 C CG1 . VAL   A 1  178 ? 17.55515  18.19888 26.17946 1.000 58.43448  ? 178 VAL   A CG1 1 
ATOM   1373 C CG2 . VAL   A 1  178 ? 17.76045  20.58886 25.58563 1.000 56.36672  ? 178 VAL   A CG2 1 
ATOM   1374 N N   . GLN   A 1  179 ? 14.69092  17.59046 23.81169 1.000 60.37111  ? 179 GLN   A N   1 
ATOM   1375 C CA  . GLN   A 1  179 ? 14.01768  16.31686 23.55597 1.000 66.21004  ? 179 GLN   A CA  1 
ATOM   1376 C C   . GLN   A 1  179 ? 14.28764  15.82820 22.13512 1.000 65.43384  ? 179 GLN   A C   1 
ATOM   1377 O O   . GLN   A 1  179 ? 14.58830  14.64453 21.92435 1.000 63.43245  ? 179 GLN   A O   1 
ATOM   1378 C CB  . GLN   A 1  179 ? 12.51241  16.43741 23.80352 1.000 61.78225  ? 179 GLN   A CB  1 
ATOM   1379 C CG  . GLN   A 1  179 ? 12.12364  16.59493 25.26756 1.000 60.81868  ? 179 GLN   A CG  1 
ATOM   1380 C CD  . GLN   A 1  179 ? 12.55073  15.41385 26.10457 1.000 59.36259  ? 179 GLN   A CD  1 
ATOM   1381 O OE1 . GLN   A 1  179 ? 11.91924  14.35282 26.07455 1.000 64.50330  ? 179 GLN   A OE1 1 
ATOM   1382 N NE2 . GLN   A 1  179 ? 13.62485  15.58361 26.86356 1.000 62.72748  ? 179 GLN   A NE2 1 
ATOM   1383 N N   . LYS   A 1  180 ? 14.22179  16.72867 21.14836 1.000 65.55335  ? 180 LYS   A N   1 
ATOM   1384 C CA  . LYS   A 1  180 ? 14.36265  16.29864 19.75965 1.000 69.07062  ? 180 LYS   A CA  1 
ATOM   1385 C C   . LYS   A 1  180 ? 15.80479  16.02442 19.35345 1.000 68.64070  ? 180 LYS   A C   1 
ATOM   1386 O O   . LYS   A 1  180 ? 16.02016  15.22638 18.43510 1.000 69.63577  ? 180 LYS   A O   1 
ATOM   1387 C CB  . LYS   A 1  180 ? 13.76073  17.34001 18.81356 1.000 69.03101  ? 180 LYS   A CB  1 
ATOM   1388 C CG  . LYS   A 1  180 ? 12.29537  17.11640 18.54004 1.000 81.55608  ? 180 LYS   A CG  1 
ATOM   1389 C CD  . LYS   A 1  180 ? 11.67359  18.29111 17.81376 1.000 90.51471  ? 180 LYS   A CD  1 
ATOM   1390 C CE  . LYS   A 1  180 ? 10.30412  17.93020 17.26421 1.000 101.85951 ? 180 LYS   A CE  1 
ATOM   1391 N NZ  . LYS   A 1  180 ? 9.58065   19.14729 16.80991 1.000 105.61977 ? 180 LYS   A NZ  1 
ATOM   1392 N N   . ASN   A 1  181 ? 16.79389  16.64455 20.01304 1.000 61.11168  ? 181 ASN   A N   1 
ATOM   1393 C CA  . ASN   A 1  181 ? 18.14889  16.67441 19.47245 1.000 65.19669  ? 181 ASN   A CA  1 
ATOM   1394 C C   . ASN   A 1  181 ? 19.24972  16.12813 20.37342 1.000 59.85557  ? 181 ASN   A C   1 
ATOM   1395 O O   . ASN   A 1  181 ? 20.29222  15.74210 19.84311 1.000 63.61587  ? 181 ASN   A O   1 
ATOM   1396 C CB  . ASN   A 1  181 ? 18.54108  18.11319 19.08581 1.000 65.51980  ? 181 ASN   A CB  1 
ATOM   1397 C CG  . ASN   A 1  181 ? 17.67729  18.67216 17.98340 1.000 70.05398  ? 181 ASN   A CG  1 
ATOM   1398 O OD1 . ASN   A 1  181 ? 17.85499  18.35933 16.80075 1.000 71.36537  ? 181 ASN   A OD1 1 
ATOM   1399 N ND2 . ASN   A 1  181 ? 16.72680  19.50658 18.36650 1.000 67.50042  ? 181 ASN   A ND2 1 
ATOM   1400 N N   . ILE   A 1  182 ? 19.08231  16.10353 21.69738 1.000 52.67308  ? 182 ILE   A N   1 
ATOM   1401 C CA  . ILE   A 1  182 ? 20.22337  15.82560 22.56522 1.000 60.84042  ? 182 ILE   A CA  1 
ATOM   1402 C C   . ILE   A 1  182 ? 20.71405  14.37892 22.43173 1.000 61.57900  ? 182 ILE   A C   1 
ATOM   1403 O O   . ILE   A 1  182 ? 21.87588  14.08849 22.73896 1.000 59.72823  ? 182 ILE   A O   1 
ATOM   1404 C CB  . ILE   A 1  182 ? 19.86803  16.18902 24.02397 1.000 60.76806  ? 182 ILE   A CB  1 
ATOM   1405 C CG1 . ILE   A 1  182 ? 21.11854  16.56959 24.81404 1.000 59.52348  ? 182 ILE   A CG1 1 
ATOM   1406 C CG2 . ILE   A 1  182 ? 19.16811  15.04142 24.70398 1.000 60.09850  ? 182 ILE   A CG2 1 
ATOM   1407 C CD1 . ILE   A 1  182 ? 21.74915  17.86914 24.36357 1.000 64.22312  ? 182 ILE   A CD1 1 
ATOM   1408 N N   . ALA   A 1  183 ? 19.87440  13.46021 21.95589 1.000 62.01496  ? 183 ALA   A N   1 
ATOM   1409 C CA  . ALA   A 1  183 ? 20.35186  12.10106 21.72256 1.000 61.84993  ? 183 ALA   A CA  1 
ATOM   1410 C C   . ALA   A 1  183 ? 21.48901  12.07446 20.70635 1.000 67.17791  ? 183 ALA   A C   1 
ATOM   1411 O O   . ALA   A 1  183 ? 22.38060  11.21969 20.79809 1.000 66.02325  ? 183 ALA   A O   1 
ATOM   1412 C CB  . ALA   A 1  183 ? 19.20004  11.20503 21.25486 1.000 52.51143  ? 183 ALA   A CB  1 
ATOM   1413 N N   . ALA   A 1  184 ? 21.48365  12.99805 19.73427 1.000 64.52762  ? 184 ALA   A N   1 
ATOM   1414 C CA  . ALA   A 1  184 ? 22.56401  13.02869 18.75137 1.000 65.75663  ? 184 ALA   A CA  1 
ATOM   1415 C C   . ALA   A 1  184 ? 23.88324  13.47583 19.36532 1.000 68.28648  ? 184 ALA   A C   1 
ATOM   1416 O O   . ALA   A 1  184 ? 24.95112  13.13207 18.83882 1.000 71.84605  ? 184 ALA   A O   1 
ATOM   1417 C CB  . ALA   A 1  184 ? 22.20167  13.94784 17.58339 1.000 61.18342  ? 184 ALA   A CB  1 
ATOM   1418 N N   . PHE   A 1  185 ? 23.82604  14.24569 20.45014 1.000 64.15910  ? 185 PHE   A N   1 
ATOM   1419 C CA  . PHE   A 1  185 ? 24.99095  14.65730 21.22106 1.000 61.14194  ? 185 PHE   A CA  1 
ATOM   1420 C C   . PHE   A 1  185 ? 25.40359  13.62732 22.26635 1.000 67.77078  ? 185 PHE   A C   1 
ATOM   1421 O O   . PHE   A 1  185 ? 26.33470  13.88779 23.03170 1.000 67.58794  ? 185 PHE   A O   1 
ATOM   1422 C CB  . PHE   A 1  185 ? 24.71169  15.99518 21.91651 1.000 62.55910  ? 185 PHE   A CB  1 
ATOM   1423 C CG  . PHE   A 1  185 ? 24.57517  17.15625 20.97294 1.000 69.32713  ? 185 PHE   A CG  1 
ATOM   1424 C CD1 . PHE   A 1  185 ? 23.35981  17.42115 20.35034 1.000 68.57596  ? 185 PHE   A CD1 1 
ATOM   1425 C CD2 . PHE   A 1  185 ? 25.65427  17.98994 20.71398 1.000 66.33324  ? 185 PHE   A CD2 1 
ATOM   1426 C CE1 . PHE   A 1  185 ? 23.23062  18.49502 19.47364 1.000 68.91707  ? 185 PHE   A CE1 1 
ATOM   1427 C CE2 . PHE   A 1  185 ? 25.53218  19.06514 19.84152 1.000 69.46578  ? 185 PHE   A CE2 1 
ATOM   1428 C CZ  . PHE   A 1  185 ? 24.31930  19.32107 19.22198 1.000 69.92925  ? 185 PHE   A CZ  1 
ATOM   1429 N N   . GLY   A 1  186 ? 24.73405  12.47636 22.32701 1.000 66.07596  ? 186 GLY   A N   1 
ATOM   1430 C CA  . GLY   A 1  186 ? 25.03702  11.50259 23.35294 1.000 67.01178  ? 186 GLY   A CA  1 
ATOM   1431 C C   . GLY   A 1  186 ? 24.30403  11.71029 24.65806 1.000 69.43032  ? 186 GLY   A C   1 
ATOM   1432 O O   . GLY   A 1  186 ? 24.72540  11.16350 25.68277 1.000 67.87613  ? 186 GLY   A O   1 
ATOM   1433 N N   . GLY   A 1  187 ? 23.21685  12.49951 24.65617 1.000 60.86028  ? 187 GLY   A N   1 
ATOM   1434 C CA  . GLY   A 1  187 ? 22.44253  12.74629 25.84807 1.000 57.95723  ? 187 GLY   A CA  1 
ATOM   1435 C C   . GLY   A 1  187 ? 21.18810  11.90780 25.89436 1.000 67.59816  ? 187 GLY   A C   1 
ATOM   1436 O O   . GLY   A 1  187 ? 20.67853  11.45819 24.86845 1.000 66.70327  ? 187 GLY   A O   1 
ATOM   1437 N N   . ASN   A 1  188 ? 20.70091  11.69164 27.11902 1.000 68.55071  ? 188 ASN   A N   1 
ATOM   1438 C CA  . ASN   A 1  188 ? 19.49113  10.92314 27.37038 1.000 64.42535  ? 188 ASN   A CA  1 
ATOM   1439 C C   . ASN   A 1  188 ? 18.28554  11.85465 27.56985 1.000 64.24401  ? 188 ASN   A C   1 
ATOM   1440 O O   . ASN   A 1  188 ? 18.10486  12.41048 28.66993 1.000 57.18010  ? 188 ASN   A O   1 
ATOM   1441 C CB  . ASN   A 1  188 ? 19.69698  10.02901 28.59559 1.000 73.28221  ? 188 ASN   A CB  1 
ATOM   1442 C CG  . ASN   A 1  188 ? 18.47244  9.21250  28.94014 1.000 74.09606  ? 188 ASN   A CG  1 
ATOM   1443 O OD1 . ASN   A 1  188 ? 17.55315  9.07026  28.13534 1.000 75.03546  ? 188 ASN   A OD1 1 
ATOM   1444 N ND2 . ASN   A 1  188 ? 18.46288  8.65588  30.13967 1.000 73.90643  ? 188 ASN   A ND2 1 
ATOM   1445 N N   . PRO   A 1  189 ? 17.42113  12.01903 26.56336 1.000 61.28846  ? 189 PRO   A N   1 
ATOM   1446 C CA  . PRO   A 1  189 ? 16.21712  12.84840 26.74157 1.000 63.92273  ? 189 PRO   A CA  1 
ATOM   1447 C C   . PRO   A 1  189 ? 15.31426  12.39831 27.87941 1.000 65.37320  ? 189 PRO   A C   1 
ATOM   1448 O O   . PRO   A 1  189 ? 14.47151  13.18544 28.32508 1.000 64.03421  ? 189 PRO   A O   1 
ATOM   1449 C CB  . PRO   A 1  189 ? 15.49635  12.70423 25.39382 1.000 59.55504  ? 189 PRO   A CB  1 
ATOM   1450 C CG  . PRO   A 1  189 ? 15.89587  11.33376 24.91956 1.000 54.62587  ? 189 PRO   A CG  1 
ATOM   1451 C CD  . PRO   A 1  189 ? 17.34340  11.18791 25.34620 1.000 64.05156  ? 189 PRO   A CD  1 
ATOM   1452 N N   . LYS   A 1  190 ? 15.43825  11.15900 28.34528 1.000 65.64837  ? 190 LYS   A N   1 
ATOM   1453 C CA  . LYS   A 1  190 ? 14.61005  10.66199 29.43441 1.000 70.25066  ? 190 LYS   A CA  1 
ATOM   1454 C C   . LYS   A 1  190 ? 15.22382  10.89368 30.80917 1.000 67.12997  ? 190 LYS   A C   1 
ATOM   1455 O O   . LYS   A 1  190 ? 14.61682  10.49618 31.80727 1.000 74.18858  ? 190 LYS   A O   1 
ATOM   1456 C CB  . LYS   A 1  190 ? 14.31658  9.16847  29.24166 1.000 66.60290  ? 190 LYS   A CB  1 
ATOM   1457 C CG  . LYS   A 1  190 ? 13.57910  8.87063  27.94873 1.000 73.64889  ? 190 LYS   A CG  1 
ATOM   1458 C CD  . LYS   A 1  190 ? 13.33772  7.37335  27.73706 1.000 88.36225  ? 190 LYS   A CD  1 
ATOM   1459 C CE  . LYS   A 1  190 ? 13.10847  7.03896  26.25838 1.000 97.11562  ? 190 LYS   A CE  1 
ATOM   1460 N NZ  . LYS   A 1  190 ? 14.18190  7.58023  25.34671 1.000 94.17205  ? 190 LYS   A NZ  1 
ATOM   1461 N N   . SER   A 1  191 ? 16.40057  11.52695 30.89318 1.000 63.23438  ? 191 SER   A N   1 
ATOM   1462 C CA  . SER   A 1  191 ? 17.01331  11.90327 32.17584 1.000 61.35743  ? 191 SER   A CA  1 
ATOM   1463 C C   . SER   A 1  191 ? 17.47824  13.36071 32.05056 1.000 60.28842  ? 191 SER   A C   1 
ATOM   1464 O O   . SER   A 1  191 ? 18.65174  13.64871 31.80399 1.000 62.72690  ? 191 SER   A O   1 
ATOM   1465 C CB  . SER   A 1  191 ? 18.16039  10.93776 32.55038 1.000 62.57877  ? 191 SER   A CB  1 
ATOM   1466 O OG  . SER   A 1  191 ? 18.87000  11.36366 33.70458 1.000 64.25095  ? 191 SER   A OG  1 
ATOM   1467 N N   . VAL   A 1  192 ? 16.53094  14.28117 32.23257 1.000 58.30385  ? 192 VAL   A N   1 
ATOM   1468 C CA  . VAL   A 1  192 ? 16.74467  15.72146 32.12776 1.000 56.41542  ? 192 VAL   A CA  1 
ATOM   1469 C C   . VAL   A 1  192 ? 16.35179  16.35428 33.45455 1.000 57.01737  ? 192 VAL   A C   1 
ATOM   1470 O O   . VAL   A 1  192 ? 15.21527  16.18602 33.91463 1.000 62.06045  ? 192 VAL   A O   1 
ATOM   1471 C CB  . VAL   A 1  192 ? 15.92121  16.33582 30.98128 1.000 56.30525  ? 192 VAL   A CB  1 
ATOM   1472 C CG1 . VAL   A 1  192 ? 16.07258  17.84163 30.96074 1.000 54.25100  ? 192 VAL   A CG1 1 
ATOM   1473 C CG2 . VAL   A 1  192 ? 16.29129  15.70855 29.63460 1.000 55.57746  ? 192 VAL   A CG2 1 
ATOM   1474 N N   . THR   A 1  193 ? 17.27086  17.10013 34.04914 1.000 51.34477  ? 193 THR   A N   1 
ATOM   1475 C CA  . THR   A 1  193 ? 17.03101  17.82210 35.28639 1.000 53.01737  ? 193 THR   A CA  1 
ATOM   1476 C C   . THR   A 1  193 ? 17.16320  19.30765 34.99478 1.000 53.03678  ? 193 THR   A C   1 
ATOM   1477 O O   . THR   A 1  193 ? 18.19212  19.74692 34.48701 1.000 58.31585  ? 193 THR   A O   1 
ATOM   1478 C CB  . THR   A 1  193 ? 18.02144  17.37782 36.36693 1.000 54.78568  ? 193 THR   A CB  1 
ATOM   1479 O OG1 . THR   A 1  193 ? 17.80594  15.99017 36.65484 1.000 59.61634  ? 193 THR   A OG1 1 
ATOM   1480 C CG2 . THR   A 1  193 ? 17.88883  18.18892 37.64255 1.000 46.19910  ? 193 THR   A CG2 1 
ATOM   1481 N N   . LEU   A 1  194 ? 16.11438  20.06916 35.28142 1.000 53.35268  ? 194 LEU   A N   1 
ATOM   1482 C CA  . LEU   A 1  194 ? 16.18760  21.51870 35.18363 1.000 55.90392  ? 194 LEU   A CA  1 
ATOM   1483 C C   . LEU   A 1  194 ? 16.78428  22.05481 36.47480 1.000 57.41690  ? 194 LEU   A C   1 
ATOM   1484 O O   . LEU   A 1  194 ? 16.48697  21.54265 37.56218 1.000 53.21074  ? 194 LEU   A O   1 
ATOM   1485 C CB  . LEU   A 1  194 ? 14.79468  22.12517 34.95418 1.000 52.72220  ? 194 LEU   A CB  1 
ATOM   1486 C CG  . LEU   A 1  194 ? 13.93910  21.55108 33.81823 1.000 53.40494  ? 194 LEU   A CG  1 
ATOM   1487 C CD1 . LEU   A 1  194 ? 12.55164  22.19350 33.74527 1.000 52.71283  ? 194 LEU   A CD1 1 
ATOM   1488 C CD2 . LEU   A 1  194 ? 14.64978  21.68117 32.47144 1.000 50.25878  ? 194 LEU   A CD2 1 
ATOM   1489 N N   . PHE   A 1  195 ? 17.65743  23.06267 36.35438 1.000 51.41416  ? 195 PHE   A N   1 
ATOM   1490 C CA  . PHE   A 1  195 ? 18.04245  23.82904 37.52581 1.000 50.08014  ? 195 PHE   A CA  1 
ATOM   1491 C C   . PHE   A 1  195 ? 18.20198  25.29236 37.13850 1.000 55.01110  ? 195 PHE   A C   1 
ATOM   1492 O O   . PHE   A 1  195 ? 18.55325  25.61899 35.99722 1.000 54.12164  ? 195 PHE   A O   1 
ATOM   1493 C CB  . PHE   A 1  195 ? 19.30445  23.23852 38.24222 1.000 49.87720  ? 195 PHE   A CB  1 
ATOM   1494 C CG  . PHE   A 1  195 ? 20.59987  23.30522 37.45713 1.000 50.96823  ? 195 PHE   A CG  1 
ATOM   1495 C CD1 . PHE   A 1  195 ? 20.63339  23.11171 36.08119 1.000 52.61610  ? 195 PHE   A CD1 1 
ATOM   1496 C CD2 . PHE   A 1  195 ? 21.80916  23.51763 38.12100 1.000 52.21322  ? 195 PHE   A CD2 1 
ATOM   1497 C CE1 . PHE   A 1  195 ? 21.83371  23.17498 35.37763 1.000 51.04613  ? 195 PHE   A CE1 1 
ATOM   1498 C CE2 . PHE   A 1  195 ? 23.03351  23.57011 37.41777 1.000 51.28185  ? 195 PHE   A CE2 1 
ATOM   1499 C CZ  . PHE   A 1  195 ? 23.04192  23.40722 36.04787 1.000 51.04148  ? 195 PHE   A CZ  1 
ATOM   1500 N N   . GLY   A 1  196 ? 17.86197  26.16720 38.09643 1.000 53.22979  ? 196 GLY   A N   1 
ATOM   1501 C CA  . GLY   A 1  196 ? 17.98068  27.60804 37.97533 1.000 49.73419  ? 196 GLY   A CA  1 
ATOM   1502 C C   . GLY   A 1  196 ? 18.08347  28.24671 39.34492 1.000 54.31874  ? 196 GLY   A C   1 
ATOM   1503 O O   . GLY   A 1  196 ? 17.87918  27.60573 40.38073 1.000 54.79015  ? 196 GLY   A O   1 
ATOM   1504 N N   . GLU   A 1  197 ? 18.43134  29.53227 39.34014 1.000 52.62052  ? 197 GLU   A N   1 
ATOM   1505 C CA  . GLU   A 1  197 ? 18.56968  30.30935 40.56612 1.000 52.65210  ? 197 GLU   A CA  1 
ATOM   1506 C C   . GLU   A 1  197 ? 17.72595  31.57199 40.47089 1.000 52.17913  ? 197 GLU   A C   1 
ATOM   1507 O O   . GLU   A 1  197 ? 17.65741  32.19631 39.40852 1.000 54.72901  ? 197 GLU   A O   1 
ATOM   1508 C CB  . GLU   A 1  197 ? 20.02881  30.66603 40.84400 1.000 49.34486  ? 197 GLU   A CB  1 
ATOM   1509 C CG  . GLU   A 1  197 ? 20.26659  31.36688 42.19033 1.000 53.31218  ? 197 GLU   A CG  1 
ATOM   1510 C CD  . GLU   A 1  197 ? 20.34674  32.87680 42.04818 1.000 56.53270  ? 197 GLU   A CD  1 
ATOM   1511 O OE1 . GLU   A 1  197 ? 20.28208  33.34207 40.88984 1.000 54.22978  ? 197 GLU   A OE1 1 
ATOM   1512 O OE2 . GLU   A 1  197 ? 20.44438  33.58598 43.07753 1.000 51.13480  ? 197 GLU   A OE2 1 
ATOM   1513 N N   . SER   A 1  198 ? 17.06919  31.93349 41.57787 1.000 52.96252  ? 198 SER   A N   1 
ATOM   1514 C CA  . SER   A 1  198 ? 16.31732  33.19377 41.68682 1.000 55.75213  ? 198 SER   A CA  1 
ATOM   1515 C C   . SER   A 1  198 ? 15.15258  33.16386 40.70044 1.000 55.52823  ? 198 SER   A C   1 
ATOM   1516 O O   . SER   A 1  198 ? 14.33643  32.22603 40.77309 1.000 54.86235  ? 198 SER   A O   1 
ATOM   1517 C CB  . SER   A 1  198 ? 17.30238  34.35586 41.53252 1.000 51.22760  ? 198 SER   A CB  1 
ATOM   1518 O OG  . SER   A 1  198 ? 16.78935  35.52069 42.13810 1.000 55.83159  ? 198 SER   A OG  1 
ATOM   1519 N N   . ALA   A 1  199 ? 15.00596  34.14476 39.79380 1.000 51.67275  ? 199 ALA   A N   1 
ATOM   1520 C CA  . ALA   A 1  199 ? 13.93909  34.03759 38.79875 1.000 52.48500  ? 199 ALA   A CA  1 
ATOM   1521 C C   . ALA   A 1  199 ? 14.11464  32.79285 37.93088 1.000 51.91374  ? 199 ALA   A C   1 
ATOM   1522 O O   . ALA   A 1  199 ? 13.12660  32.24563 37.42159 1.000 50.11962  ? 199 ALA   A O   1 
ATOM   1523 C CB  . ALA   A 1  199 ? 13.87771  35.29669 37.92625 1.000 55.32945  ? 199 ALA   A CB  1 
ATOM   1524 N N   . GLY   A 1  200 ? 15.36128  32.33111 37.75399 1.000 54.21575  ? 200 GLY   A N   1 
ATOM   1525 C CA  . GLY   A 1  200 ? 15.58005  31.03627 37.12092 1.000 51.02377  ? 200 GLY   A CA  1 
ATOM   1526 C C   . GLY   A 1  200 ? 14.90639  29.90818 37.88625 1.000 53.50382  ? 200 GLY   A C   1 
ATOM   1527 O O   . GLY   A 1  200 ? 14.20819  29.07041 37.30786 1.000 51.43405  ? 200 GLY   A O   1 
ATOM   1528 N N   . ALA   A 1  201 ? 15.09322  29.88947 39.20887 1.000 55.46528  ? 201 ALA   A N   1 
ATOM   1529 C CA  . ALA   A 1  201 ? 14.44358  28.88219 40.04497 1.000 56.71141  ? 201 ALA   A CA  1 
ATOM   1530 C C   . ALA   A 1  201 ? 12.91959  29.00562 39.99126 1.000 56.68257  ? 201 ALA   A C   1 
ATOM   1531 O O   . ALA   A 1  201 ? 12.21856  27.99099 39.86600 1.000 55.86835  ? 201 ALA   A O   1 
ATOM   1532 C CB  . ALA   A 1  201 ? 14.95654  28.97647 41.48839 1.000 49.29348  ? 201 ALA   A CB  1 
ATOM   1533 N N   . ALA   A 1  202 ? 12.38063  30.23244 40.06127 1.000 52.08659  ? 202 ALA   A N   1 
ATOM   1534 C CA  . ALA   A 1  202 ? 10.92280  30.36437 39.98543 1.000 51.07736  ? 202 ALA   A CA  1 
ATOM   1535 C C   . ALA   A 1  202 ? 10.40386  29.86699 38.63600 1.000 53.26106  ? 202 ALA   A C   1 
ATOM   1536 O O   . ALA   A 1  202 ? 9.34687   29.21916 38.57499 1.000 53.06645  ? 202 ALA   A O   1 
ATOM   1537 C CB  . ALA   A 1  202 ? 10.48866  31.80167 40.25216 1.000 46.49829  ? 202 ALA   A CB  1 
ATOM   1538 N N   . SER   A 1  203 ? 11.17401  30.09331 37.55975 1.000 44.79674  ? 203 SER   A N   1 
ATOM   1539 C CA  . SER   A 1  203 ? 10.85929  29.52124 36.25038 1.000 44.58136  ? 203 SER   A CA  1 
ATOM   1540 C C   . SER   A 1  203 ? 10.78834  28.00013 36.31291 1.000 53.53180  ? 203 SER   A C   1 
ATOM   1541 O O   . SER   A 1  203 ? 9.81793   27.38570 35.84541 1.000 54.45155  ? 203 SER   A O   1 
ATOM   1542 C CB  . SER   A 1  203 ? 11.90730  29.94062 35.21320 1.000 53.77970  ? 203 SER   A CB  1 
ATOM   1543 O OG  . SER   A 1  203 ? 11.98653  31.35231 35.02762 1.000 51.05223  ? 203 SER   A OG  1 
ATOM   1544 N N   . VAL   A 1  204 ? 11.81307  27.36876 36.89127 1.000 54.15501  ? 204 VAL   A N   1 
ATOM   1545 C CA  . VAL   A 1  204 ? 11.78263  25.91694 37.06164 1.000 51.33367  ? 204 VAL   A CA  1 
ATOM   1546 C C   . VAL   A 1  204 ? 10.49374  25.49654 37.75379 1.000 51.00764  ? 204 VAL   A C   1 
ATOM   1547 O O   . VAL   A 1  204 ? 9.77445   24.59950 37.28603 1.000 55.07383  ? 204 VAL   A O   1 
ATOM   1548 C CB  . VAL   A 1  204 ? 13.02458  25.43666 37.83491 1.000 57.47714  ? 204 VAL   A CB  1 
ATOM   1549 C CG1 . VAL   A 1  204 ? 12.80372  24.01794 38.36901 1.000 52.50562  ? 204 VAL   A CG1 1 
ATOM   1550 C CG2 . VAL   A 1  204 ? 14.26181  25.50483 36.94578 1.000 50.26207  ? 204 VAL   A CG2 1 
ATOM   1551 N N   . SER   A 1  205 ? 10.14580  26.17754 38.84863 1.000 54.05138  ? 205 SER   A N   1 
ATOM   1552 C CA  . SER   A 1  205 ? 8.93374   25.79232 39.57401 1.000 55.89132  ? 205 SER   A CA  1 
ATOM   1553 C C   . SER   A 1  205 ? 7.68374   25.94150 38.70937 1.000 54.61181  ? 205 SER   A C   1 
ATOM   1554 O O   . SER   A 1  205 ? 6.74904   25.14406 38.83022 1.000 55.97569  ? 205 SER   A O   1 
ATOM   1555 C CB  . SER   A 1  205 ? 8.80479   26.59752 40.87195 1.000 51.00072  ? 205 SER   A CB  1 
ATOM   1556 O OG  . SER   A 1  205 ? 8.53696   27.96788 40.62246 1.000 62.32650  ? 205 SER   A OG  1 
ATOM   1557 N N   . LEU   A 1  206 ? 7.65945   26.92865 37.81334 1.000 53.56649  ? 206 LEU   A N   1 
ATOM   1558 C CA  . LEU   A 1  206 ? 6.50931   27.07921 36.93080 1.000 54.45072  ? 206 LEU   A CA  1 
ATOM   1559 C C   . LEU   A 1  206 ? 6.47319   26.01580 35.83881 1.000 53.40758  ? 206 LEU   A C   1 
ATOM   1560 O O   . LEU   A 1  206 ? 5.38618   25.67576 35.35802 1.000 56.71622  ? 206 LEU   A O   1 
ATOM   1561 C CB  . LEU   A 1  206 ? 6.51326   28.47205 36.31487 1.000 59.81836  ? 206 LEU   A CB  1 
ATOM   1562 C CG  . LEU   A 1  206 ? 6.05237   29.56230 37.27437 1.000 62.02716  ? 206 LEU   A CG  1 
ATOM   1563 C CD1 . LEU   A 1  206 ? 6.20351   30.89809 36.59207 1.000 58.27026  ? 206 LEU   A CD1 1 
ATOM   1564 C CD2 . LEU   A 1  206 ? 4.61829   29.30597 37.69553 1.000 50.37166  ? 206 LEU   A CD2 1 
ATOM   1565 N N   . HIS   A 1  207 ? 7.63656   25.49214 35.41981 1.000 51.63977  ? 207 HIS   A N   1 
ATOM   1566 C CA  . HIS   A 1  207 ? 7.63565   24.35909 34.48917 1.000 57.11162  ? 207 HIS   A CA  1 
ATOM   1567 C C   . HIS   A 1  207 ? 7.06849   23.09808 35.15096 1.000 54.46965  ? 207 HIS   A C   1 
ATOM   1568 O O   . HIS   A 1  207 ? 6.50416   22.23605 34.47397 1.000 57.48222  ? 207 HIS   A O   1 
ATOM   1569 C CB  . HIS   A 1  207 ? 9.05295   24.12340 33.93145 1.000 53.13874  ? 207 HIS   A CB  1 
ATOM   1570 C CG  . HIS   A 1  207 ? 9.46269   25.13710 32.90865 1.000 55.59391  ? 207 HIS   A CG  1 
ATOM   1571 N ND1 . HIS   A 1  207 ? 8.95474   25.15284 31.62403 1.000 54.87535  ? 207 HIS   A ND1 1 
ATOM   1572 C CD2 . HIS   A 1  207 ? 10.28559  26.21214 32.99927 1.000 56.20987  ? 207 HIS   A CD2 1 
ATOM   1573 C CE1 . HIS   A 1  207 ? 9.46923   26.17949 30.96039 1.000 54.34542  ? 207 HIS   A CE1 1 
ATOM   1574 N NE2 . HIS   A 1  207 ? 10.27596  26.84107 31.77315 1.000 53.89068  ? 207 HIS   A NE2 1 
ATOM   1575 N N   . LEU   A 1  208 ? 7.17804   22.98975 36.47159 1.000 57.86651  ? 208 LEU   A N   1 
ATOM   1576 C CA  . LEU   A 1  208 ? 6.49892   21.91301 37.17532 1.000 53.33682  ? 208 LEU   A CA  1 
ATOM   1577 C C   . LEU   A 1  208 ? 4.98758   22.11878 37.19271 1.000 54.93876  ? 208 LEU   A C   1 
ATOM   1578 O O   . LEU   A 1  208 ? 4.23713   21.15361 37.33324 1.000 56.09757  ? 208 LEU   A O   1 
ATOM   1579 C CB  . LEU   A 1  208 ? 7.01763   21.80626 38.60747 1.000 52.96982  ? 208 LEU   A CB  1 
ATOM   1580 C CG  . LEU   A 1  208 ? 8.41823   21.28390 38.87820 1.000 54.34987  ? 208 LEU   A CG  1 
ATOM   1581 C CD1 . LEU   A 1  208 ? 8.82420   21.59815 40.33093 1.000 53.38562  ? 208 LEU   A CD1 1 
ATOM   1582 C CD2 . LEU   A 1  208 ? 8.46521   19.77888 38.62343 1.000 50.33384  ? 208 LEU   A CD2 1 
ATOM   1583 N N   . LEU   A 1  209 ? 4.52219   23.34925 37.06101 1.000 55.10817  ? 209 LEU   A N   1 
ATOM   1584 C CA  . LEU   A 1  209 ? 3.08595   23.57127 37.00564 1.000 61.29229  ? 209 LEU   A CA  1 
ATOM   1585 C C   . LEU   A 1  209 ? 2.53128   23.53948 35.58656 1.000 60.18700  ? 209 LEU   A C   1 
ATOM   1586 O O   . LEU   A 1  209 ? 1.35793   23.19551 35.41217 1.000 60.56061  ? 209 LEU   A O   1 
ATOM   1587 C CB  . LEU   A 1  209 ? 2.71776   24.91285 37.65537 1.000 57.87599  ? 209 LEU   A CB  1 
ATOM   1588 C CG  . LEU   A 1  209 ? 3.08117   25.11552 39.13221 1.000 60.40834  ? 209 LEU   A CG  1 
ATOM   1589 C CD1 . LEU   A 1  209 ? 2.21781   26.16482 39.76095 1.000 61.07813  ? 209 LEU   A CD1 1 
ATOM   1590 C CD2 . LEU   A 1  209 ? 2.96590   23.85489 39.93714 1.000 59.16925  ? 209 LEU   A CD2 1 
ATOM   1591 N N   . SER   A 1  210 ? 3.31830   23.89953 34.56751 1.000 57.59750  ? 210 SER   A N   1 
ATOM   1592 C CA  . SER   A 1  210 ? 2.73618   24.06702 33.23872 1.000 61.66193  ? 210 SER   A CA  1 
ATOM   1593 C C   . SER   A 1  210 ? 2.57375   22.71273 32.57557 1.000 61.39036  ? 210 SER   A C   1 
ATOM   1594 O O   . SER   A 1  210 ? 3.56422   21.98969 32.41914 1.000 62.17502  ? 210 SER   A O   1 
ATOM   1595 C CB  . SER   A 1  210 ? 3.57846   24.96177 32.34389 1.000 66.15880  ? 210 SER   A CB  1 
ATOM   1596 O OG  . SER   A 1  210 ? 2.89788   25.14805 31.10268 1.000 62.13824  ? 210 SER   A OG  1 
ATOM   1597 N N   . PRO   A 1  211 ? 1.35829   22.32482 32.18911 1.000 71.44305  ? 211 PRO   A N   1 
ATOM   1598 C CA  . PRO   A 1  211 ? 1.18159   20.99337 31.58065 1.000 71.92590  ? 211 PRO   A CA  1 
ATOM   1599 C C   . PRO   A 1  211 ? 1.98168   20.81114 30.29928 1.000 72.26584  ? 211 PRO   A C   1 
ATOM   1600 O O   . PRO   A 1  211 ? 2.45302   19.69498 30.03570 1.000 74.87248  ? 211 PRO   A O   1 
ATOM   1601 C CB  . PRO   A 1  211 ? -0.33066  20.90132 31.32640 1.000 66.19150  ? 211 PRO   A CB  1 
ATOM   1602 C CG  . PRO   A 1  211 ? -0.95269  22.03078 32.08535 1.000 77.10463  ? 211 PRO   A CG  1 
ATOM   1603 C CD  . PRO   A 1  211 ? 0.09691   22.92639 32.64966 1.000 67.36293  ? 211 PRO   A CD  1 
ATOM   1604 N N   . GLY   A 1  212 ? 2.17378   21.87180 29.50778 1.000 60.09508  ? 212 GLY   A N   1 
ATOM   1605 C CA  . GLY   A 1  212 ? 2.97754   21.76655 28.29978 1.000 53.27629  ? 212 GLY   A CA  1 
ATOM   1606 C C   . GLY   A 1  212 ? 4.44185   21.42060 28.53681 1.000 63.03531  ? 212 GLY   A C   1 
ATOM   1607 O O   . GLY   A 1  212 ? 5.14606   21.09525 27.57375 1.000 60.03514  ? 212 GLY   A O   1 
ATOM   1608 N N   . SER   A 1  213 ? 4.92250   21.49216 29.77866 1.000 58.92548  ? 213 SER   A N   1 
ATOM   1609 C CA  . SER   A 1  213 ? 6.31575   21.17525 30.06908 1.000 60.45201  ? 213 SER   A CA  1 
ATOM   1610 C C   . SER   A 1  213 ? 6.51413   19.79297 30.67895 1.000 59.50911  ? 213 SER   A C   1 
ATOM   1611 O O   . SER   A 1  213 ? 7.65883   19.34400 30.76690 1.000 60.13764  ? 213 SER   A O   1 
ATOM   1612 C CB  . SER   A 1  213 ? 6.91479   22.22247 31.01656 1.000 53.38085  ? 213 SER   A CB  1 
ATOM   1613 O OG  . SER   A 1  213 ? 7.20089   23.42019 30.31579 1.000 55.88043  ? 213 SER   A OG  1 
ATOM   1614 N N   . HIS   A 1  214 ? 5.43998   19.10419 31.08708 1.000 58.12294  ? 214 HIS   A N   1 
ATOM   1615 C CA  . HIS   A 1  214 ? 5.61937   17.94201 31.95637 1.000 64.30745  ? 214 HIS   A CA  1 
ATOM   1616 C C   . HIS   A 1  214 ? 6.45877   16.85707 31.30583 1.000 57.26518  ? 214 HIS   A C   1 
ATOM   1617 O O   . HIS   A 1  214 ? 7.24810   16.19576 31.99146 1.000 58.51852  ? 214 HIS   A O   1 
ATOM   1618 C CB  . HIS   A 1  214 ? 4.26872   17.37750 32.39907 1.000 63.21394  ? 214 HIS   A CB  1 
ATOM   1619 C CG  . HIS   A 1  214 ? 3.61070   18.19829 33.46802 1.000 79.16684  ? 214 HIS   A CG  1 
ATOM   1620 N ND1 . HIS   A 1  214 ? 2.39476   17.86506 34.02938 1.000 72.15960  ? 214 HIS   A ND1 1 
ATOM   1621 C CD2 . HIS   A 1  214 ? 3.99737   19.35609 34.06729 1.000 69.00455  ? 214 HIS   A CD2 1 
ATOM   1622 C CE1 . HIS   A 1  214 ? 2.05931   18.77520 34.92957 1.000 67.89052  ? 214 HIS   A CE1 1 
ATOM   1623 N NE2 . HIS   A 1  214 ? 3.01542   19.68766 34.97484 1.000 73.34062  ? 214 HIS   A NE2 1 
ATOM   1624 N N   . SER   A 1  215 ? 6.34985   16.68687 29.99330 1.000 52.45855  ? 215 SER   A N   1 
ATOM   1625 C CA  . SER   A 1  215 ? 7.07746   15.62096 29.31233 1.000 55.34919  ? 215 SER   A CA  1 
ATOM   1626 C C   . SER   A 1  215 ? 8.45400   16.04929 28.82821 1.000 58.51459  ? 215 SER   A C   1 
ATOM   1627 O O   . SER   A 1  215 ? 9.10967   15.27689 28.12584 1.000 57.39767  ? 215 SER   A O   1 
ATOM   1628 C CB  . SER   A 1  215 ? 6.27884   15.10791 28.11311 1.000 62.01529  ? 215 SER   A CB  1 
ATOM   1629 O OG  . SER   A 1  215 ? 6.74125   15.76918 26.93205 1.000 71.17566  ? 215 SER   A OG  1 
ATOM   1630 N N   . LEU   A 1  216 ? 8.90619   17.25357 29.18394 1.000 59.49599  ? 216 LEU   A N   1 
ATOM   1631 C CA  . LEU   A 1  216 ? 10.17363  17.78701 28.71462 1.000 58.95016  ? 216 LEU   A CA  1 
ATOM   1632 C C   . LEU   A 1  216 ? 11.28803  17.69686 29.74812 1.000 60.65923  ? 216 LEU   A C   1 
ATOM   1633 O O   . LEU   A 1  216 ? 12.39018  18.18358 29.47556 1.000 56.88224  ? 216 LEU   A O   1 
ATOM   1634 C CB  . LEU   A 1  216 ? 9.98940   19.24598 28.28563 1.000 56.75171  ? 216 LEU   A CB  1 
ATOM   1635 C CG  . LEU   A 1  216 ? 8.84363   19.51925 27.30704 1.000 58.18474  ? 216 LEU   A CG  1 
ATOM   1636 C CD1 . LEU   A 1  216 ? 8.76227   21.00054 26.93311 1.000 52.85371  ? 216 LEU   A CD1 1 
ATOM   1637 C CD2 . LEU   A 1  216 ? 8.97237   18.61617 26.05929 1.000 54.21815  ? 216 LEU   A CD2 1 
ATOM   1638 N N   . PHE   A 1  217 ? 11.03266  17.12060 30.92703 1.000 51.88296  ? 217 PHE   A N   1 
ATOM   1639 C CA  . PHE   A 1  217 ? 12.09339  16.97766 31.92347 1.000 53.23445  ? 217 PHE   A CA  1 
ATOM   1640 C C   . PHE   A 1  217 ? 11.68645  15.93189 32.95364 1.000 54.40154  ? 217 PHE   A C   1 
ATOM   1641 O O   . PHE   A 1  217 ? 10.51415  15.58064 33.07617 1.000 53.97832  ? 217 PHE   A O   1 
ATOM   1642 C CB  . PHE   A 1  217 ? 12.43388  18.32181 32.60136 1.000 53.75915  ? 217 PHE   A CB  1 
ATOM   1643 C CG  . PHE   A 1  217 ? 11.33375  18.90032 33.47389 1.000 56.83630  ? 217 PHE   A CG  1 
ATOM   1644 C CD1 . PHE   A 1  217 ? 10.25599  19.58254 32.91060 1.000 56.07849  ? 217 PHE   A CD1 1 
ATOM   1645 C CD2 . PHE   A 1  217 ? 11.41764  18.81662 34.86621 1.000 54.61144  ? 217 PHE   A CD2 1 
ATOM   1646 C CE1 . PHE   A 1  217 ? 9.25765   20.15434 33.71855 1.000 54.98960  ? 217 PHE   A CE1 1 
ATOM   1647 C CE2 . PHE   A 1  217 ? 10.42454  19.37981 35.68385 1.000 55.07259  ? 217 PHE   A CE2 1 
ATOM   1648 C CZ  . PHE   A 1  217 ? 9.34396   20.04773 35.11170 1.000 53.50121  ? 217 PHE   A CZ  1 
ATOM   1649 N N   . THR   A 1  218 ? 12.67432  15.45051 33.70408 1.000 57.64554  ? 218 THR   A N   1 
ATOM   1650 C CA  . THR   A 1  218 ? 12.46304  14.43815 34.73234 1.000 57.07559  ? 218 THR   A CA  1 
ATOM   1651 C C   . THR   A 1  218 ? 12.31866  15.03687 36.12927 1.000 60.90596  ? 218 THR   A C   1 
ATOM   1652 O O   . THR   A 1  218 ? 11.34025  14.74655 36.83810 1.000 53.70134  ? 218 THR   A O   1 
ATOM   1653 C CB  . THR   A 1  218 ? 13.63112  13.44878 34.73078 1.000 61.16173  ? 218 THR   A CB  1 
ATOM   1654 O OG1 . THR   A 1  218 ? 13.98773  13.12402 33.37768 1.000 60.62415  ? 218 THR   A OG1 1 
ATOM   1655 C CG2 . THR   A 1  218 ? 13.25942  12.17933 35.49549 1.000 59.83082  ? 218 THR   A CG2 1 
ATOM   1656 N N   . ARG   A 1  219 ? 13.27521  15.88345 36.52059 1.000 53.34237  ? 219 ARG   A N   1 
ATOM   1657 C CA  . ARG   A 1  219 ? 13.45411  16.35077 37.88910 1.000 55.47040  ? 219 ARG   A CA  1 
ATOM   1658 C C   . ARG   A 1  219 ? 13.77372  17.84208 37.88232 1.000 56.44957  ? 219 ARG   A C   1 
ATOM   1659 O O   . ARG   A 1  219 ? 14.06138  18.43731 36.83609 1.000 56.80401  ? 219 ARG   A O   1 
ATOM   1660 C CB  . ARG   A 1  219 ? 14.60806  15.61205 38.57485 1.000 53.17287  ? 219 ARG   A CB  1 
ATOM   1661 C CG  . ARG   A 1  219 ? 14.24943  14.32763 39.18931 1.000 65.12136  ? 219 ARG   A CG  1 
ATOM   1662 C CD  . ARG   A 1  219 ? 15.42407  13.78604 39.98109 1.000 61.69416  ? 219 ARG   A CD  1 
ATOM   1663 N NE  . ARG   A 1  219 ? 16.24822  12.90652 39.16911 1.000 60.00289  ? 219 ARG   A NE  1 
ATOM   1664 C CZ  . ARG   A 1  219 ? 15.83477  11.75584 38.66476 1.000 63.26765  ? 219 ARG   A CZ  1 
ATOM   1665 N NH1 . ARG   A 1  219 ? 14.60894  11.31241 38.88412 1.000 62.19266  ? 219 ARG   A NH1 1 
ATOM   1666 N NH2 . ARG   A 1  219 ? 16.68027  11.02196 37.93684 1.000 65.14799  ? 219 ARG   A NH2 1 
ATOM   1667 N N   . ALA   A 1  220 ? 13.80930  18.42929 39.07840 1.000 55.98423  ? 220 ALA   A N   1 
ATOM   1668 C CA  . ALA   A 1  220 ? 13.94735  19.87644 39.19859 1.000 55.14381  ? 220 ALA   A CA  1 
ATOM   1669 C C   . ALA   A 1  220 ? 14.76266  20.23352 40.42630 1.000 50.57021  ? 220 ALA   A C   1 
ATOM   1670 O O   . ALA   A 1  220 ? 14.65702  19.58341 41.47452 1.000 52.96058  ? 220 ALA   A O   1 
ATOM   1671 C CB  . ALA   A 1  220 ? 12.56987  20.56382 39.28351 1.000 58.33887  ? 220 ALA   A CB  1 
ATOM   1672 N N   . ILE   A 1  221 ? 15.56440  21.27744 40.27519 1.000 50.07246  ? 221 ILE   A N   1 
ATOM   1673 C CA  . ILE   A 1  221 ? 16.41491  21.84171 41.31763 1.000 51.56818  ? 221 ILE   A CA  1 
ATOM   1674 C C   . ILE   A 1  221 ? 16.15155  23.34256 41.35992 1.000 57.04357  ? 221 ILE   A C   1 
ATOM   1675 O O   . ILE   A 1  221 ? 16.27847  24.01987 40.32894 1.000 53.35129  ? 221 ILE   A O   1 
ATOM   1676 C CB  . ILE   A 1  221 ? 17.91129  21.59151 41.03982 1.000 52.87034  ? 221 ILE   A CB  1 
ATOM   1677 C CG1 . ILE   A 1  221 ? 18.25723  20.09350 40.95325 1.000 51.93218  ? 221 ILE   A CG1 1 
ATOM   1678 C CG2 . ILE   A 1  221 ? 18.78983  22.32153 42.06617 1.000 51.56638  ? 221 ILE   A CG2 1 
ATOM   1679 C CD1 . ILE   A 1  221 ? 19.75125  19.83732 40.60732 1.000 45.96456  ? 221 ILE   A CD1 1 
ATOM   1680 N N   . LEU   A 1  222 ? 15.81539  23.86764 42.54604 1.000 51.70121  ? 222 LEU   A N   1 
ATOM   1681 C CA  . LEU   A 1  222 ? 15.40801  25.27098 42.70208 1.000 56.87257  ? 222 LEU   A CA  1 
ATOM   1682 C C   . LEU   A 1  222 ? 16.31922  25.98019 43.70397 1.000 54.61156  ? 222 LEU   A C   1 
ATOM   1683 O O   . LEU   A 1  222 ? 16.20038  25.76367 44.91710 1.000 52.35768  ? 222 LEU   A O   1 
ATOM   1684 C CB  . LEU   A 1  222 ? 13.95340  25.37276 43.15786 1.000 52.18750  ? 222 LEU   A CB  1 
ATOM   1685 C CG  . LEU   A 1  222 ? 12.85202  24.81665 42.24961 1.000 57.10852  ? 222 LEU   A CG  1 
ATOM   1686 C CD1 . LEU   A 1  222 ? 12.84072  23.29316 42.29683 1.000 59.20879  ? 222 LEU   A CD1 1 
ATOM   1687 C CD2 . LEU   A 1  222 ? 11.53046  25.33367 42.72242 1.000 53.03100  ? 222 LEU   A CD2 1 
ATOM   1688 N N   . GLN   A 1  223 ? 17.19530  26.85153 43.20309 1.000 48.49389  ? 223 GLN   A N   1 
ATOM   1689 C CA  . GLN   A 1  223 ? 18.16207  27.57198 44.02600 1.000 49.30217  ? 223 GLN   A CA  1 
ATOM   1690 C C   . GLN   A 1  223 ? 17.66504  28.99371 44.28836 1.000 51.22334  ? 223 GLN   A C   1 
ATOM   1691 O O   . GLN   A 1  223 ? 17.50479  29.78112 43.34676 1.000 53.00123  ? 223 GLN   A O   1 
ATOM   1692 C CB  . GLN   A 1  223 ? 19.53690  27.57455 43.33489 1.000 49.15309  ? 223 GLN   A CB  1 
ATOM   1693 C CG  . GLN   A 1  223 ? 20.06562  26.12573 43.03244 1.000 45.43252  ? 223 GLN   A CG  1 
ATOM   1694 C CD  . GLN   A 1  223 ? 21.33613  26.03809 42.13983 1.000 51.53413  ? 223 GLN   A CD  1 
ATOM   1695 O OE1 . GLN   A 1  223 ? 21.60067  24.98116 41.55060 1.000 59.90472  ? 223 GLN   A OE1 1 
ATOM   1696 N NE2 . GLN   A 1  223 ? 22.12481  27.11862 42.06181 1.000 49.07323  ? 223 GLN   A NE2 1 
ATOM   1697 N N   . SER   A 1  224 ? 17.40467  29.31354 45.56475 1.000 49.76967  ? 224 SER   A N   1 
ATOM   1698 C CA  . SER   A 1  224 ? 16.97628  30.66404 45.99040 1.000 53.82455  ? 224 SER   A CA  1 
ATOM   1699 C C   . SER   A 1  224 ? 15.83308  31.22148 45.13900 1.000 51.17227  ? 224 SER   A C   1 
ATOM   1700 O O   . SER   A 1  224 ? 15.91314  32.33615 44.62532 1.000 55.60727  ? 224 SER   A O   1 
ATOM   1701 C CB  . SER   A 1  224 ? 18.15023  31.65862 45.97083 1.000 50.00576  ? 224 SER   A CB  1 
ATOM   1702 O OG  . SER   A 1  224 ? 19.24059  31.21688 46.77881 1.000 55.04044  ? 224 SER   A OG  1 
ATOM   1703 N N   . GLY   A 1  225 ? 14.76150  30.44719 44.97400 1.000 50.76429  ? 225 GLY   A N   1 
ATOM   1704 C CA  . GLY   A 1  225 ? 13.61209  30.97744 44.25496 1.000 47.96053  ? 225 GLY   A CA  1 
ATOM   1705 C C   . GLY   A 1  225 ? 12.49772  29.98137 44.02068 1.000 54.77287  ? 225 GLY   A C   1 
ATOM   1706 O O   . GLY   A 1  225 ? 12.75068  28.77454 43.98542 1.000 50.06580  ? 225 GLY   A O   1 
ATOM   1707 N N   . SER   A 1  226 ? 11.26404  30.47197 43.86836 1.000 52.97444  ? 226 SER   A N   1 
ATOM   1708 C CA  . SER   A 1  226 ? 10.09878  29.63498 43.62119 1.000 56.98017  ? 226 SER   A CA  1 
ATOM   1709 C C   . SER   A 1  226 ? 8.95358   30.56144 43.24431 1.000 59.50326  ? 226 SER   A C   1 
ATOM   1710 O O   . SER   A 1  226 ? 8.95799   31.73415 43.61572 1.000 59.25300  ? 226 SER   A O   1 
ATOM   1711 C CB  . SER   A 1  226 ? 9.72830   28.77159 44.84520 1.000 56.12160  ? 226 SER   A CB  1 
ATOM   1712 O OG  . SER   A 1  226 ? 9.58433   29.55087 46.02861 1.000 52.25369  ? 226 SER   A OG  1 
ATOM   1713 N N   . PHE   A 1  227 ? 7.94767   30.01507 42.53790 1.000 57.94314  ? 227 PHE   A N   1 
ATOM   1714 C CA  . PHE   A 1  227 ? 6.89840   30.86993 41.97127 1.000 56.51975  ? 227 PHE   A CA  1 
ATOM   1715 C C   . PHE   A 1  227 ? 6.07425   31.57812 43.04838 1.000 62.46306  ? 227 PHE   A C   1 
ATOM   1716 O O   . PHE   A 1  227 ? 5.49163   32.63021 42.77929 1.000 63.54542  ? 227 PHE   A O   1 
ATOM   1717 C CB  . PHE   A 1  227 ? 5.96656   30.06341 41.04471 1.000 58.00027  ? 227 PHE   A CB  1 
ATOM   1718 C CG  . PHE   A 1  227 ? 5.08438   29.07290 41.76853 1.000 59.56446  ? 227 PHE   A CG  1 
ATOM   1719 C CD1 . PHE   A 1  227 ? 3.98227   29.49592 42.49086 1.000 63.82280  ? 227 PHE   A CD1 1 
ATOM   1720 C CD2 . PHE   A 1  227 ? 5.36231   27.71946 41.71672 1.000 60.56374  ? 227 PHE   A CD2 1 
ATOM   1721 C CE1 . PHE   A 1  227 ? 3.20131   28.59750 43.17105 1.000 69.14823  ? 227 PHE   A CE1 1 
ATOM   1722 C CE2 . PHE   A 1  227 ? 4.58263   26.81443 42.39135 1.000 60.44529  ? 227 PHE   A CE2 1 
ATOM   1723 C CZ  . PHE   A 1  227 ? 3.49481   27.25223 43.12170 1.000 65.92870  ? 227 PHE   A CZ  1 
ATOM   1724 N N   . ASN   A 1  228 ? 5.96234   31.00979 44.25035 1.000 61.47845  ? 228 ASN   A N   1 
ATOM   1725 C CA  . ASN   A 1  228 ? 5.14358   31.65424 45.26995 1.000 53.74050  ? 228 ASN   A CA  1 
ATOM   1726 C C   . ASN   A 1  228 ? 5.88389   32.76826 46.00686 1.000 60.43622  ? 228 ASN   A C   1 
ATOM   1727 O O   . ASN   A 1  228 ? 5.32655   33.33355 46.95105 1.000 61.19441  ? 228 ASN   A O   1 
ATOM   1728 C CB  . ASN   A 1  228 ? 4.61595   30.61152 46.26221 1.000 52.13579  ? 228 ASN   A CB  1 
ATOM   1729 C CG  . ASN   A 1  228 ? 5.72638   29.86581 46.98841 1.000 57.14443  ? 228 ASN   A CG  1 
ATOM   1730 O OD1 . ASN   A 1  228 ? 6.82271   29.62871 46.44493 1.000 57.80492  ? 228 ASN   A OD1 1 
ATOM   1731 N ND2 . ASN   A 1  228 ? 5.44831   29.48559 48.21000 1.000 54.91637  ? 228 ASN   A ND2 1 
ATOM   1732 N N   . ALA   A 1  229 ? 7.11628   33.09474 45.61564 1.000 54.42364  ? 229 ALA   A N   1 
ATOM   1733 C CA  . ALA   A 1  229 ? 7.75219   34.29598 46.13647 1.000 60.95323  ? 229 ALA   A CA  1 
ATOM   1734 C C   . ALA   A 1  229 ? 6.96619   35.54150 45.71129 1.000 61.82258  ? 229 ALA   A C   1 
ATOM   1735 O O   . ALA   A 1  229 ? 6.43607   35.59541 44.59872 1.000 62.43751  ? 229 ALA   A O   1 
ATOM   1736 C CB  . ALA   A 1  229 ? 9.18911   34.39773 45.63554 1.000 55.73913  ? 229 ALA   A CB  1 
ATOM   1737 N N   . PRO   A 1  230 ? 6.89055   36.56533 46.57233 1.000 61.02757  ? 230 PRO   A N   1 
ATOM   1738 C CA  . PRO   A 1  230 ? 5.97587   37.69563 46.27985 1.000 60.67374  ? 230 PRO   A CA  1 
ATOM   1739 C C   . PRO   A 1  230 ? 6.30652   38.43991 44.97994 1.000 62.66989  ? 230 PRO   A C   1 
ATOM   1740 O O   . PRO   A 1  230 ? 5.39550   38.99694 44.35284 1.000 63.81547  ? 230 PRO   A O   1 
ATOM   1741 C CB  . PRO   A 1  230 ? 6.11526   38.60592 47.51661 1.000 58.92797  ? 230 PRO   A CB  1 
ATOM   1742 C CG  . PRO   A 1  230 ? 7.42624   38.20243 48.17886 1.000 61.16520  ? 230 PRO   A CG  1 
ATOM   1743 C CD  . PRO   A 1  230 ? 7.60970   36.72836 47.85078 1.000 56.62260  ? 230 PRO   A CD  1 
ATOM   1744 N N   . TRP   A 1  231 ? 7.57015   38.44377 44.54671 1.000 61.03046  ? 231 TRP   A N   1 
ATOM   1745 C CA  . TRP   A 1  231 ? 8.00081   39.10095 43.31178 1.000 63.33493  ? 231 TRP   A CA  1 
ATOM   1746 C C   . TRP   A 1  231 ? 7.79513   38.24883 42.05745 1.000 61.69253  ? 231 TRP   A C   1 
ATOM   1747 O O   . TRP   A 1  231 ? 8.08582   38.72203 40.95616 1.000 64.41143  ? 231 TRP   A O   1 
ATOM   1748 C CB  . TRP   A 1  231 ? 9.49597   39.47025 43.41910 1.000 56.89552  ? 231 TRP   A CB  1 
ATOM   1749 C CG  . TRP   A 1  231 ? 10.35031  38.30019 43.90005 1.000 60.44922  ? 231 TRP   A CG  1 
ATOM   1750 C CD1 . TRP   A 1  231 ? 10.72019  38.02770 45.19054 1.000 61.21946  ? 231 TRP   A CD1 1 
ATOM   1751 C CD2 . TRP   A 1  231 ? 10.93560  37.26158 43.09513 1.000 58.26910  ? 231 TRP   A CD2 1 
ATOM   1752 N NE1 . TRP   A 1  231 ? 11.48536  36.88865 45.23821 1.000 54.97670  ? 231 TRP   A NE1 1 
ATOM   1753 C CE2 . TRP   A 1  231 ? 11.63095  36.39692 43.96916 1.000 57.52116  ? 231 TRP   A CE2 1 
ATOM   1754 C CE3 . TRP   A 1  231 ? 10.94131  36.98042 41.72175 1.000 55.53881  ? 231 TRP   A CE3 1 
ATOM   1755 C CZ2 . TRP   A 1  231 ? 12.31994  35.26337 43.51511 1.000 60.23141  ? 231 TRP   A CZ2 1 
ATOM   1756 C CZ3 . TRP   A 1  231 ? 11.61790  35.85577 41.27394 1.000 54.48051  ? 231 TRP   A CZ3 1 
ATOM   1757 C CH2 . TRP   A 1  231 ? 12.30091  35.00712 42.16701 1.000 55.65636  ? 231 TRP   A CH2 1 
ATOM   1758 N N   . ALA   A 1  232 ? 7.31848   37.00900 42.18147 1.000 56.22817  ? 232 ALA   A N   1 
ATOM   1759 C CA  . ALA   A 1  232 ? 7.47284   36.05933 41.07710 1.000 58.12600  ? 232 ALA   A CA  1 
ATOM   1760 C C   . ALA   A 1  232 ? 6.35957   36.11984 40.03278 1.000 64.85767  ? 232 ALA   A C   1 
ATOM   1761 O O   . ALA   A 1  232 ? 6.59587   35.76129 38.87230 1.000 61.83861  ? 232 ALA   A O   1 
ATOM   1762 C CB  . ALA   A 1  232 ? 7.55911   34.63760 41.61815 1.000 58.09293  ? 232 ALA   A CB  1 
ATOM   1763 N N   . VAL   A 1  233 ? 5.14780   36.52802 40.40557 1.000 62.18999  ? 233 VAL   A N   1 
ATOM   1764 C CA  . VAL   A 1  233 ? 4.02373   36.56566 39.47579 1.000 64.20756  ? 233 VAL   A CA  1 
ATOM   1765 C C   . VAL   A 1  233 ? 3.41307   37.96126 39.48533 1.000 68.21993  ? 233 VAL   A C   1 
ATOM   1766 O O   . VAL   A 1  233 ? 3.20614   38.54433 40.55346 1.000 70.22702  ? 233 VAL   A O   1 
ATOM   1767 C CB  . VAL   A 1  233 ? 2.95843   35.50758 39.82909 1.000 69.31321  ? 233 VAL   A CB  1 
ATOM   1768 C CG1 . VAL   A 1  233 ? 1.79514   35.57173 38.85653 1.000 59.63585  ? 233 VAL   A CG1 1 
ATOM   1769 C CG2 . VAL   A 1  233 ? 3.58830   34.09645 39.84367 1.000 61.50309  ? 233 VAL   A CG2 1 
ATOM   1770 N N   . THR   A 1  234 ? 3.16581   38.50798 38.29818 1.000 71.25227  ? 234 THR   A N   1 
ATOM   1771 C CA  . THR   A 1  234 ? 2.41670   39.74541 38.14368 1.000 68.33127  ? 234 THR   A CA  1 
ATOM   1772 C C   . THR   A 1  234 ? 0.93943   39.39919 37.96345 1.000 78.05645  ? 234 THR   A C   1 
ATOM   1773 O O   . THR   A 1  234 ? 0.59957   38.42842 37.28002 1.000 73.03548  ? 234 THR   A O   1 
ATOM   1774 C CB  . THR   A 1  234 ? 2.91268   40.53263 36.93187 1.000 59.56573  ? 234 THR   A CB  1 
ATOM   1775 O OG1 . THR   A 1  234 ? 4.33954   40.45020 36.85531 1.000 73.98575  ? 234 THR   A OG1 1 
ATOM   1776 C CG2 . THR   A 1  234 ? 2.49903   42.00741 37.03960 1.000 79.76183  ? 234 THR   A CG2 1 
ATOM   1777 N N   . SER   A 1  235 ? 0.06240   40.18891 38.58195 1.000 79.59299  ? 235 SER   A N   1 
ATOM   1778 C CA  . SER   A 1  235 ? -1.37014  39.93477 38.48319 1.000 84.64733  ? 235 SER   A CA  1 
ATOM   1779 C C   . SER   A 1  235 ? -1.90293  40.33489 37.11027 1.000 85.84595  ? 235 SER   A C   1 
ATOM   1780 O O   . SER   A 1  235 ? -1.30581  41.14574 36.39705 1.000 84.57091  ? 235 SER   A O   1 
ATOM   1781 C CB  . SER   A 1  235 ? -2.12866  40.70398 39.56031 1.000 84.88982  ? 235 SER   A CB  1 
ATOM   1782 O OG  . SER   A 1  235 ? -2.27096  42.07215 39.19151 1.000 98.69013  ? 235 SER   A OG  1 
ATOM   1783 N N   . LEU   A 1  236 ? -3.04978  39.75587 36.74020 1.000 84.65973  ? 236 LEU   A N   1 
ATOM   1784 C CA  . LEU   A 1  236 ? -3.73256  40.23365 35.54000 1.000 90.97375  ? 236 LEU   A CA  1 
ATOM   1785 C C   . LEU   A 1  236 ? -4.06720  41.71420 35.65166 1.000 88.78269  ? 236 LEU   A C   1 
ATOM   1786 O O   . LEU   A 1  236 ? -4.00405  42.44037 34.65388 1.000 85.05118  ? 236 LEU   A O   1 
ATOM   1787 C CB  . LEU   A 1  236 ? -4.99956  39.41989 35.27348 1.000 90.42366  ? 236 LEU   A CB  1 
ATOM   1788 C CG  . LEU   A 1  236 ? -4.69232  37.94505 35.00190 1.000 96.98411  ? 236 LEU   A CG  1 
ATOM   1789 C CD1 . LEU   A 1  236 ? -5.93907  37.22326 34.45923 1.000 97.59279  ? 236 LEU   A CD1 1 
ATOM   1790 C CD2 . LEU   A 1  236 ? -3.46665  37.78199 34.07395 1.000 72.35878  ? 236 LEU   A CD2 1 
ATOM   1791 N N   . TYR   A 1  237 ? -4.40431  42.18070 36.85530 1.000 93.46371  ? 237 TYR   A N   1 
ATOM   1792 C CA  . TYR   A 1  237 ? -4.58266  43.60431 37.10329 1.000 94.55564  ? 237 TYR   A CA  1 
ATOM   1793 C C   . TYR   A 1  237 ? -3.31455  44.37365 36.75121 1.000 97.28205  ? 237 TYR   A C   1 
ATOM   1794 O O   . TYR   A 1  237 ? -3.30620  45.15187 35.78793 1.000 97.25698  ? 237 TYR   A O   1 
ATOM   1795 C CB  . TYR   A 1  237 ? -4.97130  43.86072 38.56568 1.000 103.16389 ? 237 TYR   A CB  1 
ATOM   1796 C CG  . TYR   A 1  237 ? -5.06322  45.33641 38.92927 1.000 117.50918 ? 237 TYR   A CG  1 
ATOM   1797 C CD1 . TYR   A 1  237 ? -5.96393  46.17430 38.27882 1.000 119.84436 ? 237 TYR   A CD1 1 
ATOM   1798 C CD2 . TYR   A 1  237 ? -4.24125  45.89503 39.91131 1.000 118.41205 ? 237 TYR   A CD2 1 
ATOM   1799 C CE1 . TYR   A 1  237 ? -6.05592  47.51794 38.58892 1.000 125.05740 ? 237 TYR   A CE1 1 
ATOM   1800 C CE2 . TYR   A 1  237 ? -4.32806  47.25921 40.23447 1.000 124.63108 ? 237 TYR   A CE2 1 
ATOM   1801 C CZ  . TYR   A 1  237 ? -5.24748  48.06057 39.55669 1.000 126.58447 ? 237 TYR   A CZ  1 
ATOM   1802 O OH  . TYR   A 1  237 ? -5.40680  49.40753 39.79749 1.000 127.83531 ? 237 TYR   A OH  1 
ATOM   1803 N N   . GLU   A 1  238 ? -2.23675  44.15895 37.51448 1.000 90.05160  ? 238 GLU   A N   1 
ATOM   1804 C CA  . GLU   A 1  238 ? -1.03131  44.96047 37.31473 1.000 90.07592  ? 238 GLU   A CA  1 
ATOM   1805 C C   . GLU   A 1  238 ? -0.48345  44.82290 35.89854 1.000 83.97907  ? 238 GLU   A C   1 
ATOM   1806 O O   . GLU   A 1  238 ? 0.06490   45.78380 35.34935 1.000 82.38878  ? 238 GLU   A O   1 
ATOM   1807 C CB  . GLU   A 1  238 ? 0.05649   44.57741 38.31458 1.000 91.98327  ? 238 GLU   A CB  1 
ATOM   1808 C CG  . GLU   A 1  238 ? -0.25592  44.80443 39.77831 1.000 97.31844  ? 238 GLU   A CG  1 
ATOM   1809 C CD  . GLU   A 1  238 ? 0.57136   43.87737 40.66306 1.000 107.97006 ? 238 GLU   A CD  1 
ATOM   1810 O OE1 . GLU   A 1  238 ? 0.74653   42.69305 40.28715 1.000 104.13499 ? 238 GLU   A OE1 1 
ATOM   1811 O OE2 . GLU   A 1  238 ? 1.07985   44.33797 41.71068 1.000 113.64556 ? 238 GLU   A OE2 1 
ATOM   1812 N N   . ALA   A 1  239 ? -0.59580  43.63523 35.29474 1.000 82.41143  ? 239 ALA   A N   1 
ATOM   1813 C CA  . ALA   A 1  239 ? -0.08474  43.47446 33.93613 1.000 78.12509  ? 239 ALA   A CA  1 
ATOM   1814 C C   . ALA   A 1  239 ? -0.78781  44.41788 32.97107 1.000 84.66805  ? 239 ALA   A C   1 
ATOM   1815 O O   . ALA   A 1  239 ? -0.14246  45.02600 32.11062 1.000 81.06888  ? 239 ALA   A O   1 
ATOM   1816 C CB  . ALA   A 1  239 ? -0.22653  42.02986 33.46869 1.000 73.43525  ? 239 ALA   A CB  1 
ATOM   1817 N N   . ARG   A 1  240 ? -2.10868  44.57068 33.10911 1.000 85.35467  ? 240 ARG   A N   1 
ATOM   1818 C CA  . ARG   A 1  240 ? -2.82144  45.52765 32.27288 1.000 82.57129  ? 240 ARG   A CA  1 
ATOM   1819 C C   . ARG   A 1  240 ? -2.38891  46.96014 32.57998 1.000 80.69929  ? 240 ARG   A C   1 
ATOM   1820 O O   . ARG   A 1  240 ? -2.00652  47.70244 31.66940 1.000 81.07345  ? 240 ARG   A O   1 
ATOM   1821 C CB  . ARG   A 1  240 ? -4.33423  45.36200 32.44829 1.000 94.34981  ? 240 ARG   A CB  1 
ATOM   1822 C CG  . ARG   A 1  240 ? -5.17424  46.42261 31.72034 1.000 87.89530  ? 240 ARG   A CG  1 
ATOM   1823 C CD  . ARG   A 1  240 ? -6.67315  46.11846 31.78567 1.000 99.08361  ? 240 ARG   A CD  1 
ATOM   1824 N NE  . ARG   A 1  240 ? -7.42015  46.76513 30.70890 1.000 98.58282  ? 240 ARG   A NE  1 
ATOM   1825 C CZ  . ARG   A 1  240 ? -7.41357  46.35286 29.44797 1.000 99.12447  ? 240 ARG   A CZ  1 
ATOM   1826 N NH1 . ARG   A 1  240 ? -6.73645  45.27398 29.07784 1.000 101.09472 ? 240 ARG   A NH1 1 
ATOM   1827 N NH2 . ARG   A 1  240 ? -8.09141  47.04573 28.53377 1.000 99.25974  ? 240 ARG   A NH2 1 
ATOM   1828 N N   . ASN   A 1  241 ? -2.42876  47.36653 33.86160 1.000 85.32231  ? 241 ASN   A N   1 
ATOM   1829 C CA  . ASN   A 1  241 ? -2.03248  48.73350 34.22127 1.000 87.79789  ? 241 ASN   A CA  1 
ATOM   1830 C C   . ASN   A 1  241 ? -0.61815  49.02799 33.73551 1.000 86.35364  ? 241 ASN   A C   1 
ATOM   1831 O O   . ASN   A 1  241 ? -0.33007  50.14551 33.28141 1.000 84.21709  ? 241 ASN   A O   1 
ATOM   1832 C CB  . ASN   A 1  241 ? -2.14646  48.96396 35.74586 1.000 94.10086  ? 241 ASN   A CB  1 
ATOM   1833 C CG  . ASN   A 1  241 ? -2.66157  50.39040 36.12581 1.000 101.85004 ? 241 ASN   A CG  1 
ATOM   1834 O OD1 . ASN   A 1  241 ? -3.70276  50.83756 35.64336 1.000 98.27648  ? 241 ASN   A OD1 1 
ATOM   1835 N ND2 . ASN   A 1  241 ? -1.92186  51.08420 37.01313 1.000 107.67372 ? 241 ASN   A ND2 1 
ATOM   1836 N N   . ARG   A 1  242 ? 0.26976   48.02073 33.78947 1.000 83.00756  ? 242 ARG   A N   1 
ATOM   1837 C CA  . ARG   A 1  242 ? 1.65214   48.21210 33.34711 1.000 82.86447  ? 242 ARG   A CA  1 
ATOM   1838 C C   . ARG   A 1  242 ? 1.73746   48.32385 31.82760 1.000 81.25584  ? 242 ARG   A C   1 
ATOM   1839 O O   . ARG   A 1  242 ? 2.41137   49.22095 31.29954 1.000 76.32752  ? 242 ARG   A O   1 
ATOM   1840 C CB  . ARG   A 1  242 ? 2.53377   47.07624 33.86732 1.000 75.66595  ? 242 ARG   A CB  1 
ATOM   1841 C CG  . ARG   A 1  242 ? 2.96289   47.27214 35.32492 1.000 81.58573  ? 242 ARG   A CG  1 
ATOM   1842 C CD  . ARG   A 1  242 ? 3.35401   45.97086 35.98578 1.000 76.56203  ? 242 ARG   A CD  1 
ATOM   1843 N NE  . ARG   A 1  242 ? 3.17320   45.97990 37.43337 1.000 81.95057  ? 242 ARG   A NE  1 
ATOM   1844 C CZ  . ARG   A 1  242 ? 3.95110   45.32387 38.28634 1.000 87.76485  ? 242 ARG   A CZ  1 
ATOM   1845 N NH1 . ARG   A 1  242 ? 5.02004   44.65807 37.87666 1.000 80.84437  ? 242 ARG   A NH1 1 
ATOM   1846 N NH2 . ARG   A 1  242 ? 3.64591   45.33082 39.58129 1.000 88.58876  ? 242 ARG   A NH2 1 
ATOM   1847 N N   . THR   A 1  243 ? 1.03359   47.44497 31.11265 1.000 79.31673  ? 243 THR   A N   1 
ATOM   1848 C CA  . THR   A 1  243 ? 0.96428   47.54415 29.65800 1.000 78.24928  ? 243 THR   A CA  1 
ATOM   1849 C C   . THR   A 1  243 ? 0.41581   48.89573 29.21036 1.000 81.01215  ? 243 THR   A C   1 
ATOM   1850 O O   . THR   A 1  243 ? 0.95931   49.52611 28.29719 1.000 84.03130  ? 243 THR   A O   1 
ATOM   1851 C CB  . THR   A 1  243 ? 0.09961   46.41590 29.09984 1.000 79.24792  ? 243 THR   A CB  1 
ATOM   1852 O OG1 . THR   A 1  243 ? 0.82935   45.18754 29.15392 1.000 77.39427  ? 243 THR   A OG1 1 
ATOM   1853 C CG2 . THR   A 1  243 ? -0.28050  46.70800 27.65337 1.000 79.30986  ? 243 THR   A CG2 1 
ATOM   1854 N N   . LEU   A 1  244 ? -0.66792  49.35988 29.83355 1.000 80.04800  ? 244 LEU   A N   1 
ATOM   1855 C CA  . LEU   A 1  244 ? -1.24450  50.63446 29.41325 1.000 84.40027  ? 244 LEU   A CA  1 
ATOM   1856 C C   . LEU   A 1  244 ? -0.30572  51.79211 29.71094 1.000 86.60063  ? 244 LEU   A C   1 
ATOM   1857 O O   . LEU   A 1  244 ? -0.23962  52.76782 28.94367 1.000 83.43456  ? 244 LEU   A O   1 
ATOM   1858 C CB  . LEU   A 1  244 ? -2.59644  50.84978 30.09435 1.000 91.28918  ? 244 LEU   A CB  1 
ATOM   1859 C CG  . LEU   A 1  244 ? -3.65802  49.81389 29.73512 1.000 83.80851  ? 244 LEU   A CG  1 
ATOM   1860 C CD1 . LEU   A 1  244 ? -4.97380  50.18088 30.37237 1.000 83.77980  ? 244 LEU   A CD1 1 
ATOM   1861 C CD2 . LEU   A 1  244 ? -3.79240  49.77153 28.21367 1.000 82.03904  ? 244 LEU   A CD2 1 
ATOM   1862 N N   . ASN   A 1  245 ? 0.41379   51.71374 30.83244 1.000 83.80867  ? 245 ASN   A N   1 
ATOM   1863 C CA  . ASN   A 1  245 ? 1.34915   52.78137 31.15831 1.000 85.13663  ? 245 ASN   A CA  1 
ATOM   1864 C C   . ASN   A 1  245 ? 2.47374   52.83016 30.13468 1.000 84.47678  ? 245 ASN   A C   1 
ATOM   1865 O O   . ASN   A 1  245 ? 2.83839   53.91458 29.65704 1.000 86.41709  ? 245 ASN   A O   1 
ATOM   1866 C CB  . ASN   A 1  245 ? 1.89135   52.59665 32.57787 1.000 86.58755  ? 245 ASN   A CB  1 
ATOM   1867 C CG  . ASN   A 1  245 ? 0.88202   52.99736 33.65374 1.000 94.43929  ? 245 ASN   A CG  1 
ATOM   1868 O OD1 . ASN   A 1  245 ? -0.19614  53.52789 33.35858 1.000 99.43109  ? 245 ASN   A OD1 1 
ATOM   1869 N ND2 . ASN   A 1  245 ? 1.23523   52.75098 34.90940 1.000 95.15482  ? 245 ASN   A ND2 1 
ATOM   1870 N N   . LEU   A 1  246 ? 2.99837   51.66078 29.75073 1.000 79.25411  ? 246 LEU   A N   1 
ATOM   1871 C CA  . LEU   A 1  246 ? 3.99534   51.61122 28.69138 1.000 81.92181  ? 246 LEU   A CA  1 
ATOM   1872 C C   . LEU   A 1  246 ? 3.47473   52.23568 27.39885 1.000 85.40245  ? 246 LEU   A C   1 
ATOM   1873 O O   . LEU   A 1  246 ? 4.17984   53.02506 26.75824 1.000 79.55553  ? 246 LEU   A O   1 
ATOM   1874 C CB  . LEU   A 1  246 ? 4.42540   50.17180 28.44881 1.000 74.94058  ? 246 LEU   A CB  1 
ATOM   1875 C CG  . LEU   A 1  246 ? 5.74800   50.16317 27.69123 1.000 82.21393  ? 246 LEU   A CG  1 
ATOM   1876 C CD1 . LEU   A 1  246 ? 6.84681   50.74148 28.57316 1.000 75.38499  ? 246 LEU   A CD1 1 
ATOM   1877 C CD2 . LEU   A 1  246 ? 6.07352   48.75779 27.24433 1.000 80.49450  ? 246 LEU   A CD2 1 
ATOM   1878 N N   . ALA   A 1  247 ? 2.23667   51.90082 27.00577 1.000 86.07124  ? 247 ALA   A N   1 
ATOM   1879 C CA  . ALA   A 1  247 ? 1.65214   52.48112 25.79753 1.000 85.07856  ? 247 ALA   A CA  1 
ATOM   1880 C C   . ALA   A 1  247 ? 1.54004   53.99327 25.90419 1.000 83.09134  ? 247 ALA   A C   1 
ATOM   1881 O O   . ALA   A 1  247 ? 1.76359   54.71456 24.92128 1.000 84.80244  ? 247 ALA   A O   1 
ATOM   1882 C CB  . ALA   A 1  247 ? 0.27754   51.87249 25.52315 1.000 82.42345  ? 247 ALA   A CB  1 
ATOM   1883 N N   . LYS   A 1  248 ? 1.19322   54.50003 27.08354 1.000 80.34560  ? 248 LYS   A N   1 
ATOM   1884 C CA  . LYS   A 1  248 ? 1.10353   55.94849 27.21125 1.000 86.05105  ? 248 LYS   A CA  1 
ATOM   1885 C C   . LYS   A 1  248 ? 2.48737   56.58034 27.17939 1.000 89.16260  ? 248 LYS   A C   1 
ATOM   1886 O O   . LYS   A 1  248 ? 2.67780   57.63084 26.55264 1.000 87.12255  ? 248 LYS   A O   1 
ATOM   1887 C CB  . LYS   A 1  248 ? 0.34187   56.34107 28.47928 1.000 84.34344  ? 248 LYS   A CB  1 
ATOM   1888 C CG  . LYS   A 1  248 ? 0.14368   57.84727 28.59908 1.000 101.78517 ? 248 LYS   A CG  1 
ATOM   1889 C CD  . LYS   A 1  248 ? -0.84514  58.25366 29.69280 1.000 106.80933 ? 248 LYS   A CD  1 
ATOM   1890 C CE  . LYS   A 1  248 ? -1.44521  59.62641 29.37738 1.000 103.33424 ? 248 LYS   A CE  1 
ATOM   1891 N NZ  . LYS   A 1  248 ? -2.92390  59.73403 29.61909 1.000 111.49444 ? 248 LYS   A NZ  1 
ATOM   1892 N N   . LEU   A 1  249 ? 3.47613   55.93690 27.81713 1.000 87.84809  ? 249 LEU   A N   1 
ATOM   1893 C CA  . LEU   A 1  249 ? 4.81822   56.51252 27.83781 1.000 85.37040  ? 249 LEU   A CA  1 
ATOM   1894 C C   . LEU   A 1  249 ? 5.40716   56.57963 26.43497 1.000 86.40784  ? 249 LEU   A C   1 
ATOM   1895 O O   . LEU   A 1  249 ? 6.09060   57.54984 26.09025 1.000 87.28715  ? 249 LEU   A O   1 
ATOM   1896 C CB  . LEU   A 1  249 ? 5.74814   55.73226 28.76697 1.000 83.67551  ? 249 LEU   A CB  1 
ATOM   1897 C CG  . LEU   A 1  249 ? 5.54527   55.93033 30.27275 1.000 85.12985  ? 249 LEU   A CG  1 
ATOM   1898 C CD1 . LEU   A 1  249 ? 5.47380   54.62727 31.05316 1.000 86.19497  ? 249 LEU   A CD1 1 
ATOM   1899 C CD2 . LEU   A 1  249 ? 6.60106   56.83470 30.84528 1.000 92.62588  ? 249 LEU   A CD2 1 
ATOM   1900 N N   . THR   A 1  250 ? 5.14473   55.57228 25.60726 1.000 84.14060  ? 250 THR   A N   1 
ATOM   1901 C CA  . THR   A 1  250 ? 5.64651   55.55251 24.23707 1.000 83.93622  ? 250 THR   A CA  1 
ATOM   1902 C C   . THR   A 1  250 ? 4.74173   56.27540 23.24474 1.000 90.54422  ? 250 THR   A C   1 
ATOM   1903 O O   . THR   A 1  250 ? 5.02537   56.24896 22.04163 1.000 94.49223  ? 250 THR   A O   1 
ATOM   1904 C CB  . THR   A 1  250 ? 5.82252   54.11732 23.75825 1.000 82.84511  ? 250 THR   A CB  1 
ATOM   1905 O OG1 . THR   A 1  250 ? 4.60631   53.40469 24.00314 1.000 84.50773  ? 250 THR   A OG1 1 
ATOM   1906 C CG2 . THR   A 1  250 ? 6.98454   53.43584 24.48197 1.000 82.51113  ? 250 THR   A CG2 1 
ATOM   1907 N N   . GLY   A 1  251 ? 3.66202   56.90664 23.69837 1.000 87.19635  ? 251 GLY   A N   1 
ATOM   1908 C CA  . GLY   A 1  251 ? 2.74801   57.51659 22.74833 1.000 86.79807  ? 251 GLY   A CA  1 
ATOM   1909 C C   . GLY   A 1  251 ? 1.97389   56.52363 21.91379 1.000 89.79243  ? 251 GLY   A C   1 
ATOM   1910 O O   . GLY   A 1  251 ? 1.54481   56.86025 20.80742 1.000 89.79509  ? 251 GLY   A O   1 
ATOM   1911 N N   . CYS   A 1  252 ? 1.78202   55.30260 22.42068 1.000 84.56640  ? 252 CYS   A N   1 
ATOM   1912 C CA  . CYS   A 1  252 ? 1.11861   54.22633 21.69532 1.000 90.13510  ? 252 CYS   A CA  1 
ATOM   1913 C C   . CYS   A 1  252 ? -0.27195  53.93160 22.22850 1.000 93.02941  ? 252 CYS   A C   1 
ATOM   1914 O O   . CYS   A 1  252 ? -0.84216  52.88457 21.90007 1.000 92.92824  ? 252 CYS   A O   1 
ATOM   1915 C CB  . CYS   A 1  252 ? 1.95614   52.95068 21.74842 1.000 84.60243  ? 252 CYS   A CB  1 
ATOM   1916 S SG  . CYS   A 1  252 ? 3.26717   52.90498 20.54425 1.000 85.68338  ? 252 CYS   A SG  1 
ATOM   1917 N N   . SER   A 1  253 ? -0.81873  54.80789 23.06324 1.000 93.22157  ? 253 SER   A N   1 
ATOM   1918 C CA  . SER   A 1  253 ? -2.19064  54.63209 23.51389 1.000 97.51841  ? 253 SER   A CA  1 
ATOM   1919 C C   . SER   A 1  253 ? -3.12421  54.63086 22.31015 1.000 96.57164  ? 253 SER   A C   1 
ATOM   1920 O O   . SER   A 1  253 ? -3.14883  55.58427 21.52587 1.000 93.49706  ? 253 SER   A O   1 
ATOM   1921 C CB  . SER   A 1  253 ? -2.56758  55.72891 24.50911 1.000 86.04633  ? 253 SER   A CB  1 
ATOM   1922 O OG  . SER   A 1  253 ? -1.81113  55.58560 25.70670 1.000 90.81927  ? 253 SER   A OG  1 
ATOM   1923 N N   . ARG   A 1  254 ? -3.82740  53.52008 22.12870 1.000 99.19075  ? 254 ARG   A N   1 
ATOM   1924 C CA  . ARG   A 1  254 ? -4.84291  53.38811 21.09338 1.000 107.45346 ? 254 ARG   A CA  1 
ATOM   1925 C C   . ARG   A 1  254 ? -6.10125  52.89243 21.80265 1.000 117.35410 ? 254 ARG   A C   1 
ATOM   1926 O O   . ARG   A 1  254 ? -6.22214  52.97170 23.03173 1.000 119.59308 ? 254 ARG   A O   1 
ATOM   1927 C CB  . ARG   A 1  254 ? -4.35594  52.46191 19.96669 1.000 106.39991 ? 254 ARG   A CB  1 
ATOM   1928 C CG  . ARG   A 1  254 ? -3.00888  52.85927 19.36905 1.000 101.78948 ? 254 ARG   A CG  1 
ATOM   1929 C CD  . ARG   A 1  254 ? -3.14848  54.12504 18.52530 1.000 100.97150 ? 254 ARG   A CD  1 
ATOM   1930 N NE  . ARG   A 1  254 ? -1.92995  54.44970 17.79154 1.000 103.59679 ? 254 ARG   A NE  1 
ATOM   1931 C CZ  . ARG   A 1  254 ? -0.94533  55.20745 18.26092 1.000 99.30154  ? 254 ARG   A CZ  1 
ATOM   1932 N NH1 . ARG   A 1  254 ? -0.98431  55.71894 19.48168 1.000 93.03089  ? 254 ARG   A NH1 1 
ATOM   1933 N NH2 . ARG   A 1  254 ? 0.10292   55.46351 17.48352 1.000 98.72525  ? 254 ARG   A NH2 1 
ATOM   1934 N N   . GLU   A 1  255 ? -7.06567  52.38614 21.03381 1.000 118.43933 ? 255 GLU   A N   1 
ATOM   1935 C CA  . GLU   A 1  255 ? -8.19779  51.66530 21.61045 1.000 118.49420 ? 255 GLU   A CA  1 
ATOM   1936 C C   . GLU   A 1  255 ? -8.34006  50.24827 21.08012 1.000 116.66965 ? 255 GLU   A C   1 
ATOM   1937 O O   . GLU   A 1  255 ? -8.65176  49.34079 21.85426 1.000 118.78686 ? 255 GLU   A O   1 
ATOM   1938 C CB  . GLU   A 1  255 ? -9.51142  52.41966 21.38137 1.000 121.24541 ? 255 GLU   A CB  1 
ATOM   1939 C CG  . GLU   A 1  255 ? -10.74090 51.56975 21.70374 1.000 126.83014 ? 255 GLU   A CG  1 
ATOM   1940 C CD  . GLU   A 1  255 ? -11.94320 52.38227 22.15624 1.000 134.40700 ? 255 GLU   A CD  1 
ATOM   1941 O OE1 . GLU   A 1  255 ? -12.45332 53.20143 21.35945 1.000 134.31811 ? 255 GLU   A OE1 1 
ATOM   1942 O OE2 . GLU   A 1  255 ? -12.38550 52.18910 23.31168 1.000 139.10340 ? 255 GLU   A OE2 1 
ATOM   1943 N N   . ASN   A 1  256 ? -8.14355  50.03047 19.77769 1.000 120.06487 ? 256 ASN   A N   1 
ATOM   1944 C CA  . ASN   A 1  256 ? -7.95942  48.67538 19.27363 1.000 114.96068 ? 256 ASN   A CA  1 
ATOM   1945 C C   . ASN   A 1  256 ? -6.76908  48.06975 20.00185 1.000 113.91752 ? 256 ASN   A C   1 
ATOM   1946 O O   . ASN   A 1  256 ? -5.62526  48.48893 19.78625 1.000 112.57014 ? 256 ASN   A O   1 
ATOM   1947 C CB  . ASN   A 1  256 ? -7.73882  48.66335 17.75571 1.000 118.96377 ? 256 ASN   A CB  1 
ATOM   1948 C CG  . ASN   A 1  256 ? -8.11601  47.33696 17.11901 1.000 120.01461 ? 256 ASN   A CG  1 
ATOM   1949 O OD1 . ASN   A 1  256 ? -7.56093  46.29096 17.46120 1.000 120.58774 ? 256 ASN   A OD1 1 
ATOM   1950 N ND2 . ASN   A 1  256 ? -9.06777  47.37952 16.18199 1.000 132.24764 ? 256 ASN   A ND2 1 
ATOM   1951 N N   . GLU   A 1  257 ? -7.03828  47.11367 20.89493 1.000 106.01007 ? 257 GLU   A N   1 
ATOM   1952 C CA  . GLU   A 1  257 ? -5.97491  46.51119 21.69237 1.000 109.13074 ? 257 GLU   A CA  1 
ATOM   1953 C C   . GLU   A 1  257 ? -4.82020  46.02564 20.83726 1.000 104.94231 ? 257 GLU   A C   1 
ATOM   1954 O O   . GLU   A 1  257 ? -3.67658  45.97109 21.30307 1.000 97.42970  ? 257 GLU   A O   1 
ATOM   1955 C CB  . GLU   A 1  257 ? -6.52163  45.33750 22.49480 1.000 112.21432 ? 257 GLU   A CB  1 
ATOM   1956 C CG  . GLU   A 1  257 ? -7.18619  45.73867 23.77222 1.000 107.68563 ? 257 GLU   A CG  1 
ATOM   1957 C CD  . GLU   A 1  257 ? -6.84713  44.79274 24.88658 1.000 95.74170  ? 257 GLU   A CD  1 
ATOM   1958 O OE1 . GLU   A 1  257 ? -6.45258  43.63123 24.59472 1.000 89.88190  ? 257 GLU   A OE1 1 
ATOM   1959 O OE2 . GLU   A 1  257 ? -6.96815  45.22798 26.05024 1.000 94.21167  ? 257 GLU   A OE2 1 
ATOM   1960 N N   . THR   A 1  258 ? -5.09989  45.65070 19.59419 1.000 111.30115 ? 258 THR   A N   1 
ATOM   1961 C CA  . THR   A 1  258 ? -4.03448  45.19566 18.71920 1.000 107.13016 ? 258 THR   A CA  1 
ATOM   1962 C C   . THR   A 1  258 ? -3.26680  46.36910 18.11755 1.000 104.11120 ? 258 THR   A C   1 
ATOM   1963 O O   . THR   A 1  258 ? -2.03930  46.29555 17.97705 1.000 99.03640  ? 258 THR   A O   1 
ATOM   1964 C CB  . THR   A 1  258 ? -4.61460  44.28971 17.63798 1.000 111.10867 ? 258 THR   A CB  1 
ATOM   1965 O OG1 . THR   A 1  258 ? -5.42930  43.28683 18.26045 1.000 108.74538 ? 258 THR   A OG1 1 
ATOM   1966 C CG2 . THR   A 1  258 ? -3.49839  43.61282 16.86946 1.000 111.20291 ? 258 THR   A CG2 1 
ATOM   1967 N N   . GLU   A 1  259 ? -3.96079  47.46890 17.78989 1.000 108.93524 ? 259 GLU   A N   1 
ATOM   1968 C CA  . GLU   A 1  259 ? -3.30026  48.64908 17.23675 1.000 107.64811 ? 259 GLU   A CA  1 
ATOM   1969 C C   . GLU   A 1  259 ? -2.29028  49.26441 18.20637 1.000 103.68649 ? 259 GLU   A C   1 
ATOM   1970 O O   . GLU   A 1  259 ? -1.48970  50.10942 17.79467 1.000 102.60200 ? 259 GLU   A O   1 
ATOM   1971 C CB  . GLU   A 1  259 ? -4.35457  49.68382 16.81305 1.000 116.58844 ? 259 GLU   A CB  1 
ATOM   1972 C CG  . GLU   A 1  259 ? -4.95173  49.43958 15.41067 1.000 124.68753 ? 259 GLU   A CG  1 
ATOM   1973 C CD  . GLU   A 1  259 ? -6.08741  50.40377 15.04785 1.000 134.01418 ? 259 GLU   A CD  1 
ATOM   1974 O OE1 . GLU   A 1  259 ? -6.12411  51.52768 15.59156 1.000 132.80293 ? 259 GLU   A OE1 1 
ATOM   1975 O OE2 . GLU   A 1  259 ? -6.94668  50.03518 14.21241 1.000 139.82967 ? 259 GLU   A OE2 1 
ATOM   1976 N N   . ILE   A 1  260 ? -2.30328  48.85928 19.47192 1.000 92.18164  ? 260 ILE   A N   1 
ATOM   1977 C CA  . ILE   A 1  260 ? -1.25775  49.25195 20.40785 1.000 95.08702  ? 260 ILE   A CA  1 
ATOM   1978 C C   . ILE   A 1  260 ? 0.00225   48.41808 20.20154 1.000 90.39571  ? 260 ILE   A C   1 
ATOM   1979 O O   . ILE   A 1  260 ? 1.11850   48.95316 20.16467 1.000 83.82695  ? 260 ILE   A O   1 
ATOM   1980 C CB  . ILE   A 1  260 ? -1.78331  49.13095 21.84942 1.000 93.38309  ? 260 ILE   A CB  1 
ATOM   1981 C CG1 . ILE   A 1  260 ? -2.92429  50.11353 22.08484 1.000 98.38598  ? 260 ILE   A CG1 1 
ATOM   1982 C CG2 . ILE   A 1  260 ? -0.66092  49.31364 22.85599 1.000 84.30997  ? 260 ILE   A CG2 1 
ATOM   1983 C CD1 . ILE   A 1  260 ? -3.43264  50.10382 23.49381 1.000 98.43179  ? 260 ILE   A CD1 1 
ATOM   1984 N N   . ILE   A 1  261 ? -0.15231  47.09727 20.07446 1.000 85.92570  ? 261 ILE   A N   1 
ATOM   1985 C CA  . ILE   A 1  261 ? 1.00592   46.23609 19.85378 1.000 82.95921  ? 261 ILE   A CA  1 
ATOM   1986 C C   . ILE   A 1  261 ? 1.70060   46.61441 18.55805 1.000 84.19043  ? 261 ILE   A C   1 
ATOM   1987 O O   . ILE   A 1  261 ? 2.93182   46.69909 18.50342 1.000 86.52265  ? 261 ILE   A O   1 
ATOM   1988 C CB  . ILE   A 1  261 ? 0.60002   44.75307 19.85578 1.000 80.73712  ? 261 ILE   A CB  1 
ATOM   1989 C CG1 . ILE   A 1  261 ? -0.09499  44.38857 21.16399 1.000 79.13818  ? 261 ILE   A CG1 1 
ATOM   1990 C CG2 . ILE   A 1  261 ? 1.81776   43.87574 19.69254 1.000 76.10891  ? 261 ILE   A CG2 1 
ATOM   1991 C CD1 . ILE   A 1  261 ? 0.63055   44.85538 22.39796 1.000 70.98954  ? 261 ILE   A CD1 1 
ATOM   1992 N N   . LYS   A 1  262 ? 0.92123   46.84091 17.49442 1.000 83.14040  ? 262 LYS   A N   1 
ATOM   1993 C CA  . LYS   A 1  262 ? 1.49985   47.32887 16.24789 1.000 81.61094  ? 262 LYS   A CA  1 
ATOM   1994 C C   . LYS   A 1  262 ? 2.34553   48.56574 16.50762 1.000 85.24199  ? 262 LYS   A C   1 
ATOM   1995 O O   . LYS   A 1  262 ? 3.50272   48.64316 16.07413 1.000 79.57617  ? 262 LYS   A O   1 
ATOM   1996 C CB  . LYS   A 1  262 ? 0.40184   47.62218 15.22358 1.000 80.01077  ? 262 LYS   A CB  1 
ATOM   1997 C CG  . LYS   A 1  262 ? 0.88145   48.38223 13.98318 1.000 88.30179  ? 262 LYS   A CG  1 
ATOM   1998 C CD  . LYS   A 1  262 ? 0.00623   49.62198 13.62759 1.000 98.04984  ? 262 LYS   A CD  1 
ATOM   1999 C CE  . LYS   A 1  262 ? 0.00076   50.77870 14.66107 1.000 99.88505  ? 262 LYS   A CE  1 
ATOM   2000 N NZ  . LYS   A 1  262 ? 1.12811   51.77318 14.56868 1.000 92.08622  ? 262 LYS   A NZ  1 
ATOM   2001 N N   . CYS   A 1  263 ? 1.78026   49.53644 17.23995 1.000 88.41647  ? 263 CYS   A N   1 
ATOM   2002 C CA  . CYS   A 1  263 ? 2.50084   50.76471 17.56989 1.000 82.13222  ? 263 CYS   A CA  1 
ATOM   2003 C C   . CYS   A 1  263 ? 3.76178   50.46679 18.37403 1.000 86.60945  ? 263 CYS   A C   1 
ATOM   2004 O O   . CYS   A 1  263 ? 4.83161   51.01927 18.09812 1.000 85.43702  ? 263 CYS   A O   1 
ATOM   2005 C CB  . CYS   A 1  263 ? 1.58933   51.72306 18.34120 1.000 87.06403  ? 263 CYS   A CB  1 
ATOM   2006 S SG  . CYS   A 1  263 ? 2.32960   53.34083 18.79571 1.000 93.57320  ? 263 CYS   A SG  1 
ATOM   2007 N N   . LEU   A 1  264 ? 3.65905   49.60027 19.38381 1.000 83.14457  ? 264 LEU   A N   1 
ATOM   2008 C CA  . LEU   A 1  264 ? 4.85108   49.28932 20.15969 1.000 82.31069  ? 264 LEU   A CA  1 
ATOM   2009 C C   . LEU   A 1  264 ? 5.86186   48.48662 19.36217 1.000 80.77419  ? 264 LEU   A C   1 
ATOM   2010 O O   . LEU   A 1  264 ? 7.02123   48.39626 19.77074 1.000 79.88571  ? 264 LEU   A O   1 
ATOM   2011 C CB  . LEU   A 1  264 ? 4.49916   48.51966 21.42362 1.000 79.68720  ? 264 LEU   A CB  1 
ATOM   2012 C CG  . LEU   A 1  264 ? 3.84421   49.35057 22.51236 1.000 86.91379  ? 264 LEU   A CG  1 
ATOM   2013 C CD1 . LEU   A 1  264 ? 3.18888   48.38641 23.46992 1.000 77.37583  ? 264 LEU   A CD1 1 
ATOM   2014 C CD2 . LEU   A 1  264 ? 4.86608   50.24364 23.20896 1.000 83.20992  ? 264 LEU   A CD2 1 
ATOM   2015 N N   . ARG   A 1  265 ? 5.44689   47.89082 18.24969 1.000 82.41800  ? 265 ARG   A N   1 
ATOM   2016 C CA  . ARG   A 1  265 ? 6.34593   47.12392 17.40255 1.000 75.85427  ? 265 ARG   A CA  1 
ATOM   2017 C C   . ARG   A 1  265 ? 7.17841   48.00012 16.48375 1.000 83.47334  ? 265 ARG   A C   1 
ATOM   2018 O O   . ARG   A 1  265 ? 8.14613   47.50892 15.89988 1.000 83.13351  ? 265 ARG   A O   1 
ATOM   2019 C CB  . ARG   A 1  265 ? 5.54476   46.13711 16.55898 1.000 78.55533  ? 265 ARG   A CB  1 
ATOM   2020 C CG  . ARG   A 1  265 ? 5.12611   44.87004 17.26266 1.000 71.51833  ? 265 ARG   A CG  1 
ATOM   2021 C CD  . ARG   A 1  265 ? 4.83244   43.81974 16.21685 1.000 74.20531  ? 265 ARG   A CD  1 
ATOM   2022 N NE  . ARG   A 1  265 ? 4.41217   42.56859 16.81985 1.000 82.56941  ? 265 ARG   A NE  1 
ATOM   2023 C CZ  . ARG   A 1  265 ? 3.14654   42.24592 17.04073 1.000 88.99228  ? 265 ARG   A CZ  1 
ATOM   2024 N NH1 . ARG   A 1  265 ? 2.15154   43.02476 16.62030 1.000 85.39693  ? 265 ARG   A NH1 1 
ATOM   2025 N NH2 . ARG   A 1  265 ? 2.87380   41.13186 17.71965 1.000 75.79462  ? 265 ARG   A NH2 1 
ATOM   2026 N N   . ASN   A 1  266 ? 6.81670   49.26871 16.32569 1.000 80.97585  ? 266 ASN   A N   1 
ATOM   2027 C CA  . ASN   A 1  266 ? 7.60305   50.20259 15.53610 1.000 84.58616  ? 266 ASN   A CA  1 
ATOM   2028 C C   . ASN   A 1  266 ? 8.62656   50.95934 16.37133 1.000 83.04589  ? 266 ASN   A C   1 
ATOM   2029 O O   . ASN   A 1  266 ? 9.37569   51.76587 15.82281 1.000 93.28059  ? 266 ASN   A O   1 
ATOM   2030 C CB  . ASN   A 1  266 ? 6.68962   51.20709 14.82069 1.000 86.68925  ? 266 ASN   A CB  1 
ATOM   2031 C CG  . ASN   A 1  266 ? 6.08654   50.63893 13.55411 1.000 99.58274  ? 266 ASN   A CG  1 
ATOM   2032 O OD1 . ASN   A 1  266 ? 6.61589   49.68233 12.97860 1.000 101.60191 ? 266 ASN   A OD1 1 
ATOM   2033 N ND2 . ASN   A 1  266 ? 4.99098   51.24075 13.09285 1.000 103.34638 ? 266 ASN   A ND2 1 
ATOM   2034 N N   . LYS   A 1  267 ? 8.68475   50.72681 17.67369 1.000 83.91448  ? 267 LYS   A N   1 
ATOM   2035 C CA  . LYS   A 1  267 ? 9.65183   51.40673 18.52219 1.000 83.68331  ? 267 LYS   A CA  1 
ATOM   2036 C C   . LYS   A 1  267 ? 10.96007  50.62557 18.57372 1.000 82.77740  ? 267 LYS   A C   1 
ATOM   2037 O O   . LYS   A 1  267 ? 10.95937  49.38975 18.59842 1.000 85.83299  ? 267 LYS   A O   1 
ATOM   2038 C CB  . LYS   A 1  267 ? 9.09183   51.57831 19.93446 1.000 83.67195  ? 267 LYS   A CB  1 
ATOM   2039 C CG  . LYS   A 1  267 ? 7.69114   52.18805 19.98517 1.000 88.22701  ? 267 LYS   A CG  1 
ATOM   2040 C CD  . LYS   A 1  267 ? 7.74605   53.71335 20.08317 1.000 85.54639  ? 267 LYS   A CD  1 
ATOM   2041 C CE  . LYS   A 1  267 ? 6.40113   54.35747 19.77681 1.000 89.78061  ? 267 LYS   A CE  1 
ATOM   2042 N NZ  . LYS   A 1  267 ? 6.10167   54.44423 18.31659 1.000 96.64052  ? 267 LYS   A NZ  1 
ATOM   2043 N N   . ASP   A 1  268 ? 12.07778  51.35396 18.58977 1.000 84.52793  ? 268 ASP   A N   1 
ATOM   2044 C CA  . ASP   A 1  268 ? 13.37569  50.72984 18.81019 1.000 83.66639  ? 268 ASP   A CA  1 
ATOM   2045 C C   . ASP   A 1  268 ? 13.41385  50.06102 20.18472 1.000 78.70050  ? 268 ASP   A C   1 
ATOM   2046 O O   . ASP   A 1  268 ? 12.82834  50.56445 21.14750 1.000 77.01855  ? 268 ASP   A O   1 
ATOM   2047 C CB  . ASP   A 1  268 ? 14.49503  51.76438 18.72594 1.000 83.69509  ? 268 ASP   A CB  1 
ATOM   2048 C CG  . ASP   A 1  268 ? 14.42951  52.59006 17.46036 1.000 98.05062  ? 268 ASP   A CG  1 
ATOM   2049 O OD1 . ASP   A 1  268 ? 15.16452  53.60142 17.36593 1.000 101.15197 ? 268 ASP   A OD1 1 
ATOM   2050 O OD2 . ASP   A 1  268 ? 13.64358  52.22767 16.55739 1.000 103.04391 ? 268 ASP   A OD2 1 
ATOM   2051 N N   . PRO   A 1  269 ? 14.11957  48.94317 20.31251 1.000 72.95124  ? 269 PRO   A N   1 
ATOM   2052 C CA  . PRO   A 1  269 ? 14.24766  48.31522 21.63985 1.000 78.24968  ? 269 PRO   A CA  1 
ATOM   2053 C C   . PRO   A 1  269 ? 14.64714  49.29934 22.73606 1.000 81.47937  ? 269 PRO   A C   1 
ATOM   2054 O O   . PRO   A 1  269 ? 14.21061  49.15921 23.88933 1.000 75.60546  ? 269 PRO   A O   1 
ATOM   2055 C CB  . PRO   A 1  269 ? 15.32030  47.24066 21.40924 1.000 76.61951  ? 269 PRO   A CB  1 
ATOM   2056 C CG  . PRO   A 1  269 ? 15.24548  46.93886 19.92073 1.000 75.17965  ? 269 PRO   A CG  1 
ATOM   2057 C CD  . PRO   A 1  269 ? 14.85417  48.21911 19.25918 1.000 70.98082  ? 269 PRO   A CD  1 
ATOM   2058 N N   . GLN   A 1  270 ? 15.42205  50.33011 22.38908 1.000 79.91400  ? 270 GLN   A N   1 
ATOM   2059 C CA  . GLN   A 1  270 ? 15.94506  51.23831 23.39900 1.000 79.94287  ? 270 GLN   A CA  1 
ATOM   2060 C C   . GLN   A 1  270 ? 14.83982  52.09843 24.00783 1.000 80.95714  ? 270 GLN   A C   1 
ATOM   2061 O O   . GLN   A 1  270 ? 14.82967  52.34164 25.22253 1.000 78.92713  ? 270 GLN   A O   1 
ATOM   2062 C CB  . GLN   A 1  270 ? 17.04529  52.09564 22.77935 1.000 81.91114  ? 270 GLN   A CB  1 
ATOM   2063 C CG  . GLN   A 1  270 ? 18.04584  52.63739 23.78359 1.000 90.86777  ? 270 GLN   A CG  1 
ATOM   2064 C CD  . GLN   A 1  270 ? 18.30191  51.69711 24.96498 1.000 95.29689  ? 270 GLN   A CD  1 
ATOM   2065 O OE1 . GLN   A 1  270 ? 18.10679  52.08028 26.12087 1.000 93.61220  ? 270 GLN   A OE1 1 
ATOM   2066 N NE2 . GLN   A 1  270 ? 18.78311  50.47814 24.68076 1.000 90.48038  ? 270 GLN   A NE2 1 
ATOM   2067 N N   . GLU   A 1  271 ? 13.88325  52.54219 23.18998 1.000 77.17473  ? 271 GLU   A N   1 
ATOM   2068 C CA  . GLU   A 1  271 ? 12.77126  53.32622 23.72232 1.000 80.43328  ? 271 GLU   A CA  1 
ATOM   2069 C C   . GLU   A 1  271 ? 11.93932  52.50444 24.69630 1.000 82.25002  ? 271 GLU   A C   1 
ATOM   2070 O O   . GLU   A 1  271 ? 11.47867  53.01383 25.72556 1.000 83.85437  ? 271 GLU   A O   1 
ATOM   2071 C CB  . GLU   A 1  271 ? 11.89258  53.84437 22.58238 1.000 82.23268  ? 271 GLU   A CB  1 
ATOM   2072 C CG  . GLU   A 1  271 ? 10.77147  54.74453 23.06037 1.000 89.09498  ? 271 GLU   A CG  1 
ATOM   2073 C CD  . GLU   A 1  271 ? 10.09864  55.51007 21.93408 1.000 95.14476  ? 271 GLU   A CD  1 
ATOM   2074 O OE1 . GLU   A 1  271 ? 10.68948  55.60586 20.83221 1.000 96.49560  ? 271 GLU   A OE1 1 
ATOM   2075 O OE2 . GLU   A 1  271 ? 8.99634   56.05498 22.17193 1.000 94.84237  ? 271 GLU   A OE2 1 
ATOM   2076 N N   . ILE   A 1  272 ? 11.74128  51.22418 24.38738 1.000 82.48105  ? 272 ILE   A N   1 
ATOM   2077 C CA  . ILE   A 1  272 ? 10.93483  50.37016 25.24689 1.000 78.75521  ? 272 ILE   A CA  1 
ATOM   2078 C C   . ILE   A 1  272 ? 11.62741  50.13026 26.57969 1.000 80.12403  ? 272 ILE   A C   1 
ATOM   2079 O O   . ILE   A 1  272 ? 10.97896  50.13835 27.63882 1.000 77.95190  ? 272 ILE   A O   1 
ATOM   2080 C CB  . ILE   A 1  272 ? 10.60601  49.06664 24.50434 1.000 75.92705  ? 272 ILE   A CB  1 
ATOM   2081 C CG1 . ILE   A 1  272 ? 9.78941   49.42189 23.25757 1.000 79.00503  ? 272 ILE   A CG1 1 
ATOM   2082 C CG2 . ILE   A 1  272 ? 9.92932   48.06790 25.42587 1.000 75.28713  ? 272 ILE   A CG2 1 
ATOM   2083 C CD1 . ILE   A 1  272 ? 9.01396   48.30171 22.64664 1.000 77.43544  ? 272 ILE   A CD1 1 
ATOM   2084 N N   . LEU   A 1  273 ? 12.95480  49.94387 26.55974 1.000 76.91640  ? 273 LEU   A N   1 
ATOM   2085 C CA  . LEU   A 1  273 ? 13.68056  49.72049 27.81100 1.000 74.88596  ? 273 LEU   A CA  1 
ATOM   2086 C C   . LEU   A 1  273 ? 13.69759  50.97414 28.68201 1.000 78.86578  ? 273 LEU   A C   1 
ATOM   2087 O O   . LEU   A 1  273 ? 13.58447  50.87603 29.91434 1.000 74.55462  ? 273 LEU   A O   1 
ATOM   2088 C CB  . LEU   A 1  273 ? 15.10166  49.25100 27.52433 1.000 69.77600  ? 273 LEU   A CB  1 
ATOM   2089 C CG  . LEU   A 1  273 ? 15.26693  47.82100 26.99880 1.000 68.91749  ? 273 LEU   A CG  1 
ATOM   2090 C CD1 . LEU   A 1  273 ? 16.64555  47.64584 26.37604 1.000 72.03313  ? 273 LEU   A CD1 1 
ATOM   2091 C CD2 . LEU   A 1  273 ? 15.04598  46.77511 28.10496 1.000 64.23830  ? 273 LEU   A CD2 1 
ATOM   2092 N N   . LEU   A 1  274 ? 13.84279  52.15390 28.05528 1.000 73.16260  ? 274 LEU   A N   1 
ATOM   2093 C CA  . LEU   A 1  274 ? 13.75489  53.42613 28.77033 1.000 81.50353  ? 274 LEU   A CA  1 
ATOM   2094 C C   . LEU   A 1  274 ? 12.52757  53.48881 29.66339 1.000 85.40402  ? 274 LEU   A C   1 
ATOM   2095 O O   . LEU   A 1  274 ? 12.59714  53.97058 30.80000 1.000 86.33312  ? 274 LEU   A O   1 
ATOM   2096 C CB  . LEU   A 1  274 ? 13.70220  54.59194 27.77460 1.000 83.49058  ? 274 LEU   A CB  1 
ATOM   2097 C CG  . LEU   A 1  274 ? 13.90177  56.05774 28.22620 1.000 96.64298  ? 274 LEU   A CG  1 
ATOM   2098 C CD1 . LEU   A 1  274 ? 14.48470  56.94361 27.10533 1.000 79.64930  ? 274 LEU   A CD1 1 
ATOM   2099 C CD2 . LEU   A 1  274 ? 12.61958  56.70400 28.76376 1.000 96.37824  ? 274 LEU   A CD2 1 
ATOM   2100 N N   . ASN   A 1  275 ? 11.38241  53.05061 29.14749 1.000 85.65531  ? 275 ASN   A N   1 
ATOM   2101 C CA  . ASN   A 1  275 ? 10.10384  53.31779 29.78850 1.000 84.24554  ? 275 ASN   A CA  1 
ATOM   2102 C C   . ASN   A 1  275 ? 9.64399   52.19980 30.71575 1.000 80.69859  ? 275 ASN   A C   1 
ATOM   2103 O O   . ASN   A 1  275 ? 8.72477   52.41717 31.51266 1.000 83.37065  ? 275 ASN   A O   1 
ATOM   2104 C CB  . ASN   A 1  275 ? 9.06109   53.60150 28.70630 1.000 79.42584  ? 275 ASN   A CB  1 
ATOM   2105 C CG  . ASN   A 1  275 ? 9.32489   54.92265 27.98259 1.000 87.14365  ? 275 ASN   A CG  1 
ATOM   2106 O OD1 . ASN   A 1  275 ? 9.15223   55.99270 28.56191 1.000 84.78162  ? 275 ASN   A OD1 1 
ATOM   2107 N ND2 . ASN   A 1  275 ? 9.74500   54.85113 26.71724 1.000 86.26255  ? 275 ASN   A ND2 1 
ATOM   2108 N N   . GLU   A 1  276 ? 10.28153  51.02885 30.64747 1.000 74.79832  ? 276 GLU   A N   1 
ATOM   2109 C CA  . GLU   A 1  276 ? 9.95074   49.92066 31.53965 1.000 77.04961  ? 276 GLU   A CA  1 
ATOM   2110 C C   . GLU   A 1  276 ? 10.06298  50.30056 33.01461 1.000 78.87774  ? 276 GLU   A C   1 
ATOM   2111 O O   . GLU   A 1  276 ? 9.35395   49.73333 33.85492 1.000 82.89702  ? 276 GLU   A O   1 
ATOM   2112 C CB  . GLU   A 1  276 ? 10.87827  48.74257 31.26239 1.000 74.53782  ? 276 GLU   A CB  1 
ATOM   2113 C CG  . GLU   A 1  276 ? 10.56780  47.90233 30.04090 1.000 72.73286  ? 276 GLU   A CG  1 
ATOM   2114 C CD  . GLU   A 1  276 ? 11.44838  46.65052 30.01420 1.000 78.55367  ? 276 GLU   A CD  1 
ATOM   2115 O OE1 . GLU   A 1  276 ? 12.10318  46.36642 31.04642 1.000 76.85624  ? 276 GLU   A OE1 1 
ATOM   2116 O OE2 . GLU   A 1  276 ? 11.50467  45.95766 28.97404 1.000 75.11412  ? 276 GLU   A OE2 1 
ATOM   2117 N N   . ALA   A 1  277 ? 10.95646  51.23286 33.35633 1.000 80.02971  ? 277 ALA   A N   1 
ATOM   2118 C CA  . ALA   A 1  277 ? 11.20055  51.53388 34.76540 1.000 84.62297  ? 277 ALA   A CA  1 
ATOM   2119 C C   . ALA   A 1  277 ? 10.00491  52.22742 35.40815 1.000 93.90334  ? 277 ALA   A C   1 
ATOM   2120 O O   . ALA   A 1  277 ? 9.65827   51.94488 36.56463 1.000 91.95232  ? 277 ALA   A O   1 
ATOM   2121 C CB  . ALA   A 1  277 ? 12.45443  52.39390 34.90731 1.000 88.90353  ? 277 ALA   A CB  1 
ATOM   2122 N N   . PHE   A 1  278 ? 9.35405   53.12442 34.67246 1.000 90.29512  ? 278 PHE   A N   1 
ATOM   2123 C CA  . PHE   A 1  278 ? 8.28604   53.93532 35.22812 1.000 93.64796  ? 278 PHE   A CA  1 
ATOM   2124 C C   . PHE   A 1  278 ? 6.89185   53.35692 35.01375 1.000 97.31807  ? 278 PHE   A C   1 
ATOM   2125 O O   . PHE   A 1  278 ? 5.91445   54.06927 35.26191 1.000 96.50084  ? 278 PHE   A O   1 
ATOM   2126 C CB  . PHE   A 1  278 ? 8.31754   55.34837 34.63995 1.000 101.04043 ? 278 PHE   A CB  1 
ATOM   2127 C CG  . PHE   A 1  278 ? 9.66893   55.79142 34.17247 1.000 99.85508  ? 278 PHE   A CG  1 
ATOM   2128 C CD1 . PHE   A 1  278 ? 9.94226   55.91026 32.81986 1.000 101.34782 ? 278 PHE   A CD1 1 
ATOM   2129 C CD2 . PHE   A 1  278 ? 10.66576  56.10198 35.08522 1.000 106.07415 ? 278 PHE   A CD2 1 
ATOM   2130 C CE1 . PHE   A 1  278 ? 11.19442  56.33178 32.38285 1.000 106.86969 ? 278 PHE   A CE1 1 
ATOM   2131 C CE2 . PHE   A 1  278 ? 11.91760  56.52133 34.65878 1.000 109.47723 ? 278 PHE   A CE2 1 
ATOM   2132 C CZ  . PHE   A 1  278 ? 12.18240  56.63863 33.30580 1.000 110.56083 ? 278 PHE   A CZ  1 
ATOM   2133 N N   . VAL   A 1  279 ? 6.75256   52.11108 34.54618 1.000 93.64194  ? 279 VAL   A N   1 
ATOM   2134 C CA  . VAL   A 1  279 ? 5.39075   51.58469 34.49457 1.000 92.63032  ? 279 VAL   A CA  1 
ATOM   2135 C C   . VAL   A 1  279 ? 4.93406   51.20779 35.89780 1.000 98.32436  ? 279 VAL   A C   1 
ATOM   2136 O O   . VAL   A 1  279 ? 3.74051   51.26386 36.20600 1.000 90.25135  ? 279 VAL   A O   1 
ATOM   2137 C CB  . VAL   A 1  279 ? 5.26025   50.40979 33.50264 1.000 88.67623  ? 279 VAL   A CB  1 
ATOM   2138 C CG1 . VAL   A 1  279 ? 5.83621   50.79929 32.14077 1.000 88.12745  ? 279 VAL   A CG1 1 
ATOM   2139 C CG2 . VAL   A 1  279 ? 5.90337   49.13040 34.04404 1.000 81.48231  ? 279 VAL   A CG2 1 
ATOM   2140 N N   . VAL   A 1  280 ? 5.86404   50.85491 36.77451 1.000 114.13236 ? 280 VAL   A N   1 
ATOM   2141 C CA  . VAL   A 1  280 ? 5.53527   50.64918 38.18619 1.000 113.49724 ? 280 VAL   A CA  1 
ATOM   2142 C C   . VAL   A 1  280 ? 5.45311   52.01357 38.86875 1.000 121.01223 ? 280 VAL   A C   1 
ATOM   2143 O O   . VAL   A 1  280 ? 6.35277   52.85365 38.67708 1.000 118.64751 ? 280 VAL   A O   1 
ATOM   2144 C CB  . VAL   A 1  280 ? 6.57528   49.74435 38.85514 1.000 115.84826 ? 280 VAL   A CB  1 
ATOM   2145 C CG1 . VAL   A 1  280 ? 7.98945   50.33980 38.75435 1.000 111.46250 ? 280 VAL   A CG1 1 
ATOM   2146 C CG2 . VAL   A 1  280 ? 6.20525   49.45130 40.30171 1.000 112.19409 ? 280 VAL   A CG2 1 
ATOM   2147 N N   . PRO   A 1  281 ? 4.38899   52.29692 39.62523 1.000 119.36134 ? 281 PRO   A N   1 
ATOM   2148 C CA  . PRO   A 1  281 ? 4.30141   53.62810 40.24696 1.000 118.85616 ? 281 PRO   A CA  1 
ATOM   2149 C C   . PRO   A 1  281 ? 5.30453   53.80569 41.36739 1.000 127.12961 ? 281 PRO   A C   1 
ATOM   2150 O O   . PRO   A 1  281 ? 5.91788   54.87360 41.49081 1.000 121.11884 ? 281 PRO   A O   1 
ATOM   2151 C CB  . PRO   A 1  281 ? 2.85342   53.69509 40.75180 1.000 119.58820 ? 281 PRO   A CB  1 
ATOM   2152 C CG  . PRO   A 1  281 ? 2.34083   52.26859 40.75749 1.000 120.22720 ? 281 PRO   A CG  1 
ATOM   2153 C CD  . PRO   A 1  281 ? 3.36201   51.36679 40.12700 1.000 118.84178 ? 281 PRO   A CD  1 
ATOM   2154 N N   . TYR   A 1  282 ? 5.49266   52.77532 42.18662 1.000 140.04080 ? 282 TYR   A N   1 
ATOM   2155 C CA  . TYR   A 1  282 ? 6.49329   52.76891 43.24607 1.000 134.30588 ? 282 TYR   A CA  1 
ATOM   2156 C C   . TYR   A 1  282 ? 7.32680   51.50846 43.08509 1.000 127.03641 ? 282 TYR   A C   1 
ATOM   2157 O O   . TYR   A 1  282 ? 6.85398   50.40563 43.38025 1.000 129.67185 ? 282 TYR   A O   1 
ATOM   2158 C CB  . TYR   A 1  282 ? 5.84332   52.81857 44.62931 1.000 138.05807 ? 282 TYR   A CB  1 
ATOM   2159 C CG  . TYR   A 1  282 ? 5.24708   54.16257 44.99121 1.000 143.09203 ? 282 TYR   A CG  1 
ATOM   2160 C CD1 . TYR   A 1  282 ? 5.95875   55.34022 44.77860 1.000 147.69551 ? 282 TYR   A CD1 1 
ATOM   2161 C CD2 . TYR   A 1  282 ? 3.98365   54.25455 45.56629 1.000 144.57727 ? 282 TYR   A CD2 1 
ATOM   2162 C CE1 . TYR   A 1  282 ? 5.42283   56.58022 45.11696 1.000 156.18880 ? 282 TYR   A CE1 1 
ATOM   2163 C CE2 . TYR   A 1  282 ? 3.43530   55.48954 45.90797 1.000 157.47545 ? 282 TYR   A CE2 1 
ATOM   2164 C CZ  . TYR   A 1  282 ? 4.15969   56.65322 45.68148 1.000 160.66115 ? 282 TYR   A CZ  1 
ATOM   2165 O OH  . TYR   A 1  282 ? 3.62859   57.88886 46.01724 1.000 150.74361 ? 282 TYR   A OH  1 
ATOM   2166 N N   . GLY   A 1  283 ? 8.55583   51.66553 42.61214 1.000 117.02771 ? 283 GLY   A N   1 
ATOM   2167 C CA  . GLY   A 1  283 ? 9.44400   50.53144 42.50932 1.000 106.27379 ? 283 GLY   A CA  1 
ATOM   2168 C C   . GLY   A 1  283 ? 10.15649  50.22318 43.81548 1.000 92.71740  ? 283 GLY   A C   1 
ATOM   2169 O O   . GLY   A 1  283 ? 10.24538  51.04647 44.72672 1.000 91.41182  ? 283 GLY   A O   1 
ATOM   2170 N N   . THR   A 1  284 ? 10.65758  49.00015 43.90849 1.000 86.00042  ? 284 THR   A N   1 
ATOM   2171 C CA  . THR   A 1  284 ? 11.53160  48.56251 44.98637 1.000 79.18669  ? 284 THR   A CA  1 
ATOM   2172 C C   . THR   A 1  284 ? 12.73383  47.90124 44.34061 1.000 81.17812  ? 284 THR   A C   1 
ATOM   2173 O O   . THR   A 1  284 ? 12.72447  47.61408 43.13905 1.000 81.31728  ? 284 THR   A O   1 
ATOM   2174 C CB  . THR   A 1  284 ? 10.82473  47.58326 45.95056 1.000 75.14202  ? 284 THR   A CB  1 
ATOM   2175 O OG1 . THR   A 1  284 ? 10.73764  46.28157 45.35807 1.000 81.48228  ? 284 THR   A OG1 1 
ATOM   2176 C CG2 . THR   A 1  284 ? 9.43451   48.04716 46.28753 1.000 75.28125  ? 284 THR   A CG2 1 
ATOM   2177 N N   . PRO   A 1  285 ? 13.80490  47.65619 45.10276 1.000 77.01447  ? 285 PRO   A N   1 
ATOM   2178 C CA  . PRO   A 1  285 ? 14.93668  46.92203 44.51920 1.000 74.76914  ? 285 PRO   A CA  1 
ATOM   2179 C C   . PRO   A 1  285 ? 14.54195  45.57714 43.93474 1.000 77.63792  ? 285 PRO   A C   1 
ATOM   2180 O O   . PRO   A 1  285 ? 15.23912  45.07610 43.04576 1.000 80.00003  ? 285 PRO   A O   1 
ATOM   2181 C CB  . PRO   A 1  285 ? 15.89500  46.76947 45.70689 1.000 71.21989  ? 285 PRO   A CB  1 
ATOM   2182 C CG  . PRO   A 1  285 ? 15.64804  47.98571 46.52091 1.000 69.55052  ? 285 PRO   A CG  1 
ATOM   2183 C CD  . PRO   A 1  285 ? 14.14713  48.21128 46.42799 1.000 74.70110  ? 285 PRO   A CD  1 
ATOM   2184 N N   . LEU   A 1  286 ? 13.43469  44.98556 44.39065 1.000 76.51444  ? 286 LEU   A N   1 
ATOM   2185 C CA  . LEU   A 1  286 ? 12.96574  43.69193 43.91520 1.000 72.95468  ? 286 LEU   A CA  1 
ATOM   2186 C C   . LEU   A 1  286 ? 11.80198  43.81052 42.93741 1.000 70.34308  ? 286 LEU   A C   1 
ATOM   2187 O O   . LEU   A 1  286 ? 11.10738  42.82192 42.68479 1.000 72.57887  ? 286 LEU   A O   1 
ATOM   2188 C CB  . LEU   A 1  286 ? 12.57098  42.81971 45.10138 1.000 66.81834  ? 286 LEU   A CB  1 
ATOM   2189 C CG  . LEU   A 1  286 ? 13.69764  42.48388 46.06401 1.000 67.81625  ? 286 LEU   A CG  1 
ATOM   2190 C CD1 . LEU   A 1  286 ? 13.54171  43.28917 47.32668 1.000 65.82873  ? 286 LEU   A CD1 1 
ATOM   2191 C CD2 . LEU   A 1  286 ? 13.66783  40.99318 46.37958 1.000 64.78813  ? 286 LEU   A CD2 1 
ATOM   2192 N N   . SER   A 1  287 ? 11.58487  44.98660 42.36703 1.000 72.38138  ? 287 SER   A N   1 
ATOM   2193 C CA  . SER   A 1  287 ? 10.46315  45.15910 41.45223 1.000 74.07727  ? 287 SER   A CA  1 
ATOM   2194 C C   . SER   A 1  287 ? 10.63275  44.27615 40.22750 1.000 70.42719  ? 287 SER   A C   1 
ATOM   2195 O O   . SER   A 1  287 ? 11.72247  44.18599 39.65702 1.000 76.19658  ? 287 SER   A O   1 
ATOM   2196 C CB  . SER   A 1  287 ? 10.33833  46.62094 41.02787 1.000 70.47874  ? 287 SER   A CB  1 
ATOM   2197 O OG  . SER   A 1  287 ? 9.63325   47.36389 42.00581 1.000 78.90139  ? 287 SER   A OG  1 
ATOM   2198 N N   . VAL   A 1  288 ? 9.55229   43.62622 39.82981 1.000 63.97514  ? 288 VAL   A N   1 
ATOM   2199 C CA  . VAL   A 1  288 ? 9.51934   42.80575 38.62616 1.000 63.94563  ? 288 VAL   A CA  1 
ATOM   2200 C C   . VAL   A 1  288 ? 8.48468   43.46163 37.72137 1.000 67.24272  ? 288 VAL   A C   1 
ATOM   2201 O O   . VAL   A 1  288 ? 7.29457   43.14025 37.76673 1.000 75.94132  ? 288 VAL   A O   1 
ATOM   2202 C CB  . VAL   A 1  288 ? 9.18201   41.34426 38.92899 1.000 65.97719  ? 288 VAL   A CB  1 
ATOM   2203 C CG1 . VAL   A 1  288 ? 8.96968   40.57309 37.64905 1.000 60.99098  ? 288 VAL   A CG1 1 
ATOM   2204 C CG2 . VAL   A 1  288 ? 10.29063  40.71225 39.77663 1.000 64.65877  ? 288 VAL   A CG2 1 
ATOM   2205 N N   . ASN   A 1  289 ? 8.93671   44.41863 36.90642 1.000 69.34880  ? 289 ASN   A N   1 
ATOM   2206 C CA  . ASN   A 1  289 ? 8.01086   45.23997 36.13287 1.000 69.46069  ? 289 ASN   A CA  1 
ATOM   2207 C C   . ASN   A 1  289 ? 7.16417   44.39702 35.19145 1.000 68.70817  ? 289 ASN   A C   1 
ATOM   2208 O O   . ASN   A 1  289 ? 5.97882   44.68078 34.98631 1.000 66.50067  ? 289 ASN   A O   1 
ATOM   2209 C CB  . ASN   A 1  289 ? 8.78181   46.28728 35.33428 1.000 70.87539  ? 289 ASN   A CB  1 
ATOM   2210 C CG  . ASN   A 1  289 ? 9.54174   47.25915 36.21780 1.000 83.37296  ? 289 ASN   A CG  1 
ATOM   2211 O OD1 . ASN   A 1  289 ? 8.98491   47.83465 37.16158 1.000 84.25329  ? 289 ASN   A OD1 1 
ATOM   2212 N ND2 . ASN   A 1  289 ? 10.82138  47.46555 35.89830 1.000 67.78729  ? 289 ASN   A ND2 1 
ATOM   2213 N N   . PHE   A 1  290 ? 7.76074   43.36731 34.60064 1.000 63.95023  ? 290 PHE   A N   1 
ATOM   2214 C CA  . PHE   A 1  290 ? 7.11015   42.51628 33.60629 1.000 60.81949  ? 290 PHE   A CA  1 
ATOM   2215 C C   . PHE   A 1  290 ? 7.57722   41.10159 33.89167 1.000 59.37319  ? 290 PHE   A C   1 
ATOM   2216 O O   . PHE   A 1  290 ? 8.71399   40.76009 33.56509 1.000 61.39350  ? 290 PHE   A O   1 
ATOM   2217 C CB  . PHE   A 1  290 ? 7.46758   42.92495 32.18342 1.000 62.53761  ? 290 PHE   A CB  1 
ATOM   2218 C CG  . PHE   A 1  290 ? 6.82370   44.18891 31.74569 1.000 66.19519  ? 290 PHE   A CG  1 
ATOM   2219 C CD1 . PHE   A 1  290 ? 5.52303   44.18160 31.24890 1.000 64.74644  ? 290 PHE   A CD1 1 
ATOM   2220 C CD2 . PHE   A 1  290 ? 7.50552   45.39200 31.83940 1.000 69.18163  ? 290 PHE   A CD2 1 
ATOM   2221 C CE1 . PHE   A 1  290 ? 4.91170   45.35712 30.84856 1.000 70.79769  ? 290 PHE   A CE1 1 
ATOM   2222 C CE2 . PHE   A 1  290 ? 6.90094   46.58584 31.43748 1.000 71.01830  ? 290 PHE   A CE2 1 
ATOM   2223 C CZ  . PHE   A 1  290 ? 5.60754   46.57193 30.94411 1.000 72.76304  ? 290 PHE   A CZ  1 
ATOM   2224 N N   . GLY   A 1  291 ? 6.71166   40.29053 34.49641 1.000 64.50291  ? 291 GLY   A N   1 
ATOM   2225 C CA  . GLY   A 1  291 ? 7.03445   38.91539 34.75747 1.000 55.60050  ? 291 GLY   A CA  1 
ATOM   2226 C C   . GLY   A 1  291 ? 5.92194   37.95624 34.37548 1.000 57.73977  ? 291 GLY   A C   1 
ATOM   2227 O O   . GLY   A 1  291 ? 5.01683   38.26993 33.59176 1.000 56.74334  ? 291 GLY   A O   1 
ATOM   2228 N N   . PRO   A 1  292 ? 5.98171   36.75037 34.91388 1.000 57.17097  ? 292 PRO   A N   1 
ATOM   2229 C CA  . PRO   A 1  292 ? 4.98243   35.75120 34.55399 1.000 60.34354  ? 292 PRO   A CA  1 
ATOM   2230 C C   . PRO   A 1  292 ? 3.58443   36.22565 34.92079 1.000 63.87983  ? 292 PRO   A C   1 
ATOM   2231 O O   . PRO   A 1  292 ? 3.38425   36.99405 35.86435 1.000 66.45326  ? 292 PRO   A O   1 
ATOM   2232 C CB  . PRO   A 1  292 ? 5.40121   34.52225 35.37648 1.000 56.43342  ? 292 PRO   A CB  1 
ATOM   2233 C CG  . PRO   A 1  292 ? 6.85032   34.66190 35.53402 1.000 54.72595  ? 292 PRO   A CG  1 
ATOM   2234 C CD  . PRO   A 1  292 ? 7.09187   36.16079 35.68170 1.000 57.02485  ? 292 PRO   A CD  1 
ATOM   2235 N N   . THR   A 1  293 ? 2.61407   35.77597 34.14460 1.000 58.40418  ? 293 THR   A N   1 
ATOM   2236 C CA  . THR   A 1  293 ? 1.22190   36.04631 34.43417 1.000 65.02183  ? 293 THR   A CA  1 
ATOM   2237 C C   . THR   A 1  293 ? 0.43520   34.75496 34.27729 1.000 61.97184  ? 293 THR   A C   1 
ATOM   2238 O O   . THR   A 1  293 ? 0.92462   33.76607 33.72524 1.000 63.86003  ? 293 THR   A O   1 
ATOM   2239 C CB  . THR   A 1  293 ? 0.63020   37.14706 33.51674 1.000 62.07637  ? 293 THR   A CB  1 
ATOM   2240 O OG1 . THR   A 1  293 ? 1.00412   36.89648 32.16167 1.000 63.25967  ? 293 THR   A OG1 1 
ATOM   2241 C CG2 . THR   A 1  293 ? 1.14197   38.51075 33.91815 1.000 66.00422  ? 293 THR   A CG2 1 
ATOM   2242 N N   . VAL   A 1  294 ? -0.79414  34.77467 34.78311 1.000 60.74084  ? 294 VAL   A N   1 
ATOM   2243 C CA  . VAL   A 1  294 ? -1.76303  33.73303 34.47928 1.000 59.68727  ? 294 VAL   A CA  1 
ATOM   2244 C C   . VAL   A 1  294 ? -2.30782  34.00007 33.08149 1.000 58.98396  ? 294 VAL   A C   1 
ATOM   2245 O O   . VAL   A 1  294 ? -3.33756  34.66041 32.90285 1.000 63.46187  ? 294 VAL   A O   1 
ATOM   2246 C CB  . VAL   A 1  294 ? -2.86056  33.67719 35.55696 1.000 69.77207  ? 294 VAL   A CB  1 
ATOM   2247 C CG1 . VAL   A 1  294 ? -3.72985  32.40399 35.40663 1.000 64.29266  ? 294 VAL   A CG1 1 
ATOM   2248 C CG2 . VAL   A 1  294 ? -2.20527  33.72708 36.93158 1.000 68.36192  ? 294 VAL   A CG2 1 
ATOM   2249 N N   . ASP   A 1  295 ? -1.59704  33.49818 32.07586 1.000 63.00742  ? 295 ASP   A N   1 
ATOM   2250 C CA  . ASP   A 1  295 ? -1.96726  33.74054 30.69038 1.000 65.01345  ? 295 ASP   A CA  1 
ATOM   2251 C C   . ASP   A 1  295 ? -3.11102  32.85134 30.19770 1.000 63.53065  ? 295 ASP   A C   1 
ATOM   2252 O O   . ASP   A 1  295 ? -3.74714  33.18936 29.19456 1.000 64.86118  ? 295 ASP   A O   1 
ATOM   2253 C CB  . ASP   A 1  295 ? -0.73901  33.55819 29.79238 1.000 59.78696  ? 295 ASP   A CB  1 
ATOM   2254 C CG  . ASP   A 1  295 ? -0.15473  32.14002 29.84914 1.000 62.71885  ? 295 ASP   A CG  1 
ATOM   2255 O OD1 . ASP   A 1  295 ? -0.48410  31.35301 30.77091 1.000 66.30025  ? 295 ASP   A OD1 1 
ATOM   2256 O OD2 . ASP   A 1  295 ? 0.63725   31.80028 28.94781 1.000 64.53296  ? 295 ASP   A OD2 1 
ATOM   2257 N N   . GLY   A 1  296 ? -3.38660  31.72708 30.86225 1.000 69.30543  ? 296 GLY   A N   1 
ATOM   2258 C CA  . GLY   A 1  296 ? -4.32384  30.73900 30.34513 1.000 62.76108  ? 296 GLY   A CA  1 
ATOM   2259 C C   . GLY   A 1  296 ? -3.73815  29.78923 29.31856 1.000 68.58194  ? 296 GLY   A C   1 
ATOM   2260 O O   . GLY   A 1  296 ? -4.49057  29.03723 28.67860 1.000 59.69582  ? 296 GLY   A O   1 
ATOM   2261 N N   . ASP   A 1  297 ? -2.41339  29.80752 29.14126 1.000 67.49025  ? 297 ASP   A N   1 
ATOM   2262 C CA  . ASP   A 1  297 ? -1.71279  29.01619 28.13937 1.000 64.50954  ? 297 ASP   A CA  1 
ATOM   2263 C C   . ASP   A 1  297 ? -0.55939  28.28541 28.81477 1.000 63.27216  ? 297 ASP   A C   1 
ATOM   2264 O O   . ASP   A 1  297 ? -0.59804  27.06856 29.01222 1.000 63.19434  ? 297 ASP   A O   1 
ATOM   2265 C CB  . ASP   A 1  297 ? -1.21201  29.92609 27.01727 1.000 57.33743  ? 297 ASP   A CB  1 
ATOM   2266 C CG  . ASP   A 1  297 ? -0.90914  29.17321 25.73688 1.000 68.18803  ? 297 ASP   A CG  1 
ATOM   2267 O OD1 . ASP   A 1  297 ? -0.89631  27.91120 25.76268 1.000 63.84213  ? 297 ASP   A OD1 1 
ATOM   2268 O OD2 . ASP   A 1  297 ? -0.68290  29.85623 24.70135 1.000 62.07631  ? 297 ASP   A OD2 1 
ATOM   2269 N N   . PHE   A 1  298 ? 0.46850   29.02910 29.19701 1.000 60.95599  ? 298 PHE   A N   1 
ATOM   2270 C CA  . PHE   A 1  298 ? 1.51347   28.42163 30.00059 1.000 65.48934  ? 298 PHE   A CA  1 
ATOM   2271 C C   . PHE   A 1  298 ? 1.00468   28.10686 31.39669 1.000 65.61816  ? 298 PHE   A C   1 
ATOM   2272 O O   . PHE   A 1  298 ? 1.43150   27.12319 32.00782 1.000 63.46093  ? 298 PHE   A O   1 
ATOM   2273 C CB  . PHE   A 1  298 ? 2.72582   29.34959 30.08726 1.000 58.33570  ? 298 PHE   A CB  1 
ATOM   2274 C CG  . PHE   A 1  298 ? 3.93137   28.69659 30.64370 1.000 56.21830  ? 298 PHE   A CG  1 
ATOM   2275 C CD1 . PHE   A 1  298 ? 4.81695   28.02241 29.80936 1.000 59.07277  ? 298 PHE   A CD1 1 
ATOM   2276 C CD2 . PHE   A 1  298 ? 4.19712   28.74697 32.00607 1.000 57.01500  ? 298 PHE   A CD2 1 
ATOM   2277 C CE1 . PHE   A 1  298 ? 5.95223   27.41444 30.32484 1.000 53.98632  ? 298 PHE   A CE1 1 
ATOM   2278 C CE2 . PHE   A 1  298 ? 5.32639   28.14161 32.53370 1.000 52.49576  ? 298 PHE   A CE2 1 
ATOM   2279 C CZ  . PHE   A 1  298 ? 6.20809   27.47466 31.68856 1.000 54.47823  ? 298 PHE   A CZ  1 
ATOM   2280 N N   . LEU   A 1  299 ? 0.09753   28.92802 31.91047 1.000 61.55359  ? 299 LEU   A N   1 
ATOM   2281 C CA  . LEU   A 1  299 ? -0.33642  28.84996 33.29752 1.000 62.23479  ? 299 LEU   A CA  1 
ATOM   2282 C C   . LEU   A 1  299 ? -1.84380  29.03564 33.30201 1.000 65.57949  ? 299 LEU   A C   1 
ATOM   2283 O O   . LEU   A 1  299 ? -2.32987  30.12170 32.98627 1.000 60.61422  ? 299 LEU   A O   1 
ATOM   2284 C CB  . LEU   A 1  299 ? 0.36282   29.91855 34.12407 1.000 65.88079  ? 299 LEU   A CB  1 
ATOM   2285 C CG  . LEU   A 1  299 ? 0.53185   29.67657 35.60594 1.000 71.37592  ? 299 LEU   A CG  1 
ATOM   2286 C CD1 . LEU   A 1  299 ? 1.41057   28.45675 35.77377 1.000 72.28236  ? 299 LEU   A CD1 1 
ATOM   2287 C CD2 . LEU   A 1  299 ? 1.22037   30.92883 36.16785 1.000 61.87520  ? 299 LEU   A CD2 1 
ATOM   2288 N N   . THR   A 1  300 ? -2.57992  27.97225 33.62934 1.000 70.09490  ? 300 THR   A N   1 
ATOM   2289 C CA  . THR   A 1  300 ? -4.02959  27.90850 33.44785 1.000 68.18671  ? 300 THR   A CA  1 
ATOM   2290 C C   . THR   A 1  300 ? -4.82026  28.47086 34.62329 1.000 65.82280  ? 300 THR   A C   1 
ATOM   2291 O O   . THR   A 1  300 ? -6.02737  28.70566 34.48798 1.000 66.04608  ? 300 THR   A O   1 
ATOM   2292 C CB  . THR   A 1  300 ? -4.44864  26.45500 33.20471 1.000 68.82873  ? 300 THR   A CB  1 
ATOM   2293 O OG1 . THR   A 1  300 ? -4.05020  25.65547 34.32532 1.000 71.25054  ? 300 THR   A OG1 1 
ATOM   2294 C CG2 . THR   A 1  300 ? -3.73290  25.91534 31.97829 1.000 73.94115  ? 300 THR   A CG2 1 
ATOM   2295 N N   . ASP   A 1  301 ? -4.16797  28.70863 35.75516 1.000 64.88452  ? 301 ASP   A N   1 
ATOM   2296 C CA  . ASP   A 1  301 ? -4.82774  29.14175 36.98044 1.000 67.48576  ? 301 ASP   A CA  1 
ATOM   2297 C C   . ASP   A 1  301 ? -3.75046  29.77132 37.85090 1.000 65.95948  ? 301 ASP   A C   1 
ATOM   2298 O O   . ASP   A 1  301 ? -2.54986  29.65414 37.57561 1.000 59.76377  ? 301 ASP   A O   1 
ATOM   2299 C CB  . ASP   A 1  301 ? -5.52435  27.96088 37.69602 1.000 59.71177  ? 301 ASP   A CB  1 
ATOM   2300 C CG  . ASP   A 1  301 ? -6.62213  28.40299 38.69507 1.000 66.03977  ? 301 ASP   A CG  1 
ATOM   2301 O OD1 . ASP   A 1  301 ? -6.77683  29.61674 38.95207 1.000 62.85334  ? 301 ASP   A OD1 1 
ATOM   2302 O OD2 . ASP   A 1  301 ? -7.34437  27.51707 39.22353 1.000 65.87585  ? 301 ASP   A OD2 1 
ATOM   2303 N N   . MET   A 1  302 ? -4.18425  30.42293 38.90644 1.000 60.87899  ? 302 MET   A N   1 
ATOM   2304 C CA  . MET   A 1  302 ? -3.22272  31.07410 39.77851 1.000 67.70806  ? 302 MET   A CA  1 
ATOM   2305 C C   . MET   A 1  302 ? -2.37173  30.02573 40.48065 1.000 66.61409  ? 302 MET   A C   1 
ATOM   2306 O O   . MET   A 1  302 ? -2.91125  29.08040 41.06776 1.000 67.42243  ? 302 MET   A O   1 
ATOM   2307 C CB  . MET   A 1  302 ? -3.94256  32.00672 40.74582 1.000 73.27370  ? 302 MET   A CB  1 
ATOM   2308 C CG  . MET   A 1  302 ? -4.83946  32.96276 39.94044 1.000 67.71160  ? 302 MET   A CG  1 
ATOM   2309 S SD  . MET   A 1  302 ? -5.90057  34.08290 40.85559 1.000 108.80526 ? 302 MET   A SD  1 
ATOM   2310 C CE  . MET   A 1  302 ? -5.33237  33.72609 42.49349 1.000 80.86580  ? 302 MET   A CE  1 
ATOM   2311 N N   . PRO   A 1  303 ? -1.04624  30.12660 40.39552 1.000 64.70293  ? 303 PRO   A N   1 
ATOM   2312 C CA  . PRO   A 1  303 ? -0.20502  28.98850 40.78456 1.000 62.87033  ? 303 PRO   A CA  1 
ATOM   2313 C C   . PRO   A 1  303 ? -0.36329  28.57549 42.23940 1.000 64.59918  ? 303 PRO   A C   1 
ATOM   2314 O O   . PRO   A 1  303 ? -0.25889  27.37930 42.53373 1.000 67.76801  ? 303 PRO   A O   1 
ATOM   2315 C CB  . PRO   A 1  303 ? 1.21743   29.48115 40.46971 1.000 65.45582  ? 303 PRO   A CB  1 
ATOM   2316 C CG  . PRO   A 1  303 ? 1.10776   30.96425 40.31875 1.000 63.59181  ? 303 PRO   A CG  1 
ATOM   2317 C CD  . PRO   A 1  303 ? -0.26207  31.24029 39.82930 1.000 64.17763  ? 303 PRO   A CD  1 
ATOM   2318 N N   . ASP   A 1  304 ? -0.62439  29.50601 43.15913 1.000 60.52444  ? 304 ASP   A N   1 
ATOM   2319 C CA  . ASP   A 1  304 ? -0.86040  29.10085 44.54243 1.000 62.35976  ? 304 ASP   A CA  1 
ATOM   2320 C C   . ASP   A 1  304 ? -1.99760  28.09900 44.64865 1.000 64.50436  ? 304 ASP   A C   1 
ATOM   2321 O O   . ASP   A 1  304 ? -1.95574  27.20030 45.49902 1.000 65.16600  ? 304 ASP   A O   1 
ATOM   2322 C CB  . ASP   A 1  304 ? -1.15111  30.31776 45.41845 1.000 64.25406  ? 304 ASP   A CB  1 
ATOM   2323 C CG  . ASP   A 1  304 ? -2.02356  31.32429 44.72051 1.000 84.62495  ? 304 ASP   A CG  1 
ATOM   2324 O OD1 . ASP   A 1  304 ? -3.15470  31.59287 45.20649 1.000 84.90564  ? 304 ASP   A OD1 1 
ATOM   2325 O OD2 . ASP   A 1  304 ? -1.54529  31.86936 43.68684 1.000 88.66680  ? 304 ASP   A OD2 1 
ATOM   2326 N N   . ILE   A 1  305 ? -3.01102  28.22314 43.79003 1.000 65.88194  ? 305 ILE   A N   1 
ATOM   2327 C CA  . ILE   A 1  305 ? -4.11128  27.26677 43.79552 1.000 64.57837  ? 305 ILE   A CA  1 
ATOM   2328 C C   . ILE   A 1  305 ? -3.63560  25.90750 43.27664 1.000 61.26937  ? 305 ILE   A C   1 
ATOM   2329 O O   . ILE   A 1  305 ? -3.91924  24.86758 43.87676 1.000 57.85541  ? 305 ILE   A O   1 
ATOM   2330 C CB  . ILE   A 1  305 ? -5.30069  27.82187 42.98462 1.000 68.57708  ? 305 ILE   A CB  1 
ATOM   2331 C CG1 . ILE   A 1  305 ? -5.74134  29.17179 43.55981 1.000 69.95415  ? 305 ILE   A CG1 1 
ATOM   2332 C CG2 . ILE   A 1  305 ? -6.47937  26.81275 42.95350 1.000 58.50730  ? 305 ILE   A CG2 1 
ATOM   2333 C CD1 . ILE   A 1  305 ? -7.02351  29.75407 42.94541 1.000 56.14157  ? 305 ILE   A CD1 1 
ATOM   2334 N N   . LEU   A 1  306 ? -2.87601  25.89745 42.17459 1.000 61.90709  ? 306 LEU   A N   1 
ATOM   2335 C CA  . LEU   A 1  306 ? -2.34034  24.63734 41.64611 1.000 64.24469  ? 306 LEU   A CA  1 
ATOM   2336 C C   . LEU   A 1  306 ? -1.45749  23.93608 42.67338 1.000 63.03374  ? 306 LEU   A C   1 
ATOM   2337 O O   . LEU   A 1  306 ? -1.61799  22.72958 42.93575 1.000 61.56676  ? 306 LEU   A O   1 
ATOM   2338 C CB  . LEU   A 1  306 ? -1.56014  24.89075 40.35091 1.000 57.66132  ? 306 LEU   A CB  1 
ATOM   2339 C CG  . LEU   A 1  306 ? -2.36674  25.70597 39.31634 1.000 57.90872  ? 306 LEU   A CG  1 
ATOM   2340 C CD1 . LEU   A 1  306 ? -1.55314  25.99622 38.07341 1.000 60.82159  ? 306 LEU   A CD1 1 
ATOM   2341 C CD2 . LEU   A 1  306 ? -3.67275  25.03232 38.94442 1.000 55.08506  ? 306 LEU   A CD2 1 
ATOM   2342 N N   . LEU   A 1  307 ? -0.51032  24.67816 43.26087 1.000 59.90811  ? 307 LEU   A N   1 
ATOM   2343 C CA  . LEU   A 1  307 ? 0.30028   24.14547 44.35355 1.000 59.32309  ? 307 LEU   A CA  1 
ATOM   2344 C C   . LEU   A 1  307 ? -0.57663  23.55056 45.44999 1.000 64.95528  ? 307 LEU   A C   1 
ATOM   2345 O O   . LEU   A 1  307 ? -0.46332  22.36170 45.77842 1.000 65.89997  ? 307 LEU   A O   1 
ATOM   2346 C CB  . LEU   A 1  307 ? 1.20580   25.23840 44.92393 1.000 62.21664  ? 307 LEU   A CB  1 
ATOM   2347 C CG  . LEU   A 1  307 ? 2.17599   24.78143 46.02342 1.000 62.15362  ? 307 LEU   A CG  1 
ATOM   2348 C CD1 . LEU   A 1  307 ? 2.97233   23.55538 45.57833 1.000 64.27437  ? 307 LEU   A CD1 1 
ATOM   2349 C CD2 . LEU   A 1  307 ? 3.12537   25.89671 46.41284 1.000 53.12114  ? 307 LEU   A CD2 1 
ATOM   2350 N N   . GLU   A 1  308 ? -1.49651  24.36039 45.99347 1.000 60.13379  ? 308 GLU   A N   1 
ATOM   2351 C CA  . GLU   A 1  308 ? -2.25977  23.93651 47.15830 1.000 57.49095  ? 308 GLU   A CA  1 
ATOM   2352 C C   . GLU   A 1  308 ? -3.06859  22.67614 46.87581 1.000 64.49647  ? 308 GLU   A C   1 
ATOM   2353 O O   . GLU   A 1  308 ? -3.25454  21.84861 47.77841 1.000 65.24601  ? 308 GLU   A O   1 
ATOM   2354 C CB  . GLU   A 1  308 ? -3.17304  25.07159 47.62957 1.000 57.12278  ? 308 GLU   A CB  1 
ATOM   2355 C CG  . GLU   A 1  308 ? -4.16353  24.67664 48.74173 1.000 62.00341  ? 308 GLU   A CG  1 
ATOM   2356 C CD  . GLU   A 1  308 ? -3.48330  24.35331 50.07378 1.000 63.76020  ? 308 GLU   A CD  1 
ATOM   2357 O OE1 . GLU   A 1  308 ? -2.33105  24.75845 50.26715 1.000 66.37756  ? 308 GLU   A OE1 1 
ATOM   2358 O OE2 . GLU   A 1  308 ? -4.10935  23.70793 50.94514 1.000 68.12596  ? 308 GLU   A OE2 1 
ATOM   2359 N N   . LEU   A 1  309 ? -3.54470  22.49919 45.63734 1.000 62.70567  ? 309 LEU   A N   1 
ATOM   2360 C CA  . LEU   A 1  309 ? -4.40374  21.37084 45.29580 1.000 64.71774  ? 309 LEU   A CA  1 
ATOM   2361 C C   . LEU   A 1  309 ? -3.66648  20.28249 44.53122 1.000 63.03450  ? 309 LEU   A C   1 
ATOM   2362 O O   . LEU   A 1  309 ? -4.31020  19.42721 43.91853 1.000 61.16132  ? 309 LEU   A O   1 
ATOM   2363 C CB  . LEU   A 1  309 ? -5.61800  21.83912 44.49627 1.000 57.21998  ? 309 LEU   A CB  1 
ATOM   2364 C CG  . LEU   A 1  309 ? -6.54558  22.79552 45.23894 1.000 56.81597  ? 309 LEU   A CG  1 
ATOM   2365 C CD1 . LEU   A 1  309 ? -7.64692  23.24145 44.28730 1.000 56.10280  ? 309 LEU   A CD1 1 
ATOM   2366 C CD2 . LEU   A 1  309 ? -7.12780  22.15835 46.53212 1.000 52.15965  ? 309 LEU   A CD2 1 
ATOM   2367 N N   . GLY   A 1  310 ? -2.33475  20.30082 44.55163 1.000 68.53571  ? 310 GLY   A N   1 
ATOM   2368 C CA  . GLY   A 1  310 ? -1.55370  19.20316 44.00486 1.000 66.73755  ? 310 GLY   A CA  1 
ATOM   2369 C C   . GLY   A 1  310 ? -1.58413  19.06973 42.49617 1.000 67.38866  ? 310 GLY   A C   1 
ATOM   2370 O O   . GLY   A 1  310 ? -1.42338  17.96165 41.98404 1.000 64.64188  ? 310 GLY   A O   1 
ATOM   2371 N N   . GLN   A 1  311 ? -1.77921  20.16929 41.76225 1.000 65.46746  ? 311 GLN   A N   1 
ATOM   2372 C CA  . GLN   A 1  311 ? -1.82812  20.11709 40.29953 1.000 63.40764  ? 311 GLN   A CA  1 
ATOM   2373 C C   . GLN   A 1  311 ? -0.44738  20.43851 39.73318 1.000 61.70180  ? 311 GLN   A C   1 
ATOM   2374 O O   . GLN   A 1  311 ? -0.19619  21.53665 39.24381 1.000 62.90058  ? 311 GLN   A O   1 
ATOM   2375 C CB  . GLN   A 1  311 ? -2.87745  21.07372 39.77710 1.000 59.29557  ? 311 GLN   A CB  1 
ATOM   2376 C CG  . GLN   A 1  311 ? -4.19293  20.85545 40.45342 1.000 69.94382  ? 311 GLN   A CG  1 
ATOM   2377 C CD  . GLN   A 1  311 ? -4.71272  19.45122 40.22080 1.000 68.46560  ? 311 GLN   A CD  1 
ATOM   2378 O OE1 . GLN   A 1  311 ? -4.68382  18.94951 39.09305 1.000 66.64795  ? 311 GLN   A OE1 1 
ATOM   2379 N NE2 . GLN   A 1  311 ? -5.19594  18.80923 41.28372 1.000 61.19605  ? 311 GLN   A NE2 1 
ATOM   2380 N N   . PHE   A 1  312 ? 0.44893   19.44743 39.77369 1.000 61.57455  ? 312 PHE   A N   1 
ATOM   2381 C CA  . PHE   A 1  312 ? 1.80982   19.66043 39.29571 1.000 58.87852  ? 312 PHE   A CA  1 
ATOM   2382 C C   . PHE   A 1  312 ? 2.50813   18.33181 38.99891 1.000 57.53368  ? 312 PHE   A C   1 
ATOM   2383 O O   . PHE   A 1  312 ? 2.08122   17.25838 39.43568 1.000 57.02901  ? 312 PHE   A O   1 
ATOM   2384 C CB  . PHE   A 1  312 ? 2.62100   20.47965 40.30361 1.000 58.93013  ? 312 PHE   A CB  1 
ATOM   2385 C CG  . PHE   A 1  312 ? 2.54220   19.97822 41.70963 1.000 62.51938  ? 312 PHE   A CG  1 
ATOM   2386 C CD1 . PHE   A 1  312 ? 3.25624   18.85738 42.10162 1.000 57.11965  ? 312 PHE   A CD1 1 
ATOM   2387 C CD2 . PHE   A 1  312 ? 1.77343   20.64661 42.65426 1.000 64.59102  ? 312 PHE   A CD2 1 
ATOM   2388 C CE1 . PHE   A 1  312 ? 3.19011   18.39051 43.41669 1.000 64.31931  ? 312 PHE   A CE1 1 
ATOM   2389 C CE2 . PHE   A 1  312 ? 1.70305   20.18921 43.96801 1.000 67.13642  ? 312 PHE   A CE2 1 
ATOM   2390 C CZ  . PHE   A 1  312 ? 2.41383   19.05249 44.34963 1.000 64.21597  ? 312 PHE   A CZ  1 
ATOM   2391 N N   . LYS   A 1  313 ? 3.61144   18.42940 38.25410 1.000 58.17293  ? 313 LYS   A N   1 
ATOM   2392 C CA  . LYS   A 1  313 ? 4.40663   17.25514 37.91375 1.000 64.59815  ? 313 LYS   A CA  1 
ATOM   2393 C C   . LYS   A 1  313 ? 4.86718   16.52854 39.17384 1.000 57.53771  ? 313 LYS   A C   1 
ATOM   2394 O O   . LYS   A 1  313 ? 5.41154   17.14626 40.08941 1.000 58.55764  ? 313 LYS   A O   1 
ATOM   2395 C CB  . LYS   A 1  313 ? 5.62180   17.66756 37.07702 1.000 60.53811  ? 313 LYS   A CB  1 
ATOM   2396 C CG  . LYS   A 1  313 ? 6.35340   16.48682 36.46296 1.000 52.76196  ? 313 LYS   A CG  1 
ATOM   2397 C CD  . LYS   A 1  313 ? 7.54585   16.93967 35.66339 1.000 61.85062  ? 313 LYS   A CD  1 
ATOM   2398 C CE  . LYS   A 1  313 ? 8.44735   15.76733 35.29156 1.000 60.50785  ? 313 LYS   A CE  1 
ATOM   2399 N NZ  . LYS   A 1  313 ? 7.99634   15.07856 34.04037 1.000 55.17781  ? 313 LYS   A NZ  1 
ATOM   2400 N N   . LYS   A 1  314 ? 4.64789   15.21321 39.21500 1.000 53.66149  ? 314 LYS   A N   1 
ATOM   2401 C CA  . LYS   A 1  314 ? 5.00975   14.37834 40.35921 1.000 54.96074  ? 314 LYS   A CA  1 
ATOM   2402 C C   . LYS   A 1  314 ? 6.40485   13.80861 40.11673 1.000 56.06164  ? 314 LYS   A C   1 
ATOM   2403 O O   . LYS   A 1  314 ? 6.59452   12.98229 39.21951 1.000 57.03809  ? 314 LYS   A O   1 
ATOM   2404 C CB  . LYS   A 1  314 ? 3.98141   13.26308 40.56502 1.000 58.21527  ? 314 LYS   A CB  1 
ATOM   2405 C CG  . LYS   A 1  314 ? 2.53264   13.74309 40.83213 1.000 56.08116  ? 314 LYS   A CG  1 
ATOM   2406 C CD  . LYS   A 1  314 ? 2.45013   14.54069 42.14728 1.000 68.13489  ? 314 LYS   A CD  1 
ATOM   2407 C CE  . LYS   A 1  314 ? 1.13386   15.28960 42.34562 1.000 63.31667  ? 314 LYS   A CE  1 
ATOM   2408 N NZ  . LYS   A 1  314 ? 0.71680   16.00101 41.11696 1.000 62.52173  ? 314 LYS   A NZ  1 
ATOM   2409 N N   . THR   A 1  315 ? 7.38219   14.26660 40.89986 1.000 53.49139  ? 315 THR   A N   1 
ATOM   2410 C CA  . THR   A 1  315 ? 8.79781   13.97497 40.67762 1.000 56.09395  ? 315 THR   A CA  1 
ATOM   2411 C C   . THR   A 1  315 ? 9.57041   14.51531 41.87809 1.000 56.32453  ? 315 THR   A C   1 
ATOM   2412 O O   . THR   A 1  315 ? 8.98838   15.08866 42.80064 1.000 60.28660  ? 315 THR   A O   1 
ATOM   2413 C CB  . THR   A 1  315 ? 9.30768   14.57968 39.36489 1.000 53.04515  ? 315 THR   A CB  1 
ATOM   2414 O OG1 . THR   A 1  315 ? 10.61804  14.07336 39.08266 1.000 55.86002  ? 315 THR   A OG1 1 
ATOM   2415 C CG2 . THR   A 1  315 ? 9.37230   16.09054 39.46085 1.000 46.24514  ? 315 THR   A CG2 1 
ATOM   2416 N N   . GLN   A 1  316 ? 10.88469  14.34008 41.86143 1.000 54.44853  ? 316 GLN   A N   1 
ATOM   2417 C CA  . GLN   A 1  316 ? 11.70571  14.73846 42.99443 1.000 53.86546  ? 316 GLN   A CA  1 
ATOM   2418 C C   . GLN   A 1  316 ? 12.15897  16.16776 42.80181 1.000 54.21151  ? 316 GLN   A C   1 
ATOM   2419 O O   . GLN   A 1  316 ? 12.43025  16.59860 41.67543 1.000 58.84106  ? 316 GLN   A O   1 
ATOM   2420 C CB  . GLN   A 1  316 ? 12.92126  13.81763 43.15231 1.000 54.00861  ? 316 GLN   A CB  1 
ATOM   2421 C CG  . GLN   A 1  316 ? 12.58577  12.31299 43.28405 1.000 54.41703  ? 316 GLN   A CG  1 
ATOM   2422 C CD  . GLN   A 1  316 ? 12.23072  11.64600 41.94030 1.000 55.44719  ? 316 GLN   A CD  1 
ATOM   2423 O OE1 . GLN   A 1  316 ? 12.77599  11.97702 40.88118 1.000 57.38847  ? 316 GLN   A OE1 1 
ATOM   2424 N NE2 . GLN   A 1  316 ? 11.30779  10.71527 41.99095 1.000 62.05502  ? 316 GLN   A NE2 1 
ATOM   2425 N N   . ILE   A 1  317 ? 12.24310  16.90815 43.89823 1.000 47.38100  ? 317 ILE   A N   1 
ATOM   2426 C CA  . ILE   A 1  317 ? 12.76315  18.26314 43.80910 1.000 52.91781  ? 317 ILE   A CA  1 
ATOM   2427 C C   . ILE   A 1  317 ? 13.92100  18.42583 44.77990 1.000 56.02329  ? 317 ILE   A C   1 
ATOM   2428 O O   . ILE   A 1  317 ? 14.00092  17.76364 45.82299 1.000 56.14522  ? 317 ILE   A O   1 
ATOM   2429 C CB  . ILE   A 1  317 ? 11.69880  19.34929 44.07543 1.000 52.06495  ? 317 ILE   A CB  1 
ATOM   2430 C CG1 . ILE   A 1  317 ? 11.04100  19.12768 45.43334 1.000 51.25554  ? 317 ILE   A CG1 1 
ATOM   2431 C CG2 . ILE   A 1  317 ? 10.68213  19.43817 42.91620 1.000 48.92102  ? 317 ILE   A CG2 1 
ATOM   2432 C CD1 . ILE   A 1  317 ? 10.25420  20.34112 45.90343 1.000 59.32510  ? 317 ILE   A CD1 1 
ATOM   2433 N N   . LEU   A 1  318 ? 14.82536  19.32541 44.41387 1.000 54.42438  ? 318 LEU   A N   1 
ATOM   2434 C CA  . LEU   A 1  318 ? 15.92461  19.76391 45.25545 1.000 51.57905  ? 318 LEU   A CA  1 
ATOM   2435 C C   . LEU   A 1  318 ? 15.78890  21.27416 45.40314 1.000 50.31351  ? 318 LEU   A C   1 
ATOM   2436 O O   . LEU   A 1  318 ? 15.84936  22.00731 44.40325 1.000 53.34168  ? 318 LEU   A O   1 
ATOM   2437 C CB  . LEU   A 1  318 ? 17.26554  19.36193 44.63127 1.000 51.50731  ? 318 LEU   A CB  1 
ATOM   2438 C CG  . LEU   A 1  318 ? 18.51427  19.26368 45.50434 1.000 52.73936  ? 318 LEU   A CG  1 
ATOM   2439 C CD1 . LEU   A 1  318 ? 19.63114  18.58543 44.73812 1.000 54.72321  ? 318 LEU   A CD1 1 
ATOM   2440 C CD2 . LEU   A 1  318 ? 18.96995  20.64419 45.94115 1.000 55.51834  ? 318 LEU   A CD2 1 
ATOM   2441 N N   . VAL   A 1  319 ? 15.59126  21.73662 46.64171 1.000 50.82042  ? 319 VAL   A N   1 
ATOM   2442 C CA  . VAL   A 1  319 ? 15.31672  23.14491 46.92993 1.000 49.20853  ? 319 VAL   A CA  1 
ATOM   2443 C C   . VAL   A 1  319 ? 16.27299  23.63301 48.01334 1.000 51.91312  ? 319 VAL   A C   1 
ATOM   2444 O O   . VAL   A 1  319 ? 16.67535  22.86537 48.89635 1.000 55.89631  ? 319 VAL   A O   1 
ATOM   2445 C CB  . VAL   A 1  319 ? 13.85011  23.34512 47.38185 1.000 52.18923  ? 319 VAL   A CB  1 
ATOM   2446 C CG1 . VAL   A 1  319 ? 13.53268  24.81987 47.63126 1.000 47.17765  ? 319 VAL   A CG1 1 
ATOM   2447 C CG2 . VAL   A 1  319 ? 12.87456  22.71701 46.39259 1.000 53.86481  ? 319 VAL   A CG2 1 
ATOM   2448 N N   . GLY   A 1  320 ? 16.63746  24.91292 47.95068 1.000 50.91849  ? 320 GLY   A N   1 
ATOM   2449 C CA  . GLY   A 1  320 ? 17.45478  25.49126 49.00399 1.000 50.64519  ? 320 GLY   A CA  1 
ATOM   2450 C C   . GLY   A 1  320 ? 17.58276  26.99826 48.89313 1.000 52.36151  ? 320 GLY   A C   1 
ATOM   2451 O O   . GLY   A 1  320 ? 17.10268  27.62657 47.94391 1.000 52.75681  ? 320 GLY   A O   1 
ATOM   2452 N N   . VAL   A 1  321 ? 18.25795  27.57462 49.89010 1.000 48.81575  ? 321 VAL   A N   1 
ATOM   2453 C CA  . VAL   A 1  321 ? 18.39701  29.02164 50.02741 1.000 54.61762  ? 321 VAL   A CA  1 
ATOM   2454 C C   . VAL   A 1  321 ? 19.74112  29.30096 50.68716 1.000 54.86370  ? 321 VAL   A C   1 
ATOM   2455 O O   . VAL   A 1  321 ? 20.39497  28.40588 51.23217 1.000 58.14352  ? 321 VAL   A O   1 
ATOM   2456 C CB  . VAL   A 1  321 ? 17.26810  29.65951 50.87096 1.000 52.91206  ? 321 VAL   A CB  1 
ATOM   2457 C CG1 . VAL   A 1  321 ? 15.91665  29.57125 50.15668 1.000 49.66760  ? 321 VAL   A CG1 1 
ATOM   2458 C CG2 . VAL   A 1  321 ? 17.22768  28.99476 52.25921 1.000 51.67427  ? 321 VAL   A CG2 1 
ATOM   2459 N N   . ASN   A 1  322 ? 20.15337  30.55713 50.63534 1.000 54.27778  ? 322 ASN   A N   1 
ATOM   2460 C CA  . ASN   A 1  322 ? 21.39244  30.99968 51.24607 1.000 53.46960  ? 322 ASN   A CA  1 
ATOM   2461 C C   . ASN   A 1  322 ? 21.08676  31.72882 52.55006 1.000 57.38937  ? 322 ASN   A C   1 
ATOM   2462 O O   . ASN   A 1  322 ? 19.96979  32.22196 52.77805 1.000 52.16739  ? 322 ASN   A O   1 
ATOM   2463 C CB  . ASN   A 1  322 ? 22.17947  31.89994 50.27861 1.000 52.57706  ? 322 ASN   A CB  1 
ATOM   2464 C CG  . ASN   A 1  322 ? 22.52201  31.18484 48.96510 1.000 55.71671  ? 322 ASN   A CG  1 
ATOM   2465 O OD1 . ASN   A 1  322 ? 22.32829  29.97740 48.85469 1.000 60.02411  ? 322 ASN   A OD1 1 
ATOM   2466 N ND2 . ASN   A 1  322 ? 23.03376  31.91796 47.98131 1.000 47.98047  ? 322 ASN   A ND2 1 
ATOM   2467 N N   . LYS   A 1  323 ? 22.10824  31.77766 53.41058 1.000 53.07815  ? 323 LYS   A N   1 
ATOM   2468 C CA  . LYS   A 1  323 ? 21.96550  32.33473 54.75724 1.000 57.29381  ? 323 LYS   A CA  1 
ATOM   2469 C C   . LYS   A 1  323 ? 21.59977  33.82035 54.72783 1.000 59.07317  ? 323 LYS   A C   1 
ATOM   2470 O O   . LYS   A 1  323 ? 20.80395  34.28121 55.55306 1.000 59.28882  ? 323 LYS   A O   1 
ATOM   2471 C CB  . LYS   A 1  323 ? 23.26815  32.11499 55.53555 1.000 61.86355  ? 323 LYS   A CB  1 
ATOM   2472 C CG  . LYS   A 1  323 ? 23.31372  32.67427 56.96815 1.000 62.09146  ? 323 LYS   A CG  1 
ATOM   2473 C CD  . LYS   A 1  323 ? 24.55402  32.14167 57.70786 1.000 56.85197  ? 323 LYS   A CD  1 
ATOM   2474 C CE  . LYS   A 1  323 ? 25.31719  33.25831 58.41139 1.000 72.59781  ? 323 LYS   A CE  1 
ATOM   2475 N NZ  . LYS   A 1  323 ? 24.83508  33.42638 59.80913 1.000 76.97710  ? 323 LYS   A NZ  1 
ATOM   2476 N N   . ASP   A 1  324 ? 22.19347  34.59421 53.80955 1.000 53.51533  ? 324 ASP   A N   1 
ATOM   2477 C CA  . ASP   A 1  324 ? 21.93836  36.03134 53.76554 1.000 56.11475  ? 324 ASP   A CA  1 
ATOM   2478 C C   . ASP   A 1  324 ? 21.34523  36.47398 52.42536 1.000 57.28813  ? 324 ASP   A C   1 
ATOM   2479 O O   . ASP   A 1  324 ? 21.88601  37.37084 51.76878 1.000 58.18710  ? 324 ASP   A O   1 
ATOM   2480 C CB  . ASP   A 1  324 ? 23.22752  36.81541 54.05423 1.000 59.13580  ? 324 ASP   A CB  1 
ATOM   2481 C CG  . ASP   A 1  324 ? 23.79566  36.56132 55.46695 1.000 63.13391  ? 324 ASP   A CG  1 
ATOM   2482 O OD1 . ASP   A 1  324 ? 23.25464  37.10261 56.46153 1.000 59.02648  ? 324 ASP   A OD1 1 
ATOM   2483 O OD2 . ASP   A 1  324 ? 24.81025  35.83505 55.57620 1.000 59.54611  ? 324 ASP   A OD2 1 
ATOM   2484 N N   . GLU   A 1  325 ? 20.22340  35.85682 52.02822 1.000 55.62370  ? 325 GLU   A N   1 
ATOM   2485 C CA  . GLU   A 1  325 ? 19.52130  36.22389 50.79553 1.000 54.09377  ? 325 GLU   A CA  1 
ATOM   2486 C C   . GLU   A 1  325 ? 19.21698  37.72371 50.70481 1.000 58.22294  ? 325 GLU   A C   1 
ATOM   2487 O O   . GLU   A 1  325 ? 19.32227  38.32907 49.62614 1.000 48.21414  ? 325 GLU   A O   1 
ATOM   2488 C CB  . GLU   A 1  325 ? 18.20812  35.44552 50.70990 1.000 54.67621  ? 325 GLU   A CB  1 
ATOM   2489 C CG  . GLU   A 1  325 ? 18.38366  33.95394 50.70104 1.000 54.92935  ? 325 GLU   A CG  1 
ATOM   2490 C CD  . GLU   A 1  325 ? 18.73895  33.44916 49.31144 1.000 54.07336  ? 325 GLU   A CD  1 
ATOM   2491 O OE1 . GLU   A 1  325 ? 19.03854  34.28639 48.42023 1.000 47.75376  ? 325 GLU   A OE1 1 
ATOM   2492 O OE2 . GLU   A 1  325 ? 18.74770  32.21962 49.12617 1.000 54.25994  ? 325 GLU   A OE2 1 
ATOM   2493 N N   . GLY   A 1  326 ? 18.80652  38.33257 51.81988 1.000 52.42225  ? 326 GLY   A N   1 
ATOM   2494 C CA  . GLY   A 1  326 ? 18.26360  39.67862 51.75988 1.000 55.62083  ? 326 GLY   A CA  1 
ATOM   2495 C C   . GLY   A 1  326 ? 19.26027  40.82164 51.66128 1.000 57.13432  ? 326 GLY   A C   1 
ATOM   2496 O O   . GLY   A 1  326 ? 18.84284  41.93285 51.32672 1.000 62.42443  ? 326 GLY   A O   1 
ATOM   2497 N N   . THR   A 1  327 ? 20.55557  40.60622 51.92703 1.000 56.68734  ? 327 THR   A N   1 
ATOM   2498 C CA  . THR   A 1  327 ? 21.44153  41.76230 52.10231 1.000 56.55951  ? 327 THR   A CA  1 
ATOM   2499 C C   . THR   A 1  327 ? 21.79444  42.45681 50.78901 1.000 55.57351  ? 327 THR   A C   1 
ATOM   2500 O O   . THR   A 1  327 ? 21.94959  43.68244 50.77491 1.000 62.52209  ? 327 THR   A O   1 
ATOM   2501 C CB  . THR   A 1  327 ? 22.72110  41.35688 52.81508 1.000 53.86181  ? 327 THR   A CB  1 
ATOM   2502 O OG1 . THR   A 1  327 ? 23.38220  40.35367 52.04236 1.000 58.63869  ? 327 THR   A OG1 1 
ATOM   2503 C CG2 . THR   A 1  327 ? 22.41334  40.80402 54.19522 1.000 57.66624  ? 327 THR   A CG2 1 
ATOM   2504 N N   . ALA   A 1  328 ? 21.89529  41.71313 49.68509 1.000 57.76284  ? 328 ALA   A N   1 
ATOM   2505 C CA  . ALA   A 1  328 ? 22.23559  42.31370 48.39487 1.000 59.82248  ? 328 ALA   A CA  1 
ATOM   2506 C C   . ALA   A 1  328 ? 21.32894  43.49436 48.07577 1.000 62.47961  ? 328 ALA   A C   1 
ATOM   2507 O O   . ALA   A 1  328 ? 21.78058  44.51904 47.54906 1.000 62.05828  ? 328 ALA   A O   1 
ATOM   2508 C CB  . ALA   A 1  328 ? 22.13287  41.26667 47.28126 1.000 58.89904  ? 328 ALA   A CB  1 
ATOM   2509 N N   . PHE   A 1  329 ? 20.04944  43.38498 48.42191 1.000 58.29492  ? 329 PHE   A N   1 
ATOM   2510 C CA  . PHE   A 1  329 ? 19.09480  44.42256 48.03613 1.000 63.23640  ? 329 PHE   A CA  1 
ATOM   2511 C C   . PHE   A 1  329 ? 19.18057  45.65589 48.91391 1.000 56.96035  ? 329 PHE   A C   1 
ATOM   2512 O O   . PHE   A 1  329 ? 18.76077  46.72750 48.47723 1.000 61.00135  ? 329 PHE   A O   1 
ATOM   2513 C CB  . PHE   A 1  329 ? 17.67381  43.83807 48.03066 1.000 56.52980  ? 329 PHE   A CB  1 
ATOM   2514 C CG  . PHE   A 1  329 ? 17.58192  42.55445 47.25266 1.000 58.46266  ? 329 PHE   A CG  1 
ATOM   2515 C CD1 . PHE   A 1  329 ? 17.30806  42.56857 45.89039 1.000 65.91827  ? 329 PHE   A CD1 1 
ATOM   2516 C CD2 . PHE   A 1  329 ? 17.85680  41.33881 47.86281 1.000 54.50114  ? 329 PHE   A CD2 1 
ATOM   2517 C CE1 . PHE   A 1  329 ? 17.26611  41.38147 45.15537 1.000 61.99636  ? 329 PHE   A CE1 1 
ATOM   2518 C CE2 . PHE   A 1  329 ? 17.83079  40.15739 47.13577 1.000 56.42951  ? 329 PHE   A CE2 1 
ATOM   2519 C CZ  . PHE   A 1  329 ? 17.53411  40.18524 45.77841 1.000 58.16246  ? 329 PHE   A CZ  1 
ATOM   2520 N N   . LEU   A 1  330 ? 19.76296  45.54727 50.10946 1.000 58.64795  ? 330 LEU   A N   1 
ATOM   2521 C CA  . LEU   A 1  330 ? 19.78259  46.69403 51.01882 1.000 63.61283  ? 330 LEU   A CA  1 
ATOM   2522 C C   . LEU   A 1  330 ? 20.56984  47.87072 50.44803 1.000 63.71752  ? 330 LEU   A C   1 
ATOM   2523 O O   . LEU   A 1  330 ? 20.21770  49.02663 50.68987 1.000 62.96399  ? 330 LEU   A O   1 
ATOM   2524 C CB  . LEU   A 1  330 ? 20.35930  46.27299 52.37365 1.000 64.26335  ? 330 LEU   A CB  1 
ATOM   2525 C CG  . LEU   A 1  330 ? 19.64512  45.09047 53.04576 1.000 66.56943  ? 330 LEU   A CG  1 
ATOM   2526 C CD1 . LEU   A 1  330 ? 20.29099  44.74672 54.36947 1.000 64.57453  ? 330 LEU   A CD1 1 
ATOM   2527 C CD2 . LEU   A 1  330 ? 18.14942  45.38954 53.24488 1.000 59.15564  ? 330 LEU   A CD2 1 
ATOM   2528 N N   . VAL   A 1  331 ? 21.63559  47.60763 49.68655 1.000 65.83557  ? 331 VAL   A N   1 
ATOM   2529 C CA  . VAL   A 1  331 ? 22.46373  48.69758 49.18356 1.000 65.68137  ? 331 VAL   A CA  1 
ATOM   2530 C C   . VAL   A 1  331 ? 21.96529  49.24328 47.85661 1.000 67.29490  ? 331 VAL   A C   1 
ATOM   2531 O O   . VAL   A 1  331 ? 22.58854  50.15786 47.30851 1.000 70.66882  ? 331 VAL   A O   1 
ATOM   2532 C CB  . VAL   A 1  331 ? 23.94530  48.26895 49.07269 1.000 71.78147  ? 331 VAL   A CB  1 
ATOM   2533 C CG1 . VAL   A 1  331 ? 24.49843  47.95776 50.45677 1.000 70.71602  ? 331 VAL   A CG1 1 
ATOM   2534 C CG2 . VAL   A 1  331 ? 24.11100  47.05425 48.12889 1.000 65.14402  ? 331 VAL   A CG2 1 
ATOM   2535 N N   . TYR   A 1  332 ? 20.85467  48.72092 47.32641 1.000 71.72226  ? 332 TYR   A N   1 
ATOM   2536 C CA  . TYR   A 1  332 ? 20.21488  49.26549 46.13295 1.000 63.42689  ? 332 TYR   A CA  1 
ATOM   2537 C C   . TYR   A 1  332 ? 19.03463  50.16399 46.47214 1.000 74.52635  ? 332 TYR   A C   1 
ATOM   2538 O O   . TYR   A 1  332 ? 18.08254  50.25611 45.68938 1.000 76.24386  ? 332 TYR   A O   1 
ATOM   2539 C CB  . TYR   A 1  332 ? 19.75402  48.14367 45.21025 1.000 65.33166  ? 332 TYR   A CB  1 
ATOM   2540 C CG  . TYR   A 1  332 ? 20.85712  47.51379 44.42087 1.000 69.69669  ? 332 TYR   A CG  1 
ATOM   2541 C CD1 . TYR   A 1  332 ? 21.59957  46.45634 44.94615 1.000 64.69044  ? 332 TYR   A CD1 1 
ATOM   2542 C CD2 . TYR   A 1  332 ? 21.17545  47.98134 43.15061 1.000 65.36459  ? 332 TYR   A CD2 1 
ATOM   2543 C CE1 . TYR   A 1  332 ? 22.61522  45.87183 44.21777 1.000 61.17509  ? 332 TYR   A CE1 1 
ATOM   2544 C CE2 . TYR   A 1  332 ? 22.19049  47.40439 42.41864 1.000 70.19208  ? 332 TYR   A CE2 1 
ATOM   2545 C CZ  . TYR   A 1  332 ? 22.90682  46.34608 42.95503 1.000 70.42638  ? 332 TYR   A CZ  1 
ATOM   2546 O OH  . TYR   A 1  332 ? 23.92550  45.76730 42.23162 1.000 73.82353  ? 332 TYR   A OH  1 
ATOM   2547 N N   . GLY   A 1  333 ? 19.05854  50.81890 47.63132 1.000 75.97593  ? 333 GLY   A N   1 
ATOM   2548 C CA  . GLY   A 1  333 ? 17.95638  51.69840 47.96838 1.000 73.40443  ? 333 GLY   A CA  1 
ATOM   2549 C C   . GLY   A 1  333 ? 17.76497  52.06673 49.43086 1.000 77.01728  ? 333 GLY   A C   1 
ATOM   2550 O O   . GLY   A 1  333 ? 17.30412  53.17211 49.72381 1.000 74.92686  ? 333 GLY   A O   1 
ATOM   2551 N N   . ALA   A 1  334 ? 18.10021  51.17040 50.35727 1.000 73.58504  ? 334 ALA   A N   1 
ATOM   2552 C CA  . ALA   A 1  334 ? 17.78864  51.41839 51.75846 1.000 69.49434  ? 334 ALA   A CA  1 
ATOM   2553 C C   . ALA   A 1  334 ? 18.66744  52.53681 52.31771 1.000 72.34039  ? 334 ALA   A C   1 
ATOM   2554 O O   . ALA   A 1  334 ? 19.86011  52.61323 52.00351 1.000 73.77472  ? 334 ALA   A O   1 
ATOM   2555 C CB  . ALA   A 1  334 ? 17.97276  50.14731 52.58428 1.000 70.67588  ? 334 ALA   A CB  1 
ATOM   2556 N N   . PRO   A 1  335 ? 18.11632  53.40601 53.16071 1.000 71.80776  ? 335 PRO   A N   1 
ATOM   2557 C CA  . PRO   A 1  335 ? 18.90936  54.52443 53.68088 1.000 73.00559  ? 335 PRO   A CA  1 
ATOM   2558 C C   . PRO   A 1  335 ? 19.90186  54.06879 54.74244 1.000 72.56645  ? 335 PRO   A C   1 
ATOM   2559 O O   . PRO   A 1  335 ? 19.59465  53.24237 55.60072 1.000 76.26885  ? 335 PRO   A O   1 
ATOM   2560 C CB  . PRO   A 1  335 ? 17.84649  55.47354 54.26053 1.000 67.52633  ? 335 PRO   A CB  1 
ATOM   2561 C CG  . PRO   A 1  335 ? 16.70200  54.55528 54.67323 1.000 73.08507  ? 335 PRO   A CG  1 
ATOM   2562 C CD  . PRO   A 1  335 ? 16.73747  53.37796 53.69879 1.000 72.93555  ? 335 PRO   A CD  1 
ATOM   2563 N N   . GLY   A 1  336 ? 21.10946  54.62383 54.67601 1.000 78.67704  ? 336 GLY   A N   1 
ATOM   2564 C CA  . GLY   A 1  336 ? 22.15858  54.29862 55.61391 1.000 71.23767  ? 336 GLY   A CA  1 
ATOM   2565 C C   . GLY   A 1  336 ? 23.00573  53.11282 55.23223 1.000 72.38752  ? 336 GLY   A C   1 
ATOM   2566 O O   . GLY   A 1  336 ? 23.96089  52.80110 55.95276 1.000 75.03684  ? 336 GLY   A O   1 
ATOM   2567 N N   . PHE   A 1  337 ? 22.69722  52.44478 54.12544 1.000 72.22348  ? 337 PHE   A N   1 
ATOM   2568 C CA  . PHE   A 1  337 ? 23.41831  51.25243 53.71095 1.000 73.48567  ? 337 PHE   A CA  1 
ATOM   2569 C C   . PHE   A 1  337 ? 24.45833  51.59700 52.65097 1.000 74.13472  ? 337 PHE   A C   1 
ATOM   2570 O O   . PHE   A 1  337 ? 24.23665  52.46426 51.80135 1.000 70.32460  ? 337 PHE   A O   1 
ATOM   2571 C CB  . PHE   A 1  337 ? 22.44618  50.19500 53.19281 1.000 69.98372  ? 337 PHE   A CB  1 
ATOM   2572 C CG  . PHE   A 1  337 ? 21.71412  49.48014 54.28719 1.000 73.25917  ? 337 PHE   A CG  1 
ATOM   2573 C CD1 . PHE   A 1  337 ? 22.16830  48.26326 54.76906 1.000 66.62146  ? 337 PHE   A CD1 1 
ATOM   2574 C CD2 . PHE   A 1  337 ? 20.59096  50.04567 54.86860 1.000 73.52858  ? 337 PHE   A CD2 1 
ATOM   2575 C CE1 . PHE   A 1  337 ? 21.50329  47.61457 55.80085 1.000 69.92109  ? 337 PHE   A CE1 1 
ATOM   2576 C CE2 . PHE   A 1  337 ? 19.91671  49.39112 55.89799 1.000 74.69645  ? 337 PHE   A CE2 1 
ATOM   2577 C CZ  . PHE   A 1  337 ? 20.37422  48.17632 56.36187 1.000 65.72803  ? 337 PHE   A CZ  1 
ATOM   2578 N N   . SER   A 1  338 ? 25.60360  50.92442 52.72144 1.000 73.74285  ? 338 SER   A N   1 
ATOM   2579 C CA  . SER   A 1  338 ? 26.66757  51.13255 51.74842 1.000 73.45199  ? 338 SER   A CA  1 
ATOM   2580 C C   . SER   A 1  338 ? 27.51941  49.87960 51.71704 1.000 72.78412  ? 338 SER   A C   1 
ATOM   2581 O O   . SER   A 1  338 ? 27.82395  49.30678 52.76587 1.000 75.48314  ? 338 SER   A O   1 
ATOM   2582 C CB  . SER   A 1  338 ? 27.53837  52.35271 52.08438 1.000 72.93396  ? 338 SER   A CB  1 
ATOM   2583 O OG  . SER   A 1  338 ? 28.68140  52.42177 51.24187 1.000 75.09125  ? 338 SER   A OG  1 
ATOM   2584 N N   . LYS   A 1  339 ? 27.88643  49.44811 50.51514 1.000 72.30144  ? 339 LYS   A N   1 
ATOM   2585 C CA  . LYS   A 1  339 ? 28.86565  48.38045 50.42349 1.000 69.37941  ? 339 LYS   A CA  1 
ATOM   2586 C C   . LYS   A 1  339 ? 30.25853  48.81296 50.90304 1.000 70.18848  ? 339 LYS   A C   1 
ATOM   2587 O O   . LYS   A 1  339 ? 31.11009  47.94460 51.12537 1.000 72.91087  ? 339 LYS   A O   1 
ATOM   2588 C CB  . LYS   A 1  339 ? 28.92412  47.86506 48.98266 1.000 67.23302  ? 339 LYS   A CB  1 
ATOM   2589 C CG  . LYS   A 1  339 ? 29.71642  48.75281 48.01721 1.000 69.22550  ? 339 LYS   A CG  1 
ATOM   2590 C CD  . LYS   A 1  339 ? 30.09405  48.00816 46.73251 1.000 69.76240  ? 339 LYS   A CD  1 
ATOM   2591 C CE  . LYS   A 1  339 ? 31.06566  48.82631 45.87553 1.000 68.09297  ? 339 LYS   A CE  1 
ATOM   2592 N NZ  . LYS   A 1  339 ? 32.40604  48.99179 46.52573 1.000 69.88457  ? 339 LYS   A NZ  1 
ATOM   2593 N N   . ASP   A 1  340 ? 30.50505  50.11571 51.08592 1.000 66.10091  ? 340 ASP   A N   1 
ATOM   2594 C CA  . ASP   A 1  340 ? 31.82519  50.64453 51.43410 1.000 72.73054  ? 340 ASP   A CA  1 
ATOM   2595 C C   . ASP   A 1  340 ? 31.93181  51.09341 52.89046 1.000 72.04059  ? 340 ASP   A C   1 
ATOM   2596 O O   . ASP   A 1  340 ? 32.88470  51.79004 53.23999 1.000 69.73504  ? 340 ASP   A O   1 
ATOM   2597 C CB  . ASP   A 1  340 ? 32.19460  51.80743 50.50727 1.000 62.86654  ? 340 ASP   A CB  1 
ATOM   2598 C CG  . ASP   A 1  340 ? 32.25817  51.38294 49.05288 1.000 71.78780  ? 340 ASP   A CG  1 
ATOM   2599 O OD1 . ASP   A 1  340 ? 32.83013  50.30618 48.77714 1.000 66.18802  ? 340 ASP   A OD1 1 
ATOM   2600 O OD2 . ASP   A 1  340 ? 31.70514  52.10180 48.19099 1.000 72.67175  ? 340 ASP   A OD2 1 
ATOM   2601 N N   . ASN   A 1  341 ? 30.97607  50.71969 53.73871 1.000 70.00723  ? 341 ASN   A N   1 
ATOM   2602 C CA  . ASN   A 1  341 ? 31.09220  50.87974 55.18450 1.000 71.23626  ? 341 ASN   A CA  1 
ATOM   2603 C C   . ASN   A 1  341 ? 30.20768  49.80928 55.81768 1.000 71.18112  ? 341 ASN   A C   1 
ATOM   2604 O O   . ASN   A 1  341 ? 29.51758  49.05891 55.11520 1.000 67.61871  ? 341 ASN   A O   1 
ATOM   2605 C CB  . ASN   A 1  341 ? 30.75957  52.32827 55.64035 1.000 67.60996  ? 341 ASN   A CB  1 
ATOM   2606 C CG  . ASN   A 1  341 ? 29.27544  52.71810 55.45054 1.000 72.81467  ? 341 ASN   A CG  1 
ATOM   2607 O OD1 . ASN   A 1  341 ? 28.37260  51.86892 55.39051 1.000 71.70568  ? 341 ASN   A OD1 1 
ATOM   2608 N ND2 . ASN   A 1  341 ? 29.03164  54.01948 55.35585 1.000 71.47710  ? 341 ASN   A ND2 1 
ATOM   2609 N N   . ASN   A 1  342 ? 30.23332  49.73040 57.15139 1.000 68.10739  ? 342 ASN   A N   1 
ATOM   2610 C CA  . ASN   A 1  342 ? 29.56860  48.61261 57.82313 1.000 73.99502  ? 342 ASN   A CA  1 
ATOM   2611 C C   . ASN   A 1  342 ? 28.06932  48.82383 58.02571 1.000 73.59966  ? 342 ASN   A C   1 
ATOM   2612 O O   . ASN   A 1  342 ? 27.41819  47.93372 58.57641 1.000 69.88766  ? 342 ASN   A O   1 
ATOM   2613 C CB  . ASN   A 1  342 ? 30.23133  48.30303 59.17259 1.000 71.79261  ? 342 ASN   A CB  1 
ATOM   2614 C CG  . ASN   A 1  342 ? 30.16714  49.46883 60.15065 1.000 80.70291  ? 342 ASN   A CG  1 
ATOM   2615 O OD1 . ASN   A 1  342 ? 29.53262  50.49887 59.89228 1.000 79.28710  ? 342 ASN   A OD1 1 
ATOM   2616 N ND2 . ASN   A 1  342 ? 30.82838  49.30498 61.29180 1.000 90.80374  ? 342 ASN   A ND2 1 
ATOM   2617 N N   . SER   A 1  343 ? 27.51464  49.97233 57.62250 1.000 68.59998  ? 343 SER   A N   1 
ATOM   2618 C CA  . SER   A 1  343 ? 26.06910  50.11281 57.44507 1.000 71.87079  ? 343 SER   A CA  1 
ATOM   2619 C C   . SER   A 1  343 ? 25.30830  49.92353 58.75798 1.000 72.70340  ? 343 SER   A C   1 
ATOM   2620 O O   . SER   A 1  343 ? 24.22255  49.34178 58.78946 1.000 71.63583  ? 343 SER   A O   1 
ATOM   2621 C CB  . SER   A 1  343 ? 25.56306  49.14235 56.37449 1.000 67.86572  ? 343 SER   A CB  1 
ATOM   2622 O OG  . SER   A 1  343 ? 25.97554  49.56940 55.09186 1.000 69.30056  ? 343 SER   A OG  1 
ATOM   2623 N N   . ILE   A 1  344 ? 25.88993  50.41077 59.84987 1.000 70.34374  ? 344 ILE   A N   1 
ATOM   2624 C CA  . ILE   A 1  344 ? 25.21396  50.45581 61.14219 1.000 74.60689  ? 344 ILE   A CA  1 
ATOM   2625 C C   . ILE   A 1  344 ? 24.06586  51.45165 61.03175 1.000 77.23328  ? 344 ILE   A C   1 
ATOM   2626 O O   . ILE   A 1  344 ? 24.29471  52.66046 60.95692 1.000 82.62227  ? 344 ILE   A O   1 
ATOM   2627 C CB  . ILE   A 1  344 ? 26.17771  50.85605 62.26591 1.000 79.28801  ? 344 ILE   A CB  1 
ATOM   2628 C CG1 . ILE   A 1  344 ? 27.22863  49.75899 62.49368 1.000 80.37564  ? 344 ILE   A CG1 1 
ATOM   2629 C CG2 . ILE   A 1  344 ? 25.40266  51.18101 63.54109 1.000 69.81818  ? 344 ILE   A CG2 1 
ATOM   2630 C CD1 . ILE   A 1  344 ? 26.64480  48.43607 62.92015 1.000 76.61779  ? 344 ILE   A CD1 1 
ATOM   2631 N N   . ILE   A 1  345 ? 22.83452  50.96450 61.03355 1.000 74.35543  ? 345 ILE   A N   1 
ATOM   2632 C CA  . ILE   A 1  345 ? 21.69163  51.84352 60.88674 1.000 75.30883  ? 345 ILE   A CA  1 
ATOM   2633 C C   . ILE   A 1  345 ? 20.95670  51.96390 62.21311 1.000 77.25065  ? 345 ILE   A C   1 
ATOM   2634 O O   . ILE   A 1  345 ? 21.04736  51.10677 63.09720 1.000 80.03689  ? 345 ILE   A O   1 
ATOM   2635 C CB  . ILE   A 1  345 ? 20.74500  51.36966 59.77678 1.000 74.14899  ? 345 ILE   A CB  1 
ATOM   2636 C CG1 . ILE   A 1  345 ? 20.35762  49.90552 59.99066 1.000 74.65106  ? 345 ILE   A CG1 1 
ATOM   2637 C CG2 . ILE   A 1  345 ? 21.40796  51.56953 58.42499 1.000 73.64027  ? 345 ILE   A CG2 1 
ATOM   2638 C CD1 . ILE   A 1  345 ? 19.04465  49.54485 59.35354 1.000 67.79543  ? 345 ILE   A CD1 1 
ATOM   2639 N N   . THR   A 1  346 ? 20.21157  53.05272 62.34121 1.000 74.63570  ? 346 THR   A N   1 
ATOM   2640 C CA  . THR   A 1  346 ? 19.39083  53.31354 63.51168 1.000 75.42275  ? 346 THR   A CA  1 
ATOM   2641 C C   . THR   A 1  346 ? 17.97640  52.74164 63.34231 1.000 79.82034  ? 346 THR   A C   1 
ATOM   2642 O O   . THR   A 1  346 ? 17.58325  52.25780 62.27437 1.000 79.75349  ? 346 THR   A O   1 
ATOM   2643 C CB  . THR   A 1  346 ? 19.31321  54.81306 63.75833 1.000 82.09274  ? 346 THR   A CB  1 
ATOM   2644 O OG1 . THR   A 1  346 ? 18.69005  55.42153 62.62197 1.000 81.90350  ? 346 THR   A OG1 1 
ATOM   2645 C CG2 . THR   A 1  346 ? 20.71285  55.41682 63.96095 1.000 76.23309  ? 346 THR   A CG2 1 
ATOM   2646 N N   . ARG   A 1  347 ? 17.20647  52.80768 64.43146 1.000 80.47888  ? 347 ARG   A N   1 
ATOM   2647 C CA  . ARG   A 1  347 ? 15.79947  52.41594 64.39415 1.000 78.83781  ? 347 ARG   A CA  1 
ATOM   2648 C C   . ARG   A 1  347 ? 15.04806  53.16260 63.29731 1.000 77.88408  ? 347 ARG   A C   1 
ATOM   2649 O O   . ARG   A 1  347 ? 14.34985  52.55845 62.47474 1.000 79.57671  ? 347 ARG   A O   1 
ATOM   2650 C CB  . ARG   A 1  347 ? 15.16549  52.67211 65.76308 1.000 77.87403  ? 347 ARG   A CB  1 
ATOM   2651 C CG  . ARG   A 1  347 ? 13.64828  52.55992 65.82044 1.000 78.54680  ? 347 ARG   A CG  1 
ATOM   2652 C CD  . ARG   A 1  347 ? 13.19434  52.34090 67.26874 1.000 82.33264  ? 347 ARG   A CD  1 
ATOM   2653 N NE  . ARG   A 1  347 ? 11.75380  52.14894 67.41013 1.000 92.46775  ? 347 ARG   A NE  1 
ATOM   2654 C CZ  . ARG   A 1  347 ? 11.14398  50.96820 67.41896 1.000 91.64679  ? 347 ARG   A CZ  1 
ATOM   2655 N NH1 . ARG   A 1  347 ? 11.81329  49.83714 67.23373 1.000 85.80017  ? 347 ARG   A NH1 1 
ATOM   2656 N NH2 . ARG   A 1  347 ? 9.82760   50.92033 67.60942 1.000 91.24222  ? 347 ARG   A NH2 1 
ATOM   2657 N N   . LYS   A 1  348 ? 15.20774  54.48248 63.25649 1.000 81.12176  ? 348 LYS   A N   1 
ATOM   2658 C CA  . LYS   A 1  348 ? 14.52432  55.30638 62.26616 1.000 79.35446  ? 348 LYS   A CA  1 
ATOM   2659 C C   . LYS   A 1  348 ? 14.95403  54.96476 60.84572 1.000 78.00728  ? 348 LYS   A C   1 
ATOM   2660 O O   . LYS   A 1  348 ? 14.12804  54.99844 59.92402 1.000 72.50748  ? 348 LYS   A O   1 
ATOM   2661 C CB  . LYS   A 1  348 ? 14.75725  56.78492 62.58701 1.000 84.76595  ? 348 LYS   A CB  1 
ATOM   2662 C CG  . LYS   A 1  348 ? 14.82898  57.05982 64.09681 1.000 92.99482  ? 348 LYS   A CG  1 
ATOM   2663 C CD  . LYS   A 1  348 ? 16.23034  56.79686 64.67930 1.000 96.15030  ? 348 LYS   A CD  1 
ATOM   2664 C CE  . LYS   A 1  348 ? 16.17310  56.42539 66.15330 1.000 93.98292  ? 348 LYS   A CE  1 
ATOM   2665 N NZ  . LYS   A 1  348 ? 17.54210  56.14868 66.67740 1.000 101.67009 ? 348 LYS   A NZ  1 
ATOM   2666 N N   . GLU   A 1  349 ? 16.22678  54.60387 60.65094 1.000 83.49005  ? 349 GLU   A N   1 
ATOM   2667 C CA  . GLU   A 1  349 ? 16.66920  54.15164 59.33540 1.000 75.56815  ? 349 GLU   A CA  1 
ATOM   2668 C C   . GLU   A 1  349 ? 15.98043  52.84799 58.95411 1.000 74.10847  ? 349 GLU   A C   1 
ATOM   2669 O O   . GLU   A 1  349 ? 15.44344  52.71920 57.84526 1.000 74.64071  ? 349 GLU   A O   1 
ATOM   2670 C CB  . GLU   A 1  349 ? 18.19405  54.00800 59.31669 1.000 77.16250  ? 349 GLU   A CB  1 
ATOM   2671 C CG  . GLU   A 1  349 ? 18.90430  55.34741 59.05342 1.000 82.38700  ? 349 GLU   A CG  1 
ATOM   2672 C CD  . GLU   A 1  349 ? 20.32222  55.38953 59.58597 1.000 80.47951  ? 349 GLU   A CD  1 
ATOM   2673 O OE1 . GLU   A 1  349 ? 20.63018  54.63510 60.53419 1.000 83.15933  ? 349 GLU   A OE1 1 
ATOM   2674 O OE2 . GLU   A 1  349 ? 21.12534  56.18527 59.06008 1.000 72.35294  ? 349 GLU   A OE2 1 
ATOM   2675 N N   . PHE   A 1  350 ? 15.96701  51.87887 59.87697 1.000 75.19730  ? 350 PHE   A N   1 
ATOM   2676 C CA  . PHE   A 1  350 ? 15.21227  50.64216 59.67978 1.000 71.08420  ? 350 PHE   A CA  1 
ATOM   2677 C C   . PHE   A 1  350 ? 13.77171  50.92649 59.25658 1.000 71.36482  ? 350 PHE   A C   1 
ATOM   2678 O O   . PHE   A 1  350 ? 13.30279  50.41147 58.23405 1.000 72.76299  ? 350 PHE   A O   1 
ATOM   2679 C CB  . PHE   A 1  350 ? 15.24522  49.80637 60.96329 1.000 72.12457  ? 350 PHE   A CB  1 
ATOM   2680 C CG  . PHE   A 1  350 ? 14.49369  48.49685 60.87425 1.000 69.47227  ? 350 PHE   A CG  1 
ATOM   2681 C CD1 . PHE   A 1  350 ? 15.11112  47.36353 60.36313 1.000 68.30880  ? 350 PHE   A CD1 1 
ATOM   2682 C CD2 . PHE   A 1  350 ? 13.17560  48.39442 61.33099 1.000 69.34408  ? 350 PHE   A CD2 1 
ATOM   2683 C CE1 . PHE   A 1  350 ? 14.42826  46.14725 60.28962 1.000 67.97729  ? 350 PHE   A CE1 1 
ATOM   2684 C CE2 . PHE   A 1  350 ? 12.48446  47.19547 61.26399 1.000 68.74962  ? 350 PHE   A CE2 1 
ATOM   2685 C CZ  . PHE   A 1  350 ? 13.11065  46.06056 60.74159 1.000 67.44096  ? 350 PHE   A CZ  1 
ATOM   2686 N N   . GLN   A 1  351 ? 13.05798  51.76191 60.02248 1.000 73.05979  ? 351 GLN   A N   1 
ATOM   2687 C CA  . GLN   A 1  351 ? 11.66173  52.05644 59.69177 1.000 76.93453  ? 351 GLN   A CA  1 
ATOM   2688 C C   . GLN   A 1  351 ? 11.52843  52.62547 58.28084 1.000 75.55521  ? 351 GLN   A C   1 
ATOM   2689 O O   . GLN   A 1  351 ? 10.65275  52.20715 57.51032 1.000 70.30460  ? 351 GLN   A O   1 
ATOM   2690 C CB  . GLN   A 1  351 ? 11.05984  53.02292 60.71655 1.000 68.55125  ? 351 GLN   A CB  1 
ATOM   2691 C CG  . GLN   A 1  351 ? 10.61835  52.35208 62.00633 1.000 75.64427  ? 351 GLN   A CG  1 
ATOM   2692 C CD  . GLN   A 1  351 ? 10.47966  53.32475 63.16724 1.000 78.76693  ? 351 GLN   A CD  1 
ATOM   2693 O OE1 . GLN   A 1  351 ? 11.14269  54.36369 63.21503 1.000 79.01894  ? 351 GLN   A OE1 1 
ATOM   2694 N NE2 . GLN   A 1  351 ? 9.62506   52.97976 64.12148 1.000 76.98111  ? 351 GLN   A NE2 1 
ATOM   2695 N N   . GLU   A 1  352 ? 12.39780  53.57022 57.91453 1.000 75.64603  ? 352 GLU   A N   1 
ATOM   2696 C CA  . GLU   A 1  352 ? 12.35292  54.08975 56.55289 1.000 75.81608  ? 352 GLU   A CA  1 
ATOM   2697 C C   . GLU   A 1  352 ? 12.67026  53.01163 55.53284 1.000 73.95258  ? 352 GLU   A C   1 
ATOM   2698 O O   . GLU   A 1  352 ? 12.17227  53.06424 54.40331 1.000 75.93492  ? 352 GLU   A O   1 
ATOM   2699 C CB  . GLU   A 1  352 ? 13.31495  55.25968 56.39571 1.000 78.53839  ? 352 GLU   A CB  1 
ATOM   2700 C CG  . GLU   A 1  352 ? 12.74313  56.36299 55.54179 1.000 82.82420  ? 352 GLU   A CG  1 
ATOM   2701 C CD  . GLU   A 1  352 ? 11.78763  57.25187 56.31583 1.000 94.05786  ? 352 GLU   A CD  1 
ATOM   2702 O OE1 . GLU   A 1  352 ? 11.98014  57.39927 57.54050 1.000 98.20021  ? 352 GLU   A OE1 1 
ATOM   2703 O OE2 . GLU   A 1  352 ? 10.85474  57.81953 55.70368 1.000 102.71186 ? 352 GLU   A OE2 1 
ATOM   2704 N N   . GLY   A 1  353 ? 13.47904  52.01925 55.91467 1.000 74.00107  ? 353 GLY   A N   1 
ATOM   2705 C CA  . GLY   A 1  353 ? 13.78561  50.92500 55.00161 1.000 72.50034  ? 353 GLY   A CA  1 
ATOM   2706 C C   . GLY   A 1  353 ? 12.59218  50.04097 54.68471 1.000 70.77376  ? 353 GLY   A C   1 
ATOM   2707 O O   . GLY   A 1  353 ? 12.48724  49.50868 53.57551 1.000 70.10030  ? 353 GLY   A O   1 
ATOM   2708 N N   . LEU   A 1  354 ? 11.68741  49.85094 55.65711 1.000 72.41060  ? 354 LEU   A N   1 
ATOM   2709 C CA  . LEU   A 1  354 ? 10.46245  49.09173 55.39350 1.000 68.70557  ? 354 LEU   A CA  1 
ATOM   2710 C C   . LEU   A 1  354 ? 9.57904   49.81553 54.37973 1.000 71.86965  ? 354 LEU   A C   1 
ATOM   2711 O O   . LEU   A 1  354 ? 8.95327   49.18042 53.51738 1.000 71.05335  ? 354 LEU   A O   1 
ATOM   2712 C CB  . LEU   A 1  354 ? 9.69117   48.84381 56.69069 1.000 69.23879  ? 354 LEU   A CB  1 
ATOM   2713 C CG  . LEU   A 1  354 ? 10.31988  48.00187 57.80534 1.000 69.24275  ? 354 LEU   A CG  1 
ATOM   2714 C CD1 . LEU   A 1  354 ? 9.32951   47.78849 58.94867 1.000 64.31723  ? 354 LEU   A CD1 1 
ATOM   2715 C CD2 . LEU   A 1  354 ? 10.81748  46.66802 57.26481 1.000 64.11909  ? 354 LEU   A CD2 1 
ATOM   2716 N N   . LYS   A 1  355 ? 9.52297   51.14913 54.46205 1.000 71.45013  ? 355 LYS   A N   1 
ATOM   2717 C CA  . LYS   A 1  355 ? 8.76193   51.91667 53.48069 1.000 75.80188  ? 355 LYS   A CA  1 
ATOM   2718 C C   . LYS   A 1  355 ? 9.30187   51.71103 52.06881 1.000 75.74144  ? 355 LYS   A C   1 
ATOM   2719 O O   . LYS   A 1  355 ? 8.52990   51.73687 51.09800 1.000 74.99028  ? 355 LYS   A O   1 
ATOM   2720 C CB  . LYS   A 1  355 ? 8.77238   53.40029 53.85098 1.000 67.51023  ? 355 LYS   A CB  1 
ATOM   2721 C CG  . LYS   A 1  355 ? 7.87246   53.72538 55.02800 1.000 78.88073  ? 355 LYS   A CG  1 
ATOM   2722 C CD  . LYS   A 1  355 ? 7.87158   55.22113 55.39800 1.000 82.25250  ? 355 LYS   A CD  1 
ATOM   2723 C CE  . LYS   A 1  355 ? 7.83477   56.11877 54.16176 1.000 85.24681  ? 355 LYS   A CE  1 
ATOM   2724 N NZ  . LYS   A 1  355 ? 7.80182   57.59398 54.50993 1.000 96.61686  ? 355 LYS   A NZ  1 
ATOM   2725 N N   . ILE   A 1  356 ? 10.61805  51.49210 51.94714 1.000 73.58395  ? 356 ILE   A N   1 
ATOM   2726 C CA  . ILE   A 1  356 ? 11.25391  51.24287 50.65380 1.000 71.93133  ? 356 ILE   A CA  1 
ATOM   2727 C C   . ILE   A 1  356 ? 10.88877  49.85902 50.12298 1.000 75.21561  ? 356 ILE   A C   1 
ATOM   2728 O O   . ILE   A 1  356 ? 10.57738  49.69273 48.93759 1.000 78.86634  ? 356 ILE   A O   1 
ATOM   2729 C CB  . ILE   A 1  356 ? 12.78053  51.38378 50.77558 1.000 75.46964  ? 356 ILE   A CB  1 
ATOM   2730 C CG1 . ILE   A 1  356 ? 13.18512  52.80907 51.15930 1.000 73.47938  ? 356 ILE   A CG1 1 
ATOM   2731 C CG2 . ILE   A 1  356 ? 13.45629  50.94336 49.48033 1.000 73.65370  ? 356 ILE   A CG2 1 
ATOM   2732 C CD1 . ILE   A 1  356 ? 13.30410  53.72205 49.99423 1.000 67.88767  ? 356 ILE   A CD1 1 
ATOM   2733 N N   . PHE   A 1  357 ? 10.96114  48.83767 50.97806 1.000 71.19513  ? 357 PHE   A N   1 
ATOM   2734 C CA  . PHE   A 1  357 ? 10.68550  47.47545 50.54027 1.000 71.78796  ? 357 PHE   A CA  1 
ATOM   2735 C C   . PHE   A 1  357 ? 9.21688   47.07486 50.63926 1.000 62.43948  ? 357 PHE   A C   1 
ATOM   2736 O O   . PHE   A 1  357 ? 8.84001   46.04883 50.06815 1.000 77.22917  ? 357 PHE   A O   1 
ATOM   2737 C CB  . PHE   A 1  357 ? 11.55099  46.48990 51.33644 1.000 71.06641  ? 357 PHE   A CB  1 
ATOM   2738 C CG  . PHE   A 1  357 ? 12.99989  46.48287 50.91665 1.000 68.08900  ? 357 PHE   A CG  1 
ATOM   2739 C CD1 . PHE   A 1  357 ? 13.39503  45.85175 49.74124 1.000 63.09132  ? 357 PHE   A CD1 1 
ATOM   2740 C CD2 . PHE   A 1  357 ? 13.96040  47.14901 51.67702 1.000 67.10327  ? 357 PHE   A CD2 1 
ATOM   2741 C CE1 . PHE   A 1  357 ? 14.73501  45.84905 49.34959 1.000 69.21359  ? 357 PHE   A CE1 1 
ATOM   2742 C CE2 . PHE   A 1  357 ? 15.30865  47.16137 51.28567 1.000 69.02464  ? 357 PHE   A CE2 1 
ATOM   2743 C CZ  . PHE   A 1  357 ? 15.69661  46.50998 50.12214 1.000 64.96996  ? 357 PHE   A CZ  1 
ATOM   2744 N N   . PHE   A 1  358 ? 8.37716   47.84160 51.33136 1.000 69.08104  ? 358 PHE   A N   1 
ATOM   2745 C CA  . PHE   A 1  358 ? 6.94592   47.54352 51.43900 1.000 70.25891  ? 358 PHE   A CA  1 
ATOM   2746 C C   . PHE   A 1  358 ? 6.12657   48.79615 51.14434 1.000 78.59855  ? 358 PHE   A C   1 
ATOM   2747 O O   . PHE   A 1  358 ? 5.33375   49.26041 51.97583 1.000 71.03803  ? 358 PHE   A O   1 
ATOM   2748 C CB  . PHE   A 1  358 ? 6.63888   46.96933 52.81740 1.000 68.30471  ? 358 PHE   A CB  1 
ATOM   2749 C CG  . PHE   A 1  358 ? 7.41376   45.71402 53.11901 1.000 68.98588  ? 358 PHE   A CG  1 
ATOM   2750 C CD1 . PHE   A 1  358 ? 6.91748   44.47791 52.76195 1.000 62.53846  ? 358 PHE   A CD1 1 
ATOM   2751 C CD2 . PHE   A 1  358 ? 8.65974   45.77728 53.73009 1.000 71.15027  ? 358 PHE   A CD2 1 
ATOM   2752 C CE1 . PHE   A 1  358 ? 7.63547   43.32653 53.03280 1.000 63.14546  ? 358 PHE   A CE1 1 
ATOM   2753 C CE2 . PHE   A 1  358 ? 9.38378   44.62796 53.99205 1.000 64.81034  ? 358 PHE   A CE2 1 
ATOM   2754 C CZ  . PHE   A 1  358 ? 8.86673   43.40552 53.64200 1.000 59.84068  ? 358 PHE   A CZ  1 
ATOM   2755 N N   . PRO   A 1  359 ? 6.28097   49.35471 49.93349 1.000 81.23039  ? 359 PRO   A N   1 
ATOM   2756 C CA  . PRO   A 1  359 ? 5.71902   50.68641 49.65940 1.000 79.45855  ? 359 PRO   A CA  1 
ATOM   2757 C C   . PRO   A 1  359 ? 4.21639   50.76312 49.79923 1.000 82.24038  ? 359 PRO   A C   1 
ATOM   2758 O O   . PRO   A 1  359 ? 3.70380   51.73413 50.37387 1.000 81.66320  ? 359 PRO   A O   1 
ATOM   2759 C CB  . PRO   A 1  359 ? 6.15704   50.94875 48.21156 1.000 90.18642  ? 359 PRO   A CB  1 
ATOM   2760 C CG  . PRO   A 1  359 ? 6.33499   49.58926 47.62465 1.000 80.96980  ? 359 PRO   A CG  1 
ATOM   2761 C CD  . PRO   A 1  359 ? 6.91675   48.77702 48.73429 1.000 77.39916  ? 359 PRO   A CD  1 
ATOM   2762 N N   . GLY   A 1  360 ? 3.49096   49.77694 49.27977 1.000 81.50664  ? 360 GLY   A N   1 
ATOM   2763 C CA  . GLY   A 1  360 ? 2.04379   49.83354 49.33286 1.000 82.76328  ? 360 GLY   A CA  1 
ATOM   2764 C C   . GLY   A 1  360 ? 1.45035   49.16605 50.56061 1.000 87.34381  ? 360 GLY   A C   1 
ATOM   2765 O O   . GLY   A 1  360 ? 0.26834   48.81111 50.55739 1.000 88.79697  ? 360 GLY   A O   1 
ATOM   2766 N N   . VAL   A 1  361 ? 2.25016   48.98826 51.62143 1.000 83.04601  ? 361 VAL   A N   1 
ATOM   2767 C CA  . VAL   A 1  361 ? 1.81291   48.29534 52.83328 1.000 79.67984  ? 361 VAL   A CA  1 
ATOM   2768 C C   . VAL   A 1  361 ? 1.39058   49.32577 53.87884 1.000 81.92103  ? 361 VAL   A C   1 
ATOM   2769 O O   . VAL   A 1  361 ? 1.98625   50.40855 53.98916 1.000 84.10685  ? 361 VAL   A O   1 
ATOM   2770 C CB  . VAL   A 1  361 ? 2.91963   47.35263 53.36060 1.000 74.89749  ? 361 VAL   A CB  1 
ATOM   2771 C CG1 . VAL   A 1  361 ? 2.73704   47.02646 54.84264 1.000 72.33397  ? 361 VAL   A CG1 1 
ATOM   2772 C CG2 . VAL   A 1  361 ? 2.95489   46.06891 52.53644 1.000 62.88232  ? 361 VAL   A CG2 1 
ATOM   2773 N N   . SER   A 1  362 ? 0.34030   48.99426 54.62994 1.000 78.53799  ? 362 SER   A N   1 
ATOM   2774 C CA  . SER   A 1  362 ? -0.24664  49.87941 55.62769 1.000 78.56105  ? 362 SER   A CA  1 
ATOM   2775 C C   . SER   A 1  362 ? 0.72784   50.19925 56.75748 1.000 71.62192  ? 362 SER   A C   1 
ATOM   2776 O O   . SER   A 1  362 ? 1.67775   49.46408 57.03246 1.000 78.12056  ? 362 SER   A O   1 
ATOM   2777 C CB  . SER   A 1  362 ? -1.49827  49.23589 56.22671 1.000 76.89498  ? 362 SER   A CB  1 
ATOM   2778 O OG  . SER   A 1  362 ? -1.15796  48.02490 56.90327 1.000 71.01933  ? 362 SER   A OG  1 
ATOM   2779 N N   . GLU   A 1  363 ? 0.44348   51.30143 57.44538 1.000 76.06369  ? 363 GLU   A N   1 
ATOM   2780 C CA  . GLU   A 1  363 ? 1.17508   51.63207 58.66003 1.000 79.98892  ? 363 GLU   A CA  1 
ATOM   2781 C C   . GLU   A 1  363 ? 1.21430   50.44282 59.60582 1.000 76.95657  ? 363 GLU   A C   1 
ATOM   2782 O O   . GLU   A 1  363 ? 2.27108   50.10572 60.15245 1.000 80.97197  ? 363 GLU   A O   1 
ATOM   2783 C CB  . GLU   A 1  363 ? 0.53292   52.84915 59.33413 1.000 70.13866  ? 363 GLU   A CB  1 
ATOM   2784 C CG  . GLU   A 1  363 ? 0.97542   54.12595 58.68760 1.000 82.63948  ? 363 GLU   A CG  1 
ATOM   2785 C CD  . GLU   A 1  363 ? 2.48694   54.13548 58.47398 1.000 97.96442  ? 363 GLU   A CD  1 
ATOM   2786 O OE1 . GLU   A 1  363 ? 3.23325   54.19819 59.47797 1.000 102.82646 ? 363 GLU   A OE1 1 
ATOM   2787 O OE2 . GLU   A 1  363 ? 2.93094   54.02852 57.30311 1.000 89.94055  ? 363 GLU   A OE2 1 
ATOM   2788 N N   . PHE   A 1  364 ? 0.07468   49.76609 59.77277 1.000 73.08452  ? 364 PHE   A N   1 
ATOM   2789 C CA  . PHE   A 1  364 ? -0.00016  48.65229 60.70809 1.000 71.36479  ? 364 PHE   A CA  1 
ATOM   2790 C C   . PHE   A 1  364 ? 0.78489   47.45752 60.20191 1.000 70.44120  ? 364 PHE   A C   1 
ATOM   2791 O O   . PHE   A 1  364 ? 1.42421   46.74871 60.98755 1.000 68.11753  ? 364 PHE   A O   1 
ATOM   2792 C CB  . PHE   A 1  364 ? -1.45471  48.26884 60.94499 1.000 76.08314  ? 364 PHE   A CB  1 
ATOM   2793 C CG  . PHE   A 1  364 ? -1.63301  46.92815 61.60888 1.000 76.63448  ? 364 PHE   A CG  1 
ATOM   2794 C CD1 . PHE   A 1  364 ? -1.57759  46.80895 62.99185 1.000 77.61165  ? 364 PHE   A CD1 1 
ATOM   2795 C CD2 . PHE   A 1  364 ? -1.87455  45.78804 60.85073 1.000 73.40936  ? 364 PHE   A CD2 1 
ATOM   2796 C CE1 . PHE   A 1  364 ? -1.75950  45.58419 63.60871 1.000 76.16563  ? 364 PHE   A CE1 1 
ATOM   2797 C CE2 . PHE   A 1  364 ? -2.04179  44.54775 61.46411 1.000 76.17119  ? 364 PHE   A CE2 1 
ATOM   2798 C CZ  . PHE   A 1  364 ? -1.98561  44.44940 62.84317 1.000 76.93783  ? 364 PHE   A CZ  1 
ATOM   2799 N N   . GLY   A 1  365 ? 0.73018   47.20585 58.89663 1.000 71.16964  ? 365 GLY   A N   1 
ATOM   2800 C CA  . GLY   A 1  365 ? 1.53579   46.13622 58.33217 1.000 69.47211  ? 365 GLY   A CA  1 
ATOM   2801 C C   . GLY   A 1  365 ? 3.02034   46.33446 58.57560 1.000 70.28771  ? 365 GLY   A C   1 
ATOM   2802 O O   . GLY   A 1  365 ? 3.73940   45.38802 58.89994 1.000 68.74480  ? 365 GLY   A O   1 
ATOM   2803 N N   . LYS   A 1  366 ? 3.49636   47.57053 58.43630 1.000 71.24067  ? 366 LYS   A N   1 
ATOM   2804 C CA  . LYS   A 1  366 ? 4.91677   47.82140 58.63099 1.000 71.59383  ? 366 LYS   A CA  1 
ATOM   2805 C C   . LYS   A 1  366 ? 5.27964   47.76508 60.10719 1.000 65.79352  ? 366 LYS   A C   1 
ATOM   2806 O O   . LYS   A 1  366 ? 6.36207   47.29019 60.46436 1.000 67.86562  ? 366 LYS   A O   1 
ATOM   2807 C CB  . LYS   A 1  366 ? 5.30006   49.16689 58.01551 1.000 73.39280  ? 366 LYS   A CB  1 
ATOM   2808 C CG  . LYS   A 1  366 ? 5.19988   49.17682 56.49664 1.000 73.44361  ? 366 LYS   A CG  1 
ATOM   2809 C CD  . LYS   A 1  366 ? 5.56583   50.51884 55.90624 1.000 77.79984  ? 366 LYS   A CD  1 
ATOM   2810 C CE  . LYS   A 1  366 ? 4.50229   51.55466 56.21457 1.000 82.02117  ? 366 LYS   A CE  1 
ATOM   2811 N NZ  . LYS   A 1  366 ? 4.20779   52.33410 54.99680 1.000 84.45519  ? 366 LYS   A NZ  1 
ATOM   2812 N N   . GLU   A 1  367 ? 4.40307   48.26989 60.97819 1.000 67.04746  ? 367 GLU   A N   1 
ATOM   2813 C CA  . GLU   A 1  367 ? 4.64441   48.15161 62.41555 1.000 69.21081  ? 367 GLU   A CA  1 
ATOM   2814 C C   . GLU   A 1  367 ? 4.78478   46.68731 62.82152 1.000 67.79414  ? 367 GLU   A C   1 
ATOM   2815 O O   . GLU   A 1  367 ? 5.59920   46.34166 63.68473 1.000 66.24197  ? 367 GLU   A O   1 
ATOM   2816 C CB  . GLU   A 1  367 ? 3.51176   48.81400 63.19784 1.000 68.01164  ? 367 GLU   A CB  1 
ATOM   2817 C CG  . GLU   A 1  367 ? 3.81589   50.17074 63.80229 1.000 77.98194  ? 367 GLU   A CG  1 
ATOM   2818 C CD  . GLU   A 1  367 ? 2.54196   50.98237 64.07071 1.000 95.30464  ? 367 GLU   A CD  1 
ATOM   2819 O OE1 . GLU   A 1  367 ? 2.23515   51.27526 65.25495 1.000 102.64407 ? 367 GLU   A OE1 1 
ATOM   2820 O OE2 . GLU   A 1  367 ? 1.84315   51.33846 63.08958 1.000 96.34252  ? 367 GLU   A OE2 1 
ATOM   2821 N N   . SER   A 1  368 ? 4.01169   45.80762 62.19131 1.000 64.57691  ? 368 SER   A N   1 
ATOM   2822 C CA  . SER   A 1  368 ? 4.03065   44.40326 62.57845 1.000 67.40130  ? 368 SER   A CA  1 
ATOM   2823 C C   . SER   A 1  368 ? 5.32239   43.71590 62.14118 1.000 67.23377  ? 368 SER   A C   1 
ATOM   2824 O O   . SER   A 1  368 ? 5.83606   42.84002 62.85417 1.000 66.49152  ? 368 SER   A O   1 
ATOM   2825 C CB  . SER   A 1  368 ? 2.81249   43.68576 61.99406 1.000 70.79888  ? 368 SER   A CB  1 
ATOM   2826 O OG  . SER   A 1  368 ? 3.04987   43.34192 60.63714 1.000 69.73320  ? 368 SER   A OG  1 
ATOM   2827 N N   . ILE   A 1  369 ? 5.85209   44.07081 60.96355 1.000 63.85359  ? 369 ILE   A N   1 
ATOM   2828 C CA  . ILE   A 1  369 ? 7.19883   43.62244 60.61260 1.000 63.94304  ? 369 ILE   A CA  1 
ATOM   2829 C C   . ILE   A 1  369 ? 8.18172   44.09727 61.67390 1.000 64.57089  ? 369 ILE   A C   1 
ATOM   2830 O O   . ILE   A 1  369 ? 8.98607   43.31969 62.19780 1.000 66.42556  ? 369 ILE   A O   1 
ATOM   2831 C CB  . ILE   A 1  369 ? 7.60529   44.12153 59.21126 1.000 65.01994  ? 369 ILE   A CB  1 
ATOM   2832 C CG1 . ILE   A 1  369 ? 6.65524   43.60791 58.13161 1.000 62.47083  ? 369 ILE   A CG1 1 
ATOM   2833 C CG2 . ILE   A 1  369 ? 9.04496   43.70473 58.87554 1.000 56.13771  ? 369 ILE   A CG2 1 
ATOM   2834 C CD1 . ILE   A 1  369 ? 6.87662   44.32199 56.78445 1.000 61.49192  ? 369 ILE   A CD1 1 
ATOM   2835 N N   . LEU   A 1  370 ? 8.11711   45.38041 62.02061 1.000 59.08272  ? 370 LEU   A N   1 
ATOM   2836 C CA  . LEU   A 1  370 ? 9.04489   45.90289 63.01541 1.000 71.34534  ? 370 LEU   A CA  1 
ATOM   2837 C C   . LEU   A 1  370 ? 8.94138   45.11742 64.31269 1.000 69.82319  ? 370 LEU   A C   1 
ATOM   2838 O O   . LEU   A 1  370 ? 9.95635   44.78347 64.93138 1.000 72.59019  ? 370 LEU   A O   1 
ATOM   2839 C CB  . LEU   A 1  370 ? 8.78236   47.39063 63.26120 1.000 66.65754  ? 370 LEU   A CB  1 
ATOM   2840 C CG  . LEU   A 1  370 ? 9.56957   48.01104 64.42246 1.000 73.46360  ? 370 LEU   A CG  1 
ATOM   2841 C CD1 . LEU   A 1  370 ? 10.27948  49.25478 63.97354 1.000 73.49637  ? 370 LEU   A CD1 1 
ATOM   2842 C CD2 . LEU   A 1  370 ? 8.66375   48.33154 65.60481 1.000 71.34105  ? 370 LEU   A CD2 1 
ATOM   2843 N N   . PHE   A 1  371 ? 7.72186   44.77201 64.70779 1.000 67.80058  ? 371 PHE   A N   1 
ATOM   2844 C CA  . PHE   A 1  371 ? 7.50056   44.11597 65.99134 1.000 71.55649  ? 371 PHE   A CA  1 
ATOM   2845 C C   . PHE   A 1  371 ? 8.10638   42.71541 66.01815 1.000 68.44252  ? 371 PHE   A C   1 
ATOM   2846 O O   . PHE   A 1  371 ? 8.77487   42.33604 66.98558 1.000 68.83394  ? 371 PHE   A O   1 
ATOM   2847 C CB  . PHE   A 1  371 ? 6.00187   44.05817 66.27307 1.000 71.38145  ? 371 PHE   A CB  1 
ATOM   2848 C CG  . PHE   A 1  371 ? 5.64146   43.27963 67.50483 1.000 81.23046  ? 371 PHE   A CG  1 
ATOM   2849 C CD1 . PHE   A 1  371 ? 5.15298   41.97822 67.40258 1.000 76.17563  ? 371 PHE   A CD1 1 
ATOM   2850 C CD2 . PHE   A 1  371 ? 5.74851   43.85727 68.76726 1.000 82.08389  ? 371 PHE   A CD2 1 
ATOM   2851 C CE1 . PHE   A 1  371 ? 4.80427   41.25819 68.54375 1.000 82.60606  ? 371 PHE   A CE1 1 
ATOM   2852 C CE2 . PHE   A 1  371 ? 5.40587   43.13958 69.91210 1.000 82.56656  ? 371 PHE   A CE2 1 
ATOM   2853 C CZ  . PHE   A 1  371 ? 4.93210   41.84239 69.80107 1.000 82.72291  ? 371 PHE   A CZ  1 
ATOM   2854 N N   . HIS   A 1  372 ? 7.88541   41.93008 64.96263 1.000 66.43424  ? 372 HIS   A N   1 
ATOM   2855 C CA  A HIS   A 1  372 ? 8.37810   40.55131 64.93001 0.521 67.78874  ? 372 HIS   A CA  1 
ATOM   2856 C CA  B HIS   A 1  372 ? 8.37721   40.56024 64.99788 0.479 67.77181  ? 372 HIS   A CA  1 
ATOM   2857 C C   . HIS   A 1  372 ? 9.89843   40.48961 64.84518 1.000 66.86817  ? 372 HIS   A C   1 
ATOM   2858 O O   . HIS   A 1  372 ? 10.51589  39.54648 65.34854 1.000 70.40652  ? 372 HIS   A O   1 
ATOM   2859 C CB  A HIS   A 1  372 ? 7.76088   39.78606 63.75177 0.521 64.92355  ? 372 HIS   A CB  1 
ATOM   2860 C CB  B HIS   A 1  372 ? 7.63673   39.72457 63.94812 0.479 65.07880  ? 372 HIS   A CB  1 
ATOM   2861 C CG  A HIS   A 1  372 ? 8.03003   38.31005 63.78163 0.521 67.40657  ? 372 HIS   A CG  1 
ATOM   2862 C CG  B HIS   A 1  372 ? 6.29017   39.25271 64.41737 0.479 67.21770  ? 372 HIS   A CG  1 
ATOM   2863 N ND1 A HIS   A 1  372 ? 7.18266   37.40836 64.39083 0.521 59.37904  ? 372 HIS   A ND1 1 
ATOM   2864 N ND1 B HIS   A 1  372 ? 5.20403   40.09585 64.53666 0.479 68.68809  ? 372 HIS   A ND1 1 
ATOM   2865 C CD2 A HIS   A 1  372 ? 9.05832   37.58050 63.28296 0.521 66.46378  ? 372 HIS   A CD2 1 
ATOM   2866 C CD2 B HIS   A 1  372 ? 5.87097   38.03982 64.85106 0.479 65.96457  ? 372 HIS   A CD2 1 
ATOM   2867 C CE1 A HIS   A 1  372 ? 7.67985   36.19197 64.27069 0.521 62.82406  ? 372 HIS   A CE1 1 
ATOM   2868 C CE1 B HIS   A 1  372 ? 4.16999   39.41842 65.00038 0.479 66.83348  ? 372 HIS   A CE1 1 
ATOM   2869 N NE2 A HIS   A 1  372 ? 8.81590   36.26822 63.60195 0.521 64.85146  ? 372 HIS   A NE2 1 
ATOM   2870 N NE2 B HIS   A 1  372 ? 4.54731   38.16795 65.19830 0.479 67.26921  ? 372 HIS   A NE2 1 
ATOM   2871 N N   . TYR   A 1  373 ? 10.52810  41.48231 64.22717 1.000 67.68909  ? 373 TYR   A N   1 
ATOM   2872 C CA  . TYR   A 1  373 ? 11.96764  41.43737 63.99386 1.000 63.19166  ? 373 TYR   A CA  1 
ATOM   2873 C C   . TYR   A 1  373 ? 12.79414  42.35516 64.89413 1.000 68.06881  ? 373 TYR   A C   1 
ATOM   2874 O O   . TYR   A 1  373 ? 14.00624  42.43263 64.70200 1.000 70.92771  ? 373 TYR   A O   1 
ATOM   2875 C CB  . TYR   A 1  373 ? 12.26288  41.77938 62.52822 1.000 65.80452  ? 373 TYR   A CB  1 
ATOM   2876 C CG  . TYR   A 1  373 ? 12.05698  40.62242 61.57333 1.000 67.64768  ? 373 TYR   A CG  1 
ATOM   2877 C CD1 . TYR   A 1  373 ? 10.82218  40.40701 60.96609 1.000 59.94332  ? 373 TYR   A CD1 1 
ATOM   2878 C CD2 . TYR   A 1  373 ? 13.10636  39.74216 61.27015 1.000 64.30534  ? 373 TYR   A CD2 1 
ATOM   2879 C CE1 . TYR   A 1  373 ? 10.63426  39.34319 60.08075 1.000 60.16676  ? 373 TYR   A CE1 1 
ATOM   2880 C CE2 . TYR   A 1  373 ? 12.92407  38.66727 60.39285 1.000 57.76997  ? 373 TYR   A CE2 1 
ATOM   2881 C CZ  . TYR   A 1  373 ? 11.69174  38.47888 59.79932 1.000 62.08066  ? 373 TYR   A CZ  1 
ATOM   2882 O OH  . TYR   A 1  373 ? 11.51452  37.41422 58.94175 1.000 62.23500  ? 373 TYR   A OH  1 
ATOM   2883 N N   . THR   A 1  374 ? 12.20452  43.07017 65.85447 1.000 72.55747  ? 374 THR   A N   1 
ATOM   2884 C CA  . THR   A 1  374 ? 13.02573  43.89804 66.74224 1.000 78.34853  ? 374 THR   A CA  1 
ATOM   2885 C C   . THR   A 1  374 ? 12.89712  43.48540 68.20150 1.000 80.97650  ? 374 THR   A C   1 
ATOM   2886 O O   . THR   A 1  374 ? 13.09863  44.29841 69.10454 1.000 83.57430  ? 374 THR   A O   1 
ATOM   2887 C CB  . THR   A 1  374 ? 12.72620  45.39405 66.59614 1.000 76.87762  ? 374 THR   A CB  1 
ATOM   2888 O OG1 . THR   A 1  374 ? 11.37448  45.67828 66.99362 1.000 82.63020  ? 374 THR   A OG1 1 
ATOM   2889 C CG2 . THR   A 1  374 ? 12.98199  45.85953 65.17161 1.000 72.32076  ? 374 THR   A CG2 1 
ATOM   2890 N N   . ASP   A 1  375 ? 12.57577  42.22522 68.45186 1.000 83.66642  ? 375 ASP   A N   1 
ATOM   2891 C CA  . ASP   A 1  375 ? 12.70920  41.67947 69.79613 1.000 88.02732  ? 375 ASP   A CA  1 
ATOM   2892 C C   . ASP   A 1  375 ? 14.10664  41.08930 69.93181 1.000 97.13351  ? 375 ASP   A C   1 
ATOM   2893 O O   . ASP   A 1  375 ? 14.35047  39.93654 69.55773 1.000 93.20071  ? 375 ASP   A O   1 
ATOM   2894 C CB  . ASP   A 1  375 ? 11.64932  40.63898 70.08592 1.000 93.50245  ? 375 ASP   A CB  1 
ATOM   2895 C CG  . ASP   A 1  375 ? 11.71849  40.17947 71.50001 1.000 105.84859 ? 375 ASP   A CG  1 
ATOM   2896 O OD1 . ASP   A 1  375 ? 12.08098  41.03133 72.35054 1.000 100.18917 ? 375 ASP   A OD1 1 
ATOM   2897 O OD2 . ASP   A 1  375 ? 11.45909  38.97866 71.75104 1.000 106.99252 ? 375 ASP   A OD2 1 
ATOM   2898 N N   . TRP   A 1  376 ? 15.00972  41.87598 70.51228 1.000 97.24481  ? 376 TRP   A N   1 
ATOM   2899 C CA  . TRP   A 1  376 ? 16.43981  41.63856 70.39426 1.000 103.21338 ? 376 TRP   A CA  1 
ATOM   2900 C C   . TRP   A 1  376 ? 16.92645  40.56326 71.35734 1.000 114.21446 ? 376 TRP   A C   1 
ATOM   2901 O O   . TRP   A 1  376 ? 16.70496  40.65411 72.57087 1.000 113.96263 ? 376 TRP   A O   1 
ATOM   2902 C CB  . TRP   A 1  376 ? 17.20000  42.93076 70.66659 1.000 104.79787 ? 376 TRP   A CB  1 
ATOM   2903 C CG  . TRP   A 1  376 ? 16.84395  44.09367 69.79287 1.000 98.48172  ? 376 TRP   A CG  1 
ATOM   2904 C CD1 . TRP   A 1  376 ? 16.50461  45.35538 70.20770 1.000 94.95316  ? 376 TRP   A CD1 1 
ATOM   2905 C CD2 . TRP   A 1  376 ? 16.82654  44.12496 68.35704 1.000 90.76421  ? 376 TRP   A CD2 1 
ATOM   2906 N NE1 . TRP   A 1  376 ? 16.26173  46.16190 69.12015 1.000 90.27276  ? 376 TRP   A NE1 1 
ATOM   2907 C CE2 . TRP   A 1  376 ? 16.45340  45.43352 67.97357 1.000 84.44135  ? 376 TRP   A CE2 1 
ATOM   2908 C CE3 . TRP   A 1  376 ? 17.08133  43.17426 67.35959 1.000 84.60853  ? 376 TRP   A CE3 1 
ATOM   2909 C CZ2 . TRP   A 1  376 ? 16.33347  45.81339 66.63763 1.000 80.46246  ? 376 TRP   A CZ2 1 
ATOM   2910 C CZ3 . TRP   A 1  376 ? 16.95862  43.55508 66.03392 1.000 78.15977  ? 376 TRP   A CZ3 1 
ATOM   2911 C CH2 . TRP   A 1  376 ? 16.58815  44.86158 65.68449 1.000 76.86919  ? 376 TRP   A CH2 1 
ATOM   2912 N N   . VAL   A 1  377 ? 17.62873  39.56319 70.81390 1.000 118.33978 ? 377 VAL   A N   1 
ATOM   2913 C CA  . VAL   A 1  377 ? 18.40076  38.66518 71.66334 1.000 116.57034 ? 377 VAL   A CA  1 
ATOM   2914 C C   . VAL   A 1  377 ? 19.43643  39.46027 72.45216 1.000 123.60849 ? 377 VAL   A C   1 
ATOM   2915 O O   . VAL   A 1  377 ? 19.81900  39.07280 73.56245 1.000 125.35975 ? 377 VAL   A O   1 
ATOM   2916 C CB  . VAL   A 1  377 ? 19.03213  37.54781 70.81021 1.000 120.08738 ? 377 VAL   A CB  1 
ATOM   2917 C CG1 . VAL   A 1  377 ? 17.93817  36.67024 70.21227 1.000 115.32753 ? 377 VAL   A CG1 1 
ATOM   2918 C CG2 . VAL   A 1  377 ? 19.89438  38.13854 69.70896 1.000 125.04833 ? 377 VAL   A CG2 1 
ATOM   2919 N N   . ASP   A 1  378 ? 19.88813  40.59047 71.90740 1.000 130.06593 ? 378 ASP   A N   1 
ATOM   2920 C CA  . ASP   A 1  378 ? 20.59380  41.61567 72.67292 1.000 130.84066 ? 378 ASP   A CA  1 
ATOM   2921 C C   . ASP   A 1  378 ? 20.19113  42.97512 72.12467 1.000 130.65830 ? 378 ASP   A C   1 
ATOM   2922 O O   . ASP   A 1  378 ? 20.34333  43.22393 70.92453 1.000 128.70056 ? 378 ASP   A O   1 
ATOM   2923 C CB  . ASP   A 1  378 ? 22.11371  41.44174 72.59890 1.000 131.13630 ? 378 ASP   A CB  1 
ATOM   2924 C CG  . ASP   A 1  378 ? 22.85985  42.44700 73.46892 1.000 130.72460 ? 378 ASP   A CG  1 
ATOM   2925 O OD1 . ASP   A 1  378 ? 22.79555  43.66227 73.18687 1.000 127.99341 ? 378 ASP   A OD1 1 
ATOM   2926 O OD2 . ASP   A 1  378 ? 23.50783  42.02535 74.44609 1.000 121.85862 ? 378 ASP   A OD2 1 
ATOM   2927 N N   . ASP   A 1  379 ? 19.69303  43.85701 72.99719 1.000 122.20874 ? 379 ASP   A N   1 
ATOM   2928 C CA  . ASP   A 1  379 ? 19.17607  45.15038 72.55507 1.000 121.68452 ? 379 ASP   A CA  1 
ATOM   2929 C C   . ASP   A 1  379 ? 20.25321  46.21634 72.39218 1.000 125.64907 ? 379 ASP   A C   1 
ATOM   2930 O O   . ASP   A 1  379 ? 19.93244  47.33601 71.97373 1.000 122.03068 ? 379 ASP   A O   1 
ATOM   2931 C CB  . ASP   A 1  379 ? 18.06370  45.63295 73.50788 1.000 125.53103 ? 379 ASP   A CB  1 
ATOM   2932 C CG  . ASP   A 1  379 ? 18.57716  46.47118 74.68876 1.000 135.21012 ? 379 ASP   A CG  1 
ATOM   2933 O OD1 . ASP   A 1  379 ? 19.78252  46.44649 75.01552 1.000 136.91877 ? 379 ASP   A OD1 1 
ATOM   2934 O OD2 . ASP   A 1  379 ? 17.74662  47.17307 75.30579 1.000 136.97443 ? 379 ASP   A OD2 1 
ATOM   2935 N N   . GLN   A 1  380 ? 21.51419  45.89410 72.69265 1.000 126.31411 ? 380 GLN   A N   1 
ATOM   2936 C CA  . GLN   A 1  380 ? 22.60201  46.86099 72.64703 1.000 127.09260 ? 380 GLN   A CA  1 
ATOM   2937 C C   . GLN   A 1  380 ? 23.51078  46.72081 71.43335 1.000 119.20885 ? 380 GLN   A C   1 
ATOM   2938 O O   . GLN   A 1  380 ? 24.33507  47.61107 71.19863 1.000 112.14769 ? 380 GLN   A O   1 
ATOM   2939 C CB  . GLN   A 1  380 ? 23.45488  46.75519 73.91890 1.000 131.13048 ? 380 GLN   A CB  1 
ATOM   2940 C CG  . GLN   A 1  380 ? 22.73285  47.18976 75.17996 1.000 135.95154 ? 380 GLN   A CG  1 
ATOM   2941 C CD  . GLN   A 1  380 ? 22.55430  48.69724 75.25941 1.000 142.09920 ? 380 GLN   A CD  1 
ATOM   2942 O OE1 . GLN   A 1  380 ? 23.47825  49.43430 75.60921 1.000 146.42788 ? 380 GLN   A OE1 1 
ATOM   2943 N NE2 . GLN   A 1  380 ? 21.35439  49.16281 74.92691 1.000 143.38018 ? 380 GLN   A NE2 1 
ATOM   2944 N N   . ARG   A 1  381 ? 23.38296  45.64549 70.66479 1.000 114.62637 ? 381 ARG   A N   1 
ATOM   2945 C CA  . ARG   A 1  381 ? 24.25227  45.42603 69.51169 1.000 105.77599 ? 381 ARG   A CA  1 
ATOM   2946 C C   . ARG   A 1  381 ? 24.00005  46.49167 68.44638 1.000 100.17531 ? 381 ARG   A C   1 
ATOM   2947 O O   . ARG   A 1  381 ? 22.85431  46.67108 68.01946 1.000 105.45833 ? 381 ARG   A O   1 
ATOM   2948 C CB  . ARG   A 1  381 ? 23.99030  44.03868 68.93640 1.000 108.44132 ? 381 ARG   A CB  1 
ATOM   2949 C CG  . ARG   A 1  381 ? 24.16261  42.89536 69.92758 1.000 115.46617 ? 381 ARG   A CG  1 
ATOM   2950 C CD  . ARG   A 1  381 ? 24.14215  41.56329 69.19774 1.000 118.64696 ? 381 ARG   A CD  1 
ATOM   2951 N NE  . ARG   A 1  381 ? 24.74045  41.69523 67.87432 1.000 120.79936 ? 381 ARG   A NE  1 
ATOM   2952 C CZ  . ARG   A 1  381 ? 25.58359  40.82475 67.33661 1.000 125.01215 ? 381 ARG   A CZ  1 
ATOM   2953 N NH1 . ARG   A 1  381 ? 25.93535  39.71805 67.97292 1.000 129.82626 ? 381 ARG   A NH1 1 
ATOM   2954 N NH2 . ARG   A 1  381 ? 26.08905  41.07237 66.13101 1.000 114.67758 ? 381 ARG   A NH2 1 
ATOM   2955 N N   . PRO   A 1  382 ? 25.02811  47.21747 67.99368 1.000 96.19743  ? 382 PRO   A N   1 
ATOM   2956 C CA  . PRO   A 1  382 ? 24.79273  48.26762 66.98278 1.000 93.35883  ? 382 PRO   A CA  1 
ATOM   2957 C C   . PRO   A 1  382 ? 24.36642  47.74806 65.61719 1.000 83.40796  ? 382 PRO   A C   1 
ATOM   2958 O O   . PRO   A 1  382 ? 23.82956  48.53291 64.82816 1.000 80.37320  ? 382 PRO   A O   1 
ATOM   2959 C CB  . PRO   A 1  382 ? 26.14469  49.00039 66.90264 1.000 93.18238  ? 382 PRO   A CB  1 
ATOM   2960 C CG  . PRO   A 1  382 ? 27.13653  48.08799 67.54884 1.000 92.48104  ? 382 PRO   A CG  1 
ATOM   2961 C CD  . PRO   A 1  382 ? 26.38535  47.28119 68.55926 1.000 93.21548  ? 382 PRO   A CD  1 
ATOM   2962 N N   . GLU   A 1  383 ? 24.59157  46.47448 65.30227 1.000 79.67017  ? 383 GLU   A N   1 
ATOM   2963 C CA  . GLU   A 1  383 ? 24.14887  45.92113 64.02552 1.000 78.68254  ? 383 GLU   A CA  1 
ATOM   2964 C C   . GLU   A 1  383 ? 22.70002  45.45742 64.04392 1.000 80.36433  ? 383 GLU   A C   1 
ATOM   2965 O O   . GLU   A 1  383 ? 22.21904  44.98009 63.01006 1.000 73.53669  ? 383 GLU   A O   1 
ATOM   2966 C CB  . GLU   A 1  383 ? 25.02801  44.73457 63.59616 1.000 79.07919  ? 383 GLU   A CB  1 
ATOM   2967 C CG  . GLU   A 1  383 ? 26.51411  44.88828 63.84808 1.000 86.55077  ? 383 GLU   A CG  1 
ATOM   2968 C CD  . GLU   A 1  383 ? 26.89536  44.62752 65.29564 1.000 100.43257 ? 383 GLU   A CD  1 
ATOM   2969 O OE1 . GLU   A 1  383 ? 26.02598  44.12507 66.04744 1.000 98.67115  ? 383 GLU   A OE1 1 
ATOM   2970 O OE2 . GLU   A 1  383 ? 28.04976  44.95379 65.68247 1.000 99.73140  ? 383 GLU   A OE2 1 
ATOM   2971 N N   . ASN   A 1  384 ? 22.00582  45.59040 65.18272 1.000 85.94283  ? 384 ASN   A N   1 
ATOM   2972 C CA  . ASN   A 1  384 ? 20.68611  44.98316 65.36335 1.000 79.04122  ? 384 ASN   A CA  1 
ATOM   2973 C C   . ASN   A 1  384 ? 19.74322  45.32815 64.21723 1.000 76.17382  ? 384 ASN   A C   1 
ATOM   2974 O O   . ASN   A 1  384 ? 19.10632  44.44293 63.63492 1.000 76.92606  ? 384 ASN   A O   1 
ATOM   2975 C CB  . ASN   A 1  384 ? 20.08357  45.42777 66.69869 1.000 79.46067  ? 384 ASN   A CB  1 
ATOM   2976 C CG  . ASN   A 1  384 ? 20.46138  44.51095 67.84736 1.000 91.14875  ? 384 ASN   A CG  1 
ATOM   2977 O OD1 . ASN   A 1  384 ? 20.86489  43.35844 67.64609 1.000 91.08320  ? 384 ASN   A OD1 1 
ATOM   2978 N ND2 . ASN   A 1  384 ? 20.35178  45.02807 69.06571 1.000 96.70005  ? 384 ASN   A ND2 1 
ATOM   2979 N N   . TYR   A 1  385 ? 19.65255  46.61217 63.86514 1.000 71.46649  ? 385 TYR   A N   1 
ATOM   2980 C CA  . TYR   A 1  385 ? 18.72691  46.99874 62.80674 1.000 73.06366  ? 385 TYR   A CA  1 
ATOM   2981 C C   . TYR   A 1  385 ? 19.26750  46.63452 61.42636 1.000 71.75958  ? 385 TYR   A C   1 
ATOM   2982 O O   . TYR   A 1  385 ? 18.49410  46.21383 60.55405 1.000 62.55460  ? 385 TYR   A O   1 
ATOM   2983 C CB  . TYR   A 1  385 ? 18.39707  48.48895 62.90927 1.000 73.94908  ? 385 TYR   A CB  1 
ATOM   2984 C CG  . TYR   A 1  385 ? 17.53715  48.80415 64.12230 1.000 80.35293  ? 385 TYR   A CG  1 
ATOM   2985 C CD1 . TYR   A 1  385 ? 16.18439  48.45357 64.15767 1.000 79.54861  ? 385 TYR   A CD1 1 
ATOM   2986 C CD2 . TYR   A 1  385 ? 18.07667  49.43799 65.23627 1.000 78.45712  ? 385 TYR   A CD2 1 
ATOM   2987 C CE1 . TYR   A 1  385 ? 15.39342  48.73734 65.27583 1.000 75.59432  ? 385 TYR   A CE1 1 
ATOM   2988 C CE2 . TYR   A 1  385 ? 17.30240  49.72033 66.34391 1.000 77.80383  ? 385 TYR   A CE2 1 
ATOM   2989 C CZ  . TYR   A 1  385 ? 15.96815  49.36946 66.36465 1.000 82.44060  ? 385 TYR   A CZ  1 
ATOM   2990 O OH  . TYR   A 1  385 ? 15.22649  49.66439 67.48736 1.000 84.11711  ? 385 TYR   A OH  1 
ATOM   2991 N N   . ARG   A 1  386 ? 20.58552  46.76320 61.22030 1.000 66.74026  ? 386 ARG   A N   1 
ATOM   2992 C CA  . ARG   A 1  386 ? 21.18720  46.36744 59.94640 1.000 68.41986  ? 386 ARG   A CA  1 
ATOM   2993 C C   . ARG   A 1  386 ? 20.89244  44.90014 59.62493 1.000 66.31181  ? 386 ARG   A C   1 
ATOM   2994 O O   . ARG   A 1  386 ? 20.43034  44.56508 58.52480 1.000 64.38079  ? 386 ARG   A O   1 
ATOM   2995 C CB  . ARG   A 1  386 ? 22.69621  46.62358 59.98285 1.000 65.63625  ? 386 ARG   A CB  1 
ATOM   2996 C CG  . ARG   A 1  386 ? 23.45250  46.13950 58.75834 1.000 59.38729  ? 386 ARG   A CG  1 
ATOM   2997 C CD  . ARG   A 1  386 ? 24.93586  46.18401 59.03294 1.000 68.93752  ? 386 ARG   A CD  1 
ATOM   2998 N NE  . ARG   A 1  386 ? 25.44127  44.93345 59.58445 1.000 68.87300  ? 386 ARG   A NE  1 
ATOM   2999 C CZ  . ARG   A 1  386 ? 26.64649  44.77374 60.11791 1.000 67.10714  ? 386 ARG   A CZ  1 
ATOM   3000 N NH1 . ARG   A 1  386 ? 27.49564  45.77867 60.22574 1.000 71.85404  ? 386 ARG   A NH1 1 
ATOM   3001 N NH2 . ARG   A 1  386 ? 27.00418  43.57548 60.56765 1.000 67.43690  ? 386 ARG   A NH2 1 
ATOM   3002 N N   . GLU   A 1  387 ? 21.14457  44.00752 60.58120 1.000 64.42153  ? 387 GLU   A N   1 
ATOM   3003 C CA  . GLU   A 1  387 ? 20.86106  42.59427 60.35269 1.000 67.20394  ? 387 GLU   A CA  1 
ATOM   3004 C C   . GLU   A 1  387 ? 19.36869  42.33663 60.20352 1.000 66.01086  ? 387 GLU   A C   1 
ATOM   3005 O O   . GLU   A 1  387 ? 18.95449  41.50862 59.37973 1.000 63.81502  ? 387 GLU   A O   1 
ATOM   3006 C CB  . GLU   A 1  387 ? 21.42303  41.76405 61.49775 1.000 69.73615  ? 387 GLU   A CB  1 
ATOM   3007 C CG  . GLU   A 1  387 ? 22.83595  42.12840 61.82356 1.000 78.71244  ? 387 GLU   A CG  1 
ATOM   3008 C CD  . GLU   A 1  387 ? 23.58325  41.00744 62.48842 1.000 93.57949  ? 387 GLU   A CD  1 
ATOM   3009 O OE1 . GLU   A 1  387 ? 24.62390  40.57928 61.94396 1.000 97.45970  ? 387 GLU   A OE1 1 
ATOM   3010 O OE2 . GLU   A 1  387 ? 23.12627  40.56319 63.56520 1.000 98.86641  ? 387 GLU   A OE2 1 
ATOM   3011 N N   . ALA   A 1  388 ? 18.54561  43.02419 61.00231 1.000 67.17096  ? 388 ALA   A N   1 
ATOM   3012 C CA  . ALA   A 1  388 ? 17.10672  42.77712 60.96384 1.000 63.40229  ? 388 ALA   A CA  1 
ATOM   3013 C C   . ALA   A 1  388 ? 16.52483  43.06578 59.58482 1.000 63.14790  ? 388 ALA   A C   1 
ATOM   3014 O O   . ALA   A 1  388 ? 15.68023  42.30783 59.09833 1.000 59.20439  ? 388 ALA   A O   1 
ATOM   3015 C CB  . ALA   A 1  388 ? 16.40087  43.61057 62.03405 1.000 62.81828  ? 388 ALA   A CB  1 
ATOM   3016 N N   . LEU   A 1  389 ? 16.98070  44.14370 58.92718 1.000 60.63870  ? 389 LEU   A N   1 
ATOM   3017 C CA  . LEU   A 1  389 ? 16.40044  44.51424 57.63941 1.000 60.72563  ? 389 LEU   A CA  1 
ATOM   3018 C C   . LEU   A 1  389 ? 16.75428  43.50958 56.55168 1.000 63.42609  ? 389 LEU   A C   1 
ATOM   3019 O O   . LEU   A 1  389 ? 15.88474  43.13653 55.74927 1.000 61.40716  ? 389 LEU   A O   1 
ATOM   3020 C CB  . LEU   A 1  389 ? 16.82223  45.92938 57.23923 1.000 65.80812  ? 389 LEU   A CB  1 
ATOM   3021 C CG  . LEU   A 1  389 ? 15.95472  46.50191 56.10328 1.000 66.22925  ? 389 LEU   A CG  1 
ATOM   3022 C CD1 . LEU   A 1  389 ? 14.46950  46.55453 56.48912 1.000 52.29585  ? 389 LEU   A CD1 1 
ATOM   3023 C CD2 . LEU   A 1  389 ? 16.46583  47.87823 55.66079 1.000 56.11187  ? 389 LEU   A CD2 1 
ATOM   3024 N N   . GLY   A 1  390 ? 18.01299  43.04081 56.52692 1.000 60.14719  ? 390 GLY   A N   1 
ATOM   3025 C CA  . GLY   A 1  390 ? 18.38235  41.96553 55.61669 1.000 54.85582  ? 390 GLY   A CA  1 
ATOM   3026 C C   . GLY   A 1  390 ? 17.56397  40.70250 55.83078 1.000 59.29408  ? 390 GLY   A C   1 
ATOM   3027 O O   . GLY   A 1  390 ? 17.05041  40.11088 54.87291 1.000 54.22673  ? 390 GLY   A O   1 
ATOM   3028 N N   . ASP   A 1  391 ? 17.41310  40.28130 57.09356 1.000 56.55273  ? 391 ASP   A N   1 
ATOM   3029 C CA  . ASP   A 1  391 ? 16.60684  39.09374 57.39004 1.000 56.03713  ? 391 ASP   A CA  1 
ATOM   3030 C C   . ASP   A 1  391 ? 15.15971  39.27513 56.94693 1.000 57.97218  ? 391 ASP   A C   1 
ATOM   3031 O O   . ASP   A 1  391 ? 14.54551  38.34680 56.40770 1.000 58.70595  ? 391 ASP   A O   1 
ATOM   3032 C CB  . ASP   A 1  391 ? 16.65203  38.78539 58.88489 1.000 60.57431  ? 391 ASP   A CB  1 
ATOM   3033 C CG  . ASP   A 1  391 ? 17.91296  38.04775 59.29466 1.000 62.33431  ? 391 ASP   A CG  1 
ATOM   3034 O OD1 . ASP   A 1  391 ? 18.47357  37.26892 58.48737 1.000 64.05846  ? 391 ASP   A OD1 1 
ATOM   3035 O OD2 . ASP   A 1  391 ? 18.33685  38.25649 60.44422 1.000 66.85349  ? 391 ASP   A OD2 1 
ATOM   3036 N N   . VAL   A 1  392 ? 14.59097  40.46111 57.17402 1.000 56.37794  ? 392 VAL   A N   1 
ATOM   3037 C CA  . VAL   A 1  392 ? 13.22751  40.73137 56.71461 1.000 59.87010  ? 392 VAL   A CA  1 
ATOM   3038 C C   . VAL   A 1  392 ? 13.12183  40.51340 55.20740 1.000 55.52688  ? 392 VAL   A C   1 
ATOM   3039 O O   . VAL   A 1  392 ? 12.27482  39.75417 54.73495 1.000 55.23032  ? 392 VAL   A O   1 
ATOM   3040 C CB  . VAL   A 1  392 ? 12.79202  42.15652 57.11095 1.000 58.34337  ? 392 VAL   A CB  1 
ATOM   3041 C CG1 . VAL   A 1  392 ? 11.59410  42.60333 56.29258 1.000 62.48065  ? 392 VAL   A CG1 1 
ATOM   3042 C CG2 . VAL   A 1  392 ? 12.46033  42.21873 58.57916 1.000 61.34507  ? 392 VAL   A CG2 1 
ATOM   3043 N N   . VAL   A 1  393 ? 13.99315  41.16689 54.43802 1.000 54.79570  ? 393 VAL   A N   1 
ATOM   3044 C CA  . VAL   A 1  393 ? 13.93445  41.08059 52.97868 1.000 56.62197  ? 393 VAL   A CA  1 
ATOM   3045 C C   . VAL   A 1  393 ? 14.18429  39.65449 52.52243 1.000 56.28955  ? 393 VAL   A C   1 
ATOM   3046 O O   . VAL   A 1  393 ? 13.52265  39.15116 51.60579 1.000 55.89549  ? 393 VAL   A O   1 
ATOM   3047 C CB  . VAL   A 1  393 ? 14.95482  42.05789 52.34783 1.000 59.70947  ? 393 VAL   A CB  1 
ATOM   3048 C CG1 . VAL   A 1  393 ? 15.16746  41.75204 50.84839 1.000 54.81849  ? 393 VAL   A CG1 1 
ATOM   3049 C CG2 . VAL   A 1  393 ? 14.52432  43.51999 52.57994 1.000 54.96021  ? 393 VAL   A CG2 1 
ATOM   3050 N N   . GLY   A 1  394 ? 15.13624  38.97778 53.16493 1.000 55.21582  ? 394 GLY   A N   1 
ATOM   3051 C CA  . GLY   A 1  394 ? 15.46922  37.62776 52.75527 1.000 53.45125  ? 394 GLY   A CA  1 
ATOM   3052 C C   . GLY   A 1  394 ? 14.38669  36.63184 53.11061 1.000 58.35992  ? 394 GLY   A C   1 
ATOM   3053 O O   . GLY   A 1  394 ? 14.04482  35.75848 52.30046 1.000 57.65465  ? 394 GLY   A O   1 
ATOM   3054 N N   . ASP   A 1  395 ? 13.84611  36.72890 54.33414 1.000 51.09079  ? 395 ASP   A N   1 
ATOM   3055 C CA  . ASP   A 1  395 ? 12.83681  35.75755 54.75109 1.000 52.23540  ? 395 ASP   A CA  1 
ATOM   3056 C C   . ASP   A 1  395 ? 11.55853  35.94545 53.95563 1.000 58.86639  ? 395 ASP   A C   1 
ATOM   3057 O O   . ASP   A 1  395 ? 10.95452  34.97382 53.48349 1.000 58.00579  ? 395 ASP   A O   1 
ATOM   3058 C CB  . ASP   A 1  395 ? 12.54010  35.88428 56.25068 1.000 51.83174  ? 395 ASP   A CB  1 
ATOM   3059 C CG  . ASP   A 1  395 ? 13.72241  35.49056 57.12838 1.000 60.57659  ? 395 ASP   A CG  1 
ATOM   3060 O OD1 . ASP   A 1  395 ? 14.63845  34.74559 56.65547 1.000 58.35746  ? 395 ASP   A OD1 1 
ATOM   3061 O OD2 . ASP   A 1  395 ? 13.74498  35.96338 58.29272 1.000 55.88080  ? 395 ASP   A OD2 1 
ATOM   3062 N N   . TYR   A 1  396 ? 11.12777  37.19667 53.80115 1.000 59.10468  ? 396 TYR   A N   1 
ATOM   3063 C CA  . TYR   A 1  396 ? 9.90196   37.47132 53.07029 1.000 54.41462  ? 396 TYR   A CA  1 
ATOM   3064 C C   . TYR   A 1  396 ? 10.04692  37.12032 51.59419 1.000 56.03744  ? 396 TYR   A C   1 
ATOM   3065 O O   . TYR   A 1  396 ? 9.13621   36.54529 50.99356 1.000 52.43649  ? 396 TYR   A O   1 
ATOM   3066 C CB  . TYR   A 1  396 ? 9.53218   38.93865 53.25172 1.000 57.48505  ? 396 TYR   A CB  1 
ATOM   3067 C CG  . TYR   A 1  396 ? 8.45131   39.44253 52.32814 1.000 57.79564  ? 396 TYR   A CG  1 
ATOM   3068 C CD1 . TYR   A 1  396 ? 7.16675   38.91291 52.38795 1.000 62.04417  ? 396 TYR   A CD1 1 
ATOM   3069 C CD2 . TYR   A 1  396 ? 8.69954   40.47136 51.42672 1.000 59.65122  ? 396 TYR   A CD2 1 
ATOM   3070 C CE1 . TYR   A 1  396 ? 6.14572   39.36960 51.57006 1.000 55.71285  ? 396 TYR   A CE1 1 
ATOM   3071 C CE2 . TYR   A 1  396 ? 7.69007   40.95291 50.59718 1.000 61.61753  ? 396 TYR   A CE2 1 
ATOM   3072 C CZ  . TYR   A 1  396 ? 6.40555   40.38462 50.67947 1.000 70.23374  ? 396 TYR   A CZ  1 
ATOM   3073 O OH  . TYR   A 1  396 ? 5.36875   40.81043 49.88361 1.000 64.88447  ? 396 TYR   A OH  1 
ATOM   3074 N N   . ASN   A 1  397 ? 11.18318  37.44115 50.99349 1.000 56.10297  ? 397 ASN   A N   1 
ATOM   3075 C CA  . ASN   A 1  397 ? 11.27970  37.35762 49.54306 1.000 55.72957  ? 397 ASN   A CA  1 
ATOM   3076 C C   . ASN   A 1  397 ? 11.80257  36.02457 49.02025 1.000 60.58951  ? 397 ASN   A C   1 
ATOM   3077 O O   . ASN   A 1  397 ? 11.59876  35.72968 47.83273 1.000 55.91608  ? 397 ASN   A O   1 
ATOM   3078 C CB  . ASN   A 1  397 ? 12.16649  38.48271 49.02018 1.000 52.33231  ? 397 ASN   A CB  1 
ATOM   3079 C CG  . ASN   A 1  397 ? 11.42964  39.78389 48.92943 1.000 57.05051  ? 397 ASN   A CG  1 
ATOM   3080 O OD1 . ASN   A 1  397 ? 10.51786  39.92031 48.11159 1.000 58.24299  ? 397 ASN   A OD1 1 
ATOM   3081 N ND2 . ASN   A 1  397 ? 11.79389  40.74555 49.76853 1.000 54.28410  ? 397 ASN   A ND2 1 
ATOM   3082 N N   . PHE   A 1  398 ? 12.45621  35.21152 49.85906 1.000 54.06712  ? 398 PHE   A N   1 
ATOM   3083 C CA  . PHE   A 1  398 ? 13.10574  34.00486 49.35810 1.000 53.12091  ? 398 PHE   A CA  1 
ATOM   3084 C C   . PHE   A 1  398 ? 12.95251  32.79883 50.28261 1.000 59.50972  ? 398 PHE   A C   1 
ATOM   3085 O O   . PHE   A 1  398 ? 12.44672  31.74698 49.86324 1.000 52.78272  ? 398 PHE   A O   1 
ATOM   3086 C CB  . PHE   A 1  398 ? 14.58958  34.27276 49.12036 1.000 51.54146  ? 398 PHE   A CB  1 
ATOM   3087 C CG  . PHE   A 1  398 ? 14.84863  35.34832 48.08656 1.000 60.15173  ? 398 PHE   A CG  1 
ATOM   3088 C CD1 . PHE   A 1  398 ? 14.79452  35.05188 46.72506 1.000 55.01017  ? 398 PHE   A CD1 1 
ATOM   3089 C CD2 . PHE   A 1  398 ? 15.12111  36.66633 48.47791 1.000 55.81951  ? 398 PHE   A CD2 1 
ATOM   3090 C CE1 . PHE   A 1  398 ? 15.03037  36.05137 45.76951 1.000 58.51723  ? 398 PHE   A CE1 1 
ATOM   3091 C CE2 . PHE   A 1  398 ? 15.34973  37.67953 47.52176 1.000 55.43621  ? 398 PHE   A CE2 1 
ATOM   3092 C CZ  . PHE   A 1  398 ? 15.30884  37.36948 46.16971 1.000 54.69797  ? 398 PHE   A CZ  1 
ATOM   3093 N N   . ILE   A 1  399 ? 13.40025  32.93623 51.53289 1.000 56.25232  ? 399 ILE   A N   1 
ATOM   3094 C CA  . ILE   A 1  399 ? 13.55456  31.77452 52.40653 1.000 54.37913  ? 399 ILE   A CA  1 
ATOM   3095 C C   . ILE   A 1  399 ? 12.19222  31.15311 52.73753 1.000 60.74841  ? 399 ILE   A C   1 
ATOM   3096 O O   . ILE   A 1  399 ? 11.96300  29.95656 52.49846 1.000 57.89550  ? 399 ILE   A O   1 
ATOM   3097 C CB  . ILE   A 1  399 ? 14.33614  32.17982 53.67005 1.000 57.81277  ? 399 ILE   A CB  1 
ATOM   3098 C CG1 . ILE   A 1  399 ? 15.79850  32.47588 53.31433 1.000 49.03017  ? 399 ILE   A CG1 1 
ATOM   3099 C CG2 . ILE   A 1  399 ? 14.22865  31.10325 54.74339 1.000 57.14964  ? 399 ILE   A CG2 1 
ATOM   3100 C CD1 . ILE   A 1  399 ? 16.61378  32.94919 54.47835 1.000 56.40211  ? 399 ILE   A CD1 1 
ATOM   3101 N N   . CYS   A 1  400 ? 11.25069  31.95939 53.25447 1.000 52.74314  ? 400 CYS   A N   1 
ATOM   3102 C CA  . CYS   A 1  400 ? 9.93376   31.43798 53.62612 1.000 55.92524  ? 400 CYS   A CA  1 
ATOM   3103 C C   . CYS   A 1  400 ? 9.09639   30.96721 52.43212 1.000 59.03222  ? 400 CYS   A C   1 
ATOM   3104 O O   . CYS   A 1  400 ? 8.41715   29.93661 52.54619 1.000 56.35621  ? 400 CYS   A O   1 
ATOM   3105 C CB  . CYS   A 1  400 ? 9.14894   32.47904 54.42650 1.000 52.48876  ? 400 CYS   A CB  1 
ATOM   3106 S SG  . CYS   A 1  400 ? 9.94653   32.88323 56.00080 1.000 60.75298  ? 400 CYS   A SG  1 
ATOM   3107 N N   . PRO   A 1  401 ? 9.08208   31.66342 51.28341 1.000 56.01365  ? 401 PRO   A N   1 
ATOM   3108 C CA  . PRO   A 1  401 ? 8.35233   31.08039 50.14539 1.000 57.74382  ? 401 PRO   A CA  1 
ATOM   3109 C C   . PRO   A 1  401 ? 8.95670   29.76090 49.69481 1.000 57.74023  ? 401 PRO   A C   1 
ATOM   3110 O O   . PRO   A 1  401 ? 8.21514   28.84601 49.31128 1.000 54.07864  ? 401 PRO   A O   1 
ATOM   3111 C CB  . PRO   A 1  401 ? 8.44241   32.16437 49.05599 1.000 56.21163  ? 401 PRO   A CB  1 
ATOM   3112 C CG  . PRO   A 1  401 ? 8.75011   33.41974 49.78136 1.000 51.11449  ? 401 PRO   A CG  1 
ATOM   3113 C CD  . PRO   A 1  401 ? 9.62408   32.99106 50.93786 1.000 50.81580  ? 401 PRO   A CD  1 
ATOM   3114 N N   . ALA   A 1  402 ? 10.28178  29.60647 49.76486 1.000 50.22250  ? 402 ALA   A N   1 
ATOM   3115 C CA  . ALA   A 1  402 ? 10.85649  28.33500 49.32341 1.000 52.12209  ? 402 ALA   A CA  1 
ATOM   3116 C C   . ALA   A 1  402 ? 10.51209  27.21167 50.29113 1.000 55.53300  ? 402 ALA   A C   1 
ATOM   3117 O O   . ALA   A 1  402 ? 10.14552  26.11171 49.86358 1.000 52.86682  ? 402 ALA   A O   1 
ATOM   3118 C CB  . ALA   A 1  402 ? 12.36167  28.43702 49.14696 1.000 49.11390  ? 402 ALA   A CB  1 
ATOM   3119 N N   . LEU   A 1  403 ? 10.61387  27.46140 51.59677 1.000 55.74360  ? 403 LEU   A N   1 
ATOM   3120 C CA  . LEU   A 1  403 ? 10.17145  26.44532 52.55034 1.000 57.78654  ? 403 LEU   A CA  1 
ATOM   3121 C C   . LEU   A 1  403 ? 8.72764   26.04351 52.29805 1.000 56.53714  ? 403 LEU   A C   1 
ATOM   3122 O O   . LEU   A 1  403 ? 8.39853   24.84966 52.31576 1.000 59.73354  ? 403 LEU   A O   1 
ATOM   3123 C CB  . LEU   A 1  403 ? 10.33347  26.94292 53.98182 1.000 55.21611  ? 403 LEU   A CB  1 
ATOM   3124 C CG  . LEU   A 1  403 ? 11.80426  26.99217 54.37042 1.000 55.99010  ? 403 LEU   A CG  1 
ATOM   3125 C CD1 . LEU   A 1  403 ? 11.96362  28.00389 55.47930 1.000 54.97482  ? 403 LEU   A CD1 1 
ATOM   3126 C CD2 . LEU   A 1  403 ? 12.33530  25.59352 54.77143 1.000 44.22527  ? 403 LEU   A CD2 1 
ATOM   3127 N N   . GLU   A 1  404 ? 7.85815   27.02431 52.03645 1.000 53.55923  ? 404 GLU   A N   1 
ATOM   3128 C CA  . GLU   A 1  404 ? 6.43488   26.73818 51.86821 1.000 58.57167  ? 404 GLU   A CA  1 
ATOM   3129 C C   . GLU   A 1  404 ? 6.16979   25.93943 50.59033 1.000 57.76157  ? 404 GLU   A C   1 
ATOM   3130 O O   . GLU   A 1  404 ? 5.30211   25.05882 50.56664 1.000 54.39657  ? 404 GLU   A O   1 
ATOM   3131 C CB  . GLU   A 1  404 ? 5.64172   28.04880 51.87547 1.000 53.61247  ? 404 GLU   A CB  1 
ATOM   3132 C CG  . GLU   A 1  404 ? 4.13753   27.88282 52.04910 1.000 74.83509  ? 404 GLU   A CG  1 
ATOM   3133 C CD  . GLU   A 1  404 ? 3.74517   27.06896 53.29827 1.000 83.73761  ? 404 GLU   A CD  1 
ATOM   3134 O OE1 . GLU   A 1  404 ? 4.49414   27.06708 54.31322 1.000 80.21542  ? 404 GLU   A OE1 1 
ATOM   3135 O OE2 . GLU   A 1  404 ? 2.67757   26.42294 53.25129 1.000 84.40734  ? 404 GLU   A OE2 1 
ATOM   3136 N N   . PHE   A 1  405 ? 6.90732   26.23589 49.51888 1.000 55.91569  ? 405 PHE   A N   1 
ATOM   3137 C CA  . PHE   A 1  405 ? 6.78416   25.45122 48.29838 1.000 58.02113  ? 405 PHE   A CA  1 
ATOM   3138 C C   . PHE   A 1  405 ? 7.16577   23.99686 48.54843 1.000 59.31033  ? 405 PHE   A C   1 
ATOM   3139 O O   . PHE   A 1  405 ? 6.44411   23.07049 48.14506 1.000 57.10251  ? 405 PHE   A O   1 
ATOM   3140 C CB  . PHE   A 1  405 ? 7.65580   26.05197 47.20242 1.000 52.64400  ? 405 PHE   A CB  1 
ATOM   3141 C CG  . PHE   A 1  405 ? 7.68854   25.23274 45.96521 1.000 58.08422  ? 405 PHE   A CG  1 
ATOM   3142 C CD1 . PHE   A 1  405 ? 8.64476   24.22281 45.80369 1.000 55.12040  ? 405 PHE   A CD1 1 
ATOM   3143 C CD2 . PHE   A 1  405 ? 6.76925   25.45732 44.95116 1.000 53.69515  ? 405 PHE   A CD2 1 
ATOM   3144 C CE1 . PHE   A 1  405 ? 8.66060   23.43994 44.64616 1.000 57.88019  ? 405 PHE   A CE1 1 
ATOM   3145 C CE2 . PHE   A 1  405 ? 6.78927   24.69515 43.79386 1.000 58.20010  ? 405 PHE   A CE2 1 
ATOM   3146 C CZ  . PHE   A 1  405 ? 7.73929   23.68114 43.64125 1.000 59.64198  ? 405 PHE   A CZ  1 
ATOM   3147 N N   . THR   A 1  406 ? 8.30022   23.78637 49.22551 1.000 48.27543  ? 406 THR   A N   1 
ATOM   3148 C CA  . THR   A 1  406 ? 8.77384   22.44063 49.53549 1.000 48.15451  ? 406 THR   A CA  1 
ATOM   3149 C C   . THR   A 1  406 ? 7.78731   21.66794 50.41645 1.000 54.94750  ? 406 THR   A C   1 
ATOM   3150 O O   . THR   A 1  406 ? 7.54301   20.48070 50.17830 1.000 57.48064  ? 406 THR   A O   1 
ATOM   3151 C CB  . THR   A 1  406 ? 10.13698  22.51606 50.21695 1.000 56.83693  ? 406 THR   A CB  1 
ATOM   3152 O OG1 . THR   A 1  406 ? 11.04032  23.31339 49.42127 1.000 50.94900  ? 406 THR   A OG1 1 
ATOM   3153 C CG2 . THR   A 1  406 ? 10.70836  21.09942 50.41404 1.000 49.91143  ? 406 THR   A CG2 1 
ATOM   3154 N N   . LYS   A 1  407 ? 7.21580   22.30925 51.44483 1.000 58.81087  ? 407 LYS   A N   1 
ATOM   3155 C CA  . LYS   A 1  407 ? 6.20284   21.63087 52.25295 1.000 61.79219  ? 407 LYS   A CA  1 
ATOM   3156 C C   . LYS   A 1  407 ? 5.01099   21.23153 51.39805 1.000 60.50769  ? 407 LYS   A C   1 
ATOM   3157 O O   . LYS   A 1  407 ? 4.56338   20.07913 51.43454 1.000 60.10656  ? 407 LYS   A O   1 
ATOM   3158 C CB  . LYS   A 1  407 ? 5.72891   22.51918 53.40909 1.000 64.52886  ? 407 LYS   A CB  1 
ATOM   3159 C CG  . LYS   A 1  407 ? 6.77569   22.81713 54.45525 1.000 72.79704  ? 407 LYS   A CG  1 
ATOM   3160 C CD  . LYS   A 1  407 ? 6.19380   23.60498 55.62723 1.000 76.83839  ? 407 LYS   A CD  1 
ATOM   3161 C CE  . LYS   A 1  407 ? 7.21167   24.63381 56.15162 1.000 77.13174  ? 407 LYS   A CE  1 
ATOM   3162 N NZ  . LYS   A 1  407 ? 6.76740   25.30352 57.42114 1.000 81.04466  ? 407 LYS   A NZ  1 
ATOM   3163 N N   . LYS   A 1  408 ? 4.47542   22.18400 50.63170 1.000 61.34690  ? 408 LYS   A N   1 
ATOM   3164 C CA  . LYS   A 1  408 ? 3.28954   21.91444 49.82437 1.000 64.47061  ? 408 LYS   A CA  1 
ATOM   3165 C C   . LYS   A 1  408 ? 3.56930   20.79319 48.83940 1.000 61.32745  ? 408 LYS   A C   1 
ATOM   3166 O O   . LYS   A 1  408 ? 2.78866   19.84392 48.70793 1.000 61.22086  ? 408 LYS   A O   1 
ATOM   3167 C CB  . LYS   A 1  408 ? 2.86937   23.18510 49.07769 1.000 55.91941  ? 408 LYS   A CB  1 
ATOM   3168 C CG  . LYS   A 1  408 ? 1.74969   23.99413 49.69673 1.000 67.44438  ? 408 LYS   A CG  1 
ATOM   3169 C CD  . LYS   A 1  408 ? 1.72643   23.85796 51.20830 1.000 80.33469  ? 408 LYS   A CD  1 
ATOM   3170 C CE  . LYS   A 1  408 ? 0.37161   24.27245 51.78224 1.000 85.94489  ? 408 LYS   A CE  1 
ATOM   3171 N NZ  . LYS   A 1  408 ? 0.03592   23.57651 53.07290 1.000 91.54907  ? 408 LYS   A NZ  1 
ATOM   3172 N N   . PHE   A 1  409 ? 4.70907   20.87718 48.16269 1.000 57.12612  ? 409 PHE   A N   1 
ATOM   3173 C CA  . PHE   A 1  409 ? 5.01003   19.93498 47.10080 1.000 59.38692  ? 409 PHE   A CA  1 
ATOM   3174 C C   . PHE   A 1  409 ? 5.22297   18.53606 47.66314 1.000 62.95698  ? 409 PHE   A C   1 
ATOM   3175 O O   . PHE   A 1  409 ? 4.76972   17.54528 47.07597 1.000 62.08626  ? 409 PHE   A O   1 
ATOM   3176 C CB  . PHE   A 1  409 ? 6.24205   20.41863 46.32744 1.000 57.27182  ? 409 PHE   A CB  1 
ATOM   3177 C CG  . PHE   A 1  409 ? 6.54552   19.60879 45.09958 1.000 61.41011  ? 409 PHE   A CG  1 
ATOM   3178 C CD1 . PHE   A 1  409 ? 7.20351   18.38429 45.20204 1.000 59.66229  ? 409 PHE   A CD1 1 
ATOM   3179 C CD2 . PHE   A 1  409 ? 6.17920   20.06719 43.84143 1.000 58.32408  ? 409 PHE   A CD2 1 
ATOM   3180 C CE1 . PHE   A 1  409 ? 7.48483   17.61566 44.06938 1.000 60.81852  ? 409 PHE   A CE1 1 
ATOM   3181 C CE2 . PHE   A 1  409 ? 6.47322   19.30950 42.69504 1.000 62.28730  ? 409 PHE   A CE2 1 
ATOM   3182 C CZ  . PHE   A 1  409 ? 7.12481   18.07542 42.81322 1.000 60.48688  ? 409 PHE   A CZ  1 
ATOM   3183 N N   . SER   A 1  410 ? 5.91097   18.43110 48.79899 1.000 59.55018  ? 410 SER   A N   1 
ATOM   3184 C CA  . SER   A 1  410 ? 6.18613   17.11171 49.35035 1.000 60.75399  ? 410 SER   A CA  1 
ATOM   3185 C C   . SER   A 1  410 ? 4.93493   16.47001 49.93380 1.000 62.44742  ? 410 SER   A C   1 
ATOM   3186 O O   . SER   A 1  410 ? 4.87644   15.24051 50.03203 1.000 67.00800  ? 410 SER   A O   1 
ATOM   3187 C CB  . SER   A 1  410 ? 7.30683   17.19907 50.40021 1.000 61.28054  ? 410 SER   A CB  1 
ATOM   3188 O OG  . SER   A 1  410 ? 6.81623   17.70555 51.63033 1.000 68.96287  ? 410 SER   A OG  1 
ATOM   3189 N N   . GLU   A 1  411 ? 3.91513   17.26108 50.28251 1.000 64.75867  ? 411 GLU   A N   1 
ATOM   3190 C CA  . GLU   A 1  411 ? 2.67412   16.67428 50.78615 1.000 63.31411  ? 411 GLU   A CA  1 
ATOM   3191 C C   . GLU   A 1  411 ? 1.98067   15.77549 49.76745 1.000 61.47690  ? 411 GLU   A C   1 
ATOM   3192 O O   . GLU   A 1  411 ? 1.03067   15.07510 50.12670 1.000 60.08823  ? 411 GLU   A O   1 
ATOM   3193 C CB  . GLU   A 1  411 ? 1.70085   17.76953 51.22507 1.000 63.21305  ? 411 GLU   A CB  1 
ATOM   3194 C CG  . GLU   A 1  411 ? 1.80344   18.17414 52.68892 1.000 69.78905  ? 411 GLU   A CG  1 
ATOM   3195 C CD  . GLU   A 1  411 ? 1.48618   19.66016 52.91113 1.000 84.89265  ? 411 GLU   A CD  1 
ATOM   3196 O OE1 . GLU   A 1  411 ? 0.84324   20.28891 52.03450 1.000 86.64148  ? 411 GLU   A OE1 1 
ATOM   3197 O OE2 . GLU   A 1  411 ? 1.88447   20.20714 53.96580 1.000 88.53183  ? 411 GLU   A OE2 1 
ATOM   3198 N N   . TRP   A 1  412 ? 2.40848   15.76284 48.51169 1.000 65.79205  ? 412 TRP   A N   1 
ATOM   3199 C CA  . TRP   A 1  412 ? 1.73597   14.92462 47.53072 1.000 68.18998  ? 412 TRP   A CA  1 
ATOM   3200 C C   . TRP   A 1  412 ? 2.54995   13.69223 47.17375 1.000 70.52865  ? 412 TRP   A C   1 
ATOM   3201 O O   . TRP   A 1  412 ? 2.36368   13.11799 46.09509 1.000 74.07302  ? 412 TRP   A O   1 
ATOM   3202 C CB  . TRP   A 1  412 ? 1.38680   15.74519 46.29140 1.000 69.34464  ? 412 TRP   A CB  1 
ATOM   3203 C CG  . TRP   A 1  412 ? 0.33988   16.75646 46.62177 1.000 69.10633  ? 412 TRP   A CG  1 
ATOM   3204 C CD1 . TRP   A 1  412 ? 0.54297   18.01632 47.09188 1.000 67.21305  ? 412 TRP   A CD1 1 
ATOM   3205 C CD2 . TRP   A 1  412 ? -1.08678  16.57700 46.55179 1.000 69.47131  ? 412 TRP   A CD2 1 
ATOM   3206 N NE1 . TRP   A 1  412 ? -0.66901  18.64481 47.29922 1.000 70.38053  ? 412 TRP   A NE1 1 
ATOM   3207 C CE2 . TRP   A 1  412 ? -1.68065  17.78112 46.97987 1.000 62.79255  ? 412 TRP   A CE2 1 
ATOM   3208 C CE3 . TRP   A 1  412 ? -1.91657  15.51686 46.16040 1.000 69.44951  ? 412 TRP   A CE3 1 
ATOM   3209 C CZ2 . TRP   A 1  412 ? -3.06664  17.95816 47.02167 1.000 70.28012  ? 412 TRP   A CZ2 1 
ATOM   3210 C CZ3 . TRP   A 1  412 ? -3.30010  15.69313 46.20760 1.000 65.93999  ? 412 TRP   A CZ3 1 
ATOM   3211 C CH2 . TRP   A 1  412 ? -3.85779  16.90121 46.63212 1.000 66.14413  ? 412 TRP   A CH2 1 
ATOM   3212 N N   . GLY   A 1  413 ? 3.45855   13.28053 48.05374 1.000 67.35135  ? 413 GLY   A N   1 
ATOM   3213 C CA  . GLY   A 1  413 ? 4.05723   11.97227 47.96374 1.000 63.25290  ? 413 GLY   A CA  1 
ATOM   3214 C C   . GLY   A 1  413 ? 5.48463   11.93735 47.46843 1.000 64.05242  ? 413 GLY   A C   1 
ATOM   3215 O O   . GLY   A 1  413 ? 6.13774   10.90102 47.61669 1.000 75.08697  ? 413 GLY   A O   1 
ATOM   3216 N N   . ASN   A 1  414 ? 5.99409   13.02501 46.90775 1.000 67.46932  ? 414 ASN   A N   1 
ATOM   3217 C CA  . ASN   A 1  414 ? 7.30561   13.02290 46.27146 1.000 69.46490  ? 414 ASN   A CA  1 
ATOM   3218 C C   . ASN   A 1  414 ? 8.42482   13.36668 47.24006 1.000 61.62794  ? 414 ASN   A C   1 
ATOM   3219 O O   . ASN   A 1  414 ? 8.27509   14.20470 48.13321 1.000 62.07383  ? 414 ASN   A O   1 
ATOM   3220 C CB  . ASN   A 1  414 ? 7.35810   14.01853 45.10958 1.000 66.18948  ? 414 ASN   A CB  1 
ATOM   3221 C CG  . ASN   A 1  414 ? 6.56245   13.55113 43.91688 1.000 69.68639  ? 414 ASN   A CG  1 
ATOM   3222 O OD1 . ASN   A 1  414 ? 5.57864   14.19669 43.53251 1.000 62.40487  ? 414 ASN   A OD1 1 
ATOM   3223 N ND2 . ASN   A 1  414 ? 6.95879   12.39511 43.33844 1.000 61.62759  ? 414 ASN   A ND2 1 
ATOM   3224 N N   . ASN   A 1  415 ? 9.56882   12.73205 47.01118 1.000 62.50665  ? 415 ASN   A N   1 
ATOM   3225 C CA  . ASN   A 1  415 ? 10.79413  13.05313 47.72951 1.000 63.14394  ? 415 ASN   A CA  1 
ATOM   3226 C C   . ASN   A 1  415 ? 11.25881  14.47783 47.41557 1.000 59.54626  ? 415 ASN   A C   1 
ATOM   3227 O O   . ASN   A 1  415 ? 11.29409  14.91416 46.25509 1.000 55.04367  ? 415 ASN   A O   1 
ATOM   3228 C CB  . ASN   A 1  415 ? 11.88933  12.04431 47.36175 1.000 60.81337  ? 415 ASN   A CB  1 
ATOM   3229 C CG  . ASN   A 1  415 ? 11.79375  10.74026 48.16050 1.000 63.30919  ? 415 ASN   A CG  1 
ATOM   3230 O OD1 . ASN   A 1  415 ? 10.85076  10.53060 48.92000 1.000 65.05085  ? 415 ASN   A OD1 1 
ATOM   3231 N ND2 . ASN   A 1  415 ? 12.78032  9.85784  47.98298 1.000 59.72374  ? 415 ASN   A ND2 1 
ATOM   3232 N N   . ALA   A 1  416 ? 11.63017  15.18890 48.46728 1.000 56.26088  ? 416 ALA   A N   1 
ATOM   3233 C CA  . ALA   A 1  416 ? 12.11816  16.55340 48.40333 1.000 55.35088  ? 416 ALA   A CA  1 
ATOM   3234 C C   . ALA   A 1  416 ? 13.34743  16.64108 49.28566 1.000 57.11245  ? 416 ALA   A C   1 
ATOM   3235 O O   . ALA   A 1  416 ? 13.39788  16.00009 50.33897 1.000 56.48573  ? 416 ALA   A O   1 
ATOM   3236 C CB  . ALA   A 1  416 ? 11.06037  17.54256 48.89526 1.000 52.79120  ? 416 ALA   A CB  1 
ATOM   3237 N N   . PHE   A 1  417 ? 14.33232  17.42298 48.85419 1.000 50.31178  ? 417 PHE   A N   1 
ATOM   3238 C CA  . PHE   A 1  417 ? 15.54580  17.63831 49.62194 1.000 49.85046  ? 417 PHE   A CA  1 
ATOM   3239 C C   . PHE   A 1  417 ? 15.77058  19.13696 49.74015 1.000 53.21176  ? 417 PHE   A C   1 
ATOM   3240 O O   . PHE   A 1  417 ? 15.65342  19.87085 48.74674 1.000 52.39504  ? 417 PHE   A O   1 
ATOM   3241 C CB  . PHE   A 1  417 ? 16.74617  16.93491 48.96984 1.000 53.75228  ? 417 PHE   A CB  1 
ATOM   3242 C CG  . PHE   A 1  417 ? 16.52267  15.47221 48.73779 1.000 52.75935  ? 417 PHE   A CG  1 
ATOM   3243 C CD1 . PHE   A 1  417 ? 15.91037  15.03043 47.57632 1.000 48.92334  ? 417 PHE   A CD1 1 
ATOM   3244 C CD2 . PHE   A 1  417 ? 16.90692  14.53876 49.68684 1.000 57.78949  ? 417 PHE   A CD2 1 
ATOM   3245 C CE1 . PHE   A 1  417 ? 15.65219  13.68673 47.36206 1.000 52.85118  ? 417 PHE   A CE1 1 
ATOM   3246 C CE2 . PHE   A 1  417 ? 16.68390  13.18466 49.47378 1.000 56.85974  ? 417 PHE   A CE2 1 
ATOM   3247 C CZ  . PHE   A 1  417 ? 16.04860  12.75920 48.30326 1.000 55.88301  ? 417 PHE   A CZ  1 
ATOM   3248 N N   . PHE   A 1  418 ? 16.05852  19.59213 50.95857 1.000 50.65984  ? 418 PHE   A N   1 
ATOM   3249 C CA  . PHE   A 1  418 ? 16.23262  21.01039 51.24146 1.000 53.11564  ? 418 PHE   A CA  1 
ATOM   3250 C C   . PHE   A 1  418 ? 17.62037  21.26484 51.81222 1.000 55.53174  ? 418 PHE   A C   1 
ATOM   3251 O O   . PHE   A 1  418 ? 18.07079  20.55411 52.72687 1.000 53.03430  ? 418 PHE   A O   1 
ATOM   3252 C CB  . PHE   A 1  418 ? 15.16680  21.53489 52.21130 1.000 47.93221  ? 418 PHE   A CB  1 
ATOM   3253 C CG  . PHE   A 1  418 ? 15.01901  23.02389 52.16666 1.000 54.25563  ? 418 PHE   A CG  1 
ATOM   3254 C CD1 . PHE   A 1  418 ? 15.90873  23.84449 52.86515 1.000 53.46097  ? 418 PHE   A CD1 1 
ATOM   3255 C CD2 . PHE   A 1  418 ? 14.02065  23.62115 51.38205 1.000 53.04208  ? 418 PHE   A CD2 1 
ATOM   3256 C CE1 . PHE   A 1  418 ? 15.79285  25.23193 52.80257 1.000 51.79039  ? 418 PHE   A CE1 1 
ATOM   3257 C CE2 . PHE   A 1  418 ? 13.89783  25.00560 51.31624 1.000 48.38180  ? 418 PHE   A CE2 1 
ATOM   3258 C CZ  . PHE   A 1  418 ? 14.77395  25.80370 52.03151 1.000 54.56024  ? 418 PHE   A CZ  1 
ATOM   3259 N N   . TYR   A 1  419 ? 18.27875  22.29559 51.28968 1.000 53.23416  ? 419 TYR   A N   1 
ATOM   3260 C CA  . TYR   A 1  419 ? 19.60376  22.68244 51.75299 1.000 54.46297  ? 419 TYR   A CA  1 
ATOM   3261 C C   . TYR   A 1  419 ? 19.60499  24.12304 52.23328 1.000 53.02029  ? 419 TYR   A C   1 
ATOM   3262 O O   . TYR   A 1  419 ? 18.74815  24.92757 51.85671 1.000 57.14251  ? 419 TYR   A O   1 
ATOM   3263 C CB  . TYR   A 1  419 ? 20.66173  22.51395 50.65919 1.000 51.43632  ? 419 TYR   A CB  1 
ATOM   3264 C CG  . TYR   A 1  419 ? 20.59694  23.54382 49.54886 1.000 53.29092  ? 419 TYR   A CG  1 
ATOM   3265 C CD1 . TYR   A 1  419 ? 21.11145  24.82692 49.71880 1.000 44.91210  ? 419 TYR   A CD1 1 
ATOM   3266 C CD2 . TYR   A 1  419 ? 20.03521  23.22077 48.31519 1.000 53.55530  ? 419 TYR   A CD2 1 
ATOM   3267 C CE1 . TYR   A 1  419 ? 21.05118  25.75199 48.70626 1.000 53.26816  ? 419 TYR   A CE1 1 
ATOM   3268 C CE2 . TYR   A 1  419 ? 19.99068  24.14615 47.28330 1.000 48.90497  ? 419 TYR   A CE2 1 
ATOM   3269 C CZ  . TYR   A 1  419 ? 20.49821  25.40247 47.48138 1.000 52.68271  ? 419 TYR   A CZ  1 
ATOM   3270 O OH  . TYR   A 1  419 ? 20.43792  26.32746 46.45980 1.000 52.97724  ? 419 TYR   A OH  1 
ATOM   3271 N N   . TYR   A 1  420 ? 20.62457  24.43970 53.02806 1.000 54.08448  ? 420 TYR   A N   1 
ATOM   3272 C CA  . TYR   A 1  420 ? 20.85882  25.77186 53.57654 1.000 52.57189  ? 420 TYR   A CA  1 
ATOM   3273 C C   . TYR   A 1  420 ? 22.33017  26.09537 53.36051 1.000 57.32098  ? 420 TYR   A C   1 
ATOM   3274 O O   . TYR   A 1  420 ? 23.19503  25.55212 54.06066 1.000 51.21189  ? 420 TYR   A O   1 
ATOM   3275 C CB  . TYR   A 1  420 ? 20.52007  25.80400 55.06348 1.000 53.35442  ? 420 TYR   A CB  1 
ATOM   3276 C CG  . TYR   A 1  420 ? 20.51385  27.16484 55.71603 1.000 56.43647  ? 420 TYR   A CG  1 
ATOM   3277 C CD1 . TYR   A 1  420 ? 19.76451  28.21391 55.18416 1.000 55.05070  ? 420 TYR   A CD1 1 
ATOM   3278 C CD2 . TYR   A 1  420 ? 21.23351  27.39409 56.88884 1.000 49.14562  ? 420 TYR   A CD2 1 
ATOM   3279 C CE1 . TYR   A 1  420 ? 19.73048  29.46833 55.80511 1.000 52.38688  ? 420 TYR   A CE1 1 
ATOM   3280 C CE2 . TYR   A 1  420 ? 21.20263  28.63628 57.51469 1.000 57.63009  ? 420 TYR   A CE2 1 
ATOM   3281 C CZ  . TYR   A 1  420 ? 20.44820  29.67684 56.96416 1.000 57.53000  ? 420 TYR   A CZ  1 
ATOM   3282 O OH  . TYR   A 1  420 ? 20.40934  30.91687 57.57441 1.000 63.21510  ? 420 TYR   A OH  1 
ATOM   3283 N N   . PHE   A 1  421 ? 22.61751  26.96521 52.39342 1.000 57.84276  ? 421 PHE   A N   1 
ATOM   3284 C CA  . PHE   A 1  421 ? 23.99669  27.28647 52.01652 1.000 54.79736  ? 421 PHE   A CA  1 
ATOM   3285 C C   . PHE   A 1  421 ? 24.51681  28.42082 52.89617 1.000 52.00636  ? 421 PHE   A C   1 
ATOM   3286 O O   . PHE   A 1  421 ? 23.94876  29.51777 52.89080 1.000 53.01638  ? 421 PHE   A O   1 
ATOM   3287 C CB  . PHE   A 1  421 ? 24.04874  27.66992 50.53456 1.000 51.85160  ? 421 PHE   A CB  1 
ATOM   3288 C CG  . PHE   A 1  421 ? 25.44329  27.88929 49.99007 1.000 56.44488  ? 421 PHE   A CG  1 
ATOM   3289 C CD1 . PHE   A 1  421 ? 26.26995  26.81194 49.66803 1.000 55.44656  ? 421 PHE   A CD1 1 
ATOM   3290 C CD2 . PHE   A 1  421 ? 25.92736  29.18296 49.78749 1.000 56.01443  ? 421 PHE   A CD2 1 
ATOM   3291 C CE1 . PHE   A 1  421 ? 27.56802  27.01915 49.15732 1.000 60.33676  ? 421 PHE   A CE1 1 
ATOM   3292 C CE2 . PHE   A 1  421 ? 27.21155  29.40029 49.27747 1.000 57.46109  ? 421 PHE   A CE2 1 
ATOM   3293 C CZ  . PHE   A 1  421 ? 28.03447  28.31284 48.96136 1.000 61.61882  ? 421 PHE   A CZ  1 
ATOM   3294 N N   . GLU   A 1  422 ? 25.60900  28.17553 53.63571 1.000 56.67359  ? 422 GLU   A N   1 
ATOM   3295 C CA  . GLU   A 1  422 ? 26.12195  29.19964 54.54124 1.000 55.93053  ? 422 GLU   A CA  1 
ATOM   3296 C C   . GLU   A 1  422 ? 27.63023  29.38042 54.41617 1.000 59.76234  ? 422 GLU   A C   1 
ATOM   3297 O O   . GLU   A 1  422 ? 28.31741  29.70643 55.39150 1.000 62.99914  ? 422 GLU   A O   1 
ATOM   3298 C CB  . GLU   A 1  422 ? 25.73351  28.89998 55.99025 1.000 55.71184  ? 422 GLU   A CB  1 
ATOM   3299 C CG  . GLU   A 1  422 ? 26.11005  27.54669 56.50352 1.000 63.94445  ? 422 GLU   A CG  1 
ATOM   3300 C CD  . GLU   A 1  422 ? 25.33173  27.17322 57.77027 1.000 70.59623  ? 422 GLU   A CD  1 
ATOM   3301 O OE1 . GLU   A 1  422 ? 24.38780  27.90736 58.13722 1.000 67.59396  ? 422 GLU   A OE1 1 
ATOM   3302 O OE2 . GLU   A 1  422 ? 25.66916  26.14665 58.39552 1.000 73.88797  ? 422 GLU   A OE2 1 
ATOM   3303 N N   . HIS   A 1  423 ? 28.18030  29.20000 53.23169 1.000 62.07040  ? 423 HIS   A N   1 
ATOM   3304 C CA  . HIS   A 1  423 ? 29.58155  29.50959 53.01899 1.000 59.53730  ? 423 HIS   A CA  1 
ATOM   3305 C C   . HIS   A 1  423 ? 29.70228  30.80937 52.23991 1.000 60.44000  ? 423 HIS   A C   1 
ATOM   3306 O O   . HIS   A 1  423 ? 29.16484  30.92768 51.13338 1.000 55.18568  ? 423 HIS   A O   1 
ATOM   3307 C CB  . HIS   A 1  423 ? 30.32050  28.40315 52.28257 1.000 58.74885  ? 423 HIS   A CB  1 
ATOM   3308 C CG  . HIS   A 1  423 ? 31.74571  28.75937 52.01258 1.000 60.57465  ? 423 HIS   A CG  1 
ATOM   3309 N ND1 . HIS   A 1  423 ? 32.65459  28.98840 53.02567 1.000 65.04598  ? 423 HIS   A ND1 1 
ATOM   3310 C CD2 . HIS   A 1  423 ? 32.40770  28.98897 50.85473 1.000 61.84579  ? 423 HIS   A CD2 1 
ATOM   3311 C CE1 . HIS   A 1  423 ? 33.82428  29.31798 52.50408 1.000 60.14687  ? 423 HIS   A CE1 1 
ATOM   3312 N NE2 . HIS   A 1  423 ? 33.70056  29.33066 51.18797 1.000 65.20068  ? 423 HIS   A NE2 1 
ATOM   3313 N N   . ARG   A 1  424 ? 30.41705  31.77521 52.81846 1.000 63.71459  ? 424 ARG   A N   1 
ATOM   3314 C CA  . ARG   A 1  424 ? 30.74928  33.01387 52.12695 1.000 59.93739  ? 424 ARG   A CA  1 
ATOM   3315 C C   . ARG   A 1  424 ? 32.00595  32.80477 51.29110 1.000 62.44675  ? 424 ARG   A C   1 
ATOM   3316 O O   . ARG   A 1  424 ? 33.07495  32.54234 51.84505 1.000 59.71525  ? 424 ARG   A O   1 
ATOM   3317 C CB  . ARG   A 1  424 ? 30.97165  34.14297 53.12988 1.000 63.27263  ? 424 ARG   A CB  1 
ATOM   3318 C CG  . ARG   A 1  424 ? 31.66725  35.37112 52.53309 1.000 63.50809  ? 424 ARG   A CG  1 
ATOM   3319 C CD  . ARG   A 1  424 ? 31.64984  36.54340 53.49236 1.000 65.63587  ? 424 ARG   A CD  1 
ATOM   3320 N NE  . ARG   A 1  424 ? 31.68583  37.83474 52.81392 1.000 77.13297  ? 424 ARG   A NE  1 
ATOM   3321 C CZ  . ARG   A 1  424 ? 32.78707  38.39135 52.32682 1.000 79.08952  ? 424 ARG   A CZ  1 
ATOM   3322 N NH1 . ARG   A 1  424 ? 33.96183  37.78610 52.41069 1.000 84.23479  ? 424 ARG   A NH1 1 
ATOM   3323 N NH2 . ARG   A 1  424 ? 32.70983  39.58297 51.73791 1.000 76.06670  ? 424 ARG   A NH2 1 
ATOM   3324 N N   . SER   A 1  425 ? 31.86908  32.91771 49.96780 1.000 62.46389  ? 425 SER   A N   1 
ATOM   3325 C CA  . SER   A 1  425 ? 32.99644  32.79729 49.04900 1.000 64.52200  ? 425 SER   A CA  1 
ATOM   3326 C C   . SER   A 1  425 ? 34.19764  33.59673 49.54870 1.000 69.62686  ? 425 SER   A C   1 
ATOM   3327 O O   . SER   A 1  425 ? 34.05531  34.71673 50.04466 1.000 74.39076  ? 425 SER   A O   1 
ATOM   3328 C CB  . SER   A 1  425 ? 32.57624  33.27836 47.65354 1.000 65.62515  ? 425 SER   A CB  1 
ATOM   3329 O OG  . SER   A 1  425 ? 33.64738  33.23730 46.72201 1.000 74.58197  ? 425 SER   A OG  1 
ATOM   3330 N N   . SER   A 1  426 ? 35.38805  32.99785 49.44483 1.000 69.30986  ? 426 SER   A N   1 
ATOM   3331 C CA  . SER   A 1  426 ? 36.61846  33.70226 49.79877 1.000 71.91715  ? 426 SER   A CA  1 
ATOM   3332 C C   . SER   A 1  426 ? 36.99705  34.76446 48.77118 1.000 72.38758  ? 426 SER   A C   1 
ATOM   3333 O O   . SER   A 1  426 ? 37.75312  35.68363 49.09756 1.000 67.45315  ? 426 SER   A O   1 
ATOM   3334 C CB  . SER   A 1  426 ? 37.77678  32.70708 49.97290 1.000 67.15239  ? 426 SER   A CB  1 
ATOM   3335 O OG  . SER   A 1  426 ? 38.35049  32.36002 48.71533 1.000 73.46631  ? 426 SER   A OG  1 
ATOM   3336 N N   . LYS   A 1  427 ? 36.50517  34.66069 47.54256 1.000 73.88878  ? 427 LYS   A N   1 
ATOM   3337 C CA  . LYS   A 1  427 ? 36.75153  35.67792 46.53055 1.000 78.03593  ? 427 LYS   A CA  1 
ATOM   3338 C C   . LYS   A 1  427 ? 35.61552  36.70498 46.44580 1.000 78.62097  ? 427 LYS   A C   1 
ATOM   3339 O O   . LYS   A 1  427 ? 35.65130  37.58319 45.57640 1.000 79.84218  ? 427 LYS   A O   1 
ATOM   3340 C CB  . LYS   A 1  427 ? 36.98628  35.01012 45.16442 1.000 78.77749  ? 427 LYS   A CB  1 
ATOM   3341 C CG  . LYS   A 1  427 ? 38.02855  33.88174 45.19112 1.000 85.95193  ? 427 LYS   A CG  1 
ATOM   3342 C CD  . LYS   A 1  427 ? 38.49045  33.41095 43.79798 1.000 91.44323  ? 427 LYS   A CD  1 
ATOM   3343 C CE  . LYS   A 1  427 ? 38.05939  34.33738 42.65838 1.000 91.28087  ? 427 LYS   A CE  1 
ATOM   3344 N NZ  . LYS   A 1  427 ? 38.71319  33.92124 41.37666 1.000 97.91493  ? 427 LYS   A NZ  1 
ATOM   3345 N N   . LEU   A 1  428 ? 34.61562  36.61367 47.32369 1.000 77.73522  ? 428 LEU   A N   1 
ATOM   3346 C CA  . LEU   A 1  428 ? 33.41222  37.44077 47.21846 1.000 75.28719  ? 428 LEU   A CA  1 
ATOM   3347 C C   . LEU   A 1  428 ? 33.77390  38.91008 47.36299 1.000 71.10000  ? 428 LEU   A C   1 
ATOM   3348 O O   . LEU   A 1  428 ? 34.32885  39.30321 48.39859 1.000 77.47567  ? 428 LEU   A O   1 
ATOM   3349 C CB  . LEU   A 1  428 ? 32.38153  37.07060 48.27823 1.000 68.21637  ? 428 LEU   A CB  1 
ATOM   3350 C CG  . LEU   A 1  428 ? 31.05618  37.82625 48.16806 1.000 69.60035  ? 428 LEU   A CG  1 
ATOM   3351 C CD1 . LEU   A 1  428 ? 30.02308  36.93403 47.59531 1.000 64.82566  ? 428 LEU   A CD1 1 
ATOM   3352 C CD2 . LEU   A 1  428 ? 30.57505  38.37414 49.51244 1.000 73.61353  ? 428 LEU   A CD2 1 
ATOM   3353 N N   . PRO   A 1  429 ? 33.48139  39.75051 46.36889 1.000 68.21378  ? 429 PRO   A N   1 
ATOM   3354 C CA  . PRO   A 1  429 ? 33.97643  41.13723 46.40748 1.000 68.63603  ? 429 PRO   A CA  1 
ATOM   3355 C C   . PRO   A 1  429 ? 33.15013  42.09158 47.26030 1.000 67.85379  ? 429 PRO   A C   1 
ATOM   3356 O O   . PRO   A 1  429 ? 33.68342  43.13011 47.66885 1.000 67.91472  ? 429 PRO   A O   1 
ATOM   3357 C CB  . PRO   A 1  429 ? 33.96475  41.55217 44.93204 1.000 60.97927  ? 429 PRO   A CB  1 
ATOM   3358 C CG  . PRO   A 1  429 ? 33.04149  40.62092 44.26137 1.000 61.84952  ? 429 PRO   A CG  1 
ATOM   3359 C CD  . PRO   A 1  429 ? 32.91175  39.38106 45.06580 1.000 68.17595  ? 429 PRO   A CD  1 
ATOM   3360 N N   . TRP   A 1  430 ? 31.88846  41.77679 47.54500 1.000 62.46681  ? 430 TRP   A N   1 
ATOM   3361 C CA  . TRP   A 1  430 ? 31.06698  42.57783 48.44294 1.000 68.00562  ? 430 TRP   A CA  1 
ATOM   3362 C C   . TRP   A 1  430 ? 31.61614  42.52161 49.87604 1.000 65.80753  ? 430 TRP   A C   1 
ATOM   3363 O O   . TRP   A 1  430 ? 32.35792  41.60537 50.23136 1.000 61.38105  ? 430 TRP   A O   1 
ATOM   3364 C CB  . TRP   A 1  430 ? 29.62339  42.07612 48.41905 1.000 63.35866  ? 430 TRP   A CB  1 
ATOM   3365 C CG  . TRP   A 1  430 ? 28.94799  42.10687 47.07719 1.000 61.88365  ? 430 TRP   A CG  1 
ATOM   3366 C CD1 . TRP   A 1  430 ? 28.87260  41.08282 46.18082 1.000 56.80438  ? 430 TRP   A CD1 1 
ATOM   3367 C CD2 . TRP   A 1  430 ? 28.23213  43.20736 46.48778 1.000 64.06082  ? 430 TRP   A CD2 1 
ATOM   3368 N NE1 . TRP   A 1  430 ? 28.16184  41.47288 45.06804 1.000 57.49362  ? 430 TRP   A NE1 1 
ATOM   3369 C CE2 . TRP   A 1  430 ? 27.75481  42.76955 45.22900 1.000 59.16092  ? 430 TRP   A CE2 1 
ATOM   3370 C CE3 . TRP   A 1  430 ? 27.94434  44.51855 46.90183 1.000 62.27853  ? 430 TRP   A CE3 1 
ATOM   3371 C CZ2 . TRP   A 1  430 ? 27.01215  43.59433 44.37483 1.000 52.78985  ? 430 TRP   A CZ2 1 
ATOM   3372 C CZ3 . TRP   A 1  430 ? 27.20347  45.33478 46.05548 1.000 61.52371  ? 430 TRP   A CZ3 1 
ATOM   3373 C CH2 . TRP   A 1  430 ? 26.74255  44.86440 44.80492 1.000 60.44075  ? 430 TRP   A CH2 1 
ATOM   3374 N N   . PRO   A 1  431 ? 31.24225  43.47131 50.73158 1.000 64.61137  ? 431 PRO   A N   1 
ATOM   3375 C CA  . PRO   A 1  431 ? 31.83221  43.51349 52.07524 1.000 69.28103  ? 431 PRO   A CA  1 
ATOM   3376 C C   . PRO   A 1  431 ? 31.30565  42.38226 52.94310 1.000 65.49191  ? 431 PRO   A C   1 
ATOM   3377 O O   . PRO   A 1  431 ? 30.29909  41.73631 52.64953 1.000 67.74674  ? 431 PRO   A O   1 
ATOM   3378 C CB  . PRO   A 1  431 ? 31.39367  44.87415 52.62300 1.000 61.60646  ? 431 PRO   A CB  1 
ATOM   3379 C CG  . PRO   A 1  431 ? 30.04074  45.06875 51.98147 1.000 66.28289  ? 431 PRO   A CG  1 
ATOM   3380 C CD  . PRO   A 1  431 ? 30.19644  44.50399 50.57065 1.000 67.51427  ? 431 PRO   A CD  1 
ATOM   3381 N N   . GLU   A 1  432 ? 31.98811  42.19971 54.07029 1.000 69.01880  ? 432 GLU   A N   1 
ATOM   3382 C CA  . GLU   A 1  432 ? 31.73833  41.06821 54.95258 1.000 71.74950  ? 432 GLU   A CA  1 
ATOM   3383 C C   . GLU   A 1  432 ? 30.37480  41.14211 55.65239 1.000 66.22978  ? 432 GLU   A C   1 
ATOM   3384 O O   . GLU   A 1  432 ? 29.77619  40.09695 55.92645 1.000 64.49510  ? 432 GLU   A O   1 
ATOM   3385 C CB  . GLU   A 1  432 ? 32.88800  40.96079 55.96888 1.000 75.63860  ? 432 GLU   A CB  1 
ATOM   3386 C CG  . GLU   A 1  432 ? 34.32289  41.06175 55.35111 1.000 84.19566  ? 432 GLU   A CG  1 
ATOM   3387 C CD  . GLU   A 1  432 ? 34.86571  42.50817 55.11166 1.000 94.88304  ? 432 GLU   A CD  1 
ATOM   3388 O OE1 . GLU   A 1  432 ? 34.47961  43.45638 55.84441 1.000 93.81974  ? 432 GLU   A OE1 1 
ATOM   3389 O OE2 . GLU   A 1  432 ? 35.71447  42.67927 54.19555 1.000 92.54363  ? 432 GLU   A OE2 1 
ATOM   3390 N N   . TRP   A 1  433 ? 29.84922  42.33818 55.94457 1.000 69.23656  ? 433 TRP   A N   1 
ATOM   3391 C CA  . TRP   A 1  433 ? 28.55609  42.38379 56.63660 1.000 65.05578  ? 433 TRP   A CA  1 
ATOM   3392 C C   . TRP   A 1  433 ? 27.42871  41.87422 55.76262 1.000 62.67510  ? 433 TRP   A C   1 
ATOM   3393 O O   . TRP   A 1  433 ? 26.37848  41.50432 56.29169 1.000 68.71586  ? 433 TRP   A O   1 
ATOM   3394 C CB  . TRP   A 1  433 ? 28.19960  43.79813 57.14222 1.000 63.89465  ? 433 TRP   A CB  1 
ATOM   3395 C CG  . TRP   A 1  433 ? 27.83793  44.78767 56.05814 1.000 69.66232  ? 433 TRP   A CG  1 
ATOM   3396 C CD1 . TRP   A 1  433 ? 28.67525  45.71328 55.48519 1.000 63.51585  ? 433 TRP   A CD1 1 
ATOM   3397 C CD2 . TRP   A 1  433 ? 26.55680  44.94738 55.40915 1.000 61.12989  ? 433 TRP   A CD2 1 
ATOM   3398 N NE1 . TRP   A 1  433 ? 27.98831  46.43960 54.53048 1.000 70.07709  ? 433 TRP   A NE1 1 
ATOM   3399 C CE2 . TRP   A 1  433 ? 26.69402  45.98803 54.46001 1.000 65.76158  ? 433 TRP   A CE2 1 
ATOM   3400 C CE3 . TRP   A 1  433 ? 25.31595  44.31652 55.53815 1.000 60.64549  ? 433 TRP   A CE3 1 
ATOM   3401 C CZ2 . TRP   A 1  433 ? 25.62857  46.41105 53.64382 1.000 70.25522  ? 433 TRP   A CZ2 1 
ATOM   3402 C CZ3 . TRP   A 1  433 ? 24.25289  44.73492 54.71706 1.000 64.79347  ? 433 TRP   A CZ3 1 
ATOM   3403 C CH2 . TRP   A 1  433 ? 24.42001  45.76871 53.78496 1.000 65.41073  ? 433 TRP   A CH2 1 
ATOM   3404 N N   . MET   A 1  434 ? 27.61276  41.83735 54.44345 1.000 65.51898  ? 434 MET   A N   1 
ATOM   3405 C CA  . MET   A 1  434 ? 26.55645  41.28848 53.60090 1.000 64.20207  ? 434 MET   A CA  1 
ATOM   3406 C C   . MET   A 1  434 ? 26.46410  39.77317 53.65511 1.000 58.44635  ? 434 MET   A C   1 
ATOM   3407 O O   . MET   A 1  434 ? 25.46773  39.23123 53.16945 1.000 56.75182  ? 434 MET   A O   1 
ATOM   3408 C CB  . MET   A 1  434 ? 26.73089  41.73248 52.14896 1.000 61.41584  ? 434 MET   A CB  1 
ATOM   3409 C CG  . MET   A 1  434 ? 26.05849  43.05172 51.88044 1.000 67.90177  ? 434 MET   A CG  1 
ATOM   3410 S SD  . MET   A 1  434 ? 26.77653  43.95731 50.51942 1.000 71.19180  ? 434 MET   A SD  1 
ATOM   3411 C CE  . MET   A 1  434 ? 25.35545  44.04626 49.46110 1.000 65.34234  ? 434 MET   A CE  1 
ATOM   3412 N N   . GLY   A 1  435 ? 27.48339  39.08457 54.18395 1.000 58.14356  ? 435 GLY   A N   1 
ATOM   3413 C CA  . GLY   A 1  435 ? 27.35543  37.66077 54.48512 1.000 54.02467  ? 435 GLY   A CA  1 
ATOM   3414 C C   . GLY   A 1  435 ? 27.24119  36.76734 53.25895 1.000 61.49363  ? 435 GLY   A C   1 
ATOM   3415 O O   . GLY   A 1  435 ? 27.90066  36.97569 52.22783 1.000 61.49889  ? 435 GLY   A O   1 
ATOM   3416 N N   . VAL   A 1  436 ? 26.39512  35.74351 53.38064 1.000 57.06037  ? 436 VAL   A N   1 
ATOM   3417 C CA  . VAL   A 1  436 ? 26.28996  34.67087 52.35892 1.000 58.20511  ? 436 VAL   A CA  1 
ATOM   3418 C C   . VAL   A 1  436 ? 25.20468  35.13199 51.38867 1.000 56.35864  ? 436 VAL   A C   1 
ATOM   3419 O O   . VAL   A 1  436 ? 24.02321  34.79100 51.49621 1.000 59.19076  ? 436 VAL   A O   1 
ATOM   3420 C CB  . VAL   A 1  436 ? 25.99687  33.30135 52.99305 1.000 59.52510  ? 436 VAL   A CB  1 
ATOM   3421 C CG1 . VAL   A 1  436 ? 26.01662  32.17721 51.95686 1.000 55.30821  ? 436 VAL   A CG1 1 
ATOM   3422 C CG2 . VAL   A 1  436 ? 26.98455  33.00848 54.12309 1.000 55.78289  ? 436 VAL   A CG2 1 
ATOM   3423 N N   . MET   A 1  437 ? 25.61351  35.93870 50.41865 1.000 55.84728  ? 437 MET   A N   1 
ATOM   3424 C CA  . MET   A 1  437 ? 24.64441  36.69762 49.64154 1.000 58.01149  ? 437 MET   A CA  1 
ATOM   3425 C C   . MET   A 1  437 ? 23.86938  35.87551 48.61916 1.000 56.89654  ? 437 MET   A C   1 
ATOM   3426 O O   . MET   A 1  437 ? 24.27534  34.79388 48.18220 1.000 55.00440  ? 437 MET   A O   1 
ATOM   3427 C CB  . MET   A 1  437 ? 25.32194  37.85988 48.93447 1.000 59.94754  ? 437 MET   A CB  1 
ATOM   3428 C CG  . MET   A 1  437 ? 25.78378  38.96468 49.85042 1.000 59.60529  ? 437 MET   A CG  1 
ATOM   3429 S SD  . MET   A 1  437 ? 26.91990  39.93743 48.88900 1.000 63.74847  ? 437 MET   A SD  1 
ATOM   3430 C CE  . MET   A 1  437 ? 25.80805  40.95907 47.96379 1.000 59.38037  ? 437 MET   A CE  1 
ATOM   3431 N N   . HIS   A 1  438 ? 22.72901  36.44319 48.23713 1.000 55.35440  ? 438 HIS   A N   1 
ATOM   3432 C CA  . HIS   A 1  438 ? 21.93037  35.96381 47.11593 1.000 56.76589  ? 438 HIS   A CA  1 
ATOM   3433 C C   . HIS   A 1  438 ? 22.78205  35.79596 45.86278 1.000 51.41611  ? 438 HIS   A C   1 
ATOM   3434 O O   . HIS   A 1  438 ? 23.39277  36.75340 45.38864 1.000 53.29452  ? 438 HIS   A O   1 
ATOM   3435 C CB  . HIS   A 1  438 ? 20.78783  36.95533 46.85619 1.000 46.15094  ? 438 HIS   A CB  1 
ATOM   3436 C CG  . HIS   A 1  438 ? 19.84650  36.52491 45.77800 1.000 55.40036  ? 438 HIS   A CG  1 
ATOM   3437 N ND1 . HIS   A 1  438 ? 18.87493  35.55977 45.97512 1.000 48.99059  ? 438 HIS   A ND1 1 
ATOM   3438 C CD2 . HIS   A 1  438 ? 19.70187  36.94795 44.49762 1.000 57.88999  ? 438 HIS   A CD2 1 
ATOM   3439 C CE1 . HIS   A 1  438 ? 18.17631  35.40850 44.86266 1.000 49.28674  ? 438 HIS   A CE1 1 
ATOM   3440 N NE2 . HIS   A 1  438 ? 18.65189  36.24239 43.95227 1.000 54.44000  ? 438 HIS   A NE2 1 
ATOM   3441 N N   . GLY   A 1  439 ? 22.80957  34.57747 45.32777 1.000 56.07792  ? 439 GLY   A N   1 
ATOM   3442 C CA  . GLY   A 1  439 ? 23.46769  34.27372 44.07272 1.000 58.34436  ? 439 GLY   A CA  1 
ATOM   3443 C C   . GLY   A 1  439 ? 24.86272  33.68229 44.17939 1.000 58.37388  ? 439 GLY   A C   1 
ATOM   3444 O O   . GLY   A 1  439 ? 25.40374  33.24183 43.16014 1.000 57.84874  ? 439 GLY   A O   1 
ATOM   3445 N N   . TYR   A 1  440 ? 25.47663  33.66957 45.36356 1.000 60.78358  ? 440 TYR   A N   1 
ATOM   3446 C CA  . TYR   A 1  440 ? 26.88942  33.31396 45.47705 1.000 57.91707  ? 440 TYR   A CA  1 
ATOM   3447 C C   . TYR   A 1  440 ? 27.10245  31.87111 45.92384 1.000 56.18677  ? 440 TYR   A C   1 
ATOM   3448 O O   . TYR   A 1  440 ? 28.19735  31.51553 46.38584 1.000 54.11578  ? 440 TYR   A O   1 
ATOM   3449 C CB  . TYR   A 1  440 ? 27.60563  34.32187 46.38485 1.000 56.90589  ? 440 TYR   A CB  1 
ATOM   3450 C CG  . TYR   A 1  440 ? 27.81939  35.60372 45.62020 1.000 55.94339  ? 440 TYR   A CG  1 
ATOM   3451 C CD1 . TYR   A 1  440 ? 28.87494  35.72119 44.72926 1.000 55.79424  ? 440 TYR   A CD1 1 
ATOM   3452 C CD2 . TYR   A 1  440 ? 26.90074  36.65525 45.69293 1.000 60.68144  ? 440 TYR   A CD2 1 
ATOM   3453 C CE1 . TYR   A 1  440 ? 29.06028  36.85503 43.98052 1.000 52.30845  ? 440 TYR   A CE1 1 
ATOM   3454 C CE2 . TYR   A 1  440 ? 27.08782  37.81401 44.93739 1.000 56.50213  ? 440 TYR   A CE2 1 
ATOM   3455 C CZ  . TYR   A 1  440 ? 28.18138  37.89337 44.08083 1.000 56.29624  ? 440 TYR   A CZ  1 
ATOM   3456 O OH  . TYR   A 1  440 ? 28.39334  39.01011 43.31628 1.000 58.77050  ? 440 TYR   A OH  1 
ATOM   3457 N N   . GLU   A 1  441 ? 26.07204  31.03864 45.78055 1.000 53.18627  ? 441 GLU   A N   1 
ATOM   3458 C CA  . GLU   A 1  441 ? 26.22502  29.59903 45.74685 1.000 58.38787  ? 441 GLU   A CA  1 
ATOM   3459 C C   . GLU   A 1  441 ? 26.47340  29.09386 44.33439 1.000 60.95844  ? 441 GLU   A C   1 
ATOM   3460 O O   . GLU   A 1  441 ? 26.93764  27.95647 44.16822 1.000 60.43360  ? 441 GLU   A O   1 
ATOM   3461 C CB  . GLU   A 1  441 ? 24.97042  28.92238 46.32928 1.000 54.28037  ? 441 GLU   A CB  1 
ATOM   3462 C CG  . GLU   A 1  441 ? 23.90724  28.57780 45.29071 1.000 57.03888  ? 441 GLU   A CG  1 
ATOM   3463 C CD  . GLU   A 1  441 ? 23.08260  29.79932 44.81796 1.000 59.16110  ? 441 GLU   A CD  1 
ATOM   3464 O OE1 . GLU   A 1  441 ? 23.25430  30.91042 45.37876 1.000 56.64177  ? 441 GLU   A OE1 1 
ATOM   3465 O OE2 . GLU   A 1  441 ? 22.25700  29.63056 43.87969 1.000 55.76917  ? 441 GLU   A OE2 1 
ATOM   3466 N N   . ILE   A 1  442 ? 26.17123  29.91409 43.32033 1.000 56.89430  ? 442 ILE   A N   1 
ATOM   3467 C CA  . ILE   A 1  442 ? 26.21964  29.44355 41.93770 1.000 55.21996  ? 442 ILE   A CA  1 
ATOM   3468 C C   . ILE   A 1  442 ? 27.63207  29.01051 41.56136 1.000 56.06157  ? 442 ILE   A C   1 
ATOM   3469 O O   . ILE   A 1  442 ? 27.81323  27.98884 40.88654 1.000 57.14425  ? 442 ILE   A O   1 
ATOM   3470 C CB  . ILE   A 1  442 ? 25.68380  30.53039 40.98601 1.000 56.92395  ? 442 ILE   A CB  1 
ATOM   3471 C CG1 . ILE   A 1  442 ? 24.20717  30.79293 41.25754 1.000 51.82270  ? 442 ILE   A CG1 1 
ATOM   3472 C CG2 . ILE   A 1  442 ? 25.93121  30.16707 39.51222 1.000 48.66652  ? 442 ILE   A CG2 1 
ATOM   3473 C CD1 . ILE   A 1  442 ? 23.69378  32.05284 40.55396 1.000 50.63441  ? 442 ILE   A CD1 1 
ATOM   3474 N N   . GLU   A 1  443 ? 28.64961  29.78323 41.98207 1.000 53.38688  ? 443 GLU   A N   1 
ATOM   3475 C CA  . GLU   A 1  443 ? 30.05127  29.40493 41.76397 1.000 55.42098  ? 443 GLU   A CA  1 
ATOM   3476 C C   . GLU   A 1  443 ? 30.30657  27.96429 42.16783 1.000 56.59045  ? 443 GLU   A C   1 
ATOM   3477 O O   . GLU   A 1  443 ? 31.03388  27.23497 41.48527 1.000 60.45713  ? 443 GLU   A O   1 
ATOM   3478 C CB  . GLU   A 1  443 ? 31.00409  30.28622 42.58065 1.000 58.15711  ? 443 GLU   A CB  1 
ATOM   3479 C CG  . GLU   A 1  443 ? 31.17222  31.69547 42.17470 1.000 70.60518  ? 443 GLU   A CG  1 
ATOM   3480 C CD  . GLU   A 1  443 ? 31.51931  32.55716 43.36622 1.000 72.47679  ? 443 GLU   A CD  1 
ATOM   3481 O OE1 . GLU   A 1  443 ? 32.70925  32.63953 43.75974 1.000 74.76471  ? 443 GLU   A OE1 1 
ATOM   3482 O OE2 . GLU   A 1  443 ? 30.57159  33.12721 43.93265 1.000 71.10619  ? 443 GLU   A OE2 1 
ATOM   3483 N N   . PHE   A 1  444 ? 29.77796  27.56949 43.32985 1.000 55.05070  ? 444 PHE   A N   1 
ATOM   3484 C CA  . PHE   A 1  444 ? 30.07197  26.25931 43.88004 1.000 58.28239  ? 444 PHE   A CA  1 
ATOM   3485 C C   . PHE   A 1  444 ? 29.29069  25.19006 43.15114 1.000 57.54938  ? 444 PHE   A C   1 
ATOM   3486 O O   . PHE   A 1  444 ? 29.81904  24.10158 42.90339 1.000 56.39564  ? 444 PHE   A O   1 
ATOM   3487 C CB  . PHE   A 1  444 ? 29.79766  26.25498 45.38456 1.000 57.26566  ? 444 PHE   A CB  1 
ATOM   3488 C CG  . PHE   A 1  444 ? 30.77285  27.09091 46.14106 1.000 63.67320  ? 444 PHE   A CG  1 
ATOM   3489 C CD1 . PHE   A 1  444 ? 30.61609  28.46408 46.21535 1.000 57.95159  ? 444 PHE   A CD1 1 
ATOM   3490 C CD2 . PHE   A 1  444 ? 31.90312  26.51945 46.70865 1.000 61.40987  ? 444 PHE   A CD2 1 
ATOM   3491 C CE1 . PHE   A 1  444 ? 31.55552  29.25120 46.88203 1.000 57.44055  ? 444 PHE   A CE1 1 
ATOM   3492 C CE2 . PHE   A 1  444 ? 32.84565  27.31682 47.37163 1.000 62.41863  ? 444 PHE   A CE2 1 
ATOM   3493 C CZ  . PHE   A 1  444 ? 32.66309  28.67375 47.45535 1.000 59.79106  ? 444 PHE   A CZ  1 
ATOM   3494 N N   . VAL   A 1  445 ? 28.05904  25.50339 42.74601 1.000 54.31393  ? 445 VAL   A N   1 
ATOM   3495 C CA  . VAL   A 1  445 ? 27.26544  24.53137 41.99774 1.000 52.87530  ? 445 VAL   A CA  1 
ATOM   3496 C C   . VAL   A 1  445 ? 27.93366  24.19930 40.65950 1.000 58.85730  ? 445 VAL   A C   1 
ATOM   3497 O O   . VAL   A 1  445 ? 27.91342  23.03882 40.21129 1.000 55.26768  ? 445 VAL   A O   1 
ATOM   3498 C CB  . VAL   A 1  445 ? 25.82657  25.04893 41.82381 1.000 54.37786  ? 445 VAL   A CB  1 
ATOM   3499 C CG1 . VAL   A 1  445 ? 25.04171  24.22188 40.77161 1.000 44.13987  ? 445 VAL   A CG1 1 
ATOM   3500 C CG2 . VAL   A 1  445 ? 25.11434  25.06261 43.18011 1.000 53.08616  ? 445 VAL   A CG2 1 
ATOM   3501 N N   . PHE   A 1  446 ? 28.57121  25.19491 40.02122 1.000 52.67908  ? 446 PHE   A N   1 
ATOM   3502 C CA  . PHE   A 1  446 ? 29.17462  25.01306 38.70447 1.000 53.04710  ? 446 PHE   A CA  1 
ATOM   3503 C C   . PHE   A 1  446 ? 30.62850  24.55062 38.76568 1.000 58.18455  ? 446 PHE   A C   1 
ATOM   3504 O O   . PHE   A 1  446 ? 31.22240  24.25643 37.71372 1.000 55.98704  ? 446 PHE   A O   1 
ATOM   3505 C CB  . PHE   A 1  446 ? 29.06472  26.31483 37.89111 1.000 52.52708  ? 446 PHE   A CB  1 
ATOM   3506 C CG  . PHE   A 1  446 ? 27.77518  26.43776 37.14257 1.000 52.65993  ? 446 PHE   A CG  1 
ATOM   3507 C CD1 . PHE   A 1  446 ? 26.64214  26.95700 37.76369 1.000 54.25028  ? 446 PHE   A CD1 1 
ATOM   3508 C CD2 . PHE   A 1  446 ? 27.67345  25.99271 35.83599 1.000 52.81990  ? 446 PHE   A CD2 1 
ATOM   3509 C CE1 . PHE   A 1  446 ? 25.41728  27.05156 37.07604 1.000 50.58904  ? 446 PHE   A CE1 1 
ATOM   3510 C CE2 . PHE   A 1  446 ? 26.47839  26.07440 35.14063 1.000 50.94401  ? 446 PHE   A CE2 1 
ATOM   3511 C CZ  . PHE   A 1  446 ? 25.33163  26.60792 35.76074 1.000 49.60849  ? 446 PHE   A CZ  1 
ATOM   3512 N N   . GLY   A 1  447 ? 31.21154  24.45846 39.96340 1.000 59.48668  ? 447 GLY   A N   1 
ATOM   3513 C CA  . GLY   A 1  447 ? 32.51740  23.84644 40.10273 1.000 57.13743  ? 447 GLY   A CA  1 
ATOM   3514 C C   . GLY   A 1  447 ? 33.68034  24.75718 39.79691 1.000 62.14627  ? 447 GLY   A C   1 
ATOM   3515 O O   . GLY   A 1  447 ? 34.76380  24.26910 39.47789 1.000 62.11979  ? 447 GLY   A O   1 
ATOM   3516 N N   . LEU   A 1  448 ? 33.48059  26.07153 39.86364 1.000 66.48695  ? 448 LEU   A N   1 
ATOM   3517 C CA  . LEU   A 1  448 ? 34.59572  26.99735 39.68810 1.000 63.24312  ? 448 LEU   A CA  1 
ATOM   3518 C C   . LEU   A 1  448 ? 35.69299  26.79296 40.72680 1.000 63.24090  ? 448 LEU   A C   1 
ATOM   3519 O O   . LEU   A 1  448 ? 36.87356  26.78044 40.33672 1.000 70.94149  ? 448 LEU   A O   1 
ATOM   3520 C CB  . LEU   A 1  448 ? 34.07075  28.44322 39.69676 1.000 58.17641  ? 448 LEU   A CB  1 
ATOM   3521 C CG  . LEU   A 1  448 ? 33.60622  29.01211 38.34429 1.000 55.04551  ? 448 LEU   A CG  1 
ATOM   3522 C CD1 . LEU   A 1  448 ? 32.35268  28.31498 37.81240 1.000 60.94646  ? 448 LEU   A CD1 1 
ATOM   3523 C CD2 . LEU   A 1  448 ? 33.36107  30.50323 38.44246 1.000 61.96978  ? 448 LEU   A CD2 1 
ATOM   3524 N N   . PRO   A 1  449 ? 35.40559  26.61283 42.02175 1.000 66.18705  ? 449 PRO   A N   1 
ATOM   3525 C CA  . PRO   A 1  449 ? 36.49833  26.32919 42.97222 1.000 64.74122  ? 449 PRO   A CA  1 
ATOM   3526 C C   . PRO   A 1  449 ? 37.29789  25.08015 42.64387 1.000 64.67928  ? 449 PRO   A C   1 
ATOM   3527 O O   . PRO   A 1  449 ? 38.40473  24.91824 43.17342 1.000 70.78886  ? 449 PRO   A O   1 
ATOM   3528 C CB  . PRO   A 1  449 ? 35.77121  26.19880 44.31313 1.000 66.64692  ? 449 PRO   A CB  1 
ATOM   3529 C CG  . PRO   A 1  449 ? 34.58087  27.12510 44.15851 1.000 61.39303  ? 449 PRO   A CG  1 
ATOM   3530 C CD  . PRO   A 1  449 ? 34.14501  26.92385 42.72325 1.000 60.73417  ? 449 PRO   A CD  1 
ATOM   3531 N N   . LEU   A 1  450 ? 36.79868  24.19349 41.78742 1.000 67.13412  ? 450 LEU   A N   1 
ATOM   3532 C CA  . LEU   A 1  450 ? 37.64549  23.08027 41.37814 1.000 69.81427  ? 450 LEU   A CA  1 
ATOM   3533 C C   . LEU   A 1  450 ? 38.83207  23.55587 40.55569 1.000 71.65341  ? 450 LEU   A C   1 
ATOM   3534 O O   . LEU   A 1  450 ? 39.86341  22.87242 40.52977 1.000 68.45817  ? 450 LEU   A O   1 
ATOM   3535 C CB  . LEU   A 1  450 ? 36.83352  22.02656 40.61187 1.000 57.65961  ? 450 LEU   A CB  1 
ATOM   3536 C CG  . LEU   A 1  450 ? 35.63932  21.50760 41.42979 1.000 66.35044  ? 450 LEU   A CG  1 
ATOM   3537 C CD1 . LEU   A 1  450 ? 34.79866  20.46884 40.66008 1.000 60.78086  ? 450 LEU   A CD1 1 
ATOM   3538 C CD2 . LEU   A 1  450 ? 36.10081  20.96041 42.78860 1.000 63.38229  ? 450 LEU   A CD2 1 
ATOM   3539 N N   . GLU   A 1  451 ? 38.72395  24.71846 39.90998 1.000 70.92648  ? 451 GLU   A N   1 
ATOM   3540 C CA  . GLU   A 1  451 ? 39.86773  25.30205 39.20969 1.000 80.48432  ? 451 GLU   A CA  1 
ATOM   3541 C C   . GLU   A 1  451 ? 40.90537  25.74751 40.23643 1.000 84.95481  ? 451 GLU   A C   1 
ATOM   3542 O O   . GLU   A 1  451 ? 40.74948  26.77396 40.90637 1.000 84.07111  ? 451 GLU   A O   1 
ATOM   3543 C CB  . GLU   A 1  451 ? 39.43896  26.46463 38.32950 1.000 86.35893  ? 451 GLU   A CB  1 
ATOM   3544 C CG  . GLU   A 1  451 ? 40.61023  27.14741 37.65464 1.000 88.95718  ? 451 GLU   A CG  1 
ATOM   3545 C CD  . GLU   A 1  451 ? 41.39723  26.19170 36.76316 1.000 99.80999  ? 451 GLU   A CD  1 
ATOM   3546 O OE1 . GLU   A 1  451 ? 40.96379  26.00875 35.60505 1.000 100.18915 ? 451 GLU   A OE1 1 
ATOM   3547 O OE2 . GLU   A 1  451 ? 42.43116  25.61750 37.20764 1.000 99.86248  ? 451 GLU   A OE2 1 
ATOM   3548 N N   . ARG   A 1  452 ? 41.97944  24.96685 40.35423 1.000 85.33039  ? 452 ARG   A N   1 
ATOM   3549 C CA  . ARG   A 1  452 ? 43.02713  25.26176 41.32253 1.000 94.82573  ? 452 ARG   A CA  1 
ATOM   3550 C C   . ARG   A 1  452 ? 43.75210  26.56641 41.00302 1.000 101.89012 ? 452 ARG   A C   1 
ATOM   3551 O O   . ARG   A 1  452 ? 44.33180  27.17290 41.90996 1.000 97.40541  ? 452 ARG   A O   1 
ATOM   3552 C CB  . ARG   A 1  452 ? 44.01453  24.09352 41.37855 1.000 96.25374  ? 452 ARG   A CB  1 
ATOM   3553 C CG  . ARG   A 1  452 ? 44.05892  23.37446 42.72723 1.000 100.48098 ? 452 ARG   A CG  1 
ATOM   3554 C CD  . ARG   A 1  452 ? 45.18470  22.30473 42.79373 1.000 114.76451 ? 452 ARG   A CD  1 
ATOM   3555 N NE  . ARG   A 1  452 ? 44.86446  21.02248 42.16131 1.000 110.78687 ? 452 ARG   A NE  1 
ATOM   3556 C CZ  . ARG   A 1  452 ? 45.65720  20.38440 41.30592 1.000 109.70705 ? 452 ARG   A CZ  1 
ATOM   3557 N NH1 . ARG   A 1  452 ? 46.80642  20.90378 40.90649 1.000 101.71617 ? 452 ARG   A NH1 1 
ATOM   3558 N NH2 . ARG   A 1  452 ? 45.28486  19.19678 40.83510 1.000 108.17684 ? 452 ARG   A NH2 1 
ATOM   3559 N N   . ARG   A 1  453 ? 43.70248  27.02747 39.74428 1.000 102.59802 ? 453 ARG   A N   1 
ATOM   3560 C CA  . ARG   A 1  453 ? 44.33896  28.29320 39.37347 1.000 105.44010 ? 453 ARG   A CA  1 
ATOM   3561 C C   . ARG   A 1  453 ? 43.69979  29.49675 40.06813 1.000 108.69203 ? 453 ARG   A C   1 
ATOM   3562 O O   . ARG   A 1  453 ? 44.39843  30.46833 40.38111 1.000 106.44399 ? 453 ARG   A O   1 
ATOM   3563 C CB  . ARG   A 1  453 ? 44.28417  28.48665 37.85580 1.000 104.64613 ? 453 ARG   A CB  1 
ATOM   3564 C CG  . ARG   A 1  453 ? 45.29662  27.66525 37.04939 1.000 117.75639 ? 453 ARG   A CG  1 
ATOM   3565 C CD  . ARG   A 1  453 ? 46.73219  27.82917 37.56325 1.000 121.08928 ? 453 ARG   A CD  1 
ATOM   3566 N NE  . ARG   A 1  453 ? 47.16195  26.66277 38.32380 1.000 127.18897 ? 453 ARG   A NE  1 
ATOM   3567 C CZ  . ARG   A 1  453 ? 47.90281  26.71591 39.42177 1.000 127.67602 ? 453 ARG   A CZ  1 
ATOM   3568 N NH1 . ARG   A 1  453 ? 48.35840  27.86544 39.89314 1.000 124.29358 ? 453 ARG   A NH1 1 
ATOM   3569 N NH2 . ARG   A 1  453 ? 48.18853  25.58754 40.06568 1.000 134.41426 ? 453 ARG   A NH2 1 
ATOM   3570 N N   . ASP   A 1  454 ? 42.38298  29.47038 40.30136 1.000 111.87693 ? 454 ASP   A N   1 
ATOM   3571 C CA  . ASP   A 1  454 ? 41.71150  30.60967 40.92372 1.000 108.88800 ? 454 ASP   A CA  1 
ATOM   3572 C C   . ASP   A 1  454 ? 42.17670  30.80783 42.35939 1.000 109.15694 ? 454 ASP   A C   1 
ATOM   3573 O O   . ASP   A 1  454 ? 43.05980  30.09352 42.84610 1.000 110.53236 ? 454 ASP   A O   1 
ATOM   3574 C CB  . ASP   A 1  454 ? 40.19824  30.43999 40.88735 1.000 106.08728 ? 454 ASP   A CB  1 
ATOM   3575 C CG  . ASP   A 1  454 ? 39.64774  30.51123 39.48858 1.000 118.84786 ? 454 ASP   A CG  1 
ATOM   3576 O OD1 . ASP   A 1  454 ? 40.43572  30.83013 38.57073 1.000 111.02002 ? 454 ASP   A OD1 1 
ATOM   3577 O OD2 . ASP   A 1  454 ? 38.43104  30.24189 39.31681 1.000 120.83302 ? 454 ASP   A OD2 1 
ATOM   3578 N N   . GLN   A 1  455 ? 41.58914  31.77744 43.05284 1.000 95.88491  ? 455 GLN   A N   1 
ATOM   3579 C CA  . GLN   A 1  455 ? 42.03626  32.11263 44.39532 1.000 99.38118  ? 455 GLN   A CA  1 
ATOM   3580 C C   . GLN   A 1  455 ? 41.20241  31.44070 45.48150 1.000 94.10483  ? 455 GLN   A C   1 
ATOM   3581 O O   . GLN   A 1  455 ? 41.28801  31.83556 46.65093 1.000 95.23119  ? 455 GLN   A O   1 
ATOM   3582 C CB  . GLN   A 1  455 ? 42.04165  33.63199 44.57870 1.000 104.79024 ? 455 GLN   A CB  1 
ATOM   3583 C CG  . GLN   A 1  455 ? 43.29624  34.30966 44.03883 1.000 110.32837 ? 455 GLN   A CG  1 
ATOM   3584 C CD  . GLN   A 1  455 ? 43.35005  34.29066 42.52246 1.000 113.87229 ? 455 GLN   A CD  1 
ATOM   3585 O OE1 . GLN   A 1  455 ? 44.36971  33.92531 41.93228 1.000 108.82979 ? 455 GLN   A OE1 1 
ATOM   3586 N NE2 . GLN   A 1  455 ? 42.23782  34.66252 41.88193 1.000 110.98704 ? 455 GLN   A NE2 1 
ATOM   3587 N N   . TYR   A 1  456 ? 40.40721  30.43638 45.12575 1.000 86.48520  ? 456 TYR   A N   1 
ATOM   3588 C CA  . TYR   A 1  456 ? 39.63814  29.70751 46.12394 1.000 81.67690  ? 456 TYR   A CA  1 
ATOM   3589 C C   . TYR   A 1  456 ? 40.56633  28.87666 47.00835 1.000 80.79866  ? 456 TYR   A C   1 
ATOM   3590 O O   . TYR   A 1  456 ? 41.61820  28.41198 46.57391 1.000 75.30579  ? 456 TYR   A O   1 
ATOM   3591 C CB  . TYR   A 1  456 ? 38.61937  28.79293 45.45132 1.000 71.63514  ? 456 TYR   A CB  1 
ATOM   3592 C CG  . TYR   A 1  456 ? 37.58288  29.49383 44.61348 1.000 69.69580  ? 456 TYR   A CG  1 
ATOM   3593 C CD1 . TYR   A 1  456 ? 36.52474  30.17397 45.20855 1.000 66.01719  ? 456 TYR   A CD1 1 
ATOM   3594 C CD2 . TYR   A 1  456 ? 37.64496  29.45631 43.22581 1.000 73.78356  ? 456 TYR   A CD2 1 
ATOM   3595 C CE1 . TYR   A 1  456 ? 35.57121  30.80644 44.45290 1.000 66.02192  ? 456 TYR   A CE1 1 
ATOM   3596 C CE2 . TYR   A 1  456 ? 36.69026  30.08587 42.45320 1.000 71.02777  ? 456 TYR   A CE2 1 
ATOM   3597 C CZ  . TYR   A 1  456 ? 35.65465  30.75869 43.07474 1.000 70.56959  ? 456 TYR   A CZ  1 
ATOM   3598 O OH  . TYR   A 1  456 ? 34.69482  31.37987 42.31704 1.000 64.09431  ? 456 TYR   A OH  1 
ATOM   3599 N N   . THR   A 1  457 ? 40.16688  28.68372 48.26146 1.000 79.06086  ? 457 THR   A N   1 
ATOM   3600 C CA  . THR   A 1  457 ? 40.94605  27.84680 49.16476 1.000 72.35423  ? 457 THR   A CA  1 
ATOM   3601 C C   . THR   A 1  457 ? 40.72043  26.36483 48.85718 1.000 76.49937  ? 457 THR   A C   1 
ATOM   3602 O O   . THR   A 1  457 ? 39.82671  25.97627 48.09296 1.000 69.85288  ? 457 THR   A O   1 
ATOM   3603 C CB  . THR   A 1  457 ? 40.56244  28.11496 50.61762 1.000 69.11984  ? 457 THR   A CB  1 
ATOM   3604 O OG1 . THR   A 1  457 ? 39.18312  27.75604 50.79893 1.000 69.07035  ? 457 THR   A OG1 1 
ATOM   3605 C CG2 . THR   A 1  457 ? 40.74610  29.57771 50.97330 1.000 61.92184  ? 457 THR   A CG2 1 
ATOM   3606 N N   . LYS   A 1  458 ? 41.52948  25.51925 49.49582 1.000 74.92879  ? 458 LYS   A N   1 
ATOM   3607 C CA  . LYS   A 1  458 ? 41.31392  24.08436 49.34943 1.000 79.33905  ? 458 LYS   A CA  1 
ATOM   3608 C C   . LYS   A 1  458 ? 39.98093  23.66072 49.95807 1.000 78.41987  ? 458 LYS   A C   1 
ATOM   3609 O O   . LYS   A 1  458 ? 39.31176  22.75537 49.43435 1.000 78.21136  ? 458 LYS   A O   1 
ATOM   3610 C CB  . LYS   A 1  458 ? 42.47531  23.30712 49.97999 1.000 78.82266  ? 458 LYS   A CB  1 
ATOM   3611 C CG  . LYS   A 1  458 ? 42.38288  21.78638 49.77830 1.000 84.38112  ? 458 LYS   A CG  1 
ATOM   3612 C CD  . LYS   A 1  458 ? 43.25793  21.30669 48.60048 1.000 95.44708  ? 458 LYS   A CD  1 
ATOM   3613 C CE  . LYS   A 1  458 ? 42.56017  20.20698 47.76682 1.000 100.02445 ? 458 LYS   A CE  1 
ATOM   3614 N NZ  . LYS   A 1  458 ? 43.48150  19.48536 46.81096 1.000 101.31152 ? 458 LYS   A NZ  1 
ATOM   3615 N N   . ALA   A 1  459 ? 39.57460  24.31081 51.05097 1.000 73.31769  ? 459 ALA   A N   1 
ATOM   3616 C CA  . ALA   A 1  459 ? 38.29340  23.98928 51.66174 1.000 72.76613  ? 459 ALA   A CA  1 
ATOM   3617 C C   . ALA   A 1  459 ? 37.14978  24.21253 50.67872 1.000 70.84211  ? 459 ALA   A C   1 
ATOM   3618 O O   . ALA   A 1  459 ? 36.19140  23.43103 50.63810 1.000 73.31016  ? 459 ALA   A O   1 
ATOM   3619 C CB  . ALA   A 1  459 ? 38.10430  24.82653 52.92740 1.000 69.76229  ? 459 ALA   A CB  1 
ATOM   3620 N N   . GLU   A 1  460 ? 37.24313  25.26803 49.86541 1.000 69.76787  ? 460 GLU   A N   1 
ATOM   3621 C CA  . GLU   A 1  460 ? 36.18190  25.56280 48.91214 1.000 69.54749  ? 460 GLU   A CA  1 
ATOM   3622 C C   . GLU   A 1  460 ? 36.20208  24.59877 47.73736 1.000 66.61356  ? 460 GLU   A C   1 
ATOM   3623 O O   . GLU   A 1  460 ? 35.14035  24.26222 47.20362 1.000 63.03695  ? 460 GLU   A O   1 
ATOM   3624 C CB  . GLU   A 1  460 ? 36.29994  27.01155 48.44235 1.000 70.23331  ? 460 GLU   A CB  1 
ATOM   3625 C CG  . GLU   A 1  460 ? 36.07652  27.99861 49.57392 1.000 67.83595  ? 460 GLU   A CG  1 
ATOM   3626 C CD  . GLU   A 1  460 ? 36.26336  29.45903 49.17478 1.000 68.38129  ? 460 GLU   A CD  1 
ATOM   3627 O OE1 . GLU   A 1  460 ? 37.20187  29.77559 48.41235 1.000 69.65775  ? 460 GLU   A OE1 1 
ATOM   3628 O OE2 . GLU   A 1  460 ? 35.45795  30.29344 49.63851 1.000 67.57447  ? 460 GLU   A OE2 1 
ATOM   3629 N N   . GLU   A 1  461 ? 37.38951  24.13238 47.33974 1.000 67.15477  ? 461 GLU   A N   1 
ATOM   3630 C CA  . GLU   A 1  461 ? 37.48217  23.08999 46.32259 1.000 67.98909  ? 461 GLU   A CA  1 
ATOM   3631 C C   . GLU   A 1  461 ? 36.72944  21.84429 46.76400 1.000 68.86977  ? 461 GLU   A C   1 
ATOM   3632 O O   . GLU   A 1  461 ? 35.91277  21.29201 46.01563 1.000 66.21003  ? 461 GLU   A O   1 
ATOM   3633 C CB  . GLU   A 1  461 ? 38.94856  22.74526 46.04545 1.000 69.17678  ? 461 GLU   A CB  1 
ATOM   3634 C CG  . GLU   A 1  461 ? 39.11656  21.84158 44.82247 1.000 76.15804  ? 461 GLU   A CG  1 
ATOM   3635 C CD  . GLU   A 1  461 ? 40.46890  21.11314 44.72705 1.000 80.00147  ? 461 GLU   A CD  1 
ATOM   3636 O OE1 . GLU   A 1  461 ? 41.48908  21.61376 45.24920 1.000 89.58214  ? 461 GLU   A OE1 1 
ATOM   3637 O OE2 . GLU   A 1  461 ? 40.51027  20.05159 44.06906 1.000 78.03913  ? 461 GLU   A OE2 1 
ATOM   3638 N N   . ILE   A 1  462 ? 36.98054  21.40189 47.99750 1.000 71.57988  ? 462 ILE   A N   1 
ATOM   3639 C CA  . ILE   A 1  462 ? 36.31320  20.21394 48.51910 1.000 69.43686  ? 462 ILE   A CA  1 
ATOM   3640 C C   . ILE   A 1  462 ? 34.80478  20.43639 48.61976 1.000 68.22283  ? 462 ILE   A C   1 
ATOM   3641 O O   . ILE   A 1  462 ? 34.01477  19.53570 48.30144 1.000 67.66196  ? 462 ILE   A O   1 
ATOM   3642 C CB  . ILE   A 1  462 ? 36.93843  19.81218 49.87339 1.000 75.22484  ? 462 ILE   A CB  1 
ATOM   3643 C CG1 . ILE   A 1  462 ? 38.34527  19.24953 49.66261 1.000 74.97256  ? 462 ILE   A CG1 1 
ATOM   3644 C CG2 . ILE   A 1  462 ? 36.08211  18.78101 50.62047 1.000 71.95090  ? 462 ILE   A CG2 1 
ATOM   3645 C CD1 . ILE   A 1  462 ? 39.34572  19.68880 50.72613 1.000 81.87217  ? 462 ILE   A CD1 1 
ATOM   3646 N N   . LEU   A 1  463 ? 34.37291  21.63485 49.04844 1.000 64.12544  ? 463 LEU   A N   1 
ATOM   3647 C CA  . LEU   A 1  463 ? 32.92979  21.86271 49.20779 1.000 68.38920  ? 463 LEU   A CA  1 
ATOM   3648 C C   . LEU   A 1  463 ? 32.22825  21.93542 47.86035 1.000 62.95625  ? 463 LEU   A C   1 
ATOM   3649 O O   . LEU   A 1  463 ? 31.10668  21.43214 47.70995 1.000 62.73184  ? 463 LEU   A O   1 
ATOM   3650 C CB  . LEU   A 1  463 ? 32.64132  23.14058 50.00722 1.000 61.97746  ? 463 LEU   A CB  1 
ATOM   3651 C CG  . LEU   A 1  463 ? 31.18288  23.62075 50.04420 1.000 60.30503  ? 463 LEU   A CG  1 
ATOM   3652 C CD1 . LEU   A 1  463 ? 30.21083  22.55292 50.58075 1.000 55.84806  ? 463 LEU   A CD1 1 
ATOM   3653 C CD2 . LEU   A 1  463 ? 31.02121  24.91981 50.84954 1.000 62.71320  ? 463 LEU   A CD2 1 
ATOM   3654 N N   . SER   A 1  464 ? 32.86156  22.57497 46.87569 1.000 61.04821  ? 464 SER   A N   1 
ATOM   3655 C CA  . SER   A 1  464 ? 32.32635  22.52915 45.52092 1.000 61.23547  ? 464 SER   A CA  1 
ATOM   3656 C C   . SER   A 1  464 ? 32.32711  21.10350 45.00225 1.000 62.36980  ? 464 SER   A C   1 
ATOM   3657 O O   . SER   A 1  464 ? 31.40069  20.68304 44.30257 1.000 65.85647  ? 464 SER   A O   1 
ATOM   3658 C CB  . SER   A 1  464 ? 33.14483  23.42442 44.59038 1.000 59.41573  ? 464 SER   A CB  1 
ATOM   3659 O OG  . SER   A 1  464 ? 32.59508  23.39234 43.28737 1.000 58.53408  ? 464 SER   A OG  1 
ATOM   3660 N N   . ARG   A 1  465 ? 33.36337  20.34474 45.34956 1.000 61.70616  ? 465 ARG   A N   1 
ATOM   3661 C CA  . ARG   A 1  465 ? 33.48648  18.98652 44.84776 1.000 67.21335  ? 465 ARG   A CA  1 
ATOM   3662 C C   . ARG   A 1  465 ? 32.31789  18.12923 45.31328 1.000 62.79462  ? 465 ARG   A C   1 
ATOM   3663 O O   . ARG   A 1  465 ? 31.80305  17.30285 44.55025 1.000 65.33608  ? 465 ARG   A O   1 
ATOM   3664 C CB  . ARG   A 1  465 ? 34.83332  18.39528 45.28978 1.000 65.59746  ? 465 ARG   A CB  1 
ATOM   3665 C CG  . ARG   A 1  465 ? 35.09608  16.99037 44.78535 1.000 65.54649  ? 465 ARG   A CG  1 
ATOM   3666 C CD  . ARG   A 1  465 ? 35.08075  16.93779 43.26560 1.000 69.52659  ? 465 ARG   A CD  1 
ATOM   3667 N NE  . ARG   A 1  465 ? 34.87350  15.58824 42.73841 1.000 78.31411  ? 465 ARG   A NE  1 
ATOM   3668 C CZ  . ARG   A 1  465 ? 33.71761  15.10589 42.28858 1.000 74.75147  ? 465 ARG   A CZ  1 
ATOM   3669 N NH1 . ARG   A 1  465 ? 32.59833  15.82505 42.32256 1.000 60.75073  ? 465 ARG   A NH1 1 
ATOM   3670 N NH2 . ARG   A 1  465 ? 33.68619  13.87511 41.77720 1.000 71.12336  ? 465 ARG   A NH2 1 
ATOM   3671 N N   A SER   A 1  466 ? 31.87140  18.33045 46.55270 0.411 60.00807  ? 466 SER   A N   1 
ATOM   3672 N N   B SER   A 1  466 ? 31.87416  18.31455 46.55845 0.589 61.17296  ? 466 SER   A N   1 
ATOM   3673 C CA  A SER   A 1  466 ? 30.75795  17.54860 47.07215 0.411 61.93963  ? 466 SER   A CA  1 
ATOM   3674 C CA  B SER   A 1  466 ? 30.74659  17.52627 47.04449 0.589 61.90820  ? 466 SER   A CA  1 
ATOM   3675 C C   A SER   A 1  466 ? 29.42202  18.04784 46.52740 0.411 59.81362  ? 466 SER   A C   1 
ATOM   3676 C C   B SER   A 1  466 ? 29.41628  18.04681 46.50615 0.589 59.78766  ? 466 SER   A C   1 
ATOM   3677 O O   A SER   A 1  466 ? 28.54599  17.24333 46.18888 0.411 58.29266  ? 466 SER   A O   1 
ATOM   3678 O O   B SER   A 1  466 ? 28.53150  17.25510 46.15962 0.589 58.37590  ? 466 SER   A O   1 
ATOM   3679 C CB  A SER   A 1  466 ? 30.77103  17.58370 48.60155 0.411 62.39518  ? 466 SER   A CB  1 
ATOM   3680 C CB  B SER   A 1  466 ? 30.73342  17.49889 48.57544 0.589 62.45269  ? 466 SER   A CB  1 
ATOM   3681 O OG  A SER   A 1  466 ? 29.83050  16.67685 49.14428 0.411 61.48203  ? 466 SER   A OG  1 
ATOM   3682 O OG  B SER   A 1  466 ? 31.90531  18.07931 49.11606 0.589 60.83827  ? 466 SER   A OG  1 
ATOM   3683 N N   . ILE   A 1  467 ? 29.24876  19.36571 46.42581 1.000 62.70872  ? 467 ILE   A N   1 
ATOM   3684 C CA  . ILE   A 1  467 ? 28.00308  19.91544 45.88480 1.000 59.87363  ? 467 ILE   A CA  1 
ATOM   3685 C C   . ILE   A 1  467 ? 27.78871  19.41617 44.46128 1.000 56.77953  ? 467 ILE   A C   1 
ATOM   3686 O O   . ILE   A 1  467 ? 26.72339  18.89796 44.11266 1.000 54.51006  ? 467 ILE   A O   1 
ATOM   3687 C CB  . ILE   A 1  467 ? 28.02312  21.45329 45.95497 1.000 63.49143  ? 467 ILE   A CB  1 
ATOM   3688 C CG1 . ILE   A 1  467 ? 27.84390  21.90676 47.40804 1.000 65.02179  ? 467 ILE   A CG1 1 
ATOM   3689 C CG2 . ILE   A 1  467 ? 26.94090  22.05985 45.04615 1.000 55.22113  ? 467 ILE   A CG2 1 
ATOM   3690 C CD1 . ILE   A 1  467 ? 28.07766  23.38751 47.63578 1.000 58.32200  ? 467 ILE   A CD1 1 
ATOM   3691 N N   . VAL   A 1  468 ? 28.83027  19.50355 43.64389 1.000 55.93501  ? 468 VAL   A N   1 
ATOM   3692 C CA  . VAL   A 1  468 ? 28.75611  19.02864 42.26799 1.000 56.18265  ? 468 VAL   A CA  1 
ATOM   3693 C C   . VAL   A 1  468 ? 28.38217  17.54832 42.22054 1.000 59.46647  ? 468 VAL   A C   1 
ATOM   3694 O O   . VAL   A 1  468 ? 27.50417  17.13404 41.44954 1.000 57.19198  ? 468 VAL   A O   1 
ATOM   3695 C CB  . VAL   A 1  468 ? 30.09065  19.31999 41.56717 1.000 61.72011  ? 468 VAL   A CB  1 
ATOM   3696 C CG1 . VAL   A 1  468 ? 30.22798  18.52441 40.28772 1.000 54.43761  ? 468 VAL   A CG1 1 
ATOM   3697 C CG2 . VAL   A 1  468 ? 30.18355  20.83033 41.33037 1.000 56.40500  ? 468 VAL   A CG2 1 
ATOM   3698 N N   . LYS   A 1  469 ? 29.02501  16.72736 43.05668 1.000 59.80507  ? 469 LYS   A N   1 
ATOM   3699 C CA  . LYS   A 1  469 ? 28.64286  15.32112 43.14479 1.000 56.95025  ? 469 LYS   A CA  1 
ATOM   3700 C C   . LYS   A 1  469 ? 27.16885  15.16909 43.53969 1.000 59.30363  ? 469 LYS   A C   1 
ATOM   3701 O O   . LYS   A 1  469 ? 26.41900  14.39987 42.91879 1.000 58.27188  ? 469 LYS   A O   1 
ATOM   3702 C CB  . LYS   A 1  469 ? 29.54416  14.59735 44.14573 1.000 56.01636  ? 469 LYS   A CB  1 
ATOM   3703 C CG  . LYS   A 1  469 ? 29.08888  13.18374 44.45515 1.000 57.29974  ? 469 LYS   A CG  1 
ATOM   3704 C CD  . LYS   A 1  469 ? 29.04349  12.34971 43.17641 1.000 61.48628  ? 469 LYS   A CD  1 
ATOM   3705 C CE  . LYS   A 1  469 ? 30.44758  11.95430 42.69324 1.000 57.41697  ? 469 LYS   A CE  1 
ATOM   3706 N NZ  . LYS   A 1  469 ? 30.36474  11.29164 41.36353 1.000 51.26453  ? 469 LYS   A NZ  1 
ATOM   3707 N N   . ARG   A 1  470 ? 26.73078  15.89179 44.57633 1.000 58.89802  ? 470 ARG   A N   1 
ATOM   3708 C CA  . ARG   A 1  470 ? 25.34650  15.74406 45.03144 1.000 59.32140  ? 470 ARG   A CA  1 
ATOM   3709 C C   . ARG   A 1  470 ? 24.36377  16.16097 43.94352 1.000 56.08590  ? 470 ARG   A C   1 
ATOM   3710 O O   . ARG   A 1  470 ? 23.37405  15.47248 43.68671 1.000 53.51071  ? 470 ARG   A O   1 
ATOM   3711 C CB  . ARG   A 1  470 ? 25.10511  16.55837 46.30635 1.000 56.01636  ? 470 ARG   A CB  1 
ATOM   3712 C CG  . ARG   A 1  470 ? 25.85353  16.06313 47.54169 1.000 57.24327  ? 470 ARG   A CG  1 
ATOM   3713 C CD  . ARG   A 1  470 ? 25.19594  16.61129 48.80376 1.000 58.88426  ? 470 ARG   A CD  1 
ATOM   3714 N NE  . ARG   A 1  470 ? 26.03451  16.40063 49.97174 1.000 55.22240  ? 470 ARG   A NE  1 
ATOM   3715 C CZ  . ARG   A 1  470 ? 25.86093  15.43870 50.87046 1.000 60.67266  ? 470 ARG   A CZ  1 
ATOM   3716 N NH1 . ARG   A 1  470 ? 24.84338  14.59269 50.79367 1.000 60.39667  ? 470 ARG   A NH1 1 
ATOM   3717 N NH2 . ARG   A 1  470 ? 26.73838  15.31383 51.86557 1.000 61.61403  ? 470 ARG   A NH2 1 
ATOM   3718 N N   . TRP   A 1  471 ? 24.62169  17.29185 43.28940 1.000 56.86344  ? 471 TRP   A N   1 
ATOM   3719 C CA  . TRP   A 1  471 ? 23.73413  17.73266 42.21397 1.000 58.38911  ? 471 TRP   A CA  1 
ATOM   3720 C C   . TRP   A 1  471 ? 23.66630  16.69066 41.09462 1.000 54.42337  ? 471 TRP   A C   1 
ATOM   3721 O O   . TRP   A 1  471 ? 22.58674  16.37922 40.57722 1.000 51.23680  ? 471 TRP   A O   1 
ATOM   3722 C CB  . TRP   A 1  471 ? 24.21705  19.08419 41.67492 1.000 51.30900  ? 471 TRP   A CB  1 
ATOM   3723 C CG  . TRP   A 1  471 ? 23.52887  20.32766 42.23859 1.000 52.42139  ? 471 TRP   A CG  1 
ATOM   3724 C CD1 . TRP   A 1  471 ? 22.95009  21.33209 41.51088 1.000 53.93090  ? 471 TRP   A CD1 1 
ATOM   3725 C CD2 . TRP   A 1  471 ? 23.38390  20.70636 43.62564 1.000 53.55981  ? 471 TRP   A CD2 1 
ATOM   3726 N NE1 . TRP   A 1  471 ? 22.44548  22.30304 42.35118 1.000 55.45433  ? 471 TRP   A NE1 1 
ATOM   3727 C CE2 . TRP   A 1  471 ? 22.69350  21.94414 43.65106 1.000 55.14404  ? 471 TRP   A CE2 1 
ATOM   3728 C CE3 . TRP   A 1  471 ? 23.77371  20.12318 44.84316 1.000 52.57431  ? 471 TRP   A CE3 1 
ATOM   3729 C CZ2 . TRP   A 1  471 ? 22.37313  22.60772 44.84838 1.000 51.49317  ? 471 TRP   A CZ2 1 
ATOM   3730 C CZ3 . TRP   A 1  471 ? 23.45611  20.78264 46.03555 1.000 54.16112  ? 471 TRP   A CZ3 1 
ATOM   3731 C CH2 . TRP   A 1  471 ? 22.75652  22.01122 46.02848 1.000 48.72692  ? 471 TRP   A CH2 1 
ATOM   3732 N N   . ALA   A 1  472 ? 24.81199  16.13173 40.72006 1.000 54.04726  ? 472 ALA   A N   1 
ATOM   3733 C CA  . ALA   A 1  472 ? 24.83380  15.15779 39.63533 1.000 51.69551  ? 472 ALA   A CA  1 
ATOM   3734 C C   . ALA   A 1  472 ? 24.10198  13.89235 40.03576 1.000 54.96950  ? 472 ALA   A C   1 
ATOM   3735 O O   . ALA   A 1  472 ? 23.32200  13.34072 39.24746 1.000 57.40954  ? 472 ALA   A O   1 
ATOM   3736 C CB  . ALA   A 1  472 ? 26.27946  14.85208 39.24804 1.000 56.43966  ? 472 ALA   A CB  1 
ATOM   3737 N N   . ASN   A 1  473 ? 24.32386  13.42967 41.26785 1.000 53.89527  ? 473 ASN   A N   1 
ATOM   3738 C CA  . ASN   A 1  473 ? 23.59946  12.25526 41.74123 1.000 53.80462  ? 473 ASN   A CA  1 
ATOM   3739 C C   . ASN   A 1  473 ? 22.11444  12.51850 41.86026 1.000 53.05015  ? 473 ASN   A C   1 
ATOM   3740 O O   . ASN   A 1  473 ? 21.30553  11.61695 41.61318 1.000 59.74148  ? 473 ASN   A O   1 
ATOM   3741 C CB  . ASN   A 1  473 ? 24.17526  11.78917 43.07046 1.000 54.71929  ? 473 ASN   A CB  1 
ATOM   3742 C CG  . ASN   A 1  473 ? 25.38690  10.94087 42.86823 1.000 54.78740  ? 473 ASN   A CG  1 
ATOM   3743 O OD1 . ASN   A 1  473 ? 25.64147  10.50217 41.75174 1.000 60.08352  ? 473 ASN   A OD1 1 
ATOM   3744 N ND2 . ASN   A 1  473 ? 26.14781  10.70622 43.92214 1.000 61.77811  ? 473 ASN   A ND2 1 
ATOM   3745 N N   . PHE   A 1  474 ? 21.72449  13.73851 42.20305 1.000 50.81577  ? 474 PHE   A N   1 
ATOM   3746 C CA  . PHE   A 1  474 ? 20.30991  14.05583 42.13076 1.000 53.34123  ? 474 PHE   A CA  1 
ATOM   3747 C C   . PHE   A 1  474 ? 19.79937  13.98960 40.69410 1.000 53.17431  ? 474 PHE   A C   1 
ATOM   3748 O O   . PHE   A 1  474 ? 18.76834  13.36382 40.42538 1.000 53.22776  ? 474 PHE   A O   1 
ATOM   3749 C CB  . PHE   A 1  474 ? 20.02049  15.42812 42.72354 1.000 51.78020  ? 474 PHE   A CB  1 
ATOM   3750 C CG  . PHE   A 1  474 ? 18.57678  15.79308 42.63287 1.000 54.56650  ? 474 PHE   A CG  1 
ATOM   3751 C CD1 . PHE   A 1  474 ? 17.64746  15.16720 43.46240 1.000 55.72066  ? 474 PHE   A CD1 1 
ATOM   3752 C CD2 . PHE   A 1  474 ? 18.13384  16.69083 41.68514 1.000 45.90358  ? 474 PHE   A CD2 1 
ATOM   3753 C CE1 . PHE   A 1  474 ? 16.30019  15.46864 43.37641 1.000 53.60008  ? 474 PHE   A CE1 1 
ATOM   3754 C CE2 . PHE   A 1  474 ? 16.79333  17.00138 41.58625 1.000 53.40163  ? 474 PHE   A CE2 1 
ATOM   3755 C CZ  . PHE   A 1  474 ? 15.87124  16.39190 42.42990 1.000 54.76343  ? 474 PHE   A CZ  1 
ATOM   3756 N N   . ALA   A 1  475 ? 20.49212  14.63622 39.75580 1.000 48.46118  ? 475 ALA   A N   1 
ATOM   3757 C CA  . ALA   A 1  475 ? 20.03004  14.58817 38.37217 1.000 48.93183  ? 475 ALA   A CA  1 
ATOM   3758 C C   . ALA   A 1  475 ? 19.96972  13.15301 37.87071 1.000 61.86584  ? 475 ALA   A C   1 
ATOM   3759 O O   . ALA   A 1  475 ? 18.96894  12.72959 37.27773 1.000 58.53435  ? 475 ALA   A O   1 
ATOM   3760 C CB  . ALA   A 1  475 ? 20.94464  15.40811 37.48341 1.000 50.95326  ? 475 ALA   A CB  1 
ATOM   3761 N N   . LYS   A 1  476 ? 21.02717  12.37680 38.12779 1.000 53.60644  ? 476 LYS   A N   1 
ATOM   3762 C CA  . LYS   A 1  476 ? 21.08808  11.03048 37.58553 1.000 58.55744  ? 476 LYS   A CA  1 
ATOM   3763 C C   . LYS   A 1  476 ? 20.12658  10.09386 38.31059 1.000 60.99108  ? 476 LYS   A C   1 
ATOM   3764 O O   . LYS   A 1  476 ? 19.39650  9.32950  37.67592 1.000 58.44691  ? 476 LYS   A O   1 
ATOM   3765 C CB  . LYS   A 1  476 ? 22.51427  10.48503 37.67165 1.000 64.89010  ? 476 LYS   A CB  1 
ATOM   3766 C CG  . LYS   A 1  476 ? 23.57068  11.28345 36.92889 1.000 61.36988  ? 476 LYS   A CG  1 
ATOM   3767 C CD  . LYS   A 1  476 ? 24.89263  10.54457 36.99492 1.000 53.45373  ? 476 LYS   A CD  1 
ATOM   3768 C CE  . LYS   A 1  476 ? 25.96689  11.20881 36.16499 1.000 60.70318  ? 476 LYS   A CE  1 
ATOM   3769 N NZ  . LYS   A 1  476 ? 27.26933  11.25420 36.92032 1.000 66.47465  ? 476 LYS   A NZ  1 
ATOM   3770 N N   . TYR   A 1  477 ? 20.12173  10.12080 39.64105 1.000 59.97980  ? 477 TYR   A N   1 
ATOM   3771 C CA  . TYR   A 1  477 ? 19.45200  9.07757  40.41668 1.000 61.67282  ? 477 TYR   A CA  1 
ATOM   3772 C C   . TYR   A 1  477 ? 18.33184  9.58568  41.31305 1.000 58.56485  ? 477 TYR   A C   1 
ATOM   3773 O O   . TYR   A 1  477 ? 17.80122  8.81096  42.11198 1.000 59.36556  ? 477 TYR   A O   1 
ATOM   3774 C CB  . TYR   A 1  477 ? 20.47476  8.33432  41.26980 1.000 60.74640  ? 477 TYR   A CB  1 
ATOM   3775 C CG  . TYR   A 1  477 ? 21.70830  7.99689  40.49395 1.000 62.81575  ? 477 TYR   A CG  1 
ATOM   3776 C CD1 . TYR   A 1  477 ? 21.61182  7.24654  39.32555 1.000 63.72183  ? 477 TYR   A CD1 1 
ATOM   3777 C CD2 . TYR   A 1  477 ? 22.95950  8.40753  40.91932 1.000 55.12815  ? 477 TYR   A CD2 1 
ATOM   3778 C CE1 . TYR   A 1  477 ? 22.71634  6.91900  38.60092 1.000 61.39570  ? 477 TYR   A CE1 1 
ATOM   3779 C CE2 . TYR   A 1  477 ? 24.08931  8.09591  40.18926 1.000 59.69396  ? 477 TYR   A CE2 1 
ATOM   3780 C CZ  . TYR   A 1  477 ? 23.95797  7.34711  39.02517 1.000 63.42350  ? 477 TYR   A CZ  1 
ATOM   3781 O OH  . TYR   A 1  477 ? 25.05699  7.02351  38.27517 1.000 61.86103  ? 477 TYR   A OH  1 
ATOM   3782 N N   . GLY   A 1  478 ? 17.97237  10.85722 41.21255 1.000 56.36740  ? 478 GLY   A N   1 
ATOM   3783 C CA  . GLY   A 1  478 ? 17.01231  11.45144 42.11771 1.000 58.32141  ? 478 GLY   A CA  1 
ATOM   3784 C C   . GLY   A 1  478 ? 17.39112  11.42779 43.58566 1.000 59.05432  ? 478 GLY   A C   1 
ATOM   3785 O O   . GLY   A 1  478 ? 16.52799  11.63639 44.43491 1.000 60.32043  ? 478 GLY   A O   1 
ATOM   3786 N N   . ASN   A 1  479 ? 18.66069  11.20493 43.91021 1.000 56.08424  ? 479 ASN   A N   1 
ATOM   3787 C CA  . ASN   A 1  479 ? 19.05512  11.10750 45.31081 1.000 55.35542  ? 479 ASN   A CA  1 
ATOM   3788 C C   . ASN   A 1  479 ? 20.37749  11.83804 45.54020 1.000 51.73621  ? 479 ASN   A C   1 
ATOM   3789 O O   . ASN   A 1  479 ? 21.42142  11.36296 45.09408 1.000 54.80720  ? 479 ASN   A O   1 
ATOM   3790 C CB  . ASN   A 1  479 ? 19.16760  9.63906  45.70605 1.000 55.99587  ? 479 ASN   A CB  1 
ATOM   3791 C CG  . ASN   A 1  479 ? 19.02763  9.42331  47.19786 1.000 62.72965  ? 479 ASN   A CG  1 
ATOM   3792 O OD1 . ASN   A 1  479 ? 18.89564  10.38454 47.95396 1.000 63.10140  ? 479 ASN   A OD1 1 
ATOM   3793 N ND2 . ASN   A 1  479 ? 19.05306  8.15038  47.63409 1.000 57.11462  ? 479 ASN   A ND2 1 
ATOM   3794 N N   . PRO   A 1  480 ? 20.38589  13.00327 46.21294 1.000 58.65567  ? 480 PRO   A N   1 
ATOM   3795 C CA  . PRO   A 1  480 ? 21.57750  13.86006 46.24071 1.000 53.47082  ? 480 PRO   A CA  1 
ATOM   3796 C C   . PRO   A 1  480 ? 22.57529  13.46824 47.33251 1.000 59.49668  ? 480 PRO   A C   1 
ATOM   3797 O O   . PRO   A 1  480 ? 22.99148  14.29601 48.15401 1.000 63.37871  ? 480 PRO   A O   1 
ATOM   3798 C CB  . PRO   A 1  480 ? 20.98140  15.25068 46.48118 1.000 54.58183  ? 480 PRO   A CB  1 
ATOM   3799 C CG  . PRO   A 1  480 ? 19.79800  14.98026 47.37033 1.000 52.52200  ? 480 PRO   A CG  1 
ATOM   3800 C CD  . PRO   A 1  480 ? 19.23939  13.64391 46.89447 1.000 55.22941  ? 480 PRO   A CD  1 
ATOM   3801 N N   . GLN   A 1  481 ? 22.97176  12.20195 47.34581 1.000 55.32553  ? 481 GLN   A N   1 
ATOM   3802 C CA  . GLN   A 1  481 ? 23.98534  11.74773 48.28177 1.000 63.48624  ? 481 GLN   A CA  1 
ATOM   3803 C C   . GLN   A 1  481 ? 25.38049  11.86371 47.66982 1.000 64.01819  ? 481 GLN   A C   1 
ATOM   3804 O O   . GLN   A 1  481 ? 25.55707  11.93061 46.44646 1.000 62.41385  ? 481 GLN   A O   1 
ATOM   3805 C CB  . GLN   A 1  481 ? 23.71087  10.30364 48.72079 1.000 54.53744  ? 481 GLN   A CB  1 
ATOM   3806 C CG  . GLN   A 1  481 ? 22.24418  10.02976 49.06792 1.000 56.20706  ? 481 GLN   A CG  1 
ATOM   3807 C CD  . GLN   A 1  481 ? 21.70106  10.94926 50.16174 1.000 59.61893  ? 481 GLN   A CD  1 
ATOM   3808 O OE1 . GLN   A 1  481 ? 22.41816  11.33900 51.08716 1.000 64.66057  ? 481 GLN   A OE1 1 
ATOM   3809 N NE2 . GLN   A 1  481 ? 20.43085  11.29892 50.05407 1.000 56.49457  ? 481 GLN   A NE2 1 
ATOM   3810 N N   . GLU   A 1  482 ? 26.37042  11.94775 48.55660 1.000 63.59134  ? 482 GLU   A N   1 
ATOM   3811 C CA  . GLU   A 1  482 ? 27.77603  11.67924 48.25479 1.000 61.67999  ? 482 GLU   A CA  1 
ATOM   3812 C C   . GLU   A 1  482 ? 28.05525  10.38418 48.99129 1.000 62.83149  ? 482 GLU   A C   1 
ATOM   3813 O O   . GLU   A 1  482 ? 28.19358  10.38552 50.21312 1.000 68.02472  ? 482 GLU   A O   1 
ATOM   3814 C CB  . GLU   A 1  482 ? 28.69094  12.80368 48.72226 1.000 61.91710  ? 482 GLU   A CB  1 
ATOM   3815 C CG  . GLU   A 1  482 ? 30.09313  12.78612 48.11623 1.000 66.57155  ? 482 GLU   A CG  1 
ATOM   3816 C CD  . GLU   A 1  482 ? 30.87569  11.52946 48.47493 1.000 75.49965  ? 482 GLU   A CD  1 
ATOM   3817 O OE1 . GLU   A 1  482 ? 31.05918  11.25087 49.68576 1.000 72.39538  ? 482 GLU   A OE1 1 
ATOM   3818 O OE2 . GLU   A 1  482 ? 31.29149  10.80675 47.54054 1.000 79.33901  ? 482 GLU   A OE2 1 
ATOM   3819 N N   . THR   A 1  483 ? 28.08435  9.27742  48.25924 1.000 62.90664  ? 483 THR   A N   1 
ATOM   3820 C CA  . THR   A 1  483 ? 28.07777  7.95264  48.86502 1.000 66.24487  ? 483 THR   A CA  1 
ATOM   3821 C C   . THR   A 1  483 ? 29.47047  7.45641  49.23549 1.000 74.51746  ? 483 THR   A C   1 
ATOM   3822 O O   . THR   A 1  483 ? 29.63238  6.28320  49.58637 1.000 65.89257  ? 483 THR   A O   1 
ATOM   3823 C CB  . THR   A 1  483 ? 27.41270  6.94218  47.92195 1.000 64.16317  ? 483 THR   A CB  1 
ATOM   3824 O OG1 . THR   A 1  483 ? 28.19584  6.79605  46.72728 1.000 69.30200  ? 483 THR   A OG1 1 
ATOM   3825 C CG2 . THR   A 1  483 ? 26.02621  7.40393  47.54060 1.000 64.88684  ? 483 THR   A CG2 1 
ATOM   3826 N N   . GLN   A 1  484 ? 30.48373  8.30757  49.19218 1.000 76.36470  ? 484 GLN   A N   1 
ATOM   3827 C CA  . GLN   A 1  484 ? 31.80638  7.71320  49.18694 1.000 79.62547  ? 484 GLN   A CA  1 
ATOM   3828 C C   . GLN   A 1  484 ? 32.76067  8.25502  50.23045 1.000 81.17734  ? 484 GLN   A C   1 
ATOM   3829 O O   . GLN   A 1  484 ? 33.41377  7.48143  50.93113 1.000 78.05384  ? 484 GLN   A O   1 
ATOM   3830 C CB  . GLN   A 1  484 ? 32.38189  7.87871  47.80043 1.000 84.18633  ? 484 GLN   A CB  1 
ATOM   3831 C CG  . GLN   A 1  484 ? 31.98435  6.70285  47.03647 1.000 87.77195  ? 484 GLN   A CG  1 
ATOM   3832 C CD  . GLN   A 1  484 ? 32.44867  6.69934  45.62771 1.000 89.39845  ? 484 GLN   A CD  1 
ATOM   3833 O OE1 . GLN   A 1  484 ? 33.08292  7.63879  45.14408 1.000 88.49327  ? 484 GLN   A OE1 1 
ATOM   3834 N NE2 . GLN   A 1  484 ? 32.14237  5.61041  44.94671 1.000 97.29605  ? 484 GLN   A NE2 1 
ATOM   3835 N N   . ASN   A 1  485 ? 32.87077  9.57185  50.32654 1.000 92.41462  ? 485 ASN   A N   1 
ATOM   3836 C CA  . ASN   A 1  485 ? 33.81685  10.17716 51.26051 1.000 89.82655  ? 485 ASN   A CA  1 
ATOM   3837 C C   . ASN   A 1  485 ? 33.16831  10.37065 52.63742 1.000 91.87595  ? 485 ASN   A C   1 
ATOM   3838 O O   . ASN   A 1  485 ? 33.26698  11.42886 53.26588 1.000 94.67177  ? 485 ASN   A O   1 
ATOM   3839 C CB  . ASN   A 1  485 ? 34.36036  11.47944 50.66738 1.000 90.38842  ? 485 ASN   A CB  1 
ATOM   3840 C CG  . ASN   A 1  485 ? 35.26692  11.23156 49.44160 1.000 92.48825  ? 485 ASN   A CG  1 
ATOM   3841 O OD1 . ASN   A 1  485 ? 35.25326  10.13815 48.89038 1.000 96.19971  ? 485 ASN   A OD1 1 
ATOM   3842 N ND2 . ASN   A 1  485 ? 36.05642  12.24254 49.02573 1.000 102.52558 ? 485 ASN   A ND2 1 
ATOM   3843 N N   . GLN   A 1  486 ? 32.50305  9.29732  53.09530 1.000 86.97367  ? 486 GLN   A N   1 
ATOM   3844 C CA  . GLN   A 1  486 ? 31.73924  9.23444  54.35379 1.000 80.93631  ? 486 GLN   A CA  1 
ATOM   3845 C C   . GLN   A 1  486 ? 30.95488  10.51872 54.61508 1.000 84.81508  ? 486 GLN   A C   1 
ATOM   3846 O O   . GLN   A 1  486 ? 30.99808  11.10587 55.69869 1.000 85.99395  ? 486 GLN   A O   1 
ATOM   3847 C CB  . GLN   A 1  486 ? 32.64753  8.90962  55.53340 1.000 88.22233  ? 486 GLN   A CB  1 
ATOM   3848 N N   . SER   A 1  487 ? 30.21758  10.95439 53.60357 1.000 79.72817  ? 487 SER   A N   1 
ATOM   3849 C CA  . SER   A 1  487 ? 29.49811  12.20880 53.73599 1.000 82.63743  ? 487 SER   A CA  1 
ATOM   3850 C C   . SER   A 1  487 ? 28.28916  12.04986 54.64919 1.000 84.37385  ? 487 SER   A C   1 
ATOM   3851 O O   . SER   A 1  487 ? 27.77461  10.94770 54.87606 1.000 77.93583  ? 487 SER   A O   1 
ATOM   3852 C CB  . SER   A 1  487 ? 29.04407  12.72404 52.37447 1.000 69.43564  ? 487 SER   A CB  1 
ATOM   3853 O OG  . SER   A 1  487 ? 30.14343  12.78142 51.49164 1.000 78.22650  ? 487 SER   A OG  1 
ATOM   3854 N N   . THR   A 1  488 ? 27.86618  13.18335 55.20240 1.000 83.16742  ? 488 THR   A N   1 
ATOM   3855 C CA  . THR   A 1  488 ? 26.57952  13.27367 55.87204 1.000 73.23238  ? 488 THR   A CA  1 
ATOM   3856 C C   . THR   A 1  488 ? 25.48026  12.90350 54.88849 1.000 71.62070  ? 488 THR   A C   1 
ATOM   3857 O O   . THR   A 1  488 ? 25.45713  13.37817 53.74645 1.000 72.10587  ? 488 THR   A O   1 
ATOM   3858 C CB  . THR   A 1  488 ? 26.35957  14.69823 56.40040 1.000 76.49697  ? 488 THR   A CB  1 
ATOM   3859 O OG1 . THR   A 1  488 ? 27.43926  15.07103 57.26519 1.000 82.11924  ? 488 THR   A OG1 1 
ATOM   3860 C CG2 . THR   A 1  488 ? 25.06297  14.79305 57.16714 1.000 68.89891  ? 488 THR   A CG2 1 
ATOM   3861 N N   . SER   A 1  489 ? 24.57147  12.05234 55.32704 1.000 67.94783  ? 489 SER   A N   1 
ATOM   3862 C CA  . SER   A 1  489 ? 23.47202  11.64285 54.47374 1.000 65.88799  ? 489 SER   A CA  1 
ATOM   3863 C C   . SER   A 1  489 ? 22.42474  12.75379 54.46515 1.000 67.60476  ? 489 SER   A C   1 
ATOM   3864 O O   . SER   A 1  489 ? 22.11277  13.32760 55.51418 1.000 65.62946  ? 489 SER   A O   1 
ATOM   3865 C CB  . SER   A 1  489 ? 22.89601  10.32227 54.98286 1.000 64.94917  ? 489 SER   A CB  1 
ATOM   3866 O OG  . SER   A 1  489 ? 22.39506  9.52785  53.92209 1.000 77.88761  ? 489 SER   A OG  1 
ATOM   3867 N N   . TRP   A 1  490 ? 21.92826  13.09359 53.27260 1.000 61.37363  ? 490 TRP   A N   1 
ATOM   3868 C CA  . TRP   A 1  490 ? 20.92111  14.13249 53.11408 1.000 60.34533  ? 490 TRP   A CA  1 
ATOM   3869 C C   . TRP   A 1  490 ? 19.53779  13.49541 53.24665 1.000 61.39417  ? 490 TRP   A C   1 
ATOM   3870 O O   . TRP   A 1  490 ? 19.13058  12.73970 52.35380 1.000 56.49487  ? 490 TRP   A O   1 
ATOM   3871 C CB  . TRP   A 1  490 ? 21.08226  14.80549 51.75877 1.000 54.32288  ? 490 TRP   A CB  1 
ATOM   3872 C CG  . TRP   A 1  490 ? 20.32244  16.06326 51.54827 1.000 58.36027  ? 490 TRP   A CG  1 
ATOM   3873 C CD1 . TRP   A 1  490 ? 19.20240  16.49003 52.22478 1.000 57.52816  ? 490 TRP   A CD1 1 
ATOM   3874 C CD2 . TRP   A 1  490 ? 20.62923  17.09266 50.59382 1.000 55.02806  ? 490 TRP   A CD2 1 
ATOM   3875 N NE1 . TRP   A 1  490 ? 18.79924  17.72299 51.74317 1.000 53.38404  ? 490 TRP   A NE1 1 
ATOM   3876 C CE2 . TRP   A 1  490 ? 19.65101  18.10923 50.74009 1.000 52.40445  ? 490 TRP   A CE2 1 
ATOM   3877 C CE3 . TRP   A 1  490 ? 21.63106  17.25182 49.62797 1.000 55.08468  ? 490 TRP   A CE3 1 
ATOM   3878 C CZ2 . TRP   A 1  490 ? 19.64340  19.26326 49.94604 1.000 53.39111  ? 490 TRP   A CZ2 1 
ATOM   3879 C CZ3 . TRP   A 1  490 ? 21.62937  18.41372 48.84056 1.000 57.37412  ? 490 TRP   A CZ3 1 
ATOM   3880 C CH2 . TRP   A 1  490 ? 20.63718  19.39844 49.00390 1.000 53.88518  ? 490 TRP   A CH2 1 
ATOM   3881 N N   . PRO   A 1  491 ? 18.78821  13.76360 54.31089 1.000 59.39166  ? 491 PRO   A N   1 
ATOM   3882 C CA  . PRO   A 1  491 ? 17.45629  13.16221 54.45484 1.000 60.64450  ? 491 PRO   A CA  1 
ATOM   3883 C C   . PRO   A 1  491 ? 16.41450  13.87062 53.59691 1.000 56.13426  ? 491 PRO   A C   1 
ATOM   3884 O O   . PRO   A 1  491 ? 16.56419  15.03141 53.20302 1.000 60.87343  ? 491 PRO   A O   1 
ATOM   3885 C CB  . PRO   A 1  491 ? 17.14808  13.35552 55.94371 1.000 53.16066  ? 491 PRO   A CB  1 
ATOM   3886 C CG  . PRO   A 1  491 ? 17.81539  14.68001 56.26102 1.000 66.13439  ? 491 PRO   A CG  1 
ATOM   3887 C CD  . PRO   A 1  491 ? 19.03586  14.79900 55.33186 1.000 62.59089  ? 491 PRO   A CD  1 
ATOM   3888 N N   . VAL   A 1  492 ? 15.32741  13.15576 53.32129 1.000 54.80269  ? 492 VAL   A N   1 
ATOM   3889 C CA  . VAL   A 1  492 ? 14.24055  13.78613 52.58393 1.000 57.83284  ? 492 VAL   A CA  1 
ATOM   3890 C C   . VAL   A 1  492 ? 13.51751  14.75810 53.50885 1.000 61.69936  ? 492 VAL   A C   1 
ATOM   3891 O O   . VAL   A 1  492 ? 13.46753  14.57246 54.73951 1.000 62.16045  ? 492 VAL   A O   1 
ATOM   3892 C CB  . VAL   A 1  492 ? 13.26920  12.74848 51.98752 1.000 57.85171  ? 492 VAL   A CB  1 
ATOM   3893 C CG1 . VAL   A 1  492 ? 14.04774  11.60055 51.31823 1.000 59.81862  ? 492 VAL   A CG1 1 
ATOM   3894 C CG2 . VAL   A 1  492 ? 12.35330  12.21910 53.03916 1.000 52.84419  ? 492 VAL   A CG2 1 
ATOM   3895 N N   . PHE   A 1  493 ? 12.97395  15.81944 52.91208 1.000 54.52421  ? 493 PHE   A N   1 
ATOM   3896 C CA  . PHE   A 1  493 ? 12.21732  16.83952 53.63051 1.000 59.91526  ? 493 PHE   A CA  1 
ATOM   3897 C C   . PHE   A 1  493 ? 10.77635  16.37173 53.78030 1.000 61.58513  ? 493 PHE   A C   1 
ATOM   3898 O O   . PHE   A 1  493 ? 10.02331  16.35199 52.80912 1.000 66.23983  ? 493 PHE   A O   1 
ATOM   3899 C CB  . PHE   A 1  493 ? 12.29404  18.16770 52.87671 1.000 63.08916  ? 493 PHE   A CB  1 
ATOM   3900 C CG  . PHE   A 1  493 ? 11.60838  19.32575 53.57134 1.000 63.22952  ? 493 PHE   A CG  1 
ATOM   3901 C CD1 . PHE   A 1  493 ? 10.24056  19.52373 53.44183 1.000 60.40086  ? 493 PHE   A CD1 1 
ATOM   3902 C CD2 . PHE   A 1  493 ? 12.34021  20.23366 54.32761 1.000 62.62963  ? 493 PHE   A CD2 1 
ATOM   3903 C CE1 . PHE   A 1  493 ? 9.61069   20.58195 54.06450 1.000 59.33340  ? 493 PHE   A CE1 1 
ATOM   3904 C CE2 . PHE   A 1  493 ? 11.71235  21.30471 54.94369 1.000 59.67596  ? 493 PHE   A CE2 1 
ATOM   3905 C CZ  . PHE   A 1  493 ? 10.34497  21.46906 54.81314 1.000 62.78998  ? 493 PHE   A CZ  1 
ATOM   3906 N N   . LYS   A 1  494 ? 10.39670  15.97656 54.98689 1.000 68.00576  ? 494 LYS   A N   1 
ATOM   3907 C CA  . LYS   A 1  494 ? 9.01609   15.65332 55.31265 1.000 71.12307  ? 494 LYS   A CA  1 
ATOM   3908 C C   . LYS   A 1  494 ? 8.35044   16.83888 56.00200 1.000 69.54354  ? 494 LYS   A C   1 
ATOM   3909 O O   . LYS   A 1  494 ? 8.98629   17.58556 56.74977 1.000 68.55473  ? 494 LYS   A O   1 
ATOM   3910 C CB  . LYS   A 1  494 ? 8.93716   14.41619 56.21284 1.000 72.50078  ? 494 LYS   A CB  1 
ATOM   3911 C CG  . LYS   A 1  494 ? 8.75383   13.10339 55.47927 1.000 73.66062  ? 494 LYS   A CG  1 
ATOM   3912 C CD  . LYS   A 1  494 ? 9.56156   12.01280 56.17714 1.000 89.47780  ? 494 LYS   A CD  1 
ATOM   3913 C CE  . LYS   A 1  494 ? 9.13428   10.58513 55.79809 1.000 90.12255  ? 494 LYS   A CE  1 
ATOM   3914 N NZ  . LYS   A 1  494 ? 10.28108  9.61520  55.94172 1.000 80.58714  ? 494 LYS   A NZ  1 
ATOM   3915 N N   . SER   A 1  495 ? 7.04997   16.99255 55.75714 1.000 75.15803  ? 495 SER   A N   1 
ATOM   3916 C CA  . SER   A 1  495 ? 6.32379   18.15211 56.27059 1.000 78.46555  ? 495 SER   A CA  1 
ATOM   3917 C C   . SER   A 1  495 ? 6.20765   18.14174 57.79404 1.000 78.10125  ? 495 SER   A C   1 
ATOM   3918 O O   . SER   A 1  495 ? 6.08870   19.20665 58.41022 1.000 76.95459  ? 495 SER   A O   1 
ATOM   3919 C CB  . SER   A 1  495 ? 4.93791   18.21253 55.63224 1.000 91.85969  ? 495 SER   A CB  1 
ATOM   3920 O OG  . SER   A 1  495 ? 3.98853   17.52210 56.43690 1.000 97.23919  ? 495 SER   A OG  1 
ATOM   3921 N N   . THR   A 1  496 ? 6.21586   16.96697 58.41941 1.000 74.22765  ? 496 THR   A N   1 
ATOM   3922 C CA  . THR   A 1  496 ? 6.28783   16.92398 59.87471 1.000 75.10151  ? 496 THR   A CA  1 
ATOM   3923 C C   . THR   A 1  496 ? 7.65943   17.35655 60.37374 1.000 72.88209  ? 496 THR   A C   1 
ATOM   3924 O O   . THR   A 1  496 ? 7.78185   18.32477 61.13650 1.000 66.63772  ? 496 THR   A O   1 
ATOM   3925 C CB  . THR   A 1  496 ? 5.98908   15.51994 60.38886 1.000 83.50721  ? 496 THR   A CB  1 
ATOM   3926 O OG1 . THR   A 1  496 ? 4.93591   14.93120 59.61376 1.000 85.35613  ? 496 THR   A OG1 1 
ATOM   3927 C CG2 . THR   A 1  496 ? 5.61144   15.59522 61.85414 1.000 68.54149  ? 496 THR   A CG2 1 
ATOM   3928 N N   . GLU   A 1  497 ? 8.70850   16.63678 59.95348 1.000 72.51518  ? 497 GLU   A N   1 
ATOM   3929 C CA  . GLU   A 1  497 ? 10.03035  16.80575 60.55069 1.000 67.04757  ? 497 GLU   A CA  1 
ATOM   3930 C C   . GLU   A 1  497 ? 10.75633  18.02275 60.00197 1.000 64.34610  ? 497 GLU   A C   1 
ATOM   3931 O O   . GLU   A 1  497 ? 11.45330  18.71750 60.75293 1.000 59.49850  ? 497 GLU   A O   1 
ATOM   3932 C CB  . GLU   A 1  497 ? 10.89775  15.57568 60.31019 1.000 66.98656  ? 497 GLU   A CB  1 
ATOM   3933 C CG  . GLU   A 1  497 ? 10.27899  14.25539 60.68782 1.000 78.88626  ? 497 GLU   A CG  1 
ATOM   3934 C CD  . GLU   A 1  497 ? 10.90560  13.08245 59.91736 1.000 89.70030  ? 497 GLU   A CD  1 
ATOM   3935 O OE1 . GLU   A 1  497 ? 11.57300  13.27966 58.85187 1.000 63.27740  ? 497 GLU   A OE1 1 
ATOM   3936 O OE2 . GLU   A 1  497 ? 10.69631  11.94137 60.38669 1.000 104.31164 ? 497 GLU   A OE2 1 
ATOM   3937 N N   . GLN   A 1  498 ? 10.63603  18.27345 58.69715 1.000 64.47981  ? 498 GLN   A N   1 
ATOM   3938 C CA  . GLN   A 1  498 ? 11.27713  19.42339 58.05551 1.000 59.49641  ? 498 GLN   A CA  1 
ATOM   3939 C C   . GLN   A 1  498 ? 12.78516  19.41905 58.29592 1.000 56.94642  ? 498 GLN   A C   1 
ATOM   3940 O O   . GLN   A 1  498 ? 13.37186  20.41694 58.71207 1.000 59.82975  ? 498 GLN   A O   1 
ATOM   3941 C CB  . GLN   A 1  498 ? 10.65077  20.74012 58.52824 1.000 65.96617  ? 498 GLN   A CB  1 
ATOM   3942 C CG  . GLN   A 1  498 ? 9.17510   20.94883 58.12875 1.000 67.09413  ? 498 GLN   A CG  1 
ATOM   3943 C CD  . GLN   A 1  498 ? 8.49200   22.07320 58.92006 1.000 69.09797  ? 498 GLN   A CD  1 
ATOM   3944 O OE1 . GLN   A 1  498 ? 8.89794   23.23474 58.87225 1.000 76.27121  ? 498 GLN   A OE1 1 
ATOM   3945 N NE2 . GLN   A 1  498 ? 7.45178   21.71576 59.65884 1.000 76.12851  ? 498 GLN   A NE2 1 
ATOM   3946 N N   . LYS   A 1  499 ? 13.41491  18.27220 58.04397 1.000 58.24938  ? 499 LYS   A N   1 
ATOM   3947 C CA  . LYS   A 1  499 ? 14.86731  18.17682 58.09080 1.000 55.50494  ? 499 LYS   A CA  1 
ATOM   3948 C C   . LYS   A 1  499 ? 15.47038  18.77545 56.83352 1.000 56.13396  ? 499 LYS   A C   1 
ATOM   3949 O O   . LYS   A 1  499 ? 14.94967  18.56830 55.73470 1.000 52.09604  ? 499 LYS   A O   1 
ATOM   3950 C CB  . LYS   A 1  499 ? 15.32013  16.72273 58.20265 1.000 53.40854  ? 499 LYS   A CB  1 
ATOM   3951 C CG  . LYS   A 1  499 ? 14.69158  15.94966 59.32620 1.000 59.88727  ? 499 LYS   A CG  1 
ATOM   3952 C CD  . LYS   A 1  499 ? 15.44296  14.66022 59.56398 1.000 54.57319  ? 499 LYS   A CD  1 
ATOM   3953 C CE  . LYS   A 1  499 ? 14.67696  13.71537 60.47023 1.000 57.08960  ? 499 LYS   A CE  1 
ATOM   3954 N NZ  . LYS   A 1  499 ? 15.30793  12.36855 60.46805 1.000 54.42469  ? 499 LYS   A NZ  1 
ATOM   3955 N N   . TYR   A 1  500 ? 16.59128  19.49547 57.00665 1.000 56.93606  ? 500 TYR   A N   1 
ATOM   3956 C CA  . TYR   A 1  500 ? 17.35971  20.08221 55.91639 1.000 53.10618  ? 500 TYR   A CA  1 
ATOM   3957 C C   . TYR   A 1  500 ? 18.84929  19.87977 56.17403 1.000 56.58642  ? 500 TYR   A C   1 
ATOM   3958 O O   . TYR   A 1  500 ? 19.27950  19.66807 57.30736 1.000 56.10754  ? 500 TYR   A O   1 
ATOM   3959 C CB  . TYR   A 1  500 ? 17.06187  21.58432 55.73493 1.000 54.27272  ? 500 TYR   A CB  1 
ATOM   3960 C CG  . TYR   A 1  500 ? 17.41180  22.49914 56.91834 1.000 57.44560  ? 500 TYR   A CG  1 
ATOM   3961 C CD1 . TYR   A 1  500 ? 16.54985  22.62780 58.01740 1.000 52.59586  ? 500 TYR   A CD1 1 
ATOM   3962 C CD2 . TYR   A 1  500 ? 18.60193  23.24178 56.93158 1.000 53.42435  ? 500 TYR   A CD2 1 
ATOM   3963 C CE1 . TYR   A 1  500 ? 16.85518  23.47777 59.08728 1.000 51.96438  ? 500 TYR   A CE1 1 
ATOM   3964 C CE2 . TYR   A 1  500 ? 18.91798  24.08172 57.99758 1.000 55.30186  ? 500 TYR   A CE2 1 
ATOM   3965 C CZ  . TYR   A 1  500 ? 18.04261  24.20649 59.06869 1.000 58.90853  ? 500 TYR   A CZ  1 
ATOM   3966 O OH  . TYR   A 1  500 ? 18.36958  25.04124 60.13056 1.000 54.33480  ? 500 TYR   A OH  1 
ATOM   3967 N N   . LEU   A 1  501 ? 19.63095  19.97513 55.10176 1.000 54.43918  ? 501 LEU   A N   1 
ATOM   3968 C CA  . LEU   A 1  501 ? 21.08197  19.82920 55.13923 1.000 59.04418  ? 501 LEU   A CA  1 
ATOM   3969 C C   . LEU   A 1  501 ? 21.74424  21.20938 55.05637 1.000 58.90748  ? 501 LEU   A C   1 
ATOM   3970 O O   . LEU   A 1  501 ? 21.36142  22.03894 54.22551 1.000 61.08411  ? 501 LEU   A O   1 
ATOM   3971 C CB  . LEU   A 1  501 ? 21.54999  18.93793 53.98206 1.000 54.90869  ? 501 LEU   A CB  1 
ATOM   3972 C CG  . LEU   A 1  501 ? 23.03264  18.57416 53.90406 1.000 61.33810  ? 501 LEU   A CG  1 
ATOM   3973 C CD1 . LEU   A 1  501 ? 23.31308  17.54634 54.94195 1.000 56.06348  ? 501 LEU   A CD1 1 
ATOM   3974 C CD2 . LEU   A 1  501 ? 23.42674  18.03120 52.53058 1.000 57.15019  ? 501 LEU   A CD2 1 
ATOM   3975 N N   . THR   A 1  502 ? 22.71078  21.47273 55.92932 1.000 57.34517  ? 502 THR   A N   1 
ATOM   3976 C CA  . THR   A 1  502 ? 23.50975  22.68548 55.80994 1.000 62.57016  ? 502 THR   A CA  1 
ATOM   3977 C C   . THR   A 1  502 ? 24.78057  22.39236 55.02047 1.000 58.73894  ? 502 THR   A C   1 
ATOM   3978 O O   . THR   A 1  502 ? 25.39453  21.33114 55.17284 1.000 66.44790  ? 502 THR   A O   1 
ATOM   3979 C CB  . THR   A 1  502 ? 23.86471  23.26181 57.18313 1.000 61.67639  ? 502 THR   A CB  1 
ATOM   3980 O OG1 . THR   A 1  502 ? 24.83089  22.42735 57.82628 1.000 65.41014  ? 502 THR   A OG1 1 
ATOM   3981 C CG2 . THR   A 1  502 ? 22.62909  23.35370 58.03996 1.000 59.13599  ? 502 THR   A CG2 1 
ATOM   3982 N N   . LEU   A 1  503 ? 25.15191  23.32752 54.15834 1.000 55.88269  ? 503 LEU   A N   1 
ATOM   3983 C CA  . LEU   A 1  503 ? 26.32694  23.21638 53.29955 1.000 58.92863  ? 503 LEU   A CA  1 
ATOM   3984 C C   . LEU   A 1  503 ? 27.33359  24.27748 53.69833 1.000 59.59433  ? 503 LEU   A C   1 
ATOM   3985 O O   . LEU   A 1  503 ? 27.03255  25.47172 53.64599 1.000 58.26629  ? 503 LEU   A O   1 
ATOM   3986 C CB  . LEU   A 1  503 ? 25.94852  23.38256 51.82703 1.000 57.45699  ? 503 LEU   A CB  1 
ATOM   3987 C CG  . LEU   A 1  503 ? 24.87643  22.43499 51.30599 1.000 58.01880  ? 503 LEU   A CG  1 
ATOM   3988 C CD1 . LEU   A 1  503 ? 24.45133  22.87106 49.91243 1.000 45.23602  ? 503 LEU   A CD1 1 
ATOM   3989 C CD2 . LEU   A 1  503 ? 25.49052  21.01848 51.28682 1.000 51.73333  ? 503 LEU   A CD2 1 
ATOM   3990 N N   . ASN   A 1  504 ? 28.52953  23.84694 54.06292 1.000 67.68572  ? 504 ASN   A N   1 
ATOM   3991 C CA  . ASN   A 1  504 ? 29.58109  24.77647 54.44328 1.000 67.94399  ? 504 ASN   A CA  1 
ATOM   3992 C C   . ASN   A 1  504 ? 30.89563  24.01257 54.41263 1.000 70.95839  ? 504 ASN   A C   1 
ATOM   3993 O O   . ASN   A 1  504 ? 30.92726  22.81674 54.12373 1.000 72.62648  ? 504 ASN   A O   1 
ATOM   3994 C CB  . ASN   A 1  504 ? 29.30006  25.38413 55.81479 1.000 65.07690  ? 504 ASN   A CB  1 
ATOM   3995 C CG  . ASN   A 1  504 ? 29.10089  24.32638 56.85462 1.000 76.72794  ? 504 ASN   A CG  1 
ATOM   3996 O OD1 . ASN   A 1  504 ? 30.06611  23.76399 57.37003 1.000 78.82526  ? 504 ASN   A OD1 1 
ATOM   3997 N ND2 . ASN   A 1  504 ? 27.83677  24.02672 57.16548 1.000 78.23525  ? 504 ASN   A ND2 1 
ATOM   3998 N N   . THR   A 1  505 ? 31.98979  24.70300 54.72336 1.000 71.59007  ? 505 THR   A N   1 
ATOM   3999 C CA  . THR   A 1  505 ? 33.27804  24.04315 54.61153 1.000 76.14491  ? 505 THR   A CA  1 
ATOM   4000 C C   . THR   A 1  505 ? 33.67709  23.28481 55.86831 1.000 82.65518  ? 505 THR   A C   1 
ATOM   4001 O O   . THR   A 1  505 ? 34.54820  22.40827 55.78994 1.000 83.01805  ? 505 THR   A O   1 
ATOM   4002 C CB  . THR   A 1  505 ? 34.39798  25.03913 54.27424 1.000 71.77393  ? 505 THR   A CB  1 
ATOM   4003 O OG1 . THR   A 1  505 ? 34.52737  25.98117 55.33888 1.000 70.27659  ? 505 THR   A OG1 1 
ATOM   4004 C CG2 . THR   A 1  505 ? 34.14754  25.76821 52.94847 1.000 59.62968  ? 505 THR   A CG2 1 
ATOM   4005 N N   . GLU   A 1  506 ? 33.09645  23.59432 57.02286 1.000 79.73159  ? 506 GLU   A N   1 
ATOM   4006 C CA  . GLU   A 1  506 ? 33.54587  22.93485 58.25489 1.000 88.42731  ? 506 GLU   A CA  1 
ATOM   4007 C C   . GLU   A 1  506 ? 32.79835  21.61911 58.46614 1.000 91.79466  ? 506 GLU   A C   1 
ATOM   4008 O O   . GLU   A 1  506 ? 33.37545  20.53556 58.32646 1.000 98.56903  ? 506 GLU   A O   1 
ATOM   4009 C CB  . GLU   A 1  506 ? 33.40866  23.88554 59.44761 1.000 90.66917  ? 506 GLU   A CB  1 
ATOM   4010 C CG  . GLU   A 1  506 ? 32.01310  24.40984 59.68883 1.000 95.79601  ? 506 GLU   A CG  1 
ATOM   4011 C CD  . GLU   A 1  506 ? 31.97204  25.88742 59.98230 1.000 109.43333 ? 506 GLU   A CD  1 
ATOM   4012 O OE1 . GLU   A 1  506 ? 33.04621  26.48486 60.20106 1.000 115.62265 ? 506 GLU   A OE1 1 
ATOM   4013 O OE2 . GLU   A 1  506 ? 30.85715  26.45646 59.97447 1.000 112.40652 ? 506 GLU   A OE2 1 
ATOM   4014 N N   . SER   A 1  507 ? 31.50759  21.70277 58.77832 1.000 92.33096  ? 507 SER   A N   1 
ATOM   4015 C CA  . SER   A 1  507 ? 30.73632  20.55896 59.22753 1.000 92.17225  ? 507 SER   A CA  1 
ATOM   4016 C C   . SER   A 1  507 ? 29.36921  20.61536 58.58106 1.000 88.57720  ? 507 SER   A C   1 
ATOM   4017 O O   . SER   A 1  507 ? 28.67605  21.63002 58.66363 1.000 87.29166  ? 507 SER   A O   1 
ATOM   4018 C CB  . SER   A 1  507 ? 30.57697  20.54217 60.74700 1.000 96.60279  ? 507 SER   A CB  1 
ATOM   4019 O OG  . SER   A 1  507 ? 29.51535  21.40469 61.11502 1.000 99.05848  ? 507 SER   A OG  1 
ATOM   4020 N N   . THR   A 1  508 ? 28.98950  19.52856 57.95068 1.000 84.08610  ? 508 THR   A N   1 
ATOM   4021 C CA  . THR   A 1  508 ? 27.70371  19.41559 57.29709 1.000 81.76402  ? 508 THR   A CA  1 
ATOM   4022 C C   . THR   A 1  508 ? 26.73149  18.70856 58.23759 1.000 77.63855  ? 508 THR   A C   1 
ATOM   4023 O O   . THR   A 1  508 ? 26.93433  17.54368 58.58351 1.000 76.63582  ? 508 THR   A O   1 
ATOM   4024 C CB  . THR   A 1  508 ? 27.89093  18.68401 55.97300 1.000 78.61574  ? 508 THR   A CB  1 
ATOM   4025 O OG1 . THR   A 1  508 ? 28.50325  19.59188 55.03690 1.000 86.77449  ? 508 THR   A OG1 1 
ATOM   4026 C CG2 . THR   A 1  508 ? 26.58835  18.20623 55.44676 1.000 74.93680  ? 508 THR   A CG2 1 
ATOM   4027 N N   . ARG   A 1  509 ? 25.69575  19.41772 58.67747 1.000 72.42497  ? 509 ARG   A N   1 
ATOM   4028 C CA  . ARG   A 1  509 ? 24.80086  18.87510 59.68568 1.000 73.27054  ? 509 ARG   A CA  1 
ATOM   4029 C C   . ARG   A 1  509 ? 23.35526  18.83408 59.21351 1.000 69.27144  ? 509 ARG   A C   1 
ATOM   4030 O O   . ARG   A 1  509 ? 22.94830  19.53134 58.27555 1.000 66.79730  ? 509 ARG   A O   1 
ATOM   4031 C CB  . ARG   A 1  509 ? 24.87539  19.66827 60.99160 1.000 71.98286  ? 509 ARG   A CB  1 
ATOM   4032 C CG  . ARG   A 1  509 ? 26.22661  20.23312 61.29480 1.000 83.43155  ? 509 ARG   A CG  1 
ATOM   4033 C CD  . ARG   A 1  509 ? 26.10814  21.25788 62.38809 1.000 89.69341  ? 509 ARG   A CD  1 
ATOM   4034 N NE  . ARG   A 1  509 ? 25.40775  22.44970 61.90792 1.000 102.66487 ? 509 ARG   A NE  1 
ATOM   4035 C CZ  . ARG   A 1  509 ? 25.90585  23.36128 61.07477 1.000 95.53740  ? 509 ARG   A CZ  1 
ATOM   4036 N NH1 . ARG   A 1  509 ? 27.15197  23.29716 60.63288 1.000 97.92519  ? 509 ARG   A NH1 1 
ATOM   4037 N NH2 . ARG   A 1  509 ? 25.13495  24.36943 60.68120 1.000 80.74591  ? 509 ARG   A NH2 1 
ATOM   4038 N N   . ILE   A 1  510 ? 22.58653  17.98473 59.89422 1.000 68.78002  ? 510 ILE   A N   1 
ATOM   4039 C CA  . ILE   A 1  510 ? 21.14490  17.91816 59.72983 1.000 58.83692  ? 510 ILE   A CA  1 
ATOM   4040 C C   . ILE   A 1  510 ? 20.49625  18.75272 60.81467 1.000 60.14332  ? 510 ILE   A C   1 
ATOM   4041 O O   . ILE   A 1  510 ? 20.77883  18.56035 62.00459 1.000 61.22173  ? 510 ILE   A O   1 
ATOM   4042 C CB  . ILE   A 1  510 ? 20.61765  16.47823 59.79604 1.000 59.78025  ? 510 ILE   A CB  1 
ATOM   4043 C CG1 . ILE   A 1  510 ? 21.34040  15.59096 58.78945 1.000 61.59414  ? 510 ILE   A CG1 1 
ATOM   4044 C CG2 . ILE   A 1  510 ? 19.10730  16.50213 59.48414 1.000 53.82584  ? 510 ILE   A CG2 1 
ATOM   4045 C CD1 . ILE   A 1  510 ? 21.46058  16.23844 57.43276 1.000 60.85401  ? 510 ILE   A CD1 1 
ATOM   4046 N N   . MET   A 1  511 ? 19.58021  19.63022 60.39901 1.000 60.67656  ? 511 MET   A N   1 
ATOM   4047 C CA  . MET   A 1  511 ? 18.78572  20.50811 61.24564 1.000 54.95812  ? 511 MET   A CA  1 
ATOM   4048 C C   . MET   A 1  511 ? 17.31452  20.35791 60.89238 1.000 57.15096  ? 511 MET   A C   1 
ATOM   4049 O O   . MET   A 1  511 ? 16.96327  19.68601 59.91935 1.000 59.20274  ? 511 MET   A O   1 
ATOM   4050 C CB  . MET   A 1  511 ? 19.20631  21.95857 61.04985 1.000 59.97189  ? 511 MET   A CB  1 
ATOM   4051 C CG  . MET   A 1  511 ? 20.68063  22.14560 60.99745 1.000 63.70169  ? 511 MET   A CG  1 
ATOM   4052 S SD  . MET   A 1  511 ? 21.21364  22.32679 62.68654 1.000 84.54279  ? 511 MET   A SD  1 
ATOM   4053 C CE  . MET   A 1  511 ? 21.69221  24.04961 62.56184 1.000 74.13353  ? 511 MET   A CE  1 
ATOM   4054 N N   . THR   A 1  512 ? 16.44942  21.04111 61.65427 1.000 54.12991  ? 512 THR   A N   1 
ATOM   4055 C CA  . THR   A 1  512 ? 15.00411  20.94564 61.47673 1.000 52.55412  ? 512 THR   A CA  1 
ATOM   4056 C C   . THR   A 1  512 ? 14.34667  22.31538 61.55296 1.000 55.32221  ? 512 THR   A C   1 
ATOM   4057 O O   . THR   A 1  512 ? 14.75648  23.16937 62.35016 1.000 49.79264  ? 512 THR   A O   1 
ATOM   4058 C CB  . THR   A 1  512 ? 14.35333  20.03521 62.54679 1.000 59.36277  ? 512 THR   A CB  1 
ATOM   4059 O OG1 . THR   A 1  512 ? 14.59916  20.57772 63.84967 1.000 55.13381  ? 512 THR   A OG1 1 
ATOM   4060 C CG2 . THR   A 1  512 ? 14.89344  18.57537 62.48034 1.000 47.95898  ? 512 THR   A CG2 1 
ATOM   4061 N N   . LYS   A 1  513 ? 13.31814  22.50616 60.71640 1.000 52.54319  ? 513 LYS   A N   1 
ATOM   4062 C CA  . LYS   A 1  513 ? 12.37439  23.62315 60.81856 1.000 45.63801  ? 513 LYS   A CA  1 
ATOM   4063 C C   . LYS   A 1  513 ? 13.07988  24.96846 60.72389 1.000 51.85218  ? 513 LYS   A C   1 
ATOM   4064 O O   . LYS   A 1  513 ? 13.01993  25.78896 61.63940 1.000 58.33810  ? 513 LYS   A O   1 
ATOM   4065 C CB  . LYS   A 1  513 ? 11.55999  23.52762 62.11945 1.000 55.91891  ? 513 LYS   A CB  1 
ATOM   4066 C CG  . LYS   A 1  513 ? 10.55590  22.37456 62.13532 1.000 58.18479  ? 513 LYS   A CG  1 
ATOM   4067 C CD  . LYS   A 1  513 ? 10.02658  22.12092 63.52595 1.000 56.80938  ? 513 LYS   A CD  1 
ATOM   4068 C CE  . LYS   A 1  513 ? 9.02993   20.97330 63.51786 1.000 56.23057  ? 513 LYS   A CE  1 
ATOM   4069 N NZ  . LYS   A 1  513 ? 8.35383   20.76596 64.84146 1.000 62.82691  ? 513 LYS   A NZ  1 
ATOM   4070 N N   . LEU   A 1  514 ? 13.75037  25.18004 59.59433 1.000 52.08071  ? 514 LEU   A N   1 
ATOM   4071 C CA  . LEU   A 1  514 ? 14.49372  26.41793 59.37326 1.000 59.37935  ? 514 LEU   A CA  1 
ATOM   4072 C C   . LEU   A 1  514 ? 13.59089  27.65305 59.45164 1.000 60.01031  ? 514 LEU   A C   1 
ATOM   4073 O O   . LEU   A 1  514 ? 12.50173  27.67144 58.86761 1.000 56.55684  ? 514 LEU   A O   1 
ATOM   4074 C CB  . LEU   A 1  514 ? 15.18341  26.35866 58.00992 1.000 58.13572  ? 514 LEU   A CB  1 
ATOM   4075 C CG  . LEU   A 1  514 ? 15.81977  27.63268 57.47592 1.000 57.66175  ? 514 LEU   A CG  1 
ATOM   4076 C CD1 . LEU   A 1  514 ? 17.10286  27.84909 58.26050 1.000 58.83908  ? 514 LEU   A CD1 1 
ATOM   4077 C CD2 . LEU   A 1  514 ? 16.12072  27.49420 55.98308 1.000 51.82647  ? 514 LEU   A CD2 1 
ATOM   4078 N N   . ARG   A 1  515 ? 14.05509  28.68057 60.18673 1.000 58.54240  ? 515 ARG   A N   1 
ATOM   4079 C CA  A ARG   A 1  515 ? 13.38928  29.98573 60.29920 0.610 63.16436  ? 515 ARG   A CA  1 
ATOM   4080 C CA  B ARG   A 1  515 ? 13.36857  29.97324 60.23216 0.390 63.20604  ? 515 ARG   A CA  1 
ATOM   4081 C C   . ARG   A 1  515 ? 11.91756  29.82650 60.69354 1.000 63.56568  ? 515 ARG   A C   1 
ATOM   4082 O O   . ARG   A 1  515 ? 11.04509  30.59165 60.27667 1.000 61.29131  ? 515 ARG   A O   1 
ATOM   4083 C CB  A ARG   A 1  515 ? 13.54281  30.79595 59.00313 0.610 61.75107  ? 515 ARG   A CB  1 
ATOM   4084 C CB  B ARG   A 1  515 ? 13.41708  30.67195 58.86513 0.390 61.79266  ? 515 ARG   A CB  1 
ATOM   4085 C CG  A ARG   A 1  515 ? 14.97169  31.32584 58.74446 0.610 64.78974  ? 515 ARG   A CG  1 
ATOM   4086 C CG  B ARG   A 1  515 ? 14.50046  31.72422 58.70136 0.390 64.34216  ? 515 ARG   A CG  1 
ATOM   4087 C CD  A ARG   A 1  515 ? 15.08118  32.83291 58.94602 0.610 61.31925  ? 515 ARG   A CD  1 
ATOM   4088 C CD  B ARG   A 1  515 ? 15.88487  31.17000 58.99367 0.390 65.02992  ? 515 ARG   A CD  1 
ATOM   4089 N NE  A ARG   A 1  515 ? 16.31950  33.21219 59.60361 0.610 66.21122  ? 515 ARG   A NE  1 
ATOM   4090 N NE  B ARG   A 1  515 ? 16.92558  31.67261 58.10358 0.390 64.39506  ? 515 ARG   A NE  1 
ATOM   4091 C CZ  A ARG   A 1  515 ? 16.59548  34.43711 60.02866 0.610 68.59381  ? 515 ARG   A CZ  1 
ATOM   4092 C CZ  B ARG   A 1  515 ? 17.27952  32.94489 58.00022 0.390 64.33394  ? 515 ARG   A CZ  1 
ATOM   4093 N NH1 A ARG   A 1  515 ? 15.73840  35.43683 59.86030 0.610 62.52620  ? 515 ARG   A NH1 1 
ATOM   4094 N NH1 B ARG   A 1  515 ? 16.64251  33.89532 58.66679 0.390 67.02778  ? 515 ARG   A NH1 1 
ATOM   4095 N NH2 A ARG   A 1  515 ? 17.75404  34.66198 60.64809 0.610 67.00453  ? 515 ARG   A NH2 1 
ATOM   4096 N NH2 B ARG   A 1  515 ? 18.30007  33.27179 57.21053 0.390 58.40908  ? 515 ARG   A NH2 1 
ATOM   4097 N N   . ALA   A 1  516 ? 11.64521  28.82708 61.53911 1.000 60.10035  ? 516 ALA   A N   1 
ATOM   4098 C CA  . ALA   A 1  516 ? 10.27657  28.50892 61.94976 1.000 66.24642  ? 516 ALA   A CA  1 
ATOM   4099 C C   . ALA   A 1  516 ? 9.49165   29.73175 62.44249 1.000 68.37219  ? 516 ALA   A C   1 
ATOM   4100 O O   . ALA   A 1  516 ? 8.34211   29.94973 62.04127 1.000 66.08143  ? 516 ALA   A O   1 
ATOM   4101 C CB  . ALA   A 1  516 ? 10.30206  27.43308 63.03518 1.000 56.97557  ? 516 ALA   A CB  1 
ATOM   4102 N N   . GLN   A 1  517 ? 10.07602  30.51632 63.34983 1.000 69.71460  ? 517 GLN   A N   1 
ATOM   4103 C CA  . GLN   A 1  517 ? 9.33844   31.64286 63.91894 1.000 75.07553  ? 517 GLN   A CA  1 
ATOM   4104 C C   . GLN   A 1  517 ? 9.09242   32.72691 62.87715 1.000 68.12927  ? 517 GLN   A C   1 
ATOM   4105 O O   . GLN   A 1  517 ? 7.97573   33.24494 62.75445 1.000 64.89077  ? 517 GLN   A O   1 
ATOM   4106 C CB  . GLN   A 1  517 ? 10.10423  32.21257 65.11449 1.000 83.70648  ? 517 GLN   A CB  1 
ATOM   4107 C CG  . GLN   A 1  517 ? 9.67882   31.64323 66.45155 1.000 88.22595  ? 517 GLN   A CG  1 
ATOM   4108 C CD  . GLN   A 1  517 ? 9.66045   32.70181 67.53738 1.000 104.08057 ? 517 GLN   A CD  1 
ATOM   4109 O OE1 . GLN   A 1  517 ? 9.65115   33.90838 67.24937 1.000 101.50804 ? 517 GLN   A OE1 1 
ATOM   4110 N NE2 . GLN   A 1  517 ? 9.65186   32.25976 68.79430 1.000 103.92777 ? 517 GLN   A NE2 1 
ATOM   4111 N N   . GLN   A 1  518 ? 10.12810  33.05604 62.10913 1.000 62.86107  ? 518 GLN   A N   1 
ATOM   4112 C CA  . GLN   A 1  518 ? 10.01623  34.06305 61.07119 1.000 60.89169  ? 518 GLN   A CA  1 
ATOM   4113 C C   . GLN   A 1  518 ? 8.99945   33.66108 60.00383 1.000 61.23594  ? 518 GLN   A C   1 
ATOM   4114 O O   . GLN   A 1  518 ? 8.16569   34.47792 59.58609 1.000 63.48118  ? 518 GLN   A O   1 
ATOM   4115 C CB  . GLN   A 1  518 ? 11.40751  34.29216 60.46911 1.000 66.98485  ? 518 GLN   A CB  1 
ATOM   4116 C CG  . GLN   A 1  518 ? 12.43159  34.82274 61.48744 1.000 64.39803  ? 518 GLN   A CG  1 
ATOM   4117 C CD  . GLN   A 1  518 ? 13.24892  33.73361 62.16715 1.000 66.64213  ? 518 GLN   A CD  1 
ATOM   4118 O OE1 . GLN   A 1  518 ? 12.73419  32.65714 62.48365 1.000 69.42258  ? 518 GLN   A OE1 1 
ATOM   4119 N NE2 . GLN   A 1  518 ? 14.53446  34.00365 62.37917 1.000 68.75712  ? 518 GLN   A NE2 1 
ATOM   4120 N N   . CYS   A 1  519 ? 9.02656   32.40329 59.56501 1.000 61.74389  ? 519 CYS   A N   1 
ATOM   4121 C CA  . CYS   A 1  519 ? 8.17186   32.01962 58.44546 1.000 57.37493  ? 519 CYS   A CA  1 
ATOM   4122 C C   . CYS   A 1  519 ? 6.71314   31.88367 58.85328 1.000 61.53304  ? 519 CYS   A C   1 
ATOM   4123 O O   . CYS   A 1  519 ? 5.82267   32.06031 58.01436 1.000 68.87793  ? 519 CYS   A O   1 
ATOM   4124 C CB  . CYS   A 1  519 ? 8.70448   30.73830 57.80051 1.000 49.36226  ? 519 CYS   A CB  1 
ATOM   4125 S SG  . CYS   A 1  519 ? 10.25050  31.03918 56.85201 1.000 64.09176  ? 519 CYS   A SG  1 
ATOM   4126 N N   . ARG   A 1  520 ? 6.43340   31.61661 60.12776 1.000 59.66591  ? 520 ARG   A N   1 
ATOM   4127 C CA  . ARG   A 1  520 ? 5.03969   31.64665 60.57680 1.000 67.96287  ? 520 ARG   A CA  1 
ATOM   4128 C C   . ARG   A 1  520 ? 4.45893   33.04887 60.44168 1.000 66.61145  ? 520 ARG   A C   1 
ATOM   4129 O O   . ARG   A 1  520 ? 3.31000   33.21841 60.02543 1.000 65.99887  ? 520 ARG   A O   1 
ATOM   4130 C CB  . ARG   A 1  520 ? 4.93498   31.16184 62.02319 1.000 64.67354  ? 520 ARG   A CB  1 
ATOM   4131 C CG  . ARG   A 1  520 ? 4.22110   29.84055 62.19776 1.000 79.03491  ? 520 ARG   A CG  1 
ATOM   4132 C CD  . ARG   A 1  520 ? 4.30230   29.35730 63.65250 1.000 85.09736  ? 520 ARG   A CD  1 
ATOM   4133 N NE  . ARG   A 1  520 ? 5.30075   28.30857 63.85684 1.000 90.33436  ? 520 ARG   A NE  1 
ATOM   4134 C CZ  . ARG   A 1  520 ? 6.26028   28.34065 64.77820 1.000 87.26353  ? 520 ARG   A CZ  1 
ATOM   4135 N NH1 . ARG   A 1  520 ? 6.41947   29.38273 65.58192 1.000 81.36471  ? 520 ARG   A NH1 1 
ATOM   4136 N NH2 . ARG   A 1  520 ? 7.07747   27.29748 64.90148 1.000 87.12613  ? 520 ARG   A NH2 1 
ATOM   4137 N N   . PHE   A 1  521 ? 5.25399   34.07087 60.76211 1.000 67.16650  ? 521 PHE   A N   1 
ATOM   4138 C CA  . PHE   A 1  521 ? 4.79749   35.44066 60.56571 1.000 65.75615  ? 521 PHE   A CA  1 
ATOM   4139 C C   . PHE   A 1  521 ? 4.51128   35.71476 59.09191 1.000 66.69153  ? 521 PHE   A C   1 
ATOM   4140 O O   . PHE   A 1  521 ? 3.42001   36.16426 58.74032 1.000 64.74393  ? 521 PHE   A O   1 
ATOM   4141 C CB  . PHE   A 1  521 ? 5.83129   36.42561 61.11688 1.000 63.96666  ? 521 PHE   A CB  1 
ATOM   4142 C CG  . PHE   A 1  521 ? 5.58410   37.85219 60.69859 1.000 69.75079  ? 521 PHE   A CG  1 
ATOM   4143 C CD1 . PHE   A 1  521 ? 4.67445   38.65301 61.40281 1.000 60.08081  ? 521 PHE   A CD1 1 
ATOM   4144 C CD2 . PHE   A 1  521 ? 6.24237   38.38918 59.59007 1.000 64.44663  ? 521 PHE   A CD2 1 
ATOM   4145 C CE1 . PHE   A 1  521 ? 4.42921   39.95032 61.01393 1.000 62.30076  ? 521 PHE   A CE1 1 
ATOM   4146 C CE2 . PHE   A 1  521 ? 5.99329   39.70342 59.19155 1.000 66.91243  ? 521 PHE   A CE2 1 
ATOM   4147 C CZ  . PHE   A 1  521 ? 5.08440   40.48310 59.91209 1.000 65.20813  ? 521 PHE   A CZ  1 
ATOM   4148 N N   . TRP   A 1  522 ? 5.47503   35.42676 58.20894 1.000 64.66920  ? 522 TRP   A N   1 
ATOM   4149 C CA  . TRP   A 1  522 ? 5.33565   35.82128 56.80712 1.000 65.63169  ? 522 TRP   A CA  1 
ATOM   4150 C C   . TRP   A 1  522 ? 4.28699   34.99144 56.07446 1.000 73.60234  ? 522 TRP   A C   1 
ATOM   4151 O O   . TRP   A 1  522 ? 3.61868   35.49844 55.16770 1.000 71.39019  ? 522 TRP   A O   1 
ATOM   4152 C CB  . TRP   A 1  522 ? 6.68137   35.69881 56.08097 1.000 65.24816  ? 522 TRP   A CB  1 
ATOM   4153 C CG  . TRP   A 1  522 ? 7.67931   36.74714 56.48127 1.000 63.21591  ? 522 TRP   A CG  1 
ATOM   4154 C CD1 . TRP   A 1  522 ? 8.85297   36.54717 57.15680 1.000 62.24325  ? 522 TRP   A CD1 1 
ATOM   4155 C CD2 . TRP   A 1  522 ? 7.59761   38.15287 56.23092 1.000 62.42286  ? 522 TRP   A CD2 1 
ATOM   4156 N NE1 . TRP   A 1  522 ? 9.49690   37.73892 57.35195 1.000 60.18933  ? 522 TRP   A NE1 1 
ATOM   4157 C CE2 . TRP   A 1  522 ? 8.74979   38.74327 56.79002 1.000 62.55264  ? 522 TRP   A CE2 1 
ATOM   4158 C CE3 . TRP   A 1  522 ? 6.65609   38.97367 55.60007 1.000 61.98628  ? 522 TRP   A CE3 1 
ATOM   4159 C CZ2 . TRP   A 1  522 ? 8.98953   40.11562 56.72715 1.000 61.71959  ? 522 TRP   A CZ2 1 
ATOM   4160 C CZ3 . TRP   A 1  522 ? 6.89211   40.33418 55.54377 1.000 61.44188  ? 522 TRP   A CZ3 1 
ATOM   4161 C CH2 . TRP   A 1  522 ? 8.04655   40.89296 56.10298 1.000 64.48017  ? 522 TRP   A CH2 1 
ATOM   4162 N N   . THR   A 1  523 ? 4.13991   33.71816 56.43066 1.000 75.48350  ? 523 THR   A N   1 
ATOM   4163 C CA  . THR   A 1  523 ? 3.32463   32.80290 55.64775 1.000 73.66743  ? 523 THR   A CA  1 
ATOM   4164 C C   . THR   A 1  523 ? 1.92478   32.65203 56.20659 1.000 76.39474  ? 523 THR   A C   1 
ATOM   4165 O O   . THR   A 1  523 ? 0.98554   32.42723 55.43641 1.000 75.86335  ? 523 THR   A O   1 
ATOM   4166 C CB  . THR   A 1  523 ? 4.02478   31.43642 55.55151 1.000 71.08574  ? 523 THR   A CB  1 
ATOM   4167 O OG1 . THR   A 1  523 ? 5.32605   31.63417 54.99634 1.000 67.25934  ? 523 THR   A OG1 1 
ATOM   4168 C CG2 . THR   A 1  523 ? 3.28316   30.46925 54.64700 1.000 72.05996  ? 523 THR   A CG2 1 
ATOM   4169 N N   . SER   A 1  524 ? 1.75155   32.82522 57.51786 1.000 87.11390  ? 524 SER   A N   1 
ATOM   4170 C CA  . SER   A 1  524 ? 0.42782   32.80031 58.13457 1.000 83.30943  ? 524 SER   A CA  1 
ATOM   4171 C C   . SER   A 1  524 ? -0.14559  34.20251 58.29546 1.000 90.47229  ? 524 SER   A C   1 
ATOM   4172 O O   . SER   A 1  524 ? -1.20144  34.51041 57.73777 1.000 101.41684 ? 524 SER   A O   1 
ATOM   4173 C CB  . SER   A 1  524 ? 0.46848   32.10989 59.50307 1.000 90.65303  ? 524 SER   A CB  1 
ATOM   4174 O OG  . SER   A 1  524 ? 0.80293   30.74156 59.37503 1.000 107.80418 ? 524 SER   A OG  1 
ATOM   4175 N N   . PHE   A 1  525 ? 0.52339   35.06302 59.06227 1.000 81.55262  ? 525 PHE   A N   1 
ATOM   4176 C CA  . PHE   A 1  525 ? -0.08263  36.34162 59.43780 1.000 83.54325  ? 525 PHE   A CA  1 
ATOM   4177 C C   . PHE   A 1  525 ? -0.04377  37.33764 58.27664 1.000 85.53964  ? 525 PHE   A C   1 
ATOM   4178 O O   . PHE   A 1  525 ? -1.09217  37.74434 57.76165 1.000 81.40806  ? 525 PHE   A O   1 
ATOM   4179 C CB  . PHE   A 1  525 ? 0.62955   36.90380 60.67500 1.000 80.01602  ? 525 PHE   A CB  1 
ATOM   4180 C CG  . PHE   A 1  525 ? 0.23242   38.30658 61.03224 1.000 81.64230  ? 525 PHE   A CG  1 
ATOM   4181 C CD1 . PHE   A 1  525 ? 0.96416   39.00571 61.96561 1.000 87.25802  ? 525 PHE   A CD1 1 
ATOM   4182 C CD2 . PHE   A 1  525 ? -0.91782  38.90272 60.50567 1.000 87.74804  ? 525 PHE   A CD2 1 
ATOM   4183 C CE1 . PHE   A 1  525 ? 0.60845   40.29712 62.31855 1.000 86.59097  ? 525 PHE   A CE1 1 
ATOM   4184 C CE2 . PHE   A 1  525 ? -1.27940  40.17660 60.84704 1.000 85.24954  ? 525 PHE   A CE2 1 
ATOM   4185 C CZ  . PHE   A 1  525 ? -0.50832  40.88017 61.76642 1.000 88.18140  ? 525 PHE   A CZ  1 
ATOM   4186 N N   . PHE   A 1  526 ? 1.17011   37.77779 57.89300 1.000 82.18391  ? 526 PHE   A N   1 
ATOM   4187 C CA  . PHE   A 1  526 ? 1.41357   38.91435 56.99829 1.000 81.10315  ? 526 PHE   A CA  1 
ATOM   4188 C C   . PHE   A 1  526 ? 0.53672   38.93040 55.74188 1.000 79.47003  ? 526 PHE   A C   1 
ATOM   4189 O O   . PHE   A 1  526 ? 0.12894   40.01221 55.30038 1.000 77.76357  ? 526 PHE   A O   1 
ATOM   4190 C CB  . PHE   A 1  526 ? 2.90257   38.99967 56.59026 1.000 71.17556  ? 526 PHE   A CB  1 
ATOM   4191 C CG  . PHE   A 1  526 ? 3.23798   40.26107 55.82287 1.000 71.44157  ? 526 PHE   A CG  1 
ATOM   4192 C CD1 . PHE   A 1  526 ? 3.29386   41.49328 56.47116 1.000 65.21848  ? 526 PHE   A CD1 1 
ATOM   4193 C CD2 . PHE   A 1  526 ? 3.45123   40.22271 54.45248 1.000 67.77419  ? 526 PHE   A CD2 1 
ATOM   4194 C CE1 . PHE   A 1  526 ? 3.56086   42.64506 55.77181 1.000 66.42094  ? 526 PHE   A CE1 1 
ATOM   4195 C CE2 . PHE   A 1  526 ? 3.72592   41.38141 53.74515 1.000 62.97303  ? 526 PHE   A CE2 1 
ATOM   4196 C CZ  . PHE   A 1  526 ? 3.77959   42.59075 54.40372 1.000 67.20151  ? 526 PHE   A CZ  1 
ATOM   4197 N N   . PRO   A 1  527 ? 0.23284   37.78631 55.11714 1.000 78.68797  ? 527 PRO   A N   1 
ATOM   4198 C CA  . PRO   A 1  527 ? -0.68635  37.81576 53.97050 1.000 78.97652  ? 527 PRO   A CA  1 
ATOM   4199 C C   . PRO   A 1  527 ? -2.05132  38.41114 54.28597 1.000 85.46633  ? 527 PRO   A C   1 
ATOM   4200 O O   . PRO   A 1  527 ? -2.75019  38.81623 53.35084 1.000 85.70643  ? 527 PRO   A O   1 
ATOM   4201 C CB  . PRO   A 1  527 ? -0.79796  36.33830 53.57089 1.000 76.81892  ? 527 PRO   A CB  1 
ATOM   4202 C CG  . PRO   A 1  527 ? 0.48538   35.74819 53.98391 1.000 80.48603  ? 527 PRO   A CG  1 
ATOM   4203 C CD  . PRO   A 1  527 ? 0.88249   36.46593 55.24127 1.000 82.88096  ? 527 PRO   A CD  1 
ATOM   4204 N N   . LYS   A 1  528 ? -2.46271  38.48528 55.55917 1.000 83.46151  ? 528 LYS   A N   1 
ATOM   4205 C CA  . LYS   A 1  528 ? -3.76066  39.08575 55.85757 1.000 87.55543  ? 528 LYS   A CA  1 
ATOM   4206 C C   . LYS   A 1  528 ? -3.74750  40.58945 55.59892 1.000 87.98900  ? 528 LYS   A C   1 
ATOM   4207 O O   . LYS   A 1  528 ? -4.71322  41.13293 55.05601 1.000 96.08395  ? 528 LYS   A O   1 
ATOM   4208 C CB  . LYS   A 1  528 ? -4.17387  38.79281 57.30469 1.000 87.63307  ? 528 LYS   A CB  1 
ATOM   4209 C CG  . LYS   A 1  528 ? -4.81475  37.42142 57.53113 1.000 86.31456  ? 528 LYS   A CG  1 
ATOM   4210 C CD  . LYS   A 1  528 ? -4.28780  36.78291 58.81215 1.000 87.52690  ? 528 LYS   A CD  1 
ATOM   4211 C CE  . LYS   A 1  528 ? -4.29544  35.27010 58.72554 1.000 82.42364  ? 528 LYS   A CE  1 
ATOM   4212 N NZ  . LYS   A 1  528 ? -4.38159  34.68199 60.08728 1.000 86.05329  ? 528 LYS   A NZ  1 
ATOM   4213 N N   . VAL   A 1  529 ? -2.65796  41.27346 55.94803 1.000 90.99859  ? 529 VAL   A N   1 
ATOM   4214 C CA  . VAL   A 1  529 ? -2.63362  42.74411 55.94373 1.000 91.45301  ? 529 VAL   A CA  1 
ATOM   4215 C C   . VAL   A 1  529 ? -2.72839  43.35586 54.53576 1.000 90.24993  ? 529 VAL   A C   1 
ATOM   4216 O O   . VAL   A 1  529 ? -2.40621  42.74423 53.51118 1.000 85.98539  ? 529 VAL   A O   1 
ATOM   4217 C CB  . VAL   A 1  529 ? -1.36569  43.27802 56.65905 1.000 82.93486  ? 529 VAL   A CB  1 
ATOM   4218 C CG1 . VAL   A 1  529 ? -1.08975  42.50172 57.94631 1.000 83.07252  ? 529 VAL   A CG1 1 
ATOM   4219 C CG2 . VAL   A 1  529 ? -0.19098  43.23236 55.74127 1.000 76.70080  ? 529 VAL   A CG2 1 
ATOM   4220 O OXT . VAL   A 1  529 ? -3.13646  44.51323 54.39653 1.000 92.51210  ? 529 VAL   A OXT 1 
HETATM 4221 C C1  . NAG   B 2  .   ? 32.56870  28.20216 9.92208  1.000 100.22812 ? 1   NAG   B C1  1 
HETATM 4222 C C2  . NAG   B 2  .   ? 32.77563  29.21212 8.79079  1.000 102.58209 ? 1   NAG   B C2  1 
HETATM 4223 C C3  . NAG   B 2  .   ? 33.66335  28.61668 7.69632  1.000 108.23298 ? 1   NAG   B C3  1 
HETATM 4224 C C4  . NAG   B 2  .   ? 34.95050  28.05420 8.28502  1.000 113.83571 ? 1   NAG   B C4  1 
HETATM 4225 C C5  . NAG   B 2  .   ? 34.62290  27.07622 9.40708  1.000 113.21595 ? 1   NAG   B C5  1 
HETATM 4226 C C6  . NAG   B 2  .   ? 35.85240  26.56174 10.11580 1.000 114.70160 ? 1   NAG   B C6  1 
HETATM 4227 C C7  . NAG   B 2  .   ? 30.83637  30.71419 8.64661  1.000 102.73785 ? 1   NAG   B C7  1 
HETATM 4228 C C8  . NAG   B 2  .   ? 29.52992  30.98733 7.95866  1.000 93.10076  ? 1   NAG   B C8  1 
HETATM 4229 N N2  . NAG   B 2  .   ? 31.49875  29.62783 8.23518  1.000 95.44267  ? 1   NAG   B N2  1 
HETATM 4230 O O3  . NAG   B 2  .   ? 33.97394  29.62948 6.74766  1.000 108.60891 ? 1   NAG   B O3  1 
HETATM 4231 O O4  . NAG   B 2  .   ? 35.71549  27.39733 7.27891  1.000 118.64821 ? 1   NAG   B O4  1 
HETATM 4232 O O5  . NAG   B 2  .   ? 33.83355  27.74941 10.39914 1.000 107.60119 ? 1   NAG   B O5  1 
HETATM 4233 O O6  . NAG   B 2  .   ? 36.28960  27.53838 11.04848 1.000 123.92870 ? 1   NAG   B O6  1 
HETATM 4234 O O7  . NAG   B 2  .   ? 31.27128  31.44544 9.53369  1.000 106.65831 ? 1   NAG   B O7  1 
HETATM 4235 C C1  . FUC   B 2  .   ? 37.39197  27.09711 11.84913 1.000 129.71002 ? 2   FUC   B C1  1 
HETATM 4236 C C2  . FUC   B 2  .   ? 38.59425  27.81969 11.30775 1.000 128.94594 ? 2   FUC   B C2  1 
HETATM 4237 C C3  . FUC   B 2  .   ? 38.35205  29.35584 11.38035 1.000 134.07645 ? 2   FUC   B C3  1 
HETATM 4238 C C4  . FUC   B 2  .   ? 37.86357  29.82621 12.80281 1.000 134.37189 ? 2   FUC   B C4  1 
HETATM 4239 C C5  . FUC   B 2  .   ? 36.79661  28.85783 13.38541 1.000 134.77375 ? 2   FUC   B C5  1 
HETATM 4240 C C6  . FUC   B 2  .   ? 36.52936  29.06412 14.88499 1.000 122.41537 ? 2   FUC   B C6  1 
HETATM 4241 O O2  . FUC   B 2  .   ? 38.88371  27.41412 9.97274  1.000 128.44700 ? 2   FUC   B O2  1 
HETATM 4242 O O3  . FUC   B 2  .   ? 39.54901  30.07513 11.04519 1.000 137.52190 ? 2   FUC   B O3  1 
HETATM 4243 O O4  . FUC   B 2  .   ? 38.95707  29.94874 13.70671 1.000 136.44553 ? 2   FUC   B O4  1 
HETATM 4244 O O5  . FUC   B 2  .   ? 37.15997  27.44788 13.18513 1.000 136.44510 ? 2   FUC   B O5  1 
HETATM 4245 C C1  . NAG   C 3  .   ? 19.23770  5.45600  27.02133 1.000 108.00701 ? 1   NAG   C C1  1 
HETATM 4246 C C2  . NAG   C 3  .   ? 19.24027  4.21985  26.17684 1.000 111.53137 ? 1   NAG   C C2  1 
HETATM 4247 C C3  . NAG   C 3  .   ? 17.79659  3.77684  25.96572 1.000 108.97794 ? 1   NAG   C C3  1 
HETATM 4248 C C4  . NAG   C 3  .   ? 17.03537  3.71682  27.29429 1.000 116.44598 ? 1   NAG   C C4  1 
HETATM 4249 C C5  . NAG   C 3  .   ? 17.41823  4.82439  28.30489 1.000 111.37041 ? 1   NAG   C C5  1 
HETATM 4250 C C6  . NAG   C 3  .   ? 17.02570  4.48948  29.72953 1.000 113.24300 ? 1   NAG   C C6  1 
HETATM 4251 C C7  . NAG   C 3  .   ? 21.19175  4.16152  24.68448 1.000 101.01403 ? 1   NAG   C C7  1 
HETATM 4252 C C8  . NAG   C 3  .   ? 21.93502  3.52933  25.82983 1.000 99.11350  ? 1   NAG   C C8  1 
HETATM 4253 N N2  . NAG   C 3  .   ? 19.90613  4.45873  24.90544 1.000 102.50083 ? 1   NAG   C N2  1 
HETATM 4254 O O3  . NAG   C 3  .   ? 17.78599  2.50361  25.32938 1.000 116.55428 ? 1   NAG   C O3  1 
HETATM 4255 O O4  . NAG   C 3  .   ? 15.64213  3.90346  27.05188 1.000 114.68059 ? 1   NAG   C O4  1 
HETATM 4256 O O5  . NAG   C 3  .   ? 18.82718  5.13120  28.31188 1.000 106.74385 ? 1   NAG   C O5  1 
HETATM 4257 O O6  . NAG   C 3  .   ? 17.33195  5.54429  30.63361 1.000 109.93413 ? 1   NAG   C O6  1 
HETATM 4258 O O7  . NAG   C 3  .   ? 21.72769  4.37916  23.60586 1.000 103.75963 ? 1   NAG   C O7  1 
HETATM 4259 C C1  . NAG   C 3  .   ? 14.93734  2.86989  26.34022 1.000 120.80502 ? 2   NAG   C C1  1 
HETATM 4260 C C2  . NAG   C 3  .   ? 13.76587  2.39852  27.20562 1.000 125.02024 ? 2   NAG   C C2  1 
HETATM 4261 C C3  . NAG   C 3  .   ? 12.90966  1.37697  26.45108 1.000 129.58959 ? 2   NAG   C C3  1 
HETATM 4262 C C4  . NAG   C 3  .   ? 12.47669  1.93458  25.10178 1.000 130.34948 ? 2   NAG   C C4  1 
HETATM 4263 C C5  . NAG   C 3  .   ? 13.70368  2.37805  24.31142 1.000 130.80766 ? 2   NAG   C C5  1 
HETATM 4264 C C6  . NAG   C 3  .   ? 13.35208  3.03310  22.99514 1.000 132.80542 ? 2   NAG   C C6  1 
HETATM 4265 C C7  . NAG   C 3  .   ? 13.84173  2.28493  29.66133 1.000 123.13112 ? 2   NAG   C C7  1 
HETATM 4266 C C8  . NAG   C 3  .   ? 14.44907  1.60341  30.84969 1.000 117.63703 ? 2   NAG   C C8  1 
HETATM 4267 N N2  . NAG   C 3  .   ? 14.24271  1.84339  28.46286 1.000 126.54308 ? 2   NAG   C N2  1 
HETATM 4268 O O3  . NAG   C 3  .   ? 11.75694  1.05866  27.22302 1.000 128.30105 ? 2   NAG   C O3  1 
HETATM 4269 O O4  . NAG   C 3  .   ? 11.75087  0.95491  24.36479 1.000 133.40164 ? 2   NAG   C O4  1 
HETATM 4270 O O5  . NAG   C 3  .   ? 14.44967  3.34307  25.07226 1.000 126.03366 ? 2   NAG   C O5  1 
HETATM 4271 O O6  . NAG   C 3  .   ? 14.48463  3.65592  22.40409 1.000 131.09151 ? 2   NAG   C O6  1 
HETATM 4272 O O7  . NAG   C 3  .   ? 13.02238  3.19053  29.78025 1.000 121.28759 ? 2   NAG   C O7  1 
HETATM 4273 C C1  . FUC   C 3  .   ? 16.38948  5.59292  31.74010 1.000 115.04478 ? 3   FUC   C C1  1 
HETATM 4274 C C2  . FUC   C 3  .   ? 17.17247  5.87085  33.10100 1.000 116.52896 ? 3   FUC   C C2  1 
HETATM 4275 C C3  . FUC   C 3  .   ? 16.22687  6.22499  34.30497 1.000 124.65014 ? 3   FUC   C C3  1 
HETATM 4276 C C4  . FUC   C 3  .   ? 15.11397  7.25809  33.92195 1.000 120.27236 ? 3   FUC   C C4  1 
HETATM 4277 C C5  . FUC   C 3  .   ? 14.42082  6.89109  32.57783 1.000 116.74432 ? 3   FUC   C C5  1 
HETATM 4278 C C6  . FUC   C 3  .   ? 13.38544  5.75716  32.69015 1.000 110.50809 ? 3   FUC   C C6  1 
HETATM 4279 O O2  . FUC   C 3  .   ? 18.25553  6.81557  32.98561 1.000 96.17244  ? 3   FUC   C O2  1 
HETATM 4280 O O3  . FUC   C 3  .   ? 15.61687  5.03477  34.87137 1.000 117.11675 ? 3   FUC   C O3  1 
HETATM 4281 O O4  . FUC   C 3  .   ? 14.13206  7.37009  34.96865 1.000 123.06218 ? 3   FUC   C O4  1 
HETATM 4282 O O5  . FUC   C 3  .   ? 15.36230  6.55620  31.48781 1.000 113.47191 ? 3   FUC   C O5  1 
HETATM 4283 C C1  . NAG   D 3  .   ? 27.71481  54.59742 55.20918 1.000 76.60787  ? 1   NAG   D C1  1 
HETATM 4284 C C2  . NAG   D 3  .   ? 27.46891  55.54174 56.40216 1.000 76.21617  ? 1   NAG   D C2  1 
HETATM 4285 C C3  . NAG   D 3  .   ? 26.13995  56.27991 56.25032 1.000 75.18913  ? 1   NAG   D C3  1 
HETATM 4286 C C4  . NAG   D 3  .   ? 26.02453  56.93747 54.88194 1.000 82.08064  ? 1   NAG   D C4  1 
HETATM 4287 C C5  . NAG   D 3  .   ? 26.24045  55.86608 53.82600 1.000 81.16133  ? 1   NAG   D C5  1 
HETATM 4288 C C6  . NAG   D 3  .   ? 26.12546  56.36092 52.40386 1.000 87.81046  ? 1   NAG   D C6  1 
HETATM 4289 C C7  . NAG   D 3  .   ? 28.59844  54.47423 58.31043 1.000 75.57073  ? 1   NAG   D C7  1 
HETATM 4290 C C8  . NAG   D 3  .   ? 28.41352  53.67979 59.56892 1.000 74.83011  ? 1   NAG   D C8  1 
HETATM 4291 N N2  . NAG   D 3  .   ? 27.48272  54.79086 57.64768 1.000 79.35185  ? 1   NAG   D N2  1 
HETATM 4292 O O3  . NAG   D 3  .   ? 26.04288  57.24508 57.28802 1.000 80.71650  ? 1   NAG   D O3  1 
HETATM 4293 O O4  . NAG   D 3  .   ? 24.72391  57.49184 54.70839 1.000 84.95366  ? 1   NAG   D O4  1 
HETATM 4294 O O5  . NAG   D 3  .   ? 27.55021  55.31158 53.98370 1.000 75.17225  ? 1   NAG   D O5  1 
HETATM 4295 O O6  . NAG   D 3  .   ? 26.83370  57.57142 52.18965 1.000 94.72023  ? 1   NAG   D O6  1 
HETATM 4296 O O7  . NAG   D 3  .   ? 29.70385  54.81195 57.91356 1.000 83.70827  ? 1   NAG   D O7  1 
HETATM 4297 C C1  . NAG   D 3  .   ? 24.68535  58.93336 54.67865 1.000 93.92495  ? 2   NAG   D C1  1 
HETATM 4298 C C2  . NAG   D 3  .   ? 23.42328  59.31730 53.90677 1.000 93.30346  ? 2   NAG   D C2  1 
HETATM 4299 C C3  . NAG   D 3  .   ? 23.22921  60.83272 53.89193 1.000 101.12389 ? 2   NAG   D C3  1 
HETATM 4300 C C4  . NAG   D 3  .   ? 23.28142  61.39768 55.30355 1.000 109.99110 ? 2   NAG   D C4  1 
HETATM 4301 C C5  . NAG   D 3  .   ? 24.56370  60.94430 56.00073 1.000 109.60713 ? 2   NAG   D C5  1 
HETATM 4302 C C6  . NAG   D 3  .   ? 24.62084  61.35736 57.45286 1.000 111.29257 ? 2   NAG   D C6  1 
HETATM 4303 C C7  . NAG   D 3  .   ? 22.64235  57.86079 52.09577 1.000 98.69037  ? 2   NAG   D C7  1 
HETATM 4304 C C8  . NAG   D 3  .   ? 21.62043  57.35253 53.07205 1.000 91.64754  ? 2   NAG   D C8  1 
HETATM 4305 N N2  . NAG   D 3  .   ? 23.47626  58.80001 52.55103 1.000 94.51498  ? 2   NAG   D N2  1 
HETATM 4306 O O3  . NAG   D 3  .   ? 21.96428  61.13658 53.31515 1.000 93.09415  ? 2   NAG   D O3  1 
HETATM 4307 O O4  . NAG   D 3  .   ? 23.21147  62.82022 55.25603 1.000 122.21064 ? 2   NAG   D O4  1 
HETATM 4308 O O5  . NAG   D 3  .   ? 24.64646  59.50894 55.98379 1.000 101.94789 ? 2   NAG   D O5  1 
HETATM 4309 O O6  . NAG   D 3  .   ? 24.28065  60.27090 58.30505 1.000 105.45966 ? 2   NAG   D O6  1 
HETATM 4310 O O7  . NAG   D 3  .   ? 22.70732  57.44127 50.94829 1.000 103.35224 ? 2   NAG   D O7  1 
HETATM 4311 C C1  . FUC   D 3  .   ? 27.68732  57.39438 51.03485 1.000 96.29602  ? 3   FUC   D C1  1 
HETATM 4312 C C2  . FUC   D 3  .   ? 28.23802  58.77571 50.56382 1.000 99.49681  ? 3   FUC   D C2  1 
HETATM 4313 C C3  . FUC   D 3  .   ? 29.19281  59.34780 51.60729 1.000 94.81331  ? 3   FUC   D C3  1 
HETATM 4314 C C4  . FUC   D 3  .   ? 30.34369  58.33220 51.90803 1.000 99.75131  ? 3   FUC   D C4  1 
HETATM 4315 C C5  . FUC   D 3  .   ? 29.74371  56.95300 52.30502 1.000 93.34304  ? 3   FUC   D C5  1 
HETATM 4316 C C6  . FUC   D 3  .   ? 30.78554  55.80594 52.46453 1.000 79.19568  ? 3   FUC   D C6  1 
HETATM 4317 O O2  . FUC   D 3  .   ? 27.21262  59.71636 50.23689 1.000 102.12627 ? 3   FUC   D O2  1 
HETATM 4318 O O3  . FUC   D 3  .   ? 29.75505  60.56252 51.12427 1.000 101.35953 ? 3   FUC   D O3  1 
HETATM 4319 O O4  . FUC   D 3  .   ? 31.20945  58.18291 50.78020 1.000 94.65317  ? 3   FUC   D O4  1 
HETATM 4320 O O5  . FUC   D 3  .   ? 28.76147  56.50603 51.33539 1.000 91.77719  ? 3   FUC   D O5  1 
HETATM 4321 C C1  . NAG   E 3  .   ? -2.22600  52.42505 37.50520 1.000 113.23212 ? 1   NAG   E C1  1 
HETATM 4322 C C2  . NAG   E 3  .   ? -1.60089  52.70683 38.86223 1.000 114.94794 ? 1   NAG   E C2  1 
HETATM 4323 C C3  . NAG   E 3  .   ? -2.03272  54.07796 39.35076 1.000 117.49026 ? 1   NAG   E C3  1 
HETATM 4324 C C4  . NAG   E 3  .   ? -1.58003  55.14627 38.36676 1.000 120.02022 ? 1   NAG   E C4  1 
HETATM 4325 C C5  . NAG   E 3  .   ? -2.03525  54.83005 36.93244 1.000 117.33025 ? 1   NAG   E C5  1 
HETATM 4326 C C6  . NAG   E 3  .   ? -1.29825  55.67339 35.91266 1.000 115.11718 ? 1   NAG   E C6  1 
HETATM 4327 C C7  . NAG   E 3  .   ? -3.05534  51.45143 40.44328 1.000 125.12390 ? 1   NAG   E C7  1 
HETATM 4328 C C8  . NAG   E 3  .   ? -3.06832  50.37087 41.48677 1.000 119.30193 ? 1   NAG   E C8  1 
HETATM 4329 N N2  . NAG   E 3  .   ? -1.86843  51.68227 39.86440 1.000 119.98949 ? 1   NAG   E N2  1 
HETATM 4330 O O3  . NAG   E 3  .   ? -1.47706  54.32846 40.63659 1.000 117.63181 ? 1   NAG   E O3  1 
HETATM 4331 O O4  . NAG   E 3  .   ? -2.13855  56.39376 38.77346 1.000 126.45221 ? 1   NAG   E O4  1 
HETATM 4332 O O5  . NAG   E 3  .   ? -1.80401  53.45328 36.55894 1.000 112.77666 ? 1   NAG   E O5  1 
HETATM 4333 O O6  . NAG   E 3  .   ? 0.10834   55.62746 36.13107 1.000 115.18058 ? 1   NAG   E O6  1 
HETATM 4334 O O7  . NAG   E 3  .   ? -4.07780  52.06111 40.12349 1.000 127.20272 ? 1   NAG   E O7  1 
HETATM 4335 C C1  . NAG   E 3  .   ? -1.16423  57.42001 39.09754 1.000 126.49592 ? 2   NAG   E C1  1 
HETATM 4336 C C2  . NAG   E 3  .   ? -1.76900  58.78984 38.76618 1.000 128.32861 ? 2   NAG   E C2  1 
HETATM 4337 C C3  . NAG   E 3  .   ? -0.77099  59.90285 39.10164 1.000 131.76542 ? 2   NAG   E C3  1 
HETATM 4338 C C4  . NAG   E 3  .   ? -0.35747  59.80440 40.56447 1.000 135.63404 ? 2   NAG   E C4  1 
HETATM 4339 C C5  . NAG   E 3  .   ? 0.20371   58.41115 40.85748 1.000 135.09246 ? 2   NAG   E C5  1 
HETATM 4340 C C6  . NAG   E 3  .   ? 0.51362   58.19644 42.32063 1.000 133.32276 ? 2   NAG   E C6  1 
HETATM 4341 C C7  . NAG   E 3  .   ? -3.33000  58.35220 36.91984 1.000 122.21742 ? 2   NAG   E C7  1 
HETATM 4342 C C8  . NAG   E 3  .   ? -3.58046  58.49533 35.44827 1.000 122.75216 ? 2   NAG   E C8  1 
HETATM 4343 N N2  . NAG   E 3  .   ? -2.17476  58.85679 37.37013 1.000 125.49101 ? 2   NAG   E N2  1 
HETATM 4344 O O3  . NAG   E 3  .   ? -1.33628  61.18481 38.84723 1.000 134.71627 ? 2   NAG   E O3  1 
HETATM 4345 O O4  . NAG   E 3  .   ? 0.60404   60.80616 40.88532 1.000 133.22499 ? 2   NAG   E O4  1 
HETATM 4346 O O5  . NAG   E 3  .   ? -0.74664  57.39432 40.48772 1.000 129.99442 ? 2   NAG   E O5  1 
HETATM 4347 O O6  . NAG   E 3  .   ? 0.11678   56.89643 42.73684 1.000 128.23148 ? 2   NAG   E O6  1 
HETATM 4348 O O7  . NAG   E 3  .   ? -4.13619  57.80214 37.66730 1.000 119.04171 ? 2   NAG   E O7  1 
HETATM 4349 C C1  . FUC   E 3  .   ? 0.80013   56.88194 35.85755 1.000 111.74352 ? 3   FUC   E C1  1 
HETATM 4350 C C2  . FUC   E 3  .   ? 2.07240   57.03343 36.77572 1.000 113.96399 ? 3   FUC   E C2  1 
HETATM 4351 C C3  . FUC   E 3  .   ? 3.16874   56.00290 36.41716 1.000 108.14051 ? 3   FUC   E C3  1 
HETATM 4352 C C4  . FUC   E 3  .   ? 3.56472   56.14566 34.94505 1.000 105.92450 ? 3   FUC   E C4  1 
HETATM 4353 C C5  . FUC   E 3  .   ? 2.29842   56.14936 34.01660 1.000 104.21651 ? 3   FUC   E C5  1 
HETATM 4354 C C6  . FUC   E 3  .   ? 2.58889   56.55666 32.56455 1.000 92.49273  ? 3   FUC   E C6  1 
HETATM 4355 O O2  . FUC   E 3  .   ? 1.77394   57.00387 38.16229 1.000 120.72578 ? 3   FUC   E O2  1 
HETATM 4356 O O3  . FUC   E 3  .   ? 4.35490   56.22166 37.20070 1.000 110.48133 ? 3   FUC   E O3  1 
HETATM 4357 O O4  . FUC   E 3  .   ? 4.36085   57.31450 34.76638 1.000 102.50107 ? 3   FUC   E O4  1 
HETATM 4358 O O5  . FUC   E 3  .   ? 1.20146   57.00477 34.49077 1.000 105.35756 ? 3   FUC   E O5  1 
HETATM 4359 C C1  . NAG   F 4  .   ? -9.57311  46.22156 15.48159 1.000 132.67772 ? 601 NAG   A C1  1 
HETATM 4360 C C2  . NAG   F 4  .   ? -8.54392  45.53772 14.56053 1.000 134.21970 ? 601 NAG   A C2  1 
HETATM 4361 C C3  . NAG   F 4  .   ? -9.14387  44.27424 13.93604 1.000 137.65587 ? 601 NAG   A C3  1 
HETATM 4362 C C4  . NAG   F 4  .   ? -9.69954  43.35529 15.01610 1.000 138.95393 ? 601 NAG   A C4  1 
HETATM 4363 C C5  . NAG   F 4  .   ? -10.70831 44.11513 15.87440 1.000 138.85645 ? 601 NAG   A C5  1 
HETATM 4364 C C6  . NAG   F 4  .   ? -11.24192 43.29935 17.03136 1.000 142.02075 ? 601 NAG   A C6  1 
HETATM 4365 C C7  . NAG   F 4  .   ? -7.01509  46.23941 12.75788 1.000 133.87563 ? 601 NAG   A C7  1 
HETATM 4366 C C8  . NAG   F 4  .   ? -6.70571  47.30299 11.74365 1.000 132.35925 ? 601 NAG   A C8  1 
HETATM 4367 N N2  . NAG   F 4  .   ? -8.09069  46.45580 13.52507 1.000 135.79834 ? 601 NAG   A N2  1 
HETATM 4368 O O3  . NAG   F 4  .   ? -8.15875  43.58264 13.17491 1.000 133.21574 ? 601 NAG   A O3  1 
HETATM 4369 O O4  . NAG   F 4  .   ? -10.31722 42.21876 14.42072 1.000 137.24240 ? 601 NAG   A O4  1 
HETATM 4370 O O5  . NAG   F 4  .   ? -10.07702 45.27116 16.44354 1.000 134.55320 ? 601 NAG   A O5  1 
HETATM 4371 O O6  . NAG   F 4  .   ? -12.02574 44.09121 17.91443 1.000 142.82414 ? 601 NAG   A O6  1 
HETATM 4372 O O7  . NAG   F 4  .   ? -6.32572  45.22941 12.87279 1.000 128.73590 ? 601 NAG   A O7  1 
HETATM 4373 C C1  . NAG   G 4  .   ? 36.98985  12.14703 47.90679 1.000 100.38196 ? 602 NAG   A C1  1 
HETATM 4374 C C2  . NAG   G 4  .   ? 36.70778  13.15081 46.77325 1.000 98.00603  ? 602 NAG   A C2  1 
HETATM 4375 C C3  . NAG   G 4  .   ? 37.81937  13.09470 45.71646 1.000 103.75549 ? 602 NAG   A C3  1 
HETATM 4376 C C4  . NAG   G 4  .   ? 39.18827  13.31496 46.35107 1.000 104.10970 ? 602 NAG   A C4  1 
HETATM 4377 C C5  . NAG   G 4  .   ? 39.42868  12.27623 47.43931 1.000 107.09859 ? 602 NAG   A C5  1 
HETATM 4378 C C6  . NAG   G 4  .   ? 40.73450  12.50298 48.17381 1.000 106.80637 ? 602 NAG   A C6  1 
HETATM 4379 C C7  . NAG   G 4  .   ? 34.30407  13.62440 46.40384 1.000 87.69270  ? 602 NAG   A C7  1 
HETATM 4380 C C8  . NAG   G 4  .   ? 33.07970  13.23094 45.62922 1.000 76.07155  ? 602 NAG   A C8  1 
HETATM 4381 N N2  . NAG   G 4  .   ? 35.41245  12.90737 46.15390 1.000 89.53809  ? 602 NAG   A N2  1 
HETATM 4382 O O3  . NAG   G 4  .   ? 37.57238  14.08326 44.72133 1.000 101.96929 ? 602 NAG   A O3  1 
HETATM 4383 O O4  . NAG   G 4  .   ? 40.22945  13.21087 45.38362 1.000 97.46205  ? 602 NAG   A O4  1 
HETATM 4384 O O5  . NAG   G 4  .   ? 38.37479  12.33997 48.41650 1.000 104.96527 ? 602 NAG   A O5  1 
HETATM 4385 O O6  . NAG   G 4  .   ? 41.00320  11.48232 49.12610 1.000 103.08718 ? 602 NAG   A O6  1 
HETATM 4386 O O7  . NAG   G 4  .   ? 34.28378  14.54203 47.22121 1.000 82.85367  ? 602 NAG   A O7  1 
HETATM 4387 O O1  . MES   H 5  .   ? 15.49490  29.88543 63.29033 0.782 85.99604  ? 603 MES   A O1  1 
HETATM 4388 C C2  . MES   H 5  .   ? 16.25502  31.09795 63.36591 0.782 73.13594  ? 603 MES   A C2  1 
HETATM 4389 C C3  . MES   H 5  .   ? 17.13025  31.30399 62.13529 0.782 75.62908  ? 603 MES   A C3  1 
HETATM 4390 N N4  . MES   H 5  .   ? 17.73304  30.03140 61.74810 0.782 74.25271  ? 603 MES   A N4  1 
HETATM 4391 C C5  . MES   H 5  .   ? 16.96327  28.79090 61.77638 0.782 68.59893  ? 603 MES   A C5  1 
HETATM 4392 C C6  . MES   H 5  .   ? 16.27589  28.70179 63.12319 0.782 68.69989  ? 603 MES   A C6  1 
HETATM 4393 C C7  . MES   H 5  .   ? 18.91183  30.07110 60.88147 0.782 71.61237  ? 603 MES   A C7  1 
HETATM 4394 C C8  . MES   H 5  .   ? 20.02958  30.71176 61.70328 0.782 76.67919  ? 603 MES   A C8  1 
HETATM 4395 S S   . MES   H 5  .   ? 20.59409  32.05244 60.88087 0.782 96.53973  ? 603 MES   A S   1 
HETATM 4396 O O1S . MES   H 5  .   ? 21.52051  31.60197 59.80332 0.782 72.63723  ? 603 MES   A O1S 1 
HETATM 4397 O O2S . MES   H 5  .   ? 19.40764  32.79011 60.33679 0.782 85.47148  ? 603 MES   A O2S 1 
HETATM 4398 O O3S . MES   H 5  .   ? 21.36695  32.95736 61.76646 0.782 84.15296  ? 603 MES   A O3S 1 
HETATM 4399 S S   . SO4   I 6  .   ? 9.47329   9.71224  44.99548 1.000 97.51659  ? 604 SO4   A S   1 
HETATM 4400 O O1  . SO4   I 6  .   ? 9.41607   8.87615  43.79353 1.000 98.61811  ? 604 SO4   A O1  1 
HETATM 4401 O O2  . SO4   I 6  .   ? 9.42992   11.13012 44.61420 1.000 75.89335  ? 604 SO4   A O2  1 
HETATM 4402 O O3  . SO4   I 6  .   ? 10.73398  9.46884  45.69995 1.000 84.60252  ? 604 SO4   A O3  1 
HETATM 4403 O O4  . SO4   I 6  .   ? 8.32639   9.34179  45.84147 1.000 86.48535  ? 604 SO4   A O4  1 
HETATM 4404 S S   . SO4   J 6  .   ? 30.68039  15.94183 55.37065 1.000 102.64078 ? 605 SO4   A S   1 
HETATM 4405 O O1  . SO4   J 6  .   ? 29.60018  15.74809 54.39197 1.000 87.60222  ? 605 SO4   A O1  1 
HETATM 4406 O O2  . SO4   J 6  .   ? 31.71939  14.92221 55.18881 1.000 98.45737  ? 605 SO4   A O2  1 
HETATM 4407 O O3  . SO4   J 6  .   ? 31.30103  17.26259 55.20308 1.000 98.32490  ? 605 SO4   A O3  1 
HETATM 4408 O O4  . SO4   J 6  .   ? 30.13090  15.82675 56.72393 1.000 89.02927  ? 605 SO4   A O4  1 
HETATM 4409 S S   . SO4   K 6  .   ? 8.50449   54.68186 67.27277 1.000 117.53326 ? 606 SO4   A S   1 
HETATM 4410 O O1  . SO4   K 6  .   ? 8.08530   55.54933 66.16245 1.000 101.89700 ? 606 SO4   A O1  1 
HETATM 4411 O O2  . SO4   K 6  .   ? 9.93101   54.36578 67.18383 1.000 106.81270 ? 606 SO4   A O2  1 
HETATM 4412 O O3  . SO4   K 6  .   ? 8.24963   55.36967 68.53736 1.000 124.81999 ? 606 SO4   A O3  1 
HETATM 4413 O O4  . SO4   K 6  .   ? 7.74366   53.43302 67.24368 1.000 114.50513 ? 606 SO4   A O4  1 
HETATM 4414 C C1  . GOL   L 7  .   ? 5.91444   44.61161 41.84749 1.000 87.18082  ? 607 GOL   A C1  1 
HETATM 4415 O O1  . GOL   L 7  .   ? 7.06282   45.42929 41.70591 1.000 76.43129  ? 607 GOL   A O1  1 
HETATM 4416 C C2  . GOL   L 7  .   ? 6.21237   43.24390 41.16830 1.000 82.30742  ? 607 GOL   A C2  1 
HETATM 4417 O O2  . GOL   L 7  .   ? 5.04551   42.61165 40.65870 1.000 85.65820  ? 607 GOL   A O2  1 
HETATM 4418 C C3  . GOL   L 7  .   ? 6.90793   42.41665 42.27643 1.000 76.97826  ? 607 GOL   A C3  1 
HETATM 4419 O O3  . GOL   L 7  .   ? 8.06641   43.09803 42.64335 1.000 78.83634  ? 607 GOL   A O3  1 
HETATM 4420 C C1  . SIA   M 8  .   ? 39.21078  45.37558 50.97246 1.000 106.05408 ? 608 SIA   A C1  1 
HETATM 4421 C C2  . SIA   M 8  .   ? 38.69605  46.83469 50.65198 1.000 101.43877 ? 608 SIA   A C2  1 
HETATM 4422 C C3  . SIA   M 8  .   ? 39.64630  47.74292 49.83131 1.000 98.09058  ? 608 SIA   A C3  1 
HETATM 4423 C C4  . SIA   M 8  .   ? 39.00702  48.97687 49.15711 1.000 97.72554  ? 608 SIA   A C4  1 
HETATM 4424 C C5  . SIA   M 8  .   ? 37.50347  49.03634 49.47554 1.000 94.79536  ? 608 SIA   A C5  1 
HETATM 4425 C C6  . SIA   M 8  .   ? 36.90705  47.66580 49.04818 1.000 94.85954  ? 608 SIA   A C6  1 
HETATM 4426 C C7  . SIA   M 8  .   ? 35.35673  47.55481 49.13573 1.000 88.45147  ? 608 SIA   A C7  1 
HETATM 4427 C C8  . SIA   M 8  .   ? 34.89618  46.11173 49.49702 1.000 82.98630  ? 608 SIA   A C8  1 
HETATM 4428 C C9  . SIA   M 8  .   ? 33.38402  45.92171 49.33844 1.000 72.92665  ? 608 SIA   A C9  1 
HETATM 4429 C C10 . SIA   M 8  .   ? 36.44234  50.61993 47.70481 1.000 87.57129  ? 608 SIA   A C10 1 
HETATM 4430 C C11 . SIA   M 8  .   ? 35.66073  51.93665 47.63465 1.000 70.06097  ? 608 SIA   A C11 1 
HETATM 4431 N N5  . SIA   M 8  .   ? 36.77366  50.22442 48.96929 1.000 92.76272  ? 608 SIA   A N5  1 
HETATM 4432 O O1A . SIA   M 8  .   ? 39.60728  44.81124 49.91098 1.000 105.88157 ? 608 SIA   A O1A 1 
HETATM 4433 O O1B . SIA   M 8  .   ? 39.14644  44.96886 52.17026 1.000 104.77747 ? 608 SIA   A O1B 1 
HETATM 4434 O O2  . SIA   M 8  .   ? 38.41921  47.38135 51.89399 1.000 97.51936  ? 608 SIA   A O2  1 
HETATM 4435 O O4  . SIA   M 8  .   ? 39.59715  50.22895 49.55851 1.000 100.02884 ? 608 SIA   A O4  1 
HETATM 4436 O O6  . SIA   M 8  .   ? 37.42114  46.64623 49.91172 1.000 101.71735 ? 608 SIA   A O6  1 
HETATM 4437 O O7  . SIA   M 8  .   ? 34.83064  48.54769 50.00619 1.000 83.80339  ? 608 SIA   A O7  1 
HETATM 4438 O O8  . SIA   M 8  .   ? 35.64744  45.15279 48.74257 1.000 83.97373  ? 608 SIA   A O8  1 
HETATM 4439 O O9  . SIA   M 8  .   ? 32.83623  46.74801 48.30241 1.000 74.14162  ? 608 SIA   A O9  1 
HETATM 4440 O O10 . SIA   M 8  .   ? 36.72488  49.99751 46.67672 1.000 94.84863  ? 608 SIA   A O10 1 
HETATM 4441 C C02 A A1H77 N 9  .   ? 19.61536  43.01075 40.63977 0.815 76.39018  ? 609 A1H77 A C02 1 
HETATM 4442 C C02 B A1H77 N 9  .   ? 19.90154  42.27426 42.33132 0.185 72.19430  ? 609 A1H77 A C02 1 
HETATM 4443 C C03 A A1H77 N 9  .   ? 19.43278  43.50828 42.14361 0.815 76.21697  ? 609 A1H77 A C03 1 
HETATM 4444 C C03 B A1H77 N 9  .   ? 20.52102  43.70136 42.05094 0.185 73.78473  ? 609 A1H77 A C03 1 
HETATM 4445 C C05 A A1H77 N 9  .   ? 18.10947  45.70217 42.21107 0.815 80.81446  ? 609 A1H77 A C05 1 
HETATM 4446 C C05 B A1H77 N 9  .   ? 18.83533  45.60023 42.07164 0.185 78.02353  ? 609 A1H77 A C05 1 
HETATM 4447 C C06 A A1H77 N 9  .   ? 17.47612  46.25838 40.88671 0.815 83.44424  ? 609 A1H77 A C06 1 
HETATM 4448 C C06 B A1H77 N 9  .   ? 18.11377  46.65500 41.22055 0.185 80.53501  ? 609 A1H77 A C06 1 
HETATM 4449 C C07 A A1H77 N 9  .   ? 17.72924  47.82706 40.53778 0.815 80.55842  ? 609 A1H77 A C07 1 
HETATM 4450 C C07 B A1H77 N 9  .   ? 16.98017  46.09734 40.21108 0.185 79.25360  ? 609 A1H77 A C07 1 
HETATM 4451 C C08 A A1H77 N 9  .   ? 18.50125  46.69009 39.71956 0.815 81.78703  ? 609 A1H77 A C08 1 
HETATM 4452 C C08 B A1H77 N 9  .   ? 18.37592  46.61331 39.63866 0.185 81.29219  ? 609 A1H77 A C08 1 
HETATM 4453 C C09 A A1H77 N 9  .   ? 20.06709  41.52119 40.56165 0.815 72.58195  ? 609 A1H77 A C09 1 
HETATM 4454 C C09 B A1H77 N 9  .   ? 19.99508  41.27098 41.09208 0.185 72.12045  ? 609 A1H77 A C09 1 
HETATM 4455 C C10 A A1H77 N 9  .   ? 21.62356  41.40148 40.06638 0.815 68.40722  ? 609 A1H77 A C10 1 
HETATM 4456 C C10 B A1H77 N 9  .   ? 21.50269  41.10137 40.58425 0.185 70.17687  ? 609 A1H77 A C10 1 
HETATM 4457 C C11 A A1H77 N 9  .   ? 22.55389  41.09226 41.29092 0.815 70.81920  ? 609 A1H77 A C11 1 
HETATM 4458 C C11 B A1H77 N 9  .   ? 22.57495  40.91729 41.69773 0.185 69.12972  ? 609 A1H77 A C11 1 
HETATM 4459 C C12 A A1H77 N 9  .   ? 22.73994  39.76220 41.77936 0.815 67.92136  ? 609 A1H77 A C12 1 
HETATM 4460 C C12 B A1H77 N 9  .   ? 22.58026  39.77863 42.55086 0.185 66.87529  ? 609 A1H77 A C12 1 
HETATM 4461 C C13 A A1H77 N 9  .   ? 23.54408  39.50230 42.93222 0.815 66.70444  ? 609 A1H77 A C13 1 
HETATM 4462 C C13 B A1H77 N 9  .   ? 23.56228  39.62799 43.57648 0.185 64.33485  ? 609 A1H77 A C13 1 
HETATM 4463 C C14 A A1H77 N 9  .   ? 24.16647  40.58018 43.62078 0.815 61.26892  ? 609 A1H77 A C14 1 
HETATM 4464 C C14 B A1H77 N 9  .   ? 24.55003  40.62722 43.75979 0.185 62.16723  ? 609 A1H77 A C14 1 
HETATM 4465 C C15 A A1H77 N 9  .   ? 23.96863  41.89047 43.15491 0.815 62.76633  ? 609 A1H77 A C15 1 
HETATM 4466 C C15 B A1H77 N 9  .   ? 24.54717  41.76174 42.91671 0.185 63.71369  ? 609 A1H77 A C15 1 
HETATM 4467 C C16 A A1H77 N 9  .   ? 23.16563  42.14712 42.00680 0.815 66.95436  ? 609 A1H77 A C16 1 
HETATM 4468 C C16 B A1H77 N 9  .   ? 23.56621  41.90487 41.89618 0.185 66.14896  ? 609 A1H77 A C16 1 
HETATM 4469 C C18 A A1H77 N 9  .   ? 17.48901  40.87172 39.66678 0.815 70.43232  ? 609 A1H77 A C18 1 
HETATM 4470 C C18 B A1H77 N 9  .   ? 17.79960  41.11934 39.64991 0.185 71.06900  ? 609 A1H77 A C18 1 
HETATM 4471 C C19 A A1H77 N 9  .   ? 16.80149  42.13972 39.07981 0.815 73.23109  ? 609 A1H77 A C19 1 
HETATM 4472 C C19 B A1H77 N 9  .   ? 16.83321  42.12805 39.01829 0.185 71.56762  ? 609 A1H77 A C19 1 
HETATM 4473 C C20 A A1H77 N 9  .   ? 17.18435  43.00956 38.01479 0.815 72.50463  ? 609 A1H77 A C20 1 
HETATM 4474 C C20 B A1H77 N 9  .   ? 17.02263  43.02669 37.92366 0.185 72.29549  ? 609 A1H77 A C20 1 
HETATM 4475 C C21 A A1H77 N 9  .   ? 16.32928  44.06787 37.59614 0.815 72.24316  ? 609 A1H77 A C21 1 
HETATM 4476 C C21 B A1H77 N 9  .   ? 15.98196  43.88822 37.48966 0.185 72.01048  ? 609 A1H77 A C21 1 
HETATM 4477 C C22 A A1H77 N 9  .   ? 15.04634  44.22960 38.23210 0.815 74.89926  ? 609 A1H77 A C22 1 
HETATM 4478 C C22 B A1H77 N 9  .   ? 14.72151  43.84566 38.17240 0.185 72.79116  ? 609 A1H77 A C22 1 
HETATM 4479 C C23 A A1H77 N 9  .   ? 14.64741  43.33245 39.28020 0.815 72.37372  ? 609 A1H77 A C23 1 
HETATM 4480 C C23 B A1H77 N 9  .   ? 14.53926  42.94116 39.27214 0.185 71.77665  ? 609 A1H77 A C23 1 
HETATM 4481 C C24 A A1H77 N 9  .   ? 15.48941  42.27384 39.72088 0.815 72.63561  ? 609 A1H77 A C24 1 
HETATM 4482 C C24 B A1H77 N 9  .   ? 15.57648  42.07107 39.72116 0.185 72.44620  ? 609 A1H77 A C24 1 
HETATM 4483 C C25 A A1H77 N 9  .   ? 15.30366  41.19227 40.80692 0.815 71.75195  ? 609 A1H77 A C25 1 
HETATM 4484 C C25 B A1H77 N 9  .   ? 15.67030  41.01759 40.84753 0.185 71.45954  ? 609 A1H77 A C25 1 
HETATM 4485 C C26 A A1H77 N 9  .   ? 16.50517  40.36825 40.86540 0.815 70.48074  ? 609 A1H77 A C26 1 
HETATM 4486 C C26 B A1H77 N 9  .   ? 16.99065  40.44158 40.83950 0.185 70.48387  ? 609 A1H77 A C26 1 
HETATM 4487 C C27 A A1H77 N 9  .   ? 16.54942  39.25804 41.78517 0.815 72.71204  ? 609 A1H77 A C27 1 
HETATM 4488 C C27 B A1H77 N 9  .   ? 17.33214  39.41534 41.78996 0.185 70.57584  ? 609 A1H77 A C27 1 
HETATM 4489 C C28 A A1H77 N 9  .   ? 15.45634  38.98319 42.68871 0.815 68.50236  ? 609 A1H77 A C28 1 
HETATM 4490 C C28 B A1H77 N 9  .   ? 16.39728  38.96181 42.76888 0.185 68.65386  ? 609 A1H77 A C28 1 
HETATM 4491 C C29 A A1H77 N 9  .   ? 14.27431  39.82194 42.65912 0.815 69.44352  ? 609 A1H77 A C29 1 
HETATM 4492 C C29 B A1H77 N 9  .   ? 15.08548  39.53715 42.78964 0.185 69.04188  ? 609 A1H77 A C29 1 
HETATM 4493 C C30 A A1H77 N 9  .   ? 14.21817  40.90976 41.71860 0.815 69.75514  ? 609 A1H77 A C30 1 
HETATM 4494 C C30 B A1H77 N 9  .   ? 14.74275  40.55232 41.83148 0.185 70.46080  ? 609 A1H77 A C30 1 
HETATM 4495 N N04 A A1H77 N 9  .   ? 18.06107  44.14537 42.30438 0.815 77.39507  ? 609 A1H77 A N04 1 
HETATM 4496 N N04 B A1H77 N 9  .   ? 19.58649  44.58410 41.22801 0.185 75.76127  ? 609 A1H77 A N04 1 
HETATM 4497 N N17 A A1H77 N 9  .   ? 19.12140  40.72596 39.65819 0.815 78.27917  ? 609 A1H77 A N17 1 
HETATM 4498 N N17 B A1H77 N 9  .   ? 19.12848  41.82850 39.99085 0.185 73.52061  ? 609 A1H77 A N17 1 
HETATM 4499 O O01 A A1H77 N 9  .   ? 20.69376  43.73867 39.96991 0.815 78.62552  ? 609 A1H77 A O01 1 
HETATM 4500 O O01 B A1H77 N 9  .   ? 18.47514  42.43020 42.50917 0.185 72.58621  ? 609 A1H77 A O01 1 
HETATM 4501 O O   . HOH   O 10 .   ? 22.13235  49.08513 62.56950 1.000 74.48357  ? 701 HOH   A O   1 
HETATM 4502 O O   . HOH   O 10 .   ? 10.56282  26.46824 58.26069 1.000 66.98318  ? 702 HOH   A O   1 
HETATM 4503 O O   . HOH   O 10 .   ? 24.44282  32.26692 25.73359 1.000 66.95105  ? 703 HOH   A O   1 
HETATM 4504 O O   . HOH   O 10 .   ? 5.50567   13.71179 57.58002 1.000 83.52484  ? 704 HOH   A O   1 
HETATM 4505 O O   . HOH   O 10 .   ? 27.58492  32.30690 18.36721 1.000 70.69222  ? 705 HOH   A O   1 
HETATM 4506 O O   . HOH   O 10 .   ? 21.16653  32.22810 45.20307 1.000 50.82027  ? 706 HOH   A O   1 
HETATM 4507 O O   . HOH   O 10 .   ? 21.77850  38.74578 49.47286 1.000 50.89144  ? 707 HOH   A O   1 
HETATM 4508 O O   . HOH   O 10 .   ? -0.55450  22.24544 36.70810 1.000 61.38725  ? 708 HOH   A O   1 
HETATM 4509 O O   . HOH   O 10 .   ? 29.63229  32.41723 48.96086 1.000 58.81886  ? 709 HOH   A O   1 
HETATM 4510 O O   . HOH   O 10 .   ? 17.20653  34.78066 18.08515 1.000 58.99619  ? 710 HOH   A O   1 
HETATM 4511 O O   . HOH   O 10 .   ? 24.90238  31.33931 23.39364 1.000 57.67179  ? 711 HOH   A O   1 
HETATM 4512 O O   . HOH   O 10 .   ? 42.81664  23.77136 35.54704 1.000 81.07764  ? 712 HOH   A O   1 
HETATM 4513 O O   . HOH   O 10 .   ? 44.25783  20.07165 38.71360 1.000 94.84689  ? 713 HOH   A O   1 
HETATM 4514 O O   . HOH   O 10 .   ? 30.40568  23.70231 34.93570 1.000 54.96124  ? 714 HOH   A O   1 
HETATM 4515 O O   . HOH   O 10 .   ? 28.21157  30.73492 30.64629 1.000 59.29583  ? 715 HOH   A O   1 
HETATM 4516 O O   . HOH   O 10 .   ? -1.46401  37.11187 36.57222 1.000 66.11664  ? 716 HOH   A O   1 
HETATM 4517 O O   . HOH   O 10 .   ? 20.63136  29.08043 47.05241 1.000 54.81762  ? 717 HOH   A O   1 
HETATM 4518 O O   . HOH   O 10 .   ? 9.57467   44.17676 10.42063 1.000 91.46550  ? 718 HOH   A O   1 
HETATM 4519 O O   . HOH   O 10 .   ? 17.67522  13.70259 35.25186 1.000 52.88819  ? 719 HOH   A O   1 
HETATM 4520 O O   . HOH   O 10 .   ? 21.35435  43.32957 32.49095 1.000 56.49687  ? 720 HOH   A O   1 
HETATM 4521 O O   . HOH   O 10 .   ? 25.715    41.221   75.606   1.000 77.04140  ? 721 HOH   A O   1 
HETATM 4522 O O   . HOH   O 10 .   ? -4.71804  20.42361 36.91477 1.000 65.26485  ? 722 HOH   A O   1 
HETATM 4523 O O   . HOH   O 10 .   ? 14.44171  40.84181 26.64367 1.000 63.52219  ? 723 HOH   A O   1 
HETATM 4524 O O   . HOH   O 10 .   ? 4.65708   15.21064 45.78760 1.000 64.33451  ? 724 HOH   A O   1 
HETATM 4525 O O   . HOH   O 10 .   ? 11.77964  40.54640 20.42228 1.000 61.56616  ? 725 HOH   A O   1 
HETATM 4526 O O   . HOH   O 10 .   ? 17.34301  32.29129 17.07054 1.000 56.97131  ? 726 HOH   A O   1 
HETATM 4527 O O   . HOH   O 10 .   ? 17.75044  44.06390 18.52475 1.000 70.54544  ? 727 HOH   A O   1 
HETATM 4528 O O   . HOH   O 10 .   ? 16.78926  25.11144 62.26247 1.000 58.57672  ? 728 HOH   A O   1 
HETATM 4529 O O   . HOH   O 10 .   ? 32.84309  27.62586 28.23969 1.000 67.31856  ? 729 HOH   A O   1 
HETATM 4530 O O   . HOH   O 10 .   ? 31.05130  17.71990 58.38067 1.000 88.58470  ? 730 HOH   A O   1 
HETATM 4531 O O   . HOH   O 10 .   ? 16.30253  36.82725 39.84865 1.000 62.29337  ? 731 HOH   A O   1 
HETATM 4532 O O   . HOH   O 10 .   ? 25.52898  28.65916 30.78644 1.000 53.59424  ? 732 HOH   A O   1 
HETATM 4533 O O   . HOH   O 10 .   ? 17.08978  35.83582 56.44866 1.000 57.99837  ? 733 HOH   A O   1 
HETATM 4534 O O   . HOH   O 10 .   ? 26.88210  51.10617 48.64457 1.000 66.87054  ? 734 HOH   A O   1 
HETATM 4535 O O   . HOH   O 10 .   ? 35.70255  47.58188 46.04188 1.000 78.53764  ? 735 HOH   A O   1 
HETATM 4536 O O   . HOH   O 10 .   ? 14.42806  18.59651 27.41762 1.000 61.67138  ? 736 HOH   A O   1 
HETATM 4537 O O   . HOH   O 10 .   ? 19.47766  29.87121 31.07847 1.000 52.85542  ? 737 HOH   A O   1 
HETATM 4538 O O   . HOH   O 10 .   ? 24.82590  53.58713 58.45223 1.000 69.87896  ? 738 HOH   A O   1 
HETATM 4539 O O   . HOH   O 10 .   ? 8.19426   35.59471 18.30691 1.000 62.12159  ? 739 HOH   A O   1 
HETATM 4540 O O   . HOH   O 10 .   ? 10.01252  33.58738 16.83350 1.000 67.54190  ? 740 HOH   A O   1 
HETATM 4541 O O   . HOH   O 10 .   ? 12.23606  15.61144 56.97543 1.000 58.68480  ? 741 HOH   A O   1 
HETATM 4542 O O   . HOH   O 10 .   ? 12.60584  44.16055 27.21427 1.000 57.17247  ? 742 HOH   A O   1 
HETATM 4543 O O   . HOH   O 10 .   ? 3.75258   37.71609 31.21743 1.000 58.12913  ? 743 HOH   A O   1 
HETATM 4544 O O   . HOH   O 10 .   ? 20.71183  32.90557 38.00889 1.000 52.22662  ? 744 HOH   A O   1 
HETATM 4545 O O   . HOH   O 10 .   ? 9.51813   39.95232 21.86840 1.000 64.54550  ? 745 HOH   A O   1 
HETATM 4546 O O   . HOH   O 10 .   ? 20.77492  49.06624 38.94374 1.000 71.19344  ? 746 HOH   A O   1 
HETATM 4547 O O   . HOH   O 10 .   ? 21.71538  35.88520 34.90177 1.000 52.09754  ? 747 HOH   A O   1 
HETATM 4548 O O   . HOH   O 10 .   ? 15.50152  36.67581 34.53131 1.000 54.33251  ? 748 HOH   A O   1 
HETATM 4549 O O   . HOH   O 10 .   ? 22.54378  38.35156 35.55320 1.000 50.75714  ? 749 HOH   A O   1 
HETATM 4550 O O   . HOH   O 10 .   ? 20.65554  50.15701 31.04714 1.000 72.22575  ? 750 HOH   A O   1 
HETATM 4551 O O   . HOH   O 10 .   ? 2.39567   43.57884 30.81045 1.000 70.23131  ? 751 HOH   A O   1 
HETATM 4552 O O   . HOH   O 10 .   ? 28.24585  32.63017 42.45026 1.000 57.36421  ? 752 HOH   A O   1 
HETATM 4553 O O   . HOH   O 10 .   ? 11.60689  31.33212 46.79983 1.000 56.11793  ? 753 HOH   A O   1 
HETATM 4554 O O   . HOH   O 10 .   ? 16.02247  17.82902 53.25128 1.000 53.37152  ? 754 HOH   A O   1 
HETATM 4555 O O   . HOH   O 10 .   ? 3.00027   13.96684 37.30074 1.000 54.86377  ? 755 HOH   A O   1 
HETATM 4556 O O   . HOH   O 10 .   ? 20.13434  27.22586 60.49945 1.000 67.30466  ? 756 HOH   A O   1 
HETATM 4557 O O   . HOH   O 10 .   ? 24.77010  35.00036 25.37903 1.000 60.85586  ? 757 HOH   A O   1 
HETATM 4558 O O   . HOH   O 10 .   ? 28.30223  9.42263  45.40626 1.000 63.72913  ? 758 HOH   A O   1 
HETATM 4559 O O   . HOH   O 10 .   ? 14.07705  39.59872 21.87845 1.000 59.65595  ? 759 HOH   A O   1 
HETATM 4560 O O   . HOH   O 10 .   ? 12.81425  19.33474 65.75490 1.000 56.90093  ? 760 HOH   A O   1 
HETATM 4561 O O   . HOH   O 10 .   ? 6.10774   32.72679 52.43307 1.000 63.44906  ? 761 HOH   A O   1 
HETATM 4562 O O   . HOH   O 10 .   ? 11.41893  44.18980 16.14430 1.000 73.91630  ? 762 HOH   A O   1 
HETATM 4563 O O   . HOH   O 10 .   ? 16.37560  49.64915 70.15999 1.000 76.27094  ? 763 HOH   A O   1 
HETATM 4564 O O   . HOH   O 10 .   ? 25.76115  11.38402 51.51947 1.000 65.29010  ? 764 HOH   A O   1 
HETATM 4565 O O   . HOH   O 10 .   ? 3.57773   30.36983 50.30608 1.000 71.20461  ? 765 HOH   A O   1 
HETATM 4566 O O   . HOH   O 10 .   ? 15.23844  41.06175 23.71580 1.000 59.62648  ? 766 HOH   A O   1 
HETATM 4567 O O   . HOH   O 10 .   ? 20.06977  36.77686 27.30763 1.000 55.82467  ? 767 HOH   A O   1 
HETATM 4568 O O   . HOH   O 10 .   ? 3.86199   41.02696 33.06018 1.000 65.20822  ? 768 HOH   A O   1 
HETATM 4569 O O   . HOH   O 10 .   ? 24.26835  35.99172 17.96100 1.000 61.89191  ? 769 HOH   A O   1 
HETATM 4570 O O   . HOH   O 10 .   ? 36.03481  45.54781 41.37644 1.000 70.53592  ? 770 HOH   A O   1 
HETATM 4571 O O   . HOH   O 10 .   ? 20.39127  38.00900 56.14179 1.000 60.07498  ? 771 HOH   A O   1 
HETATM 4572 O O   . HOH   O 10 .   ? 1.74195   32.51702 52.51158 1.000 78.78793  ? 772 HOH   A O   1 
HETATM 4573 O O   . HOH   O 10 .   ? 11.36131  35.50540 65.06561 1.000 79.23820  ? 773 HOH   A O   1 
HETATM 4574 O O   . HOH   O 10 .   ? 18.56736  37.36174 54.71535 1.000 56.76393  ? 774 HOH   A O   1 
HETATM 4575 O O   . HOH   O 10 .   ? 27.28966  38.36020 20.70286 1.000 65.24853  ? 775 HOH   A O   1 
HETATM 4576 O O   . HOH   O 10 .   ? 35.58425  42.20458 50.06982 1.000 70.02757  ? 776 HOH   A O   1 
HETATM 4577 O O   . HOH   O 10 .   ? 32.35497  35.73810 42.88659 1.000 72.35261  ? 777 HOH   A O   1 
HETATM 4578 O O   . HOH   O 10 .   ? 3.48993   14.80226 33.98225 1.000 62.71499  ? 778 HOH   A O   1 
HETATM 4579 O O   . HOH   O 10 .   ? -2.13425  53.29890 56.64979 1.000 66.98398  ? 779 HOH   A O   1 
HETATM 4580 O O   . HOH   O 10 .   ? 3.15419   35.18196 64.43251 1.000 66.52084  ? 780 HOH   A O   1 
HETATM 4581 O O   . HOH   O 10 .   ? -4.33113  36.93664 38.16049 1.000 83.95467  ? 781 HOH   A O   1 
HETATM 4582 O O   . HOH   O 10 .   ? 6.01249   23.38214 62.34124 1.000 69.82887  ? 782 HOH   A O   1 
HETATM 4583 O O   . HOH   O 10 .   ? 15.22285  9.82763  54.78553 1.000 66.58689  ? 783 HOH   A O   1 
HETATM 4584 O O   . HOH   O 10 .   ? 33.22885  37.36330 31.82803 1.000 83.47699  ? 784 HOH   A O   1 
HETATM 4585 O O   . HOH   O 10 .   ? 18.69699  46.36836 36.13124 1.000 71.39307  ? 785 HOH   A O   1 
HETATM 4586 O O   . HOH   O 10 .   ? 33.11558  35.72945 39.46825 1.000 74.16749  ? 786 HOH   A O   1 
HETATM 4587 O O   . HOH   O 10 .   ? 21.73482  37.25173 40.81252 1.000 68.38037  ? 787 HOH   A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . ILE A 4   ? 1.08799 1.04876 0.94244 -0.00655 0.29364  -0.07424 4   ILE A N   
2    C CA  . ILE A 4   ? 1.31651 1.24333 1.14819 -0.00336 0.27951  -0.07857 4   ILE A CA  
3    C C   . ILE A 4   ? 1.25624 1.16198 1.05665 -0.02019 0.26276  -0.07063 4   ILE A C   
4    O O   . ILE A 4   ? 1.17690 1.09345 0.99106 -0.02860 0.25010  -0.05864 4   ILE A O   
5    C CB  . ILE A 4   ? 1.34252 1.27405 1.20774 0.00974  0.26680  -0.07723 4   ILE A CB  
6    C CG1 . ILE A 4   ? 1.39850 1.36069 1.30289 0.02586  0.28075  -0.08110 4   ILE A CG1 
7    C CG2 . ILE A 4   ? 1.32132 1.21662 1.16346 0.01508  0.25807  -0.08466 4   ILE A CG2 
8    C CD1 . ILE A 4   ? 1.24576 1.20733 1.17629 0.04260  0.27141  -0.08202 4   ILE A CD1 
9    N N   . ILE A 5   ? 1.21122 1.08678 0.96951 -0.02456 0.26242  -0.07786 5   ILE A N   
10   C CA  . ILE A 5   ? 1.13390 0.99009 0.85956 -0.03975 0.24680  -0.07138 5   ILE A CA  
11   C C   . ILE A 5   ? 1.20879 1.04002 0.92477 -0.03800 0.22984  -0.07561 5   ILE A C   
12   O O   . ILE A 5   ? 1.25673 1.07172 0.96615 -0.02853 0.23591  -0.08791 5   ILE A O   
13   C CB  . ILE A 5   ? 1.11259 0.95568 0.79374 -0.04899 0.25914  -0.07571 5   ILE A CB  
14   C CG1 . ILE A 5   ? 1.17882 1.04316 0.86467 -0.05792 0.26821  -0.06510 5   ILE A CG1 
15   C CG2 . ILE A 5   ? 1.11673 0.93184 0.75719 -0.06033 0.24251  -0.07500 5   ILE A CG2 
16   C CD1 . ILE A 5   ? 1.24739 1.10781 0.90112 -0.06162 0.29010  -0.07185 5   ILE A CD1 
17   N N   . ILE A 6   ? 1.06508 0.89285 0.78076 -0.04714 0.20919  -0.06554 6   ILE A N   
18   C CA  . ILE A 6   ? 1.13780 0.94545 0.84739 -0.04790 0.19224  -0.06807 6   ILE A CA  
19   C C   . ILE A 6   ? 1.15911 0.95139 0.83342 -0.06275 0.17851  -0.06446 6   ILE A C   
20   O O   . ILE A 6   ? 1.19498 0.99837 0.86950 -0.07091 0.17123  -0.05239 6   ILE A O   
21   C CB  . ILE A 6   ? 1.12288 0.94451 0.87154 -0.04329 0.17893  -0.05937 6   ILE A CB  
22   C CG1 . ILE A 6   ? 1.08464 0.92141 0.86715 -0.02767 0.19046  -0.06290 6   ILE A CG1 
23   C CG2 . ILE A 6   ? 1.06656 0.86817 0.80708 -0.04694 0.16160  -0.06075 6   ILE A CG2 
24   C CD1 . ILE A 6   ? 1.04459 0.86081 0.82403 -0.01708 0.19292  -0.07384 6   ILE A CD1 
25   N N   . ALA A 7   ? 1.16519 0.93159 0.80945 -0.06615 0.17440  -0.07484 7   ALA A N   
26   C CA  . ALA A 7   ? 1.14558 0.89854 0.75815 -0.08008 0.15821  -0.07221 7   ALA A CA  
27   C C   . ALA A 7   ? 1.17256 0.93006 0.80694 -0.08333 0.13664  -0.06371 7   ALA A C   
28   O O   . ALA A 7   ? 1.17313 0.92428 0.82463 -0.07803 0.13299  -0.06836 7   ALA A O   
29   C CB  . ALA A 7   ? 1.10000 0.82401 0.67294 -0.08377 0.16115  -0.08786 7   ALA A CB  
30   N N   . THR A 8   ? 1.21283 0.98082 0.84656 -0.09153 0.12307  -0.05095 8   THR A N   
31   C CA  . THR A 8   ? 1.17885 0.95161 0.82920 -0.09566 0.10237  -0.04323 8   THR A CA  
32   C C   . THR A 8   ? 1.25086 1.01071 0.86754 -0.10799 0.08717  -0.04445 8   THR A C   
33   O O   . THR A 8   ? 1.27049 1.01642 0.84955 -0.11330 0.09246  -0.05133 8   THR A O   
34   C CB  . THR A 8   ? 1.14424 0.93955 0.82318 -0.09409 0.09723  -0.02789 8   THR A CB  
35   O OG1 . THR A 8   ? 1.15762 0.95411 0.81437 -0.10241 0.09022  -0.01871 8   THR A OG1 
36   C CG2 . THR A 8   ? 1.07563 0.88495 0.77862 -0.08469 0.11455  -0.02722 8   THR A CG2 
37   N N   . LYS A 9   ? 1.19035 0.95643 0.82080 -0.11269 0.06799  -0.03785 9   LYS A N   
38   C CA  . LYS A 9   ? 1.25472 1.01208 0.85732 -0.12452 0.05154  -0.03940 9   LYS A CA  
39   C C   . LYS A 9   ? 1.30653 1.06763 0.88289 -0.13008 0.04688  -0.03033 9   LYS A C   
40   O O   . LYS A 9   ? 1.36188 1.11260 0.90416 -0.13958 0.03726  -0.03410 9   LYS A O   
41   C CB  . LYS A 9   ? 1.25923 1.02610 0.88690 -0.12787 0.03300  -0.03446 9   LYS A CB  
42   C CG  . LYS A 9   ? 1.30259 1.05810 0.94354 -0.12638 0.03566  -0.04512 9   LYS A CG  
43   C CD  . LYS A 9   ? 1.33992 1.09710 0.98707 -0.13620 0.01686  -0.04515 9   LYS A CD  
44   C CE  . LYS A 9   ? 1.38436 1.12433 1.03816 -0.13647 0.02117  -0.05631 9   LYS A CE  
45   N NZ  . LYS A 9   ? 1.46528 1.18028 1.09380 -0.13270 0.03804  -0.07014 9   LYS A NZ  
46   N N   . ASN A 10  ? 1.29856 1.07257 0.88766 -0.12495 0.05374  -0.01874 10  ASN A N   
47   C CA  . ASN A 10  ? 1.37980 1.15451 0.94295 -0.12974 0.05086  -0.00848 10  ASN A CA  
48   C C   . ASN A 10  ? 1.36910 1.13884 0.91365 -0.12794 0.07253  -0.01023 10  ASN A C   
49   O O   . ASN A 10  ? 1.40468 1.17361 0.92700 -0.13204 0.07250  -0.00051 10  ASN A O   
50   C CB  . ASN A 10  ? 1.41647 1.20783 1.00564 -0.12725 0.03961  0.00856  10  ASN A CB  
51   C CG  . ASN A 10  ? 1.38886 1.18921 1.00089 -0.12805 0.01992  0.01104  10  ASN A CG  
52   O OD1 . ASN A 10  ? 1.32613 1.13109 0.96709 -0.12397 0.02133  0.00571  10  ASN A OD1 
53   N ND2 . ASN A 10  ? 1.48629 1.28990 1.08527 -0.13321 0.00144  0.01944  10  ASN A ND2 
54   N N   . GLY A 11  ? 1.31812 1.08527 0.87179 -0.12167 0.09116  -0.02141 11  GLY A N   
55   C CA  . GLY A 11  ? 1.32601 1.09065 0.86223 -0.12037 0.11287  -0.02437 11  GLY A CA  
56   C C   . GLY A 11  ? 1.26924 1.04458 0.83927 -0.10974 0.13108  -0.02978 11  GLY A C   
57   O O   . GLY A 11  ? 1.21944 1.00401 0.82599 -0.10316 0.12630  -0.02941 11  GLY A O   
58   N N   . LYS A 12  ? 1.23830 1.01348 0.79507 -0.10809 0.15242  -0.03462 12  LYS A N   
59   C CA  . LYS A 12  ? 1.25512 1.04415 0.84386 -0.09763 0.17088  -0.03958 12  LYS A CA  
60   C C   . LYS A 12  ? 1.20208 1.01378 0.82511 -0.09656 0.17185  -0.02590 12  LYS A C   
61   O O   . LYS A 12  ? 1.21880 1.03273 0.83002 -0.10432 0.16945  -0.01405 12  LYS A O   
62   C CB  . LYS A 12  ? 1.32899 1.11275 0.89356 -0.09608 0.19466  -0.05025 12  LYS A CB  
63   C CG  . LYS A 12  ? 1.32269 1.08032 0.84206 -0.09985 0.19548  -0.06395 12  LYS A CG  
64   C CD  . LYS A 12  ? 1.39484 1.14942 0.90279 -0.09306 0.22223  -0.07790 12  LYS A CD  
65   C CE  . LYS A 12  ? 1.37830 1.10958 0.87005 -0.08754 0.22523  -0.09649 12  LYS A CE  
66   N NZ  . LYS A 12  ? 1.42426 1.13037 0.85923 -0.09755 0.22544  -0.10547 12  LYS A NZ  
67   N N   . VAL A 13  ? 1.14449 0.97143 0.80880 -0.08705 0.17496  -0.02756 13  VAL A N   
68   C CA  . VAL A 13  ? 1.14244 0.99188 0.84152 -0.08560 0.17806  -0.01767 13  VAL A CA  
69   C C   . VAL A 13  ? 1.11714 0.98270 0.83898 -0.07661 0.19861  -0.02569 13  VAL A C   
70   O O   . VAL A 13  ? 1.14663 1.00794 0.87335 -0.06700 0.20397  -0.03731 13  VAL A O   
71   C CB  . VAL A 13  ? 1.08396 0.94060 0.81437 -0.08291 0.15975  -0.01072 13  VAL A CB  
72   C CG1 . VAL A 13  ? 1.05413 0.89771 0.76463 -0.09067 0.13954  -0.00320 13  VAL A CG1 
73   C CG2 . VAL A 13  ? 1.02554 0.88257 0.77717 -0.07238 0.15864  -0.02013 13  VAL A CG2 
74   N N   . ARG A 14  ? 1.13605 1.01992 0.87180 -0.07983 0.21025  -0.01939 14  ARG A N   
75   C CA  . ARG A 14  ? 1.09848 1.00429 0.86091 -0.07229 0.22952  -0.02554 14  ARG A CA  
76   C C   . ARG A 14  ? 1.02797 0.95698 0.83655 -0.06808 0.22323  -0.01977 14  ARG A C   
77   O O   . ARG A 14  ? 0.99876 0.93202 0.81530 -0.07607 0.21383  -0.00849 14  ARG A O   
78   C CB  . ARG A 14  ? 1.10450 1.01740 0.85125 -0.08058 0.24874  -0.02338 14  ARG A CB  
79   C CG  . ARG A 14  ? 1.12589 1.06880 0.90702 -0.07518 0.26816  -0.02725 14  ARG A CG  
80   C CD  . ARG A 14  ? 1.22170 1.17064 0.98457 -0.08584 0.28801  -0.02444 14  ARG A CD  
81   N NE  . ARG A 14  ? 1.31843 1.25432 1.04772 -0.08298 0.30344  -0.03572 14  ARG A NE  
82   C CZ  . ARG A 14  ? 1.33550 1.24820 1.01651 -0.09265 0.30504  -0.03401 14  ARG A CZ  
83   N NH1 . ARG A 14  ? 1.31015 1.21113 0.97122 -0.10542 0.29310  -0.02021 14  ARG A NH1 
84   N NH2 . ARG A 14  ? 1.39506 1.29507 1.04586 -0.08881 0.31869  -0.04651 14  ARG A NH2 
85   N N   . GLY A 15  ? 1.00039 0.94326 0.83792 -0.05513 0.22833  -0.02763 15  GLY A N   
86   C CA  . GLY A 15  ? 0.92486 0.89132 0.80514 -0.05017 0.22291  -0.02357 15  GLY A CA  
87   C C   . GLY A 15  ? 1.02059 1.01778 0.92813 -0.04856 0.24051  -0.02519 15  GLY A C   
88   O O   . GLY A 15  ? 0.98399 0.98546 0.87819 -0.05248 0.25835  -0.02833 15  GLY A O   
89   N N   . MET A 16  ? 0.98017 1.00048 0.92682 -0.04330 0.23516  -0.02301 16  MET A N   
90   C CA  . MET A 16  ? 0.98924 1.04399 0.96928 -0.04098 0.24884  -0.02490 16  MET A CA  
91   C C   . MET A 16  ? 0.97473 1.04604 0.98873 -0.02463 0.24349  -0.02944 16  MET A C   
92   O O   . MET A 16  ? 1.00893 1.06629 1.02331 -0.01895 0.22724  -0.02792 16  MET A O   
93   C CB  . MET A 16  ? 0.96285 1.03239 0.95652 -0.05593 0.24664  -0.01513 16  MET A CB  
94   C CG  . MET A 16  ? 0.93836 1.01543 0.95781 -0.05502 0.22850  -0.00983 16  MET A CG  
95   S SD  . MET A 16  ? 1.14218 1.21864 1.16157 -0.07418 0.22266  0.00175  16  MET A SD  
96   C CE  . MET A 16  ? 1.09208 1.21192 1.15534 -0.07740 0.23418  -0.00043 16  MET A CE  
97   N N   . GLN A 17  ? 0.93326 1.03535 0.97608 -0.01690 0.25728  -0.03455 17  GLN A N   
98   C CA  . GLN A 17  ? 0.94290 1.06198 1.01707 0.00100  0.25373  -0.03891 17  GLN A CA  
99   C C   . GLN A 17  ? 0.88797 1.04263 1.00251 -0.00172 0.24798  -0.03397 17  GLN A C   
100  O O   . GLN A 17  ? 0.86986 1.05126 1.00066 -0.01077 0.25938  -0.03326 17  GLN A O   
101  C CB  . GLN A 17  ? 0.99336 1.12173 1.07202 0.01560  0.27269  -0.04944 17  GLN A CB  
102  C CG  . GLN A 17  ? 1.13820 1.23101 1.18842 0.02734  0.27156  -0.05645 17  GLN A CG  
103  C CD  . GLN A 17  ? 1.29661 1.39621 1.35060 0.04315  0.29142  -0.06778 17  GLN A CD  
104  O OE1 . GLN A 17  ? 1.27821 1.41386 1.36180 0.04762  0.30516  -0.07008 17  GLN A OE1 
105  N NE2 . GLN A 17  ? 1.38397 1.44915 1.40840 0.05147  0.29346  -0.07549 17  GLN A NE2 
106  N N   . LEU A 18  ? 0.83359 0.98846 0.96328 0.00527  0.23063  -0.03087 18  LEU A N   
107  C CA  . LEU A 18  ? 0.79929 0.98561 0.96457 0.00291  0.22239  -0.02681 18  LEU A CA  
108  C C   . LEU A 18  ? 0.82275 1.03571 1.02054 0.02237  0.22327  -0.03137 18  LEU A C   
109  O O   . LEU A 18  ? 0.86851 1.06533 1.05848 0.03877  0.22282  -0.03525 18  LEU A O   
110  C CB  . LEU A 18  ? 0.77874 0.94802 0.93740 -0.00337 0.20194  -0.01966 18  LEU A CB  
111  C CG  . LEU A 18  ? 0.93436 1.07292 1.05960 -0.01894 0.19760  -0.01433 18  LEU A CG  
112  C CD1 . LEU A 18  ? 0.80689 0.93580 0.93293 -0.02462 0.17874  -0.00758 18  LEU A CD1 
113  C CD2 . LEU A 18  ? 0.88559 1.03233 1.00538 -0.03478 0.21115  -0.01259 18  LEU A CD2 
114  N N   . THR A 19  ? 0.74947 1.00308 0.98379 0.02040  0.22431  -0.03080 19  THR A N   
115  C CA  . THR A 19  ? 0.77286 1.05686 1.04223 0.03853  0.22116  -0.03330 19  THR A CA  
116  C C   . THR A 19  ? 0.76414 1.05219 1.04580 0.03783  0.19967  -0.02734 19  THR A C   
117  O O   . THR A 19  ? 0.77126 1.07420 1.06359 0.02196  0.19378  -0.02386 19  THR A O   
118  C CB  . THR A 19  ? 0.78718 1.11853 1.09180 0.03716  0.23552  -0.03710 19  THR A CB  
119  O OG1 . THR A 19  ? 0.93085 1.25645 1.21815 0.02814  0.25579  -0.04071 19  THR A OG1 
120  C CG2 . THR A 19  ? 0.75708 1.11556 1.09231 0.06134  0.23776  -0.04154 19  THR A CG2 
121  N N   . VAL A 20  ? 0.78579 1.05819 1.06358 0.05434  0.18863  -0.02629 20  VAL A N   
122  C CA  . VAL A 20  ? 0.79977 1.07238 1.08459 0.05545  0.16866  -0.02058 20  VAL A CA  
123  C C   . VAL A 20  ? 0.80098 1.08934 1.10734 0.07841  0.16353  -0.02103 20  VAL A C   
124  O O   . VAL A 20  ? 0.83096 1.09486 1.12296 0.09406  0.16613  -0.02263 20  VAL A O   
125  C CB  . VAL A 20  ? 0.80502 1.03369 1.05537 0.05008  0.15781  -0.01632 20  VAL A CB  
126  C CG1 . VAL A 20  ? 0.71885 0.95217 0.97639 0.04468  0.13980  -0.01060 20  VAL A CG1 
127  C CG2 . VAL A 20  ? 0.69155 0.89677 0.91395 0.03330  0.16544  -0.01648 20  VAL A CG2 
128  N N   . PHE A 21  ? 0.81392 1.14136 1.15332 0.08025  0.15548  -0.01944 21  PHE A N   
129  C CA  . PHE A 21  ? 0.73432 1.08034 1.09600 0.10206  0.14717  -0.01801 21  PHE A CA  
130  C C   . PHE A 21  ? 0.68873 1.03334 1.05460 0.12319  0.16124  -0.02294 21  PHE A C   
131  O O   . PHE A 21  ? 0.72033 1.03346 1.06829 0.13859  0.15899  -0.02193 21  PHE A O   
132  C CB  . PHE A 21  ? 0.74569 1.06220 1.08830 0.10771  0.12965  -0.01156 21  PHE A CB  
133  C CG  . PHE A 21  ? 0.71450 1.02669 1.04877 0.08873  0.11654  -0.00738 21  PHE A CG  
134  C CD1 . PHE A 21  ? 0.76737 1.11393 1.12378 0.07412  0.11383  -0.00832 21  PHE A CD1 
135  C CD2 . PHE A 21  ? 0.78489 1.05842 1.08963 0.08561  0.10720  -0.00293 21  PHE A CD2 
136  C CE1 . PHE A 21  ? 0.73183 1.07115 1.07894 0.05743  0.10229  -0.00539 21  PHE A CE1 
137  C CE2 . PHE A 21  ? 0.80399 1.07323 1.10120 0.06953  0.09612  0.00033  21  PHE A CE2 
138  C CZ  . PHE A 21  ? 0.73812 1.03928 1.05596 0.05602  0.09377  -0.00116 21  PHE A CZ  
139  N N   . GLY A 22  ? 0.76316 1.14153 1.15263 0.12310  0.17673  -0.02864 22  GLY A N   
140  C CA  . GLY A 22  ? 0.70065 1.08032 1.09553 0.14298  0.19282  -0.03473 22  GLY A CA  
141  C C   . GLY A 22  ? 0.77177 1.09755 1.12623 0.14929  0.19915  -0.03721 22  GLY A C   
142  O O   . GLY A 22  ? 0.86324 1.17728 1.21722 0.17158  0.20434  -0.04016 22  GLY A O   
143  N N   . GLY A 23  ? 0.79744 1.08954 1.11779 0.12986  0.19794  -0.03603 23  GLY A N   
144  C CA  . GLY A 23  ? 0.78710 1.02868 1.06735 0.13131  0.20205  -0.03855 23  GLY A CA  
145  C C   . GLY A 23  ? 0.89150 1.11592 1.14469 0.10786  0.20821  -0.03954 23  GLY A C   
146  O O   . GLY A 23  ? 0.95386 1.20570 1.22081 0.09300  0.21279  -0.03891 23  GLY A O   
147  N N   . THR A 24  ? 0.88620 1.06583 1.10107 0.10351  0.20761  -0.04058 24  THR A N   
148  C CA  . THR A 24  ? 0.79670 0.95903 0.98345 0.08400  0.21452  -0.04182 24  THR A CA  
149  C C   . THR A 24  ? 0.86056 0.98411 1.01578 0.07388  0.20050  -0.03721 24  THR A C   
150  O O   . THR A 24  ? 0.83156 0.92714 0.97266 0.08378  0.19427  -0.03780 24  THR A O   
151  C CB  . THR A 24  ? 0.84563 0.99660 1.01540 0.08946  0.23475  -0.05127 24  THR A CB  
152  O OG1 . THR A 24  ? 0.87475 1.06592 1.07680 0.09853  0.24924  -0.05565 24  THR A OG1 
153  C CG2 . THR A 24  ? 0.85969 0.99169 0.99682 0.06943  0.24096  -0.05172 24  THR A CG2 
154  N N   . VAL A 25  ? 0.81424 0.93633 0.95936 0.05420  0.19585  -0.03244 25  VAL A N   
155  C CA  . VAL A 25  ? 0.88012 0.96801 0.99458 0.04314  0.18509  -0.02868 25  VAL A CA  
156  C C   . VAL A 25  ? 0.86491 0.94068 0.95316 0.02912  0.19524  -0.03059 25  VAL A C   
157  O O   . VAL A 25  ? 0.85673 0.95467 0.95468 0.02164  0.20584  -0.03075 25  VAL A O   
158  C CB  . VAL A 25  ? 0.73155 0.82605 0.85625 0.03408  0.16836  -0.02024 25  VAL A CB  
159  C CG1 . VAL A 25  ? 0.80280 0.86641 0.89820 0.02207  0.15917  -0.01647 25  VAL A CG1 
160  C CG2 . VAL A 25  ? 0.72455 0.82613 0.86844 0.04801  0.15761  -0.01799 25  VAL A CG2 
161  N N   . THR A 26  ? 0.89272 0.93376 0.94730 0.02543  0.19243  -0.03214 26  THR A N   
162  C CA  . THR A 26  ? 0.92337 0.94973 0.94817 0.01207  0.19936  -0.03303 26  THR A CA  
163  C C   . THR A 26  ? 0.85371 0.86938 0.86723 -0.00261 0.18457  -0.02422 26  THR A C   
164  O O   . THR A 26  ? 0.76173 0.75983 0.76828 -0.00185 0.17073  -0.02173 26  THR A O   
165  C CB  . THR A 26  ? 0.90259 0.89849 0.89594 0.01690  0.20551  -0.04138 26  THR A CB  
166  O OG1 . THR A 26  ? 0.97970 0.98427 0.98524 0.03297  0.21952  -0.04991 26  THR A OG1 
167  C CG2 . THR A 26  ? 0.88865 0.87176 0.84976 0.00332  0.21292  -0.04233 26  THR A CG2 
168  N N   . ALA A 27  ? 0.86622 0.89257 0.87891 -0.01564 0.18804  -0.01928 27  ALA A N   
169  C CA  . ALA A 27  ? 0.82217 0.84047 0.82775 -0.02804 0.17494  -0.01043 27  ALA A CA  
170  C C   . ALA A 27  ? 0.83523 0.83276 0.80563 -0.03933 0.17760  -0.00845 27  ALA A C   
171  O O   . ALA A 27  ? 0.88671 0.88742 0.84574 -0.04308 0.19240  -0.01110 27  ALA A O   
172  C CB  . ALA A 27  ? 0.76239 0.80621 0.79487 -0.03447 0.17428  -0.00501 27  ALA A CB  
173  N N   . PHE A 28  ? 0.78038 0.75746 0.73326 -0.04413 0.16334  -0.00391 28  PHE A N   
174  C CA  . PHE A 28  ? 0.91143 0.86963 0.83184 -0.05494 0.16115  0.00023  28  PHE A CA  
175  C C   . PHE A 28  ? 0.90149 0.86171 0.82965 -0.06288 0.14945  0.01071  28  PHE A C   
176  O O   . PHE A 28  ? 0.87393 0.82909 0.80876 -0.06090 0.13506  0.01357  28  PHE A O   
177  C CB  . PHE A 28  ? 0.90433 0.83798 0.79847 -0.05325 0.15347  -0.00400 28  PHE A CB  
178  C CG  . PHE A 28  ? 0.91820 0.84471 0.80025 -0.04590 0.16587  -0.01525 28  PHE A CG  
179  C CD1 . PHE A 28  ? 0.92498 0.85477 0.82559 -0.03317 0.16745  -0.02187 28  PHE A CD1 
180  C CD2 . PHE A 28  ? 0.89498 0.81018 0.74583 -0.05107 0.17643  -0.01916 28  PHE A CD2 
181  C CE1 . PHE A 28  ? 0.97557 0.89640 0.86518 -0.02482 0.17971  -0.03269 28  PHE A CE1 
182  C CE2 . PHE A 28  ? 0.99810 0.90525 0.83668 -0.04369 0.18919  -0.03082 28  PHE A CE2 
183  C CZ  . PHE A 28  ? 0.97400 0.88349 0.83277 -0.03005 0.19107  -0.03787 28  PHE A CZ  
184  N N   . LEU A 29  ? 0.82788 0.79509 0.75587 -0.07173 0.15652  0.01622  29  LEU A N   
185  C CA  . LEU A 29  ? 0.86919 0.83658 0.80503 -0.07887 0.14741  0.02566  29  LEU A CA  
186  C C   . LEU A 29  ? 0.88633 0.83306 0.79010 -0.08769 0.14366  0.03345  29  LEU A C   
187  O O   . LEU A 29  ? 0.86633 0.80809 0.74885 -0.09354 0.15504  0.03409  29  LEU A O   
188  C CB  . LEU A 29  ? 0.84955 0.83835 0.81027 -0.08337 0.15690  0.02685  29  LEU A CB  
189  C CG  . LEU A 29  ? 0.78965 0.80360 0.78418 -0.07469 0.16024  0.01985  29  LEU A CG  
190  C CD1 . LEU A 29  ? 0.74790 0.78312 0.76571 -0.08218 0.16719  0.02172  29  LEU A CD1 
191  C CD2 . LEU A 29  ? 0.80173 0.81476 0.81013 -0.06623 0.14516  0.01918  29  LEU A CD2 
192  N N   . GLY A 30  ? 0.84800 0.78344 0.74802 -0.08807 0.12784  0.03959  30  GLY A N   
193  C CA  . GLY A 30  ? 0.81771 0.73516 0.69051 -0.09485 0.12169  0.04858  30  GLY A CA  
194  C C   . GLY A 30  ? 0.90567 0.80805 0.74634 -0.09488 0.11864  0.04608  30  GLY A C   
195  O O   . GLY A 30  ? 0.94172 0.83428 0.75441 -0.10107 0.12543  0.04896  30  GLY A O   
196  N N   . ILE A 31  ? 0.92966 0.82950 0.77253 -0.08898 0.10884  0.04047  31  ILE A N   
197  C CA  . ILE A 31  ? 0.92111 0.80562 0.73355 -0.09068 0.10240  0.03811  31  ILE A CA  
198  C C   . ILE A 31  ? 0.93138 0.80866 0.73751 -0.09322 0.08491  0.04801  31  ILE A C   
199  O O   . ILE A 31  ? 0.93335 0.81742 0.76352 -0.08946 0.07524  0.05066  31  ILE A O   
200  C CB  . ILE A 31  ? 0.95714 0.84029 0.77354 -0.08463 0.10067  0.02693  31  ILE A CB  
201  C CG1 . ILE A 31  ? 0.94092 0.83262 0.76913 -0.07878 0.11711  0.01736  31  ILE A CG1 
202  C CG2 . ILE A 31  ? 0.97963 0.84594 0.76199 -0.08870 0.09477  0.02324  31  ILE A CG2 
203  C CD1 . ILE A 31  ? 0.85769 0.74412 0.69002 -0.07171 0.11476  0.00742  31  ILE A CD1 
204  N N   . PRO A 32  ? 0.96542 0.82991 0.74012 -0.09877 0.08022  0.05374  32  PRO A N   
205  C CA  . PRO A 32  ? 0.96166 0.82148 0.73245 -0.09928 0.06222  0.06322  32  PRO A CA  
206  C C   . PRO A 32  ? 0.96492 0.82559 0.73798 -0.09715 0.04908  0.05717  32  PRO A C   
207  O O   . PRO A 32  ? 0.94332 0.79885 0.70160 -0.09853 0.05217  0.04731  32  PRO A O   
208  C CB  . PRO A 32  ? 1.01048 0.85645 0.74366 -0.10563 0.06205  0.07074  32  PRO A CB  
209  C CG  . PRO A 32  ? 1.02938 0.87086 0.74051 -0.10864 0.07604  0.06037  32  PRO A CG  
210  C CD  . PRO A 32  ? 1.03670 0.89100 0.77700 -0.10431 0.09083  0.05194  32  PRO A CD  
211  N N   . TYR A 33  ? 0.98045 0.84706 0.77195 -0.09421 0.03495  0.06280  33  TYR A N   
212  C CA  . TYR A 33  ? 0.93146 0.80069 0.72659 -0.09389 0.02201  0.05816  33  TYR A CA  
213  C C   . TYR A 33  ? 0.97912 0.84912 0.76788 -0.09495 0.00420  0.06747  33  TYR A C   
214  O O   . TYR A 33  ? 0.93425 0.81093 0.73286 -0.09496 -0.00768 0.06505  33  TYR A O   
215  C CB  . TYR A 33  ? 0.82743 0.70764 0.65642 -0.08856 0.02253  0.05337  33  TYR A CB  
216  C CG  . TYR A 33  ? 0.87727 0.76731 0.73351 -0.08385 0.01780  0.06132  33  TYR A CG  
217  C CD1 . TYR A 33  ? 0.81646 0.70987 0.68711 -0.08137 0.02816  0.06351  33  TYR A CD1 
218  C CD2 . TYR A 33  ? 0.85122 0.74799 0.71968 -0.08215 0.00348  0.06557  33  TYR A CD2 
219  C CE1 . TYR A 33  ? 0.78204 0.68204 0.67540 -0.07749 0.02429  0.06916  33  TYR A CE1 
220  C CE2 . TYR A 33  ? 0.78326 0.68788 0.67561 -0.07700 0.00044  0.07165  33  TYR A CE2 
221  C CZ  . TYR A 33  ? 0.79372 0.69839 0.69715 -0.07473 0.01089  0.07304  33  TYR A CZ  
222  O OH  . TYR A 33  ? 0.71081 0.62095 0.63567 -0.07009 0.00827  0.07765  33  TYR A OH  
223  N N   . ALA A 34  ? 0.96556 0.82923 0.73833 -0.09581 0.00199  0.07835  34  ALA A N   
224  C CA  . ALA A 34  ? 1.00920 0.87407 0.77532 -0.09507 -0.01582 0.08811  34  ALA A CA  
225  C C   . ALA A 34  ? 1.03225 0.88414 0.77064 -0.09681 -0.01490 0.09958  34  ALA A C   
226  O O   . ALA A 34  ? 1.03073 0.87496 0.76418 -0.09815 -0.00014 0.10148  34  ALA A O   
227  C CB  . ALA A 34  ? 0.88218 0.75952 0.68327 -0.08788 -0.02395 0.09313  34  ALA A CB  
228  N N   . GLN A 35  ? 1.04680 0.89686 0.76729 -0.09713 -0.03097 0.10769  35  GLN A N   
229  C CA  . GLN A 35  ? 1.07459 0.91135 0.77128 -0.09688 -0.03241 0.12174  35  GLN A CA  
230  C C   . GLN A 35  ? 1.03287 0.86769 0.75362 -0.09058 -0.02726 0.13041  35  GLN A C   
231  O O   . GLN A 35  ? 1.02399 0.87045 0.77695 -0.08384 -0.03383 0.13040  35  GLN A O   
232  C CB  . GLN A 35  ? 1.05236 0.89015 0.73169 -0.09553 -0.05350 0.13107  35  GLN A CB  
233  C CG  . GLN A 35  ? 1.21294 1.04011 0.84714 -0.10354 -0.05610 0.13028  35  GLN A CG  
234  C CD  . GLN A 35  ? 1.34717 1.18376 0.97216 -0.10367 -0.07945 0.13307  35  GLN A CD  
235  O OE1 . GLN A 35  ? 1.32503 1.17229 0.95439 -0.10826 -0.08611 0.12128  35  GLN A OE1 
236  N NE2 . GLN A 35  ? 1.27581 1.10891 0.88974 -0.09842 -0.09274 0.14920  35  GLN A NE2 
237  N N   . PRO A 36  ? 1.05517 0.87505 0.76092 -0.09328 -0.01506 0.13731  36  PRO A N   
238  C CA  . PRO A 36  ? 1.01852 0.83245 0.74278 -0.08855 -0.01150 0.14628  36  PRO A CA  
239  C C   . PRO A 36  ? 1.00709 0.82201 0.74011 -0.07928 -0.02988 0.15731  36  PRO A C   
240  O O   . PRO A 36  ? 1.04820 0.85799 0.75693 -0.07816 -0.04309 0.16626  36  PRO A O   
241  C CB  . PRO A 36  ? 0.98633 0.78048 0.68060 -0.09538 0.00103  0.15448  36  PRO A CB  
242  C CG  . PRO A 36  ? 0.94352 0.73977 0.61739 -0.10343 0.01182  0.14386  36  PRO A CG  
243  C CD  . PRO A 36  ? 1.01176 0.81900 0.68228 -0.10184 -0.00244 0.13630  36  PRO A CD  
244  N N   . PRO A 37  ? 1.00264 0.82559 0.77019 -0.07188 -0.03176 0.15658  37  PRO A N   
245  C CA  . PRO A 37  ? 0.95989 0.78710 0.73979 -0.06129 -0.04882 0.16579  37  PRO A CA  
246  C C   . PRO A 37  ? 0.96626 0.77163 0.73440 -0.05638 -0.04951 0.18151  37  PRO A C   
247  O O   . PRO A 37  ? 0.99558 0.79749 0.78605 -0.04864 -0.04914 0.18500  37  PRO A O   
248  C CB  . PRO A 37  ? 0.93998 0.78426 0.76056 -0.05610 -0.04726 0.15650  37  PRO A CB  
249  C CG  . PRO A 37  ? 0.94715 0.78626 0.77502 -0.06212 -0.02821 0.14870  37  PRO A CG  
250  C CD  . PRO A 37  ? 0.94884 0.77940 0.74605 -0.07234 -0.01889 0.14649  37  PRO A CD  
251  N N   . LEU A 38  ? 1.04325 0.83135 0.77376 -0.06123 -0.04963 0.19102  38  LEU A N   
252  C CA  . LEU A 38  ? 1.01981 0.78206 0.73197 -0.05832 -0.04892 0.20734  38  LEU A CA  
253  C C   . LEU A 38  ? 1.10235 0.86059 0.79520 -0.05001 -0.06901 0.22175  38  LEU A C   
254  O O   . LEU A 38  ? 1.12247 0.89670 0.80694 -0.05038 -0.08222 0.21896  38  LEU A O   
255  C CB  . LEU A 38  ? 1.03059 0.77312 0.71133 -0.07068 -0.03217 0.20982  38  LEU A CB  
256  C CG  . LEU A 38  ? 1.12863 0.87811 0.81583 -0.08186 -0.01246 0.19549  38  LEU A CG  
257  C CD1 . LEU A 38  ? 1.15421 0.88718 0.80222 -0.09300 -0.00052 0.20034  38  LEU A CD1 
258  C CD2 . LEU A 38  ? 1.02917 0.77519 0.74573 -0.08156 -0.00083 0.19270  38  LEU A CD2 
259  N N   . GLY A 39  ? 1.10450 0.83984 0.78898 -0.04289 -0.07126 0.23751  39  GLY A N   
260  C CA  . GLY A 39  ? 1.10365 0.83220 0.76766 -0.03346 -0.09039 0.25387  39  GLY A CA  
261  C C   . GLY A 39  ? 1.20323 0.95878 0.89852 -0.02045 -0.10921 0.25184  39  GLY A C   
262  O O   . GLY A 39  ? 1.14149 0.90601 0.87408 -0.01224 -0.10739 0.24685  39  GLY A O   
263  N N   . ARG A 40  ? 1.19697 0.96702 0.87700 -0.01918 -0.12738 0.25525  40  ARG A N   
264  C CA  . ARG A 40  ? 1.16209 0.96300 0.87233 -0.00914 -0.14579 0.25243  40  ARG A CA  
265  C C   . ARG A 40  ? 1.14283 0.97024 0.88729 -0.01470 -0.13922 0.23263  40  ARG A C   
266  O O   . ARG A 40  ? 1.12881 0.98110 0.90666 -0.00623 -0.14975 0.22941  40  ARG A O   
267  C CB  . ARG A 40  ? 1.21707 1.02850 0.90034 -0.00971 -0.16685 0.25943  40  ARG A CB  
268  C CG  . ARG A 40  ? 1.25901 1.08028 0.92010 -0.02633 -0.16496 0.24610  40  ARG A CG  
269  C CD  . ARG A 40  ? 1.39447 1.18675 1.01030 -0.03865 -0.14939 0.24818  40  ARG A CD  
270  N NE  . ARG A 40  ? 1.49041 1.25730 1.06752 -0.03482 -0.15569 0.26815  40  ARG A NE  
271  C CZ  . ARG A 40  ? 1.42453 1.15987 0.97952 -0.03776 -0.13986 0.27725  40  ARG A CZ  
272  N NH1 . ARG A 40  ? 1.32152 1.04824 0.89289 -0.04348 -0.11757 0.26867  40  ARG A NH1 
273  N NH2 . ARG A 40  ? 1.47888 1.19103 0.99348 -0.03569 -0.14678 0.29567  40  ARG A NH2 
274  N N   . LEU A 41  ? 1.10919 0.93175 0.84715 -0.02799 -0.12151 0.21996  41  LEU A N   
275  C CA  . LEU A 41  ? 1.01285 0.85685 0.77983 -0.03313 -0.11459 0.20219  41  LEU A CA  
276  C C   . LEU A 41  ? 1.02123 0.86552 0.82354 -0.02726 -0.10286 0.19756  41  LEU A C   
277  O O   . LEU A 41  ? 0.88497 0.74848 0.71481 -0.02894 -0.09924 0.18463  41  LEU A O   
278  C CB  . LEU A 41  ? 0.99276 0.83158 0.73725 -0.04815 -0.10126 0.19080  41  LEU A CB  
279  C CG  . LEU A 41  ? 1.07097 0.92485 0.80130 -0.05664 -0.11037 0.18164  41  LEU A CG  
280  C CD1 . LEU A 41  ? 1.10969 0.97310 0.82835 -0.05178 -0.13401 0.19173  41  LEU A CD1 
281  C CD2 . LEU A 41  ? 1.05847 0.89723 0.75299 -0.06926 -0.09717 0.17557  41  LEU A CD2 
282  N N   . ARG A 42  ? 0.97809 0.80010 0.77857 -0.02110 -0.09671 0.20752  42  ARG A N   
283  C CA  . ARG A 42  ? 1.00545 0.82627 0.83717 -0.01601 -0.08617 0.20235  42  ARG A CA  
284  C C   . ARG A 42  ? 0.99093 0.83574 0.85784 -0.00383 -0.09757 0.20019  42  ARG A C   
285  O O   . ARG A 42  ? 0.99119 0.84242 0.85874 0.00649  -0.11370 0.21036  42  ARG A O   
286  C CB  . ARG A 42  ? 1.04027 0.82957 0.86081 -0.01196 -0.07899 0.21409  42  ARG A CB  
287  C CG  . ARG A 42  ? 1.00853 0.79388 0.85987 -0.00476 -0.07087 0.20991  42  ARG A CG  
288  C CD  . ARG A 42  ? 1.00975 0.76177 0.84995 0.00202  -0.06818 0.22350  42  ARG A CD  
289  N NE  . ARG A 42  ? 1.06171 0.78860 0.87769 -0.01138 -0.05297 0.22513  42  ARG A NE  
290  C CZ  . ARG A 42  ? 1.05530 0.74858 0.85214 -0.01082 -0.04843 0.23764  42  ARG A CZ  
291  N NH1 . ARG A 42  ? 1.15227 0.82957 0.95051 0.00416  -0.05786 0.25004  42  ARG A NH1 
292  N NH2 . ARG A 42  ? 1.06201 0.73698 0.83792 -0.02557 -0.03366 0.23801  42  ARG A NH2 
293  N N   . PHE A 43  ? 0.87604 0.73504 0.77215 -0.00497 -0.08888 0.18719  43  PHE A N   
294  C CA  . PHE A 43  ? 0.89174 0.77536 0.82359 0.00430  -0.09515 0.18229  43  PHE A CA  
295  C C   . PHE A 43  ? 0.92117 0.83375 0.86015 -0.00043 -0.10591 0.17578  43  PHE A C   
296  O O   . PHE A 43  ? 0.92916 0.86479 0.89806 0.00304  -0.10793 0.16891  43  PHE A O   
297  C CB  . PHE A 43  ? 0.98458 0.86547 0.92772 0.02120  -0.10544 0.19440  43  PHE A CB  
298  C CG  . PHE A 43  ? 0.96000 0.81095 0.89992 0.02732  -0.09546 0.20028  43  PHE A CG  
299  C CD1 . PHE A 43  ? 0.90387 0.74927 0.86004 0.02504  -0.08046 0.19026  43  PHE A CD1 
300  C CD2 . PHE A 43  ? 1.01061 0.83812 0.93055 0.03547  -0.10201 0.21620  43  PHE A CD2 
301  C CE1 . PHE A 43  ? 0.91356 0.73048 0.86632 0.02935  -0.07183 0.19470  43  PHE A CE1 
302  C CE2 . PHE A 43  ? 0.97565 0.77243 0.89186 0.04050  -0.09276 0.22167  43  PHE A CE2 
303  C CZ  . PHE A 43  ? 0.93242 0.72387 0.86530 0.03688  -0.07759 0.21035  43  PHE A CZ  
304  N N   . LYS A 44  ? 0.89355 0.80472 0.80456 -0.00886 -0.11279 0.17778  44  LYS A N   
305  C CA  . LYS A 44  ? 0.87011 0.80588 0.78545 -0.01560 -0.12266 0.17031  44  LYS A CA  
306  C C   . LYS A 44  ? 0.83963 0.77926 0.76036 -0.02695 -0.10942 0.15501  44  LYS A C   
307  O O   . LYS A 44  ? 0.85545 0.77942 0.77178 -0.03044 -0.09371 0.15080  44  LYS A O   
308  C CB  . LYS A 44  ? 0.89326 0.82472 0.77394 -0.02167 -0.13450 0.17609  44  LYS A CB  
309  C CG  . LYS A 44  ? 0.99093 0.91037 0.85508 -0.01151 -0.14600 0.19331  44  LYS A CG  
310  C CD  . LYS A 44  ? 1.08293 1.02632 0.95127 -0.00732 -0.16843 0.19856  44  LYS A CD  
311  C CE  . LYS A 44  ? 1.16468 1.11100 1.00255 -0.02180 -0.17512 0.19317  44  LYS A CE  
312  N NZ  . LYS A 44  ? 1.17907 1.14961 1.01826 -0.01944 -0.19902 0.19837  44  LYS A NZ  
313  N N   . LYS A 45  ? 0.87200 0.83270 0.80173 -0.03308 -0.11657 0.14697  45  LYS A N   
314  C CA  . LYS A 45  ? 0.86620 0.82898 0.79775 -0.04368 -0.10599 0.13320  45  LYS A CA  
315  C C   . LYS A 45  ? 0.89747 0.83958 0.79376 -0.05313 -0.09780 0.13037  45  LYS A C   
316  O O   . LYS A 45  ? 0.94598 0.87735 0.81401 -0.05428 -0.10425 0.13809  45  LYS A O   
317  C CB  . LYS A 45  ? 0.77095 0.75728 0.71535 -0.04956 -0.11663 0.12639  45  LYS A CB  
318  C CG  . LYS A 45  ? 0.81897 0.82819 0.80262 -0.04294 -0.11860 0.12501  45  LYS A CG  
319  C CD  . LYS A 45  ? 0.80697 0.84151 0.80274 -0.04958 -0.13167 0.12080  45  LYS A CD  
320  C CE  . LYS A 45  ? 0.84075 0.87876 0.84502 -0.06009 -0.12251 0.10800  45  LYS A CE  
321  N NZ  . LYS A 45  ? 0.82088 0.88732 0.85128 -0.06402 -0.13176 0.10485  45  LYS A NZ  
322  N N   . PRO A 46  ? 0.77538 0.71193 0.67230 -0.05931 -0.08327 0.11973  46  PRO A N   
323  C CA  . PRO A 46  ? 0.84370 0.76313 0.70958 -0.06752 -0.07397 0.11583  46  PRO A CA  
324  C C   . PRO A 46  ? 0.88547 0.80694 0.72749 -0.07568 -0.08441 0.11245  46  PRO A C   
325  O O   . PRO A 46  ? 0.95242 0.88908 0.80670 -0.07889 -0.09332 0.10667  46  PRO A O   
326  C CB  . PRO A 46  ? 0.83453 0.75377 0.71419 -0.07029 -0.05858 0.10436  46  PRO A CB  
327  C CG  . PRO A 46  ? 0.77280 0.71039 0.68464 -0.06709 -0.06326 0.10042  46  PRO A CG  
328  C CD  . PRO A 46  ? 0.84306 0.78935 0.76882 -0.05831 -0.07469 0.11109  46  PRO A CD  
329  N N   . GLN A 47  ? 0.96851 0.87411 0.77519 -0.08006 -0.08286 0.11573  47  GLN A N   
330  C CA  . GLN A 47  ? 1.01039 0.91457 0.78763 -0.08843 -0.09256 0.11244  47  GLN A CA  
331  C C   . GLN A 47  ? 1.03947 0.93001 0.79460 -0.09696 -0.07784 0.10049  47  GLN A C   
332  O O   . GLN A 47  ? 0.98997 0.87066 0.74610 -0.09576 -0.06071 0.09851  47  GLN A O   
333  C CB  . GLN A 47  ? 1.00666 0.90276 0.75551 -0.08655 -0.10353 0.12596  47  GLN A CB  
334  C CG  . GLN A 47  ? 1.00728 0.91193 0.77755 -0.07492 -0.11449 0.13951  47  GLN A CG  
335  C CD  . GLN A 47  ? 1.14349 1.07117 0.92743 -0.07336 -0.13561 0.14105  47  GLN A CD  
336  O OE1 . GLN A 47  ? 1.26349 1.19390 1.02310 -0.08032 -0.14801 0.14007  47  GLN A OE1 
337  N NE2 . GLN A 47  ? 1.04152 0.98728 0.86468 -0.06474 -0.13972 0.14288  47  GLN A NE2 
338  N N   . SER A 48  ? 1.22373 1.11437 0.95943 -0.10561 -0.08481 0.09202  48  SER A N   
339  C CA  . SER A 48  ? 1.25850 1.13678 0.97618 -0.11290 -0.07153 0.07823  48  SER A CA  
340  C C   . SER A 48  ? 1.21158 1.07143 0.89136 -0.11558 -0.06133 0.08047  48  SER A C   
341  O O   . SER A 48  ? 1.25167 1.10703 0.90918 -0.11534 -0.06956 0.09160  48  SER A O   
342  C CB  . SER A 48  ? 1.19916 1.08105 0.90753 -0.12217 -0.08246 0.06748  48  SER A CB  
343  O OG  . SER A 48  ? 1.29527 1.17873 0.97732 -0.12687 -0.09960 0.07275  48  SER A OG  
344  N N   . LEU A 49  ? 1.23004 1.07949 0.90267 -0.11767 -0.04281 0.07029  49  LEU A N   
345  C CA  . LEU A 49  ? 1.33269 1.16687 0.97403 -0.11993 -0.02900 0.07181  49  LEU A CA  
346  C C   . LEU A 49  ? 1.46210 1.28438 1.06009 -0.12866 -0.03197 0.06474  49  LEU A C   
347  O O   . LEU A 49  ? 1.47151 1.29303 1.06567 -0.13357 -0.03562 0.05206  49  LEU A O   
348  C CB  . LEU A 49  ? 1.23030 1.06194 0.88605 -0.11724 -0.00693 0.06414  49  LEU A CB  
349  C CG  . LEU A 49  ? 1.22801 1.06114 0.89898 -0.11234 0.00229  0.07488  49  LEU A CG  
350  C CD1 . LEU A 49  ? 1.13652 0.97471 0.83332 -0.10886 0.01957  0.06663  49  LEU A CD1 
351  C CD2 . LEU A 49  ? 1.23119 1.05080 0.86608 -0.11657 0.00839  0.08305  49  LEU A CD2 
352  N N   . THR A 50  ? 1.52946 1.34067 1.09292 -0.13119 -0.03006 0.07296  50  THR A N   
353  C CA  . THR A 50  ? 1.61098 1.40840 1.12822 -0.13961 -0.02884 0.06571  50  THR A CA  
354  C C   . THR A 50  ? 1.63189 1.41903 1.14028 -0.14084 -0.00418 0.05290  50  THR A C   
355  O O   . THR A 50  ? 1.56483 1.35412 1.09271 -0.13595 0.01245  0.05524  50  THR A O   
356  C CB  . THR A 50  ? 1.68984 1.47837 1.17034 -0.14179 -0.03539 0.08025  50  THR A CB  
357  O OG1 . THR A 50  ? 1.60637 1.39377 1.10076 -0.13591 -0.02621 0.09402  50  THR A OG1 
358  C CG2 . THR A 50  ? 1.68791 1.48513 1.16325 -0.14263 -0.06290 0.08810  50  THR A CG2 
359  N N   . LYS A 51  ? 1.63372 1.41024 1.11318 -0.14735 -0.00207 0.03872  51  LYS A N   
360  C CA  . LYS A 51  ? 1.60043 1.36638 1.06851 -0.14743 0.02148  0.02549  51  LYS A CA  
361  C C   . LYS A 51  ? 1.59457 1.35434 1.04141 -0.14763 0.03823  0.03342  51  LYS A C   
362  O O   . LYS A 51  ? 1.62531 1.37958 1.04298 -0.15163 0.03065  0.04540  51  LYS A O   
363  C CB  . LYS A 51  ? 1.68134 1.43284 1.11375 -0.15512 0.01962  0.00945  51  LYS A CB  
364  C CG  . LYS A 51  ? 1.74282 1.49614 1.19702 -0.15585 0.01128  -0.00295 51  LYS A CG  
365  C CD  . LYS A 51  ? 1.82012 1.55514 1.23505 -0.16486 0.01029  -0.01971 51  LYS A CD  
366  C CE  . LYS A 51  ? 1.82204 1.54180 1.22467 -0.16144 0.03615  -0.03433 51  LYS A CE  
367  N NZ  . LYS A 51  ? 1.74177 1.46527 1.18600 -0.15279 0.04619  -0.04126 51  LYS A NZ  
368  N N   . TRP A 52  ? 1.52138 1.28284 0.98375 -0.14336 0.06101  0.02740  52  TRP A N   
369  C CA  . TRP A 52  ? 1.49023 1.24544 0.92901 -0.14563 0.08109  0.03031  52  TRP A CA  
370  C C   . TRP A 52  ? 1.54431 1.29029 0.96268 -0.14640 0.09981  0.01214  52  TRP A C   
371  O O   . TRP A 52  ? 1.47422 1.21994 0.90814 -0.14260 0.10089  -0.00192 52  TRP A O   
372  C CB  . TRP A 52  ? 1.42038 1.18796 0.89463 -0.14072 0.09390  0.03924  52  TRP A CB  
373  C CG  . TRP A 52  ? 1.41406 1.19288 0.92664 -0.13349 0.10633  0.02784  52  TRP A CG  
374  C CD1 . TRP A 52  ? 1.43470 1.21470 0.94750 -0.13111 0.12898  0.01626  52  TRP A CD1 
375  C CD2 . TRP A 52  ? 1.32046 1.11159 0.87680 -0.12681 0.09675  0.02715  52  TRP A CD2 
376  N NE1 . TRP A 52  ? 1.37010 1.16236 0.92458 -0.12267 0.13281  0.00905  52  TRP A NE1 
377  C CE2 . TRP A 52  ? 1.29117 1.08959 0.87143 -0.12047 0.11338  0.01567  52  TRP A CE2 
378  C CE3 . TRP A 52  ? 1.31667 1.11406 0.89422 -0.12509 0.07612  0.03527  52  TRP A CE3 
379  C CZ2 . TRP A 52  ? 1.27681 1.08684 0.89851 -0.11309 0.10926  0.01280  52  TRP A CZ2 
380  C CZ3 . TRP A 52  ? 1.28980 1.09914 0.90880 -0.11838 0.07358  0.03167  52  TRP A CZ3 
381  C CH2 . TRP A 52  ? 1.24560 1.06029 0.88485 -0.11275 0.08964  0.02083  52  TRP A CH2 
382  N N   . SER A 53  ? 1.56895 1.30603 0.95135 -0.15110 0.11555  0.01282  53  SER A N   
383  C CA  . SER A 53  ? 1.58216 1.30825 0.93683 -0.15219 0.13397  -0.00426 53  SER A CA  
384  C C   . SER A 53  ? 1.56714 1.30233 0.93935 -0.14724 0.16246  -0.00829 53  SER A C   
385  O O   . SER A 53  ? 1.58500 1.31421 0.94474 -0.14479 0.17982  -0.02418 53  SER A O   
386  C CB  . SER A 53  ? 1.68177 1.39024 0.97540 -0.16204 0.13148  -0.00316 53  SER A CB  
387  O OG  . SER A 53  ? 1.71818 1.41964 0.99444 -0.16684 0.10520  -0.00331 53  SER A OG  
388  N N   . ASP A 54  ? 1.66226 1.41184 1.06290 -0.14587 0.16788  0.00505  54  ASP A N   
389  C CA  . ASP A 54  ? 1.66297 1.42539 1.08350 -0.14254 0.19413  0.00196  54  ASP A CA  
390  C C   . ASP A 54  ? 1.62455 1.40290 1.09683 -0.13154 0.19652  -0.00662 54  ASP A C   
391  O O   . ASP A 54  ? 1.56073 1.33531 1.04443 -0.12715 0.18162  -0.01303 54  ASP A O   
392  C CB  . ASP A 54  ? 1.71105 1.47897 1.13240 -0.14883 0.19911  0.02008  54  ASP A CB  
393  C CG  . ASP A 54  ? 1.80500 1.58617 1.27179 -0.14556 0.18605  0.03212  54  ASP A CG  
394  O OD1 . ASP A 54  ? 1.84746 1.64447 1.35877 -0.13766 0.18785  0.02608  54  ASP A OD1 
395  O OD2 . ASP A 54  ? 1.83626 1.61044 1.29182 -0.15061 0.17314  0.04810  54  ASP A OD2 
396  N N   . ILE A 55  ? 1.52186 1.31847 1.02514 -0.12752 0.21513  -0.00666 55  ILE A N   
397  C CA  . ILE A 55  ? 1.42414 1.23864 0.97820 -0.11696 0.21647  -0.01192 55  ILE A CA  
398  C C   . ILE A 55  ? 1.35185 1.18133 0.93950 -0.11879 0.20863  0.00311  55  ILE A C   
399  O O   . ILE A 55  ? 1.37105 1.21120 0.96534 -0.12349 0.22226  0.01012  55  ILE A O   
400  C CB  . ILE A 55  ? 1.38600 1.21336 0.95410 -0.10981 0.24233  -0.02417 55  ILE A CB  
401  C CG1 . ILE A 55  ? 1.36082 1.16941 0.88679 -0.10949 0.25324  -0.03865 55  ILE A CG1 
402  C CG2 . ILE A 55  ? 1.28579 1.12971 0.90356 -0.09734 0.24042  -0.02980 55  ILE A CG2 
403  C CD1 . ILE A 55  ? 1.15775 0.97496 0.70041 -0.09778 0.27433  -0.05437 55  ILE A CD1 
404  N N   . TRP A 56  ? 1.22574 1.05553 0.83404 -0.11585 0.18750  0.00773  56  TRP A N   
405  C CA  . TRP A 56  ? 1.19793 1.03961 0.83685 -0.11701 0.17966  0.02074  56  TRP A CA  
406  C C   . TRP A 56  ? 1.16245 1.02723 0.84410 -0.11125 0.19328  0.01696  56  TRP A C   
407  O O   . TRP A 56  ? 1.18285 1.05566 0.88728 -0.10171 0.19460  0.00657  56  TRP A O   
408  C CB  . TRP A 56  ? 1.18253 1.02078 0.83475 -0.11412 0.15544  0.02496  56  TRP A CB  
409  C CG  . TRP A 56  ? 1.15861 1.00689 0.83985 -0.11472 0.14834  0.03722  56  TRP A CG  
410  C CD1 . TRP A 56  ? 1.11370 0.98009 0.83625 -0.10994 0.15274  0.03634  56  TRP A CD1 
411  C CD2 . TRP A 56  ? 1.16036 0.99985 0.83004 -0.12018 0.13574  0.05192  56  TRP A CD2 
412  N NE1 . TRP A 56  ? 1.13087 0.99896 0.86710 -0.11303 0.14417  0.04857  56  TRP A NE1 
413  C CE2 . TRP A 56  ? 1.13080 0.98185 0.83579 -0.11860 0.13403  0.05849  56  TRP A CE2 
414  C CE3 . TRP A 56  ? 1.20215 1.02475 0.83456 -0.12561 0.12502  0.06024  56  TRP A CE3 
415  C CZ2 . TRP A 56  ? 1.13376 0.97774 0.83793 -0.12171 0.12326  0.07252  56  TRP A CZ2 
416  C CZ3 . TRP A 56  ? 1.25444 1.07172 0.88722 -0.12780 0.11348  0.07542  56  TRP A CZ3 
417  C CH2 . TRP A 56  ? 1.19846 1.02534 0.86709 -0.12554 0.11322  0.08119  56  TRP A CH2 
418  N N   . ASN A 57  ? 1.09632 0.97153 0.78931 -0.11732 0.20230  0.02590  57  ASN A N   
419  C CA  . ASN A 57  ? 1.14928 1.04960 0.88234 -0.11390 0.21567  0.02245  57  ASN A CA  
420  C C   . ASN A 57  ? 1.09003 1.00012 0.86006 -0.11028 0.20041  0.02741  57  ASN A C   
421  O O   . ASN A 57  ? 1.11069 1.01962 0.88641 -0.11701 0.19445  0.03866  57  ASN A O   
422  C CB  . ASN A 57  ? 1.19932 1.10690 0.92660 -0.12420 0.23411  0.02843  57  ASN A CB  
423  C CG  . ASN A 57  ? 1.30475 1.21302 1.00886 -0.12457 0.25561  0.01912  57  ASN A CG  
424  O OD1 . ASN A 57  ? 1.28350 1.18957 0.98292 -0.11524 0.25812  0.00650  57  ASN A OD1 
425  N ND2 . ASN A 57  ? 1.34738 1.25722 1.03589 -0.13548 0.27204  0.02510  57  ASN A ND2 
426  N N   . ALA A 58  ? 1.02576 0.94371 0.81932 -0.09944 0.19474  0.01881  58  ALA A N   
427  C CA  . ALA A 58  ? 0.96409 0.89108 0.79066 -0.09498 0.18062  0.02198  58  ALA A CA  
428  C C   . ALA A 58  ? 0.96316 0.91703 0.82871 -0.09036 0.19102  0.01760  58  ALA A C   
429  O O   . ALA A 58  ? 0.96762 0.93148 0.85587 -0.07984 0.18840  0.01060  58  ALA A O   
430  C CB  . ALA A 58  ? 0.97873 0.89526 0.80343 -0.08707 0.16593  0.01683  58  ALA A CB  
431  N N   . THR A 59  ? 0.95733 0.92290 0.83001 -0.09905 0.20254  0.02246  59  THR A N   
432  C CA  . THR A 59  ? 0.92722 0.92187 0.83486 -0.09717 0.21494  0.01801  59  THR A CA  
433  C C   . THR A 59  ? 0.88449 0.89082 0.81727 -0.10493 0.21008  0.02555  59  THR A C   
434  O O   . THR A 59  ? 0.86831 0.90083 0.83071 -0.10625 0.21960  0.02264  59  THR A O   
435  C CB  . THR A 59  ? 0.99319 0.99605 0.88941 -0.10178 0.23748  0.01432  59  THR A CB  
436  O OG1 . THR A 59  ? 1.01551 1.00026 0.87977 -0.11529 0.24028  0.02387  59  THR A OG1 
437  C CG2 . THR A 59  ? 0.96022 0.95555 0.83831 -0.09144 0.24457  0.00333  59  THR A CG2 
438  N N   . LYS A 60  ? 0.92225 0.91016 0.84397 -0.11030 0.19587  0.03475  60  LYS A N   
439  C CA  . LYS A 60  ? 0.93285 0.92706 0.87673 -0.11644 0.18944  0.04073  60  LYS A CA  
440  C C   . LYS A 60  ? 0.85718 0.83183 0.79304 -0.11331 0.16977  0.04637  60  LYS A C   
441  O O   . LYS A 60  ? 0.82464 0.77994 0.73369 -0.11075 0.16266  0.04847  60  LYS A O   
442  C CB  . LYS A 60  ? 0.86247 0.85429 0.79882 -0.13177 0.20082  0.04838  60  LYS A CB  
443  C CG  . LYS A 60  ? 0.97202 0.93303 0.86971 -0.13900 0.19706  0.05928  60  LYS A CG  
444  C CD  . LYS A 60  ? 1.03385 0.99174 0.91870 -0.15416 0.21340  0.06615  60  LYS A CD  
445  C CE  . LYS A 60  ? 1.18151 1.11266 1.04856 -0.16277 0.20492  0.07981  60  LYS A CE  
446  N NZ  . LYS A 60  ? 1.16291 1.09580 1.03784 -0.17808 0.21684  0.08563  60  LYS A NZ  
447  N N   . TYR A 61  ? 0.84945 0.83119 0.80983 -0.11336 0.16109  0.04792  61  TYR A N   
448  C CA  . TYR A 61  ? 0.79416 0.75937 0.74995 -0.11094 0.14421  0.05358  61  TYR A CA  
449  C C   . TYR A 61  ? 0.77864 0.71903 0.70454 -0.11839 0.14200  0.06427  61  TYR A C   
450  O O   . TYR A 61  ? 0.91717 0.85347 0.83320 -0.12859 0.15291  0.06919  61  TYR A O   
451  C CB  . TYR A 61  ? 0.77807 0.75403 0.76239 -0.11221 0.13875  0.05343  61  TYR A CB  
452  C CG  . TYR A 61  ? 0.76550 0.76370 0.77779 -0.10334 0.13610  0.04473  61  TYR A CG  
453  C CD1 . TYR A 61  ? 0.77327 0.76814 0.78641 -0.09254 0.12493  0.04201  61  TYR A CD1 
454  C CD2 . TYR A 61  ? 0.72398 0.74679 0.76234 -0.10633 0.14395  0.03995  61  TYR A CD2 
455  C CE1 . TYR A 61  ? 0.78860 0.80134 0.82501 -0.08418 0.12213  0.03549  61  TYR A CE1 
456  C CE2 . TYR A 61  ? 0.62794 0.67135 0.69119 -0.09729 0.14000  0.03310  61  TYR A CE2 
457  C CZ  . TYR A 61  ? 0.77824 0.81504 0.83918 -0.08592 0.12911  0.03136  61  TYR A CZ  
458  O OH  . TYR A 61  ? 0.77374 0.82878 0.85688 -0.07661 0.12513  0.02582  61  TYR A OH  
459  N N   . ALA A 62  ? 0.83326 0.75757 0.74494 -0.11328 0.12771  0.06841  62  ALA A N   
460  C CA  . ALA A 62  ? 0.92901 0.83016 0.81307 -0.11792 0.12256  0.07957  62  ALA A CA  
461  C C   . ALA A 62  ? 0.88470 0.77723 0.77988 -0.12029 0.11561  0.08703  62  ALA A C   
462  O O   . ALA A 62  ? 0.85881 0.76350 0.78149 -0.11979 0.11547  0.08268  62  ALA A O   
463  C CB  . ALA A 62  ? 0.80852 0.69899 0.67255 -0.11138 0.10999  0.08031  62  ALA A CB  
464  N N   . ASN A 63  ? 0.90038 0.77060 0.77239 -0.12260 0.10979  0.09833  63  ASN A N   
465  C CA  . ASN A 63  ? 0.89080 0.74754 0.76940 -0.12264 0.10212  0.10600  63  ASN A CA  
466  C C   . ASN A 63  ? 0.86418 0.72958 0.76649 -0.11270 0.08949  0.10103  63  ASN A C   
467  O O   . ASN A 63  ? 0.77788 0.64974 0.67991 -0.10494 0.08098  0.09728  63  ASN A O   
468  C CB  . ASN A 63  ? 0.88131 0.71290 0.72956 -0.12244 0.09476  0.11925  63  ASN A CB  
469  C CG  . ASN A 63  ? 0.99136 0.81021 0.81075 -0.13292 0.10712  0.12636  63  ASN A CG  
470  O OD1 . ASN A 63  ? 0.96283 0.78438 0.78791 -0.14298 0.12152  0.12552  63  ASN A OD1 
471  N ND2 . ASN A 63  ? 1.02849 0.83398 0.81619 -0.13124 0.10127  0.13361  63  ASN A ND2 
472  N N   . SER A 64  ? 0.80190 0.66642 0.72350 -0.11383 0.08877  0.10078  64  SER A N   
473  C CA  . SER A 64  ? 0.80073 0.66810 0.73964 -0.10467 0.07687  0.09840  64  SER A CA  
474  C C   . SER A 64  ? 0.81819 0.66449 0.74291 -0.09954 0.06627  0.10914  64  SER A C   
475  O O   . SER A 64  ? 0.89031 0.71675 0.79544 -0.10436 0.06892  0.11895  64  SER A O   
476  C CB  . SER A 64  ? 0.77859 0.65301 0.74189 -0.10782 0.08034  0.09267  64  SER A CB  
477  O OG  . SER A 64  ? 0.77363 0.67062 0.75247 -0.11116 0.08843  0.08323  64  SER A OG  
478  N N   . CYS A 65  ? 0.73048 0.58163 0.66543 -0.08942 0.05444  0.10776  65  CYS A N   
479  C CA  . CYS A 65  ? 0.78736 0.62310 0.71423 -0.08224 0.04345  0.11733  65  CYS A CA  
480  C C   . CYS A 65  ? 0.86286 0.68108 0.79540 -0.08290 0.04542  0.12164  65  CYS A C   
481  O O   . CYS A 65  ? 0.80922 0.63231 0.75923 -0.08661 0.05147  0.11434  65  CYS A O   
482  C CB  . CYS A 65  ? 0.74578 0.59528 0.68643 -0.07189 0.03168  0.11364  65  CYS A CB  
483  S SG  . CYS A 65  ? 0.80376 0.66927 0.73556 -0.07158 0.02763  0.10848  65  CYS A SG  
484  N N   . CYS A 66  ? 0.80251 0.59901 0.71876 -0.07920 0.03984  0.13365  66  CYS A N   
485  C CA  . CYS A 66  ? 0.85205 0.62637 0.77072 -0.07818 0.04100  0.13871  66  CYS A CA  
486  C C   . CYS A 66  ? 0.83704 0.61994 0.78186 -0.07088 0.03769  0.13016  66  CYS A C   
487  O O   . CYS A 66  ? 0.88179 0.68177 0.83890 -0.06165 0.02944  0.12627  66  CYS A O   
488  C CB  . CYS A 66  ? 0.89940 0.65120 0.79826 -0.07073 0.03234  0.15345  66  CYS A CB  
489  S SG  . CYS A 66  ? 1.01153 0.74879 0.87329 -0.07947 0.03594  0.16538  66  CYS A SG  
490  N N   . GLN A 67  ? 0.87136 0.64181 0.82356 -0.07609 0.04466  0.12696  67  GLN A N   
491  C CA  . GLN A 67  ? 0.88468 0.66197 0.85895 -0.07114 0.04343  0.11738  67  GLN A CA  
492  C C   . GLN A 67  ? 0.85598 0.61127 0.83070 -0.07916 0.05126  0.11576  67  GLN A C   
493  O O   . GLN A 67  ? 0.87207 0.61605 0.83581 -0.09191 0.05970  0.11873  67  GLN A O   
494  C CB  . GLN A 67  ? 0.80422 0.61207 0.79551 -0.07353 0.04505  0.10505  67  GLN A CB  
495  C CG  . GLN A 67  ? 0.80319 0.61884 0.79450 -0.08769 0.05558  0.10003  67  GLN A CG  
496  C CD  . GLN A 67  ? 0.83522 0.68041 0.83912 -0.08752 0.05591  0.09083  67  GLN A CD  
497  O OE1 . GLN A 67  ? 0.80078 0.65958 0.82187 -0.08739 0.05629  0.08152  67  GLN A OE1 
498  N NE2 . GLN A 67  ? 0.84992 0.70376 0.84370 -0.08707 0.05548  0.09340  67  GLN A NE2 
499  N N   . ASN A 68  ? 0.82357 0.57282 0.81071 -0.07219 0.04893  0.11051  68  ASN A N   
500  C CA  . ASN A 68  ? 0.87787 0.60833 0.86762 -0.08038 0.05594  0.10533  68  ASN A CA  
501  C C   . ASN A 68  ? 0.86286 0.61596 0.86622 -0.09261 0.06192  0.09259  68  ASN A C   
502  O O   . ASN A 68  ? 0.88890 0.67141 0.90371 -0.09000 0.05931  0.08620  68  ASN A O   
503  C CB  . ASN A 68  ? 0.86764 0.58480 0.86524 -0.06790 0.05184  0.10243  68  ASN A CB  
504  C CG  . ASN A 68  ? 1.01942 0.70634 1.00308 -0.05713 0.04772  0.11590  68  ASN A CG  
505  O OD1 . ASN A 68  ? 1.03152 0.68978 0.99841 -0.06415 0.05220  0.12433  68  ASN A OD1 
506  N ND2 . ASN A 68  ? 1.03343 0.72744 1.02431 -0.04004 0.03917  0.11852  68  ASN A ND2 
507  N N   . ILE A 69  ? 0.92609 0.66517 0.92790 -0.10646 0.06976  0.08940  69  ILE A N   
508  C CA  . ILE A 69  ? 0.96462 0.72578 0.98004 -0.11942 0.07504  0.07795  69  ILE A CA  
509  C C   . ILE A 69  ? 0.95273 0.70738 0.97821 -0.12072 0.07459  0.06688  69  ILE A C   
510  O O   . ILE A 69  ? 0.93098 0.65380 0.94852 -0.12037 0.07585  0.06864  69  ILE A O   
511  C CB  . ILE A 69  ? 1.00917 0.76489 1.01729 -0.13725 0.08492  0.08137  69  ILE A CB  
512  C CG1 . ILE A 69  ? 0.95516 0.70582 0.94559 -0.13528 0.08610  0.09435  69  ILE A CG1 
513  C CG2 . ILE A 69  ? 0.97766 0.76575 1.00330 -0.14827 0.08907  0.07040  69  ILE A CG2 
514  C CD1 . ILE A 69  ? 0.89020 0.67287 0.88625 -0.12957 0.08339  0.09225  69  ILE A CD1 
515  N N   . ASP A 70  ? 0.96288 0.74617 1.00421 -0.12212 0.07286  0.05545  70  ASP A N   
516  C CA  . ASP A 70  ? 1.06885 0.84907 1.11808 -0.12549 0.07245  0.04346  70  ASP A CA  
517  C C   . ASP A 70  ? 0.99490 0.76265 1.04287 -0.14526 0.07969  0.03959  70  ASP A C   
518  O O   . ASP A 70  ? 0.96660 0.75558 1.02184 -0.15757 0.08357  0.03782  70  ASP A O   
519  C CB  . ASP A 70  ? 1.00212 0.81763 1.06627 -0.12112 0.06770  0.03399  70  ASP A CB  
520  C CG  . ASP A 70  ? 1.00139 0.82270 1.07375 -0.12992 0.06763  0.02034  70  ASP A CG  
521  O OD1 . ASP A 70  ? 1.08636 0.88096 1.15267 -0.13434 0.06969  0.01596  70  ASP A OD1 
522  O OD2 . ASP A 70  ? 0.88912 0.74114 0.97299 -0.13081 0.06465  0.01375  70  ASP A OD2 
523  N N   . GLN A 71  ? 0.99052 0.72328 1.02958 -0.14839 0.08204  0.03841  71  GLN A N   
524  C CA  . GLN A 71  ? 1.02075 0.73525 1.05645 -0.16845 0.08923  0.03523  71  GLN A CA  
525  C C   . GLN A 71  ? 0.95380 0.66371 0.99525 -0.17592 0.08837  0.02000  71  GLN A C   
526  O O   . GLN A 71  ? 0.90046 0.58770 0.93716 -0.19227 0.09379  0.01631  71  GLN A O   
527  C CB  . GLN A 71  ? 1.04250 0.71283 1.05897 -0.16919 0.09396  0.04719  71  GLN A CB  
528  C CG  . GLN A 71  ? 1.17333 0.84598 1.18102 -0.17230 0.09784  0.06106  71  GLN A CG  
529  C CD  . GLN A 71  ? 1.21020 0.84397 1.19752 -0.16265 0.09774  0.07551  71  GLN A CD  
530  O OE1 . GLN A 71  ? 1.23438 0.87333 1.21526 -0.14898 0.09314  0.08585  71  GLN A OE1 
531  N NE2 . GLN A 71  ? 1.24162 0.83481 1.21800 -0.16949 0.10222  0.07630  71  GLN A NE2 
532  N N   . SER A 72  ? 1.02634 0.75717 1.07668 -0.16564 0.08190  0.01085  72  SER A N   
533  C CA  . SER A 72  ? 0.97935 0.70457 1.03159 -0.17135 0.08047  -0.00411 72  SER A CA  
534  C C   . SER A 72  ? 0.90388 0.65191 0.96724 -0.19236 0.08126  -0.01410 72  SER A C   
535  O O   . SER A 72  ? 0.99182 0.72605 1.05301 -0.20450 0.08193  -0.02558 72  SER A O   
536  C CB  . SER A 72  ? 0.97241 0.71550 1.02927 -0.15418 0.07384  -0.00987 72  SER A CB  
537  O OG  . SER A 72  ? 0.99450 0.72155 1.04465 -0.13517 0.07295  -0.00064 72  SER A OG  
538  N N   . PHE A 73  ? 0.96848 0.75229 1.04438 -0.19682 0.08097  -0.01078 73  PHE A N   
539  C CA  . PHE A 73  ? 0.88190 0.69411 0.97254 -0.21525 0.08095  -0.01989 73  PHE A CA  
540  C C   . PHE A 73  ? 0.86938 0.69445 0.96621 -0.22632 0.08799  -0.01125 73  PHE A C   
541  O O   . PHE A 73  ? 0.89872 0.76222 1.01005 -0.22481 0.08668  -0.01051 73  PHE A O   
542  C CB  . PHE A 73  ? 0.92125 0.77371 1.02522 -0.20739 0.07235  -0.02763 73  PHE A CB  
543  C CG  . PHE A 73  ? 0.90346 0.74516 0.99975 -0.19650 0.06656  -0.03581 73  PHE A CG  
544  C CD1 . PHE A 73  ? 0.87910 0.71036 0.97215 -0.20798 0.06475  -0.04942 73  PHE A CD1 
545  C CD2 . PHE A 73  ? 0.83075 0.67217 0.92230 -0.17576 0.06358  -0.03041 73  PHE A CD2 
546  C CE1 . PHE A 73  ? 0.83348 0.65409 0.91738 -0.19793 0.06076  -0.05760 73  PHE A CE1 
547  C CE2 . PHE A 73  ? 0.87639 0.70914 0.96111 -0.16598 0.05989  -0.03799 73  PHE A CE2 
548  C CZ  . PHE A 73  ? 0.84551 0.66757 0.92565 -0.17645 0.05886  -0.05156 73  PHE A CZ  
549  N N   . PRO A 74  ? 0.88648 0.67890 0.97174 -0.23746 0.09631  -0.00450 74  PRO A N   
550  C CA  . PRO A 74  ? 0.91941 0.72289 1.00893 -0.25051 0.10495  0.00331  74  PRO A CA  
551  C C   . PRO A 74  ? 0.88353 0.73082 0.99674 -0.26568 0.10509  -0.00610 74  PRO A C   
552  O O   . PRO A 74  ? 0.88483 0.73615 1.00615 -0.27986 0.10259  -0.01819 74  PRO A O   
553  C CB  . PRO A 74  ? 0.92240 0.67933 0.99522 -0.26482 0.11327  0.00810  74  PRO A CB  
554  C CG  . PRO A 74  ? 0.97341 0.69301 1.03064 -0.25106 0.10872  0.00752  74  PRO A CG  
555  C CD  . PRO A 74  ? 0.88065 0.62436 0.94892 -0.24152 0.09908  -0.00544 74  PRO A CD  
556  N N   . GLY A 75  ? 0.85880 0.73921 0.98309 -0.26251 0.10793  -0.00078 75  GLY A N   
557  C CA  . GLY A 75  ? 0.84652 0.77064 0.99525 -0.27554 0.10975  -0.00739 75  GLY A CA  
558  C C   . GLY A 75  ? 0.80938 0.77219 0.97616 -0.26672 0.09861  -0.01754 75  GLY A C   
559  O O   . GLY A 75  ? 0.84413 0.84636 1.03356 -0.27604 0.09845  -0.02343 75  GLY A O   
560  N N   . PHE A 76  ? 0.83393 0.78700 0.99154 -0.24931 0.08946  -0.01944 76  PHE A N   
561  C CA  . PHE A 76  ? 0.80489 0.78902 0.97461 -0.23981 0.07846  -0.02794 76  PHE A CA  
562  C C   . PHE A 76  ? 0.83158 0.83643 1.00440 -0.22007 0.07661  -0.02072 76  PHE A C   
563  O O   . PHE A 76  ? 0.78122 0.76388 0.93845 -0.20624 0.07753  -0.01245 76  PHE A O   
564  C CB  . PHE A 76  ? 0.81502 0.77406 0.97078 -0.23363 0.07113  -0.03462 76  PHE A CB  
565  C CG  . PHE A 76  ? 0.75383 0.74037 0.91693 -0.22312 0.06011  -0.04210 76  PHE A CG  
566  C CD1 . PHE A 76  ? 0.84492 0.86665 1.02582 -0.23351 0.05422  -0.05155 76  PHE A CD1 
567  C CD2 . PHE A 76  ? 0.79808 0.77569 0.95002 -0.20336 0.05535  -0.03942 76  PHE A CD2 
568  C CE1 . PHE A 76  ? 0.77236 0.81792 0.95725 -0.22320 0.04331  -0.05727 76  PHE A CE1 
569  C CE2 . PHE A 76  ? 0.74238 0.74296 0.89838 -0.19425 0.04590  -0.04535 76  PHE A CE2 
570  C CZ  . PHE A 76  ? 0.76144 0.79480 0.93262 -0.20390 0.03968  -0.05393 76  PHE A CZ  
571  N N   . HIS A 77  ? 0.76357 0.81080 0.95682 -0.21862 0.07356  -0.02408 77  HIS A N   
572  C CA  . HIS A 77  ? 0.76737 0.83247 0.96360 -0.20120 0.07337  -0.01747 77  HIS A CA  
573  C C   . HIS A 77  ? 0.71987 0.77490 0.90432 -0.18235 0.06489  -0.01645 77  HIS A C   
574  O O   . HIS A 77  ? 0.72291 0.77684 0.90160 -0.16819 0.06583  -0.00926 77  HIS A O   
575  C CB  . HIS A 77  ? 0.68733 0.79913 0.90886 -0.20189 0.07187  -0.02142 77  HIS A CB  
576  C CG  . HIS A 77  ? 0.74390 0.87065 0.96795 -0.18534 0.07400  -0.01492 77  HIS A CG  
577  N ND1 . HIS A 77  ? 0.77616 0.92663 1.00875 -0.17033 0.06561  -0.01672 77  HIS A ND1 
578  C CD2 . HIS A 77  ? 0.75650 0.87537 0.97342 -0.18162 0.08367  -0.00683 77  HIS A CD2 
579  C CE1 . HIS A 77  ? 0.78485 0.94020 1.01630 -0.15820 0.07038  -0.01055 77  HIS A CE1 
580  N NE2 . HIS A 77  ? 0.75369 0.89095 0.97547 -0.16493 0.08123  -0.00499 77  HIS A NE2 
581  N N   . GLY A 78  ? 0.72132 0.76914 0.90152 -0.18270 0.05711  -0.02399 78  GLY A N   
582  C CA  . GLY A 78  ? 0.66836 0.70857 0.83794 -0.16571 0.05020  -0.02326 78  GLY A CA  
583  C C   . GLY A 78  ? 0.72987 0.73694 0.88174 -0.15656 0.05406  -0.01501 78  GLY A C   
584  O O   . GLY A 78  ? 0.70572 0.71239 0.85214 -0.14139 0.05101  -0.01066 78  GLY A O   
585  N N   . SER A 79  ? 0.75931 0.73809 0.90206 -0.16582 0.06043  -0.01242 79  SER A N   
586  C CA  . SER A 79  ? 0.78290 0.73285 0.90994 -0.15591 0.06305  -0.00329 79  SER A CA  
587  C C   . SER A 79  ? 0.68835 0.63975 0.81360 -0.15601 0.06956  0.00664  79  SER A C   
588  O O   . SER A 79  ? 0.73436 0.68043 0.85166 -0.14350 0.06870  0.01411  79  SER A O   
589  C CB  . SER A 79  ? 0.67632 0.58924 0.79071 -0.16206 0.06571  -0.00435 79  SER A CB  
590  O OG  . SER A 79  ? 0.94888 0.85571 1.06562 -0.18037 0.07206  -0.00548 79  SER A OG  
591  N N   . GLU A 80  ? 0.65762 0.61763 0.79001 -0.17055 0.07620  0.00636  80  GLU A N   
592  C CA  . GLU A 80  ? 0.75175 0.70738 0.87800 -0.17238 0.08429  0.01588  80  GLU A CA  
593  C C   . GLU A 80  ? 0.79222 0.77545 0.92560 -0.16240 0.08437  0.01814  80  GLU A C   
594  O O   . GLU A 80  ? 0.80388 0.78034 0.92739 -0.16025 0.09003  0.02613  80  GLU A O   
595  C CB  . GLU A 80  ? 0.78666 0.74020 0.91705 -0.19264 0.09328  0.01515  80  GLU A CB  
596  C CG  . GLU A 80  ? 0.84859 0.76563 0.96712 -0.20164 0.09386  0.01411  80  GLU A CG  
597  C CD  . GLU A 80  ? 0.92601 0.82985 1.04215 -0.22182 0.10418  0.01669  80  GLU A CD  
598  O OE1 . GLU A 80  ? 0.95091 0.88370 1.08389 -0.23434 0.10896  0.01264  80  GLU A OE1 
599  O OE2 . GLU A 80  ? 1.00907 0.87360 1.10723 -0.22547 0.10765  0.02273  80  GLU A OE2 
600  N N   . MET A 81  ? 0.74100 0.75194 0.88845 -0.15515 0.07791  0.01173  81  MET A N   
601  C CA  . MET A 81  ? 0.63344 0.66448 0.78505 -0.14332 0.07773  0.01421  81  MET A CA  
602  C C   . MET A 81  ? 0.70334 0.71506 0.83810 -0.12975 0.07486  0.02112  81  MET A C   
603  O O   . MET A 81  ? 0.68082 0.70256 0.81470 -0.12118 0.07583  0.02381  81  MET A O   
604  C CB  . MET A 81  ? 0.67543 0.73535 0.84255 -0.13573 0.07022  0.00757  81  MET A CB  
605  C CG  . MET A 81  ? 0.73634 0.78799 0.89939 -0.13047 0.06072  0.00337  81  MET A CG  
606  S SD  . MET A 81  ? 0.76411 0.84846 0.94305 -0.12536 0.05134  -0.00444 81  MET A SD  
607  C CE  . MET A 81  ? 0.73028 0.82805 0.91068 -0.10879 0.05146  0.00120  81  MET A CE  
608  N N   . TRP A 82  ? 0.61127 0.59705 0.73395 -0.12706 0.07093  0.02324  82  TRP A N   
609  C CA  . TRP A 82  ? 0.73105 0.70104 0.84029 -0.11484 0.06732  0.02972  82  TRP A CA  
610  C C   . TRP A 82  ? 0.70055 0.64524 0.79331 -0.11752 0.07160  0.03877  82  TRP A C   
611  O O   . TRP A 82  ? 0.75922 0.69496 0.84133 -0.10834 0.06856  0.04483  82  TRP A O   
612  C CB  . TRP A 82  ? 0.65256 0.61395 0.76088 -0.10738 0.05992  0.02653  82  TRP A CB  
613  C CG  . TRP A 82  ? 0.74703 0.73033 0.86776 -0.10556 0.05526  0.01820  82  TRP A CG  
614  C CD1 . TRP A 82  ? 0.67830 0.66540 0.80548 -0.11297 0.05357  0.01026  82  TRP A CD1 
615  C CD2 . TRP A 82  ? 0.71385 0.71730 0.84024 -0.09589 0.05123  0.01728  82  TRP A CD2 
616  N NE1 . TRP A 82  ? 0.70819 0.71798 0.84412 -0.10802 0.04800  0.00495  82  TRP A NE1 
617  C CE2 . TRP A 82  ? 0.68360 0.70268 0.81922 -0.09718 0.04677  0.00967  82  TRP A CE2 
618  C CE3 . TRP A 82  ? 0.66858 0.67614 0.79149 -0.08668 0.05073  0.02210  82  TRP A CE3 
619  C CZ2 . TRP A 82  ? 0.70372 0.74182 0.84483 -0.08860 0.04193  0.00813  82  TRP A CZ2 
620  C CZ3 . TRP A 82  ? 0.70305 0.72779 0.83197 -0.07870 0.04660  0.01982  82  TRP A CZ3 
621  C CH2 . TRP A 82  ? 0.70396 0.74348 0.84174 -0.07928 0.04232  0.01357  82  TRP A CH2 
622  N N   . ASN A 83  ? 0.73386 0.66704 0.82380 -0.13036 0.07818  0.04012  83  ASN A N   
623  C CA  . ASN A 83  ? 0.75577 0.66296 0.82771 -0.13341 0.08246  0.04996  83  ASN A CA  
624  C C   . ASN A 83  ? 0.77060 0.68684 0.83524 -0.13299 0.08766  0.05527  83  ASN A C   
625  O O   . ASN A 83  ? 0.82031 0.76240 0.89662 -0.13447 0.09123  0.05033  83  ASN A O   
626  C CB  . ASN A 83  ? 0.79692 0.68813 0.86744 -0.14895 0.08909  0.04973  83  ASN A CB  
627  C CG  . ASN A 83  ? 0.84920 0.72133 0.92019 -0.14858 0.08445  0.04541  83  ASN A CG  
628  O OD1 . ASN A 83  ? 0.87373 0.73675 0.94088 -0.13555 0.07745  0.04627  83  ASN A OD1 
629  N ND2 . ASN A 83  ? 0.87007 0.73592 0.94577 -0.16342 0.08893  0.04024  83  ASN A ND2 
630  N N   . PRO A 84  ? 0.79215 0.68748 0.83683 -0.13033 0.08804  0.06515  84  PRO A N   
631  C CA  . PRO A 84  ? 0.86497 0.76737 0.89901 -0.12933 0.09249  0.06936  84  PRO A CA  
632  C C   . PRO A 84  ? 0.71984 0.63239 0.75681 -0.14291 0.10505  0.06827  84  PRO A C   
633  O O   . PRO A 84  ? 0.84367 0.74564 0.88116 -0.15515 0.11073  0.06945  84  PRO A O   
634  C CB  . PRO A 84  ? 0.81384 0.68850 0.82391 -0.12539 0.08913  0.08079  84  PRO A CB  
635  C CG  . PRO A 84  ? 0.88294 0.74053 0.89524 -0.12004 0.08149  0.08182  84  PRO A CG  
636  C CD  . PRO A 84  ? 0.78804 0.65187 0.81782 -0.12788 0.08446  0.07305  84  PRO A CD  
637  N N   . ASN A 85  ? 0.80347 0.73624 0.84243 -0.14092 0.11008  0.06576  85  ASN A N   
638  C CA  . ASN A 85  ? 0.83026 0.77836 0.87485 -0.15236 0.12335  0.06388  85  ASN A CA  
639  C C   . ASN A 85  ? 0.85074 0.79255 0.87340 -0.15262 0.13108  0.06994  85  ASN A C   
640  O O   . ASN A 85  ? 0.85060 0.81128 0.87866 -0.15716 0.14219  0.06661  85  ASN A O   
641  C CB  . ASN A 85  ? 0.68028 0.66368 0.75194 -0.14986 0.12442  0.05327  85  ASN A CB  
642  C CG  . ASN A 85  ? 0.76428 0.75943 0.83590 -0.13490 0.11971  0.05026  85  ASN A CG  
643  O OD1 . ASN A 85  ? 0.76478 0.74337 0.82016 -0.12597 0.11228  0.05434  85  ASN A OD1 
644  N ND2 . ASN A 85  ? 0.70044 0.72444 0.79094 -0.13219 0.12399  0.04309  85  ASN A ND2 
645  N N   . THR A 86  ? 0.89656 0.81408 0.89486 -0.14686 0.12498  0.07819  86  THR A N   
646  C CA  . THR A 86  ? 0.87715 0.78096 0.84817 -0.15040 0.13187  0.08609  86  THR A CA  
647  C C   . THR A 86  ? 0.87283 0.74337 0.82242 -0.15198 0.12632  0.09779  86  THR A C   
648  O O   . THR A 86  ? 0.91807 0.77807 0.87528 -0.14775 0.11689  0.09845  86  THR A O   
649  C CB  . THR A 86  ? 0.84874 0.75917 0.80864 -0.13964 0.12856  0.08390  86  THR A CB  
650  O OG1 . THR A 86  ? 0.83947 0.74053 0.79642 -0.12825 0.11326  0.08549  86  THR A OG1 
651  C CG2 . THR A 86  ? 0.84115 0.78169 0.82282 -0.13604 0.13386  0.07264  86  THR A CG2 
652  N N   . ASP A 87  ? 0.86804 0.72144 0.78977 -0.15739 0.13246  0.10720  87  ASP A N   
653  C CA  . ASP A 87  ? 0.92844 0.74865 0.82687 -0.15734 0.12660  0.12015  87  ASP A CA  
654  C C   . ASP A 87  ? 0.92192 0.73561 0.81971 -0.14210 0.10943  0.12178  87  ASP A C   
655  O O   . ASP A 87  ? 0.87440 0.70286 0.77378 -0.13300 0.10311  0.11686  87  ASP A O   
656  C CB  . ASP A 87  ? 0.94668 0.75149 0.81114 -0.16282 0.13364  0.13032  87  ASP A CB  
657  C CG  . ASP A 87  ? 0.99212 0.80242 0.85546 -0.17887 0.15230  0.12998  87  ASP A CG  
658  O OD1 . ASP A 87  ? 1.14720 0.98687 1.03159 -0.18146 0.16076  0.11887  87  ASP A OD1 
659  O OD2 . ASP A 87  ? 1.07739 0.86313 0.91994 -0.18883 0.15873  0.14106  87  ASP A OD2 
660  N N   . LEU A 88  ? 0.92508 0.71648 0.82151 -0.13964 0.10258  0.12835  88  LEU A N   
661  C CA  . LEU A 88  ? 0.89329 0.67571 0.78598 -0.12541 0.08718  0.13278  88  LEU A CA  
662  C C   . LEU A 88  ? 0.95729 0.72230 0.81780 -0.12312 0.08318  0.14537  88  LEU A C   
663  O O   . LEU A 88  ? 0.88080 0.62566 0.71939 -0.13200 0.09084  0.15499  88  LEU A O   
664  C CB  . LEU A 88  ? 0.83781 0.60165 0.73992 -0.12208 0.08218  0.13526  88  LEU A CB  
665  C CG  . LEU A 88  ? 0.88078 0.65835 0.81099 -0.12603 0.08592  0.12304  88  LEU A CG  
666  C CD1 . LEU A 88  ? 0.84391 0.60412 0.78212 -0.11889 0.07876  0.12368  88  LEU A CD1 
667  C CD2 . LEU A 88  ? 0.74790 0.55846 0.69650 -0.12102 0.08361  0.11149  88  LEU A CD2 
668  N N   . SER A 89  ? 0.92395 0.69709 0.78086 -0.11201 0.07101  0.14539  89  SER A N   
669  C CA  . SER A 89  ? 0.92252 0.68272 0.74881 -0.10935 0.06468  0.15633  89  SER A CA  
670  C C   . SER A 89  ? 0.93475 0.70600 0.76749 -0.09623 0.04830  0.15484  89  SER A C   
671  O O   . SER A 89  ? 0.92061 0.71361 0.77598 -0.09231 0.04602  0.14347  89  SER A O   
672  C CB  . SER A 89  ? 0.95207 0.71890 0.75842 -0.11850 0.07536  0.15437  89  SER A CB  
673  O OG  . SER A 89  ? 1.02827 0.78807 0.80606 -0.11459 0.06652  0.16173  89  SER A OG  
674  N N   . GLU A 90  ? 0.99192 0.74831 0.80528 -0.08960 0.03666  0.16694  90  GLU A N   
675  C CA  . GLU A 90  ? 0.93222 0.70217 0.74943 -0.07910 0.02090  0.16597  90  GLU A CA  
676  C C   . GLU A 90  ? 0.93104 0.71797 0.73865 -0.08345 0.02204  0.15768  90  GLU A C   
677  O O   . GLU A 90  ? 0.95141 0.75632 0.77206 -0.07805 0.01324  0.15044  90  GLU A O   
678  C CB  . GLU A 90  ? 0.94703 0.69953 0.74372 -0.07157 0.00773  0.18140  90  GLU A CB  
679  C CG  . GLU A 90  ? 0.94884 0.68816 0.76004 -0.06148 0.00167  0.18835  90  GLU A CG  
680  C CD  . GLU A 90  ? 1.06393 0.79446 0.86043 -0.05030 -0.01493 0.20225  90  GLU A CD  
681  O OE1 . GLU A 90  ? 1.10777 0.81342 0.87520 -0.05187 -0.01514 0.21633  90  GLU A OE1 
682  O OE2 . GLU A 90  ? 1.04282 0.79254 0.85687 -0.04014 -0.02797 0.19943  90  GLU A OE2 
683  N N   . ASP A 91  ? 0.92752 0.70818 0.71220 -0.09352 0.03372  0.15819  91  ASP A N   
684  C CA  . ASP A 91  ? 0.95086 0.74494 0.72499 -0.09765 0.03741  0.14895  91  ASP A CA  
685  C C   . ASP A 91  ? 0.91392 0.72732 0.71691 -0.09930 0.04759  0.13442  91  ASP A C   
686  O O   . ASP A 91  ? 0.93981 0.75538 0.74410 -0.10695 0.06296  0.13033  91  ASP A O   
687  C CB  . ASP A 91  ? 0.90369 0.68387 0.64199 -0.10698 0.04736  0.15478  91  ASP A CB  
688  C CG  . ASP A 91  ? 1.00305 0.79489 0.72848 -0.11109 0.05343  0.14394  91  ASP A CG  
689  O OD1 . ASP A 91  ? 0.90927 0.71773 0.65169 -0.10661 0.04847  0.13276  91  ASP A OD1 
690  O OD2 . ASP A 91  ? 1.01267 0.79528 0.70924 -0.11898 0.06399  0.14665  91  ASP A OD2 
691  N N   . CYS A 92  ? 0.89057 0.71939 0.71740 -0.09198 0.03887  0.12688  92  CYS A N   
692  C CA  . CYS A 92  ? 0.86018 0.70557 0.71507 -0.09206 0.04682  0.11506  92  CYS A CA  
693  C C   . CYS A 92  ? 0.83556 0.69699 0.70034 -0.08773 0.04163  0.10480  92  CYS A C   
694  O O   . CYS A 92  ? 0.84566 0.72056 0.73426 -0.08585 0.04577  0.09602  92  CYS A O   
695  C CB  . CYS A 92  ? 0.80050 0.64551 0.68043 -0.08836 0.04477  0.11639  92  CYS A CB  
696  S SG  . CYS A 92  ? 0.86403 0.70990 0.75472 -0.07686 0.02668  0.12071  92  CYS A SG  
697  N N   . LEU A 93  ? 0.85020 0.70984 0.69633 -0.08681 0.03277  0.10551  93  LEU A N   
698  C CA  . LEU A 93  ? 0.75641 0.62838 0.61203 -0.08357 0.02649  0.09637  93  LEU A CA  
699  C C   . LEU A 93  ? 0.85809 0.73297 0.70444 -0.08756 0.03799  0.08630  93  LEU A C   
700  O O   . LEU A 93  ? 0.86926 0.73840 0.69067 -0.09077 0.03711  0.08417  93  LEU A O   
701  C CB  . LEU A 93  ? 0.79709 0.66718 0.64026 -0.08143 0.01025  0.10131  93  LEU A CB  
702  C CG  . LEU A 93  ? 0.89971 0.77035 0.75887 -0.07472 -0.00041 0.11018  93  LEU A CG  
703  C CD1 . LEU A 93  ? 0.87363 0.74822 0.72647 -0.07147 -0.01795 0.11499  93  LEU A CD1 
704  C CD2 . LEU A 93  ? 0.84802 0.73055 0.74053 -0.07033 0.00255  0.10389  93  LEU A CD2 
705  N N   . TYR A 94  ? 0.86361 0.74784 0.73058 -0.08683 0.04891  0.07959  94  TYR A N   
706  C CA  . TYR A 94  ? 0.80523 0.69435 0.66918 -0.08823 0.06117  0.06981  94  TYR A CA  
707  C C   . TYR A 94  ? 0.83667 0.73936 0.72901 -0.08258 0.06210  0.06160  94  TYR A C   
708  O O   . TYR A 94  ? 0.82684 0.73548 0.74044 -0.07916 0.05576  0.06366  94  TYR A O   
709  C CB  . TYR A 94  ? 0.82841 0.71651 0.68596 -0.09377 0.07668  0.07125  94  TYR A CB  
710  C CG  . TYR A 94  ? 0.88860 0.76103 0.71628 -0.09992 0.07677  0.08121  94  TYR A CG  
711  C CD1 . TYR A 94  ? 0.82412 0.68750 0.65193 -0.10074 0.06995  0.09259  94  TYR A CD1 
712  C CD2 . TYR A 94  ? 0.85312 0.71807 0.65068 -0.10442 0.08401  0.07942  94  TYR A CD2 
713  C CE1 . TYR A 94  ? 0.88813 0.73512 0.68722 -0.10554 0.06946  0.10310  94  TYR A CE1 
714  C CE2 . TYR A 94  ? 0.85965 0.70927 0.62685 -0.11020 0.08391  0.08953  94  TYR A CE2 
715  C CZ  . TYR A 94  ? 0.93451 0.77502 0.70273 -0.11058 0.07621  0.10195  94  TYR A CZ  
716  O OH  . TYR A 94  ? 0.91537 0.73861 0.65217 -0.11547 0.07539  0.11342  94  TYR A OH  
717  N N   . LEU A 95  ? 0.80881 0.71534 0.70010 -0.08103 0.07046  0.05235  95  LEU A N   
718  C CA  . LEU A 95  ? 0.80449 0.72228 0.71990 -0.07485 0.07194  0.04523  95  LEU A CA  
719  C C   . LEU A 95  ? 0.82552 0.75056 0.74444 -0.07302 0.08694  0.03778  95  LEU A C   
720  O O   . LEU A 95  ? 0.77613 0.69677 0.67669 -0.07677 0.09672  0.03660  95  LEU A O   
721  C CB  . LEU A 95  ? 0.75906 0.67244 0.67218 -0.07194 0.06196  0.04138  95  LEU A CB  
722  C CG  . LEU A 95  ? 0.85690 0.75766 0.74217 -0.07495 0.06188  0.03670  95  LEU A CG  
723  C CD1 . LEU A 95  ? 0.82331 0.72290 0.70504 -0.07161 0.07480  0.02668  95  LEU A CD1 
724  C CD2 . LEU A 95  ? 0.81753 0.71373 0.70046 -0.07569 0.04785  0.03606  95  LEU A CD2 
725  N N   . ASN A 96  ? 0.77475 0.71180 0.71748 -0.06655 0.08878  0.03286  96  ASN A N   
726  C CA  . ASN A 96  ? 0.78996 0.73822 0.74283 -0.06228 0.10171  0.02607  96  ASN A CA  
727  C C   . ASN A 96  ? 0.78207 0.72868 0.73984 -0.05350 0.10065  0.01880  96  ASN A C   
728  O O   . ASN A 96  ? 0.77757 0.72014 0.74087 -0.05096 0.09009  0.01971  96  ASN A O   
729  C CB  . ASN A 96  ? 0.77819 0.74523 0.75783 -0.06237 0.10533  0.02786  96  ASN A CB  
730  C CG  . ASN A 96  ? 0.83021 0.79443 0.80742 -0.07116 0.10298  0.03604  96  ASN A CG  
731  O OD1 . ASN A 96  ? 0.79042 0.74955 0.75238 -0.07816 0.11053  0.03911  96  ASN A OD1 
732  N ND2 . ASN A 96  ? 0.75094 0.71632 0.74139 -0.07064 0.09293  0.03973  96  ASN A ND2 
733  N N   . VAL A 97  ? 0.80566 0.75446 0.76096 -0.04871 0.11248  0.01167  97  VAL A N   
734  C CA  . VAL A 97  ? 0.79340 0.73718 0.75151 -0.03923 0.11333  0.00463  97  VAL A CA  
735  C C   . VAL A 97  ? 0.82573 0.78733 0.80378 -0.03058 0.12531  -0.00002 97  VAL A C   
736  O O   . VAL A 97  ? 0.78826 0.75773 0.76334 -0.03236 0.13786  -0.00234 97  VAL A O   
737  C CB  . VAL A 97  ? 0.76955 0.69125 0.69779 -0.04077 0.11497  -0.00121 97  VAL A CB  
738  C CG1 . VAL A 97  ? 0.81668 0.72870 0.74744 -0.03150 0.11505  -0.00799 97  VAL A CG1 
739  C CG2 . VAL A 97  ? 0.80420 0.71226 0.71310 -0.05034 0.10216  0.00380  97  VAL A CG2 
740  N N   . TRP A 98  ? 0.76561 0.73505 0.76439 -0.02126 0.12148  -0.00085 98  TRP A N   
741  C CA  . TRP A 98  ? 0.76218 0.74932 0.78144 -0.01041 0.13080  -0.00525 98  TRP A CA  
742  C C   . TRP A 98  ? 0.80824 0.77931 0.82095 0.00093  0.13167  -0.01097 98  TRP A C   
743  O O   . TRP A 98  ? 0.83215 0.79257 0.84566 0.00360  0.12127  -0.00865 98  TRP A O   
744  C CB  . TRP A 98  ? 0.74302 0.75321 0.79180 -0.00771 0.12485  -0.00098 98  TRP A CB  
745  C CG  . TRP A 98  ? 0.77324 0.80113 0.83296 -0.01798 0.12599  0.00321  98  TRP A CG  
746  C CD1 . TRP A 98  ? 0.79326 0.84482 0.86993 -0.01895 0.13625  0.00146  98  TRP A CD1 
747  C CD2 . TRP A 98  ? 0.74790 0.77100 0.80382 -0.02867 0.11686  0.00968  98  TRP A CD2 
748  N NE1 . TRP A 98  ? 0.76006 0.81938 0.84183 -0.03097 0.13414  0.00635  98  TRP A NE1 
749  C CE2 . TRP A 98  ? 0.73846 0.77944 0.80719 -0.03624 0.12237  0.01143  98  TRP A CE2 
750  C CE3 . TRP A 98  ? 0.73332 0.73918 0.77710 -0.03244 0.10517  0.01395  98  TRP A CE3 
751  C CZ2 . TRP A 98  ? 0.67799 0.71618 0.74569 -0.04682 0.11657  0.01726  98  TRP A CZ2 
752  C CZ3 . TRP A 98  ? 0.75078 0.75688 0.79551 -0.04161 0.09943  0.01982  98  TRP A CZ3 
753  C CH2 . TRP A 98  ? 0.74647 0.76665 0.80195 -0.04834 0.10519  0.02135  98  TRP A CH2 
754  N N   . ILE A 99  ? 0.77549 0.74287 0.78034 0.00724  0.14472  -0.01848 99  ILE A N   
755  C CA  . ILE A 99  ? 0.87392 0.82225 0.87126 0.01881  0.14672  -0.02460 99  ILE A CA  
756  C C   . ILE A 99  ? 0.93692 0.90440 0.95791 0.03451  0.15670  -0.02830 99  ILE A C   
757  O O   . ILE A 99  ? 0.86087 0.85251 0.89521 0.03465  0.16716  -0.02971 99  ILE A O   
758  C CB  . ILE A 99  ? 0.88192 0.80242 0.84527 0.01424  0.15230  -0.03181 99  ILE A CB  
759  C CG1 . ILE A 99  ? 0.95311 0.88096 0.91001 0.01633  0.16979  -0.03872 99  ILE A CG1 
760  C CG2 . ILE A 99  ? 0.83671 0.74530 0.77947 -0.00179 0.14184  -0.02722 99  ILE A CG2 
761  C CD1 . ILE A 99  ? 0.94865 0.84790 0.87602 0.01944  0.17817  -0.04930 99  ILE A CD1 
762  N N   . PRO A 100 ? 0.94001 0.89890 0.96828 0.04792  0.15343  -0.02912 100 PRO A N   
763  C CA  . PRO A 100 ? 0.88004 0.85720 0.93160 0.06533  0.16177  -0.03209 100 PRO A CA  
764  C C   . PRO A 100 ? 0.90487 0.87571 0.94549 0.07212  0.17919  -0.04219 100 PRO A C   
765  O O   . PRO A 100 ? 0.90261 0.84564 0.91291 0.06625  0.18351  -0.04798 100 PRO A O   
766  C CB  . PRO A 100 ? 0.90547 0.86546 0.95922 0.07715  0.15280  -0.02947 100 PRO A CB  
767  C CG  . PRO A 100 ? 0.86216 0.80634 0.90276 0.06348  0.13838  -0.02311 100 PRO A CG  
768  C CD  . PRO A 100 ? 0.86509 0.79991 0.88337 0.04732  0.14079  -0.02569 100 PRO A CD  
769  N N   . ALA A 101 ? 0.89181 0.89091 0.95805 0.08434  0.18940  -0.04468 101 ALA A N   
770  C CA  . ALA A 101 ? 0.93226 0.92881 0.99340 0.09489  0.20744  -0.05474 101 ALA A CA  
771  C C   . ALA A 101 ? 0.96607 0.96657 1.04786 0.11848  0.20949  -0.05655 101 ALA A C   
772  O O   . ALA A 101 ? 0.96895 0.99935 1.08271 0.12603  0.20294  -0.05041 101 ALA A O   
773  C CB  . ALA A 101 ? 0.92111 0.95083 0.99539 0.08870  0.22104  -0.05672 101 ALA A CB  
774  N N   . PRO A 102 ? 1.00044 0.97044 1.06425 0.13086  0.21769  -0.06468 102 PRO A N   
775  C CA  . PRO A 102 ? 1.02580 0.95890 1.04997 0.12228  0.22501  -0.07341 102 PRO A CA  
776  C C   . PRO A 102 ? 0.98215 0.88405 0.97963 0.10624  0.20963  -0.06919 102 PRO A C   
777  O O   . PRO A 102 ? 1.00030 0.89684 1.00613 0.10796  0.19543  -0.06146 102 PRO A O   
778  C CB  . PRO A 102 ? 0.96956 0.87930 0.98815 0.14341  0.23595  -0.08268 102 PRO A CB  
779  C CG  . PRO A 102 ? 1.01170 0.95649 1.07147 0.16392  0.23852  -0.07927 102 PRO A CG  
780  C CD  . PRO A 102 ? 1.00606 0.97659 1.08817 0.15577  0.22105  -0.06643 102 PRO A CD  
781  N N   . LYS A 103 ? 0.98322 0.86686 0.94916 0.09075  0.21280  -0.07415 103 LYS A N   
782  C CA  . LYS A 103 ? 0.96410 0.82115 0.90318 0.07380  0.19961  -0.07159 103 LYS A CA  
783  C C   . LYS A 103 ? 1.03815 0.86766 0.97416 0.08026  0.18943  -0.06995 103 LYS A C   
784  O O   . LYS A 103 ? 0.95956 0.76833 0.89094 0.09498  0.19712  -0.07690 103 LYS A O   
785  C CB  . LYS A 103 ? 1.03520 0.86882 0.93668 0.06350  0.20801  -0.08139 103 LYS A CB  
786  C CG  . LYS A 103 ? 1.10285 0.90906 0.97540 0.04638  0.19433  -0.08028 103 LYS A CG  
787  C CD  . LYS A 103 ? 1.20395 0.99380 1.03967 0.03507  0.20192  -0.08916 103 LYS A CD  
788  C CE  . LYS A 103 ? 1.26279 1.02178 1.06810 0.02027  0.18864  -0.09090 103 LYS A CE  
789  N NZ  . LYS A 103 ? 1.28454 1.00871 1.07882 0.02714  0.18801  -0.09874 103 LYS A NZ  
790  N N   . PRO A 104 ? 1.05030 0.87849 0.98921 0.07022  0.17312  -0.06069 104 PRO A N   
791  C CA  . PRO A 104 ? 0.99696 0.80034 0.93375 0.07522  0.16412  -0.05782 104 PRO A CA  
792  C C   . PRO A 104 ? 1.03054 0.79223 0.93242 0.06620  0.16359  -0.06576 104 PRO A C   
793  O O   . PRO A 104 ? 0.98524 0.73837 0.86366 0.05534  0.16809  -0.07304 104 PRO A O   
794  C CB  . PRO A 104 ? 0.90662 0.72777 0.85862 0.06551  0.14849  -0.04558 104 PRO A CB  
795  C CG  . PRO A 104 ? 0.92529 0.76286 0.87173 0.04959  0.14716  -0.04450 104 PRO A CG  
796  C CD  . PRO A 104 ? 0.93261 0.78130 0.87665 0.05403  0.16301  -0.05225 104 PRO A CD  
797  N N   . LYS A 105 ? 1.04854 0.78341 0.94614 0.07039  0.15789  -0.06423 105 LYS A N   
798  C CA  . LYS A 105 ? 1.05146 0.74496 0.91737 0.06089  0.15667  -0.07198 105 LYS A CA  
799  C C   . LYS A 105 ? 1.17326 0.86435 1.03225 0.04055  0.14115  -0.06552 105 LYS A C   
800  O O   . LYS A 105 ? 1.25658 0.94248 1.09526 0.02461  0.13828  -0.07008 105 LYS A O   
801  C CB  . LYS A 105 ? 1.12148 0.78263 0.98411 0.07614  0.16096  -0.07474 105 LYS A CB  
802  C CG  . LYS A 105 ? 1.10654 0.75842 0.96541 0.09441  0.17815  -0.08571 105 LYS A CG  
803  C CD  . LYS A 105 ? 1.15987 0.79218 0.98636 0.08335  0.18628  -0.09966 105 LYS A CD  
804  C CE  . LYS A 105 ? 1.24286 0.87410 1.06712 0.10050  0.20537  -0.11100 105 LYS A CE  
805  N NZ  . LYS A 105 ? 1.21682 0.81684 1.04088 0.12021  0.21190  -0.11489 105 LYS A NZ  
806  N N   . ASN A 106 ? 1.12410 0.82067 0.99997 0.04109  0.13095  -0.05465 106 ASN A N   
807  C CA  . ASN A 106 ? 1.08227 0.78213 0.95617 0.02290  0.11720  -0.04803 106 ASN A CA  
808  C C   . ASN A 106 ? 0.99302 0.72258 0.89508 0.02625  0.10935  -0.03512 106 ASN A C   
809  O O   . ASN A 106 ? 1.03325 0.75529 0.94134 0.02674  0.10289  -0.02815 106 ASN A O   
810  C CB  . ASN A 106 ? 1.20155 0.86402 1.05560 0.01350  0.11260  -0.05103 106 ASN A CB  
811  C CG  . ASN A 106 ? 1.28520 0.94465 1.12163 -0.00782 0.10484  -0.05455 106 ASN A CG  
812  O OD1 . ASN A 106 ? 1.29730 0.97955 1.13435 -0.01267 0.10420  -0.05472 106 ASN A OD1 
813  N ND2 . ASN A 106 ? 1.49224 1.12633 1.31374 -0.02112 0.09853  -0.05679 106 ASN A ND2 
814  N N   . ALA A 107 ? 0.96195 0.72491 0.87938 0.02693  0.11011  -0.03213 107 ALA A N   
815  C CA  . ALA A 107 ? 0.89150 0.68431 0.83554 0.03138  0.10443  -0.02192 107 ALA A CA  
816  C C   . ALA A 107 ? 0.88988 0.69167 0.83671 0.01661  0.09232  -0.01462 107 ALA A C   
817  O O   . ALA A 107 ? 0.85798 0.66025 0.79349 0.00303  0.08886  -0.01642 107 ALA A O   
818  C CB  . ALA A 107 ? 0.76619 0.58990 0.72554 0.03677  0.11104  -0.02259 107 ALA A CB  
819  N N   . THR A 108 ? 0.84530 0.65509 0.80717 0.02016  0.08596  -0.00620 108 THR A N   
820  C CA  . THR A 108 ? 0.78075 0.60495 0.74995 0.00877  0.07604  0.00089  108 THR A CA  
821  C C   . THR A 108 ? 0.85265 0.70382 0.83109 0.00436  0.07571  0.00170  108 THR A C   
822  O O   . THR A 108 ? 0.82642 0.69490 0.81655 0.01280  0.08151  0.00078  108 THR A O   
823  C CB  . THR A 108 ? 0.77746 0.60910 0.76140 0.01539  0.07123  0.00931  108 THR A CB  
824  O OG1 . THR A 108 ? 0.79135 0.59472 0.76372 0.01584  0.07052  0.01027  108 THR A OG1 
825  C CG2 . THR A 108 ? 0.81317 0.66466 0.80735 0.00576  0.06298  0.01570  108 THR A CG2 
826  N N   . VAL A 109 ? 0.76599 0.62104 0.74009 -0.00893 0.06885  0.00384  109 VAL A N   
827  C CA  . VAL A 109 ? 0.80332 0.67879 0.78287 -0.01440 0.06771  0.00561  109 VAL A CA  
828  C C   . VAL A 109 ? 0.77220 0.66617 0.76917 -0.01626 0.06048  0.01328  109 VAL A C   
829  O O   . VAL A 109 ? 0.75180 0.64109 0.75022 -0.01985 0.05418  0.01694  109 VAL A O   
830  C CB  . VAL A 109 ? 0.82186 0.68798 0.78258 -0.02651 0.06484  0.00273  109 VAL A CB  
831  C CG1 . VAL A 109 ? 0.73579 0.61977 0.70006 -0.03093 0.06427  0.00572  109 VAL A CG1 
832  C CG2 . VAL A 109 ? 0.81925 0.66407 0.75906 -0.02536 0.07224  -0.00629 109 VAL A CG2 
833  N N   A LEU A 110 ? 0.74466 0.65920 0.75439 -0.01446 0.06213  0.01524  110 LEU A N   
834  N N   B LEU A 110 ? 0.74371 0.65822 0.75339 -0.01443 0.06219  0.01521  110 LEU A N   
835  C CA  A LEU A 110 ? 0.72825 0.65903 0.75227 -0.01708 0.05597  0.02109  110 LEU A CA  
836  C CA  B LEU A 110 ? 0.70190 0.63305 0.72607 -0.01695 0.05620  0.02100  110 LEU A CA  
837  C C   A LEU A 110 ? 0.73760 0.67650 0.75987 -0.02492 0.05506  0.02234  110 LEU A C   
838  C C   B LEU A 110 ? 0.73446 0.67280 0.75601 -0.02511 0.05513  0.02221  110 LEU A C   
839  O O   A LEU A 110 ? 0.71718 0.66187 0.73846 -0.02452 0.06145  0.02014  110 LEU A O   
840  O O   B LEU A 110 ? 0.71954 0.66239 0.73860 -0.02509 0.06150  0.01985  110 LEU A O   
841  C CB  A LEU A 110 ? 0.71643 0.66340 0.75792 -0.00811 0.05760  0.02259  110 LEU A CB  
842  C CB  B LEU A 110 ? 0.71450 0.66278 0.75632 -0.00813 0.05832  0.02224  110 LEU A CB  
843  C CG  A LEU A 110 ? 0.74398 0.68593 0.78891 -0.00311 0.05319  0.02597  110 LEU A CG  
844  C CG  B LEU A 110 ? 0.74116 0.68708 0.78887 -0.00026 0.05545  0.02486  110 LEU A CG  
845  C CD1 A LEU A 110 ? 0.71938 0.66570 0.77229 0.00971  0.05673  0.02530  110 LEU A CD1 
846  C CD1 B LEU A 110 ? 0.70781 0.63105 0.74271 0.00444  0.05845  0.02229  110 LEU A CD1 
847  C CD2 A LEU A 110 ? 0.64088 0.59465 0.69488 -0.00740 0.04664  0.03077  110 LEU A CD2 
848  C CD2 B LEU A 110 ? 0.70260 0.66860 0.76719 0.00848  0.05691  0.02538  110 LEU A CD2 
849  N N   . ILE A 111 ? 0.74641 0.68566 0.76850 -0.03165 0.04764  0.02627  111 ILE A N   
850  C CA  . ILE A 111 ? 0.75684 0.70020 0.77551 -0.03829 0.04528  0.02880  111 ILE A CA  
851  C C   . ILE A 111 ? 0.67973 0.63636 0.71378 -0.03828 0.04186  0.03316  111 ILE A C   
852  O O   . ILE A 111 ? 0.72692 0.68547 0.76780 -0.03815 0.03661  0.03552  111 ILE A O   
853  C CB  . ILE A 111 ? 0.73320 0.66615 0.73855 -0.04536 0.03886  0.02952  111 ILE A CB  
854  C CG1 . ILE A 111 ? 0.67200 0.58961 0.65902 -0.04651 0.04263  0.02367  111 ILE A CG1 
855  C CG2 . ILE A 111 ? 0.59656 0.53437 0.59968 -0.05022 0.03506  0.03396  111 ILE A CG2 
856  C CD1 . ILE A 111 ? 0.67720 0.58484 0.64968 -0.05483 0.03536  0.02311  111 ILE A CD1 
857  N N   . TRP A 112 ? 0.63303 0.59780 0.67150 -0.03917 0.04556  0.03383  112 TRP A N   
858  C CA  . TRP A 112 ? 0.65694 0.63215 0.70865 -0.03971 0.04358  0.03649  112 TRP A CA  
859  C C   . TRP A 112 ? 0.65198 0.62308 0.69926 -0.04486 0.03921  0.04086  112 TRP A C   
860  O O   . TRP A 112 ? 0.64812 0.61283 0.68341 -0.04868 0.04072  0.04227  112 TRP A O   
861  C CB  . TRP A 112 ? 0.67893 0.66500 0.73901 -0.03906 0.05021  0.03447  112 TRP A CB  
862  C CG  . TRP A 112 ? 0.63892 0.63350 0.71058 -0.04171 0.04850  0.03606  112 TRP A CG  
863  C CD1 . TRP A 112 ? 0.64253 0.63660 0.71342 -0.04761 0.05092  0.03783  112 TRP A CD1 
864  C CD2 . TRP A 112 ? 0.61899 0.62165 0.70254 -0.03890 0.04451  0.03551  112 TRP A CD2 
865  N NE1 . TRP A 112 ? 0.67225 0.67264 0.75447 -0.04893 0.04872  0.03761  112 TRP A NE1 
866  C CE2 . TRP A 112 ? 0.59504 0.60158 0.68470 -0.04356 0.04467  0.03583  112 TRP A CE2 
867  C CE3 . TRP A 112 ? 0.62570 0.63105 0.71324 -0.03328 0.04112  0.03489  112 TRP A CE3 
868  C CZ2 . TRP A 112 ? 0.57923 0.59272 0.67838 -0.04289 0.04137  0.03438  112 TRP A CZ2 
869  C CZ3 . TRP A 112 ? 0.62670 0.64004 0.72311 -0.03235 0.03786  0.03448  112 TRP A CZ3 
870  C CH2 . TRP A 112 ? 0.58071 0.59839 0.68269 -0.03718 0.03792  0.03362  112 TRP A CH2 
871  N N   . ILE A 113 ? 0.68890 0.66347 0.74522 -0.04423 0.03423  0.04317  113 ILE A N   
872  C CA  . ILE A 113 ? 0.66764 0.63892 0.72296 -0.04670 0.03003  0.04759  113 ILE A CA  
873  C C   . ILE A 113 ? 0.68006 0.65650 0.74655 -0.04626 0.03157  0.04737  113 ILE A C   
874  O O   . ILE A 113 ? 0.68533 0.66803 0.76145 -0.04339 0.03023  0.04552  113 ILE A O   
875  C CB  . ILE A 113 ? 0.67621 0.64679 0.73257 -0.04596 0.02299  0.04981  113 ILE A CB  
876  C CG1 . ILE A 113 ? 0.56253 0.52710 0.60671 -0.04847 0.02081  0.04903  113 ILE A CG1 
877  C CG2 . ILE A 113 ? 0.57531 0.54444 0.63383 -0.04592 0.01845  0.05468  113 ILE A CG2 
878  C CD1 . ILE A 113 ? 0.60400 0.57092 0.65174 -0.04951 0.01384  0.05053  113 ILE A CD1 
879  N N   . TYR A 114 ? 0.64827 0.62086 0.71187 -0.04992 0.03473  0.04901  114 TYR A N   
880  C CA  . TYR A 114 ? 0.62935 0.60477 0.70223 -0.05148 0.03684  0.04761  114 TYR A CA  
881  C C   . TYR A 114 ? 0.70475 0.67480 0.78118 -0.04935 0.03225  0.04992  114 TYR A C   
882  O O   . TYR A 114 ? 0.66938 0.63383 0.74131 -0.04715 0.02764  0.05419  114 TYR A O   
883  C CB  . TYR A 114 ? 0.69713 0.66837 0.76542 -0.05773 0.04275  0.04877  114 TYR A CB  
884  C CG  . TYR A 114 ? 0.69820 0.65505 0.75185 -0.06024 0.04184  0.05533  114 TYR A CG  
885  C CD1 . TYR A 114 ? 0.61881 0.56479 0.67087 -0.05908 0.03745  0.06010  114 TYR A CD1 
886  C CD2 . TYR A 114 ? 0.73321 0.68680 0.77347 -0.06308 0.04550  0.05685  114 TYR A CD2 
887  C CE1 . TYR A 114 ? 0.71965 0.65235 0.75735 -0.06023 0.03544  0.06736  114 TYR A CE1 
888  C CE2 . TYR A 114 ? 0.68359 0.62371 0.70736 -0.06551 0.04392  0.06354  114 TYR A CE2 
889  C CZ  . TYR A 114 ? 0.69388 0.62390 0.71656 -0.06389 0.03829  0.06931  114 TYR A CZ  
890  O OH  . TYR A 114 ? 0.71535 0.63222 0.72085 -0.06517 0.03557  0.07698  114 TYR A OH  
891  N N   . GLY A 115 ? 0.64014 0.61262 0.72498 -0.04992 0.03356  0.04660  115 GLY A N   
892  C CA  . GLY A 115 ? 0.67272 0.63871 0.76085 -0.04748 0.03118  0.04727  115 GLY A CA  
893  C C   . GLY A 115 ? 0.72406 0.67733 0.80916 -0.05195 0.03400  0.04862  115 GLY A C   
894  O O   . GLY A 115 ? 0.69457 0.64363 0.77369 -0.05770 0.03766  0.05058  115 GLY A O   
895  N N   . GLY A 116 ? 0.72443 0.67038 0.81307 -0.04943 0.03314  0.04733  116 GLY A N   
896  C CA  . GLY A 116 ? 0.75655 0.68497 0.84082 -0.05259 0.03541  0.04934  116 GLY A CA  
897  C C   . GLY A 116 ? 0.83409 0.75049 0.91797 -0.04468 0.03219  0.05327  116 GLY A C   
898  O O   . GLY A 116 ? 0.85946 0.75837 0.93609 -0.04462 0.03232  0.05915  116 GLY A O   
899  N N   . GLY A 117 ? 0.78125 0.70707 0.87300 -0.03752 0.02965  0.05059  117 GLY A N   
900  C CA  . GLY A 117 ? 0.81903 0.73739 0.91427 -0.02862 0.02748  0.05315  117 GLY A CA  
901  C C   . GLY A 117 ? 0.78766 0.70358 0.88006 -0.02332 0.02200  0.06252  117 GLY A C   
902  O O   . GLY A 117 ? 0.77022 0.67749 0.86539 -0.01536 0.02002  0.06609  117 GLY A O   
903  N N   . PHE A 118 ? 0.64746 0.57094 0.73414 -0.02697 0.01915  0.06629  118 PHE A N   
904  C CA  . PHE A 118 ? 0.73758 0.65761 0.81717 -0.02438 0.01312  0.07514  118 PHE A CA  
905  C C   . PHE A 118 ? 0.73120 0.62923 0.79944 -0.02470 0.01362  0.08204  118 PHE A C   
906  O O   . PHE A 118 ? 0.67749 0.57035 0.73877 -0.02077 0.00759  0.09057  118 PHE A O   
907  C CB  . PHE A 118 ? 0.65957 0.59063 0.74997 -0.01526 0.00671  0.07772  118 PHE A CB  
908  C CG  . PHE A 118 ? 0.65673 0.60778 0.75628 -0.01624 0.00614  0.07270  118 PHE A CG  
909  C CD1 . PHE A 118 ? 0.61106 0.57005 0.70458 -0.02161 0.00325  0.07339  118 PHE A CD1 
910  C CD2 . PHE A 118 ? 0.65400 0.61369 0.76624 -0.01226 0.00932  0.06709  118 PHE A CD2 
911  C CE1 . PHE A 118 ? 0.62270 0.59648 0.72333 -0.02316 0.00326  0.06916  118 PHE A CE1 
912  C CE2 . PHE A 118 ? 0.60908 0.58487 0.72782 -0.01393 0.00957  0.06351  118 PHE A CE2 
913  C CZ  . PHE A 118 ? 0.57991 0.56215 0.69318 -0.01951 0.00635  0.06488  118 PHE A CZ  
914  N N   . GLN A 119 ? 0.68140 0.56580 0.74693 -0.02974 0.02023  0.07887  119 GLN A N   
915  C CA  . GLN A 119 ? 0.79610 0.65653 0.84909 -0.03193 0.02197  0.08579  119 GLN A CA  
916  C C   . GLN A 119 ? 0.80134 0.65689 0.84399 -0.04464 0.02854  0.08515  119 GLN A C   
917  O O   . GLN A 119 ? 0.80079 0.63744 0.82962 -0.04838 0.03034  0.09260  119 GLN A O   
918  C CB  . GLN A 119 ? 0.68718 0.52962 0.74449 -0.02770 0.02496  0.08346  119 GLN A CB  
919  C CG  . GLN A 119 ? 0.81339 0.66469 0.88537 -0.01610 0.02234  0.07938  119 GLN A CG  
920  C CD  . GLN A 119 ? 0.84403 0.70066 0.91923 -0.00445 0.01404  0.08804  119 GLN A CD  
921  O OE1 . GLN A 119 ? 0.87568 0.71458 0.94314 0.00096  0.01085  0.09720  119 GLN A OE1 
922  N NE2 . GLN A 119 ? 0.74485 0.62618 0.83147 -0.00096 0.01016  0.08557  119 GLN A NE2 
923  N N   . THR A 120 ? 0.78604 0.65833 0.83536 -0.05106 0.03250  0.07689  120 THR A N   
924  C CA  . THR A 120 ? 0.83467 0.70683 0.87870 -0.06275 0.03968  0.07509  120 THR A CA  
925  C C   . THR A 120 ? 0.77317 0.66789 0.82114 -0.06446 0.04021  0.07058  120 THR A C   
926  O O   . THR A 120 ? 0.71445 0.62160 0.76774 -0.05777 0.03510  0.06899  120 THR A O   
927  C CB  . THR A 120 ? 0.78684 0.65359 0.83781 -0.06993 0.04545  0.06800  120 THR A CB  
928  O OG1 . THR A 120 ? 0.84794 0.73340 0.91283 -0.06796 0.04437  0.05840  120 THR A OG1 
929  C CG2 . THR A 120 ? 0.67797 0.51896 0.72505 -0.06724 0.04539  0.07087  120 THR A CG2 
930  N N   . GLY A 121 ? 0.74170 0.64126 0.78753 -0.07356 0.04709  0.06848  121 GLY A N   
931  C CA  . GLY A 121 ? 0.71776 0.63749 0.76859 -0.07425 0.04889  0.06344  121 GLY A CA  
932  C C   . GLY A 121 ? 0.75579 0.67488 0.79324 -0.07832 0.05313  0.06733  121 GLY A C   
933  O O   . GLY A 121 ? 0.71733 0.62102 0.73891 -0.07918 0.05229  0.07524  121 GLY A O   
934  N N   . THR A 122 ? 0.69997 0.63544 0.74283 -0.08030 0.05793  0.06187  122 THR A N   
935  C CA  . THR A 122 ? 0.78489 0.72119 0.81485 -0.08292 0.06305  0.06374  122 THR A CA  
936  C C   . THR A 122 ? 0.74394 0.69984 0.78429 -0.08048 0.06648  0.05621  122 THR A C   
937  O O   . THR A 122 ? 0.72292 0.69260 0.78048 -0.08018 0.06725  0.05057  122 THR A O   
938  C CB  . THR A 122 ? 0.70148 0.62887 0.72207 -0.09297 0.07203  0.06778  122 THR A CB  
939  O OG1 . THR A 122 ? 0.76593 0.69320 0.77082 -0.09473 0.07731  0.06956  122 THR A OG1 
940  C CG2 . THR A 122 ? 0.65882 0.59938 0.69652 -0.10031 0.07939  0.06182  122 THR A CG2 
941  N N   . SER A 123 ? 0.72420 0.68029 0.75288 -0.07836 0.06817  0.05612  123 SER A N   
942  C CA  . SER A 123 ? 0.70367 0.67466 0.74037 -0.07397 0.07139  0.04932  123 SER A CA  
943  C C   . SER A 123 ? 0.74527 0.72959 0.78987 -0.07854 0.08259  0.04564  123 SER A C   
944  O O   . SER A 123 ? 0.73957 0.73889 0.79541 -0.07357 0.08547  0.03987  123 SER A O   
945  C CB  . SER A 123 ? 0.67335 0.63734 0.69364 -0.07031 0.06970  0.04926  123 SER A CB  
946  O OG  . SER A 123 ? 0.71443 0.66788 0.71459 -0.07577 0.07468  0.05311  123 SER A OG  
947  N N   . SER A 124 ? 0.70916 0.68864 0.74862 -0.08769 0.08924  0.04919  124 SER A N   
948  C CA  . SER A 124 ? 0.69572 0.69033 0.74378 -0.09336 0.10115  0.04578  124 SER A CA  
949  C C   . SER A 124 ? 0.72085 0.73404 0.79436 -0.09596 0.10118  0.04113  124 SER A C   
950  O O   . SER A 124 ? 0.74204 0.77236 0.82752 -0.10131 0.11039  0.03792  124 SER A O   
951  C CB  . SER A 124 ? 0.76664 0.74844 0.79768 -0.10392 0.10958  0.05188  124 SER A CB  
952  O OG  . SER A 124 ? 0.71879 0.68132 0.74178 -0.10853 0.10403  0.05882  124 SER A OG  
953  N N   . LEU A 125 ? 0.73712 0.74889 0.81922 -0.09267 0.09128  0.04027  125 LEU A N   
954  C CA  . LEU A 125 ? 0.64853 0.67636 0.75159 -0.09641 0.09013  0.03552  125 LEU A CA  
955  C C   . LEU A 125 ? 0.62999 0.68514 0.75142 -0.09104 0.09266  0.02922  125 LEU A C   
956  O O   . LEU A 125 ? 0.69538 0.75366 0.81473 -0.08060 0.09129  0.02792  125 LEU A O   
957  C CB  . LEU A 125 ? 0.66829 0.68828 0.77365 -0.09249 0.07933  0.03515  125 LEU A CB  
958  C CG  . LEU A 125 ? 0.70440 0.69956 0.79697 -0.09607 0.07592  0.04048  125 LEU A CG  
959  C CD1 . LEU A 125 ? 0.63051 0.62361 0.72961 -0.09158 0.06719  0.03769  125 LEU A CD1 
960  C CD2 . LEU A 125 ? 0.71920 0.70637 0.80959 -0.10912 0.08323  0.04263  125 LEU A CD2 
961  N N   . HIS A 126 ? 0.62650 0.70113 0.76646 -0.09842 0.09600  0.02532  126 HIS A N   
962  C CA  . HIS A 126 ? 0.61964 0.72444 0.78090 -0.09367 0.09814  0.01970  126 HIS A CA  
963  C C   . HIS A 126 ? 0.71966 0.83030 0.88630 -0.08030 0.08791  0.01756  126 HIS A C   
964  O O   . HIS A 126 ? 0.62266 0.74790 0.79730 -0.07019 0.08937  0.01533  126 HIS A O   
965  C CB  . HIS A 126 ? 0.74392 0.86853 0.92497 -0.10591 0.10041  0.01596  126 HIS A CB  
966  C CG  . HIS A 126 ? 0.79450 0.95459 1.00144 -0.10125 0.10019  0.01025  126 HIS A CG  
967  N ND1 . HIS A 126 ? 0.84566 1.02330 1.06948 -0.10283 0.09110  0.00588  126 HIS A ND1 
968  C CD2 . HIS A 126 ? 0.80167 0.98407 1.02103 -0.09502 0.10798  0.00810  126 HIS A CD2 
969  C CE1 . HIS A 126 ? 0.82463 1.03498 1.07081 -0.09718 0.09196  0.00210  126 HIS A CE1 
970  N NE2 . HIS A 126 ? 0.79623 1.01015 1.04121 -0.09176 0.10261  0.00330  126 HIS A NE2 
971  N N   . VAL A 127 ? 0.61135 0.70981 0.77306 -0.07969 0.07820  0.01838  127 VAL A N   
972  C CA  . VAL A 127 ? 0.66997 0.77275 0.83468 -0.06827 0.06920  0.01714  127 VAL A CA  
973  C C   . VAL A 127 ? 0.69304 0.77868 0.84199 -0.05862 0.06796  0.02050  127 VAL A C   
974  O O   . VAL A 127 ? 0.58628 0.67187 0.73513 -0.04969 0.06141  0.02048  127 VAL A O   
975  C CB  . VAL A 127 ? 0.68433 0.78240 0.84962 -0.07181 0.06059  0.01582  127 VAL A CB  
976  C CG1 . VAL A 127 ? 0.56676 0.68311 0.74806 -0.08230 0.06108  0.01103  127 VAL A CG1 
977  C CG2 . VAL A 127 ? 0.52616 0.59645 0.67428 -0.07548 0.05953  0.01973  127 VAL A CG2 
978  N N   . TYR A 128 ? 0.70151 0.77233 0.83604 -0.06096 0.07395  0.02342  128 TYR A N   
979  C CA  . TYR A 128 ? 0.68064 0.73638 0.80004 -0.05350 0.07281  0.02551  128 TYR A CA  
980  C C   . TYR A 128 ? 0.71438 0.77523 0.83196 -0.04910 0.08139  0.02333  128 TYR A C   
981  O O   . TYR A 128 ? 0.71808 0.76372 0.81969 -0.04560 0.08216  0.02427  128 TYR A O   
982  C CB  . TYR A 128 ? 0.71038 0.74359 0.81145 -0.05854 0.07112  0.03034  128 TYR A CB  
983  C CG  . TYR A 128 ? 0.71008 0.73505 0.81140 -0.06139 0.06378  0.03252  128 TYR A CG  
984  C CD1 . TYR A 128 ? 0.63854 0.67139 0.75029 -0.05745 0.05741  0.03009  128 TYR A CD1 
985  C CD2 . TYR A 128 ? 0.62425 0.63262 0.71406 -0.06724 0.06354  0.03714  128 TYR A CD2 
986  C CE1 . TYR A 128 ? 0.57709 0.60161 0.68789 -0.05951 0.05213  0.03108  128 TYR A CE1 
987  C CE2 . TYR A 128 ? 0.60373 0.60351 0.69414 -0.06819 0.05781  0.03869  128 TYR A CE2 
988  C CZ  . TYR A 128 ? 0.63344 0.64144 0.73451 -0.06453 0.05274  0.03507  128 TYR A CZ  
989  O OH  . TYR A 128 ? 0.66111 0.65965 0.76166 -0.06504 0.04842  0.03575  128 TYR A OH  
990  N N   . ASP A 129 ? 0.61419 0.69653 0.74781 -0.04967 0.08820  0.01991  129 ASP A N   
991  C CA  . ASP A 129 ? 0.64148 0.73067 0.77519 -0.04465 0.09830  0.01699  129 ASP A CA  
992  C C   . ASP A 129 ? 0.69081 0.77700 0.82366 -0.03067 0.09502  0.01516  129 ASP A C   
993  O O   . ASP A 129 ? 0.65603 0.75712 0.80496 -0.02304 0.09010  0.01390  129 ASP A O   
994  C CB  . ASP A 129 ? 0.63026 0.74799 0.78645 -0.04780 0.10577  0.01363  129 ASP A CB  
995  C CG  . ASP A 129 ? 0.69795 0.82177 0.85213 -0.04636 0.11980  0.01091  129 ASP A CG  
996  O OD1 . ASP A 129 ? 0.75025 0.85907 0.88865 -0.03849 0.12272  0.00986  129 ASP A OD1 
997  O OD2 . ASP A 129 ? 0.73302 0.87679 0.90129 -0.05365 0.12850  0.00928  129 ASP A OD2 
998  N N   . GLY A 130 ? 0.67871 0.74457 0.79155 -0.02764 0.09751  0.01510  130 GLY A N   
999  C CA  . GLY A 130 ? 0.64910 0.70631 0.75775 -0.01585 0.09519  0.01332  130 GLY A CA  
1000 C C   . GLY A 130 ? 0.76097 0.82945 0.87850 -0.00513 0.10428  0.00839  130 GLY A C   
1001 O O   . GLY A 130 ? 0.74582 0.80271 0.85763 0.00529  0.10327  0.00683  130 GLY A O   
1002 N N   . LYS A 131 ? 0.66487 0.75546 0.79697 -0.00712 0.11364  0.00583  131 LYS A N   
1003 C CA  . LYS A 131 ? 0.70639 0.80893 0.84783 0.00422  0.12386  0.00067  131 LYS A CA  
1004 C C   . LYS A 131 ? 0.74502 0.86183 0.90631 0.01867  0.11761  0.00048  131 LYS A C   
1005 O O   . LYS A 131 ? 0.74312 0.85779 0.90578 0.03244  0.12271  -0.00279 131 LYS A O   
1006 C CB  . LYS A 131 ? 0.70353 0.83004 0.85840 -0.00241 0.13614  -0.00178 131 LYS A CB  
1007 C CG  . LYS A 131 ? 0.71584 0.87308 0.89898 -0.00689 0.13196  -0.00062 131 LYS A CG  
1008 C CD  . LYS A 131 ? 0.79502 0.97015 0.98658 -0.01963 0.14365  -0.00177 131 LYS A CD  
1009 C CE  . LYS A 131 ? 0.71219 0.92486 0.93761 -0.02131 0.14197  -0.00321 131 LYS A CE  
1010 N NZ  . LYS A 131 ? 0.75059 0.97946 0.98442 -0.03709 0.15288  -0.00378 131 LYS A NZ  
1011 N N   . PHE A 132 ? 0.67262 0.80264 0.84786 0.01644  0.10661  0.00394  132 PHE A N   
1012 C CA  . PHE A 132 ? 0.63819 0.78205 0.83011 0.03036  0.09968  0.00473  132 PHE A CA  
1013 C C   . PHE A 132 ? 0.70280 0.81798 0.87679 0.03990  0.09415  0.00699  132 PHE A C   
1014 O O   . PHE A 132 ? 0.68880 0.80402 0.86796 0.05527  0.09489  0.00642  132 PHE A O   
1015 C CB  . PHE A 132 ? 0.72170 0.88566 0.92936 0.02422  0.08890  0.00733  132 PHE A CB  
1016 C CG  . PHE A 132 ? 0.71514 0.90800 0.94238 0.01357  0.09401  0.00468  132 PHE A CG  
1017 C CD1 . PHE A 132 ? 0.71606 0.90679 0.93975 -0.00294 0.09092  0.00585  132 PHE A CD1 
1018 C CD2 . PHE A 132 ? 0.60472 0.82600 0.85405 0.01981  0.10265  0.00090  132 PHE A CD2 
1019 C CE1 . PHE A 132 ? 0.71704 0.93113 0.95730 -0.01461 0.09621  0.00348  132 PHE A CE1 
1020 C CE2 . PHE A 132 ? 0.73347 0.98229 1.00173 0.00798  0.10820  -0.00158 132 PHE A CE2 
1021 C CZ  . PHE A 132 ? 0.71122 0.95530 0.97416 -0.01012 0.10491  -0.00021 132 PHE A CZ  
1022 N N   . LEU A 133 ? 0.71408 0.80420 0.86723 0.03089  0.08904  0.00970  133 LEU A N   
1023 C CA  . LEU A 133 ? 0.70169 0.76414 0.83744 0.03669  0.08425  0.01184  133 LEU A CA  
1024 C C   . LEU A 133 ? 0.76406 0.80836 0.88735 0.04462  0.09361  0.00738  133 LEU A C   
1025 O O   . LEU A 133 ? 0.78654 0.81715 0.90598 0.05656  0.09242  0.00781  133 LEU A O   
1026 C CB  . LEU A 133 ? 0.68185 0.72602 0.80083 0.02389  0.07816  0.01489  133 LEU A CB  
1027 C CG  . LEU A 133 ? 0.69150 0.74518 0.81850 0.02005  0.06769  0.01928  133 LEU A CG  
1028 C CD1 . LEU A 133 ? 0.69692 0.73882 0.81224 0.00717  0.06382  0.02144  133 LEU A CD1 
1029 C CD2 . LEU A 133 ? 0.73986 0.78489 0.86467 0.03026  0.06120  0.02272  133 LEU A CD2 
1030 N N   . ALA A 134 ? 0.76854 0.81053 0.88354 0.03805  0.10337  0.00303  134 ALA A N   
1031 C CA  . ALA A 134 ? 0.77766 0.80274 0.87916 0.04503  0.11359  -0.00282 134 ALA A CA  
1032 C C   . ALA A 134 ? 0.78869 0.82871 0.90871 0.06270  0.11959  -0.00567 134 ALA A C   
1033 O O   . ALA A 134 ? 0.70055 0.72107 0.81252 0.07492  0.12152  -0.00769 134 ALA A O   
1034 C CB  . ALA A 134 ? 0.71635 0.74099 0.80613 0.03419  0.12342  -0.00661 134 ALA A CB  
1035 N N   . ARG A 135 ? 0.75920 0.83412 0.90523 0.06432  0.12198  -0.00561 135 ARG A N   
1036 C CA  . ARG A 135 ? 0.72091 0.81709 0.88942 0.08155  0.12741  -0.00811 135 ARG A CA  
1037 C C   . ARG A 135 ? 0.73903 0.83010 0.91346 0.09613  0.11678  -0.00326 135 ARG A C   
1038 O O   . ARG A 135 ? 0.80200 0.88219 0.97584 0.11289  0.12100  -0.00516 135 ARG A O   
1039 C CB  . ARG A 135 ? 0.70850 0.84654 0.90558 0.07688  0.12982  -0.00840 135 ARG A CB  
1040 C CG  . ARG A 135 ? 0.79773 0.96618 1.02441 0.09460  0.13282  -0.01005 135 ARG A CG  
1041 C CD  . ARG A 135 ? 0.70814 0.87078 0.93193 0.10668  0.14892  -0.01714 135 ARG A CD  
1042 N NE  . ARG A 135 ? 0.88512 1.08048 1.14057 0.12485  0.15270  -0.01884 135 ARG A NE  
1043 C CZ  . ARG A 135 ? 0.89570 1.08235 1.15483 0.14657  0.15141  -0.01848 135 ARG A CZ  
1044 N NH1 . ARG A 135 ? 0.85179 0.99636 1.08426 0.15181  0.14652  -0.01646 135 ARG A NH1 
1045 N NH2 . ARG A 135 ? 0.83434 1.05543 1.12531 0.16341  0.15513  -0.01991 135 ARG A NH2 
1046 N N   . VAL A 136 ? 0.74170 0.83979 0.92101 0.09040  0.10340  0.00314  136 VAL A N   
1047 C CA  . VAL A 136 ? 0.67877 0.77883 0.86594 0.10366  0.09287  0.00884  136 VAL A CA  
1048 C C   . VAL A 136 ? 0.74494 0.80415 0.90681 0.10817  0.08980  0.01166  136 VAL A C   
1049 O O   . VAL A 136 ? 0.70065 0.75066 0.86361 0.12474  0.08804  0.01427  136 VAL A O   
1050 C CB  . VAL A 136 ? 0.73330 0.85507 0.93193 0.09453  0.08044  0.01377  136 VAL A CB  
1051 C CG1 . VAL A 136 ? 0.69836 0.81617 0.89709 0.10571  0.06830  0.02079  136 VAL A CG1 
1052 C CG2 . VAL A 136 ? 0.67842 0.84204 0.90532 0.09205  0.08300  0.01074  136 VAL A CG2 
1053 N N   . GLU A 137 ? 0.77249 0.80676 0.91181 0.09348  0.08869  0.01167  137 GLU A N   
1054 C CA  . GLU A 137 ? 0.77401 0.77249 0.89125 0.09426  0.08444  0.01487  137 GLU A CA  
1055 C C   . GLU A 137 ? 0.77407 0.74108 0.86891 0.09165  0.09336  0.00869  137 GLU A C   
1056 O O   . GLU A 137 ? 0.68835 0.62403 0.76462 0.09123  0.09076  0.01035  137 GLU A O   
1057 C CB  . GLU A 137 ? 0.73677 0.73160 0.84651 0.08000  0.07421  0.02033  137 GLU A CB  
1058 C CG  . GLU A 137 ? 0.67877 0.69449 0.80313 0.08429  0.06400  0.02680  137 GLU A CG  
1059 C CD  . GLU A 137 ? 0.80928 0.81317 0.93178 0.10075  0.05981  0.03237  137 GLU A CD  
1060 O OE1 . GLU A 137 ? 0.83219 0.80332 0.93694 0.10471  0.06273  0.03294  137 GLU A OE1 
1061 O OE2 . GLU A 137 ? 0.75112 0.77785 0.88915 0.10941  0.05307  0.03647  137 GLU A OE2 
1062 N N   . ARG A 138 ? 0.77752 0.75154 0.87233 0.08883  0.10392  0.00146  138 ARG A N   
1063 C CA  . ARG A 138 ? 0.77382 0.71942 0.84565 0.08641  0.11296  -0.00581 138 ARG A CA  
1064 C C   . ARG A 138 ? 0.79209 0.71444 0.84086 0.06923  0.10718  -0.00489 138 ARG A C   
1065 O O   . ARG A 138 ? 0.82548 0.71820 0.85210 0.06665  0.11063  -0.00974 138 ARG A O   
1066 C CB  . ARG A 138 ? 0.84203 0.76340 0.90724 0.10341  0.11782  -0.00849 138 ARG A CB  
1067 C CG  . ARG A 138 ? 0.96011 0.90269 1.04709 0.12298  0.12626  -0.01136 138 ARG A CG  
1068 C CD  . ARG A 138 ? 1.09116 1.04809 1.18017 0.12045  0.14014  -0.02018 138 ARG A CD  
1069 N NE  . ARG A 138 ? 1.22910 1.15264 1.29265 0.12216  0.15084  -0.02922 138 ARG A NE  
1070 C CZ  . ARG A 138 ? 1.15645 1.08483 1.21994 0.12879  0.16601  -0.03824 138 ARG A CZ  
1071 N NH1 . ARG A 138 ? 1.02789 0.99500 1.11827 0.13518  0.17312  -0.03914 138 ARG A NH1 
1072 N NH2 . ARG A 138 ? 1.13810 1.03235 1.17351 0.12785  0.17466  -0.04711 138 ARG A NH2 
1073 N N   . VAL A 139 ? 0.72589 0.66165 0.77989 0.05741  0.09833  0.00076  139 VAL A N   
1074 C CA  . VAL A 139 ? 0.79986 0.72118 0.83638 0.04122  0.09341  0.00147  139 VAL A CA  
1075 C C   . VAL A 139 ? 0.76331 0.69318 0.79426 0.03165  0.09938  -0.00255 139 VAL A C   
1076 O O   . VAL A 139 ? 0.72121 0.67339 0.76572 0.03455  0.10597  -0.00413 139 VAL A O   
1077 C CB  . VAL A 139 ? 0.79533 0.72620 0.83984 0.03429  0.08205  0.00927  139 VAL A CB  
1078 C CG1 . VAL A 139 ? 0.69573 0.60982 0.73666 0.03996  0.07642  0.01363  139 VAL A CG1 
1079 C CG2 . VAL A 139 ? 0.70896 0.67259 0.77645 0.03642  0.08087  0.01188  139 VAL A CG2 
1080 N N   . ILE A 140 ? 0.78934 0.70217 0.80012 0.01949  0.09674  -0.00371 140 ILE A N   
1081 C CA  . ILE A 140 ? 0.77626 0.69622 0.77944 0.00879  0.09947  -0.00478 140 ILE A CA  
1082 C C   . ILE A 140 ? 0.72025 0.65255 0.73157 -0.00069 0.08968  0.00254  140 ILE A C   
1083 O O   . ILE A 140 ? 0.82224 0.74604 0.83135 -0.00443 0.08050  0.00626  140 ILE A O   
1084 C CB  . ILE A 140 ? 0.78124 0.67647 0.75624 0.00154  0.10138  -0.01029 140 ILE A CB  
1085 C CG1 . ILE A 140 ? 0.79388 0.68056 0.76022 0.01030  0.11453  -0.01905 140 ILE A CG1 
1086 C CG2 . ILE A 140 ? 0.77439 0.67433 0.73892 -0.01179 0.09841  -0.00773 140 ILE A CG2 
1087 C CD1 . ILE A 140 ? 0.85315 0.70837 0.79316 0.00770  0.11519  -0.02585 140 ILE A CD1 
1088 N N   . VAL A 141 ? 0.75301 0.70447 0.77357 -0.00478 0.09246  0.00439  141 VAL A N   
1089 C CA  . VAL A 141 ? 0.76894 0.73098 0.79731 -0.01295 0.08468  0.01067  141 VAL A CA  
1090 C C   . VAL A 141 ? 0.71575 0.67144 0.72759 -0.02380 0.08512  0.01180  141 VAL A C   
1091 O O   . VAL A 141 ? 0.74651 0.70335 0.75024 -0.02550 0.09427  0.00888  141 VAL A O   
1092 C CB  . VAL A 141 ? 0.78318 0.77044 0.83522 -0.01008 0.08638  0.01243  141 VAL A CB  
1093 C CG1 . VAL A 141 ? 0.63350 0.62769 0.69189 -0.01835 0.07860  0.01792  141 VAL A CG1 
1094 C CG2 . VAL A 141 ? 0.73488 0.72955 0.80198 0.00212  0.08516  0.01177  141 VAL A CG2 
1095 N N   . VAL A 142 ? 0.70851 0.65811 0.71523 -0.03061 0.07545  0.01645  142 VAL A N   
1096 C CA  . VAL A 142 ? 0.74842 0.69227 0.74025 -0.03980 0.07317  0.01943  142 VAL A CA  
1097 C C   . VAL A 142 ? 0.78095 0.73363 0.78483 -0.04351 0.06601  0.02607  142 VAL A C   
1098 O O   . VAL A 142 ? 0.74106 0.69750 0.75728 -0.04086 0.05965  0.02780  142 VAL A O   
1099 C CB  . VAL A 142 ? 0.78112 0.70686 0.75236 -0.04404 0.06722  0.01802  142 VAL A CB  
1100 C CG1 . VAL A 142 ? 0.77523 0.69671 0.73039 -0.05247 0.06374  0.02202  142 VAL A CG1 
1101 C CG2 . VAL A 142 ? 0.79228 0.70512 0.75014 -0.04015 0.07435  0.01002  142 VAL A CG2 
1102 N N   . SER A 143 ? 0.70689 0.66122 0.70582 -0.04951 0.06784  0.02978  143 SER A N   
1103 C CA  . SER A 143 ? 0.67987 0.63721 0.68597 -0.05318 0.06139  0.03604  143 SER A CA  
1104 C C   . SER A 143 ? 0.74507 0.69232 0.73269 -0.05975 0.06001  0.04097  143 SER A C   
1105 O O   . SER A 143 ? 0.74684 0.68935 0.71907 -0.06270 0.06721  0.03972  143 SER A O   
1106 C CB  . SER A 143 ? 0.67248 0.64400 0.69734 -0.05294 0.06579  0.03623  143 SER A CB  
1107 O OG  . SER A 143 ? 0.72497 0.70042 0.74630 -0.05665 0.07605  0.03528  143 SER A OG  
1108 N N   . MET A 144 ? 0.72040 0.66432 0.70889 -0.06137 0.05096  0.04688  144 MET A N   
1109 C CA  . MET A 144 ? 0.74249 0.67617 0.71336 -0.06602 0.04731  0.05319  144 MET A CA  
1110 C C   . MET A 144 ? 0.77430 0.70745 0.75338 -0.06703 0.04469  0.05987  144 MET A C   
1111 O O   . MET A 144 ? 0.68976 0.62948 0.68716 -0.06386 0.04177  0.05942  144 MET A O   
1112 C CB  . MET A 144 ? 0.70900 0.63627 0.66818 -0.06630 0.03653  0.05440  144 MET A CB  
1113 C CG  . MET A 144 ? 0.66180 0.59332 0.63435 -0.06367 0.02561  0.05821  144 MET A CG  
1114 S SD  . MET A 144 ? 0.69715 0.64044 0.69686 -0.05838 0.02638  0.05467  144 MET A SD  
1115 C CE  . MET A 144 ? 0.55702 0.49969 0.55437 -0.05809 0.02340  0.04904  144 MET A CE  
1116 N N   . ASN A 145 ? 0.74313 0.66628 0.70631 -0.07149 0.04611  0.06612  145 ASN A N   
1117 C CA  . ASN A 145 ? 0.74192 0.65836 0.70773 -0.07174 0.04175  0.07383  145 ASN A CA  
1118 C C   . ASN A 145 ? 0.78270 0.69474 0.74329 -0.06803 0.02879  0.07914  145 ASN A C   
1119 O O   . ASN A 145 ? 0.79214 0.70094 0.73619 -0.06916 0.02392  0.07997  145 ASN A O   
1120 C CB  . ASN A 145 ? 0.76912 0.67454 0.71917 -0.07820 0.04913  0.07955  145 ASN A CB  
1121 C CG  . ASN A 145 ? 0.76854 0.68149 0.72963 -0.08281 0.06163  0.07507  145 ASN A CG  
1122 O OD1 . ASN A 145 ? 0.73877 0.66520 0.72044 -0.08020 0.06318  0.06838  145 ASN A OD1 
1123 N ND2 . ASN A 145 ? 0.74192 0.64729 0.68911 -0.09017 0.07059  0.07902  145 ASN A ND2 
1124 N N   . TYR A 146 ? 0.74136 0.65448 0.71666 -0.06359 0.02312  0.08212  146 TYR A N   
1125 C CA  . TYR A 146 ? 0.74614 0.65810 0.72045 -0.05903 0.01113  0.08783  146 TYR A CA  
1126 C C   . TYR A 146 ? 0.68459 0.58657 0.66200 -0.05578 0.00928  0.09543  146 TYR A C   
1127 O O   . TYR A 146 ? 0.73535 0.63406 0.72195 -0.05678 0.01629  0.09371  146 TYR A O   
1128 C CB  . TYR A 146 ? 0.71523 0.64094 0.70740 -0.05479 0.00555  0.08280  146 TYR A CB  
1129 C CG  . TYR A 146 ? 0.71643 0.64845 0.72970 -0.05156 0.00971  0.07876  146 TYR A CG  
1130 C CD1 . TYR A 146 ? 0.63619 0.56718 0.66097 -0.04614 0.00605  0.08229  146 TYR A CD1 
1131 C CD2 . TYR A 146 ? 0.66449 0.60320 0.68522 -0.05329 0.01720  0.07126  146 TYR A CD2 
1132 C CE1 . TYR A 146 ? 0.68084 0.61644 0.72183 -0.04378 0.01009  0.07764  146 TYR A CE1 
1133 C CE2 . TYR A 146 ? 0.65170 0.59655 0.68929 -0.05077 0.01993  0.06756  146 TYR A CE2 
1134 C CZ  . TYR A 146 ? 0.69106 0.63381 0.73761 -0.04662 0.01651  0.07040  146 TYR A CZ  
1135 O OH  . TYR A 146 ? 0.70846 0.65604 0.76877 -0.04459 0.01933  0.06592  146 TYR A OH  
1136 N N   . ARG A 147 ? 0.74878 0.64548 0.71826 -0.05180 -0.00061 0.10367  147 ARG A N   
1137 C CA  . ARG A 147 ? 0.72567 0.60912 0.69547 -0.04710 -0.00279 0.11213  147 ARG A CA  
1138 C C   . ARG A 147 ? 0.75060 0.63978 0.74489 -0.04037 -0.00290 0.10857  147 ARG A C   
1139 O O   . ARG A 147 ? 0.72880 0.63412 0.73872 -0.03661 -0.00697 0.10358  147 ARG A O   
1140 C CB  . ARG A 147 ? 0.76548 0.64430 0.72214 -0.04249 -0.01491 0.12227  147 ARG A CB  
1141 C CG  . ARG A 147 ? 0.84148 0.70704 0.76814 -0.04892 -0.01385 0.12850  147 ARG A CG  
1142 C CD  . ARG A 147 ? 0.83445 0.69896 0.74755 -0.04418 -0.02836 0.13806  147 ARG A CD  
1143 N NE  . ARG A 147 ? 0.80342 0.68597 0.71829 -0.04596 -0.03599 0.13187  147 ARG A NE  
1144 C CZ  . ARG A 147 ? 0.88099 0.77321 0.79541 -0.04177 -0.05078 0.13631  147 ARG A CZ  
1145 N NH1 . ARG A 147 ? 0.80485 0.69142 0.71682 -0.03352 -0.06063 0.14805  147 ARG A NH1 
1146 N NH2 . ARG A 147 ? 0.80973 0.71753 0.72633 -0.04601 -0.05615 0.12888  147 ARG A NH2 
1147 N N   . VAL A 148 ? 0.70649 0.58091 0.70260 -0.03955 0.00220  0.11102  148 VAL A N   
1148 C CA  . VAL A 148 ? 0.71973 0.59582 0.73556 -0.03402 0.00397  0.10648  148 VAL A CA  
1149 C C   . VAL A 148 ? 0.79738 0.65490 0.81127 -0.02640 0.00076  0.11486  148 VAL A C   
1150 O O   . VAL A 148 ? 0.75557 0.59686 0.75185 -0.02645 -0.00191 0.12487  148 VAL A O   
1151 C CB  . VAL A 148 ? 0.80259 0.67844 0.82453 -0.04135 0.01468  0.09795  148 VAL A CB  
1152 C CG1 . VAL A 148 ? 0.63180 0.52714 0.65949 -0.04553 0.01714  0.08958  148 VAL A CG1 
1153 C CG2 . VAL A 148 ? 0.66426 0.52151 0.67083 -0.04975 0.02182  0.10222  148 VAL A CG2 
1154 N N   . GLY A 149 ? 0.74628 0.60482 0.77724 -0.01934 0.00157  0.11068  149 GLY A N   
1155 C CA  . GLY A 149 ? 0.75037 0.58985 0.78096 -0.01025 -0.00070 0.11762  149 GLY A CA  
1156 C C   . GLY A 149 ? 0.80505 0.64923 0.83378 -0.00026 -0.01259 0.12760  149 GLY A C   
1157 O O   . GLY A 149 ? 0.80364 0.66947 0.83657 -0.00007 -0.01934 0.12680  149 GLY A O   
1158 N N   . ALA A 150 ? 0.81070 0.63363 0.83300 0.00814  -0.01565 0.13728  150 ALA A N   
1159 C CA  . ALA A 150 ? 0.83519 0.66364 0.85725 0.01949  -0.02842 0.14775  150 ALA A CA  
1160 C C   . ALA A 150 ? 0.86377 0.70054 0.86790 0.01216  -0.03535 0.15302  150 ALA A C   
1161 O O   . ALA A 150 ? 0.82078 0.67763 0.83063 0.01710  -0.04656 0.15569  150 ALA A O   
1162 C CB  . ALA A 150 ? 0.87868 0.67819 0.89243 0.02972  -0.03026 0.15888  150 ALA A CB  
1163 N N   . LEU A 151 ? 0.86161 0.68419 0.84408 -0.00032 -0.02841 0.15380  151 LEU A N   
1164 C CA  . LEU A 151 ? 0.83574 0.66297 0.79727 -0.00733 -0.03359 0.15828  151 LEU A CA  
1165 C C   . LEU A 151 ? 0.83860 0.69462 0.81070 -0.01131 -0.03683 0.14877  151 LEU A C   
1166 O O   . LEU A 151 ? 0.82997 0.69422 0.78905 -0.01397 -0.04509 0.15180  151 LEU A O   
1167 C CB  . LEU A 151 ? 0.83818 0.64611 0.77644 -0.02029 -0.02253 0.15944  151 LEU A CB  
1168 C CG  . LEU A 151 ? 0.90295 0.67798 0.82211 -0.01942 -0.01985 0.17177  151 LEU A CG  
1169 C CD1 . LEU A 151 ? 0.90362 0.66390 0.80549 -0.03449 -0.00599 0.17047  151 LEU A CD1 
1170 C CD2 . LEU A 151 ? 0.87533 0.64073 0.77452 -0.01174 -0.03280 0.18710  151 LEU A CD2 
1171 N N   . GLY A 152 ? 0.79812 0.66805 0.79202 -0.01193 -0.03085 0.13752  152 GLY A N   
1172 C CA  . GLY A 152 ? 0.75835 0.65225 0.76227 -0.01572 -0.03297 0.12895  152 GLY A CA  
1173 C C   . GLY A 152 ? 0.79229 0.70689 0.82130 -0.00702 -0.03968 0.12645  152 GLY A C   
1174 O O   . GLY A 152 ? 0.74644 0.68041 0.78230 -0.01057 -0.04340 0.12123  152 GLY A O   
1175 N N   . PHE A 153 ? 0.77197 0.68239 0.81497 0.00406  -0.04038 0.12965  153 PHE A N   
1176 C CA  . PHE A 153 ? 0.76819 0.70033 0.83737 0.01235  -0.04402 0.12610  153 PHE A CA  
1177 C C   . PHE A 153 ? 0.80947 0.73994 0.88920 0.02734  -0.05103 0.13445  153 PHE A C   
1178 O O   . PHE A 153 ? 0.83501 0.78310 0.93878 0.03564  -0.05173 0.13112  153 PHE A O   
1179 C CB  . PHE A 153 ? 0.70547 0.64122 0.78914 0.01060  -0.03267 0.11512  153 PHE A CB  
1180 C CG  . PHE A 153 ? 0.69385 0.63650 0.77243 -0.00145 -0.02720 0.10693  153 PHE A CG  
1181 C CD1 . PHE A 153 ? 0.65915 0.62355 0.74862 -0.00438 -0.02980 0.10193  153 PHE A CD1 
1182 C CD2 . PHE A 153 ? 0.71468 0.64181 0.77764 -0.00990 -0.01935 0.10468  153 PHE A CD2 
1183 C CE1 . PHE A 153 ? 0.70989 0.67767 0.79366 -0.01415 -0.02477 0.09496  153 PHE A CE1 
1184 C CE2 . PHE A 153 ? 0.67065 0.60477 0.73003 -0.01912 -0.01437 0.09740  153 PHE A CE2 
1185 C CZ  . PHE A 153 ? 0.69070 0.64364 0.75976 -0.02055 -0.01721 0.09270  153 PHE A CZ  
1186 N N   . LEU A 154 ? 0.75450 0.66451 0.81732 0.03174  -0.05573 0.14544  154 LEU A N   
1187 C CA  . LEU A 154 ? 0.86363 0.77388 0.93659 0.04782  -0.06463 0.15476  154 LEU A CA  
1188 C C   . LEU A 154 ? 0.88346 0.82764 0.97374 0.05179  -0.07729 0.15577  154 LEU A C   
1189 O O   . LEU A 154 ? 0.82768 0.78477 0.90870 0.04149  -0.08341 0.15479  154 LEU A O   
1190 C CB  . LEU A 154 ? 0.89576 0.77877 0.94317 0.05053  -0.06964 0.16821  154 LEU A CB  
1191 C CG  . LEU A 154 ? 0.89209 0.77024 0.94676 0.06896  -0.07939 0.17995  154 LEU A CG  
1192 C CD1 . LEU A 154 ? 0.93826 0.78420 0.99108 0.07573  -0.06888 0.18080  154 LEU A CD1 
1193 C CD2 . LEU A 154 ? 0.91793 0.78825 0.94833 0.06972  -0.09244 0.19420  154 LEU A CD2 
1194 N N   . ALA A 155 ? 0.81599 0.77547 0.93234 0.06619  -0.08065 0.15683  155 ALA A N   
1195 C CA  . ALA A 155 ? 0.89640 0.89334 1.03558 0.06819  -0.09034 0.15538  155 ALA A CA  
1196 C C   . ALA A 155 ? 0.95274 0.96141 1.10904 0.08669  -0.10201 0.16547  155 ALA A C   
1197 O O   . ALA A 155 ? 0.86113 0.86105 1.03100 0.10132  -0.09655 0.16646  155 ALA A O   
1198 C CB  . ALA A 155 ? 0.76698 0.78346 0.92921 0.06435  -0.07988 0.14247  155 ALA A CB  
1199 N N   . LEU A 156 ? 0.88984 0.91820 1.04497 0.08622  -0.11838 0.17264  156 LEU A N   
1200 C CA  . LEU A 156 ? 0.97154 1.02762 1.15191 0.10158  -0.13206 0.17998  156 LEU A CA  
1201 C C   . LEU A 156 ? 0.99201 1.08896 1.19085 0.09114  -0.13956 0.17367  156 LEU A C   
1202 O O   . LEU A 156 ? 0.91974 1.02520 1.10366 0.08145  -0.15250 0.17704  156 LEU A O   
1203 C CB  . LEU A 156 ? 0.99899 1.04187 1.16001 0.11062  -0.14741 0.19581  156 LEU A CB  
1204 C CG  . LEU A 156 ? 1.03930 1.04423 1.18559 0.12526  -0.14450 0.20638  156 LEU A CG  
1205 C CD1 . LEU A 156 ? 1.07051 1.07247 1.20016 0.13331  -0.16347 0.22287  156 LEU A CD1 
1206 C CD2 . LEU A 156 ? 0.94896 0.95672 1.12599 0.14470  -0.13722 0.20453  156 LEU A CD2 
1207 N N   . PRO A 157 ? 1.01889 1.14093 1.24866 0.09179  -0.13154 0.16433  157 PRO A N   
1208 C CA  . PRO A 157 ? 0.99370 1.14798 1.23653 0.07672  -0.13455 0.15641  157 PRO A CA  
1209 C C   . PRO A 157 ? 0.95376 1.13675 1.20298 0.07602  -0.15535 0.16343  157 PRO A C   
1210 O O   . PRO A 157 ? 0.94970 1.14913 1.21710 0.09243  -0.16634 0.17235  157 PRO A O   
1211 C CB  . PRO A 157 ? 1.04958 1.22612 1.32716 0.08240  -0.12280 0.14838  157 PRO A CB  
1212 C CG  . PRO A 157 ? 0.99772 1.14758 1.27468 0.09784  -0.11081 0.14919  157 PRO A CG  
1213 C CD  . PRO A 157 ? 0.94725 1.06760 1.19977 0.10637  -0.11902 0.16080  157 PRO A CD  
1214 N N   . GLY A 158 ? 0.89378 1.08118 1.12614 0.05710  -0.16122 0.15933  158 GLY A N   
1215 C CA  . GLY A 158 ? 0.92686 1.13827 1.15864 0.05226  -0.18149 0.16429  158 GLY A CA  
1216 C C   . GLY A 158 ? 1.00052 1.18893 1.19667 0.05392  -0.19408 0.17492  158 GLY A C   
1217 O O   . GLY A 158 ? 1.01026 1.21166 1.19439 0.04407  -0.20959 0.17648  158 GLY A O   
1218 N N   . ASN A 159 ? 1.04012 1.19421 1.21782 0.06532  -0.18789 0.18228  159 ASN A N   
1219 C CA  . ASN A 159 ? 0.95374 1.08294 1.09519 0.06707  -0.19822 0.19377  159 ASN A CA  
1220 C C   . ASN A 159 ? 1.01066 1.11148 1.11425 0.04864  -0.18937 0.18765  159 ASN A C   
1221 O O   . ASN A 159 ? 1.00671 1.08207 1.10256 0.04622  -0.17151 0.18241  159 ASN A O   
1222 C CB  . ASN A 159 ? 0.93906 1.04135 1.07665 0.08634  -0.19432 0.20471  159 ASN A CB  
1223 C CG  . ASN A 159 ? 0.98978 1.07481 1.09721 0.09242  -0.20938 0.22018  159 ASN A CG  
1224 O OD1 . ASN A 159 ? 0.94383 1.01784 1.01760 0.07842  -0.21449 0.22097  159 ASN A OD1 
1225 N ND2 . ASN A 159 ? 0.98592 1.06744 1.10388 0.11391  -0.21634 0.23280  159 ASN A ND2 
1226 N N   . PRO A 160 ? 1.04947 1.15340 1.12838 0.03579  -0.20105 0.18784  160 PRO A N   
1227 C CA  . PRO A 160 ? 0.97245 1.05076 1.01685 0.01876  -0.19085 0.18049  160 PRO A CA  
1228 C C   . PRO A 160 ? 1.00393 1.04240 1.01524 0.02224  -0.18286 0.18850  160 PRO A C   
1229 O O   . PRO A 160 ? 1.00747 1.02440 0.99514 0.01024  -0.17032 0.18199  160 PRO A O   
1230 C CB  . PRO A 160 ? 0.86893 0.96240 0.89583 0.00584  -0.20729 0.17896  160 PRO A CB  
1231 C CG  . PRO A 160 ? 0.93715 1.06712 0.99182 0.01560  -0.22731 0.18593  160 PRO A CG  
1232 C CD  . PRO A 160 ? 0.92438 1.05359 1.00341 0.03730  -0.22438 0.19530  160 PRO A CD  
1233 N N   . GLU A 161 ? 1.05354 1.08146 1.06271 0.03823  -0.18946 0.20267  161 GLU A N   
1234 C CA  . GLU A 161 ? 1.05832 1.04651 1.03760 0.04079  -0.18033 0.21075  161 GLU A CA  
1235 C C   . GLU A 161 ? 1.01593 0.98610 1.00545 0.03998  -0.15856 0.20259  161 GLU A C   
1236 O O   . GLU A 161 ? 1.00464 0.94451 0.96883 0.03391  -0.14667 0.20341  161 GLU A O   
1237 C CB  . GLU A 161 ? 1.02835 1.00788 1.00510 0.05925  -0.19242 0.22827  161 GLU A CB  
1238 C CG  . GLU A 161 ? 1.09425 1.08470 1.05076 0.06020  -0.21504 0.23937  161 GLU A CG  
1239 C CD  . GLU A 161 ? 1.19211 1.17127 1.10762 0.04115  -0.21540 0.23579  161 GLU A CD  
1240 O OE1 . GLU A 161 ? 1.20201 1.15266 1.09448 0.03133  -0.19819 0.23154  161 GLU A OE1 
1241 O OE2 . GLU A 161 ? 1.22941 1.22892 1.13558 0.03595  -0.23299 0.23689  161 GLU A OE2 
1242 N N   . ALA A 162 ? 0.97955 0.96913 1.00546 0.04538  -0.15326 0.19468  162 ALA A N   
1243 C CA  . ALA A 162 ? 0.98805 0.96571 1.02555 0.04376  -0.13413 0.18521  162 ALA A CA  
1244 C C   . ALA A 162 ? 0.95465 0.96440 1.02779 0.04353  -0.13219 0.17429  162 ALA A C   
1245 O O   . ALA A 162 ? 0.94026 0.95970 1.04110 0.05667  -0.13021 0.17460  162 ALA A O   
1246 C CB  . ALA A 162 ? 0.92368 0.87602 0.96298 0.05803  -0.12797 0.19303  162 ALA A CB  
1247 N N   . PRO A 163 ? 0.92517 0.95137 0.99793 0.02893  -0.13239 0.16464  163 PRO A N   
1248 C CA  . PRO A 163 ? 0.87482 0.93227 0.98024 0.02753  -0.13168 0.15579  163 PRO A CA  
1249 C C   . PRO A 163 ? 0.85035 0.90196 0.96862 0.02574  -0.11368 0.14569  163 PRO A C   
1250 O O   . PRO A 163 ? 0.79971 0.87422 0.94664 0.02818  -0.11087 0.14011  163 PRO A O   
1251 C CB  . PRO A 163 ? 0.77845 0.84928 0.87252 0.01133  -0.13921 0.15023  163 PRO A CB  
1252 C CG  . PRO A 163 ? 0.85027 0.89074 0.90634 0.00192  -0.13353 0.15001  163 PRO A CG  
1253 C CD  . PRO A 163 ? 0.96404 0.97919 1.00547 0.01312  -0.13234 0.16132  163 PRO A CD  
1254 N N   . GLY A 164 ? 0.80333 0.82638 0.90151 0.02146  -0.10159 0.14344  164 GLY A N   
1255 C CA  . GLY A 164 ? 0.70599 0.72355 0.81339 0.01876  -0.08589 0.13382  164 GLY A CA  
1256 C C   . GLY A 164 ? 0.72696 0.74455 0.82305 0.00330  -0.08009 0.12463  164 GLY A C   
1257 O O   . GLY A 164 ? 0.80448 0.83034 0.89069 -0.00540 -0.08795 0.12389  164 GLY A O   
1258 N N   . ASN A 165 ? 0.69590 0.70267 0.79220 0.00010  -0.06629 0.11739  165 ASN A N   
1259 C CA  . ASN A 165 ? 0.63553 0.64200 0.72466 -0.01195 -0.05919 0.10842  165 ASN A CA  
1260 C C   . ASN A 165 ? 0.67541 0.66703 0.73585 -0.02111 -0.06005 0.10907  165 ASN A C   
1261 O O   . ASN A 165 ? 0.72838 0.72025 0.78165 -0.03043 -0.05584 0.10192  165 ASN A O   
1262 C CB  . ASN A 165 ? 0.69995 0.73080 0.80634 -0.01652 -0.06277 0.10323  165 ASN A CB  
1263 C CG  . ASN A 165 ? 0.69118 0.73579 0.82411 -0.00979 -0.05686 0.10005  165 ASN A CG  
1264 O OD1 . ASN A 165 ? 0.70022 0.73420 0.83668 -0.00279 -0.04887 0.09957  165 ASN A OD1 
1265 N ND2 . ASN A 165 ? 0.65702 0.72479 0.80766 -0.01288 -0.06011 0.09736  165 ASN A ND2 
1266 N N   . MET A 166 ? 0.63438 0.61166 0.67724 -0.01823 -0.06453 0.11757  166 MET A N   
1267 C CA  . MET A 166 ? 0.73881 0.70057 0.75215 -0.02649 -0.06358 0.11871  166 MET A CA  
1268 C C   . MET A 166 ? 0.70528 0.65735 0.71178 -0.03405 -0.04950 0.11017  166 MET A C   
1269 O O   . MET A 166 ? 0.72672 0.67717 0.71840 -0.04251 -0.04776 0.10517  166 MET A O   
1270 C CB  . MET A 166 ? 0.81070 0.75402 0.80775 -0.02101 -0.06620 0.12992  166 MET A CB  
1271 C CG  . MET A 166 ? 0.78647 0.73893 0.78707 -0.01256 -0.08176 0.13967  166 MET A CG  
1272 S SD  . MET A 166 ? 0.81579 0.77506 0.84758 0.00393  -0.08312 0.14404  166 MET A SD  
1273 C CE  . MET A 166 ? 0.80712 0.73202 0.82364 0.00916  -0.07424 0.15158  166 MET A CE  
1274 N N   . GLY A 167 ? 0.67292 0.61829 0.68968 -0.03078 -0.03955 0.10821  167 GLY A N   
1275 C CA  . GLY A 167 ? 0.69902 0.63909 0.71281 -0.03698 -0.02737 0.10040  167 GLY A CA  
1276 C C   . GLY A 167 ? 0.70439 0.65779 0.72715 -0.04107 -0.02579 0.09153  167 GLY A C   
1277 O O   . GLY A 167 ? 0.68567 0.63528 0.69888 -0.04702 -0.01926 0.08592  167 GLY A O   
1278 N N   . LEU A 168 ? 0.70072 0.66950 0.74213 -0.03770 -0.03113 0.09040  168 LEU A N   
1279 C CA  . LEU A 168 ? 0.67974 0.65908 0.72723 -0.04281 -0.03052 0.08335  168 LEU A CA  
1280 C C   . LEU A 168 ? 0.73386 0.71184 0.76392 -0.05022 -0.03670 0.08243  168 LEU A C   
1281 O O   . LEU A 168 ? 0.69290 0.66749 0.71564 -0.05625 -0.03219 0.07580  168 LEU A O   
1282 C CB  . LEU A 168 ? 0.66728 0.66408 0.73819 -0.03881 -0.03420 0.08307  168 LEU A CB  
1283 C CG  . LEU A 168 ? 0.65271 0.65084 0.73933 -0.03267 -0.02628 0.08108  168 LEU A CG  
1284 C CD1 . LEU A 168 ? 0.61099 0.62669 0.71966 -0.02716 -0.02987 0.08220  168 LEU A CD1 
1285 C CD2 . LEU A 168 ? 0.57133 0.56659 0.65662 -0.03694 -0.01733 0.07405  168 LEU A CD2 
1286 N N   . PHE A 169 ? 0.65382 0.63322 0.67562 -0.04954 -0.04732 0.08891  169 PHE A N   
1287 C CA  . PHE A 169 ? 0.70714 0.68358 0.70836 -0.05757 -0.05342 0.08719  169 PHE A CA  
1288 C C   . PHE A 169 ? 0.73519 0.69315 0.71150 -0.06164 -0.04468 0.08495  169 PHE A C   
1289 O O   . PHE A 169 ? 0.68348 0.63635 0.64406 -0.06880 -0.04357 0.07886  169 PHE A O   
1290 C CB  . PHE A 169 ? 0.69508 0.67894 0.69239 -0.05570 -0.06810 0.09504  169 PHE A CB  
1291 C CG  . PHE A 169 ? 0.74350 0.75016 0.76277 -0.05603 -0.07802 0.09435  169 PHE A CG  
1292 C CD1 . PHE A 169 ? 0.76723 0.78062 0.78667 -0.06603 -0.07986 0.08653  169 PHE A CD1 
1293 C CD2 . PHE A 169 ? 0.70073 0.72188 0.74121 -0.04648 -0.08468 0.10127  169 PHE A CD2 
1294 C CE1 . PHE A 169 ? 0.66548 0.70140 0.70642 -0.06830 -0.08831 0.08585  169 PHE A CE1 
1295 C CE2 . PHE A 169 ? 0.72536 0.77111 0.78887 -0.04696 -0.09282 0.10049  169 PHE A CE2 
1296 C CZ  . PHE A 169 ? 0.76138 0.81540 0.82546 -0.05875 -0.09464 0.09288  169 PHE A CZ  
1297 N N   . ASP A 170 ? 0.71130 0.65893 0.68421 -0.05760 -0.03751 0.08915  170 ASP A N   
1298 C CA  . ASP A 170 ? 0.77975 0.71362 0.73427 -0.06176 -0.02661 0.08616  170 ASP A CA  
1299 C C   . ASP A 170 ? 0.80583 0.74183 0.76667 -0.06446 -0.01757 0.07599  170 ASP A C   
1300 O O   . ASP A 170 ? 0.75648 0.68637 0.70095 -0.06953 -0.01420 0.07041  170 ASP A O   
1301 C CB  . ASP A 170 ? 0.72268 0.64766 0.67867 -0.05819 -0.01944 0.09152  170 ASP A CB  
1302 C CG  . ASP A 170 ? 0.79534 0.71112 0.73682 -0.05609 -0.02645 0.10246  170 ASP A CG  
1303 O OD1 . ASP A 170 ? 0.77714 0.69364 0.70350 -0.05793 -0.03652 0.10571  170 ASP A OD1 
1304 O OD2 . ASP A 170 ? 0.78379 0.69061 0.72815 -0.05274 -0.02232 0.10798  170 ASP A OD2 
1305 N N   . GLN A 171 ? 0.72718 0.67087 0.71064 -0.06045 -0.01365 0.07354  171 GLN A N   
1306 C CA  . GLN A 171 ? 0.73025 0.67635 0.72057 -0.06166 -0.00700 0.06537  171 GLN A CA  
1307 C C   . GLN A 171 ? 0.72091 0.66661 0.70254 -0.06698 -0.01189 0.06069  171 GLN A C   
1308 O O   . GLN A 171 ? 0.76124 0.69966 0.73335 -0.06952 -0.00565 0.05418  171 GLN A O   
1309 C CB  . GLN A 171 ? 0.65328 0.60925 0.66738 -0.05697 -0.00574 0.06471  171 GLN A CB  
1310 C CG  . GLN A 171 ? 0.59544 0.55061 0.61832 -0.05254 -0.00110 0.06771  171 GLN A CG  
1311 C CD  . GLN A 171 ? 0.66358 0.62836 0.70739 -0.04796 -0.00116 0.06679  171 GLN A CD  
1312 O OE1 . GLN A 171 ? 0.65103 0.62333 0.70300 -0.04839 -0.00243 0.06365  171 GLN A OE1 
1313 N NE2 . GLN A 171 ? 0.58119 0.54416 0.63221 -0.04407 0.00075  0.06941  171 GLN A NE2 
1314 N N   . GLN A 172 ? 0.71053 0.66398 0.69577 -0.06876 -0.02306 0.06360  172 GLN A N   
1315 C CA  . GLN A 172 ? 0.71474 0.66893 0.69475 -0.07563 -0.02819 0.05838  172 GLN A CA  
1316 C C   . GLN A 172 ? 0.79080 0.73187 0.74247 -0.08162 -0.02858 0.05490  172 GLN A C   
1317 O O   . GLN A 172 ? 0.72882 0.66113 0.67067 -0.08637 -0.02494 0.04709  172 GLN A O   
1318 C CB  . GLN A 172 ? 0.73070 0.70037 0.72408 -0.07697 -0.04048 0.06225  172 GLN A CB  
1319 C CG  . GLN A 172 ? 0.68123 0.65441 0.67691 -0.08526 -0.04431 0.05632  172 GLN A CG  
1320 C CD  . GLN A 172 ? 0.72506 0.71699 0.73435 -0.08790 -0.05706 0.06003  172 GLN A CD  
1321 O OE1 . GLN A 172 ? 0.74862 0.74465 0.74889 -0.08867 -0.06740 0.06426  172 GLN A OE1 
1322 N NE2 . GLN A 172 ? 0.73400 0.73885 0.76548 -0.08908 -0.05650 0.05898  172 GLN A NE2 
1323 N N   . LEU A 173 ? 0.81368 0.75139 0.75008 -0.08131 -0.03260 0.06063  173 LEU A N   
1324 C CA  . LEU A 173 ? 0.77400 0.69820 0.68016 -0.08678 -0.03113 0.05734  173 LEU A CA  
1325 C C   . LEU A 173 ? 0.80634 0.71927 0.70548 -0.08593 -0.01589 0.05020  173 LEU A C   
1326 O O   . LEU A 173 ? 0.84999 0.75182 0.72952 -0.09057 -0.01230 0.04258  173 LEU A O   
1327 C CB  . LEU A 173 ? 0.83059 0.75146 0.72103 -0.08544 -0.03551 0.06637  173 LEU A CB  
1328 C CG  . LEU A 173 ? 0.91450 0.82884 0.77528 -0.09271 -0.04406 0.06534  173 LEU A CG  
1329 C CD1 . LEU A 173 ? 0.85737 0.78580 0.72738 -0.09574 -0.06082 0.06686  173 LEU A CD1 
1330 C CD2 . LEU A 173 ? 0.83226 0.73776 0.67079 -0.09152 -0.04399 0.07400  173 LEU A CD2 
1331 N N   . ALA A 174 ? 0.73933 0.65553 0.65492 -0.07976 -0.00687 0.05195  174 ALA A N   
1332 C CA  . ALA A 174 ? 0.76053 0.67046 0.67392 -0.07785 0.00689  0.04548  174 ALA A CA  
1333 C C   . ALA A 174 ? 0.82813 0.73559 0.74766 -0.07795 0.00903  0.03735  174 ALA A C   
1334 O O   . ALA A 174 ? 0.86218 0.75916 0.76862 -0.07837 0.01696  0.03004  174 ALA A O   
1335 C CB  . ALA A 174 ? 0.74817 0.66465 0.67916 -0.07228 0.01435  0.04918  174 ALA A CB  
1336 N N   . LEU A 175 ? 0.77578 0.69154 0.71438 -0.07731 0.00288  0.03861  175 LEU A N   
1337 C CA  . LEU A 175 ? 0.80214 0.71243 0.74345 -0.07894 0.00416  0.03206  175 LEU A CA  
1338 C C   . LEU A 175 ? 0.85010 0.74742 0.76805 -0.08690 0.00057  0.02581  175 LEU A C   
1339 O O   . LEU A 175 ? 0.80617 0.68987 0.71523 -0.08755 0.00670  0.01814  175 LEU A O   
1340 C CB  . LEU A 175 ? 0.73539 0.65720 0.69826 -0.07919 -0.00234 0.03534  175 LEU A CB  
1341 C CG  . LEU A 175 ? 0.82413 0.75806 0.80927 -0.07203 0.00045  0.04032  175 LEU A CG  
1342 C CD1 . LEU A 175 ? 0.73252 0.67420 0.73523 -0.07263 -0.00236 0.04103  175 LEU A CD1 
1343 C CD2 . LEU A 175 ? 0.79667 0.72711 0.78292 -0.06571 0.01145  0.03818  175 LEU A CD2 
1344 N N   . GLN A 176 ? 0.84048 0.74106 0.74749 -0.09274 -0.00983 0.02888  176 GLN A N   
1345 C CA  . GLN A 176 ? 0.83911 0.72810 0.72147 -0.10163 -0.01478 0.02251  176 GLN A CA  
1346 C C   . GLN A 176 ? 0.91833 0.79062 0.77579 -0.10067 -0.00376 0.01599  176 GLN A C   
1347 O O   . GLN A 176 ? 0.90497 0.76147 0.74526 -0.10520 -0.00094 0.00653  176 GLN A O   
1348 C CB  . GLN A 176 ? 0.88928 0.78796 0.76498 -0.10679 -0.02916 0.02845  176 GLN A CB  
1349 C CG  . GLN A 176 ? 1.07264 0.97930 0.95643 -0.11499 -0.04132 0.02679  176 GLN A CG  
1350 C CD  . GLN A 176 ? 1.28403 1.17462 1.14143 -0.12567 -0.04373 0.01654  176 GLN A CD  
1351 O OE1 . GLN A 176 ? 1.36345 1.24161 1.19269 -0.12741 -0.04161 0.01330  176 GLN A OE1 
1352 N NE2 . GLN A 176 ? 1.18469 1.07336 1.04958 -0.13333 -0.04673 0.01080  176 GLN A NE2 
1353 N N   . TRP A 177 ? 0.89786 0.77291 0.75322 -0.09510 0.00345  0.02056  177 TRP A N   
1354 C CA  . TRP A 177 ? 0.87567 0.73835 0.70984 -0.09378 0.01590  0.01487  177 TRP A CA  
1355 C C   . TRP A 177 ? 0.87969 0.73395 0.72013 -0.08856 0.02753  0.00624  177 TRP A C   
1356 O O   . TRP A 177 ? 0.93095 0.77032 0.75102 -0.08902 0.03582  -0.00261 177 TRP A O   
1357 C CB  . TRP A 177 ? 0.91400 0.78401 0.75097 -0.08942 0.02251  0.02238  177 TRP A CB  
1358 C CG  . TRP A 177 ? 0.96922 0.83003 0.78587 -0.08867 0.03684  0.01734  177 TRP A CG  
1359 C CD1 . TRP A 177 ? 0.93674 0.78970 0.72385 -0.09380 0.03799  0.01824  177 TRP A CD1 
1360 C CD2 . TRP A 177 ? 0.91657 0.77653 0.74115 -0.08211 0.05222  0.01082  177 TRP A CD2 
1361 N NE1 . TRP A 177 ? 0.92412 0.77153 0.70038 -0.09146 0.05437  0.01220  177 TRP A NE1 
1362 C CE2 . TRP A 177 ? 0.95229 0.80494 0.75265 -0.08383 0.06319  0.00744  177 TRP A CE2 
1363 C CE3 . TRP A 177 ? 0.91587 0.78131 0.76526 -0.07452 0.05759  0.00786  177 TRP A CE3 
1364 C CZ2 . TRP A 177 ? 0.87847 0.73119 0.68161 -0.07780 0.07988  0.00059  177 TRP A CZ2 
1365 C CZ3 . TRP A 177 ? 0.89645 0.76160 0.74824 -0.06793 0.07263  0.00172  177 TRP A CZ3 
1366 C CH2 . TRP A 177 ? 0.99156 0.85147 0.82189 -0.06942 0.08386  -0.00208 177 TRP A CH2 
1367 N N   . VAL A 178 ? 0.82456 0.68759 0.69216 -0.08274 0.02848  0.00882  178 VAL A N   
1368 C CA  . VAL A 178 ? 0.86908 0.72427 0.74353 -0.07631 0.03810  0.00230  178 VAL A CA  
1369 C C   . VAL A 178 ? 0.90460 0.74191 0.76587 -0.08196 0.03470  -0.00551 178 VAL A C   
1370 O O   . VAL A 178 ? 0.93457 0.75534 0.78443 -0.07869 0.04378  -0.01400 178 VAL A O   
1371 C CB  . VAL A 178 ? 0.85028 0.71946 0.75457 -0.06916 0.03860  0.00795  178 VAL A CB  
1372 C CG1 . VAL A 178 ? 0.81640 0.67681 0.72703 -0.06209 0.04602  0.00269  178 VAL A CG1 
1373 C CG2 . VAL A 178 ? 0.78092 0.66468 0.69608 -0.06445 0.04377  0.01342  178 VAL A CG2 
1374 N N   . GLN A 179 ? 0.86387 0.70378 0.72617 -0.09084 0.02191  -0.00324 179 GLN A N   
1375 C CA  . GLN A 179 ? 0.94820 0.77049 0.79699 -0.09899 0.01831  -0.01121 179 GLN A CA  
1376 C C   . GLN A 179 ? 0.95536 0.75966 0.77117 -0.10401 0.02133  -0.02049 179 GLN A C   
1377 O O   . GLN A 179 ? 0.94214 0.72436 0.74364 -0.10462 0.02768  -0.03037 179 GLN A O   
1378 C CB  . GLN A 179 ? 0.88544 0.71851 0.74350 -0.10904 0.00367  -0.00701 179 GLN A CB  
1379 C CG  . GLN A 179 ? 0.85883 0.70542 0.74658 -0.10550 0.00211  -0.00017 179 GLN A CG  
1380 C CD  . GLN A 179 ? 0.84458 0.67502 0.73590 -0.10223 0.01014  -0.00446 179 GLN A CD  
1381 O OE1 . GLN A 179 ? 0.91710 0.73291 0.80082 -0.11089 0.00757  -0.00968 179 GLN A OE1 
1382 N NE2 . GLN A 179 ? 0.88275 0.71522 0.78539 -0.09004 0.01950  -0.00203 179 GLN A NE2 
1383 N N   . LYS A 180 ? 0.95925 0.77071 0.76077 -0.10712 0.01759  -0.01750 180 LYS A N   
1384 C CA  . LYS A 180 ? 1.02105 0.81572 0.78760 -0.11327 0.01944  -0.02624 180 LYS A CA  
1385 C C   . LYS A 180 ? 1.02363 0.80655 0.77785 -0.10461 0.03716  -0.03283 180 LYS A C   
1386 O O   . LYS A 180 ? 1.05239 0.81517 0.77829 -0.10820 0.04227  -0.04372 180 LYS A O   
1387 C CB  . LYS A 180 ? 1.02165 0.82713 0.77408 -0.11964 0.00868  -0.01974 180 LYS A CB  
1388 C CG  . LYS A 180 ? 1.18055 0.98964 0.92856 -0.13173 -0.00911 -0.01969 180 LYS A CG  
1389 C CD  . LYS A 180 ? 1.29159 1.11551 1.03204 -0.13491 -0.02144 -0.01016 180 LYS A CD  
1390 C CE  . LYS A 180 ? 1.43749 1.26480 1.16790 -0.14773 -0.03949 -0.01230 180 LYS A CE  
1391 N NZ  . LYS A 180 ? 1.47860 1.32470 1.20977 -0.14807 -0.05359 -0.00036 180 LYS A NZ  
1392 N N   . ASN A 181 ? 0.91710 0.71272 0.69215 -0.09360 0.04687  -0.02727 181 ASN A N   
1393 C CA  . ASN A 181 ? 0.97339 0.76518 0.73860 -0.08622 0.06323  -0.03185 181 ASN A CA  
1394 C C   . ASN A 181 ? 0.89866 0.69100 0.68458 -0.07334 0.07603  -0.03478 181 ASN A C   
1395 O O   . ASN A 181 ? 0.95214 0.73732 0.72765 -0.06718 0.09026  -0.04208 181 ASN A O   
1396 C CB  . ASN A 181 ? 0.97139 0.78015 0.73792 -0.08605 0.06482  -0.02251 181 ASN A CB  
1397 C CG  . ASN A 181 ? 1.03831 0.84457 0.77885 -0.09671 0.05409  -0.01930 181 ASN A CG  
1398 O OD1 . ASN A 181 ? 1.07019 0.86289 0.77848 -0.10131 0.05839  -0.02606 181 ASN A OD1 
1399 N ND2 . ASN A 181 ? 0.99714 0.81665 0.75092 -0.10009 0.03987  -0.00892 181 ASN A ND2 
1400 N N   . ILE A 182 ? 0.79506 0.59679 0.60949 -0.06850 0.07175  -0.02919 182 ILE A N   
1401 C CA  . ILE A 182 ? 0.88957 0.69699 0.72510 -0.05526 0.08260  -0.02964 182 ILE A CA  
1402 C C   . ILE A 182 ? 0.91033 0.69461 0.73478 -0.04876 0.09184  -0.04063 182 ILE A C   
1403 O O   . ILE A 182 ? 0.88210 0.66961 0.71769 -0.03622 0.10359  -0.04312 182 ILE A O   
1404 C CB  . ILE A 182 ? 0.87368 0.69617 0.73906 -0.05229 0.07477  -0.02058 182 ILE A CB  
1405 C CG1 . ILE A 182 ? 0.84431 0.68385 0.73346 -0.04031 0.08353  -0.01755 182 ILE A CG1 
1406 C CG2 . ILE A 182 ? 0.87011 0.67665 0.73671 -0.05317 0.06968  -0.02305 182 ILE A CG2 
1407 C CD1 . ILE A 182 ? 0.89633 0.75444 0.78942 -0.04146 0.08782  -0.01324 182 ILE A CD1 
1408 N N   . ALA A 183 ? 0.93093 0.69162 0.73373 -0.05684 0.08692  -0.04765 183 ALA A N   
1409 C CA  . ALA A 183 ? 0.94249 0.67641 0.73112 -0.05081 0.09669  -0.05906 183 ALA A CA  
1410 C C   . ALA A 183 ? 1.01624 0.74693 0.78928 -0.04407 0.11221  -0.06723 183 ALA A C   
1411 O O   . ALA A 183 ? 1.00539 0.72396 0.77923 -0.03174 0.12456  -0.07439 183 ALA A O   
1412 C CB  . ALA A 183 ? 0.84081 0.54872 0.60566 -0.06385 0.08832  -0.06621 183 ALA A CB  
1413 N N   . ALA A 184 ? 0.98395 0.72522 0.74259 -0.05135 0.11243  -0.06594 184 ALA A N   
1414 C CA  . ALA A 184 ? 1.00520 0.74504 0.74821 -0.04601 0.12867  -0.07330 184 ALA A CA  
1415 C C   . ALA A 184 ? 1.01978 0.78283 0.79196 -0.03199 0.14065  -0.06914 184 ALA A C   
1416 O O   . ALA A 184 ? 1.06719 0.82849 0.83414 -0.02309 0.15700  -0.07693 184 ALA A O   
1417 C CB  . ALA A 184 ? 0.95384 0.69860 0.67225 -0.05817 0.12560  -0.07128 184 ALA A CB  
1418 N N   . PHE A 185 ? 0.94975 0.73553 0.75247 -0.03024 0.13297  -0.05760 185 PHE A N   
1419 C CA  . PHE A 185 ? 0.89315 0.70305 0.72692 -0.01816 0.14122  -0.05326 185 PHE A CA  
1420 C C   . PHE A 185 ? 0.97268 0.77701 0.82530 -0.00425 0.14314  -0.05531 185 PHE A C   
1421 O O   . PHE A 185 ? 0.95397 0.77975 0.83431 0.00651  0.14775  -0.05142 185 PHE A O   
1422 C CB  . PHE A 185 ? 0.89556 0.73051 0.75089 -0.02362 0.13137  -0.04054 185 PHE A CB  
1423 C CG  . PHE A 185 ? 0.98341 0.82633 0.82437 -0.03444 0.13148  -0.03645 185 PHE A CG  
1424 C CD1 . PHE A 185 ? 0.98544 0.81657 0.80356 -0.04686 0.11981  -0.03422 185 PHE A CD1 
1425 C CD2 . PHE A 185 ? 0.93574 0.79834 0.78628 -0.03248 0.14290  -0.03421 185 PHE A CD2 
1426 C CE1 . PHE A 185 ? 0.99301 0.82960 0.79592 -0.05577 0.11922  -0.02908 185 PHE A CE1 
1427 C CE2 . PHE A 185 ? 0.97920 0.84598 0.81420 -0.04287 0.14355  -0.02929 185 PHE A CE2 
1428 C CZ  . PHE A 185 ? 0.99801 0.85073 0.80825 -0.05385 0.13147  -0.02627 185 PHE A CZ  
1429 N N   . GLY A 186 ? 0.96560 0.74145 0.80354 -0.00466 0.13920  -0.06091 186 GLY A N   
1430 C CA  . GLY A 186 ? 0.97529 0.74215 0.82870 0.00823  0.14001  -0.06108 186 GLY A CA  
1431 C C   . GLY A 186 ? 0.99706 0.77126 0.86971 0.00559  0.12600  -0.05045 186 GLY A C   
1432 O O   . GLY A 186 ? 0.97157 0.74576 0.86165 0.01751  0.12636  -0.04744 186 GLY A O   
1433 N N   . GLY A 187 ? 0.88722 0.66825 0.75694 -0.00906 0.11378  -0.04438 187 GLY A N   
1434 C CA  . GLY A 187 ? 0.84220 0.63094 0.72897 -0.01240 0.10155  -0.03494 187 GLY A CA  
1435 C C   . GLY A 187 ? 0.97762 0.74158 0.84922 -0.02231 0.09310  -0.03691 187 GLY A C   
1436 O O   . GLY A 187 ? 0.98108 0.72578 0.82756 -0.03118 0.09308  -0.04473 187 GLY A O   
1437 N N   . ASN A 188 ? 0.98429 0.74932 0.87101 -0.02152 0.08605  -0.02989 188 ASN A N   
1438 C CA  . ASN A 188 ? 0.94205 0.68669 0.81913 -0.03192 0.07825  -0.03021 188 ASN A CA  
1439 C C   . ASN A 188 ? 0.93137 0.69400 0.81561 -0.04545 0.06585  -0.02317 188 ASN A C   
1440 O O   . ASN A 188 ? 0.82906 0.60947 0.73406 -0.04335 0.06120  -0.01423 188 ASN A O   
1441 C CB  . ASN A 188 ? 1.05482 0.78740 0.94217 -0.02260 0.07957  -0.02636 188 ASN A CB  
1442 C CG  . ASN A 188 ? 1.07530 0.78633 0.95368 -0.03447 0.07284  -0.02590 188 ASN A CG  
1443 O OD1 . ASN A 188 ? 1.09581 0.79695 0.95824 -0.04910 0.06812  -0.03113 188 ASN A OD1 
1444 N ND2 . ASN A 188 ? 1.07202 0.77597 0.96012 -0.02881 0.07229  -0.01949 188 ASN A ND2 
1445 N N   . PRO A 189 ? 0.90088 0.65948 0.76832 -0.05890 0.05998  -0.02705 189 PRO A N   
1446 C CA  . PRO A 189 ? 0.92547 0.70191 0.80139 -0.07039 0.04767  -0.02025 189 PRO A CA  
1447 C C   . PRO A 189 ? 0.93997 0.71509 0.82883 -0.07501 0.04157  -0.01514 189 PRO A C   
1448 O O   . PRO A 189 ? 0.91162 0.70672 0.81466 -0.08073 0.03322  -0.00815 189 PRO A O   
1449 C CB  . PRO A 189 ? 0.88173 0.64797 0.73312 -0.08336 0.04249  -0.02721 189 PRO A CB  
1450 C CG  . PRO A 189 ? 0.83704 0.57124 0.66725 -0.08239 0.05036  -0.03832 189 PRO A CG  
1451 C CD  . PRO A 189 ? 0.95392 0.68708 0.79267 -0.06477 0.06330  -0.03853 189 PRO A CD  
1452 N N   . LYS A 190 ? 0.95313 0.70441 0.83680 -0.07275 0.04604  -0.01825 190 LYS A N   
1453 C CA  . LYS A 190 ? 1.00930 0.75692 0.90298 -0.07803 0.04178  -0.01288 190 LYS A CA  
1454 C C   . LYS A 190 ? 0.95952 0.71825 0.87286 -0.06546 0.04499  -0.00421 190 LYS A C   
1455 O O   . LYS A 190 ? 1.04754 0.80316 0.96813 -0.06885 0.04273  0.00119  190 LYS A O   
1456 C CB  . LYS A 190 ? 0.98110 0.69320 0.85631 -0.08420 0.04449  -0.01997 190 LYS A CB  
1457 C CG  . LYS A 190 ? 1.08119 0.78164 0.93549 -0.09928 0.03972  -0.02943 190 LYS A CG  
1458 C CD  . LYS A 190 ? 1.28721 0.94880 1.12136 -0.10637 0.04305  -0.03792 190 LYS A CD  
1459 C CE  . LYS A 190 ? 1.41232 1.05802 1.21961 -0.11689 0.04143  -0.05057 190 LYS A CE  
1460 N NZ  . LYS A 190 ? 1.37674 1.02740 1.17396 -0.10560 0.04804  -0.05533 190 LYS A NZ  
1461 N N   . SER A 191 ? 0.90285 0.67524 0.82453 -0.05198 0.05012  -0.00276 191 SER A N   
1462 C CA  . SER A 191 ? 0.86772 0.65514 0.80844 -0.04071 0.05144  0.00520  191 SER A CA  
1463 C C   . SER A 191 ? 0.83993 0.65685 0.79390 -0.03749 0.05030  0.00800  191 SER A C   
1464 O O   . SER A 191 ? 0.86738 0.69134 0.82461 -0.02752 0.05632  0.00612  191 SER A O   
1465 C CB  . SER A 191 ? 0.88972 0.66016 0.82783 -0.02590 0.05949  0.00377  191 SER A CB  
1466 O OG  . SER A 191 ? 0.89913 0.68712 0.85499 -0.01446 0.05963  0.01112  191 SER A OG  
1467 N N   . VAL A 192 ? 0.80630 0.64034 0.76864 -0.04621 0.04290  0.01253  192 VAL A N   
1468 C CA  . VAL A 192 ? 0.77054 0.62896 0.74403 -0.04519 0.04089  0.01576  192 VAL A CA  
1469 C C   . VAL A 192 ? 0.76670 0.64162 0.75809 -0.04409 0.03691  0.02316  192 VAL A C   
1470 O O   . VAL A 192 ? 0.82976 0.70452 0.82373 -0.05152 0.03199  0.02595  192 VAL A O   
1471 C CB  . VAL A 192 ? 0.77089 0.63291 0.73554 -0.05573 0.03541  0.01415  192 VAL A CB  
1472 C CG1 . VAL A 192 ? 0.73400 0.61766 0.70964 -0.05443 0.03330  0.01884  192 VAL A CG1 
1473 C CG2 . VAL A 192 ? 0.77469 0.61933 0.71767 -0.05773 0.03953  0.00603  192 VAL A CG2 
1474 N N   . THR A 193 ? 0.68573 0.57579 0.68935 -0.03569 0.03929  0.02574  193 THR A N   
1475 C CA  . THR A 193 ? 0.69666 0.60249 0.71527 -0.03422 0.03610  0.03151  193 THR A CA  
1476 C C   . THR A 193 ? 0.68831 0.61190 0.71495 -0.03545 0.03450  0.03267  193 THR A C   
1477 O O   . THR A 193 ? 0.75334 0.68188 0.78052 -0.03152 0.03855  0.03055  193 THR A O   
1478 C CB  . THR A 193 ? 0.71661 0.62354 0.74146 -0.02363 0.03926  0.03342  193 THR A CB  
1479 O OG1 . THR A 193 ? 0.78769 0.67420 0.80326 -0.02242 0.04065  0.03359  193 THR A OG1 
1480 C CG2 . THR A 193 ? 0.59807 0.52154 0.63575 -0.02222 0.03613  0.03836  193 THR A CG2 
1481 N N   . LEU A 194 ? 0.68728 0.61972 0.72016 -0.04098 0.02925  0.03602  194 LEU A N   
1482 C CA  . LEU A 194 ? 0.71234 0.65869 0.75306 -0.04121 0.02773  0.03791  194 LEU A CA  
1483 C C   . LEU A 194 ? 0.72364 0.68121 0.77673 -0.03554 0.02903  0.03971  194 LEU A C   
1484 O O   . LEU A 194 ? 0.66921 0.62680 0.72576 -0.03380 0.02836  0.04151  194 LEU A O   
1485 C CB  . LEU A 194 ? 0.66968 0.62073 0.71279 -0.04765 0.02147  0.04068  194 LEU A CB  
1486 C CG  . LEU A 194 ? 0.68498 0.62755 0.71661 -0.05493 0.01744  0.03919  194 LEU A CG  
1487 C CD1 . LEU A 194 ? 0.67055 0.62306 0.70924 -0.05987 0.01013  0.04269  194 LEU A CD1 
1488 C CD2 . LEU A 194 ? 0.65209 0.58768 0.66984 -0.05551 0.01955  0.03631  194 LEU A CD2 
1489 N N   . PHE A 195 ? 0.64290 0.60937 0.70123 -0.03350 0.03104  0.03912  195 PHE A N   
1490 C CA  . PHE A 195 ? 0.61837 0.59649 0.68796 -0.03055 0.03068  0.04014  195 PHE A CA  
1491 C C   . PHE A 195 ? 0.67740 0.66171 0.75106 -0.03342 0.03067  0.04039  195 PHE A C   
1492 O O   . PHE A 195 ? 0.66902 0.65023 0.73713 -0.03591 0.03278  0.03983  195 PHE A O   
1493 C CB  . PHE A 195 ? 0.61290 0.59565 0.68656 -0.02362 0.03340  0.03866  195 PHE A CB  
1494 C CG  . PHE A 195 ? 0.62496 0.61176 0.69984 -0.02124 0.03816  0.03562  195 PHE A CG  
1495 C CD1 . PHE A 195 ? 0.65164 0.63028 0.71726 -0.02391 0.04150  0.03379  195 PHE A CD1 
1496 C CD2 . PHE A 195 ? 0.63270 0.63308 0.71808 -0.01645 0.03947  0.03433  195 PHE A CD2 
1497 C CE1 . PHE A 195 ? 0.62962 0.61334 0.69656 -0.02182 0.04764  0.03079  195 PHE A CE1 
1498 C CE2 . PHE A 195 ? 0.61697 0.62487 0.70664 -0.01440 0.04485  0.03134  195 PHE A CE2 
1499 C CZ  . PHE A 195 ? 0.61982 0.61922 0.70031 -0.01702 0.04975  0.02959  195 PHE A CZ  
1500 N N   . GLY A 196 ? 0.65003 0.64094 0.73152 -0.03338 0.02866  0.04134  196 GLY A N   
1501 C CA  . GLY A 196 ? 0.60343 0.59728 0.68896 -0.03575 0.02876  0.04148  196 GLY A CA  
1502 C C   . GLY A 196 ? 0.65647 0.65747 0.74992 -0.03420 0.02807  0.04002  196 GLY A C   
1503 O O   . GLY A 196 ? 0.66093 0.66513 0.75572 -0.03136 0.02704  0.03982  196 GLY A O   
1504 N N   . GLU A 197 ? 0.63356 0.63540 0.73038 -0.03667 0.02895  0.03890  197 GLU A N   
1505 C CA  . GLU A 197 ? 0.63053 0.63714 0.73287 -0.03642 0.02846  0.03604  197 GLU A CA  
1506 C C   . GLU A 197 ? 0.62680 0.62611 0.72966 -0.03770 0.02806  0.03686  197 GLU A C   
1507 O O   . GLU A 197 ? 0.66257 0.65437 0.76251 -0.04008 0.02865  0.03938  197 GLU A O   
1508 C CB  . GLU A 197 ? 0.58439 0.59909 0.69139 -0.03865 0.03009  0.03223  197 GLU A CB  
1509 C CG  . GLU A 197 ? 0.63158 0.65170 0.74234 -0.03940 0.02858  0.02797  197 GLU A CG  
1510 C CD  . GLU A 197 ? 0.67422 0.68764 0.78613 -0.04486 0.03009  0.02564  197 GLU A CD  
1511 O OE1 . GLU A 197 ? 0.64855 0.65362 0.75832 -0.04769 0.03228  0.02854  197 GLU A OE1 
1512 O OE2 . GLU A 197 ? 0.60514 0.61961 0.71814 -0.04644 0.02918  0.02103  197 GLU A OE2 
1513 N N   . SER A 198 ? 0.63543 0.63602 0.74089 -0.03543 0.02743  0.03501  198 SER A N   
1514 C CA  . SER A 198 ? 0.67268 0.66588 0.77977 -0.03473 0.02787  0.03468  198 SER A CA  
1515 C C   . SER A 198 ? 0.67145 0.66003 0.77834 -0.03254 0.02588  0.04025  198 SER A C   
1516 O O   . SER A 198 ? 0.66070 0.65488 0.76894 -0.03060 0.02427  0.04230  198 SER A O   
1517 C CB  . SER A 198 ? 0.61753 0.60470 0.72418 -0.03941 0.02976  0.03174  198 SER A CB  
1518 O OG  . SER A 198 ? 0.67830 0.65730 0.78575 -0.03822 0.03085  0.02897  198 SER A OG  
1519 N N   . ALA A 199 ? 0.62658 0.60522 0.73153 -0.03310 0.02545  0.04319  199 ALA A N   
1520 C CA  . ALA A 199 ? 0.63790 0.61433 0.74196 -0.03071 0.02173  0.04914  199 ALA A CA  
1521 C C   . ALA A 199 ? 0.63132 0.61145 0.72972 -0.03364 0.01985  0.05128  199 ALA A C   
1522 O O   . ALA A 199 ? 0.60753 0.59066 0.70613 -0.03261 0.01584  0.05454  199 ALA A O   
1523 C CB  . ALA A 199 ? 0.67975 0.64275 0.77977 -0.03041 0.02110  0.05316  199 ALA A CB  
1524 N N   . GLY A 200 ? 0.66187 0.64235 0.75573 -0.03734 0.02277  0.04892  200 GLY A N   
1525 C CA  . GLY A 200 ? 0.62257 0.60531 0.71079 -0.03892 0.02233  0.04928  200 GLY A CA  
1526 C C   . GLY A 200 ? 0.65064 0.63982 0.74245 -0.03696 0.02081  0.04832  200 GLY A C   
1527 O O   . GLY A 200 ? 0.62580 0.61434 0.71412 -0.03812 0.01808  0.05013  200 GLY A O   
1528 N N   . ALA A 201 ? 0.67173 0.66643 0.76927 -0.03487 0.02255  0.04547  201 ALA A N   
1529 C CA  . ALA A 201 ? 0.68528 0.68474 0.78476 -0.03356 0.02212  0.04547  201 ALA A CA  
1530 C C   . ALA A 201 ? 0.68227 0.68456 0.78685 -0.03322 0.01969  0.04813  201 ALA A C   
1531 O O   . ALA A 201 ? 0.67150 0.67560 0.77565 -0.03524 0.01827  0.04966  201 ALA A O   
1532 C CB  . ALA A 201 ? 0.58883 0.59331 0.69078 -0.03141 0.02431  0.04237  201 ALA A CB  
1533 N N   . ALA A 202 ? 0.62200 0.62481 0.73225 -0.03072 0.01926  0.04863  202 ALA A N   
1534 C CA  . ALA A 202 ? 0.60447 0.61349 0.72275 -0.02897 0.01681  0.05131  202 ALA A CA  
1535 C C   . ALA A 202 ? 0.63336 0.64177 0.74855 -0.03202 0.01134  0.05507  202 ALA A C   
1536 O O   . ALA A 202 ? 0.62635 0.64285 0.74708 -0.03378 0.00866  0.05663  202 ALA A O   
1537 C CB  . ALA A 202 ? 0.54462 0.55256 0.66954 -0.02374 0.01757  0.05117  202 ALA A CB  
1538 N N   . SER A 203 ? 0.53243 0.53181 0.63783 -0.03381 0.00993  0.05616  203 SER A N   
1539 C CA  . SER A 203 ? 0.53311 0.53007 0.63070 -0.03760 0.00494  0.05876  203 SER A CA  
1540 C C   . SER A 203 ? 0.64730 0.64540 0.74126 -0.04221 0.00511  0.05657  203 SER A C   
1541 O O   . SER A 203 ? 0.65723 0.65956 0.75212 -0.04581 0.00032  0.05782  203 SER A O   
1542 C CB  . SER A 203 ? 0.65749 0.64354 0.74235 -0.03926 0.00593  0.05952  203 SER A CB  
1543 O OG  . SER A 203 ? 0.62438 0.60531 0.71006 -0.03623 0.00589  0.06242  203 SER A OG  
1544 N N   . VAL A 204 ? 0.65791 0.65191 0.74782 -0.04226 0.01025  0.05333  204 VAL A N   
1545 C CA  . VAL A 204 ? 0.62454 0.61581 0.71009 -0.04549 0.01115  0.05168  204 VAL A CA  
1546 C C   . VAL A 204 ? 0.61456 0.61418 0.70932 -0.04763 0.00963  0.05301  204 VAL A C   
1547 O O   . VAL A 204 ? 0.66702 0.66593 0.75961 -0.05333 0.00669  0.05321  204 VAL A O   
1548 C CB  . VAL A 204 ? 0.70457 0.69207 0.78722 -0.04256 0.01650  0.04912  204 VAL A CB  
1549 C CG1 . VAL A 204 ? 0.64406 0.62732 0.72359 -0.04433 0.01775  0.04877  204 VAL A CG1 
1550 C CG2 . VAL A 204 ? 0.61811 0.59921 0.69241 -0.04190 0.01868  0.04728  204 VAL A CG2 
1551 N N   . SER A 205 ? 0.64682 0.65492 0.75197 -0.04389 0.01197  0.05349  205 SER A N   
1552 C CA  . SER A 205 ? 0.66352 0.68166 0.77844 -0.04606 0.01243  0.05466  205 SER A CA  
1553 C C   . SER A 205 ? 0.64161 0.66898 0.76441 -0.04914 0.00628  0.05688  205 SER A C   
1554 O O   . SER A 205 ? 0.65469 0.68910 0.78303 -0.05494 0.00531  0.05750  205 SER A O   
1555 C CB  . SER A 205 ? 0.59640 0.62187 0.71953 -0.04080 0.01710  0.05394  205 SER A CB  
1556 O OG  . SER A 205 ? 0.73614 0.76557 0.86640 -0.03570 0.01554  0.05423  205 SER A OG  
1557 N N   . LEU A 206 ? 0.62822 0.65578 0.75128 -0.04589 0.00170  0.05849  206 LEU A N   
1558 C CA  . LEU A 206 ? 0.63381 0.67135 0.76372 -0.04789 -0.00600 0.06134  206 LEU A CA  
1559 C C   . LEU A 206 ? 0.62645 0.65810 0.74469 -0.05638 -0.01121 0.06057  206 LEU A C   
1560 O O   . LEU A 206 ? 0.66251 0.70510 0.78735 -0.06141 -0.01768 0.06175  206 LEU A O   
1561 C CB  . LEU A 206 ? 0.70159 0.73842 0.83282 -0.04089 -0.00970 0.06448  206 LEU A CB  
1562 C CG  . LEU A 206 ? 0.72196 0.76680 0.86799 -0.03251 -0.00615 0.06504  206 LEU A CG  
1563 C CD1 . LEU A 206 ? 0.67744 0.71532 0.82125 -0.02570 -0.00946 0.06851  206 LEU A CD1 
1564 C CD2 . LEU A 206 ? 0.56137 0.62654 0.72598 -0.03269 -0.00773 0.06603  206 LEU A CD2 
1565 N N   . HIS A 207 ? 0.61512 0.63048 0.71648 -0.05815 -0.00854 0.05805  207 HIS A N   
1566 C CA  . HIS A 207 ? 0.69168 0.69845 0.77985 -0.06624 -0.01181 0.05569  207 HIS A CA  
1567 C C   . HIS A 207 ? 0.65669 0.66433 0.74858 -0.07326 -0.00983 0.05375  207 HIS A C   
1568 O O   . HIS A 207 ? 0.69737 0.70276 0.78394 -0.08204 -0.01441 0.05196  207 HIS A O   
1569 C CB  . HIS A 207 ? 0.65305 0.64260 0.72338 -0.06490 -0.00758 0.05292  207 HIS A CB  
1570 C CG  . HIS A 207 ? 0.68777 0.67446 0.75008 -0.06208 -0.01027 0.05505  207 HIS A CG  
1571 N ND1 . HIS A 207 ? 0.68243 0.66802 0.73456 -0.06641 -0.01784 0.05622  207 HIS A ND1 
1572 C CD2 . HIS A 207 ? 0.69636 0.68073 0.75863 -0.05614 -0.00659 0.05674  207 HIS A CD2 
1573 C CE1 . HIS A 207 ? 0.67954 0.66100 0.72433 -0.06264 -0.01815 0.05934  207 HIS A CE1 
1574 N NE2 . HIS A 207 ? 0.67194 0.65226 0.72340 -0.05686 -0.01105 0.05961  207 HIS A NE2 
1575 N N   . LEU A 208 ? 0.69628 0.70638 0.79600 -0.07040 -0.00314 0.05416  208 LEU A N   
1576 C CA  . LEU A 208 ? 0.63705 0.64858 0.74092 -0.07752 -0.00067 0.05388  208 LEU A CA  
1577 C C   . LEU A 208 ? 0.64453 0.67691 0.76598 -0.08253 -0.00516 0.05582  208 LEU A C   
1578 O O   . LEU A 208 ? 0.65741 0.69214 0.78191 -0.09233 -0.00526 0.05528  208 LEU A O   
1579 C CB  . LEU A 208 ? 0.63278 0.64168 0.73815 -0.07275 0.00764  0.05472  208 LEU A CB  
1580 C CG  . LEU A 208 ? 0.66097 0.65210 0.75198 -0.06841 0.01227  0.05327  208 LEU A CG  
1581 C CD1 . LEU A 208 ? 0.64637 0.64098 0.74106 -0.06218 0.01815  0.05484  208 LEU A CD1 
1582 C CD2 . LEU A 208 ? 0.61965 0.59404 0.69877 -0.07545 0.01325  0.05190  208 LEU A CD2 
1583 N N   . LEU A 209 ? 0.63742 0.68509 0.77135 -0.07600 -0.00862 0.05814  209 LEU A N   
1584 C CA  . LEU A 209 ? 0.70159 0.77229 0.85495 -0.07913 -0.01347 0.06009  209 LEU A CA  
1585 C C   . LEU A 209 ? 0.68656 0.76242 0.83786 -0.08423 -0.02513 0.06047  209 LEU A C   
1586 O O   . LEU A 209 ? 0.68067 0.77459 0.84577 -0.09154 -0.03045 0.06092  209 LEU A O   
1587 C CB  . LEU A 209 ? 0.64777 0.73351 0.81775 -0.06795 -0.01122 0.06253  209 LEU A CB  
1588 C CG  . LEU A 209 ? 0.67937 0.76364 0.85223 -0.06277 -0.00025 0.06165  209 LEU A CG  
1589 C CD1 . LEU A 209 ? 0.67468 0.77834 0.86767 -0.05484 0.00208  0.06288  209 LEU A CD1 
1590 C CD2 . LEU A 209 ? 0.66573 0.74683 0.83561 -0.07160 0.00600  0.06075  209 LEU A CD2 
1591 N N   . SER A 210 ? 0.66396 0.72602 0.79847 -0.08117 -0.02939 0.06036  210 SER A N   
1592 C CA  . SER A 210 ? 0.71440 0.78285 0.84562 -0.08463 -0.04133 0.06167  210 SER A CA  
1593 C C   . SER A 210 ? 0.71792 0.77823 0.83641 -0.09848 -0.04511 0.05707  210 SER A C   
1594 O O   . SER A 210 ? 0.74199 0.77957 0.84080 -0.10108 -0.03990 0.05314  210 SER A O   
1595 C CB  . SER A 210 ? 0.78078 0.83671 0.89624 -0.07731 -0.04402 0.06383  210 SER A CB  
1596 O OG  . SER A 210 ? 0.72869 0.79218 0.84010 -0.08039 -0.05654 0.06616  210 SER A OG  
1597 N N   . PRO A 211 ? 0.83559 0.91376 0.96516 -0.10762 -0.05389 0.05692  211 PRO A N   
1598 C CA  . PRO A 211 ? 0.84954 0.91761 0.96571 -0.12277 -0.05742 0.05131  211 PRO A CA  
1599 C C   . PRO A 211 ? 0.87049 0.91735 0.95794 -0.12437 -0.06175 0.04808  211 PRO A C   
1600 O O   . PRO A 211 ? 0.91666 0.94240 0.98576 -0.13285 -0.05851 0.04196  211 PRO A O   
1601 C CB  . PRO A 211 ? 0.76039 0.85742 0.89717 -0.13164 -0.06807 0.05231  211 PRO A CB  
1602 C CG  . PRO A 211 ? 0.88086 1.00363 1.04514 -0.12014 -0.06694 0.05834  211 PRO A CG  
1603 C CD  . PRO A 211 ? 0.76401 0.87296 0.92251 -0.10517 -0.05781 0.06088  211 PRO A CD  
1604 N N   . GLY A 212 ? 0.71727 0.76719 0.79888 -0.11612 -0.06798 0.05207  212 GLY A N   
1605 C CA  . GLY A 212 ? 0.64729 0.67716 0.69980 -0.11741 -0.07048 0.04940  212 GLY A CA  
1606 C C   . GLY A 212 ? 0.78540 0.78915 0.82050 -0.11322 -0.05758 0.04572  212 GLY A C   
1607 O O   . GLY A 212 ? 0.76165 0.74752 0.77189 -0.11562 -0.05725 0.04181  212 GLY A O   
1608 N N   . SER A 213 ? 0.72975 0.73210 0.77705 -0.10671 -0.04707 0.04677  213 SER A N   
1609 C CA  . SER A 213 ? 0.76044 0.74192 0.79454 -0.10174 -0.03580 0.04374  213 SER A CA  
1610 C C   . SER A 213 ? 0.75439 0.72194 0.78475 -0.10767 -0.02916 0.03859  213 SER A C   
1611 O O   . SER A 213 ? 0.77259 0.72191 0.79045 -0.10359 -0.02090 0.03547  213 SER A O   
1612 C CB  . SER A 213 ? 0.66481 0.65180 0.71162 -0.08984 -0.02904 0.04828  213 SER A CB  
1613 O OG  . SER A 213 ? 0.69727 0.68635 0.73958 -0.08374 -0.03218 0.05227  213 SER A OG  
1614 N N   . HIS A 214 ? 0.73059 0.70610 0.77172 -0.11711 -0.03232 0.03793  214 HIS A N   
1615 C CA  . HIS A 214 ? 0.81392 0.77555 0.85392 -0.12126 -0.02444 0.03535  214 HIS A CA  
1616 C C   . HIS A 214 ? 0.74254 0.67545 0.75783 -0.12447 -0.02062 0.02854  214 HIS A C   
1617 O O   . HIS A 214 ? 0.76573 0.68177 0.77594 -0.12021 -0.01165 0.02756  214 HIS A O   
1618 C CB  . HIS A 214 ? 0.79070 0.76551 0.84563 -0.13328 -0.02808 0.03586  214 HIS A CB  
1619 C CG  . HIS A 214 ? 0.97593 0.97566 1.05639 -0.12824 -0.02657 0.04201  214 HIS A CG  
1620 N ND1 . HIS A 214 ? 0.87530 0.89247 0.97396 -0.13755 -0.02780 0.04341  214 HIS A ND1 
1621 C CD2 . HIS A 214 ? 0.84047 0.85042 0.93097 -0.11513 -0.02324 0.04643  214 HIS A CD2 
1622 C CE1 . HIS A 214 ? 0.80786 0.84524 0.92643 -0.12931 -0.02468 0.04832  214 HIS A CE1 
1623 N NE2 . HIS A 214 ? 0.88047 0.91250 0.99364 -0.11573 -0.02216 0.04995  214 HIS A NE2 
1624 N N   . SER A 215 ? 0.68932 0.61580 0.68807 -0.13071 -0.02710 0.02381  215 SER A N   
1625 C CA  . SER A 215 ? 0.74378 0.64167 0.71756 -0.13402 -0.02282 0.01586  215 SER A CA  
1626 C C   . SER A 215 ? 0.79207 0.67924 0.75197 -0.12233 -0.01624 0.01456  215 SER A C   
1627 O O   . SER A 215 ? 0.79253 0.65731 0.73102 -0.12344 -0.01200 0.00739  215 SER A O   
1628 C CB  . SER A 215 ? 0.83427 0.72848 0.79354 -0.14824 -0.03259 0.00969  215 SER A CB  
1629 O OG  . SER A 215 ? 0.95598 0.84964 0.89873 -0.14455 -0.03616 0.00836  215 SER A OG  
1630 N N   . LEU A 216 ? 0.79553 0.69785 0.76720 -0.11165 -0.01461 0.02079  216 LEU A N   
1631 C CA  . LEU A 216 ? 0.79414 0.69027 0.75542 -0.10213 -0.00834 0.02016  216 LEU A CA  
1632 C C   . LEU A 216 ? 0.81461 0.70641 0.78376 -0.09131 0.00216  0.02132  216 LEU A C   
1633 O O   . LEU A 216 ? 0.76870 0.65913 0.73344 -0.08347 0.00800  0.02099  216 LEU A O   
1634 C CB  . LEU A 216 ? 0.75857 0.67239 0.72535 -0.09873 -0.01391 0.02625  216 LEU A CB  
1635 C CG  . LEU A 216 ? 0.77563 0.69819 0.73693 -0.10741 -0.02645 0.02721  216 LEU A CG  
1636 C CD1 . LEU A 216 ? 0.70194 0.63861 0.66765 -0.10162 -0.03127 0.03471  216 LEU A CD1 
1637 C CD2 . LEU A 216 ? 0.74083 0.64494 0.67427 -0.11571 -0.02795 0.01904  216 LEU A CD2 
1638 N N   . PHE A 217 ? 0.69985 0.59090 0.68058 -0.09103 0.00447  0.02310  217 PHE A N   
1639 C CA  . PHE A 217 ? 0.71627 0.60350 0.70290 -0.08044 0.01293  0.02460  217 PHE A CA  
1640 C C   . PHE A 217 ? 0.73290 0.61087 0.72324 -0.08305 0.01494  0.02563  217 PHE A C   
1641 O O   . PHE A 217 ? 0.72564 0.60585 0.71943 -0.09331 0.01023  0.02634  217 PHE A O   
1642 C CB  . PHE A 217 ? 0.71084 0.61804 0.71372 -0.07260 0.01334  0.03034  217 PHE A CB  
1643 C CG  . PHE A 217 ? 0.73840 0.66262 0.75850 -0.07534 0.00863  0.03566  217 PHE A CG  
1644 C CD1 . PHE A 217 ? 0.72286 0.65997 0.74789 -0.08107 0.00077  0.03758  217 PHE A CD1 
1645 C CD2 . PHE A 217 ? 0.70508 0.63354 0.73636 -0.07105 0.01230  0.03891  217 PHE A CD2 
1646 C CE1 . PHE A 217 ? 0.69717 0.65191 0.74027 -0.08195 -0.00241 0.04208  217 PHE A CE1 
1647 C CE2 . PHE A 217 ? 0.70044 0.64507 0.74700 -0.07304 0.00969  0.04309  217 PHE A CE2 
1648 C CZ  . PHE A 217 ? 0.67365 0.63185 0.72730 -0.07813 0.00286  0.04440  217 PHE A CZ  
1649 N N   . THR A 218 ? 0.77727 0.64573 0.76727 -0.07374 0.02193  0.02627  218 THR A N   
1650 C CA  . THR A 218 ? 0.77404 0.63011 0.76446 -0.07447 0.02476  0.02862  218 THR A CA  
1651 C C   . THR A 218 ? 0.81167 0.68437 0.81810 -0.07017 0.02507  0.03581  218 THR A C   
1652 O O   . THR A 218 ? 0.71788 0.59286 0.72967 -0.07736 0.02395  0.03924  218 THR A O   
1653 C CB  . THR A 218 ? 0.83731 0.67071 0.81585 -0.06537 0.03170  0.02565  218 THR A CB  
1654 O OG1 . THR A 218 ? 0.83997 0.66026 0.80322 -0.06686 0.03305  0.01785  218 THR A OG1 
1655 C CG2 . THR A 218 ? 0.82955 0.64162 0.80213 -0.06854 0.03409  0.02769  218 THR A CG2 
1656 N N   . ARG A 219 ? 0.70941 0.59426 0.72309 -0.05944 0.02695  0.03762  219 ARG A N   
1657 C CA  . ARG A 219 ? 0.72866 0.62558 0.75339 -0.05352 0.02809  0.04306  219 ARG A CA  
1658 C C   . ARG A 219 ? 0.73030 0.64838 0.76615 -0.04938 0.02634  0.04359  219 ARG A C   
1659 O O   . ARG A 219 ? 0.73428 0.65567 0.76834 -0.04959 0.02522  0.04063  219 ARG A O   
1660 C CB  . ARG A 219 ? 0.70505 0.59039 0.72488 -0.04301 0.03252  0.04440  219 ARG A CB  
1661 C CG  . ARG A 219 ? 0.86589 0.73138 0.87705 -0.04526 0.03462  0.04721  219 ARG A CG  
1662 C CD  . ARG A 219 ? 0.82626 0.68362 0.83423 -0.03230 0.03766  0.05024  219 ARG A CD  
1663 N NE  . ARG A 219 ? 0.81475 0.65255 0.81253 -0.02619 0.04098  0.04579  219 ARG A NE  
1664 C CZ  . ARG A 219 ? 0.86934 0.68093 0.85360 -0.03151 0.04308  0.04330  219 ARG A CZ  
1665 N NH1 . ARG A 219 ? 0.85993 0.66287 0.84024 -0.04432 0.04184  0.04526  219 ARG A NH1 
1666 N NH2 . ARG A 219 ? 0.90234 0.69587 0.87712 -0.02404 0.04710  0.03828  219 ARG A NH2 
1667 N N   . ALA A 220 ? 0.71721 0.64744 0.76249 -0.04550 0.02672  0.04731  220 ALA A N   
1668 C CA  . ALA A 220 ? 0.69722 0.64517 0.75282 -0.04300 0.02518  0.04752  220 ALA A CA  
1669 C C   . ALA A 220 ? 0.63530 0.59054 0.69560 -0.03552 0.02698  0.04922  220 ALA A C   
1670 O O   . ALA A 220 ? 0.66759 0.61910 0.72557 -0.03404 0.02824  0.05223  220 ALA A O   
1671 C CB  . ALA A 220 ? 0.73100 0.69035 0.79526 -0.04930 0.02204  0.04926  220 ALA A CB  
1672 N N   . ILE A 221 ? 0.62386 0.58906 0.68960 -0.03175 0.02685  0.04741  221 ILE A N   
1673 C CA  . ILE A 221 ? 0.63776 0.61278 0.70881 -0.02601 0.02727  0.04763  221 ILE A CA  
1674 C C   . ILE A 221 ? 0.70061 0.68710 0.77968 -0.02808 0.02608  0.04644  221 ILE A C   
1675 O O   . ILE A 221 ? 0.65325 0.64039 0.73346 -0.03011 0.02580  0.04489  221 ILE A O   
1676 C CB  . ILE A 221 ? 0.65412 0.62976 0.72495 -0.01957 0.02884  0.04554  221 ILE A CB  
1677 C CG1 . ILE A 221 ? 0.64968 0.61125 0.71226 -0.01521 0.03059  0.04649  221 ILE A CG1 
1678 C CG2 . ILE A 221 ? 0.63055 0.62011 0.70863 -0.01524 0.02770  0.04511  221 ILE A CG2 
1679 C CD1 . ILE A 221 ? 0.57224 0.53690 0.63731 -0.00703 0.03288  0.04406  221 ILE A CD1 
1680 N N   . LEU A 222 ? 0.62931 0.62296 0.71214 -0.02734 0.02585  0.04716  222 LEU A N   
1681 C CA  . LEU A 222 ? 0.69001 0.69130 0.77959 -0.02874 0.02540  0.04560  222 LEU A CA  
1682 C C   . LEU A 222 ? 0.65828 0.66683 0.74987 -0.02583 0.02549  0.04300  222 LEU A C   
1683 O O   . LEU A 222 ? 0.62966 0.64101 0.71868 -0.02415 0.02574  0.04350  222 LEU A O   
1684 C CB  . LEU A 222 ? 0.62885 0.63251 0.72152 -0.03119 0.02582  0.04739  222 LEU A CB  
1685 C CG  . LEU A 222 ? 0.69197 0.69251 0.78538 -0.03573 0.02446  0.04956  222 LEU A CG  
1686 C CD1 . LEU A 222 ? 0.72410 0.71572 0.80985 -0.03780 0.02526  0.05142  222 LEU A CD1 
1687 C CD2 . LEU A 222 ? 0.63470 0.64375 0.73649 -0.03714 0.02506  0.05056  222 LEU A CD2 
1688 N N   . GLN A 223 ? 0.57860 0.59015 0.67380 -0.02631 0.02531  0.04016  223 GLN A N   
1689 C CA  . GLN A 223 ? 0.58530 0.60468 0.68328 -0.02551 0.02466  0.03664  223 GLN A CA  
1690 C C   . GLN A 223 ? 0.60871 0.62789 0.70965 -0.02816 0.02527  0.03382  223 GLN A C   
1691 O O   . GLN A 223 ? 0.63195 0.64656 0.73529 -0.03064 0.02604  0.03381  223 GLN A O   
1692 C CB  . GLN A 223 ? 0.58073 0.60459 0.68227 -0.02544 0.02493  0.03490  223 GLN A CB  
1693 C CG  . GLN A 223 ? 0.53497 0.55747 0.63379 -0.02072 0.02520  0.03716  223 GLN A CG  
1694 C CD  . GLN A 223 ? 0.60886 0.63670 0.71251 -0.01973 0.02733  0.03523  223 GLN A CD  
1695 O OE1 . GLN A 223 ? 0.71743 0.74056 0.81811 -0.01589 0.02912  0.03635  223 GLN A OE1 
1696 N NE2 . GLN A 223 ? 0.57212 0.60933 0.68311 -0.02343 0.02793  0.03197  223 GLN A NE2 
1697 N N   . SER A 224 ? 0.58988 0.61223 0.68891 -0.02724 0.02523  0.03156  224 SER A N   
1698 C CA  . SER A 224 ? 0.64143 0.66167 0.74199 -0.02874 0.02665  0.02746  224 SER A CA  
1699 C C   . SER A 224 ? 0.60881 0.62226 0.71324 -0.02857 0.02825  0.02970  224 SER A C   
1700 O O   . SER A 224 ? 0.66612 0.67376 0.77294 -0.03001 0.02878  0.02811  224 SER A O   
1701 C CB  . SER A 224 ? 0.59186 0.61351 0.69462 -0.03241 0.02575  0.02243  224 SER A CB  
1702 O OG  . SER A 224 ? 0.65280 0.68441 0.75408 -0.03240 0.02285  0.02012  224 SER A OG  
1703 N N   . GLY A 225 ? 0.60315 0.61731 0.70836 -0.02702 0.02864  0.03380  225 GLY A N   
1704 C CA  . GLY A 225 ? 0.56666 0.57819 0.67743 -0.02610 0.02884  0.03609  225 GLY A CA  
1705 C C   . GLY A 225 ? 0.65076 0.66631 0.76405 -0.02623 0.02841  0.04037  225 GLY A C   
1706 O O   . GLY A 225 ? 0.59257 0.60827 0.70143 -0.02807 0.02775  0.04235  225 GLY A O   
1707 N N   . SER A 226 ? 0.62428 0.64314 0.74537 -0.02430 0.02881  0.04170  226 SER A N   
1708 C CA  . SER A 226 ? 0.67088 0.69671 0.79740 -0.02582 0.02806  0.04536  226 SER A CA  
1709 C C   . SER A 226 ? 0.69725 0.72839 0.83522 -0.02204 0.02721  0.04655  226 SER A C   
1710 O O   . SER A 226 ? 0.69413 0.72252 0.83470 -0.01723 0.02938  0.04388  226 SER A O   
1711 C CB  . SER A 226 ? 0.65862 0.69018 0.78356 -0.02712 0.03238  0.04515  226 SER A CB  
1712 O OG  . SER A 226 ? 0.60839 0.64301 0.73400 -0.02350 0.03723  0.04135  226 SER A OG  
1713 N N   . PHE A 227 ? 0.67253 0.71139 0.81766 -0.02407 0.02381  0.05033  227 PHE A N   
1714 C CA  . PHE A 227 ? 0.64812 0.69390 0.80547 -0.01938 0.02088  0.05262  227 PHE A CA  
1715 C C   . PHE A 227 ? 0.71653 0.77148 0.88530 -0.01309 0.02680  0.05014  227 PHE A C   
1716 O O   . PHE A 227 ? 0.72663 0.78328 0.90452 -0.00589 0.02579  0.05089  227 PHE A O   
1717 C CB  . PHE A 227 ? 0.66146 0.71717 0.82512 -0.02389 0.01486  0.05672  227 PHE A CB  
1718 C CG  . PHE A 227 ? 0.67398 0.74334 0.84586 -0.02858 0.01820  0.05662  227 PHE A CG  
1719 C CD1 . PHE A 227 ? 0.71720 0.80253 0.90525 -0.02447 0.02232  0.05624  227 PHE A CD1 
1720 C CD2 . PHE A 227 ? 0.69091 0.75613 0.85411 -0.03714 0.01810  0.05694  227 PHE A CD2 
1721 C CE1 . PHE A 227 ? 0.77789 0.87615 0.97327 -0.03011 0.02678  0.05642  227 PHE A CE1 
1722 C CE2 . PHE A 227 ? 0.68416 0.75915 0.85334 -0.04280 0.02193  0.05745  227 PHE A CE2 
1723 C CZ  . PHE A 227 ? 0.74236 0.83480 0.92783 -0.03999 0.02647  0.05737  227 PHE A CZ  
1724 N N   . ASN A 228 ? 0.70250 0.76300 0.87040 -0.01505 0.03337  0.04749  228 ASN A N   
1725 C CA  . ASN A 228 ? 0.59816 0.66796 0.77577 -0.00914 0.04047  0.04444  228 ASN A CA  
1726 C C   . ASN A 228 ? 0.68981 0.74725 0.85924 -0.00379 0.04477  0.03865  228 ASN A C   
1727 O O   . ASN A 228 ? 0.69631 0.75847 0.87033 0.00139  0.05189  0.03455  228 ASN A O   
1728 C CB  . ASN A 228 ? 0.57383 0.65476 0.75232 -0.01421 0.04680  0.04436  228 ASN A CB  
1729 C CG  . ASN A 228 ? 0.64714 0.71703 0.80706 -0.01922 0.04879  0.04308  228 ASN A CG  
1730 O OD1 . ASN A 228 ? 0.66311 0.72093 0.81229 -0.02149 0.04365  0.04368  228 ASN A OD1 
1731 N ND2 . ASN A 228 ? 0.61855 0.69337 0.77466 -0.02051 0.05637  0.04169  228 ASN A ND2 
1732 N N   . ALA A 229 ? 0.62271 0.66492 0.78022 -0.00557 0.04122  0.03757  229 ALA A N   
1733 C CA  . ALA A 229 ? 0.71158 0.74139 0.86297 -0.00177 0.04420  0.03181  229 ALA A CA  
1734 C C   . ALA A 229 ? 0.72019 0.74673 0.88206 0.00691  0.04456  0.03203  229 ALA A C   
1735 O O   . ALA A 229 ? 0.72436 0.75366 0.89433 0.00901  0.03896  0.03802  229 ALA A O   
1736 C CB  . ALA A 229 ? 0.65379 0.67055 0.79349 -0.00672 0.04005  0.03131  229 ALA A CB  
1737 N N   . PRO A 230 ? 0.71291 0.73228 0.87358 0.01255  0.05076  0.02550  230 PRO A N   
1738 C CA  . PRO A 230 ? 0.70558 0.72191 0.87783 0.02325  0.05223  0.02582  230 PRO A CA  
1739 C C   . PRO A 230 ? 0.73623 0.73764 0.90731 0.02508  0.04527  0.03115  230 PRO A C   
1740 O O   . PRO A 230 ? 0.74618 0.74957 0.92895 0.03391  0.04292  0.03571  230 PRO A O   
1741 C CB  . PRO A 230 ? 0.68908 0.69507 0.85485 0.02742  0.06096  0.01599  230 PRO A CB  
1742 C CG  . PRO A 230 ? 0.72560 0.72476 0.87364 0.01739  0.06098  0.01108  230 PRO A CG  
1743 C CD  . PRO A 230 ? 0.66341 0.67668 0.81131 0.00990  0.05637  0.01730  230 PRO A CD  
1744 N N   . TRP A 231 ? 0.72451 0.71228 0.88209 0.01714  0.04195  0.03129  231 TRP A N   
1745 C CA  . TRP A 231 ? 0.76028 0.73265 0.91351 0.01690  0.03652  0.03680  231 TRP A CA  
1746 C C   . TRP A 231 ? 0.73572 0.71739 0.89093 0.01373  0.02871  0.04553  231 TRP A C   
1747 O O   . TRP A 231 ? 0.77594 0.74573 0.92568 0.01337  0.02410  0.05111  231 TRP A O   
1748 C CB  . TRP A 231 ? 0.68906 0.64494 0.82777 0.00828  0.03768  0.03250  231 TRP A CB  
1749 C CG  . TRP A 231 ? 0.73224 0.69931 0.86524 -0.00077 0.03755  0.02970  231 TRP A CG  
1750 C CD1 . TRP A 231 ? 0.74175 0.71365 0.87067 -0.00324 0.04168  0.02230  231 TRP A CD1 
1751 C CD2 . TRP A 231 ? 0.70358 0.67714 0.83324 -0.00741 0.03298  0.03447  231 TRP A CD2 
1752 N NE1 . TRP A 231 ? 0.66112 0.64230 0.78545 -0.01009 0.03931  0.02317  231 TRP A NE1 
1753 C CE2 . TRP A 231 ? 0.69277 0.67473 0.81805 -0.01248 0.03455  0.03011  231 TRP A CE2 
1754 C CE3 . TRP A 231 ? 0.66984 0.64205 0.79833 -0.00913 0.02785  0.04180  231 TRP A CE3 
1755 C CZ2 . TRP A 231 ? 0.72619 0.71454 0.84779 -0.01800 0.03162  0.03281  231 TRP A CZ2 
1756 C CZ3 . TRP A 231 ? 0.65595 0.63450 0.77956 -0.01562 0.02562  0.04340  231 TRP A CZ3 
1757 C CH2 . TRP A 231 ? 0.66914 0.65533 0.79022 -0.01946 0.02775  0.03888  231 TRP A CH2 
1758 N N   . ALA A 232 ? 0.65825 0.65903 0.81914 0.01059  0.02736  0.04674  232 ALA A N   
1759 C CA  . ALA A 232 ? 0.68182 0.68756 0.83914 0.00430  0.02056  0.05254  232 ALA A CA  
1760 C C   . ALA A 232 ? 0.76125 0.77520 0.92784 0.00900  0.01335  0.05982  232 ALA A C   
1761 O O   . ALA A 232 ? 0.72642 0.73752 0.88564 0.00469  0.00686  0.06484  232 ALA A O   
1762 C CB  . ALA A 232 ? 0.67733 0.69591 0.83403 -0.00252 0.02199  0.05052  232 ALA A CB  
1763 N N   . VAL A 233 ? 0.71819 0.74392 0.90082 0.01779  0.01413  0.06036  233 VAL A N   
1764 C CA  . VAL A 233 ? 0.73563 0.77386 0.93011 0.02293  0.00600  0.06739  233 VAL A CA  
1765 C C   . VAL A 233 ? 0.78561 0.81749 0.98895 0.03671  0.00642  0.06942  233 VAL A C   
1766 O O   . VAL A 233 ? 0.80927 0.83989 1.01915 0.04323  0.01476  0.06368  233 VAL A O   
1767 C CB  . VAL A 233 ? 0.78590 0.85124 0.99645 0.02030  0.00557  0.06699  233 VAL A CB  
1768 C CG1 . VAL A 233 ? 0.65313 0.73484 0.87792 0.02505  -0.00428 0.07391  233 VAL A CG1 
1769 C CG2 . VAL A 233 ? 0.69008 0.75692 0.88983 0.00695  0.00569  0.06509  233 VAL A CG2 
1770 N N   . THR A 234 ? 0.82675 0.85241 1.02811 0.04148  -0.00233 0.07753  234 THR A N   
1771 C CA  . THR A 234 ? 0.78812 0.80879 0.99936 0.05647  -0.00392 0.08163  234 THR A CA  
1772 C C   . THR A 234 ? 0.89313 0.94433 1.12833 0.06367  -0.00995 0.08551  234 THR A C   
1773 O O   . THR A 234 ? 0.82292 0.89160 1.06049 0.05613  -0.01812 0.08902  234 THR A O   
1774 C CB  . THR A 234 ? 0.69032 0.68744 0.88546 0.05827  -0.01085 0.08997  234 THR A CB  
1775 O OG1 . THR A 234 ? 0.88710 0.86329 1.06074 0.04664  -0.00673 0.08702  234 THR A OG1 
1776 C CG2 . THR A 234 ? 0.95016 0.93041 1.15001 0.07393  -0.00910 0.09273  234 THR A CG2 
1777 N N   . SER A 235 ? 0.90411 0.96238 1.15769 0.07801  -0.00565 0.08423  235 SER A N   
1778 C CA  . SER A 235 ? 0.94806 1.03938 1.22877 0.08585  -0.01056 0.08753  235 SER A CA  
1779 C C   . SER A 235 ? 0.96156 1.05543 1.24477 0.09320  -0.02541 0.09899  235 SER A C   
1780 O O   . SER A 235 ? 0.96059 1.02674 1.22598 0.09692  -0.02944 0.10464  235 SER A O   
1781 C CB  . SER A 235 ? 0.94210 1.04081 1.24251 0.10063  -0.00024 0.08231  235 SER A CB  
1782 O OG  . SER A 235 ? 1.12360 1.20236 1.42381 0.11701  -0.00222 0.08691  235 SER A OG  
1783 N N   . LEU A 236 ? 0.92778 1.05591 1.23300 0.09464  -0.03386 0.10274  236 LEU A N   
1784 C CA  . LEU A 236 ? 1.00357 1.13849 1.31453 0.10445  -0.04902 0.11387  236 LEU A CA  
1785 C C   . LEU A 236 ? 0.97846 1.09842 1.29646 0.12588  -0.04719 0.11790  236 LEU A C   
1786 O O   . LEU A 236 ? 0.94050 1.04362 1.24744 0.13375  -0.05727 0.12789  236 LEU A O   
1787 C CB  . LEU A 236 ? 0.97290 1.15173 1.31106 0.10288  -0.05821 0.11601  236 LEU A CB  
1788 C CG  . LEU A 236 ? 1.05572 1.24503 1.38420 0.08104  -0.06144 0.11268  236 LEU A CG  
1789 C CD1 . LEU A 236 ? 1.04168 1.27201 1.39440 0.07788  -0.07392 0.11605  236 LEU A CD1 
1790 C CD2 . LEU A 236 ? 0.76642 0.92396 1.05892 0.07048  -0.06643 0.11548  236 LEU A CD2 
1791 N N   . TYR A 237 ? 1.03124 1.15461 1.36534 0.13561  -0.03390 0.11027  237 TYR A N   
1792 C CA  . TYR A 237 ? 1.05094 1.15327 1.38847 0.15573  -0.02926 0.11181  237 TYR A CA  
1793 C C   . TYR A 237 ? 1.11251 1.16697 1.41680 0.15265  -0.02759 0.11371  237 TYR A C   
1794 O O   . TYR A 237 ? 1.12167 1.15723 1.41642 0.16153  -0.03686 0.12435  237 TYR A O   
1795 C CB  . TYR A 237 ? 1.15149 1.26192 1.50635 0.16345  -0.01256 0.10042  237 TYR A CB  
1796 C CG  . TYR A 237 ? 1.34205 1.42529 1.69748 0.18381  -0.00550 0.09962  237 TYR A CG  
1797 C CD1 . TYR A 237 ? 1.36458 1.45236 1.73659 0.20486  -0.01410 0.10932  237 TYR A CD1 
1798 C CD2 . TYR A 237 ? 1.36961 1.42139 1.70812 0.18212  0.00919  0.08914  237 TYR A CD2 
1799 C CE1 . TYR A 237 ? 1.44018 1.49961 1.81183 0.22445  -0.00739 0.10878  237 TYR A CE1 
1800 C CE2 . TYR A 237 ? 1.45831 1.48146 1.79564 0.20021  0.01602  0.08745  237 TYR A CE2 
1801 C CZ  . TYR A 237 ? 1.47654 1.50259 1.83051 0.22180  0.00800  0.09751  237 TYR A CZ  
1802 O OH  . TYR A 237 ? 1.50260 1.49856 1.85599 0.24164  0.01417  0.09690  237 TYR A OH  
1803 N N   . GLU A 238 ? 1.03328 1.06857 1.31969 0.13963  -0.01611 0.10398  238 GLU A N   
1804 C CA  . GLU A 238 ? 1.05754 1.04930 1.31563 0.13601  -0.01278 0.10435  238 GLU A CA  
1805 C C   . GLU A 238 ? 0.99144 0.97046 1.22893 0.12807  -0.02507 0.11541  238 GLU A C   
1806 O O   . GLU A 238 ? 0.98859 0.93394 1.20787 0.13166  -0.02619 0.12142  238 GLU A O   
1807 C CB  . GLU A 238 ? 1.09030 1.07038 1.33427 0.12120  -0.00058 0.09215  238 GLU A CB  
1808 C CG  . GLU A 238 ? 1.15209 1.13736 1.40820 0.12712  0.01312  0.08016  238 GLU A CG  
1809 C CD  . GLU A 238 ? 1.28874 1.27872 1.53491 0.11001  0.02090  0.07001  238 GLU A CD  
1810 O OE1 . GLU A 238 ? 1.23469 1.24276 1.47920 0.09721  0.01542  0.07221  238 GLU A OE1 
1811 O OE2 . GLU A 238 ? 1.36861 1.34246 1.60695 0.10934  0.03196  0.05993  238 GLU A OE2 
1812 N N   . ALA A 239 ? 0.96327 0.96672 1.20127 0.11637  -0.03359 0.11791  239 ALA A N   
1813 C CA  . ALA A 239 ? 0.92027 0.91174 1.13638 0.10861  -0.04455 0.12756  239 ALA A CA  
1814 C C   . ALA A 239 ? 1.00525 0.98940 1.22235 0.12464  -0.05595 0.14093  239 ALA A C   
1815 O O   . ALA A 239 ? 0.97761 0.93215 1.17049 0.12351  -0.05959 0.14916  239 ALA A O   
1816 C CB  . ALA A 239 ? 0.85122 0.87049 1.06849 0.09450  -0.05189 0.12689  239 ALA A CB  
1817 N N   . ARG A 240 ? 0.99561 1.00673 1.24075 0.14008  -0.06144 0.14376  240 ARG A N   
1818 C CA  . ARG A 240 ? 0.96143 0.96627 1.20964 0.15831  -0.07276 0.15705  240 ARG A CA  
1819 C C   . ARG A 240 ? 0.95540 0.91818 1.19263 0.17082  -0.06417 0.15867  240 ARG A C   
1820 O O   . ARG A 240 ? 0.97761 0.91007 1.19274 0.17418  -0.07016 0.16982  240 ARG A O   
1821 C CB  . ARG A 240 ? 1.08416 1.13142 1.36929 0.17289  -0.07982 0.15875  240 ARG A CB  
1822 C CG  . ARG A 240 ? 1.00090 1.04457 1.29415 0.19590  -0.09162 0.17259  240 ARG A CG  
1823 C CD  . ARG A 240 ? 1.11284 1.20620 1.44568 0.20882  -0.10052 0.17456  240 ARG A CD  
1824 N NE  . ARG A 240 ? 1.10386 1.20125 1.44059 0.22620  -0.11833 0.19042  240 ARG A NE  
1825 C CZ  . ARG A 240 ? 1.11442 1.21715 1.43472 0.21860  -0.13589 0.20085  240 ARG A CZ  
1826 N NH1 . ARG A 240 ? 1.14523 1.25044 1.44547 0.19430  -0.13750 0.19647  240 ARG A NH1 
1827 N NH2 . ARG A 240 ? 1.11482 1.21919 1.43741 0.23638  -0.15224 0.21602  240 ARG A NH2 
1828 N N   . ASN A 241 ? 1.01110 0.96939 1.26136 0.17699  -0.04963 0.14743  241 ASN A N   
1829 C CA  . ASN A 241 ? 1.06023 0.97613 1.29956 0.18814  -0.04067 0.14713  241 ASN A CA  
1830 C C   . ASN A 241 ? 1.06740 0.94259 1.27106 0.17263  -0.03791 0.14917  241 ASN A C   
1831 O O   . ASN A 241 ? 1.05849 0.89562 1.24576 0.18029  -0.03814 0.15710  241 ASN A O   
1832 C CB  . ASN A 241 ? 1.13455 1.05187 1.38899 0.19287  -0.02419 0.13179  241 ASN A CB  
1833 C CG  . ASN A 241 ? 1.23880 1.13052 1.50052 0.21653  -0.01839 0.13267  241 ASN A CG  
1834 O OD1 . ASN A 241 ? 1.18399 1.08688 1.46319 0.23663  -0.02693 0.14239  241 ASN A OD1 
1835 N ND2 . ASN A 241 ? 1.32844 1.18594 1.57674 0.21406  -0.00396 0.12191  241 ASN A ND2 
1836 N N   . ARG A 242 ? 1.02643 0.90937 1.21811 0.15081  -0.03521 0.14267  242 ARG A N   
1837 C CA  . ARG A 242 ? 1.04597 0.89573 1.20677 0.13493  -0.03161 0.14374  242 ARG A CA  
1838 C C   . ARG A 242 ? 1.03564 0.87471 1.17700 0.13373  -0.04423 0.15950  242 ARG A C   
1839 O O   . ARG A 242 ? 0.99353 0.79460 1.11197 0.13261  -0.04249 0.16653  242 ARG A O   
1840 C CB  . ARG A 242 ? 0.95150 0.81559 1.10787 0.11433  -0.02515 0.13229  242 ARG A CB  
1841 C CG  . ARG A 242 ? 1.02667 0.88447 1.18875 0.11177  -0.01075 0.11736  242 ARG A CG  
1842 C CD  . ARG A 242 ? 0.95269 0.83684 1.11947 0.09711  -0.00680 0.10702  242 ARG A CD  
1843 N NE  . ARG A 242 ? 1.01399 0.90586 1.19390 0.09995  0.00397  0.09417  242 ARG A NE  
1844 C CZ  . ARG A 242 ? 1.08736 0.98450 1.26281 0.08677  0.01138  0.08350  242 ARG A CZ  
1845 N NH1 . ARG A 242 ? 1.00564 0.90033 1.16574 0.07063  0.01003  0.08350  242 ARG A NH1 
1846 N NH2 . ARG A 242 ? 1.09138 0.99694 1.27765 0.09053  0.02046  0.07273  242 ARG A NH2 
1847 N N   . THR A 243 ? 0.99773 0.86909 1.14685 0.13352  -0.05696 0.16525  243 THR A N   
1848 C CA  . THR A 243 ? 0.99308 0.85693 1.12310 0.13385  -0.07050 0.18045  243 THR A CA  
1849 C C   . THR A 243 ? 1.03755 0.87595 1.16459 0.15402  -0.07585 0.19363  243 THR A C   
1850 O O   . THR A 243 ? 1.09577 0.90189 1.19516 0.15216  -0.07882 0.20499  243 THR A O   
1851 C CB  . THR A 243 ? 0.98742 0.89338 1.13026 0.13202  -0.08422 0.18285  243 THR A CB  
1852 O OG1 . THR A 243 ? 0.96238 0.88113 1.09713 0.11129  -0.08041 0.17377  243 THR A OG1 
1853 C CG2 . THR A 243 ? 0.99554 0.89610 1.12177 0.13772  -0.10061 0.19960  243 THR A CG2 
1854 N N   . LEU A 244 ? 1.01156 0.86341 1.16650 0.17402  -0.07665 0.19277  244 LEU A N   
1855 C CA  . LEU A 244 ? 1.07525 0.90271 1.22887 0.19586  -0.08218 0.20580  244 LEU A CA  
1856 C C   . LEU A 244 ? 1.12819 0.90229 1.25995 0.19511  -0.06934 0.20512  244 LEU A C   
1857 O O   . LEU A 244 ? 1.10616 0.84531 1.21867 0.20397  -0.07394 0.21917  244 LEU A O   
1858 C CB  . LEU A 244 ? 1.14040 0.99636 1.33181 0.21837  -0.08408 0.20346  244 LEU A CB  
1859 C CG  . LEU A 244 ? 1.01932 0.92963 1.23539 0.22008  -0.09819 0.20560  244 LEU A CG  
1860 C CD1 . LEU A 244 ? 0.99702 0.93450 1.25173 0.24372  -0.09900 0.20435  244 LEU A CD1 
1861 C CD2 . LEU A 244 ? 1.00404 0.91276 1.20031 0.21996  -0.11706 0.22282  244 LEU A CD2 
1862 N N   . ASN A 245 ? 1.09472 0.86114 1.22849 0.18430  -0.05351 0.18907  245 ASN A N   
1863 C CA  . ASN A 245 ? 1.13491 0.85164 1.24825 0.18073  -0.04129 0.18667  245 ASN A CA  
1864 C C   . ASN A 245 ? 1.14705 0.83665 1.22603 0.16290  -0.04264 0.19541  245 ASN A C   
1865 O O   . ASN A 245 ? 1.19321 0.83920 1.25105 0.16627  -0.04095 0.20511  245 ASN A O   
1866 C CB  . ASN A 245 ? 1.14966 0.86830 1.27197 0.17129  -0.02560 0.16688  245 ASN A CB  
1867 C CG  . ASN A 245 ? 1.23622 0.96578 1.38626 0.19122  -0.02010 0.15853  245 ASN A CG  
1868 O OD1 . ASN A 245 ? 1.29351 1.02667 1.45775 0.21362  -0.02713 0.16756  245 ASN A OD1 
1869 N ND2 . ASN A 245 ? 1.24084 0.97627 1.39834 0.18364  -0.00734 0.14128  245 ASN A ND2 
1870 N N   . LEU A 246 ? 1.07476 0.78912 1.14741 0.14432  -0.04535 0.19265  246 LEU A N   
1871 C CA  . LEU A 246 ? 1.12596 0.81973 1.16696 0.12805  -0.04651 0.20115  246 LEU A CA  
1872 C C   . LEU A 246 ? 1.18151 0.85793 1.20546 0.13978  -0.05937 0.22153  246 LEU A C   
1873 O O   . LEU A 246 ? 1.13011 0.76658 1.12605 0.13461  -0.05626 0.23116  246 LEU A O   
1874 C CB  . LEU A 246 ? 1.02669 0.75405 1.06666 0.11018  -0.04860 0.19493  246 LEU A CB  
1875 C CG  . LEU A 246 ? 1.13701 0.84087 1.14587 0.09068  -0.04335 0.19843  246 LEU A CG  
1876 C CD1 . LEU A 246 ? 1.06048 0.73844 1.06537 0.07991  -0.02730 0.18781  246 LEU A CD1 
1877 C CD2 . LEU A 246 ? 1.10597 0.84095 1.11151 0.07599  -0.04682 0.19426  246 LEU A CD2 
1878 N N   . ALA A 247 ? 1.17450 0.88098 1.21484 0.15529  -0.07414 0.22874  247 ALA A N   
1879 C CA  . ALA A 247 ? 1.17148 0.86462 1.19650 0.16842  -0.08864 0.24888  247 ALA A CA  
1880 C C   . ALA A 247 ? 1.16392 0.81135 1.18182 0.18513  -0.08470 0.25778  247 ALA A C   
1881 O O   . ALA A 247 ? 1.20649 0.81973 1.19589 0.18738  -0.08955 0.27432  247 ALA A O   
1882 C CB  . ALA A 247 ? 1.11451 0.85288 1.16433 0.18300  -0.10559 0.25318  247 ALA A CB  
1883 N N   . LYS A 248 ? 1.12246 0.76630 1.16401 0.19706  -0.07543 0.24717  248 LYS A N   
1884 C CA  . LYS A 248 ? 1.21322 0.80945 1.24687 0.21316  -0.07066 0.25447  248 LYS A CA  
1885 C C   . LYS A 248 ? 1.27954 0.82645 1.28178 0.19433  -0.05699 0.25322  248 LYS A C   
1886 O O   . LYS A 248 ? 1.27702 0.77804 1.25521 0.19988  -0.05738 0.26747  248 LYS A O   
1887 C CB  . LYS A 248 ? 1.17805 0.78238 1.24423 0.23163  -0.06343 0.24237  248 LYS A CB  
1888 C CG  . LYS A 248 ? 1.41839 0.97185 1.47713 0.25110  -0.05880 0.24966  248 LYS A CG  
1889 C CD  . LYS A 248 ? 1.46711 1.03175 1.55941 0.27476  -0.05364 0.23978  248 LYS A CD  
1890 C CE  . LYS A 248 ? 1.43863 0.96143 1.52618 0.30193  -0.05658 0.25386  248 LYS A CE  
1891 N NZ  . LYS A 248 ? 1.51917 1.07409 1.64302 0.33299  -0.06456 0.25649  248 LYS A NZ  
1892 N N   . LEU A 249 ? 1.25994 0.81615 1.26173 0.17142  -0.04520 0.23702  249 LEU A N   
1893 C CA  . LEU A 249 ? 1.25127 0.76549 1.22693 0.15199  -0.03200 0.23457  249 LEU A CA  
1894 C C   . LEU A 249 ? 1.28220 0.77683 1.22407 0.14069  -0.03717 0.25158  249 LEU A C   
1895 O O   . LEU A 249 ? 1.31768 0.76460 1.23423 0.13464  -0.03019 0.25929  249 LEU A O   
1896 C CB  . LEU A 249 ? 1.22047 0.75441 1.20440 0.13041  -0.02020 0.21440  249 LEU A CB  
1897 C CG  . LEU A 249 ? 1.22963 0.76778 1.23714 0.13628  -0.01026 0.19620  249 LEU A CG  
1898 C CD1 . LEU A 249 ? 1.21881 0.80708 1.24912 0.12890  -0.00939 0.18086  249 LEU A CD1 
1899 C CD2 . LEU A 249 ? 1.34399 0.83889 1.33649 0.12352  0.00414  0.18817  249 LEU A CD2 
1900 N N   . THR A 250 ? 1.24269 0.77206 1.18221 0.13712  -0.04885 0.25751  250 THR A N   
1901 C CA  . THR A 250 ? 1.25660 0.77046 1.16213 0.12665  -0.05397 0.27330  250 THR A CA  
1902 C C   . THR A 250 ? 1.35105 0.84642 1.24280 0.14706  -0.06858 0.29542  250 THR A C   
1903 O O   . THR A 250 ? 1.41512 0.89878 1.27637 0.14019  -0.07466 0.31019  250 THR A O   
1904 C CB  . THR A 250 ? 1.22833 0.78554 1.13386 0.11261  -0.05966 0.26871  250 THR A CB  
1905 O OG1 . THR A 250 ? 1.22540 0.82609 1.15942 0.12748  -0.07232 0.26557  250 THR A OG1 
1906 C CG2 . THR A 250 ? 1.21873 0.78725 1.12906 0.08985  -0.04486 0.25039  250 THR A CG2 
1907 N N   . GLY A 251 ? 1.30240 0.79560 1.21507 0.17251  -0.07445 0.29840  251 GLY A N   
1908 C CA  . GLY A 251 ? 1.30505 0.78571 1.20718 0.19392  -0.09040 0.32007  251 GLY A CA  
1909 C C   . GLY A 251 ? 1.32613 0.85293 1.23264 0.19777  -0.10949 0.32712  251 GLY A C   
1910 O O   . GLY A 251 ? 1.33684 0.85256 1.22240 0.20752  -0.12370 0.34701  251 GLY A O   
1911 N N   . CYS A 252 ? 1.23458 0.81195 1.16661 0.18980  -0.11050 0.31132  252 CYS A N   
1912 C CA  . CYS A 252 ? 1.28831 0.91132 1.22510 0.18920  -0.12757 0.31475  252 CYS A CA  
1913 C C   . CYS A 252 ? 1.29674 0.96295 1.27500 0.20993  -0.13882 0.31106  252 CYS A C   
1914 O O   . CYS A 252 ? 1.27645 0.98769 1.26671 0.20673  -0.15113 0.30879  252 CYS A O   
1915 C CB  . CYS A 252 ? 1.21133 0.85942 1.14376 0.16269  -0.12069 0.30025  252 CYS A CB  
1916 S SG  . CYS A 252 ? 1.25224 0.86897 1.13437 0.13940  -0.11580 0.30925  252 CYS A SG  
1917 N N   . SER A 253 ? 1.29563 0.94976 1.29660 0.23022  -0.13395 0.30940  253 SER A N   
1918 C CA  . SER A 253 ? 1.32275 1.01825 1.36426 0.25203  -0.14413 0.30745  253 SER A CA  
1919 C C   . SER A 253 ? 1.30667 1.01923 1.34338 0.26638  -0.16792 0.32688  253 SER A C   
1920 O O   . SER A 253 ? 1.28825 0.96394 1.30027 0.27828  -0.17483 0.34555  253 SER A O   
1921 C CB  . SER A 253 ? 1.17842 0.85075 1.24020 0.27332  -0.13377 0.30385  253 SER A CB  
1922 O OG  . SER A 253 ? 1.23877 0.90391 1.30803 0.25937  -0.11344 0.28369  253 SER A OG  
1923 N N   . ARG A 254 ? 1.31474 1.08196 1.37210 0.26307  -0.18067 0.32263  254 ARG A N   
1924 C CA  . ARG A 254 ? 1.40984 1.20380 1.46910 0.27627  -0.20522 0.33854  254 ARG A CA  
1925 C C   . ARG A 254 ? 1.49911 1.34966 1.61015 0.29025  -0.21184 0.32984  254 ARG A C   
1926 O O   . ARG A 254 ? 1.51507 1.37303 1.65590 0.29502  -0.19691 0.31542  254 ARG A O   
1927 C CB  . ARG A 254 ? 1.40431 1.20758 1.43082 0.25364  -0.21526 0.34235  254 ARG A CB  
1928 C CG  . ARG A 254 ? 1.37997 1.13044 1.35713 0.23677  -0.20469 0.34833  254 ARG A CG  
1929 C CD  . ARG A 254 ? 1.39311 1.10068 1.34267 0.25439  -0.21338 0.37189  254 ARG A CD  
1930 N NE  . ARG A 254 ? 1.45864 1.11884 1.35873 0.23677  -0.20476 0.37971  254 ARG A NE  
1931 C CZ  . ARG A 254 ? 1.42487 1.03794 1.31020 0.22998  -0.18476 0.37697  254 ARG A CZ  
1932 N NH1 . ARG A 254 ? 1.33908 0.94319 1.25248 0.23876  -0.17108 0.36565  254 ARG A NH1 
1933 N NH2 . ARG A 254 ? 1.44533 1.01963 1.28614 0.21321  -0.17803 0.38543  254 ARG A NH2 
1934 N N   . GLU A 255 ? 1.49531 1.38737 1.61747 0.29653  -0.23429 0.33848  255 GLU A N   
1935 C CA  . GLU A 255 ? 1.45925 1.41265 1.63034 0.30321  -0.24095 0.32890  255 GLU A CA  
1936 C C   . GLU A 255 ? 1.42178 1.41877 1.59237 0.28118  -0.25275 0.32285  255 GLU A C   
1937 O O   . GLU A 255 ? 1.42513 1.46147 1.62676 0.27174  -0.24697 0.30683  255 GLU A O   
1938 C CB  . GLU A 255 ? 1.47808 1.45134 1.67735 0.33572  -0.25780 0.34319  255 GLU A CB  
1939 C CG  . GLU A 255 ? 1.50875 1.55286 1.75735 0.34005  -0.26877 0.33568  255 GLU A CG  
1940 C CD  . GLU A 255 ? 1.58314 1.64856 1.87515 0.37399  -0.27358 0.34146  255 GLU A CD  
1941 O OE1 . GLU A 255 ? 1.58753 1.64283 1.87312 0.39651  -0.29054 0.36101  255 GLU A OE1 
1942 O OE2 . GLU A 255 ? 1.61998 1.71286 1.95245 0.37864  -0.26014 0.32659  255 GLU A OE2 
1943 N N   . ASN A 256 ? 1.47899 1.46902 1.61391 0.27257  -0.26901 0.33519  256 ASN A N   
1944 C CA  . ASN A 256 ? 1.40860 1.42696 1.53243 0.24685  -0.27585 0.32691  256 ASN A CA  
1945 C C   . ASN A 256 ? 1.40528 1.40526 1.51781 0.22308  -0.25219 0.30910  256 ASN A C   
1946 O O   . ASN A 256 ? 1.41603 1.36917 1.49195 0.21420  -0.24033 0.31148  256 ASN A O   
1947 C CB  . ASN A 256 ? 1.47949 1.48264 1.55795 0.24064  -0.29384 0.34263  256 ASN A CB  
1948 C CG  . ASN A 256 ? 1.47886 1.52491 1.55624 0.22221  -0.30938 0.33655  256 ASN A CG  
1949 O OD1 . ASN A 256 ? 1.48376 1.53874 1.55929 0.19908  -0.29834 0.31995  256 ASN A OD1 
1950 N ND2 . ASN A 256 ? 1.62498 1.69697 1.70286 0.23260  -0.33572 0.35008  256 ASN A ND2 
1951 N N   . GLU A 257 ? 1.28199 1.31896 1.42694 0.21323  -0.24497 0.29173  257 GLU A N   
1952 C CA  . GLU A 257 ? 1.32849 1.35141 1.46657 0.19276  -0.22322 0.27483  257 GLU A CA  
1953 C C   . GLU A 257 ? 1.29986 1.29592 1.39154 0.17054  -0.22111 0.27515  257 GLU A C   
1954 O O   . GLU A 257 ? 1.21931 1.18741 1.29517 0.15759  -0.20244 0.26643  257 GLU A O   
1955 C CB  . GLU A 257 ? 1.33989 1.41004 1.51370 0.18281  -0.22052 0.25864  257 GLU A CB  
1956 C CG  . GLU A 257 ? 1.26240 1.34996 1.47921 0.19869  -0.21035 0.25172  257 GLU A CG  
1957 C CD  . GLU A 257 ? 1.10075 1.20344 1.33356 0.18227  -0.19356 0.23285  257 GLU A CD  
1958 O OE1 . GLU A 257 ? 1.02728 1.14062 1.24720 0.16011  -0.19483 0.22559  257 GLU A OE1 
1959 O OE2 . GLU A 257 ? 1.07378 1.17561 1.33023 0.19206  -0.17894 0.22546  257 GLU A OE2 
1960 N N   . THR A 258 ? 1.38440 1.39028 1.45426 0.16570  -0.23995 0.28452  258 THR A N   
1961 C CA  . THR A 258 ? 1.35519 1.33593 1.37933 0.14538  -0.23742 0.28478  258 THR A CA  
1962 C C   . THR A 258 ? 1.34659 1.27598 1.33319 0.15128  -0.23305 0.29958  258 THR A C   
1963 O O   . THR A 258 ? 1.30280 1.20097 1.25917 0.13556  -0.21852 0.29588  258 THR A O   
1964 C CB  . THR A 258 ? 1.39967 1.40988 1.41207 0.13618  -0.25849 0.28740  258 THR A CB  
1965 O OG1 . THR A 258 ? 1.34093 1.39884 1.39206 0.13135  -0.26249 0.27431  258 THR A OG1 
1966 C CG2 . THR A 258 ? 1.42308 1.41117 1.39095 0.11328  -0.25276 0.28332  258 THR A CG2 
1967 N N   . GLU A 259 ? 1.41007 1.32978 1.39919 0.17401  -0.24463 0.31647  259 GLU A N   
1968 C CA  . GLU A 259 ? 1.42303 1.29076 1.37634 0.18046  -0.24049 0.33207  259 GLU A CA  
1969 C C   . GLU A 259 ? 1.38514 1.21586 1.33862 0.17712  -0.21523 0.32413  259 GLU A C   
1970 O O   . GLU A 259 ? 1.39780 1.18221 1.31840 0.17575  -0.20763 0.33411  259 GLU A O   
1971 C CB  . GLU A 259 ? 1.53427 1.40048 1.49508 0.20822  -0.25838 0.35158  259 GLU A CB  
1972 C CG  . GLU A 259 ? 1.63984 1.52112 1.57659 0.20976  -0.28424 0.36678  259 GLU A CG  
1973 C CD  . GLU A 259 ? 1.75217 1.63821 1.70155 0.23950  -0.30405 0.38626  259 GLU A CD  
1974 O OE1 . GLU A 259 ? 1.74295 1.60041 1.70255 0.25866  -0.29572 0.39284  259 GLU A OE1 
1975 O OE2 . GLU A 259 ? 1.81521 1.73354 1.76414 0.24401  -0.32845 0.39484  259 GLU A OE2 
1976 N N   . ILE A 260 ? 1.22142 1.07128 1.20978 0.17475  -0.20226 0.30656  260 ILE A N   
1977 C CA  . ILE A 260 ? 1.26895 1.08805 1.25588 0.16737  -0.17886 0.29627  260 ILE A CA  
1978 C C   . ILE A 260 ? 1.22088 1.03167 1.18207 0.14050  -0.16715 0.28638  260 ILE A C   
1979 O O   . ILE A 260 ? 1.15883 0.93100 1.09522 0.13148  -0.15308 0.28742  260 ILE A O   
1980 C CB  . ILE A 260 ? 1.22411 1.06774 1.25628 0.17566  -0.17005 0.28150  260 ILE A CB  
1981 C CG1 . ILE A 260 ? 1.27819 1.12478 1.33525 0.20418  -0.17844 0.29121  260 ILE A CG1 
1982 C CG2 . ILE A 260 ? 1.11848 0.93633 1.14858 0.16437  -0.14694 0.26811  260 ILE A CG2 
1983 C CD1 . ILE A 260 ? 1.25770 1.12543 1.35683 0.21342  -0.16788 0.27700  260 ILE A CD1 
1984 N N   . ILE A 261 ? 1.15010 0.99694 1.11775 0.12731  -0.17228 0.27635  261 ILE A N   
1985 C CA  . ILE A 261 ? 1.12233 0.96294 1.06680 0.10357  -0.16142 0.26659  261 ILE A CA  
1986 C C   . ILE A 261 ? 1.16410 0.97280 1.06195 0.09635  -0.16369 0.27992  261 ILE A C   
1987 O O   . ILE A 261 ? 1.21002 0.99207 1.08537 0.08234  -0.14813 0.27669  261 ILE A O   
1988 C CB  . ILE A 261 ? 1.07574 0.95824 1.03366 0.09222  -0.16815 0.25457  261 ILE A CB  
1989 C CG1 . ILE A 261 ? 1.03003 0.94356 1.03329 0.09852  -0.16457 0.24219  261 ILE A CG1 
1990 C CG2 . ILE A 261 ? 1.02733 0.90160 0.96286 0.06994  -0.15561 0.24387  261 ILE A CG2 
1991 C CD1 . ILE A 261 ? 0.92884 0.82387 0.94457 0.09857  -0.14436 0.23277  261 ILE A CD1 
1992 N N   . LYS A 262 ? 1.15463 0.96706 1.03726 0.10555  -0.18315 0.29528  262 LYS A N   
1993 C CA  . LYS A 262 ? 1.16201 0.94136 0.99748 0.10056  -0.18575 0.31032  262 LYS A CA  
1994 C C   . LYS A 262 ? 1.22840 0.96057 1.04984 0.10305  -0.16989 0.31729  262 LYS A C   
1995 O O   . LYS A 262 ? 1.17636 0.88099 0.96618 0.08739  -0.15699 0.31797  262 LYS A O   
1996 C CB  . LYS A 262 ? 1.14228 0.93087 0.96689 0.11488  -0.21052 0.32793  262 LYS A CB  
1997 C CG  . LYS A 262 ? 1.27718 1.02623 1.05165 0.11393  -0.21393 0.34727  262 LYS A CG  
1998 C CD  . LYS A 262 ? 1.40661 1.13931 1.17953 0.13895  -0.22906 0.36899  262 LYS A CD  
1999 C CE  . LYS A 262 ? 1.43014 1.13762 1.22742 0.15512  -0.21723 0.37076  262 LYS A CE  
2000 N NZ  . LYS A 262 ? 1.36034 1.01194 1.12657 0.14919  -0.19943 0.37832  262 LYS A NZ  
2001 N N   . CYS A 263 ? 1.26367 0.98633 1.10942 0.12225  -0.16982 0.32168  263 CYS A N   
2002 C CA  . CYS A 263 ? 1.20353 0.87918 1.03794 0.12508  -0.15501 0.32741  263 CYS A CA  
2003 C C   . CYS A 263 ? 1.26239 0.92887 1.09950 0.10574  -0.13224 0.31044  263 CYS A C   
2004 O O   . CYS A 263 ? 1.26881 0.89876 1.07865 0.09430  -0.11920 0.31439  263 CYS A O   
2005 C CB  . CYS A 263 ? 1.25758 0.92848 1.12197 0.14992  -0.15849 0.33158  263 CYS A CB  
2006 S SG  . CYS A 263 ? 1.36530 0.97360 1.21645 0.15546  -0.14130 0.33845  263 CYS A SG  
2007 N N   . LEU A 264 ? 1.19634 0.89629 1.06648 0.10158  -0.12724 0.29183  264 LEU A N   
2008 C CA  . LEU A 264 ? 1.18687 0.88048 1.06008 0.08419  -0.10725 0.27618  264 LEU A CA  
2009 C C   . LEU A 264 ? 1.17704 0.87062 1.02139 0.06271  -0.10176 0.27344  264 LEU A C   
2010 O O   . LEU A 264 ? 1.17087 0.85328 1.01114 0.04781  -0.08491 0.26397  264 LEU A O   
2011 C CB  . LEU A 264 ? 1.12881 0.85738 1.04156 0.08514  -0.10358 0.25796  264 LEU A CB  
2012 C CG  . LEU A 264 ? 1.21188 0.93641 1.15404 0.10291  -0.10112 0.25565  264 LEU A CG  
2013 C CD1 . LEU A 264 ? 1.06461 0.83224 1.04308 0.10486  -0.10239 0.24080  264 LEU A CD1 
2014 C CD2 . LEU A 264 ? 1.17932 0.86672 1.11556 0.09727  -0.08306 0.25102  264 LEU A CD2 
2015 N N   . ARG A 265 ? 1.19979 0.90700 1.02471 0.06095  -0.11556 0.28078  265 ARG A N   
2016 C CA  . ARG A 265 ? 1.12700 0.83334 0.92178 0.04180  -0.11034 0.27818  265 ARG A CA  
2017 C C   . ARG A 265 ? 1.25069 0.91598 1.00494 0.03523  -0.10326 0.29238  265 ARG A C   
2018 O O   . ARG A 265 ? 1.25627 0.91656 0.98587 0.01817  -0.09363 0.28914  265 ARG A O   
2019 C CB  . ARG A 265 ? 1.15393 0.88965 0.94117 0.04167  -0.12813 0.27946  265 ARG A CB  
2020 C CG  . ARG A 265 ? 1.04100 0.81725 0.85912 0.03808  -0.13055 0.26216  265 ARG A CG  
2021 C CD  . ARG A 265 ? 1.07550 0.87084 0.87312 0.02959  -0.14283 0.26155  265 ARG A CD  
2022 N NE  . ARG A 265 ? 1.16037 0.99179 0.98510 0.02477  -0.14540 0.24553  265 ARG A NE  
2023 C CZ  . ARG A 265 ? 1.22298 1.08481 1.07352 0.03421  -0.16127 0.24506  265 ARG A CZ  
2024 N NH1 . ARG A 265 ? 1.17618 1.03980 1.02872 0.04997  -0.17777 0.25979  265 ARG A NH1 
2025 N NH2 . ARG A 265 ? 1.03751 0.92884 0.91350 0.02798  -0.16029 0.22988  265 ARG A NH2 
2026 N N   . ASN A 266 ? 1.23165 0.86710 0.97796 0.04851  -0.10729 0.30822  266 ASN A N   
2027 C CA  . ASN A 266 ? 1.30465 0.89670 1.01254 0.04197  -0.09919 0.32280  266 ASN A CA  
2028 C C   . ASN A 266 ? 1.29214 0.85625 1.00697 0.03395  -0.07842 0.31695  266 ASN A C   
2029 O O   . ASN A 266 ? 1.44413 0.97078 1.12933 0.02601  -0.06898 0.32787  266 ASN A O   
2030 C CB  . ASN A 266 ? 1.34451 0.91401 1.03528 0.06054  -0.11518 0.34524  266 ASN A CB  
2031 C CG  . ASN A 266 ? 1.51160 1.09631 1.17578 0.06188  -0.13365 0.35573  266 ASN A CG  
2032 O OD1 . ASN A 266 ? 1.53849 1.13754 1.18439 0.04542  -0.13065 0.34873  266 ASN A OD1 
2033 N ND2 . ASN A 266 ? 1.56173 1.14259 1.22237 0.08176  -0.15299 0.37260  266 ASN A ND2 
2034 N N   . LYS A 267 ? 1.28521 0.86614 1.03701 0.03478  -0.07110 0.30015  267 LYS A N   
2035 C CA  . LYS A 267 ? 1.28774 0.84482 1.04702 0.02609  -0.05257 0.29286  267 LYS A CA  
2036 C C   . LYS A 267 ? 1.27409 0.84227 1.02880 0.00322  -0.03699 0.27970  267 LYS A C   
2037 O O   . LYS A 267 ? 1.29793 0.90117 1.06216 -0.00203 -0.03934 0.26851  267 LYS A O   
2038 C CB  . LYS A 267 ? 1.27028 0.83927 1.06960 0.03835  -0.05219 0.28091  267 LYS A CB  
2039 C CG  . LYS A 267 ? 1.32456 0.89169 1.13598 0.06341  -0.06772 0.29141  267 LYS A CG  
2040 C CD  . LYS A 267 ? 1.31035 0.82885 1.11117 0.07229  -0.06278 0.30293  267 LYS A CD  
2041 C CE  . LYS A 267 ? 1.36456 0.87730 1.16939 0.09847  -0.07967 0.31808  267 LYS A CE  
2042 N NZ  . LYS A 267 ? 1.46603 0.96908 1.23679 0.10149  -0.09318 0.33856  267 LYS A NZ  
2043 N N   . ASP A 268 ? 1.31094 0.84898 1.05176 -0.01034 -0.02087 0.28108  268 ASP A N   
2044 C CA  . ASP A 268 ? 1.29530 0.84544 1.03820 -0.03098 -0.00474 0.26757  268 ASP A CA  
2045 C C   . ASP A 268 ? 1.20917 0.78982 0.99127 -0.03029 -0.00170 0.24737  268 ASP A C   
2046 O O   . ASP A 268 ? 1.18140 0.75877 0.98619 -0.01855 -0.00465 0.24366  268 ASP A O   
2047 C CB  . ASP A 268 ? 1.31344 0.82671 1.03989 -0.04538 0.01176  0.27237  268 ASP A CB  
2048 C CG  . ASP A 268 ? 1.52086 0.99756 1.20705 -0.04547 0.00972  0.29415  268 ASP A CG  
2049 O OD1 . ASP A 268 ? 1.57726 1.01769 1.24836 -0.05558 0.02197  0.30097  268 ASP A OD1 
2050 O OD2 . ASP A 268 ? 1.58763 1.07135 1.25621 -0.03615 -0.00438 0.30468  268 ASP A OD2 
2051 N N   . PRO A 269 ? 1.12442 0.73350 0.91389 -0.04237 0.00488  0.23419  269 PRO A N   
2052 C CA  . PRO A 269 ? 1.17100 0.80694 0.99520 -0.04245 0.00833  0.21591  269 PRO A CA  
2053 C C   . PRO A 269 ? 1.21294 0.83007 1.05284 -0.04373 0.01727  0.21048  269 PRO A C   
2054 O O   . PRO A 269 ? 1.12470 0.75611 0.99185 -0.03588 0.01504  0.19980  269 PRO A O   
2055 C CB  . PRO A 269 ? 1.14400 0.80167 0.96552 -0.05825 0.01806  0.20580  269 PRO A CB  
2056 C CG  . PRO A 269 ? 1.13840 0.79124 0.92684 -0.06125 0.01404  0.21728  269 PRO A CG  
2057 C CD  . PRO A 269 ? 1.10511 0.72151 0.87033 -0.05590 0.01019  0.23547  269 PRO A CD  
2058 N N   . GLN A 270 ? 1.21042 0.79393 1.03202 -0.05373 0.02733  0.21789  270 GLN A N   
2059 C CA  . GLN A 270 ? 1.21293 0.77724 1.04729 -0.05858 0.03690  0.21106  270 GLN A CA  
2060 C C   . GLN A 270 ? 1.22873 0.77435 1.07292 -0.03995 0.02884  0.21459  270 GLN A C   
2061 O O   . GLN A 270 ? 1.19504 0.74254 1.06129 -0.03756 0.03213  0.20246  270 GLN A O   
2062 C CB  . GLN A 270 ? 1.25629 0.78871 1.06725 -0.07591 0.04998  0.21867  270 GLN A CB  
2063 C CG  . GLN A 270 ? 1.36743 0.89194 1.19319 -0.08985 0.06290  0.20652  270 GLN A CG  
2064 C CD  . GLN A 270 ? 1.40000 0.96352 1.25732 -0.09114 0.06353  0.18680  270 GLN A CD  
2065 O OE1 . GLN A 270 ? 1.37334 0.93414 1.24936 -0.08671 0.06333  0.17710  270 GLN A OE1 
2066 N NE2 . GLN A 270 ? 1.32612 0.92408 1.18764 -0.09745 0.06497  0.18080  270 GLN A NE2 
2067 N N   . GLU A 271 ? 1.19175 0.72058 1.01996 -0.02569 0.01800  0.23082  271 GLU A N   
2068 C CA  . GLU A 271 ? 1.23438 0.74783 1.07389 -0.00527 0.01006  0.23463  271 GLU A CA  
2069 C C   . GLU A 271 ? 1.23377 0.78552 1.10583 0.00693  0.00288  0.22154  271 GLU A C   
2070 O O   . GLU A 271 ? 1.24957 0.79573 1.14078 0.01732  0.00386  0.21455  271 GLU A O   
2071 C CB  . GLU A 271 ? 1.27141 0.76465 1.08840 0.00888  -0.00200 0.25558  271 GLU A CB  
2072 C CG  . GLU A 271 ? 1.36049 0.83560 1.18912 0.03180  -0.00964 0.26094  271 GLU A CG  
2073 C CD  . GLU A 271 ? 1.45540 0.90132 1.25835 0.04510  -0.02010 0.28374  271 GLU A CD  
2074 O OE1 . GLU A 271 ? 1.48895 0.91763 1.25981 0.03339  -0.01814 0.29600  271 GLU A OE1 
2075 O OE2 . GLU A 271 ? 1.44991 0.88923 1.26444 0.06771  -0.02969 0.28962  271 GLU A OE2 
2076 N N   . ILE A 272 ? 1.22223 0.81193 1.09975 0.00522  -0.00354 0.21777  272 ILE A N   
2077 C CA  . ILE A 272 ? 1.15299 0.77937 1.05998 0.01518  -0.01008 0.20638  272 ILE A CA  
2078 C C   . ILE A 272 ? 1.15977 0.79713 1.08745 0.00654  0.00101  0.18818  272 ILE A C   
2079 O O   . ILE A 272 ? 1.12075 0.76940 1.07166 0.01712  -0.00034 0.17954  272 ILE A O   
2080 C CB  . ILE A 272 ? 1.10697 0.76676 1.01116 0.01333  -0.01935 0.20727  272 ILE A CB  
2081 C CG1 . ILE A 272 ? 1.15652 0.80510 1.04021 0.02373  -0.03252 0.22558  272 ILE A CG1 
2082 C CG2 . ILE A 272 ? 1.07615 0.77412 1.01030 0.01945  -0.02391 0.19445  272 ILE A CG2 
2083 C CD1 . ILE A 272 ? 1.12506 0.80679 1.01035 0.02731  -0.04604 0.22678  272 ILE A CD1 
2084 N N   . LEU A 273 ? 1.12273 0.75753 1.04221 -0.01257 0.01224  0.18221  273 LEU A N   
2085 C CA  . LEU A 273 ? 1.08689 0.73336 1.02508 -0.02130 0.02152  0.16536  273 LEU A CA  
2086 C C   . LEU A 273 ? 1.14560 0.76244 1.08851 -0.01810 0.02729  0.16192  273 LEU A C   
2087 O O   . LEU A 273 ? 1.08062 0.70882 1.04330 -0.01524 0.02963  0.14870  273 LEU A O   
2088 C CB  . LEU A 273 ? 1.02266 0.67578 0.95273 -0.04172 0.03146  0.16050  273 LEU A CB  
2089 C CG  . LEU A 273 ? 1.00075 0.68699 0.93081 -0.04606 0.02858  0.15792  273 LEU A CG  
2090 C CD1 . LEU A 273 ? 1.04532 0.72998 0.96163 -0.06442 0.03937  0.15750  273 LEU A CD1 
2091 C CD2 . LEU A 273 ? 0.92175 0.64168 0.87733 -0.04260 0.02653  0.14361  273 LEU A CD2 
2092 N N   . LEU A 274 ? 1.09335 0.67021 1.01628 -0.01889 0.02998  0.17362  274 LEU A N   
2093 C CA  . LEU A 274 ? 1.21016 0.75227 1.13433 -0.01447 0.03504  0.17150  274 LEU A CA  
2094 C C   . LEU A 274 ? 1.24959 0.80083 1.19454 0.00629  0.02881  0.16614  274 LEU A C   
2095 O O   . LEU A 274 ? 1.26050 0.80294 1.21683 0.00726  0.03480  0.15410  274 LEU A O   
2096 C CB  . LEU A 274 ? 1.25907 0.75605 1.15714 -0.01249 0.03535  0.18907  274 LEU A CB  
2097 C CG  . LEU A 274 ? 1.44433 0.89294 1.33472 -0.01288 0.04314  0.18943  274 LEU A CG  
2098 C CD1 . LEU A 274 ? 1.25344 0.66010 1.11278 -0.02306 0.04795  0.20579  274 LEU A CD1 
2099 C CD2 . LEU A 274 ? 1.44217 0.87662 1.34315 0.01202  0.03691  0.19083  274 LEU A CD2 
2100 N N   . ASN A 275 ? 1.24545 0.81401 1.19505 0.02287  0.01699  0.17491  275 ASN A N   
2101 C CA  . ASN A 275 ? 1.21979 0.79317 1.18798 0.04480  0.01114  0.17346  275 ASN A CA  
2102 C C   . ASN A 275 ? 1.15136 0.76905 1.14578 0.04812  0.00907  0.15982  275 ASN A C   
2103 O O   . ASN A 275 ? 1.17704 0.80090 1.18976 0.06382  0.00780  0.15481  275 ASN A O   
2104 C CB  . ASN A 275 ? 1.16365 0.73050 1.12367 0.06190  -0.00130 0.19181  275 ASN A CB  
2105 C CG  . ASN A 275 ? 1.28695 0.80279 1.22132 0.06310  0.00107  0.20618  275 ASN A CG  
2106 O OD1 . ASN A 275 ? 1.26721 0.75105 1.20306 0.07163  0.00621  0.20469  275 ASN A OD1 
2107 N ND2 . ASN A 275 ? 1.28743 0.79362 1.19653 0.05437  -0.00205 0.22006  275 ASN A ND2 
2108 N N   . GLU A 276 ? 1.06630 0.71332 1.06237 0.03379  0.00975  0.15370  276 GLU A N   
2109 C CA  . GLU A 276 ? 1.07436 0.76048 1.09269 0.03492  0.00870  0.14123  276 GLU A CA  
2110 C C   . GLU A 276 ? 1.09401 0.77673 1.12625 0.03605  0.01721  0.12641  276 GLU A C   
2111 O O   . GLU A 276 ? 1.12986 0.83836 1.18150 0.04415  0.01590  0.11840  276 GLU A O   
2112 C CB  . GLU A 276 ? 1.03621 0.74550 1.05039 0.01780  0.01039  0.13666  276 GLU A CB  
2113 C CG  . GLU A 276 ? 1.01075 0.73667 1.01610 0.01739  0.00123  0.14653  276 GLU A CG  
2114 C CD  . GLU A 276 ? 1.07655 0.82663 1.08149 0.00235  0.00456  0.13865  276 GLU A CD  
2115 O OE1 . GLU A 276 ? 1.04849 0.80746 1.06424 -0.00477 0.01202  0.12605  276 GLU A OE1 
2116 O OE2 . GLU A 276 ? 1.03388 0.79326 1.02685 -0.00197 -0.00025 0.14481  276 GLU A OE2 
2117 N N   . ALA A 277 ? 1.12252 0.77406 1.14418 0.02679  0.02625  0.12213  277 ALA A N   
2118 C CA  . ALA A 277 ? 1.17833 0.82700 1.20995 0.02492  0.03422  0.10637  277 ALA A CA  
2119 C C   . ALA A 277 ? 1.29531 0.93443 1.33816 0.04542  0.03382  0.10466  277 ALA A C   
2120 O O   . ALA A 277 ? 1.26011 0.91593 1.31773 0.04991  0.03709  0.09216  277 ALA A O   
2121 C CB  . ALA A 277 ? 1.24797 0.86504 1.26492 0.00832  0.04326  0.10199  277 ALA A CB  
2122 N N   . PHE A 278 ? 1.26077 0.87353 1.29650 0.05881  0.03011  0.11741  278 PHE A N   
2123 C CA  . PHE A 278 ? 1.30438 0.90344 1.35038 0.07975  0.03088  0.11625  278 PHE A CA  
2124 C C   . PHE A 278 ? 1.33359 0.96500 1.39906 0.09914  0.02137  0.12252  278 PHE A C   
2125 O O   . PHE A 278 ? 1.32336 0.94465 1.39859 0.11929  0.02096  0.12448  278 PHE A O   
2126 C CB  . PHE A 278 ? 1.42074 0.96923 1.44911 0.08594  0.03254  0.12664  278 PHE A CB  
2127 C CG  . PHE A 278 ? 1.42338 0.94213 1.42853 0.06434  0.03824  0.12867  278 PHE A CG  
2128 C CD1 . PHE A 278 ? 1.45299 0.95807 1.43970 0.05964  0.03334  0.14555  278 PHE A CD1 
2129 C CD2 . PHE A 278 ? 1.50786 1.01317 1.50930 0.04805  0.04860  0.11366  278 PHE A CD2 
2130 C CE1 . PHE A 278 ? 1.53861 1.01735 1.50461 0.03874  0.04016  0.14760  278 PHE A CE1 
2131 C CE2 . PHE A 278 ? 1.56538 1.04613 1.54812 0.02689  0.05423  0.11526  278 PHE A CE2 
2132 C CZ  . PHE A 278 ? 1.58924 1.05677 1.55480 0.02213  0.05074  0.13235  278 PHE A CZ  
2133 N N   . VAL A 279 ? 1.27211 0.94171 1.34415 0.09395  0.01380  0.12560  279 VAL A N   
2134 C CA  . VAL A 279 ? 1.24124 0.94352 1.33477 0.11103  0.00534  0.12945  279 VAL A CA  
2135 C C   . VAL A 279 ? 1.29843 1.02398 1.41346 0.11561  0.01228  0.11408  279 VAL A C   
2136 O O   . VAL A 279 ? 1.18377 0.92632 1.31905 0.13348  0.01002  0.11448  279 VAL A O   
2137 C CB  . VAL A 279 ? 1.18093 0.91449 1.27387 0.10444  -0.00566 0.13772  279 VAL A CB  
2138 C CG1 . VAL A 279 ? 1.19103 0.89929 1.25812 0.09801  -0.01080 0.15211  279 VAL A CG1 
2139 C CG2 . VAL A 279 ? 1.07876 0.84117 1.17603 0.08745  -0.00201 0.12616  279 VAL A CG2 
2140 N N   . VAL A 280 ? 1.49951 1.22654 1.61045 0.10007  0.02099  0.10062  280 VAL A N   
2141 C CA  . VAL A 280 ? 1.48132 1.22381 1.60725 0.10364  0.02901  0.08570  280 VAL A CA  
2142 C C   . VAL A 280 ? 1.58989 1.29614 1.71189 0.11352  0.03782  0.07943  280 VAL A C   
2143 O O   . VAL A 280 ? 1.57879 1.24769 1.68158 0.10492  0.04164  0.07947  280 VAL A O   
2144 C CB  . VAL A 280 ? 1.50768 1.26521 1.62882 0.08385  0.03360  0.07451  280 VAL A CB  
2145 C CG1 . VAL A 280 ? 1.46967 1.19573 1.56967 0.06749  0.03839  0.07165  280 VAL A CG1 
2146 C CG2 . VAL A 280 ? 1.45142 1.22617 1.58526 0.08716  0.04128  0.06018  280 VAL A CG2 
2147 N N   . PRO A 281 ? 1.56044 1.27500 1.69975 0.13136  0.04178  0.07404  281 PRO A N   
2148 C CA  . PRO A 281 ? 1.56861 1.24491 1.70247 0.14186  0.05091  0.06731  281 PRO A CA  
2149 C C   . PRO A 281 ? 1.68280 1.34364 1.80391 0.12643  0.06154  0.05030  281 PRO A C   
2150 O O   . PRO A 281 ? 1.62628 1.24491 1.73077 0.12277  0.06717  0.04645  281 PRO A O   
2151 C CB  . PRO A 281 ? 1.56261 1.25993 1.72127 0.16537  0.05270  0.06553  281 PRO A CB  
2152 C CG  . PRO A 281 ? 1.54693 1.29704 1.72411 0.16185  0.04705  0.06675  281 PRO A CG  
2153 C CD  . PRO A 281 ? 1.53102 1.28988 1.69455 0.13972  0.04062  0.07087  281 PRO A CD  
2154 N N   . TYR A 282 ? 1.83324 1.52680 1.96087 0.11666  0.06394  0.04021  282 TYR A N   
2155 C CA  . TYR A 282 ? 1.76744 1.45285 1.88272 0.10060  0.07175  0.02458  282 TYR A CA  
2156 C C   . TYR A 282 ? 1.66647 1.38068 1.77966 0.08171  0.06661  0.02542  282 TYR A C   
2157 O O   . TYR A 282 ? 1.68318 1.43445 1.80931 0.08279  0.06460  0.02481  282 TYR A O   
2158 C CB  . TYR A 282 ? 1.80901 1.50394 1.93263 0.10996  0.08127  0.00992  282 TYR A CB  
2159 C CG  . TYR A 282 ? 1.88483 1.54510 2.00691 0.12702  0.08917  0.00490  282 TYR A CG  
2160 C CD1 . TYR A 282 ? 1.96553 1.57770 2.06853 0.12225  0.09196  0.00338  282 TYR A CD1 
2161 C CD2 . TYR A 282 ? 1.89284 1.56776 2.03268 0.14766  0.09477  0.00117  282 TYR A CD2 
2162 C CE1 . TYR A 282 ? 2.08613 1.66217 2.18617 0.13842  0.09975  -0.00168 282 TYR A CE1 
2163 C CE2 . TYR A 282 ? 2.06752 1.70956 2.20627 0.16511  0.10295  -0.00412 282 TYR A CE2 
2164 C CZ  . TYR A 282 ? 2.13188 1.72268 2.24983 0.16078  0.10527  -0.00560 282 TYR A CZ  
2165 O OH  . TYR A 282 ? 2.01952 1.57326 2.13479 0.17854  0.11385  -0.01117 282 TYR A OH  
2166 N N   . GLY A 283 ? 1.55066 1.24771 1.64815 0.06460  0.06505  0.02694  283 GLY A N   
2167 C CA  . GLY A 283 ? 1.40662 1.12909 1.50221 0.04754  0.06128  0.02659  283 GLY A CA  
2168 C C   . GLY A 283 ? 1.23349 0.96423 1.32512 0.03617  0.06669  0.01090  283 GLY A C   
2169 O O   . GLY A 283 ? 1.22603 0.93607 1.31112 0.03690  0.07362  -0.00073 283 GLY A O   
2170 N N   . THR A 284 ? 1.13738 0.89830 1.23194 0.02596  0.06311  0.01056  284 THR A N   
2171 C CA  . THR A 284 ? 1.04930 0.82083 1.13859 0.01333  0.06571  -0.00180 284 THR A CA  
2172 C C   . THR A 284 ? 1.07240 0.85426 1.15773 -0.00257 0.06085  0.00252  284 THR A C   
2173 O O   . THR A 284 ? 1.07270 0.85730 1.15969 -0.00264 0.05626  0.01445  284 THR A O   
2174 C CB  . THR A 284 ? 0.98497 0.78679 1.08329 0.01949  0.06707  -0.00686 284 THR A CB  
2175 O OG1 . THR A 284 ? 1.05290 0.88369 1.15936 0.01750  0.06090  0.00204  284 THR A OG1 
2176 C CG2 . THR A 284 ? 0.98450 0.78387 1.09197 0.03759  0.07172  -0.00768 284 THR A CG2 
2177 N N   . PRO A 285 ? 1.01931 0.80776 1.09913 -0.01607 0.06169  -0.00714 285 PRO A N   
2178 C CA  . PRO A 285 ? 0.98608 0.78936 1.06546 -0.02954 0.05751  -0.00321 285 PRO A CA  
2179 C C   . PRO A 285 ? 1.01021 0.84151 1.09817 -0.02511 0.05262  0.00588  285 PRO A C   
2180 O O   . PRO A 285 ? 1.03784 0.87641 1.12539 -0.03258 0.04966  0.01231  285 PRO A O   
2181 C CB  . PRO A 285 ? 0.93959 0.75164 1.01481 -0.04081 0.05832  -0.01614 285 PRO A CB  
2182 C CG  . PRO A 285 ? 0.92992 0.71551 0.99717 -0.03908 0.06368  -0.02657 285 PRO A CG  
2183 C CD  . PRO A 285 ? 0.99568 0.77470 1.06792 -0.02054 0.06636  -0.02219 285 PRO A CD  
2184 N N   . LEU A 286 ? 0.98837 0.83499 1.08384 -0.01369 0.05239  0.00626  286 LEU A N   
2185 C CA  . LEU A 286 ? 0.93226 0.80407 1.03562 -0.01035 0.04795  0.01389  286 LEU A CA  
2186 C C   . LEU A 286 ? 0.89763 0.76752 1.00757 0.00091  0.04516  0.02431  286 LEU A C   
2187 O O   . LEU A 286 ? 0.91635 0.80701 1.03431 0.00514  0.04173  0.02931  286 LEU A O   
2188 C CB  . LEU A 286 ? 0.84617 0.73906 0.95356 -0.00772 0.04942  0.00772  286 LEU A CB  
2189 C CG  . LEU A 286 ? 0.85885 0.75851 0.95935 -0.01805 0.04995  -0.00114 286 LEU A CG  
2190 C CD1 . LEU A 286 ? 0.83921 0.72826 0.93373 -0.01633 0.05521  -0.01261 286 LEU A CD1 
2191 C CD2 . LEU A 286 ? 0.81082 0.73616 0.91468 -0.01864 0.04729  0.00109  286 LEU A CD2 
2192 N N   . SER A 287 ? 0.93289 0.77804 1.03924 0.00547  0.04597  0.02801  287 SER A N   
2193 C CA  . SER A 287 ? 0.95263 0.79669 1.06528 0.01754  0.04191  0.03858  287 SER A CA  
2194 C C   . SER A 287 ? 0.90264 0.75934 1.01393 0.01280  0.03507  0.04870  287 SER A C   
2195 O O   . SER A 287 ? 0.98106 0.83159 1.08247 0.00141  0.03479  0.05034  287 SER A O   
2196 C CB  . SER A 287 ? 0.92025 0.73123 1.02639 0.02327  0.04373  0.04180  287 SER A CB  
2197 O OG  . SER A 287 ? 1.02842 0.83007 1.13941 0.03405  0.04936  0.03418  287 SER A OG  
2198 N N   . VAL A 288 ? 0.81142 0.68655 0.93279 0.02108  0.02997  0.05480  288 VAL A N   
2199 C CA  . VAL A 288 ? 0.80816 0.69432 0.92715 0.01765  0.02279  0.06395  288 VAL A CA  
2200 C C   . VAL A 288 ? 0.85139 0.73034 0.97318 0.02941  0.01692  0.07422  288 VAL A C   
2201 O O   . VAL A 288 ? 0.95092 0.84776 1.08674 0.03911  0.01298  0.07669  288 VAL A O   
2202 C CB  . VAL A 288 ? 0.82138 0.73657 0.94889 0.01510  0.02060  0.06186  288 VAL A CB  
2203 C CG1 . VAL A 288 ? 0.75625 0.68050 0.88063 0.01258  0.01283  0.07055  288 VAL A CG1 
2204 C CG2 . VAL A 288 ? 0.80442 0.72487 0.92745 0.00461  0.02547  0.05318  288 VAL A CG2 
2205 N N   . ASN A 289 ? 0.89117 0.74394 0.99983 0.02859  0.01629  0.08070  289 ASN A N   
2206 C CA  . ASN A 289 ? 0.89634 0.73721 1.00564 0.04149  0.01070  0.09114  289 ASN A CA  
2207 C C   . ASN A 289 ? 0.87763 0.74098 0.99199 0.04519  0.00024  0.09994  289 ASN A C   
2208 O O   . ASN A 289 ? 0.84335 0.71405 0.96932 0.05889  -0.00563 0.10568  289 ASN A O   
2209 C CB  . ASN A 289 ? 0.93195 0.73886 1.02213 0.03731  0.01199  0.09789  289 ASN A CB  
2210 C CG  . ASN A 289 ? 1.10030 0.88205 1.18544 0.03311  0.02171  0.08913  289 ASN A CG  
2211 O OD1 . ASN A 289 ? 1.11014 0.88659 1.20450 0.04273  0.02576  0.08261  289 ASN A OD1 
2212 N ND2 . ASN A 289 ? 0.91302 0.67924 0.98334 0.01818  0.02584  0.08849  289 ASN A ND2 
2213 N N   . PHE A 290 ? 0.81638 0.69107 0.92237 0.03321  -0.00236 0.10072  290 PHE A N   
2214 C CA  . PHE A 290 ? 0.77051 0.66363 0.87672 0.03354  -0.01251 0.10801  290 PHE A CA  
2215 C C   . PHE A 290 ? 0.74497 0.65843 0.85251 0.02206  -0.01075 0.10075  290 PHE A C   
2216 O O   . PHE A 290 ? 0.77773 0.68375 0.87119 0.01083  -0.00722 0.09899  290 PHE A O   
2217 C CB  . PHE A 290 ? 0.80526 0.68022 0.89067 0.03082  -0.01791 0.11917  290 PHE A CB  
2218 C CG  . PHE A 290 ? 0.85870 0.71442 0.94199 0.04383  -0.02213 0.12903  290 PHE A CG  
2219 C CD1 . PHE A 290 ? 0.83212 0.70234 0.92561 0.05634  -0.03334 0.13702  290 PHE A CD1 
2220 C CD2 . PHE A 290 ? 0.91128 0.73428 0.98302 0.04374  -0.01522 0.13048  290 PHE A CD2 
2221 C CE1 . PHE A 290 ? 0.91518 0.76743 1.00738 0.07060  -0.03792 0.14707  290 PHE A CE1 
2222 C CE2 . PHE A 290 ? 0.94296 0.74398 1.01143 0.05700  -0.01889 0.14037  290 PHE A CE2 
2223 C CZ  . PHE A 290 ? 0.95684 0.77231 1.03552 0.07145  -0.03035 0.14902  290 PHE A CZ  
2224 N N   . GLY A 291 ? 0.79588 0.73441 0.92053 0.02503  -0.01262 0.09680  291 GLY A N   
2225 C CA  . GLY A 291 ? 0.67721 0.63272 0.80263 0.01512  -0.01140 0.09098  291 GLY A CA  
2226 C C   . GLY A 291 ? 0.69280 0.67241 0.82864 0.01593  -0.01969 0.09355  291 GLY A C   
2227 O O   . GLY A 291 ? 0.67725 0.66197 0.81676 0.02253  -0.02870 0.10115  291 GLY A O   
2228 N N   . PRO A 292 ? 0.67904 0.67373 0.81947 0.00868  -0.01727 0.08745  292 PRO A N   
2229 C CA  . PRO A 292 ? 0.70888 0.72545 0.85845 0.00648  -0.02466 0.08900  292 PRO A CA  
2230 C C   . PRO A 292 ? 0.74034 0.77442 0.91238 0.01727  -0.02796 0.09140  292 PRO A C   
2231 O O   . PRO A 292 ? 0.76988 0.80237 0.95266 0.02563  -0.02131 0.08863  292 PRO A O   
2232 C CB  . PRO A 292 ? 0.65646 0.68082 0.80693 -0.00244 -0.01842 0.08138  292 PRO A CB  
2233 C CG  . PRO A 292 ? 0.64612 0.65205 0.78116 -0.00699 -0.01163 0.07798  292 PRO A CG  
2234 C CD  . PRO A 292 ? 0.68068 0.67118 0.81483 0.00060  -0.00883 0.07979  292 PRO A CD  
2235 N N   . THR A 293 ? 0.66274 0.71434 0.84201 0.01713  -0.03839 0.09615  293 THR A N   
2236 C CA  . THR A 293 ? 0.73036 0.80534 0.93484 0.02662  -0.04233 0.09837  293 THR A CA  
2237 C C   . THR A 293 ? 0.67941 0.78057 0.89467 0.01740  -0.04795 0.09687  293 THR A C   
2238 O O   . THR A 293 ? 0.70969 0.80685 0.90984 0.00502  -0.05071 0.09529  293 THR A O   
2239 C CB  . THR A 293 ? 0.69349 0.76533 0.89980 0.03899  -0.05230 0.10804  293 THR A CB  
2240 O OG1 . THR A 293 ? 0.71864 0.78112 0.90382 0.03241  -0.06219 0.11392  293 THR A OG1 
2241 C CG2 . THR A 293 ? 0.75323 0.80015 0.95447 0.04965  -0.04514 0.10895  293 THR A CG2 
2242 N N   . VAL A 294 ? 0.64599 0.77382 0.88806 0.02331  -0.04887 0.09689  294 VAL A N   
2243 C CA  . VAL A 294 ? 0.61856 0.77456 0.87473 0.01499  -0.05641 0.09691  294 VAL A CA  
2244 C C   . VAL A 294 ? 0.60812 0.77088 0.86212 0.01773  -0.07291 0.10502  294 VAL A C   
2245 O O   . VAL A 294 ? 0.65146 0.83364 0.92616 0.02932  -0.08003 0.11029  294 VAL A O   
2246 C CB  . VAL A 294 ? 0.72636 0.91102 1.01364 0.01960  -0.05016 0.09391  294 VAL A CB  
2247 C CG1 . VAL A 294 ? 0.64287 0.85584 0.94412 0.00633  -0.05540 0.09238  294 VAL A CG1 
2248 C CG2 . VAL A 294 ? 0.71382 0.88598 0.99765 0.01985  -0.03377 0.08690  294 VAL A CG2 
2249 N N   . ASP A 295 ? 0.67313 0.81977 0.90109 0.00775  -0.07906 0.10613  295 ASP A N   
2250 C CA  . ASP A 295 ? 0.70080 0.84975 0.91967 0.00919  -0.09489 0.11391  295 ASP A CA  
2251 C C   . ASP A 295 ? 0.66648 0.84709 0.90031 0.00107  -0.10736 0.11388  295 ASP A C   
2252 O O   . ASP A 295 ? 0.67961 0.87098 0.91384 0.00521  -0.12248 0.12105  295 ASP A O   
2253 C CB  . ASP A 295 ? 0.65653 0.77558 0.83953 0.00116  -0.09533 0.11443  295 ASP A CB  
2254 C CG  . ASP A 295 ? 0.69933 0.81417 0.86953 -0.01574 -0.09066 0.10598  295 ASP A CG  
2255 O OD1 . ASP A 295 ? 0.73474 0.86341 0.92096 -0.02146 -0.08438 0.09968  295 ASP A OD1 
2256 O OD2 . ASP A 295 ? 0.73755 0.83396 0.88045 -0.02314 -0.09281 0.10585  295 ASP A OD2 
2257 N N   . GLY A 296 ? 0.73090 0.92624 0.97615 -0.01100 -0.10194 0.10635  296 GLY A N   
2258 C CA  . GLY A 296 ? 0.63580 0.85742 0.89141 -0.02314 -0.11317 0.10492  296 GLY A CA  
2259 C C   . GLY A 296 ? 0.72497 0.93032 0.95052 -0.03860 -0.11975 0.10209  296 GLY A C   
2260 O O   . GLY A 296 ? 0.60481 0.82900 0.83437 -0.04954 -0.13156 0.10088  296 GLY A O   
2261 N N   . ASP A 297 ? 0.73232 0.90382 0.92818 -0.04004 -0.11217 0.10040  297 ASP A N   
2262 C CA  . ASP A 297 ? 0.71147 0.86371 0.87589 -0.05244 -0.11619 0.09733  297 ASP A CA  
2263 C C   . ASP A 297 ? 0.70826 0.83720 0.85859 -0.05927 -0.10076 0.08974  297 ASP A C   
2264 O O   . ASP A 297 ? 0.70767 0.83720 0.85622 -0.07211 -0.09819 0.08293  297 ASP A O   
2265 C CB  . ASP A 297 ? 0.63446 0.76924 0.77487 -0.04514 -0.12345 0.10473  297 ASP A CB  
2266 C CG  . ASP A 297 ? 0.78564 0.90932 0.89588 -0.05748 -0.13209 0.10260  297 ASP A CG  
2267 O OD1 . ASP A 297 ? 0.73205 0.85606 0.83759 -0.07179 -0.13055 0.09406  297 ASP A OD1 
2268 O OD2 . ASP A 297 ? 0.71879 0.83154 0.80829 -0.05285 -0.14001 0.10952  297 ASP A OD2 
2269 N N   . PHE A 298 ? 0.68895 0.79723 0.82987 -0.05064 -0.09060 0.09102  298 PHE A N   
2270 C CA  . PHE A 298 ? 0.75486 0.84586 0.88758 -0.05493 -0.07644 0.08444  298 PHE A CA  
2271 C C   . PHE A 298 ? 0.74334 0.84928 0.90058 -0.05467 -0.06831 0.08121  298 PHE A C   
2272 O O   . PHE A 298 ? 0.71969 0.81856 0.87298 -0.06249 -0.06026 0.07552  298 PHE A O   
2273 C CB  . PHE A 298 ? 0.67636 0.74490 0.79524 -0.04665 -0.06827 0.08642  298 PHE A CB  
2274 C CG  . PHE A 298 ? 0.65922 0.71046 0.76637 -0.05128 -0.05619 0.08008  298 PHE A CG  
2275 C CD1 . PHE A 298 ? 0.70931 0.74340 0.79179 -0.05854 -0.05526 0.07695  298 PHE A CD1 
2276 C CD2 . PHE A 298 ? 0.66453 0.71703 0.78475 -0.04775 -0.04569 0.07713  298 PHE A CD2 
2277 C CE1 . PHE A 298 ? 0.65252 0.67237 0.72634 -0.06104 -0.04428 0.07139  298 PHE A CE1 
2278 C CE2 . PHE A 298 ? 0.61552 0.65364 0.72544 -0.05099 -0.03589 0.07203  298 PHE A CE2 
2279 C CZ  . PHE A 298 ? 0.65315 0.67559 0.74119 -0.05708 -0.03532 0.06936  298 PHE A CZ  
2280 N N   . LEU A 299 ? 0.67711 0.80289 0.85876 -0.04520 -0.06983 0.08503  299 LEU A N   
2281 C CA  . LEU A 299 ? 0.67388 0.81311 0.87765 -0.04295 -0.06003 0.08229  299 LEU A CA  
2282 C C   . LEU A 299 ? 0.69573 0.86793 0.92806 -0.04043 -0.06762 0.08524  299 LEU A C   
2283 O O   . LEU A 299 ? 0.62642 0.80745 0.86920 -0.02807 -0.07364 0.09084  299 LEU A O   
2284 C CB  . LEU A 299 ? 0.72450 0.85061 0.92806 -0.03081 -0.04993 0.08269  299 LEU A CB  
2285 C CG  . LEU A 299 ? 0.79075 0.91814 1.00307 -0.03064 -0.03660 0.07789  299 LEU A CG  
2286 C CD1 . LEU A 299 ? 0.81326 0.92531 1.00782 -0.04221 -0.03153 0.07327  299 LEU A CD1 
2287 C CD2 . LEU A 299 ? 0.67628 0.78921 0.88549 -0.01855 -0.02957 0.07817  299 LEU A CD2 
2288 N N   . THR A 300 ? 0.74255 0.93289 0.98785 -0.05216 -0.06742 0.08178  300 THR A N   
2289 C CA  . THR A 300 ? 0.69732 0.92304 0.97042 -0.05379 -0.07629 0.08388  300 THR A CA  
2290 C C   . THR A 300 ? 0.64932 0.89851 0.95313 -0.04432 -0.06749 0.08430  300 THR A C   
2291 O O   . THR A 300 ? 0.63209 0.91396 0.96340 -0.04127 -0.07442 0.08695  300 THR A O   
2292 C CB  . THR A 300 ? 0.70309 0.93677 0.97531 -0.07352 -0.07981 0.07936  300 THR A CB  
2293 O OG1 . THR A 300 ? 0.73803 0.96141 1.00776 -0.08089 -0.06520 0.07458  300 THR A OG1 
2294 C CG2 . THR A 300 ? 0.78596 0.99650 1.02697 -0.08222 -0.08848 0.07791  300 THR A CG2 
2295 N N   . ASP A 301 ? 0.64370 0.87817 0.94344 -0.03924 -0.05260 0.08152  301 ASP A N   
2296 C CA  . ASP A 301 ? 0.66202 0.91556 0.98657 -0.03147 -0.04160 0.08035  301 ASP A CA  
2297 C C   . ASP A 301 ? 0.65683 0.88367 0.96566 -0.02278 -0.02917 0.07797  301 ASP A C   
2298 O O   . ASP A 301 ? 0.59697 0.79474 0.87905 -0.02546 -0.02869 0.07699  301 ASP A O   
2299 C CB  . ASP A 301 ? 0.55228 0.82541 0.89109 -0.04607 -0.03506 0.07688  301 ASP A CB  
2300 C CG  . ASP A 301 ? 0.61085 0.91575 0.98261 -0.03879 -0.02624 0.07656  301 ASP A CG  
2301 O OD1 . ASP A 301 ? 0.56560 0.87452 0.94802 -0.02120 -0.02383 0.07804  301 ASP A OD1 
2302 O OD2 . ASP A 301 ? 0.59692 0.92228 0.98378 -0.05106 -0.02090 0.07463  301 ASP A OD2 
2303 N N   . MET A 302 ? 0.58309 0.82110 0.90894 -0.01282 -0.01895 0.07645  302 MET A N   
2304 C CA  . MET A 302 ? 0.68249 0.89647 0.99364 -0.00513 -0.00778 0.07324  302 MET A CA  
2305 C C   . MET A 302 ? 0.68039 0.87821 0.97243 -0.01750 0.00059  0.06917  302 MET A C   
2306 O O   . MET A 302 ? 0.68316 0.89513 0.98345 -0.02731 0.00590  0.06769  302 MET A O   
2307 C CB  . MET A 302 ? 0.74082 0.96997 1.07328 0.00848  0.00163  0.07147  302 MET A CB  
2308 C CG  . MET A 302 ? 0.65791 0.90396 1.01087 0.02194  -0.00830 0.07665  302 MET A CG  
2309 S SD  . MET A 302 ? 1.16090 1.42896 1.54424 0.04084  0.00136  0.07496  302 MET A SD  
2310 C CE  . MET A 302 ? 0.81475 1.07145 1.18633 0.03534  0.02093  0.06649  302 MET A CE  
2311 N N   . PRO A 303 ? 0.67430 0.84304 0.94108 -0.01771 0.00157  0.06787  303 PRO A N   
2312 C CA  . PRO A 303 ? 0.66237 0.81596 0.91046 -0.02928 0.00615  0.06533  303 PRO A CA  
2313 C C   . PRO A 303 ? 0.68143 0.84027 0.93277 -0.03162 0.01885  0.06224  303 PRO A C   
2314 O O   . PRO A 303 ? 0.72493 0.88096 0.96899 -0.04298 0.02163  0.06194  303 PRO A O   
2315 C CB  . PRO A 303 ? 0.71192 0.83781 0.93728 -0.02556 0.00525  0.06453  303 PRO A CB  
2316 C CG  . PRO A 303 ? 0.68658 0.81116 0.91846 -0.01226 0.00402  0.06572  303 PRO A CG  
2317 C CD  . PRO A 303 ? 0.67832 0.82717 0.93297 -0.00805 -0.00224 0.06932  303 PRO A CD  
2318 N N   . ASP A 304 ? 0.62489 0.78960 0.88517 -0.02139 0.02702  0.05998  304 ASP A N   
2319 C CA  . ASP A 304 ? 0.64556 0.81657 0.90726 -0.02413 0.03960  0.05717  304 ASP A CA  
2320 C C   . ASP A 304 ? 0.65941 0.85386 0.93760 -0.03456 0.04147  0.05909  304 ASP A C   
2321 O O   . ASP A 304 ? 0.67081 0.86345 0.94175 -0.04341 0.04967  0.05867  304 ASP A O   
2322 C CB  . ASP A 304 ? 0.66501 0.84103 0.93532 -0.01105 0.04823  0.05350  304 ASP A CB  
2323 C CG  . ASP A 304 ? 0.91069 1.10186 1.20281 0.00016  0.04283  0.05525  304 ASP A CG  
2324 O OD1 . ASP A 304 ? 0.89847 1.11407 1.21349 0.00536  0.04894  0.05441  304 ASP A OD1 
2325 O OD2 . ASP A 304 ? 0.96832 1.14651 1.25411 0.00440  0.03277  0.05779  304 ASP A OD2 
2326 N N   . ILE A 305 ? 0.66224 0.87879 0.96218 -0.03434 0.03360  0.06161  305 ILE A N   
2327 C CA  . ILE A 305 ? 0.63150 0.87279 0.94939 -0.04633 0.03427  0.06310  305 ILE A CA  
2328 C C   . ILE A 305 ? 0.60057 0.82644 0.90095 -0.06256 0.02914  0.06425  305 ILE A C   
2329 O O   . ILE A 305 ? 0.55682 0.78524 0.85617 -0.07492 0.03602  0.06441  305 ILE A O   
2330 C CB  . ILE A 305 ? 0.66217 0.93388 1.00956 -0.04107 0.02548  0.06535  305 ILE A CB  
2331 C CG1 . ILE A 305 ? 0.66997 0.95382 1.03415 -0.02293 0.03198  0.06393  305 ILE A CG1 
2332 C CG2 . ILE A 305 ? 0.51753 0.81889 0.88659 -0.05564 0.02543  0.06640  305 ILE A CG2 
2333 C CD1 . ILE A 305 ? 0.47241 0.79057 0.87014 -0.01489 0.02477  0.06661  305 ILE A CD1 
2334 N N   . LEU A 306 ? 0.62005 0.82741 0.90472 -0.06264 0.01802  0.06499  306 LEU A N   
2335 C CA  . LEU A 306 ? 0.66196 0.85119 0.92786 -0.07644 0.01387  0.06497  306 LEU A CA  
2336 C C   . LEU A 306 ? 0.66083 0.82784 0.90632 -0.08011 0.02432  0.06399  306 LEU A C   
2337 O O   . LEU A 306 ? 0.64563 0.80791 0.88572 -0.09305 0.02770  0.06455  306 LEU A O   
2338 C CB  . LEU A 306 ? 0.58957 0.76148 0.83983 -0.07364 0.00222  0.06527  306 LEU A CB  
2339 C CG  . LEU A 306 ? 0.58043 0.77225 0.84759 -0.06798 -0.00941 0.06759  306 LEU A CG  
2340 C CD1 . LEU A 306 ? 0.63009 0.80280 0.87805 -0.06538 -0.01965 0.06853  306 LEU A CD1 
2341 C CD2 . LEU A 306 ? 0.52862 0.74793 0.81644 -0.07925 -0.01517 0.06825  306 LEU A CD2 
2342 N N   . LEU A 307 ? 0.63017 0.78257 0.86349 -0.06907 0.02902  0.06275  307 LEU A N   
2343 C CA  . LEU A 307 ? 0.63467 0.76950 0.84983 -0.07055 0.03819  0.06226  307 LEU A CA  
2344 C C   . LEU A 307 ? 0.69861 0.84705 0.92234 -0.07769 0.04875  0.06342  307 LEU A C   
2345 O O   . LEU A 307 ? 0.71801 0.85547 0.93042 -0.08844 0.05224  0.06538  307 LEU A O   
2346 C CB  . LEU A 307 ? 0.67764 0.80240 0.88391 -0.05770 0.04143  0.05994  307 LEU A CB  
2347 C CG  . LEU A 307 ? 0.68944 0.79674 0.87537 -0.05797 0.04864  0.05946  307 LEU A CG  
2348 C CD1 . LEU A 307 ? 0.72881 0.81614 0.89718 -0.06556 0.04485  0.06137  307 LEU A CD1 
2349 C CD2 . LEU A 307 ? 0.58093 0.67901 0.75842 -0.04694 0.04949  0.05617  307 LEU A CD2 
2350 N N   . GLU A 308 ? 0.62290 0.79504 0.86687 -0.07184 0.05450  0.06243  308 GLU A N   
2351 C CA  . GLU A 308 ? 0.58258 0.76829 0.83353 -0.07748 0.06709  0.06317  308 GLU A CA  
2352 C C   . GLU A 308 ? 0.66572 0.86032 0.92453 -0.09448 0.06686  0.06606  308 GLU A C   
2353 O O   . GLU A 308 ? 0.67856 0.87005 0.93044 -0.10372 0.07688  0.06821  308 GLU A O   
2354 C CB  . GLU A 308 ? 0.56136 0.77340 0.83564 -0.06715 0.07336  0.06075  308 GLU A CB  
2355 C CG  . GLU A 308 ? 0.61248 0.84485 0.89852 -0.07348 0.08768  0.06122  308 GLU A CG  
2356 C CD  . GLU A 308 ? 0.64936 0.86316 0.91008 -0.07452 0.09933  0.06119  308 GLU A CD  
2357 O OE1 . GLU A 308 ? 0.69737 0.88813 0.93655 -0.06676 0.09682  0.05942  308 GLU A OE1 
2358 O OE2 . GLU A 308 ? 0.70101 0.92425 0.96322 -0.08345 0.11104  0.06315  308 GLU A OE2 
2359 N N   . LEU A 309 ? 0.63561 0.83989 0.90703 -0.09973 0.05543  0.06624  309 LEU A N   
2360 C CA  . LEU A 309 ? 0.65429 0.86921 0.93548 -0.11740 0.05413  0.06782  309 LEU A CA  
2361 C C   . LEU A 309 ? 0.65010 0.83623 0.90869 -0.12774 0.04663  0.06815  309 LEU A C   
2362 O O   . LEU A 309 ? 0.62227 0.81411 0.88747 -0.14261 0.04197  0.06815  309 LEU A O   
2363 C CB  . LEU A 309 ? 0.53698 0.78706 0.85006 -0.11806 0.04632  0.06721  309 LEU A CB  
2364 C CG  . LEU A 309 ? 0.51197 0.79452 0.85226 -0.10827 0.05491  0.06669  309 LEU A CG  
2365 C CD1 . LEU A 309 ? 0.48085 0.79790 0.85290 -0.10716 0.04422  0.06679  309 LEU A CD1 
2366 C CD2 . LEU A 309 ? 0.44811 0.74074 0.79298 -0.11803 0.07168  0.06772  309 LEU A CD2 
2367 N N   . GLY A 310 ? 0.73842 0.89443 0.97119 -0.12026 0.04556  0.06784  310 GLY A N   
2368 C CA  . GLY A 310 ? 0.73315 0.85953 0.94303 -0.12835 0.04129  0.06791  310 GLY A CA  
2369 C C   . GLY A 310 ? 0.74192 0.86647 0.95207 -0.13246 0.02799  0.06535  310 GLY A C   
2370 O O   . GLY A 310 ? 0.71758 0.82388 0.91463 -0.14408 0.02518  0.06445  310 GLY A O   
2371 N N   . GLN A 311 ? 0.70794 0.84892 0.93060 -0.12310 0.01979  0.06419  311 GLN A N   
2372 C CA  . GLN A 311 ? 0.68285 0.82290 0.90345 -0.12660 0.00648  0.06227  311 GLN A CA  
2373 C C   . GLN A 311 ? 0.67776 0.79148 0.87515 -0.11691 0.00298  0.06103  311 GLN A C   
2374 O O   . GLN A 311 ? 0.69041 0.80911 0.89042 -0.10562 -0.00214 0.06136  311 GLN A O   
2375 C CB  . GLN A 311 ? 0.61107 0.78412 0.85777 -0.12219 -0.00119 0.06304  311 GLN A CB  
2376 C CG  . GLN A 311 ? 0.72704 0.93027 1.00024 -0.13006 0.00412  0.06410  311 GLN A CG  
2377 C CD  . GLN A 311 ? 0.70966 0.91054 0.98118 -0.15105 0.00309  0.06283  311 GLN A CD  
2378 O OE1 . GLN A 311 ? 0.69208 0.88526 0.95498 -0.15954 -0.00795 0.06049  311 GLN A OE1 
2379 N NE2 . GLN A 311 ? 0.61366 0.81974 0.89177 -0.16030 0.01498  0.06418  311 GLN A NE2 
2380 N N   . PHE A 312 ? 0.69321 0.77837 0.86798 -0.12155 0.00609  0.05980  312 PHE A N   
2381 C CA  . PHE A 312 ? 0.67357 0.73564 0.82791 -0.11269 0.00436  0.05833  312 PHE A CA  
2382 C C   . PHE A 312 ? 0.67344 0.70674 0.80584 -0.12028 0.00561  0.05614  312 PHE A C   
2383 O O   . PHE A 312 ? 0.67006 0.69642 0.80036 -0.13125 0.00972  0.05656  312 PHE A O   
2384 C CB  . PHE A 312 ? 0.67581 0.73508 0.82818 -0.09932 0.01155  0.05985  312 PHE A CB  
2385 C CG  . PHE A 312 ? 0.72202 0.77941 0.87403 -0.10111 0.02177  0.06199  312 PHE A CG  
2386 C CD1 . PHE A 312 ? 0.66771 0.70121 0.80137 -0.10487 0.02617  0.06271  312 PHE A CD1 
2387 C CD2 . PHE A 312 ? 0.73566 0.81418 0.90433 -0.09807 0.02745  0.06353  312 PHE A CD2 
2388 C CE1 . PHE A 312 ? 0.76109 0.79126 0.89148 -0.10638 0.03531  0.06598  312 PHE A CE1 
2389 C CE2 . PHE A 312 ? 0.76979 0.84601 0.93508 -0.10016 0.03760  0.06576  312 PHE A CE2 
2390 C CZ  . PHE A 312 ? 0.74768 0.79931 0.89292 -0.10467 0.04114  0.06752  312 PHE A CZ  
2391 N N   . LYS A 313 ? 0.69300 0.70855 0.80875 -0.11399 0.00287  0.05382  313 LYS A N   
2392 C CA  . LYS A 313 ? 0.79101 0.77791 0.88551 -0.11797 0.00473  0.05102  313 LYS A CA  
2393 C C   . LYS A 313 ? 0.70856 0.68102 0.79659 -0.11646 0.01413  0.05385  313 LYS A C   
2394 O O   . LYS A 313 ? 0.71925 0.69590 0.80977 -0.10618 0.01877  0.05664  313 LYS A O   
2395 C CB  . LYS A 313 ? 0.74852 0.72276 0.82889 -0.10863 0.00260  0.04839  313 LYS A CB  
2396 C CG  . LYS A 313 ? 0.66647 0.61258 0.72566 -0.11217 0.00398  0.04410  313 LYS A CG  
2397 C CD  . LYS A 313 ? 0.78857 0.72570 0.83577 -0.10280 0.00355  0.04141  313 LYS A CD  
2398 C CE  . LYS A 313 ? 0.78772 0.69635 0.81495 -0.10268 0.00777  0.03705  313 LYS A CE  
2399 N NZ  . LYS A 313 ? 0.72839 0.62557 0.74255 -0.11361 0.00281  0.03105  313 LYS A NZ  
2400 N N   . LYS A 314 ? 0.66890 0.62293 0.74706 -0.12710 0.01655  0.05321  314 LYS A N   
2401 C CA  . LYS A 314 ? 0.69417 0.63078 0.76331 -0.12667 0.02500  0.05719  314 LYS A CA  
2402 C C   . LYS A 314 ? 0.72422 0.63265 0.77322 -0.11773 0.02664  0.05559  314 LYS A C   
2403 O O   . LYS A 314 ? 0.74762 0.63581 0.78375 -0.12288 0.02475  0.05113  314 LYS A O   
2404 C CB  . LYS A 314 ? 0.73757 0.66746 0.80689 -0.14361 0.02752  0.05817  314 LYS A CB  
2405 C CG  . LYS A 314 ? 0.69207 0.65387 0.78489 -0.15337 0.02677  0.05967  314 LYS A CG  
2406 C CD  . LYS A 314 ? 0.83515 0.81484 0.93883 -0.14468 0.03370  0.06491  314 LYS A CD  
2407 C CE  . LYS A 314 ? 0.75347 0.76894 0.88333 -0.14955 0.03341  0.06555  314 LYS A CE  
2408 N NZ  . LYS A 314 ? 0.73323 0.76686 0.87545 -0.14919 0.02268  0.06145  314 LYS A NZ  
2409 N N   . THR A 315 ? 0.69247 0.60072 0.73924 -0.10419 0.03005  0.05860  315 THR A N   
2410 C CA  . THR A 315 ? 0.73630 0.62574 0.76927 -0.09286 0.03107  0.05713  315 THR A CA  
2411 C C   . THR A 315 ? 0.73630 0.63260 0.77118 -0.08074 0.03426  0.06176  315 THR A C   
2412 O O   . THR A 315 ? 0.77789 0.69065 0.82208 -0.08173 0.03604  0.06526  315 THR A O   
2413 C CB  . THR A 315 ? 0.69668 0.58990 0.72890 -0.08911 0.02624  0.05120  315 THR A CB  
2414 O OG1 . THR A 315 ? 0.74305 0.61714 0.76223 -0.07960 0.02872  0.04907  315 THR A OG1 
2415 C CG2 . THR A 315 ? 0.59744 0.51617 0.64349 -0.08251 0.02371  0.05191  315 THR A CG2 
2416 N N   . GLN A 316 ? 0.71920 0.60412 0.74547 -0.06930 0.03498  0.06125  316 GLN A N   
2417 C CA  . GLN A 316 ? 0.70965 0.60062 0.73637 -0.05826 0.03664  0.06533  316 GLN A CA  
2418 C C   . GLN A 316 ? 0.70289 0.61597 0.74093 -0.05207 0.03380  0.06233  316 GLN A C   
2419 O O   . GLN A 316 ? 0.75976 0.67574 0.80019 -0.05169 0.03128  0.05757  316 GLN A O   
2420 C CB  . GLN A 316 ? 0.72259 0.59281 0.73669 -0.04817 0.03822  0.06687  316 GLN A CB  
2421 C CG  . GLN A 316 ? 0.74220 0.58342 0.74198 -0.05331 0.04153  0.07005  316 GLN A CG  
2422 C CD  . GLN A 316 ? 0.76263 0.58746 0.75665 -0.06159 0.04118  0.06367  316 GLN A CD  
2423 O OE1 . GLN A 316 ? 0.78605 0.61342 0.78103 -0.05794 0.03930  0.05732  316 GLN A OE1 
2424 N NE2 . GLN A 316 ? 0.85431 0.66223 0.84127 -0.07378 0.04325  0.06514  316 GLN A NE2 
2425 N N   . ILE A 317 ? 0.61002 0.53704 0.65321 -0.04784 0.03454  0.06500  317 ILE A N   
2426 C CA  . ILE A 317 ? 0.67116 0.61581 0.72367 -0.04227 0.03228  0.06189  317 ILE A CA  
2427 C C   . ILE A 317 ? 0.71077 0.65785 0.76001 -0.03254 0.03230  0.06350  317 ILE A C   
2428 O O   . ILE A 317 ? 0.71725 0.65762 0.75838 -0.03041 0.03389  0.06827  317 ILE A O   
2429 C CB  . ILE A 317 ? 0.65044 0.61312 0.71467 -0.04675 0.03222  0.06135  317 ILE A CB  
2430 C CG1 . ILE A 317 ? 0.63969 0.60539 0.70240 -0.04889 0.03628  0.06551  317 ILE A CG1 
2431 C CG2 . ILE A 317 ? 0.60740 0.57324 0.67814 -0.05479 0.02977  0.05929  317 ILE A CG2 
2432 C CD1 . ILE A 317 ? 0.73165 0.71636 0.80607 -0.04961 0.03759  0.06404  317 ILE A CD1 
2433 N N   . LEU A 318 ? 0.68518 0.64230 0.74040 -0.02726 0.03018  0.05976  318 LEU A N   
2434 C CA  . LEU A 318 ? 0.64615 0.61165 0.70197 -0.01943 0.02877  0.05983  318 LEU A CA  
2435 C C   . LEU A 318 ? 0.62160 0.60332 0.68677 -0.02106 0.02781  0.05620  318 LEU A C   
2436 O O   . LEU A 318 ? 0.65645 0.64214 0.72815 -0.02293 0.02715  0.05268  318 LEU A O   
2437 C CB  . LEU A 318 ? 0.64643 0.60863 0.70198 -0.01214 0.02781  0.05810  318 LEU A CB  
2438 C CG  . LEU A 318 ? 0.65991 0.62866 0.71528 -0.00276 0.02545  0.05958  318 LEU A CG  
2439 C CD1 . LEU A 318 ? 0.68625 0.65028 0.74270 0.00478  0.02596  0.05823  318 LEU A CD1 
2440 C CD2 . LEU A 318 ? 0.68571 0.67385 0.74988 -0.00307 0.02305  0.05600  318 LEU A CD2 
2441 N N   . VAL A 319 ? 0.62603 0.61501 0.68991 -0.02042 0.02811  0.05707  319 VAL A N   
2442 C CA  . VAL A 319 ? 0.59930 0.60020 0.67020 -0.02201 0.02820  0.05309  319 VAL A CA  
2443 C C   . VAL A 319 ? 0.63202 0.64061 0.69984 -0.01774 0.02606  0.05133  319 VAL A C   
2444 O O   . VAL A 319 ? 0.68629 0.69247 0.74504 -0.01420 0.02494  0.05491  319 VAL A O   
2445 C CB  . VAL A 319 ? 0.63578 0.63892 0.70826 -0.02672 0.03180  0.05422  319 VAL A CB  
2446 C CG1 . VAL A 319 ? 0.56660 0.57959 0.64635 -0.02671 0.03264  0.04957  319 VAL A CG1 
2447 C CG2 . VAL A 319 ? 0.65764 0.65539 0.73359 -0.03208 0.03261  0.05621  319 VAL A CG2 
2448 N N   . GLY A 320 ? 0.61446 0.63142 0.68879 -0.01845 0.02501  0.04599  320 GLY A N   
2449 C CA  . GLY A 320 ? 0.60929 0.63442 0.68058 -0.01645 0.02240  0.04290  320 GLY A CA  
2450 C C   . GLY A 320 ? 0.62703 0.65754 0.70493 -0.01948 0.02249  0.03625  320 GLY A C   
2451 O O   . GLY A 320 ? 0.63068 0.65815 0.71569 -0.02202 0.02442  0.03494  320 GLY A O   
2452 N N   . VAL A 321 ? 0.58108 0.61848 0.65521 -0.01936 0.01988  0.03215  321 VAL A N   
2453 C CA  . VAL A 321 ? 0.65268 0.69233 0.73022 -0.02309 0.02021  0.02486  321 VAL A CA  
2454 C C   . VAL A 321 ? 0.65282 0.70262 0.72913 -0.02379 0.01463  0.02070  321 VAL A C   
2455 O O   . VAL A 321 ? 0.69375 0.74987 0.76557 -0.01998 0.01032  0.02395  321 VAL A O   
2456 C CB  . VAL A 321 ? 0.63432 0.67020 0.70590 -0.02387 0.02461  0.02194  321 VAL A CB  
2457 C CG1 . VAL A 321 ? 0.59327 0.62334 0.67054 -0.02350 0.02961  0.02536  321 VAL A CG1 
2458 C CG2 . VAL A 321 ? 0.62229 0.66113 0.67996 -0.02190 0.02395  0.02347  321 VAL A CG2 
2459 N N   . ASN A 322 ? 0.64354 0.69472 0.72405 -0.02881 0.01429  0.01362  322 ASN A N   
2460 C CA  . ASN A 322 ? 0.62934 0.69185 0.71040 -0.03190 0.00860  0.00815  322 ASN A CA  
2461 C C   . ASN A 322 ? 0.68360 0.74444 0.75250 -0.03446 0.00810  0.00154  322 ASN A C   
2462 O O   . ASN A 322 ? 0.62295 0.67289 0.68628 -0.03441 0.01384  -0.00033 322 ASN A O   
2463 C CB  . ASN A 322 ? 0.61320 0.67779 0.70670 -0.03803 0.00893  0.00411  322 ASN A CB  
2464 C CG  . ASN A 322 ? 0.64907 0.71542 0.75249 -0.03558 0.01049  0.00994  322 ASN A CG  
2465 O OD1 . ASN A 322 ? 0.70426 0.77082 0.80557 -0.02913 0.01018  0.01609  322 ASN A OD1 
2466 N ND2 . ASN A 322 ? 0.54821 0.61415 0.66069 -0.04110 0.01278  0.00784  322 ASN A ND2 
2467 N N   . LYS A 323 ? 0.62626 0.69927 0.69120 -0.03636 0.00101  -0.00232 323 LYS A N   
2468 C CA  . LYS A 323 ? 0.68493 0.75742 0.73455 -0.03902 -0.00075 -0.00914 323 LYS A CA  
2469 C C   . LYS A 323 ? 0.71149 0.77243 0.76059 -0.04586 0.00394  -0.01898 323 LYS A C   
2470 O O   . LYS A 323 ? 0.72161 0.77356 0.75754 -0.04577 0.00802  -0.02377 323 LYS A O   
2471 C CB  . LYS A 323 ? 0.73773 0.82796 0.78484 -0.04044 -0.01131 -0.01139 323 LYS A CB  
2472 C CG  . LYS A 323 ? 0.74639 0.83789 0.77492 -0.04434 -0.01519 -0.01939 323 LYS A CG  
2473 C CD  . LYS A 323 ? 0.67402 0.78612 0.69998 -0.04354 -0.02772 -0.01856 323 LYS A CD  
2474 C CE  . LYS A 323 ? 0.87222 0.99213 0.89404 -0.05391 -0.03432 -0.03114 323 LYS A CE  
2475 N NZ  . LYS A 323 ? 0.93848 1.05271 0.93359 -0.05466 -0.03564 -0.03588 323 LYS A NZ  
2476 N N   . ASP A 324 ? 0.63703 0.69695 0.69936 -0.05177 0.00409  -0.02223 324 ASP A N   
2477 C CA  . ASP A 324 ? 0.67524 0.72075 0.73612 -0.05843 0.00835  -0.03121 324 ASP A CA  
2478 C C   . ASP A 324 ? 0.69109 0.72299 0.76261 -0.05768 0.01503  -0.02731 324 ASP A C   
2479 O O   . ASP A 324 ? 0.70201 0.72826 0.78057 -0.06479 0.01577  -0.03075 324 ASP A O   
2480 C CB  . ASP A 324 ? 0.70995 0.76347 0.77347 -0.06907 0.00222  -0.04012 324 ASP A CB  
2481 C CG  . ASP A 324 ? 0.76042 0.82732 0.81106 -0.07072 -0.00596 -0.04539 324 ASP A CG  
2482 O OD1 . ASP A 324 ? 0.71736 0.77427 0.75110 -0.07200 -0.00421 -0.05289 324 ASP A OD1 
2483 O OD2 . ASP A 324 ? 0.70587 0.79369 0.76292 -0.07037 -0.01431 -0.04218 324 ASP A OD2 
2484 N N   . GLU A 325 ? 0.67163 0.69823 0.74359 -0.04976 0.01964  -0.01990 325 GLU A N   
2485 C CA  . GLU A 325 ? 0.65344 0.66809 0.73379 -0.04794 0.02473  -0.01545 325 GLU A CA  
2486 C C   . GLU A 325 ? 0.71214 0.70903 0.79104 -0.05148 0.02890  -0.02226 325 GLU A C   
2487 O O   . GLU A 325 ? 0.58629 0.57366 0.67197 -0.05406 0.03063  -0.02003 325 GLU A O   
2488 C CB  . GLU A 325 ? 0.66155 0.67475 0.74115 -0.03975 0.02845  -0.00865 325 GLU A CB  
2489 C CG  . GLU A 325 ? 0.66073 0.68587 0.74047 -0.03635 0.02538  -0.00129 325 GLU A CG  
2490 C CD  . GLU A 325 ? 0.64611 0.67262 0.73581 -0.03640 0.02430  0.00512  325 GLU A CD  
2491 O OE1 . GLU A 325 ? 0.56617 0.58647 0.66179 -0.04019 0.02531  0.00388  325 GLU A OE1 
2492 O OE2 . GLU A 325 ? 0.64650 0.67873 0.73640 -0.03295 0.02286  0.01121  325 GLU A OE2 
2493 N N   . GLY A 326 ? 0.64441 0.63457 0.71282 -0.05122 0.03115  -0.03040 326 GLY A N   
2494 C CA  . GLY A 326 ? 0.69259 0.66209 0.75866 -0.05168 0.03660  -0.03651 326 GLY A CA  
2495 C C   . GLY A 326 ? 0.71569 0.67454 0.78061 -0.06237 0.03521  -0.04438 326 GLY A C   
2496 O O   . GLY A 326 ? 0.79011 0.72764 0.85409 -0.06253 0.04001  -0.04741 326 GLY A O   
2497 N N   . THR A 327 ? 0.70513 0.67788 0.77086 -0.07140 0.02885  -0.04760 327 THR A N   
2498 C CA  . THR A 327 ? 0.70750 0.67072 0.77079 -0.08365 0.02777  -0.05746 327 THR A CA  
2499 C C   . THR A 327 ? 0.69598 0.64679 0.76877 -0.08948 0.03057  -0.05350 327 THR A C   
2500 O O   . THR A 327 ? 0.79230 0.72243 0.86082 -0.09702 0.03355  -0.06041 327 THR A O   
2501 C CB  . THR A 327 ? 0.66595 0.65133 0.72922 -0.09217 0.01929  -0.06245 327 THR A CB  
2502 O OG1 . THR A 327 ? 0.71502 0.72102 0.79196 -0.09097 0.01555  -0.05307 327 THR A OG1 
2503 C CG2 . THR A 327 ? 0.71577 0.71018 0.76511 -0.08741 0.01618  -0.06663 327 THR A CG2 
2504 N N   . ALA A 328 ? 0.71688 0.67745 0.80040 -0.08633 0.03029  -0.04258 328 ALA A N   
2505 C CA  . ALA A 328 ? 0.74461 0.69373 0.83464 -0.09201 0.03349  -0.03776 328 ALA A CA  
2506 C C   . ALA A 328 ? 0.79081 0.70882 0.87432 -0.08944 0.03947  -0.03831 328 ALA A C   
2507 O O   . ALA A 328 ? 0.79170 0.69190 0.87434 -0.09845 0.04227  -0.03985 328 ALA A O   
2508 C CB  . ALA A 328 ? 0.72614 0.68723 0.82452 -0.08592 0.03336  -0.02589 328 ALA A CB  
2509 N N   . PHE A 329 ? 0.74162 0.65253 0.82079 -0.07712 0.04184  -0.03705 329 PHE A N   
2510 C CA  . PHE A 329 ? 0.81472 0.69786 0.89012 -0.07130 0.04729  -0.03602 329 PHE A CA  
2511 C C   . PHE A 329 ? 0.74594 0.60711 0.81119 -0.07632 0.05047  -0.04851 329 PHE A C   
2512 O O   . PHE A 329 ? 0.80755 0.64091 0.86932 -0.07467 0.05504  -0.04830 329 PHE A O   
2513 C CB  . PHE A 329 ? 0.72757 0.61481 0.80550 -0.05589 0.04890  -0.03000 329 PHE A CB  
2514 C CG  . PHE A 329 ? 0.74245 0.65030 0.82856 -0.05226 0.04542  -0.01922 329 PHE A CG  
2515 C CD1 . PHE A 329 ? 0.83742 0.73920 0.92797 -0.04985 0.04534  -0.00898 329 PHE A CD1 
2516 C CD2 . PHE A 329 ? 0.68399 0.61545 0.77135 -0.05204 0.04198  -0.01945 329 PHE A CD2 
2517 C CE1 . PHE A 329 ? 0.78019 0.69920 0.87620 -0.04759 0.04225  -0.00045 329 PHE A CE1 
2518 C CE2 . PHE A 329 ? 0.70118 0.64813 0.79476 -0.04927 0.03925  -0.01041 329 PHE A CE2 
2519 C CZ  . PHE A 329 ? 0.72382 0.66444 0.82165 -0.04740 0.03956  -0.00161 329 PHE A CZ  
2520 N N   . LEU A 330 ? 0.76593 0.63738 0.82505 -0.08279 0.04780  -0.05935 330 LEU A N   
2521 C CA  . LEU A 330 ? 0.84034 0.68960 0.88706 -0.08778 0.05092  -0.07299 330 LEU A CA  
2522 C C   . LEU A 330 ? 0.84994 0.67582 0.89522 -0.10123 0.05256  -0.07624 330 LEU A C   
2523 O O   . LEU A 330 ? 0.85389 0.64882 0.88963 -0.10170 0.05778  -0.08354 330 LEU A O   
2524 C CB  . LEU A 330 ? 0.84524 0.71261 0.88386 -0.09367 0.04611  -0.08369 330 LEU A CB  
2525 C CG  . LEU A 330 ? 0.86776 0.75668 0.90489 -0.08192 0.04501  -0.08026 330 LEU A CG  
2526 C CD1 . LEU A 330 ? 0.84102 0.74556 0.86696 -0.08830 0.03951  -0.09002 330 LEU A CD1 
2527 C CD2 . LEU A 330 ? 0.78035 0.65376 0.81353 -0.06752 0.05328  -0.08014 330 LEU A CD2 
2528 N N   . VAL A 331 ? 0.86933 0.70837 0.92376 -0.11238 0.04907  -0.07104 331 VAL A N   
2529 C CA  . VAL A 331 ? 0.87462 0.69316 0.92782 -0.12777 0.05134  -0.07414 331 VAL A CA  
2530 C C   . VAL A 331 ? 0.90286 0.69689 0.95715 -0.12333 0.05681  -0.06250 331 VAL A C   
2531 O O   . VAL A 331 ? 0.95319 0.72670 1.00520 -0.13597 0.05988  -0.06283 331 VAL A O   
2532 C CB  . VAL A 331 ? 0.93939 0.78527 1.00271 -0.14384 0.04594  -0.07549 331 VAL A CB  
2533 C CG1 . VAL A 331 ? 0.92024 0.78656 0.98009 -0.14951 0.03924  -0.08801 331 VAL A CG1 
2534 C CG2 . VAL A 331 ? 0.84175 0.71493 0.91850 -0.13781 0.04387  -0.06199 331 VAL A CG2 
2535 N N   . TYR A 332 ? 0.95758 0.75294 1.01461 -0.10638 0.05784  -0.05195 332 TYR A N   
2536 C CA  . TYR A 332 ? 0.86087 0.63223 0.91683 -0.09969 0.06173  -0.04053 332 TYR A CA  
2537 C C   . TYR A 332 ? 1.01420 0.75522 1.06224 -0.08695 0.06634  -0.04327 332 TYR A C   
2538 O O   . TYR A 332 ? 1.03893 0.76939 1.08860 -0.07374 0.06761  -0.03263 332 TYR A O   
2539 C CB  . TYR A 332 ? 0.87494 0.66783 0.93954 -0.08967 0.05892  -0.02684 332 TYR A CB  
2540 C CG  . TYR A 332 ? 0.92145 0.73410 0.99261 -0.10077 0.05689  -0.02127 332 TYR A CG  
2541 C CD1 . TYR A 332 ? 0.84438 0.69032 0.92324 -0.10507 0.05253  -0.02514 332 TYR A CD1 
2542 C CD2 . TYR A 332 ? 0.87225 0.66999 0.94132 -0.10646 0.05983  -0.01193 332 TYR A CD2 
2543 C CE1 . TYR A 332 ? 0.79090 0.65604 0.87744 -0.11366 0.05160  -0.02050 332 TYR A CE1 
2544 C CE2 . TYR A 332 ? 0.92500 0.74186 1.00012 -0.11640 0.05961  -0.00744 332 TYR A CE2 
2545 C CZ  . TYR A 332 ? 0.91322 0.76446 0.99820 -0.11949 0.05572  -0.01214 332 TYR A CZ  
2546 O OH  . TYR A 332 ? 0.94699 0.81833 1.03964 -0.12788 0.05638  -0.00823 332 TYR A OH  
2547 N N   . GLY A 333 ? 1.03991 0.76746 1.07937 -0.08990 0.06872  -0.05766 333 GLY A N   
2548 C CA  . GLY A 333 ? 1.01969 0.71743 1.05191 -0.07665 0.07445  -0.06128 333 GLY A CA  
2549 C C   . GLY A 333 ? 1.07093 0.76206 1.09331 -0.07599 0.07738  -0.07825 333 GLY A C   
2550 O O   . GLY A 333 ? 1.05920 0.71572 1.07196 -0.07166 0.08353  -0.08521 333 GLY A O   
2551 N N   . ALA A 334 ? 1.01704 0.73893 1.03993 -0.07963 0.07335  -0.08501 334 ALA A N   
2552 C CA  . ALA A 334 ? 0.97064 0.68813 0.98169 -0.07734 0.07635  -0.10037 334 ALA A CA  
2553 C C   . ALA A 334 ? 1.02020 0.71121 1.01719 -0.09409 0.07758  -0.11539 334 ALA A C   
2554 O O   . ALA A 334 ? 1.03603 0.73196 1.03511 -0.11198 0.07283  -0.11589 334 ALA A O   
2555 C CB  . ALA A 334 ? 0.97215 0.72843 0.98479 -0.07765 0.07099  -0.10229 334 ALA A CB  
2556 N N   . PRO A 335 ? 1.02734 0.69082 1.01021 -0.08933 0.08425  -0.12854 335 PRO A N   
2557 C CA  . PRO A 335 ? 1.05743 0.69141 1.02504 -0.10622 0.08567  -0.14405 335 PRO A CA  
2558 C C   . PRO A 335 ? 1.04596 0.70494 1.00629 -0.12234 0.07834  -0.15658 335 PRO A C   
2559 O O   . PRO A 335 ? 1.08528 0.77011 1.04248 -0.11566 0.07615  -0.15976 335 PRO A O   
2560 C CB  . PRO A 335 ? 1.00456 0.60212 0.95901 -0.09234 0.09594  -0.15406 335 PRO A CB  
2561 C CG  . PRO A 335 ? 1.06414 0.68796 1.02480 -0.07187 0.09827  -0.14966 335 PRO A CG  
2562 C CD  . PRO A 335 ? 1.04380 0.70308 1.02434 -0.06853 0.09140  -0.13060 335 PRO A CD  
2563 N N   . GLY A 336 ? 1.12680 0.77826 1.08432 -0.14427 0.07429  -0.16330 336 GLY A N   
2564 C CA  . GLY A 336 ? 1.02636 0.70200 0.97835 -0.16125 0.06565  -0.17523 336 GLY A CA  
2565 C C   . GLY A 336 ? 1.01967 0.74145 0.98927 -0.16712 0.05574  -0.16464 336 GLY A C   
2566 O O   . GLY A 336 ? 1.04588 0.79161 1.01357 -0.18090 0.04701  -0.17313 336 GLY A O   
2567 N N   . PHE A 337 ? 1.00762 0.74261 0.99393 -0.15681 0.05648  -0.14674 337 PHE A N   
2568 C CA  . PHE A 337 ? 1.00399 0.78116 1.00697 -0.15965 0.04841  -0.13636 337 PHE A CA  
2569 C C   . PHE A 337 ? 1.00804 0.78513 1.02362 -0.17553 0.04750  -0.13072 337 PHE A C   
2570 O O   . PHE A 337 ? 0.97072 0.71601 0.98529 -0.17708 0.05442  -0.12634 337 PHE A O   
2571 C CB  . PHE A 337 ? 0.95115 0.74461 0.96330 -0.13926 0.04988  -0.12127 337 PHE A CB  
2572 C CG  . PHE A 337 ? 0.99062 0.79868 0.99421 -0.12699 0.04901  -0.12524 337 PHE A CG  
2573 C CD1 . PHE A 337 ? 0.89284 0.73805 0.90043 -0.12687 0.04097  -0.12253 337 PHE A CD1 
2574 C CD2 . PHE A 337 ? 1.00639 0.79022 0.99714 -0.11556 0.05688  -0.13185 337 PHE A CD2 
2575 C CE1 . PHE A 337 ? 0.93432 0.79091 0.93145 -0.11666 0.04083  -0.12544 337 PHE A CE1 
2576 C CE2 . PHE A 337 ? 1.01943 0.81734 1.00136 -0.10527 0.05756  -0.13554 337 PHE A CE2 
2577 C CZ  . PHE A 337 ? 0.89321 0.72678 0.87738 -0.10649 0.04955  -0.13197 337 PHE A CZ  
2578 N N   . SER A 338 ? 0.98722 0.80021 1.01447 -0.18713 0.03923  -0.13064 338 SER A N   
2579 C CA  . SER A 338 ? 0.97640 0.79633 1.01811 -0.20277 0.03902  -0.12541 338 SER A CA  
2580 C C   . SER A 338 ? 0.94594 0.81470 1.00483 -0.20394 0.03055  -0.12003 338 SER A C   
2581 O O   . SER A 338 ? 0.97253 0.86617 1.02932 -0.20388 0.02222  -0.12720 338 SER A O   
2582 C CB  . SER A 338 ? 0.97832 0.77876 1.01408 -0.22615 0.03927  -0.13934 338 SER A CB  
2583 O OG  . SER A 338 ? 0.99514 0.81052 1.04747 -0.24304 0.03883  -0.13464 338 SER A OG  
2584 N N   . LYS A 339 ? 0.93040 0.81179 1.00494 -0.20405 0.03286  -0.10721 339 LYS A N   
2585 C CA  . LYS A 339 ? 0.87242 0.79868 0.96500 -0.20675 0.02584  -0.10332 339 LYS A CA  
2586 C C   . LYS A 339 ? 0.87341 0.81869 0.97474 -0.22892 0.01988  -0.11456 339 LYS A C   
2587 O O   . LYS A 339 ? 0.88923 0.87540 1.00565 -0.23040 0.01202  -0.11388 339 LYS A O   
2588 C CB  . LYS A 339 ? 0.83855 0.77174 0.94425 -0.20184 0.03124  -0.08805 339 LYS A CB  
2589 C CG  . LYS A 339 ? 0.86542 0.78685 0.97798 -0.21986 0.03775  -0.08651 339 LYS A CG  
2590 C CD  . LYS A 339 ? 0.86093 0.80161 0.98811 -0.21684 0.04167  -0.07303 339 LYS A CD  
2591 C CE  . LYS A 339 ? 0.83899 0.77421 0.97403 -0.23731 0.04849  -0.07219 339 LYS A CE  
2592 N NZ  . LYS A 339 ? 0.84706 0.81135 0.99689 -0.25652 0.04310  -0.08340 339 LYS A NZ  
2593 N N   . ASP A 340 ? 0.83391 0.75097 0.92665 -0.24595 0.02306  -0.12501 340 ASP A N   
2594 C CA  . ASP A 340 ? 0.90932 0.84262 1.01149 -0.27019 0.01801  -0.13604 340 ASP A CA  
2595 C C   . ASP A 340 ? 0.90659 0.83678 0.99384 -0.27822 0.00988  -0.15364 340 ASP A C   
2596 O O   . ASP A 340 ? 0.87475 0.80930 0.96556 -0.30061 0.00604  -0.16527 340 ASP A O   
2597 C CB  . ASP A 340 ? 0.79368 0.69756 0.89739 -0.28810 0.02774  -0.13535 340 ASP A CB  
2598 C CG  . ASP A 340 ? 0.90015 0.81005 1.01740 -0.28305 0.03552  -0.11852 340 ASP A CG  
2599 O OD1 . ASP A 340 ? 0.80892 0.76101 0.94491 -0.27832 0.03152  -0.11204 340 ASP A OD1 
2600 O OD2 . ASP A 340 ? 0.92734 0.79884 1.03502 -0.28256 0.04557  -0.11157 340 ASP A OD2 
2601 N N   . ASN A 341 ? 0.88904 0.81190 0.95901 -0.26147 0.00754  -0.15617 341 ASN A N   
2602 C CA  . ASN A 341 ? 0.90842 0.83557 0.96266 -0.26659 -0.00129 -0.17190 341 ASN A CA  
2603 C C   . ASN A 341 ? 0.90682 0.84626 0.95147 -0.24358 -0.00440 -0.16670 341 ASN A C   
2604 O O   . ASN A 341 ? 0.85878 0.80064 0.90979 -0.22586 0.00056  -0.15217 341 ASN A O   
2605 C CB  . ASN A 341 ? 0.88561 0.76537 0.91789 -0.27855 0.00447  -0.18705 341 ASN A CB  
2606 C CG  . ASN A 341 ? 0.97203 0.80792 0.98668 -0.26010 0.01624  -0.18341 341 ASN A CG  
2607 O OD1 . ASN A 341 ? 0.95580 0.79904 0.96965 -0.23825 0.01801  -0.17327 341 ASN A OD1 
2608 N ND2 . ASN A 341 ? 0.97481 0.76490 0.97609 -0.26919 0.02432  -0.19182 341 ASN A ND2 
2609 N N   . ASN A 342 ? 0.87087 0.81791 0.89899 -0.24486 -0.01262 -0.17865 342 ASN A N   
2610 C CA  . ASN A 342 ? 0.94273 0.90666 0.96208 -0.22537 -0.01649 -0.17308 342 ASN A CA  
2611 C C   . ASN A 342 ? 0.95584 0.88520 0.95541 -0.20896 -0.00570 -0.17266 342 ASN A C   
2612 O O   . ASN A 342 ? 0.90776 0.84855 0.89910 -0.19346 -0.00704 -0.16786 342 ASN A O   
2613 C CB  . ASN A 342 ? 0.90968 0.89985 0.91826 -0.23223 -0.03050 -0.18401 342 ASN A CB  
2614 C CG  . ASN A 342 ? 1.04018 1.00253 1.02363 -0.24581 -0.03061 -0.20400 342 ASN A CG  
2615 O OD1 . ASN A 342 ? 1.03976 0.96020 1.01258 -0.24802 -0.01923 -0.20993 342 ASN A OD1 
2616 N ND2 . ASN A 342 ? 1.16423 1.14905 1.13685 -0.25451 -0.04390 -0.21465 342 ASN A ND2 
2617 N N   . SER A 343 ? 0.90883 0.79679 0.90087 -0.21185 0.00505  -0.17743 343 SER A N   
2618 C CA  . SER A 343 ? 0.96341 0.82204 0.94532 -0.19342 0.01658  -0.17287 343 SER A CA  
2619 C C   . SER A 343 ? 0.98283 0.83801 0.94155 -0.18385 0.01684  -0.18193 343 SER A C   
2620 O O   . SER A 343 ? 0.97056 0.82492 0.92636 -0.16534 0.02262  -0.17417 343 SER A O   
2621 C CB  . SER A 343 ? 0.90199 0.77486 0.90174 -0.17747 0.01969  -0.15322 343 SER A CB  
2622 O OG  . SER A 343 ? 0.91785 0.78199 0.93327 -0.18450 0.02342  -0.14556 343 SER A OG  
2623 N N   . ILE A 344 ? 0.95896 0.81313 0.90066 -0.19749 0.01066  -0.19869 344 ILE A N   
2624 C CA  . ILE A 344 ? 1.02502 0.87003 0.93967 -0.19112 0.01233  -0.21018 344 ILE A CA  
2625 C C   . ILE A 344 ? 1.07737 0.87715 0.97999 -0.18241 0.02743  -0.21596 344 ILE A C   
2626 O O   . ILE A 344 ? 1.15872 0.92628 1.05427 -0.19434 0.03135  -0.22767 344 ILE A O   
2627 C CB  . ILE A 344 ? 1.08757 0.93987 0.98515 -0.20993 0.00148  -0.22801 344 ILE A CB  
2628 C CG1 . ILE A 344 ? 1.08105 0.98221 0.99065 -0.21476 -0.01453 -0.22130 344 ILE A CG1 
2629 C CG2 . ILE A 344 ? 0.98511 0.81777 0.84989 -0.20465 0.00623  -0.24248 344 ILE A CG2 
2630 C CD1 . ILE A 344 ? 1.02689 0.95187 0.93237 -0.19614 -0.01652 -0.20958 344 ILE A CD1 
2631 N N   . ILE A 345 ? 1.04253 0.83938 0.94326 -0.16178 0.03606  -0.20803 345 ILE A N   
2632 C CA  . ILE A 345 ? 1.07013 0.82803 0.96324 -0.15050 0.05042  -0.21210 345 ILE A CA  
2633 C C   . ILE A 345 ? 1.10675 0.85523 0.97320 -0.14339 0.05622  -0.22571 345 ILE A C   
2634 O O   . ILE A 345 ? 1.13675 0.91177 0.99252 -0.14215 0.05046  -0.22648 345 ILE A O   
2635 C CB  . ILE A 345 ? 1.04811 0.80767 0.96155 -0.13214 0.05745  -0.19344 345 ILE A CB  
2636 C CG1 . ILE A 345 ? 1.04017 0.83659 0.95964 -0.12018 0.05401  -0.18132 345 ILE A CG1 
2637 C CG2 . ILE A 345 ? 1.03518 0.79313 0.96968 -0.14005 0.05449  -0.18262 345 ILE A CG2 
2638 C CD1 . ILE A 345 ? 0.95033 0.74404 0.88154 -0.10017 0.06344  -0.16861 345 ILE A CD1 
2639 N N   . THR A 346 ? 1.09081 0.79956 0.94545 -0.13804 0.06842  -0.23629 346 THR A N   
2640 C CA  . THR A 346 ? 1.11396 0.80854 0.94323 -0.12954 0.07745  -0.25027 346 THR A CA  
2641 C C   . THR A 346 ? 1.16466 0.86553 1.00262 -0.10538 0.08878  -0.23896 346 THR A C   
2642 O O   . THR A 346 ? 1.15184 0.86367 1.01475 -0.09536 0.08949  -0.22117 346 THR A O   
2643 C CB  . THR A 346 ? 1.22020 0.86676 1.03218 -0.13543 0.08587  -0.26888 346 THR A CB  
2644 O OG1 . THR A 346 ? 1.22076 0.84095 1.05025 -0.12458 0.09490  -0.25971 346 THR A OG1 
2645 C CG2 . THR A 346 ? 1.15104 0.79116 0.95431 -0.16199 0.07469  -0.28144 346 THR A CG2 
2646 N N   . ARG A 347 ? 1.18228 0.87687 0.99868 -0.09682 0.09797  -0.25021 347 ARG A N   
2647 C CA  . ARG A 347 ? 1.15746 0.85656 0.98146 -0.07473 0.11086  -0.24244 347 ARG A CA  
2648 C C   . ARG A 347 ? 1.14719 0.82077 0.99129 -0.06192 0.12002  -0.23598 347 ARG A C   
2649 O O   . ARG A 347 ? 1.15533 0.84507 1.02315 -0.04852 0.12200  -0.21892 347 ARG A O   
2650 C CB  . ARG A 347 ? 1.15831 0.84742 0.95312 -0.06952 0.12167  -0.25938 347 ARG A CB  
2651 C CG  . ARG A 347 ? 1.16469 0.85318 0.96655 -0.04693 0.13835  -0.25562 347 ARG A CG  
2652 C CD  . ARG A 347 ? 1.22080 0.91436 0.99310 -0.04427 0.14690  -0.26874 347 ARG A CD  
2653 N NE  . ARG A 347 ? 1.34489 1.04344 1.12502 -0.02358 0.16384  -0.26536 347 ARG A NE  
2654 C CZ  . ARG A 347 ? 1.31919 1.05182 1.11115 -0.01552 0.16562  -0.25063 347 ARG A CZ  
2655 N NH1 . ARG A 347 ? 1.23326 0.99590 1.03085 -0.02451 0.15158  -0.23672 347 ARG A NH1 
2656 N NH2 . ARG A 347 ? 1.31032 1.04692 1.10956 0.00203  0.18227  -0.24988 347 ARG A NH2 
2657 N N   . LYS A 348 ? 1.20519 0.83777 1.03930 -0.06641 0.12488  -0.24927 348 LYS A N   
2658 C CA  . LYS A 348 ? 1.18739 0.79053 1.03719 -0.05370 0.13332  -0.24355 348 LYS A CA  
2659 C C   . LYS A 348 ? 1.15775 0.77223 1.03394 -0.05680 0.12422  -0.22372 348 LYS A C   
2660 O O   . LYS A 348 ? 1.08280 0.69367 0.97849 -0.04096 0.12901  -0.21048 348 LYS A O   
2661 C CB  . LYS A 348 ? 1.27927 0.83241 1.10903 -0.06036 0.13966  -0.26269 348 LYS A CB  
2662 C CG  . LYS A 348 ? 1.39738 0.94167 1.19433 -0.06633 0.14424  -0.28559 348 LYS A CG  
2663 C CD  . LYS A 348 ? 1.43765 0.99684 1.21878 -0.09234 0.12939  -0.29398 348 LYS A CD  
2664 C CE  . LYS A 348 ? 1.41547 0.98774 1.16771 -0.09491 0.13060  -0.30887 348 LYS A CE  
2665 N NZ  . LYS A 348 ? 1.51148 1.10135 1.25017 -0.11933 0.11406  -0.31568 348 LYS A NZ  
2666 N N   . GLU A 349 ? 1.22145 0.85190 1.09889 -0.07657 0.11105  -0.22128 349 GLU A N   
2667 C CA  . GLU A 349 ? 1.10814 0.75349 1.00962 -0.07969 0.10317  -0.20256 349 GLU A CA  
2668 C C   . GLU A 349 ? 1.07112 0.75377 0.99089 -0.06546 0.10182  -0.18524 349 GLU A C   
2669 O O   . GLU A 349 ? 1.07116 0.75445 1.01040 -0.05487 0.10321  -0.17017 349 GLU A O   
2670 C CB  . GLU A 349 ? 1.12453 0.78291 1.02439 -0.10358 0.09039  -0.20513 349 GLU A CB  
2671 C CG  . GLU A 349 ? 1.20646 0.82556 1.09831 -0.11928 0.09130  -0.21553 349 GLU A CG  
2672 C CD  . GLU A 349 ? 1.18139 0.81191 1.06456 -0.14445 0.08031  -0.22645 349 GLU A CD  
2673 O OE1 . GLU A 349 ? 1.20834 0.86850 1.08283 -0.14809 0.07347  -0.23185 349 GLU A OE1 
2674 O OE2 . GLU A 349 ? 1.08463 0.69479 0.96966 -0.16085 0.07838  -0.22932 349 GLU A OE2 
2675 N N   . PHE A 350 ? 1.07752 0.79003 0.98960 -0.06540 0.09905  -0.18725 350 PHE A N   
2676 C CA  . PHE A 350 ? 1.00991 0.75472 0.93625 -0.05231 0.09942  -0.17256 350 PHE A CA  
2677 C C   . PHE A 350 ? 1.01316 0.74711 0.95127 -0.03177 0.11124  -0.16717 350 PHE A C   
2678 O O   . PHE A 350 ? 1.01933 0.76630 0.97903 -0.02319 0.10976  -0.15102 350 PHE A O   
2679 C CB  . PHE A 350 ? 1.02077 0.78929 0.93034 -0.05419 0.09805  -0.17849 350 PHE A CB  
2680 C CG  . PHE A 350 ? 0.97266 0.77268 0.89430 -0.04277 0.09905  -0.16404 350 PHE A CG  
2681 C CD1 . PHE A 350 ? 0.94444 0.77277 0.87822 -0.04785 0.08815  -0.15026 350 PHE A CD1 
2682 C CD2 . PHE A 350 ? 0.97094 0.77210 0.89172 -0.02741 0.11159  -0.16489 350 PHE A CD2 
2683 C CE1 . PHE A 350 ? 0.92847 0.78254 0.87182 -0.03865 0.08925  -0.13745 350 PHE A CE1 
2684 C CE2 . PHE A 350 ? 0.95016 0.77987 0.88214 -0.01910 0.11290  -0.15195 350 PHE A CE2 
2685 C CZ  . PHE A 350 ? 0.92175 0.77654 0.86416 -0.02516 0.10148  -0.13815 350 PHE A CZ  
2686 N N   . GLN A 351 ? 1.04701 0.75750 0.97143 -0.02343 0.12295  -0.18103 351 GLN A N   
2687 C CA  . GLN A 351 ? 1.09417 0.79711 1.03188 -0.00226 0.13459  -0.17665 351 GLN A CA  
2688 C C   . GLN A 351 ? 1.07619 0.76156 1.03300 0.00330  0.13262  -0.16479 351 GLN A C   
2689 O O   . GLN A 351 ? 0.99782 0.69750 0.97593 0.01735  0.13387  -0.15067 351 GLN A O   
2690 C CB  . GLN A 351 ? 1.00337 0.67909 0.92217 0.00543  0.14819  -0.19543 351 GLN A CB  
2691 C CG  . GLN A 351 ? 1.09099 0.78816 0.99498 0.00806  0.15465  -0.20341 351 GLN A CG  
2692 C CD  . GLN A 351 ? 1.14948 0.81748 1.02582 0.00854  0.16576  -0.22599 351 GLN A CD  
2693 O OE1 . GLN A 351 ? 1.16887 0.80258 1.03091 -0.00079 0.16447  -0.23820 351 GLN A OE1 
2694 N NE2 . GLN A 351 ? 1.12551 0.80646 0.99296 0.01844  0.17733  -0.23212 351 GLN A NE2 
2695 N N   . GLU A 352 ? 1.09026 0.74488 1.03906 -0.00851 0.12917  -0.16993 352 GLU A N   
2696 C CA  . GLU A 352 ? 1.09341 0.73004 1.05722 -0.00470 0.12695  -0.15729 352 GLU A CA  
2697 C C   . GLU A 352 ? 1.05294 0.72156 1.03536 -0.00841 0.11655  -0.13848 352 GLU A C   
2698 O O   . GLU A 352 ? 1.07360 0.73957 1.07202 0.00126  0.11562  -0.12430 352 GLU A O   
2699 C CB  . GLU A 352 ? 1.14564 0.74297 1.09549 -0.01972 0.12570  -0.16626 352 GLU A CB  
2700 C CG  . GLU A 352 ? 1.21123 0.76975 1.16596 -0.00786 0.13166  -0.16138 352 GLU A CG  
2701 C CD  . GLU A 352 ? 1.36654 0.89612 1.31112 0.00817  0.14486  -0.17507 352 GLU A CD  
2702 O OE1 . GLU A 352 ? 1.42675 0.95220 1.35221 0.00205  0.14928  -0.19324 352 GLU A OE1 
2703 O OE2 . GLU A 352 ? 1.47900 0.98960 1.43398 0.02731  0.15080  -0.16795 352 GLU A OE2 
2704 N N   . GLY A 353 ? 1.04447 0.74303 1.02420 -0.02151 0.10853  -0.13813 353 GLY A N   
2705 C CA  . GLY A 353 ? 1.00994 0.73851 1.00623 -0.02432 0.09954  -0.12147 353 GLY A CA  
2706 C C   . GLY A 353 ? 0.97450 0.72747 0.98711 -0.00768 0.10182  -0.10944 353 GLY A C   
2707 O O   . GLY A 353 ? 0.95658 0.72205 0.98486 -0.00510 0.09667  -0.09446 353 GLY A O   
2708 N N   . LEU A 354 ? 0.99383 0.75489 1.00256 0.00275  0.10980  -0.11619 354 LEU A N   
2709 C CA  . LEU A 354 ? 0.93333 0.71778 0.95938 0.01799  0.11321  -0.10566 354 LEU A CA  
2710 C C   . LEU A 354 ? 0.97350 0.74195 1.01527 0.03274  0.11637  -0.09773 354 LEU A C   
2711 O O   . LEU A 354 ? 0.95052 0.73818 1.01101 0.04039  0.11298  -0.08363 354 LEU A O   
2712 C CB  . LEU A 354 ? 0.93919 0.73445 0.95712 0.02519  0.12302  -0.11544 354 LEU A CB  
2713 C CG  . LEU A 354 ? 0.93864 0.75274 0.93953 0.01372  0.12053  -0.12166 354 LEU A CG  
2714 C CD1 . LEU A 354 ? 0.87536 0.69929 0.86912 0.02311  0.13246  -0.12914 354 LEU A CD1 
2715 C CD2 . LEU A 354 ? 0.86088 0.70403 0.87132 0.00647  0.10987  -0.10767 354 LEU A CD2 
2716 N N   . LYS A 355 ? 0.98302 0.71521 1.01655 0.03689  0.12229  -0.10654 355 LYS A N   
2717 C CA  . LYS A 355 ? 1.04005 0.75333 1.08674 0.05167  0.12429  -0.09813 355 LYS A CA  
2718 C C   . LYS A 355 ? 1.03619 0.75010 1.09155 0.04524  0.11363  -0.08234 355 LYS A C   
2719 O O   . LYS A 355 ? 1.02057 0.73711 1.09162 0.05791  0.11169  -0.06948 355 LYS A O   
2720 C CB  . LYS A 355 ? 0.95454 0.62328 0.98726 0.05563  0.13242  -0.11091 355 LYS A CB  
2721 C CG  . LYS A 355 ? 1.10109 0.76706 1.12896 0.06876  0.14538  -0.12486 355 LYS A CG  
2722 C CD  . LYS A 355 ? 1.16508 0.78267 1.17747 0.07351  0.15430  -0.13886 355 LYS A CD  
2723 C CE  . LYS A 355 ? 1.21124 0.79717 1.23057 0.07992  0.15123  -0.12809 355 LYS A CE  
2724 N NZ  . LYS A 355 ? 1.37788 0.91186 1.38127 0.08532  0.16059  -0.14139 355 LYS A NZ  
2725 N N   . ILE A 356 ? 1.01237 0.72574 1.05774 0.02576  0.10667  -0.08325 356 ILE A N   
2726 C CA  . ILE A 356 ? 0.98868 0.70412 1.04026 0.01778  0.09781  -0.06939 356 ILE A CA  
2727 C C   . ILE A 356 ? 1.01232 0.76639 1.07914 0.02074  0.09170  -0.05655 356 ILE A C   
2728 O O   . ILE A 356 ? 1.05395 0.81119 1.13141 0.02568  0.08701  -0.04270 356 ILE A O   
2729 C CB  . ILE A 356 ? 1.04040 0.74807 1.07903 -0.00408 0.09340  -0.07551 356 ILE A CB  
2730 C CG1 . ILE A 356 ? 1.03436 0.70009 1.05743 -0.00960 0.09888  -0.08787 356 ILE A CG1 
2731 C CG2 . ILE A 356 ? 1.01220 0.72827 1.05803 -0.01259 0.08552  -0.06129 356 ILE A CG2 
2732 C CD1 . ILE A 356 ? 0.97398 0.60815 0.99729 -0.00947 0.09864  -0.07881 356 ILE A CD1 
2733 N N   . PHE A 357 ? 0.95224 0.73452 1.01833 0.01683  0.09132  -0.06087 357 PHE A N   
2734 C CA  . PHE A 357 ? 0.94432 0.76044 1.02285 0.01783  0.08588  -0.04966 357 PHE A CA  
2735 C C   . PHE A 357 ? 0.81533 0.64883 0.90825 0.03394  0.09024  -0.04537 357 PHE A C   
2736 O O   . PHE A 357 ? 0.99042 0.84857 1.09537 0.03535  0.08551  -0.03486 357 PHE A O   
2737 C CB  . PHE A 357 ? 0.93085 0.76806 1.00129 0.00525  0.08254  -0.05441 357 PHE A CB  
2738 C CG  . PHE A 357 ? 0.89653 0.72979 0.96075 -0.01068 0.07558  -0.05400 357 PHE A CG  
2739 C CD1 . PHE A 357 ? 0.82673 0.67076 0.89970 -0.01453 0.06898  -0.04172 357 PHE A CD1 
2740 C CD2 . PHE A 357 ? 0.89354 0.71259 0.94348 -0.02213 0.07604  -0.06653 357 PHE A CD2 
2741 C CE1 . PHE A 357 ? 0.90593 0.74878 0.97509 -0.02884 0.06400  -0.04161 357 PHE A CE1 
2742 C CE2 . PHE A 357 ? 0.91875 0.73773 0.96614 -0.03750 0.06985  -0.06633 357 PHE A CE2 
2743 C CZ  . PHE A 357 ? 0.85971 0.69132 0.91754 -0.04043 0.06441  -0.05369 357 PHE A CZ  
2744 N N   . PHE A 358 ? 0.90331 0.72537 0.99608 0.04579  0.09943  -0.05355 358 PHE A N   
2745 C CA  . PHE A 358 ? 0.90631 0.74729 1.01592 0.06166  0.10471  -0.05001 358 PHE A CA  
2746 C C   . PHE A 358 ? 1.01747 0.83507 1.13384 0.07807  0.11025  -0.05090 358 PHE A C   
2747 O O   . PHE A 358 ? 0.92202 0.73698 1.04013 0.08971  0.12067  -0.05986 358 PHE A O   
2748 C CB  . PHE A 358 ? 0.87756 0.73630 0.98141 0.06107  0.11261  -0.05975 358 PHE A CB  
2749 C CG  . PHE A 358 ? 0.88146 0.76164 0.97804 0.04665  0.10669  -0.05750 358 PHE A CG  
2750 C CD1 . PHE A 358 ? 0.78557 0.69516 0.89545 0.04687  0.10327  -0.04695 358 PHE A CD1 
2751 C CD2 . PHE A 358 ? 0.91880 0.78907 0.99552 0.03282  0.10392  -0.06578 358 PHE A CD2 
2752 C CE1 . PHE A 358 ? 0.79037 0.71617 0.89270 0.03492  0.09810  -0.04446 358 PHE A CE1 
2753 C CE2 . PHE A 358 ? 0.83384 0.72385 0.90480 0.02156  0.09780  -0.06284 358 PHE A CE2 
2754 C CZ  . PHE A 358 ? 0.75808 0.67427 0.84133 0.02329  0.09527  -0.05197 358 PHE A CZ  
2755 N N   . PRO A 359 ? 1.05549 0.85543 1.17546 0.08024  0.10373  -0.04103 359 PRO A N   
2756 C CA  . PRO A 359 ? 1.04262 0.81199 1.16445 0.09513  0.10834  -0.04184 359 PRO A CA  
2757 C C   . PRO A 359 ? 1.06576 0.85093 1.20808 0.11643  0.11420  -0.04001 359 PRO A C   
2758 O O   . PRO A 359 ? 1.06570 0.83047 1.20666 0.12938  0.12391  -0.04904 359 PRO A O   
2759 C CB  . PRO A 359 ? 1.18328 0.93812 1.30528 0.09192  0.09836  -0.02778 359 PRO A CB  
2760 C CG  . PRO A 359 ? 1.05247 0.84163 1.18238 0.08292  0.08940  -0.01766 359 PRO A CG  
2761 C CD  . PRO A 359 ? 1.00412 0.81078 1.12591 0.07037  0.09237  -0.02802 359 PRO A CD  
2762 N N   . GLY A 360 ? 1.03790 0.85905 1.19993 0.12041  0.10883  -0.02903 360 GLY A N   
2763 C CA  . GLY A 360 ? 1.03938 0.88033 1.22492 0.14016  0.11358  -0.02644 360 GLY A CA  
2764 C C   . GLY A 360 ? 1.08605 0.95512 1.27750 0.14126  0.12405  -0.03594 360 GLY A C   
2765 O O   . GLY A 360 ? 1.08689 0.98513 1.30186 0.15345  0.12698  -0.03205 360 GLY A O   
2766 N N   . VAL A 361 ? 1.04109 0.90295 1.21133 0.12823  0.12973  -0.04818 361 VAL A N   
2767 C CA  . VAL A 361 ? 0.99023 0.87675 1.16050 0.12685  0.13977  -0.05671 361 VAL A CA  
2768 C C   . VAL A 361 ? 1.02752 0.89466 1.19045 0.13871  0.15470  -0.07203 361 VAL A C   
2769 O O   . VAL A 361 ? 1.07356 0.90260 1.21951 0.13892  0.15653  -0.08017 361 VAL A O   
2770 C CB  . VAL A 361 ? 0.93409 0.82728 1.08440 0.10588  0.13573  -0.05950 361 VAL A CB  
2771 C CG1 . VAL A 361 ? 0.90206 0.80560 1.04070 0.10364  0.14773  -0.07185 361 VAL A CG1 
2772 C CG2 . VAL A 361 ? 0.76850 0.69003 0.93071 0.09755  0.12484  -0.04533 361 VAL A CG2 
2773 N N   . SER A 362 ? 0.97182 0.86468 1.14758 0.14833  0.16616  -0.07625 362 SER A N   
2774 C CA  . SER A 362 ? 0.97794 0.85750 1.14952 0.16194  0.18248  -0.09097 362 SER A CA  
2775 C C   . SER A 362 ? 0.91018 0.76405 1.04707 0.14944  0.18836  -0.10729 362 SER A C   
2776 O O   . SER A 362 ? 0.99685 0.85527 1.11610 0.13056  0.18168  -0.10731 362 SER A O   
2777 C CB  . SER A 362 ? 0.93672 0.85582 1.12912 0.17134  0.19405  -0.09143 362 SER A CB  
2778 O OG  . SER A 362 ? 0.85831 0.80070 1.03940 0.15438  0.19452  -0.09171 362 SER A OG  
2779 N N   . GLU A 363 ? 0.97838 0.80592 1.10577 0.16101  0.20117  -0.12176 363 GLU A N   
2780 C CA  . GLU A 363 ? 1.04654 0.85204 1.14063 0.15055  0.20861  -0.13960 363 GLU A CA  
2781 C C   . GLU A 363 ? 1.00069 0.83806 1.08525 0.13877  0.21216  -0.14169 363 GLU A C   
2782 O O   . GLU A 363 ? 1.06253 0.89315 1.12089 0.12082  0.20692  -0.14701 363 GLU A O   
2783 C CB  . GLU A 363 ? 0.93234 0.71137 1.02124 0.16806  0.22514  -0.15538 363 GLU A CB  
2784 C CG  . GLU A 363 ? 1.10818 0.84095 1.19080 0.17287  0.22117  -0.15754 363 GLU A CG  
2785 C CD  . GLU A 363 ? 1.31784 1.02823 1.37613 0.14926  0.20789  -0.15807 363 GLU A CD  
2786 O OE1 . GLU A 363 ? 1.39309 1.09111 1.42274 0.13528  0.21095  -0.17286 363 GLU A OE1 
2787 O OE2 . GLU A 363 ? 1.21365 0.92185 1.28183 0.14414  0.19417  -0.14348 363 GLU A OE2 
2788 N N   . PHE A 364 ? 0.93232 0.80578 1.03878 0.14828  0.22036  -0.13644 364 PHE A N   
2789 C CA  . PHE A 364 ? 0.90429 0.80629 1.00095 0.13788  0.22577  -0.13769 364 PHE A CA  
2790 C C   . PHE A 364 ? 0.88756 0.80644 0.98244 0.11987  0.20980  -0.12424 364 PHE A C   
2791 O O   . PHE A 364 ? 0.86394 0.78829 0.93593 0.10548  0.20880  -0.12721 364 PHE A O   
2792 C CB  . PHE A 364 ? 0.94370 0.88025 1.06686 0.15191  0.23950  -0.13495 364 PHE A CB  
2793 C CG  . PHE A 364 ? 0.94080 0.91098 1.05999 0.14009  0.24314  -0.13057 364 PHE A CG  
2794 C CD1 . PHE A 364 ? 0.96268 0.93165 1.05456 0.13514  0.25659  -0.14325 364 PHE A CD1 
2795 C CD2 . PHE A 364 ? 0.88237 0.88354 1.02331 0.13369  0.23343  -0.11372 364 PHE A CD2 
2796 C CE1 . PHE A 364 ? 0.93675 0.93418 1.02301 0.12438  0.26051  -0.13799 364 PHE A CE1 
2797 C CE2 . PHE A 364 ? 0.90990 0.93837 1.04588 0.12230  0.23731  -0.10918 364 PHE A CE2 
2798 C CZ  . PHE A 364 ? 0.92944 0.95575 1.03809 0.11784  0.25095  -0.12067 364 PHE A CZ  
2799 N N   . GLY A 365 ? 0.88631 0.81346 1.00434 0.12117  0.19730  -0.10930 365 GLY A N   
2800 C CA  . GLY A 365 ? 0.86159 0.80085 0.97718 0.10493  0.18236  -0.09741 365 GLY A CA  
2801 C C   . GLY A 365 ? 0.89011 0.80404 0.97646 0.08963  0.17377  -0.10345 365 GLY A C   
2802 O O   . GLY A 365 ? 0.87136 0.79629 0.94434 0.07542  0.16754  -0.10054 365 GLY A O   
2803 N N   . LYS A 366 ? 0.91683 0.79660 0.99340 0.09233  0.17337  -0.11192 366 LYS A N   
2804 C CA  . LYS A 366 ? 0.93718 0.79453 0.98854 0.07654  0.16490  -0.11816 366 LYS A CA  
2805 C C   . LYS A 366 ? 0.87431 0.72852 0.89703 0.06902  0.17214  -0.13296 366 LYS A C   
2806 O O   . LYS A 366 ? 0.90642 0.76161 0.91056 0.05340  0.16351  -0.13436 366 LYS A O   
2807 C CB  . LYS A 366 ? 0.97305 0.79324 1.02230 0.07995  0.16272  -0.12250 366 LYS A CB  
2808 C CG  . LYS A 366 ? 0.96594 0.78696 1.03762 0.08409  0.15279  -0.10648 366 LYS A CG  
2809 C CD  . LYS A 366 ? 1.03580 0.81721 1.10303 0.08721  0.15148  -0.10961 366 LYS A CD  
2810 C CE  . LYS A 366 ? 1.09323 0.85707 1.16613 0.10720  0.16453  -0.11744 366 LYS A CE  
2811 N NZ  . LYS A 366 ? 1.12577 0.86992 1.21322 0.11839  0.16021  -0.10739 366 LYS A NZ  
2812 N N   . GLU A 367 ? 0.89295 0.74346 0.91109 0.08037  0.18788  -0.14437 367 GLU A N   
2813 C CA  . GLU A 367 ? 0.93061 0.77995 0.91913 0.07357  0.19575  -0.15824 367 GLU A CA  
2814 C C   . GLU A 367 ? 0.90345 0.78490 0.88752 0.06348  0.19173  -0.14905 367 GLU A C   
2815 O O   . GLU A 367 ? 0.89338 0.77354 0.84997 0.05086  0.18820  -0.15504 367 GLU A O   
2816 C CB  . GLU A 367 ? 0.91731 0.76188 0.90494 0.08929  0.21541  -0.17055 367 GLU A CB  
2817 C CG  . GLU A 367 ? 1.06447 0.86956 1.02893 0.09162  0.22269  -0.19027 367 GLU A CG  
2818 C CD  . GLU A 367 ? 1.28252 1.08043 1.25820 0.11315  0.24156  -0.19896 367 GLU A CD  
2819 O OE1 . GLU A 367 ? 1.38477 1.17636 1.33887 0.11600  0.25631  -0.21489 367 GLU A OE1 
2820 O OE2 . GLU A 367 ? 1.28526 1.08412 1.29120 0.12798  0.24167  -0.18990 367 GLU A OE2 
2821 N N   . SER A 368 ? 0.84453 0.75419 0.85491 0.06856  0.19142  -0.13413 368 SER A N   
2822 C CA  . SER A 368 ? 0.87239 0.80982 0.87873 0.05969  0.18927  -0.12496 368 SER A CA  
2823 C C   . SER A 368 ? 0.87294 0.81056 0.87107 0.04477  0.17143  -0.11678 368 SER A C   
2824 O O   . SER A 368 ? 0.86646 0.81421 0.84571 0.03473  0.16827  -0.11511 368 SER A O   
2825 C CB  . SER A 368 ? 0.89525 0.86171 0.93308 0.06811  0.19414  -0.11214 368 SER A CB  
2826 O OG  . SER A 368 ? 0.87283 0.84439 0.93233 0.06633  0.18015  -0.09838 368 SER A OG  
2827 N N   . ILE A 369 ? 0.82893 0.75614 0.84107 0.04370  0.15996  -0.11090 369 ILE A N   
2828 C CA  . ILE A 369 ? 0.83390 0.75870 0.83695 0.02987  0.14445  -0.10615 369 ILE A CA  
2829 C C   . ILE A 369 ? 0.85762 0.76628 0.82950 0.02031  0.14294  -0.12033 369 ILE A C   
2830 O O   . ILE A 369 ? 0.88321 0.80158 0.83908 0.00977  0.13540  -0.11858 369 ILE A O   
2831 C CB  . ILE A 369 ? 0.84554 0.75862 0.86629 0.03024  0.13474  -0.09946 369 ILE A CB  
2832 C CG1 . ILE A 369 ? 0.79781 0.72818 0.84761 0.03889  0.13427  -0.08525 369 ILE A CG1 
2833 C CG2 . ILE A 369 ? 0.73617 0.64829 0.74852 0.01589  0.12022  -0.09574 369 ILE A CG2 
2834 C CD1 . ILE A 369 ? 0.78562 0.70063 0.85016 0.04175  0.12685  -0.07964 369 ILE A CD1 
2835 N N   . LEU A 370 ? 0.79974 0.68310 0.76203 0.02412  0.14981  -0.13478 370 LEU A N   
2836 C CA  . LEU A 370 ? 0.97077 0.83754 0.90249 0.01371  0.14779  -0.14986 370 LEU A CA  
2837 C C   . LEU A 370 ? 0.95398 0.83641 0.86257 0.01013  0.15233  -0.15328 370 LEU A C   
2838 O O   . LEU A 370 ? 0.99558 0.88010 0.88241 -0.00206 0.14301  -0.15652 370 LEU A O   
2839 C CB  . LEU A 370 ? 0.92473 0.75949 0.84847 0.01967  0.15731  -0.16606 370 LEU A CB  
2840 C CG  . LEU A 370 ? 1.02874 0.84452 0.91803 0.00902  0.15735  -0.18473 370 LEU A CG  
2841 C CD1 . LEU A 370 ? 1.04111 0.82403 0.92739 0.00343  0.15301  -0.19410 370 LEU A CD1 
2842 C CD2 . LEU A 370 ? 1.00963 0.82038 0.88063 0.01766  0.17448  -0.19825 370 LEU A CD2 
2843 N N   . PHE A 371 ? 0.92228 0.81773 0.83611 0.02051  0.16625  -0.15146 371 PHE A N   
2844 C CA  . PHE A 371 ? 0.97396 0.88163 0.86324 0.01766  0.17351  -0.15503 371 PHE A CA  
2845 C C   . PHE A 371 ? 0.92869 0.85799 0.81382 0.00807  0.16179  -0.14087 371 PHE A C   
2846 O O   . PHE A 371 ? 0.94277 0.87360 0.79900 -0.00070 0.15748  -0.14470 371 PHE A O   
2847 C CB  . PHE A 371 ? 0.96412 0.88313 0.86492 0.03091  0.19237  -0.15498 371 PHE A CB  
2848 C CG  . PHE A 371 ? 1.09172 1.02548 0.96919 0.02797  0.20188  -0.15605 371 PHE A CG  
2849 C CD1 . PHE A 371 ? 1.01523 0.97550 0.90360 0.02669  0.20280  -0.14022 371 PHE A CD1 
2850 C CD2 . PHE A 371 ? 1.11873 1.03829 0.96179 0.02613  0.21079  -0.17302 371 PHE A CD2 
2851 C CE1 . PHE A 371 ? 1.10054 1.07250 0.96561 0.02333  0.21256  -0.14008 371 PHE A CE1 
2852 C CE2 . PHE A 371 ? 1.12875 1.06115 0.94726 0.02317  0.22023  -0.17333 371 PHE A CE2 
2853 C CZ  . PHE A 371 ? 1.11836 1.07678 0.94795 0.02180  0.22138  -0.15629 371 PHE A CZ  
2854 N N   . HIS A 372 ? 0.88881 0.83394 0.80145 0.00996  0.15617  -0.12446 372 HIS A N   
2855 C CA  A HIS A 372 ? 0.90072 0.86417 0.81077 0.00244  0.14627  -0.11050 372 HIS A CA  
2856 C CA  B HIS A 372 ? 0.90108 0.86431 0.80963 0.00234  0.14665  -0.11105 372 HIS A CA  
2857 C C   . HIS A 372 ? 0.89488 0.85282 0.79299 -0.00841 0.12894  -0.11092 372 HIS A C   
2858 O O   . HIS A 372 ? 0.94128 0.90974 0.82411 -0.01495 0.12126  -0.10483 372 HIS A O   
2859 C CB  A HIS A 372 ? 0.84845 0.82762 0.79073 0.00676  0.14467  -0.09443 372 HIS A CB  
2860 C CB  B HIS A 372 ? 0.85089 0.83141 0.79039 0.00704  0.14683  -0.09495 372 HIS A CB  
2861 C CG  A HIS A 372 ? 0.87530 0.87121 0.81463 0.00057  0.13798  -0.08035 372 HIS A CG  
2862 C CG  B HIS A 372 ? 0.87117 0.86681 0.81599 0.01325  0.16254  -0.09194 372 HIS A CG  
2863 N ND1 A HIS A 372 ? 0.77030 0.78060 0.70523 0.00130  0.14787  -0.07407 372 HIS A ND1 
2864 N ND1 B HIS A 372 ? 0.88686 0.88056 0.84242 0.02388  0.17742  -0.10015 372 HIS A ND1 
2865 C CD2 A HIS A 372 ? 0.86209 0.86128 0.80195 -0.00621 0.12307  -0.07139 372 HIS A CD2 
2866 C CD2 B HIS A 372 ? 0.85109 0.86390 0.79136 0.00995  0.16649  -0.08199 372 HIS A CD2 
2867 C CE1 A HIS A 372 ? 0.81226 0.83113 0.74364 -0.00487 0.13892  -0.06161 372 HIS A CE1 
2868 C CE1 B HIS A 372 ? 0.85584 0.86805 0.81548 0.02648  0.19002  -0.09551 372 HIS A CE1 
2869 N NE2 A HIS A 372 ? 0.83884 0.85163 0.77359 -0.00864 0.12383  -0.05999 372 HIS A NE2 
2870 N NE2 B HIS A 372 ? 0.86108 0.88408 0.81077 0.01732  0.18381  -0.08433 372 HIS A NE2 
2871 N N   . TYR A 373 ? 0.90831 0.85020 0.81336 -0.01045 0.12269  -0.11772 373 TYR A N   
2872 C CA  . TYR A 373 ? 0.85358 0.79392 0.75349 -0.02124 0.10645  -0.11745 373 TYR A CA  
2873 C C   . TYR A 373 ? 0.92924 0.85406 0.80300 -0.02956 0.10321  -0.13446 373 TYR A C   
2874 O O   . TYR A 373 ? 0.96603 0.89108 0.83782 -0.03936 0.08974  -0.13556 373 TYR A O   
2875 C CB  . TYR A 373 ? 0.87920 0.81464 0.80644 -0.02081 0.10000  -0.11108 373 TYR A CB  
2876 C CG  . TYR A 373 ? 0.88932 0.84287 0.83811 -0.01813 0.09555  -0.09343 373 TYR A CG  
2877 C CD1 . TYR A 373 ? 0.78330 0.74239 0.75188 -0.00849 0.10420  -0.08587 373 TYR A CD1 
2878 C CD2 . TYR A 373 ? 0.84266 0.80820 0.79245 -0.02519 0.08249  -0.08485 373 TYR A CD2 
2879 C CE1 . TYR A 373 ? 0.77501 0.74935 0.76170 -0.00748 0.09966  -0.07082 373 TYR A CE1 
2880 C CE2 . TYR A 373 ? 0.74941 0.72865 0.71693 -0.02278 0.07904  -0.06980 373 TYR A CE2 
2881 C CZ  . TYR A 373 ? 0.79712 0.77970 0.78196 -0.01473 0.08748  -0.06322 373 TYR A CZ  
2882 O OH  . TYR A 373 ? 0.78979 0.78461 0.79025 -0.01378 0.08366  -0.04954 373 TYR A OH  
2883 N N   . THR A 374 ? 0.99704 0.90880 0.85101 -0.02656 0.11512  -0.14851 374 THR A N   
2884 C CA  . THR A 374 ? 1.08480 0.98111 0.91098 -0.03614 0.11109  -0.16574 374 THR A CA  
2885 C C   . THR A 374 ? 1.12748 1.02962 0.91963 -0.03823 0.11519  -0.17205 374 THR A C   
2886 O O   . THR A 374 ? 1.17461 1.06078 0.94006 -0.04286 0.11815  -0.18935 374 THR A O   
2887 C CB  . THR A 374 ? 1.07583 0.94280 0.90238 -0.03344 0.11988  -0.18119 374 THR A CB  
2888 O OG1 . THR A 374 ? 1.15114 1.01220 0.97623 -0.02040 0.13841  -0.18590 374 THR A OG1 
2889 C CG2 . THR A 374 ? 1.01115 0.86962 0.86709 -0.03290 0.11459  -0.17452 374 THR A CG2 
2890 N N   . ASP A 375 ? 1.15507 1.07827 0.94560 -0.03555 0.11545  -0.15829 375 ASP A N   
2891 C CA  . ASP A 375 ? 1.21975 1.14976 0.97513 -0.03967 0.11559  -0.16113 375 ASP A CA  
2892 C C   . ASP A 375 ? 1.33441 1.27587 1.08036 -0.05009 0.09491  -0.15594 375 ASP A C   
2893 O O   . ASP A 375 ? 1.27515 1.23417 1.03188 -0.04923 0.08700  -0.13906 375 ASP A O   
2894 C CB  . ASP A 375 ? 1.28418 1.22886 1.03963 -0.03228 0.12733  -0.14883 375 ASP A CB  
2895 C CG  . ASP A 375 ? 1.45261 1.40083 1.16832 -0.03637 0.12940  -0.15202 375 ASP A CG  
2896 O OD1 . ASP A 375 ? 1.39493 1.32931 1.08250 -0.04130 0.12972  -0.16939 375 ASP A OD1 
2897 O OD2 . ASP A 375 ? 1.46373 1.42688 1.17461 -0.03544 0.13004  -0.13728 375 ASP A OD2 
2898 N N   . TRP A 376 ? 1.34600 1.27763 1.07123 -0.05982 0.08634  -0.17106 376 TRP A N   
2899 C CA  . TRP A 376 ? 1.41786 1.36048 1.14330 -0.07016 0.06551  -0.16871 376 TRP A CA  
2900 C C   . TRP A 376 ? 1.55988 1.52025 1.25950 -0.07280 0.05551  -0.16102 376 TRP A C   
2901 O O   . TRP A 376 ? 1.57003 1.52583 1.23419 -0.07463 0.05984  -0.16967 376 TRP A O   
2902 C CB  . TRP A 376 ? 1.44739 1.37340 1.16105 -0.08119 0.05994  -0.18871 376 TRP A CB  
2903 C CG  . TRP A 376 ? 1.36786 1.27154 1.10246 -0.07957 0.06875  -0.19706 376 TRP A CG  
2904 C CD1 . TRP A 376 ? 1.33724 1.21380 1.05675 -0.08122 0.07882  -0.21641 376 TRP A CD1 
2905 C CD2 . TRP A 376 ? 1.25743 1.16159 1.02960 -0.07591 0.06795  -0.18633 376 TRP A CD2 
2906 N NE1 . TRP A 376 ? 1.27487 1.13424 1.02084 -0.07805 0.08421  -0.21728 376 TRP A NE1 
2907 C CE2 . TRP A 376 ? 1.18468 1.06119 0.96251 -0.07510 0.07747  -0.19881 376 TRP A CE2 
2908 C CE3 . TRP A 376 ? 1.16379 1.08743 0.96352 -0.07296 0.06047  -0.16758 376 TRP A CE3 
2909 C CZ2 . TRP A 376 ? 1.12649 0.99512 0.93559 -0.07161 0.07898  -0.19194 376 TRP A CZ2 
2910 C CZ3 . TRP A 376 ? 1.07429 0.99085 0.90457 -0.07010 0.06245  -0.16204 376 TRP A CZ3 
2911 C CH2 . TRP A 376 ? 1.06553 0.95523 0.89992 -0.06951 0.07130  -0.17357 376 TRP A CH2 
2912 N N   . VAL A 377 ? 1.60027 1.57980 1.31631 -0.07270 0.04190  -0.14489 377 VAL A N   
2913 C CA  . VAL A 377 ? 1.58021 1.57589 1.27304 -0.07584 0.02781  -0.13808 377 VAL A CA  
2914 C C   . VAL A 377 ? 1.67739 1.67200 1.34717 -0.08775 0.01480  -0.15462 377 VAL A C   
2915 O O   . VAL A 377 ? 1.70802 1.70990 1.34518 -0.09092 0.00664  -0.15551 377 VAL A O   
2916 C CB  . VAL A 377 ? 1.60981 1.62441 1.32855 -0.07239 0.01561  -0.11893 377 VAL A CB  
2917 C CG1 . VAL A 377 ? 1.54421 1.55871 1.27901 -0.06206 0.02852  -0.10338 377 VAL A CG1 
2918 C CG2 . VAL A 377 ? 1.66110 1.67877 1.41140 -0.07752 0.00649  -0.12221 377 VAL A CG2 
2919 N N   . ASP A 378 ? 1.75746 1.74219 1.44226 -0.09522 0.01258  -0.16794 378 ASP A N   
2920 C CA  . ASP A 378 ? 1.77780 1.75433 1.43922 -0.10806 0.00507  -0.18821 378 ASP A CA  
2921 C C   . ASP A 378 ? 1.78032 1.73070 1.45339 -0.11095 0.01694  -0.20350 378 ASP A C   
2922 O O   . ASP A 378 ? 1.74472 1.69345 1.45187 -0.11048 0.01696  -0.19862 378 ASP A O   
2923 C CB  . ASP A 378 ? 1.77173 1.77000 1.44086 -0.11842 -0.01825 -0.18701 378 ASP A CB  
2924 C CG  . ASP A 378 ? 1.77722 1.76928 1.42044 -0.13370 -0.02759 -0.20846 378 ASP A CG  
2925 O OD1 . ASP A 378 ? 1.74841 1.71880 1.39596 -0.14116 -0.02099 -0.22452 378 ASP A OD1 
2926 O OD2 . ASP A 378 ? 1.66838 1.67612 1.28558 -0.13848 -0.04194 -0.20931 378 ASP A OD2 
2927 N N   . ASP A 379 ? 1.69050 1.61898 1.33390 -0.11365 0.02721  -0.22190 379 ASP A N   
2928 C CA  . ASP A 379 ? 1.69099 1.59002 1.34245 -0.11394 0.04062  -0.23646 379 ASP A CA  
2929 C C   . ASP A 379 ? 1.74420 1.63256 1.39733 -0.13012 0.02940  -0.25193 379 ASP A C   
2930 O O   . ASP A 379 ? 1.70548 1.56600 1.36512 -0.13139 0.03945  -0.26375 379 ASP A O   
2931 C CB  . ASP A 379 ? 1.75700 1.63497 1.37763 -0.10770 0.05948  -0.24975 379 ASP A CB  
2932 C CG  . ASP A 379 ? 1.89808 1.76116 1.47813 -0.12052 0.05535  -0.27292 379 ASP A CG  
2933 O OD1 . ASP A 379 ? 1.91891 1.79411 1.48927 -0.13446 0.03581  -0.27697 379 ASP A OD1 
2934 O OD2 . ASP A 379 ? 1.93586 1.77519 1.49336 -0.11648 0.07213  -0.28797 379 ASP A OD2 
2935 N N   . GLN A 380 ? 1.74695 1.65685 1.39557 -0.14241 0.00888  -0.25167 380 GLN A N   
2936 C CA  . GLN A 380 ? 1.75867 1.66235 1.40792 -0.16048 -0.00291 -0.26708 380 GLN A CA  
2937 C C   . GLN A 380 ? 1.63980 1.56033 1.32927 -0.16598 -0.01406 -0.25623 380 GLN A C   
2938 O O   . GLN A 380 ? 1.55066 1.46396 1.24649 -0.18157 -0.02105 -0.26824 380 GLN A O   
2939 C CB  . GLN A 380 ? 1.81656 1.73435 1.43145 -0.17296 -0.01924 -0.27772 380 GLN A CB  
2940 C CG  . GLN A 380 ? 1.89998 1.79618 1.46937 -0.17220 -0.00859 -0.29417 380 GLN A CG  
2941 C CD  . GLN A 380 ? 1.99433 1.85249 1.55230 -0.18132 0.00151  -0.31826 380 GLN A CD  
2942 O OE1 . GLN A 380 ? 2.05469 1.90807 1.60083 -0.19955 -0.01055 -0.33474 380 GLN A OE1 
2943 N NE2 . GLN A 380 ? 2.01831 1.84896 1.58052 -0.16853 0.02370  -0.32043 380 GLN A NE2 
2944 N N   . ARG A 381 ? 1.56596 1.50766 1.28166 -0.15446 -0.01510 -0.23461 381 ARG A N   
2945 C CA  . ARG A 381 ? 1.43557 1.39504 1.18839 -0.15873 -0.02473 -0.22392 381 ARG A CA  
2946 C C   . ARG A 381 ? 1.36653 1.29922 1.14045 -0.16168 -0.01383 -0.22886 381 ARG A C   
2947 O O   . ARG A 381 ? 1.43895 1.35089 1.21710 -0.14935 0.00247  -0.22544 381 ARG A O   
2948 C CB  . ARG A 381 ? 1.45513 1.43753 1.22761 -0.14398 -0.02534 -0.20066 381 ARG A CB  
2949 C CG  . ARG A 381 ? 1.54336 1.54906 1.29477 -0.13899 -0.03509 -0.19267 381 ARG A CG  
2950 C CD  . ARG A 381 ? 1.56861 1.59570 1.34374 -0.12673 -0.03763 -0.16996 381 ARG A CD  
2951 N NE  . ARG A 381 ? 1.58099 1.61514 1.39369 -0.12962 -0.04056 -0.16426 381 ARG A NE  
2952 C CZ  . ARG A 381 ? 1.61801 1.67912 1.45276 -0.12769 -0.05218 -0.15126 381 ARG A CZ  
2953 N NH1 . ARG A 381 ? 1.67508 1.75807 1.49965 -0.12171 -0.06290 -0.14129 381 ARG A NH1 
2954 N NH2 . ARG A 381 ? 1.47501 1.54028 1.34193 -0.13134 -0.05254 -0.14799 381 ARG A NH2 
2955 N N   . PRO A 382 ? 1.31161 1.24421 1.09924 -0.17781 -0.02226 -0.23635 382 PRO A N   
2956 C CA  . PRO A 382 ? 1.27972 1.18303 1.08446 -0.18114 -0.01147 -0.24020 382 PRO A CA  
2957 C C   . PRO A 382 ? 1.14147 1.04916 0.97849 -0.16876 -0.00476 -0.22079 382 PRO A C   
2958 O O   . PRO A 382 ? 1.10904 0.98892 0.95586 -0.16638 0.00678  -0.22161 382 PRO A O   
2959 C CB  . PRO A 382 ? 1.27372 1.18182 1.08496 -0.20382 -0.02395 -0.25148 382 PRO A CB  
2960 C CG  . PRO A 382 ? 1.25164 1.20118 1.06104 -0.20912 -0.04274 -0.24797 382 PRO A CG  
2961 C CD  . PRO A 382 ? 1.26792 1.22318 1.05066 -0.19526 -0.04116 -0.24473 382 PRO A CD  
2962 N N   . GLU A 383 ? 1.07826 1.01807 0.93077 -0.16077 -0.01180 -0.20360 383 GLU A N   
2963 C CA  . GLU A 383 ? 1.05524 0.99875 0.93558 -0.14915 -0.00551 -0.18591 383 GLU A CA  
2964 C C   . GLU A 383 ? 1.08181 1.01490 0.95676 -0.13076 0.00780  -0.17800 383 GLU A C   
2965 O O   . GLU A 383 ? 0.98736 0.92299 0.88371 -0.12088 0.01298  -0.16374 383 GLU A O   
2966 C CB  . GLU A 383 ? 1.04111 1.02192 0.94162 -0.14823 -0.01797 -0.17122 383 GLU A CB  
2967 C CG  . GLU A 383 ? 1.12652 1.12975 1.03226 -0.16475 -0.03369 -0.17789 383 GLU A CG  
2968 C CD  . GLU A 383 ? 1.30650 1.32397 1.18551 -0.16889 -0.04497 -0.18649 383 GLU A CD  
2969 O OE1 . GLU A 383 ? 1.29322 1.30558 1.15025 -0.15749 -0.04019 -0.18431 383 GLU A OE1 
2970 O OE2 . GLU A 383 ? 1.29202 1.32589 1.17143 -0.18422 -0.05845 -0.19562 383 GLU A OE2 
2971 N N   . ASN A 384 ? 1.16528 1.08785 1.01231 -0.12672 0.01358  -0.18730 384 ASN A N   
2972 C CA  . ASN A 384 ? 1.08046 1.00044 0.92231 -0.11016 0.02561  -0.17937 384 ASN A CA  
2973 C C   . ASN A 384 ? 1.04252 0.94556 0.90618 -0.09994 0.03823  -0.17234 384 ASN A C   
2974 O O   . ASN A 384 ? 1.04307 0.95786 0.92191 -0.08855 0.04182  -0.15707 384 ASN A O   
2975 C CB  . ASN A 384 ? 1.10199 1.00716 0.90999 -0.10928 0.03302  -0.19419 384 ASN A CB  
2976 C CG  . ASN A 384 ? 1.25044 1.17785 1.03495 -0.11096 0.02370  -0.19273 384 ASN A CG  
2977 O OD1 . ASN A 384 ? 1.23760 1.19085 1.03230 -0.10797 0.01446  -0.17756 384 ASN A OD1 
2978 N ND2 . ASN A 384 ? 1.33573 1.25162 1.08681 -0.11560 0.02596  -0.20865 384 ASN A ND2 
2979 N N   . TYR A 385 ? 0.99193 0.86653 0.85694 -0.10412 0.04447  -0.18309 385 TYR A N   
2980 C CA  . TYR A 385 ? 1.01156 0.86897 0.89556 -0.09318 0.05567  -0.17606 385 TYR A CA  
2981 C C   . TYR A 385 ? 0.98191 0.85054 0.89409 -0.09515 0.04934  -0.16146 385 TYR A C   
2982 O O   . TYR A 385 ? 0.85874 0.72976 0.78830 -0.08346 0.05473  -0.14839 385 TYR A O   
2983 C CB  . TYR A 385 ? 1.03863 0.85838 0.91272 -0.09509 0.06508  -0.19156 385 TYR A CB  
2984 C CG  . TYR A 385 ? 1.13262 0.93937 0.98105 -0.08821 0.07572  -0.20471 385 TYR A CG  
2985 C CD1 . TYR A 385 ? 1.12071 0.92868 0.97309 -0.07059 0.08844  -0.19864 385 TYR A CD1 
2986 C CD2 . TYR A 385 ? 1.12204 0.91676 0.94221 -0.09987 0.07334  -0.22362 385 TYR A CD2 
2987 C CE1 . TYR A 385 ? 1.08179 0.87944 0.91101 -0.06410 0.09995  -0.21101 385 TYR A CE1 
2988 C CE2 . TYR A 385 ? 1.12650 0.90878 0.92091 -0.09362 0.08410  -0.23634 385 TYR A CE2 
2989 C CZ  . TYR A 385 ? 1.18309 0.96704 0.98223 -0.07546 0.09802  -0.22994 385 TYR A CZ  
2990 O OH  . TYR A 385 ? 1.21669 0.98941 0.98997 -0.06956 0.11012  -0.24332 385 TYR A OH  
2991 N N   . ARG A 386 ? 0.91380 0.79123 0.83080 -0.11010 0.03801  -0.16369 386 ARG A N   
2992 C CA  . ARG A 386 ? 0.92220 0.81266 0.86478 -0.11259 0.03271  -0.15037 386 ARG A CA  
2993 C C   . ARG A 386 ? 0.88252 0.80035 0.83668 -0.10146 0.03013  -0.13374 386 ARG A C   
2994 O O   . ARG A 386 ? 0.85196 0.77017 0.82404 -0.09367 0.03388  -0.12125 386 ARG A O   
2995 C CB  . ARG A 386 ? 0.88200 0.78410 0.82777 -0.13084 0.02099  -0.15642 386 ARG A CB  
2996 C CG  . ARG A 386 ? 0.78829 0.70827 0.75989 -0.13420 0.01583  -0.14353 386 ARG A CG  
2997 C CD  . ARG A 386 ? 0.90102 0.84167 0.87662 -0.15106 0.00358  -0.14966 386 ARG A CD  
2998 N NE  . ARG A 386 ? 0.88807 0.86407 0.86472 -0.14746 -0.00707 -0.14367 386 ARG A NE  
2999 C CZ  . ARG A 386 ? 0.85711 0.85763 0.83503 -0.15897 -0.01981 -0.14892 386 ARG A CZ  
3000 N NH1 . ARG A 386 ? 0.91880 0.91421 0.89711 -0.17694 -0.02370 -0.16148 386 ARG A NH1 
3001 N NH2 . ARG A 386 ? 0.85084 0.88172 0.82974 -0.15240 -0.02920 -0.14127 386 ARG A NH2 
3002 N N   . GLU A 387 ? 0.85535 0.79465 0.79772 -0.10079 0.02354  -0.13333 387 GLU A N   
3003 C CA  . GLU A 387 ? 0.88036 0.84193 0.83115 -0.09062 0.02151  -0.11786 387 GLU A CA  
3004 C C   . GLU A 387 ? 0.86824 0.82036 0.81951 -0.07656 0.03368  -0.11167 387 GLU A C   
3005 O O   . GLU A 387 ? 0.83208 0.79346 0.79915 -0.06884 0.03497  -0.09797 387 GLU A O   
3006 C CB  . GLU A 387 ? 0.91076 0.89350 0.84539 -0.09254 0.01202  -0.11859 387 GLU A CB  
3007 C CG  . GLU A 387 ? 1.02116 1.01524 0.95432 -0.10668 -0.00064 -0.12694 387 GLU A CG  
3008 C CD  . GLU A 387 ? 1.20174 1.22436 1.12950 -0.10606 -0.01323 -0.12100 387 GLU A CD  
3009 O OE1 . GLU A 387 ? 1.23792 1.28121 1.18389 -0.10986 -0.02295 -0.11517 387 GLU A OE1 
3010 O OE2 . GLU A 387 ? 1.27584 1.29998 1.18065 -0.10128 -0.01301 -0.12195 387 GLU A OE2 
3011 N N   . ALA A 388 ? 0.89433 0.82910 0.82877 -0.07328 0.04287  -0.12219 388 ALA A N   
3012 C CA  . ALA A 388 ? 0.84748 0.77748 0.78404 -0.05984 0.05496  -0.11705 388 ALA A CA  
3013 C C   . ALA A 388 ? 0.83937 0.76032 0.79964 -0.05338 0.05988  -0.10864 388 ALA A C   
3014 O O   . ALA A 388 ? 0.78228 0.71266 0.75456 -0.04393 0.06381  -0.09715 388 ALA A O   
3015 C CB  . ALA A 388 ? 0.85311 0.76531 0.76839 -0.05738 0.06513  -0.13164 388 ALA A CB  
3016 N N   . LEU A 389 ? 0.81169 0.71417 0.77814 -0.05916 0.05923  -0.11380 389 LEU A N   
3017 C CA  . LEU A 389 ? 0.81022 0.70132 0.79576 -0.05256 0.06373  -0.10560 389 LEU A CA  
3018 C C   . LEU A 389 ? 0.83200 0.74219 0.83571 -0.05250 0.05700  -0.09022 389 LEU A C   
3019 O O   . LEU A 389 ? 0.80117 0.71372 0.81831 -0.04301 0.06066  -0.07982 389 LEU A O   
3020 C CB  . LEU A 389 ? 0.88427 0.74741 0.86873 -0.05936 0.06521  -0.11425 389 LEU A CB  
3021 C CG  . LEU A 389 ? 0.89065 0.73613 0.88963 -0.04940 0.07176  -0.10683 389 LEU A CG  
3022 C CD1 . LEU A 389 ? 0.71552 0.55702 0.71447 -0.03339 0.08227  -0.10738 389 LEU A CD1 
3023 C CD2 . LEU A 389 ? 0.77374 0.58830 0.76995 -0.05713 0.07299  -0.11381 389 LEU A CD2 
3024 N N   . GLY A 390 ? 0.78526 0.71033 0.78973 -0.06271 0.04711  -0.08906 390 GLY A N   
3025 C CA  . GLY A 390 ? 0.70682 0.65097 0.72648 -0.06171 0.04148  -0.07553 390 GLY A CA  
3026 C C   . GLY A 390 ? 0.75759 0.71727 0.77804 -0.05186 0.04308  -0.06625 390 GLY A C   
3027 O O   . GLY A 390 ? 0.68746 0.65159 0.72132 -0.04594 0.04431  -0.05526 390 GLY A O   
3028 N N   . ASP A 391 ? 0.72573 0.69273 0.73029 -0.05080 0.04329  -0.07064 391 ASP A N   
3029 C CA  . ASP A 391 ? 0.71542 0.69508 0.71866 -0.04282 0.04602  -0.06179 391 ASP A CA  
3030 C C   . ASP A 391 ? 0.73945 0.71155 0.75168 -0.03339 0.05627  -0.05828 391 ASP A C   
3031 O O   . ASP A 391 ? 0.74202 0.72393 0.76461 -0.02824 0.05737  -0.04743 391 ASP A O   
3032 C CB  . ASP A 391 ? 0.77844 0.76373 0.75938 -0.04391 0.04582  -0.06770 391 ASP A CB  
3033 C CG  . ASP A 391 ? 0.79760 0.79872 0.77210 -0.04983 0.03385  -0.06550 391 ASP A CG  
3034 O OD1 . ASP A 391 ? 0.81105 0.82340 0.79947 -0.04960 0.02765  -0.05570 391 ASP A OD1 
3035 O OD2 . ASP A 391 ? 0.86089 0.86343 0.81580 -0.05419 0.03058  -0.07395 391 ASP A OD2 
3036 N N   . VAL A 392 ? 0.72611 0.68100 0.73499 -0.03085 0.06373  -0.06766 392 VAL A N   
3037 C CA  . VAL A 392 ? 0.76825 0.71778 0.78877 -0.02044 0.07295  -0.06443 392 VAL A CA  
3038 C C   . VAL A 392 ? 0.70590 0.65713 0.74674 -0.01828 0.06929  -0.05299 392 VAL A C   
3039 O O   . VAL A 392 ? 0.69460 0.65703 0.74687 -0.01232 0.07113  -0.04365 392 VAL A O   
3040 C CB  . VAL A 392 ? 0.75832 0.68588 0.77258 -0.01711 0.08099  -0.07685 392 VAL A CB  
3041 C CG1 . VAL A 392 ? 0.80707 0.72820 0.83871 -0.00563 0.08789  -0.07203 392 VAL A CG1 
3042 C CG2 . VAL A 392 ? 0.80291 0.73066 0.79726 -0.01617 0.08782  -0.08727 392 VAL A CG2 
3043 N N   . VAL A 393 ? 0.69907 0.63937 0.74355 -0.02420 0.06413  -0.05377 393 VAL A N   
3044 C CA  . VAL A 393 ? 0.71726 0.65656 0.77756 -0.02267 0.06113  -0.04345 393 VAL A CA  
3045 C C   . VAL A 393 ? 0.70433 0.66367 0.77075 -0.02403 0.05551  -0.03296 393 VAL A C   
3046 O O   . VAL A 393 ? 0.69374 0.65818 0.77185 -0.01923 0.05541  -0.02361 393 VAL A O   
3047 C CB  . VAL A 393 ? 0.76187 0.68501 0.82180 -0.03086 0.05769  -0.04672 393 VAL A CB  
3048 C CG1 . VAL A 393 ? 0.69501 0.62024 0.76760 -0.03160 0.05361  -0.03521 393 VAL A CG1 
3049 C CG2 . VAL A 393 ? 0.71206 0.60932 0.76686 -0.02803 0.06417  -0.05570 393 VAL A CG2 
3050 N N   . GLY A 394 ? 0.68981 0.66027 0.74787 -0.03027 0.05039  -0.03455 394 GLY A N   
3051 C CA  . GLY A 394 ? 0.66056 0.64699 0.72336 -0.03079 0.04527  -0.02504 394 GLY A CA  
3052 C C   . GLY A 394 ? 0.71954 0.71541 0.78246 -0.02457 0.04912  -0.01919 394 GLY A C   
3053 O O   . GLY A 394 ? 0.70538 0.70781 0.77742 -0.02257 0.04776  -0.01001 394 GLY A O   
3054 N N   . ASP A 395 ? 0.63101 0.62744 0.68276 -0.02244 0.05441  -0.02477 395 ASP A N   
3055 C CA  . ASP A 395 ? 0.64239 0.64864 0.69368 -0.01817 0.05928  -0.01904 395 ASP A CA  
3056 C C   . ASP A 395 ? 0.72101 0.72720 0.78844 -0.01207 0.06472  -0.01481 395 ASP A C   
3057 O O   . ASP A 395 ? 0.70416 0.71980 0.77999 -0.01094 0.06476  -0.00620 395 ASP A O   
3058 C CB  . ASP A 395 ? 0.64288 0.64966 0.67683 -0.01766 0.06512  -0.02621 395 ASP A CB  
3059 C CG  . ASP A 395 ? 0.75832 0.76864 0.77467 -0.02329 0.05817  -0.02876 395 ASP A CG  
3060 O OD1 . ASP A 395 ? 0.72707 0.74368 0.74656 -0.02613 0.04952  -0.02247 395 ASP A OD1 
3061 O OD2 . ASP A 395 ? 0.70568 0.71271 0.70482 -0.02442 0.06124  -0.03755 395 ASP A OD2 
3062 N N   . TYR A 396 ? 0.72616 0.72141 0.79814 -0.00801 0.06896  -0.02088 396 TYR A N   
3063 C CA  . TYR A 396 ? 0.66075 0.65744 0.74932 -0.00055 0.07318  -0.01679 396 TYR A CA  
3064 C C   . TYR A 396 ? 0.67667 0.67468 0.77781 -0.00164 0.06598  -0.00744 396 TYR A C   
3065 O O   . TYR A 396 ? 0.62352 0.63172 0.73710 0.00147  0.06621  -0.00027 396 TYR A O   
3066 C CB  . TYR A 396 ? 0.70453 0.68604 0.79359 0.00536  0.07885  -0.02535 396 TYR A CB  
3067 C CG  . TYR A 396 ? 0.70261 0.68334 0.81002 0.01452  0.08095  -0.02068 396 TYR A CG  
3068 C CD1 . TYR A 396 ? 0.74637 0.74408 0.86695 0.02081  0.08604  -0.01633 396 TYR A CD1 
3069 C CD2 . TYR A 396 ? 0.73045 0.69397 0.84205 0.01681  0.07783  -0.02035 396 TYR A CD2 
3070 C CE1 . TYR A 396 ? 0.65898 0.65959 0.79826 0.03003  0.08679  -0.01188 396 TYR A CE1 
3071 C CE2 . TYR A 396 ? 0.75030 0.71306 0.87782 0.02665  0.07867  -0.01512 396 TYR A CE2 
3072 C CZ  . TYR A 396 ? 0.84778 0.83077 0.99001 0.03371  0.08260  -0.01100 396 TYR A CZ  
3073 O OH  . TYR A 396 ? 0.77280 0.75950 0.93302 0.04409  0.08221  -0.00549 396 TYR A OH  
3074 N N   . ASN A 397 ? 0.68172 0.67051 0.77943 -0.00685 0.05974  -0.00769 397 ASN A N   
3075 C CA  . ASN A 397 ? 0.67439 0.66123 0.78185 -0.00731 0.05442  0.00009  397 ASN A CA  
3076 C C   . ASN A 397 ? 0.73239 0.72973 0.84001 -0.01223 0.04893  0.00714  397 ASN A C   
3077 O O   . ASN A 397 ? 0.67042 0.66862 0.78551 -0.01200 0.04545  0.01399  397 ASN A O   
3078 C CB  . ASN A 397 ? 0.63804 0.60799 0.74236 -0.01060 0.05221  -0.00324 397 ASN A CB  
3079 C CG  . ASN A 397 ? 0.70163 0.65663 0.80939 -0.00370 0.05668  -0.00640 397 ASN A CG  
3080 O OD1 . ASN A 397 ? 0.71311 0.66837 0.83149 0.00313  0.05643  -0.00001 397 ASN A OD1 
3081 N ND2 . ASN A 397 ? 0.67416 0.61566 0.77273 -0.00495 0.06045  -0.01640 397 ASN A ND2 
3082 N N   . PHE A 398 ? 0.65053 0.65476 0.74901 -0.01605 0.04791  0.00573  398 PHE A N   
3083 C CA  . PHE A 398 ? 0.63653 0.64741 0.73442 -0.01959 0.04286  0.01183  398 PHE A CA  
3084 C C   . PHE A 398 ? 0.71681 0.73662 0.80767 -0.01982 0.04386  0.01414  398 PHE A C   
3085 O O   . PHE A 398 ? 0.62888 0.65338 0.72325 -0.01982 0.04352  0.02078  398 PHE A O   
3086 C CB  . PHE A 398 ? 0.61877 0.62661 0.71296 -0.02456 0.03820  0.00921  398 PHE A CB  
3087 C CG  . PHE A 398 ? 0.72957 0.72684 0.82908 -0.02612 0.03759  0.00856  398 PHE A CG  
3088 C CD1 . PHE A 398 ? 0.66290 0.65888 0.76835 -0.02634 0.03543  0.01529  398 PHE A CD1 
3089 C CD2 . PHE A 398 ? 0.67933 0.66579 0.77576 -0.02782 0.03953  0.00123  398 PHE A CD2 
3090 C CE1 . PHE A 398 ? 0.71038 0.69501 0.81800 -0.02804 0.03522  0.01590  398 PHE A CE1 
3091 C CE2 . PHE A 398 ? 0.67779 0.65111 0.77741 -0.02978 0.03956  0.00167  398 PHE A CE2 
3092 C CZ  . PHE A 398 ? 0.66688 0.63959 0.77180 -0.02976 0.03744  0.00961  398 PHE A CZ  
3093 N N   . ILE A 399 ? 0.67911 0.69987 0.75835 -0.02069 0.04486  0.00882  399 ILE A N   
3094 C CA  . ILE A 399 ? 0.65678 0.68381 0.72557 -0.02129 0.04438  0.01216  399 ILE A CA  
3095 C C   . ILE A 399 ? 0.73562 0.76676 0.80578 -0.01950 0.05101  0.01635  399 ILE A C   
3096 O O   . ILE A 399 ? 0.69850 0.73227 0.76900 -0.02066 0.05034  0.02370  399 ILE A O   
3097 C CB  . ILE A 399 ? 0.70505 0.73243 0.75915 -0.02281 0.04298  0.00528  399 ILE A CB  
3098 C CG1 . ILE A 399 ? 0.59323 0.62130 0.64840 -0.02613 0.03522  0.00262  399 ILE A CG1 
3099 C CG2 . ILE A 399 ? 0.69974 0.73190 0.73979 -0.02231 0.04378  0.00934  399 ILE A CG2 
3100 C CD1 . ILE A 399 ? 0.69022 0.72050 0.73230 -0.02893 0.03202  -0.00495 399 ILE A CD1 
3101 N N   . CYS A 400 ? 0.63350 0.66508 0.70542 -0.01689 0.05815  0.01149  400 CYS A N   
3102 C CA  . CYS A 400 ? 0.67010 0.70911 0.74570 -0.01573 0.06576  0.01484  400 CYS A CA  
3103 C C   . CYS A 400 ? 0.70194 0.74603 0.79498 -0.01582 0.06490  0.02152  400 CYS A C   
3104 O O   . CYS A 400 ? 0.66539 0.71593 0.75996 -0.01855 0.06773  0.02725  400 CYS A O   
3105 C CB  . CYS A 400 ? 0.62646 0.66622 0.70165 -0.01163 0.07456  0.00711  400 CYS A CB  
3106 S SG  . CYS A 400 ? 0.74126 0.77560 0.79148 -0.01301 0.07639  -0.00154 400 CYS A SG  
3107 N N   . PRO A 401 ? 0.66063 0.70171 0.76592 -0.01373 0.06095  0.02130  401 PRO A N   
3108 C CA  . PRO A 401 ? 0.67611 0.72281 0.79508 -0.01481 0.05836  0.02794  401 PRO A CA  
3109 C C   . PRO A 401 ? 0.67879 0.72323 0.79185 -0.02020 0.05329  0.03377  401 PRO A C   
3110 O O   . PRO A 401 ? 0.62873 0.67851 0.74750 -0.02348 0.05358  0.03889  401 PRO A O   
3111 C CB  . PRO A 401 ? 0.65560 0.69653 0.78366 -0.01125 0.05418  0.02677  401 PRO A CB  
3112 C CG  . PRO A 401 ? 0.59522 0.62865 0.71825 -0.00733 0.05777  0.01901  401 PRO A CG  
3113 C CD  . PRO A 401 ? 0.59752 0.62923 0.70402 -0.01095 0.05883  0.01558  401 PRO A CD  
3114 N N   . ALA A 402 ? 0.58971 0.62665 0.69187 -0.02127 0.04890  0.03279  402 ALA A N   
3115 C CA  . ALA A 402 ? 0.61652 0.65024 0.71364 -0.02448 0.04481  0.03810  402 ALA A CA  
3116 C C   . ALA A 402 ? 0.66234 0.69727 0.75040 -0.02667 0.04854  0.04198  402 ALA A C   
3117 O O   . ALA A 402 ? 0.62902 0.66201 0.71767 -0.03016 0.04821  0.04735  402 ALA A O   
3118 C CB  . ALA A 402 ? 0.58235 0.61079 0.67296 -0.02391 0.03957  0.03627  402 ALA A CB  
3119 N N   . LEU A 403 ? 0.66793 0.70439 0.74568 -0.02537 0.05233  0.03936  403 LEU A N   
3120 C CA  . LEU A 403 ? 0.69727 0.73391 0.76445 -0.02786 0.05703  0.04408  403 LEU A CA  
3121 C C   . LEU A 403 ? 0.67555 0.71880 0.75380 -0.03165 0.06303  0.04736  403 LEU A C   
3122 O O   . LEU A 403 ? 0.71835 0.75843 0.79282 -0.03647 0.06448  0.05363  403 LEU A O   
3123 C CB  . LEU A 403 ? 0.66883 0.70710 0.72204 -0.02608 0.06106  0.04003  403 LEU A CB  
3124 C CG  . LEU A 403 ? 0.68438 0.71808 0.72491 -0.02396 0.05372  0.03832  403 LEU A CG  
3125 C CD1 . LEU A 403 ? 0.67417 0.71018 0.70444 -0.02260 0.05616  0.03055  403 LEU A CD1 
3126 C CD2 . LEU A 403 ? 0.54187 0.56978 0.56871 -0.02434 0.05078  0.04653  403 LEU A CD2 
3127 N N   . GLU A 404 ? 0.62989 0.68235 0.72276 -0.02959 0.06636  0.04327  404 GLU A N   
3128 C CA  . GLU A 404 ? 0.68485 0.74884 0.79177 -0.03281 0.07203  0.04582  404 GLU A CA  
3129 C C   . GLU A 404 ? 0.67157 0.73496 0.78814 -0.03779 0.06625  0.05066  404 GLU A C   
3130 O O   . GLU A 404 ? 0.62551 0.69428 0.74703 -0.04443 0.06950  0.05487  404 GLU A O   
3131 C CB  . GLU A 404 ? 0.61357 0.68827 0.73519 -0.02698 0.07621  0.04017  404 GLU A CB  
3132 C CG  . GLU A 404 ? 0.87129 0.96323 1.00888 -0.02889 0.08413  0.04171  404 GLU A CG  
3133 C CD  . GLU A 404 ? 0.98674 1.08187 1.11304 -0.03422 0.09394  0.04412  404 GLU A CD  
3134 O OE1 . GLU A 404 ? 0.95231 1.03786 1.05765 -0.03319 0.09629  0.04246  404 GLU A OE1 
3135 O OE2 . GLU A 404 ? 0.98709 1.09482 1.12518 -0.04016 0.09907  0.04798  404 GLU A OE2 
3136 N N   . PHE A 405 ? 0.64987 0.70643 0.76824 -0.03564 0.05807  0.04973  405 PHE A N   
3137 C CA  . PHE A 405 ? 0.67598 0.72951 0.79905 -0.04053 0.05236  0.05336  405 PHE A CA  
3138 C C   . PHE A 405 ? 0.70044 0.74287 0.81022 -0.04614 0.05271  0.05792  405 PHE A C   
3139 O O   . PHE A 405 ? 0.67120 0.71386 0.78458 -0.05348 0.05311  0.06130  405 PHE A O   
3140 C CB  . PHE A 405 ? 0.61012 0.65672 0.73339 -0.03699 0.04494  0.05138  405 PHE A CB  
3141 C CG  . PHE A 405 ? 0.68077 0.72190 0.80427 -0.04178 0.03936  0.05411  405 PHE A CG  
3142 C CD1 . PHE A 405 ? 0.65206 0.67974 0.76252 -0.04364 0.03746  0.05566  405 PHE A CD1 
3143 C CD2 . PHE A 405 ? 0.61829 0.66752 0.75436 -0.04392 0.03570  0.05488  405 PHE A CD2 
3144 C CE1 . PHE A 405 ? 0.69000 0.71048 0.79870 -0.04813 0.03322  0.05695  405 PHE A CE1 
3145 C CE2 . PHE A 405 ? 0.67812 0.72151 0.81170 -0.04925 0.03019  0.05646  405 PHE A CE2 
3146 C CZ  . PHE A 405 ? 0.70636 0.73429 0.82548 -0.05163 0.02954  0.05697  405 PHE A CZ  
3147 N N   . THR A 406 ? 0.56923 0.60146 0.66355 -0.04277 0.05223  0.05809  406 THR A N   
3148 C CA  . THR A 406 ? 0.57681 0.59589 0.65694 -0.04562 0.05227  0.06319  406 THR A CA  
3149 C C   . THR A 406 ? 0.66367 0.68405 0.74004 -0.05206 0.05981  0.06776  406 THR A C   
3150 O O   . THR A 406 ? 0.70066 0.71095 0.77239 -0.05843 0.06041  0.07249  406 THR A O   
3151 C CB  . THR A 406 ? 0.69372 0.70587 0.75996 -0.03913 0.04963  0.06273  406 THR A CB  
3152 O OG1 . THR A 406 ? 0.61700 0.63022 0.68861 -0.03456 0.04386  0.05815  406 THR A OG1 
3153 C CG2 . THR A 406 ? 0.61590 0.61260 0.66790 -0.03968 0.04858  0.06888  406 THR A CG2 
3154 N N   . LYS A 407 ? 0.70864 0.74005 0.78586 -0.05108 0.06650  0.06621  407 LYS A N   
3155 C CA  . LYS A 407 ? 0.74608 0.78094 0.82081 -0.05820 0.07539  0.07059  407 LYS A CA  
3156 C C   . LYS A 407 ? 0.72091 0.76462 0.81349 -0.06673 0.07654  0.07176  407 LYS A C   
3157 O O   . LYS A 407 ? 0.71954 0.75625 0.80799 -0.07589 0.07947  0.07703  407 LYS A O   
3158 C CB  . LYS A 407 ? 0.77679 0.82422 0.85079 -0.05516 0.08359  0.06722  407 LYS A CB  
3159 C CG  . LYS A 407 ? 0.89099 0.93061 0.94436 -0.04900 0.08289  0.06600  407 LYS A CG  
3160 C CD  . LYS A 407 ? 0.93983 0.99019 0.98949 -0.04727 0.09240  0.06189  407 LYS A CD  
3161 C CE  . LYS A 407 ? 0.94797 0.99579 0.98689 -0.03948 0.08832  0.05502  407 LYS A CE  
3162 N NZ  . LYS A 407 ? 0.99869 1.05297 1.02767 -0.03794 0.09787  0.05026  407 LYS A NZ  
3163 N N   . LYS A 408 ? 0.71991 0.77881 0.83218 -0.06415 0.07387  0.06708  408 LYS A N   
3164 C CA  . LYS A 408 ? 0.74872 0.82072 0.88015 -0.07182 0.07347  0.06784  408 LYS A CA  
3165 C C   . LYS A 408 ? 0.71568 0.77277 0.84172 -0.07917 0.06687  0.07059  408 LYS A C   
3166 O O   . LYS A 408 ? 0.71295 0.77069 0.84247 -0.09036 0.06924  0.07364  408 LYS A O   
3167 C CB  . LYS A 408 ? 0.62843 0.71668 0.77957 -0.06510 0.06926  0.06313  408 LYS A CB  
3168 C CG  . LYS A 408 ? 0.76107 0.87200 0.92951 -0.06227 0.07719  0.06089  408 LYS A CG  
3169 C CD  . LYS A 408 ? 0.92871 1.03887 1.08477 -0.06248 0.08865  0.06129  408 LYS A CD  
3170 C CE  . LYS A 408 ? 0.98518 1.12014 1.16019 -0.06302 0.09910  0.05984  408 LYS A CE  
3171 N NZ  . LYS A 408 ? 1.06001 1.19533 1.22311 -0.06971 0.11157  0.06286  408 LYS A NZ  
3172 N N   . PHE A 409 ? 0.67032 0.71311 0.78711 -0.07348 0.05930  0.06904  409 PHE A N   
3173 C CA  . PHE A 409 ? 0.70561 0.73377 0.81705 -0.07893 0.05329  0.06998  409 PHE A CA  
3174 C C   . PHE A 409 ? 0.76281 0.77158 0.85768 -0.08522 0.05732  0.07496  409 PHE A C   
3175 O O   . PHE A 409 ? 0.75494 0.75507 0.84898 -0.09520 0.05639  0.07630  409 PHE A O   
3176 C CB  . PHE A 409 ? 0.68401 0.70276 0.78930 -0.07039 0.04621  0.06691  409 PHE A CB  
3177 C CG  . PHE A 409 ? 0.74284 0.74771 0.84275 -0.07478 0.04053  0.06630  409 PHE A CG  
3178 C CD1 . PHE A 409 ? 0.73337 0.71642 0.81711 -0.07662 0.04157  0.06863  409 PHE A CD1 
3179 C CD2 . PHE A 409 ? 0.69817 0.71038 0.80750 -0.07647 0.03420  0.06339  409 PHE A CD2 
3180 C CE1 . PHE A 409 ? 0.75521 0.72324 0.83238 -0.08033 0.03743  0.06683  409 PHE A CE1 
3181 C CE2 . PHE A 409 ? 0.75571 0.75395 0.85697 -0.08096 0.02936  0.06187  409 PHE A CE2 
3182 C CZ  . PHE A 409 ? 0.74575 0.72151 0.83096 -0.08300 0.03151  0.06296  409 PHE A CZ  
3183 N N   . SER A 410 ? 0.72736 0.72767 0.80761 -0.07972 0.06142  0.07785  410 SER A N   
3184 C CA  . SER A 410 ? 0.75578 0.73462 0.81798 -0.08399 0.06474  0.08400  410 SER A CA  
3185 C C   . SER A 410 ? 0.77500 0.75785 0.83987 -0.09651 0.07309  0.08827  410 SER A C   
3186 O O   . SER A 410 ? 0.84347 0.80641 0.89613 -0.10416 0.07556  0.09334  410 SER A O   
3187 C CB  . SER A 410 ? 0.77118 0.74111 0.81610 -0.07378 0.06524  0.08672  410 SER A CB  
3188 O OG  . SER A 410 ? 0.86501 0.84710 0.90816 -0.07375 0.07225  0.08808  410 SER A OG  
3189 N N   . GLU A 411 ? 0.79046 0.79826 0.87182 -0.09905 0.07805  0.08623  411 GLU A N   
3190 C CA  . GLU A 411 ? 0.76748 0.78333 0.85484 -0.11207 0.08702  0.08992  411 GLU A CA  
3191 C C   . GLU A 411 ? 0.74264 0.75467 0.83854 -0.12574 0.08409  0.08999  411 GLU A C   
3192 O O   . GLU A 411 ? 0.72281 0.73796 0.82231 -0.13919 0.09134  0.09353  411 GLU A O   
3193 C CB  . GLU A 411 ? 0.74913 0.79605 0.85663 -0.11061 0.09296  0.08652  411 GLU A CB  
3194 C CG  . GLU A 411 ? 0.83530 0.88532 0.93104 -0.10541 0.10255  0.08826  411 GLU A CG  
3195 C CD  . GLU A 411 ? 1.01339 1.08743 1.12471 -0.09569 0.10454  0.08154  411 GLU A CD  
3196 O OE1 . GLU A 411 ? 1.02143 1.11391 1.15664 -0.09489 0.10066  0.07725  411 GLU A OE1 
3197 O OE2 . GLU A 411 ? 1.06401 1.13730 1.16250 -0.08850 0.10968  0.08047  411 GLU A OE2 
3198 N N   . TRP A 412 ? 0.79865 0.80406 0.89708 -0.12394 0.07408  0.08588  412 TRP A N   
3199 C CA  . TRP A 412 ? 0.82830 0.82975 0.93287 -0.13786 0.07059  0.08471  412 TRP A CA  
3200 C C   . TRP A 412 ? 0.87736 0.84294 0.95946 -0.14058 0.06836  0.08657  412 TRP A C   
3201 O O   . TRP A 412 ? 0.92494 0.88175 1.00775 -0.14881 0.06280  0.08314  412 TRP A O   
3202 C CB  . TRP A 412 ? 0.82998 0.85124 0.95357 -0.13608 0.06115  0.07843  412 TRP A CB  
3203 C CG  . TRP A 412 ? 0.80720 0.86319 0.95533 -0.13513 0.06413  0.07733  412 TRP A CG  
3204 C CD1 . TRP A 412 ? 0.77601 0.84688 0.93090 -0.12160 0.06557  0.07574  412 TRP A CD1 
3205 C CD2 . TRP A 412 ? 0.79637 0.87683 0.96640 -0.14808 0.06677  0.07745  412 TRP A CD2 
3206 N NE1 . TRP A 412 ? 0.79761 0.89954 0.97699 -0.12364 0.06930  0.07480  412 TRP A NE1 
3207 C CE2 . TRP A 412 ? 0.69498 0.80548 0.88537 -0.13963 0.06999  0.07605  412 TRP A CE2 
3208 C CE3 . TRP A 412 ? 0.79446 0.87469 0.96961 -0.16640 0.06673  0.07816  412 TRP A CE3 
3209 C CZ2 . TRP A 412 ? 0.76991 0.91285 0.98756 -0.14741 0.07325  0.07572  412 TRP A CZ2 
3210 C CZ3 . TRP A 412 ? 0.72972 0.84342 0.93228 -0.17611 0.06945  0.07777  412 TRP A CZ3 
3211 C CH2 . TRP A 412 ? 0.71429 0.86018 0.93871 -0.16591 0.07271  0.07676  412 TRP A CH2 
3212 N N   . GLY A 413 ? 0.85109 0.79540 0.91256 -0.13314 0.07227  0.09169  413 GLY A N   
3213 C CA  . GLY A 413 ? 0.81810 0.72699 0.85824 -0.13596 0.07262  0.09526  413 GLY A CA  
3214 C C   . GLY A 413 ? 0.83869 0.72902 0.86599 -0.12161 0.06617  0.09319  413 GLY A C   
3215 O O   . GLY A 413 ? 0.99489 0.85491 1.00316 -0.11974 0.06736  0.09714  413 GLY A O   
3216 N N   . ASN A 414 ? 0.87305 0.78018 0.91030 -0.11122 0.06003  0.08752  414 ASN A N   
3217 C CA  . ASN A 414 ? 0.90589 0.79917 0.93429 -0.09915 0.05445  0.08455  414 ASN A CA  
3218 C C   . ASN A 414 ? 0.81022 0.70184 0.82952 -0.08462 0.05499  0.08819  414 ASN A C   
3219 O O   . ASN A 414 ? 0.80815 0.71798 0.83239 -0.08124 0.05711  0.08959  414 ASN A O   
3220 C CB  . ASN A 414 ? 0.85389 0.76487 0.89614 -0.09628 0.04774  0.07702  414 ASN A CB  
3221 C CG  . ASN A 414 ? 0.89757 0.80592 0.94427 -0.10874 0.04438  0.07264  414 ASN A CG  
3222 O OD1 . ASN A 414 ? 0.79222 0.72344 0.85544 -0.11531 0.04190  0.07027  414 ASN A OD1 
3223 N ND2 . ASN A 414 ? 0.80998 0.69000 0.84159 -0.11202 0.04406  0.07137  414 ASN A ND2 
3224 N N   . ASN A 415 ? 0.83269 0.70318 0.83910 -0.07569 0.05270  0.08892  415 ASN A N   
3225 C CA  . ASN A 415 ? 0.84270 0.71395 0.84254 -0.06091 0.05085  0.09143  415 ASN A CA  
3226 C C   . ASN A 415 ? 0.78411 0.68050 0.79787 -0.05389 0.04652  0.08523  415 ASN A C   
3227 O O   . ASN A 415 ? 0.72203 0.62440 0.74498 -0.05481 0.04330  0.07895  415 ASN A O   
3228 C CB  . ASN A 415 ? 0.82615 0.67148 0.81300 -0.05216 0.04914  0.09279  415 ASN A CB  
3229 C CG  . ASN A 415 ? 0.87320 0.69068 0.84158 -0.05377 0.05335  0.10180  415 ASN A CG  
3230 O OD1 . ASN A 415 ? 0.89665 0.71365 0.86133 -0.06372 0.05820  0.10700  415 ASN A OD1 
3231 N ND2 . ASN A 415 ? 0.83967 0.63327 0.79629 -0.04356 0.05211  0.10397  415 ASN A ND2 
3232 N N   . ALA A 416 ? 0.73842 0.64765 0.75159 -0.04740 0.04654  0.08714  416 ALA A N   
3233 C CA  . ALA A 416 ? 0.71621 0.64658 0.74029 -0.04129 0.04312  0.08171  416 ALA A CA  
3234 C C   . ALA A 416 ? 0.74128 0.67188 0.75686 -0.03016 0.04034  0.08410  416 ALA A C   
3235 O O   . ALA A 416 ? 0.74086 0.66246 0.74288 -0.02855 0.04207  0.09082  416 ALA A O   
3236 C CB  . ALA A 416 ? 0.67408 0.62381 0.70794 -0.04687 0.04627  0.07995  416 ALA A CB  
3237 N N   . PHE A 417 ? 0.64904 0.59035 0.67222 -0.02311 0.03581  0.07902  417 PHE A N   
3238 C CA  . PHE A 417 ? 0.64281 0.58969 0.66159 -0.01323 0.03174  0.08007  417 PHE A CA  
3239 C C   . PHE A 417 ? 0.67494 0.64269 0.70418 -0.01297 0.02968  0.07356  417 PHE A C   
3240 O O   . PHE A 417 ? 0.65838 0.63287 0.69952 -0.01570 0.02948  0.06798  417 PHE A O   
3241 C CB  . PHE A 417 ? 0.69532 0.63344 0.71358 -0.00439 0.02850  0.08032  417 PHE A CB  
3242 C CG  . PHE A 417 ? 0.69474 0.60792 0.70195 -0.00437 0.03108  0.08569  417 PHE A CG  
3243 C CD1 . PHE A 417 ? 0.64923 0.55088 0.65875 -0.01124 0.03392  0.08265  417 PHE A CD1 
3244 C CD2 . PHE A 417 ? 0.76778 0.66733 0.76063 0.00213  0.03036  0.09386  417 PHE A CD2 
3245 C CE1 . PHE A 417 ? 0.71143 0.58721 0.70947 -0.01288 0.03669  0.08655  417 PHE A CE1 
3246 C CE2 . PHE A 417 ? 0.76896 0.64124 0.75020 0.00187  0.03334  0.09901  417 PHE A CE2 
3247 C CZ  . PHE A 417 ? 0.75984 0.61959 0.74386 -0.00621 0.03685  0.09476  417 PHE A CZ  
3248 N N   . PHE A 418 ? 0.64195 0.61804 0.66485 -0.01024 0.02820  0.07435  418 PHE A N   
3249 C CA  . PHE A 418 ? 0.66512 0.65789 0.69514 -0.01090 0.02674  0.06759  418 PHE A CA  
3250 C C   . PHE A 418 ? 0.69355 0.69511 0.72130 -0.00384 0.02013  0.06637  418 PHE A C   
3251 O O   . PHE A 418 ? 0.66730 0.66531 0.68245 0.00117  0.01727  0.07202  418 PHE A O   
3252 C CB  . PHE A 418 ? 0.59980 0.59682 0.62459 -0.01584 0.03166  0.06716  418 PHE A CB  
3253 C CG  . PHE A 418 ? 0.67254 0.68209 0.70684 -0.01765 0.03211  0.05899  418 PHE A CG  
3254 C CD1 . PHE A 418 ? 0.66067 0.67887 0.69174 -0.01483 0.02799  0.05428  418 PHE A CD1 
3255 C CD2 . PHE A 418 ? 0.65222 0.66428 0.69885 -0.02209 0.03598  0.05589  418 PHE A CD2 
3256 C CE1 . PHE A 418 ? 0.63447 0.66024 0.67309 -0.01700 0.02887  0.04625  418 PHE A CE1 
3257 C CE2 . PHE A 418 ? 0.58780 0.60803 0.64246 -0.02248 0.03653  0.04893  418 PHE A CE2 
3258 C CZ  . PHE A 418 ? 0.66590 0.69125 0.71590 -0.02022 0.03356  0.04396  418 PHE A CZ  
3259 N N   . TYR A 419 ? 0.65647 0.66993 0.69626 -0.00394 0.01743  0.05939  419 TYR A N   
3260 C CA  . TYR A 419 ? 0.66726 0.69331 0.70878 0.00077  0.01079  0.05681  419 TYR A CA  
3261 C C   . TYR A 419 ? 0.64431 0.68169 0.68852 -0.00407 0.01007  0.04904  419 TYR A C   
3262 O O   . TYR A 419 ? 0.69559 0.73102 0.74455 -0.00952 0.01484  0.04503  419 TYR A O   
3263 C CB  . TYR A 419 ? 0.62315 0.65366 0.67754 0.00468  0.00845  0.05519  419 TYR A CB  
3264 C CG  . TYR A 419 ? 0.64078 0.67569 0.70834 -0.00105 0.01115  0.04864  419 TYR A CG  
3265 C CD1 . TYR A 419 ? 0.52815 0.57570 0.60260 -0.00480 0.00907  0.04197  419 TYR A CD1 
3266 C CD2 . TYR A 419 ? 0.64620 0.67105 0.71761 -0.00323 0.01551  0.04933  419 TYR A CD2 
3267 C CE1 . TYR A 419 ? 0.63040 0.67879 0.71476 -0.01003 0.01188  0.03733  419 TYR A CE1 
3268 C CE2 . TYR A 419 ? 0.58323 0.61087 0.66407 -0.00801 0.01750  0.04464  419 TYR A CE2 
3269 C CZ  . TYR A 419 ? 0.62532 0.66392 0.71246 -0.01112 0.01599  0.03924  419 TYR A CZ  
3270 O OH  . TYR A 419 ? 0.62668 0.66502 0.72119 -0.01601 0.01836  0.03580  419 TYR A OH  
3271 N N   . TYR A 420 ? 0.65474 0.70387 0.69636 -0.00169 0.00349  0.04673  420 TYR A N   
3272 C CA  . TYR A 420 ? 0.63204 0.69108 0.67438 -0.00673 0.00156  0.03823  420 TYR A CA  
3273 C C   . TYR A 420 ? 0.68324 0.75789 0.73680 -0.00555 -0.00567 0.03450  420 TYR A C   
3274 O O   . TYR A 420 ? 0.60414 0.68818 0.65350 -0.00025 -0.01304 0.03735  420 TYR A O   
3275 C CB  . TYR A 420 ? 0.64825 0.70716 0.67182 -0.00694 0.00037  0.03855  420 TYR A CB  
3276 C CG  . TYR A 420 ? 0.68656 0.75104 0.70673 -0.01286 0.00006  0.02860  420 TYR A CG  
3277 C CD1 . TYR A 420 ? 0.66829 0.72743 0.69596 -0.01807 0.00673  0.02217  420 TYR A CD1 
3278 C CD2 . TYR A 420 ? 0.59520 0.66894 0.60317 -0.01297 -0.00721 0.02557  420 TYR A CD2 
3279 C CE1 . TYR A 420 ? 0.63574 0.69601 0.65872 -0.02303 0.00733  0.01240  420 TYR A CE1 
3280 C CE2 . TYR A 420 ? 0.70372 0.77987 0.70609 -0.01928 -0.00713 0.01512  420 TYR A CE2 
3281 C CZ  . TYR A 420 ? 0.70263 0.77069 0.71256 -0.02421 0.00075  0.00828  420 TYR A CZ  
3282 O OH  . TYR A 420 ? 0.77724 0.84398 0.78066 -0.02995 0.00164  -0.00269 420 TYR A OH  
3283 N N   . PHE A 421 ? 0.68381 0.76206 0.75190 -0.01047 -0.00367 0.02873  421 PHE A N   
3284 C CA  . PHE A 421 ? 0.63511 0.72975 0.71718 -0.01099 -0.00871 0.02509  421 PHE A CA  
3285 C C   . PHE A 421 ? 0.59662 0.70234 0.67705 -0.01768 -0.01372 0.01677  421 PHE A C   
3286 O O   . PHE A 421 ? 0.61259 0.71077 0.69102 -0.02502 -0.00971 0.01050  421 PHE A O   
3287 C CB  . PHE A 421 ? 0.59413 0.68572 0.69028 -0.01444 -0.00307 0.02339  421 PHE A CB  
3288 C CG  . PHE A 421 ? 0.64108 0.75021 0.75336 -0.01533 -0.00589 0.02037  421 PHE A CG  
3289 C CD1 . PHE A 421 ? 0.62295 0.74116 0.74261 -0.00671 -0.00797 0.02488  421 PHE A CD1 
3290 C CD2 . PHE A 421 ? 0.63045 0.74667 0.75118 -0.02494 -0.00562 0.01288  421 PHE A CD2 
3291 C CE1 . PHE A 421 ? 0.67240 0.81039 0.80973 -0.00724 -0.00946 0.02178  421 PHE A CE1 
3292 C CE2 . PHE A 421 ? 0.63714 0.77171 0.77442 -0.02738 -0.00716 0.01005  421 PHE A CE2 
3293 C CZ  . PHE A 421 ? 0.68241 0.82978 0.82905 -0.01830 -0.00891 0.01444  421 PHE A CZ  
3294 N N   . GLU A 422 ? 0.64953 0.77290 0.73091 -0.01507 -0.02287 0.01638  422 GLU A N   
3295 C CA  . GLU A 422 ? 0.63759 0.77196 0.71556 -0.02264 -0.02892 0.00769  422 GLU A CA  
3296 C C   . GLU A 422 ? 0.67196 0.83151 0.76723 -0.02443 -0.03693 0.00427  422 GLU A C   
3297 O O   . GLU A 422 ? 0.70903 0.88393 0.80072 -0.02741 -0.04626 -0.00025 422 GLU A O   
3298 C CB  . GLU A 422 ? 0.64312 0.77503 0.69864 -0.01998 -0.03360 0.00911  422 GLU A CB  
3299 C CG  . GLU A 422 ? 0.74769 0.88530 0.79660 -0.00886 -0.04008 0.01913  422 GLU A CG  
3300 C CD  . GLU A 422 ? 0.84436 0.97145 0.86653 -0.00663 -0.04069 0.02281  422 GLU A CD  
3301 O OE1 . GLU A 422 ? 0.81412 0.92936 0.82478 -0.01307 -0.03417 0.01737  422 GLU A OE1 
3302 O OE2 . GLU A 422 ? 0.88828 1.01856 0.90056 0.00202  -0.04718 0.03143  422 GLU A OE2 
3303 N N   . HIS A 423 ? 0.69271 0.85861 0.80707 -0.02332 -0.03347 0.00583  423 HIS A N   
3304 C CA  . HIS A 423 ? 0.64523 0.83739 0.77953 -0.02671 -0.03906 0.00163  423 HIS A CA  
3305 C C   . HIS A 423 ? 0.65394 0.84378 0.79873 -0.04033 -0.03293 -0.00639 423 HIS A C   
3306 O O   . HIS A 423 ? 0.59146 0.76611 0.73924 -0.04141 -0.02334 -0.00447 423 HIS A O   
3307 C CB  . HIS A 423 ? 0.62586 0.83053 0.77580 -0.01567 -0.03897 0.00841  423 HIS A CB  
3308 C CG  . HIS A 423 ? 0.63085 0.86598 0.80473 -0.01939 -0.04331 0.00377  423 HIS A CG  
3309 N ND1 . HIS A 423 ? 0.67741 0.93799 0.85605 -0.02138 -0.05550 0.00006  423 HIS A ND1 
3310 C CD2 . HIS A 423 ? 0.63654 0.88222 0.83110 -0.02285 -0.03685 0.00175  423 HIS A CD2 
3311 C CE1 . HIS A 423 ? 0.59797 0.88546 0.80188 -0.02590 -0.05657 -0.00404 423 HIS A CE1 
3312 N NE2 . HIS A 423 ? 0.66168 0.94028 0.87537 -0.02693 -0.04456 -0.00303 423 HIS A NE2 
3313 N N   . ARG A 424 ? 0.68924 0.89327 0.83836 -0.05118 -0.03887 -0.01516 424 ARG A N   
3314 C CA  . ARG A 424 ? 0.63805 0.84111 0.79819 -0.06541 -0.03372 -0.02270 424 ARG A CA  
3315 C C   . ARG A 424 ? 0.65271 0.88142 0.83857 -0.06658 -0.03351 -0.02200 424 ARG A C   
3316 O O   . ARG A 424 ? 0.60434 0.86218 0.80239 -0.06574 -0.04292 -0.02369 424 ARG A O   
3317 C CB  . ARG A 424 ? 0.68203 0.88728 0.83476 -0.07814 -0.03978 -0.03345 424 ARG A CB  
3318 C CG  . ARG A 424 ? 0.67887 0.88827 0.84588 -0.09457 -0.03653 -0.04163 424 ARG A CG  
3319 C CD  . ARG A 424 ? 0.71212 0.91460 0.86714 -0.10787 -0.04087 -0.05324 424 ARG A CD  
3320 N NE  . ARG A 424 ? 0.86146 1.04845 1.02079 -0.12282 -0.03315 -0.05975 424 ARG A NE  
3321 C CZ  . ARG A 424 ? 0.87399 1.07833 1.05273 -0.13579 -0.03338 -0.06408 424 ARG A CZ  
3322 N NH1 . ARG A 424 ? 0.92026 1.16141 1.11887 -0.13508 -0.04099 -0.06315 424 ARG A NH1 
3323 N NH2 . ARG A 424 ? 0.84228 1.02680 1.02111 -0.14966 -0.02548 -0.06909 424 ARG A NH2 
3324 N N   . SER A 425 ? 0.65345 0.87256 0.84733 -0.06822 -0.02280 -0.01945 425 SER A N   
3325 C CA  . SER A 425 ? 0.66409 0.90580 0.88165 -0.07026 -0.01948 -0.01922 425 SER A CA  
3326 C C   . SER A 425 ? 0.71400 0.98365 0.94785 -0.08317 -0.02618 -0.02759 425 SER A C   
3327 O O   . SER A 425 ? 0.77970 1.04065 1.00616 -0.09675 -0.02798 -0.03515 425 SER A O   
3328 C CB  . SER A 425 ? 0.68446 0.90665 0.90235 -0.07591 -0.00649 -0.01760 425 SER A CB  
3329 O OG  . SER A 425 ? 0.78382 1.02692 1.02303 -0.07927 -0.00117 -0.01776 425 SER A OG  
3330 N N   . SER A 426 ? 0.69097 0.99490 0.94759 -0.07867 -0.03009 -0.02663 426 SER A N   
3331 C CA  . SER A 426 ? 0.70641 1.04262 0.98349 -0.09179 -0.03638 -0.03450 426 SER A CA  
3332 C C   . SER A 426 ? 0.70896 1.04326 0.99817 -0.10914 -0.02538 -0.03903 426 SER A C   
3333 O O   . SER A 426 ? 0.63704 0.98813 0.93774 -0.12563 -0.02914 -0.04722 426 SER A O   
3334 C CB  . SER A 426 ? 0.62458 1.00142 0.92548 -0.08015 -0.04385 -0.03151 426 SER A CB  
3335 O OG  . SER A 426 ? 0.69360 1.08259 1.01520 -0.07718 -0.03274 -0.02858 426 SER A OG  
3336 N N   . LYS A 427 ? 0.73588 1.04982 1.02174 -0.10672 -0.01211 -0.03383 427 LYS A N   
3337 C CA  . LYS A 427 ? 0.78863 1.09535 1.08103 -0.12300 -0.00077 -0.03649 427 LYS A CA  
3338 C C   . LYS A 427 ? 0.81802 1.08298 1.08624 -0.13196 0.00389  -0.03786 427 LYS A C   
3339 O O   . LYS A 427 ? 0.83791 1.08920 1.10653 -0.14468 0.01365  -0.03850 427 LYS A O   
3340 C CB  . LYS A 427 ? 0.79344 1.10401 1.09573 -0.11574 0.01133  -0.03006 427 LYS A CB  
3341 C CG  . LYS A 427 ? 0.86341 1.21285 1.18952 -0.10298 0.00817  -0.02825 427 LYS A CG  
3342 C CD  . LYS A 427 ? 0.92617 1.28332 1.26494 -0.09904 0.02216  -0.02454 427 LYS A CD  
3343 C CE  . LYS A 427 ? 0.93674 1.26708 1.26444 -0.11304 0.03578  -0.02386 427 LYS A CE  
3344 N NZ  . LYS A 427 ? 1.01181 1.35555 1.35296 -0.11096 0.04944  -0.02144 427 LYS A NZ  
3345 N N   . LEU A 428 ? 0.82061 1.06511 1.06786 -0.12512 -0.00235 -0.03793 428 LEU A N   
3346 C CA  . LEU A 428 ? 0.81012 1.01517 1.03528 -0.12925 0.00268  -0.03829 428 LEU A CA  
3347 C C   . LEU A 428 ? 0.75954 0.95669 0.98525 -0.14938 0.00402  -0.04695 428 LEU A C   
3348 O O   . LEU A 428 ? 0.83443 1.04614 1.06316 -0.15756 -0.00493 -0.05539 428 LEU A O   
3349 C CB  . LEU A 428 ? 0.73216 0.92236 0.93739 -0.11875 -0.00404 -0.03803 428 LEU A CB  
3350 C CG  . LEU A 428 ? 0.76934 0.92114 0.95401 -0.11993 0.00169  -0.03799 428 LEU A CG  
3351 C CD1 . LEU A 428 ? 0.71661 0.85390 0.89257 -0.10531 0.00604  -0.02867 428 LEU A CD1 
3352 C CD2 . LEU A 428 ? 0.82876 0.97039 0.99783 -0.12248 -0.00475 -0.04566 428 LEU A CD2 
3353 N N   . PRO A 429 ? 0.73247 0.90550 0.95384 -0.15821 0.01456  -0.04518 429 PRO A N   
3354 C CA  . PRO A 429 ? 0.73993 0.90469 0.96323 -0.17893 0.01695  -0.05297 429 PRO A CA  
3355 C C   . PRO A 429 ? 0.74721 0.88102 0.94990 -0.18355 0.01417  -0.05983 429 PRO A C   
3356 O O   . PRO A 429 ? 0.74856 0.87934 0.95254 -0.20083 0.01286  -0.06903 429 PRO A O   
3357 C CB  . PRO A 429 ? 0.64785 0.79676 0.87232 -0.18469 0.03008  -0.04628 429 PRO A CB  
3358 C CG  . PRO A 429 ? 0.66593 0.80323 0.88084 -0.16660 0.03362  -0.03629 429 PRO A CG  
3359 C CD  . PRO A 429 ? 0.73883 0.89579 0.95576 -0.15063 0.02462  -0.03553 429 PRO A CD  
3360 N N   . TRP A 430 ? 0.69254 0.80394 0.87697 -0.16925 0.01374  -0.05631 430 TRP A N   
3361 C CA  . TRP A 430 ? 0.77808 0.86249 0.94333 -0.17092 0.01173  -0.06339 430 TRP A CA  
3362 C C   . TRP A 430 ? 0.74372 0.84834 0.90833 -0.17515 0.00031  -0.07372 430 TRP A C   
3363 O O   . TRP A 430 ? 0.67212 0.81091 0.84917 -0.17094 -0.00735 -0.07262 430 TRP A O   
3364 C CB  . TRP A 430 ? 0.73146 0.79473 0.88116 -0.15332 0.01413  -0.05660 430 TRP A CB  
3365 C CG  . TRP A 430 ? 0.72014 0.76331 0.86785 -0.14804 0.02335  -0.04647 430 TRP A CG  
3366 C CD1 . TRP A 430 ? 0.65006 0.70403 0.80422 -0.13821 0.02580  -0.03656 430 TRP A CD1 
3367 C CD2 . TRP A 430 ? 0.76314 0.77087 0.90001 -0.15173 0.03069  -0.04520 430 TRP A CD2 
3368 N NE1 . TRP A 430 ? 0.66929 0.69853 0.81668 -0.13642 0.03351  -0.02938 430 TRP A NE1 
3369 C CE2 . TRP A 430 ? 0.70321 0.70419 0.84044 -0.14391 0.03637  -0.03373 430 TRP A CE2 
3370 C CE3 . TRP A 430 ? 0.75364 0.73319 0.87948 -0.16034 0.03288  -0.05269 430 TRP A CE3 
3371 C CZ2 . TRP A 430 ? 0.63642 0.60558 0.76378 -0.14401 0.04305  -0.02843 430 TRP A CZ2 
3372 C CZ3 . TRP A 430 ? 0.75827 0.70428 0.87508 -0.15952 0.04041  -0.04736 430 TRP A CZ3 
3373 C CH2 . TRP A 430 ? 0.74553 0.68760 0.86334 -0.15111 0.04489  -0.03476 430 TRP A CH2 
3374 N N   . PRO A 431 ? 0.74093 0.82426 0.88975 -0.18248 -0.00130 -0.08381 431 PRO A N   
3375 C CA  . PRO A 431 ? 0.79485 0.89691 0.94060 -0.18890 -0.01268 -0.09475 431 PRO A CA  
3376 C C   . PRO A 431 ? 0.74602 0.86021 0.88217 -0.17169 -0.01973 -0.09120 431 PRO A C   
3377 O O   . PRO A 431 ? 0.78115 0.88300 0.90992 -0.15612 -0.01495 -0.08231 431 PRO A O   
3378 C CB  . PRO A 431 ? 0.71512 0.78316 0.84248 -0.20036 -0.00993 -0.10654 431 PRO A CB  
3379 C CG  . PRO A 431 ? 0.79050 0.82251 0.90544 -0.18824 0.00082  -0.09926 431 PRO A CG  
3380 C CD  . PRO A 431 ? 0.79793 0.83824 0.92907 -0.18337 0.00680  -0.08588 431 PRO A CD  
3381 N N   . GLU A 432 ? 0.78328 0.92100 0.91812 -0.17592 -0.03159 -0.09865 432 GLU A N   
3382 C CA  . GLU A 432 ? 0.81543 0.96911 0.94162 -0.16114 -0.03986 -0.09453 432 GLU A CA  
3383 C C   . GLU A 432 ? 0.76423 0.88878 0.86342 -0.15186 -0.03601 -0.09582 432 GLU A C   
3384 O O   . GLU A 432 ? 0.74340 0.87163 0.83549 -0.13649 -0.03699 -0.08749 432 GLU A O   
3385 C CB  . GLU A 432 ? 0.85201 1.03898 0.98293 -0.16922 -0.05472 -0.10220 432 GLU A CB  
3386 C CG  . GLU A 432 ? 0.93932 1.15924 1.10049 -0.18114 -0.05848 -0.10320 432 GLU A CG  
3387 C CD  . GLU A 432 ? 1.07621 1.28618 1.24273 -0.20494 -0.05515 -0.11506 432 GLU A CD  
3388 O OE1 . GLU A 432 ? 1.07763 1.26337 1.22372 -0.21485 -0.05578 -0.12651 432 GLU A OE1 
3389 O OE2 . GLU A 432 ? 1.03293 1.25936 1.22395 -0.21419 -0.05142 -0.11313 432 GLU A OE2 
3390 N N   . TRP A 433 ? 0.81721 0.91219 0.90128 -0.16055 -0.03077 -0.10600 433 TRP A N   
3391 C CA  . TRP A 433 ? 0.78043 0.85080 0.84059 -0.15057 -0.02604 -0.10767 433 TRP A CA  
3392 C C   . TRP A 433 ? 0.75467 0.80975 0.81695 -0.13571 -0.01587 -0.09538 433 TRP A C   
3393 O O   . TRP A 433 ? 0.83965 0.88421 0.88703 -0.12445 -0.01261 -0.09331 433 TRP A O   
3394 C CB  . TRP A 433 ? 0.78160 0.82136 0.82474 -0.16147 -0.02151 -0.12213 433 TRP A CB  
3395 C CG  . TRP A 433 ? 0.86249 0.87277 0.91159 -0.16614 -0.01029 -0.12160 433 TRP A CG  
3396 C CD1 . TRP A 433 ? 0.78292 0.78791 0.84249 -0.18301 -0.00934 -0.12678 433 TRP A CD1 
3397 C CD2 . TRP A 433 ? 0.76512 0.74755 0.80998 -0.15395 0.00117  -0.11474 433 TRP A CD2 
3398 N NE1 . TRP A 433 ? 0.87678 0.84950 0.93633 -0.18148 0.00211  -0.12289 433 TRP A NE1 
3399 C CE2 . TRP A 433 ? 0.82920 0.78887 0.88057 -0.16321 0.00800  -0.11550 433 TRP A CE2 
3400 C CE3 . TRP A 433 ? 0.76390 0.73957 0.80078 -0.13668 0.00609  -0.10779 433 TRP A CE3 
3401 C CZ2 . TRP A 433 ? 0.89651 0.82699 0.94588 -0.15413 0.01839  -0.10902 433 TRP A CZ2 
3402 C CZ3 . TRP A 433 ? 0.82487 0.77448 0.86251 -0.12840 0.01649  -0.10215 433 TRP A CZ3 
3403 C CH2 . TRP A 433 ? 0.83810 0.76560 0.88161 -0.13638 0.02191  -0.10256 433 TRP A CH2 
3404 N N   . MET A 434 ? 0.78495 0.83957 0.86490 -0.13599 -0.01073 -0.08731 434 MET A N   
3405 C CA  . MET A 434 ? 0.77185 0.81425 0.85328 -0.12234 -0.00274 -0.07572 434 MET A CA  
3406 C C   . MET A 434 ? 0.69074 0.75416 0.77580 -0.10927 -0.00666 -0.06531 434 MET A C   
3407 O O   . MET A 434 ? 0.67317 0.72666 0.75648 -0.09816 -0.00092 -0.05682 434 MET A O   
3408 C CB  . MET A 434 ? 0.73509 0.76802 0.83040 -0.12676 0.00405  -0.07018 434 MET A CB  
3409 C CG  . MET A 434 ? 0.83166 0.83014 0.91816 -0.13142 0.01199  -0.07498 434 MET A CG  
3410 S SD  . MET A 434 ? 0.87281 0.86044 0.97172 -0.14477 0.01759  -0.07274 434 MET A SD  
3411 C CE  . MET A 434 ? 0.80957 0.76935 0.90379 -0.13138 0.02674  -0.06172 434 MET A CE  
3412 N N   . GLY A 435 ? 0.67556 0.76727 0.76636 -0.11040 -0.01643 -0.06548 435 GLY A N   
3413 C CA  . GLY A 435 ? 0.61855 0.72603 0.70811 -0.09718 -0.02076 -0.05625 435 GLY A CA  
3414 C C   . GLY A 435 ? 0.70743 0.81819 0.81085 -0.08853 -0.01613 -0.04441 435 GLY A C   
3415 O O   . GLY A 435 ? 0.70011 0.81669 0.81988 -0.09362 -0.01361 -0.04293 435 GLY A O   
3416 N N   . VAL A 436 ? 0.65531 0.76182 0.75091 -0.07605 -0.01452 -0.03619 436 VAL A N   
3417 C CA  . VAL A 436 ? 0.66528 0.77523 0.77102 -0.06704 -0.01143 -0.02532 436 VAL A CA  
3418 C C   . VAL A 436 ? 0.64998 0.73668 0.75471 -0.06654 -0.00162 -0.02271 436 VAL A C   
3419 O O   . VAL A 436 ? 0.69335 0.76692 0.78871 -0.05965 0.00235  -0.01877 436 VAL A O   
3420 C CB  . VAL A 436 ? 0.68270 0.79886 0.78013 -0.05522 -0.01527 -0.01776 436 VAL A CB  
3421 C CG1 . VAL A 436 ? 0.62522 0.74371 0.73254 -0.04675 -0.01244 -0.00801 436 VAL A CG1 
3422 C CG2 . VAL A 436 ? 0.62912 0.76651 0.72387 -0.05533 -0.02639 -0.02048 436 VAL A CG2 
3423 N N   . MET A 437 ? 0.64158 0.72396 0.75640 -0.07432 0.00222  -0.02457 437 MET A N   
3424 C CA  . MET A 437 ? 0.67797 0.73661 0.78959 -0.07524 0.01006  -0.02340 437 MET A CA  
3425 C C   . MET A 437 ? 0.66522 0.71783 0.77876 -0.06659 0.01436  -0.01355 437 MET A C   
3426 O O   . MET A 437 ? 0.63512 0.70008 0.75471 -0.06170 0.01295  -0.00786 437 MET A O   
3427 C CB  . MET A 437 ? 0.70203 0.75479 0.82092 -0.08705 0.01299  -0.02760 437 MET A CB  
3428 C CG  . MET A 437 ? 0.70027 0.74994 0.81451 -0.09777 0.01035  -0.03878 437 MET A CG  
3429 S SD  . MET A 437 ? 0.74827 0.79849 0.87539 -0.11310 0.01334  -0.04148 437 MET A SD  
3430 C CE  . MET A 437 ? 0.70784 0.72169 0.82665 -0.11285 0.02268  -0.03820 437 MET A CE  
3431 N N   . HIS A 438 ? 0.65410 0.68685 0.76226 -0.06467 0.01952  -0.01212 438 HIS A N   
3432 C CA  . HIS A 438 ? 0.67402 0.69894 0.78389 -0.05894 0.02323  -0.00377 438 HIS A CA  
3433 C C   . HIS A 438 ? 0.60173 0.63171 0.72013 -0.06266 0.02465  -0.00002 438 HIS A C   
3434 O O   . HIS A 438 ? 0.62595 0.65134 0.74766 -0.07108 0.02684  -0.00266 438 HIS A O   
3435 C CB  . HIS A 438 ? 0.54803 0.55220 0.65329 -0.05785 0.02760  -0.00393 438 HIS A CB  
3436 C CG  . HIS A 438 ? 0.66697 0.66450 0.77349 -0.05200 0.02981  0.00443  438 HIS A CG  
3437 N ND1 . HIS A 438 ? 0.58504 0.58633 0.69004 -0.04444 0.02941  0.00872  438 HIS A ND1 
3438 C CD2 . HIS A 438 ? 0.70139 0.68867 0.80950 -0.05341 0.03205  0.00928  438 HIS A CD2 
3439 C CE1 . HIS A 438 ? 0.59026 0.58535 0.69707 -0.04178 0.03056  0.01511  438 HIS A CE1 
3440 N NE2 . HIS A 438 ? 0.65815 0.64444 0.76588 -0.04653 0.03189  0.01582  438 HIS A NE2 
3441 N N   . GLY A 439 ? 0.65729 0.69529 0.77813 -0.05678 0.02426  0.00591  439 GLY A N   
3442 C CA  . GLY A 439 ? 0.68274 0.72453 0.80954 -0.05863 0.02706  0.00956  439 GLY A CA  
3443 C C   . GLY A 439 ? 0.67273 0.73572 0.80949 -0.05964 0.02528  0.00774  439 GLY A C   
3444 O O   . GLY A 439 ? 0.66278 0.73064 0.80457 -0.05949 0.02873  0.01057  439 GLY A O   
3445 N N   . TYR A 440 ? 0.69763 0.77442 0.83744 -0.06035 0.01999  0.00294  440 TYR A N   
3446 C CA  . TYR A 440 ? 0.64921 0.74955 0.80182 -0.06188 0.01739  0.00072  440 TYR A CA  
3447 C C   . TYR A 440 ? 0.62276 0.73559 0.77649 -0.05051 0.01313  0.00446  440 TYR A C   
3448 O O   . TYR A 440 ? 0.58581 0.72046 0.74988 -0.04909 0.00852  0.00262  440 TYR A O   
3449 C CB  . TYR A 440 ? 0.63190 0.74167 0.78859 -0.07157 0.01316  -0.00731 440 TYR A CB  
3450 C CG  . TYR A 440 ? 0.62216 0.72173 0.78171 -0.08379 0.01890  -0.01017 440 TYR A CG  
3451 C CD1 . TYR A 440 ? 0.61153 0.72402 0.78438 -0.09022 0.02302  -0.00999 440 TYR A CD1 
3452 C CD2 . TYR A 440 ? 0.69409 0.76913 0.84240 -0.08801 0.02146  -0.01205 440 TYR A CD2 
3453 C CE1 . TYR A 440 ? 0.57100 0.67192 0.74457 -0.10209 0.02923  -0.01127 440 TYR A CE1 
3454 C CE2 . TYR A 440 ? 0.64533 0.70706 0.79444 -0.09869 0.02703  -0.01330 440 TYR A CE2 
3455 C CZ  . TYR A 440 ? 0.63451 0.70892 0.79557 -0.10634 0.03088  -0.01254 440 TYR A CZ  
3456 O OH  . TYR A 440 ? 0.67090 0.73088 0.83123 -0.11789 0.03716  -0.01273 440 TYR A OH  
3457 N N   . GLU A 441 ? 0.59266 0.69183 0.73635 -0.04252 0.01441  0.00993  441 GLU A N   
3458 C CA  . GLU A 441 ? 0.65687 0.76095 0.80066 -0.03206 0.01312  0.01488  441 GLU A CA  
3459 C C   . GLU A 441 ? 0.68869 0.79035 0.83711 -0.03016 0.01939  0.01757  441 GLU A C   
3460 O O   . GLU A 441 ? 0.67905 0.78666 0.83049 -0.02163 0.01934  0.02022  441 GLU A O   
3461 C CB  . GLU A 441 ? 0.61449 0.70374 0.74418 -0.02625 0.01195  0.01910  441 GLU A CB  
3462 C CG  . GLU A 441 ? 0.65734 0.72886 0.78102 -0.02535 0.01734  0.02316  441 GLU A CG  
3463 C CD  . GLU A 441 ? 0.68902 0.74863 0.81020 -0.03261 0.02056  0.02139  441 GLU A CD  
3464 O OE1 . GLU A 441 ? 0.65601 0.71758 0.77854 -0.03819 0.01946  0.01667  441 GLU A OE1 
3465 O OE2 . GLU A 441 ? 0.65140 0.69890 0.76867 -0.03241 0.02378  0.02472  441 GLU A OE2 
3466 N N   . ILE A 442 ? 0.64095 0.73247 0.78830 -0.03745 0.02496  0.01700  442 ILE A N   
3467 C CA  . ILE A 442 ? 0.62188 0.70769 0.76854 -0.03615 0.03129  0.01965  442 ILE A CA  
3468 C C   . ILE A 442 ? 0.62142 0.72701 0.78165 -0.03396 0.03395  0.01786  442 ILE A C   
3469 O O   . ILE A 442 ? 0.63570 0.74029 0.79523 -0.02687 0.03752  0.01976  442 ILE A O   
3470 C CB  . ILE A 442 ? 0.65003 0.72157 0.79125 -0.04478 0.03590  0.02013  442 ILE A CB  
3471 C CG1 . ILE A 442 ? 0.59513 0.64884 0.72506 -0.04412 0.03346  0.02251  442 ILE A CG1 
3472 C CG2 . ILE A 442 ? 0.54753 0.61515 0.68642 -0.04507 0.04274  0.02225  442 ILE A CG2 
3473 C CD1 . ILE A 442 ? 0.58620 0.62606 0.71161 -0.05137 0.03628  0.02330  442 ILE A CD1 
3474 N N   . GLU A 443 ? 0.57694 0.70120 0.75032 -0.04021 0.03261  0.01360  443 GLU A N   
3475 C CA  . GLU A 443 ? 0.58861 0.73778 0.77935 -0.03791 0.03462  0.01151  443 GLU A CA  
3476 C C   . GLU A 443 ? 0.60025 0.75666 0.79326 -0.02324 0.03126  0.01405  443 GLU A C   
3477 O O   . GLU A 443 ? 0.64319 0.80921 0.84469 -0.01666 0.03634  0.01422  443 GLU A O   
3478 C CB  . GLU A 443 ? 0.61094 0.78247 0.81630 -0.04606 0.02995  0.00634  443 GLU A CB  
3479 C CG  . GLU A 443 ? 0.76887 0.93737 0.97644 -0.06146 0.03417  0.00295  443 GLU A CG  
3480 C CD  . GLU A 443 ? 0.78736 0.96637 1.00005 -0.06962 0.02646  -0.00259 443 GLU A CD  
3481 O OE1 . GLU A 443 ? 0.80093 1.00815 1.03163 -0.07296 0.02330  -0.00662 443 GLU A OE1 
3482 O OE2 . GLU A 443 ? 0.78121 0.94075 0.97975 -0.07234 0.02336  -0.00331 443 GLU A OE2 
3483 N N   . PHE A 444 ? 0.58472 0.73682 0.77013 -0.01778 0.02307  0.01597  444 PHE A N   
3484 C CA  . PHE A 444 ? 0.62348 0.78111 0.80987 -0.00387 0.01878  0.01938  444 PHE A CA  
3485 C C   . PHE A 444 ? 0.62610 0.76093 0.79958 0.00350  0.02380  0.02352  444 PHE A C   
3486 O O   . PHE A 444 ? 0.60923 0.74698 0.78657 0.01463  0.02548  0.02524  444 PHE A O   
3487 C CB  . PHE A 444 ? 0.61199 0.77189 0.79196 -0.00187 0.00867  0.02055  444 PHE A CB  
3488 C CG  . PHE A 444 ? 0.68015 0.86566 0.87348 -0.00784 0.00228  0.01567  444 PHE A CG  
3489 C CD1 . PHE A 444 ? 0.60810 0.79257 0.80123 -0.02204 0.00283  0.01031  444 PHE A CD1 
3490 C CD2 . PHE A 444 ? 0.63829 0.84948 0.84553 0.00057  -0.00431 0.01614  444 PHE A CD2 
3491 C CE1 . PHE A 444 ? 0.58979 0.79749 0.79520 -0.02960 -0.00314 0.00464  444 PHE A CE1 
3492 C CE2 . PHE A 444 ? 0.63742 0.87553 0.85867 -0.00654 -0.01122 0.01087  444 PHE A CE2 
3493 C CZ  . PHE A 444 ? 0.60543 0.84116 0.82520 -0.02248 -0.01049 0.00473  444 PHE A CZ  
3494 N N   . VAL A 445 ? 0.59746 0.70984 0.75639 -0.00266 0.02640  0.02469  445 VAL A N   
3495 C CA  . VAL A 445 ? 0.59053 0.68158 0.73691 0.00195  0.03056  0.02776  445 VAL A CA  
3496 C C   . VAL A 445 ? 0.66420 0.75702 0.81508 0.00373  0.03888  0.02569  445 VAL A C   
3497 O O   . VAL A 445 ? 0.62401 0.70655 0.76936 0.01215  0.04194  0.02684  445 VAL A O   
3498 C CB  . VAL A 445 ? 0.62055 0.69210 0.75345 -0.00580 0.03068  0.02914  445 VAL A CB  
3499 C CG1 . VAL A 445 ? 0.50148 0.55310 0.62253 -0.00445 0.03511  0.03102  445 VAL A CG1 
3500 C CG2 . VAL A 445 ? 0.60721 0.67575 0.73407 -0.00509 0.02424  0.03130  445 VAL A CG2 
3501 N N   . PHE A 446 ? 0.57885 0.68380 0.73891 -0.00432 0.04341  0.02233  446 PHE A N   
3502 C CA  . PHE A 446 ? 0.58207 0.68892 0.74456 -0.00430 0.05295  0.02019  446 PHE A CA  
3503 C C   . PHE A 446 ? 0.63238 0.76436 0.81401 0.00371  0.05573  0.01765  446 PHE A C   
3504 O O   . PHE A 446 ? 0.60236 0.73785 0.78704 0.00567  0.06510  0.01531  446 PHE A O   
3505 C CB  . PHE A 446 ? 0.57685 0.68165 0.73730 -0.01777 0.05778  0.01899  446 PHE A CB  
3506 C CG  . PHE A 446 ? 0.59360 0.67279 0.73444 -0.02233 0.05874  0.02158  446 PHE A CG  
3507 C CD1 . PHE A 446 ? 0.62029 0.68756 0.75342 -0.02616 0.05211  0.02401  446 PHE A CD1 
3508 C CD2 . PHE A 446 ? 0.60296 0.67100 0.73295 -0.02219 0.06599  0.02130  446 PHE A CD2 
3509 C CE1 . PHE A 446 ? 0.58588 0.63281 0.70347 -0.02955 0.05194  0.02672  446 PHE A CE1 
3510 C CE2 . PHE A 446 ? 0.59240 0.63892 0.70432 -0.02643 0.06517  0.02378  446 PHE A CE2 
3511 C CZ  . PHE A 446 ? 0.58032 0.61730 0.68728 -0.02995 0.05765  0.02682  446 PHE A CZ  
3512 N N   . GLY A 447 ? 0.63843 0.78896 0.83283 0.00891  0.04785  0.01802  447 GLY A N   
3513 C CA  . GLY A 447 ? 0.59381 0.76949 0.80766 0.01950  0.04876  0.01654  447 GLY A CA  
3514 C C   . GLY A 447 ? 0.64015 0.84554 0.87559 0.01162  0.05297  0.01213  447 GLY A C   
3515 O O   . GLY A 447 ? 0.62674 0.85374 0.87978 0.01966  0.05777  0.01012  447 GLY A O   
3516 N N   . LEU A 448 ? 0.69487 0.90144 0.92989 -0.00406 0.05204  0.01044  448 LEU A N   
3517 C CA  . LEU A 448 ? 0.63742 0.87213 0.89339 -0.01407 0.05557  0.00622  448 LEU A CA  
3518 C C   . LEU A 448 ? 0.61804 0.88726 0.89756 -0.00804 0.04718  0.00449  448 LEU A C   
3519 O O   . LEU A 448 ? 0.69820 0.99665 1.00061 -0.00728 0.05259  0.00150  448 LEU A O   
3520 C CB  . LEU A 448 ? 0.57959 0.80323 0.82762 -0.03201 0.05507  0.00508  448 LEU A CB  
3521 C CG  . LEU A 448 ? 0.55114 0.75449 0.78585 -0.04152 0.06619  0.00602  448 LEU A CG  
3522 C CD1 . LEU A 448 ? 0.64447 0.81611 0.85511 -0.03479 0.06719  0.01002  448 LEU A CD1 
3523 C CD2 . LEU A 448 ? 0.64238 0.83850 0.87369 -0.05839 0.06556  0.00500  448 LEU A CD2 
3524 N N   . PRO A 449 ? 0.65646 0.92613 0.93221 -0.00344 0.03428  0.00628  449 PRO A N   
3525 C CA  . PRO A 449 ? 0.61936 0.92365 0.91686 0.00376  0.02497  0.00530  449 PRO A CA  
3526 C C   . PRO A 449 ? 0.60856 0.92842 0.92053 0.02224  0.02815  0.00715  449 PRO A C   
3527 O O   . PRO A 449 ? 0.66620 1.02125 1.00221 0.02833  0.02228  0.00599  449 PRO A O   
3528 C CB  . PRO A 449 ? 0.65278 0.94506 0.93444 0.00681  0.01170  0.00833  449 PRO A CB  
3529 C CG  . PRO A 449 ? 0.60309 0.86583 0.86373 -0.00716 0.01435  0.00743  449 PRO A CG  
3530 C CD  . PRO A 449 ? 0.60390 0.84673 0.85699 -0.00763 0.02746  0.00853  449 PRO A CD  
3531 N N   . LEU A 450 ? 0.65215 0.94771 0.95094 0.03168  0.03703  0.00954  450 LEU A N   
3532 C CA  . LEU A 450 ? 0.67647 0.98616 0.99000 0.04930  0.04210  0.00992  450 LEU A CA  
3533 C C   . LEU A 450 ? 0.68000 1.02244 1.02006 0.04440  0.05245  0.00444  450 LEU A C   
3534 O O   . LEU A 450 ? 0.62298 0.99241 0.98571 0.05852  0.05409  0.00371  450 LEU A O   
3535 C CB  . LEU A 450 ? 0.54208 0.81539 0.83333 0.05922  0.04997  0.01234  450 LEU A CB  
3536 C CG  . LEU A 450 ? 0.67105 0.91278 0.93718 0.06293  0.04065  0.01809  450 LEU A CG  
3537 C CD1 . LEU A 450 ? 0.62013 0.82512 0.86414 0.07027  0.04810  0.01982  450 LEU A CD1 
3538 C CD2 . LEU A 450 ? 0.62555 0.88284 0.89985 0.07562  0.02720  0.02261  450 LEU A CD2 
3539 N N   . GLU A 451 ? 0.67172 1.01303 1.01013 0.02501  0.05966  0.00097  451 GLU A N   
3540 C CA  . GLU A 451 ? 0.77335 1.14740 1.13728 0.01701  0.06985  -0.00394 451 GLU A CA  
3541 C C   . GLU A 451 ? 0.80586 1.22277 1.19927 0.01433  0.05898  -0.00613 451 GLU A C   
3542 O O   . GLU A 451 ? 0.79405 1.21396 1.18630 -0.00129 0.05072  -0.00763 451 GLU A O   
3543 C CB  . GLU A 451 ? 0.85722 1.21532 1.20870 -0.00395 0.07953  -0.00575 451 GLU A CB  
3544 C CG  . GLU A 451 ? 0.87065 1.26188 1.24744 -0.01500 0.09078  -0.01027 451 GLU A CG  
3545 C CD  . GLU A 451 ? 0.99813 1.40549 1.38870 -0.00074 0.10413  -0.01210 451 GLU A CD  
3546 O OE1 . GLU A 451 ? 1.01744 1.40045 1.38884 -0.00156 0.11729  -0.01204 451 GLU A OE1 
3547 O OE2 . GLU A 451 ? 0.97688 1.42085 1.39659 0.01188  0.10145  -0.01374 451 GLU A OE2 
3548 N N   . ARG A 452 ? 0.79044 1.24105 1.21067 0.02999  0.05879  -0.00672 452 ARG A N   
3549 C CA  . ARG A 452 ? 0.88539 1.38140 1.33615 0.02944  0.04697  -0.00859 452 ARG A CA  
3550 C C   . ARG A 452 ? 0.95848 1.48292 1.42996 0.00637  0.05244  -0.01466 452 ARG A C   
3551 O O   . ARG A 452 ? 0.88568 1.44007 1.37521 -0.00227 0.04038  -0.01723 452 ARG A O   
3552 C CB  . ARG A 452 ? 0.88473 1.41114 1.36134 0.05339  0.04680  -0.00738 452 ARG A CB  
3553 C CG  . ARG A 452 ? 0.93554 1.46915 1.41313 0.07002  0.02754  -0.00208 452 ARG A CG  
3554 C CD  . ARG A 452 ? 1.09454 1.66341 1.60259 0.09477  0.02663  -0.00052 452 ARG A CD  
3555 N NE  . ARG A 452 ? 1.05813 1.59833 1.55294 0.11648  0.03625  0.00281  452 ARG A NE  
3556 C CZ  . ARG A 452 ? 1.03157 1.58942 1.54738 0.13069  0.04978  0.00013  452 ARG A CZ  
3557 N NH1 . ARG A 452 ? 0.90214 1.50801 1.45460 0.12518  0.05674  -0.00555 452 ARG A NH1 
3558 N NH2 . ARG A 452 ? 1.02816 1.55435 1.52772 0.15038  0.05727  0.00269  452 ARG A NH2 
3559 N N   . ARG A 453 ? 0.97248 1.48628 1.43949 -0.00496 0.07010  -0.01691 453 ARG A N   
3560 C CA  . ARG A 453 ? 0.99559 1.53138 1.47927 -0.02872 0.07704  -0.02180 453 ARG A CA  
3561 C C   . ARG A 453 ? 1.04824 1.56572 1.51584 -0.04926 0.06705  -0.02279 453 ARG A C   
3562 O O   . ARG A 453 ? 1.00438 1.54854 1.49146 -0.06717 0.06454  -0.02745 453 ARG A O   
3563 C CB  . ARG A 453 ? 0.99326 1.51435 1.46847 -0.03586 0.09851  -0.02246 453 ARG A CB  
3564 C CG  . ARG A 453 ? 1.14086 1.69244 1.64090 -0.02215 0.11265  -0.02459 453 ARG A CG  
3565 C CD  . ARG A 453 ? 1.14741 1.75977 1.69366 -0.02329 0.10917  -0.02877 453 ARG A CD  
3566 N NE  . ARG A 453 ? 1.21150 1.84592 1.77519 0.00254  0.09798  -0.02720 453 ARG A NE  
3567 C CZ  . ARG A 453 ? 1.19486 1.86953 1.78672 0.00509  0.08209  -0.02815 453 ARG A CZ  
3568 N NH1 . ARG A 453 ? 1.13823 1.83815 1.74621 -0.01759 0.07582  -0.03206 453 ARG A NH1 
3569 N NH2 . ARG A 453 ? 1.27188 1.96051 1.87473 0.03083  0.07173  -0.02502 453 ARG A NH2 
3570 N N   . ASP A 454 ? 1.11517 1.58758 1.54806 -0.04760 0.06196  -0.01905 454 ASP A N   
3571 C CA  . ASP A 454 ? 1.08963 1.54170 1.50591 -0.06540 0.05404  -0.02044 454 ASP A CA  
3572 C C   . ASP A 454 ? 1.07964 1.55805 1.50979 -0.06681 0.03618  -0.02350 454 ASP A C   
3573 O O   . ASP A 454 ? 1.07683 1.59176 1.53114 -0.05428 0.02926  -0.02377 454 ASP A O   
3574 C CB  . ASP A 454 ? 1.08321 1.48535 1.46227 -0.06085 0.05264  -0.01574 454 ASP A CB  
3575 C CG  . ASP A 454 ? 1.25993 1.63396 1.62179 -0.06405 0.06838  -0.01323 454 ASP A CG  
3576 O OD1 . ASP A 454 ? 1.15028 1.54128 1.52670 -0.07202 0.08115  -0.01525 454 ASP A OD1 
3577 O OD2 . ASP A 454 ? 1.30699 1.64334 1.64078 -0.05893 0.06782  -0.00918 454 ASP A OD2 
3578 N N   . GLN A 455 ? 0.92296 1.38298 1.33725 -0.08143 0.02831  -0.02595 455 GLN A N   
3579 C CA  . GLN A 455 ? 0.95599 1.43972 1.38032 -0.08613 0.01158  -0.03027 455 GLN A CA  
3580 C C   . GLN A 455 ? 0.90278 1.36781 1.30496 -0.07144 -0.00221 -0.02646 455 GLN A C   
3581 O O   . GLN A 455 ? 0.91459 1.38886 1.31490 -0.07686 -0.01632 -0.03002 455 GLN A O   
3582 C CB  . GLN A 455 ? 1.02765 1.50486 1.44904 -0.11248 0.01145  -0.03702 455 GLN A CB  
3583 C CG  . GLN A 455 ? 1.07510 1.58875 1.52813 -0.12949 0.01886  -0.04238 455 GLN A CG  
3584 C CD  . GLN A 455 ? 1.12258 1.62686 1.57719 -0.13147 0.03905  -0.03909 455 GLN A CD  
3585 O OE1 . GLN A 455 ? 1.03745 1.57737 1.52022 -0.12916 0.04704  -0.03974 455 GLN A OE1 
3586 N NE2 . GLN A 455 ? 1.11205 1.56903 1.53592 -0.13493 0.04742  -0.03540 455 GLN A NE2 
3587 N N   . TYR A 456 ? 0.82096 1.25972 1.20536 -0.05400 0.00184  -0.01957 456 TYR A N   
3588 C CA  . TYR A 456 ? 0.77273 1.19410 1.13651 -0.04011 -0.00978 -0.01498 456 TYR A CA  
3589 C C   . TYR A 456 ? 0.74313 1.20099 1.12586 -0.02556 -0.02287 -0.01334 456 TYR A C   
3590 O O   . TYR A 456 ? 0.65328 1.14413 1.06387 -0.01811 -0.01993 -0.01344 456 TYR A O   
3591 C CB  . TYR A 456 ? 0.66464 1.05027 1.00690 -0.02640 -0.00151 -0.00816 456 TYR A CB  
3592 C CG  . TYR A 456 ? 0.65923 1.00816 0.98073 -0.03793 0.00932  -0.00833 456 TYR A CG  
3593 C CD1 . TYR A 456 ? 0.62950 0.95087 0.92799 -0.04611 0.00482  -0.00896 456 TYR A CD1 
3594 C CD2 . TYR A 456 ? 0.71251 1.05436 1.03657 -0.03961 0.02405  -0.00763 456 TYR A CD2 
3595 C CE1 . TYR A 456 ? 0.64605 0.93537 0.92712 -0.05475 0.01373  -0.00839 456 TYR A CE1 
3596 C CE2 . TYR A 456 ? 0.69534 1.00405 0.99934 -0.04922 0.03251  -0.00674 456 TYR A CE2 
3597 C CZ  . TYR A 456 ? 0.70487 0.98795 0.98850 -0.05624 0.02682  -0.00682 456 TYR A CZ  
3598 O OH  . TYR A 456 ? 0.63954 0.89103 0.90472 -0.06402 0.03429  -0.00526 456 TYR A OH  
3599 N N   . THR A 457 ? 0.72824 1.18042 1.09530 -0.02075 -0.03729 -0.01147 457 THR A N   
3600 C CA  . THR A 457 ? 0.62855 1.11164 1.00895 -0.00524 -0.05145 -0.00813 457 THR A CA  
3601 C C   . THR A 457 ? 0.68708 1.15727 1.06228 0.01937  -0.04818 0.00108  457 THR A C   
3602 O O   . THR A 457 ? 0.62075 1.05539 0.97795 0.02322  -0.03657 0.00439  457 THR A O   
3603 C CB  . THR A 457 ? 0.59562 1.07421 0.95641 -0.00843 -0.06776 -0.00863 457 THR A CB  
3604 O OG1 . THR A 457 ? 0.62156 1.05500 0.94780 -0.00320 -0.06482 -0.00336 457 THR A OG1 
3605 C CG2 . THR A 457 ? 0.50094 0.98796 0.86385 -0.03302 -0.07112 -0.01895 457 THR A CG2 
3606 N N   . LYS A 458 ? 0.65269 1.15128 1.04298 0.03635  -0.05944 0.00534  458 LYS A N   
3607 C CA  . LYS A 458 ? 0.71633 1.19899 1.09921 0.06061  -0.05761 0.01448  458 LYS A CA  
3608 C C   . LYS A 458 ? 0.73244 1.17050 1.07665 0.06436  -0.06074 0.02081  458 LYS A C   
3609 O O   . LYS A 458 ? 0.74524 1.15199 1.07444 0.07594  -0.05234 0.02647  458 LYS A O   
3610 C CB  . LYS A 458 ? 0.68847 1.21083 1.09560 0.07924  -0.07031 0.01860  458 LYS A CB  
3611 C CG  . LYS A 458 ? 0.76633 1.27174 1.16803 0.10613  -0.06765 0.02813  458 LYS A CG  
3612 C CD  . LYS A 458 ? 0.88952 1.41555 1.32149 0.11706  -0.05439 0.02595  458 LYS A CD  
3613 C CE  . LYS A 458 ? 0.96770 1.45168 1.38109 0.13202  -0.04082 0.03076  458 LYS A CE  
3614 N NZ  . LYS A 458 ? 0.96839 1.47186 1.40913 0.14864  -0.02948 0.02944  458 LYS A NZ  
3615 N N   . ALA A 459 ? 0.67456 1.10914 1.00204 0.05380  -0.07202 0.01933  459 ALA A N   
3616 C CA  . ALA A 459 ? 0.69286 1.08753 0.98439 0.05572  -0.07368 0.02482  459 ALA A CA  
3617 C C   . ALA A 459 ? 0.68659 1.04309 0.96200 0.04758  -0.05787 0.02352  459 ALA A C   
3618 O O   . ALA A 459 ? 0.73624 1.05962 0.98959 0.05571  -0.05389 0.03004  459 ALA A O   
3619 C CB  . ALA A 459 ? 0.65792 1.05760 0.93512 0.04347  -0.08648 0.02116  459 ALA A CB  
3620 N N   . GLU A 460 ? 0.66792 1.02880 0.95414 0.03120  -0.04900 0.01554  460 GLU A N   
3621 C CA  . GLU A 460 ? 0.68154 1.00826 0.95269 0.02335  -0.03538 0.01465  460 GLU A CA  
3622 C C   . GLU A 460 ? 0.64625 0.96269 0.92208 0.03526  -0.02392 0.01836  460 GLU A C   
3623 O O   . GLU A 460 ? 0.61865 0.90143 0.87504 0.03602  -0.01620 0.02118  460 GLU A O   
3624 C CB  . GLU A 460 ? 0.68572 1.01814 0.96469 0.00255  -0.03007 0.00602  460 GLU A CB  
3625 C CG  . GLU A 460 ? 0.65830 0.99207 0.92708 -0.01022 -0.03992 0.00111  460 GLU A CG  
3626 C CD  . GLU A 460 ? 0.66154 0.99885 0.93779 -0.03118 -0.03509 -0.00770 460 GLU A CD  
3627 O OE1 . GLU A 460 ? 0.66225 1.02219 0.96224 -0.03696 -0.02973 -0.01104 460 GLU A OE1 
3628 O OE2 . GLU A 460 ? 0.66447 0.98077 0.92228 -0.04183 -0.03599 -0.01123 460 GLU A OE2 
3629 N N   . GLU A 461 ? 0.63481 0.98048 0.93629 0.04476  -0.02274 0.01793  461 GLU A N   
3630 C CA  . GLU A 461 ? 0.64763 0.98331 0.95234 0.05868  -0.01204 0.02087  461 GLU A CA  
3631 C C   . GLU A 461 ? 0.67598 0.98217 0.95858 0.07444  -0.01531 0.02916  461 GLU A C   
3632 O O   . GLU A 461 ? 0.65842 0.93257 0.92469 0.07695  -0.00590 0.03104  461 GLU A O   
3633 C CB  . GLU A 461 ? 0.63823 1.01415 0.97603 0.06895  -0.01146 0.01911  461 GLU A CB  
3634 C CG  . GLU A 461 ? 0.72843 1.09462 1.07061 0.08138  0.00276  0.01964  461 GLU A CG  
3635 C CD  . GLU A 461 ? 0.75487 1.15711 1.12771 0.09922  0.00267  0.01984  461 GLU A CD  
3636 O OE1 . GLU A 461 ? 0.85316 1.29790 1.25265 0.09674  -0.00529 0.01729  461 GLU A OE1 
3637 O OE2 . GLU A 461 ? 0.73529 1.12353 1.10630 0.11548  0.01129  0.02187  461 GLU A OE2 
3638 N N   . ILE A 462 ? 0.70778 1.02372 0.98821 0.08414  -0.02903 0.03435  462 ILE A N   
3639 C CA  . ILE A 462 ? 0.69759 0.98483 0.95586 0.09858  -0.03246 0.04341  462 ILE A CA  
3640 C C   . ILE A 462 ? 0.70495 0.95400 0.93321 0.08744  -0.02899 0.04471  462 ILE A C   
3641 O O   . ILE A 462 ? 0.71439 0.93129 0.92516 0.09399  -0.02333 0.04958  462 ILE A O   
3642 C CB  . ILE A 462 ? 0.76341 1.07070 1.02410 0.11020  -0.04887 0.04943  462 ILE A CB  
3643 C CG1 . ILE A 462 ? 0.73858 1.08040 1.02963 0.12679  -0.05148 0.05012  462 ILE A CG1 
3644 C CG2 . ILE A 462 ? 0.74294 1.01639 0.97447 0.12093  -0.05317 0.05976  462 ILE A CG2 
3645 C CD1 . ILE A 462 ? 0.80600 1.19024 1.11453 0.12766  -0.06801 0.04986  462 ILE A CD1 
3646 N N   . LEU A 463 ? 0.65400 0.90591 0.87656 0.07034  -0.03192 0.03997  463 LEU A N   
3647 C CA  . LEU A 463 ? 0.72775 0.94656 0.92417 0.06112  -0.02865 0.04121  463 LEU A CA  
3648 C C   . LEU A 463 ? 0.66745 0.86434 0.86027 0.05505  -0.01517 0.03863  463 LEU A C   
3649 O O   . LEU A 463 ? 0.68112 0.84784 0.85457 0.05522  -0.01098 0.04234  463 LEU A O   
3650 C CB  . LEU A 463 ? 0.64600 0.87195 0.83691 0.04581  -0.03438 0.03606  463 LEU A CB  
3651 C CG  . LEU A 463 ? 0.64204 0.83832 0.81095 0.03520  -0.02919 0.03547  463 LEU A CG  
3652 C CD1 . LEU A 463 ? 0.60203 0.77176 0.74818 0.04357  -0.02959 0.04402  463 LEU A CD1 
3653 C CD2 . LEU A 463 ? 0.67149 0.87530 0.83602 0.02146  -0.03423 0.02907  463 LEU A CD2 
3654 N N   . SER A 464 ? 0.63219 0.84449 0.84288 0.04869  -0.00842 0.03241  464 SER A N   
3655 C CA  . SER A 464 ? 0.64256 0.83532 0.84878 0.04470  0.00396  0.03061  464 SER A CA  
3656 C C   . SER A 464 ? 0.66358 0.84093 0.86526 0.05986  0.00867  0.03484  464 SER A C   
3657 O O   . SER A 464 ? 0.72235 0.87151 0.90839 0.05839  0.01548  0.03585  464 SER A O   
3658 C CB  . SER A 464 ? 0.60621 0.81966 0.83166 0.03569  0.01082  0.02399  464 SER A CB  
3659 O OG  . SER A 464 ? 0.60443 0.79773 0.82187 0.03166  0.02226  0.02278  464 SER A OG  
3660 N N   . ARG A 465 ? 0.64460 0.84004 0.85991 0.07475  0.00468  0.03715  465 ARG A N   
3661 C CA  . ARG A 465 ? 0.72062 0.90051 0.93267 0.09074  0.00983  0.04051  465 ARG A CA  
3662 C C   . ARG A 465 ? 0.68553 0.82927 0.87111 0.09409  0.00782  0.04721  465 ARG A C   
3663 O O   . ARG A 465 ? 0.73065 0.84739 0.90444 0.09794  0.01559  0.04781  465 ARG A O   
3664 C CB  . ARG A 465 ? 0.68365 0.89185 0.91691 0.10780  0.00439  0.04252  465 ARG A CB  
3665 C CG  . ARG A 465 ? 0.68880 0.88112 0.92055 0.12678  0.01023  0.04553  465 ARG A CG  
3666 C CD  . ARG A 465 ? 0.74190 0.92453 0.97527 0.12367  0.02552  0.03877  465 ARG A CD  
3667 N NE  . ARG A 465 ? 0.86728 1.01998 1.08832 0.13801  0.03237  0.04067  465 ARG A NE  
3668 C CZ  . ARG A 465 ? 0.84386 0.95710 1.03926 0.13287  0.03735  0.04128  465 ARG A CZ  
3669 N NH1 . ARG A 465 ? 0.67626 0.77584 0.85614 0.11509  0.03595  0.04104  465 ARG A NH1 
3670 N NH2 . ARG A 465 ? 0.80981 0.89696 0.99560 0.14589  0.04398  0.04168  465 ARG A NH2 
3671 N N   A SER A 466 ? 0.65418 0.79664 0.82921 0.09137  -0.00200 0.05180  466 SER A N   
3672 N N   B SER A 466 ? 0.66900 0.81133 0.84396 0.09158  -0.00204 0.05189  466 SER A N   
3673 C CA  A SER A 466 ? 0.69778 0.80765 0.84800 0.09305  -0.00318 0.05869  466 SER A CA  
3674 C CA  B SER A 466 ? 0.69767 0.80686 0.84770 0.09315  -0.00292 0.05869  466 SER A CA  
3675 C C   A SER A 466 ? 0.68297 0.77083 0.81885 0.07753  0.00332  0.05592  466 SER A C   
3676 C C   B SER A 466 ? 0.68272 0.77035 0.81859 0.07746  0.00348  0.05585  466 SER A C   
3677 O O   A SER A 466 ? 0.67871 0.73737 0.79877 0.07801  0.00802  0.05884  466 SER A O   
3678 O O   B SER A 466 ? 0.67984 0.73829 0.79989 0.07774  0.00823  0.05869  466 SER A O   
3679 C CB  A SER A 466 ? 0.70371 0.82088 0.84614 0.09568  -0.01511 0.06479  466 SER A CB  
3680 C CB  B SER A 466 ? 0.70547 0.82051 0.84694 0.09625  -0.01473 0.06516  466 SER A CB  
3681 O OG  A SER A 466 ? 0.71031 0.79662 0.82910 0.09889  -0.01546 0.07279  466 SER A OG  
3682 O OG  B SER A 466 ? 0.66666 0.81784 0.82708 0.09922  -0.02322 0.06299  466 SER A OG  
3683 N N   . ILE A 467 ? 0.71328 0.81450 0.85487 0.06370  0.00343  0.05031  467 ILE A N   
3684 C CA  . ILE A 467 ? 0.68727 0.77016 0.81749 0.05040  0.00886  0.04804  467 ILE A CA  
3685 C C   . ILE A 467 ? 0.65394 0.72105 0.78238 0.05057  0.01826  0.04568  467 ILE A C   
3686 O O   . ILE A 467 ? 0.63851 0.68062 0.75200 0.04742  0.02161  0.04751  467 ILE A O   
3687 C CB  . ILE A 467 ? 0.72491 0.82448 0.86300 0.03741  0.00766  0.04233  467 ILE A CB  
3688 C CG1 . ILE A 467 ? 0.74385 0.85064 0.87604 0.03511  -0.00097 0.04396  467 ILE A CG1 
3689 C CG2 . ILE A 467 ? 0.62803 0.71128 0.75884 0.02591  0.01428  0.03970  467 ILE A CG2 
3690 C CD1 . ILE A 467 ? 0.65071 0.77428 0.79098 0.02353  -0.00308 0.03741  467 ILE A CD1 
3691 N N   . VAL A 468 ? 0.63318 0.71552 0.77658 0.05429  0.02270  0.04139  468 VAL A N   
3692 C CA  . VAL A 468 ? 0.64203 0.71045 0.78221 0.05497  0.03226  0.03821  468 VAL A CA  
3693 C C   . VAL A 468 ? 0.69706 0.73896 0.82344 0.06523  0.03399  0.04198  468 VAL A C   
3694 O O   . VAL A 468 ? 0.68118 0.69869 0.79317 0.06034  0.03900  0.04088  468 VAL A O   
3695 C CB  . VAL A 468 ? 0.69744 0.79033 0.85732 0.05876  0.03742  0.03320  468 VAL A CB  
3696 C CG1 . VAL A 468 ? 0.61154 0.69003 0.76681 0.06405  0.04775  0.02999  468 VAL A CG1 
3697 C CG2 . VAL A 468 ? 0.62154 0.73159 0.79000 0.04415  0.03806  0.02917  468 VAL A CG2 
3698 N N   . LYS A 469 ? 0.69916 0.74433 0.82883 0.07927  0.02930  0.04669  469 LYS A N   
3699 C CA  . LYS A 469 ? 0.67782 0.69367 0.79236 0.08892  0.03060  0.05134  469 LYS A CA  
3700 C C   . LYS A 469 ? 0.72288 0.71333 0.81706 0.07842  0.02890  0.05530  469 LYS A C   
3701 O O   . LYS A 469 ? 0.72391 0.68639 0.80377 0.07602  0.03396  0.05492  469 LYS A O   
3702 C CB  . LYS A 469 ? 0.66115 0.68539 0.78183 0.10599  0.02405  0.05761  469 LYS A CB  
3703 C CG  . LYS A 469 ? 0.69486 0.68508 0.79718 0.11560  0.02439  0.06434  469 LYS A CG  
3704 C CD  . LYS A 469 ? 0.75779 0.72419 0.85422 0.11938  0.03498  0.05919  469 LYS A CD  
3705 C CE  . LYS A 469 ? 0.69495 0.67727 0.80936 0.13671  0.03897  0.05586  469 LYS A CE  
3706 N NZ  . LYS A 469 ? 0.62721 0.58660 0.73401 0.13844  0.05074  0.04876  469 LYS A NZ  
3707 N N   . ARG A 470 ? 0.71490 0.71530 0.80766 0.07153  0.02215  0.05855  470 ARG A N   
3708 C CA  . ARG A 470 ? 0.73288 0.71260 0.80846 0.06212  0.02147  0.06247  470 ARG A CA  
3709 C C   . ARG A 470 ? 0.69669 0.66621 0.76811 0.04889  0.02713  0.05730  470 ARG A C   
3710 O O   . ARG A 470 ? 0.67653 0.62214 0.73449 0.04408  0.02982  0.05891  470 ARG A O   
3711 C CB  . ARG A 470 ? 0.68623 0.68077 0.76137 0.05734  0.01452  0.06545  470 ARG A CB  
3712 C CG  . ARG A 470 ? 0.69992 0.70153 0.77354 0.06929  0.00707  0.07218  470 ARG A CG  
3713 C CD  . ARG A 470 ? 0.72280 0.72809 0.78645 0.06241  0.00192  0.07570  470 ARG A CD  
3714 N NE  . ARG A 470 ? 0.67256 0.69048 0.73516 0.07263  -0.00686 0.08112  470 ARG A NE  
3715 C CZ  . ARG A 470 ? 0.75240 0.75433 0.79855 0.07997  -0.01005 0.09066  470 ARG A CZ  
3716 N NH1 . ARG A 470 ? 0.76447 0.73631 0.79402 0.07688  -0.00440 0.09568  470 ARG A NH1 
3717 N NH2 . ARG A 470 ? 0.75956 0.77601 0.80548 0.09020  -0.01947 0.09564  470 ARG A NH2 
3718 N N   . TRP A 471 ? 0.69685 0.68428 0.77942 0.04240  0.02860  0.05139  471 TRP A N   
3719 C CA  . TRP A 471 ? 0.72064 0.69930 0.79858 0.03093  0.03285  0.04736  471 TRP A CA  
3720 C C   . TRP A 471 ? 0.68039 0.63802 0.74944 0.03346  0.03880  0.04488  471 TRP A C   
3721 O O   . TRP A 471 ? 0.64995 0.58941 0.70740 0.02532  0.04029  0.04438  471 TRP A O   
3722 C CB  . TRP A 471 ? 0.61986 0.61949 0.71015 0.02512  0.03383  0.04241  471 TRP A CB  
3723 C CG  . TRP A 471 ? 0.63026 0.63895 0.72257 0.01537  0.03013  0.04262  471 TRP A CG  
3724 C CD1 . TRP A 471 ? 0.64894 0.65846 0.74172 0.00562  0.03182  0.03993  471 TRP A CD1 
3725 C CD2 . TRP A 471 ? 0.64168 0.65868 0.73467 0.01540  0.02452  0.04542  471 TRP A CD2 
3726 N NE1 . TRP A 471 ? 0.66508 0.68190 0.76003 0.00036  0.02814  0.04055  471 TRP A NE1 
3727 C CE2 . TRP A 471 ? 0.65969 0.68133 0.75421 0.00567  0.02400  0.04329  471 TRP A CE2 
3728 C CE3 . TRP A 471 ? 0.62889 0.64894 0.71976 0.02314  0.01985  0.04965  471 TRP A CE3 
3729 C CZ2 . TRP A 471 ? 0.61131 0.64000 0.70519 0.00318  0.02002  0.04395  471 TRP A CZ2 
3730 C CZ3 . TRP A 471 ? 0.64704 0.67503 0.73581 0.01981  0.01519  0.05086  471 TRP A CZ3 
3731 C CH2 . TRP A 471 ? 0.57638 0.60839 0.66663 0.00976  0.01583  0.04738  471 TRP A CH2 
3732 N N   . ALA A 472 ? 0.67283 0.63329 0.74744 0.04474  0.04226  0.04277  472 ALA A N   
3733 C CA  . ALA A 472 ? 0.65334 0.59262 0.71824 0.04795  0.04903  0.03891  472 ALA A CA  
3734 C C   . ALA A 472 ? 0.70997 0.61964 0.75898 0.04991  0.04836  0.04301  472 ALA A C   
3735 O O   . ALA A 472 ? 0.75302 0.63998 0.78829 0.04308  0.05170  0.04003  472 ALA A O   
3736 C CB  . ALA A 472 ? 0.70569 0.65665 0.78211 0.06147  0.05385  0.03558  472 ALA A CB  
3737 N N   . ASN A 473 ? 0.69646 0.60540 0.74592 0.05819  0.04375  0.05006  473 ASN A N   
3738 C CA  . ASN A 473 ? 0.71082 0.58971 0.74379 0.05882  0.04351  0.05536  473 ASN A CA  
3739 C C   . ASN A 473 ? 0.70732 0.57735 0.73099 0.04231  0.04204  0.05675  473 ASN A C   
3740 O O   . ASN A 473 ? 0.80582 0.64878 0.81530 0.03684  0.04445  0.05731  473 ASN A O   
3741 C CB  . ASN A 473 ? 0.72143 0.60236 0.75529 0.07128  0.03843  0.06395  473 ASN A CB  
3742 C CG  . ASN A 473 ? 0.72235 0.59888 0.76044 0.08958  0.04081  0.06379  473 ASN A CG  
3743 O OD1 . ASN A 473 ? 0.79378 0.65881 0.83032 0.09226  0.04782  0.05706  473 ASN A OD1 
3744 N ND2 . ASN A 473 ? 0.80600 0.69212 0.84916 0.10286  0.03505  0.07090  473 ASN A ND2 
3745 N N   . PHE A 474 ? 0.66879 0.56110 0.70087 0.03394  0.03847  0.05681  474 PHE A N   
3746 C CA  . PHE A 474 ? 0.70435 0.59153 0.73085 0.01911  0.03789  0.05701  474 PHE A CA  
3747 C C   . PHE A 474 ? 0.70711 0.58432 0.72895 0.01074  0.04124  0.05029  474 PHE A C   
3748 O O   . PHE A 474 ? 0.71740 0.57616 0.72885 0.00174  0.04198  0.05032  474 PHE A O   
3749 C CB  . PHE A 474 ? 0.67289 0.58491 0.70961 0.01343  0.03413  0.05759  474 PHE A CB  
3750 C CG  . PHE A 474 ? 0.70982 0.61962 0.74384 0.00006  0.03385  0.05772  474 PHE A CG  
3751 C CD1 . PHE A 474 ? 0.73107 0.62917 0.75689 -0.00463 0.03393  0.06319  474 PHE A CD1 
3752 C CD2 . PHE A 474 ? 0.59524 0.51417 0.63472 -0.00763 0.03379  0.05292  474 PHE A CD2 
3753 C CE1 . PHE A 474 ? 0.70360 0.60301 0.72995 -0.01682 0.03413  0.06314  474 PHE A CE1 
3754 C CE2 . PHE A 474 ? 0.69020 0.60940 0.72942 -0.01851 0.03277  0.05337  474 PHE A CE2 
3755 C CZ  . PHE A 474 ? 0.71185 0.62291 0.74600 -0.02316 0.03307  0.05808  474 PHE A CZ  
3756 N N   . ALA A 475 ? 0.64102 0.53066 0.66963 0.01251  0.04318  0.04450  475 ALA A N   
3757 C CA  . ALA A 475 ? 0.65277 0.53267 0.67374 0.00458  0.04593  0.03834  475 ALA A CA  
3758 C C   . ALA A 475 ? 0.83148 0.68172 0.83743 0.00668  0.04991  0.03582  475 ALA A C   
3759 O O   . ALA A 475 ? 0.79842 0.63250 0.79312 -0.00412 0.04963  0.03337  475 ALA A O   
3760 C CB  . ALA A 475 ? 0.67060 0.56656 0.69883 0.00732  0.04889  0.03329  475 ALA A CB  
3761 N N   . LYS A 476 ? 0.72951 0.57195 0.73534 0.02069  0.05331  0.03625  476 LYS A N   
3762 C CA  . LYS A 476 ? 0.80761 0.61888 0.79843 0.02442  0.05825  0.03284  476 LYS A CA  
3763 C C   . LYS A 476 ? 0.85060 0.63713 0.82965 0.01874  0.05629  0.03824  476 LYS A C   
3764 O O   . LYS A 476 ? 0.83164 0.59297 0.79611 0.00990  0.05827  0.03432  476 LYS A O   
3765 C CB  . LYS A 476 ? 0.88633 0.69700 0.88220 0.04319  0.06277  0.03215  476 LYS A CB  
3766 C CG  . LYS A 476 ? 0.82935 0.66460 0.83783 0.04885  0.06666  0.02648  476 LYS A CG  
3767 C CD  . LYS A 476 ? 0.72770 0.56121 0.74208 0.06812  0.07182  0.02548  476 LYS A CD  
3768 C CE  . LYS A 476 ? 0.80722 0.66477 0.83445 0.07324  0.07786  0.01905  476 LYS A CE  
3769 N NZ  . LYS A 476 ? 0.86564 0.74674 0.91335 0.09000  0.07716  0.02256  476 LYS A NZ  
3770 N N   . TYR A 477 ? 0.83413 0.62679 0.81804 0.02281  0.05265  0.04710  477 TYR A N   
3771 C CA  . TYR A 477 ? 0.86859 0.63490 0.83979 0.02006  0.05253  0.05359  477 TYR A CA  
3772 C C   . TYR A 477 ? 0.82501 0.60178 0.79841 0.00765  0.04852  0.05978  477 TYR A C   
3773 O O   . TYR A 477 ? 0.84470 0.60270 0.80821 0.00482  0.04899  0.06656  477 TYR A O   
3774 C CB  . TYR A 477 ? 0.86055 0.61729 0.83024 0.03805  0.05296  0.06013  477 TYR A CB  
3775 C CG  . TYR A 477 ? 0.88652 0.64077 0.85942 0.05312  0.05729  0.05414  477 TYR A CG  
3776 C CD1 . TYR A 477 ? 0.91062 0.63906 0.87146 0.05107  0.06348  0.04572  477 TYR A CD1 
3777 C CD2 . TYR A 477 ? 0.77615 0.55438 0.76409 0.06900  0.05555  0.05622  477 TYR A CD2 
3778 C CE1 . TYR A 477 ? 0.88122 0.60709 0.84445 0.06526  0.06912  0.03948  477 TYR A CE1 
3779 C CE2 . TYR A 477 ? 0.83187 0.61088 0.82535 0.08311  0.06068  0.05041  477 TYR A CE2 
3780 C CZ  . TYR A 477 ? 0.89227 0.64450 0.87303 0.08164  0.06816  0.04198  477 TYR A CZ  
3781 O OH  . TYR A 477 ? 0.87076 0.62337 0.85631 0.09600  0.07494  0.03537  477 TYR A OH  
3782 N N   . GLY A 478 ? 0.78365 0.58878 0.76927 0.00063  0.04542  0.05782  478 GLY A N   
3783 C CA  . GLY A 478 ? 0.80250 0.62099 0.79246 -0.00858 0.04256  0.06305  478 GLY A CA  
3784 C C   . GLY A 478 ? 0.81013 0.63366 0.80000 -0.00052 0.04089  0.07167  478 GLY A C   
3785 O O   . GLY A 478 ? 0.82495 0.65308 0.81386 -0.00824 0.04033  0.07654  478 GLY A O   
3786 N N   . ASN A 479 ? 0.77173 0.59643 0.76279 0.01495  0.03998  0.07359  479 ASN A N   
3787 C CA  . ASN A 479 ? 0.76206 0.59073 0.75047 0.02313  0.03696  0.08233  479 ASN A CA  
3788 C C   . ASN A 479 ? 0.70340 0.55755 0.70480 0.03600  0.03290  0.08099  479 ASN A C   
3789 O O   . ASN A 479 ? 0.74249 0.59312 0.74681 0.04833  0.03360  0.07925  479 ASN A O   
3790 C CB  . ASN A 479 ? 0.78662 0.58233 0.75863 0.02963  0.03908  0.08927  479 ASN A CB  
3791 C CG  . ASN A 479 ? 0.87580 0.66915 0.83849 0.03211  0.03659  0.10026  479 ASN A CG  
3792 O OD1 . ASN A 479 ? 0.87043 0.68814 0.83899 0.02941  0.03333  0.10163  479 ASN A OD1 
3793 N ND2 . ASN A 479 ? 0.82079 0.58254 0.76677 0.03723  0.03847  0.10821  479 ASN A ND2 
3794 N N   . PRO A 480 ? 0.77924 0.65993 0.78948 0.03331  0.02896  0.08105  480 PRO A N   
3795 C CA  . PRO A 480 ? 0.69973 0.60722 0.72469 0.04160  0.02517  0.07760  480 PRO A CA  
3796 C C   . PRO A 480 ? 0.77469 0.68760 0.79831 0.05553  0.01975  0.08427  480 PRO A C   
3797 O O   . PRO A 480 ? 0.81424 0.74999 0.84387 0.05674  0.01425  0.08485  480 PRO A O   
3798 C CB  . PRO A 480 ? 0.70435 0.63288 0.73663 0.03065  0.02359  0.07426  480 PRO A CB  
3799 C CG  . PRO A 480 ? 0.68611 0.60346 0.70603 0.02302  0.02436  0.08006  480 PRO A CG  
3800 C CD  . PRO A 480 ? 0.73433 0.62189 0.74225 0.02119  0.02870  0.08298  480 PRO A CD  
3801 N N   . GLN A 481 ? 0.73199 0.62315 0.74698 0.06640  0.02076  0.08925  481 GLN A N   
3802 C CA  . GLN A 481 ? 0.83401 0.72997 0.84821 0.08205  0.01469  0.09641  481 GLN A CA  
3803 C C   . GLN A 481 ? 0.82826 0.74329 0.86085 0.09522  0.01352  0.09145  481 GLN A C   
3804 O O   . GLN A 481 ? 0.80525 0.72001 0.84619 0.09387  0.01952  0.08349  481 GLN A O   
3805 C CB  . GLN A 481 ? 0.73893 0.59973 0.73351 0.08869  0.01617  0.10599  481 GLN A CB  
3806 C CG  . GLN A 481 ? 0.77321 0.61197 0.75043 0.07336  0.02019  0.10999  481 GLN A CG  
3807 C CD  . GLN A 481 ? 0.81095 0.66864 0.78566 0.06460  0.01655  0.11280  481 GLN A CD  
3808 O OE1 . GLN A 481 ? 0.86826 0.74426 0.84429 0.07255  0.00949  0.11644  481 GLN A OE1 
3809 N NE2 . GLN A 481 ? 0.77372 0.62786 0.74496 0.04833  0.02131  0.11057  481 GLN A NE2 
3810 N N   . GLU A 482 ? 0.81421 0.74861 0.85336 0.10730  0.00556  0.09606  482 GLU A N   
3811 C CA  . GLU A 482 ? 0.77907 0.72955 0.83494 0.12423  0.00353  0.09468  482 GLU A CA  
3812 C C   . GLU A 482 ? 0.80551 0.73376 0.84804 0.14038  -0.00002 0.10587  482 GLU A C   
3813 O O   . GLU A 482 ? 0.87152 0.80627 0.90684 0.14467  -0.00883 0.11433  482 GLU A O   
3814 C CB  . GLU A 482 ? 0.76158 0.75407 0.83692 0.12497  -0.00422 0.09151  482 GLU A CB  
3815 C CG  . GLU A 482 ? 0.80435 0.82130 0.90377 0.13830  -0.00407 0.08697  482 GLU A CG  
3816 C CD  . GLU A 482 ? 0.92079 0.92841 1.01944 0.16050  -0.00734 0.09497  482 GLU A CD  
3817 O OE1 . GLU A 482 ? 0.88332 0.89324 0.97413 0.16823  -0.01745 0.10446  482 GLU A OE1 
3818 O OE2 . GLU A 482 ? 0.97128 0.96762 1.07562 0.17078  0.00039  0.09189  482 GLU A OE2 
3819 N N   . THR A 483 ? 0.81814 0.71733 0.85469 0.14881  0.00695  0.10606  483 THR A N   
3820 C CA  . THR A 483 ? 0.87726 0.74395 0.89580 0.16189  0.00557  0.11726  483 THR A CA  
3821 C C   . THR A 483 ? 0.97339 0.85379 1.00415 0.18635  -0.00091 0.12246  483 THR A C   
3822 O O   . THR A 483 ? 0.87818 0.72978 0.89566 0.20105  -0.00156 0.13173  483 THR A O   
3823 C CB  . THR A 483 ? 0.86977 0.69408 0.87406 0.15908  0.01631  0.11459  483 THR A CB  
3824 O OG1 . THR A 483 ? 0.92808 0.75746 0.94762 0.16819  0.02274  0.10495  483 THR A OG1 
3825 C CG2 . THR A 483 ? 0.88568 0.69966 0.88007 0.13516  0.02151  0.10970  483 THR A CG2 
3826 N N   . GLN A 484 ? 0.97391 0.89756 1.03004 0.19131  -0.00598 0.11724  484 GLN A N   
3827 C CA  . GLN A 484 ? 1.00557 0.94197 1.07786 0.21546  -0.00941 0.11992  484 GLN A CA  
3828 C C   . GLN A 484 ? 1.00670 0.98373 1.09394 0.22450  -0.02360 0.12501  484 GLN A C   
3829 O O   . GLN A 484 ? 0.96850 0.94315 1.05404 0.24441  -0.03149 0.13532  484 GLN A O   
3830 C CB  . GLN A 484 ? 1.05232 1.00082 1.14555 0.21782  0.00082  0.10735  484 GLN A CB  
3831 C CG  . GLN A 484 ? 1.11788 1.02163 1.19542 0.22364  0.01142  0.10663  484 GLN A CG  
3832 C CD  . GLN A 484 ? 1.13227 1.04031 1.22415 0.22623  0.02325  0.09412  484 GLN A CD  
3833 O OE1 . GLN A 484 ? 1.10017 1.04675 1.21543 0.22270  0.02452  0.08592  484 GLN A OE1 
3834 N NE2 . GLN A 484 ? 1.25136 1.11775 1.32770 0.23204  0.03271  0.09237  484 GLN A NE2 
3835 N N   . ASN A 485 ? 1.13193 1.14579 1.23361 0.21034  -0.02738 0.11784  485 ASN A N   
3836 C CA  . ASN A 485 ? 1.08003 1.13564 1.19733 0.21647  -0.04138 0.12055  485 ASN A CA  
3837 C C   . ASN A 485 ? 1.11627 1.16519 1.20941 0.20907  -0.05163 0.12962  485 ASN A C   
3838 O O   . ASN A 485 ? 1.14038 1.21847 1.23825 0.19823  -0.05956 0.12644  485 ASN A O   
3839 C CB  . ASN A 485 ? 1.06393 1.16149 1.20893 0.20479  -0.03993 0.10773  485 ASN A CB  
3840 C CG  . ASN A 485 ? 1.07744 1.18831 1.24838 0.21562  -0.03066 0.10010  485 ASN A CG  
3841 O OD1 . ASN A 485 ? 1.13595 1.21849 1.30071 0.22891  -0.02310 0.10236  485 ASN A OD1 
3842 N ND2 . ASN A 485 ? 1.18115 1.33413 1.38023 0.20948  -0.03050 0.09082  485 ASN A ND2 
3843 N N   . GLN A 486 ? 1.07710 1.08491 1.14260 0.21487  -0.05055 0.14087  486 GLN A N   
3844 C CA  . GLN A 486 ? 1.01556 1.00757 1.05208 0.20831  -0.05717 0.15116  486 GLN A CA  
3845 C C   . GLN A 486 ? 1.06113 1.06765 1.09380 0.18454  -0.05644 0.14346  486 GLN A C   
3846 O O   . GLN A 486 ? 1.07285 1.09695 1.09758 0.18024  -0.06643 0.14634  486 GLN A O   
3847 C CB  . GLN A 486 ? 1.10309 1.11173 1.13723 0.22594  -0.07310 0.16268  486 GLN A CB  
3848 N N   . SER A 487 ? 0.99805 0.99600 1.03526 0.16942  -0.04449 0.13340  487 SER A N   
3849 C CA  . SER A 487 ? 1.03067 1.04219 1.06699 0.14862  -0.04301 0.12551  487 SER A CA  
3850 C C   . SER A 487 ? 1.07077 1.05759 1.07746 0.13850  -0.04197 0.13280  487 SER A C   
3851 O O   . SER A 487 ? 1.00726 0.96026 0.99369 0.14325  -0.03874 0.14267  487 SER A O   
3852 C CB  . SER A 487 ? 0.85983 0.86939 0.90902 0.13640  -0.03130 0.11376  487 SER A CB  
3853 O OG  . SER A 487 ? 0.95586 0.98593 1.03046 0.14568  -0.03019 0.10747  487 SER A OG  
3854 N N   . THR A 488 ? 1.05054 1.05471 1.05473 0.12431  -0.04425 0.12767  488 THR A N   
3855 C CA  . THR A 488 ? 0.93919 0.92401 0.91930 0.11132  -0.03983 0.13115  488 THR A CA  
3856 C C   . THR A 488 ? 0.92866 0.88634 0.90626 0.10170  -0.02664 0.12859  488 THR A C   
3857 O O   . THR A 488 ? 0.92650 0.89112 0.92208 0.09623  -0.02103 0.11871  488 THR A O   
3858 C CB  . THR A 488 ? 0.97142 0.98122 0.95389 0.09793  -0.04265 0.12269  488 THR A CB  
3859 O OG1 . THR A 488 ? 1.03254 1.06950 1.01812 0.10549  -0.05599 0.12361  488 THR A OG1 
3860 C CG2 . THR A 488 ? 0.88908 0.88144 0.84732 0.08604  -0.03728 0.12610  488 THR A CG2 
3861 N N   . SER A 489 ? 0.90001 0.82704 0.85465 0.09889  -0.02190 0.13767  489 SER A N   
3862 C CA  . SER A 489 ? 0.88339 0.78519 0.83486 0.08825  -0.01036 0.13550  489 SER A CA  
3863 C C   . SER A 489 ? 0.90046 0.81378 0.85443 0.07029  -0.00533 0.12774  489 SER A C   
3864 O O   . SER A 489 ? 0.87560 0.79882 0.81920 0.06526  -0.00782 0.12947  489 SER A O   
3865 C CB  . SER A 489 ? 0.89208 0.75701 0.81868 0.09044  -0.00687 0.14824  489 SER A CB  
3866 O OG  . SER A 489 ? 1.06471 0.90272 0.99195 0.08719  0.00182  0.14647  489 SER A OG  
3867 N N   . TRP A 490 ? 0.81713 0.73005 0.78475 0.06160  0.00143  0.11886  490 TRP A N   
3868 C CA  . TRP A 490 ? 0.79899 0.72230 0.77156 0.04633  0.00620  0.11160  490 TRP A CA  
3869 C C   . TRP A 490 ? 0.82496 0.72462 0.78312 0.03566  0.01426  0.11653  490 TRP A C   
3870 O O   . TRP A 490 ? 0.76929 0.64933 0.72793 0.03286  0.01935  0.11637  490 TRP A O   
3871 C CB  . TRP A 490 ? 0.71198 0.64677 0.70528 0.04279  0.00854  0.10086  490 TRP A CB  
3872 C CG  . TRP A 490 ? 0.75534 0.70498 0.75710 0.03044  0.01132  0.09306  490 TRP A CG  
3873 C CD1 . TRP A 490 ? 0.74748 0.69696 0.74137 0.02064  0.01481  0.09383  490 TRP A CD1 
3874 C CD2 . TRP A 490 ? 0.70150 0.66801 0.72131 0.02725  0.01143  0.08353  490 TRP A CD2 
3875 N NE1 . TRP A 490 ? 0.68557 0.65036 0.69242 0.01294  0.01655  0.08520  490 TRP A NE1 
3876 C CE2 . TRP A 490 ? 0.66514 0.63914 0.68684 0.01638  0.01431  0.07929  490 TRP A CE2 
3877 C CE3 . TRP A 490 ? 0.69443 0.66998 0.72856 0.03264  0.01015  0.07847  490 TRP A CE3 
3878 C CZ2 . TRP A 490 ? 0.66840 0.65575 0.70447 0.01116  0.01512  0.07102  490 TRP A CZ2 
3879 C CZ3 . TRP A 490 ? 0.71408 0.70400 0.76188 0.02588  0.01159  0.07019  490 TRP A CZ3 
3880 C CH2 . TRP A 490 ? 0.66840 0.66264 0.71635 0.01544  0.01364  0.06697  490 TRP A CH2 
3881 N N   . PRO A 491 ? 0.80339 0.70451 0.74872 0.02874  0.01614  0.12034  491 PRO A N   
3882 C CA  . PRO A 491 ? 0.82960 0.71121 0.76340 0.01733  0.02484  0.12510  491 PRO A CA  
3883 C C   . PRO A 491 ? 0.76438 0.65497 0.71350 0.00439  0.03086  0.11619  491 PRO A C   
3884 O O   . PRO A 491 ? 0.81198 0.72438 0.77656 0.00326  0.02887  0.10725  491 PRO A O   
3885 C CB  . PRO A 491 ? 0.73971 0.62489 0.65526 0.01550  0.02503  0.13148  491 PRO A CB  
3886 C CG  . PRO A 491 ? 0.89102 0.80548 0.81630 0.01887  0.01855  0.12338  491 PRO A CG  
3887 C CD  . PRO A 491 ? 0.83724 0.76081 0.78012 0.02877  0.01155  0.11816  491 PRO A CD  
3888 N N   . VAL A 492 ? 0.75487 0.62803 0.69935 -0.00582 0.03805  0.11915  492 VAL A N   
3889 C CA  . VAL A 492 ? 0.78479 0.66856 0.74403 -0.01805 0.04286  0.11177  492 VAL A CA  
3890 C C   . VAL A 492 ? 0.82728 0.73001 0.78700 -0.02376 0.04621  0.11039  492 VAL A C   
3891 O O   . VAL A 492 ? 0.83952 0.73942 0.78287 -0.02286 0.04792  0.11697  492 VAL A O   
3892 C CB  . VAL A 492 ? 0.79313 0.65565 0.74933 -0.02878 0.04884  0.11439  492 VAL A CB  
3893 C CG1 . VAL A 492 ? 0.82891 0.66581 0.77811 -0.02166 0.04656  0.11676  492 VAL A CG1 
3894 C CG2 . VAL A 492 ? 0.73760 0.59077 0.67948 -0.03733 0.05569  0.12271  492 VAL A CG2 
3895 N N   . PHE A 493 ? 0.72428 0.64571 0.70169 -0.02887 0.04731  0.10178  493 PHE A N   
3896 C CA  . PHE A 493 ? 0.78533 0.72492 0.76625 -0.03349 0.05154  0.09857  493 PHE A CA  
3897 C C   . PHE A 493 ? 0.80753 0.74384 0.78858 -0.04549 0.06054  0.10188  493 PHE A C   
3898 O O   . PHE A 493 ? 0.86075 0.79976 0.85630 -0.05265 0.06214  0.09855  493 PHE A O   
3899 C CB  . PHE A 493 ? 0.81278 0.77142 0.81290 -0.03236 0.04868  0.08854  493 PHE A CB  
3900 C CG  . PHE A 493 ? 0.80735 0.78326 0.81182 -0.03490 0.05299  0.08389  493 PHE A CG  
3901 C CD1 . PHE A 493 ? 0.76578 0.74903 0.78015 -0.04307 0.06016  0.08276  493 PHE A CD1 
3902 C CD2 . PHE A 493 ? 0.79821 0.78364 0.79779 -0.02898 0.04984  0.07989  493 PHE A CD2 
3903 C CE1 . PHE A 493 ? 0.74551 0.74417 0.76472 -0.04368 0.06514  0.07799  493 PHE A CE1 
3904 C CE2 . PHE A 493 ? 0.75563 0.75398 0.75781 -0.03085 0.05462  0.07442  493 PHE A CE2 
3905 C CZ  . PHE A 493 ? 0.78976 0.79420 0.80177 -0.03739 0.06277  0.07358  493 PHE A CZ  
3906 N N   . LYS A 494 ? 0.89597 0.82731 0.86062 -0.04828 0.06631  0.10865  494 LYS A N   
3907 C CA  . LYS A 494 ? 0.93473 0.86734 0.90028 -0.06054 0.07655  0.11168  494 LYS A CA  
3908 C C   . LYS A 494 ? 0.90473 0.86068 0.87693 -0.06184 0.08231  0.10625  494 LYS A C   
3909 O O   . LYS A 494 ? 0.89263 0.85567 0.85647 -0.05425 0.07990  0.10359  494 LYS A O   
3910 C CB  . LYS A 494 ? 0.96764 0.87796 0.90909 -0.06409 0.08145  0.12340  494 LYS A CB  
3911 C CG  . LYS A 494 ? 0.99130 0.87730 0.93016 -0.07048 0.08200  0.12864  494 LYS A CG  
3912 C CD  . LYS A 494 ? 1.20986 1.06785 1.12204 -0.06423 0.08020  0.13976  494 LYS A CD  
3913 C CE  . LYS A 494 ? 1.23100 1.05888 1.13437 -0.07330 0.08443  0.14694  494 LYS A CE  
3914 N NZ  . LYS A 494 ? 1.12661 0.92522 1.01011 -0.06151 0.07860  0.15499  494 LYS A NZ  
3915 N N   . SER A 495 ? 0.96666 0.93481 0.95419 -0.07159 0.09007  0.10420  495 SER A N   
3916 C CA  . SER A 495 ? 0.99746 0.98868 0.99519 -0.07161 0.09652  0.09797  495 SER A CA  
3917 C C   . SER A 495 ? 1.00022 0.99083 0.97644 -0.07182 0.10480  0.10194  495 SER A C   
3918 O O   . SER A 495 ? 0.98057 0.98585 0.95751 -0.06761 0.10822  0.09553  495 SER A O   
3919 C CB  . SER A 495 ? 1.15409 1.16067 1.17549 -0.08135 0.10265  0.09570  495 SER A CB  
3920 O OG  . SER A 495 ? 1.22434 1.23107 1.23924 -0.09176 0.11438  0.10192  495 SER A OG  
3921 N N   . THR A 496 ? 0.96424 0.93652 0.91955 -0.07683 0.10858  0.11233  496 THR A N   
3922 C CA  . THR A 496 ? 0.98507 0.95393 0.91451 -0.07602 0.11500  0.11718  496 THR A CA  
3923 C C   . THR A 496 ? 0.96423 0.92840 0.87656 -0.06363 0.10459  0.11573  496 THR A C   
3924 O O   . THR A 496 ? 0.88323 0.85959 0.78911 -0.05942 0.10610  0.10960  496 THR A O   
3925 C CB  . THR A 496 ? 1.10552 1.05274 1.01463 -0.08458 0.12127  0.13025  496 THR A CB  
3926 O OG1 . THR A 496 ? 1.12241 1.07066 1.05008 -0.09712 0.12731  0.13144  496 THR A OG1 
3927 C CG2 . THR A 496 ? 0.92317 0.87230 0.80880 -0.08729 0.13209  0.13468  496 THR A CG2 
3928 N N   . GLU A 497 ? 0.96770 0.91468 0.87287 -0.05772 0.09396  0.12084  497 GLU A N   
3929 C CA  . GLU A 497 ? 0.90574 0.84855 0.79321 -0.04658 0.08375  0.12191  497 GLU A CA  
3930 C C   . GLU A 497 ? 0.86035 0.81975 0.76476 -0.03917 0.07504  0.11002  497 GLU A C   
3931 O O   . GLU A 497 ? 0.80024 0.76693 0.69350 -0.03337 0.07023  0.10621  497 GLU A O   
3932 C CB  . GLU A 497 ? 0.91659 0.83630 0.79229 -0.04138 0.07600  0.13199  497 GLU A CB  
3933 C CG  . GLU A 497 ? 1.08063 0.97755 0.93913 -0.04893 0.08380  0.14470  497 GLU A CG  
3934 C CD  . GLU A 497 ? 1.22618 1.09867 1.08336 -0.04486 0.07744  0.15151  497 GLU A CD  
3935 O OE1 . GLU A 497 ? 0.88441 0.76034 0.75951 -0.03844 0.06922  0.14500  497 GLU A OE1 
3936 O OE2 . GLU A 497 ? 1.42612 1.27421 1.26303 -0.04844 0.08179  0.16355  497 GLU A OE2 
3937 N N   . GLN A 498 ? 0.85199 0.81636 0.78159 -0.03999 0.07259  0.10428  498 GLN A N   
3938 C CA  . GLN A 498 ? 0.77877 0.75687 0.72495 -0.03429 0.06535  0.09373  498 GLN A CA  
3939 C C   . GLN A 498 ? 0.75055 0.72621 0.68694 -0.02480 0.05381  0.09431  498 GLN A C   
3940 O O   . GLN A 498 ? 0.78352 0.77083 0.71891 -0.02113 0.04945  0.08719  498 GLN A O   
3941 C CB  . GLN A 498 ? 0.85318 0.84821 0.80503 -0.03593 0.07127  0.08447  498 GLN A CB  
3942 C CG  . GLN A 498 ? 0.85883 0.86258 0.82786 -0.04343 0.08182  0.08225  498 GLN A CG  
3943 C CD  . GLN A 498 ? 0.87934 0.89732 0.84875 -0.04358 0.09024  0.07463  498 GLN A CD  
3944 O OE1 . GLN A 498 ? 0.96587 0.99131 0.94078 -0.03856 0.08685  0.06543  498 GLN A OE1 
3945 N NE2 . GLN A 498 ? 0.96961 0.99032 0.93261 -0.04966 0.10215  0.07827  498 GLN A NE2 
3946 N N   . LYS A 499 ? 0.77441 0.73484 0.70396 -0.02082 0.04887  0.10266  499 LYS A N   
3947 C CA  . LYS A 499 ? 0.74084 0.70160 0.66649 -0.01056 0.03743  0.10354  499 LYS A CA  
3948 C C   . LYS A 499 ? 0.73786 0.70798 0.68700 -0.00781 0.03220  0.09520  499 LYS A C   
3949 O O   . LYS A 499 ? 0.68350 0.64917 0.64674 -0.01176 0.03563  0.09369  499 LYS A O   
3950 C CB  . LYS A 499 ? 0.72595 0.66594 0.63739 -0.00536 0.03463  0.11555  499 LYS A CB  
3951 C CG  . LYS A 499 ? 0.82120 0.74682 0.70742 -0.00902 0.04069  0.12611  499 LYS A CG  
3952 C CD  . LYS A 499 ? 0.76645 0.67092 0.63616 -0.00055 0.03521  0.13831  499 LYS A CD  
3953 C CE  . LYS A 499 ? 0.81368 0.69753 0.65793 -0.00619 0.04309  0.15060  499 LYS A CE  
3954 N NZ  . LYS A 499 ? 0.79342 0.65094 0.62353 0.00210  0.03867  0.16295  499 LYS A NZ  
3955 N N   . TYR A 500 ? 0.74261 0.72587 0.69483 -0.00176 0.02373  0.08999  500 TYR A N   
3956 C CA  . TYR A 500 ? 0.68405 0.67705 0.65670 0.00087  0.01874  0.08272  500 TYR A CA  
3957 C C   . TYR A 500 ? 0.72640 0.72614 0.69749 0.01035  0.00828  0.08424  500 TYR A C   
3958 O O   . TYR A 500 ? 0.72525 0.72667 0.67992 0.01436  0.00337  0.08862  500 TYR A O   
3959 C CB  . TYR A 500 ? 0.69008 0.69741 0.67463 -0.00439 0.02066  0.07169  500 TYR A CB  
3960 C CG  . TYR A 500 ? 0.73011 0.74847 0.70409 -0.00453 0.01760  0.06655  500 TYR A CG  
3961 C CD1 . TYR A 500 ? 0.67497 0.69103 0.63240 -0.00817 0.02367  0.06736  500 TYR A CD1 
3962 C CD2 . TYR A 500 ? 0.67278 0.70419 0.65292 -0.00195 0.00912  0.06019  500 TYR A CD2 
3963 C CE1 . TYR A 500 ? 0.66825 0.69278 0.61338 -0.00877 0.02121  0.06133  500 TYR A CE1 
3964 C CE2 . TYR A 500 ? 0.69715 0.73766 0.66641 -0.00355 0.00571  0.05429  500 TYR A CE2 
3965 C CZ  . TYR A 500 ? 0.75049 0.78659 0.70118 -0.00672 0.01165  0.05450  500 TYR A CZ  
3966 O OH  . TYR A 500 ? 0.69457 0.73823 0.63168 -0.00860 0.00837  0.04747  500 TYR A OH  
3967 N N   . LEU A 501 ? 0.69148 0.69680 0.68015 0.01385  0.00490  0.08051  501 LEU A N   
3968 C CA  . LEU A 501 ? 0.74442 0.76070 0.73829 0.02305  -0.00441 0.08089  501 LEU A CA  
3969 C C   . LEU A 501 ? 0.73102 0.76897 0.73823 0.01969  -0.00859 0.07038  501 LEU A C   
3970 O O   . LEU A 501 ? 0.75350 0.79399 0.77342 0.01305  -0.00392 0.06325  501 LEU A O   
3971 C CB  . LEU A 501 ? 0.69125 0.69913 0.69590 0.02933  -0.00372 0.08353  501 LEU A CB  
3972 C CG  . LEU A 501 ? 0.76611 0.78538 0.77908 0.04103  -0.01190 0.08490  501 LEU A CG  
3973 C CD1 . LEU A 501 ? 0.70824 0.71844 0.70348 0.05035  -0.01707 0.09560  501 LEU A CD1 
3974 C CD2 . LEU A 501 ? 0.71023 0.72382 0.73740 0.04547  -0.00847 0.08353  501 LEU A CD2 
3975 N N   . THR A 502 ? 0.70753 0.76037 0.71096 0.02359  -0.01769 0.06960  502 THR A N   
3976 C CA  . THR A 502 ? 0.76223 0.83564 0.77951 0.01964  -0.02245 0.05954  502 THR A CA  
3977 C C   . THR A 502 ? 0.70291 0.78953 0.73937 0.02648  -0.02753 0.05936  502 THR A C   
3978 O O   . THR A 502 ? 0.80128 0.88750 0.83594 0.03726  -0.03225 0.06706  502 THR A O   
3979 C CB  . THR A 502 ? 0.75160 0.83668 0.75514 0.01787  -0.03004 0.05672  502 THR A CB  
3980 O OG1 . THR A 502 ? 0.79814 0.89125 0.79590 0.02793  -0.04034 0.06400  502 THR A OG1 
3981 C CG2 . THR A 502 ? 0.73118 0.80248 0.71324 0.01293  -0.02368 0.05798  502 THR A CG2 
3982 N N   . LEU A 503 ? 0.65704 0.75449 0.71176 0.02055  -0.02568 0.05089  503 LEU A N   
3983 C CA  . LEU A 503 ? 0.68374 0.79622 0.75906 0.02509  -0.02810 0.04920  503 LEU A CA  
3984 C C   . LEU A 503 ? 0.68012 0.81781 0.76638 0.01991  -0.03542 0.04127  503 LEU A C   
3985 O O   . LEU A 503 ? 0.66244 0.80116 0.75025 0.00877  -0.03285 0.03323  503 LEU A O   
3986 C CB  . LEU A 503 ? 0.66423 0.76769 0.75118 0.02107  -0.01869 0.04639  503 LEU A CB  
3987 C CG  . LEU A 503 ? 0.68283 0.76164 0.75998 0.02333  -0.01148 0.05242  503 LEU A CG  
3988 C CD1 . LEU A 503 ? 0.51991 0.59223 0.60662 0.01708  -0.00371 0.04817  503 LEU A CD1 
3989 C CD2 . LEU A 503 ? 0.60515 0.67956 0.68093 0.03632  -0.01395 0.06005  503 LEU A CD2 
3990 N N   . ASN A 504 ? 0.77307 0.93090 0.86777 0.02793  -0.04456 0.04341  504 ASN A N   
3991 C CA  . ASN A 504 ? 0.76292 0.94831 0.87033 0.02222  -0.05274 0.03574  504 ASN A CA  
3992 C C   . ASN A 504 ? 0.78786 0.99656 0.91168 0.03425  -0.06075 0.03983  504 ASN A C   
3993 O O   . ASN A 504 ? 0.81221 1.01202 0.93525 0.04736  -0.05925 0.04829  504 ASN A O   
3994 C CB  . ASN A 504 ? 0.73246 0.91929 0.82087 0.01608  -0.05974 0.03259  504 ASN A CB  
3995 C CG  . ASN A 504 ? 0.88927 1.06909 0.95696 0.02670  -0.06593 0.04257  504 ASN A CG  
3996 O OD1 . ASN A 504 ? 0.90877 1.10634 0.97989 0.03593  -0.07686 0.04708  504 ASN A OD1 
3997 N ND2 . ASN A 504 ? 0.92406 1.07823 0.97030 0.02572  -0.05885 0.04679  504 ASN A ND2 
3998 N N   . THR A 505 ? 0.78060 1.01949 0.92001 0.02989  -0.06935 0.03353  505 THR A N   
3999 C CA  . THR A 505 ? 0.82236 1.08830 0.98250 0.04173  -0.07663 0.03683  505 THR A CA  
4000 C C   . THR A 505 ? 0.90561 1.18083 1.05409 0.05371  -0.09069 0.04461  505 THR A C   
4001 O O   . THR A 505 ? 0.90039 1.19136 1.06257 0.06874  -0.09621 0.05076  505 THR A O   
4002 C CB  . THR A 505 ? 0.74676 1.04623 0.93410 0.03182  -0.07964 0.02705  505 THR A CB  
4003 O OG1 . THR A 505 ? 0.72660 1.03783 0.90576 0.02021  -0.08952 0.02037  505 THR A OG1 
4004 C CG2 . THR A 505 ? 0.59178 0.88281 0.79106 0.02059  -0.06560 0.02063  505 THR A CG2 
4005 N N   . GLU A 506 ? 0.87996 1.14627 1.00320 0.04835  -0.09661 0.04470  506 GLU A N   
4006 C CA  . GLU A 506 ? 0.99116 1.26769 1.10099 0.05913  -0.11125 0.05249  506 GLU A CA  
4007 C C   . GLU A 506 ? 1.05125 1.29759 1.13894 0.07278  -0.10777 0.06607  506 GLU A C   
4008 O O   . GLU A 506 ? 1.13365 1.38308 1.22844 0.08951  -0.11154 0.07535  506 GLU A O   
4009 C CB  . GLU A 506 ? 1.02346 1.30674 1.11481 0.04667  -0.12001 0.04565  506 GLU A CB  
4010 C CG  . GLU A 506 ? 1.10736 1.35951 1.17295 0.03559  -0.10962 0.04229  506 GLU A CG  
4011 C CD  . GLU A 506 ? 1.27795 1.53751 1.34252 0.01756  -0.11017 0.02796  506 GLU A CD  
4012 O OE1 . GLU A 506 ? 1.34130 1.63059 1.42125 0.01219  -0.12077 0.02083  506 GLU A OE1 
4013 O OE2 . GLU A 506 ? 1.32873 1.56420 1.37800 0.00868  -0.09971 0.02355  506 GLU A OE2 
4014 N N   . SER A 507 ? 1.07665 1.29318 1.13832 0.06569  -0.09979 0.06721  507 SER A N   
4015 C CA  . SER A 507 ? 1.09259 1.28055 1.12899 0.07511  -0.09721 0.07989  507 SER A CA  
4016 C C   . SER A 507 ? 1.06011 1.21765 1.08778 0.06664  -0.08115 0.07854  507 SER A C   
4017 O O   . SER A 507 ? 1.04672 1.20083 1.06913 0.05279  -0.07576 0.06993  507 SER A O   
4018 C CB  . SER A 507 ? 1.15876 1.34601 1.16569 0.07502  -0.10727 0.08450  507 SER A CB  
4019 O OG  . SER A 507 ? 1.20024 1.37398 1.18956 0.06001  -0.09966 0.07733  507 SER A OG  
4020 N N   . THR A 508 ? 1.01092 1.14667 1.03729 0.07518  -0.07392 0.08678  508 THR A N   
4021 C CA  . THR A 508 ? 0.99310 1.10124 1.01232 0.06785  -0.05985 0.08652  508 THR A CA  
4022 C C   . THR A 508 ? 0.95926 1.04265 0.94800 0.06851  -0.05774 0.09634  508 THR A C   
4023 O O   . THR A 508 ? 0.95444 1.02546 0.93192 0.08036  -0.06112 0.10795  508 THR A O   
4024 C CB  . THR A 508 ? 0.95062 1.04984 0.98658 0.07474  -0.05293 0.08805  508 THR A CB  
4025 O OG1 . THR A 508 ? 1.03845 1.15846 1.10012 0.06924  -0.05119 0.07738  508 THR A OG1 
4026 C CG2 . THR A 508 ? 0.91806 0.98661 0.94258 0.06956  -0.04093 0.09076  508 THR A CG2 
4027 N N   . ARG A 509 ? 0.90023 0.97624 0.87535 0.05614  -0.05175 0.09195  509 ARG A N   
4028 C CA  . ARG A 509 ? 0.92724 0.98370 0.87301 0.05508  -0.04901 0.10049  509 ARG A CA  
4029 C C   . ARG A 509 ? 0.88522 0.92022 0.82656 0.04556  -0.03452 0.09986  509 ARG A C   
4030 O O   . ARG A 509 ? 0.84728 0.88494 0.80577 0.03803  -0.02770 0.09101  509 ARG A O   
4031 C CB  . ARG A 509 ? 0.91263 0.98177 0.84062 0.04998  -0.05571 0.09686  509 ARG A CB  
4032 C CG  . ARG A 509 ? 1.04424 1.14236 0.98341 0.05352  -0.06993 0.09153  509 ARG A CG  
4033 C CD  . ARG A 509 ? 1.12569 1.23412 1.04814 0.04422  -0.07414 0.08375  509 ARG A CD  
4034 N NE  . ARG A 509 ? 1.28720 1.39487 1.21873 0.03097  -0.06418 0.07066  509 ARG A NE  
4035 C CZ  . ARG A 509 ? 1.18359 1.30593 1.14046 0.02554  -0.06436 0.05977  509 ARG A CZ  
4036 N NH1 . ARG A 509 ? 1.19993 1.34292 1.17786 0.03081  -0.07362 0.05889  509 ARG A NH1 
4037 N NH2 . ARG A 509 ? 0.99674 1.11309 0.95815 0.01475  -0.05462 0.04985  509 ARG A NH2 
4038 N N   . ILE A 510 ? 0.89383 0.90795 0.81155 0.04594  -0.03021 0.11012  510 ILE A N   
4039 C CA  . ILE A 510 ? 0.77594 0.77267 0.68693 0.03584  -0.01694 0.11043  510 ILE A CA  
4040 C C   . ILE A 510 ? 0.79621 0.79860 0.69036 0.02749  -0.01405 0.10630  510 ILE A C   
4041 O O   . ILE A 510 ? 0.81735 0.82024 0.68855 0.03061  -0.01973 0.11186  510 ILE A O   
4042 C CB  . ILE A 510 ? 0.80218 0.77146 0.69774 0.03904  -0.01191 0.12382  510 ILE A CB  
4043 C CG1 . ILE A 510 ? 0.82327 0.78427 0.73275 0.04900  -0.01479 0.12743  510 ILE A CG1 
4044 C CG2 . ILE A 510 ? 0.73140 0.68779 0.62595 0.02645  0.00202  0.12239  510 ILE A CG2 
4045 C CD1 . ILE A 510 ? 0.80093 0.77298 0.73826 0.04560  -0.01205 0.11611  510 ILE A CD1 
4046 N N   . MET A 511 ? 0.79869 0.80393 0.70282 0.01751  -0.00477 0.09703  511 MET A N   
4047 C CA  . MET A 511 ? 0.72902 0.73839 0.62074 0.00943  0.00126  0.09098  511 MET A CA  
4048 C C   . MET A 511 ? 0.75977 0.75773 0.65397 0.00159  0.01550  0.09184  511 MET A C   
4049 O O   . MET A 511 ? 0.78486 0.77302 0.69156 0.00117  0.01932  0.09570  511 MET A O   
4050 C CB  . MET A 511 ? 0.78172 0.80926 0.68767 0.00592  -0.00208 0.07666  511 MET A CB  
4051 C CG  . MET A 511 ? 0.82133 0.86388 0.73516 0.01187  -0.01574 0.07428  511 MET A CG  
4052 S SD  . MET A 511 ? 1.09250 1.14283 0.97691 0.01317  -0.02505 0.07505  511 MET A SD  
4053 C CE  . MET A 511 ? 0.94966 1.01879 0.84829 0.00543  -0.02849 0.05690  511 MET A CE  
4054 N N   . THR A 512 ? 0.72409 0.72496 0.60764 -0.00491 0.02349  0.08707  512 THR A N   
4055 C CA  . THR A 512 ? 0.70515 0.69975 0.59192 -0.01239 0.03743  0.08777  512 THR A CA  
4056 C C   . THR A 512 ? 0.73340 0.73982 0.62877 -0.01721 0.04414  0.07510  512 THR A C   
4057 O O   . THR A 512 ? 0.66453 0.67856 0.54881 -0.01666 0.04113  0.06774  512 THR A O   
4058 C CB  . THR A 512 ? 0.80453 0.78660 0.66438 -0.01507 0.04451  0.09867  512 THR A CB  
4059 O OG1 . THR A 512 ? 0.75704 0.74474 0.59306 -0.01457 0.04297  0.09597  512 THR A OG1 
4060 C CG2 . THR A 512 ? 0.66942 0.63415 0.51864 -0.00984 0.03904  0.11287  512 THR A CG2 
4061 N N   . LYS A 513 ? 0.69142 0.69873 0.60625 -0.02170 0.05290  0.07250  513 LYS A N   
4062 C CA  . LYS A 513 ? 0.59823 0.61443 0.52138 -0.02539 0.06219  0.06276  513 LYS A CA  
4063 C C   . LYS A 513 ? 0.67189 0.69649 0.60176 -0.02294 0.05624  0.05054  513 LYS A C   
4064 O O   . LYS A 513 ? 0.75711 0.78527 0.67421 -0.02354 0.05901  0.04298  513 LYS A O   
4065 C CB  . LYS A 513 ? 0.73601 0.75138 0.63727 -0.02883 0.07284  0.06454  513 LYS A CB  
4066 C CG  . LYS A 513 ? 0.76792 0.77614 0.66671 -0.03419 0.08240  0.07539  513 LYS A CG  
4067 C CD  . LYS A 513 ? 0.76043 0.76608 0.63199 -0.03753 0.09197  0.07926  513 LYS A CD  
4068 C CE  . LYS A 513 ? 0.75609 0.75428 0.62613 -0.04478 0.10231  0.09035  513 LYS A CE  
4069 N NZ  . LYS A 513 ? 0.84868 0.84544 0.69302 -0.04959 0.11471  0.09429  513 LYS A NZ  
4070 N N   . LEU A 514 ? 0.66782 0.69424 0.61677 -0.02092 0.04867  0.04839  514 LEU A N   
4071 C CA  . LEU A 514 ? 0.75549 0.78833 0.71232 -0.02007 0.04295  0.03757  514 LEU A CA  
4072 C C   . LEU A 514 ? 0.76060 0.79576 0.72376 -0.02210 0.05178  0.02758  514 LEU A C   
4073 O O   . LEU A 514 ? 0.71217 0.74752 0.68921 -0.02297 0.05976  0.02868  514 LEU A O   
4074 C CB  . LEU A 514 ? 0.73256 0.76635 0.70998 -0.01853 0.03610  0.03822  514 LEU A CB  
4075 C CG  . LEU A 514 ? 0.72069 0.75954 0.71065 -0.01941 0.03200  0.02809  514 LEU A CG  
4076 C CD1 . LEU A 514 ? 0.73739 0.78242 0.71580 -0.01882 0.02248  0.02464  514 LEU A CD1 
4077 C CD2 . LEU A 514 ? 0.64015 0.67853 0.65049 -0.01883 0.02920  0.03016  514 LEU A CD2 
4078 N N   . ARG A 515 ? 0.74482 0.78177 0.69775 -0.02263 0.04997  0.01754  515 ARG A N   
4079 C CA  A ARG A 515 ? 0.80215 0.83828 0.75953 -0.02325 0.05768  0.00634  515 ARG A CA  
4080 C CA  B ARG A 515 ? 0.80226 0.83841 0.76087 -0.02320 0.05772  0.00660  515 ARG A CA  
4081 C C   . ARG A 515 ? 0.80739 0.84413 0.76368 -0.02291 0.07152  0.00794  515 ARG A C   
4082 O O   . ARG A 515 ? 0.77336 0.81100 0.74443 -0.02134 0.07919  0.00275  515 ARG A O   
4083 C CB  A ARG A 515 ? 0.77669 0.81168 0.75789 -0.02281 0.05514  0.00214  515 ARG A CB  
4084 C CB  B ARG A 515 ? 0.77637 0.81153 0.75994 -0.02259 0.05574  0.00358  515 ARG A CB  
4085 C CG  A ARG A 515 ? 0.81449 0.85016 0.79706 -0.02477 0.04394  -0.00289 515 ARG A CG  
4086 C CG  B ARG A 515 ? 0.80865 0.84216 0.79391 -0.02444 0.04827  -0.00560 515 ARG A CG  
4087 C CD  A ARG A 515 ? 0.77251 0.80293 0.75441 -0.02690 0.04569  -0.01605 515 ARG A CD  
4088 C CD  B ARG A 515 ? 0.81844 0.85731 0.79509 -0.02588 0.03652  -0.00307 515 ARG A CD  
4089 N NE  A ARG A 515 ? 0.83772 0.87072 0.80729 -0.03103 0.03663  -0.02268 515 ARG A NE  
4090 N NE  B ARG A 515 ? 0.80485 0.84597 0.79590 -0.02798 0.02871  -0.00610 515 ARG A NE  
4091 C CZ  A ARG A 515 ? 0.87194 0.89911 0.83520 -0.03487 0.03683  -0.03524 515 ARG A CZ  
4092 C CZ  B ARG A 515 ? 0.80407 0.84171 0.79862 -0.03179 0.02807  -0.01653 515 ARG A CZ  
4093 N NH1 A ARG A 515 ? 0.79720 0.81351 0.76500 -0.03359 0.04616  -0.04239 515 ARG A NH1 
4094 N NH1 B ARG A 515 ? 0.84380 0.87377 0.82919 -0.03275 0.03485  -0.02575 515 ARG A NH1 
4095 N NH2 A ARG A 515 ? 0.85381 0.88602 0.80604 -0.03999 0.02717  -0.04094 515 ARG A NH2 
4096 N NH2 B ARG A 515 ? 0.72370 0.76470 0.73088 -0.03494 0.02128  -0.01797 515 ARG A NH2 
4097 N N   . ALA A 516 ? 0.76944 0.80619 0.70791 -0.02421 0.07500  0.01556  516 ALA A N   
4098 C CA  . ALA A 516 ? 0.84670 0.88614 0.78423 -0.02541 0.08904  0.01846  516 ALA A CA  
4099 C C   . ALA A 516 ? 0.87253 0.91461 0.81069 -0.02364 0.10007  0.00649  516 ALA A C   
4100 O O   . ALA A 516 ? 0.83546 0.88354 0.79179 -0.02232 0.11005  0.00584  516 ALA A O   
4101 C CB  . ALA A 516 ? 0.73918 0.77552 0.65011 -0.02793 0.09118  0.02720  516 ALA A CB  
4102 N N   . GLN A 517 ? 0.89759 0.93559 0.81565 -0.02337 0.09858  -0.00336 517 GLN A N   
4103 C CA  . GLN A 517 ? 0.96666 1.00414 0.88172 -0.02108 0.11033  -0.01568 517 GLN A CA  
4104 C C   . GLN A 517 ? 0.87037 0.90627 0.81196 -0.01700 0.11052  -0.02287 517 GLN A C   
4105 O O   . GLN A 517 ? 0.82357 0.86315 0.77884 -0.01282 0.12219  -0.02667 517 GLN A O   
4106 C CB  . GLN A 517 ? 1.08828 1.11943 0.97276 -0.02286 0.10748  -0.02552 517 GLN A CB  
4107 C CG  . GLN A 517 ? 1.15502 1.18719 1.00997 -0.02496 0.11636  -0.02318 517 GLN A CG  
4108 C CD  . GLN A 517 ? 1.36561 1.39205 1.19693 -0.02488 0.12282  -0.03854 517 GLN A CD  
4109 O OE1 . GLN A 517 ? 1.33153 1.35255 1.17276 -0.02241 0.12438  -0.05135 517 GLN A OE1 
4110 N NE2 . GLN A 517 ? 1.37511 1.40064 1.17303 -0.02771 0.12690  -0.03740 517 GLN A NE2 
4111 N N   . GLN A 518 ? 0.80266 0.83365 0.75212 -0.01785 0.09782  -0.02404 518 GLN A N   
4112 C CA  . GLN A 518 ? 0.77173 0.79836 0.74352 -0.01463 0.09690  -0.02928 518 GLN A CA  
4113 C C   . GLN A 518 ? 0.76474 0.79892 0.76303 -0.01142 0.10092  -0.02089 518 GLN A C   
4114 O O   . GLN A 518 ? 0.78785 0.82197 0.80218 -0.00608 0.10763  -0.02524 518 GLN A O   
4115 C CB  . GLN A 518 ? 0.85006 0.87154 0.82352 -0.01808 0.08272  -0.03018 518 GLN A CB  
4116 C CG  . GLN A 518 ? 0.82696 0.84319 0.77668 -0.02231 0.07731  -0.03998 518 GLN A CG  
4117 C CD  . GLN A 518 ? 0.85918 0.88217 0.79074 -0.02568 0.06887  -0.03311 518 GLN A CD  
4118 O OE1 . GLN A 518 ? 0.89464 0.92273 0.82038 -0.02457 0.07258  -0.02342 518 GLN A OE1 
4119 N NE2 . GLN A 518 ? 0.88869 0.91187 0.81190 -0.02989 0.05718  -0.03765 518 GLN A NE2 
4120 N N   . CYS A 519 ? 0.76754 0.80800 0.77044 -0.01436 0.09673  -0.00899 519 CYS A N   
4121 C CA  . CYS A 519 ? 0.70159 0.74909 0.72931 -0.01298 0.09819  -0.00174 519 CYS A CA  
4122 C C   . CYS A 519 ? 0.74804 0.80650 0.78344 -0.01118 0.11166  -0.00093 519 CYS A C   
4123 O O   . CYS A 519 ? 0.83054 0.89691 0.88959 -0.00820 0.11422  0.00105  519 CYS A O   
4124 C CB  . CYS A 519 ? 0.59937 0.64750 0.62866 -0.01730 0.08950  0.00933  519 CYS A CB  
4125 S SG  . CYS A 519 ? 0.78774 0.82768 0.81978 -0.01786 0.07488  0.00838  519 CYS A SG  
4126 N N   . ARG A 520 ? 0.73011 0.79060 0.74631 -0.01285 0.12054  -0.00258 520 ARG A N   
4127 C CA  . ARG A 520 ? 0.82828 0.90109 0.85291 -0.01097 0.13555  -0.00346 520 ARG A CA  
4128 C C   . ARG A 520 ? 0.80630 0.87981 0.84483 -0.00228 0.14203  -0.01424 520 ARG A C   
4129 O O   . ARG A 520 ? 0.78630 0.87297 0.84838 0.00202  0.14951  -0.01334 520 ARG A O   
4130 C CB  . ARG A 520 ? 0.79566 0.86869 0.79294 -0.01472 0.14483  -0.00365 520 ARG A CB  
4131 C CG  . ARG A 520 ? 0.97423 1.05655 0.97219 -0.02129 0.15114  0.00788  520 ARG A CG  
4132 C CD  . ARG A 520 ? 1.06316 1.14188 1.02827 -0.02545 0.15915  0.00894  520 ARG A CD  
4133 N NE  . ARG A 520 ? 1.14035 1.20799 1.08396 -0.03060 0.14852  0.01849  520 ARG A NE  
4134 C CZ  . ARG A 520 ? 1.11515 1.17259 1.02788 -0.03083 0.14324  0.01650  520 ARG A CZ  
4135 N NH1 . ARG A 520 ? 1.04633 1.10148 0.94368 -0.02766 0.14713  0.00420  520 ARG A NH1 
4136 N NH2 . ARG A 520 ? 1.12164 1.17068 1.01808 -0.03404 0.13350  0.02690  520 ARG A NH2 
4137 N N   . PHE A 521 ? 0.82261 0.88177 0.84764 0.00047  0.13871  -0.02449 521 PHE A N   
4138 C CA  . PHE A 521 ? 0.80242 0.85677 0.83925 0.00928  0.14415  -0.03470 521 PHE A CA  
4139 C C   . PHE A 521 ? 0.80368 0.86051 0.86979 0.01361  0.13738  -0.02957 521 PHE A C   
4140 O O   . PHE A 521 ? 0.76874 0.83489 0.85634 0.02137  0.14457  -0.03025 521 PHE A O   
4141 C CB  . PHE A 521 ? 0.79340 0.82853 0.80851 0.00896  0.14032  -0.04655 521 PHE A CB  
4142 C CG  . PHE A 521 ? 0.86670 0.89013 0.89338 0.01737  0.14321  -0.05617 521 PHE A CG  
4143 C CD1 . PHE A 521 ? 0.74482 0.76725 0.77073 0.02559  0.15800  -0.06626 521 PHE A CD1 
4144 C CD2 . PHE A 521 ? 0.79949 0.81181 0.83738 0.01754  0.13204  -0.05480 521 PHE A CD2 
4145 C CE1 . PHE A 521 ? 0.77405 0.78286 0.81024 0.03472  0.16091  -0.07460 521 PHE A CE1 
4146 C CE2 . PHE A 521 ? 0.83235 0.83057 0.87945 0.02552  0.13492  -0.06241 521 PHE A CE2 
4147 C CZ  . PHE A 521 ? 0.81193 0.80750 0.85818 0.03461  0.14910  -0.07228 521 PHE A CZ  
4148 N N   . TRP A 522 ? 0.78001 0.82984 0.84729 0.00905  0.12353  -0.02404 522 TRP A N   
4149 C CA  . TRP A 522 ? 0.78497 0.83373 0.87501 0.01287  0.11655  -0.01998 522 TRP A CA  
4150 C C   . TRP A 522 ? 0.87223 0.93960 0.98473 0.01309  0.11742  -0.01005 522 TRP A C   
4151 O O   . TRP A 522 ? 0.83549 0.90744 0.96958 0.01946  0.11622  -0.00824 522 TRP A O   
4152 C CB  . TRP A 522 ? 0.78605 0.82324 0.86984 0.00712  0.10291  -0.01709 522 TRP A CB  
4153 C CG  . TRP A 522 ? 0.77125 0.79084 0.83982 0.00647  0.10039  -0.02719 522 TRP A CG  
4154 C CD1 . TRP A 522 ? 0.76777 0.78161 0.81558 -0.00042 0.09508  -0.03060 522 TRP A CD1 
4155 C CD2 . TRP A 522 ? 0.76454 0.76970 0.83755 0.01234  0.10260  -0.03517 522 TRP A CD2 
4156 N NE1 . TRP A 522 ? 0.74971 0.74790 0.78931 -0.00072 0.09387  -0.04100 522 TRP A NE1 
4157 C CE2 . TRP A 522 ? 0.77748 0.76790 0.83133 0.00691  0.09892  -0.04398 522 TRP A CE2 
4158 C CE3 . TRP A 522 ? 0.75371 0.75652 0.84497 0.02197  0.10703  -0.03551 522 TRP A CE3 
4159 C CZ2 . TRP A 522 ? 0.77428 0.74515 0.82563 0.00936  0.10032  -0.05350 522 TRP A CZ2 
4160 C CZ3 . TRP A 522 ? 0.75466 0.73698 0.84288 0.02631  0.10845  -0.04409 522 TRP A CZ3 
4161 C CH2 . TRP A 522 ? 0.80560 0.77088 0.87348 0.01937  0.10555  -0.05322 522 TRP A CH2 
4162 N N   . THR A 523 ? 0.89442 0.97190 1.00171 0.00580  0.11880  -0.00327 523 THR A N   
4163 C CA  . THR A 523 ? 0.85974 0.95277 0.98651 0.00273  0.11744  0.00620  523 THR A CA  
4164 C C   . THR A 523 ? 0.88328 0.99607 1.02330 0.00462  0.13062  0.00609  523 THR A C   
4165 O O   . THR A 523 ? 0.86296 0.99196 1.02754 0.00539  0.13022  0.01095  523 THR A O   
4166 C CB  . THR A 523 ? 0.83236 0.92192 0.94665 -0.00721 0.11062  0.01436  523 THR A CB  
4167 O OG1 . THR A 523 ? 0.79200 0.86633 0.89722 -0.00793 0.09917  0.01390  523 THR A OG1 
4168 C CG2 . THR A 523 ? 0.83460 0.93641 0.96694 -0.01217 0.10798  0.02323  523 THR A CG2 
4169 N N   . SER A 524 ? 1.02399 1.13715 1.14879 0.00541  0.14245  0.00014  524 SER A N   
4170 C CA  . SER A 524 ? 0.96496 1.09808 1.10234 0.00782  0.15751  -0.00127 524 SER A CA  
4171 C C   . SER A 524 ? 1.05130 1.18600 1.20023 0.02104  0.16545  -0.01136 524 SER A C   
4172 O O   . SER A 524 ? 1.17441 1.32679 1.35218 0.02784  0.16879  -0.01025 524 SER A O   
4173 C CB  . SER A 524 ? 1.06630 1.19940 1.17870 0.00089  0.16800  -0.00139 524 SER A CB  
4174 O OG  . SER A 524 ? 1.28678 1.41868 1.39061 -0.01040 0.16238  0.00917  524 SER A OG  
4175 N N   . PHE A 525 ? 0.95181 1.06814 1.07868 0.02506  0.16837  -0.02151 525 PHE A N   
4176 C CA  . PHE A 525 ? 0.97513 1.09018 1.10895 0.03772  0.17908  -0.03246 525 PHE A CA  
4177 C C   . PHE A 525 ? 0.99689 1.10332 1.14990 0.04739  0.17020  -0.03319 525 PHE A C   
4178 O O   . PHE A 525 ? 0.93027 1.05166 1.11120 0.05724  0.17410  -0.03202 525 PHE A O   
4179 C CB  . PHE A 525 ? 0.94790 1.04381 1.04853 0.03729  0.18512  -0.04409 525 PHE A CB  
4180 C CG  . PHE A 525 ? 0.97093 1.05749 1.07362 0.05014  0.19500  -0.05722 525 PHE A CG  
4181 C CD1 . PHE A 525 ? 1.05928 1.12413 1.13200 0.04971  0.19814  -0.06954 525 PHE A CD1 
4182 C CD2 . PHE A 525 ? 1.03335 1.13335 1.16733 0.06294  0.20177  -0.05773 525 PHE A CD2 
4183 C CE1 . PHE A 525 ? 1.05508 1.10754 1.12744 0.06140  0.20803  -0.08278 525 PHE A CE1 
4184 C CE2 . PHE A 525 ? 1.00490 1.09391 1.14029 0.07625  0.21146  -0.06980 525 PHE A CE2 
4185 C CZ  . PHE A 525 ? 1.06124 1.12460 1.16466 0.07527  0.21519  -0.08283 525 PHE A CZ  
4186 N N   . PHE A 526 ? 0.96744 1.04990 1.10528 0.04488  0.15852  -0.03508 526 PHE A N   
4187 C CA  . PHE A 526 ? 0.95604 1.02226 1.10324 0.05324  0.15164  -0.03747 526 PHE A CA  
4188 C C   . PHE A 526 ? 0.91973 1.00084 1.09892 0.06026  0.14662  -0.02857 526 PHE A C   
4189 O O   . PHE A 526 ? 0.89622 0.97016 1.08828 0.07259  0.14757  -0.03147 526 PHE A O   
4190 C CB  . PHE A 526 ? 0.84384 0.88787 0.97264 0.04492  0.13827  -0.03711 526 PHE A CB  
4191 C CG  . PHE A 526 ? 0.85273 0.87565 0.98608 0.05189  0.13314  -0.04045 526 PHE A CG  
4192 C CD1 . PHE A 526 ? 0.78392 0.78723 0.90685 0.05876  0.14078  -0.05291 526 PHE A CD1 
4193 C CD2 . PHE A 526 ? 0.80249 0.82348 0.94914 0.05149  0.12144  -0.03116 526 PHE A CD2 
4194 C CE1 . PHE A 526 ? 0.80549 0.78645 0.93176 0.06482  0.13683  -0.05526 526 PHE A CE1 
4195 C CE2 . PHE A 526 ? 0.74785 0.74781 0.89703 0.05759  0.11745  -0.03293 526 PHE A CE2 
4196 C CZ  . PHE A 526 ? 0.81158 0.79083 0.95094 0.06418  0.12514  -0.04460 526 PHE A CZ  
4197 N N   . PRO A 527 ? 0.89921 0.99955 1.09103 0.05302  0.14057  -0.01772 527 PRO A N   
4198 C CA  . PRO A 527 ? 0.88718 1.00437 1.10920 0.05939  0.13533  -0.01002 527 PRO A CA  
4199 C C   . PRO A 527 ? 0.95505 1.09141 1.20088 0.07281  0.14713  -0.01357 527 PRO A C   
4200 O O   . PRO A 527 ? 0.94638 1.09303 1.21704 0.08210  0.14195  -0.00878 527 PRO A O   
4201 C CB  . PRO A 527 ? 0.85241 0.98717 1.07919 0.04655  0.12955  -0.00019 527 PRO A CB  
4202 C CG  . PRO A 527 ? 0.91436 1.03133 1.11241 0.03527  0.12543  -0.00063 527 PRO A CG  
4203 C CD  . PRO A 527 ? 0.95617 1.05921 1.13371 0.03854  0.13524  -0.01154 527 PRO A CD  
4204 N N   . LYS A 528 ? 0.92981 1.07229 1.16906 0.07481  0.16285  -0.02166 528 LYS A N   
4205 C CA  . LYS A 528 ? 0.96687 1.12914 1.23070 0.08896  0.17553  -0.02576 528 LYS A CA  
4206 C C   . LYS A 528 ? 0.97811 1.11973 1.24534 0.10581  0.17587  -0.03243 528 LYS A C   
4207 O O   . LYS A 528 ? 1.06623 1.22239 1.36214 0.11997  0.17681  -0.03025 528 LYS A O   
4208 C CB  . LYS A 528 ? 0.96785 1.14069 1.22111 0.08655  0.19395  -0.03328 528 LYS A CB  
4209 C CG  . LYS A 528 ? 0.93790 1.14073 1.20093 0.07429  0.19839  -0.02559 528 LYS A CG  
4210 C CD  . LYS A 528 ? 0.96687 1.16153 1.19722 0.06273  0.20778  -0.02932 528 LYS A CD  
4211 C CE  . LYS A 528 ? 0.89825 1.10656 1.12691 0.04593  0.20414  -0.01845 528 LYS A CE  
4212 N NZ  . LYS A 528 ? 0.95062 1.16200 1.15702 0.03801  0.21911  -0.02106 528 LYS A NZ  
4213 N N   . VAL A 529 ? 1.03709 1.14454 1.27590 0.10443  0.17441  -0.04015 529 VAL A N   
4214 C CA  . VAL A 529 ? 1.05167 1.13428 1.28885 0.11944  0.17795  -0.04868 529 VAL A CA  
4215 C C   . VAL A 529 ? 1.03289 1.10793 1.28826 0.12854  0.16498  -0.04022 529 VAL A C   
4216 O O   . VAL A 529 ? 0.97554 1.05564 1.23588 0.12051  0.15068  -0.02908 529 VAL A O   
4217 C CB  . VAL A 529 ? 0.96777 1.01494 1.16843 0.11240  0.17854  -0.05943 529 VAL A CB  
4218 C CG1 . VAL A 529 ? 0.97477 1.02893 1.15268 0.10077  0.18733  -0.06527 529 VAL A CG1 
4219 C CG2 . VAL A 529 ? 0.89908 0.92649 1.08872 0.10263  0.16177  -0.05313 529 VAL A CG2 
4220 O OXT . VAL A 529 ? 1.06312 1.12488 1.32705 0.14493  0.16891  -0.04441 529 VAL A OXT 
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