data_9FDH
# 
_entry.id   9FDH 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   9FDH         pdb_00009fdh 10.2210/pdb9fdh/pdb 
WWPDB D_1292138707 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-05-28 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9FDH 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-17 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB 'starting crystal complex'           2wzb unspecified 
PDB 'bromide soak of TSA of same enzyme' 3zoz unspecified 
PDB 'BeF3 GSA complex of same enzyme'    4axx unspecified 
PDB 'GSA complex of same enzyme'         2x14 unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              j.waltho@manchester.ac.uk 
_pdbx_contact_author.name_first         Jonathan 
_pdbx_contact_author.name_last          Waltho 
_pdbx_contact_author.name_mi            P 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-7402-5492 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Cliff, M.J.'     1 0000-0002-7482-0234 
'Waltho, J.P.'    2 0000-0002-7402-5492 
'Bowler, M.W.'    3 0000-0003-0465-3351 
'Baxter, N.J.'    4 0009-0000-8292-7800 
'Bisson, C.'      5 0000-0002-9430-6822 
'Blackburn, G.M.' 6 0000-0002-3941-0459 
# 
loop_
_citation.abstract 
_citation.abstract_id_CAS 
_citation.book_id_ISBN 
_citation.book_publisher 
_citation.book_publisher_city 
_citation.book_title 
_citation.coordinate_linkage 
_citation.country 
_citation.database_id_Medline 
_citation.details 
_citation.id 
_citation.journal_abbrev 
_citation.journal_id_ASTM 
_citation.journal_id_CSD 
_citation.journal_id_ISSN 
_citation.journal_full 
_citation.journal_issue 
_citation.journal_volume 
_citation.language 
_citation.page_first 
_citation.page_last 
_citation.title 
_citation.year 
_citation.database_id_CSD 
_citation.pdbx_database_id_DOI 
_citation.pdbx_database_id_PubMed 
_citation.pdbx_database_id_patent 
_citation.unpublished_flag 
? ? ? ? ? ? ? US ? ? primary 'To be published'                                ?      0353 ?         ? ? ?  ? ?   ?   
'The role of magnesium in catalysis by phosphoglycerate kinase'                                              ?    ? ? ?        ? ? 
? ? ? ? ? ? ? DK ? ? 1       'Acta Crystallogr., Sect. D: Biol. Crystallogr.' ABCRE6 0766 0907-4449 ? ? 75 ? 861 877 
'Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix' 2019 ? 
10.1107/S2059798319011471 31588918 ? ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Cliff, M.J.'       1  0000-0002-7482-0234 
primary 'Serimbetov, Z.'    2  ?                   
primary 'Bisson, C.'        3  0000-0002-9430-6822 
primary 'Baxter, N.J.'      4  0009-0000-8292-7800 
primary 'Blackburn, G.M.'   5  0000-0002-3941-0459 
primary 'Hay, S.'           6  0000-0002-9430-6822 
primary 'Bowler, M.W.'      7  0000-0003-0465-3351 
primary 'Waltho, J.P.'      8  0000-0002-7402-5492 
1       'Liebschner, D.'    9  0000-0003-3921-3209 
1       'Afonine, P.V.'     10 0000-0002-5052-991X 
1       'Baker, M.L.'       11 ?                   
1       'Bunkoczi, G.'      12 ?                   
1       'Chen, V.B.'        13 0000-0003-2492-979X 
1       'Croll, T.I.'       14 ?                   
1       'Hintze, B.'        15 0000-0002-4871-2096 
1       'Hung, L.W.'        16 0000-0001-6690-8458 
1       'Jain, S.'          17 ?                   
1       'McCoy, A.J.'       18 ?                   
1       'Moriarty, N.W.'    19 0000-0001-8857-9464 
1       'Oeffner, R.D.'     20 0000-0003-3107-2202 
1       'Poon, B.K.'        21 0000-0001-9633-6067 
1       'Prisant, M.G.'     22 ?                   
1       'Read, R.J.'        23 0000-0001-8273-0047 
1       'Richardson, J.S.'  24 0000-0002-3311-2944 
1       'Richardson, D.C.'  25 ?                   
1       'Sammito, M.D.'     26 0000-0002-8346-9247 
1       'Sobolev, O.V.'     27 0000-0002-0623-3214 
1       'Stockwell, D.H.'   28 ?                   
1       'Terwilliger, T.C.' 29 0000-0001-6384-0320 
1       'Urzhumtsev, A.G.'  30 ?                   
1       'Videau, L.L.'      31 ?                   
1       'Williams, C.J.'    32 ?                   
1       'Adams, P.D.'       33 0000-0001-9333-8219 
# 
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 'Phosphoglycerate kinase 1'   44672.621 1   2.7.2.3 ? ? ? 
2 non-polymer syn "ADENOSINE-5'-DIPHOSPHATE"    427.201   1   ?       ? ? ? 
3 non-polymer syn '1,3-BISPHOSPHOGLYCERIC ACID' 266.037   1   ?       ? ? ? 
4 non-polymer syn 'DI(HYDROXYETHYL)ETHER'       106.120   2   ?       ? ? ? 
5 non-polymer nat 'CHLORIDE ION'                35.453    1   ?       ? ? ? 
6 non-polymer syn 'MAGNESIUM ION'               24.305    1   ?       ? ? ? 
7 non-polymer syn 'SODIUM ION'                  22.990    1   ?       ? ? ? 
8 water       nat water                         18.015    246 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Cell migration-inducing gene 10 protein,Primer recognition protein 2,PRP 2' 
# 
_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       
;MSLSNKLTLDKLDVKGKRVVMRVDFNVPMKNNQITNNQRIKAAVPSIKFCLDNGAKSVVLMSHLGRPDGVPMPDKYSLEP
VAVELKSLLGKDVLFLKDCVGPEVEKACANPAAGSVILLENLRFHVEEEGKGKDASGNKVKAEPAKIEAFRASLSKLGDV
YVNDAFGTAHRAHSSMVGVNLPQKAGGFLMKKELNYFAKALESPERPFLAILGGAKVADKIQLINNMLDKVNEMIIGGGM
AFTFLKVLNNMEIGTSLFDEEGAKIVKDLMSKAEKNGVKITLPVDFVTADKFDENAKTGQATVASGIPAGWMGLDCGPES
SKKYAEAVTRAKQIVWNGPVGVFEWEAFARGTKALMDEVVKATSRGCITIIGGGDTATCCAKWNTEDKVSHVSTGGGASL
ELLEGKVLPGVDALSNI
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSLSNKLTLDKLDVKGKRVVMRVDFNVPMKNNQITNNQRIKAAVPSIKFCLDNGAKSVVLMSHLGRPDGVPMPDKYSLEP
VAVELKSLLGKDVLFLKDCVGPEVEKACANPAAGSVILLENLRFHVEEEGKGKDASGNKVKAEPAKIEAFRASLSKLGDV
YVNDAFGTAHRAHSSMVGVNLPQKAGGFLMKKELNYFAKALESPERPFLAILGGAKVADKIQLINNMLDKVNEMIIGGGM
AFTFLKVLNNMEIGTSLFDEEGAKIVKDLMSKAEKNGVKITLPVDFVTADKFDENAKTGQATVASGIPAGWMGLDCGPES
SKKYAEAVTRAKQIVWNGPVGVFEWEAFARGTKALMDEVVKATSRGCITIIGGGDTATCCAKWNTEDKVSHVSTGGGASL
ELLEGKVLPGVDALSNI
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 "ADENOSINE-5'-DIPHOSPHATE"    ADP 
3 '1,3-BISPHOSPHOGLYCERIC ACID' X15 
4 'DI(HYDROXYETHYL)ETHER'       PEG 
5 'CHLORIDE ION'                CL  
6 'MAGNESIUM ION'               MG  
7 'SODIUM ION'                  NA  
8 water                         HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   LEU n 
1 4   SER n 
1 5   ASN n 
1 6   LYS n 
1 7   LEU n 
1 8   THR n 
1 9   LEU n 
1 10  ASP n 
1 11  LYS n 
1 12  LEU n 
1 13  ASP n 
1 14  VAL n 
1 15  LYS n 
1 16  GLY n 
1 17  LYS n 
1 18  ARG n 
1 19  VAL n 
1 20  VAL n 
1 21  MET n 
1 22  ARG n 
1 23  VAL n 
1 24  ASP n 
1 25  PHE n 
1 26  ASN n 
1 27  VAL n 
1 28  PRO n 
1 29  MET n 
1 30  LYS n 
1 31  ASN n 
1 32  ASN n 
1 33  GLN n 
1 34  ILE n 
1 35  THR n 
1 36  ASN n 
1 37  ASN n 
1 38  GLN n 
1 39  ARG n 
1 40  ILE n 
1 41  LYS n 
1 42  ALA n 
1 43  ALA n 
1 44  VAL n 
1 45  PRO n 
1 46  SER n 
1 47  ILE n 
1 48  LYS n 
1 49  PHE n 
1 50  CYS n 
1 51  LEU n 
1 52  ASP n 
1 53  ASN n 
1 54  GLY n 
1 55  ALA n 
1 56  LYS n 
1 57  SER n 
1 58  VAL n 
1 59  VAL n 
1 60  LEU n 
1 61  MET n 
1 62  SER n 
1 63  HIS n 
1 64  LEU n 
1 65  GLY n 
1 66  ARG n 
1 67  PRO n 
1 68  ASP n 
1 69  GLY n 
1 70  VAL n 
1 71  PRO n 
1 72  MET n 
1 73  PRO n 
1 74  ASP n 
1 75  LYS n 
1 76  TYR n 
1 77  SER n 
1 78  LEU n 
1 79  GLU n 
1 80  PRO n 
1 81  VAL n 
1 82  ALA n 
1 83  VAL n 
1 84  GLU n 
1 85  LEU n 
1 86  LYS n 
1 87  SER n 
1 88  LEU n 
1 89  LEU n 
1 90  GLY n 
1 91  LYS n 
1 92  ASP n 
1 93  VAL n 
1 94  LEU n 
1 95  PHE n 
1 96  LEU n 
1 97  LYS n 
1 98  ASP n 
1 99  CYS n 
1 100 VAL n 
1 101 GLY n 
1 102 PRO n 
1 103 GLU n 
1 104 VAL n 
1 105 GLU n 
1 106 LYS n 
1 107 ALA n 
1 108 CYS n 
1 109 ALA n 
1 110 ASN n 
1 111 PRO n 
1 112 ALA n 
1 113 ALA n 
1 114 GLY n 
1 115 SER n 
1 116 VAL n 
1 117 ILE n 
1 118 LEU n 
1 119 LEU n 
1 120 GLU n 
1 121 ASN n 
1 122 LEU n 
1 123 ARG n 
1 124 PHE n 
1 125 HIS n 
1 126 VAL n 
1 127 GLU n 
1 128 GLU n 
1 129 GLU n 
1 130 GLY n 
1 131 LYS n 
1 132 GLY n 
1 133 LYS n 
1 134 ASP n 
1 135 ALA n 
1 136 SER n 
1 137 GLY n 
1 138 ASN n 
1 139 LYS n 
1 140 VAL n 
1 141 LYS n 
1 142 ALA n 
1 143 GLU n 
1 144 PRO n 
1 145 ALA n 
1 146 LYS n 
1 147 ILE n 
1 148 GLU n 
1 149 ALA n 
1 150 PHE n 
1 151 ARG n 
1 152 ALA n 
1 153 SER n 
1 154 LEU n 
1 155 SER n 
1 156 LYS n 
1 157 LEU n 
1 158 GLY n 
1 159 ASP n 
1 160 VAL n 
1 161 TYR n 
1 162 VAL n 
1 163 ASN n 
1 164 ASP n 
1 165 ALA n 
1 166 PHE n 
1 167 GLY n 
1 168 THR n 
1 169 ALA n 
1 170 HIS n 
1 171 ARG n 
1 172 ALA n 
1 173 HIS n 
1 174 SER n 
1 175 SER n 
1 176 MET n 
1 177 VAL n 
1 178 GLY n 
1 179 VAL n 
1 180 ASN n 
1 181 LEU n 
1 182 PRO n 
1 183 GLN n 
1 184 LYS n 
1 185 ALA n 
1 186 GLY n 
1 187 GLY n 
1 188 PHE n 
1 189 LEU n 
1 190 MET n 
1 191 LYS n 
1 192 LYS n 
1 193 GLU n 
1 194 LEU n 
1 195 ASN n 
1 196 TYR n 
1 197 PHE n 
1 198 ALA n 
1 199 LYS n 
1 200 ALA n 
1 201 LEU n 
1 202 GLU n 
1 203 SER n 
1 204 PRO n 
1 205 GLU n 
1 206 ARG n 
1 207 PRO n 
1 208 PHE n 
1 209 LEU n 
1 210 ALA n 
1 211 ILE n 
1 212 LEU n 
1 213 GLY n 
1 214 GLY n 
1 215 ALA n 
1 216 LYS n 
1 217 VAL n 
1 218 ALA n 
1 219 ASP n 
1 220 LYS n 
1 221 ILE n 
1 222 GLN n 
1 223 LEU n 
1 224 ILE n 
1 225 ASN n 
1 226 ASN n 
1 227 MET n 
1 228 LEU n 
1 229 ASP n 
1 230 LYS n 
1 231 VAL n 
1 232 ASN n 
1 233 GLU n 
1 234 MET n 
1 235 ILE n 
1 236 ILE n 
1 237 GLY n 
1 238 GLY n 
1 239 GLY n 
1 240 MET n 
1 241 ALA n 
1 242 PHE n 
1 243 THR n 
1 244 PHE n 
1 245 LEU n 
1 246 LYS n 
1 247 VAL n 
1 248 LEU n 
1 249 ASN n 
1 250 ASN n 
1 251 MET n 
1 252 GLU n 
1 253 ILE n 
1 254 GLY n 
1 255 THR n 
1 256 SER n 
1 257 LEU n 
1 258 PHE n 
1 259 ASP n 
1 260 GLU n 
1 261 GLU n 
1 262 GLY n 
1 263 ALA n 
1 264 LYS n 
1 265 ILE n 
1 266 VAL n 
1 267 LYS n 
1 268 ASP n 
1 269 LEU n 
1 270 MET n 
1 271 SER n 
1 272 LYS n 
1 273 ALA n 
1 274 GLU n 
1 275 LYS n 
1 276 ASN n 
1 277 GLY n 
1 278 VAL n 
1 279 LYS n 
1 280 ILE n 
1 281 THR n 
1 282 LEU n 
1 283 PRO n 
1 284 VAL n 
1 285 ASP n 
1 286 PHE n 
1 287 VAL n 
1 288 THR n 
1 289 ALA n 
1 290 ASP n 
1 291 LYS n 
1 292 PHE n 
1 293 ASP n 
1 294 GLU n 
1 295 ASN n 
1 296 ALA n 
1 297 LYS n 
1 298 THR n 
1 299 GLY n 
1 300 GLN n 
1 301 ALA n 
1 302 THR n 
1 303 VAL n 
1 304 ALA n 
1 305 SER n 
1 306 GLY n 
1 307 ILE n 
1 308 PRO n 
1 309 ALA n 
1 310 GLY n 
1 311 TRP n 
1 312 MET n 
1 313 GLY n 
1 314 LEU n 
1 315 ASP n 
1 316 CYS n 
1 317 GLY n 
1 318 PRO n 
1 319 GLU n 
1 320 SER n 
1 321 SER n 
1 322 LYS n 
1 323 LYS n 
1 324 TYR n 
1 325 ALA n 
1 326 GLU n 
1 327 ALA n 
1 328 VAL n 
1 329 THR n 
1 330 ARG n 
1 331 ALA n 
1 332 LYS n 
1 333 GLN n 
1 334 ILE n 
1 335 VAL n 
1 336 TRP n 
1 337 ASN n 
1 338 GLY n 
1 339 PRO n 
1 340 VAL n 
1 341 GLY n 
1 342 VAL n 
1 343 PHE n 
1 344 GLU n 
1 345 TRP n 
1 346 GLU n 
1 347 ALA n 
1 348 PHE n 
1 349 ALA n 
1 350 ARG n 
1 351 GLY n 
1 352 THR n 
1 353 LYS n 
1 354 ALA n 
1 355 LEU n 
1 356 MET n 
1 357 ASP n 
1 358 GLU n 
1 359 VAL n 
1 360 VAL n 
1 361 LYS n 
1 362 ALA n 
1 363 THR n 
1 364 SER n 
1 365 ARG n 
1 366 GLY n 
1 367 CYS n 
1 368 ILE n 
1 369 THR n 
1 370 ILE n 
1 371 ILE n 
1 372 GLY n 
1 373 GLY n 
1 374 GLY n 
1 375 ASP n 
1 376 THR n 
1 377 ALA n 
1 378 THR n 
1 379 CYS n 
1 380 CYS n 
1 381 ALA n 
1 382 LYS n 
1 383 TRP n 
1 384 ASN n 
1 385 THR n 
1 386 GLU n 
1 387 ASP n 
1 388 LYS n 
1 389 VAL n 
1 390 SER n 
1 391 HIS n 
1 392 VAL n 
1 393 SER n 
1 394 THR n 
1 395 GLY n 
1 396 GLY n 
1 397 GLY n 
1 398 ALA n 
1 399 SER n 
1 400 LEU n 
1 401 GLU n 
1 402 LEU n 
1 403 LEU n 
1 404 GLU n 
1 405 GLY n 
1 406 LYS n 
1 407 VAL n 
1 408 LEU n 
1 409 PRO n 
1 410 GLY n 
1 411 VAL n 
1 412 ASP n 
1 413 ALA n 
1 414 LEU n 
1 415 SER n 
1 416 ASN n 
1 417 ILE n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   417 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'PGK1, PGKA, MIG10, OK/SW-cl.110' 
_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      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ADP non-polymer         n "ADENOSINE-5'-DIPHOSPHATE"    ? 'C10 H15 N5 O10 P2' 427.201 
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 
CL  non-polymer         . 'CHLORIDE ION'                ? 'Cl -1'             35.453  
CYS 'L-peptide linking' y CYSTEINE                      ? 'C3 H7 N O2 S'      121.158 
GLN 'L-peptide linking' y GLUTAMINE                     ? 'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'               ? 'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                       ? 'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE                     ? 'C6 H10 N3 O2 1'    156.162 
HOH non-polymer         . WATER                         ? 'H2 O'              18.015  
ILE 'L-peptide linking' y ISOLEUCINE                    ? 'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE                       ? 'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE                        ? 'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE                    ? 'C5 H11 N O2 S'     149.211 
MG  non-polymer         . 'MAGNESIUM ION'               ? 'Mg 2'              24.305  
NA  non-polymer         . 'SODIUM ION'                  ? 'Na 1'              22.990  
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER'       ? 'C4 H10 O3'         106.120 
PHE 'L-peptide linking' y PHENYLALANINE                 ? 'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE                       ? 'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE                        ? 'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE                     ? 'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                    ? 'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE                      ? 'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE                        ? 'C5 H11 N O2'       117.146 
X15 non-polymer         . '1,3-BISPHOSPHOGLYCERIC ACID' ? 'C3 H8 O10 P2'      266.037 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   0   ?   ?   ?   A . n 
A 1 2   SER 2   1   1   SER SER A . n 
A 1 3   LEU 3   2   2   LEU LEU A . n 
A 1 4   SER 4   3   3   SER SER A . n 
A 1 5   ASN 5   4   4   ASN ASN A . n 
A 1 6   LYS 6   5   5   LYS LYS A . n 
A 1 7   LEU 7   6   6   LEU LEU A . n 
A 1 8   THR 8   7   7   THR THR A . n 
A 1 9   LEU 9   8   8   LEU LEU A . n 
A 1 10  ASP 10  9   9   ASP ASP A . n 
A 1 11  LYS 11  10  10  LYS LYS A . n 
A 1 12  LEU 12  11  11  LEU LEU A . n 
A 1 13  ASP 13  12  12  ASP ASP A . n 
A 1 14  VAL 14  13  13  VAL VAL A . n 
A 1 15  LYS 15  14  14  LYS LYS A . n 
A 1 16  GLY 16  15  15  GLY GLY A . n 
A 1 17  LYS 17  16  16  LYS LYS A . n 
A 1 18  ARG 18  17  17  ARG ARG A . n 
A 1 19  VAL 19  18  18  VAL VAL A . n 
A 1 20  VAL 20  19  19  VAL VAL A . n 
A 1 21  MET 21  20  20  MET MET A . n 
A 1 22  ARG 22  21  21  ARG ARG A . n 
A 1 23  VAL 23  22  22  VAL VAL A . n 
A 1 24  ASP 24  23  23  ASP ASP A . n 
A 1 25  PHE 25  24  24  PHE PHE A . n 
A 1 26  ASN 26  25  25  ASN ASN A . n 
A 1 27  VAL 27  26  26  VAL VAL A . n 
A 1 28  PRO 28  27  27  PRO PRO A . n 
A 1 29  MET 29  28  28  MET MET A . n 
A 1 30  LYS 30  29  29  LYS LYS A . n 
A 1 31  ASN 31  30  30  ASN ASN A . n 
A 1 32  ASN 32  31  31  ASN ASN A . n 
A 1 33  GLN 33  32  32  GLN GLN A . n 
A 1 34  ILE 34  33  33  ILE ILE A . n 
A 1 35  THR 35  34  34  THR THR A . n 
A 1 36  ASN 36  35  35  ASN ASN A . n 
A 1 37  ASN 37  36  36  ASN ASN A . n 
A 1 38  GLN 38  37  37  GLN GLN A . n 
A 1 39  ARG 39  38  38  ARG ARG A . n 
A 1 40  ILE 40  39  39  ILE ILE A . n 
A 1 41  LYS 41  40  40  LYS LYS A . n 
A 1 42  ALA 42  41  41  ALA ALA A . n 
A 1 43  ALA 43  42  42  ALA ALA A . n 
A 1 44  VAL 44  43  43  VAL VAL A . n 
A 1 45  PRO 45  44  44  PRO PRO A . n 
A 1 46  SER 46  45  45  SER SER A . n 
A 1 47  ILE 47  46  46  ILE ILE A . n 
A 1 48  LYS 48  47  47  LYS LYS A . n 
A 1 49  PHE 49  48  48  PHE PHE A . n 
A 1 50  CYS 50  49  49  CYS CYS A . n 
A 1 51  LEU 51  50  50  LEU LEU A . n 
A 1 52  ASP 52  51  51  ASP ASP A . n 
A 1 53  ASN 53  52  52  ASN ASN A . n 
A 1 54  GLY 54  53  53  GLY GLY A . n 
A 1 55  ALA 55  54  54  ALA ALA A . n 
A 1 56  LYS 56  55  55  LYS LYS A . n 
A 1 57  SER 57  56  56  SER SER A . n 
A 1 58  VAL 58  57  57  VAL VAL A . n 
A 1 59  VAL 59  58  58  VAL VAL A . n 
A 1 60  LEU 60  59  59  LEU LEU A . n 
A 1 61  MET 61  60  60  MET MET A . n 
A 1 62  SER 62  61  61  SER SER A . n 
A 1 63  HIS 63  62  62  HIS HIS A . n 
A 1 64  LEU 64  63  63  LEU LEU A . n 
A 1 65  GLY 65  64  64  GLY GLY A . n 
A 1 66  ARG 66  65  65  ARG ARG A . n 
A 1 67  PRO 67  66  66  PRO PRO A . n 
A 1 68  ASP 68  67  67  ASP ASP A . n 
A 1 69  GLY 69  68  68  GLY GLY A . n 
A 1 70  VAL 70  69  69  VAL VAL A . n 
A 1 71  PRO 71  70  70  PRO PRO A . n 
A 1 72  MET 72  71  71  MET MET A . n 
A 1 73  PRO 73  72  72  PRO PRO A . n 
A 1 74  ASP 74  73  73  ASP ASP A . n 
A 1 75  LYS 75  74  74  LYS LYS A . n 
A 1 76  TYR 76  75  75  TYR TYR A . n 
A 1 77  SER 77  76  76  SER SER A . n 
A 1 78  LEU 78  77  77  LEU LEU A . n 
A 1 79  GLU 79  78  78  GLU GLU A . n 
A 1 80  PRO 80  79  79  PRO PRO A . n 
A 1 81  VAL 81  80  80  VAL VAL A . n 
A 1 82  ALA 82  81  81  ALA ALA A . n 
A 1 83  VAL 83  82  82  VAL VAL A . n 
A 1 84  GLU 84  83  83  GLU GLU A . n 
A 1 85  LEU 85  84  84  LEU LEU A . n 
A 1 86  LYS 86  85  85  LYS LYS A . n 
A 1 87  SER 87  86  86  SER SER A . n 
A 1 88  LEU 88  87  87  LEU LEU A . n 
A 1 89  LEU 89  88  88  LEU LEU A . n 
A 1 90  GLY 90  89  89  GLY GLY A . n 
A 1 91  LYS 91  90  90  LYS LYS A . n 
A 1 92  ASP 92  91  91  ASP ASP A . n 
A 1 93  VAL 93  92  92  VAL VAL A . n 
A 1 94  LEU 94  93  93  LEU LEU A . n 
A 1 95  PHE 95  94  94  PHE PHE A . n 
A 1 96  LEU 96  95  95  LEU LEU A . n 
A 1 97  LYS 97  96  96  LYS LYS A . n 
A 1 98  ASP 98  97  97  ASP ASP A . n 
A 1 99  CYS 99  98  98  CYS CYS A . n 
A 1 100 VAL 100 99  99  VAL VAL A . n 
A 1 101 GLY 101 100 100 GLY GLY A . n 
A 1 102 PRO 102 101 101 PRO PRO A . n 
A 1 103 GLU 103 102 102 GLU GLU A . n 
A 1 104 VAL 104 103 103 VAL VAL A . n 
A 1 105 GLU 105 104 104 GLU GLU A . n 
A 1 106 LYS 106 105 105 LYS LYS A . n 
A 1 107 ALA 107 106 106 ALA ALA A . n 
A 1 108 CYS 108 107 107 CYS CYS A . n 
A 1 109 ALA 109 108 108 ALA ALA A . n 
A 1 110 ASN 110 109 109 ASN ASN A . n 
A 1 111 PRO 111 110 110 PRO PRO A . n 
A 1 112 ALA 112 111 111 ALA ALA A . n 
A 1 113 ALA 113 112 112 ALA ALA A . n 
A 1 114 GLY 114 113 113 GLY GLY A . n 
A 1 115 SER 115 114 114 SER SER A . n 
A 1 116 VAL 116 115 115 VAL VAL A . n 
A 1 117 ILE 117 116 116 ILE ILE A . n 
A 1 118 LEU 118 117 117 LEU LEU A . n 
A 1 119 LEU 119 118 118 LEU LEU A . n 
A 1 120 GLU 120 119 119 GLU GLU A . n 
A 1 121 ASN 121 120 120 ASN ASN A . n 
A 1 122 LEU 122 121 121 LEU LEU A . n 
A 1 123 ARG 123 122 122 ARG ARG A . n 
A 1 124 PHE 124 123 123 PHE PHE A . n 
A 1 125 HIS 125 124 124 HIS HIS A . n 
A 1 126 VAL 126 125 125 VAL VAL A . n 
A 1 127 GLU 127 126 126 GLU GLU A . n 
A 1 128 GLU 128 127 127 GLU GLU A . n 
A 1 129 GLU 129 128 128 GLU GLU A . n 
A 1 130 GLY 130 129 129 GLY GLY A . n 
A 1 131 LYS 131 130 130 LYS LYS A . n 
A 1 132 GLY 132 131 131 GLY GLY A . n 
A 1 133 LYS 133 132 132 LYS LYS A . n 
A 1 134 ASP 134 133 133 ASP ASP A . n 
A 1 135 ALA 135 134 134 ALA ALA A . n 
A 1 136 SER 136 135 135 SER SER A . n 
A 1 137 GLY 137 136 136 GLY GLY A . n 
A 1 138 ASN 138 137 137 ASN ASN A . n 
A 1 139 LYS 139 138 138 LYS LYS A . n 
A 1 140 VAL 140 139 139 VAL VAL A . n 
A 1 141 LYS 141 140 140 LYS LYS A . n 
A 1 142 ALA 142 141 141 ALA ALA A . n 
A 1 143 GLU 143 142 142 GLU GLU A . n 
A 1 144 PRO 144 143 143 PRO PRO A . n 
A 1 145 ALA 145 144 144 ALA ALA A . n 
A 1 146 LYS 146 145 145 LYS LYS A . n 
A 1 147 ILE 147 146 146 ILE ILE A . n 
A 1 148 GLU 148 147 147 GLU GLU A . n 
A 1 149 ALA 149 148 148 ALA ALA A . n 
A 1 150 PHE 150 149 149 PHE PHE A . n 
A 1 151 ARG 151 150 150 ARG ARG A . n 
A 1 152 ALA 152 151 151 ALA ALA A . n 
A 1 153 SER 153 152 152 SER SER A . n 
A 1 154 LEU 154 153 153 LEU LEU A . n 
A 1 155 SER 155 154 154 SER SER A . n 
A 1 156 LYS 156 155 155 LYS LYS A . n 
A 1 157 LEU 157 156 156 LEU LEU A . n 
A 1 158 GLY 158 157 157 GLY GLY A . n 
A 1 159 ASP 159 158 158 ASP ASP A . n 
A 1 160 VAL 160 159 159 VAL VAL A . n 
A 1 161 TYR 161 160 160 TYR TYR A . n 
A 1 162 VAL 162 161 161 VAL VAL A . n 
A 1 163 ASN 163 162 162 ASN ASN A . n 
A 1 164 ASP 164 163 163 ASP ASP A . n 
A 1 165 ALA 165 164 164 ALA ALA A . n 
A 1 166 PHE 166 165 165 PHE PHE A . n 
A 1 167 GLY 167 166 166 GLY GLY A . n 
A 1 168 THR 168 167 167 THR THR A . n 
A 1 169 ALA 169 168 168 ALA ALA A . n 
A 1 170 HIS 170 169 169 HIS HIS A . n 
A 1 171 ARG 171 170 170 ARG ARG A . n 
A 1 172 ALA 172 171 171 ALA ALA A . n 
A 1 173 HIS 173 172 172 HIS HIS A . n 
A 1 174 SER 174 173 173 SER SER A . n 
A 1 175 SER 175 174 174 SER SER A . n 
A 1 176 MET 176 175 175 MET MET A . n 
A 1 177 VAL 177 176 176 VAL VAL A . n 
A 1 178 GLY 178 177 177 GLY GLY A . n 
A 1 179 VAL 179 178 178 VAL VAL A . n 
A 1 180 ASN 180 179 179 ASN ASN A . n 
A 1 181 LEU 181 180 180 LEU LEU A . n 
A 1 182 PRO 182 181 181 PRO PRO A . n 
A 1 183 GLN 183 182 182 GLN GLN A . n 
A 1 184 LYS 184 183 183 LYS LYS A . n 
A 1 185 ALA 185 184 184 ALA ALA A . n 
A 1 186 GLY 186 185 185 GLY GLY A . n 
A 1 187 GLY 187 186 186 GLY GLY A . n 
A 1 188 PHE 188 187 187 PHE PHE A . n 
A 1 189 LEU 189 188 188 LEU LEU A . n 
A 1 190 MET 190 189 189 MET MET A . n 
A 1 191 LYS 191 190 190 LYS LYS A . n 
A 1 192 LYS 192 191 191 LYS LYS A . n 
A 1 193 GLU 193 192 192 GLU GLU A . n 
A 1 194 LEU 194 193 193 LEU LEU A . n 
A 1 195 ASN 195 194 194 ASN ASN A . n 
A 1 196 TYR 196 195 195 TYR TYR A . n 
A 1 197 PHE 197 196 196 PHE PHE A . n 
A 1 198 ALA 198 197 197 ALA ALA A . n 
A 1 199 LYS 199 198 198 LYS LYS A . n 
A 1 200 ALA 200 199 199 ALA ALA A . n 
A 1 201 LEU 201 200 200 LEU LEU A . n 
A 1 202 GLU 202 201 201 GLU GLU A . n 
A 1 203 SER 203 202 202 SER SER A . n 
A 1 204 PRO 204 203 203 PRO PRO A . n 
A 1 205 GLU 205 204 204 GLU GLU A . n 
A 1 206 ARG 206 205 205 ARG ARG A . n 
A 1 207 PRO 207 206 206 PRO PRO A . n 
A 1 208 PHE 208 207 207 PHE PHE A . n 
A 1 209 LEU 209 208 208 LEU LEU A . n 
A 1 210 ALA 210 209 209 ALA ALA A . n 
A 1 211 ILE 211 210 210 ILE ILE A . n 
A 1 212 LEU 212 211 211 LEU LEU A . n 
A 1 213 GLY 213 212 212 GLY GLY A . n 
A 1 214 GLY 214 213 213 GLY GLY A . n 
A 1 215 ALA 215 214 214 ALA ALA A . n 
A 1 216 LYS 216 215 215 LYS LYS A . n 
A 1 217 VAL 217 216 216 VAL VAL A . n 
A 1 218 ALA 218 217 217 ALA ALA A . n 
A 1 219 ASP 219 218 218 ASP ASP A . n 
A 1 220 LYS 220 219 219 LYS LYS A . n 
A 1 221 ILE 221 220 220 ILE ILE A . n 
A 1 222 GLN 222 221 221 GLN GLN A . n 
A 1 223 LEU 223 222 222 LEU LEU A . n 
A 1 224 ILE 224 223 223 ILE ILE A . n 
A 1 225 ASN 225 224 224 ASN ASN A . n 
A 1 226 ASN 226 225 225 ASN ASN A . n 
A 1 227 MET 227 226 226 MET MET A . n 
A 1 228 LEU 228 227 227 LEU LEU A . n 
A 1 229 ASP 229 228 228 ASP ASP A . n 
A 1 230 LYS 230 229 229 LYS LYS A . n 
A 1 231 VAL 231 230 230 VAL VAL A . n 
A 1 232 ASN 232 231 231 ASN ASN A . n 
A 1 233 GLU 233 232 232 GLU GLU A . n 
A 1 234 MET 234 233 233 MET MET A . n 
A 1 235 ILE 235 234 234 ILE ILE A . n 
A 1 236 ILE 236 235 235 ILE ILE A . n 
A 1 237 GLY 237 236 236 GLY GLY A . n 
A 1 238 GLY 238 237 237 GLY GLY A . n 
A 1 239 GLY 239 238 238 GLY GLY A . n 
A 1 240 MET 240 239 239 MET MET A . n 
A 1 241 ALA 241 240 240 ALA ALA A . n 
A 1 242 PHE 242 241 241 PHE PHE A . n 
A 1 243 THR 243 242 242 THR THR A . n 
A 1 244 PHE 244 243 243 PHE PHE A . n 
A 1 245 LEU 245 244 244 LEU LEU A . n 
A 1 246 LYS 246 245 245 LYS LYS A . n 
A 1 247 VAL 247 246 246 VAL VAL A . n 
A 1 248 LEU 248 247 247 LEU LEU A . n 
A 1 249 ASN 249 248 248 ASN ASN A . n 
A 1 250 ASN 250 249 249 ASN ASN A . n 
A 1 251 MET 251 250 250 MET MET A . n 
A 1 252 GLU 252 251 251 GLU GLU A . n 
A 1 253 ILE 253 252 252 ILE ILE A . n 
A 1 254 GLY 254 253 253 GLY GLY A . n 
A 1 255 THR 255 254 254 THR THR A . n 
A 1 256 SER 256 255 255 SER SER A . n 
A 1 257 LEU 257 256 256 LEU LEU A . n 
A 1 258 PHE 258 257 257 PHE PHE A . n 
A 1 259 ASP 259 258 258 ASP ASP A . n 
A 1 260 GLU 260 259 259 GLU GLU A . n 
A 1 261 GLU 261 260 260 GLU GLU A . n 
A 1 262 GLY 262 261 261 GLY GLY A . n 
A 1 263 ALA 263 262 262 ALA ALA A . n 
A 1 264 LYS 264 263 263 LYS LYS A . n 
A 1 265 ILE 265 264 264 ILE ILE A . n 
A 1 266 VAL 266 265 265 VAL VAL A . n 
A 1 267 LYS 267 266 266 LYS LYS A . n 
A 1 268 ASP 268 267 267 ASP ASP A . n 
A 1 269 LEU 269 268 268 LEU LEU A . n 
A 1 270 MET 270 269 269 MET MET A . n 
A 1 271 SER 271 270 270 SER SER A . n 
A 1 272 LYS 272 271 271 LYS LYS A . n 
A 1 273 ALA 273 272 272 ALA ALA A . n 
A 1 274 GLU 274 273 273 GLU GLU A . n 
A 1 275 LYS 275 274 274 LYS LYS A . n 
A 1 276 ASN 276 275 275 ASN ASN A . n 
A 1 277 GLY 277 276 276 GLY GLY A . n 
A 1 278 VAL 278 277 277 VAL VAL A . n 
A 1 279 LYS 279 278 278 LYS LYS A . n 
A 1 280 ILE 280 279 279 ILE ILE A . n 
A 1 281 THR 281 280 280 THR THR A . n 
A 1 282 LEU 282 281 281 LEU LEU A . n 
A 1 283 PRO 283 282 282 PRO PRO A . n 
A 1 284 VAL 284 283 283 VAL VAL A . n 
A 1 285 ASP 285 284 284 ASP ASP A . n 
A 1 286 PHE 286 285 285 PHE PHE A . n 
A 1 287 VAL 287 286 286 VAL VAL A . n 
A 1 288 THR 288 287 287 THR THR A . n 
A 1 289 ALA 289 288 288 ALA ALA A . n 
A 1 290 ASP 290 289 289 ASP ASP A . n 
A 1 291 LYS 291 290 290 LYS LYS A . n 
A 1 292 PHE 292 291 291 PHE PHE A . n 
A 1 293 ASP 293 292 292 ASP ASP A . n 
A 1 294 GLU 294 293 293 GLU GLU A . n 
A 1 295 ASN 295 294 294 ASN ASN A . n 
A 1 296 ALA 296 295 295 ALA ALA A . n 
A 1 297 LYS 297 296 296 LYS LYS A . n 
A 1 298 THR 298 297 297 THR THR A . n 
A 1 299 GLY 299 298 298 GLY GLY A . n 
A 1 300 GLN 300 299 299 GLN GLN A . n 
A 1 301 ALA 301 300 300 ALA ALA A . n 
A 1 302 THR 302 301 301 THR THR A . n 
A 1 303 VAL 303 302 302 VAL VAL A . n 
A 1 304 ALA 304 303 303 ALA ALA A . n 
A 1 305 SER 305 304 304 SER SER A . n 
A 1 306 GLY 306 305 305 GLY GLY A . n 
A 1 307 ILE 307 306 306 ILE ILE A . n 
A 1 308 PRO 308 307 307 PRO PRO A . n 
A 1 309 ALA 309 308 308 ALA ALA A . n 
A 1 310 GLY 310 309 309 GLY GLY A . n 
A 1 311 TRP 311 310 310 TRP TRP A . n 
A 1 312 MET 312 311 311 MET MET A . n 
A 1 313 GLY 313 312 312 GLY GLY A . n 
A 1 314 LEU 314 313 313 LEU LEU A . n 
A 1 315 ASP 315 314 314 ASP ASP A . n 
A 1 316 CYS 316 315 315 CYS CYS A . n 
A 1 317 GLY 317 316 316 GLY GLY A . n 
A 1 318 PRO 318 317 317 PRO PRO A . n 
A 1 319 GLU 319 318 318 GLU GLU A . n 
A 1 320 SER 320 319 319 SER SER A . n 
A 1 321 SER 321 320 320 SER SER A . n 
A 1 322 LYS 322 321 321 LYS LYS A . n 
A 1 323 LYS 323 322 322 LYS LYS A . n 
A 1 324 TYR 324 323 323 TYR TYR A . n 
A 1 325 ALA 325 324 324 ALA ALA A . n 
A 1 326 GLU 326 325 325 GLU GLU A . n 
A 1 327 ALA 327 326 326 ALA ALA A . n 
A 1 328 VAL 328 327 327 VAL VAL A . n 
A 1 329 THR 329 328 328 THR THR A . n 
A 1 330 ARG 330 329 329 ARG ARG A . n 
A 1 331 ALA 331 330 330 ALA ALA A . n 
A 1 332 LYS 332 331 331 LYS LYS A . n 
A 1 333 GLN 333 332 332 GLN GLN A . n 
A 1 334 ILE 334 333 333 ILE ILE A . n 
A 1 335 VAL 335 334 334 VAL VAL A . n 
A 1 336 TRP 336 335 335 TRP TRP A . n 
A 1 337 ASN 337 336 336 ASN ASN A . n 
A 1 338 GLY 338 337 337 GLY GLY A . n 
A 1 339 PRO 339 338 338 PRO PRO A . n 
A 1 340 VAL 340 339 339 VAL VAL A . n 
A 1 341 GLY 341 340 340 GLY GLY A . n 
A 1 342 VAL 342 341 341 VAL VAL A . n 
A 1 343 PHE 343 342 342 PHE PHE A . n 
A 1 344 GLU 344 343 343 GLU GLU A . n 
A 1 345 TRP 345 344 344 TRP TRP A . n 
A 1 346 GLU 346 345 345 GLU GLU A . n 
A 1 347 ALA 347 346 346 ALA ALA A . n 
A 1 348 PHE 348 347 347 PHE PHE A . n 
A 1 349 ALA 349 348 348 ALA ALA A . n 
A 1 350 ARG 350 349 349 ARG ARG A . n 
A 1 351 GLY 351 350 350 GLY GLY A . n 
A 1 352 THR 352 351 351 THR THR A . n 
A 1 353 LYS 353 352 352 LYS LYS A . n 
A 1 354 ALA 354 353 353 ALA ALA A . n 
A 1 355 LEU 355 354 354 LEU LEU A . n 
A 1 356 MET 356 355 355 MET MET A . n 
A 1 357 ASP 357 356 356 ASP ASP A . n 
A 1 358 GLU 358 357 357 GLU GLU A . n 
A 1 359 VAL 359 358 358 VAL VAL A . n 
A 1 360 VAL 360 359 359 VAL VAL A . n 
A 1 361 LYS 361 360 360 LYS LYS A . n 
A 1 362 ALA 362 361 361 ALA ALA A . n 
A 1 363 THR 363 362 362 THR THR A . n 
A 1 364 SER 364 363 363 SER SER A . n 
A 1 365 ARG 365 364 364 ARG ARG A . n 
A 1 366 GLY 366 365 365 GLY GLY A . n 
A 1 367 CYS 367 366 366 CYS CYS A . n 
A 1 368 ILE 368 367 367 ILE ILE A . n 
A 1 369 THR 369 368 368 THR THR A . n 
A 1 370 ILE 370 369 369 ILE ILE A . n 
A 1 371 ILE 371 370 370 ILE ILE A . n 
A 1 372 GLY 372 371 371 GLY GLY A . n 
A 1 373 GLY 373 372 372 GLY GLY A . n 
A 1 374 GLY 374 373 373 GLY GLY A . n 
A 1 375 ASP 375 374 374 ASP ASP A . n 
A 1 376 THR 376 375 375 THR THR A . n 
A 1 377 ALA 377 376 376 ALA ALA A . n 
A 1 378 THR 378 377 377 THR THR A . n 
A 1 379 CYS 379 378 378 CYS CYS A . n 
A 1 380 CYS 380 379 379 CYS CYS A . n 
A 1 381 ALA 381 380 380 ALA ALA A . n 
A 1 382 LYS 382 381 381 LYS LYS A . n 
A 1 383 TRP 383 382 382 TRP TRP A . n 
A 1 384 ASN 384 383 383 ASN ASN A . n 
A 1 385 THR 385 384 384 THR THR A . n 
A 1 386 GLU 386 385 385 GLU GLU A . n 
A 1 387 ASP 387 386 386 ASP ASP A . n 
A 1 388 LYS 388 387 387 LYS LYS A . n 
A 1 389 VAL 389 388 388 VAL VAL A . n 
A 1 390 SER 390 389 389 SER SER A . n 
A 1 391 HIS 391 390 390 HIS HIS A . n 
A 1 392 VAL 392 391 391 VAL VAL A . n 
A 1 393 SER 393 392 392 SER SER A . n 
A 1 394 THR 394 393 393 THR THR A . n 
A 1 395 GLY 395 394 394 GLY GLY A . n 
A 1 396 GLY 396 395 395 GLY GLY A . n 
A 1 397 GLY 397 396 396 GLY GLY A . n 
A 1 398 ALA 398 397 397 ALA ALA A . n 
A 1 399 SER 399 398 398 SER SER A . n 
A 1 400 LEU 400 399 399 LEU LEU A . n 
A 1 401 GLU 401 400 400 GLU GLU A . n 
A 1 402 LEU 402 401 401 LEU LEU A . n 
A 1 403 LEU 403 402 402 LEU LEU A . n 
A 1 404 GLU 404 403 403 GLU GLU A . n 
A 1 405 GLY 405 404 404 GLY GLY A . n 
A 1 406 LYS 406 405 405 LYS LYS A . n 
A 1 407 VAL 407 406 406 VAL VAL A . n 
A 1 408 LEU 408 407 407 LEU LEU A . n 
A 1 409 PRO 409 408 408 PRO PRO A . n 
A 1 410 GLY 410 409 409 GLY GLY A . n 
A 1 411 VAL 411 410 410 VAL VAL A . n 
A 1 412 ASP 412 411 411 ASP ASP A . n 
A 1 413 ALA 413 412 412 ALA ALA A . n 
A 1 414 LEU 414 413 413 LEU LEU A . n 
A 1 415 SER 415 414 414 SER SER A . n 
A 1 416 ASN 416 415 415 ASN ASN A . n 
A 1 417 ILE 417 416 416 ILE ILE A . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 ADP ? ? ADP ? ? 'SUBJECT OF INVESTIGATION' ? 
2 X15 ? ? X15 ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 ADP 1   501 1   ADP ADP A . 
C 3 X15 1   502 2   X15 X15 A . 
D 4 PEG 1   503 1   PEG PEG A . 
E 4 PEG 1   504 2   PEG PEG A . 
F 5 CL  1   505 418 CL  CL  A . 
G 6 MG  1   506 1   MG  MG  A . 
H 7 NA  1   507 1   NA  NA  A . 
I 8 HOH 1   601 276 HOH HOH A . 
I 8 HOH 2   602 202 HOH HOH A . 
I 8 HOH 3   603 140 HOH HOH A . 
I 8 HOH 4   604 200 HOH HOH A . 
I 8 HOH 5   605 295 HOH HOH A . 
I 8 HOH 6   606 3   HOH HOH A . 
I 8 HOH 7   607 232 HOH HOH A . 
I 8 HOH 8   608 219 HOH HOH A . 
I 8 HOH 9   609 180 HOH HOH A . 
I 8 HOH 10  610 49  HOH HOH A . 
I 8 HOH 11  611 110 HOH HOH A . 
I 8 HOH 12  612 89  HOH HOH A . 
I 8 HOH 13  613 290 HOH HOH A . 
I 8 HOH 14  614 32  HOH HOH A . 
I 8 HOH 15  615 142 HOH HOH A . 
I 8 HOH 16  616 15  HOH HOH A . 
I 8 HOH 17  617 164 HOH HOH A . 
I 8 HOH 18  618 116 HOH HOH A . 
I 8 HOH 19  619 231 HOH HOH A . 
I 8 HOH 20  620 53  HOH HOH A . 
I 8 HOH 21  621 145 HOH HOH A . 
I 8 HOH 22  622 297 HOH HOH A . 
I 8 HOH 23  623 105 HOH HOH A . 
I 8 HOH 24  624 135 HOH HOH A . 
I 8 HOH 25  625 51  HOH HOH A . 
I 8 HOH 26  626 102 HOH HOH A . 
I 8 HOH 27  627 184 HOH HOH A . 
I 8 HOH 28  628 162 HOH HOH A . 
I 8 HOH 29  629 72  HOH HOH A . 
I 8 HOH 30  630 7   HOH HOH A . 
I 8 HOH 31  631 46  HOH HOH A . 
I 8 HOH 32  632 90  HOH HOH A . 
I 8 HOH 33  633 100 HOH HOH A . 
I 8 HOH 34  634 120 HOH HOH A . 
I 8 HOH 35  635 88  HOH HOH A . 
I 8 HOH 36  636 150 HOH HOH A . 
I 8 HOH 37  637 254 HOH HOH A . 
I 8 HOH 38  638 155 HOH HOH A . 
I 8 HOH 39  639 45  HOH HOH A . 
I 8 HOH 40  640 123 HOH HOH A . 
I 8 HOH 41  641 258 HOH HOH A . 
I 8 HOH 42  642 76  HOH HOH A . 
I 8 HOH 43  643 287 HOH HOH A . 
I 8 HOH 44  644 181 HOH HOH A . 
I 8 HOH 45  645 58  HOH HOH A . 
I 8 HOH 46  646 9   HOH HOH A . 
I 8 HOH 47  647 40  HOH HOH A . 
I 8 HOH 48  648 172 HOH HOH A . 
I 8 HOH 49  649 152 HOH HOH A . 
I 8 HOH 50  650 66  HOH HOH A . 
I 8 HOH 51  651 159 HOH HOH A . 
I 8 HOH 52  652 22  HOH HOH A . 
I 8 HOH 53  653 34  HOH HOH A . 
I 8 HOH 54  654 271 HOH HOH A . 
I 8 HOH 55  655 130 HOH HOH A . 
I 8 HOH 56  656 107 HOH HOH A . 
I 8 HOH 57  657 174 HOH HOH A . 
I 8 HOH 58  658 113 HOH HOH A . 
I 8 HOH 59  659 28  HOH HOH A . 
I 8 HOH 60  660 211 HOH HOH A . 
I 8 HOH 61  661 63  HOH HOH A . 
I 8 HOH 62  662 111 HOH HOH A . 
I 8 HOH 63  663 78  HOH HOH A . 
I 8 HOH 64  664 214 HOH HOH A . 
I 8 HOH 65  665 138 HOH HOH A . 
I 8 HOH 66  666 23  HOH HOH A . 
I 8 HOH 67  667 67  HOH HOH A . 
I 8 HOH 68  668 127 HOH HOH A . 
I 8 HOH 69  669 132 HOH HOH A . 
I 8 HOH 70  670 12  HOH HOH A . 
I 8 HOH 71  671 4   HOH HOH A . 
I 8 HOH 72  672 82  HOH HOH A . 
I 8 HOH 73  673 104 HOH HOH A . 
I 8 HOH 74  674 10  HOH HOH A . 
I 8 HOH 75  675 47  HOH HOH A . 
I 8 HOH 76  676 27  HOH HOH A . 
I 8 HOH 77  677 119 HOH HOH A . 
I 8 HOH 78  678 77  HOH HOH A . 
I 8 HOH 79  679 11  HOH HOH A . 
I 8 HOH 80  680 8   HOH HOH A . 
I 8 HOH 81  681 122 HOH HOH A . 
I 8 HOH 82  682 73  HOH HOH A . 
I 8 HOH 83  683 240 HOH HOH A . 
I 8 HOH 84  684 81  HOH HOH A . 
I 8 HOH 85  685 21  HOH HOH A . 
I 8 HOH 86  686 95  HOH HOH A . 
I 8 HOH 87  687 94  HOH HOH A . 
I 8 HOH 88  688 2   HOH HOH A . 
I 8 HOH 89  689 13  HOH HOH A . 
I 8 HOH 90  690 24  HOH HOH A . 
I 8 HOH 91  691 114 HOH HOH A . 
I 8 HOH 92  692 103 HOH HOH A . 
I 8 HOH 93  693 52  HOH HOH A . 
I 8 HOH 94  694 129 HOH HOH A . 
I 8 HOH 95  695 6   HOH HOH A . 
I 8 HOH 96  696 156 HOH HOH A . 
I 8 HOH 97  697 30  HOH HOH A . 
I 8 HOH 98  698 185 HOH HOH A . 
I 8 HOH 99  699 117 HOH HOH A . 
I 8 HOH 100 700 87  HOH HOH A . 
I 8 HOH 101 701 233 HOH HOH A . 
I 8 HOH 102 702 1   HOH HOH A . 
I 8 HOH 103 703 112 HOH HOH A . 
I 8 HOH 104 704 176 HOH HOH A . 
I 8 HOH 105 705 149 HOH HOH A . 
I 8 HOH 106 706 86  HOH HOH A . 
I 8 HOH 107 707 167 HOH HOH A . 
I 8 HOH 108 708 57  HOH HOH A . 
I 8 HOH 109 709 17  HOH HOH A . 
I 8 HOH 110 710 188 HOH HOH A . 
I 8 HOH 111 711 226 HOH HOH A . 
I 8 HOH 112 712 196 HOH HOH A . 
I 8 HOH 113 713 26  HOH HOH A . 
I 8 HOH 114 714 170 HOH HOH A . 
I 8 HOH 115 715 143 HOH HOH A . 
I 8 HOH 116 716 62  HOH HOH A . 
I 8 HOH 117 717 193 HOH HOH A . 
I 8 HOH 118 718 16  HOH HOH A . 
I 8 HOH 119 719 38  HOH HOH A . 
I 8 HOH 120 720 70  HOH HOH A . 
I 8 HOH 121 721 166 HOH HOH A . 
I 8 HOH 122 722 133 HOH HOH A . 
I 8 HOH 123 723 74  HOH HOH A . 
I 8 HOH 124 724 125 HOH HOH A . 
I 8 HOH 125 725 128 HOH HOH A . 
I 8 HOH 126 726 65  HOH HOH A . 
I 8 HOH 127 727 33  HOH HOH A . 
I 8 HOH 128 728 96  HOH HOH A . 
I 8 HOH 129 729 43  HOH HOH A . 
I 8 HOH 130 730 19  HOH HOH A . 
I 8 HOH 131 731 183 HOH HOH A . 
I 8 HOH 132 732 179 HOH HOH A . 
I 8 HOH 133 733 18  HOH HOH A . 
I 8 HOH 134 734 146 HOH HOH A . 
I 8 HOH 135 735 55  HOH HOH A . 
I 8 HOH 136 736 279 HOH HOH A . 
I 8 HOH 137 737 25  HOH HOH A . 
I 8 HOH 138 738 60  HOH HOH A . 
I 8 HOH 139 739 79  HOH HOH A . 
I 8 HOH 140 740 151 HOH HOH A . 
I 8 HOH 141 741 294 HOH HOH A . 
I 8 HOH 142 742 14  HOH HOH A . 
I 8 HOH 143 743 64  HOH HOH A . 
I 8 HOH 144 744 153 HOH HOH A . 
I 8 HOH 145 745 175 HOH HOH A . 
I 8 HOH 146 746 118 HOH HOH A . 
I 8 HOH 147 747 269 HOH HOH A . 
I 8 HOH 148 748 215 HOH HOH A . 
I 8 HOH 149 749 148 HOH HOH A . 
I 8 HOH 150 750 42  HOH HOH A . 
I 8 HOH 151 751 98  HOH HOH A . 
I 8 HOH 152 752 91  HOH HOH A . 
I 8 HOH 153 753 255 HOH HOH A . 
I 8 HOH 154 754 173 HOH HOH A . 
I 8 HOH 155 755 203 HOH HOH A . 
I 8 HOH 156 756 286 HOH HOH A . 
I 8 HOH 157 757 285 HOH HOH A . 
I 8 HOH 158 758 61  HOH HOH A . 
I 8 HOH 159 759 48  HOH HOH A . 
I 8 HOH 160 760 191 HOH HOH A . 
I 8 HOH 161 761 108 HOH HOH A . 
I 8 HOH 162 762 56  HOH HOH A . 
I 8 HOH 163 763 126 HOH HOH A . 
I 8 HOH 164 764 92  HOH HOH A . 
I 8 HOH 165 765 41  HOH HOH A . 
I 8 HOH 166 766 5   HOH HOH A . 
I 8 HOH 167 767 20  HOH HOH A . 
I 8 HOH 168 768 54  HOH HOH A . 
I 8 HOH 169 769 83  HOH HOH A . 
I 8 HOH 170 770 131 HOH HOH A . 
I 8 HOH 171 771 99  HOH HOH A . 
I 8 HOH 172 772 192 HOH HOH A . 
I 8 HOH 173 773 36  HOH HOH A . 
I 8 HOH 174 774 80  HOH HOH A . 
I 8 HOH 175 775 243 HOH HOH A . 
I 8 HOH 176 776 29  HOH HOH A . 
I 8 HOH 177 777 147 HOH HOH A . 
I 8 HOH 178 778 39  HOH HOH A . 
I 8 HOH 179 779 268 HOH HOH A . 
I 8 HOH 180 780 154 HOH HOH A . 
I 8 HOH 181 781 71  HOH HOH A . 
I 8 HOH 182 782 177 HOH HOH A . 
I 8 HOH 183 783 165 HOH HOH A . 
I 8 HOH 184 784 35  HOH HOH A . 
I 8 HOH 185 785 97  HOH HOH A . 
I 8 HOH 186 786 106 HOH HOH A . 
I 8 HOH 187 787 68  HOH HOH A . 
I 8 HOH 188 788 139 HOH HOH A . 
I 8 HOH 189 789 169 HOH HOH A . 
I 8 HOH 190 790 31  HOH HOH A . 
I 8 HOH 191 791 37  HOH HOH A . 
I 8 HOH 192 792 199 HOH HOH A . 
I 8 HOH 193 793 178 HOH HOH A . 
I 8 HOH 194 794 273 HOH HOH A . 
I 8 HOH 195 795 197 HOH HOH A . 
I 8 HOH 196 796 288 HOH HOH A . 
I 8 HOH 197 797 115 HOH HOH A . 
I 8 HOH 198 798 234 HOH HOH A . 
I 8 HOH 199 799 236 HOH HOH A . 
I 8 HOH 200 800 189 HOH HOH A . 
I 8 HOH 201 801 194 HOH HOH A . 
I 8 HOH 202 802 144 HOH HOH A . 
I 8 HOH 203 803 136 HOH HOH A . 
I 8 HOH 204 804 121 HOH HOH A . 
I 8 HOH 205 805 206 HOH HOH A . 
I 8 HOH 206 806 182 HOH HOH A . 
I 8 HOH 207 807 201 HOH HOH A . 
I 8 HOH 208 808 210 HOH HOH A . 
I 8 HOH 209 809 101 HOH HOH A . 
I 8 HOH 210 810 239 HOH HOH A . 
I 8 HOH 211 811 161 HOH HOH A . 
I 8 HOH 212 812 244 HOH HOH A . 
I 8 HOH 213 813 137 HOH HOH A . 
I 8 HOH 214 814 44  HOH HOH A . 
I 8 HOH 215 815 141 HOH HOH A . 
I 8 HOH 216 816 247 HOH HOH A . 
I 8 HOH 217 817 168 HOH HOH A . 
I 8 HOH 218 818 75  HOH HOH A . 
I 8 HOH 219 819 186 HOH HOH A . 
I 8 HOH 220 820 217 HOH HOH A . 
I 8 HOH 221 821 190 HOH HOH A . 
I 8 HOH 222 822 69  HOH HOH A . 
I 8 HOH 223 823 256 HOH HOH A . 
I 8 HOH 224 824 109 HOH HOH A . 
I 8 HOH 225 825 253 HOH HOH A . 
I 8 HOH 226 826 292 HOH HOH A . 
I 8 HOH 227 827 84  HOH HOH A . 
I 8 HOH 228 828 227 HOH HOH A . 
I 8 HOH 229 829 198 HOH HOH A . 
I 8 HOH 230 830 221 HOH HOH A . 
I 8 HOH 231 831 212 HOH HOH A . 
I 8 HOH 232 832 50  HOH HOH A . 
I 8 HOH 233 833 230 HOH HOH A . 
I 8 HOH 234 834 246 HOH HOH A . 
I 8 HOH 235 835 260 HOH HOH A . 
I 8 HOH 236 836 171 HOH HOH A . 
I 8 HOH 237 837 207 HOH HOH A . 
I 8 HOH 238 838 157 HOH HOH A . 
I 8 HOH 239 839 85  HOH HOH A . 
I 8 HOH 240 840 59  HOH HOH A . 
I 8 HOH 241 841 274 HOH HOH A . 
I 8 HOH 242 842 237 HOH HOH A . 
I 8 HOH 243 843 251 HOH HOH A . 
I 8 HOH 244 844 134 HOH HOH A . 
I 8 HOH 245 845 242 HOH HOH A . 
I 8 HOH 246 846 158 HOH HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? '(1.11.1_2575: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? xia2   ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? xia2   ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.11.1               4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9FDH 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     38.845 
_cell.length_a_esd                 ? 
_cell.length_b                     91.626 
_cell.length_b_esd                 ? 
_cell.length_c                     108.734 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9FDH 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9FDH 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.17 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          43.21 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              6.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    'room temperature' 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;Produced from MgF3 TSA crystals produced in 50 mM Tris (pH 7.5), 20 mM DTT, 25 mM MgCl2, 50 mM 3PG, and 10 mM ADP and supplemented with 20 mM NH4F and 1 mM deferoxamine. Cross-soaked with 35% PEG 2000 MME; 0.1 M Bis/Tris pH 6.5, 20 mM DTT, 25 mM MgCl2, 10mM ATP and 50 mM 3PG
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     83 
_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 EIGER2 XE 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         2016-05-15 
_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   0.97625 
_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                        'DIAMOND BEAMLINE I03' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97625 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I03 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          25.68 
_reflns.entry_id                                       9FDH 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.756 
_reflns.d_resolution_low                               70.12 
_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                                     39322 
_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                           99.25 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                1.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          12.2 
_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                                0.041 
_reflns.pdbx_Rpim_I_all                                0.029 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.029 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.76 
_reflns_shell.d_res_low                                     1.82 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.2 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3849 
_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                               1.9 
_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                               0.544 
_reflns_shell.pdbx_Rpim_I_all                               0.385 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.687 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.3 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.385 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9FDH 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.756 
_refine.ls_d_res_low                             70.067 
_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                     39322 
_refine.ls_number_reflns_R_free                  2000 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.25 
_refine.ls_percent_reflns_R_free                 5.09 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1496 
_refine.ls_R_factor_R_free                       0.1777 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1481 
_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       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 19.25 
_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                            0.19 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.756 
_refine_hist.d_res_low                        70.067 
_refine_hist.number_atoms_solvent             246 
_refine_hist.number_atoms_total               3421 
_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        3116 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         59 
_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' ? 0.010  ? 3260 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.057  ? 4400 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 12.315 ? 1999 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.057  ? 499  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.007  ? 562  ? f_plane_restr      ? ? 
# 
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' 1.7562 1.8001 . . 139 2604 99.00  . . . . 0.3009 . . . . . . . . . . . 0.3283 
'X-RAY DIFFRACTION' 1.8001 1.8488 . . 142 2637 100.00 . . . . 0.2731 . . . . . . . . . . . 0.3258 
'X-RAY DIFFRACTION' 1.8488 1.9032 . . 140 2615 100.00 . . . . 0.2157 . . . . . . . . . . . 0.2596 
'X-RAY DIFFRACTION' 1.9032 1.9646 . . 142 2646 100.00 . . . . 0.1869 . . . . . . . . . . . 0.2223 
'X-RAY DIFFRACTION' 1.9646 2.0349 . . 142 2657 100.00 . . . . 0.1726 . . . . . . . . . . . 0.2329 
'X-RAY DIFFRACTION' 2.0349 2.1163 . . 140 2607 99.00  . . . . 0.1471 . . . . . . . . . . . 0.1888 
'X-RAY DIFFRACTION' 2.1163 2.2127 . . 142 2650 99.00  . . . . 0.1345 . . . . . . . . . . . 0.1652 
'X-RAY DIFFRACTION' 2.2127 2.3293 . . 142 2640 99.00  . . . . 0.1349 . . . . . . . . . . . 0.1695 
'X-RAY DIFFRACTION' 2.3293 2.4753 . . 143 2684 100.00 . . . . 0.1372 . . . . . . . . . . . 0.1695 
'X-RAY DIFFRACTION' 2.4753 2.6664 . . 144 2662 99.00  . . . . 0.1439 . . . . . . . . . . . 0.1609 
'X-RAY DIFFRACTION' 2.6664 2.9347 . . 143 2685 99.00  . . . . 0.1529 . . . . . . . . . . . 0.1953 
'X-RAY DIFFRACTION' 2.9347 3.3594 . . 143 2672 99.00  . . . . 0.1495 . . . . . . . . . . . 0.1765 
'X-RAY DIFFRACTION' 3.3594 4.2324 . . 145 2708 98.00  . . . . 0.1224 . . . . . . . . . . . 0.1560 
'X-RAY DIFFRACTION' 4.2324 70.067 . . 153 2855 98.00  . . . . 0.1363 . . . . . . . . . . . 0.1484 
# 
_struct.entry_id                     9FDH 
_struct.title                        
'Closed Human phosphoglycerate kinase complex with BPG and ADP produced by cross-soaking a TSA crystal' 
_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        9FDH 
_struct_keywords.text            'Phosphoryl transfer Glycolysis ATP binding Rossmann fold, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
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 4 ? 
E N N 4 ? 
F N N 5 ? 
G N N 6 ? 
H N N 7 ? 
I N N 8 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    PGK1_HUMAN 
_struct_ref.pdbx_db_accession          P00558 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSLSNKLTLDKLDVKGKRVVMRVDFNVPMKNNQITNNQRIKAAVPSIKFCLDNGAKSVVLMSHLGRPDGVPMPDKYSLEP
VAVELKSLLGKDVLFLKDCVGPEVEKACANPAAGSVILLENLRFHVEEEGKGKDASGNKVKAEPAKIEAFRASLSKLGDV
YVNDAFGTAHRAHSSMVGVNLPQKAGGFLMKKELNYFAKALESPERPFLAILGGAKVADKIQLINNMLDKVNEMIIGGGM
AFTFLKVLNNMEIGTSLFDEEGAKIVKDLMSKAEKNGVKITLPVDFVTADKFDENAKTGQATVASGIPAGWMGLDCGPES
SKKYAEAVTRAKQIVWNGPVGVFEWEAFARGTKALMDEVVKATSRGCITIIGGGDTATCCAKWNTEDKVSHVSTGGGASL
ELLEGKVLPGVDALSNI
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9FDH 
_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                 417 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P00558 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  417 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       0 
_struct_ref_seq.pdbx_auth_seq_align_end       416 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 1850  ? 
1 MORE         -34   ? 
1 'SSA (A^2)'  17020 ? 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'NMR relaxation study' 
_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 THR A 8   ? LEU A 12  ? THR A 7   LEU A 11  5 ? 5  
HELX_P HELX_P2  AA2 ASN A 37  ? ASN A 53  ? ASN A 36  ASN A 52  1 ? 17 
HELX_P HELX_P3  AA3 MET A 72  ? SER A 77  ? MET A 71  SER A 76  1 ? 6  
HELX_P HELX_P4  AA4 LEU A 78  ? GLY A 90  ? LEU A 77  GLY A 89  1 ? 13 
HELX_P HELX_P5  AA5 GLY A 101 ? ASN A 110 ? GLY A 100 ASN A 109 1 ? 10 
HELX_P HELX_P6  AA6 ASN A 121 ? HIS A 125 ? ASN A 120 HIS A 124 5 ? 5  
HELX_P HELX_P7  AA7 GLU A 143 ? LYS A 156 ? GLU A 142 LYS A 155 1 ? 14 
HELX_P HELX_P8  AA8 ALA A 165 ? ALA A 169 ? ALA A 164 ALA A 168 5 ? 5  
HELX_P HELX_P9  AA9 HIS A 173 ? GLY A 178 ? HIS A 172 GLY A 177 1 ? 6  
HELX_P HELX_P10 AB1 GLY A 187 ? SER A 203 ? GLY A 186 SER A 202 1 ? 17 
HELX_P HELX_P11 AB2 LYS A 216 ? ILE A 221 ? LYS A 215 ILE A 220 1 ? 6  
HELX_P HELX_P12 AB3 LEU A 223 ? LEU A 228 ? LEU A 222 LEU A 227 1 ? 6  
HELX_P HELX_P13 AB4 MET A 240 ? ASN A 250 ? MET A 239 ASN A 249 1 ? 11 
HELX_P HELX_P14 AB5 ASP A 259 ? LYS A 264 ? ASP A 258 LYS A 263 1 ? 6  
HELX_P HELX_P15 AB6 ILE A 265 ? ASN A 276 ? ILE A 264 ASN A 275 1 ? 12 
HELX_P HELX_P16 AB7 GLY A 317 ? ALA A 331 ? GLY A 316 ALA A 330 1 ? 15 
HELX_P HELX_P17 AB8 TRP A 345 ? PHE A 348 ? TRP A 344 PHE A 347 5 ? 4  
HELX_P HELX_P18 AB9 ALA A 349 ? ARG A 365 ? ALA A 348 ARG A 364 1 ? 17 
HELX_P HELX_P19 AC1 ASP A 375 ? TRP A 383 ? ASP A 374 TRP A 382 1 ? 9  
HELX_P HELX_P20 AC2 GLY A 396 ? GLU A 404 ? GLY A 395 GLU A 403 1 ? 9  
HELX_P HELX_P21 AC3 LEU A 408 ? ALA A 413 ? LEU A 407 ALA A 412 1 ? 6  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A ASP 24  O   ? ? ? 1_555 H NA  . NA ? ? A ASP 23  A NA  507 1_555 ? ? ? ? ? ? ? 2.708 ? ? 
metalc2  metalc ? ? A ARG 39  O   ? ? ? 1_555 H NA  . NA ? ? A ARG 38  A NA  507 1_555 ? ? ? ? ? ? ? 2.767 ? ? 
metalc3  metalc ? ? A ASP 375 OD2 ? ? ? 1_555 G MG  . MG ? ? A ASP 374 A MG  506 1_555 ? ? ? ? ? ? ? 2.237 ? ? 
metalc4  metalc ? ? B ADP .   O2B ? ? ? 1_555 G MG  . MG ? ? A ADP 501 A MG  506 1_555 ? ? ? ? ? ? ? 1.900 ? ? 
metalc5  metalc ? ? B ADP .   O2A ? ? ? 1_555 G MG  . MG ? ? A ADP 501 A MG  506 1_555 ? ? ? ? ? ? ? 1.952 ? ? 
metalc6  metalc ? ? C X15 .   OAH ? ? ? 1_555 G MG  . MG ? ? A X15 502 A MG  506 1_555 ? ? ? ? ? ? ? 2.055 ? ? 
metalc7  metalc ? ? G MG  .   MG  ? ? ? 1_555 I HOH . O  ? ? A MG  506 A HOH 688 1_555 ? ? ? ? ? ? ? 2.078 ? ? 
metalc8  metalc ? ? G MG  .   MG  ? ? ? 1_555 I HOH . O  ? ? A MG  506 A HOH 766 1_555 ? ? ? ? ? ? ? 2.086 ? ? 
metalc9  metalc ? ? H NA  .   NA  ? ? ? 1_555 I HOH . O  ? ? A NA  507 A HOH 689 1_555 ? ? ? ? ? ? ? 2.934 ? ? 
metalc10 metalc ? ? H NA  .   NA  ? ? ? 1_555 I HOH . O  ? ? A NA  507 A HOH 742 1_555 ? ? ? ? ? ? ? 2.792 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  O   ? A ASP 24  ? A ASP 23  ? 1_555 NA ? H NA . ? A NA 507 ? 1_555 O   ? A ARG 39 ? A ARG 38  ? 1_555 86.8  ? 
2  O   ? A ASP 24  ? A ASP 23  ? 1_555 NA ? H NA . ? A NA 507 ? 1_555 O   ? I HOH .  ? A HOH 689 ? 1_555 109.9 ? 
3  O   ? A ARG 39  ? A ARG 38  ? 1_555 NA ? H NA . ? A NA 507 ? 1_555 O   ? I HOH .  ? A HOH 689 ? 1_555 154.7 ? 
4  O   ? A ASP 24  ? A ASP 23  ? 1_555 NA ? H NA . ? A NA 507 ? 1_555 O   ? I HOH .  ? A HOH 742 ? 1_555 93.4  ? 
5  O   ? A ARG 39  ? A ARG 38  ? 1_555 NA ? H NA . ? A NA 507 ? 1_555 O   ? I HOH .  ? A HOH 742 ? 1_555 106.6 ? 
6  O   ? I HOH .   ? A HOH 689 ? 1_555 NA ? H NA . ? A NA 507 ? 1_555 O   ? I HOH .  ? A HOH 742 ? 1_555 91.7  ? 
7  OD2 ? A ASP 375 ? A ASP 374 ? 1_555 MG ? G MG . ? A MG 506 ? 1_555 O2B ? B ADP .  ? A ADP 501 ? 1_555 87.1  ? 
8  OD2 ? A ASP 375 ? A ASP 374 ? 1_555 MG ? G MG . ? A MG 506 ? 1_555 O2A ? B ADP .  ? A ADP 501 ? 1_555 95.5  ? 
9  O2B ? B ADP .   ? A ADP 501 ? 1_555 MG ? G MG . ? A MG 506 ? 1_555 O2A ? B ADP .  ? A ADP 501 ? 1_555 91.6  ? 
10 OD2 ? A ASP 375 ? A ASP 374 ? 1_555 MG ? G MG . ? A MG 506 ? 1_555 OAH ? C X15 .  ? A X15 502 ? 1_555 171.7 ? 
11 O2B ? B ADP .   ? A ADP 501 ? 1_555 MG ? G MG . ? A MG 506 ? 1_555 OAH ? C X15 .  ? A X15 502 ? 1_555 93.2  ? 
12 O2A ? B ADP .   ? A ADP 501 ? 1_555 MG ? G MG . ? A MG 506 ? 1_555 OAH ? C X15 .  ? A X15 502 ? 1_555 92.8  ? 
13 OD2 ? A ASP 375 ? A ASP 374 ? 1_555 MG ? G MG . ? A MG 506 ? 1_555 O   ? I HOH .  ? A HOH 688 ? 1_555 87.9  ? 
14 O2B ? B ADP .   ? A ADP 501 ? 1_555 MG ? G MG . ? A MG 506 ? 1_555 O   ? I HOH .  ? A HOH 688 ? 1_555 94.6  ? 
15 O2A ? B ADP .   ? A ADP 501 ? 1_555 MG ? G MG . ? A MG 506 ? 1_555 O   ? I HOH .  ? A HOH 688 ? 1_555 173.2 ? 
16 OAH ? C X15 .   ? A X15 502 ? 1_555 MG ? G MG . ? A MG 506 ? 1_555 O   ? I HOH .  ? A HOH 688 ? 1_555 83.8  ? 
17 OD2 ? A ASP 375 ? A ASP 374 ? 1_555 MG ? G MG . ? A MG 506 ? 1_555 O   ? I HOH .  ? A HOH 766 ? 1_555 88.9  ? 
18 O2B ? B ADP .   ? A ADP 501 ? 1_555 MG ? G MG . ? A MG 506 ? 1_555 O   ? I HOH .  ? A HOH 766 ? 1_555 174.2 ? 
19 O2A ? B ADP .   ? A ADP 501 ? 1_555 MG ? G MG . ? A MG 506 ? 1_555 O   ? I HOH .  ? A HOH 766 ? 1_555 93.0  ? 
20 OAH ? C X15 .   ? A X15 502 ? 1_555 MG ? G MG . ? A MG 506 ? 1_555 O   ? I HOH .  ? A HOH 766 ? 1_555 90.2  ? 
21 O   ? I HOH .   ? A HOH 688 ? 1_555 MG ? G MG . ? A MG 506 ? 1_555 O   ? I HOH .  ? A HOH 766 ? 1_555 81.1  ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          ARG 
_struct_mon_prot_cis.label_seq_id           206 
_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           ARG 
_struct_mon_prot_cis.auth_seq_id            205 
_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    207 
_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     206 
_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       5.25 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 2 ? 
AA3 ? 2 ? 
AA4 ? 6 ? 
AA5 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA4 3 4 ? parallel      
AA4 4 5 ? parallel      
AA4 5 6 ? parallel      
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 94  ? PHE A 95  ? LEU A 93  PHE A 94  
AA1 2 SER A 115 ? LEU A 118 ? SER A 114 LEU A 117 
AA1 3 SER A 57  ? MET A 61  ? SER A 56  MET A 60  
AA1 4 ARG A 18  ? ARG A 22  ? ARG A 17  ARG A 21  
AA1 5 VAL A 160 ? ASN A 163 ? VAL A 159 ASN A 162 
AA1 6 LYS A 184 ? GLY A 186 ? LYS A 183 GLY A 185 
AA2 1 MET A 29  ? LYS A 30  ? MET A 28  LYS A 29  
AA2 2 GLN A 33  ? ILE A 34  ? GLN A 32  ILE A 33  
AA3 1 LYS A 131 ? LYS A 133 ? LYS A 130 LYS A 132 
AA3 2 LYS A 139 ? LYS A 141 ? LYS A 138 LYS A 140 
AA4 1 LYS A 279 ? THR A 281 ? LYS A 278 THR A 280 
AA4 2 GLU A 233 ? ILE A 236 ? GLU A 232 ILE A 235 
AA4 3 PHE A 208 ? LEU A 212 ? PHE A 207 LEU A 211 
AA4 4 GLN A 333 ? ASN A 337 ? GLN A 332 ASN A 336 
AA4 5 ILE A 368 ? GLY A 372 ? ILE A 367 GLY A 371 
AA4 6 HIS A 391 ? SER A 393 ? HIS A 390 SER A 392 
AA5 1 THR A 298 ? THR A 302 ? THR A 297 THR A 301 
AA5 2 ASP A 285 ? ALA A 289 ? ASP A 284 ALA A 288 
AA5 3 MET A 312 ? CYS A 316 ? MET A 311 CYS A 315 
# 
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 LEU A 94  ? N LEU A 93  O LEU A 118 ? O LEU A 117 
AA1 2 3 O ILE A 117 ? O ILE A 116 N LEU A 60  ? N LEU A 59  
AA1 3 4 O VAL A 59  ? O VAL A 58  N VAL A 19  ? N VAL A 18  
AA1 4 5 N VAL A 20  ? N VAL A 19  O VAL A 160 ? O VAL A 159 
AA1 5 6 N TYR A 161 ? N TYR A 160 O ALA A 185 ? O ALA A 184 
AA2 1 2 N LYS A 30  ? N LYS A 29  O GLN A 33  ? O GLN A 32  
AA3 1 2 N GLY A 132 ? N GLY A 131 O VAL A 140 ? O VAL A 139 
AA4 1 2 O THR A 281 ? O THR A 280 N MET A 234 ? N MET A 233 
AA4 2 3 O ILE A 235 ? O ILE A 234 N LEU A 212 ? N LEU A 211 
AA4 3 4 N LEU A 209 ? N LEU A 208 O GLN A 333 ? O GLN A 332 
AA4 4 5 N ILE A 334 ? N ILE A 333 O ILE A 368 ? O ILE A 367 
AA4 5 6 N ILE A 371 ? N ILE A 370 O SER A 393 ? O SER A 392 
AA5 1 2 O ALA A 301 ? O ALA A 300 N PHE A 286 ? N PHE A 285 
AA5 2 3 N VAL A 287 ? N VAL A 286 O ASP A 315 ? O ASP A 314 
# 
_pdbx_entry_details.entry_id                   9FDH 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O  A HOH 658 ? ? O A HOH 802 ? ? 2.10 
2 1 O1 A PEG 503 ? ? O A HOH 601 ? ? 2.10 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 109 ? ? -155.36 70.60  
2 1 ASN A 120 ? ? -39.59  114.16 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined -0.2012 0.5435  -7.6894  0.2023 ? -0.0321 ? 0.0212  ? 0.2364 ? 0.0165  ? 0.1405 ? 2.0168 ? -0.9191 
? 0.6566  ? 3.4021 ? -0.3780 ? 2.8715 ? 0.0220  ? -0.1874 ? -0.0624 ? 0.1787  ? 0.1039  ? 0.1698  ? 0.1383  ? -0.3376 ? -0.0968 ? 
2 'X-RAY DIFFRACTION' ? refined 2.5504  10.7609 -0.6150  0.3893 ? 0.0626  ? -0.0026 ? 0.3040 ? -0.0528 ? 0.2289 ? 2.0621 ? -0.3542 
? -0.0813 ? 3.2342 ? -0.1870 ? 2.2642 ? -0.0551 ? -0.3208 ? 0.2787  ? 0.6899  ? 0.1312  ? -0.1755 ? -0.5262 ? -0.2217 ? -0.0316 ? 
3 'X-RAY DIFFRACTION' ? refined 10.1276 2.9030  -12.4281 0.1614 ? -0.0014 ? -0.0147 ? 0.1921 ? -0.0004 ? 0.2019 ? 1.2829 ? -0.5875 
? -0.0973 ? 1.8570 ? 0.0807  ? 2.7639 ? 0.0163  ? -0.0847 ? 0.0437  ? 0.1463  ? 0.0185  ? -0.2000 ? 0.0549  ? 0.2070  ? -0.0769 ? 
4 'X-RAY DIFFRACTION' ? refined -7.7131 14.4394 -34.5149 0.2420 ? 0.0586  ? -0.0326 ? 0.2434 ? -0.0044 ? 0.2048 ? 1.7721 ? -0.2801 
? -0.2814 ? 1.9018 ? -0.3642 ? 1.5490 ? 0.1068  ? 0.1649  ? 0.1109  ? -0.2523 ? -0.0844 ? 0.1731  ? -0.1136 ? -0.1683 ? -0.0106 ? 
5 'X-RAY DIFFRACTION' ? refined -0.4150 1.0381  -24.7052 0.2059 ? 0.0053  ? 0.0122  ? 0.1679 ? 0.0070  ? 0.2133 ? 3.5596 ? 0.1350  
? 1.4695  ? 1.7242 ? 0.3801  ? 2.6654 ? -0.0113 ? -0.0131 ? 0.0667  ? -0.0582 ? -0.0190 ? 0.0435  ? 0.0914  ? -0.0369 ? 0.0363  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 1 through 88 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 89 through 142 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 143 through 201 )
;
4 'X-RAY DIFFRACTION' 4 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 202 through 364 )
;
5 'X-RAY DIFFRACTION' 5 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 365 through 416 )
;
# 
_pdbx_unobs_or_zero_occ_residues.id               1 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num    1 
_pdbx_unobs_or_zero_occ_residues.polymer_flag     Y 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag   1 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id     A 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id     MET 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id      0 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code     ? 
_pdbx_unobs_or_zero_occ_residues.label_asym_id    A 
_pdbx_unobs_or_zero_occ_residues.label_comp_id    MET 
_pdbx_unobs_or_zero_occ_residues.label_seq_id     1 
# 
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 
ADP PB     P  N N 1   
ADP O1B    O  N N 2   
ADP O2B    O  N N 3   
ADP O3B    O  N N 4   
ADP PA     P  N S 5   
ADP O1A    O  N N 6   
ADP O2A    O  N N 7   
ADP O3A    O  N N 8   
ADP "O5'"  O  N N 9   
ADP "C5'"  C  N N 10  
ADP "C4'"  C  N R 11  
ADP "O4'"  O  N N 12  
ADP "C3'"  C  N S 13  
ADP "O3'"  O  N N 14  
ADP "C2'"  C  N R 15  
ADP "O2'"  O  N N 16  
ADP "C1'"  C  N R 17  
ADP N9     N  Y N 18  
ADP C8     C  Y N 19  
ADP N7     N  Y N 20  
ADP C5     C  Y N 21  
ADP C6     C  Y N 22  
ADP N6     N  N N 23  
ADP N1     N  Y N 24  
ADP C2     C  Y N 25  
ADP N3     N  Y N 26  
ADP C4     C  Y N 27  
ADP HOB2   H  N N 28  
ADP HOB3   H  N N 29  
ADP HOA2   H  N N 30  
ADP "H5'1" H  N N 31  
ADP "H5'2" H  N N 32  
ADP "H4'"  H  N N 33  
ADP "H3'"  H  N N 34  
ADP "HO3'" H  N N 35  
ADP "H2'"  H  N N 36  
ADP "HO2'" H  N N 37  
ADP "H1'"  H  N N 38  
ADP H8     H  N N 39  
ADP HN61   H  N N 40  
ADP HN62   H  N N 41  
ADP H2     H  N N 42  
ALA N      N  N N 43  
ALA CA     C  N S 44  
ALA C      C  N N 45  
ALA O      O  N N 46  
ALA CB     C  N N 47  
ALA OXT    O  N N 48  
ALA H      H  N N 49  
ALA H2     H  N N 50  
ALA HA     H  N N 51  
ALA HB1    H  N N 52  
ALA HB2    H  N N 53  
ALA HB3    H  N N 54  
ALA HXT    H  N N 55  
ARG N      N  N N 56  
ARG CA     C  N S 57  
ARG C      C  N N 58  
ARG O      O  N N 59  
ARG CB     C  N N 60  
ARG CG     C  N N 61  
ARG CD     C  N N 62  
ARG NE     N  N N 63  
ARG CZ     C  N N 64  
ARG NH1    N  N N 65  
ARG NH2    N  N N 66  
ARG OXT    O  N N 67  
ARG H      H  N N 68  
ARG H2     H  N N 69  
ARG HA     H  N N 70  
ARG HB2    H  N N 71  
ARG HB3    H  N N 72  
ARG HG2    H  N N 73  
ARG HG3    H  N N 74  
ARG HD2    H  N N 75  
ARG HD3    H  N N 76  
ARG HE     H  N N 77  
ARG HH11   H  N N 78  
ARG HH12   H  N N 79  
ARG HH21   H  N N 80  
ARG HH22   H  N N 81  
ARG HXT    H  N N 82  
ASN N      N  N N 83  
ASN CA     C  N S 84  
ASN C      C  N N 85  
ASN O      O  N N 86  
ASN CB     C  N N 87  
ASN CG     C  N N 88  
ASN OD1    O  N N 89  
ASN ND2    N  N N 90  
ASN OXT    O  N N 91  
ASN H      H  N N 92  
ASN H2     H  N N 93  
ASN HA     H  N N 94  
ASN HB2    H  N N 95  
ASN HB3    H  N N 96  
ASN HD21   H  N N 97  
ASN HD22   H  N N 98  
ASN HXT    H  N N 99  
ASP N      N  N N 100 
ASP CA     C  N S 101 
ASP C      C  N N 102 
ASP O      O  N N 103 
ASP CB     C  N N 104 
ASP CG     C  N N 105 
ASP OD1    O  N N 106 
ASP OD2    O  N N 107 
ASP OXT    O  N N 108 
ASP H      H  N N 109 
ASP H2     H  N N 110 
ASP HA     H  N N 111 
ASP HB2    H  N N 112 
ASP HB3    H  N N 113 
ASP HD2    H  N N 114 
ASP HXT    H  N N 115 
CL  CL     CL N N 116 
CYS N      N  N N 117 
CYS CA     C  N R 118 
CYS C      C  N N 119 
CYS O      O  N N 120 
CYS CB     C  N N 121 
CYS SG     S  N N 122 
CYS OXT    O  N N 123 
CYS H      H  N N 124 
CYS H2     H  N N 125 
CYS HA     H  N N 126 
CYS HB2    H  N N 127 
CYS HB3    H  N N 128 
CYS HG     H  N N 129 
CYS HXT    H  N N 130 
GLN N      N  N N 131 
GLN CA     C  N S 132 
GLN C      C  N N 133 
GLN O      O  N N 134 
GLN CB     C  N N 135 
GLN CG     C  N N 136 
GLN CD     C  N N 137 
GLN OE1    O  N N 138 
GLN NE2    N  N N 139 
GLN OXT    O  N N 140 
GLN H      H  N N 141 
GLN H2     H  N N 142 
GLN HA     H  N N 143 
GLN HB2    H  N N 144 
GLN HB3    H  N N 145 
GLN HG2    H  N N 146 
GLN HG3    H  N N 147 
GLN HE21   H  N N 148 
GLN HE22   H  N N 149 
GLN HXT    H  N N 150 
GLU N      N  N N 151 
GLU CA     C  N S 152 
GLU C      C  N N 153 
GLU O      O  N N 154 
GLU CB     C  N N 155 
GLU CG     C  N N 156 
GLU CD     C  N N 157 
GLU OE1    O  N N 158 
GLU OE2    O  N N 159 
GLU OXT    O  N N 160 
GLU H      H  N N 161 
GLU H2     H  N N 162 
GLU HA     H  N N 163 
GLU HB2    H  N N 164 
GLU HB3    H  N N 165 
GLU HG2    H  N N 166 
GLU HG3    H  N N 167 
GLU HE2    H  N N 168 
GLU HXT    H  N N 169 
GLY N      N  N N 170 
GLY CA     C  N N 171 
GLY C      C  N N 172 
GLY O      O  N N 173 
GLY OXT    O  N N 174 
GLY H      H  N N 175 
GLY H2     H  N N 176 
GLY HA2    H  N N 177 
GLY HA3    H  N N 178 
GLY HXT    H  N N 179 
HIS N      N  N N 180 
HIS CA     C  N S 181 
HIS C      C  N N 182 
HIS O      O  N N 183 
HIS CB     C  N N 184 
HIS CG     C  Y N 185 
HIS ND1    N  Y N 186 
HIS CD2    C  Y N 187 
HIS CE1    C  Y N 188 
HIS NE2    N  Y N 189 
HIS OXT    O  N N 190 
HIS H      H  N N 191 
HIS H2     H  N N 192 
HIS HA     H  N N 193 
HIS HB2    H  N N 194 
HIS HB3    H  N N 195 
HIS HD1    H  N N 196 
HIS HD2    H  N N 197 
HIS HE1    H  N N 198 
HIS HE2    H  N N 199 
HIS HXT    H  N N 200 
HOH O      O  N N 201 
HOH H1     H  N N 202 
HOH H2     H  N N 203 
ILE N      N  N N 204 
ILE CA     C  N S 205 
ILE C      C  N N 206 
ILE O      O  N N 207 
ILE CB     C  N S 208 
ILE CG1    C  N N 209 
ILE CG2    C  N N 210 
ILE CD1    C  N N 211 
ILE OXT    O  N N 212 
ILE H      H  N N 213 
ILE H2     H  N N 214 
ILE HA     H  N N 215 
ILE HB     H  N N 216 
ILE HG12   H  N N 217 
ILE HG13   H  N N 218 
ILE HG21   H  N N 219 
ILE HG22   H  N N 220 
ILE HG23   H  N N 221 
ILE HD11   H  N N 222 
ILE HD12   H  N N 223 
ILE HD13   H  N N 224 
ILE HXT    H  N N 225 
LEU N      N  N N 226 
LEU CA     C  N S 227 
LEU C      C  N N 228 
LEU O      O  N N 229 
LEU CB     C  N N 230 
LEU CG     C  N N 231 
LEU CD1    C  N N 232 
LEU CD2    C  N N 233 
LEU OXT    O  N N 234 
LEU H      H  N N 235 
LEU H2     H  N N 236 
LEU HA     H  N N 237 
LEU HB2    H  N N 238 
LEU HB3    H  N N 239 
LEU HG     H  N N 240 
LEU HD11   H  N N 241 
LEU HD12   H  N N 242 
LEU HD13   H  N N 243 
LEU HD21   H  N N 244 
LEU HD22   H  N N 245 
LEU HD23   H  N N 246 
LEU HXT    H  N N 247 
LYS N      N  N N 248 
LYS CA     C  N S 249 
LYS C      C  N N 250 
LYS O      O  N N 251 
LYS CB     C  N N 252 
LYS CG     C  N N 253 
LYS CD     C  N N 254 
LYS CE     C  N N 255 
LYS NZ     N  N N 256 
LYS OXT    O  N N 257 
LYS H      H  N N 258 
LYS H2     H  N N 259 
LYS HA     H  N N 260 
LYS HB2    H  N N 261 
LYS HB3    H  N N 262 
LYS HG2    H  N N 263 
LYS HG3    H  N N 264 
LYS HD2    H  N N 265 
LYS HD3    H  N N 266 
LYS HE2    H  N N 267 
LYS HE3    H  N N 268 
LYS HZ1    H  N N 269 
LYS HZ2    H  N N 270 
LYS HZ3    H  N N 271 
LYS HXT    H  N N 272 
MET N      N  N N 273 
MET CA     C  N S 274 
MET C      C  N N 275 
MET O      O  N N 276 
MET CB     C  N N 277 
MET CG     C  N N 278 
MET SD     S  N N 279 
MET CE     C  N N 280 
MET OXT    O  N N 281 
MET H      H  N N 282 
MET H2     H  N N 283 
MET HA     H  N N 284 
MET HB2    H  N N 285 
MET HB3    H  N N 286 
MET HG2    H  N N 287 
MET HG3    H  N N 288 
MET HE1    H  N N 289 
MET HE2    H  N N 290 
MET HE3    H  N N 291 
MET HXT    H  N N 292 
MG  MG     MG N N 293 
NA  NA     NA N N 294 
PEG C1     C  N N 295 
PEG O1     O  N N 296 
PEG C2     C  N N 297 
PEG O2     O  N N 298 
PEG C3     C  N N 299 
PEG C4     C  N N 300 
PEG O4     O  N N 301 
PEG H11    H  N N 302 
PEG H12    H  N N 303 
PEG HO1    H  N N 304 
PEG H21    H  N N 305 
PEG H22    H  N N 306 
PEG H31    H  N N 307 
PEG H32    H  N N 308 
PEG H41    H  N N 309 
PEG H42    H  N N 310 
PEG HO4    H  N N 311 
PHE N      N  N N 312 
PHE CA     C  N S 313 
PHE C      C  N N 314 
PHE O      O  N N 315 
PHE CB     C  N N 316 
PHE CG     C  Y N 317 
PHE CD1    C  Y N 318 
PHE CD2    C  Y N 319 
PHE CE1    C  Y N 320 
PHE CE2    C  Y N 321 
PHE CZ     C  Y N 322 
PHE OXT    O  N N 323 
PHE H      H  N N 324 
PHE H2     H  N N 325 
PHE HA     H  N N 326 
PHE HB2    H  N N 327 
PHE HB3    H  N N 328 
PHE HD1    H  N N 329 
PHE HD2    H  N N 330 
PHE HE1    H  N N 331 
PHE HE2    H  N N 332 
PHE HZ     H  N N 333 
PHE HXT    H  N N 334 
PRO N      N  N N 335 
PRO CA     C  N S 336 
PRO C      C  N N 337 
PRO O      O  N N 338 
PRO CB     C  N N 339 
PRO CG     C  N N 340 
PRO CD     C  N N 341 
PRO OXT    O  N N 342 
PRO H      H  N N 343 
PRO HA     H  N N 344 
PRO HB2    H  N N 345 
PRO HB3    H  N N 346 
PRO HG2    H  N N 347 
PRO HG3    H  N N 348 
PRO HD2    H  N N 349 
PRO HD3    H  N N 350 
PRO HXT    H  N N 351 
SER N      N  N N 352 
SER CA     C  N S 353 
SER C      C  N N 354 
SER O      O  N N 355 
SER CB     C  N N 356 
SER OG     O  N N 357 
SER OXT    O  N N 358 
SER H      H  N N 359 
SER H2     H  N N 360 
SER HA     H  N N 361 
SER HB2    H  N N 362 
SER HB3    H  N N 363 
SER HG     H  N N 364 
SER HXT    H  N N 365 
THR N      N  N N 366 
THR CA     C  N S 367 
THR C      C  N N 368 
THR O      O  N N 369 
THR CB     C  N R 370 
THR OG1    O  N N 371 
THR CG2    C  N N 372 
THR OXT    O  N N 373 
THR H      H  N N 374 
THR H2     H  N N 375 
THR HA     H  N N 376 
THR HB     H  N N 377 
THR HG1    H  N N 378 
THR HG21   H  N N 379 
THR HG22   H  N N 380 
THR HG23   H  N N 381 
THR HXT    H  N N 382 
TRP N      N  N N 383 
TRP CA     C  N S 384 
TRP C      C  N N 385 
TRP O      O  N N 386 
TRP CB     C  N N 387 
TRP CG     C  Y N 388 
TRP CD1    C  Y N 389 
TRP CD2    C  Y N 390 
TRP NE1    N  Y N 391 
TRP CE2    C  Y N 392 
TRP CE3    C  Y N 393 
TRP CZ2    C  Y N 394 
TRP CZ3    C  Y N 395 
TRP CH2    C  Y N 396 
TRP OXT    O  N N 397 
TRP H      H  N N 398 
TRP H2     H  N N 399 
TRP HA     H  N N 400 
TRP HB2    H  N N 401 
TRP HB3    H  N N 402 
TRP HD1    H  N N 403 
TRP HE1    H  N N 404 
TRP HE3    H  N N 405 
TRP HZ2    H  N N 406 
TRP HZ3    H  N N 407 
TRP HH2    H  N N 408 
TRP HXT    H  N N 409 
TYR N      N  N N 410 
TYR CA     C  N S 411 
TYR C      C  N N 412 
TYR O      O  N N 413 
TYR CB     C  N N 414 
TYR CG     C  Y N 415 
TYR CD1    C  Y N 416 
TYR CD2    C  Y N 417 
TYR CE1    C  Y N 418 
TYR CE2    C  Y N 419 
TYR CZ     C  Y N 420 
TYR OH     O  N N 421 
TYR OXT    O  N N 422 
TYR H      H  N N 423 
TYR H2     H  N N 424 
TYR HA     H  N N 425 
TYR HB2    H  N N 426 
TYR HB3    H  N N 427 
TYR HD1    H  N N 428 
TYR HD2    H  N N 429 
TYR HE1    H  N N 430 
TYR HE2    H  N N 431 
TYR HH     H  N N 432 
TYR HXT    H  N N 433 
VAL N      N  N N 434 
VAL CA     C  N S 435 
VAL C      C  N N 436 
VAL O      O  N N 437 
VAL CB     C  N N 438 
VAL CG1    C  N N 439 
VAL CG2    C  N N 440 
VAL OXT    O  N N 441 
VAL H      H  N N 442 
VAL H2     H  N N 443 
VAL HA     H  N N 444 
VAL HB     H  N N 445 
VAL HG11   H  N N 446 
VAL HG12   H  N N 447 
VAL HG13   H  N N 448 
VAL HG21   H  N N 449 
VAL HG22   H  N N 450 
VAL HG23   H  N N 451 
VAL HXT    H  N N 452 
X15 OAG    O  N N 453 
X15 PAO    P  N N 454 
X15 OAH    O  N N 455 
X15 OAF    O  N N 456 
X15 OAK    O  N N 457 
X15 CAM    C  N N 458 
X15 OAB    O  N N 459 
X15 CAL    C  N R 460 
X15 OAA    O  N N 461 
X15 CAI    C  N N 462 
X15 OAJ    O  N N 463 
X15 PAN    P  N N 464 
X15 OAD    O  N N 465 
X15 OAE    O  N N 466 
X15 OAC    O  N N 467 
X15 HAG    H  N N 468 
X15 HAF    H  N N 469 
X15 HAL    H  N N 470 
X15 HAA    H  N N 471 
X15 HAI1   H  N N 472 
X15 HAI2   H  N N 473 
X15 HAD    H  N N 474 
X15 HAE    H  N N 475 
# 
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 
ADP PB    O1B    doub N N 1   
ADP PB    O2B    sing N N 2   
ADP PB    O3B    sing N N 3   
ADP PB    O3A    sing N N 4   
ADP O2B   HOB2   sing N N 5   
ADP O3B   HOB3   sing N N 6   
ADP PA    O1A    doub N N 7   
ADP PA    O2A    sing N N 8   
ADP PA    O3A    sing N N 9   
ADP PA    "O5'"  sing N N 10  
ADP O2A   HOA2   sing N N 11  
ADP "O5'" "C5'"  sing N N 12  
ADP "C5'" "C4'"  sing N N 13  
ADP "C5'" "H5'1" sing N N 14  
ADP "C5'" "H5'2" sing N N 15  
ADP "C4'" "O4'"  sing N N 16  
ADP "C4'" "C3'"  sing N N 17  
ADP "C4'" "H4'"  sing N N 18  
ADP "O4'" "C1'"  sing N N 19  
ADP "C3'" "O3'"  sing N N 20  
ADP "C3'" "C2'"  sing N N 21  
ADP "C3'" "H3'"  sing N N 22  
ADP "O3'" "HO3'" sing N N 23  
ADP "C2'" "O2'"  sing N N 24  
ADP "C2'" "C1'"  sing N N 25  
ADP "C2'" "H2'"  sing N N 26  
ADP "O2'" "HO2'" sing N N 27  
ADP "C1'" N9     sing N N 28  
ADP "C1'" "H1'"  sing N N 29  
ADP N9    C8     sing Y N 30  
ADP N9    C4     sing Y N 31  
ADP C8    N7     doub Y N 32  
ADP C8    H8     sing N N 33  
ADP N7    C5     sing Y N 34  
ADP C5    C6     sing Y N 35  
ADP C5    C4     doub Y N 36  
ADP C6    N6     sing N N 37  
ADP C6    N1     doub Y N 38  
ADP N6    HN61   sing N N 39  
ADP N6    HN62   sing N N 40  
ADP N1    C2     sing Y N 41  
ADP C2    N3     doub Y N 42  
ADP C2    H2     sing N N 43  
ADP N3    C4     sing Y N 44  
ALA N     CA     sing N N 45  
ALA N     H      sing N N 46  
ALA N     H2     sing N N 47  
ALA CA    C      sing N N 48  
ALA CA    CB     sing N N 49  
ALA CA    HA     sing N N 50  
ALA C     O      doub N N 51  
ALA C     OXT    sing N N 52  
ALA CB    HB1    sing N N 53  
ALA CB    HB2    sing N N 54  
ALA CB    HB3    sing N N 55  
ALA OXT   HXT    sing N N 56  
ARG N     CA     sing N N 57  
ARG N     H      sing N N 58  
ARG N     H2     sing N N 59  
ARG CA    C      sing N N 60  
ARG CA    CB     sing N N 61  
ARG CA    HA     sing N N 62  
ARG C     O      doub N N 63  
ARG C     OXT    sing N N 64  
ARG CB    CG     sing N N 65  
ARG CB    HB2    sing N N 66  
ARG CB    HB3    sing N N 67  
ARG CG    CD     sing N N 68  
ARG CG    HG2    sing N N 69  
ARG CG    HG3    sing N N 70  
ARG CD    NE     sing N N 71  
ARG CD    HD2    sing N N 72  
ARG CD    HD3    sing N N 73  
ARG NE    CZ     sing N N 74  
ARG NE    HE     sing N N 75  
ARG CZ    NH1    sing N N 76  
ARG CZ    NH2    doub N N 77  
ARG NH1   HH11   sing N N 78  
ARG NH1   HH12   sing N N 79  
ARG NH2   HH21   sing N N 80  
ARG NH2   HH22   sing N N 81  
ARG OXT   HXT    sing N N 82  
ASN N     CA     sing N N 83  
ASN N     H      sing N N 84  
ASN N     H2     sing N N 85  
ASN CA    C      sing N N 86  
ASN CA    CB     sing N N 87  
ASN CA    HA     sing N N 88  
ASN C     O      doub N N 89  
ASN C     OXT    sing N N 90  
ASN CB    CG     sing N N 91  
ASN CB    HB2    sing N N 92  
ASN CB    HB3    sing N N 93  
ASN CG    OD1    doub N N 94  
ASN CG    ND2    sing N N 95  
ASN ND2   HD21   sing N N 96  
ASN ND2   HD22   sing N N 97  
ASN OXT   HXT    sing N N 98  
ASP N     CA     sing N N 99  
ASP N     H      sing N N 100 
ASP N     H2     sing N N 101 
ASP CA    C      sing N N 102 
ASP CA    CB     sing N N 103 
ASP CA    HA     sing N N 104 
ASP C     O      doub N N 105 
ASP C     OXT    sing N N 106 
ASP CB    CG     sing N N 107 
ASP CB    HB2    sing N N 108 
ASP CB    HB3    sing N N 109 
ASP CG    OD1    doub N N 110 
ASP CG    OD2    sing N N 111 
ASP OD2   HD2    sing N N 112 
ASP OXT   HXT    sing N N 113 
CYS N     CA     sing N N 114 
CYS N     H      sing N N 115 
CYS N     H2     sing N N 116 
CYS CA    C      sing N N 117 
CYS CA    CB     sing N N 118 
CYS CA    HA     sing N N 119 
CYS C     O      doub N N 120 
CYS C     OXT    sing N N 121 
CYS CB    SG     sing N N 122 
CYS CB    HB2    sing N N 123 
CYS CB    HB3    sing N N 124 
CYS SG    HG     sing N N 125 
CYS OXT   HXT    sing N N 126 
GLN N     CA     sing N N 127 
GLN N     H      sing N N 128 
GLN N     H2     sing N N 129 
GLN CA    C      sing N N 130 
GLN CA    CB     sing N N 131 
GLN CA    HA     sing N N 132 
GLN C     O      doub N N 133 
GLN C     OXT    sing N N 134 
GLN CB    CG     sing N N 135 
GLN CB    HB2    sing N N 136 
GLN CB    HB3    sing N N 137 
GLN CG    CD     sing N N 138 
GLN CG    HG2    sing N N 139 
GLN CG    HG3    sing N N 140 
GLN CD    OE1    doub N N 141 
GLN CD    NE2    sing N N 142 
GLN NE2   HE21   sing N N 143 
GLN NE2   HE22   sing N N 144 
GLN OXT   HXT    sing N N 145 
GLU N     CA     sing N N 146 
GLU N     H      sing N N 147 
GLU N     H2     sing N N 148 
GLU CA    C      sing N N 149 
GLU CA    CB     sing N N 150 
GLU CA    HA     sing N N 151 
GLU C     O      doub N N 152 
GLU C     OXT    sing N N 153 
GLU CB    CG     sing N N 154 
GLU CB    HB2    sing N N 155 
GLU CB    HB3    sing N N 156 
GLU CG    CD     sing N N 157 
GLU CG    HG2    sing N N 158 
GLU CG    HG3    sing N N 159 
GLU CD    OE1    doub N N 160 
GLU CD    OE2    sing N N 161 
GLU OE2   HE2    sing N N 162 
GLU OXT   HXT    sing N N 163 
GLY N     CA     sing N N 164 
GLY N     H      sing N N 165 
GLY N     H2     sing N N 166 
GLY CA    C      sing N N 167 
GLY CA    HA2    sing N N 168 
GLY CA    HA3    sing N N 169 
GLY C     O      doub N N 170 
GLY C     OXT    sing N N 171 
GLY OXT   HXT    sing N N 172 
HIS N     CA     sing N N 173 
HIS N     H      sing N N 174 
HIS N     H2     sing N N 175 
HIS CA    C      sing N N 176 
HIS CA    CB     sing N N 177 
HIS CA    HA     sing N N 178 
HIS C     O      doub N N 179 
HIS C     OXT    sing N N 180 
HIS CB    CG     sing N N 181 
HIS CB    HB2    sing N N 182 
HIS CB    HB3    sing N N 183 
HIS CG    ND1    sing Y N 184 
HIS CG    CD2    doub Y N 185 
HIS ND1   CE1    doub Y N 186 
HIS ND1   HD1    sing N N 187 
HIS CD2   NE2    sing Y N 188 
HIS CD2   HD2    sing N N 189 
HIS CE1   NE2    sing Y N 190 
HIS CE1   HE1    sing N N 191 
HIS NE2   HE2    sing N N 192 
HIS OXT   HXT    sing N N 193 
HOH O     H1     sing N N 194 
HOH O     H2     sing N N 195 
ILE N     CA     sing N N 196 
ILE N     H      sing N N 197 
ILE N     H2     sing N N 198 
ILE CA    C      sing N N 199 
ILE CA    CB     sing N N 200 
ILE CA    HA     sing N N 201 
ILE C     O      doub N N 202 
ILE C     OXT    sing N N 203 
ILE CB    CG1    sing N N 204 
ILE CB    CG2    sing N N 205 
ILE CB    HB     sing N N 206 
ILE CG1   CD1    sing N N 207 
ILE CG1   HG12   sing N N 208 
ILE CG1   HG13   sing N N 209 
ILE CG2   HG21   sing N N 210 
ILE CG2   HG22   sing N N 211 
ILE CG2   HG23   sing N N 212 
ILE CD1   HD11   sing N N 213 
ILE CD1   HD12   sing N N 214 
ILE CD1   HD13   sing N N 215 
ILE OXT   HXT    sing N N 216 
LEU N     CA     sing N N 217 
LEU N     H      sing N N 218 
LEU N     H2     sing N N 219 
LEU CA    C      sing N N 220 
LEU CA    CB     sing N N 221 
LEU CA    HA     sing N N 222 
LEU C     O      doub N N 223 
LEU C     OXT    sing N N 224 
LEU CB    CG     sing N N 225 
LEU CB    HB2    sing N N 226 
LEU CB    HB3    sing N N 227 
LEU CG    CD1    sing N N 228 
LEU CG    CD2    sing N N 229 
LEU CG    HG     sing N N 230 
LEU CD1   HD11   sing N N 231 
LEU CD1   HD12   sing N N 232 
LEU CD1   HD13   sing N N 233 
LEU CD2   HD21   sing N N 234 
LEU CD2   HD22   sing N N 235 
LEU CD2   HD23   sing N N 236 
LEU OXT   HXT    sing N N 237 
LYS N     CA     sing N N 238 
LYS N     H      sing N N 239 
LYS N     H2     sing N N 240 
LYS CA    C      sing N N 241 
LYS CA    CB     sing N N 242 
LYS CA    HA     sing N N 243 
LYS C     O      doub N N 244 
LYS C     OXT    sing N N 245 
LYS CB    CG     sing N N 246 
LYS CB    HB2    sing N N 247 
LYS CB    HB3    sing N N 248 
LYS CG    CD     sing N N 249 
LYS CG    HG2    sing N N 250 
LYS CG    HG3    sing N N 251 
LYS CD    CE     sing N N 252 
LYS CD    HD2    sing N N 253 
LYS CD    HD3    sing N N 254 
LYS CE    NZ     sing N N 255 
LYS CE    HE2    sing N N 256 
LYS CE    HE3    sing N N 257 
LYS NZ    HZ1    sing N N 258 
LYS NZ    HZ2    sing N N 259 
LYS NZ    HZ3    sing N N 260 
LYS OXT   HXT    sing N N 261 
MET N     CA     sing N N 262 
MET N     H      sing N N 263 
MET N     H2     sing N N 264 
MET CA    C      sing N N 265 
MET CA    CB     sing N N 266 
MET CA    HA     sing N N 267 
MET C     O      doub N N 268 
MET C     OXT    sing N N 269 
MET CB    CG     sing N N 270 
MET CB    HB2    sing N N 271 
MET CB    HB3    sing N N 272 
MET CG    SD     sing N N 273 
MET CG    HG2    sing N N 274 
MET CG    HG3    sing N N 275 
MET SD    CE     sing N N 276 
MET CE    HE1    sing N N 277 
MET CE    HE2    sing N N 278 
MET CE    HE3    sing N N 279 
MET OXT   HXT    sing N N 280 
PEG C1    O1     sing N N 281 
PEG C1    C2     sing N N 282 
PEG C1    H11    sing N N 283 
PEG C1    H12    sing N N 284 
PEG O1    HO1    sing N N 285 
PEG C2    O2     sing N N 286 
PEG C2    H21    sing N N 287 
PEG C2    H22    sing N N 288 
PEG O2    C3     sing N N 289 
PEG C3    C4     sing N N 290 
PEG C3    H31    sing N N 291 
PEG C3    H32    sing N N 292 
PEG C4    O4     sing N N 293 
PEG C4    H41    sing N N 294 
PEG C4    H42    sing N N 295 
PEG O4    HO4    sing N N 296 
PHE N     CA     sing N N 297 
PHE N     H      sing N N 298 
PHE N     H2     sing N N 299 
PHE CA    C      sing N N 300 
PHE CA    CB     sing N N 301 
PHE CA    HA     sing N N 302 
PHE C     O      doub N N 303 
PHE C     OXT    sing N N 304 
PHE CB    CG     sing N N 305 
PHE CB    HB2    sing N N 306 
PHE CB    HB3    sing N N 307 
PHE CG    CD1    doub Y N 308 
PHE CG    CD2    sing Y N 309 
PHE CD1   CE1    sing Y N 310 
PHE CD1   HD1    sing N N 311 
PHE CD2   CE2    doub Y N 312 
PHE CD2   HD2    sing N N 313 
PHE CE1   CZ     doub Y N 314 
PHE CE1   HE1    sing N N 315 
PHE CE2   CZ     sing Y N 316 
PHE CE2   HE2    sing N N 317 
PHE CZ    HZ     sing N N 318 
PHE OXT   HXT    sing N N 319 
PRO N     CA     sing N N 320 
PRO N     CD     sing N N 321 
PRO N     H      sing N N 322 
PRO CA    C      sing N N 323 
PRO CA    CB     sing N N 324 
PRO CA    HA     sing N N 325 
PRO C     O      doub N N 326 
PRO C     OXT    sing N N 327 
PRO CB    CG     sing N N 328 
PRO CB    HB2    sing N N 329 
PRO CB    HB3    sing N N 330 
PRO CG    CD     sing N N 331 
PRO CG    HG2    sing N N 332 
PRO CG    HG3    sing N N 333 
PRO CD    HD2    sing N N 334 
PRO CD    HD3    sing N N 335 
PRO OXT   HXT    sing N N 336 
SER N     CA     sing N N 337 
SER N     H      sing N N 338 
SER N     H2     sing N N 339 
SER CA    C      sing N N 340 
SER CA    CB     sing N N 341 
SER CA    HA     sing N N 342 
SER C     O      doub N N 343 
SER C     OXT    sing N N 344 
SER CB    OG     sing N N 345 
SER CB    HB2    sing N N 346 
SER CB    HB3    sing N N 347 
SER OG    HG     sing N N 348 
SER OXT   HXT    sing N N 349 
THR N     CA     sing N N 350 
THR N     H      sing N N 351 
THR N     H2     sing N N 352 
THR CA    C      sing N N 353 
THR CA    CB     sing N N 354 
THR CA    HA     sing N N 355 
THR C     O      doub N N 356 
THR C     OXT    sing N N 357 
THR CB    OG1    sing N N 358 
THR CB    CG2    sing N N 359 
THR CB    HB     sing N N 360 
THR OG1   HG1    sing N N 361 
THR CG2   HG21   sing N N 362 
THR CG2   HG22   sing N N 363 
THR CG2   HG23   sing N N 364 
THR OXT   HXT    sing N N 365 
TRP N     CA     sing N N 366 
TRP N     H      sing N N 367 
TRP N     H2     sing N N 368 
TRP CA    C      sing N N 369 
TRP CA    CB     sing N N 370 
TRP CA    HA     sing N N 371 
TRP C     O      doub N N 372 
TRP C     OXT    sing N N 373 
TRP CB    CG     sing N N 374 
TRP CB    HB2    sing N N 375 
TRP CB    HB3    sing N N 376 
TRP CG    CD1    doub Y N 377 
TRP CG    CD2    sing Y N 378 
TRP CD1   NE1    sing Y N 379 
TRP CD1   HD1    sing N N 380 
TRP CD2   CE2    doub Y N 381 
TRP CD2   CE3    sing Y N 382 
TRP NE1   CE2    sing Y N 383 
TRP NE1   HE1    sing N N 384 
TRP CE2   CZ2    sing Y N 385 
TRP CE3   CZ3    doub Y N 386 
TRP CE3   HE3    sing N N 387 
TRP CZ2   CH2    doub Y N 388 
TRP CZ2   HZ2    sing N N 389 
TRP CZ3   CH2    sing Y N 390 
TRP CZ3   HZ3    sing N N 391 
TRP CH2   HH2    sing N N 392 
TRP OXT   HXT    sing N N 393 
TYR N     CA     sing N N 394 
TYR N     H      sing N N 395 
TYR N     H2     sing N N 396 
TYR CA    C      sing N N 397 
TYR CA    CB     sing N N 398 
TYR CA    HA     sing N N 399 
TYR C     O      doub N N 400 
TYR C     OXT    sing N N 401 
TYR CB    CG     sing N N 402 
TYR CB    HB2    sing N N 403 
TYR CB    HB3    sing N N 404 
TYR CG    CD1    doub Y N 405 
TYR CG    CD2    sing Y N 406 
TYR CD1   CE1    sing Y N 407 
TYR CD1   HD1    sing N N 408 
TYR CD2   CE2    doub Y N 409 
TYR CD2   HD2    sing N N 410 
TYR CE1   CZ     doub Y N 411 
TYR CE1   HE1    sing N N 412 
TYR CE2   CZ     sing Y N 413 
TYR CE2   HE2    sing N N 414 
TYR CZ    OH     sing N N 415 
TYR OH    HH     sing N N 416 
TYR OXT   HXT    sing N N 417 
VAL N     CA     sing N N 418 
VAL N     H      sing N N 419 
VAL N     H2     sing N N 420 
VAL CA    C      sing N N 421 
VAL CA    CB     sing N N 422 
VAL CA    HA     sing N N 423 
VAL C     O      doub N N 424 
VAL C     OXT    sing N N 425 
VAL CB    CG1    sing N N 426 
VAL CB    CG2    sing N N 427 
VAL CB    HB     sing N N 428 
VAL CG1   HG11   sing N N 429 
VAL CG1   HG12   sing N N 430 
VAL CG1   HG13   sing N N 431 
VAL CG2   HG21   sing N N 432 
VAL CG2   HG22   sing N N 433 
VAL CG2   HG23   sing N N 434 
VAL OXT   HXT    sing N N 435 
X15 OAG   PAO    sing N N 436 
X15 PAO   OAH    doub N N 437 
X15 PAO   OAF    sing N N 438 
X15 PAO   OAK    sing N N 439 
X15 OAK   CAM    sing N N 440 
X15 CAM   OAB    doub N N 441 
X15 CAM   CAL    sing N N 442 
X15 CAL   OAA    sing N N 443 
X15 CAL   CAI    sing N N 444 
X15 CAI   OAJ    sing N N 445 
X15 OAJ   PAN    sing N N 446 
X15 PAN   OAD    sing N N 447 
X15 PAN   OAE    sing N N 448 
X15 PAN   OAC    doub N N 449 
X15 OAG   HAG    sing N N 450 
X15 OAF   HAF    sing N N 451 
X15 CAL   HAL    sing N N 452 
X15 OAA   HAA    sing N N 453 
X15 CAI   HAI1   sing N N 454 
X15 CAI   HAI2   sing N N 455 
X15 OAD   HAD    sing N N 456 
X15 OAE   HAE    sing N N 457 
# 
_pdbx_audit_support.funding_organization   'Biotechnology and Biological Sciences Research Council (BBSRC)' 
_pdbx_audit_support.country                'United Kingdom' 
_pdbx_audit_support.grant_number           BB/M021637/1 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   1 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   2wzb 
_pdbx_initial_refinement_model.details          'starting crystal complex' 
# 
_atom_sites.entry_id                    9FDH 
_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]   0.025743 
_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]   0.010914 
_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]   0.009197 
_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 
C  
CL 
H  
MG 
N  
NA 
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N      . SER A 1 2   ? 14.646  -2.262  -24.248 1.00 82.43  ? 1   SER A N      1 
ATOM   2    C  CA     . SER A 1 2   ? 13.790  -3.128  -23.451 1.00 76.85  ? 1   SER A CA     1 
ATOM   3    C  C      . SER A 1 2   ? 14.478  -3.499  -22.131 1.00 73.51  ? 1   SER A C      1 
ATOM   4    O  O      . SER A 1 2   ? 15.328  -2.753  -21.631 1.00 72.91  ? 1   SER A O      1 
ATOM   5    C  CB     . SER A 1 2   ? 13.414  -4.386  -24.240 1.00 70.99  ? 1   SER A CB     1 
ATOM   6    O  OG     . SER A 1 2   ? 12.382  -5.114  -23.597 1.00 64.38  ? 1   SER A OG     1 
ATOM   7    N  N      . LEU A 1 3   ? 14.109  -4.656  -21.575 1.00 64.80  ? 2   LEU A N      1 
ATOM   8    C  CA     . LEU A 1 3   ? 14.528  -5.051  -20.236 1.00 52.68  ? 2   LEU A CA     1 
ATOM   9    C  C      . LEU A 1 3   ? 15.574  -6.146  -20.230 1.00 47.88  ? 2   LEU A C      1 
ATOM   10   O  O      . LEU A 1 3   ? 15.949  -6.616  -19.150 1.00 48.83  ? 2   LEU A O      1 
ATOM   11   C  CB     . LEU A 1 3   ? 13.326  -5.527  -19.415 1.00 52.84  ? 2   LEU A CB     1 
ATOM   12   C  CG     . LEU A 1 3   ? 12.296  -4.489  -18.985 1.00 56.63  ? 2   LEU A CG     1 
ATOM   13   C  CD1    . LEU A 1 3   ? 11.240  -5.126  -18.095 1.00 54.86  ? 2   LEU A CD1    1 
ATOM   14   C  CD2    . LEU A 1 3   ? 12.940  -3.342  -18.247 1.00 56.56  ? 2   LEU A CD2    1 
ATOM   15   H  HA     . LEU A 1 3   ? 14.906  -4.278  -19.788 1.00 63.24  ? 2   LEU A HA     1 
ATOM   16   H  HB2    . LEU A 1 3   ? 12.853  -6.193  -19.938 1.00 63.42  ? 2   LEU A HB2    1 
ATOM   17   H  HB3    . LEU A 1 3   ? 13.663  -5.942  -18.606 1.00 63.42  ? 2   LEU A HB3    1 
ATOM   18   H  HG     . LEU A 1 3   ? 11.854  -4.132  -19.772 1.00 67.97  ? 2   LEU A HG     1 
ATOM   19   H  HD11   . LEU A 1 3   ? 10.597  -4.448  -17.834 1.00 65.86  ? 2   LEU A HD11   1 
ATOM   20   H  HD12   . LEU A 1 3   ? 10.794  -5.832  -18.589 1.00 65.86  ? 2   LEU A HD12   1 
ATOM   21   H  HD13   . LEU A 1 3   ? 11.671  -5.494  -17.308 1.00 65.86  ? 2   LEU A HD13   1 
ATOM   22   H  HD21   . LEU A 1 3   ? 12.254  -2.706  -17.991 1.00 67.89  ? 2   LEU A HD21   1 
ATOM   23   H  HD22   . LEU A 1 3   ? 13.384  -3.686  -17.456 1.00 67.89  ? 2   LEU A HD22   1 
ATOM   24   H  HD23   . LEU A 1 3   ? 13.587  -2.915  -18.830 1.00 67.89  ? 2   LEU A HD23   1 
ATOM   25   N  N      . SER A 1 4   ? 16.055  -6.572  -21.398 1.00 46.23  ? 3   SER A N      1 
ATOM   26   C  CA     . SER A 1 4   ? 16.985  -7.692  -21.427 1.00 48.85  ? 3   SER A CA     1 
ATOM   27   C  C      . SER A 1 4   ? 18.193  -7.432  -20.542 1.00 49.70  ? 3   SER A C      1 
ATOM   28   O  O      . SER A 1 4   ? 18.759  -8.370  -19.973 1.00 52.77  ? 3   SER A O      1 
ATOM   29   C  CB     . SER A 1 4   ? 17.426  -7.963  -22.867 1.00 54.78  ? 3   SER A CB     1 
ATOM   30   O  OG     . SER A 1 4   ? 16.427  -7.550  -23.789 1.00 58.78  ? 3   SER A OG     1 
ATOM   31   H  H      . SER A 1 4   ? 15.864  -6.237  -22.166 1.00 55.50  ? 3   SER A H      1 
ATOM   32   H  HA     . SER A 1 4   ? 16.535  -8.485  -21.096 1.00 58.64  ? 3   SER A HA     1 
ATOM   33   H  HB2    . SER A 1 4   ? 18.243  -7.470  -23.045 1.00 65.75  ? 3   SER A HB2    1 
ATOM   34   H  HB3    . SER A 1 4   ? 17.583  -8.914  -22.976 1.00 65.75  ? 3   SER A HB3    1 
ATOM   35   H  HG     . SER A 1 4   ? 16.680  -7.704  -24.575 1.00 70.55  ? 3   SER A HG     1 
ATOM   36   N  N      . ASN A 1 5   ? 18.576  -6.168  -20.380 1.00 46.30  ? 4   ASN A N      1 
ATOM   37   C  CA     A ASN A 1 5   ? 19.749  -5.757  -19.621 0.50 46.28  ? 4   ASN A CA     1 
ATOM   38   C  CA     B ASN A 1 5   ? 19.759  -5.841  -19.594 0.50 46.29  ? 4   ASN A CA     1 
ATOM   39   C  C      . ASN A 1 5   ? 19.424  -5.328  -18.194 1.00 37.84  ? 4   ASN A C      1 
ATOM   40   O  O      . ASN A 1 5   ? 20.330  -4.919  -17.468 1.00 36.49  ? 4   ASN A O      1 
ATOM   41   C  CB     A ASN A 1 5   ? 20.446  -4.593  -20.343 0.50 50.74  ? 4   ASN A CB     1 
ATOM   42   C  CB     B ASN A 1 5   ? 20.610  -4.813  -20.343 0.50 51.09  ? 4   ASN A CB     1 
ATOM   43   C  CG     A ASN A 1 5   ? 19.515  -3.392  -20.568 0.50 49.03  ? 4   ASN A CG     1 
ATOM   44   C  CG     B ASN A 1 5   ? 22.048  -4.809  -19.887 0.50 55.79  ? 4   ASN A CG     1 
ATOM   45   O  OD1    A ASN A 1 5   ? 18.371  -3.542  -21.023 0.50 42.87  ? 4   ASN A OD1    1 
ATOM   46   O  OD1    B ASN A 1 5   ? 22.477  -5.678  -19.123 0.50 63.49  ? 4   ASN A OD1    1 
ATOM   47   N  ND2    A ASN A 1 5   ? 20.005  -2.193  -20.241 0.50 52.88  ? 4   ASN A ND2    1 
ATOM   48   N  ND2    B ASN A 1 5   ? 22.810  -3.832  -20.360 0.50 54.06  ? 4   ASN A ND2    1 
ATOM   49   H  H      A ASN A 1 5   ? 18.149  -5.502  -20.717 0.50 55.58  ? 4   ASN A H      1 
ATOM   50   H  H      B ASN A 1 5   ? 18.170  -5.487  -20.712 0.50 55.58  ? 4   ASN A H      1 
ATOM   51   H  HA     A ASN A 1 5   ? 20.372  -6.499  -19.576 0.50 55.56  ? 4   ASN A HA     1 
ATOM   52   H  HA     B ASN A 1 5   ? 20.292  -6.645  -19.491 0.50 55.57  ? 4   ASN A HA     1 
ATOM   53   H  HB2    A ASN A 1 5   ? 21.199  -4.294  -19.809 0.50 60.90  ? 4   ASN A HB2    1 
ATOM   54   H  HB2    B ASN A 1 5   ? 20.596  -5.021  -21.290 0.50 61.32  ? 4   ASN A HB2    1 
ATOM   55   H  HB3    A ASN A 1 5   ? 20.756  -4.899  -21.210 0.50 60.90  ? 4   ASN A HB3    1 
ATOM   56   H  HB3    B ASN A 1 5   ? 20.244  -3.928  -20.190 0.50 61.32  ? 4   ASN A HB3    1 
ATOM   57   H  HD21   A ASN A 1 5   ? 19.524  -1.489  -20.347 0.50 63.47  ? 4   ASN A HD21   1 
ATOM   58   H  HD21   B ASN A 1 5   ? 23.638  -3.783  -20.132 0.50 64.89  ? 4   ASN A HD21   1 
ATOM   59   H  HD22   A ASN A 1 5   ? 20.802  -2.126  -19.924 0.50 63.47  ? 4   ASN A HD22   1 
ATOM   60   H  HD22   B ASN A 1 5   ? 22.477  -3.248  -20.896 0.50 64.89  ? 4   ASN A HD22   1 
ATOM   61   N  N      . LYS A 1 6   ? 18.165  -5.384  -17.784 1.00 30.33  ? 5   LYS A N      1 
ATOM   62   C  CA     . LYS A 1 6   ? 17.737  -4.809  -16.513 1.00 28.62  ? 5   LYS A CA     1 
ATOM   63   C  C      . LYS A 1 6   ? 17.262  -5.886  -15.551 1.00 28.80  ? 5   LYS A C      1 
ATOM   64   O  O      . LYS A 1 6   ? 16.776  -6.937  -15.966 1.00 32.77  ? 5   LYS A O      1 
ATOM   65   C  CB     . LYS A 1 6   ? 16.603  -3.808  -16.723 1.00 31.15  ? 5   LYS A CB     1 
ATOM   66   C  CG     . LYS A 1 6   ? 16.982  -2.601  -17.582 1.00 37.12  ? 5   LYS A CG     1 
ATOM   67   C  CD     . LYS A 1 6   ? 18.090  -1.801  -16.913 1.00 37.92  ? 5   LYS A CD     1 
ATOM   68   C  CE     . LYS A 1 6   ? 18.197  -0.403  -17.456 1.00 38.67  ? 5   LYS A CE     1 
ATOM   69   N  NZ     . LYS A 1 6   ? 19.209  0.381   -16.705 1.00 37.78  1 5   LYS A NZ     1 
ATOM   70   H  H      . LYS A 1 6   ? 17.529  -5.755  -18.228 1.00 36.42  ? 5   LYS A H      1 
ATOM   71   H  HA     . LYS A 1 6   ? 18.483  -4.343  -16.105 1.00 34.36  ? 5   LYS A HA     1 
ATOM   72   H  HB2    . LYS A 1 6   ? 15.865  -4.261  -17.159 1.00 37.40  ? 5   LYS A HB2    1 
ATOM   73   H  HB3    . LYS A 1 6   ? 16.317  -3.475  -15.857 1.00 37.40  ? 5   LYS A HB3    1 
ATOM   74   H  HG2    . LYS A 1 6   ? 17.302  -2.907  -18.446 1.00 44.56  ? 5   LYS A HG2    1 
ATOM   75   H  HG3    . LYS A 1 6   ? 16.209  -2.026  -17.691 1.00 44.56  ? 5   LYS A HG3    1 
ATOM   76   H  HD2    . LYS A 1 6   ? 17.907  -1.741  -15.962 1.00 45.53  ? 5   LYS A HD2    1 
ATOM   77   H  HD3    . LYS A 1 6   ? 18.938  -2.247  -17.062 1.00 45.53  ? 5   LYS A HD3    1 
ATOM   78   H  HE2    . LYS A 1 6   ? 18.468  -0.440  -18.387 1.00 46.42  ? 5   LYS A HE2    1 
ATOM   79   H  HE3    . LYS A 1 6   ? 17.340  0.042   -17.371 1.00 46.42  ? 5   LYS A HE3    1 
ATOM   80   H  HZ1    . LYS A 1 6   ? 19.262  1.205   -17.036 1.00 45.36  ? 5   LYS A HZ1    1 
ATOM   81   H  HZ2    . LYS A 1 6   ? 18.980  0.429   -15.846 1.00 45.36  ? 5   LYS A HZ2    1 
ATOM   82   H  HZ3    . LYS A 1 6   ? 20.006  -0.009  -16.770 1.00 45.36  ? 5   LYS A HZ3    1 
ATOM   83   N  N      . LEU A 1 7   ? 17.382  -5.593  -14.259 1.00 26.81  ? 6   LEU A N      1 
ATOM   84   C  CA     . LEU A 1 7   ? 16.793  -6.429  -13.222 1.00 27.99  ? 6   LEU A CA     1 
ATOM   85   C  C      . LEU A 1 7   ? 15.267  -6.405  -13.308 1.00 26.04  ? 6   LEU A C      1 
ATOM   86   O  O      . LEU A 1 7   ? 14.652  -5.344  -13.424 1.00 23.23  ? 6   LEU A O      1 
ATOM   87   C  CB     . LEU A 1 7   ? 17.252  -5.932  -11.851 1.00 30.70  ? 6   LEU A CB     1 
ATOM   88   C  CG     . LEU A 1 7   ? 16.850  -6.719  -10.614 1.00 30.53  ? 6   LEU A CG     1 
ATOM   89   C  CD1    . LEU A 1 7   ? 17.531  -8.084  -10.615 1.00 31.14  ? 6   LEU A CD1    1 
ATOM   90   C  CD2    . LEU A 1 7   ? 17.197  -5.928  -9.354  1.00 31.09  ? 6   LEU A CD2    1 
ATOM   91   H  H      . LEU A 1 7   ? 17.804  -4.907  -13.956 1.00 32.19  ? 6   LEU A H      1 
ATOM   92   H  HA     . LEU A 1 7   ? 17.094  -7.344  -13.335 1.00 33.61  ? 6   LEU A HA     1 
ATOM   93   H  HB2    . LEU A 1 7   ? 18.221  -5.899  -11.859 1.00 36.86  ? 6   LEU A HB2    1 
ATOM   94   H  HB3    . LEU A 1 7   ? 16.909  -5.032  -11.733 1.00 36.86  ? 6   LEU A HB3    1 
ATOM   95   H  HG     . LEU A 1 7   ? 15.891  -6.861  -10.626 1.00 36.66  ? 6   LEU A HG     1 
ATOM   96   H  HD11   . LEU A 1 7   ? 17.263  -8.570  -9.819  1.00 37.39  ? 6   LEU A HD11   1 
ATOM   97   H  HD12   . LEU A 1 7   ? 17.259  -8.571  -11.408 1.00 37.39  ? 6   LEU A HD12   1 
ATOM   98   H  HD13   . LEU A 1 7   ? 18.493  -7.957  -10.617 1.00 37.39  ? 6   LEU A HD13   1 
ATOM   99   H  HD21   . LEU A 1 7   ? 16.934  -6.445  -8.576  1.00 37.32  ? 6   LEU A HD21   1 
ATOM   100  H  HD22   . LEU A 1 7   ? 18.153  -5.766  -9.337  1.00 37.32  ? 6   LEU A HD22   1 
ATOM   101  H  HD23   . LEU A 1 7   ? 16.718  -5.085  -9.369  1.00 37.32  ? 6   LEU A HD23   1 
ATOM   102  N  N      . THR A 1 8   ? 14.652  -7.583  -13.250 1.00 26.28  ? 7   THR A N      1 
ATOM   103  C  CA     . THR A 1 8   ? 13.205  -7.696  -13.215 1.00 25.42  ? 7   THR A CA     1 
ATOM   104  C  C      . THR A 1 8   ? 12.784  -8.487  -11.976 1.00 24.95  ? 7   THR A C      1 
ATOM   105  O  O      . THR A 1 8   ? 13.590  -9.150  -11.315 1.00 26.45  ? 7   THR A O      1 
ATOM   106  C  CB     . THR A 1 8   ? 12.660  -8.370  -14.492 1.00 33.25  ? 7   THR A CB     1 
ATOM   107  O  OG1    . THR A 1 8   ? 13.316  -9.629  -14.666 1.00 40.57  ? 7   THR A OG1    1 
ATOM   108  C  CG2    . THR A 1 8   ? 12.920  -7.497  -15.729 1.00 36.34  ? 7   THR A CG2    1 
ATOM   109  H  H      . THR A 1 8   ? 15.060  -8.339  -13.229 1.00 31.56  ? 7   THR A H      1 
ATOM   110  H  HA     . THR A 1 8   ? 12.818  -6.809  -13.153 1.00 30.52  ? 7   THR A HA     1 
ATOM   111  H  HB     . THR A 1 8   ? 11.704  -8.509  -14.406 1.00 39.92  ? 7   THR A HB     1 
ATOM   112  H  HG1    . THR A 1 8   ? 13.170  -10.123 -14.003 1.00 48.71  ? 7   THR A HG1    1 
ATOM   113  H  HG21   . THR A 1 8   ? 12.572  -7.934  -16.522 1.00 43.63  ? 7   THR A HG21   1 
ATOM   114  H  HG22   . THR A 1 8   ? 12.483  -6.637  -15.626 1.00 43.63  ? 7   THR A HG22   1 
ATOM   115  H  HG23   . THR A 1 8   ? 13.873  -7.355  -15.840 1.00 43.63  ? 7   THR A HG23   1 
ATOM   116  N  N      . LEU A 1 9   ? 11.502  -8.366  -11.654 1.00 23.71  ? 8   LEU A N      1 
ATOM   117  C  CA     . LEU A 1 9   ? 10.982  -8.866  -10.387 1.00 22.88  ? 8   LEU A CA     1 
ATOM   118  C  C      . LEU A 1 9   ? 11.160  -10.374 -10.247 1.00 26.13  ? 8   LEU A C      1 
ATOM   119  O  O      . LEU A 1 9   ? 11.400  -10.865 -9.143  1.00 28.67  ? 8   LEU A O      1 
ATOM   120  C  CB     . LEU A 1 9   ? 9.519   -8.438  -10.276 1.00 21.54  ? 8   LEU A CB     1 
ATOM   121  C  CG     . LEU A 1 9   ? 8.681   -8.926  -9.100  1.00 25.43  ? 8   LEU A CG     1 
ATOM   122  C  CD1    . LEU A 1 9   ? 9.304   -8.524  -7.761  1.00 27.16  ? 8   LEU A CD1    1 
ATOM   123  C  CD2    . LEU A 1 9   ? 7.267   -8.356  -9.241  1.00 24.28  ? 8   LEU A CD2    1 
ATOM   124  H  H      . LEU A 1 9   ? 10.909  -7.996  -12.155 1.00 28.47  ? 8   LEU A H      1 
ATOM   125  H  HA     . LEU A 1 9   ? 11.469  -8.443  -9.663  1.00 27.48  ? 8   LEU A HA     1 
ATOM   126  H  HB2    . LEU A 1 9   ? 9.499   -7.468  -10.246 1.00 25.86  ? 8   LEU A HB2    1 
ATOM   127  H  HB3    . LEU A 1 9   ? 9.066   -8.734  -11.081 1.00 25.86  ? 8   LEU A HB3    1 
ATOM   128  H  HG     . LEU A 1 9   ? 8.622   -9.894  -9.130  1.00 30.53  ? 8   LEU A HG     1 
ATOM   129  H  HD11   . LEU A 1 9   ? 8.743   -8.852  -7.041  1.00 32.61  ? 8   LEU A HD11   1 
ATOM   130  H  HD12   . LEU A 1 9   ? 10.189  -8.915  -7.696  1.00 32.61  ? 8   LEU A HD12   1 
ATOM   131  H  HD13   . LEU A 1 9   ? 9.364   -7.557  -7.720  1.00 32.61  ? 8   LEU A HD13   1 
ATOM   132  H  HD21   . LEU A 1 9   ? 6.728   -8.663  -8.495  1.00 29.16  ? 8   LEU A HD21   1 
ATOM   133  H  HD22   . LEU A 1 9   ? 7.316   -7.387  -9.237  1.00 29.16  ? 8   LEU A HD22   1 
ATOM   134  H  HD23   . LEU A 1 9   ? 6.884   -8.666  -10.076 1.00 29.16  ? 8   LEU A HD23   1 
ATOM   135  N  N      . ASP A 1 10  ? 11.094  -11.119 -11.347 1.00 28.94  ? 9   ASP A N      1 
ATOM   136  C  CA     . ASP A 1 10  ? 11.297  -12.563 -11.279 1.00 30.64  ? 9   ASP A CA     1 
ATOM   137  C  C      . ASP A 1 10  ? 12.695  -12.948 -10.829 1.00 32.67  ? 9   ASP A C      1 
ATOM   138  O  O      . ASP A 1 10  ? 12.912  -14.116 -10.492 1.00 36.87  ? 9   ASP A O      1 
ATOM   139  C  CB     . ASP A 1 10  ? 11.026  -13.209 -12.649 1.00 32.22  ? 9   ASP A CB     1 
ATOM   140  C  CG     . ASP A 1 10  ? 11.698  -12.474 -13.794 1.00 35.85  ? 9   ASP A CG     1 
ATOM   141  O  OD1    . ASP A 1 10  ? 11.297  -11.320 -14.090 1.00 35.16  ? 9   ASP A OD1    1 
ATOM   142  O  OD2    . ASP A 1 10  ? 12.604  -13.066 -14.414 1.00 39.35  1 9   ASP A OD2    1 
ATOM   143  H  H      . ASP A 1 10  ? 10.935  -10.818 -12.137 1.00 34.74  ? 9   ASP A H      1 
ATOM   144  H  HA     . ASP A 1 10  ? 10.667  -12.937 -10.644 1.00 36.78  ? 9   ASP A HA     1 
ATOM   145  H  HB2    . ASP A 1 10  ? 11.360  -14.119 -12.640 1.00 38.68  ? 9   ASP A HB2    1 
ATOM   146  H  HB3    . ASP A 1 10  ? 10.070  -13.209 -12.814 1.00 38.68  ? 9   ASP A HB3    1 
ATOM   147  N  N      . LYS A 1 11  ? 13.647  -12.019 -10.830 1.00 27.97  ? 10  LYS A N      1 
ATOM   148  C  CA     . LYS A 1 11  ? 15.000  -12.306 -10.378 1.00 30.20  ? 10  LYS A CA     1 
ATOM   149  C  C      . LYS A 1 11  ? 15.300  -11.656 -9.032  1.00 33.01  ? 10  LYS A C      1 
ATOM   150  O  O      . LYS A 1 11  ? 16.441  -11.717 -8.566  1.00 37.53  ? 10  LYS A O      1 
ATOM   151  C  CB     . LYS A 1 11  ? 16.006  -11.850 -11.433 1.00 33.21  ? 10  LYS A CB     1 
ATOM   152  C  CG     . LYS A 1 11  ? 15.958  -12.704 -12.712 1.00 43.34  ? 10  LYS A CG     1 
ATOM   153  C  CD     . LYS A 1 11  ? 16.775  -12.082 -13.833 1.00 56.98  ? 10  LYS A CD     1 
ATOM   154  C  CE     . LYS A 1 11  ? 16.470  -12.723 -15.190 1.00 58.48  ? 10  LYS A CE     1 
ATOM   155  N  NZ     . LYS A 1 11  ? 15.061  -12.453 -15.630 1.00 52.08  1 10  LYS A NZ     1 
ATOM   156  H  H      . LYS A 1 11  ? 13.531  -11.208 -11.090 1.00 33.58  ? 10  LYS A H      1 
ATOM   157  H  HA     . LYS A 1 11  ? 15.096  -13.265 -10.271 1.00 36.26  ? 10  LYS A HA     1 
ATOM   158  H  HB2    . LYS A 1 11  ? 15.812  -10.932 -11.679 1.00 39.87  ? 10  LYS A HB2    1 
ATOM   159  H  HB3    . LYS A 1 11  ? 16.901  -11.912 -11.064 1.00 39.87  ? 10  LYS A HB3    1 
ATOM   160  H  HG2    . LYS A 1 11  ? 16.321  -13.583 -12.523 1.00 52.02  ? 10  LYS A HG2    1 
ATOM   161  H  HG3    . LYS A 1 11  ? 15.038  -12.778 -13.012 1.00 52.02  ? 10  LYS A HG3    1 
ATOM   162  H  HD2    . LYS A 1 11  ? 16.568  -11.137 -13.892 1.00 68.40  ? 10  LYS A HD2    1 
ATOM   163  H  HD3    . LYS A 1 11  ? 17.719  -12.207 -13.646 1.00 68.40  ? 10  LYS A HD3    1 
ATOM   164  H  HE2    . LYS A 1 11  ? 17.071  -12.358 -15.858 1.00 70.19  ? 10  LYS A HE2    1 
ATOM   165  H  HE3    . LYS A 1 11  ? 16.587  -13.684 -15.123 1.00 70.19  ? 10  LYS A HE3    1 
ATOM   166  H  HZ1    . LYS A 1 11  ? 14.910  -12.836 -16.420 1.00 62.52  ? 10  LYS A HZ1    1 
ATOM   167  H  HZ2    . LYS A 1 11  ? 14.487  -12.783 -15.035 1.00 62.52  ? 10  LYS A HZ2    1 
ATOM   168  H  HZ3    . LYS A 1 11  ? 14.928  -11.576 -15.704 1.00 62.52  ? 10  LYS A HZ3    1 
ATOM   169  N  N      . LEU A 1 12  ? 14.305  -11.052 -8.388  1.00 30.86  ? 11  LEU A N      1 
ATOM   170  C  CA     . LEU A 1 12  ? 14.505  -10.270 -7.169  1.00 32.85  ? 11  LEU A CA     1 
ATOM   171  C  C      . LEU A 1 12  ? 14.058  -11.096 -5.971  1.00 37.32  ? 11  LEU A C      1 
ATOM   172  O  O      . LEU A 1 12  ? 12.916  -11.564 -5.926  1.00 38.95  ? 11  LEU A O      1 
ATOM   173  C  CB     . LEU A 1 12  ? 13.724  -8.955  -7.264  1.00 31.70  ? 11  LEU A CB     1 
ATOM   174  C  CG     . LEU A 1 12  ? 13.780  -7.968  -6.114  1.00 35.33  ? 11  LEU A CG     1 
ATOM   175  C  CD1    . LEU A 1 12  ? 15.196  -7.426  -5.922  1.00 40.43  ? 11  LEU A CD1    1 
ATOM   176  C  CD2    . LEU A 1 12  ? 12.803  -6.860  -6.355  1.00 30.10  ? 11  LEU A CD2    1 
ATOM   177  H  H      . LEU A 1 12  ? 13.484  -11.082 -8.644  1.00 37.06  ? 11  LEU A H      1 
ATOM   178  H  HA     . LEU A 1 12  ? 15.447  -10.062 -7.066  1.00 39.44  ? 11  LEU A HA     1 
ATOM   179  H  HB2    . LEU A 1 12  ? 14.041  -8.483  -8.050  1.00 38.05  ? 11  LEU A HB2    1 
ATOM   180  H  HB3    . LEU A 1 12  ? 12.789  -9.179  -7.392  1.00 38.05  ? 11  LEU A HB3    1 
ATOM   181  H  HG     . LEU A 1 12  ? 13.521  -8.422  -5.297  1.00 42.42  ? 11  LEU A HG     1 
ATOM   182  H  HD11   . LEU A 1 12  ? 15.196  -6.800  -5.181  1.00 48.54  ? 11  LEU A HD11   1 
ATOM   183  H  HD12   . LEU A 1 12  ? 15.793  -8.166  -5.731  1.00 48.54  ? 11  LEU A HD12   1 
ATOM   184  H  HD13   . LEU A 1 12  ? 15.475  -6.977  -6.735  1.00 48.54  ? 11  LEU A HD13   1 
ATOM   185  H  HD21   . LEU A 1 12  ? 12.846  -6.235  -5.615  1.00 36.14  ? 11  LEU A HD21   1 
ATOM   186  H  HD22   . LEU A 1 12  ? 13.034  -6.411  -7.183  1.00 36.14  ? 11  LEU A HD22   1 
ATOM   187  H  HD23   . LEU A 1 12  ? 11.911  -7.236  -6.420  1.00 36.14  ? 11  LEU A HD23   1 
ATOM   188  N  N      . ASP A 1 13  ? 14.962  -11.300 -5.017  1.00 38.12  ? 12  ASP A N      1 
ATOM   189  C  CA     . ASP A 1 13  ? 14.611  -12.011 -3.798  1.00 44.26  ? 12  ASP A CA     1 
ATOM   190  C  C      . ASP A 1 13  ? 13.830  -11.057 -2.899  1.00 41.70  ? 12  ASP A C      1 
ATOM   191  O  O      . ASP A 1 13  ? 14.360  -10.014 -2.487  1.00 43.78  ? 12  ASP A O      1 
ATOM   192  C  CB     . ASP A 1 13  ? 15.866  -12.524 -3.100  1.00 57.84  ? 12  ASP A CB     1 
ATOM   193  C  CG     . ASP A 1 13  ? 15.570  -13.103 -1.736  1.00 69.17  ? 12  ASP A CG     1 
ATOM   194  O  OD1    . ASP A 1 13  ? 14.400  -13.459 -1.482  1.00 70.91  ? 12  ASP A OD1    1 
ATOM   195  O  OD2    . ASP A 1 13  ? 16.505  -13.190 -0.913  1.00 76.07  1 12  ASP A OD2    1 
ATOM   196  H  H      . ASP A 1 13  ? 15.780  -11.037 -5.053  1.00 45.77  ? 12  ASP A H      1 
ATOM   197  H  HA     . ASP A 1 13  ? 14.044  -12.769 -4.013  1.00 53.13  ? 12  ASP A HA     1 
ATOM   198  H  HB2    . ASP A 1 13  ? 16.269  -13.221 -3.642  1.00 69.43  ? 12  ASP A HB2    1 
ATOM   199  H  HB3    . ASP A 1 13  ? 16.489  -11.789 -2.986  1.00 69.43  ? 12  ASP A HB3    1 
ATOM   200  N  N      . VAL A 1 14  ? 12.563  -11.382 -2.633  1.00 34.45  ? 13  VAL A N      1 
ATOM   201  C  CA     . VAL A 1 14  ? 11.714  -10.517 -1.821  1.00 30.59  ? 13  VAL A CA     1 
ATOM   202  C  C      . VAL A 1 14  ? 11.351  -11.136 -0.481  1.00 28.68  ? 13  VAL A C      1 
ATOM   203  O  O      . VAL A 1 14  ? 10.616  -10.510 0.289   1.00 29.40  ? 13  VAL A O      1 
ATOM   204  C  CB     . VAL A 1 14  ? 10.437  -10.106 -2.581  1.00 32.34  ? 13  VAL A CB     1 
ATOM   205  C  CG1    . VAL A 1 14  ? 10.798  -9.333  -3.816  1.00 33.50  ? 13  VAL A CG1    1 
ATOM   206  C  CG2    . VAL A 1 14  ? 9.603   -11.319 -2.917  1.00 32.29  ? 13  VAL A CG2    1 
ATOM   207  H  H      . VAL A 1 14  ? 12.175  -12.097 -2.911  1.00 41.36  ? 13  VAL A H      1 
ATOM   208  H  HA     . VAL A 1 14  ? 12.207  -9.703  -1.634  1.00 36.72  ? 13  VAL A HA     1 
ATOM   209  H  HB     . VAL A 1 14  ? 9.905   -9.528  -2.012  1.00 38.83  ? 13  VAL A HB     1 
ATOM   210  H  HG11   . VAL A 1 14  ? 9.984   -9.084  -4.281  1.00 40.22  ? 13  VAL A HG11   1 
ATOM   211  H  HG12   . VAL A 1 14  ? 11.289  -8.538  -3.557  1.00 40.22  ? 13  VAL A HG12   1 
ATOM   212  H  HG13   . VAL A 1 14  ? 11.348  -9.891  -4.387  1.00 40.22  ? 13  VAL A HG13   1 
ATOM   213  H  HG21   . VAL A 1 14  ? 8.808   -11.033 -3.393  1.00 38.77  ? 13  VAL A HG21   1 
ATOM   214  H  HG22   . VAL A 1 14  ? 10.126  -11.917 -3.474  1.00 38.77  ? 13  VAL A HG22   1 
ATOM   215  H  HG23   . VAL A 1 14  ? 9.353   -11.767 -2.094  1.00 38.77  ? 13  VAL A HG23   1 
ATOM   216  N  N      . LYS A 1 15  ? 11.838  -12.324 -0.170  1.00 29.82  ? 14  LYS A N      1 
ATOM   217  C  CA     . LYS A 1 15  ? 11.442  -12.968 1.075   1.00 33.10  ? 14  LYS A CA     1 
ATOM   218  C  C      . LYS A 1 15  ? 11.953  -12.160 2.259   1.00 36.19  ? 14  LYS A C      1 
ATOM   219  O  O      . LYS A 1 15  ? 13.156  -11.911 2.374   1.00 36.14  ? 14  LYS A O      1 
ATOM   220  C  CB     . LYS A 1 15  ? 11.966  -14.395 1.147   1.00 33.44  ? 14  LYS A CB     1 
ATOM   221  C  CG     . LYS A 1 15  ? 11.467  -15.102 2.410   1.00 38.22  ? 14  LYS A CG     1 
ATOM   222  C  CD     . LYS A 1 15  ? 11.891  -16.542 2.456   1.00 49.61  ? 14  LYS A CD     1 
ATOM   223  C  CE     . LYS A 1 15  ? 11.156  -17.299 3.541   1.00 60.47  ? 14  LYS A CE     1 
ATOM   224  N  NZ     . LYS A 1 15  ? 11.609  -18.725 3.624   1.00 70.29  1 14  LYS A NZ     1 
ATOM   225  H  H      . LYS A 1 15  ? 12.390  -12.775 -0.651  1.00 35.80  ? 14  LYS A H      1 
ATOM   226  H  HA     . LYS A 1 15  ? 10.473  -12.998 1.125   1.00 39.74  ? 14  LYS A HA     1 
ATOM   227  H  HB2    . LYS A 1 15  ? 11.653  -14.891 0.375   1.00 40.14  ? 14  LYS A HB2    1 
ATOM   228  H  HB3    . LYS A 1 15  ? 12.936  -14.380 1.168   1.00 40.14  ? 14  LYS A HB3    1 
ATOM   229  H  HG2    . LYS A 1 15  ? 11.831  -14.654 3.190   1.00 45.88  ? 14  LYS A HG2    1 
ATOM   230  H  HG3    . LYS A 1 15  ? 10.497  -15.071 2.429   1.00 45.88  ? 14  LYS A HG3    1 
ATOM   231  H  HD2    . LYS A 1 15  ? 11.693  -16.962 1.604   1.00 59.55  ? 14  LYS A HD2    1 
ATOM   232  H  HD3    . LYS A 1 15  ? 12.842  -16.591 2.642   1.00 59.55  ? 14  LYS A HD3    1 
ATOM   233  H  HE2    . LYS A 1 15  ? 11.326  -16.876 4.397   1.00 72.58  ? 14  LYS A HE2    1 
ATOM   234  H  HE3    . LYS A 1 15  ? 10.205  -17.293 3.346   1.00 72.58  ? 14  LYS A HE3    1 
ATOM   235  H  HZ1    . LYS A 1 15  ? 11.163  -19.148 4.268   1.00 84.37  ? 14  LYS A HZ1    1 
ATOM   236  H  HZ2    . LYS A 1 15  ? 11.459  -19.137 2.850   1.00 84.37  ? 14  LYS A HZ2    1 
ATOM   237  H  HZ3    . LYS A 1 15  ? 12.479  -18.757 3.806   1.00 84.37  ? 14  LYS A HZ3    1 
ATOM   238  N  N      . GLY A 1 16  ? 11.038  -11.769 3.141   1.00 36.43  ? 15  GLY A N      1 
ATOM   239  C  CA     . GLY A 1 16  ? 11.368  -10.972 4.298   1.00 35.57  ? 15  GLY A CA     1 
ATOM   240  C  C      . GLY A 1 16  ? 11.675  -9.525  4.002   1.00 30.97  ? 15  GLY A C      1 
ATOM   241  O  O      . GLY A 1 16  ? 12.014  -8.788  4.936   1.00 31.82  ? 15  GLY A O      1 
ATOM   242  H  H      . GLY A 1 16  ? 10.201  -11.961 3.082   1.00 43.74  ? 15  GLY A H      1 
ATOM   243  H  HA2    . GLY A 1 16  ? 10.625  -10.999 4.921   1.00 42.70  ? 15  GLY A HA2    1 
ATOM   244  H  HA3    . GLY A 1 16  ? 12.142  -11.358 4.736   1.00 42.70  ? 15  GLY A HA3    1 
ATOM   245  N  N      . LYS A 1 17  ? 11.567  -9.097  2.747   1.00 30.61  ? 16  LYS A N      1 
ATOM   246  C  CA     . LYS A 1 17  ? 11.873  -7.730  2.352   1.00 30.84  ? 16  LYS A CA     1 
ATOM   247  C  C      . LYS A 1 17  ? 10.607  -6.883  2.279   1.00 26.96  ? 16  LYS A C      1 
ATOM   248  O  O      . LYS A 1 17  ? 9.526   -7.369  1.956   1.00 28.24  ? 16  LYS A O      1 
ATOM   249  C  CB     . LYS A 1 17  ? 12.590  -7.694  0.993   1.00 32.11  ? 16  LYS A CB     1 
ATOM   250  C  CG     . LYS A 1 17  ? 13.886  -8.490  0.933   1.00 39.29  ? 16  LYS A CG     1 
ATOM   251  C  CD     . LYS A 1 17  ? 14.953  -7.896  1.834   1.00 52.19  ? 16  LYS A CD     1 
ATOM   252  C  CE     . LYS A 1 17  ? 16.282  -8.606  1.651   1.00 62.70  ? 16  LYS A CE     1 
ATOM   253  N  NZ     . LYS A 1 17  ? 16.665  -8.667  0.201   1.00 62.85  1 16  LYS A NZ     1 
ATOM   254  H  H      . LYS A 1 17  ? 11.313  -9.594  2.092   1.00 36.75  ? 16  LYS A H      1 
ATOM   255  H  HA     . LYS A 1 17  ? 12.462  -7.334  3.014   1.00 37.03  ? 16  LYS A HA     1 
ATOM   256  H  HB2    . LYS A 1 17  ? 11.993  -8.056  0.319   1.00 38.55  ? 16  LYS A HB2    1 
ATOM   257  H  HB3    . LYS A 1 17  ? 12.802  -6.772  0.779   1.00 38.55  ? 16  LYS A HB3    1 
ATOM   258  H  HG2    . LYS A 1 17  ? 13.716  -9.400  1.224   1.00 47.16  ? 16  LYS A HG2    1 
ATOM   259  H  HG3    . LYS A 1 17  ? 14.222  -8.486  0.023   1.00 47.16  ? 16  LYS A HG3    1 
ATOM   260  H  HD2    . LYS A 1 17  ? 15.075  -6.960  1.613   1.00 62.65  ? 16  LYS A HD2    1 
ATOM   261  H  HD3    . LYS A 1 17  ? 14.681  -7.992  2.760   1.00 62.65  ? 16  LYS A HD3    1 
ATOM   262  H  HE2    . LYS A 1 17  ? 16.973  -8.123  2.130   1.00 75.26  ? 16  LYS A HE2    1 
ATOM   263  H  HE3    . LYS A 1 17  ? 16.210  -9.514  1.986   1.00 75.26  ? 16  LYS A HE3    1 
ATOM   264  H  HZ1    . LYS A 1 17  ? 17.445  -9.086  0.110   1.00 75.44  ? 16  LYS A HZ1    1 
ATOM   265  H  HZ2    . LYS A 1 17  ? 16.044  -9.109  -0.259  1.00 75.44  ? 16  LYS A HZ2    1 
ATOM   266  H  HZ3    . LYS A 1 17  ? 16.738  -7.844  -0.128  1.00 75.44  ? 16  LYS A HZ3    1 
ATOM   267  N  N      . ARG A 1 18  ? 10.755  -5.616  2.633   1.00 24.95  ? 17  ARG A N      1 
ATOM   268  C  CA     . ARG A 1 18  ? 9.758   -4.616  2.319   1.00 23.83  ? 17  ARG A CA     1 
ATOM   269  C  C      . ARG A 1 18  ? 9.975   -4.142  0.885   1.00 23.07  ? 17  ARG A C      1 
ATOM   270  O  O      . ARG A 1 18  ? 11.084  -3.759  0.508   1.00 24.46  ? 17  ARG A O      1 
ATOM   271  C  CB     . ARG A 1 18  ? 9.865   -3.432  3.268   1.00 23.89  ? 17  ARG A CB     1 
ATOM   272  C  CG     . ARG A 1 18  ? 9.734   -3.815  4.757   1.00 25.77  ? 17  ARG A CG     1 
ATOM   273  C  CD     . ARG A 1 18  ? 10.020  -2.634  5.639   1.00 28.50  ? 17  ARG A CD     1 
ATOM   274  N  NE     . ARG A 1 18  ? 11.324  -2.061  5.371   1.00 33.68  ? 17  ARG A NE     1 
ATOM   275  C  CZ     . ARG A 1 18  ? 11.569  -0.759  5.223   1.00 37.21  ? 17  ARG A CZ     1 
ATOM   276  N  NH1    . ARG A 1 18  ? 10.594  0.140   5.350   1.00 35.11  1 17  ARG A NH1    1 
ATOM   277  N  NH2    . ARG A 1 18  ? 12.807  -0.348  4.954   1.00 37.72  ? 17  ARG A NH2    1 
ATOM   278  H  H      . ARG A 1 18  ? 11.434  -5.310  3.061   1.00 29.96  ? 17  ARG A H      1 
ATOM   279  H  HA     . ARG A 1 18  ? 8.871   -5.000  2.393   1.00 28.62  ? 17  ARG A HA     1 
ATOM   280  H  HB2    . ARG A 1 18  ? 10.729  -3.010  3.145   1.00 28.57  ? 17  ARG A HB2    1 
ATOM   281  H  HB3    . ARG A 1 18  ? 9.158   -2.801  3.061   1.00 28.57  ? 17  ARG A HB3    1 
ATOM   282  H  HG2    . ARG A 1 18  ? 8.830   -4.117  4.934   1.00 30.93  ? 17  ARG A HG2    1 
ATOM   283  H  HG3    . ARG A 1 18  ? 10.372  -4.515  4.967   1.00 30.93  ? 17  ARG A HG3    1 
ATOM   284  H  HD2    . ARG A 1 18  ? 9.351   -1.950  5.482   1.00 34.22  ? 17  ARG A HD2    1 
ATOM   285  H  HD3    . ARG A 1 18  ? 9.999   -2.917  6.566   1.00 34.22  ? 17  ARG A HD3    1 
ATOM   286  H  HE     . ARG A 1 18  ? 11.990  -2.601  5.302   1.00 40.44  ? 17  ARG A HE     1 
ATOM   287  H  HH11   . ARG A 1 18  ? 9.791   -0.117  5.517   1.00 42.16  ? 17  ARG A HH11   1 
ATOM   288  H  HH12   . ARG A 1 18  ? 10.767  0.977   5.257   1.00 42.16  ? 17  ARG A HH12   1 
ATOM   289  H  HH21   . ARG A 1 18  ? 13.443  -0.922  4.878   1.00 45.28  ? 17  ARG A HH21   1 
ATOM   290  H  HH22   . ARG A 1 18  ? 12.973  0.491   4.870   1.00 45.28  ? 17  ARG A HH22   1 
ATOM   291  N  N      . VAL A 1 19  ? 8.917   -4.161  0.094   1.00 23.90  ? 18  VAL A N      1 
ATOM   292  C  CA     . VAL A 1 19  ? 8.969   -3.770  -1.319  1.00 21.57  ? 18  VAL A CA     1 
ATOM   293  C  C      . VAL A 1 19  ? 8.265   -2.434  -1.459  1.00 23.25  ? 18  VAL A C      1 
ATOM   294  O  O      . VAL A 1 19  ? 7.095   -2.312  -1.086  1.00 27.21  ? 18  VAL A O      1 
ATOM   295  C  CB     . VAL A 1 19  ? 8.296   -4.813  -2.214  1.00 23.71  ? 18  VAL A CB     1 
ATOM   296  C  CG1    . VAL A 1 19  ? 8.355   -4.380  -3.703  1.00 24.36  ? 18  VAL A CG1    1 
ATOM   297  C  CG2    . VAL A 1 19  ? 8.942   -6.165  -2.006  1.00 25.36  ? 18  VAL A CG2    1 
ATOM   298  H  H      . VAL A 1 19  ? 8.133   -4.402  0.353   1.00 28.70  ? 18  VAL A H      1 
ATOM   299  H  HA     . VAL A 1 19  ? 9.892   -3.668  -1.599  1.00 25.91  ? 18  VAL A HA     1 
ATOM   300  H  HB     . VAL A 1 19  ? 7.362   -4.887  -1.962  1.00 28.47  ? 18  VAL A HB     1 
ATOM   301  H  HG11   . VAL A 1 19  ? 7.922   -5.057  -4.246  1.00 29.26  ? 18  VAL A HG11   1 
ATOM   302  H  HG12   . VAL A 1 19  ? 7.895   -3.532  -3.803  1.00 29.26  ? 18  VAL A HG12   1 
ATOM   303  H  HG13   . VAL A 1 19  ? 9.283   -4.286  -3.968  1.00 29.26  ? 18  VAL A HG13   1 
ATOM   304  H  HG21   . VAL A 1 19  ? 8.505   -6.815  -2.579  1.00 30.45  ? 18  VAL A HG21   1 
ATOM   305  H  HG22   . VAL A 1 19  ? 9.883   -6.104  -2.233  1.00 30.45  ? 18  VAL A HG22   1 
ATOM   306  H  HG23   . VAL A 1 19  ? 8.841   -6.423  -1.077  1.00 30.45  ? 18  VAL A HG23   1 
ATOM   307  N  N      . VAL A 1 20  ? 8.961   -1.428  -1.973  1.00 20.39  ? 19  VAL A N      1 
ATOM   308  C  CA     . VAL A 1 20  ? 8.302   -0.184  -2.375  1.00 19.40  ? 19  VAL A CA     1 
ATOM   309  C  C      . VAL A 1 20  ? 8.148   -0.201  -3.900  1.00 20.76  ? 19  VAL A C      1 
ATOM   310  O  O      . VAL A 1 20  ? 9.120   -0.426  -4.646  1.00 18.46  ? 19  VAL A O      1 
ATOM   311  C  CB     . VAL A 1 20  ? 9.053   1.050   -1.828  1.00 24.05  ? 19  VAL A CB     1 
ATOM   312  C  CG1    . VAL A 1 20  ? 10.503  1.093   -2.266  1.00 26.86  ? 19  VAL A CG1    1 
ATOM   313  C  CG2    . VAL A 1 20  ? 8.282   2.373   -2.156  1.00 25.54  ? 19  VAL A CG2    1 
ATOM   314  H  H      . VAL A 1 20  ? 9.811   -1.437  -2.100  1.00 24.48  ? 19  VAL A H      1 
ATOM   315  H  HA     . VAL A 1 20  ? 7.410   -0.172  -1.994  1.00 23.30  ? 19  VAL A HA     1 
ATOM   316  H  HB     . VAL A 1 20  ? 9.064   0.975   -0.861  1.00 28.88  ? 19  VAL A HB     1 
ATOM   317  H  HG11   . VAL A 1 20  ? 10.922  1.885   -1.895  1.00 32.25  ? 19  VAL A HG11   1 
ATOM   318  H  HG12   . VAL A 1 20  ? 10.953  0.297   -1.943  1.00 32.25  ? 19  VAL A HG12   1 
ATOM   319  H  HG13   . VAL A 1 20  ? 10.538  1.123   -3.235  1.00 32.25  ? 19  VAL A HG13   1 
ATOM   320  H  HG21   . VAL A 1 20  ? 8.780   3.125   -1.799  1.00 30.66  ? 19  VAL A HG21   1 
ATOM   321  H  HG22   . VAL A 1 20  ? 8.198   2.459   -3.119  1.00 30.66  ? 19  VAL A HG22   1 
ATOM   322  H  HG23   . VAL A 1 20  ? 7.402   2.335   -1.749  1.00 30.66  ? 19  VAL A HG23   1 
ATOM   323  N  N      . MET A 1 21  ? 6.906   -0.024  -4.359  1.00 18.54  ? 20  MET A N      1 
ATOM   324  C  CA     . MET A 1 21  ? 6.529   -0.313  -5.743  1.00 20.92  ? 20  MET A CA     1 
ATOM   325  C  C      . MET A 1 21  ? 5.823   0.898   -6.325  1.00 20.57  ? 20  MET A C      1 
ATOM   326  O  O      . MET A 1 21  ? 4.766   1.303   -5.816  1.00 21.64  ? 20  MET A O      1 
ATOM   327  C  CB     . MET A 1 21  ? 5.613   -1.542  -5.835  1.00 20.38  ? 20  MET A CB     1 
ATOM   328  C  CG     . MET A 1 21  ? 5.306   -1.918  -7.300  1.00 22.60  ? 20  MET A CG     1 
ATOM   329  S  SD     . MET A 1 21  ? 4.169   -3.328  -7.393  1.00 27.24  ? 20  MET A SD     1 
ATOM   330  C  CE     . MET A 1 21  ? 5.127   -4.667  -6.660  1.00 28.67  ? 20  MET A CE     1 
ATOM   331  H  H      . MET A 1 21  ? 6.254   0.267   -3.878  1.00 22.27  ? 20  MET A H      1 
ATOM   332  H  HA     . MET A 1 21  ? 7.330   -0.494  -6.260  1.00 25.13  ? 20  MET A HA     1 
ATOM   333  H  HB2    . MET A 1 21  ? 6.049   -2.298  -5.413  1.00 24.48  ? 20  MET A HB2    1 
ATOM   334  H  HB3    . MET A 1 21  ? 4.773   -1.348  -5.390  1.00 24.48  ? 20  MET A HB3    1 
ATOM   335  H  HG2    . MET A 1 21  ? 4.891   -1.162  -7.745  1.00 27.14  ? 20  MET A HG2    1 
ATOM   336  H  HG3    . MET A 1 21  ? 6.131   -2.161  -7.748  1.00 27.14  ? 20  MET A HG3    1 
ATOM   337  H  HE1    . MET A 1 21  ? 4.593   -5.477  -6.666  1.00 34.42  ? 20  MET A HE1    1 
ATOM   338  H  HE2    . MET A 1 21  ? 5.934   -4.799  -7.182  1.00 34.42  ? 20  MET A HE2    1 
ATOM   339  H  HE3    . MET A 1 21  ? 5.357   -4.429  -5.749  1.00 34.42  ? 20  MET A HE3    1 
ATOM   340  N  N      . ARG A 1 22  ? 6.422   1.487   -7.359  1.00 19.25  ? 21  ARG A N      1 
ATOM   341  C  CA     . ARG A 1 22  ? 5.745   2.491   -8.165  1.00 17.15  ? 21  ARG A CA     1 
ATOM   342  C  C      . ARG A 1 22  ? 4.782   1.788   -9.108  1.00 18.77  ? 21  ARG A C      1 
ATOM   343  O  O      . ARG A 1 22  ? 5.182   0.889   -9.863  1.00 20.16  ? 21  ARG A O      1 
ATOM   344  C  CB     . ARG A 1 22  ? 6.760   3.322   -8.954  1.00 18.91  ? 21  ARG A CB     1 
ATOM   345  C  CG     . ARG A 1 22  ? 6.490   4.836   -8.979  1.00 21.15  ? 21  ARG A CG     1 
ATOM   346  C  CD     . ARG A 1 22  ? 5.141   5.204   -9.586  1.00 20.55  ? 21  ARG A CD     1 
ATOM   347  N  NE     . ARG A 1 22  ? 5.032   6.647   -9.699  1.00 21.02  ? 21  ARG A NE     1 
ATOM   348  C  CZ     . ARG A 1 22  ? 4.028   7.292   -10.267 1.00 20.75  ? 21  ARG A CZ     1 
ATOM   349  N  NH1    . ARG A 1 22  ? 2.991   6.631   -10.788 1.00 21.33  1 21  ARG A NH1    1 
ATOM   350  N  NH2    . ARG A 1 22  ? 4.083   8.613   -10.344 1.00 20.93  ? 21  ARG A NH2    1 
ATOM   351  H  H      . ARG A 1 22  ? 7.227   1.320   -7.613  1.00 23.12  ? 21  ARG A H      1 
ATOM   352  H  HA     . ARG A 1 22  ? 5.238   3.084   -7.589  1.00 20.60  ? 21  ARG A HA     1 
ATOM   353  H  HB2    . ARG A 1 22  ? 7.638   3.189   -8.563  1.00 22.71  ? 21  ARG A HB2    1 
ATOM   354  H  HB3    . ARG A 1 22  ? 6.764   3.011   -9.873  1.00 22.71  ? 21  ARG A HB3    1 
ATOM   355  H  HG2    . ARG A 1 22  ? 6.509   5.172   -8.069  1.00 25.40  ? 21  ARG A HG2    1 
ATOM   356  H  HG3    . ARG A 1 22  ? 7.181   5.269   -9.504  1.00 25.40  ? 21  ARG A HG3    1 
ATOM   357  H  HD2    . ARG A 1 22  ? 5.067   4.817   -10.472 1.00 24.68  ? 21  ARG A HD2    1 
ATOM   358  H  HD3    . ARG A 1 22  ? 4.428   4.884   -9.012  1.00 24.68  ? 21  ARG A HD3    1 
ATOM   359  H  HE     . ARG A 1 22  ? 5.671   7.120   -9.370  1.00 25.24  ? 21  ARG A HE     1 
ATOM   360  H  HH11   . ARG A 1 22  ? 2.965   5.772   -10.751 1.00 25.62  ? 21  ARG A HH11   1 
ATOM   361  H  HH12   . ARG A 1 22  ? 2.344   7.065   -11.154 1.00 25.62  ? 21  ARG A HH12   1 
ATOM   362  H  HH21   . ARG A 1 22  ? 4.750   9.036   -10.003 1.00 25.13  ? 21  ARG A HH21   1 
ATOM   363  H  HH22   . ARG A 1 22  ? 3.432   9.050   -10.698 1.00 25.13  ? 21  ARG A HH22   1 
ATOM   364  N  N      . VAL A 1 23  ? 3.520   2.216   -9.082  1.00 19.30  ? 22  VAL A N      1 
ATOM   365  C  CA     . VAL A 1 23  ? 2.485   1.726   -9.968  1.00 20.02  ? 22  VAL A CA     1 
ATOM   366  C  C      . VAL A 1 23  ? 1.858   2.935   -10.646 1.00 20.96  ? 22  VAL A C      1 
ATOM   367  O  O      . VAL A 1 23  ? 2.006   4.067   -10.187 1.00 20.69  ? 22  VAL A O      1 
ATOM   368  C  CB     . VAL A 1 23  ? 1.422   0.901   -9.218  1.00 20.30  ? 22  VAL A CB     1 
ATOM   369  C  CG1    . VAL A 1 23  ? 2.014   -0.372  -8.734  1.00 21.79  ? 22  VAL A CG1    1 
ATOM   370  C  CG2    . VAL A 1 23  ? 0.864   1.648   -8.032  1.00 21.77  ? 22  VAL A CG2    1 
ATOM   371  H  H      . VAL A 1 23  ? 3.237   2.816   -8.535  1.00 23.18  ? 22  VAL A H      1 
ATOM   372  H  HA     . VAL A 1 23  ? 2.884   1.163   -10.650 1.00 24.04  ? 22  VAL A HA     1 
ATOM   373  H  HB     . VAL A 1 23  ? 0.691   0.691   -9.820  1.00 24.38  ? 22  VAL A HB     1 
ATOM   374  H  HG11   . VAL A 1 23  ? 1.332   -0.878  -8.265  1.00 26.17  ? 22  VAL A HG11   1 
ATOM   375  H  HG12   . VAL A 1 23  ? 2.338   -0.879  -9.495  1.00 26.17  ? 22  VAL A HG12   1 
ATOM   376  H  HG13   . VAL A 1 23  ? 2.749   -0.170  -8.134  1.00 26.17  ? 22  VAL A HG13   1 
ATOM   377  H  HG21   . VAL A 1 23  ? 0.201   1.093   -7.593  1.00 26.15  ? 22  VAL A HG21   1 
ATOM   378  H  HG22   . VAL A 1 23  ? 1.587   1.850   -7.418  1.00 26.15  ? 22  VAL A HG22   1 
ATOM   379  H  HG23   . VAL A 1 23  ? 0.454   2.471   -8.342  1.00 26.15  ? 22  VAL A HG23   1 
ATOM   380  N  N      . ASP A 1 24  ? 1.148   2.691   -11.753 1.00 18.79  ? 23  ASP A N      1 
ATOM   381  C  CA     . ASP A 1 24  ? 0.337   3.737   -12.376 1.00 20.20  ? 23  ASP A CA     1 
ATOM   382  C  C      . ASP A 1 24  ? -1.116  3.413   -12.036 1.00 21.78  ? 23  ASP A C      1 
ATOM   383  O  O      . ASP A 1 24  ? -1.764  2.608   -12.720 1.00 22.29  ? 23  ASP A O      1 
ATOM   384  C  CB     . ASP A 1 24  ? 0.541   3.854   -13.885 1.00 23.87  ? 23  ASP A CB     1 
ATOM   385  C  CG     . ASP A 1 24  ? -0.193  5.084   -14.475 1.00 24.73  ? 23  ASP A CG     1 
ATOM   386  O  OD1    . ASP A 1 24  ? -1.271  5.430   -13.936 1.00 21.52  ? 23  ASP A OD1    1 
ATOM   387  O  OD2    . ASP A 1 24  ? 0.278   5.697   -15.455 1.00 23.56  1 23  ASP A OD2    1 
ATOM   388  H  H      . ASP A 1 24  ? 1.121   1.933   -12.158 1.00 22.57  ? 23  ASP A H      1 
ATOM   389  H  HA     . ASP A 1 24  ? 0.558   4.592   -11.975 1.00 24.26  ? 23  ASP A HA     1 
ATOM   390  H  HB2    . ASP A 1 24  ? 1.489   3.948   -14.071 1.00 28.66  ? 23  ASP A HB2    1 
ATOM   391  H  HB3    . ASP A 1 24  ? 0.193   3.058   -14.316 1.00 28.66  ? 23  ASP A HB3    1 
ATOM   392  N  N      . PHE A 1 25  ? -1.607  4.057   -10.983 1.00 20.83  ? 24  PHE A N      1 
ATOM   393  C  CA     . PHE A 1 25  ? -2.989  4.006   -10.537 1.00 20.26  ? 24  PHE A CA     1 
ATOM   394  C  C      . PHE A 1 25  ? -3.725  5.288   -10.891 1.00 19.41  ? 24  PHE A C      1 
ATOM   395  O  O      . PHE A 1 25  ? -4.682  5.664   -10.217 1.00 21.26  ? 24  PHE A O      1 
ATOM   396  C  CB     . PHE A 1 25  ? -3.055  3.764   -9.014  1.00 20.85  ? 24  PHE A CB     1 
ATOM   397  C  CG     . PHE A 1 25  ? -2.779  2.336   -8.587  1.00 21.90  ? 24  PHE A CG     1 
ATOM   398  C  CD1    . PHE A 1 25  ? -2.567  1.322   -9.547  1.00 24.77  ? 24  PHE A CD1    1 
ATOM   399  C  CD2    . PHE A 1 25  ? -2.697  2.011   -7.240  1.00 25.69  ? 24  PHE A CD2    1 
ATOM   400  C  CE1    . PHE A 1 25  ? -2.315  0.011   -9.148  1.00 27.88  ? 24  PHE A CE1    1 
ATOM   401  C  CE2    . PHE A 1 25  ? -2.447  0.704   -6.828  1.00 27.89  ? 24  PHE A CE2    1 
ATOM   402  C  CZ     . PHE A 1 25  ? -2.256  -0.298  -7.792  1.00 26.70  ? 24  PHE A CZ     1 
ATOM   403  H  H      . PHE A 1 25  ? -1.122  4.561   -10.482 1.00 25.02  ? 24  PHE A H      1 
ATOM   404  H  HA     . PHE A 1 25  ? -3.438  3.269   -10.980 1.00 24.34  ? 24  PHE A HA     1 
ATOM   405  H  HB2    . PHE A 1 25  ? -2.398  4.332   -8.582  1.00 25.04  ? 24  PHE A HB2    1 
ATOM   406  H  HB3    . PHE A 1 25  ? -3.944  3.997   -8.702  1.00 25.04  ? 24  PHE A HB3    1 
ATOM   407  H  HD1    . PHE A 1 25  ? -2.616  1.527   -10.453 1.00 29.74  ? 24  PHE A HD1    1 
ATOM   408  H  HD2    . PHE A 1 25  ? -2.833  2.673   -6.601  1.00 30.85  ? 24  PHE A HD2    1 
ATOM   409  H  HE1    . PHE A 1 25  ? -2.185  -0.654  -9.785  1.00 33.47  ? 24  PHE A HE1    1 
ATOM   410  H  HE2    . PHE A 1 25  ? -2.403  0.498   -5.922  1.00 33.49  ? 24  PHE A HE2    1 
ATOM   411  H  HZ     . PHE A 1 25  ? -2.080  -1.171  -7.524  1.00 32.06  ? 24  PHE A HZ     1 
ATOM   412  N  N      . ASN A 1 26  ? -3.260  5.994   -11.912 1.00 19.45  ? 25  ASN A N      1 
ATOM   413  C  CA     . ASN A 1 26  ? -3.918  7.203   -12.389 1.00 20.35  ? 25  ASN A CA     1 
ATOM   414  C  C      . ASN A 1 26  ? -5.139  6.818   -13.237 1.00 19.99  ? 25  ASN A C      1 
ATOM   415  O  O      . ASN A 1 26  ? -5.146  6.936   -14.457 1.00 21.90  ? 25  ASN A O      1 
ATOM   416  C  CB     . ASN A 1 26  ? -2.921  8.028   -13.185 1.00 22.81  ? 25  ASN A CB     1 
ATOM   417  C  CG     . ASN A 1 26  ? -3.528  9.307   -13.738 1.00 23.08  ? 25  ASN A CG     1 
ATOM   418  O  OD1    . ASN A 1 26  ? -4.451  9.869   -13.154 1.00 23.37  ? 25  ASN A OD1    1 
ATOM   419  N  ND2    . ASN A 1 26  ? -2.999  9.783   -14.828 1.00 23.28  ? 25  ASN A ND2    1 
ATOM   420  H  H      . ASN A 1 26  ? -2.551  5.789   -12.353 1.00 23.36  ? 25  ASN A H      1 
ATOM   421  H  HA     . ASN A 1 26  ? -4.221  7.730   -11.632 1.00 24.43  ? 25  ASN A HA     1 
ATOM   422  H  HB2    . ASN A 1 26  ? -2.180  8.271   -12.608 1.00 27.40  ? 25  ASN A HB2    1 
ATOM   423  H  HB3    . ASN A 1 26  ? -2.600  7.500   -13.932 1.00 27.40  ? 25  ASN A HB3    1 
ATOM   424  H  HD21   . ASN A 1 26  ? -3.309  10.504  -15.177 1.00 27.96  ? 25  ASN A HD21   1 
ATOM   425  H  HD22   . ASN A 1 26  ? -2.338  9.375   -15.198 1.00 27.96  ? 25  ASN A HD22   1 
ATOM   426  N  N      . VAL A 1 27  ? -6.196  6.380   -12.550 1.00 19.94  ? 26  VAL A N      1 
ATOM   427  C  CA     . VAL A 1 27  ? -7.390  5.832   -13.171 1.00 21.67  ? 26  VAL A CA     1 
ATOM   428  C  C      . VAL A 1 27  ? -8.373  6.940   -13.499 1.00 23.64  ? 26  VAL A C      1 
ATOM   429  O  O      . VAL A 1 27  ? -8.430  7.967   -12.799 1.00 24.63  ? 26  VAL A O      1 
ATOM   430  C  CB     . VAL A 1 27  ? -8.076  4.784   -12.279 1.00 23.89  ? 26  VAL A CB     1 
ATOM   431  C  CG1    . VAL A 1 27  ? -7.193  3.560   -12.114 1.00 25.98  ? 26  VAL A CG1    1 
ATOM   432  C  CG2    . VAL A 1 27  ? -8.477  5.362   -10.910 1.00 24.70  ? 26  VAL A CG2    1 
ATOM   433  H  H      . VAL A 1 27  ? -6.239  6.394   -11.692 1.00 23.94  ? 26  VAL A H      1 
ATOM   434  H  HA     . VAL A 1 27  ? -7.141  5.398   -14.002 1.00 26.03  ? 26  VAL A HA     1 
ATOM   435  H  HB     . VAL A 1 27  ? -8.890  4.495   -12.720 1.00 28.69  ? 26  VAL A HB     1 
ATOM   436  H  HG11   . VAL A 1 27  ? -7.649  2.917   -11.549 1.00 31.19  ? 26  VAL A HG11   1 
ATOM   437  H  HG12   . VAL A 1 27  ? -7.025  3.173   -12.987 1.00 31.19  ? 26  VAL A HG12   1 
ATOM   438  H  HG13   . VAL A 1 27  ? -6.356  3.828   -11.704 1.00 31.19  ? 26  VAL A HG13   1 
ATOM   439  H  HG21   . VAL A 1 27  ? -8.904  4.666   -10.386 1.00 29.66  ? 26  VAL A HG21   1 
ATOM   440  H  HG22   . VAL A 1 27  ? -7.681  5.678   -10.455 1.00 29.66  ? 26  VAL A HG22   1 
ATOM   441  H  HG23   . VAL A 1 27  ? -9.094  6.098   -11.047 1.00 29.66  ? 26  VAL A HG23   1 
ATOM   442  N  N      . PRO A 1 28  ? -9.206  6.752   -14.511 1.00 22.29  ? 27  PRO A N      1 
ATOM   443  C  CA     . PRO A 1 28  ? -10.214 7.767   -14.814 1.00 23.35  ? 27  PRO A CA     1 
ATOM   444  C  C      . PRO A 1 28  ? -11.345 7.737   -13.797 1.00 26.82  ? 27  PRO A C      1 
ATOM   445  O  O      . PRO A 1 28  ? -11.691 6.684   -13.251 1.00 25.84  ? 27  PRO A O      1 
ATOM   446  C  CB     . PRO A 1 28  ? -10.689 7.390   -16.224 1.00 29.56  ? 27  PRO A CB     1 
ATOM   447  C  CG     . PRO A 1 28  ? -10.350 5.925   -16.362 1.00 29.94  ? 27  PRO A CG     1 
ATOM   448  C  CD     . PRO A 1 28  ? -9.138  5.685   -15.539 1.00 25.27  ? 27  PRO A CD     1 
ATOM   449  H  HA     . PRO A 1 28  ? -9.814  8.650   -14.831 1.00 27.92  ? 27  PRO A HA     1 
ATOM   450  H  HB2    . PRO A 1 28  ? -11.646 7.530   -16.297 1.00 35.49  ? 27  PRO A HB2    1 
ATOM   451  H  HB3    . PRO A 1 28  ? -10.211 7.917   -16.883 1.00 35.49  ? 27  PRO A HB3    1 
ATOM   452  H  HG2    . PRO A 1 28  ? -11.091 5.392   -16.035 1.00 35.94  ? 27  PRO A HG2    1 
ATOM   453  H  HG3    . PRO A 1 28  ? -10.173 5.722   -17.293 1.00 35.94  ? 27  PRO A HG3    1 
ATOM   454  H  HD2    . PRO A 1 28  ? -9.179  4.810   -15.123 1.00 30.34  ? 27  PRO A HD2    1 
ATOM   455  H  HD3    . PRO A 1 28  ? -8.338  5.786   -16.078 1.00 30.34  ? 27  PRO A HD3    1 
ATOM   456  N  N      . MET A 1 29  ? -11.867 8.929   -13.502 1.00 31.07  ? 28  MET A N      1 
ATOM   457  C  CA     . MET A 1 29  ? -12.862 9.159   -12.467 1.00 34.06  ? 28  MET A CA     1 
ATOM   458  C  C      . MET A 1 29  ? -14.008 9.963   -13.047 1.00 34.31  ? 28  MET A C      1 
ATOM   459  O  O      . MET A 1 29  ? -13.823 10.765  -13.967 1.00 32.59  ? 28  MET A O      1 
ATOM   460  C  CB     . MET A 1 29  ? -12.296 9.945   -11.278 1.00 34.04  ? 28  MET A CB     1 
ATOM   461  C  CG     . MET A 1 29  ? -11.042 9.387   -10.647 1.00 38.99  ? 28  MET A CG     1 
ATOM   462  S  SD     . MET A 1 29  ? -11.394 8.157   -9.425  1.00 51.43  ? 28  MET A SD     1 
ATOM   463  C  CE     . MET A 1 29  ? -10.166 8.494   -8.185  1.00 57.09  ? 28  MET A CE     1 
ATOM   464  H  H      . MET A 1 29  ? -11.644 9.651   -13.913 1.00 37.30  ? 28  MET A H      1 
ATOM   465  H  HA     . MET A 1 29  ? -13.194 8.307   -12.143 1.00 40.89  ? 28  MET A HA     1 
ATOM   466  H  HB2    . MET A 1 29  ? -12.092 10.844  -11.578 1.00 40.87  ? 28  MET A HB2    1 
ATOM   467  H  HB3    . MET A 1 29  ? -12.975 9.982   -10.587 1.00 40.87  ? 28  MET A HB3    1 
ATOM   468  H  HG2    . MET A 1 29  ? -10.494 8.980   -11.336 1.00 46.81  ? 28  MET A HG2    1 
ATOM   469  H  HG3    . MET A 1 29  ? -10.556 10.108  -10.217 1.00 46.81  ? 28  MET A HG3    1 
ATOM   470  H  HE1    . MET A 1 29  ? -10.272 7.863   -7.456  1.00 68.53  ? 28  MET A HE1    1 
ATOM   471  H  HE2    . MET A 1 29  ? -9.285  8.398   -8.580  1.00 68.53  ? 28  MET A HE2    1 
ATOM   472  H  HE3    . MET A 1 29  ? -10.286 9.400   -7.860  1.00 68.53  ? 28  MET A HE3    1 
ATOM   473  N  N      . LYS A 1 30  ? -15.196 9.751   -12.480 1.00 35.52  ? 29  LYS A N      1 
ATOM   474  C  CA     . LYS A 1 30  ? -16.401 10.446  -12.901 1.00 42.78  ? 29  LYS A CA     1 
ATOM   475  C  C      . LYS A 1 30  ? -17.358 10.348  -11.731 1.00 47.43  ? 29  LYS A C      1 
ATOM   476  O  O      . LYS A 1 30  ? -17.482 9.279   -11.131 1.00 42.58  ? 29  LYS A O      1 
ATOM   477  C  CB     . LYS A 1 30  ? -16.986 9.813   -14.171 1.00 46.68  ? 29  LYS A CB     1 
ATOM   478  C  CG     . LYS A 1 30  ? -18.131 10.552  -14.831 1.00 55.56  ? 29  LYS A CG     1 
ATOM   479  C  CD     . LYS A 1 30  ? -18.510 9.831   -16.130 1.00 64.77  ? 29  LYS A CD     1 
ATOM   480  C  CE     . LYS A 1 30  ? -19.701 10.447  -16.830 1.00 76.46  ? 29  LYS A CE     1 
ATOM   481  N  NZ     . LYS A 1 30  ? -20.167 9.562   -17.934 1.00 80.94  1 29  LYS A NZ     1 
ATOM   482  H  H      . LYS A 1 30  ? -15.328 9.196   -11.836 1.00 42.65  ? 29  LYS A H      1 
ATOM   483  H  HA     . LYS A 1 30  ? -16.204 11.381  -13.073 1.00 51.35  ? 29  LYS A HA     1 
ATOM   484  H  HB2    . LYS A 1 30  ? -16.276 9.739   -14.828 1.00 56.03  ? 29  LYS A HB2    1 
ATOM   485  H  HB3    . LYS A 1 30  ? -17.309 8.927   -13.947 1.00 56.03  ? 29  LYS A HB3    1 
ATOM   486  H  HG2    . LYS A 1 30  ? -18.901 10.557  -14.241 1.00 66.69  ? 29  LYS A HG2    1 
ATOM   487  H  HG3    . LYS A 1 30  ? -17.856 11.457  -15.046 1.00 66.69  ? 29  LYS A HG3    1 
ATOM   488  H  HD2    . LYS A 1 30  ? -17.756 9.864   -16.740 1.00 77.74  ? 29  LYS A HD2    1 
ATOM   489  H  HD3    . LYS A 1 30  ? -18.729 8.908   -15.926 1.00 77.74  ? 29  LYS A HD3    1 
ATOM   490  H  HE2    . LYS A 1 30  ? -20.428 10.556  -16.196 1.00 91.77  ? 29  LYS A HE2    1 
ATOM   491  H  HE3    . LYS A 1 30  ? -19.448 11.303  -17.207 1.00 91.77  ? 29  LYS A HE3    1 
ATOM   492  H  HZ1    . LYS A 1 30  ? -19.514 9.448   -18.528 1.00 97.15  ? 29  LYS A HZ1    1 
ATOM   493  H  HZ2    . LYS A 1 30  ? -20.404 8.768   -17.609 1.00 97.15  ? 29  LYS A HZ2    1 
ATOM   494  H  HZ3    . LYS A 1 30  ? -20.868 9.929   -18.342 1.00 97.15  ? 29  LYS A HZ3    1 
ATOM   495  N  N      . ASN A 1 31  ? -17.973 11.464  -11.362 1.00 55.38  ? 30  ASN A N      1 
ATOM   496  C  CA     . ASN A 1 31  ? -18.829 11.497  -10.176 1.00 57.99  ? 30  ASN A CA     1 
ATOM   497  C  C      . ASN A 1 31  ? -18.118 10.874  -8.976  1.00 58.67  ? 30  ASN A C      1 
ATOM   498  O  O      . ASN A 1 31  ? -18.722 10.154  -8.181  1.00 59.42  ? 30  ASN A O      1 
ATOM   499  C  CB     . ASN A 1 31  ? -20.159 10.793  -10.452 1.00 53.82  ? 30  ASN A CB     1 
ATOM   500  C  CG     . ASN A 1 31  ? -20.950 11.456  -11.570 1.00 54.56  ? 30  ASN A CG     1 
ATOM   501  O  OD1    . ASN A 1 31  ? -21.183 10.868  -12.637 1.00 54.60  ? 30  ASN A OD1    1 
ATOM   502  N  ND2    . ASN A 1 31  ? -21.375 12.689  -11.329 1.00 56.53  ? 30  ASN A ND2    1 
ATOM   503  H  H      . ASN A 1 31  ? -17.914 12.215  -11.777 1.00 66.47  ? 30  ASN A H      1 
ATOM   504  H  HA     . ASN A 1 31  ? -19.023 12.422  -9.957  1.00 69.61  ? 30  ASN A HA     1 
ATOM   505  H  HB2    . ASN A 1 31  ? -19.983 9.875   -10.712 1.00 64.61  ? 30  ASN A HB2    1 
ATOM   506  H  HB3    . ASN A 1 31  ? -20.701 10.813  -9.648  1.00 64.61  ? 30  ASN A HB3    1 
ATOM   507  H  HD21   . ASN A 1 31  ? -21.827 13.112  -11.925 1.00 67.85  ? 30  ASN A HD21   1 
ATOM   508  H  HD22   . ASN A 1 31  ? -21.199 13.064  -10.575 1.00 67.85  ? 30  ASN A HD22   1 
ATOM   509  N  N      . ASN A 1 32  ? -16.808 11.131  -8.867  1.00 59.45  ? 31  ASN A N      1 
ATOM   510  C  CA     . ASN A 1 32  ? -15.959 10.708  -7.749  1.00 61.34  ? 31  ASN A CA     1 
ATOM   511  C  C      . ASN A 1 32  ? -15.759 9.193   -7.683  1.00 52.83  ? 31  ASN A C      1 
ATOM   512  O  O      . ASN A 1 32  ? -15.249 8.674   -6.672  1.00 50.55  ? 31  ASN A O      1 
ATOM   513  C  CB     . ASN A 1 32  ? -16.518 11.214  -6.415  1.00 70.93  ? 31  ASN A CB     1 
ATOM   514  C  CG     . ASN A 1 32  ? -15.468 11.253  -5.306  1.00 77.28  ? 31  ASN A CG     1 
ATOM   515  O  OD1    . ASN A 1 32  ? -14.305 10.881  -5.499  1.00 77.58  ? 31  ASN A OD1    1 
ATOM   516  N  ND2    . ASN A 1 32  ? -15.881 11.722  -4.134  1.00 82.87  ? 31  ASN A ND2    1 
ATOM   517  H  H      . ASN A 1 32  ? -16.370 11.572  -9.461  1.00 71.36  ? 31  ASN A H      1 
ATOM   518  H  HA     . ASN A 1 32  ? -15.083 11.109  -7.866  1.00 73.63  ? 31  ASN A HA     1 
ATOM   519  H  HB2    . ASN A 1 32  ? -16.858 12.114  -6.537  1.00 85.13  ? 31  ASN A HB2    1 
ATOM   520  H  HB3    . ASN A 1 32  ? -17.233 10.625  -6.129  1.00 85.13  ? 31  ASN A HB3    1 
ATOM   521  H  HD21   . ASN A 1 32  ? -15.333 11.768  -3.472  1.00 99.46  ? 31  ASN A HD21   1 
ATOM   522  H  HD22   . ASN A 1 32  ? -16.695 11.980  -4.037  1.00 99.46  ? 31  ASN A HD22   1 
ATOM   523  N  N      . GLN A 1 33  ? -16.118 8.470   -8.741  1.00 41.79  ? 32  GLN A N      1 
ATOM   524  C  CA     . GLN A 1 33  ? -16.034 7.018   -8.803  1.00 38.62  ? 32  GLN A CA     1 
ATOM   525  C  C      . GLN A 1 33  ? -15.078 6.621   -9.924  1.00 31.34  ? 32  GLN A C      1 
ATOM   526  O  O      . GLN A 1 33  ? -14.995 7.311   -10.946 1.00 30.94  ? 32  GLN A O      1 
ATOM   527  C  CB     . GLN A 1 33  ? -17.415 6.398   -9.086  1.00 50.46  ? 32  GLN A CB     1 
ATOM   528  C  CG     . GLN A 1 33  ? -18.493 6.741   -8.094  1.00 64.79  ? 32  GLN A CG     1 
ATOM   529  C  CD     . GLN A 1 33  ? -18.756 5.597   -7.158  1.00 75.98  ? 32  GLN A CD     1 
ATOM   530  O  OE1    . GLN A 1 33  ? -19.715 4.854   -7.334  1.00 89.47  ? 32  GLN A OE1    1 
ATOM   531  N  NE2    . GLN A 1 33  ? -17.893 5.429   -6.167  1.00 73.49  ? 32  GLN A NE2    1 
ATOM   532  H  H      . GLN A 1 33  ? -16.427 8.817   -9.465  1.00 50.17  ? 32  GLN A H      1 
ATOM   533  H  HA     . GLN A 1 33  ? -15.698 6.669   -7.962  1.00 46.36  ? 32  GLN A HA     1 
ATOM   534  H  HB2    . GLN A 1 33  ? -17.715 6.700   -9.957  1.00 60.57  ? 32  GLN A HB2    1 
ATOM   535  H  HB3    . GLN A 1 33  ? -17.323 5.432   -9.092  1.00 60.57  ? 32  GLN A HB3    1 
ATOM   536  H  HG2    . GLN A 1 33  ? -18.213 7.507   -7.568  1.00 77.77  ? 32  GLN A HG2    1 
ATOM   537  H  HG3    . GLN A 1 33  ? -19.315 6.941   -8.569  1.00 77.77  ? 32  GLN A HG3    1 
ATOM   538  H  HE21   . GLN A 1 33  ? -17.223 5.962   -6.085  1.00 88.21  ? 32  GLN A HE21   1 
ATOM   539  H  HE22   . GLN A 1 33  ? -18.003 4.787   -5.605  1.00 88.21  ? 32  GLN A HE22   1 
ATOM   540  N  N      . ILE A 1 34  ? -14.404 5.490   -9.744  1.00 30.14  ? 33  ILE A N      1 
ATOM   541  C  CA     . ILE A 1 34  ? -13.494 4.963   -10.764 1.00 28.28  ? 33  ILE A CA     1 
ATOM   542  C  C      . ILE A 1 34  ? -14.312 4.436   -11.930 1.00 29.53  ? 33  ILE A C      1 
ATOM   543  O  O      . ILE A 1 34  ? -15.268 3.674   -11.736 1.00 31.43  ? 33  ILE A O      1 
ATOM   544  C  CB     . ILE A 1 34  ? -12.622 3.849   -10.171 1.00 27.06  ? 33  ILE A CB     1 
ATOM   545  C  CG1    . ILE A 1 34  ? -11.731 4.405   -9.053  1.00 28.13  ? 33  ILE A CG1    1 
ATOM   546  C  CG2    . ILE A 1 34  ? -11.760 3.191   -11.235 1.00 25.55  ? 33  ILE A CG2    1 
ATOM   547  C  CD1    . ILE A 1 34  ? -11.112 3.332   -8.203  1.00 35.13  ? 33  ILE A CD1    1 
ATOM   548  H  H      . ILE A 1 34  ? -14.454 5.003   -9.037  1.00 36.08  ? 33  ILE A H      1 
ATOM   549  H  HA     . ILE A 1 34  ? -12.917 5.672   -11.085 1.00 33.84  ? 33  ILE A HA     1 
ATOM   550  H  HB     . ILE A 1 34  ? -13.205 3.174   -9.790  1.00 32.38  ? 33  ILE A HB     1 
ATOM   551  H  HG12   . ILE A 1 34  ? -11.013 4.922   -9.451  1.00 33.78  ? 33  ILE A HG12   1 
ATOM   552  H  HG13   . ILE A 1 34  ? -12.266 4.972   -8.476  1.00 33.78  ? 33  ILE A HG13   1 
ATOM   553  H  HG21   . ILE A 1 34  ? -11.225 2.495   -10.821 1.00 30.57  ? 33  ILE A HG21   1 
ATOM   554  H  HG22   . ILE A 1 34  ? -12.336 2.806   -11.914 1.00 30.57  ? 33  ILE A HG22   1 
ATOM   555  H  HG23   . ILE A 1 34  ? -11.182 3.861   -11.632 1.00 30.57  ? 33  ILE A HG23   1 
ATOM   556  H  HD11   . ILE A 1 34  ? -10.564 3.748   -7.519  1.00 42.17  ? 33  ILE A HD11   1 
ATOM   557  H  HD12   . ILE A 1 34  ? -11.818 2.811   -7.790  1.00 42.17  ? 33  ILE A HD12   1 
ATOM   558  H  HD13   . ILE A 1 34  ? -10.564 2.762   -8.765  1.00 42.17  ? 33  ILE A HD13   1 
ATOM   559  N  N      . THR A 1 35  ? -13.963 4.849   -13.152 1.00 28.77  ? 34  THR A N      1 
ATOM   560  C  CA     . THR A 1 35  ? -14.742 4.400   -14.312 1.00 31.45  ? 34  THR A CA     1 
ATOM   561  C  C      . THR A 1 35  ? -14.113 3.200   -14.998 1.00 30.42  ? 34  THR A C      1 
ATOM   562  O  O      . THR A 1 35  ? -14.791 2.513   -15.761 1.00 35.21  ? 34  THR A O      1 
ATOM   563  C  CB     . THR A 1 35  ? -14.910 5.519   -15.348 1.00 34.10  ? 34  THR A CB     1 
ATOM   564  O  OG1    . THR A 1 35  ? -13.624 5.971   -15.794 1.00 31.44  ? 34  THR A OG1    1 
ATOM   565  C  CG2    . THR A 1 35  ? -15.696 6.693   -14.759 1.00 36.60  ? 34  THR A CG2    1 
ATOM   566  H  H      . THR A 1 35  ? -13.304 5.371   -13.333 1.00 34.43  ? 34  THR A H      1 
ATOM   567  H  HA     . THR A 1 35  ? -15.627 4.139   -14.011 1.00 37.76  ? 34  THR A HA     1 
ATOM   568  H  HB     . THR A 1 35  ? -15.406 5.175   -16.107 1.00 40.94  ? 34  THR A HB     1 
ATOM   569  H  HG1    . THR A 1 35  ? -13.181 6.265   -15.144 1.00 37.75  ? 34  THR A HG1    1 
ATOM   570  H  HG21   . THR A 1 35  ? -15.795 7.393   -15.424 1.00 43.94  ? 34  THR A HG21   1 
ATOM   571  H  HG22   . THR A 1 35  ? -16.577 6.396   -14.481 1.00 43.94  ? 34  THR A HG22   1 
ATOM   572  H  HG23   . THR A 1 35  ? -15.228 7.053   -13.990 1.00 43.94  ? 34  THR A HG23   1 
ATOM   573  N  N      . ASN A 1 36  ? -12.854 2.916   -14.706 1.00 28.69  ? 35  ASN A N      1 
ATOM   574  C  CA     . ASN A 1 36  ? -12.157 1.801   -15.334 1.00 28.92  ? 35  ASN A CA     1 
ATOM   575  C  C      . ASN A 1 36  ? -11.044 1.385   -14.396 1.00 25.54  ? 35  ASN A C      1 
ATOM   576  O  O      . ASN A 1 36  ? -10.158 2.187   -14.108 1.00 25.89  ? 35  ASN A O      1 
ATOM   577  C  CB     . ASN A 1 36  ? -11.598 2.212   -16.715 1.00 30.44  ? 35  ASN A CB     1 
ATOM   578  C  CG     . ASN A 1 36  ? -10.960 1.061   -17.451 1.00 32.78  ? 35  ASN A CG     1 
ATOM   579  O  OD1    . ASN A 1 36  ? -11.005 -0.080  -16.990 1.00 31.71  ? 35  ASN A OD1    1 
ATOM   580  N  ND2    . ASN A 1 36  ? -10.375 1.350   -18.618 1.00 32.37  ? 35  ASN A ND2    1 
ATOM   581  H  H      . ASN A 1 36  ? -12.375 3.356   -14.143 1.00 34.44  ? 35  ASN A H      1 
ATOM   582  H  HA     . ASN A 1 36  ? -12.766 1.054   -15.451 1.00 34.72  ? 35  ASN A HA     1 
ATOM   583  H  HB2    . ASN A 1 36  ? -12.323 2.553   -17.261 1.00 36.55  ? 35  ASN A HB2    1 
ATOM   584  H  HB3    . ASN A 1 36  ? -10.924 2.899   -16.591 1.00 36.55  ? 35  ASN A HB3    1 
ATOM   585  H  HD21   . ASN A 1 36  ? -9.998  0.727   -19.075 1.00 38.86  ? 35  ASN A HD21   1 
ATOM   586  H  HD22   . ASN A 1 36  ? -10.377 2.159   -18.911 1.00 38.86  ? 35  ASN A HD22   1 
ATOM   587  N  N      . ASN A 1 37  ? -11.075 0.150   -13.897 1.00 25.29  ? 36  ASN A N      1 
ATOM   588  C  CA     . ASN A 1 37  ? -10.027 -0.294  -12.995 1.00 24.82  ? 36  ASN A CA     1 
ATOM   589  C  C      . ASN A 1 37  ? -8.916  -1.049  -13.716 1.00 23.93  ? 36  ASN A C      1 
ATOM   590  O  O      . ASN A 1 37  ? -8.065  -1.650  -13.053 1.00 24.13  ? 36  ASN A O      1 
ATOM   591  C  CB     . ASN A 1 37  ? -10.616 -1.143  -11.861 1.00 31.60  ? 36  ASN A CB     1 
ATOM   592  C  CG     . ASN A 1 37  ? -11.301 -2.377  -12.358 1.00 39.54  ? 36  ASN A CG     1 
ATOM   593  O  OD1    . ASN A 1 37  ? -11.108 -2.783  -13.497 1.00 39.27  ? 36  ASN A OD1    1 
ATOM   594  N  ND2    . ASN A 1 37  ? -12.110 -2.991  -11.508 1.00 45.26  ? 36  ASN A ND2    1 
ATOM   595  H  H      . ASN A 1 37  ? -11.682 -0.437  -14.064 1.00 30.26  ? 36  ASN A H      1 
ATOM   596  H  HA     . ASN A 1 37  ? -9.625  0.490   -12.589 1.00 29.81  ? 36  ASN A HA     1 
ATOM   597  H  HB2    . ASN A 1 37  ? -9.901  -1.416  -11.266 1.00 37.94  ? 36  ASN A HB2    1 
ATOM   598  H  HB3    . ASN A 1 37  ? -11.268 -0.614  -11.376 1.00 37.94  ? 36  ASN A HB3    1 
ATOM   599  H  HD21   . ASN A 1 37  ? -12.525 -3.705  -11.749 1.00 54.33  ? 36  ASN A HD21   1 
ATOM   600  H  HD22   . ASN A 1 37  ? -12.220 -2.677  -10.715 1.00 54.33  ? 36  ASN A HD22   1 
ATOM   601  N  N      . GLN A 1 38  ? -8.859  -0.949  -15.050 1.00 25.50  ? 37  GLN A N      1 
ATOM   602  C  CA     . GLN A 1 38  ? -7.825  -1.612  -15.855 1.00 27.46  ? 37  GLN A CA     1 
ATOM   603  C  C      . GLN A 1 38  ? -6.426  -1.435  -15.286 1.00 22.95  ? 37  GLN A C      1 
ATOM   604  O  O      . GLN A 1 38  ? -5.659  -2.398  -15.204 1.00 22.59  ? 37  GLN A O      1 
ATOM   605  C  CB     . GLN A 1 38  ? -7.840  -1.066  -17.289 1.00 33.16  ? 37  GLN A CB     1 
ATOM   606  C  CG     . GLN A 1 38  ? -6.650  -1.516  -18.145 1.00 38.99  ? 37  GLN A CG     1 
ATOM   607  C  CD     . GLN A 1 38  ? -6.124  -0.440  -19.112 1.00 38.45  ? 37  GLN A CD     1 
ATOM   608  O  OE1    . GLN A 1 38  ? -6.189  0.768   -18.869 1.00 41.02  ? 37  GLN A OE1    1 
ATOM   609  N  NE2    . GLN A 1 38  ? -5.577  -0.900  -20.195 1.00 36.00  ? 37  GLN A NE2    1 
ATOM   610  H  H      . GLN A 1 38  ? -9.419  -0.495  -15.519 1.00 30.62  ? 37  GLN A H      1 
ATOM   611  H  HA     . GLN A 1 38  ? -8.016  -2.562  -15.894 1.00 32.97  ? 37  GLN A HA     1 
ATOM   612  H  HB2    . GLN A 1 38  ? -8.651  -1.367  -17.728 1.00 39.81  ? 37  GLN A HB2    1 
ATOM   613  H  HB3    . GLN A 1 38  ? -7.828  -0.096  -17.252 1.00 39.81  ? 37  GLN A HB3    1 
ATOM   614  H  HG2    . GLN A 1 38  ? -5.921  -1.766  -17.557 1.00 46.81  ? 37  GLN A HG2    1 
ATOM   615  H  HG3    . GLN A 1 38  ? -6.921  -2.282  -18.676 1.00 46.81  ? 37  GLN A HG3    1 
ATOM   616  H  HE21   . GLN A 1 38  ? -5.531  -1.749  -20.327 1.00 43.22  ? 37  GLN A HE21   1 
ATOM   617  H  HE22   . GLN A 1 38  ? -5.260  -0.357  -20.781 1.00 43.22  ? 37  GLN A HE22   1 
ATOM   618  N  N      . ARG A 1 39  ? -6.040  -0.194  -14.983 1.00 21.30  ? 38  ARG A N      1 
ATOM   619  C  CA     . ARG A 1 39  ? -4.675  0.058   -14.521 1.00 21.85  ? 38  ARG A CA     1 
ATOM   620  C  C      . ARG A 1 39  ? -4.390  -0.559  -13.162 1.00 22.64  ? 38  ARG A C      1 
ATOM   621  O  O      . ARG A 1 39  ? -3.229  -0.853  -12.852 1.00 24.78  ? 38  ARG A O      1 
ATOM   622  C  CB     . ARG A 1 39  ? -4.388  1.551   -14.463 1.00 25.47  ? 38  ARG A CB     1 
ATOM   623  C  CG     . ARG A 1 39  ? -3.885  2.067   -15.802 1.00 25.71  ? 38  ARG A CG     1 
ATOM   624  C  CD     . ARG A 1 39  ? -3.770  3.587   -15.882 1.00 24.08  ? 38  ARG A CD     1 
ATOM   625  N  NE     . ARG A 1 39  ? -3.087  4.008   -17.115 1.00 23.39  ? 38  ARG A NE     1 
ATOM   626  C  CZ     . ARG A 1 39  ? -2.871  5.278   -17.448 1.00 22.62  ? 38  ARG A CZ     1 
ATOM   627  N  NH1    . ARG A 1 39  ? -3.295  6.250   -16.647 1.00 23.75  1 38  ARG A NH1    1 
ATOM   628  N  NH2    . ARG A 1 39  ? -2.206  5.571   -18.560 1.00 21.26  ? 38  ARG A NH2    1 
ATOM   629  H  H      . ARG A 1 39  ? -6.538  0.505   -15.034 1.00 25.58  ? 38  ARG A H      1 
ATOM   630  H  HA     . ARG A 1 39  ? -4.056  -0.335  -15.157 1.00 26.24  ? 38  ARG A HA     1 
ATOM   631  H  HB2    . ARG A 1 39  ? -5.204  2.026   -14.239 1.00 30.58  ? 38  ARG A HB2    1 
ATOM   632  H  HB3    . ARG A 1 39  ? -3.706  1.721   -13.795 1.00 30.58  ? 38  ARG A HB3    1 
ATOM   633  H  HG2    . ARG A 1 39  ? -3.005  1.695   -15.968 1.00 30.87  ? 38  ARG A HG2    1 
ATOM   634  H  HG3    . ARG A 1 39  ? -4.499  1.781   -16.496 1.00 30.87  ? 38  ARG A HG3    1 
ATOM   635  H  HD2    . ARG A 1 39  ? -4.659  3.976   -15.877 1.00 28.92  ? 38  ARG A HD2    1 
ATOM   636  H  HD3    . ARG A 1 39  ? -3.258  3.910   -15.124 1.00 28.92  ? 38  ARG A HD3    1 
ATOM   637  H  HE     . ARG A 1 39  ? -2.878  3.400   -17.686 1.00 28.09  ? 38  ARG A HE     1 
ATOM   638  H  HH11   . ARG A 1 39  ? -3.712  6.058   -15.920 1.00 28.52  ? 38  ARG A HH11   1 
ATOM   639  H  HH12   . ARG A 1 39  ? -3.158  7.073   -16.859 1.00 28.52  ? 38  ARG A HH12   1 
ATOM   640  H  HH21   . ARG A 1 39  ? -1.937  4.940   -19.079 1.00 25.54  ? 38  ARG A HH21   1 
ATOM   641  H  HH22   . ARG A 1 39  ? -2.078  6.393   -18.780 1.00 25.54  ? 38  ARG A HH22   1 
ATOM   642  N  N      . ILE A 1 40  ? -5.416  -0.740  -12.333 1.00 20.71  ? 39  ILE A N      1 
ATOM   643  C  CA     . ILE A 1 40  ? -5.222  -1.338  -11.014 1.00 21.96  ? 39  ILE A CA     1 
ATOM   644  C  C      . ILE A 1 40  ? -5.063  -2.834  -11.149 1.00 22.38  ? 39  ILE A C      1 
ATOM   645  O  O      . ILE A 1 40  ? -4.150  -3.433  -10.574 1.00 24.53  ? 39  ILE A O      1 
ATOM   646  C  CB     . ILE A 1 40  ? -6.409  -1.003  -10.092 1.00 25.07  ? 39  ILE A CB     1 
ATOM   647  C  CG1    . ILE A 1 40  ? -6.643  0.512   -10.024 1.00 26.04  ? 39  ILE A CG1    1 
ATOM   648  C  CG2    . ILE A 1 40  ? -6.136  -1.601  -8.681  1.00 25.59  ? 39  ILE A CG2    1 
ATOM   649  C  CD1    . ILE A 1 40  ? -8.008  0.899   -9.397  1.00 28.77  ? 39  ILE A CD1    1 
ATOM   650  H  H      . ILE A 1 40  ? -6.230  -0.526  -12.509 1.00 24.88  ? 39  ILE A H      1 
ATOM   651  H  HA     . ILE A 1 40  ? -4.414  -0.980  -10.614 1.00 26.37  ? 39  ILE A HA     1 
ATOM   652  H  HB     . ILE A 1 40  ? -7.207  -1.421  -10.453 1.00 30.10  ? 39  ILE A HB     1 
ATOM   653  H  HG12   . ILE A 1 40  ? -5.943  0.914   -9.485  1.00 31.26  ? 39  ILE A HG12   1 
ATOM   654  H  HG13   . ILE A 1 40  ? -6.615  0.874   -10.924 1.00 31.26  ? 39  ILE A HG13   1 
ATOM   655  H  HG21   . ILE A 1 40  ? -6.884  -1.391  -8.099  1.00 30.73  ? 39  ILE A HG21   1 
ATOM   656  H  HG22   . ILE A 1 40  ? -6.039  -2.563  -8.759  1.00 30.73  ? 39  ILE A HG22   1 
ATOM   657  H  HG23   . ILE A 1 40  ? -5.321  -1.213  -8.326  1.00 30.73  ? 39  ILE A HG23   1 
ATOM   658  H  HD11   . ILE A 1 40  ? -8.088  1.866   -9.386  1.00 34.54  ? 39  ILE A HD11   1 
ATOM   659  H  HD12   . ILE A 1 40  ? -8.721  0.514   -9.931  1.00 34.54  ? 39  ILE A HD12   1 
ATOM   660  H  HD13   . ILE A 1 40  ? -8.049  0.553   -8.492  1.00 34.54  ? 39  ILE A HD13   1 
ATOM   661  N  N      . LYS A 1 41  ? -5.958  -3.447  -11.922 1.00 22.67  ? 40  LYS A N      1 
ATOM   662  C  CA     . LYS A 1 41  ? -5.886  -4.879  -12.162 1.00 27.08  ? 40  LYS A CA     1 
ATOM   663  C  C      . LYS A 1 41  ? -4.558  -5.260  -12.806 1.00 27.22  ? 40  LYS A C      1 
ATOM   664  O  O      . LYS A 1 41  ? -4.010  -6.336  -12.549 1.00 25.26  ? 40  LYS A O      1 
ATOM   665  C  CB     . LYS A 1 41  ? -7.060  -5.294  -13.038 1.00 37.10  ? 40  LYS A CB     1 
ATOM   666  C  CG     . LYS A 1 41  ? -7.317  -6.771  -13.055 1.00 54.52  ? 40  LYS A CG     1 
ATOM   667  C  CD     . LYS A 1 41  ? -8.677  -7.067  -13.641 1.00 69.13  ? 40  LYS A CD     1 
ATOM   668  C  CE     . LYS A 1 41  ? -9.022  -8.536  -13.461 1.00 82.23  ? 40  LYS A CE     1 
ATOM   669  N  NZ     . LYS A 1 41  ? -10.404 -8.846  -13.926 1.00 90.85  1 40  LYS A NZ     1 
ATOM   670  H  H      . LYS A 1 41  ? -6.613  -3.054  -12.316 1.00 27.22  ? 40  LYS A H      1 
ATOM   671  H  HA     . LYS A 1 41  ? -5.958  -5.348  -11.316 1.00 32.52  ? 40  LYS A HA     1 
ATOM   672  H  HB2    . LYS A 1 41  ? -7.862  -4.858  -12.710 1.00 44.53  ? 40  LYS A HB2    1 
ATOM   673  H  HB3    . LYS A 1 41  ? -6.883  -5.013  -13.949 1.00 44.53  ? 40  LYS A HB3    1 
ATOM   674  H  HG2    . LYS A 1 41  ? -6.646  -7.209  -13.602 1.00 65.44  ? 40  LYS A HG2    1 
ATOM   675  H  HG3    . LYS A 1 41  ? -7.292  -7.114  -12.148 1.00 65.44  ? 40  LYS A HG3    1 
ATOM   676  H  HD2    . LYS A 1 41  ? -9.348  -6.535  -13.185 1.00 82.97  ? 40  LYS A HD2    1 
ATOM   677  H  HD3    . LYS A 1 41  ? -8.672  -6.866  -14.590 1.00 82.97  ? 40  LYS A HD3    1 
ATOM   678  H  HE2    . LYS A 1 41  ? -8.402  -9.074  -13.976 1.00 98.70  ? 40  LYS A HE2    1 
ATOM   679  H  HE3    . LYS A 1 41  ? -8.961  -8.764  -12.520 1.00 98.70  ? 40  LYS A HE3    1 
ATOM   680  H  HZ1    . LYS A 1 41  ? -10.577 -9.711  -13.808 1.00 109.04 ? 40  LYS A HZ1    1 
ATOM   681  H  HZ2    . LYS A 1 41  ? -10.995 -8.367  -13.463 1.00 109.04 ? 40  LYS A HZ2    1 
ATOM   682  H  HZ3    . LYS A 1 41  ? -10.485 -8.649  -14.790 1.00 109.04 ? 40  LYS A HZ3    1 
ATOM   683  N  N      . ALA A 1 42  ? -4.032  -4.397  -13.665 1.00 24.74  ? 41  ALA A N      1 
ATOM   684  C  CA     . ALA A 1 42  ? -2.791  -4.719  -14.359 1.00 25.05  ? 41  ALA A CA     1 
ATOM   685  C  C      . ALA A 1 42  ? -1.605  -4.881  -13.410 1.00 24.29  ? 41  ALA A C      1 
ATOM   686  O  O      . ALA A 1 42  ? -0.646  -5.578  -13.751 1.00 24.35  ? 41  ALA A O      1 
ATOM   687  C  CB     . ALA A 1 42  ? -2.483  -3.633  -15.373 1.00 24.11  ? 41  ALA A CB     1 
ATOM   688  H  H      . ALA A 1 42  ? -4.367  -3.629  -13.862 1.00 29.71  ? 41  ALA A H      1 
ATOM   689  H  HA     . ALA A 1 42  ? -2.906  -5.553  -14.840 1.00 30.08  ? 41  ALA A HA     1 
ATOM   690  H  HB1    . ALA A 1 42  ? -1.657  -3.853  -15.830 1.00 28.96  ? 41  ALA A HB1    1 
ATOM   691  H  HB2    . ALA A 1 42  ? -3.212  -3.581  -16.011 1.00 28.96  ? 41  ALA A HB2    1 
ATOM   692  H  HB3    . ALA A 1 42  ? -2.389  -2.786  -14.909 1.00 28.96  ? 41  ALA A HB3    1 
ATOM   693  N  N      . ALA A 1 43  ? -1.622  -4.213  -12.258 1.00 24.51  ? 42  ALA A N      1 
ATOM   694  C  CA     . ALA A 1 43  ? -0.537  -4.299  -11.282 1.00 23.19  ? 42  ALA A CA     1 
ATOM   695  C  C      . ALA A 1 43  ? -0.675  -5.493  -10.344 1.00 24.26  ? 42  ALA A C      1 
ATOM   696  O  O      . ALA A 1 43  ? 0.273   -5.820  -9.617  1.00 25.42  ? 42  ALA A O      1 
ATOM   697  C  CB     . ALA A 1 43  ? -0.474  -3.014  -10.462 1.00 25.08  ? 42  ALA A CB     1 
ATOM   698  H  H      . ALA A 1 43  ? -2.263  -3.694  -12.014 1.00 29.43  ? 42  ALA A H      1 
ATOM   699  H  HA     . ALA A 1 43  ? 0.304   -4.390  -11.757 1.00 27.85  ? 42  ALA A HA     1 
ATOM   700  H  HB1    . ALA A 1 43  ? 0.249   -3.085  -9.820  1.00 30.11  ? 42  ALA A HB1    1 
ATOM   701  H  HB2    . ALA A 1 43  ? -0.315  -2.267  -11.059 1.00 30.11  ? 42  ALA A HB2    1 
ATOM   702  H  HB3    . ALA A 1 43  ? -1.318  -2.894  -9.999  1.00 30.11  ? 42  ALA A HB3    1 
ATOM   703  N  N      . VAL A 1 44  ? -1.831  -6.143  -10.331 1.00 24.79  ? 43  VAL A N      1 
ATOM   704  C  CA     . VAL A 1 44  ? -2.060  -7.215  -9.359  1.00 26.34  ? 43  VAL A CA     1 
ATOM   705  C  C      . VAL A 1 44  ? -1.060  -8.351  -9.506  1.00 30.01  ? 43  VAL A C      1 
ATOM   706  O  O      . VAL A 1 44  ? -0.621  -8.898  -8.474  1.00 30.60  ? 43  VAL A O      1 
ATOM   707  C  CB     . VAL A 1 44  ? -3.519  -7.688  -9.438  1.00 28.02  ? 43  VAL A CB     1 
ATOM   708  C  CG1    . VAL A 1 44  ? -3.711  -8.983  -8.659  1.00 30.43  ? 43  VAL A CG1    1 
ATOM   709  C  CG2    . VAL A 1 44  ? -4.408  -6.602  -8.892  1.00 31.47  ? 43  VAL A CG2    1 
ATOM   710  H  H      . VAL A 1 44  ? -2.490  -5.990  -10.862 1.00 29.77  ? 43  VAL A H      1 
ATOM   711  H  HA     . VAL A 1 44  ? -1.932  -6.843  -8.472  1.00 31.63  ? 43  VAL A HA     1 
ATOM   712  H  HB     . VAL A 1 44  ? -3.759  -7.846  -10.364 1.00 33.64  ? 43  VAL A HB     1 
ATOM   713  H  HG11   . VAL A 1 44  ? -4.640  -9.256  -8.727  1.00 36.54  ? 43  VAL A HG11   1 
ATOM   714  H  HG12   . VAL A 1 44  ? -3.137  -9.666  -9.038  1.00 36.54  ? 43  VAL A HG12   1 
ATOM   715  H  HG13   . VAL A 1 44  ? -3.478  -8.830  -7.730  1.00 36.54  ? 43  VAL A HG13   1 
ATOM   716  H  HG21   . VAL A 1 44  ? -5.331  -6.897  -8.939  1.00 37.78  ? 43  VAL A HG21   1 
ATOM   717  H  HG22   . VAL A 1 44  ? -4.163  -6.428  -7.969  1.00 37.78  ? 43  VAL A HG22   1 
ATOM   718  H  HG23   . VAL A 1 44  ? -4.289  -5.800  -9.423  1.00 37.78  ? 43  VAL A HG23   1 
ATOM   719  N  N      . PRO A 1 45  ? -0.653  -8.765  -10.714 1.00 27.90  ? 44  PRO A N      1 
ATOM   720  C  CA     . PRO A 1 45  ? 0.328   -9.866  -10.806 1.00 27.36  ? 44  PRO A CA     1 
ATOM   721  C  C      . PRO A 1 45  ? 1.636   -9.589  -10.078 1.00 23.87  ? 44  PRO A C      1 
ATOM   722  O  O      . PRO A 1 45  ? 2.151   -10.476 -9.381  1.00 23.27  ? 44  PRO A O      1 
ATOM   723  C  CB     . PRO A 1 45  ? 0.523   -10.020 -12.319 1.00 29.42  ? 44  PRO A CB     1 
ATOM   724  C  CG     . PRO A 1 45  ? -0.841  -9.644  -12.885 1.00 30.69  ? 44  PRO A CG     1 
ATOM   725  C  CD     . PRO A 1 45  ? -1.249  -8.461  -12.032 1.00 30.17  ? 44  PRO A CD     1 
ATOM   726  H  HA     . PRO A 1 45  ? -0.059  -10.683 -10.455 1.00 32.86  ? 44  PRO A HA     1 
ATOM   727  H  HB2    . PRO A 1 45  ? 1.210   -9.410  -12.630 1.00 35.33  ? 44  PRO A HB2    1 
ATOM   728  H  HB3    . PRO A 1 45  ? 0.748   -10.939 -12.533 1.00 35.33  ? 44  PRO A HB3    1 
ATOM   729  H  HG2    . PRO A 1 45  ? -0.756  -9.389  -13.817 1.00 36.85  ? 44  PRO A HG2    1 
ATOM   730  H  HG3    . PRO A 1 45  ? -1.461  -10.382 -12.778 1.00 36.85  ? 44  PRO A HG3    1 
ATOM   731  H  HD2    . PRO A 1 45  ? -0.875  -7.640  -12.390 1.00 36.22  ? 44  PRO A HD2    1 
ATOM   732  H  HD3    . PRO A 1 45  ? -2.215  -8.411  -11.962 1.00 36.22  ? 44  PRO A HD3    1 
ATOM   733  N  N      . SER A 1 46  ? 2.204   -8.395  -10.231 1.00 23.02  ? 45  SER A N      1 
ATOM   734  C  CA     . SER A 1 46  ? 3.405   -8.056  -9.475  1.00 23.18  ? 45  SER A CA     1 
ATOM   735  C  C      . SER A 1 46  ? 3.158   -8.050  -7.974  1.00 23.90  ? 45  SER A C      1 
ATOM   736  O  O      . SER A 1 46  ? 4.011   -8.505  -7.211  1.00 23.63  ? 45  SER A O      1 
ATOM   737  C  CB     . SER A 1 46  ? 3.929   -6.690  -9.909  1.00 22.62  ? 45  SER A CB     1 
ATOM   738  O  OG     . SER A 1 46  ? 4.464   -6.787  -11.200 1.00 23.27  ? 45  SER A OG     1 
ATOM   739  H  H      . SER A 1 46  ? 1.920   -7.775  -10.755 1.00 27.65  ? 45  SER A H      1 
ATOM   740  H  HA     . SER A 1 46  ? 4.092   -8.715  -9.663  1.00 27.84  ? 45  SER A HA     1 
ATOM   741  H  HB2    . SER A 1 46  ? 3.198   -6.053  -9.912  1.00 27.17  ? 45  SER A HB2    1 
ATOM   742  H  HB3    . SER A 1 46  ? 4.623   -6.404  -9.295  1.00 27.17  ? 45  SER A HB3    1 
ATOM   743  H  HG     . SER A 1 46  ? 4.755   -6.038  -11.447 1.00 27.94  ? 45  SER A HG     1 
ATOM   744  N  N      . ILE A 1 47  ? 2.037   -7.478  -7.525  1.00 23.06  ? 46  ILE A N      1 
ATOM   745  C  CA     . ILE A 1 47  ? 1.765   -7.390  -6.091  1.00 23.71  ? 46  ILE A CA     1 
ATOM   746  C  C      . ILE A 1 47  ? 1.614   -8.781  -5.498  1.00 25.48  ? 46  ILE A C      1 
ATOM   747  O  O      . ILE A 1 47  ? 2.222   -9.114  -4.471  1.00 26.42  ? 46  ILE A O      1 
ATOM   748  C  CB     . ILE A 1 47  ? 0.508   -6.544  -5.829  1.00 24.50  ? 46  ILE A CB     1 
ATOM   749  C  CG1    . ILE A 1 47  ? 0.726   -5.109  -6.309  1.00 23.54  ? 46  ILE A CG1    1 
ATOM   750  C  CG2    . ILE A 1 47  ? 0.138   -6.567  -4.342  1.00 27.13  ? 46  ILE A CG2    1 
ATOM   751  C  CD1    . ILE A 1 47  ? -0.553  -4.287  -6.334  1.00 26.24  ? 46  ILE A CD1    1 
ATOM   752  H  H      . ILE A 1 47  ? 1.425   -7.138  -8.025  1.00 27.69  ? 46  ILE A H      1 
ATOM   753  H  HA     . ILE A 1 47  ? 2.514   -6.957  -5.653  1.00 28.47  ? 46  ILE A HA     1 
ATOM   754  H  HB     . ILE A 1 47  ? -0.228  -6.927  -6.333  1.00 29.42  ? 46  ILE A HB     1 
ATOM   755  H  HG12   . ILE A 1 47  ? 1.352   -4.669  -5.713  1.00 28.27  ? 46  ILE A HG12   1 
ATOM   756  H  HG13   . ILE A 1 47  ? 1.086   -5.129  -7.210  1.00 28.27  ? 46  ILE A HG13   1 
ATOM   757  H  HG21   . ILE A 1 47  ? -0.657  -6.027  -4.207  1.00 32.57  ? 46  ILE A HG21   1 
ATOM   758  H  HG22   . ILE A 1 47  ? -0.035  -7.483  -4.074  1.00 32.57  ? 46  ILE A HG22   1 
ATOM   759  H  HG23   . ILE A 1 47  ? 0.876   -6.205  -3.828  1.00 32.57  ? 46  ILE A HG23   1 
ATOM   760  H  HD11   . ILE A 1 47  ? -0.347  -3.392  -6.646  1.00 31.50  ? 46  ILE A HD11   1 
ATOM   761  H  HD12   . ILE A 1 47  ? -1.187  -4.709  -6.934  1.00 31.50  ? 46  ILE A HD12   1 
ATOM   762  H  HD13   . ILE A 1 47  ? -0.921  -4.248  -5.437  1.00 31.50  ? 46  ILE A HD13   1 
ATOM   763  N  N      . LYS A 1 48  ? 0.802   -9.610  -6.155  1.00 24.77  ? 47  LYS A N      1 
ATOM   764  C  CA     . LYS A 1 48  ? 0.556   -10.966 -5.689  1.00 26.92  ? 47  LYS A CA     1 
ATOM   765  C  C      . LYS A 1 48  ? 1.842   -11.784 -5.674  1.00 27.92  ? 47  LYS A C      1 
ATOM   766  O  O      . LYS A 1 48  ? 2.050   -12.597 -4.764  1.00 29.68  ? 47  LYS A O      1 
ATOM   767  C  CB     . LYS A 1 48  ? -0.503  -11.622 -6.582  1.00 33.20  ? 47  LYS A CB     1 
ATOM   768  C  CG     . LYS A 1 48  ? -1.183  -12.834 -5.993  1.00 52.31  ? 47  LYS A CG     1 
ATOM   769  C  CD     . LYS A 1 48  ? -2.464  -13.194 -6.767  1.00 68.09  ? 47  LYS A CD     1 
ATOM   770  C  CE     . LYS A 1 48  ? -3.609  -12.193 -6.504  1.00 75.70  ? 47  LYS A CE     1 
ATOM   771  N  NZ     . LYS A 1 48  ? -4.895  -12.553 -7.201  1.00 79.07  1 47  LYS A NZ     1 
ATOM   772  H  H      . LYS A 1 48  ? 0.381   -9.406  -6.876  1.00 29.74  ? 47  LYS A H      1 
ATOM   773  H  HA     . LYS A 1 48  ? 0.210   -10.933 -4.784  1.00 32.33  ? 47  LYS A HA     1 
ATOM   774  H  HB2    . LYS A 1 48  ? -1.192  -10.966 -6.774  1.00 39.86  ? 47  LYS A HB2    1 
ATOM   775  H  HB3    . LYS A 1 48  ? -0.080  -11.899 -7.410  1.00 39.86  ? 47  LYS A HB3    1 
ATOM   776  H  HG2    . LYS A 1 48  ? -0.579  -13.592 -6.036  1.00 62.79  ? 47  LYS A HG2    1 
ATOM   777  H  HG3    . LYS A 1 48  ? -1.425  -12.649 -5.072  1.00 62.79  ? 47  LYS A HG3    1 
ATOM   778  H  HD2    . LYS A 1 48  ? -2.272  -13.189 -7.718  1.00 81.72  ? 47  LYS A HD2    1 
ATOM   779  H  HD3    . LYS A 1 48  ? -2.764  -14.074 -6.492  1.00 81.72  ? 47  LYS A HD3    1 
ATOM   780  H  HE2    . LYS A 1 48  ? -3.787  -12.162 -5.551  1.00 90.86  ? 47  LYS A HE2    1 
ATOM   781  H  HE3    . LYS A 1 48  ? -3.337  -11.316 -6.817  1.00 90.86  ? 47  LYS A HE3    1 
ATOM   782  H  HZ1    . LYS A 1 48  ? -5.520  -11.947 -7.018  1.00 94.90  ? 47  LYS A HZ1    1 
ATOM   783  H  HZ2    . LYS A 1 48  ? -4.766  -12.579 -8.081  1.00 94.90  ? 47  LYS A HZ2    1 
ATOM   784  H  HZ3    . LYS A 1 48  ? -5.176  -13.351 -6.926  1.00 94.90  ? 47  LYS A HZ3    1 
ATOM   785  N  N      . PHE A 1 49  ? 2.709   -11.594 -6.674  1.00 24.41  ? 48  PHE A N      1 
ATOM   786  C  CA     . PHE A 1 49  ? 4.009   -12.267 -6.688  1.00 25.98  ? 48  PHE A CA     1 
ATOM   787  C  C      . PHE A 1 49  ? 4.827   -11.905 -5.454  1.00 22.72  ? 48  PHE A C      1 
ATOM   788  O  O      . PHE A 1 49  ? 5.447   -12.770 -4.828  1.00 23.43  ? 48  PHE A O      1 
ATOM   789  C  CB     . PHE A 1 49  ? 4.795   -11.886 -7.941  1.00 27.20  ? 48  PHE A CB     1 
ATOM   790  C  CG     . PHE A 1 49  ? 6.153   -12.518 -8.045  1.00 26.44  ? 48  PHE A CG     1 
ATOM   791  C  CD1    . PHE A 1 49  ? 7.266   -11.873 -7.551  1.00 27.95  ? 48  PHE A CD1    1 
ATOM   792  C  CD2    . PHE A 1 49  ? 6.326   -13.735 -8.697  1.00 29.16  ? 48  PHE A CD2    1 
ATOM   793  C  CE1    . PHE A 1 49  ? 8.531   -12.440 -7.670  1.00 31.35  ? 48  PHE A CE1    1 
ATOM   794  C  CE2    . PHE A 1 49  ? 7.588   -14.308 -8.827  1.00 29.50  ? 48  PHE A CE2    1 
ATOM   795  C  CZ     . PHE A 1 49  ? 8.689   -13.653 -8.322  1.00 33.88  ? 48  PHE A CZ     1 
ATOM   796  H  H      . PHE A 1 49  ? 2.568   -11.083 -7.351  1.00 29.31  ? 48  PHE A H      1 
ATOM   797  H  HA     . PHE A 1 49  ? 3.874   -13.227 -6.693  1.00 31.20  ? 48  PHE A HA     1 
ATOM   798  H  HB2    . PHE A 1 49  ? 4.285   -12.156 -8.720  1.00 32.66  ? 48  PHE A HB2    1 
ATOM   799  H  HB3    . PHE A 1 49  ? 4.917   -10.924 -7.949  1.00 32.66  ? 48  PHE A HB3    1 
ATOM   800  H  HD1    . PHE A 1 49  ? 7.168   -11.054 -7.121  1.00 33.56  ? 48  PHE A HD1    1 
ATOM   801  H  HD2    . PHE A 1 49  ? 5.585   -14.174 -9.048  1.00 35.01  ? 48  PHE A HD2    1 
ATOM   802  H  HE1    . PHE A 1 49  ? 9.273   -11.997 -7.326  1.00 37.64  ? 48  PHE A HE1    1 
ATOM   803  H  HE2    . PHE A 1 49  ? 7.687   -15.126 -9.258  1.00 35.42  ? 48  PHE A HE2    1 
ATOM   804  H  HZ     . PHE A 1 49  ? 9.533   -14.036 -8.395  1.00 40.68  ? 48  PHE A HZ     1 
ATOM   805  N  N      . CYS A 1 50  ? 4.869   -10.623 -5.104  1.00 26.43  ? 49  CYS A N      1 
ATOM   806  C  CA     . CYS A 1 50  ? 5.643   -10.236 -3.924  1.00 26.88  ? 49  CYS A CA     1 
ATOM   807  C  C      . CYS A 1 50  ? 5.090   -10.907 -2.664  1.00 27.88  ? 49  CYS A C      1 
ATOM   808  O  O      . CYS A 1 50  ? 5.843   -11.492 -1.873  1.00 28.54  ? 49  CYS A O      1 
ATOM   809  C  CB     . CYS A 1 50  ? 5.649   -8.727  -3.767  1.00 24.74  ? 49  CYS A CB     1 
ATOM   810  S  SG     . CYS A 1 50  ? 6.640   -7.921  -5.011  1.00 27.21  ? 49  CYS A SG     1 
ATOM   811  H  H      . CYS A 1 50  ? 4.475   -9.978  -5.514  1.00 31.73  ? 49  CYS A H      1 
ATOM   812  H  HA     . CYS A 1 50  ? 6.560   -10.528 -4.040  1.00 32.28  ? 49  CYS A HA     1 
ATOM   813  H  HB2    . CYS A 1 50  ? 4.740   -8.396  -3.845  1.00 29.71  ? 49  CYS A HB2    1 
ATOM   814  H  HB3    . CYS A 1 50  ? 6.013   -8.499  -2.898  1.00 29.71  ? 49  CYS A HB3    1 
ATOM   815  H  HG     . CYS A 1 50  ? 6.197   -8.185  -6.095  1.00 32.67  ? 49  CYS A HG     1 
ATOM   816  N  N      . LEU A 1 51  ? 3.768   -10.850 -2.474  1.00 28.85  ? 50  LEU A N      1 
ATOM   817  C  CA     . LEU A 1 51  ? 3.145   -11.465 -1.300  1.00 31.82  ? 50  LEU A CA     1 
ATOM   818  C  C      . LEU A 1 51  ? 3.348   -12.971 -1.271  1.00 31.44  ? 50  LEU A C      1 
ATOM   819  O  O      . LEU A 1 51  ? 3.672   -13.548 -0.219  1.00 32.30  ? 50  LEU A O      1 
ATOM   820  C  CB     . LEU A 1 51  ? 1.656   -11.130 -1.291  1.00 32.87  ? 50  LEU A CB     1 
ATOM   821  C  CG     . LEU A 1 51  ? 1.354   -9.646  -1.153  1.00 32.24  ? 50  LEU A CG     1 
ATOM   822  C  CD1    . LEU A 1 51  ? -0.125  -9.432  -1.364  1.00 35.48  ? 50  LEU A CD1    1 
ATOM   823  C  CD2    . LEU A 1 51  ? 1.783   -9.151  0.228   1.00 34.30  ? 50  LEU A CD2    1 
ATOM   824  H  H      . LEU A 1 51  ? 3.215   -10.464 -3.007  1.00 34.64  ? 50  LEU A H      1 
ATOM   825  H  HA     . LEU A 1 51  ? 3.542   -11.092 -0.498  1.00 38.20  ? 50  LEU A HA     1 
ATOM   826  H  HB2    . LEU A 1 51  ? 1.264   -11.436 -2.124  1.00 39.46  ? 50  LEU A HB2    1 
ATOM   827  H  HB3    . LEU A 1 51  ? 1.239   -11.587 -0.545  1.00 39.46  ? 50  LEU A HB3    1 
ATOM   828  H  HG     . LEU A 1 51  ? 1.841   -9.148  -1.829  1.00 38.71  ? 50  LEU A HG     1 
ATOM   829  H  HD11   . LEU A 1 51  ? -0.322  -8.486  -1.277  1.00 42.59  ? 50  LEU A HD11   1 
ATOM   830  H  HD12   . LEU A 1 51  ? -0.365  -9.740  -2.252  1.00 42.59  ? 50  LEU A HD12   1 
ATOM   831  H  HD13   . LEU A 1 51  ? -0.615  -9.935  -0.696  1.00 42.59  ? 50  LEU A HD13   1 
ATOM   832  H  HD21   . LEU A 1 51  ? 1.584   -8.204  0.300   1.00 41.17  ? 50  LEU A HD21   1 
ATOM   833  H  HD22   . LEU A 1 51  ? 1.295   -9.645  0.906   1.00 41.17  ? 50  LEU A HD22   1 
ATOM   834  H  HD23   . LEU A 1 51  ? 2.736   -9.298  0.334   1.00 41.17  ? 50  LEU A HD23   1 
ATOM   835  N  N      . ASP A 1 52  ? 3.158   -13.630 -2.411  1.00 30.63  ? 51  ASP A N      1 
ATOM   836  C  CA     . ASP A 1 52  ? 3.248   -15.091 -2.458  1.00 32.83  ? 51  ASP A CA     1 
ATOM   837  C  C      . ASP A 1 52  ? 4.665   -15.592 -2.205  1.00 29.93  ? 51  ASP A C      1 
ATOM   838  O  O      . ASP A 1 52  ? 4.848   -16.698 -1.685  1.00 33.10  ? 51  ASP A O      1 
ATOM   839  C  CB     . ASP A 1 52  ? 2.760   -15.604 -3.811  1.00 41.83  ? 51  ASP A CB     1 
ATOM   840  C  CG     . ASP A 1 52  ? 1.250   -15.474 -3.984  1.00 55.75  ? 51  ASP A CG     1 
ATOM   841  O  OD1    . ASP A 1 52  ? 0.551   -15.137 -2.995  1.00 56.50  ? 51  ASP A OD1    1 
ATOM   842  O  OD2    . ASP A 1 52  ? 0.770   -15.708 -5.123  1.00 62.53  1 51  ASP A OD2    1 
ATOM   843  H  H      . ASP A 1 52  ? 2.976   -13.260 -3.166  1.00 36.77  ? 51  ASP A H      1 
ATOM   844  H  HA     . ASP A 1 52  ? 2.672   -15.464 -1.772  1.00 39.42  ? 51  ASP A HA     1 
ATOM   845  H  HB2    . ASP A 1 52  ? 3.188   -15.092 -4.515  1.00 50.22  ? 51  ASP A HB2    1 
ATOM   846  H  HB3    . ASP A 1 52  ? 2.992   -16.542 -3.895  1.00 50.22  ? 51  ASP A HB3    1 
ATOM   847  N  N      . ASN A 1 53  ? 5.674   -14.796 -2.523  1.00 28.23  ? 52  ASN A N      1 
ATOM   848  C  CA     . ASN A 1 53  ? 7.056   -15.171 -2.273  1.00 32.16  ? 52  ASN A CA     1 
ATOM   849  C  C      . ASN A 1 53  ? 7.608   -14.559 -0.986  1.00 34.90  ? 52  ASN A C      1 
ATOM   850  O  O      . ASN A 1 53  ? 8.830   -14.470 -0.826  1.00 33.34  ? 52  ASN A O      1 
ATOM   851  C  CB     . ASN A 1 53  ? 7.922   -14.785 -3.466  1.00 32.50  ? 52  ASN A CB     1 
ATOM   852  C  CG     . ASN A 1 53  ? 7.727   -15.744 -4.636  1.00 37.25  ? 52  ASN A CG     1 
ATOM   853  O  OD1    . ASN A 1 53  ? 8.192   -16.870 -4.587  1.00 42.10  ? 52  ASN A OD1    1 
ATOM   854  N  ND2    . ASN A 1 53  ? 6.979   -15.324 -5.638  1.00 33.73  ? 52  ASN A ND2    1 
ATOM   855  H  H      . ASN A 1 53  ? 5.584   -14.024 -2.890  1.00 33.89  ? 52  ASN A H      1 
ATOM   856  H  HA     . ASN A 1 53  ? 7.100   -16.135 -2.179  1.00 38.61  ? 52  ASN A HA     1 
ATOM   857  H  HB2    . ASN A 1 53  ? 7.680   -13.893 -3.761  1.00 39.02  ? 52  ASN A HB2    1 
ATOM   858  H  HB3    . ASN A 1 53  ? 8.855   -14.811 -3.205  1.00 39.02  ? 52  ASN A HB3    1 
ATOM   859  H  HD21   . ASN A 1 53  ? 6.845   -15.834 -6.317  1.00 40.50  ? 52  ASN A HD21   1 
ATOM   860  H  HD22   . ASN A 1 53  ? 6.626   -14.540 -5.612  1.00 40.50  ? 52  ASN A HD22   1 
ATOM   861  N  N      . GLY A 1 54  ? 6.741   -14.118 -0.085  1.00 33.71  ? 53  GLY A N      1 
ATOM   862  C  CA     . GLY A 1 54  ? 7.181   -13.821 1.272   1.00 35.12  ? 53  GLY A CA     1 
ATOM   863  C  C      . GLY A 1 54  ? 7.576   -12.388 1.566   1.00 32.86  ? 53  GLY A C      1 
ATOM   864  O  O      . GLY A 1 54  ? 8.220   -12.142 2.591   1.00 32.85  ? 53  GLY A O      1 
ATOM   865  H  H      . GLY A 1 54  ? 5.904   -13.985 -0.229  1.00 40.47  ? 53  GLY A H      1 
ATOM   866  H  HA2    . GLY A 1 54  ? 6.469   -14.059 1.885   1.00 42.17  ? 53  GLY A HA2    1 
ATOM   867  H  HA3    . GLY A 1 54  ? 7.946   -14.381 1.477   1.00 42.17  ? 53  GLY A HA3    1 
ATOM   868  N  N      . ALA A 1 55  ? 7.196   -11.428 0.735   1.00 30.85  ? 54  ALA A N      1 
ATOM   869  C  CA     . ALA A 1 55  ? 7.524   -10.042 1.048   1.00 27.36  ? 54  ALA A CA     1 
ATOM   870  C  C      . ALA A 1 55  ? 6.950   -9.671  2.410   1.00 29.33  ? 54  ALA A C      1 
ATOM   871  O  O      . ALA A 1 55  ? 5.846   -10.095 2.765   1.00 29.94  ? 54  ALA A O      1 
ATOM   872  C  CB     . ALA A 1 55  ? 6.978   -9.099  -0.020  1.00 23.79  ? 54  ALA A CB     1 
ATOM   873  H  H      . ALA A 1 55  ? 6.761   -11.544 0.003   1.00 37.04  ? 54  ALA A H      1 
ATOM   874  H  HA     . ALA A 1 55  ? 8.488   -9.939  1.084   1.00 32.85  ? 54  ALA A HA     1 
ATOM   875  H  HB1    . ALA A 1 55  ? 7.212   -8.187  0.215   1.00 28.56  ? 54  ALA A HB1    1 
ATOM   876  H  HB2    . ALA A 1 55  ? 7.371   -9.331  -0.876  1.00 28.56  ? 54  ALA A HB2    1 
ATOM   877  H  HB3    . ALA A 1 55  ? 6.014   -9.194  -0.062  1.00 28.56  ? 54  ALA A HB3    1 
ATOM   878  N  N      . LYS A 1 56  ? 7.729   -8.906  3.184   1.00 30.09  ? 55  LYS A N      1 
ATOM   879  C  CA     . LYS A 1 56  ? 7.226   -8.403  4.465   1.00 31.39  ? 55  LYS A CA     1 
ATOM   880  C  C      . LYS A 1 56  ? 6.070   -7.447  4.220   1.00 32.93  ? 55  LYS A C      1 
ATOM   881  O  O      . LYS A 1 56  ? 5.060   -7.474  4.935   1.00 33.56  ? 55  LYS A O      1 
ATOM   882  C  CB     . LYS A 1 56  ? 8.336   -7.703  5.257   1.00 30.94  ? 55  LYS A CB     1 
ATOM   883  C  CG     . LYS A 1 56  ? 7.841   -7.137  6.617   1.00 34.58  ? 55  LYS A CG     1 
ATOM   884  C  CD     . LYS A 1 56  ? 8.941   -6.531  7.475   1.00 40.81  ? 55  LYS A CD     1 
ATOM   885  C  CE     . LYS A 1 56  ? 9.893   -7.579  7.991   1.00 54.74  ? 55  LYS A CE     1 
ATOM   886  N  NZ     . LYS A 1 56  ? 10.949  -7.001  8.855   1.00 68.73  1 55  LYS A NZ     1 
ATOM   887  H  H      . LYS A 1 56  ? 8.534   -8.670  2.995   1.00 36.13  ? 55  LYS A H      1 
ATOM   888  H  HA     . LYS A 1 56  ? 6.898   -9.147  4.994   1.00 37.68  ? 55  LYS A HA     1 
ATOM   889  H  HB2    . LYS A 1 56  ? 9.045   -8.339  5.437   1.00 37.14  ? 55  LYS A HB2    1 
ATOM   890  H  HB3    . LYS A 1 56  ? 8.680   -6.963  4.732   1.00 37.14  ? 55  LYS A HB3    1 
ATOM   891  H  HG2    . LYS A 1 56  ? 7.185   -6.444  6.445   1.00 41.52  ? 55  LYS A HG2    1 
ATOM   892  H  HG3    . LYS A 1 56  ? 7.434   -7.856  7.123   1.00 41.52  ? 55  LYS A HG3    1 
ATOM   893  H  HD2    . LYS A 1 56  ? 9.447   -5.896  6.944   1.00 48.99  ? 55  LYS A HD2    1 
ATOM   894  H  HD3    . LYS A 1 56  ? 8.540   -6.085  8.238   1.00 48.99  ? 55  LYS A HD3    1 
ATOM   895  H  HE2    . LYS A 1 56  ? 9.398   -8.229  8.513   1.00 65.70  ? 55  LYS A HE2    1 
ATOM   896  H  HE3    . LYS A 1 56  ? 10.324  -8.015  7.238   1.00 65.70  ? 55  LYS A HE3    1 
ATOM   897  H  HZ1    . LYS A 1 56  ? 11.493  -7.644  9.142   1.00 82.49  ? 55  LYS A HZ1    1 
ATOM   898  H  HZ2    . LYS A 1 56  ? 11.423  -6.404  8.397   1.00 82.49  ? 55  LYS A HZ2    1 
ATOM   899  H  HZ3    . LYS A 1 56  ? 10.580  -6.599  9.558   1.00 82.49  ? 55  LYS A HZ3    1 
ATOM   900  N  N      . SER A 1 57  ? 6.187   -6.629  3.181   1.00 31.78  ? 56  SER A N      1 
ATOM   901  C  CA     . SER A 1 57  ? 5.161   -5.658  2.857   1.00 33.78  ? 56  SER A CA     1 
ATOM   902  C  C      . SER A 1 57  ? 5.362   -5.192  1.432   1.00 28.29  ? 56  SER A C      1 
ATOM   903  O  O      . SER A 1 57  ? 6.436   -5.358  0.841   1.00 25.54  ? 56  SER A O      1 
ATOM   904  C  CB     . SER A 1 57  ? 5.203   -4.463  3.809   1.00 40.08  ? 56  SER A CB     1 
ATOM   905  O  OG     . SER A 1 57  ? 6.413   -3.749  3.638   1.00 36.43  ? 56  SER A OG     1 
ATOM   906  H  H      . SER A 1 57  ? 6.859   -6.620  2.645   1.00 38.15  ? 56  SER A H      1 
ATOM   907  H  HA     . SER A 1 57  ? 4.287   -6.075  2.924   1.00 40.56  ? 56  SER A HA     1 
ATOM   908  H  HB2    . SER A 1 57  ? 4.457   -3.874  3.615   1.00 48.11  ? 56  SER A HB2    1 
ATOM   909  H  HB3    . SER A 1 57  ? 5.149   -4.782  4.723   1.00 48.11  ? 56  SER A HB3    1 
ATOM   910  H  HG     . SER A 1 57  ? 6.436   -3.093  4.161   1.00 43.73  ? 56  SER A HG     1 
ATOM   911  N  N      . VAL A 1 58  ? 4.293   -4.625  0.880   1.00 25.76  ? 57  VAL A N      1 
ATOM   912  C  CA     . VAL A 1 58  ? 4.329   -3.965  -0.414  1.00 25.53  ? 57  VAL A CA     1 
ATOM   913  C  C      . VAL A 1 58  ? 3.763   -2.571  -0.216  1.00 25.49  ? 57  VAL A C      1 
ATOM   914  O  O      . VAL A 1 58  ? 2.582   -2.425  0.120   1.00 27.48  ? 57  VAL A O      1 
ATOM   915  C  CB     . VAL A 1 58  ? 3.525   -4.727  -1.468  1.00 28.11  ? 57  VAL A CB     1 
ATOM   916  C  CG1    . VAL A 1 58  ? 3.641   -4.015  -2.796  1.00 27.87  ? 57  VAL A CG1    1 
ATOM   917  C  CG2    . VAL A 1 58  ? 3.988   -6.174  -1.559  1.00 30.20  ? 57  VAL A CG2    1 
ATOM   918  H  H      . VAL A 1 58  ? 3.517   -4.611  1.250   1.00 30.93  ? 57  VAL A H      1 
ATOM   919  H  HA     . VAL A 1 58  ? 5.247   -3.888  -0.718  1.00 30.65  ? 57  VAL A HA     1 
ATOM   920  H  HB     . VAL A 1 58  ? 2.589   -4.728  -1.210  1.00 33.75  ? 57  VAL A HB     1 
ATOM   921  H  HG11   . VAL A 1 58  ? 3.130   -4.502  -3.461  1.00 33.46  ? 57  VAL A HG11   1 
ATOM   922  H  HG12   . VAL A 1 58  ? 3.292   -3.115  -2.703  1.00 33.46  ? 57  VAL A HG12   1 
ATOM   923  H  HG13   . VAL A 1 58  ? 4.575   -3.983  -3.056  1.00 33.46  ? 57  VAL A HG13   1 
ATOM   924  H  HG21   . VAL A 1 58  ? 3.462   -6.632  -2.233  1.00 36.26  ? 57  VAL A HG21   1 
ATOM   925  H  HG22   . VAL A 1 58  ? 4.927   -6.190  -1.804  1.00 36.26  ? 57  VAL A HG22   1 
ATOM   926  H  HG23   . VAL A 1 58  ? 3.864   -6.600  -0.696  1.00 36.26  ? 57  VAL A HG23   1 
ATOM   927  N  N      . VAL A 1 59  ? 4.592   -1.554  -0.424  1.00 24.28  ? 58  VAL A N      1 
ATOM   928  C  CA     . VAL A 1 59  ? 4.160   -0.167  -0.323  1.00 25.32  ? 58  VAL A CA     1 
ATOM   929  C  C      . VAL A 1 59  ? 3.933   0.354   -1.750  1.00 25.00  ? 58  VAL A C      1 
ATOM   930  O  O      . VAL A 1 59  ? 4.857   0.399   -2.579  1.00 23.01  ? 58  VAL A O      1 
ATOM   931  C  CB     . VAL A 1 59  ? 5.183   0.679   0.452   1.00 24.90  ? 58  VAL A CB     1 
ATOM   932  C  CG1    . VAL A 1 59  ? 4.787   2.150   0.382   1.00 26.94  ? 58  VAL A CG1    1 
ATOM   933  C  CG2    . VAL A 1 59  ? 5.315   0.196   1.965   1.00 23.75  ? 58  VAL A CG2    1 
ATOM   934  H  H      . VAL A 1 59  ? 5.422   -1.643  -0.628  1.00 29.15  ? 58  VAL A H      1 
ATOM   935  H  HA     . VAL A 1 59  ? 3.315   -0.130  0.152   1.00 30.40  ? 58  VAL A HA     1 
ATOM   936  H  HB     . VAL A 1 59  ? 6.052   0.584   0.032   1.00 29.90  ? 58  VAL A HB     1 
ATOM   937  H  HG11   . VAL A 1 59  ? 5.439   2.675   0.874   1.00 32.35  ? 58  VAL A HG11   1 
ATOM   938  H  HG12   . VAL A 1 59  ? 4.771   2.428   -0.547  1.00 32.35  ? 58  VAL A HG12   1 
ATOM   939  H  HG13   . VAL A 1 59  ? 3.908   2.259   0.777   1.00 32.35  ? 58  VAL A HG13   1 
ATOM   940  H  HG21   . VAL A 1 59  ? 5.968   0.753   2.418   1.00 28.51  ? 58  VAL A HG21   1 
ATOM   941  H  HG22   . VAL A 1 59  ? 4.452   0.278   2.399   1.00 28.51  ? 58  VAL A HG22   1 
ATOM   942  H  HG23   . VAL A 1 59  ? 5.605   -0.730  1.977   1.00 28.51  ? 58  VAL A HG23   1 
ATOM   943  N  N      . LEU A 1 60  ? 2.693   0.718   -2.059  1.00 22.14  ? 59  LEU A N      1 
ATOM   944  C  CA     . LEU A 1 60  ? 2.318   1.155   -3.411  1.00 21.01  ? 59  LEU A CA     1 
ATOM   945  C  C      . LEU A 1 60  ? 2.272   2.678   -3.467  1.00 21.09  ? 59  LEU A C      1 
ATOM   946  O  O      . LEU A 1 60  ? 1.680   3.309   -2.588  1.00 23.01  ? 59  LEU A O      1 
ATOM   947  C  CB     . LEU A 1 60  ? 0.955   0.574   -3.776  1.00 20.90  ? 59  LEU A CB     1 
ATOM   948  C  CG     . LEU A 1 60  ? 0.911   -0.934  -3.693  1.00 24.99  ? 59  LEU A CG     1 
ATOM   949  C  CD1    . LEU A 1 60  ? -0.508  -1.446  -3.678  1.00 29.41  ? 59  LEU A CD1    1 
ATOM   950  C  CD2    . LEU A 1 60  ? 1.703   -1.505  -4.832  1.00 25.64  ? 59  LEU A CD2    1 
ATOM   951  H  H      . LEU A 1 60  ? 2.039   0.722   -1.501  1.00 26.59  ? 59  LEU A H      1 
ATOM   952  H  HA     . LEU A 1 60  ? 2.974   0.839   -4.052  1.00 25.23  ? 59  LEU A HA     1 
ATOM   953  H  HB2    . LEU A 1 60  ? 0.289   0.926   -3.165  1.00 25.10  ? 59  LEU A HB2    1 
ATOM   954  H  HB3    . LEU A 1 60  ? 0.737   0.829   -4.686  1.00 25.10  ? 59  LEU A HB3    1 
ATOM   955  H  HG     . LEU A 1 60  ? 1.335   -1.214  -2.867  1.00 30.00  ? 59  LEU A HG     1 
ATOM   956  H  HD11   . LEU A 1 60  ? -0.493  -2.414  -3.624  1.00 35.32  ? 59  LEU A HD11   1 
ATOM   957  H  HD12   . LEU A 1 60  ? -0.967  -1.079  -2.906  1.00 35.32  ? 59  LEU A HD12   1 
ATOM   958  H  HD13   . LEU A 1 60  ? -0.953  -1.166  -4.493  1.00 35.32  ? 59  LEU A HD13   1 
ATOM   959  H  HD21   . LEU A 1 60  ? 1.676   -2.473  -4.781  1.00 30.78  ? 59  LEU A HD21   1 
ATOM   960  H  HD22   . LEU A 1 60  ? 1.313   -1.206  -5.668  1.00 30.78  ? 59  LEU A HD22   1 
ATOM   961  H  HD23   . LEU A 1 60  ? 2.620   -1.195  -4.764  1.00 30.78  ? 59  LEU A HD23   1 
ATOM   962  N  N      . MET A 1 61  ? 2.886   3.269   -4.488  1.00 22.31  ? 60  MET A N      1 
ATOM   963  C  CA     . MET A 1 61  ? 2.836   4.716   -4.654  1.00 21.56  ? 60  MET A CA     1 
ATOM   964  C  C      . MET A 1 61  ? 2.474   5.072   -6.082  1.00 19.38  ? 60  MET A C      1 
ATOM   965  O  O      . MET A 1 61  ? 2.996   4.481   -7.031  1.00 19.02  ? 60  MET A O      1 
ATOM   966  C  CB     . MET A 1 61  ? 4.150   5.389   -4.296  1.00 21.64  ? 60  MET A CB     1 
ATOM   967  C  CG     . MET A 1 61  ? 5.368   4.873   -4.966  1.00 22.24  ? 60  MET A CG     1 
ATOM   968  S  SD     . MET A 1 61  ? 6.884   5.577   -4.202  1.00 27.80  ? 60  MET A SD     1 
ATOM   969  C  CE     . MET A 1 61  ? 8.119   4.742   -5.216  1.00 25.45  ? 60  MET A CE     1 
ATOM   970  H  H      . MET A 1 61  ? 3.336   2.856   -5.094  1.00 26.79  ? 60  MET A H      1 
ATOM   971  H  HA     . MET A 1 61  ? 2.154   5.071   -4.063  1.00 25.89  ? 60  MET A HA     1 
ATOM   972  H  HB2    . MET A 1 61  ? 4.078   6.330   -4.518  1.00 25.99  ? 60  MET A HB2    1 
ATOM   973  H  HB3    . MET A 1 61  ? 4.287   5.295   -3.340  1.00 25.99  ? 60  MET A HB3    1 
ATOM   974  H  HG2    . MET A 1 61  ? 5.401   3.908   -4.877  1.00 26.71  ? 60  MET A HG2    1 
ATOM   975  H  HG3    . MET A 1 61  ? 5.352   5.126   -5.902  1.00 26.71  ? 60  MET A HG3    1 
ATOM   976  H  HE1    . MET A 1 61  ? 9.003   5.017   -4.927  1.00 30.56  ? 60  MET A HE1    1 
ATOM   977  H  HE2    . MET A 1 61  ? 8.020   3.783   -5.109  1.00 30.56  ? 60  MET A HE2    1 
ATOM   978  H  HE3    . MET A 1 61  ? 7.983   4.987   -6.145  1.00 30.56  ? 60  MET A HE3    1 
ATOM   979  N  N      . SER A 1 62  ? 1.639   6.092   -6.228  1.00 19.29  ? 61  SER A N      1 
ATOM   980  C  CA     . SER A 1 62  ? 1.227   6.527   -7.565  1.00 20.21  ? 61  SER A CA     1 
ATOM   981  C  C      . SER A 1 62  ? 0.825   7.991   -7.493  1.00 22.15  ? 61  SER A C      1 
ATOM   982  O  O      . SER A 1 62  ? 0.704   8.567   -6.418  1.00 21.17  ? 61  SER A O      1 
ATOM   983  C  CB     . SER A 1 62  ? 0.063   5.683   -8.090  1.00 20.68  ? 61  SER A CB     1 
ATOM   984  O  OG     . SER A 1 62  ? -0.357  6.136   -9.375  1.00 20.60  ? 61  SER A OG     1 
ATOM   985  H  H      . SER A 1 62  ? 1.299   6.547   -5.583  1.00 23.17  ? 61  SER A H      1 
ATOM   986  H  HA     . SER A 1 62  ? 1.973   6.441   -8.179  1.00 24.27  ? 61  SER A HA     1 
ATOM   987  H  HB2    . SER A 1 62  ? 0.350   4.759   -8.160  1.00 24.83  ? 61  SER A HB2    1 
ATOM   988  H  HB3    . SER A 1 62  ? -0.681  5.754   -7.472  1.00 24.83  ? 61  SER A HB3    1 
ATOM   989  H  HG     . SER A 1 62  ? -0.608  6.937   -9.330  1.00 24.73  ? 61  SER A HG     1 
ATOM   990  N  N      . HIS A 1 63  ? 0.616   8.593   -8.665  1.00 20.33  ? 62  HIS A N      1 
ATOM   991  C  CA     . HIS A 1 63  ? -0.090  9.856   -8.731  1.00 20.92  ? 62  HIS A CA     1 
ATOM   992  C  C      . HIS A 1 63  ? -1.526  9.612   -9.187  1.00 22.52  ? 62  HIS A C      1 
ATOM   993  O  O      . HIS A 1 63  ? -1.902  8.505   -9.588  1.00 22.34  ? 62  HIS A O      1 
ATOM   994  C  CB     . HIS A 1 63  ? 0.628   10.798  -9.683  1.00 20.69  ? 62  HIS A CB     1 
ATOM   995  C  CG     . HIS A 1 63  ? 0.532   10.367  -11.104 1.00 19.90  ? 62  HIS A CG     1 
ATOM   996  N  ND1    . HIS A 1 63  ? 1.266   9.316   -11.602 1.00 19.63  ? 62  HIS A ND1    1 
ATOM   997  C  CD2    . HIS A 1 63  ? -0.257  10.793  -12.115 1.00 20.46  ? 62  HIS A CD2    1 
ATOM   998  C  CE1    . HIS A 1 63  ? 0.963   9.137   -12.876 1.00 21.27  ? 62  HIS A CE1    1 
ATOM   999  N  NE2    . HIS A 1 63  ? 0.045   10.026  -13.213 1.00 21.09  ? 62  HIS A NE2    1 
ATOM   1000 H  H      . HIS A 1 63  ? 0.874   8.287   -9.427  1.00 24.42  ? 62  HIS A H      1 
ATOM   1001 H  HA     . HIS A 1 63  ? -0.111  10.263  -7.850  1.00 25.12  ? 62  HIS A HA     1 
ATOM   1002 H  HB2    . HIS A 1 63  ? 0.233   11.681  -9.611  1.00 24.85  ? 62  HIS A HB2    1 
ATOM   1003 H  HB3    . HIS A 1 63  ? 1.567   10.834  -9.443  1.00 24.85  ? 62  HIS A HB3    1 
ATOM   1004 H  HD2    . HIS A 1 63  ? -0.867  11.494  -12.082 1.00 24.57  ? 62  HIS A HD2    1 
ATOM   1005 H  HE1    . HIS A 1 63  ? 1.334   8.496   -13.439 1.00 25.54  ? 62  HIS A HE1    1 
ATOM   1006 H  HE2    . HIS A 1 63  ? -0.314  10.103  -13.991 1.00 25.33  ? 62  HIS A HE2    1 
ATOM   1007 N  N      . LEU A 1 64  ? -2.325  10.681  -9.131  1.00 21.16  ? 63  LEU A N      1 
ATOM   1008 C  CA     . LEU A 1 64  ? -3.667  10.689  -9.687  1.00 23.49  ? 63  LEU A CA     1 
ATOM   1009 C  C      . LEU A 1 64  ? -3.881  12.084  -10.240 1.00 23.87  ? 63  LEU A C      1 
ATOM   1010 O  O      . LEU A 1 64  ? -3.785  13.063  -9.494  1.00 24.13  ? 63  LEU A O      1 
ATOM   1011 C  CB     . LEU A 1 64  ? -4.719  10.348  -8.632  1.00 27.21  ? 63  LEU A CB     1 
ATOM   1012 C  CG     . LEU A 1 64  ? -6.175  10.304  -9.073  1.00 29.86  ? 63  LEU A CG     1 
ATOM   1013 C  CD1    . LEU A 1 64  ? -6.321  9.233   -10.097 1.00 29.41  ? 63  LEU A CD1    1 
ATOM   1014 C  CD2    . LEU A 1 64  ? -7.099  10.033  -7.866  1.00 34.43  ? 63  LEU A CD2    1 
ATOM   1015 H  H      . LEU A 1 64  ? -2.101  11.427  -8.767  1.00 25.41  ? 63  LEU A H      1 
ATOM   1016 H  HA     . LEU A 1 64  ? -3.729  10.048  -10.413 1.00 28.21  ? 63  LEU A HA     1 
ATOM   1017 H  HB2    . LEU A 1 64  ? -4.506  9.474   -8.269  1.00 32.68  ? 63  LEU A HB2    1 
ATOM   1018 H  HB3    . LEU A 1 64  ? -4.657  11.008  -7.924  1.00 32.68  ? 63  LEU A HB3    1 
ATOM   1019 H  HG     . LEU A 1 64  ? -6.423  11.153  -9.471  1.00 35.86  ? 63  LEU A HG     1 
ATOM   1020 H  HD11   . LEU A 1 64  ? -7.246  9.196   -10.386 1.00 35.31  ? 63  LEU A HD11   1 
ATOM   1021 H  HD12   . LEU A 1 64  ? -5.747  9.438   -10.852 1.00 35.31  ? 63  LEU A HD12   1 
ATOM   1022 H  HD13   . LEU A 1 64  ? -6.062  8.384   -9.706  1.00 35.31  ? 63  LEU A HD13   1 
ATOM   1023 H  HD21   . LEU A 1 64  ? -8.019  10.009  -8.173  1.00 41.33  ? 63  LEU A HD21   1 
ATOM   1024 H  HD22   . LEU A 1 64  ? -6.860  9.179   -7.472  1.00 41.33  ? 63  LEU A HD22   1 
ATOM   1025 H  HD23   . LEU A 1 64  ? -6.984  10.742  -7.215  1.00 41.33  ? 63  LEU A HD23   1 
ATOM   1026 N  N      . GLY A 1 65  ? -4.130  12.179  -11.533 1.00 23.65  ? 64  GLY A N      1 
ATOM   1027 C  CA     . GLY A 1 65  ? -4.433  13.475  -12.148 1.00 23.73  ? 64  GLY A CA     1 
ATOM   1028 C  C      . GLY A 1 65  ? -3.225  14.388  -12.130 1.00 23.25  ? 64  GLY A C      1 
ATOM   1029 O  O      . GLY A 1 65  ? -2.088  13.939  -12.009 1.00 21.75  ? 64  GLY A O      1 
ATOM   1030 H  H      . GLY A 1 65  ? -4.133  11.517  -12.081 1.00 28.40  ? 64  GLY A H      1 
ATOM   1031 H  HA2    . GLY A 1 65  ? -4.709  13.342  -13.069 1.00 28.49  ? 64  GLY A HA2    1 
ATOM   1032 H  HA3    . GLY A 1 65  ? -5.156  13.905  -11.666 1.00 28.49  ? 64  GLY A HA3    1 
ATOM   1033 N  N      . ARG A 1 66  ? -3.493  15.698  -12.223 1.00 24.93  ? 65  ARG A N      1 
ATOM   1034 C  CA     . ARG A 1 66  ? -2.453  16.731  -12.238 1.00 25.17  ? 65  ARG A CA     1 
ATOM   1035 C  C      . ARG A 1 66  ? -2.790  17.806  -11.207 1.00 29.90  ? 65  ARG A C      1 
ATOM   1036 O  O      . ARG A 1 66  ? -3.174  18.929  -11.563 1.00 33.44  ? 65  ARG A O      1 
ATOM   1037 C  CB     . ARG A 1 66  ? -2.290  17.351  -13.630 1.00 25.56  ? 65  ARG A CB     1 
ATOM   1038 C  CG     . ARG A 1 66  ? -1.656  16.378  -14.633 1.00 25.27  ? 65  ARG A CG     1 
ATOM   1039 C  CD     . ARG A 1 66  ? -1.507  16.964  -16.017 1.00 29.95  ? 65  ARG A CD     1 
ATOM   1040 N  NE     . ARG A 1 66  ? -0.806  16.041  -16.900 1.00 27.34  ? 65  ARG A NE     1 
ATOM   1041 C  CZ     . ARG A 1 66  ? -0.369  16.382  -18.103 1.00 27.79  ? 65  ARG A CZ     1 
ATOM   1042 N  NH1    . ARG A 1 66  ? -0.592  17.603  -18.568 1.00 31.40  1 65  ARG A NH1    1 
ATOM   1043 N  NH2    . ARG A 1 66  ? 0.268   15.500  -18.865 1.00 26.82  ? 65  ARG A NH2    1 
ATOM   1044 H  H      . ARG A 1 66  ? -4.290  16.017  -12.279 1.00 29.93  ? 65  ARG A H      1 
ATOM   1045 H  HA     . ARG A 1 66  ? -1.606  16.331  -11.988 1.00 30.22  ? 65  ARG A HA     1 
ATOM   1046 H  HB2    . ARG A 1 66  ? -3.163  17.605  -13.967 1.00 30.69  ? 65  ARG A HB2    1 
ATOM   1047 H  HB3    . ARG A 1 66  ? -1.718  18.132  -13.564 1.00 30.69  ? 65  ARG A HB3    1 
ATOM   1048 H  HG2    . ARG A 1 66  ? -0.773  16.132  -14.317 1.00 30.34  ? 65  ARG A HG2    1 
ATOM   1049 H  HG3    . ARG A 1 66  ? -2.215  15.589  -14.702 1.00 30.34  ? 65  ARG A HG3    1 
ATOM   1050 H  HD2    . ARG A 1 66  ? -2.385  17.137  -16.390 1.00 35.96  ? 65  ARG A HD2    1 
ATOM   1051 H  HD3    . ARG A 1 66  ? -0.994  17.786  -15.965 1.00 35.96  ? 65  ARG A HD3    1 
ATOM   1052 H  HE     . ARG A 1 66  ? -0.533  15.296  -16.568 1.00 32.82  ? 65  ARG A HE     1 
ATOM   1053 H  HH11   . ARG A 1 66  ? -1.004  18.180  -18.081 1.00 37.70  ? 65  ARG A HH11   1 
ATOM   1054 H  HH12   . ARG A 1 66  ? -0.313  17.822  -19.351 1.00 37.70  ? 65  ARG A HH12   1 
ATOM   1055 H  HH21   . ARG A 1 66  ? 0.411   14.704  -18.573 1.00 32.20  ? 65  ARG A HH21   1 
ATOM   1056 H  HH22   . ARG A 1 66  ? 0.541   15.727  -19.648 1.00 32.20  ? 65  ARG A HH22   1 
ATOM   1057 N  N      . PRO A 1 67  ? -2.635  17.493  -9.914  1.00 25.63  ? 66  PRO A N      1 
ATOM   1058 C  CA     . PRO A 1 67  ? -2.869  18.492  -8.858  1.00 27.38  ? 66  PRO A CA     1 
ATOM   1059 C  C      . PRO A 1 67  ? -1.749  19.517  -8.715  1.00 29.40  ? 66  PRO A C      1 
ATOM   1060 O  O      . PRO A 1 67  ? -1.884  20.462  -7.920  1.00 32.44  ? 66  PRO A O      1 
ATOM   1061 C  CB     . PRO A 1 67  ? -2.997  17.636  -7.591  1.00 27.25  ? 66  PRO A CB     1 
ATOM   1062 C  CG     . PRO A 1 67  ? -2.185  16.381  -7.895  1.00 24.34  ? 66  PRO A CG     1 
ATOM   1063 C  CD     . PRO A 1 67  ? -2.336  16.150  -9.380  1.00 23.74  ? 66  PRO A CD     1 
ATOM   1064 H  HA     . PRO A 1 67  ? -3.707  18.955  -9.015  1.00 32.87  ? 66  PRO A HA     1 
ATOM   1065 H  HB2    . PRO A 1 67  ? -2.625  18.112  -6.833  1.00 32.72  ? 66  PRO A HB2    1 
ATOM   1066 H  HB3    . PRO A 1 67  ? -3.929  17.414  -7.437  1.00 32.72  ? 66  PRO A HB3    1 
ATOM   1067 H  HG2    . PRO A 1 67  ? -1.255  16.533  -7.666  1.00 29.23  ? 66  PRO A HG2    1 
ATOM   1068 H  HG3    . PRO A 1 67  ? -2.543  15.632  -7.395  1.00 29.23  ? 66  PRO A HG3    1 
ATOM   1069 H  HD2    . PRO A 1 67  ? -1.507  15.814  -9.756  1.00 28.51  ? 66  PRO A HD2    1 
ATOM   1070 H  HD3    . PRO A 1 67  ? -3.075  15.545  -9.554  1.00 28.51  ? 66  PRO A HD3    1 
ATOM   1071 N  N      . ASP A 1 68  ? -0.637  19.326  -9.419  1.00 29.60  ? 67  ASP A N      1 
ATOM   1072 C  CA     . ASP A 1 68  ? 0.398   20.343  -9.592  1.00 32.41  ? 67  ASP A CA     1 
ATOM   1073 C  C      . ASP A 1 68  ? 1.076   20.732  -8.287  1.00 31.48  ? 67  ASP A C      1 
ATOM   1074 O  O      . ASP A 1 68  ? 1.468   21.883  -8.102  1.00 33.13  ? 67  ASP A O      1 
ATOM   1075 C  CB     . ASP A 1 68  ? -0.171  21.575  -10.294 1.00 40.11  ? 67  ASP A CB     1 
ATOM   1076 C  CG     . ASP A 1 68  ? -0.366  21.346  -11.797 1.00 48.86  ? 67  ASP A CG     1 
ATOM   1077 O  OD1    . ASP A 1 68  ? 0.304   20.451  -12.356 1.00 48.31  ? 67  ASP A OD1    1 
ATOM   1078 O  OD2    . ASP A 1 68  ? -1.187  22.057  -12.410 1.00 52.13  1 67  ASP A OD2    1 
ATOM   1079 H  H      . ASP A 1 68  ? -0.453  18.588  -9.820  1.00 35.54  ? 67  ASP A H      1 
ATOM   1080 H  HA     . ASP A 1 68  ? 1.085   19.977  -10.171 1.00 38.91  ? 67  ASP A HA     1 
ATOM   1081 H  HB2    . ASP A 1 68  ? -1.034  21.792  -9.907  1.00 48.16  ? 67  ASP A HB2    1 
ATOM   1082 H  HB3    . ASP A 1 68  ? 0.442   22.318  -10.179 1.00 48.16  ? 67  ASP A HB3    1 
ATOM   1083 N  N      . GLY A 1 69  ? 1.256   19.764  -7.389  1.00 30.37  ? 68  GLY A N      1 
ATOM   1084 C  CA     . GLY A 1 69  ? 2.084   19.988  -6.222  1.00 31.89  ? 68  GLY A CA     1 
ATOM   1085 C  C      . GLY A 1 69  ? 1.360   20.640  -5.077  1.00 35.96  ? 68  GLY A C      1 
ATOM   1086 O  O      . GLY A 1 69  ? 2.004   21.190  -4.184  1.00 39.94  ? 68  GLY A O      1 
ATOM   1087 H  H      . GLY A 1 69  ? 0.912   18.977  -7.438  1.00 36.46  ? 68  GLY A H      1 
ATOM   1088 H  HA2    . GLY A 1 69  ? 2.435   19.138  -5.912  1.00 38.29  ? 68  GLY A HA2    1 
ATOM   1089 H  HA3    . GLY A 1 69  ? 2.833   20.553  -6.467  1.00 38.29  ? 68  GLY A HA3    1 
ATOM   1090 N  N      . VAL A 1 70  ? 0.033   20.612  -5.092  1.00 36.17  ? 69  VAL A N      1 
ATOM   1091 C  CA     . VAL A 1 70  ? -0.778  21.109  -3.987  1.00 40.64  ? 69  VAL A CA     1 
ATOM   1092 C  C      . VAL A 1 70  ? -1.645  19.954  -3.514  1.00 36.99  ? 69  VAL A C      1 
ATOM   1093 O  O      . VAL A 1 70  ? -2.170  19.201  -4.353  1.00 33.97  ? 69  VAL A O      1 
ATOM   1094 C  CB     . VAL A 1 70  ? -1.649  22.297  -4.412  1.00 49.43  ? 69  VAL A CB     1 
ATOM   1095 C  CG1    . VAL A 1 70  ? -2.545  22.732  -3.259  1.00 49.95  ? 69  VAL A CG1    1 
ATOM   1096 C  CG2    . VAL A 1 70  ? -0.769  23.436  -4.884  1.00 56.58  ? 69  VAL A CG2    1 
ATOM   1097 H  H      . VAL A 1 70  ? -0.432  20.304  -5.746  1.00 43.42  ? 69  VAL A H      1 
ATOM   1098 H  HA     . VAL A 1 70  ? -0.204  21.388  -3.257  1.00 48.78  ? 69  VAL A HA     1 
ATOM   1099 H  HB     . VAL A 1 70  ? -2.217  22.028  -5.151  1.00 59.34  ? 69  VAL A HB     1 
ATOM   1100 H  HG11   . VAL A 1 70  ? -3.087  23.483  -3.547  1.00 59.96  ? 69  VAL A HG11   1 
ATOM   1101 H  HG12   . VAL A 1 70  ? -3.116  21.989  -3.006  1.00 59.96  ? 69  VAL A HG12   1 
ATOM   1102 H  HG13   . VAL A 1 70  ? -1.989  22.993  -2.509  1.00 59.96  ? 69  VAL A HG13   1 
ATOM   1103 H  HG21   . VAL A 1 70  ? -1.332  24.180  -5.149  1.00 67.91  ? 69  VAL A HG21   1 
ATOM   1104 H  HG22   . VAL A 1 70  ? -0.186  23.705  -4.158  1.00 67.91  ? 69  VAL A HG22   1 
ATOM   1105 H  HG23   . VAL A 1 70  ? -0.241  23.135  -5.639  1.00 67.91  ? 69  VAL A HG23   1 
ATOM   1106 N  N      . PRO A 1 71  ? -1.830  19.764  -2.207  1.00 40.21  ? 70  PRO A N      1 
ATOM   1107 C  CA     . PRO A 1 71  ? -2.761  18.723  -1.760  1.00 36.66  ? 70  PRO A CA     1 
ATOM   1108 C  C      . PRO A 1 71  ? -4.180  19.072  -2.160  1.00 33.69  ? 70  PRO A C      1 
ATOM   1109 O  O      . PRO A 1 71  ? -4.676  20.166  -1.879  1.00 37.32  ? 70  PRO A O      1 
ATOM   1110 C  CB     . PRO A 1 71  ? -2.581  18.707  -0.240  1.00 43.74  ? 70  PRO A CB     1 
ATOM   1111 C  CG     . PRO A 1 71  ? -1.200  19.239  -0.031  1.00 48.02  ? 70  PRO A CG     1 
ATOM   1112 C  CD     . PRO A 1 71  ? -1.014  20.277  -1.093  1.00 46.60  ? 70  PRO A CD     1 
ATOM   1113 H  HA     . PRO A 1 71  ? -2.517  17.860  -2.130  1.00 44.01  ? 70  PRO A HA     1 
ATOM   1114 H  HB2    . PRO A 1 71  ? -3.240  19.283  0.177   1.00 52.50  ? 70  PRO A HB2    1 
ATOM   1115 H  HB3    . PRO A 1 71  ? -2.655  17.798  0.091   1.00 52.50  ? 70  PRO A HB3    1 
ATOM   1116 H  HG2    . PRO A 1 71  ? -1.133  19.636  0.851   1.00 57.64  ? 70  PRO A HG2    1 
ATOM   1117 H  HG3    . PRO A 1 71  ? -0.554  18.523  -0.136  1.00 57.64  ? 70  PRO A HG3    1 
ATOM   1118 H  HD2    . PRO A 1 71  ? -1.352  21.135  -0.791  1.00 55.93  ? 70  PRO A HD2    1 
ATOM   1119 H  HD3    . PRO A 1 71  ? -0.081  20.332  -1.353  1.00 55.93  ? 70  PRO A HD3    1 
ATOM   1120 N  N      . MET A 1 72  ? -4.840  18.124  -2.805  1.00 32.82  ? 71  MET A N      1 
ATOM   1121 C  CA     . MET A 1 72  ? -6.229  18.288  -3.238  1.00 37.31  ? 71  MET A CA     1 
ATOM   1122 C  C      . MET A 1 72  ? -6.977  16.986  -2.966  1.00 41.99  ? 71  MET A C      1 
ATOM   1123 O  O      . MET A 1 72  ? -7.494  16.343  -3.884  1.00 41.42  ? 71  MET A O      1 
ATOM   1124 C  CB     . MET A 1 72  ? -6.280  18.668  -4.721  1.00 37.64  ? 71  MET A CB     1 
ATOM   1125 C  CG     . MET A 1 72  ? -5.590  19.986  -5.069  1.00 45.09  ? 71  MET A CG     1 
ATOM   1126 S  SD     . MET A 1 72  ? -5.699  20.426  -6.838  1.00 49.70  ? 71  MET A SD     1 
ATOM   1127 C  CE     . MET A 1 72  ? -4.502  21.756  -6.922  1.00 49.61  ? 71  MET A CE     1 
ATOM   1128 H  H      . MET A 1 72  ? -4.504  17.360  -3.009  1.00 39.40  ? 71  MET A H      1 
ATOM   1129 H  HA     . MET A 1 72  ? -6.640  19.004  -2.728  1.00 44.79  ? 71  MET A HA     1 
ATOM   1130 H  HB2    . MET A 1 72  ? -5.849  17.967  -5.235  1.00 45.18  ? 71  MET A HB2    1 
ATOM   1131 H  HB3    . MET A 1 72  ? -7.209  18.744  -4.989  1.00 45.18  ? 71  MET A HB3    1 
ATOM   1132 H  HG2    . MET A 1 72  ? -6.004  20.700  -4.560  1.00 54.13  ? 71  MET A HG2    1 
ATOM   1133 H  HG3    . MET A 1 72  ? -4.651  19.918  -4.837  1.00 54.13  ? 71  MET A HG3    1 
ATOM   1134 H  HE1    . MET A 1 72  ? -4.463  22.087  -7.833  1.00 59.55  ? 71  MET A HE1    1 
ATOM   1135 H  HE2    . MET A 1 72  ? -4.778  22.467  -6.323  1.00 59.55  ? 71  MET A HE2    1 
ATOM   1136 H  HE3    . MET A 1 72  ? -3.634  21.416  -6.655  1.00 59.55  ? 71  MET A HE3    1 
ATOM   1137 N  N      . PRO A 1 73  ? -7.021  16.546  -1.705  1.00 48.35  ? 72  PRO A N      1 
ATOM   1138 C  CA     . PRO A 1 73  ? -7.707  15.279  -1.405  1.00 50.39  ? 72  PRO A CA     1 
ATOM   1139 C  C      . PRO A 1 73  ? -9.180  15.312  -1.752  1.00 55.15  ? 72  PRO A C      1 
ATOM   1140 O  O      . PRO A 1 73  ? -9.768  14.249  -1.984  1.00 55.98  ? 72  PRO A O      1 
ATOM   1141 C  CB     . PRO A 1 73  ? -7.484  15.102  0.104   1.00 50.36  ? 72  PRO A CB     1 
ATOM   1142 C  CG     . PRO A 1 73  ? -7.322  16.481  0.618   1.00 50.88  ? 72  PRO A CG     1 
ATOM   1143 C  CD     . PRO A 1 73  ? -6.611  17.248  -0.475  1.00 51.18  ? 72  PRO A CD     1 
ATOM   1144 H  HA     . PRO A 1 73  ? -7.283  14.546  -1.879  1.00 60.48  ? 72  PRO A HA     1 
ATOM   1145 H  HB2    . PRO A 1 73  ? -8.258  14.674  0.502   1.00 60.45  ? 72  PRO A HB2    1 
ATOM   1146 H  HB3    . PRO A 1 73  ? -6.682  14.580  0.258   1.00 60.45  ? 72  PRO A HB3    1 
ATOM   1147 H  HG2    . PRO A 1 73  ? -8.194  16.867  0.793   1.00 61.07  ? 72  PRO A HG2    1 
ATOM   1148 H  HG3    . PRO A 1 73  ? -6.787  16.465  1.427   1.00 61.07  ? 72  PRO A HG3    1 
ATOM   1149 H  HD2    . PRO A 1 73  ? -6.914  18.169  -0.494  1.00 61.43  ? 72  PRO A HD2    1 
ATOM   1150 H  HD3    . PRO A 1 73  ? -5.650  17.192  -0.357  1.00 61.43  ? 72  PRO A HD3    1 
ATOM   1151 N  N      . ASP A 1 74  ? -9.784  16.505  -1.794  1.00 54.95  ? 73  ASP A N      1 
ATOM   1152 C  CA     . ASP A 1 74  ? -11.163 16.670  -2.251  1.00 68.84  ? 73  ASP A CA     1 
ATOM   1153 C  C      . ASP A 1 74  ? -11.441 15.915  -3.554  1.00 76.23  ? 73  ASP A C      1 
ATOM   1154 O  O      . ASP A 1 74  ? -12.425 15.175  -3.654  1.00 79.25  ? 73  ASP A O      1 
ATOM   1155 C  CB     . ASP A 1 74  ? -11.473 18.167  -2.418  1.00 77.82  ? 73  ASP A CB     1 
ATOM   1156 C  CG     . ASP A 1 74  ? -10.252 18.984  -2.884  1.00 81.49  ? 73  ASP A CG     1 
ATOM   1157 O  OD1    . ASP A 1 74  ? -9.160  18.824  -2.296  1.00 80.70  ? 73  ASP A OD1    1 
ATOM   1158 O  OD2    . ASP A 1 74  ? -10.383 19.785  -3.836  1.00 83.16  1 73  ASP A OD2    1 
ATOM   1159 H  H      . ASP A 1 74  ? -9.408  17.242  -1.560  1.00 65.95  ? 73  ASP A H      1 
ATOM   1160 H  HA     . ASP A 1 74  ? -11.761 16.318  -1.573  1.00 82.63  ? 73  ASP A HA     1 
ATOM   1161 H  HB2    . ASP A 1 74  ? -12.174 18.272  -3.080  1.00 93.40  ? 73  ASP A HB2    1 
ATOM   1162 H  HB3    . ASP A 1 74  ? -11.766 18.526  -1.566  1.00 93.40  ? 73  ASP A HB3    1 
ATOM   1163 N  N      . LYS A 1 75  ? -10.598 16.098  -4.574  1.00 77.37  ? 74  LYS A N      1 
ATOM   1164 C  CA     . LYS A 1 75  ? -10.892 15.560  -5.896  1.00 72.67  ? 74  LYS A CA     1 
ATOM   1165 C  C      . LYS A 1 75  ? -9.844  14.605  -6.446  1.00 44.95  ? 74  LYS A C      1 
ATOM   1166 O  O      . LYS A 1 75  ? -10.144 13.885  -7.403  1.00 40.55  ? 74  LYS A O      1 
ATOM   1167 C  CB     . LYS A 1 75  ? -11.091 16.700  -6.908  1.00 98.04  ? 74  LYS A CB     1 
ATOM   1168 C  CG     . LYS A 1 75  ? -10.259 17.937  -6.636  1.00 122.26 ? 74  LYS A CG     1 
ATOM   1169 C  CD     . LYS A 1 75  ? -10.622 19.046  -7.598  1.00 144.68 ? 74  LYS A CD     1 
ATOM   1170 C  CE     . LYS A 1 75  ? -10.655 20.394  -6.904  1.00 163.17 ? 74  LYS A CE     1 
ATOM   1171 N  NZ     . LYS A 1 75  ? -11.244 21.440  -7.781  1.00 174.16 1 74  LYS A NZ     1 
ATOM   1172 H  H      . LYS A 1 75  ? -9.855  16.528  -4.523  1.00 92.86  ? 74  LYS A H      1 
ATOM   1173 H  HA     . LYS A 1 75  ? -11.727 15.070  -5.845  1.00 87.23  ? 74  LYS A HA     1 
ATOM   1174 H  HB2    . LYS A 1 75  ? -10.855 16.375  -7.791  1.00 117.67 ? 74  LYS A HB2    1 
ATOM   1175 H  HB3    . LYS A 1 75  ? -12.024 16.965  -6.896  1.00 117.67 ? 74  LYS A HB3    1 
ATOM   1176 H  HG2    . LYS A 1 75  ? -10.427 18.248  -5.733  1.00 146.73 ? 74  LYS A HG2    1 
ATOM   1177 H  HG3    . LYS A 1 75  ? -9.319  17.726  -6.752  1.00 146.73 ? 74  LYS A HG3    1 
ATOM   1178 H  HD2    . LYS A 1 75  ? -9.961  19.085  -8.306  1.00 173.64 ? 74  LYS A HD2    1 
ATOM   1179 H  HD3    . LYS A 1 75  ? -11.502 18.873  -7.968  1.00 173.64 ? 74  LYS A HD3    1 
ATOM   1180 H  HE2    . LYS A 1 75  ? -11.197 20.329  -6.102  1.00 195.83 ? 74  LYS A HE2    1 
ATOM   1181 H  HE3    . LYS A 1 75  ? -9.750  20.660  -6.677  1.00 195.83 ? 74  LYS A HE3    1 
ATOM   1182 H  HZ1    . LYS A 1 75  ? -11.254 22.222  -7.356  1.00 209.02 ? 74  LYS A HZ1    1 
ATOM   1183 H  HZ2    . LYS A 1 75  ? -10.761 21.521  -8.524  1.00 209.02 ? 74  LYS A HZ2    1 
ATOM   1184 H  HZ3    . LYS A 1 75  ? -12.077 21.219  -8.000  1.00 209.02 ? 74  LYS A HZ3    1 
ATOM   1185 N  N      . TYR A 1 76  ? -8.638  14.561  -5.871  1.00 36.23  ? 75  TYR A N      1 
ATOM   1186 C  CA     . TYR A 1 76  ? -7.556  13.741  -6.399  1.00 30.71  ? 75  TYR A CA     1 
ATOM   1187 C  C      . TYR A 1 76  ? -6.989  12.755  -5.380  1.00 28.77  ? 75  TYR A C      1 
ATOM   1188 O  O      . TYR A 1 76  ? -5.841  12.318  -5.535  1.00 30.10  ? 75  TYR A O      1 
ATOM   1189 C  CB     . TYR A 1 76  ? -6.425  14.628  -6.923  1.00 32.99  ? 75  TYR A CB     1 
ATOM   1190 C  CG     . TYR A 1 76  ? -6.775  15.513  -8.089  1.00 36.39  ? 75  TYR A CG     1 
ATOM   1191 C  CD1    . TYR A 1 76  ? -7.011  14.972  -9.343  1.00 39.36  ? 75  TYR A CD1    1 
ATOM   1192 C  CD2    . TYR A 1 76  ? -6.839  16.892  -7.950  1.00 41.08  ? 75  TYR A CD2    1 
ATOM   1193 C  CE1    . TYR A 1 76  ? -7.319  15.775  -10.429 1.00 44.05  ? 75  TYR A CE1    1 
ATOM   1194 C  CE2    . TYR A 1 76  ? -7.145  17.706  -9.037  1.00 48.48  ? 75  TYR A CE2    1 
ATOM   1195 C  CZ     . TYR A 1 76  ? -7.379  17.132  -10.277 1.00 50.09  ? 75  TYR A CZ     1 
ATOM   1196 O  OH     . TYR A 1 76  ? -7.694  17.902  -11.377 1.00 55.64  ? 75  TYR A OH     1 
ATOM   1197 H  H      . TYR A 1 76  ? -8.424  15.005  -5.166  1.00 43.50  ? 75  TYR A H      1 
ATOM   1198 H  HA     . TYR A 1 76  ? -7.896  13.226  -7.147  1.00 36.87  ? 75  TYR A HA     1 
ATOM   1199 H  HB2    . TYR A 1 76  ? -6.128  15.204  -6.201  1.00 39.60  ? 75  TYR A HB2    1 
ATOM   1200 H  HB3    . TYR A 1 76  ? -5.692  14.057  -7.203  1.00 39.60  ? 75  TYR A HB3    1 
ATOM   1201 H  HD1    . TYR A 1 76  ? -6.967  14.050  -9.456  1.00 47.25  ? 75  TYR A HD1    1 
ATOM   1202 H  HD2    . TYR A 1 76  ? -6.677  17.278  -7.119  1.00 49.31  ? 75  TYR A HD2    1 
ATOM   1203 H  HE1    . TYR A 1 76  ? -7.478  15.392  -11.261 1.00 52.88  ? 75  TYR A HE1    1 
ATOM   1204 H  HE2    . TYR A 1 76  ? -7.191  18.629  -8.933  1.00 58.19  ? 75  TYR A HE2    1 
ATOM   1205 H  HH     . TYR A 1 76  ? -7.702  18.715  -11.166 1.00 66.79  ? 75  TYR A HH     1 
ATOM   1206 N  N      . SER A 1 77  ? -7.755  12.371  -4.358  1.00 30.92  ? 76  SER A N      1 
ATOM   1207 C  CA     . SER A 1 77  ? -7.271  11.375  -3.406  1.00 32.39  ? 76  SER A CA     1 
ATOM   1208 C  C      . SER A 1 77  ? -7.245  9.991   -4.044  1.00 30.61  ? 76  SER A C      1 
ATOM   1209 O  O      . SER A 1 77  ? -8.104  9.650   -4.865  1.00 30.93  ? 76  SER A O      1 
ATOM   1210 C  CB     . SER A 1 77  ? -8.145  11.342  -2.148  1.00 38.67  ? 76  SER A CB     1 
ATOM   1211 O  OG     . SER A 1 77  ? -7.676  10.345  -1.256  1.00 36.13  ? 76  SER A OG     1 
ATOM   1212 H  H      . SER A 1 77  ? -8.546  12.667  -4.197  1.00 37.12  ? 76  SER A H      1 
ATOM   1213 H  HA     . SER A 1 77  ? -6.366  11.602  -3.140  1.00 38.89  ? 76  SER A HA     1 
ATOM   1214 H  HB2    . SER A 1 77  ? -8.104  12.206  -1.709  1.00 46.42  ? 76  SER A HB2    1 
ATOM   1215 H  HB3    . SER A 1 77  ? -9.059  11.138  -2.400  1.00 46.42  ? 76  SER A HB3    1 
ATOM   1216 H  HG     . SER A 1 77  ? -6.883  10.509  -1.033  1.00 43.38  ? 76  SER A HG     1 
ATOM   1217 N  N      . LEU A 1 78  ? -6.237  9.189   -3.675  1.00 29.53  ? 77  LEU A N      1 
ATOM   1218 C  CA     . LEU A 1 78  ? -6.206  7.781   -4.066  1.00 29.72  ? 77  LEU A CA     1 
ATOM   1219 C  C      . LEU A 1 78  ? -7.042  6.888   -3.157  1.00 28.91  ? 77  LEU A C      1 
ATOM   1220 O  O      . LEU A 1 78  ? -7.041  5.670   -3.349  1.00 31.83  ? 77  LEU A O      1 
ATOM   1221 C  CB     . LEU A 1 78  ? -4.759  7.265   -4.088  1.00 29.38  ? 77  LEU A CB     1 
ATOM   1222 C  CG     . LEU A 1 78  ? -3.949  7.670   -5.327  1.00 28.59  ? 77  LEU A CG     1 
ATOM   1223 C  CD1    . LEU A 1 78  ? -2.442  7.375   -5.097  1.00 28.26  ? 77  LEU A CD1    1 
ATOM   1224 C  CD2    . LEU A 1 78  ? -4.444  6.985   -6.593  1.00 30.32  ? 77  LEU A CD2    1 
ATOM   1225 H  H      . LEU A 1 78  ? -5.564  9.439   -3.202  1.00 35.46  ? 77  LEU A H      1 
ATOM   1226 H  HA     . LEU A 1 78  ? -6.561  7.701   -4.965  1.00 35.68  ? 77  LEU A HA     1 
ATOM   1227 H  HB2    . LEU A 1 78  ? -4.296  7.611   -3.309  1.00 35.28  ? 77  LEU A HB2    1 
ATOM   1228 H  HB3    . LEU A 1 78  ? -4.777  6.296   -4.053  1.00 35.28  ? 77  LEU A HB3    1 
ATOM   1229 H  HG     . LEU A 1 78  ? -4.042  8.627   -5.457  1.00 34.32  ? 77  LEU A HG     1 
ATOM   1230 H  HD11   . LEU A 1 78  ? -1.945  7.637   -5.888  1.00 33.93  ? 77  LEU A HD11   1 
ATOM   1231 H  HD12   . LEU A 1 78  ? -2.134  7.883   -4.330  1.00 33.93  ? 77  LEU A HD12   1 
ATOM   1232 H  HD13   . LEU A 1 78  ? -2.328  6.426   -4.933  1.00 33.93  ? 77  LEU A HD13   1 
ATOM   1233 H  HD21   . LEU A 1 78  ? -3.899  7.275   -7.342  1.00 36.40  ? 77  LEU A HD21   1 
ATOM   1234 H  HD22   . LEU A 1 78  ? -4.369  6.024   -6.482  1.00 36.40  ? 77  LEU A HD22   1 
ATOM   1235 H  HD23   . LEU A 1 78  ? -5.370  7.230   -6.743  1.00 36.40  ? 77  LEU A HD23   1 
ATOM   1236 N  N      . GLU A 1 79  ? -7.775  7.439   -2.194  1.00 29.87  ? 78  GLU A N      1 
ATOM   1237 C  CA     . GLU A 1 79  ? -8.526  6.574   -1.290  1.00 33.68  ? 78  GLU A CA     1 
ATOM   1238 C  C      . GLU A 1 79  ? -9.493  5.655   -2.027  1.00 33.91  ? 78  GLU A C      1 
ATOM   1239 O  O      . GLU A 1 79  ? -9.626  4.487   -1.617  1.00 32.87  ? 78  GLU A O      1 
ATOM   1240 C  CB     . GLU A 1 79  ? -9.274  7.412   -0.243  1.00 46.35  ? 78  GLU A CB     1 
ATOM   1241 C  CG     . GLU A 1 79  ? -9.949  6.553   0.811   1.00 64.36  ? 78  GLU A CG     1 
ATOM   1242 C  CD     . GLU A 1 79  ? -10.264 7.319   2.079   1.00 85.18  ? 78  GLU A CD     1 
ATOM   1243 O  OE1    . GLU A 1 79  ? -10.263 8.568   2.038   1.00 91.52  ? 78  GLU A OE1    1 
ATOM   1244 O  OE2    . GLU A 1 79  ? -10.504 6.670   3.120   1.00 93.06  1 78  GLU A OE2    1 
ATOM   1245 H  H      . GLU A 1 79  ? -7.854  8.282   -2.046  1.00 35.86  ? 78  GLU A H      1 
ATOM   1246 H  HA     . GLU A 1 79  ? -7.897  6.010   -0.813  1.00 40.43  ? 78  GLU A HA     1 
ATOM   1247 H  HB2    . GLU A 1 79  ? -8.643  7.998   0.204   1.00 55.64  ? 78  GLU A HB2    1 
ATOM   1248 H  HB3    . GLU A 1 79  ? -9.959  7.937   -0.688  1.00 55.64  ? 78  GLU A HB3    1 
ATOM   1249 H  HG2    . GLU A 1 79  ? -10.782 6.210   0.453   1.00 77.25  ? 78  GLU A HG2    1 
ATOM   1250 H  HG3    . GLU A 1 79  ? -9.360  5.818   1.043   1.00 77.25  ? 78  GLU A HG3    1 
ATOM   1251 N  N      . PRO A 1 80  ? -10.193 6.093   -3.077  1.00 38.23  ? 79  PRO A N      1 
ATOM   1252 C  CA     . PRO A 1 80  ? -11.087 5.162   -3.787  1.00 38.95  ? 79  PRO A CA     1 
ATOM   1253 C  C      . PRO A 1 80  ? -10.351 4.023   -4.459  1.00 34.04  ? 79  PRO A C      1 
ATOM   1254 O  O      . PRO A 1 80  ? -10.918 2.935   -4.619  1.00 35.74  ? 79  PRO A O      1 
ATOM   1255 C  CB     . PRO A 1 80  ? -11.789 6.067   -4.806  1.00 44.56  ? 79  PRO A CB     1 
ATOM   1256 C  CG     . PRO A 1 80  ? -11.669 7.449   -4.233  1.00 49.49  ? 79  PRO A CG     1 
ATOM   1257 C  CD     . PRO A 1 80  ? -10.355 7.481   -3.545  1.00 42.51  ? 79  PRO A CD     1 
ATOM   1258 H  HA     . PRO A 1 80  ? -11.746 4.799   -3.175  1.00 46.76  ? 79  PRO A HA     1 
ATOM   1259 H  HB2    . PRO A 1 80  ? -11.338 6.008   -5.662  1.00 53.50  ? 79  PRO A HB2    1 
ATOM   1260 H  HB3    . PRO A 1 80  ? -12.720 5.808   -4.888  1.00 53.50  ? 79  PRO A HB3    1 
ATOM   1261 H  HG2    . PRO A 1 80  ? -11.696 8.102   -4.950  1.00 59.40  ? 79  PRO A HG2    1 
ATOM   1262 H  HG3    . PRO A 1 80  ? -12.389 7.604   -3.602  1.00 59.40  ? 79  PRO A HG3    1 
ATOM   1263 H  HD2    . PRO A 1 80  ? -9.650  7.714   -4.170  1.00 51.03  ? 79  PRO A HD2    1 
ATOM   1264 H  HD3    . PRO A 1 80  ? -10.381 8.092   -2.792  1.00 51.03  ? 79  PRO A HD3    1 
ATOM   1265 N  N      . VAL A 1 81  ? -9.105  4.251   -4.880  1.00 29.54  ? 80  VAL A N      1 
ATOM   1266 C  CA     . VAL A 1 81  ? -8.286  3.182   -5.442  1.00 30.39  ? 80  VAL A CA     1 
ATOM   1267 C  C      . VAL A 1 81  ? -7.986  2.126   -4.392  1.00 30.88  ? 80  VAL A C      1 
ATOM   1268 O  O      . VAL A 1 81  ? -7.994  0.921   -4.678  1.00 32.18  ? 80  VAL A O      1 
ATOM   1269 C  CB     . VAL A 1 81  ? -6.996  3.766   -6.035  1.00 32.12  ? 80  VAL A CB     1 
ATOM   1270 C  CG1    . VAL A 1 81  ? -6.020  2.632   -6.413  1.00 32.46  ? 80  VAL A CG1    1 
ATOM   1271 C  CG2    . VAL A 1 81  ? -7.317  4.628   -7.260  1.00 35.84  ? 80  VAL A CG2    1 
ATOM   1272 H  H      . VAL A 1 81  ? -8.713  5.016   -4.849  1.00 35.46  ? 80  VAL A H      1 
ATOM   1273 H  HA     . VAL A 1 81  ? -8.778  2.756   -6.161  1.00 36.49  ? 80  VAL A HA     1 
ATOM   1274 H  HB     . VAL A 1 81  ? -6.566  4.328   -5.372  1.00 38.56  ? 80  VAL A HB     1 
ATOM   1275 H  HG11   . VAL A 1 81  ? -5.213  3.022   -6.785  1.00 38.97  ? 80  VAL A HG11   1 
ATOM   1276 H  HG12   . VAL A 1 81  ? -5.805  2.123   -5.616  1.00 38.97  ? 80  VAL A HG12   1 
ATOM   1277 H  HG13   . VAL A 1 81  ? -6.443  2.057   -7.069  1.00 38.97  ? 80  VAL A HG13   1 
ATOM   1278 H  HG21   . VAL A 1 81  ? -6.490  4.986   -7.619  1.00 43.03  ? 80  VAL A HG21   1 
ATOM   1279 H  HG22   . VAL A 1 81  ? -7.757  4.077   -7.927  1.00 43.03  ? 80  VAL A HG22   1 
ATOM   1280 H  HG23   . VAL A 1 81  ? -7.903  5.352   -6.991  1.00 43.03  ? 80  VAL A HG23   1 
ATOM   1281 N  N      . ALA A 1 82  ? -7.665  2.550   -3.173  1.00 32.24  ? 81  ALA A N      1 
ATOM   1282 C  CA     . ALA A 1 82  ? -7.499  1.587   -2.089  1.00 34.63  ? 81  ALA A CA     1 
ATOM   1283 C  C      . ALA A 1 82  ? -8.698  0.648   -1.969  1.00 36.84  ? 81  ALA A C      1 
ATOM   1284 O  O      . ALA A 1 82  ? -8.538  -0.570  -1.812  1.00 39.16  ? 81  ALA A O      1 
ATOM   1285 C  CB     . ALA A 1 82  ? -7.267  2.327   -0.772  1.00 39.32  ? 81  ALA A CB     1 
ATOM   1286 H  H      . ALA A 1 82  ? -7.540  3.371   -2.950  1.00 38.70  ? 81  ALA A H      1 
ATOM   1287 H  HA     . ALA A 1 82  ? -6.714  1.045   -2.268  1.00 41.57  ? 81  ALA A HA     1 
ATOM   1288 H  HB1    . ALA A 1 82  ? -7.159  1.677   -0.060  1.00 47.20  ? 81  ALA A HB1    1 
ATOM   1289 H  HB2    . ALA A 1 82  ? -6.467  2.869   -0.851  1.00 47.20  ? 81  ALA A HB2    1 
ATOM   1290 H  HB3    . ALA A 1 82  ? -8.034  2.893   -0.589  1.00 47.20  ? 81  ALA A HB3    1 
ATOM   1291 N  N      . VAL A 1 83  ? -9.919  1.180   -2.017  1.00 38.15  ? 82  VAL A N      1 
ATOM   1292 C  CA     . VAL A 1 83  ? -11.060 0.287   -1.815  1.00 40.57  ? 82  VAL A CA     1 
ATOM   1293 C  C      . VAL A 1 83  ? -11.202 -0.664  -3.000  1.00 38.00  ? 82  VAL A C      1 
ATOM   1294 O  O      . VAL A 1 83  ? -11.510 -1.852  -2.826  1.00 39.28  ? 82  VAL A O      1 
ATOM   1295 C  CB     . VAL A 1 83  ? -12.366 1.071   -1.527  1.00 51.43  ? 82  VAL A CB     1 
ATOM   1296 C  CG1    . VAL A 1 83  ? -12.105 2.326   -0.670  1.00 46.13  ? 82  VAL A CG1    1 
ATOM   1297 C  CG2    . VAL A 1 83  ? -13.135 1.420   -2.781  1.00 61.78  ? 82  VAL A CG2    1 
ATOM   1298 H  H      . VAL A 1 83  ? -10.108 2.007   -2.158  1.00 45.80  ? 82  VAL A H      1 
ATOM   1299 H  HA     . VAL A 1 83  ? -10.879 -0.258  -1.033  1.00 48.70  ? 82  VAL A HA     1 
ATOM   1300 H  HB     . VAL A 1 83  ? -12.942 0.494   -1.002  1.00 61.73  ? 82  VAL A HB     1 
ATOM   1301 H  HG11   . VAL A 1 83  ? -12.947 2.783   -0.515  1.00 55.37  ? 82  VAL A HG11   1 
ATOM   1302 H  HG12   . VAL A 1 83  ? -11.715 2.054   0.176   1.00 55.37  ? 82  VAL A HG12   1 
ATOM   1303 H  HG13   . VAL A 1 83  ? -11.493 2.910   -1.144  1.00 55.37  ? 82  VAL A HG13   1 
ATOM   1304 H  HG21   . VAL A 1 83  ? -13.937 1.906   -2.534  1.00 74.16  ? 82  VAL A HG21   1 
ATOM   1305 H  HG22   . VAL A 1 83  ? -12.576 1.970   -3.351  1.00 74.16  ? 82  VAL A HG22   1 
ATOM   1306 H  HG23   . VAL A 1 83  ? -13.374 0.601   -3.242  1.00 74.16  ? 82  VAL A HG23   1 
ATOM   1307 N  N      . GLU A 1 84  ? -10.936 -0.175  -4.221  1.00 37.32  ? 83  GLU A N      1 
ATOM   1308 C  CA     . GLU A 1 84  ? -10.983 -1.049  -5.391  1.00 40.35  ? 83  GLU A CA     1 
ATOM   1309 C  C      . GLU A 1 84  ? -9.888  -2.109  -5.337  1.00 40.05  ? 83  GLU A C      1 
ATOM   1310 O  O      . GLU A 1 84  ? -10.131 -3.272  -5.680  1.00 40.44  ? 83  GLU A O      1 
ATOM   1311 C  CB     . GLU A 1 84  ? -10.860 -0.227  -6.678  1.00 40.02  ? 83  GLU A CB     1 
ATOM   1312 C  CG     . GLU A 1 84  ? -11.084 -1.026  -7.969  1.00 47.39  ? 83  GLU A CG     1 
ATOM   1313 C  CD     . GLU A 1 84  ? -12.539 -1.414  -8.192  1.00 57.47  ? 83  GLU A CD     1 
ATOM   1314 O  OE1    . GLU A 1 84  ? -13.430 -0.785  -7.576  1.00 62.07  ? 83  GLU A OE1    1 
ATOM   1315 O  OE2    . GLU A 1 84  ? -12.790 -2.345  -8.990  1.00 58.94  1 83  GLU A OE2    1 
ATOM   1316 H  H      . GLU A 1 84  ? -10.731 0.643   -4.391  1.00 44.80  ? 83  GLU A H      1 
ATOM   1317 H  HA     . GLU A 1 84  ? -11.839 -1.505  -5.409  1.00 48.44  ? 83  GLU A HA     1 
ATOM   1318 H  HB2    . GLU A 1 84  ? -11.518 0.485   -6.656  1.00 48.05  ? 83  GLU A HB2    1 
ATOM   1319 H  HB3    . GLU A 1 84  ? -9.968  0.153   -6.719  1.00 48.05  ? 83  GLU A HB3    1 
ATOM   1320 H  HG2    . GLU A 1 84  ? -10.800 -0.488  -8.725  1.00 56.89  ? 83  GLU A HG2    1 
ATOM   1321 H  HG3    . GLU A 1 84  ? -10.560 -1.842  -7.929  1.00 56.89  ? 83  GLU A HG3    1 
ATOM   1322 N  N      . LEU A 1 85  ? -8.669  -1.728  -4.931  1.00 35.88  ? 84  LEU A N      1 
ATOM   1323 C  CA     . LEU A 1 85  ? -7.582  -2.702  -4.894  1.00 36.06  ? 84  LEU A CA     1 
ATOM   1324 C  C      . LEU A 1 85  ? -7.874  -3.826  -3.906  1.00 39.22  ? 84  LEU A C      1 
ATOM   1325 O  O      . LEU A 1 85  ? -7.509  -4.982  -4.157  1.00 39.19  ? 84  LEU A O      1 
ATOM   1326 C  CB     . LEU A 1 85  ? -6.271  -1.996  -4.551  1.00 35.73  ? 84  LEU A CB     1 
ATOM   1327 C  CG     . LEU A 1 85  ? -5.007  -2.857  -4.487  1.00 37.77  ? 84  LEU A CG     1 
ATOM   1328 C  CD1    . LEU A 1 85  ? -4.698  -3.514  -5.812  1.00 40.66  ? 84  LEU A CD1    1 
ATOM   1329 C  CD2    . LEU A 1 85  ? -3.816  -2.000  -4.033  1.00 35.77  ? 84  LEU A CD2    1 
ATOM   1330 H  H      . LEU A 1 85  ? -8.455  -0.935  -4.679  1.00 43.07  ? 84  LEU A H      1 
ATOM   1331 H  HA     . LEU A 1 85  ? -7.485  -3.097  -5.774  1.00 43.30  ? 84  LEU A HA     1 
ATOM   1332 H  HB2    . LEU A 1 85  ? -6.115  -1.310  -5.220  1.00 42.89  ? 84  LEU A HB2    1 
ATOM   1333 H  HB3    . LEU A 1 85  ? -6.373  -1.576  -3.683  1.00 42.89  ? 84  LEU A HB3    1 
ATOM   1334 H  HG     . LEU A 1 85  ? -5.137  -3.558  -3.830  1.00 45.35  ? 84  LEU A HG     1 
ATOM   1335 H  HD11   . LEU A 1 85  ? -3.892  -4.046  -5.720  1.00 48.81  ? 84  LEU A HD11   1 
ATOM   1336 H  HD12   . LEU A 1 85  ? -5.443  -4.082  -6.064  1.00 48.81  ? 84  LEU A HD12   1 
ATOM   1337 H  HD13   . LEU A 1 85  ? -4.565  -2.825  -6.482  1.00 48.81  ? 84  LEU A HD13   1 
ATOM   1338 H  HD21   . LEU A 1 85  ? -3.023  -2.557  -3.997  1.00 42.94  ? 84  LEU A HD21   1 
ATOM   1339 H  HD22   . LEU A 1 85  ? -3.686  -1.279  -4.669  1.00 42.94  ? 84  LEU A HD22   1 
ATOM   1340 H  HD23   . LEU A 1 85  ? -4.007  -1.636  -3.154  1.00 42.94  ? 84  LEU A HD23   1 
ATOM   1341 N  N      . LYS A 1 86  ? -8.552  -3.520  -2.797  1.00 41.59  ? 85  LYS A N      1 
ATOM   1342 C  CA     . LYS A 1 86  ? -8.900  -4.557  -1.826  1.00 48.59  ? 85  LYS A CA     1 
ATOM   1343 C  C      . LYS A 1 86  ? -9.678  -5.693  -2.483  1.00 47.92  ? 85  LYS A C      1 
ATOM   1344 O  O      . LYS A 1 86  ? -9.363  -6.875  -2.288  1.00 48.39  ? 85  LYS A O      1 
ATOM   1345 C  CB     . LYS A 1 86  ? -9.709  -3.957  -0.673  1.00 56.63  ? 85  LYS A CB     1 
ATOM   1346 C  CG     . LYS A 1 86  ? -8.865  -3.331  0.425   1.00 69.22  ? 85  LYS A CG     1 
ATOM   1347 C  CD     . LYS A 1 86  ? -9.687  -3.045  1.682   1.00 85.10  ? 85  LYS A CD     1 
ATOM   1348 C  CE     . LYS A 1 86  ? -10.275 -1.641  1.687   1.00 92.34  ? 85  LYS A CE     1 
ATOM   1349 N  NZ     . LYS A 1 86  ? -9.228  -0.591  1.857   1.00 92.98  1 85  LYS A NZ     1 
ATOM   1350 H  H      . LYS A 1 86  ? -8.819  -2.730  -2.587  1.00 49.93  ? 85  LYS A H      1 
ATOM   1351 H  HA     . LYS A 1 86  ? -8.083  -4.929  -1.457  1.00 58.33  ? 85  LYS A HA     1 
ATOM   1352 H  HB2    . LYS A 1 86  ? -10.290 -3.266  -1.028  1.00 67.98  ? 85  LYS A HB2    1 
ATOM   1353 H  HB3    . LYS A 1 86  ? -10.243 -4.659  -0.270  1.00 67.98  ? 85  LYS A HB3    1 
ATOM   1354 H  HG2    . LYS A 1 86  ? -8.149  -3.940  0.663   1.00 83.08  ? 85  LYS A HG2    1 
ATOM   1355 H  HG3    . LYS A 1 86  ? -8.498  -2.491  0.105   1.00 83.08  ? 85  LYS A HG3    1 
ATOM   1356 H  HD2    . LYS A 1 86  ? -10.420 -3.678  1.733   1.00 102.14 ? 85  LYS A HD2    1 
ATOM   1357 H  HD3    . LYS A 1 86  ? -9.116  -3.134  2.461   1.00 102.14 ? 85  LYS A HD3    1 
ATOM   1358 H  HE2    . LYS A 1 86  ? -10.727 -1.483  0.844   1.00 110.82 ? 85  LYS A HE2    1 
ATOM   1359 H  HE3    . LYS A 1 86  ? -10.904 -1.562  2.422   1.00 110.82 ? 85  LYS A HE3    1 
ATOM   1360 H  HZ1    . LYS A 1 86  ? -9.604  0.216   1.856   1.00 111.59 ? 85  LYS A HZ1    1 
ATOM   1361 H  HZ2    . LYS A 1 86  ? -8.801  -0.709  2.629   1.00 111.59 ? 85  LYS A HZ2    1 
ATOM   1362 H  HZ3    . LYS A 1 86  ? -8.640  -0.637  1.191   1.00 111.59 ? 85  LYS A HZ3    1 
ATOM   1363 N  N      . SER A 1 87  ? -10.715 -5.360  -3.252  1.00 45.00  ? 86  SER A N      1 
ATOM   1364 C  CA     . SER A 1 87  ? -11.549 -6.408  -3.837  1.00 50.22  ? 86  SER A CA     1 
ATOM   1365 C  C      . SER A 1 87  ? -10.829 -7.156  -4.963  1.00 48.06  ? 86  SER A C      1 
ATOM   1366 O  O      . SER A 1 87  ? -11.098 -8.341  -5.187  1.00 48.92  ? 86  SER A O      1 
ATOM   1367 C  CB     . SER A 1 87  ? -12.865 -5.806  -4.331  1.00 62.13  ? 86  SER A CB     1 
ATOM   1368 O  OG     . SER A 1 87  ? -12.651 -4.839  -5.345  1.00 72.89  ? 86  SER A OG     1 
ATOM   1369 H  H      . SER A 1 87  ? -10.953 -4.556  -3.446  1.00 54.01  ? 86  SER A H      1 
ATOM   1370 H  HA     . SER A 1 87  ? -11.763 -7.055  -3.146  1.00 60.28  ? 86  SER A HA     1 
ATOM   1371 H  HB2    . SER A 1 87  ? -13.420 -6.517  -4.688  1.00 74.58  ? 86  SER A HB2    1 
ATOM   1372 H  HB3    . SER A 1 87  ? -13.315 -5.382  -3.583  1.00 74.58  ? 86  SER A HB3    1 
ATOM   1373 H  HG     . SER A 1 87  ? -12.173 -4.214  -5.050  1.00 87.49  ? 86  SER A HG     1 
ATOM   1374 N  N      . LEU A 1 88  ? -9.907  -6.492  -5.673  1.00 44.79  ? 87  LEU A N      1 
ATOM   1375 C  CA     . LEU A 1 88  ? -9.140  -7.156  -6.728  1.00 46.55  ? 87  LEU A CA     1 
ATOM   1376 C  C      . LEU A 1 88  ? -8.081  -8.102  -6.164  1.00 52.02  ? 87  LEU A C      1 
ATOM   1377 O  O      . LEU A 1 88  ? -7.723  -9.092  -6.819  1.00 53.16  ? 87  LEU A O      1 
ATOM   1378 C  CB     . LEU A 1 88  ? -8.478  -6.111  -7.608  1.00 43.59  ? 87  LEU A CB     1 
ATOM   1379 C  CG     . LEU A 1 88  ? -9.420  -5.175  -8.360  1.00 51.49  ? 87  LEU A CG     1 
ATOM   1380 C  CD1    . LEU A 1 88  ? -8.623  -4.058  -9.034  1.00 52.20  ? 87  LEU A CD1    1 
ATOM   1381 C  CD2    . LEU A 1 88  ? -10.225 -5.932  -9.399  1.00 56.60  ? 87  LEU A CD2    1 
ATOM   1382 H  H      . LEU A 1 88  ? -9.710  -5.662  -5.562  1.00 53.77  ? 87  LEU A H      1 
ATOM   1383 H  HA     . LEU A 1 88  ? -9.745  -7.676  -7.280  1.00 55.88  ? 87  LEU A HA     1 
ATOM   1384 H  HB2    . LEU A 1 88  ? -7.907  -5.560  -7.050  1.00 52.33  ? 87  LEU A HB2    1 
ATOM   1385 H  HB3    . LEU A 1 88  ? -7.936  -6.569  -8.270  1.00 52.33  ? 87  LEU A HB3    1 
ATOM   1386 H  HG     . LEU A 1 88  ? -10.038 -4.771  -7.731  1.00 61.81  ? 87  LEU A HG     1 
ATOM   1387 H  HD11   . LEU A 1 88  ? -9.236  -3.474  -9.506  1.00 62.66  ? 87  LEU A HD11   1 
ATOM   1388 H  HD12   . LEU A 1 88  ? -8.145  -3.557  -8.354  1.00 62.66  ? 87  LEU A HD12   1 
ATOM   1389 H  HD13   . LEU A 1 88  ? -7.993  -4.452  -9.658  1.00 62.66  ? 87  LEU A HD13   1 
ATOM   1390 H  HD21   . LEU A 1 88  ? -10.812 -5.310  -9.857  1.00 67.94  ? 87  LEU A HD21   1 
ATOM   1391 H  HD22   . LEU A 1 88  ? -9.616  -6.341  -10.033 1.00 67.94  ? 87  LEU A HD22   1 
ATOM   1392 H  HD23   . LEU A 1 88  ? -10.750 -6.616  -8.954  1.00 67.94  ? 87  LEU A HD23   1 
ATOM   1393 N  N      . LEU A 1 89  ? -7.553  -7.802  -4.970  1.00 49.53  ? 88  LEU A N      1 
ATOM   1394 C  CA     . LEU A 1 89  ? -6.546  -8.630  -4.313  1.00 48.45  ? 88  LEU A CA     1 
ATOM   1395 C  C      . LEU A 1 89  ? -7.128  -9.693  -3.404  1.00 50.99  ? 88  LEU A C      1 
ATOM   1396 O  O      . LEU A 1 89  ? -6.452  -10.691 -3.133  1.00 57.40  ? 88  LEU A O      1 
ATOM   1397 C  CB     . LEU A 1 89  ? -5.612  -7.773  -3.443  1.00 48.98  ? 88  LEU A CB     1 
ATOM   1398 C  CG     . LEU A 1 89  ? -4.468  -6.984  -4.070  1.00 46.15  ? 88  LEU A CG     1 
ATOM   1399 C  CD1    . LEU A 1 89  ? -3.646  -6.320  -2.965  1.00 40.57  ? 88  LEU A CD1    1 
ATOM   1400 C  CD2    . LEU A 1 89  ? -3.591  -7.877  -4.920  1.00 48.80  ? 88  LEU A CD2    1 
ATOM   1401 H  H      . LEU A 1 89  ? -7.772  -7.106  -4.515  1.00 59.46  ? 88  LEU A H      1 
ATOM   1402 H  HA     . LEU A 1 89  ? -6.009  -9.072  -4.988  1.00 58.16  ? 88  LEU A HA     1 
ATOM   1403 H  HB2    . LEU A 1 89  ? -6.165  -7.127  -2.977  1.00 58.79  ? 88  LEU A HB2    1 
ATOM   1404 H  HB3    . LEU A 1 89  ? -5.208  -8.363  -2.787  1.00 58.79  ? 88  LEU A HB3    1 
ATOM   1405 H  HG     . LEU A 1 89  ? -4.833  -6.287  -4.637  1.00 55.40  ? 88  LEU A HG     1 
ATOM   1406 H  HD11   . LEU A 1 89  ? -2.920  -5.820  -3.369  1.00 48.71  ? 88  LEU A HD11   1 
ATOM   1407 H  HD12   . LEU A 1 89  ? -4.220  -5.723  -2.461  1.00 48.71  ? 88  LEU A HD12   1 
ATOM   1408 H  HD13   . LEU A 1 89  ? -3.289  -7.008  -2.381  1.00 48.71  ? 88  LEU A HD13   1 
ATOM   1409 H  HD21   . LEU A 1 89  ? -2.875  -7.345  -5.303  1.00 58.58  ? 88  LEU A HD21   1 
ATOM   1410 H  HD22   . LEU A 1 89  ? -3.220  -8.578  -4.362  1.00 58.58  ? 88  LEU A HD22   1 
ATOM   1411 H  HD23   . LEU A 1 89  ? -4.128  -8.266  -5.627  1.00 58.58  ? 88  LEU A HD23   1 
ATOM   1412 N  N      . GLY A 1 90  ? -8.335  -9.491  -2.889  1.00 49.94  ? 89  GLY A N      1 
ATOM   1413 C  CA     . GLY A 1 90  ? -8.805  -10.348 -1.823  1.00 58.23  ? 89  GLY A CA     1 
ATOM   1414 C  C      . GLY A 1 90  ? -8.072  -10.149 -0.517  1.00 58.95  ? 89  GLY A C      1 
ATOM   1415 O  O      . GLY A 1 90  ? -8.040  -11.062 0.311   1.00 59.38  ? 89  GLY A O      1 
ATOM   1416 H  H      . GLY A 1 90  ? -8.886  -8.879  -3.135  1.00 59.95  ? 89  GLY A H      1 
ATOM   1417 H  HA2    . GLY A 1 90  ? -9.748  -10.178 -1.670  1.00 69.90  ? 89  GLY A HA2    1 
ATOM   1418 H  HA3    . GLY A 1 90  ? -8.702  -11.274 -2.090  1.00 69.90  ? 89  GLY A HA3    1 
ATOM   1419 N  N      . LYS A 1 91  ? -7.466  -8.978  -0.316  1.00 55.72  ? 90  LYS A N      1 
ATOM   1420 C  CA     . LYS A 1 91  ? -6.696  -8.677  0.881   1.00 52.33  ? 90  LYS A CA     1 
ATOM   1421 C  C      . LYS A 1 91  ? -6.939  -7.227  1.266   1.00 46.47  ? 90  LYS A C      1 
ATOM   1422 O  O      . LYS A 1 91  ? -7.299  -6.395  0.430   1.00 42.69  ? 90  LYS A O      1 
ATOM   1423 C  CB     . LYS A 1 91  ? -5.199  -8.956  0.657   1.00 59.15  ? 90  LYS A CB     1 
ATOM   1424 C  CG     . LYS A 1 91  ? -4.926  -10.429 0.306   1.00 70.50  ? 90  LYS A CG     1 
ATOM   1425 C  CD     . LYS A 1 91  ? -3.465  -10.846 0.455   1.00 75.56  ? 90  LYS A CD     1 
ATOM   1426 C  CE     . LYS A 1 91  ? -3.314  -12.366 0.269   1.00 78.71  ? 90  LYS A CE     1 
ATOM   1427 N  NZ     . LYS A 1 91  ? -1.908  -12.861 0.388   1.00 78.19  1 90  LYS A NZ     1 
ATOM   1428 H  H      . LYS A 1 91  ? -7.491  -8.327  -0.877  1.00 66.89  ? 90  LYS A H      1 
ATOM   1429 H  HA     . LYS A 1 91  ? -7.004  -9.240  1.609   1.00 62.82  ? 90  LYS A HA     1 
ATOM   1430 H  HB2    . LYS A 1 91  ? -4.880  -8.407  -0.076  1.00 71.00  ? 90  LYS A HB2    1 
ATOM   1431 H  HB3    . LYS A 1 91  ? -4.711  -8.744  1.469   1.00 71.00  ? 90  LYS A HB3    1 
ATOM   1432 H  HG2    . LYS A 1 91  ? -5.455  -10.992 0.892   1.00 84.62  ? 90  LYS A HG2    1 
ATOM   1433 H  HG3    . LYS A 1 91  ? -5.184  -10.582 -0.617  1.00 84.62  ? 90  LYS A HG3    1 
ATOM   1434 H  HD2    . LYS A 1 91  ? -2.931  -10.400 -0.221  1.00 90.70  ? 90  LYS A HD2    1 
ATOM   1435 H  HD3    . LYS A 1 91  ? -3.152  -10.613 1.343   1.00 90.70  ? 90  LYS A HD3    1 
ATOM   1436 H  HE2    . LYS A 1 91  ? -3.843  -12.817 0.946   1.00 94.47  ? 90  LYS A HE2    1 
ATOM   1437 H  HE3    . LYS A 1 91  ? -3.638  -12.606 -0.613  1.00 94.47  ? 90  LYS A HE3    1 
ATOM   1438 H  HZ1    . LYS A 1 91  ? -1.885  -13.743 0.271   1.00 93.85  ? 90  LYS A HZ1    1 
ATOM   1439 H  HZ2    . LYS A 1 91  ? -1.396  -12.475 -0.230  1.00 93.85  ? 90  LYS A HZ2    1 
ATOM   1440 H  HZ3    . LYS A 1 91  ? -1.584  -12.668 1.194   1.00 93.85  ? 90  LYS A HZ3    1 
ATOM   1441 N  N      . ASP A 1 92  ? -6.752  -6.917  2.548   1.00 48.53  ? 91  ASP A N      1 
ATOM   1442 C  CA     A ASP A 1 92  ? -6.985  -5.548  2.963   0.55 48.57  ? 91  ASP A CA     1 
ATOM   1443 C  CA     B ASP A 1 92  ? -6.941  -5.558  3.045   0.45 48.62  ? 91  ASP A CA     1 
ATOM   1444 C  C      . ASP A 1 92  ? -5.787  -4.663  2.611   1.00 42.78  ? 91  ASP A C      1 
ATOM   1445 O  O      . ASP A 1 92  ? -4.652  -5.118  2.453   1.00 37.97  ? 91  ASP A O      1 
ATOM   1446 C  CB     A ASP A 1 92  ? -7.319  -5.480  4.450   0.55 51.71  ? 91  ASP A CB     1 
ATOM   1447 C  CB     B ASP A 1 92  ? -7.036  -5.546  4.569   0.45 51.60  ? 91  ASP A CB     1 
ATOM   1448 C  CG     A ASP A 1 92  ? -8.826  -5.660  4.719   0.55 55.03  ? 91  ASP A CG     1 
ATOM   1449 C  CG     B ASP A 1 92  ? -7.212  -4.140  5.131   0.45 50.17  ? 91  ASP A CG     1 
ATOM   1450 O  OD1    A ASP A 1 92  ? -9.507  -6.343  3.917   0.55 53.30  ? 91  ASP A OD1    1 
ATOM   1451 O  OD1    B ASP A 1 92  ? -7.988  -3.370  4.529   0.45 47.65  ? 91  ASP A OD1    1 
ATOM   1452 O  OD2    A ASP A 1 92  ? -9.336  -5.096  5.713   0.55 57.94  1 91  ASP A OD2    1 
ATOM   1453 O  OD2    B ASP A 1 92  ? -6.595  -3.807  6.174   0.45 48.94  1 91  ASP A OD2    1 
ATOM   1454 H  H      A ASP A 1 92  ? -6.502  -7.458  3.168   0.55 58.25  ? 91  ASP A H      1 
ATOM   1455 H  H      B ASP A 1 92  ? -6.515  -7.480  3.153   0.45 58.25  ? 91  ASP A H      1 
ATOM   1456 H  HA     A ASP A 1 92  ? -7.752  -5.206  2.477   0.55 58.30  ? 91  ASP A HA     1 
ATOM   1457 H  HA     B ASP A 1 92  ? -7.764  -5.194  2.683   0.45 58.36  ? 91  ASP A HA     1 
ATOM   1458 H  HB2    A ASP A 1 92  ? -6.843  -6.187  4.915   0.55 62.07  ? 91  ASP A HB2    1 
ATOM   1459 H  HB2    B ASP A 1 92  ? -7.801  -6.077  4.843   0.45 61.94  ? 91  ASP A HB2    1 
ATOM   1460 H  HB3    A ASP A 1 92  ? -7.052  -4.614  4.797   0.55 62.07  ? 91  ASP A HB3    1 
ATOM   1461 H  HB3    B ASP A 1 92  ? -6.222  -5.919  4.940   0.45 61.94  ? 91  ASP A HB3    1 
ATOM   1462 N  N      . VAL A 1 93  ? -6.079  -3.381  2.429   1.00 39.50  ? 92  VAL A N      1 
ATOM   1463 C  CA     . VAL A 1 93  ? -5.082  -2.398  2.029   1.00 35.55  ? 92  VAL A CA     1 
ATOM   1464 C  C      . VAL A 1 93  ? -5.146  -1.232  2.995   1.00 39.09  ? 92  VAL A C      1 
ATOM   1465 O  O      . VAL A 1 93  ? -6.213  -0.643  3.196   1.00 47.43  ? 92  VAL A O      1 
ATOM   1466 C  CB     . VAL A 1 93  ? -5.299  -1.904  0.586   1.00 34.78  ? 92  VAL A CB     1 
ATOM   1467 C  CG1    . VAL A 1 93  ? -4.266  -0.852  0.251   1.00 36.29  ? 92  VAL A CG1    1 
ATOM   1468 C  CG2    . VAL A 1 93  ? -5.217  -3.065  -0.387  1.00 37.63  ? 92  VAL A CG2    1 
ATOM   1469 H  H      . VAL A 1 93  ? -6.865  -3.049  2.534   1.00 47.42  ? 92  VAL A H      1 
ATOM   1470 H  HA     . VAL A 1 93  ? -4.198  -2.794  2.087   1.00 42.68  ? 92  VAL A HA     1 
ATOM   1471 H  HB     . VAL A 1 93  ? -6.179  -1.503  0.512   1.00 41.76  ? 92  VAL A HB     1 
ATOM   1472 H  HG11   . VAL A 1 93  ? -4.411  -0.547  -0.659  1.00 43.57  ? 92  VAL A HG11   1 
ATOM   1473 H  HG12   . VAL A 1 93  ? -4.361  -0.109  0.868   1.00 43.57  ? 92  VAL A HG12   1 
ATOM   1474 H  HG13   . VAL A 1 93  ? -3.382  -1.241  0.333   1.00 43.57  ? 92  VAL A HG13   1 
ATOM   1475 H  HG21   . VAL A 1 93  ? -5.357  -2.733  -1.287  1.00 45.18  ? 92  VAL A HG21   1 
ATOM   1476 H  HG22   . VAL A 1 93  ? -4.341  -3.475  -0.316  1.00 45.18  ? 92  VAL A HG22   1 
ATOM   1477 H  HG23   . VAL A 1 93  ? -5.904  -3.713  -0.163  1.00 45.18  ? 92  VAL A HG23   1 
ATOM   1478 N  N      . LEU A 1 94  ? -4.015  -0.901  3.590   1.00 35.37  ? 93  LEU A N      1 
ATOM   1479 C  CA     . LEU A 1 94  ? -3.919  0.258   4.460   1.00 36.40  ? 93  LEU A CA     1 
ATOM   1480 C  C      . LEU A 1 94  ? -3.644  1.488   3.611   1.00 36.45  ? 93  LEU A C      1 
ATOM   1481 O  O      . LEU A 1 94  ? -2.594  1.563   2.972   1.00 36.33  ? 93  LEU A O      1 
ATOM   1482 C  CB     . LEU A 1 94  ? -2.790  0.094   5.463   1.00 36.64  ? 93  LEU A CB     1 
ATOM   1483 C  CG     . LEU A 1 94  ? -2.596  1.329   6.352   1.00 44.59  ? 93  LEU A CG     1 
ATOM   1484 C  CD1    . LEU A 1 94  ? -3.850  1.601   7.194   1.00 49.88  ? 93  LEU A CD1    1 
ATOM   1485 C  CD2    . LEU A 1 94  ? -1.372  1.182   7.229   1.00 50.61  ? 93  LEU A CD2    1 
ATOM   1486 H  H      . LEU A 1 94  ? -3.279  -1.337  3.506   1.00 42.46  ? 93  LEU A H      1 
ATOM   1487 H  HA     . LEU A 1 94  ? -4.752  0.384   4.940   1.00 43.70  ? 93  LEU A HA     1 
ATOM   1488 H  HB2    . LEU A 1 94  ? -2.987  -0.662  6.039   1.00 43.99  ? 93  LEU A HB2    1 
ATOM   1489 H  HB3    . LEU A 1 94  ? -1.962  -0.063  4.983   1.00 43.99  ? 93  LEU A HB3    1 
ATOM   1490 H  HG     . LEU A 1 94  ? -2.454  2.100   5.781   1.00 53.53  ? 93  LEU A HG     1 
ATOM   1491 H  HD11   . LEU A 1 94  ? -3.696  2.385   7.744   1.00 59.88  ? 93  LEU A HD11   1 
ATOM   1492 H  HD12   . LEU A 1 94  ? -4.601  1.755   6.599   1.00 59.88  ? 93  LEU A HD12   1 
ATOM   1493 H  HD13   . LEU A 1 94  ? -4.025  0.831   7.757   1.00 59.88  ? 93  LEU A HD13   1 
ATOM   1494 H  HD21   . LEU A 1 94  ? -1.279  1.977   7.777   1.00 60.75  ? 93  LEU A HD21   1 
ATOM   1495 H  HD22   . LEU A 1 94  ? -1.481  0.401   7.795   1.00 60.75  ? 93  LEU A HD22   1 
ATOM   1496 H  HD23   . LEU A 1 94  ? -0.590  1.075   6.665   1.00 60.75  ? 93  LEU A HD23   1 
ATOM   1497 N  N      . PHE A 1 95  ? -4.533  2.472   3.677   1.00 32.69  ? 94  PHE A N      1 
ATOM   1498 C  CA     . PHE A 1 95  ? -4.346  3.737   2.983   1.00 30.41  ? 94  PHE A CA     1 
ATOM   1499 C  C      . PHE A 1 95  ? -3.825  4.803   3.940   1.00 33.03  ? 94  PHE A C      1 
ATOM   1500 O  O      . PHE A 1 95  ? -4.428  5.054   4.993   1.00 36.17  ? 94  PHE A O      1 
ATOM   1501 C  CB     . PHE A 1 95  ? -5.655  4.212   2.371   1.00 30.33  ? 94  PHE A CB     1 
ATOM   1502 C  CG     . PHE A 1 95  ? -5.517  5.477   1.605   1.00 33.02  ? 94  PHE A CG     1 
ATOM   1503 C  CD1    . PHE A 1 95  ? -4.764  5.506   0.439   1.00 33.05  ? 94  PHE A CD1    1 
ATOM   1504 C  CD2    . PHE A 1 95  ? -6.110  6.640   2.052   1.00 37.28  ? 94  PHE A CD2    1 
ATOM   1505 C  CE1    . PHE A 1 95  ? -4.624  6.673   -0.283  1.00 33.60  ? 94  PHE A CE1    1 
ATOM   1506 C  CE2    . PHE A 1 95  ? -5.973  7.812   1.338   1.00 41.38  ? 94  PHE A CE2    1 
ATOM   1507 C  CZ     . PHE A 1 95  ? -5.225  7.828   0.165   1.00 37.98  ? 94  PHE A CZ     1 
ATOM   1508 H  H      . PHE A 1 95  ? -5.265  2.429   4.126   1.00 39.25  ? 94  PHE A H      1 
ATOM   1509 H  HA     . PHE A 1 95  ? -3.698  3.621   2.271   1.00 36.51  ? 94  PHE A HA     1 
ATOM   1510 H  HB2    . PHE A 1 95  ? -5.985  3.530   1.765   1.00 36.42  ? 94  PHE A HB2    1 
ATOM   1511 H  HB3    . PHE A 1 95  ? -6.298  4.362   3.082   1.00 36.42  ? 94  PHE A HB3    1 
ATOM   1512 H  HD1    . PHE A 1 95  ? -4.360  4.725   0.134   1.00 39.68  ? 94  PHE A HD1    1 
ATOM   1513 H  HD2    . PHE A 1 95  ? -6.613  6.631   2.834   1.00 44.75  ? 94  PHE A HD2    1 
ATOM   1514 H  HE1    . PHE A 1 95  ? -4.122  6.681   -1.066  1.00 40.34  ? 94  PHE A HE1    1 
ATOM   1515 H  HE2    . PHE A 1 95  ? -6.380  8.591   1.642   1.00 49.67  ? 94  PHE A HE2    1 
ATOM   1516 H  HZ     . PHE A 1 95  ? -5.131  8.618   -0.316  1.00 45.60  ? 94  PHE A HZ     1 
ATOM   1517 N  N      . LEU A 1 96  ? -2.719  5.443   3.564   1.00 30.29  ? 95  LEU A N      1 
ATOM   1518 C  CA     . LEU A 1 96  ? -2.137  6.527   4.344   1.00 32.61  ? 95  LEU A CA     1 
ATOM   1519 C  C      . LEU A 1 96  ? -2.415  7.852   3.652   1.00 32.82  ? 95  LEU A C      1 
ATOM   1520 O  O      . LEU A 1 96  ? -2.389  7.935   2.423   1.00 35.13  ? 95  LEU A O      1 
ATOM   1521 C  CB     . LEU A 1 96  ? -0.634  6.358   4.506   1.00 34.75  ? 95  LEU A CB     1 
ATOM   1522 C  CG     . LEU A 1 96  ? -0.157  5.063   5.130   1.00 38.07  ? 95  LEU A CG     1 
ATOM   1523 C  CD1    . LEU A 1 96  ? 1.362   5.060   5.107   1.00 36.83  ? 95  LEU A CD1    1 
ATOM   1524 C  CD2    . LEU A 1 96  ? -0.706  4.967   6.532   1.00 47.92  ? 95  LEU A CD2    1 
ATOM   1525 H  H      . LEU A 1 96  ? -2.281  5.261   2.847   1.00 36.37  ? 95  LEU A H      1 
ATOM   1526 H  HA     . LEU A 1 96  ? -2.543  6.547   5.225   1.00 39.15  ? 95  LEU A HA     1 
ATOM   1527 H  HB2    . LEU A 1 96  ? -0.226  6.421   3.628   1.00 41.72  ? 95  LEU A HB2    1 
ATOM   1528 H  HB3    . LEU A 1 96  ? -0.307  7.082   5.063   1.00 41.72  ? 95  LEU A HB3    1 
ATOM   1529 H  HG     . LEU A 1 96  ? -0.481  4.309   4.613   1.00 45.71  ? 95  LEU A HG     1 
ATOM   1530 H  HD11   . LEU A 1 96  ? 1.682   4.235   5.504   1.00 44.21  ? 95  LEU A HD11   1 
ATOM   1531 H  HD12   . LEU A 1 96  ? 1.664   5.124   4.187   1.00 44.21  ? 95  LEU A HD12   1 
ATOM   1532 H  HD13   . LEU A 1 96  ? 1.687   5.820   5.615   1.00 44.21  ? 95  LEU A HD13   1 
ATOM   1533 H  HD21   . LEU A 1 96  ? -0.402  4.139   6.933   1.00 57.53  ? 95  LEU A HD21   1 
ATOM   1534 H  HD22   . LEU A 1 96  ? -0.385  5.723   7.048   1.00 57.53  ? 95  LEU A HD22   1 
ATOM   1535 H  HD23   . LEU A 1 96  ? -1.675  4.981   6.493   1.00 57.53  ? 95  LEU A HD23   1 
ATOM   1536 N  N      . LYS A 1 97  ? -2.639  8.896   4.448   1.00 36.18  ? 96  LYS A N      1 
ATOM   1537 C  CA     . LYS A 1 97  ? -3.066  10.178  3.906   1.00 39.79  ? 96  LYS A CA     1 
ATOM   1538 C  C      . LYS A 1 97  ? -1.905  11.067  3.486   1.00 38.76  ? 96  LYS A C      1 
ATOM   1539 O  O      . LYS A 1 97  ? -2.119  12.240  3.177   1.00 42.75  ? 96  LYS A O      1 
ATOM   1540 C  CB     . LYS A 1 97  ? -3.940  10.900  4.933   1.00 48.26  ? 96  LYS A CB     1 
ATOM   1541 C  CG     . LYS A 1 97  ? -5.152  10.101  5.386   1.00 62.09  ? 96  LYS A CG     1 
ATOM   1542 C  CD     . LYS A 1 97  ? -6.126  9.840   4.252   1.00 70.05  ? 96  LYS A CD     1 
ATOM   1543 C  CE     . LYS A 1 97  ? -7.470  9.312   4.762   1.00 74.98  ? 96  LYS A CE     1 
ATOM   1544 N  NZ     . LYS A 1 97  ? -8.286  10.382  5.397   1.00 75.21  1 96  LYS A NZ     1 
ATOM   1545 H  H      . LYS A 1 97  ? -2.550  8.886   5.304   1.00 43.44  ? 96  LYS A H      1 
ATOM   1546 H  HA     . LYS A 1 97  ? -3.611  10.016  3.120   1.00 47.77  ? 96  LYS A HA     1 
ATOM   1547 H  HB2    . LYS A 1 97  ? -3.404  11.094  5.718   1.00 57.93  ? 96  LYS A HB2    1 
ATOM   1548 H  HB3    . LYS A 1 97  ? -4.261  11.728  4.543   1.00 57.93  ? 96  LYS A HB3    1 
ATOM   1549 H  HG2    . LYS A 1 97  ? -4.856  9.245   5.732   1.00 74.52  ? 96  LYS A HG2    1 
ATOM   1550 H  HG3    . LYS A 1 97  ? -5.619  10.596  6.076   1.00 74.52  ? 96  LYS A HG3    1 
ATOM   1551 H  HD2    . LYS A 1 97  ? -6.288  10.668  3.774   1.00 84.08  ? 96  LYS A HD2    1 
ATOM   1552 H  HD3    . LYS A 1 97  ? -5.748  9.176   3.654   1.00 84.08  ? 96  LYS A HD3    1 
ATOM   1553 H  HE2    . LYS A 1 97  ? -7.974  8.951   4.016   1.00 89.99  ? 96  LYS A HE2    1 
ATOM   1554 H  HE3    . LYS A 1 97  ? -7.311  8.621   5.424   1.00 89.99  ? 96  LYS A HE3    1 
ATOM   1555 H  HZ1    . LYS A 1 97  ? -9.059  10.046  5.683   1.00 90.27  ? 96  LYS A HZ1    1 
ATOM   1556 H  HZ2    . LYS A 1 97  ? -7.847  10.728  6.090   1.00 90.27  ? 96  LYS A HZ2    1 
ATOM   1557 H  HZ3    . LYS A 1 97  ? -8.452  11.028  4.808   1.00 90.27  ? 96  LYS A HZ3    1 
ATOM   1558 N  N      . ASP A 1 98  ? -0.691  10.530  3.445   1.00 35.66  ? 97  ASP A N      1 
ATOM   1559 C  CA     . ASP A 1 98  ? 0.455   11.219  2.878   1.00 32.23  ? 97  ASP A CA     1 
ATOM   1560 C  C      . ASP A 1 98  ? 1.341   10.164  2.237   1.00 30.40  ? 97  ASP A C      1 
ATOM   1561 O  O      . ASP A 1 98  ? 1.042   8.967   2.292   1.00 33.59  ? 97  ASP A O      1 
ATOM   1562 C  CB     . ASP A 1 98  ? 1.197   12.013  3.959   1.00 38.70  ? 97  ASP A CB     1 
ATOM   1563 C  CG     . ASP A 1 98  ? 1.933   13.228  3.401   1.00 46.15  ? 97  ASP A CG     1 
ATOM   1564 O  OD1    . ASP A 1 98  ? 2.336   13.217  2.212   1.00 44.90  ? 97  ASP A OD1    1 
ATOM   1565 O  OD2    . ASP A 1 98  ? 2.116   14.201  4.168   1.00 50.22  1 97  ASP A OD2    1 
ATOM   1566 H  H      . ASP A 1 98  ? -0.504  9.747   3.748   1.00 42.81  ? 97  ASP A H      1 
ATOM   1567 H  HA     . ASP A 1 98  ? 0.158   11.835  2.190   1.00 38.70  ? 97  ASP A HA     1 
ATOM   1568 H  HB2    . ASP A 1 98  ? 0.556   12.327  4.615   1.00 46.46  ? 97  ASP A HB2    1 
ATOM   1569 H  HB3    . ASP A 1 98  ? 1.850   11.435  4.383   1.00 46.46  ? 97  ASP A HB3    1 
ATOM   1570 N  N      . CYS A 1 99  ? 2.422   10.607  1.585   1.00 30.75  ? 98  CYS A N      1 
ATOM   1571 C  CA     . CYS A 1 99  ? 3.366   9.675   0.976   1.00 31.43  ? 98  CYS A CA     1 
ATOM   1572 C  C      . CYS A 1 99  ? 4.780   9.818   1.509   1.00 32.00  ? 98  CYS A C      1 
ATOM   1573 O  O      . CYS A 1 99  ? 5.623   8.976   1.188   1.00 33.37  ? 98  CYS A O      1 
ATOM   1574 C  CB     . CYS A 1 99  ? 3.397   9.834   -0.551  1.00 31.57  ? 98  CYS A CB     1 
ATOM   1575 S  SG     . CYS A 1 99  ? 3.846   11.483  -1.097  1.00 31.02  ? 98  CYS A SG     1 
ATOM   1576 H  H      . CYS A 1 99  ? 2.626   11.436  1.484   1.00 36.91  ? 98  CYS A H      1 
ATOM   1577 H  HA     . CYS A 1 99  ? 3.072   8.771   1.169   1.00 37.74  ? 98  CYS A HA     1 
ATOM   1578 H  HB2    . CYS A 1 99  ? 4.047   9.214   -0.917  1.00 37.91  ? 98  CYS A HB2    1 
ATOM   1579 H  HB3    . CYS A 1 99  ? 2.516   9.634   -0.904  1.00 37.91  ? 98  CYS A HB3    1 
ATOM   1580 H  HG     . CYS A 1 99  ? 3.047   12.268  -0.668  1.00 37.24  ? 98  CYS A HG     1 
ATOM   1581 N  N      . VAL A 1 100 ? 5.065   10.851  2.300   1.00 31.06  ? 99  VAL A N      1 
ATOM   1582 C  CA     . VAL A 1 100 ? 6.386   11.078  2.861   1.00 34.65  ? 99  VAL A CA     1 
ATOM   1583 C  C      . VAL A 1 100 ? 6.235   11.645  4.269   1.00 36.40  ? 99  VAL A C      1 
ATOM   1584 O  O      . VAL A 1 100 ? 5.139   11.963  4.733   1.00 35.55  ? 99  VAL A O      1 
ATOM   1585 C  CB     . VAL A 1 100 ? 7.244   12.033  2.001   1.00 38.47  ? 99  VAL A CB     1 
ATOM   1586 C  CG1    . VAL A 1 100 ? 7.688   11.354  0.707   1.00 37.12  ? 99  VAL A CG1    1 
ATOM   1587 C  CG2    . VAL A 1 100 ? 6.498   13.321  1.726   1.00 40.63  ? 99  VAL A CG2    1 
ATOM   1588 H  H      . VAL A 1 100 ? 4.490   11.447  2.530   1.00 37.29  ? 99  VAL A H      1 
ATOM   1589 H  HA     . VAL A 1 100 ? 6.854   10.231  2.925   1.00 41.60  ? 99  VAL A HA     1 
ATOM   1590 H  HB     . VAL A 1 100 ? 8.044   12.261  2.500   1.00 46.18  ? 99  VAL A HB     1 
ATOM   1591 H  HG11   . VAL A 1 100 ? 8.223   11.978  0.191   1.00 44.56  ? 99  VAL A HG11   1 
ATOM   1592 H  HG12   . VAL A 1 100 ? 8.214   10.570  0.927   1.00 44.56  ? 99  VAL A HG12   1 
ATOM   1593 H  HG13   . VAL A 1 100 ? 6.902   11.095  0.201   1.00 44.56  ? 99  VAL A HG13   1 
ATOM   1594 H  HG21   . VAL A 1 100 ? 7.058   13.901  1.186   1.00 48.77  ? 99  VAL A HG21   1 
ATOM   1595 H  HG22   . VAL A 1 100 ? 5.678   13.115  1.250   1.00 48.77  ? 99  VAL A HG22   1 
ATOM   1596 H  HG23   . VAL A 1 100 ? 6.291   13.752  2.570   1.00 48.77  ? 99  VAL A HG23   1 
ATOM   1597 N  N      . GLY A 1 101 ? 7.365   11.794  4.941   1.00 40.56  ? 100 GLY A N      1 
ATOM   1598 C  CA     . GLY A 1 101 ? 7.385   12.386  6.258   1.00 43.49  ? 100 GLY A CA     1 
ATOM   1599 C  C      . GLY A 1 101 ? 7.438   11.341  7.348   1.00 43.69  ? 100 GLY A C      1 
ATOM   1600 O  O      . GLY A 1 101 ? 7.320   10.137  7.095   1.00 41.64  ? 100 GLY A O      1 
ATOM   1601 H  H      . GLY A 1 101 ? 8.138   11.556  4.651   1.00 48.69  ? 100 GLY A H      1 
ATOM   1602 H  HA2    . GLY A 1 101 ? 8.161   12.962  6.343   1.00 52.21  ? 100 GLY A HA2    1 
ATOM   1603 H  HA3    . GLY A 1 101 ? 6.587   12.923  6.384   1.00 52.21  ? 100 GLY A HA3    1 
ATOM   1604 N  N      . PRO A 1 102 ? 7.610   11.790  8.596   1.00 46.35  ? 101 PRO A N      1 
ATOM   1605 C  CA     . PRO A 1 102 ? 7.875   10.841  9.690   1.00 47.96  ? 101 PRO A CA     1 
ATOM   1606 C  C      . PRO A 1 102 ? 6.730   9.883   9.992   1.00 46.12  ? 101 PRO A C      1 
ATOM   1607 O  O      . PRO A 1 102 ? 6.997   8.741   10.382  1.00 45.95  ? 101 PRO A O      1 
ATOM   1608 C  CB     . PRO A 1 102 ? 8.170   11.761  10.885  1.00 57.05  ? 101 PRO A CB     1 
ATOM   1609 C  CG     . PRO A 1 102 ? 7.546   13.053  10.536  1.00 60.27  ? 101 PRO A CG     1 
ATOM   1610 C  CD     . PRO A 1 102 ? 7.660   13.186  9.050   1.00 50.47  ? 101 PRO A CD     1 
ATOM   1611 H  HA     . PRO A 1 102 ? 8.671   10.323  9.491   1.00 57.57  ? 101 PRO A HA     1 
ATOM   1612 H  HB2    . PRO A 1 102 ? 7.770   11.392  11.688  1.00 68.48  ? 101 PRO A HB2    1 
ATOM   1613 H  HB3    . PRO A 1 102 ? 9.129   11.860  10.992  1.00 68.48  ? 101 PRO A HB3    1 
ATOM   1614 H  HG2    . PRO A 1 102 ? 6.615   13.047  10.807  1.00 72.35  ? 101 PRO A HG2    1 
ATOM   1615 H  HG3    . PRO A 1 102 ? 8.024   13.773  10.979  1.00 72.35  ? 101 PRO A HG3    1 
ATOM   1616 H  HD2    . PRO A 1 102 ? 6.908   13.686  8.694   1.00 60.59  ? 101 PRO A HD2    1 
ATOM   1617 H  HD3    . PRO A 1 102 ? 8.507   13.592  8.808   1.00 60.59  ? 101 PRO A HD3    1 
ATOM   1618 N  N      . GLU A 1 103 ? 5.466   10.290  9.834   1.00 44.83  ? 102 GLU A N      1 
ATOM   1619 C  CA     . GLU A 1 103 ? 4.370   9.373   10.158  1.00 47.60  ? 102 GLU A CA     1 
ATOM   1620 C  C      . GLU A 1 103 ? 4.273   8.260   9.127   1.00 38.39  ? 102 GLU A C      1 
ATOM   1621 O  O      . GLU A 1 103 ? 4.060   7.090   9.473   1.00 38.21  ? 102 GLU A O      1 
ATOM   1622 C  CB     . GLU A 1 103 ? 3.039   10.119  10.241  1.00 64.50  ? 102 GLU A CB     1 
ATOM   1623 C  CG     . GLU A 1 103 ? 2.963   11.150  11.355  1.00 86.95  ? 102 GLU A CG     1 
ATOM   1624 C  CD     . GLU A 1 103 ? 3.625   12.468  10.987  1.00 101.67 ? 102 GLU A CD     1 
ATOM   1625 O  OE1    . GLU A 1 103 ? 4.147   12.584  9.853   1.00 102.05 ? 102 GLU A OE1    1 
ATOM   1626 O  OE2    . GLU A 1 103 ? 3.617   13.389  11.834  1.00 110.32 1 102 GLU A OE2    1 
ATOM   1627 H  H      . GLU A 1 103 ? 5.223   11.065  9.551   1.00 53.82  ? 102 GLU A H      1 
ATOM   1628 H  HA     . GLU A 1 103 ? 4.541   8.968   11.023  1.00 57.14  ? 102 GLU A HA     1 
ATOM   1629 H  HB2    . GLU A 1 103 ? 2.890   10.581  9.401   1.00 77.42  ? 102 GLU A HB2    1 
ATOM   1630 H  HB3    . GLU A 1 103 ? 2.331   9.473   10.388  1.00 77.42  ? 102 GLU A HB3    1 
ATOM   1631 H  HG2    . GLU A 1 103 ? 2.031   11.329  11.556  1.00 104.36 ? 102 GLU A HG2    1 
ATOM   1632 H  HG3    . GLU A 1 103 ? 3.410   10.799  12.141  1.00 104.36 ? 102 GLU A HG3    1 
ATOM   1633 N  N      . VAL A 1 104 ? 4.406   8.608   7.851   1.00 33.76  ? 103 VAL A N      1 
ATOM   1634 C  CA     . VAL A 1 104 ? 4.461   7.578   6.824   1.00 31.52  ? 103 VAL A CA     1 
ATOM   1635 C  C      . VAL A 1 104 ? 5.645   6.647   7.073   1.00 33.24  ? 103 VAL A C      1 
ATOM   1636 O  O      . VAL A 1 104 ? 5.524   5.422   6.966   1.00 31.21  ? 103 VAL A O      1 
ATOM   1637 C  CB     . VAL A 1 104 ? 4.529   8.223   5.425   1.00 31.20  ? 103 VAL A CB     1 
ATOM   1638 C  CG1    . VAL A 1 104 ? 4.861   7.192   4.381   1.00 29.15  ? 103 VAL A CG1    1 
ATOM   1639 C  CG2    . VAL A 1 104 ? 3.205   8.912   5.089   1.00 32.78  ? 103 VAL A CG2    1 
ATOM   1640 H  H      . VAL A 1 104 ? 4.465   9.415   7.559   1.00 40.42  ? 103 VAL A H      1 
ATOM   1641 H  HA     . VAL A 1 104 ? 3.651   7.048   6.867   1.00 37.73  ? 103 VAL A HA     1 
ATOM   1642 H  HB     . VAL A 1 104 ? 5.229   8.895   5.418   1.00 37.46  ? 103 VAL A HB     1 
ATOM   1643 H  HG11   . VAL A 1 104 ? 4.897   7.623   3.513   1.00 35.00  ? 103 VAL A HG11   1 
ATOM   1644 H  HG12   . VAL A 1 104 ? 5.721   6.796   4.591   1.00 35.00  ? 103 VAL A HG12   1 
ATOM   1645 H  HG13   . VAL A 1 104 ? 4.172   6.509   4.383   1.00 35.00  ? 103 VAL A HG13   1 
ATOM   1646 H  HG21   . VAL A 1 104 ? 3.272   9.309   4.207   1.00 39.36  ? 103 VAL A HG21   1 
ATOM   1647 H  HG22   . VAL A 1 104 ? 2.495   8.252   5.103   1.00 39.36  ? 103 VAL A HG22   1 
ATOM   1648 H  HG23   . VAL A 1 104 ? 3.031   9.600   5.750   1.00 39.36  ? 103 VAL A HG23   1 
ATOM   1649 N  N      . GLU A 1 105 ? 6.806   7.206   7.407   1.00 37.80  ? 104 GLU A N      1 
ATOM   1650 C  CA     . GLU A 1 105 ? 7.987   6.368   7.600   1.00 41.06  ? 104 GLU A CA     1 
ATOM   1651 C  C      . GLU A 1 105 ? 7.770   5.376   8.738   1.00 39.85  ? 104 GLU A C      1 
ATOM   1652 O  O      . GLU A 1 105 ? 8.176   4.211   8.651   1.00 39.67  ? 104 GLU A O      1 
ATOM   1653 C  CB     . GLU A 1 105 ? 9.214   7.254   7.854   1.00 48.07  ? 104 GLU A CB     1 
ATOM   1654 C  CG     . GLU A 1 105 ? 9.634   8.070   6.597   1.00 51.29  ? 104 GLU A CG     1 
ATOM   1655 C  CD     . GLU A 1 105 ? 10.729  9.094   6.883   1.00 50.58  ? 104 GLU A CD     1 
ATOM   1656 O  OE1    . GLU A 1 105 ? 11.280  9.086   8.008   1.00 48.26  ? 104 GLU A OE1    1 
ATOM   1657 O  OE2    . GLU A 1 105 ? 11.034  9.905   5.978   1.00 46.12  1 104 GLU A OE2    1 
ATOM   1658 H  H      . GLU A 1 105 ? 6.935   8.048   7.525   1.00 45.38  ? 104 GLU A H      1 
ATOM   1659 H  HA     . GLU A 1 105 ? 8.148   5.861   6.789   1.00 49.29  ? 104 GLU A HA     1 
ATOM   1660 H  HB2    . GLU A 1 105 ? 9.009   7.881   8.565   1.00 57.70  ? 104 GLU A HB2    1 
ATOM   1661 H  HB3    . GLU A 1 105 ? 9.961   6.692   8.111   1.00 57.70  ? 104 GLU A HB3    1 
ATOM   1662 H  HG2    . GLU A 1 105 ? 9.966   7.459   5.921   1.00 61.56  ? 104 GLU A HG2    1 
ATOM   1663 H  HG3    . GLU A 1 105 ? 8.860   8.548   6.259   1.00 61.56  ? 104 GLU A HG3    1 
ATOM   1664 N  N      . LYS A 1 106 ? 7.103   5.812   9.803   1.00 38.36  ? 105 LYS A N      1 
ATOM   1665 C  CA     . LYS A 1 106 ? 6.840   4.921   10.929  1.00 38.69  ? 105 LYS A CA     1 
ATOM   1666 C  C      . LYS A 1 106 ? 5.898   3.786   10.524  1.00 36.73  ? 105 LYS A C      1 
ATOM   1667 O  O      . LYS A 1 106 ? 6.120   2.624   10.894  1.00 38.98  ? 105 LYS A O      1 
ATOM   1668 C  CB     . LYS A 1 106 ? 6.261   5.735   12.083  1.00 42.21  ? 105 LYS A CB     1 
ATOM   1669 C  CG     . LYS A 1 106 ? 5.970   4.935   13.329  1.00 47.70  ? 105 LYS A CG     1 
ATOM   1670 C  CD     . LYS A 1 106 ? 5.316   5.818   14.395  1.00 57.29  ? 105 LYS A CD     1 
ATOM   1671 C  CE     . LYS A 1 106 ? 5.104   5.076   15.689  1.00 70.81  ? 105 LYS A CE     1 
ATOM   1672 N  NZ     . LYS A 1 106 ? 6.378   4.524   16.193  1.00 83.08  1 105 LYS A NZ     1 
ATOM   1673 H  H      . LYS A 1 106 ? 6.796   6.610   9.898   1.00 46.06  ? 105 LYS A H      1 
ATOM   1674 H  HA     . LYS A 1 106 ? 7.675   4.528   11.226  1.00 46.45  ? 105 LYS A HA     1 
ATOM   1675 H  HB2    . LYS A 1 106 ? 6.894   6.430   12.321  1.00 50.67  ? 105 LYS A HB2    1 
ATOM   1676 H  HB3    . LYS A 1 106 ? 5.428   6.138   11.791  1.00 50.67  ? 105 LYS A HB3    1 
ATOM   1677 H  HG2    . LYS A 1 106 ? 5.361   4.211   13.114  1.00 57.26  ? 105 LYS A HG2    1 
ATOM   1678 H  HG3    . LYS A 1 106 ? 6.800   4.584   13.689  1.00 57.26  ? 105 LYS A HG3    1 
ATOM   1679 H  HD2    . LYS A 1 106 ? 5.889   6.580   14.574  1.00 68.77  ? 105 LYS A HD2    1 
ATOM   1680 H  HD3    . LYS A 1 106 ? 4.451   6.118   14.074  1.00 68.77  ? 105 LYS A HD3    1 
ATOM   1681 H  HE2    . LYS A 1 106 ? 4.749   5.685   16.356  1.00 84.99  ? 105 LYS A HE2    1 
ATOM   1682 H  HE3    . LYS A 1 106 ? 4.489   4.340   15.542  1.00 84.99  ? 105 LYS A HE3    1 
ATOM   1683 H  HZ1    . LYS A 1 106 ? 6.240   4.088   16.957  1.00 99.72  ? 105 LYS A HZ1    1 
ATOM   1684 H  HZ2    . LYS A 1 106 ? 6.722   3.960   15.597  1.00 99.72  ? 105 LYS A HZ2    1 
ATOM   1685 H  HZ3    . LYS A 1 106 ? 6.959   5.183   16.337  1.00 99.72  ? 105 LYS A HZ3    1 
ATOM   1686 N  N      . ALA A 1 107 ? 4.840   4.108   9.769   1.00 34.98  ? 106 ALA A N      1 
ATOM   1687 C  CA     . ALA A 1 107 ? 3.875   3.101   9.336   1.00 38.00  ? 106 ALA A CA     1 
ATOM   1688 C  C      . ALA A 1 107 ? 4.508   2.061   8.420   1.00 38.50  ? 106 ALA A C      1 
ATOM   1689 O  O      . ALA A 1 107 ? 4.082   0.897   8.410   1.00 37.75  ? 106 ALA A O      1 
ATOM   1690 C  CB     . ALA A 1 107 ? 2.709   3.765   8.597   1.00 39.85  ? 106 ALA A CB     1 
ATOM   1691 H  H      . ALA A 1 107 ? 4.662   4.904   9.497   1.00 41.88  ? 106 ALA A H      1 
ATOM   1692 H  HA     . ALA A 1 107 ? 3.520   2.644   10.114  1.00 45.61  ? 106 ALA A HA     1 
ATOM   1693 H  HB1    . ALA A 1 107 ? 2.081   3.080   8.318   1.00 47.84  ? 106 ALA A HB1    1 
ATOM   1694 H  HB2    . ALA A 1 107 ? 2.272   4.391   9.196   1.00 47.84  ? 106 ALA A HB2    1 
ATOM   1695 H  HB3    . ALA A 1 107 ? 3.053   4.234   7.821   1.00 47.84  ? 106 ALA A HB3    1 
ATOM   1696 N  N      . CYS A 1 108 ? 5.506   2.461   7.637   1.00 34.89  ? 107 CYS A N      1 
ATOM   1697 C  CA     . CYS A 1 108 ? 6.156   1.548   6.708   1.00 32.39  ? 107 CYS A CA     1 
ATOM   1698 C  C      . CYS A 1 108 ? 7.424   0.894   7.253   1.00 34.10  ? 107 CYS A C      1 
ATOM   1699 O  O      . CYS A 1 108 ? 7.980   0.017   6.575   1.00 32.97  ? 107 CYS A O      1 
ATOM   1700 C  CB     . CYS A 1 108 ? 6.500   2.308   5.436   1.00 31.59  ? 107 CYS A CB     1 
ATOM   1701 S  SG     . CYS A 1 108 ? 5.019   2.928   4.600   1.00 31.16  ? 107 CYS A SG     1 
ATOM   1702 H  H      . CYS A 1 108 ? 5.826   3.259   7.625   1.00 41.89  ? 107 CYS A H      1 
ATOM   1703 H  HA     . CYS A 1 108 ? 5.533   0.841   6.476   1.00 38.89  ? 107 CYS A HA     1 
ATOM   1704 H  HB2    . CYS A 1 108 ? 7.062   3.066   5.660   1.00 37.93  ? 107 CYS A HB2    1 
ATOM   1705 H  HB3    . CYS A 1 108 ? 6.966   1.715   4.826   1.00 37.93  ? 107 CYS A HB3    1 
ATOM   1706 H  HG     . CYS A 1 108 ? 5.348   3.516   3.607   1.00 37.42  ? 107 CYS A HG     1 
ATOM   1707 N  N      . ALA A 1 109 ? 7.882   1.284   8.446   1.00 36.76  ? 108 ALA A N      1 
ATOM   1708 C  CA     . ALA A 1 109 ? 9.225   0.917   8.903   1.00 37.51  ? 108 ALA A CA     1 
ATOM   1709 C  C      . ALA A 1 109 ? 9.361   -0.581  9.141   1.00 37.45  ? 108 ALA A C      1 
ATOM   1710 O  O      . ALA A 1 109 ? 10.389  -1.179  8.797   1.00 37.09  ? 108 ALA A O      1 
ATOM   1711 C  CB     . ALA A 1 109 ? 9.585   1.681   10.181  1.00 41.14  ? 108 ALA A CB     1 
ATOM   1712 H  H      . ALA A 1 109 ? 7.436   1.760   9.007   1.00 44.13  ? 108 ALA A H      1 
ATOM   1713 H  HA     . ALA A 1 109 ? 9.866   1.167   8.219   1.00 45.03  ? 108 ALA A HA     1 
ATOM   1714 H  HB1    . ALA A 1 109 ? 10.476  1.422   10.464  1.00 49.39  ? 108 ALA A HB1    1 
ATOM   1715 H  HB2    . ALA A 1 109 ? 9.559   2.633   9.997   1.00 49.39  ? 108 ALA A HB2    1 
ATOM   1716 H  HB3    . ALA A 1 109 ? 8.941   1.460   10.873  1.00 49.39  ? 108 ALA A HB3    1 
ATOM   1717 N  N      . ASN A 1 110 ? 8.356   -1.198  9.737   1.00 37.88  ? 109 ASN A N      1 
ATOM   1718 C  CA     . ASN A 1 110 ? 8.435   -2.606  10.098  1.00 40.51  ? 109 ASN A CA     1 
ATOM   1719 C  C      . ASN A 1 110 ? 7.018   -3.164  10.175  1.00 40.13  ? 109 ASN A C      1 
ATOM   1720 O  O      . ASN A 1 110 ? 6.533   -3.457  11.276  1.00 42.46  ? 109 ASN A O      1 
ATOM   1721 C  CB     . ASN A 1 110 ? 9.167   -2.786  11.440  1.00 45.55  ? 109 ASN A CB     1 
ATOM   1722 C  CG     . ASN A 1 110 ? 9.630   -4.206  11.652  1.00 50.34  ? 109 ASN A CG     1 
ATOM   1723 O  OD1    . ASN A 1 110 ? 9.876   -4.932  10.692  1.00 57.00  ? 109 ASN A OD1    1 
ATOM   1724 N  ND2    . ASN A 1 110 ? 9.749   -4.615  12.898  1.00 52.64  ? 109 ASN A ND2    1 
ATOM   1725 H  H      . ASN A 1 110 ? 7.611   -0.823  9.946   1.00 45.48  ? 109 ASN A H      1 
ATOM   1726 H  HA     . ASN A 1 110 ? 8.921   -3.090  9.413   1.00 48.63  ? 109 ASN A HA     1 
ATOM   1727 H  HB2    . ASN A 1 110 ? 9.946   -2.209  11.456  1.00 54.68  ? 109 ASN A HB2    1 
ATOM   1728 H  HB3    . ASN A 1 110 ? 8.565   -2.554  12.164  1.00 54.68  ? 109 ASN A HB3    1 
ATOM   1729 H  HD21   . ASN A 1 110 ? 10.010  -5.417  13.064  1.00 63.18  ? 109 ASN A HD21   1 
ATOM   1730 H  HD22   . ASN A 1 110 ? 9.565   -4.079  13.545  1.00 63.18  ? 109 ASN A HD22   1 
ATOM   1731 N  N      . PRO A 1 111 ? 6.336   -3.318  9.042   1.00 34.73  ? 110 PRO A N      1 
ATOM   1732 C  CA     . PRO A 1 111 ? 4.925   -3.725  9.051   1.00 34.89  ? 110 PRO A CA     1 
ATOM   1733 C  C      . PRO A 1 111 ? 4.748   -5.206  9.350   1.00 38.40  ? 110 PRO A C      1 
ATOM   1734 O  O      . PRO A 1 111 ? 5.677   -6.007  9.256   1.00 39.32  ? 110 PRO A O      1 
ATOM   1735 C  CB     . PRO A 1 111 ? 4.458   -3.427  7.617   1.00 34.79  ? 110 PRO A CB     1 
ATOM   1736 C  CG     . PRO A 1 111 ? 5.489   -2.522  7.043   1.00 35.03  ? 110 PRO A CG     1 
ATOM   1737 C  CD     . PRO A 1 111 ? 6.766   -2.896  7.693   1.00 32.06  ? 110 PRO A CD     1 
ATOM   1738 H  HA     . PRO A 1 111 ? 4.414   -3.195  9.683   1.00 41.89  ? 110 PRO A HA     1 
ATOM   1739 H  HB2    . PRO A 1 111 ? 4.409   -4.253  7.112   1.00 41.77  ? 110 PRO A HB2    1 
ATOM   1740 H  HB3    . PRO A 1 111 ? 3.593   -2.988  7.641   1.00 41.77  ? 110 PRO A HB3    1 
ATOM   1741 H  HG2    . PRO A 1 111 ? 5.542   -2.658  6.084   1.00 42.05  ? 110 PRO A HG2    1 
ATOM   1742 H  HG3    . PRO A 1 111 ? 5.261   -1.601  7.244   1.00 42.05  ? 110 PRO A HG3    1 
ATOM   1743 H  HD2    . PRO A 1 111 ? 7.183   -3.635  7.223   1.00 38.49  ? 110 PRO A HD2    1 
ATOM   1744 H  HD3    . PRO A 1 111 ? 7.357   -2.128  7.749   1.00 38.49  ? 110 PRO A HD3    1 
ATOM   1745 N  N      . ALA A 1 112 ? 3.509   -5.567  9.676   1.00 40.47  ? 111 ALA A N      1 
ATOM   1746 C  CA     . ALA A 1 112 ? 3.183   -6.972  9.862   1.00 41.40  ? 111 ALA A CA     1 
ATOM   1747 C  C      . ALA A 1 112 ? 3.353   -7.718  8.544   1.00 36.49  ? 111 ALA A C      1 
ATOM   1748 O  O      . ALA A 1 112 ? 3.113   -7.179  7.460   1.00 32.66  ? 111 ALA A O      1 
ATOM   1749 C  CB     . ALA A 1 112 ? 1.755   -7.129  10.374  1.00 44.22  ? 111 ALA A CB     1 
ATOM   1750 H  H      . ALA A 1 112 ? 2.851   -5.026  9.792   1.00 48.58  ? 111 ALA A H      1 
ATOM   1751 H  HA     . ALA A 1 112 ? 3.787   -7.360  10.514  1.00 49.70  ? 111 ALA A HA     1 
ATOM   1752 H  HB1    . ALA A 1 112 ? 1.563   -8.073  10.489  1.00 53.08  ? 111 ALA A HB1    1 
ATOM   1753 H  HB2    . ALA A 1 112 ? 1.672   -6.668  11.223  1.00 53.08  ? 111 ALA A HB2    1 
ATOM   1754 H  HB3    . ALA A 1 112 ? 1.143   -6.744  9.727   1.00 53.08  ? 111 ALA A HB3    1 
ATOM   1755 N  N      . ALA A 1 113 ? 3.783   -8.973  8.643   1.00 37.89  ? 112 ALA A N      1 
ATOM   1756 C  CA     . ALA A 1 113 ? 4.048   -9.759  7.436   1.00 40.88  ? 112 ALA A CA     1 
ATOM   1757 C  C      . ALA A 1 113 ? 2.840   -9.755  6.515   1.00 40.65  ? 112 ALA A C      1 
ATOM   1758 O  O      . ALA A 1 113 ? 1.709   -9.996  6.954   1.00 36.85  ? 112 ALA A O      1 
ATOM   1759 C  CB     . ALA A 1 113 ? 4.412   -11.196 7.821   1.00 47.04  ? 112 ALA A CB     1 
ATOM   1760 H  H      . ALA A 1 113 ? 3.927   -9.389  9.382   1.00 45.49  ? 112 ALA A H      1 
ATOM   1761 H  HA     . ALA A 1 113 ? 4.798   -9.371  6.959   1.00 49.07  ? 112 ALA A HA     1 
ATOM   1762 H  HB1    . ALA A 1 113 ? 4.585   -11.704 7.013   1.00 56.47  ? 112 ALA A HB1    1 
ATOM   1763 H  HB2    . ALA A 1 113 ? 5.205   -11.182 8.380   1.00 56.47  ? 112 ALA A HB2    1 
ATOM   1764 H  HB3    . ALA A 1 113 ? 3.671   -11.589 8.308   1.00 56.47  ? 112 ALA A HB3    1 
ATOM   1765 N  N      . GLY A 1 114 ? 3.086   -9.471  5.227   1.00 36.82  ? 113 GLY A N      1 
ATOM   1766 C  CA     . GLY A 1 114 ? 2.057   -9.495  4.220   1.00 31.79  ? 113 GLY A CA     1 
ATOM   1767 C  C      . GLY A 1 114 ? 1.243   -8.231  4.098   1.00 32.11  ? 113 GLY A C      1 
ATOM   1768 O  O      . GLY A 1 114 ? 0.183   -8.263  3.467   1.00 37.31  ? 113 GLY A O      1 
ATOM   1769 H  H      . GLY A 1 114 ? 3.862   -9.259  4.922   1.00 44.21  ? 113 GLY A H      1 
ATOM   1770 H  HA2    . GLY A 1 114 ? 2.467   -9.668  3.358   1.00 38.17  ? 113 GLY A HA2    1 
ATOM   1771 H  HA3    . GLY A 1 114 ? 1.447   -10.224 4.413   1.00 38.17  ? 113 GLY A HA3    1 
ATOM   1772 N  N      . SER A 1 115 ? 1.697   -7.122  4.683   1.00 29.10  ? 114 SER A N      1 
ATOM   1773 C  CA     . SER A 1 115 ? 0.920   -5.893  4.659   1.00 29.94  ? 114 SER A CA     1 
ATOM   1774 C  C      . SER A 1 115 ? 0.993   -5.259  3.275   1.00 31.29  ? 114 SER A C      1 
ATOM   1775 O  O      . SER A 1 115 ? 2.064   -5.206  2.673   1.00 30.47  ? 114 SER A O      1 
ATOM   1776 C  CB     . SER A 1 115 ? 1.450   -4.907  5.698   1.00 30.60  ? 114 SER A CB     1 
ATOM   1777 O  OG     . SER A 1 115 ? 1.283   -5.383  7.042   1.00 35.96  ? 114 SER A OG     1 
ATOM   1778 H  H      . SER A 1 115 ? 2.448   -7.060  5.097   1.00 34.94  ? 114 SER A H      1 
ATOM   1779 H  HA     . SER A 1 115 ? -0.008  -6.089  4.862   1.00 35.95  ? 114 SER A HA     1 
ATOM   1780 H  HB2    . SER A 1 115 ? 2.396   -4.763  5.536   1.00 36.74  ? 114 SER A HB2    1 
ATOM   1781 H  HB3    . SER A 1 115 ? 0.971   -4.069  5.604   1.00 36.74  ? 114 SER A HB3    1 
ATOM   1782 H  HG     . SER A 1 115 ? 1.696   -6.107  7.144   1.00 43.17  ? 114 SER A HG     1 
ATOM   1783 N  N      . VAL A 1 116 ? -0.145  -4.772  2.785   1.00 29.19  ? 115 VAL A N      1 
ATOM   1784 C  CA     . VAL A 1 116 ? -0.212  -3.938  1.582   1.00 28.70  ? 115 VAL A CA     1 
ATOM   1785 C  C      . VAL A 1 116 ? -0.646  -2.556  2.026   1.00 28.08  ? 115 VAL A C      1 
ATOM   1786 O  O      . VAL A 1 116 ? -1.620  -2.414  2.780   1.00 29.93  ? 115 VAL A O      1 
ATOM   1787 C  CB     . VAL A 1 116 ? -1.163  -4.512  0.526   1.00 29.53  ? 115 VAL A CB     1 
ATOM   1788 C  CG1    . VAL A 1 116 ? -1.127  -3.646  -0.788  1.00 28.89  ? 115 VAL A CG1    1 
ATOM   1789 C  CG2    . VAL A 1 116 ? -0.771  -5.943  0.185   1.00 30.36  ? 115 VAL A CG2    1 
ATOM   1790 H  H      . VAL A 1 116 ? -0.915  -4.914  3.141   1.00 35.04  ? 115 VAL A H      1 
ATOM   1791 H  HA     . VAL A 1 116 ? 0.673   -3.869  1.189   1.00 34.46  ? 115 VAL A HA     1 
ATOM   1792 H  HB     . VAL A 1 116 ? -2.070  -4.513  0.871   1.00 35.45  ? 115 VAL A HB     1 
ATOM   1793 H  HG11   . VAL A 1 116 ? -1.737  -4.032  -1.436  1.00 34.69  ? 115 VAL A HG11   1 
ATOM   1794 H  HG12   . VAL A 1 116 ? -1.399  -2.740  -0.576  1.00 34.69  ? 115 VAL A HG12   1 
ATOM   1795 H  HG13   . VAL A 1 116 ? -0.224  -3.647  -1.141  1.00 34.69  ? 115 VAL A HG13   1 
ATOM   1796 H  HG21   . VAL A 1 116 ? -1.384  -6.287  -0.484  1.00 36.45  ? 115 VAL A HG21   1 
ATOM   1797 H  HG22   . VAL A 1 116 ? 0.135   -5.947  -0.163  1.00 36.45  ? 115 VAL A HG22   1 
ATOM   1798 H  HG23   . VAL A 1 116 ? -0.820  -6.483  0.989   1.00 36.45  ? 115 VAL A HG23   1 
ATOM   1799 N  N      . ILE A 1 117 ? 0.157   -1.571  1.663   1.00 25.71  ? 116 ILE A N      1 
ATOM   1800 C  CA     . ILE A 1 117 ? -0.017  -0.176  2.030   1.00 26.37  ? 116 ILE A CA     1 
ATOM   1801 C  C      . ILE A 1 117 ? -0.095  0.645   0.743   1.00 26.70  ? 116 ILE A C      1 
ATOM   1802 O  O      . ILE A 1 117 ? 0.736   0.469   -0.158  1.00 28.02  ? 116 ILE A O      1 
ATOM   1803 C  CB     . ILE A 1 117 ? 1.163   0.300   2.896   1.00 25.57  ? 116 ILE A CB     1 
ATOM   1804 C  CG1    . ILE A 1 117 ? 1.287   -0.543  4.185   1.00 27.83  ? 116 ILE A CG1    1 
ATOM   1805 C  CG2    . ILE A 1 117 ? 1.044   1.787   3.190   1.00 28.80  ? 116 ILE A CG2    1 
ATOM   1806 C  CD1    . ILE A 1 117 ? 2.643   -0.401  4.901   1.00 32.39  ? 116 ILE A CD1    1 
ATOM   1807 H  H      . ILE A 1 117 ? 0.853   -1.696  1.173   1.00 30.87  ? 116 ILE A H      1 
ATOM   1808 H  HA     . ILE A 1 117 ? -0.842  -0.063  2.528   1.00 31.67  ? 116 ILE A HA     1 
ATOM   1809 H  HB     . ILE A 1 117 ? 1.975   0.168   2.382   1.00 30.70  ? 116 ILE A HB     1 
ATOM   1810 H  HG12   . ILE A 1 117 ? 0.595   -0.267  4.806   1.00 33.41  ? 116 ILE A HG12   1 
ATOM   1811 H  HG13   . ILE A 1 117 ? 1.170   -1.479  3.957   1.00 33.41  ? 116 ILE A HG13   1 
ATOM   1812 H  HG21   . ILE A 1 117 ? 1.798   2.062   3.736   1.00 34.58  ? 116 ILE A HG21   1 
ATOM   1813 H  HG22   . ILE A 1 117 ? 1.046   2.276   2.352   1.00 34.58  ? 116 ILE A HG22   1 
ATOM   1814 H  HG23   . ILE A 1 117 ? 0.214   1.949   3.666   1.00 34.58  ? 116 ILE A HG23   1 
ATOM   1815 H  HD11   . ILE A 1 117 ? 2.640   -0.959  5.695   1.00 38.88  ? 116 ILE A HD11   1 
ATOM   1816 H  HD12   . ILE A 1 117 ? 3.348   -0.686  4.299   1.00 38.88  ? 116 ILE A HD12   1 
ATOM   1817 H  HD13   . ILE A 1 117 ? 2.773   0.527   5.148   1.00 38.88  ? 116 ILE A HD13   1 
ATOM   1818 N  N      . LEU A 1 118 ? -1.079  1.543   0.650   1.00 26.83  ? 117 LEU A N      1 
ATOM   1819 C  CA     . LEU A 1 118 ? -1.165  2.492   -0.464  1.00 26.46  ? 117 LEU A CA     1 
ATOM   1820 C  C      . LEU A 1 118 ? -0.972  3.899   0.083   1.00 26.36  ? 117 LEU A C      1 
ATOM   1821 O  O      . LEU A 1 118 ? -1.663  4.303   1.024   1.00 26.31  ? 117 LEU A O      1 
ATOM   1822 C  CB     . LEU A 1 118 ? -2.502  2.394   -1.212  1.00 26.61  ? 117 LEU A CB     1 
ATOM   1823 C  CG     . LEU A 1 118 ? -2.746  3.401   -2.350  1.00 28.32  ? 117 LEU A CG     1 
ATOM   1824 C  CD1    . LEU A 1 118 ? -1.777  3.216   -3.513  1.00 27.98  ? 117 LEU A CD1    1 
ATOM   1825 C  CD2    . LEU A 1 118 ? -4.174  3.274   -2.850  1.00 32.25  ? 117 LEU A CD2    1 
ATOM   1826 H  H      . LEU A 1 118 ? -1.714  1.624   1.224   1.00 32.22  ? 117 LEU A H      1 
ATOM   1827 H  HA     . LEU A 1 118 ? -0.450  2.310   -1.094  1.00 31.77  ? 117 LEU A HA     1 
ATOM   1828 H  HB2    . LEU A 1 118 ? -2.567  1.506   -1.597  1.00 31.95  ? 117 LEU A HB2    1 
ATOM   1829 H  HB3    . LEU A 1 118 ? -3.217  2.514   -0.567  1.00 31.95  ? 117 LEU A HB3    1 
ATOM   1830 H  HG     . LEU A 1 118 ? -2.629  4.300   -2.005  1.00 34.00  ? 117 LEU A HG     1 
ATOM   1831 H  HD11   . LEU A 1 118 ? -1.977  3.874   -4.197  1.00 33.60  ? 117 LEU A HD11   1 
ATOM   1832 H  HD12   . LEU A 1 118 ? -0.871  3.338   -3.190  1.00 33.60  ? 117 LEU A HD12   1 
ATOM   1833 H  HD13   . LEU A 1 118 ? -1.883  2.322   -3.873  1.00 33.60  ? 117 LEU A HD13   1 
ATOM   1834 H  HD21   . LEU A 1 118 ? -4.316  3.913   -3.566  1.00 38.72  ? 117 LEU A HD21   1 
ATOM   1835 H  HD22   . LEU A 1 118 ? -4.315  2.372   -3.178  1.00 38.72  ? 117 LEU A HD22   1 
ATOM   1836 H  HD23   . LEU A 1 118 ? -4.782  3.459   -2.117  1.00 38.72  ? 117 LEU A HD23   1 
ATOM   1837 N  N      . LEU A 1 119 ? -0.048  4.645   -0.520  1.00 23.64  ? 118 LEU A N      1 
ATOM   1838 C  CA     . LEU A 1 119 ? 0.242   6.009   -0.101  1.00 25.77  ? 118 LEU A CA     1 
ATOM   1839 C  C      . LEU A 1 119 ? -0.640  6.992   -0.847  1.00 26.36  ? 118 LEU A C      1 
ATOM   1840 O  O      . LEU A 1 119 ? -1.201  6.686   -1.891  1.00 24.52  ? 118 LEU A O      1 
ATOM   1841 C  CB     . LEU A 1 119 ? 1.703   6.359   -0.374  1.00 25.51  ? 118 LEU A CB     1 
ATOM   1842 C  CG     . LEU A 1 119 ? 2.737   5.388   0.199   1.00 26.62  ? 118 LEU A CG     1 
ATOM   1843 C  CD1    . LEU A 1 119 ? 4.127   5.840   -0.244  1.00 28.78  ? 118 LEU A CD1    1 
ATOM   1844 C  CD2    . LEU A 1 119 ? 2.620   5.292   1.688   1.00 28.40  ? 118 LEU A CD2    1 
ATOM   1845 H  H      . LEU A 1 119 ? 0.431   4.377   -1.182  1.00 28.38  ? 118 LEU A H      1 
ATOM   1846 H  HA     . LEU A 1 119 ? 0.073   6.101   0.850   1.00 30.95  ? 118 LEU A HA     1 
ATOM   1847 H  HB2    . LEU A 1 119 ? 1.836   6.390   -1.334  1.00 30.63  ? 118 LEU A HB2    1 
ATOM   1848 H  HB3    . LEU A 1 119 ? 1.884   7.233   0.006   1.00 30.63  ? 118 LEU A HB3    1 
ATOM   1849 H  HG     . LEU A 1 119 ? 2.578   4.505   -0.170  1.00 31.96  ? 118 LEU A HG     1 
ATOM   1850 H  HD11   . LEU A 1 119 ? 4.787   5.228   0.116   1.00 34.56  ? 118 LEU A HD11   1 
ATOM   1851 H  HD12   . LEU A 1 119 ? 4.165   5.836   -1.213  1.00 34.56  ? 118 LEU A HD12   1 
ATOM   1852 H  HD13   . LEU A 1 119 ? 4.288   6.736   0.090   1.00 34.56  ? 118 LEU A HD13   1 
ATOM   1853 H  HD21   . LEU A 1 119 ? 3.288   4.670   2.017   1.00 34.10  ? 118 LEU A HD21   1 
ATOM   1854 H  HD22   . LEU A 1 119 ? 2.768   6.170   2.073   1.00 34.10  ? 118 LEU A HD22   1 
ATOM   1855 H  HD23   . LEU A 1 119 ? 1.732   4.975   1.916   1.00 34.10  ? 118 LEU A HD23   1 
ATOM   1856 N  N      . GLU A 1 120 ? -0.765  8.185   -0.287  1.00 28.37  ? 119 GLU A N      1 
ATOM   1857 C  CA     . GLU A 1 120 ? -1.564  9.213   -0.922  1.00 29.87  ? 119 GLU A CA     1 
ATOM   1858 C  C      . GLU A 1 120 ? -0.819  9.771   -2.138  1.00 29.93  ? 119 GLU A C      1 
ATOM   1859 O  O      . GLU A 1 120 ? 0.389   9.594   -2.300  1.00 28.46  ? 119 GLU A O      1 
ATOM   1860 C  CB     . GLU A 1 120 ? -1.904  10.315  0.101   1.00 30.56  ? 119 GLU A CB     1 
ATOM   1861 C  CG     . GLU A 1 120 ? -2.723  11.496  -0.376  1.00 33.08  ? 119 GLU A CG     1 
ATOM   1862 C  CD     . GLU A 1 120 ? -4.078  11.120  -0.946  1.00 35.71  ? 119 GLU A CD     1 
ATOM   1863 O  OE1    . GLU A 1 120 ? -5.099  11.374  -0.258  1.00 37.22  ? 119 GLU A OE1    1 
ATOM   1864 O  OE2    . GLU A 1 120 ? -4.117  10.605  -2.091  1.00 33.04  1 119 GLU A OE2    1 
ATOM   1865 H  H      . GLU A 1 120 ? -0.400  8.422   0.455   1.00 34.06  ? 119 GLU A H      1 
ATOM   1866 H  HA     . GLU A 1 120 ? -2.396  8.823   -1.231  1.00 35.87  ? 119 GLU A HA     1 
ATOM   1867 H  HB2    . GLU A 1 120 ? -2.398  9.905   0.829   1.00 36.69  ? 119 GLU A HB2    1 
ATOM   1868 H  HB3    . GLU A 1 120 ? -1.070  10.670  0.445   1.00 36.69  ? 119 GLU A HB3    1 
ATOM   1869 H  HG2    . GLU A 1 120 ? -2.873  12.094  0.373   1.00 39.72  ? 119 GLU A HG2    1 
ATOM   1870 H  HG3    . GLU A 1 120 ? -2.228  11.958  -1.071  1.00 39.72  ? 119 GLU A HG3    1 
ATOM   1871 N  N      . ASN A 1 121 ? -1.578  10.438  -3.009  1.00 26.21  ? 120 ASN A N      1 
ATOM   1872 C  CA     . ASN A 1 121 ? -1.117  11.019  -4.275  1.00 23.28  ? 120 ASN A CA     1 
ATOM   1873 C  C      . ASN A 1 121 ? 0.267   11.682  -4.227  1.00 24.01  ? 120 ASN A C      1 
ATOM   1874 O  O      . ASN A 1 121 ? 0.445   12.711  -3.556  1.00 28.24  ? 120 ASN A O      1 
ATOM   1875 C  CB     . ASN A 1 121 ? -2.160  12.058  -4.700  1.00 24.26  ? 120 ASN A CB     1 
ATOM   1876 C  CG     . ASN A 1 121 ? -2.093  12.427  -6.190  1.00 23.49  ? 120 ASN A CG     1 
ATOM   1877 O  OD1    . ASN A 1 121 ? -1.047  12.378  -6.841  1.00 22.11  ? 120 ASN A OD1    1 
ATOM   1878 N  ND2    . ASN A 1 121 ? -3.234  12.845  -6.709  1.00 23.54  ? 120 ASN A ND2    1 
ATOM   1879 H  H      . ASN A 1 121 ? -2.417  10.574  -2.878  1.00 31.47  ? 120 ASN A H      1 
ATOM   1880 H  HA     . ASN A 1 121 ? -1.092  10.324  -4.950  1.00 27.95  ? 120 ASN A HA     1 
ATOM   1881 H  HB2    . ASN A 1 121 ? -3.045  11.703  -4.522  1.00 29.13  ? 120 ASN A HB2    1 
ATOM   1882 H  HB3    . ASN A 1 121 ? -2.020  12.869  -4.187  1.00 29.13  ? 120 ASN A HB3    1 
ATOM   1883 H  HD21   . ASN A 1 121 ? -3.272  13.069  -7.539  1.00 28.15  ? 120 ASN A HD21   1 
ATOM   1884 H  HD22   . ASN A 1 121 ? -3.938  12.893  -6.218  1.00 28.15  ? 120 ASN A HD22   1 
ATOM   1885 N  N      . LEU A 1 122 ? 1.247   11.121  -4.942  1.00 21.97  ? 121 LEU A N      1 
ATOM   1886 C  CA     . LEU A 1 122 ? 2.596   11.701  -4.977  1.00 21.74  ? 121 LEU A CA     1 
ATOM   1887 C  C      . LEU A 1 122 ? 2.593   13.147  -5.449  1.00 24.28  ? 121 LEU A C      1 
ATOM   1888 O  O      . LEU A 1 122 ? 3.459   13.932  -5.043  1.00 24.92  ? 121 LEU A O      1 
ATOM   1889 C  CB     . LEU A 1 122 ? 3.510   10.879  -5.896  1.00 21.12  ? 121 LEU A CB     1 
ATOM   1890 C  CG     . LEU A 1 122 ? 3.880   9.489   -5.416  1.00 21.86  ? 121 LEU A CG     1 
ATOM   1891 C  CD1    . LEU A 1 122 ? 4.379   8.584   -6.534  1.00 21.11  ? 121 LEU A CD1    1 
ATOM   1892 C  CD2    . LEU A 1 122 ? 4.927   9.577   -4.305  1.00 24.39  ? 121 LEU A CD2    1 
ATOM   1893 H  H      . LEU A 1 122 ? 1.159   10.407  -5.413  1.00 26.38  ? 121 LEU A H      1 
ATOM   1894 H  HA     . LEU A 1 122 ? 2.972   11.679  -4.083  1.00 25.99  ? 121 LEU A HA     1 
ATOM   1895 H  HB2    . LEU A 1 122 ? 3.067   10.779  -6.753  1.00 25.36  ? 121 LEU A HB2    1 
ATOM   1896 H  HB3    . LEU A 1 122 ? 4.338   11.370  -6.019  1.00 25.36  ? 121 LEU A HB3    1 
ATOM   1897 H  HG     . LEU A 1 122 ? 3.088   9.074   -5.038  1.00 26.25  ? 121 LEU A HG     1 
ATOM   1898 H  HD11   . LEU A 1 122 ? 4.597   7.715   -6.163  1.00 25.35  ? 121 LEU A HD11   1 
ATOM   1899 H  HD12   . LEU A 1 122 ? 3.682   8.494   -7.202  1.00 25.35  ? 121 LEU A HD12   1 
ATOM   1900 H  HD13   . LEU A 1 122 ? 5.169   8.982   -6.932  1.00 25.35  ? 121 LEU A HD13   1 
ATOM   1901 H  HD21   . LEU A 1 122 ? 5.151   8.680   -4.011  1.00 29.29  ? 121 LEU A HD21   1 
ATOM   1902 H  HD22   . LEU A 1 122 ? 5.718   10.019  -4.652  1.00 29.29  ? 121 LEU A HD22   1 
ATOM   1903 H  HD23   . LEU A 1 122 ? 4.560   10.086  -3.566  1.00 29.29  ? 121 LEU A HD23   1 
ATOM   1904 N  N      . ARG A 1 123 ? 1.674   13.517  -6.348  1.00 22.66  ? 122 ARG A N      1 
ATOM   1905 C  CA     . ARG A 1 123 ? 1.754   14.849  -6.931  1.00 23.68  ? 122 ARG A CA     1 
ATOM   1906 C  C      . ARG A 1 123 ? 1.140   15.928  -6.046  1.00 25.26  ? 122 ARG A C      1 
ATOM   1907 O  O      . ARG A 1 123 ? 1.115   17.097  -6.455  1.00 26.38  ? 122 ARG A O      1 
ATOM   1908 C  CB     . ARG A 1 123 ? 1.111   14.847  -8.319  1.00 23.28  ? 122 ARG A CB     1 
ATOM   1909 C  CG     . ARG A 1 123 ? 1.972   14.135  -9.315  1.00 22.24  ? 122 ARG A CG     1 
ATOM   1910 C  CD     . ARG A 1 123 ? 1.368   14.194  -10.717 1.00 22.17  ? 122 ARG A CD     1 
ATOM   1911 N  NE     . ARG A 1 123 ? 2.162   13.381  -11.638 1.00 21.31  ? 122 ARG A NE     1 
ATOM   1912 C  CZ     . ARG A 1 123 ? 1.876   13.255  -12.926 1.00 21.29  ? 122 ARG A CZ     1 
ATOM   1913 N  NH1    . ARG A 1 123 ? 0.819   13.897  -13.433 1.00 22.09  1 122 ARG A NH1    1 
ATOM   1914 N  NH2    . ARG A 1 123 ? 2.638   12.484  -13.708 1.00 20.70  ? 122 ARG A NH2    1 
ATOM   1915 H  H      . ARG A 1 123 ? 1.020   13.032  -6.625  1.00 27.10  ? 122 ARG A H      1 
ATOM   1916 H  HA     . ARG A 1 123 ? 2.690   15.073  -7.048  1.00 28.32  ? 122 ARG A HA     1 
ATOM   1917 H  HB2    . ARG A 1 123 ? 0.255   14.392  -8.276  1.00 27.84  ? 122 ARG A HB2    1 
ATOM   1918 H  HB3    . ARG A 1 123 ? 0.992   15.762  -8.619  1.00 27.84  ? 122 ARG A HB3    1 
ATOM   1919 H  HG2    . ARG A 1 123 ? 2.846   14.555  -9.342  1.00 26.60  ? 122 ARG A HG2    1 
ATOM   1920 H  HG3    . ARG A 1 123 ? 2.054   13.203  -9.058  1.00 26.60  ? 122 ARG A HG3    1 
ATOM   1921 H  HD2    . ARG A 1 123 ? 0.464   13.843  -10.697 1.00 26.51  ? 122 ARG A HD2    1 
ATOM   1922 H  HD3    . ARG A 1 123 ? 1.372   15.111  -11.034 1.00 26.51  ? 122 ARG A HD3    1 
ATOM   1923 H  HE     . ARG A 1 123 ? 2.924   13.092  -11.365 1.00 25.47  ? 122 ARG A HE     1 
ATOM   1924 H  HH11   . ARG A 1 123 ? 0.330   14.389  -12.925 1.00 26.41  ? 122 ARG A HH11   1 
ATOM   1925 H  HH12   . ARG A 1 123 ? 0.629   13.820  -14.268 1.00 26.41  ? 122 ARG A HH12   1 
ATOM   1926 H  HH21   . ARG A 1 123 ? 3.318   12.075  -13.377 1.00 24.74  ? 122 ARG A HH21   1 
ATOM   1927 H  HH22   . ARG A 1 123 ? 2.454   12.406  -14.545 1.00 24.74  ? 122 ARG A HH22   1 
ATOM   1928 N  N      . PHE A 1 124 ? 0.659   15.577  -4.852  1.00 25.60  ? 123 PHE A N      1 
ATOM   1929 C  CA     . PHE A 1 124 ? 0.365   16.577  -3.820  1.00 28.77  ? 123 PHE A CA     1 
ATOM   1930 C  C      . PHE A 1 124 ? 1.622   17.282  -3.324  1.00 29.82  ? 123 PHE A C      1 
ATOM   1931 O  O      . PHE A 1 124 ? 1.508   18.247  -2.559  1.00 30.34  ? 123 PHE A O      1 
ATOM   1932 C  CB     . PHE A 1 124 ? -0.348  15.937  -2.623  1.00 29.09  ? 123 PHE A CB     1 
ATOM   1933 C  CG     . PHE A 1 124 ? -1.759  15.501  -2.899  1.00 28.90  ? 123 PHE A CG     1 
ATOM   1934 C  CD1    . PHE A 1 124 ? -2.367  15.756  -4.129  1.00 29.39  ? 123 PHE A CD1    1 
ATOM   1935 C  CD2    . PHE A 1 124 ? -2.492  14.845  -1.915  1.00 31.80  ? 123 PHE A CD2    1 
ATOM   1936 C  CE1    . PHE A 1 124 ? -3.658  15.380  -4.366  1.00 29.97  ? 123 PHE A CE1    1 
ATOM   1937 C  CE2    . PHE A 1 124 ? -3.789  14.458  -2.150  1.00 34.82  ? 123 PHE A CE2    1 
ATOM   1938 C  CZ     . PHE A 1 124 ? -4.373  14.722  -3.388  1.00 31.51  ? 123 PHE A CZ     1 
ATOM   1939 H  H      . PHE A 1 124 ? 0.494   14.767  -4.614  1.00 30.63  ? 123 PHE A H      1 
ATOM   1940 H  HA     . PHE A 1 124 ? -0.225  17.250  -4.194  1.00 34.55  ? 123 PHE A HA     1 
ATOM   1941 H  HB2    . PHE A 1 124 ? 0.153   15.155  -2.345  1.00 34.93  ? 123 PHE A HB2    1 
ATOM   1942 H  HB3    . PHE A 1 124 ? -0.376  16.581  -1.898  1.00 34.93  ? 123 PHE A HB3    1 
ATOM   1943 H  HD1    . PHE A 1 124 ? -1.890  16.201  -4.793  1.00 35.29  ? 123 PHE A HD1    1 
ATOM   1944 H  HD2    . PHE A 1 124 ? -2.101  14.671  -1.089  1.00 38.17  ? 123 PHE A HD2    1 
ATOM   1945 H  HE1    . PHE A 1 124 ? -4.049  15.551  -5.193  1.00 35.98  ? 123 PHE A HE1    1 
ATOM   1946 H  HE2    . PHE A 1 124 ? -4.273  14.016  -1.490  1.00 41.80  ? 123 PHE A HE2    1 
ATOM   1947 H  HZ     . PHE A 1 124 ? -5.250  14.459  -3.552  1.00 37.83  ? 123 PHE A HZ     1 
ATOM   1948 N  N      . HIS A 1 125 ? 2.799   16.822  -3.739  1.00 28.40  ? 124 HIS A N      1 
ATOM   1949 C  CA     . HIS A 1 125 ? 4.090   17.399  -3.385  1.00 30.80  ? 124 HIS A CA     1 
ATOM   1950 C  C      . HIS A 1 125 ? 4.790   17.877  -4.645  1.00 30.01  ? 124 HIS A C      1 
ATOM   1951 O  O      . HIS A 1 125 ? 4.954   17.107  -5.594  1.00 27.59  ? 124 HIS A O      1 
ATOM   1952 C  CB     . HIS A 1 125 ? 4.975   16.369  -2.689  1.00 31.61  ? 124 HIS A CB     1 
ATOM   1953 C  CG     . HIS A 1 125 ? 4.446   15.942  -1.366  1.00 37.22  ? 124 HIS A CG     1 
ATOM   1954 N  ND1    . HIS A 1 125 ? 4.812   16.559  -0.195  1.00 40.29  ? 124 HIS A ND1    1 
ATOM   1955 C  CD2    . HIS A 1 125 ? 3.536   14.999  -1.031  1.00 37.94  ? 124 HIS A CD2    1 
ATOM   1956 C  CE1    . HIS A 1 125 ? 4.174   15.994  0.814   1.00 40.84  ? 124 HIS A CE1    1 
ATOM   1957 N  NE2    . HIS A 1 125 ? 3.386   15.051  0.333   1.00 39.26  ? 124 HIS A NE2    1 
ATOM   1958 H  H      . HIS A 1 125 ? 2.876   16.138  -4.255  1.00 34.10  ? 124 HIS A H      1 
ATOM   1959 H  HA     . HIS A 1 125 ? 3.962   18.155  -2.791  1.00 36.98  ? 124 HIS A HA     1 
ATOM   1960 H  HB2    . HIS A 1 125 ? 5.043   15.581  -3.251  1.00 37.96  ? 124 HIS A HB2    1 
ATOM   1961 H  HB3    . HIS A 1 125 ? 5.855   16.752  -2.549  1.00 37.96  ? 124 HIS A HB3    1 
ATOM   1962 H  HD2    . HIS A 1 125 ? 3.099   14.421  -1.613  1.00 45.54  ? 124 HIS A HD2    1 
ATOM   1963 H  HE1    . HIS A 1 125 ? 4.257   16.229  1.710   1.00 49.03  ? 124 HIS A HE1    1 
ATOM   1964 H  HE2    . HIS A 1 125 ? 2.872   14.542  0.799   1.00 47.14  ? 124 HIS A HE2    1 
ATOM   1965 N  N      . VAL A 1 126 ? 5.238   19.131  -4.633  1.00 31.20  ? 125 VAL A N      1 
ATOM   1966 C  CA     . VAL A 1 126 ? 5.885   19.696  -5.798  1.00 34.45  ? 125 VAL A CA     1 
ATOM   1967 C  C      . VAL A 1 126 ? 7.174   18.952  -6.129  1.00 33.57  ? 125 VAL A C      1 
ATOM   1968 O  O      . VAL A 1 126 ? 7.640   19.003  -7.277  1.00 31.00  ? 125 VAL A O      1 
ATOM   1969 C  CB     . VAL A 1 126 ? 6.118   21.210  -5.574  1.00 38.46  ? 125 VAL A CB     1 
ATOM   1970 C  CG1    . VAL A 1 126 ? 7.141   21.454  -4.473  1.00 39.51  ? 125 VAL A CG1    1 
ATOM   1971 C  CG2    . VAL A 1 126 ? 6.532   21.897  -6.876  1.00 43.50  ? 125 VAL A CG2    1 
ATOM   1972 H  H      . VAL A 1 126 ? 5.178   19.667  -3.963  1.00 37.46  ? 125 VAL A H      1 
ATOM   1973 H  HA     . VAL A 1 126 ? 5.290   19.601  -6.558  1.00 41.36  ? 125 VAL A HA     1 
ATOM   1974 H  HB     . VAL A 1 126 ? 5.282   21.610  -5.287  1.00 46.17  ? 125 VAL A HB     1 
ATOM   1975 H  HG11   . VAL A 1 126 ? 7.261   22.409  -4.360  1.00 47.43  ? 125 VAL A HG11   1 
ATOM   1976 H  HG12   . VAL A 1 126 ? 6.816   21.061  -3.648  1.00 47.43  ? 125 VAL A HG12   1 
ATOM   1977 H  HG13   . VAL A 1 126 ? 7.981   21.042  -4.727  1.00 47.43  ? 125 VAL A HG13   1 
ATOM   1978 H  HG21   . VAL A 1 126 ? 6.670   22.842  -6.703  1.00 52.22  ? 125 VAL A HG21   1 
ATOM   1979 H  HG22   . VAL A 1 126 ? 7.354   21.495  -7.197  1.00 52.22  ? 125 VAL A HG22   1 
ATOM   1980 H  HG23   . VAL A 1 126 ? 5.827   21.780  -7.532  1.00 52.22  ? 125 VAL A HG23   1 
ATOM   1981 N  N      . GLU A 1 127 ? 7.758   18.237  -5.158  1.00 29.46  ? 126 GLU A N      1 
ATOM   1982 C  CA     . GLU A 1 127 ? 9.031   17.563  -5.398  1.00 29.13  ? 126 GLU A CA     1 
ATOM   1983 C  C      . GLU A 1 127 ? 8.913   16.303  -6.262  1.00 27.12  ? 126 GLU A C      1 
ATOM   1984 O  O      . GLU A 1 127 ? 9.935   15.781  -6.714  1.00 26.93  ? 126 GLU A O      1 
ATOM   1985 C  CB     . GLU A 1 127 ? 9.682   17.216  -4.066  1.00 29.89  ? 126 GLU A CB     1 
ATOM   1986 C  CG     . GLU A 1 127 ? 10.082  18.454  -3.250  1.00 33.41  ? 126 GLU A CG     1 
ATOM   1987 C  CD     . GLU A 1 127 ? 8.958   19.018  -2.377  1.00 43.39  ? 126 GLU A CD     1 
ATOM   1988 O  OE1    . GLU A 1 127 ? 9.224   20.014  -1.632  1.00 47.06  ? 126 GLU A OE1    1 
ATOM   1989 O  OE2    . GLU A 1 127 ? 7.819   18.475  -2.413  1.00 35.92  1 126 GLU A OE2    1 
ATOM   1990 H  H      . GLU A 1 127 ? 7.439   18.129  -4.366  1.00 35.26  ? 126 GLU A H      1 
ATOM   1991 H  HA     . GLU A 1 127 ? 9.622   18.178  -5.861  1.00 34.85  ? 126 GLU A HA     1 
ATOM   1992 H  HB2    . GLU A 1 127 ? 9.057   16.697  -3.536  1.00 35.78  ? 126 GLU A HB2    1 
ATOM   1993 H  HB3    . GLU A 1 127 ? 10.485  16.697  -4.234  1.00 35.78  ? 126 GLU A HB3    1 
ATOM   1994 H  HG2    . GLU A 1 127 ? 10.819  18.217  -2.666  1.00 40.11  ? 126 GLU A HG2    1 
ATOM   1995 H  HG3    . GLU A 1 127 ? 10.360  19.153  -3.862  1.00 40.11  ? 126 GLU A HG3    1 
ATOM   1996 N  N      . GLU A 1 128 ? 7.710   15.793  -6.497  1.00 28.26  ? 127 GLU A N      1 
ATOM   1997 C  CA     . GLU A 1 128 ? 7.577   14.618  -7.347  1.00 26.64  ? 127 GLU A CA     1 
ATOM   1998 C  C      . GLU A 1 128 ? 7.882   14.974  -8.805  1.00 24.49  ? 127 GLU A C      1 
ATOM   1999 O  O      . GLU A 1 128 ? 8.760   14.378  -9.431  1.00 23.91  ? 127 GLU A O      1 
ATOM   2000 C  CB     . GLU A 1 128 ? 6.174   14.033  -7.189  1.00 24.36  ? 127 GLU A CB     1 
ATOM   2001 C  CG     . GLU A 1 128 ? 5.721   13.007  -8.268  1.00 21.75  ? 127 GLU A CG     1 
ATOM   2002 C  CD     . GLU A 1 128 ? 6.502   11.713  -8.283  1.00 21.82  ? 127 GLU A CD     1 
ATOM   2003 O  OE1    . GLU A 1 128 ? 7.505   11.583  -7.550  1.00 24.56  ? 127 GLU A OE1    1 
ATOM   2004 O  OE2    . GLU A 1 128 ? 6.120   10.807  -9.057  1.00 22.36  1 127 GLU A OE2    1 
ATOM   2005 H  H      . GLU A 1 128 ? 6.971   16.101  -6.184  1.00 33.94  ? 127 GLU A H      1 
ATOM   2006 H  HA     . GLU A 1 128 ? 8.216   13.946  -7.062  1.00 31.98  ? 127 GLU A HA     1 
ATOM   2007 H  HB2    . GLU A 1 128 ? 6.128   13.586  -6.329  1.00 29.25  ? 127 GLU A HB2    1 
ATOM   2008 H  HB3    . GLU A 1 128 ? 5.538   14.765  -7.203  1.00 29.25  ? 127 GLU A HB3    1 
ATOM   2009 H  HG2    . GLU A 1 128 ? 4.790   12.785  -8.111  1.00 26.01  ? 127 GLU A HG2    1 
ATOM   2010 H  HG3    . GLU A 1 128 ? 5.815   13.416  -9.142  1.00 26.01  ? 127 GLU A HG3    1 
ATOM   2011 N  N      . GLU A 1 129 ? 7.189   15.969  -9.349  1.00 25.36  ? 128 GLU A N      1 
ATOM   2012 C  CA     . GLU A 1 129 ? 7.442   16.406  -10.727 1.00 28.00  ? 128 GLU A CA     1 
ATOM   2013 C  C      . GLU A 1 129 ? 8.582   17.407  -10.820 1.00 31.81  ? 128 GLU A C      1 
ATOM   2014 O  O      . GLU A 1 129 ? 9.159   17.574  -11.900 1.00 31.37  ? 128 GLU A O      1 
ATOM   2015 C  CB     . GLU A 1 129 ? 6.188   17.033  -11.334 1.00 27.22  ? 128 GLU A CB     1 
ATOM   2016 C  CG     . GLU A 1 129 ? 4.979   16.124  -11.388 1.00 31.53  ? 128 GLU A CG     1 
ATOM   2017 C  CD     . GLU A 1 129 ? 3.801   16.799  -12.098 1.00 43.63  ? 128 GLU A CD     1 
ATOM   2018 O  OE1    . GLU A 1 129 ? 3.678   16.670  -13.329 1.00 45.44  ? 128 GLU A OE1    1 
ATOM   2019 O  OE2    . GLU A 1 129 ? 3.015   17.487  -11.414 1.00 47.93  1 128 GLU A OE2    1 
ATOM   2020 H  H      . GLU A 1 129 ? 6.569   16.409  -8.947  1.00 30.45  ? 128 GLU A H      1 
ATOM   2021 H  HA     . GLU A 1 129 ? 7.679   15.633  -11.262 1.00 33.62  ? 128 GLU A HA     1 
ATOM   2022 H  HB2    . GLU A 1 129 ? 5.946   17.811  -10.807 1.00 32.69  ? 128 GLU A HB2    1 
ATOM   2023 H  HB3    . GLU A 1 129 ? 6.389   17.306  -12.243 1.00 32.69  ? 128 GLU A HB3    1 
ATOM   2024 H  HG2    . GLU A 1 129 ? 5.207   15.317  -11.876 1.00 37.86  ? 128 GLU A HG2    1 
ATOM   2025 H  HG3    . GLU A 1 129 ? 4.704   15.903  -10.484 1.00 37.86  ? 128 GLU A HG3    1 
ATOM   2026 N  N      . GLY A 1 130 ? 8.910   18.083  -9.725  1.00 29.41  ? 129 GLY A N      1 
ATOM   2027 C  CA     . GLY A 1 130 ? 9.943   19.091  -9.733  1.00 30.03  ? 129 GLY A CA     1 
ATOM   2028 C  C      . GLY A 1 130 ? 9.439   20.484  -9.994  1.00 31.59  ? 129 GLY A C      1 
ATOM   2029 O  O      . GLY A 1 130 ? 10.207  21.446  -9.863  1.00 34.77  ? 129 GLY A O      1 
ATOM   2030 H  H      . GLY A 1 130 ? 8.540   17.970  -8.957  1.00 35.31  ? 129 GLY A H      1 
ATOM   2031 H  HA2    . GLY A 1 130 ? 10.394  19.089  -8.875  1.00 35.94  ? 129 GLY A HA2    1 
ATOM   2032 H  HA3    . GLY A 1 130 ? 10.594  18.872  -10.418 1.00 35.94  ? 129 GLY A HA3    1 
ATOM   2033 N  N      . LYS A 1 131 ? 8.164   20.620  -10.325 1.00 31.03  ? 130 LYS A N      1 
ATOM   2034 C  CA     . LYS A 1 131 ? 7.564   21.894  -10.685 1.00 38.52  ? 130 LYS A CA     1 
ATOM   2035 C  C      . LYS A 1 131 ? 6.067   21.759  -10.465 1.00 39.11  ? 130 LYS A C      1 
ATOM   2036 O  O      . LYS A 1 131 ? 5.531   20.648  -10.396 1.00 40.04  ? 130 LYS A O      1 
ATOM   2037 C  CB     . LYS A 1 131 ? 7.855   22.271  -12.141 1.00 49.49  ? 130 LYS A CB     1 
ATOM   2038 C  CG     . LYS A 1 131 ? 7.310   21.255  -13.135 1.00 62.08  ? 130 LYS A CG     1 
ATOM   2039 C  CD     . LYS A 1 131 ? 7.613   21.633  -14.580 1.00 77.98  ? 130 LYS A CD     1 
ATOM   2040 C  CE     . LYS A 1 131 ? 7.344   20.463  -15.536 1.00 82.87  ? 130 LYS A CE     1 
ATOM   2041 N  NZ     . LYS A 1 131 ? 5.965   19.898  -15.394 1.00 82.80  1 130 LYS A NZ     1 
ATOM   2042 H  H      . LYS A 1 131 ? 7.607   19.965  -10.349 1.00 37.14  ? 130 LYS A H      1 
ATOM   2043 H  HA     . LYS A 1 131 ? 7.904   22.594  -10.106 1.00 46.25  ? 130 LYS A HA     1 
ATOM   2044 H  HB2    . LYS A 1 131 ? 7.444   23.129  -12.333 1.00 59.40  ? 130 LYS A HB2    1 
ATOM   2045 H  HB3    . LYS A 1 131 ? 8.815   22.328  -12.266 1.00 59.40  ? 130 LYS A HB3    1 
ATOM   2046 H  HG2    . LYS A 1 131 ? 7.714   20.391  -12.960 1.00 74.51  ? 130 LYS A HG2    1 
ATOM   2047 H  HG3    . LYS A 1 131 ? 6.347   21.198  -13.035 1.00 74.51  ? 130 LYS A HG3    1 
ATOM   2048 H  HD2    . LYS A 1 131 ? 7.046   22.376  -14.842 1.00 93.59  ? 130 LYS A HD2    1 
ATOM   2049 H  HD3    . LYS A 1 131 ? 8.547   21.880  -14.658 1.00 93.59  ? 130 LYS A HD3    1 
ATOM   2050 H  HE2    . LYS A 1 131 ? 7.449   20.771  -16.449 1.00 99.46  ? 130 LYS A HE2    1 
ATOM   2051 H  HE3    . LYS A 1 131 ? 7.979   19.753  -15.351 1.00 99.46  ? 130 LYS A HE3    1 
ATOM   2052 H  HZ1    . LYS A 1 131 ? 5.852   19.224  -15.964 1.00 99.38  ? 130 LYS A HZ1    1 
ATOM   2053 H  HZ2    . LYS A 1 131 ? 5.843   19.599  -14.565 1.00 99.38  ? 130 LYS A HZ2    1 
ATOM   2054 H  HZ3    . LYS A 1 131 ? 5.359   20.527  -15.566 1.00 99.38  ? 130 LYS A HZ3    1 
ATOM   2055 N  N      . GLY A 1 132 ? 5.398   22.900  -10.338 1.00 37.21  ? 131 GLY A N      1 
ATOM   2056 C  CA     . GLY A 1 132 ? 3.961   22.866  -10.205 1.00 34.21  ? 131 GLY A CA     1 
ATOM   2057 C  C      . GLY A 1 132 ? 3.393   24.252  -10.061 1.00 36.22  ? 131 GLY A C      1 
ATOM   2058 O  O      . GLY A 1 132 ? 3.926   25.216  -10.608 1.00 36.86  ? 131 GLY A O      1 
ATOM   2059 H  H      . GLY A 1 132 ? 5.748   23.686  -10.326 1.00 44.68  ? 131 GLY A H      1 
ATOM   2060 H  HA2    . GLY A 1 132 ? 3.570   22.450  -10.989 1.00 41.08  ? 131 GLY A HA2    1 
ATOM   2061 H  HA3    . GLY A 1 132 ? 3.717   22.346  -9.423  1.00 41.08  ? 131 GLY A HA3    1 
ATOM   2062 N  N      . LYS A 1 133 ? 2.320   24.366  -9.292  1.00 42.32  ? 132 LYS A N      1 
ATOM   2063 C  CA     . LYS A 1 133 ? 1.696   25.646  -9.013  1.00 45.61  ? 132 LYS A CA     1 
ATOM   2064 C  C      . LYS A 1 133 ? 1.416   25.721  -7.525  1.00 45.55  ? 132 LYS A C      1 
ATOM   2065 O  O      . LYS A 1 133 ? 1.270   24.690  -6.859  1.00 47.00  ? 132 LYS A O      1 
ATOM   2066 C  CB     . LYS A 1 133 ? 0.396   25.826  -9.810  1.00 50.38  ? 132 LYS A CB     1 
ATOM   2067 C  CG     . LYS A 1 133 ? 0.600   25.852  -11.326 1.00 60.21  ? 132 LYS A CG     1 
ATOM   2068 C  CD     . LYS A 1 133 ? -0.714  26.033  -12.086 1.00 70.22  ? 132 LYS A CD     1 
ATOM   2069 C  CE     . LYS A 1 133 ? -0.504  26.107  -13.601 1.00 76.12  ? 132 LYS A CE     1 
ATOM   2070 N  NZ     . LYS A 1 133 ? -0.007  24.819  -14.188 1.00 79.13  1 132 LYS A NZ     1 
ATOM   2071 H  H      . LYS A 1 133 ? 1.927   23.701  -8.914  1.00 50.80  ? 132 LYS A H      1 
ATOM   2072 H  HA     . LYS A 1 133 ? 2.306   26.363  -9.249  1.00 54.75  ? 132 LYS A HA     1 
ATOM   2073 H  HB2    . LYS A 1 133 ? -0.201  25.090  -9.604  1.00 60.48  ? 132 LYS A HB2    1 
ATOM   2074 H  HB3    . LYS A 1 133 ? -0.016  26.665  -9.552  1.00 60.48  ? 132 LYS A HB3    1 
ATOM   2075 H  HG2    . LYS A 1 133 ? 1.185   26.591  -11.555 1.00 72.27  ? 132 LYS A HG2    1 
ATOM   2076 H  HG3    . LYS A 1 133 ? 0.998   25.013  -11.607 1.00 72.27  ? 132 LYS A HG3    1 
ATOM   2077 H  HD2    . LYS A 1 133 ? -1.296  25.280  -11.899 1.00 84.28  ? 132 LYS A HD2    1 
ATOM   2078 H  HD3    . LYS A 1 133 ? -1.136  26.859  -11.799 1.00 84.28  ? 132 LYS A HD3    1 
ATOM   2079 H  HE2    . LYS A 1 133 ? -1.348  26.324  -14.027 1.00 91.36  ? 132 LYS A HE2    1 
ATOM   2080 H  HE3    . LYS A 1 133 ? 0.151   26.796  -13.795 1.00 91.36  ? 132 LYS A HE3    1 
ATOM   2081 H  HZ1    . LYS A 1 133 ? 0.100   24.907  -15.067 1.00 94.98  ? 132 LYS A HZ1    1 
ATOM   2082 H  HZ2    . LYS A 1 133 ? 0.773   24.599  -13.821 1.00 94.98  ? 132 LYS A HZ2    1 
ATOM   2083 H  HZ3    . LYS A 1 133 ? -0.594  24.168  -14.032 1.00 94.98  ? 132 LYS A HZ3    1 
ATOM   2084 N  N      . ASP A 1 134 ? 1.372   26.941  -6.996  1.00 44.91  ? 133 ASP A N      1 
ATOM   2085 C  CA     . ASP A 1 134 ? 0.939   27.102  -5.618  1.00 50.45  ? 133 ASP A CA     1 
ATOM   2086 C  C      . ASP A 1 134 ? -0.597  27.117  -5.563  1.00 55.83  ? 133 ASP A C      1 
ATOM   2087 O  O      . ASP A 1 134 ? -1.287  26.970  -6.579  1.00 51.73  ? 133 ASP A O      1 
ATOM   2088 C  CB     . ASP A 1 134 ? 1.581   28.350  -5.004  1.00 58.02  ? 133 ASP A CB     1 
ATOM   2089 C  CG     . ASP A 1 134 ? 1.024   29.650  -5.558  1.00 66.73  ? 133 ASP A CG     1 
ATOM   2090 O  OD1    . ASP A 1 134 ? 0.065   29.622  -6.357  1.00 70.70  ? 133 ASP A OD1    1 
ATOM   2091 O  OD2    . ASP A 1 134 ? 1.562   30.711  -5.181  1.00 71.22  1 133 ASP A OD2    1 
ATOM   2092 H  H      . ASP A 1 134 ? 1.582   27.669  -7.402  1.00 53.91  ? 133 ASP A H      1 
ATOM   2093 H  HA     . ASP A 1 134 ? 1.242   26.336  -5.106  1.00 60.56  ? 133 ASP A HA     1 
ATOM   2094 H  HB2    . ASP A 1 134 ? 1.426   28.344  -4.047  1.00 69.64  ? 133 ASP A HB2    1 
ATOM   2095 H  HB3    . ASP A 1 134 ? 2.534   28.334  -5.184  1.00 69.64  ? 133 ASP A HB3    1 
ATOM   2096 N  N      . ALA A 1 135 ? -1.154  27.285  -4.357  1.00 64.11  ? 134 ALA A N      1 
ATOM   2097 C  CA     . ALA A 1 135 ? -2.603  27.192  -4.198  1.00 60.84  ? 134 ALA A CA     1 
ATOM   2098 C  C      . ALA A 1 135 ? -3.341  28.338  -4.887  1.00 58.52  ? 134 ALA A C      1 
ATOM   2099 O  O      . ALA A 1 135 ? -4.528  28.199  -5.205  1.00 59.28  ? 134 ALA A O      1 
ATOM   2100 C  CB     . ALA A 1 135 ? -2.945  27.139  -2.708  1.00 64.03  ? 134 ALA A CB     1 
ATOM   2101 H  H      . ALA A 1 135 ? -0.722  27.449  -3.631  1.00 76.95  ? 134 ALA A H      1 
ATOM   2102 H  HA     . ALA A 1 135 ? -2.906  26.363  -4.599  1.00 73.03  ? 134 ALA A HA     1 
ATOM   2103 H  HB1    . ALA A 1 135 ? -3.908  27.077  -2.607  1.00 76.86  ? 134 ALA A HB1    1 
ATOM   2104 H  HB2    . ALA A 1 135 ? -2.521  26.361  -2.314  1.00 76.86  ? 134 ALA A HB2    1 
ATOM   2105 H  HB3    . ALA A 1 135 ? -2.619  27.946  -2.280  1.00 76.86  ? 134 ALA A HB3    1 
ATOM   2106 N  N      . SER A 1 136 ? -2.670  29.461  -5.128  1.00 53.60  ? 135 SER A N      1 
ATOM   2107 C  CA     . SER A 1 136 ? -3.233  30.566  -5.890  1.00 52.11  ? 135 SER A CA     1 
ATOM   2108 C  C      . SER A 1 136 ? -3.033  30.434  -7.401  1.00 59.66  ? 135 SER A C      1 
ATOM   2109 O  O      . SER A 1 136 ? -3.462  31.321  -8.147  1.00 61.53  ? 135 SER A O      1 
ATOM   2110 C  CB     . SER A 1 136 ? -2.614  31.875  -5.418  1.00 54.02  ? 135 SER A CB     1 
ATOM   2111 O  OG     . SER A 1 136 ? -2.845  32.049  -4.027  1.00 60.41  ? 135 SER A OG     1 
ATOM   2112 H  H      . SER A 1 136 ? -1.869  29.608  -4.853  1.00 64.34  ? 135 SER A H      1 
ATOM   2113 H  HA     . SER A 1 136 ? -4.187  30.610  -5.720  1.00 62.55  ? 135 SER A HA     1 
ATOM   2114 H  HB2    . SER A 1 136 ? -1.658  31.851  -5.581  1.00 64.84  ? 135 SER A HB2    1 
ATOM   2115 H  HB3    . SER A 1 136 ? -3.018  32.611  -5.902  1.00 64.84  ? 135 SER A HB3    1 
ATOM   2116 H  HG     . SER A 1 136 ? -2.503  32.770  -3.767  1.00 72.51  ? 135 SER A HG     1 
ATOM   2117 N  N      . GLY A 1 137 ? -2.385  29.374  -7.872  1.00 66.68  ? 136 GLY A N      1 
ATOM   2118 C  CA     . GLY A 1 137 ? -2.218  29.173  -9.294  1.00 64.03  ? 136 GLY A CA     1 
ATOM   2119 C  C      . GLY A 1 137 ? -0.985  29.796  -9.914  1.00 60.58  ? 136 GLY A C      1 
ATOM   2120 O  O      . GLY A 1 137 ? -0.900  29.855  -11.148 1.00 61.68  ? 136 GLY A O      1 
ATOM   2121 H  H      . GLY A 1 137 ? -2.035  28.759  -7.383  1.00 80.04  ? 136 GLY A H      1 
ATOM   2122 H  HA2    . GLY A 1 137 ? -2.186  28.220  -9.471  1.00 76.85  ? 136 GLY A HA2    1 
ATOM   2123 H  HA3    . GLY A 1 137 ? -2.992  29.534  -9.752  1.00 76.85  ? 136 GLY A HA3    1 
ATOM   2124 N  N      . ASN A 1 138 ? -0.028  30.266  -9.116  1.00 54.35  ? 137 ASN A N      1 
ATOM   2125 C  CA     . ASN A 1 138 ? 1.233   30.749  -9.667  1.00 56.42  ? 137 ASN A CA     1 
ATOM   2126 C  C      . ASN A 1 138 ? 2.198   29.586  -9.881  1.00 52.13  ? 137 ASN A C      1 
ATOM   2127 O  O      . ASN A 1 138 ? 2.331   28.708  -9.025  1.00 46.10  ? 137 ASN A O      1 
ATOM   2128 C  CB     . ASN A 1 138 ? 1.856   31.784  -8.736  1.00 62.14  ? 137 ASN A CB     1 
ATOM   2129 C  CG     . ASN A 1 138 ? 0.915   32.944  -8.450  1.00 74.41  ? 137 ASN A CG     1 
ATOM   2130 O  OD1    . ASN A 1 138 ? 0.799   33.875  -9.247  1.00 78.85  ? 137 ASN A OD1    1 
ATOM   2131 N  ND2    . ASN A 1 138 ? 0.234   32.888  -7.310  1.00 80.53  ? 137 ASN A ND2    1 
ATOM   2132 H  H      . ASN A 1 138 ? -0.084  30.315  -8.259  1.00 65.24  ? 137 ASN A H      1 
ATOM   2133 H  HA     . ASN A 1 138 ? 1.068   31.170  -10.525 1.00 67.73  ? 137 ASN A HA     1 
ATOM   2134 H  HB2    . ASN A 1 138 ? 2.077   31.360  -7.892  1.00 74.58  ? 137 ASN A HB2    1 
ATOM   2135 H  HB3    . ASN A 1 138 ? 2.657   32.141  -9.150  1.00 74.58  ? 137 ASN A HB3    1 
ATOM   2136 H  HD21   . ASN A 1 138 ? -0.311  33.521  -7.104  1.00 96.66  ? 137 ASN A HD21   1 
ATOM   2137 H  HD22   . ASN A 1 138 ? 0.338   32.220  -6.779  1.00 96.66  ? 137 ASN A HD22   1 
ATOM   2138 N  N      . LYS A 1 139 ? 2.866   29.573  -11.036 1.00 55.99  ? 138 LYS A N      1 
ATOM   2139 C  CA     . LYS A 1 139 ? 3.792   28.489  -11.346 1.00 60.58  ? 138 LYS A CA     1 
ATOM   2140 C  C      . LYS A 1 139 ? 5.021   28.556  -10.447 1.00 53.13  ? 138 LYS A C      1 
ATOM   2141 O  O      . LYS A 1 139 ? 5.581   29.626  -10.220 1.00 55.65  ? 138 LYS A O      1 
ATOM   2142 C  CB     . LYS A 1 139 ? 4.212   28.546  -12.816 1.00 77.90  ? 138 LYS A CB     1 
ATOM   2143 C  CG     . LYS A 1 139 ? 3.140   28.056  -13.787 1.00 93.19  ? 138 LYS A CG     1 
ATOM   2144 C  CD     . LYS A 1 139 ? 3.673   27.970  -15.212 1.00 103.47 ? 138 LYS A CD     1 
ATOM   2145 C  CE     . LYS A 1 139 ? 2.688   27.285  -16.149 1.00 105.83 ? 138 LYS A CE     1 
ATOM   2146 N  NZ     . LYS A 1 139 ? 3.286   27.061  -17.497 1.00 107.93 1 138 LYS A NZ     1 
ATOM   2147 H  H      . LYS A 1 139 ? 2.800   30.174  -11.648 1.00 67.21  ? 138 LYS A H      1 
ATOM   2148 H  HA     . LYS A 1 139 ? 3.350   27.639  -11.192 1.00 72.72  ? 138 LYS A HA     1 
ATOM   2149 H  HB2    . LYS A 1 139 ? 4.420   29.466  -13.045 1.00 93.50  ? 138 LYS A HB2    1 
ATOM   2150 H  HB3    . LYS A 1 139 ? 4.998   27.992  -12.938 1.00 93.50  ? 138 LYS A HB3    1 
ATOM   2151 H  HG2    . LYS A 1 139 ? 2.847   27.171  -13.519 1.00 111.85 ? 138 LYS A HG2    1 
ATOM   2152 H  HG3    . LYS A 1 139 ? 2.393   28.674  -13.779 1.00 111.85 ? 138 LYS A HG3    1 
ATOM   2153 H  HD2    . LYS A 1 139 ? 3.834   28.866  -15.546 1.00 124.19 ? 138 LYS A HD2    1 
ATOM   2154 H  HD3    . LYS A 1 139 ? 4.497   27.458  -15.213 1.00 124.19 ? 138 LYS A HD3    1 
ATOM   2155 H  HE2    . LYS A 1 139 ? 2.440   26.423  -15.780 1.00 127.02 ? 138 LYS A HE2    1 
ATOM   2156 H  HE3    . LYS A 1 139 ? 1.903   27.845  -16.254 1.00 127.02 ? 138 LYS A HE3    1 
ATOM   2157 H  HZ1    . LYS A 1 139 ? 2.695   26.660  -18.028 1.00 129.53 ? 138 LYS A HZ1    1 
ATOM   2158 H  HZ2    . LYS A 1 139 ? 3.520   27.840  -17.859 1.00 129.53 ? 138 LYS A HZ2    1 
ATOM   2159 H  HZ3    . LYS A 1 139 ? 4.009   26.546  -17.427 1.00 129.53 ? 138 LYS A HZ3    1 
ATOM   2160 N  N      . VAL A 1 140 ? 5.446   27.401  -9.923  1.00 49.51  ? 139 VAL A N      1 
ATOM   2161 C  CA     . VAL A 1 140 ? 6.585   27.348  -9.013  1.00 49.46  ? 139 VAL A CA     1 
ATOM   2162 C  C      . VAL A 1 140 ? 7.463   26.142  -9.321  1.00 49.62  ? 139 VAL A C      1 
ATOM   2163 O  O      . VAL A 1 140 ? 7.018   25.134  -9.875  1.00 48.00  ? 139 VAL A O      1 
ATOM   2164 C  CB     . VAL A 1 140 ? 6.142   27.316  -7.533  1.00 48.54  ? 139 VAL A CB     1 
ATOM   2165 C  CG1    . VAL A 1 140 ? 5.210   28.485  -7.252  1.00 53.61  ? 139 VAL A CG1    1 
ATOM   2166 C  CG2    . VAL A 1 140 ? 5.472   26.007  -7.182  1.00 45.03  ? 139 VAL A CG2    1 
ATOM   2167 H  H      . VAL A 1 140 ? 5.089   26.635  -10.083 1.00 59.43  ? 139 VAL A H      1 
ATOM   2168 H  HA     . VAL A 1 140 ? 7.122   28.146  -9.143  1.00 59.38  ? 139 VAL A HA     1 
ATOM   2169 H  HB     . VAL A 1 140 ? 6.924   27.414  -6.967  1.00 58.26  ? 139 VAL A HB     1 
ATOM   2170 H  HG11   . VAL A 1 140 ? 4.938   28.455  -6.321  1.00 64.36  ? 139 VAL A HG11   1 
ATOM   2171 H  HG12   . VAL A 1 140 ? 5.679   29.314  -7.434  1.00 64.36  ? 139 VAL A HG12   1 
ATOM   2172 H  HG13   . VAL A 1 140 ? 4.431   28.412  -7.827  1.00 64.36  ? 139 VAL A HG13   1 
ATOM   2173 H  HG21   . VAL A 1 140 ? 5.211   26.027  -6.248  1.00 54.05  ? 139 VAL A HG21   1 
ATOM   2174 H  HG22   . VAL A 1 140 ? 4.689   25.893  -7.743  1.00 54.05  ? 139 VAL A HG22   1 
ATOM   2175 H  HG23   . VAL A 1 140 ? 6.098   25.282  -7.336  1.00 54.05  ? 139 VAL A HG23   1 
ATOM   2176 N  N      . LYS A 1 141 ? 8.731   26.267  -8.941  1.00 51.46  ? 140 LYS A N      1 
ATOM   2177 C  CA     . LYS A 1 141 ? 9.729   25.222  -9.116  1.00 53.89  ? 140 LYS A CA     1 
ATOM   2178 C  C      . LYS A 1 141 ? 10.157  24.686  -7.752  1.00 53.02  ? 140 LYS A C      1 
ATOM   2179 O  O      . LYS A 1 141 ? 10.308  25.449  -6.794  1.00 55.12  ? 140 LYS A O      1 
ATOM   2180 C  CB     . LYS A 1 141 ? 10.939  25.768  -9.880  1.00 62.57  ? 140 LYS A CB     1 
ATOM   2181 C  CG     . LYS A 1 141 ? 11.930  24.712  -10.339 1.00 71.61  ? 140 LYS A CG     1 
ATOM   2182 C  CD     . LYS A 1 141 ? 12.929  25.278  -11.353 1.00 82.99  ? 140 LYS A CD     1 
ATOM   2183 C  CE     . LYS A 1 141 ? 12.288  25.537  -12.731 1.00 86.50  ? 140 LYS A CE     1 
ATOM   2184 N  NZ     . LYS A 1 141 ? 13.271  25.990  -13.775 1.00 86.53  1 140 LYS A NZ     1 
ATOM   2185 H  H      . LYS A 1 141 ? 9.045   26.974  -8.565  1.00 61.77  ? 140 LYS A H      1 
ATOM   2186 H  HA     . LYS A 1 141 ? 9.346   24.491  -9.627  1.00 64.69  ? 140 LYS A HA     1 
ATOM   2187 H  HB2    . LYS A 1 141 ? 10.622  26.235  -10.669 1.00 75.10  ? 140 LYS A HB2    1 
ATOM   2188 H  HB3    . LYS A 1 141 ? 11.415  26.387  -9.305  1.00 75.10  ? 140 LYS A HB3    1 
ATOM   2189 H  HG2    . LYS A 1 141 ? 12.428  24.386  -9.572  1.00 85.96  ? 140 LYS A HG2    1 
ATOM   2190 H  HG3    . LYS A 1 141 ? 11.449  23.983  -10.761 1.00 85.96  ? 140 LYS A HG3    1 
ATOM   2191 H  HD2    . LYS A 1 141 ? 13.277  26.120  -11.020 1.00 99.60  ? 140 LYS A HD2    1 
ATOM   2192 H  HD3    . LYS A 1 141 ? 13.653  24.643  -11.473 1.00 99.60  ? 140 LYS A HD3    1 
ATOM   2193 H  HE2    . LYS A 1 141 ? 11.877  24.717  -13.045 1.00 103.82 ? 140 LYS A HE2    1 
ATOM   2194 H  HE3    . LYS A 1 141 ? 11.614  26.228  -12.637 1.00 103.82 ? 140 LYS A HE3    1 
ATOM   2195 H  HZ1    . LYS A 1 141 ? 12.851  26.126  -14.548 1.00 103.86 ? 140 LYS A HZ1    1 
ATOM   2196 H  HZ2    . LYS A 1 141 ? 13.658  26.750  -13.519 1.00 103.86 ? 140 LYS A HZ2    1 
ATOM   2197 H  HZ3    . LYS A 1 141 ? 13.898  25.370  -13.891 1.00 103.86 ? 140 LYS A HZ3    1 
ATOM   2198 N  N      . ALA A 1 142 ? 10.345  23.373  -7.663  1.00 47.75  ? 141 ALA A N      1 
ATOM   2199 C  CA     . ALA A 1 142 ? 10.764  22.764  -6.411  1.00 44.41  ? 141 ALA A CA     1 
ATOM   2200 C  C      . ALA A 1 142 ? 12.227  23.082  -6.120  1.00 49.89  ? 141 ALA A C      1 
ATOM   2201 O  O      . ALA A 1 142 ? 13.036  23.280  -7.026  1.00 50.27  ? 141 ALA A O      1 
ATOM   2202 C  CB     . ALA A 1 142 ? 10.558  21.254  -6.467  1.00 39.26  ? 141 ALA A CB     1 
ATOM   2203 H  H      . ALA A 1 142 ? 10.236  22.817  -8.311  1.00 57.32  ? 141 ALA A H      1 
ATOM   2204 H  HA     . ALA A 1 142 ? 10.225  23.118  -5.687  1.00 53.31  ? 141 ALA A HA     1 
ATOM   2205 H  HB1    . ALA A 1 142 ? 10.843  20.866  -5.625  1.00 47.13  ? 141 ALA A HB1    1 
ATOM   2206 H  HB2    . ALA A 1 142 ? 9.618   21.069  -6.616  1.00 47.13  ? 141 ALA A HB2    1 
ATOM   2207 H  HB3    . ALA A 1 142 ? 11.087  20.890  -7.194  1.00 47.13  ? 141 ALA A HB3    1 
ATOM   2208 N  N      . GLU A 1 143 ? 12.564  23.130  -4.829  1.00 54.33  ? 142 GLU A N      1 
ATOM   2209 C  CA     . GLU A 1 143 ? 13.936  23.408  -4.418  1.00 58.20  ? 142 GLU A CA     1 
ATOM   2210 C  C      . GLU A 1 143 ? 14.750  22.118  -4.402  1.00 43.30  ? 142 GLU A C      1 
ATOM   2211 O  O      . GLU A 1 143 ? 14.273  21.098  -3.897  1.00 39.13  ? 142 GLU A O      1 
ATOM   2212 C  CB     . GLU A 1 143 ? 13.961  24.040  -3.032  1.00 81.07  ? 142 GLU A CB     1 
ATOM   2213 C  CG     . GLU A 1 143 ? 13.167  25.332  -2.954  1.00 99.46  ? 142 GLU A CG     1 
ATOM   2214 C  CD     . GLU A 1 143 ? 12.860  25.747  -1.534  1.00 112.22 ? 142 GLU A CD     1 
ATOM   2215 O  OE1    . GLU A 1 143 ? 13.678  25.448  -0.637  1.00 116.87 ? 142 GLU A OE1    1 
ATOM   2216 O  OE2    . GLU A 1 143 ? 11.794  26.365  -1.315  1.00 116.20 1 142 GLU A OE2    1 
ATOM   2217 H  H      . GLU A 1 143 ? 12.017  23.006  -4.177  1.00 65.22  ? 142 GLU A H      1 
ATOM   2218 H  HA     . GLU A 1 143 ? 14.345  24.023  -5.046  1.00 69.86  ? 142 GLU A HA     1 
ATOM   2219 H  HB2    . GLU A 1 143 ? 13.581  23.416  -2.394  1.00 97.30  ? 142 GLU A HB2    1 
ATOM   2220 H  HB3    . GLU A 1 143 ? 14.880  24.239  -2.793  1.00 97.30  ? 142 GLU A HB3    1 
ATOM   2221 H  HG2    . GLU A 1 143 ? 13.679  26.043  -3.370  1.00 119.38 ? 142 GLU A HG2    1 
ATOM   2222 H  HG3    . GLU A 1 143 ? 12.325  25.213  -3.421  1.00 119.38 ? 142 GLU A HG3    1 
ATOM   2223 N  N      . PRO A 1 144 ? 15.983  22.124  -4.922  1.00 42.37  ? 143 PRO A N      1 
ATOM   2224 C  CA     . PRO A 1 144 ? 16.730  20.857  -5.022  1.00 44.58  ? 143 PRO A CA     1 
ATOM   2225 C  C      . PRO A 1 144 ? 16.918  20.148  -3.691  1.00 44.38  ? 143 PRO A C      1 
ATOM   2226 O  O      . PRO A 1 144 ? 16.802  18.920  -3.636  1.00 41.09  ? 143 PRO A O      1 
ATOM   2227 C  CB     . PRO A 1 144 ? 18.070  21.292  -5.627  1.00 47.80  ? 143 PRO A CB     1 
ATOM   2228 C  CG     . PRO A 1 144 ? 17.773  22.548  -6.352  1.00 49.28  ? 143 PRO A CG     1 
ATOM   2229 C  CD     . PRO A 1 144 ? 16.701  23.233  -5.572  1.00 48.40  ? 143 PRO A CD     1 
ATOM   2230 H  HA     . PRO A 1 144 ? 16.284  20.256  -5.639  1.00 53.52  ? 143 PRO A HA     1 
ATOM   2231 H  HB2    . PRO A 1 144 ? 18.713  21.449  -4.918  1.00 57.37  ? 143 PRO A HB2    1 
ATOM   2232 H  HB3    . PRO A 1 144 ? 18.390  20.610  -6.237  1.00 57.37  ? 143 PRO A HB3    1 
ATOM   2233 H  HG2    . PRO A 1 144 ? 18.572  23.097  -6.389  1.00 59.15  ? 143 PRO A HG2    1 
ATOM   2234 H  HG3    . PRO A 1 144 ? 17.462  22.339  -7.247  1.00 59.15  ? 143 PRO A HG3    1 
ATOM   2235 H  HD2    . PRO A 1 144 ? 17.092  23.820  -4.905  1.00 58.10  ? 143 PRO A HD2    1 
ATOM   2236 H  HD3    . PRO A 1 144 ? 16.108  23.717  -6.167  1.00 58.10  ? 143 PRO A HD3    1 
ATOM   2237 N  N      . ALA A 1 145 ? 17.236  20.879  -2.617  1.00 44.09  ? 144 ALA A N      1 
ATOM   2238 C  CA     . ALA A 1 145 ? 17.394  20.237  -1.316  1.00 39.65  ? 144 ALA A CA     1 
ATOM   2239 C  C      . ALA A 1 145 ? 16.118  19.527  -0.900  1.00 35.90  ? 144 ALA A C      1 
ATOM   2240 O  O      . ALA A 1 145 ? 16.167  18.440  -0.312  1.00 37.98  ? 144 ALA A O      1 
ATOM   2241 C  CB     . ALA A 1 145 ? 17.805  21.269  -0.259  1.00 42.87  ? 144 ALA A CB     1 
ATOM   2242 H  H      . ALA A 1 145 ? 17.363  21.730  -2.618  1.00 52.93  ? 144 ALA A H      1 
ATOM   2243 H  HA     . ALA A 1 145 ? 18.100  19.574  -1.375  1.00 47.60  ? 144 ALA A HA     1 
ATOM   2244 H  HB1    . ALA A 1 145 ? 17.904  20.822  0.596   1.00 51.46  ? 144 ALA A HB1    1 
ATOM   2245 H  HB2    . ALA A 1 145 ? 18.647  21.672  -0.522  1.00 51.46  ? 144 ALA A HB2    1 
ATOM   2246 H  HB3    . ALA A 1 145 ? 17.116  21.950  -0.200  1.00 51.46  ? 144 ALA A HB3    1 
ATOM   2247 N  N      . LYS A 1 146 ? 14.959  20.107  -1.219  1.00 32.87  ? 145 LYS A N      1 
ATOM   2248 C  CA     . LYS A 1 146 ? 13.708  19.463  -0.850  1.00 39.26  ? 145 LYS A CA     1 
ATOM   2249 C  C      . LYS A 1 146 ? 13.429  18.252  -1.726  1.00 32.48  ? 145 LYS A C      1 
ATOM   2250 O  O      . LYS A 1 146 ? 12.867  17.261  -1.238  1.00 29.34  ? 145 LYS A O      1 
ATOM   2251 C  CB     . LYS A 1 146 ? 12.561  20.468  -0.917  1.00 64.59  ? 145 LYS A CB     1 
ATOM   2252 C  CG     . LYS A 1 146 ? 12.695  21.573  0.116   1.00 79.89  ? 145 LYS A CG     1 
ATOM   2253 C  CD     . LYS A 1 146 ? 11.350  22.128  0.548   1.00 83.26  ? 145 LYS A CD     1 
ATOM   2254 C  CE     . LYS A 1 146 ? 11.469  22.880  1.873   1.00 82.17  ? 145 LYS A CE     1 
ATOM   2255 N  NZ     . LYS A 1 146 ? 12.503  23.949  1.813   1.00 77.14  1 145 LYS A NZ     1 
ATOM   2256 H  H      . LYS A 1 146 ? 14.875  20.853  -1.638  1.00 39.35  ? 145 LYS A H      1 
ATOM   2257 H  HA     . LYS A 1 146 ? 13.776  19.154  0.067   1.00 47.13  ? 145 LYS A HA     1 
ATOM   2258 H  HB2    . LYS A 1 146 ? 12.550  20.878  -1.796  1.00 77.52  ? 145 LYS A HB2    1 
ATOM   2259 H  HB3    . LYS A 1 146 ? 11.724  20.006  -0.756  1.00 77.52  ? 145 LYS A HB3    1 
ATOM   2260 H  HG2    . LYS A 1 146 ? 13.142  21.220  0.901   1.00 95.88  ? 145 LYS A HG2    1 
ATOM   2261 H  HG3    . LYS A 1 146 ? 13.213  22.300  -0.263  1.00 95.88  ? 145 LYS A HG3    1 
ATOM   2262 H  HD2    . LYS A 1 146 ? 11.025  22.746  -0.125  1.00 99.93  ? 145 LYS A HD2    1 
ATOM   2263 H  HD3    . LYS A 1 146 ? 10.723  21.398  0.667   1.00 99.93  ? 145 LYS A HD3    1 
ATOM   2264 H  HE2    . LYS A 1 146 ? 10.617  23.294  2.082   1.00 98.62  ? 145 LYS A HE2    1 
ATOM   2265 H  HE3    . LYS A 1 146 ? 11.719  22.256  2.572   1.00 98.62  ? 145 LYS A HE3    1 
ATOM   2266 H  HZ1    . LYS A 1 146 ? 12.551  24.369  2.596   1.00 92.59  ? 145 LYS A HZ1    1 
ATOM   2267 H  HZ2    . LYS A 1 146 ? 13.297  23.593  1.627   1.00 92.59  ? 145 LYS A HZ2    1 
ATOM   2268 H  HZ3    . LYS A 1 146 ? 12.294  24.539  1.181   1.00 92.59  ? 145 LYS A HZ3    1 
ATOM   2269 N  N      . ILE A 1 147 ? 13.821  18.305  -3.005  1.00 33.06  ? 146 ILE A N      1 
ATOM   2270 C  CA     . ILE A 1 147 ? 13.663  17.133  -3.868  1.00 30.56  ? 146 ILE A CA     1 
ATOM   2271 C  C      . ILE A 1 147 ? 14.501  15.977  -3.338  1.00 30.40  ? 146 ILE A C      1 
ATOM   2272 O  O      . ILE A 1 147 ? 14.077  14.821  -3.372  1.00 29.25  ? 146 ILE A O      1 
ATOM   2273 C  CB     . ILE A 1 147 ? 14.034  17.469  -5.324  1.00 28.42  ? 146 ILE A CB     1 
ATOM   2274 C  CG1    . ILE A 1 147 ? 13.130  18.570  -5.898  1.00 29.31  ? 146 ILE A CG1    1 
ATOM   2275 C  CG2    . ILE A 1 147 ? 13.908  16.236  -6.197  1.00 26.94  ? 146 ILE A CG2    1 
ATOM   2276 C  CD1    . ILE A 1 147 ? 13.592  19.097  -7.280  1.00 35.57  ? 146 ILE A CD1    1 
ATOM   2277 H  H      . ILE A 1 147 ? 14.172  18.990  -3.387  1.00 39.69  ? 146 ILE A H      1 
ATOM   2278 H  HA     . ILE A 1 147 ? 12.733  16.856  -3.855  1.00 36.70  ? 146 ILE A HA     1 
ATOM   2279 H  HB     . ILE A 1 147 ? 14.954  17.776  -5.348  1.00 34.13  ? 146 ILE A HB     1 
ATOM   2280 H  HG12   . ILE A 1 147 ? 12.233  18.217  -6.000  1.00 35.19  ? 146 ILE A HG12   1 
ATOM   2281 H  HG13   . ILE A 1 147 ? 13.121  19.320  -5.283  1.00 35.19  ? 146 ILE A HG13   1 
ATOM   2282 H  HG21   . ILE A 1 147 ? 14.146  16.469  -7.108  1.00 32.35  ? 146 ILE A HG21   1 
ATOM   2283 H  HG22   . ILE A 1 147 ? 14.508  15.550  -5.863  1.00 32.35  ? 146 ILE A HG22   1 
ATOM   2284 H  HG23   . ILE A 1 147 ? 12.992  15.919  -6.165  1.00 32.35  ? 146 ILE A HG23   1 
ATOM   2285 H  HD11   . ILE A 1 147 ? 12.977  19.785  -7.576  1.00 42.70  ? 146 ILE A HD11   1 
ATOM   2286 H  HD12   . ILE A 1 147 ? 14.485  19.465  -7.194  1.00 42.70  ? 146 ILE A HD12   1 
ATOM   2287 H  HD13   . ILE A 1 147 ? 13.596  18.361  -7.912  1.00 42.70  ? 146 ILE A HD13   1 
ATOM   2288 N  N      . GLU A 1 148 ? 15.710  16.262  -2.854  1.00 34.91  ? 147 GLU A N      1 
ATOM   2289 C  CA     . GLU A 1 148 ? 16.540  15.178  -2.330  1.00 37.97  ? 147 GLU A CA     1 
ATOM   2290 C  C      . GLU A 1 148 ? 15.899  14.556  -1.092  1.00 33.83  ? 147 GLU A C      1 
ATOM   2291 O  O      . GLU A 1 148 ? 15.901  13.328  -0.938  1.00 33.90  ? 147 GLU A O      1 
ATOM   2292 C  CB     . GLU A 1 148 ? 17.960  15.683  -2.027  1.00 50.08  ? 147 GLU A CB     1 
ATOM   2293 C  CG     . GLU A 1 148 ? 18.847  15.850  -3.270  1.00 71.80  ? 147 GLU A CG     1 
ATOM   2294 C  CD     . GLU A 1 148 ? 18.896  14.600  -4.162  1.00 91.74  ? 147 GLU A CD     1 
ATOM   2295 O  OE1    . GLU A 1 148 ? 18.861  13.467  -3.634  1.00 98.92  ? 147 GLU A OE1    1 
ATOM   2296 O  OE2    . GLU A 1 148 ? 18.960  14.753  -5.400  1.00 97.82  1 147 GLU A OE2    1 
ATOM   2297 H  H      . GLU A 1 148 ? 16.063  17.045  -2.819  1.00 41.91  ? 147 GLU A H      1 
ATOM   2298 H  HA     . GLU A 1 148 ? 16.611  14.486  -3.006  1.00 45.58  ? 147 GLU A HA     1 
ATOM   2299 H  HB2    . GLU A 1 148 ? 17.897  16.547  -1.591  1.00 60.11  ? 147 GLU A HB2    1 
ATOM   2300 H  HB3    . GLU A 1 148 ? 18.396  15.049  -1.436  1.00 60.11  ? 147 GLU A HB3    1 
ATOM   2301 H  HG2    . GLU A 1 148 ? 18.503  16.583  -3.804  1.00 86.18  ? 147 GLU A HG2    1 
ATOM   2302 H  HG3    . GLU A 1 148 ? 19.753  16.047  -2.984  1.00 86.18  ? 147 GLU A HG3    1 
ATOM   2303 N  N      . ALA A 1 149 ? 15.293  15.389  -0.234  1.00 33.93  ? 148 ALA A N      1 
ATOM   2304 C  CA     . ALA A 1 149 ? 14.641  14.902  0.988   1.00 34.05  ? 148 ALA A CA     1 
ATOM   2305 C  C      . ALA A 1 149 ? 13.405  14.079  0.670   1.00 29.90  ? 148 ALA A C      1 
ATOM   2306 O  O      . ALA A 1 149 ? 13.110  13.097  1.360   1.00 29.69  ? 148 ALA A O      1 
ATOM   2307 C  CB     . ALA A 1 149 ? 14.244  16.074  1.880   1.00 38.12  ? 148 ALA A CB     1 
ATOM   2308 H  H      . ALA A 1 149 ? 15.247  16.241  -0.338  1.00 40.74  ? 148 ALA A H      1 
ATOM   2309 H  HA     . ALA A 1 149 ? 15.261  14.341  1.480   1.00 40.87  ? 148 ALA A HA     1 
ATOM   2310 H  HB1    . ALA A 1 149 ? 13.815  15.730  2.680   1.00 45.76  ? 148 ALA A HB1    1 
ATOM   2311 H  HB2    . ALA A 1 149 ? 15.041  16.572  2.120   1.00 45.76  ? 148 ALA A HB2    1 
ATOM   2312 H  HB3    . ALA A 1 149 ? 13.629  16.646  1.395   1.00 45.76  ? 148 ALA A HB3    1 
ATOM   2313 N  N      . PHE A 1 150 ? 12.643  14.508  -0.340  1.00 27.68  ? 149 PHE A N      1 
ATOM   2314 C  CA     . PHE A 1 150 ? 11.491  13.743  -0.805  1.00 24.82  ? 149 PHE A CA     1 
ATOM   2315 C  C      . PHE A 1 150 ? 11.928  12.363  -1.269  1.00 25.42  ? 149 PHE A C      1 
ATOM   2316 O  O      . PHE A 1 150 ? 11.347  11.341  -0.880  1.00 26.03  ? 149 PHE A O      1 
ATOM   2317 C  CB     . PHE A 1 150 ? 10.808  14.532  -1.931  1.00 25.32  ? 149 PHE A CB     1 
ATOM   2318 C  CG     . PHE A 1 150 ? 9.508   13.937  -2.424  1.00 27.81  ? 149 PHE A CG     1 
ATOM   2319 C  CD1    . PHE A 1 150 ? 8.317   14.103  -1.711  1.00 25.37  ? 149 PHE A CD1    1 
ATOM   2320 C  CD2    . PHE A 1 150 ? 9.479   13.237  -3.624  1.00 29.07  ? 149 PHE A CD2    1 
ATOM   2321 C  CE1    . PHE A 1 150 ? 7.129   13.548  -2.181  1.00 23.15  ? 149 PHE A CE1    1 
ATOM   2322 C  CE2    . PHE A 1 150 ? 8.287   12.690  -4.116  1.00 27.95  ? 149 PHE A CE2    1 
ATOM   2323 C  CZ     . PHE A 1 150 ? 7.118   12.831  -3.402  1.00 25.94  ? 149 PHE A CZ     1 
ATOM   2324 H  H      . PHE A 1 150 ? 12.774  15.241  -0.771  1.00 33.24  ? 149 PHE A H      1 
ATOM   2325 H  HA     . PHE A 1 150 ? 10.859  13.637  -0.077  1.00 29.80  ? 149 PHE A HA     1 
ATOM   2326 H  HB2    . PHE A 1 150 ? 10.617  15.427  -1.610  1.00 30.40  ? 149 PHE A HB2    1 
ATOM   2327 H  HB3    . PHE A 1 150 ? 11.414  14.580  -2.687  1.00 30.40  ? 149 PHE A HB3    1 
ATOM   2328 H  HD1    . PHE A 1 150 ? 8.323   14.567  -0.905  1.00 30.46  ? 149 PHE A HD1    1 
ATOM   2329 H  HD2    . PHE A 1 150 ? 10.265  13.131  -4.111  1.00 34.90  ? 149 PHE A HD2    1 
ATOM   2330 H  HE1    . PHE A 1 150 ? 6.342   13.656  -1.698  1.00 27.79  ? 149 PHE A HE1    1 
ATOM   2331 H  HE2    . PHE A 1 150 ? 8.288   12.216  -4.916  1.00 33.55  ? 149 PHE A HE2    1 
ATOM   2332 H  HZ     . PHE A 1 150 ? 6.326   12.467  -3.724  1.00 31.14  ? 149 PHE A HZ     1 
ATOM   2333 N  N      . ARG A 1 151 ? 12.972  12.315  -2.092  1.00 25.68  ? 150 ARG A N      1 
ATOM   2334 C  CA     . ARG A 1 151 ? 13.473  11.033  -2.588  1.00 26.47  ? 150 ARG A CA     1 
ATOM   2335 C  C      . ARG A 1 151 ? 14.026  10.170  -1.456  1.00 24.96  ? 150 ARG A C      1 
ATOM   2336 O  O      . ARG A 1 151 ? 13.819  8.951   -1.424  1.00 27.64  ? 150 ARG A O      1 
ATOM   2337 C  CB     . ARG A 1 151 ? 14.542  11.294  -3.648  1.00 27.95  ? 150 ARG A CB     1 
ATOM   2338 C  CG     . ARG A 1 151 ? 13.923  11.886  -4.920  1.00 26.99  ? 150 ARG A CG     1 
ATOM   2339 C  CD     . ARG A 1 151 ? 14.925  12.323  -5.948  1.00 27.06  ? 150 ARG A CD     1 
ATOM   2340 N  NE     . ARG A 1 151 ? 14.245  12.938  -7.071  1.00 28.30  ? 150 ARG A NE     1 
ATOM   2341 C  CZ     . ARG A 1 151 ? 14.796  13.114  -8.263  1.00 30.96  ? 150 ARG A CZ     1 
ATOM   2342 N  NH1    . ARG A 1 151 ? 16.039  12.721  -8.489  1.00 37.10  1 150 ARG A NH1    1 
ATOM   2343 N  NH2    . ARG A 1 151 ? 14.107  13.680  -9.222  1.00 30.07  ? 150 ARG A NH2    1 
ATOM   2344 H  H      . ARG A 1 151 ? 13.404  13.002  -2.376  1.00 30.84  ? 150 ARG A H      1 
ATOM   2345 H  HA     . ARG A 1 151 ? 12.745  10.548  -3.008  1.00 31.79  ? 150 ARG A HA     1 
ATOM   2346 H  HB2    . ARG A 1 151 ? 15.190  11.926  -3.301  1.00 33.56  ? 150 ARG A HB2    1 
ATOM   2347 H  HB3    . ARG A 1 151 ? 14.976  10.458  -3.880  1.00 33.56  ? 150 ARG A HB3    1 
ATOM   2348 H  HG2    . ARG A 1 151 ? 13.353  11.217  -5.329  1.00 32.41  ? 150 ARG A HG2    1 
ATOM   2349 H  HG3    . ARG A 1 151 ? 13.394  12.662  -4.676  1.00 32.41  ? 150 ARG A HG3    1 
ATOM   2350 H  HD2    . ARG A 1 151 ? 15.529  12.974  -5.558  1.00 32.49  ? 150 ARG A HD2    1 
ATOM   2351 H  HD3    . ARG A 1 151 ? 15.418  11.552  -6.270  1.00 32.49  ? 150 ARG A HD3    1 
ATOM   2352 H  HE     . ARG A 1 151 ? 13.410  13.126  -6.982  1.00 33.98  ? 150 ARG A HE     1 
ATOM   2353 H  HH11   . ARG A 1 151 ? 16.494  12.349  -7.861  1.00 44.54  ? 150 ARG A HH11   1 
ATOM   2354 H  HH12   . ARG A 1 151 ? 16.392  12.838  -9.265  1.00 44.54  ? 150 ARG A HH12   1 
ATOM   2355 H  HH21   . ARG A 1 151 ? 13.299  13.936  -9.077  1.00 36.11  ? 150 ARG A HH21   1 
ATOM   2356 H  HH22   . ARG A 1 151 ? 14.462  13.796  -9.996  1.00 36.11  ? 150 ARG A HH22   1 
ATOM   2357 N  N      . ALA A 1 152 ? 14.749  10.776  -0.537  1.00 26.66  ? 151 ALA A N      1 
ATOM   2358 C  CA     . ALA A 1 152 ? 15.250  10.033  0.621   1.00 33.02  ? 151 ALA A CA     1 
ATOM   2359 C  C      . ALA A 1 152 ? 14.113  9.434   1.445   1.00 30.65  ? 151 ALA A C      1 
ATOM   2360 O  O      . ALA A 1 152 ? 14.206  8.293   1.909   1.00 31.09  ? 151 ALA A O      1 
ATOM   2361 C  CB     . ALA A 1 152 ? 16.117  10.947  1.477   1.00 40.07  ? 151 ALA A CB     1 
ATOM   2362 H  H      . ALA A 1 152 ? 14.967  11.608  -0.551  1.00 32.01  ? 151 ALA A H      1 
ATOM   2363 H  HA     . ALA A 1 152 ? 15.807  9.302   0.308   1.00 39.65  ? 151 ALA A HA     1 
ATOM   2364 H  HB1    . ALA A 1 152 ? 16.444  10.447  2.241   1.00 48.10  ? 151 ALA A HB1    1 
ATOM   2365 H  HB2    . ALA A 1 152 ? 16.863  11.264  0.944   1.00 48.10  ? 151 ALA A HB2    1 
ATOM   2366 H  HB3    . ALA A 1 152 ? 15.581  11.698  1.777   1.00 48.10  ? 151 ALA A HB3    1 
ATOM   2367 N  N      . SER A 1 153 ? 13.026  10.182  1.629   1.00 28.86  ? 152 SER A N      1 
ATOM   2368 C  CA     . SER A 1 153 ? 11.903  9.673   2.410   1.00 31.21  ? 152 SER A CA     1 
ATOM   2369 C  C      . SER A 1 153 ? 11.230  8.489   1.710   1.00 29.82  ? 152 SER A C      1 
ATOM   2370 O  O      . SER A 1 153 ? 10.950  7.464   2.349   1.00 29.30  ? 152 SER A O      1 
ATOM   2371 C  CB     . SER A 1 153 ? 10.908  10.804  2.677   1.00 34.30  ? 152 SER A CB     1 
ATOM   2372 O  OG     . SER A 1 153 ? 9.891   10.402  3.588   1.00 35.44  ? 152 SER A OG     1 
ATOM   2373 H  H      . SER A 1 153 ? 12.915  10.975  1.317   1.00 34.65  ? 152 SER A H      1 
ATOM   2374 H  HA     . SER A 1 153 ? 12.234  9.361   3.267   1.00 37.48  ? 152 SER A HA     1 
ATOM   2375 H  HB2    . SER A 1 153 ? 11.386  11.559  3.055   1.00 41.18  ? 152 SER A HB2    1 
ATOM   2376 H  HB3    . SER A 1 153 ? 10.494  11.061  1.839   1.00 41.18  ? 152 SER A HB3    1 
ATOM   2377 H  HG     . SER A 1 153 ? 10.234  10.177  4.321   1.00 42.54  ? 152 SER A HG     1 
ATOM   2378 N  N      . LEU A 1 154 ? 10.951  8.615   0.405   1.00 27.43  ? 153 LEU A N      1 
ATOM   2379 C  CA     . LEU A 1 154 ? 10.433  7.482   -0.362  1.00 25.71  ? 153 LEU A CA     1 
ATOM   2380 C  C      . LEU A 1 154 ? 11.347  6.265   -0.247  1.00 25.53  ? 153 LEU A C      1 
ATOM   2381 O  O      . LEU A 1 154 ? 10.866  5.129   -0.170  1.00 25.79  ? 153 LEU A O      1 
ATOM   2382 C  CB     . LEU A 1 154 ? 10.247  7.844   -1.847  1.00 24.84  ? 153 LEU A CB     1 
ATOM   2383 C  CG     . LEU A 1 154 ? 9.213   8.905   -2.229  1.00 26.22  ? 153 LEU A CG     1 
ATOM   2384 C  CD1    . LEU A 1 154 ? 9.147   9.081   -3.772  1.00 31.23  ? 153 LEU A CD1    1 
ATOM   2385 C  CD2    . LEU A 1 154 ? 7.841   8.574   -1.646  1.00 25.09  ? 153 LEU A CD2    1 
ATOM   2386 H  H      . LEU A 1 154 ? 11.053  9.337   -0.052  1.00 32.93  ? 153 LEU A H      1 
ATOM   2387 H  HA     . LEU A 1 154 ? 9.565   7.235   -0.006  1.00 30.87  ? 153 LEU A HA     1 
ATOM   2388 H  HB2    . LEU A 1 154 ? 11.102  8.156   -2.183  1.00 29.82  ? 153 LEU A HB2    1 
ATOM   2389 H  HB3    . LEU A 1 154 ? 10.001  7.033   -2.319  1.00 29.82  ? 153 LEU A HB3    1 
ATOM   2390 H  HG     . LEU A 1 154 ? 9.491   9.754   -1.852  1.00 31.49  ? 153 LEU A HG     1 
ATOM   2391 H  HD11   . LEU A 1 154 ? 8.485   9.757   -3.984  1.00 37.50  ? 153 LEU A HD11   1 
ATOM   2392 H  HD12   . LEU A 1 154 ? 10.018  9.357   -4.095  1.00 37.50  ? 153 LEU A HD12   1 
ATOM   2393 H  HD13   . LEU A 1 154 ? 8.897   8.235   -4.176  1.00 37.50  ? 153 LEU A HD13   1 
ATOM   2394 H  HD21   . LEU A 1 154 ? 7.212   9.265   -1.908  1.00 30.13  ? 153 LEU A HD21   1 
ATOM   2395 H  HD22   . LEU A 1 154 ? 7.551   7.715   -1.991  1.00 30.13  ? 153 LEU A HD22   1 
ATOM   2396 H  HD23   . LEU A 1 154 ? 7.910   8.537   -0.680  1.00 30.13  ? 153 LEU A HD23   1 
ATOM   2397 N  N      . SER A 1 155 ? 12.665  6.475   -0.276  1.00 27.37  ? 154 SER A N      1 
ATOM   2398 C  CA     . SER A 1 155 ? 13.610  5.353   -0.233  1.00 28.67  ? 154 SER A CA     1 
ATOM   2399 C  C      . SER A 1 155 ? 13.574  4.596   1.098   1.00 31.06  ? 154 SER A C      1 
ATOM   2400 O  O      . SER A 1 155 ? 13.946  3.418   1.150   1.00 33.76  ? 154 SER A O      1 
ATOM   2401 C  CB     . SER A 1 155 ? 15.019  5.872   -0.508  1.00 31.69  ? 154 SER A CB     1 
ATOM   2402 O  OG     . SER A 1 155 ? 15.067  6.482   -1.814  1.00 33.34  ? 154 SER A OG     1 
ATOM   2403 H  H      . SER A 1 155 ? 13.037  7.249   -0.321  1.00 32.87  ? 154 SER A H      1 
ATOM   2404 H  HA     . SER A 1 155 ? 13.382  4.725   -0.936  1.00 34.42  ? 154 SER A HA     1 
ATOM   2405 H  HB2    . SER A 1 155 ? 15.252  6.533   0.162   1.00 38.04  ? 154 SER A HB2    1 
ATOM   2406 H  HB3    . SER A 1 155 ? 15.643  5.130   -0.479  1.00 38.04  ? 154 SER A HB3    1 
ATOM   2407 H  HG     . SER A 1 155 ? 14.526  7.124   -1.852  1.00 40.03  ? 154 SER A HG     1 
ATOM   2408 N  N      . LYS A 1 156 ? 13.130  5.243   2.163   1.00 27.14  ? 155 LYS A N      1 
ATOM   2409 C  CA     . LYS A 1 156 ? 13.046  4.588   3.461   1.00 29.40  ? 155 LYS A CA     1 
ATOM   2410 C  C      . LYS A 1 156 ? 11.902  3.594   3.536   1.00 28.25  ? 155 LYS A C      1 
ATOM   2411 O  O      . LYS A 1 156 ? 11.872  2.784   4.469   1.00 27.26  ? 155 LYS A O      1 
ATOM   2412 C  CB     . LYS A 1 156 ? 12.870  5.636   4.556   1.00 31.24  ? 155 LYS A CB     1 
ATOM   2413 C  CG     . LYS A 1 156 ? 14.153  6.354   4.892   1.00 39.38  ? 155 LYS A CG     1 
ATOM   2414 C  CD     . LYS A 1 156 ? 13.955  7.306   6.044   1.00 51.49  ? 155 LYS A CD     1 
ATOM   2415 C  CE     . LYS A 1 156 ? 15.222  8.057   6.375   1.00 65.31  ? 155 LYS A CE     1 
ATOM   2416 N  NZ     . LYS A 1 156 ? 14.996  9.028   7.489   1.00 74.80  1 155 LYS A NZ     1 
ATOM   2417 H  H      . LYS A 1 156 ? 12.870  6.063   2.164   1.00 32.59  ? 155 LYS A H      1 
ATOM   2418 H  HA     . LYS A 1 156 ? 13.872  4.110   3.630   1.00 35.30  ? 155 LYS A HA     1 
ATOM   2419 H  HB2    . LYS A 1 156 ? 12.225  6.297   4.260   1.00 37.50  ? 155 LYS A HB2    1 
ATOM   2420 H  HB3    . LYS A 1 156 ? 12.552  5.200   5.362   1.00 37.50  ? 155 LYS A HB3    1 
ATOM   2421 H  HG2    . LYS A 1 156 ? 14.829  5.705   5.145   1.00 47.28  ? 155 LYS A HG2    1 
ATOM   2422 H  HG3    . LYS A 1 156 ? 14.448  6.864   4.121   1.00 47.28  ? 155 LYS A HG3    1 
ATOM   2423 H  HD2    . LYS A 1 156 ? 13.272  7.954   5.810   1.00 61.81  ? 155 LYS A HD2    1 
ATOM   2424 H  HD3    . LYS A 1 156 ? 13.686  6.805   6.830   1.00 61.81  ? 155 LYS A HD3    1 
ATOM   2425 H  HE2    . LYS A 1 156 ? 15.905  7.427   6.653   1.00 78.39  ? 155 LYS A HE2    1 
ATOM   2426 H  HE3    . LYS A 1 156 ? 15.516  8.551   5.594   1.00 78.39  ? 155 LYS A HE3    1 
ATOM   2427 H  HZ1    . LYS A 1 156 ? 15.751  9.462   7.672   1.00 89.78  ? 155 LYS A HZ1    1 
ATOM   2428 H  HZ2    . LYS A 1 156 ? 14.372  9.618   7.256   1.00 89.78  ? 155 LYS A HZ2    1 
ATOM   2429 H  HZ3    . LYS A 1 156 ? 14.726  8.596   8.219   1.00 89.78  ? 155 LYS A HZ3    1 
ATOM   2430 N  N      . LEU A 1 157 ? 10.951  3.663   2.604   1.00 27.07  ? 156 LEU A N      1 
ATOM   2431 C  CA     . LEU A 1 157 ? 9.707   2.923   2.750   1.00 30.56  ? 156 LEU A CA     1 
ATOM   2432 C  C      . LEU A 1 157 ? 9.805   1.484   2.274   1.00 30.81  ? 156 LEU A C      1 
ATOM   2433 O  O      . LEU A 1 157 ? 8.855   0.721   2.475   1.00 30.21  ? 156 LEU A O      1 
ATOM   2434 C  CB     . LEU A 1 157 ? 8.591   3.641   2.008   1.00 29.68  ? 156 LEU A CB     1 
ATOM   2435 C  CG     . LEU A 1 157 ? 8.449   5.122   2.400   1.00 29.42  ? 156 LEU A CG     1 
ATOM   2436 C  CD1    . LEU A 1 157 ? 7.275   5.692   1.609   1.00 31.73  ? 156 LEU A CD1    1 
ATOM   2437 C  CD2    . LEU A 1 157 ? 8.262   5.391   3.901   1.00 28.95  ? 156 LEU A CD2    1 
ATOM   2438 H  H      . LEU A 1 157 ? 11.005  4.129   1.884   1.00 32.51  ? 156 LEU A H      1 
ATOM   2439 H  HA     . LEU A 1 157 ? 9.468   2.903   3.690   1.00 36.69  ? 156 LEU A HA     1 
ATOM   2440 H  HB2    . LEU A 1 157 ? 8.771   3.601   1.056   1.00 35.63  ? 156 LEU A HB2    1 
ATOM   2441 H  HB3    . LEU A 1 157 ? 7.750   3.200   2.204   1.00 35.63  ? 156 LEU A HB3    1 
ATOM   2442 H  HG     . LEU A 1 157 ? 9.249   5.594   2.117   1.00 35.33  ? 156 LEU A HG     1 
ATOM   2443 H  HD11   . LEU A 1 157 ? 7.165   6.628   1.839   1.00 38.10  ? 156 LEU A HD11   1 
ATOM   2444 H  HD12   . LEU A 1 157 ? 7.461   5.604   0.661   1.00 38.10  ? 156 LEU A HD12   1 
ATOM   2445 H  HD13   . LEU A 1 157 ? 6.472   5.198   1.837   1.00 38.10  ? 156 LEU A HD13   1 
ATOM   2446 H  HD21   . LEU A 1 157 ? 8.183   6.347   4.042   1.00 34.76  ? 156 LEU A HD21   1 
ATOM   2447 H  HD22   . LEU A 1 157 ? 7.456   4.944   4.203   1.00 34.76  ? 156 LEU A HD22   1 
ATOM   2448 H  HD23   . LEU A 1 157 ? 9.031   5.047   4.381   1.00 34.76  ? 156 LEU A HD23   1 
ATOM   2449 N  N      . GLY A 1 158 ? 10.946  1.085   1.721   1.00 30.38  ? 157 GLY A N      1 
ATOM   2450 C  CA     . GLY A 1 158 ? 11.162  -0.295  1.343   1.00 32.25  ? 157 GLY A CA     1 
ATOM   2451 C  C      . GLY A 1 158 ? 12.638  -0.621  1.400   1.00 28.28  ? 157 GLY A C      1 
ATOM   2452 O  O      . GLY A 1 158 ? 13.491  0.257   1.529   1.00 29.47  ? 157 GLY A O      1 
ATOM   2453 H  H      . GLY A 1 158 ? 11.612  1.603   1.555   1.00 36.47  ? 157 GLY A H      1 
ATOM   2454 H  HA2    . GLY A 1 158 ? 10.686  -0.883  1.950   1.00 38.72  ? 157 GLY A HA2    1 
ATOM   2455 H  HA3    . GLY A 1 158 ? 10.841  -0.446  0.440   1.00 38.72  ? 157 GLY A HA3    1 
ATOM   2456 N  N      . ASP A 1 159 ? 12.923  -1.911  1.309   1.00 24.54  ? 158 ASP A N      1 
ATOM   2457 C  CA     . ASP A 1 159 ? 14.286  -2.413  1.192   1.00 25.47  ? 158 ASP A CA     1 
ATOM   2458 C  C      . ASP A 1 159 ? 14.714  -2.615  -0.265  1.00 26.45  ? 158 ASP A C      1 
ATOM   2459 O  O      . ASP A 1 159 ? 15.914  -2.554  -0.574  1.00 26.91  ? 158 ASP A O      1 
ATOM   2460 C  CB     . ASP A 1 159 ? 14.392  -3.741  1.930   1.00 27.80  ? 158 ASP A CB     1 
ATOM   2461 C  CG     . ASP A 1 159 ? 13.970  -3.641  3.419   1.00 34.49  ? 158 ASP A CG     1 
ATOM   2462 O  OD1    . ASP A 1 159 ? 14.428  -2.716  4.138   1.00 35.19  ? 158 ASP A OD1    1 
ATOM   2463 O  OD2    . ASP A 1 159 ? 13.181  -4.505  3.870   1.00 34.91  1 158 ASP A OD2    1 
ATOM   2464 H  H      . ASP A 1 159 ? 12.328  -2.533  1.312   1.00 29.47  ? 158 ASP A H      1 
ATOM   2465 H  HA     . ASP A 1 159 ? 14.897  -1.784  1.606   1.00 30.58  ? 158 ASP A HA     1 
ATOM   2466 H  HB2    . ASP A 1 159 ? 13.813  -4.389  1.498   1.00 33.38  ? 158 ASP A HB2    1 
ATOM   2467 H  HB3    . ASP A 1 159 ? 15.312  -4.046  1.899   1.00 33.38  ? 158 ASP A HB3    1 
ATOM   2468 N  N      . VAL A 1 160 ? 13.749  -2.888  -1.141  1.00 23.82  ? 159 VAL A N      1 
ATOM   2469 C  CA     . VAL A 1 160 ? 13.961  -3.090  -2.569  1.00 23.50  ? 159 VAL A CA     1 
ATOM   2470 C  C      . VAL A 1 160 ? 12.852  -2.325  -3.266  1.00 21.73  ? 159 VAL A C      1 
ATOM   2471 O  O      . VAL A 1 160 ? 11.799  -2.082  -2.675  1.00 22.85  ? 159 VAL A O      1 
ATOM   2472 C  CB     . VAL A 1 160 ? 13.950  -4.590  -2.961  1.00 29.12  ? 159 VAL A CB     1 
ATOM   2473 C  CG1    . VAL A 1 160 ? 15.087  -5.332  -2.322  1.00 34.84  ? 159 VAL A CG1    1 
ATOM   2474 C  CG2    . VAL A 1 160 ? 12.642  -5.242  -2.592  1.00 32.78  ? 159 VAL A CG2    1 
ATOM   2475 H  H      . VAL A 1 160 ? 12.923  -2.963  -0.916  1.00 28.60  ? 159 VAL A H      1 
ATOM   2476 H  HA     . VAL A 1 160 ? 14.813  -2.707  -2.830  1.00 28.22  ? 159 VAL A HA     1 
ATOM   2477 H  HB     . VAL A 1 160 ? 14.055  -4.661  -3.923  1.00 34.97  ? 159 VAL A HB     1 
ATOM   2478 H  HG11   . VAL A 1 160 ? 15.046  -6.264  -2.590  1.00 41.83  ? 159 VAL A HG11   1 
ATOM   2479 H  HG12   . VAL A 1 160 ? 15.925  -4.940  -2.614  1.00 41.83  ? 159 VAL A HG12   1 
ATOM   2480 H  HG13   . VAL A 1 160 ? 15.007  -5.262  -1.358  1.00 41.83  ? 159 VAL A HG13   1 
ATOM   2481 H  HG21   . VAL A 1 160 ? 12.670  -6.176  -2.851  1.00 39.35  ? 159 VAL A HG21   1 
ATOM   2482 H  HG22   . VAL A 1 160 ? 12.512  -5.168  -1.633  1.00 39.35  ? 159 VAL A HG22   1 
ATOM   2483 H  HG23   . VAL A 1 160 ? 11.921  -4.791  -3.059  1.00 39.35  ? 159 VAL A HG23   1 
ATOM   2484 N  N      . TYR A 1 161 ? 13.102  -1.928  -4.520  1.00 20.97  ? 160 TYR A N      1 
ATOM   2485 C  CA     . TYR A 1 161 ? 12.194  -1.099  -5.309  1.00 20.15  ? 160 TYR A CA     1 
ATOM   2486 C  C      . TYR A 1 161 ? 11.773  -1.845  -6.558  1.00 19.23  ? 160 TYR A C      1 
ATOM   2487 O  O      . TYR A 1 161 ? 12.590  -2.492  -7.219  1.00 19.27  ? 160 TYR A O      1 
ATOM   2488 C  CB     . TYR A 1 161 ? 12.880  0.212   -5.701  1.00 21.22  ? 160 TYR A CB     1 
ATOM   2489 C  CG     . TYR A 1 161 ? 12.225  1.110   -6.713  1.00 20.49  ? 160 TYR A CG     1 
ATOM   2490 C  CD1    . TYR A 1 161 ? 11.218  1.973   -6.347  1.00 20.65  ? 160 TYR A CD1    1 
ATOM   2491 C  CD2    . TYR A 1 161 ? 12.668  1.143   -8.037  1.00 20.35  ? 160 TYR A CD2    1 
ATOM   2492 C  CE1    . TYR A 1 161 ? 10.657  2.836   -7.254  1.00 21.01  ? 160 TYR A CE1    1 
ATOM   2493 C  CE2    . TYR A 1 161 ? 12.080  2.004   -8.978  1.00 21.38  ? 160 TYR A CE2    1 
ATOM   2494 C  CZ     . TYR A 1 161 ? 11.092  2.844   -8.572  1.00 23.01  ? 160 TYR A CZ     1 
ATOM   2495 O  OH     . TYR A 1 161 ? 10.558  3.713   -9.500  1.00 24.86  ? 160 TYR A OH     1 
ATOM   2496 H  H      . TYR A 1 161 ? 13.819  -2.137  -4.946  1.00 25.19  ? 160 TYR A H      1 
ATOM   2497 H  HA     . TYR A 1 161 ? 11.403  -0.893  -4.787  1.00 24.20  ? 160 TYR A HA     1 
ATOM   2498 H  HB2    . TYR A 1 161 ? 12.991  0.739   -4.894  1.00 25.49  ? 160 TYR A HB2    1 
ATOM   2499 H  HB3    . TYR A 1 161 ? 13.757  -0.009  -6.053  1.00 25.49  ? 160 TYR A HB3    1 
ATOM   2500 H  HD1    . TYR A 1 161 ? 10.924  1.984   -5.465  1.00 24.80  ? 160 TYR A HD1    1 
ATOM   2501 H  HD2    . TYR A 1 161 ? 13.351  0.571   -8.305  1.00 24.44  ? 160 TYR A HD2    1 
ATOM   2502 H  HE1    . TYR A 1 161 ? 9.975   3.410   -6.987  1.00 25.24  ? 160 TYR A HE1    1 
ATOM   2503 H  HE2    . TYR A 1 161 ? 12.384  2.022   -9.857  1.00 25.67  ? 160 TYR A HE2    1 
ATOM   2504 H  HH     . TYR A 1 161 ? 9.971   4.192   -9.139  1.00 29.85  ? 160 TYR A HH     1 
ATOM   2505 N  N      . VAL A 1 162 ? 10.495  -1.743  -6.879  1.00 18.08  ? 161 VAL A N      1 
ATOM   2506 C  CA     . VAL A 1 162 ? 9.958   -2.278  -8.126  1.00 18.45  ? 161 VAL A CA     1 
ATOM   2507 C  C      . VAL A 1 162 ? 9.249   -1.142  -8.817  1.00 18.45  ? 161 VAL A C      1 
ATOM   2508 O  O      . VAL A 1 162 ? 8.477   -0.420  -8.184  1.00 19.10  ? 161 VAL A O      1 
ATOM   2509 C  CB     . VAL A 1 162 ? 8.986   -3.444  -7.863  1.00 22.98  ? 161 VAL A CB     1 
ATOM   2510 C  CG1    . VAL A 1 162 ? 8.347   -3.977  -9.162  1.00 25.01  ? 161 VAL A CG1    1 
ATOM   2511 C  CG2    . VAL A 1 162 ? 9.697   -4.584  -7.079  1.00 24.29  ? 161 VAL A CG2    1 
ATOM   2512 H  H      . VAL A 1 162 ? 9.904   -1.361  -6.385  1.00 21.71  ? 161 VAL A H      1 
ATOM   2513 H  HA     . VAL A 1 162 ? 10.681  -2.590  -8.692  1.00 22.16  ? 161 VAL A HA     1 
ATOM   2514 H  HB     . VAL A 1 162 ? 8.265   -3.117  -7.303  1.00 27.59  ? 161 VAL A HB     1 
ATOM   2515 H  HG11   . VAL A 1 162 ? 7.747   -4.707  -8.942  1.00 30.03  ? 161 VAL A HG11   1 
ATOM   2516 H  HG12   . VAL A 1 162 ? 7.854   -3.259  -9.588  1.00 30.03  ? 161 VAL A HG12   1 
ATOM   2517 H  HG13   . VAL A 1 162 ? 9.050   -4.292  -9.752  1.00 30.03  ? 161 VAL A HG13   1 
ATOM   2518 H  HG21   . VAL A 1 162 ? 9.064   -5.304  -6.927  1.00 29.17  ? 161 VAL A HG21   1 
ATOM   2519 H  HG22   . VAL A 1 162 ? 10.447  -4.907  -7.602  1.00 29.17  ? 161 VAL A HG22   1 
ATOM   2520 H  HG23   . VAL A 1 162 ? 10.011  -4.234  -6.230  1.00 29.17  ? 161 VAL A HG23   1 
ATOM   2521 N  N      . ASN A 1 163 ? 9.472   -0.999  -10.123 1.00 18.56  ? 162 ASN A N      1 
ATOM   2522 C  CA     . ASN A 1 163 ? 8.675   -0.074  -10.920 1.00 19.12  ? 162 ASN A CA     1 
ATOM   2523 C  C      . ASN A 1 163 ? 7.793   -0.885  -11.865 1.00 18.19  ? 162 ASN A C      1 
ATOM   2524 O  O      . ASN A 1 163 ? 8.296   -1.566  -12.771 1.00 18.13  ? 162 ASN A O      1 
ATOM   2525 C  CB     . ASN A 1 163 ? 9.573   0.878   -11.682 1.00 22.54  ? 162 ASN A CB     1 
ATOM   2526 C  CG     . ASN A 1 163 ? 8.811   2.070   -12.210 1.00 25.40  ? 162 ASN A CG     1 
ATOM   2527 O  OD1    . ASN A 1 163 ? 7.655   1.954   -12.617 1.00 22.40  ? 162 ASN A OD1    1 
ATOM   2528 N  ND2    . ASN A 1 163 ? 9.457   3.231   -12.184 1.00 28.65  ? 162 ASN A ND2    1 
ATOM   2529 H  H      . ASN A 1 163 ? 10.074  -1.423  -10.566 1.00 22.29  ? 162 ASN A H      1 
ATOM   2530 H  HA     . ASN A 1 163 ? 8.102   0.446   -10.335 1.00 22.97  ? 162 ASN A HA     1 
ATOM   2531 H  HB2    . ASN A 1 163 ? 10.269  1.202   -11.090 1.00 27.07  ? 162 ASN A HB2    1 
ATOM   2532 H  HB3    . ASN A 1 163 ? 9.965   0.411   -12.436 1.00 27.07  ? 162 ASN A HB3    1 
ATOM   2533 H  HD21   . ASN A 1 163 ? 9.071   3.943   -12.472 1.00 34.40  ? 162 ASN A HD21   1 
ATOM   2534 H  HD22   . ASN A 1 163 ? 10.260  3.269   -11.879 1.00 34.40  ? 162 ASN A HD22   1 
ATOM   2535 N  N      . ASP A 1 164 ? 6.486   -0.853  -11.616 1.00 18.08  ? 163 ASP A N      1 
ATOM   2536 C  CA     . ASP A 1 164 ? 5.523   -1.458  -12.522 1.00 20.28  ? 163 ASP A CA     1 
ATOM   2537 C  C      . ASP A 1 164 ? 4.669   -0.411  -13.223 1.00 20.08  ? 163 ASP A C      1 
ATOM   2538 O  O      . ASP A 1 164 ? 3.632   -0.750  -13.804 1.00 20.63  ? 163 ASP A O      1 
ATOM   2539 C  CB     . ASP A 1 164 ? 4.619   -2.455  -11.798 1.00 22.78  ? 163 ASP A CB     1 
ATOM   2540 C  CG     . ASP A 1 164 ? 4.367   -3.719  -12.621 1.00 27.60  ? 163 ASP A CG     1 
ATOM   2541 O  OD1    . ASP A 1 164 ? 5.113   -3.959  -13.601 1.00 28.96  ? 163 ASP A OD1    1 
ATOM   2542 O  OD2    . ASP A 1 164 ? 3.396   -4.445  -12.313 1.00 30.20  1 163 ASP A OD2    1 
ATOM   2543 H  H      . ASP A 1 164 ? 6.133   -0.484  -10.925 1.00 21.71  ? 163 ASP A H      1 
ATOM   2544 H  HA     . ASP A 1 164 ? 6.008   -1.945  -13.206 1.00 24.35  ? 163 ASP A HA     1 
ATOM   2545 H  HB2    . ASP A 1 164 ? 5.040   -2.717  -10.965 1.00 27.35  ? 163 ASP A HB2    1 
ATOM   2546 H  HB3    . ASP A 1 164 ? 3.763   -2.035  -11.621 1.00 27.35  ? 163 ASP A HB3    1 
ATOM   2547 N  N      . ALA A 1 165 ? 5.074   0.857   -13.188 1.00 16.73  ? 164 ALA A N      1 
ATOM   2548 C  CA     . ALA A 1 165 ? 4.219   1.949   -13.648 1.00 17.24  ? 164 ALA A CA     1 
ATOM   2549 C  C      . ALA A 1 165 ? 4.478   2.230   -15.133 1.00 18.82  ? 164 ALA A C      1 
ATOM   2550 O  O      . ALA A 1 165 ? 4.990   3.266   -15.531 1.00 17.71  ? 164 ALA A O      1 
ATOM   2551 C  CB     . ALA A 1 165 ? 4.455   3.188   -12.789 1.00 16.88  ? 164 ALA A CB     1 
ATOM   2552 H  H      . ALA A 1 165 ? 5.844   1.113   -12.901 1.00 20.10  ? 164 ALA A H      1 
ATOM   2553 H  HA     . ALA A 1 165 ? 3.290   1.687   -13.549 1.00 20.71  ? 164 ALA A HA     1 
ATOM   2554 H  HB1    . ALA A 1 165 ? 3.881   3.904   -13.105 1.00 20.27  ? 164 ALA A HB1    1 
ATOM   2555 H  HB2    . ALA A 1 165 ? 4.244   2.977   -11.866 1.00 20.27  ? 164 ALA A HB2    1 
ATOM   2556 H  HB3    . ALA A 1 165 ? 5.385   3.452   -12.865 1.00 20.27  ? 164 ALA A HB3    1 
ATOM   2557 N  N      . PHE A 1 166 ? 4.089   1.277   -15.978 1.00 19.33  ? 165 PHE A N      1 
ATOM   2558 C  CA     . PHE A 1 166 ? 4.345   1.474   -17.408 1.00 17.29  ? 165 PHE A CA     1 
ATOM   2559 C  C      . PHE A 1 166 ? 3.728   2.769   -17.910 1.00 18.06  ? 165 PHE A C      1 
ATOM   2560 O  O      . PHE A 1 166 ? 4.356   3.516   -18.675 1.00 21.69  ? 165 PHE A O      1 
ATOM   2561 C  CB     . PHE A 1 166 ? 3.836   0.284   -18.225 1.00 17.25  ? 165 PHE A CB     1 
ATOM   2562 C  CG     . PHE A 1 166 ? 4.012   0.488   -19.712 1.00 17.36  ? 165 PHE A CG     1 
ATOM   2563 C  CD1    . PHE A 1 166 ? 5.283   0.416   -20.299 1.00 20.01  ? 165 PHE A CD1    1 
ATOM   2564 C  CD2    . PHE A 1 166 ? 2.926   0.791   -20.517 1.00 20.01  ? 165 PHE A CD2    1 
ATOM   2565 C  CE1    . PHE A 1 166 ? 5.450   0.624   -21.663 1.00 21.37  ? 165 PHE A CE1    1 
ATOM   2566 C  CE2    . PHE A 1 166 ? 3.090   1.002   -21.904 1.00 22.22  ? 165 PHE A CE2    1 
ATOM   2567 C  CZ     . PHE A 1 166 ? 4.348   0.920   -22.459 1.00 21.85  ? 165 PHE A CZ     1 
ATOM   2568 H  H      . PHE A 1 166 ? 3.695   0.543   -15.767 1.00 23.22  ? 165 PHE A H      1 
ATOM   2569 H  HA     . PHE A 1 166 ? 5.303   1.534   -17.545 1.00 20.76  ? 165 PHE A HA     1 
ATOM   2570 H  HB2    . PHE A 1 166 ? 4.331   -0.510  -17.970 1.00 20.72  ? 165 PHE A HB2    1 
ATOM   2571 H  HB3    . PHE A 1 166 ? 2.891   0.159   -18.049 1.00 20.72  ? 165 PHE A HB3    1 
ATOM   2572 H  HD1    . PHE A 1 166 ? 6.022   0.221   -19.770 1.00 24.03  ? 165 PHE A HD1    1 
ATOM   2573 H  HD2    . PHE A 1 166 ? 2.077   0.849   -20.140 1.00 24.03  ? 165 PHE A HD2    1 
ATOM   2574 H  HE1    . PHE A 1 166 ? 6.297   0.567   -22.042 1.00 25.66  ? 165 PHE A HE1    1 
ATOM   2575 H  HE2    . PHE A 1 166 ? 2.354   1.198   -22.438 1.00 26.68  ? 165 PHE A HE2    1 
ATOM   2576 H  HZ     . PHE A 1 166 ? 4.460   1.054   -23.373 1.00 26.24  ? 165 PHE A HZ     1 
ATOM   2577 N  N      . GLY A 1 167 ? 2.502   3.061   -17.487 1.00 19.39  ? 166 GLY A N      1 
ATOM   2578 C  CA     . GLY A 1 167 ? 1.819   4.240   -17.965 1.00 19.18  ? 166 GLY A CA     1 
ATOM   2579 C  C      . GLY A 1 167 ? 2.494   5.543   -17.611 1.00 19.89  ? 166 GLY A C      1 
ATOM   2580 O  O      . GLY A 1 167 ? 2.176   6.571   -18.205 1.00 18.53  ? 166 GLY A O      1 
ATOM   2581 H  H      . GLY A 1 167 ? 2.051   2.591   -16.925 1.00 23.29  ? 166 GLY A H      1 
ATOM   2582 H  HA2    . GLY A 1 167 ? 1.746   4.193   -18.932 1.00 23.04  ? 166 GLY A HA2    1 
ATOM   2583 H  HA3    . GLY A 1 167 ? 0.922   4.257   -17.596 1.00 23.04  ? 166 GLY A HA3    1 
ATOM   2584 N  N      . THR A 1 168 ? 3.402   5.535   -16.641 1.00 19.18  ? 167 THR A N      1 
ATOM   2585 C  CA     . THR A 1 168 ? 4.113   6.738   -16.227 1.00 16.68  ? 167 THR A CA     1 
ATOM   2586 C  C      . THR A 1 168 ? 5.581   6.687   -16.609 1.00 16.69  ? 167 THR A C      1 
ATOM   2587 O  O      . THR A 1 168 ? 6.327   7.605   -16.273 1.00 19.14  ? 167 THR A O      1 
ATOM   2588 C  CB     . THR A 1 168 ? 3.950   6.926   -14.698 1.00 19.32  ? 167 THR A CB     1 
ATOM   2589 O  OG1    . THR A 1 168 ? 2.559   6.782   -14.385 1.00 21.90  ? 167 THR A OG1    1 
ATOM   2590 C  CG2    . THR A 1 168 ? 4.386   8.278   -14.252 1.00 19.27  ? 167 THR A CG2    1 
ATOM   2591 H  H      . THR A 1 168 ? 3.626   4.833   -16.199 1.00 23.04  ? 167 THR A H      1 
ATOM   2592 H  HA     . THR A 1 168 ? 3.716   7.506   -16.667 1.00 20.03  ? 167 THR A HA     1 
ATOM   2593 H  HB     . THR A 1 168 ? 4.467   6.255   -14.225 1.00 23.20  ? 167 THR A HB     1 
ATOM   2594 H  HG1    . THR A 1 168 ? 2.438   6.879   -13.560 1.00 26.30  ? 167 THR A HG1    1 
ATOM   2595 H  HG21   . THR A 1 168 ? 4.272   8.363   -13.292 1.00 23.14  ? 167 THR A HG21   1 
ATOM   2596 H  HG22   . THR A 1 168 ? 5.321   8.414   -14.471 1.00 23.14  ? 167 THR A HG22   1 
ATOM   2597 H  HG23   . THR A 1 168 ? 3.856   8.960   -14.694 1.00 23.14  ? 167 THR A HG23   1 
ATOM   2598 N  N      . ALA A 1 169 ? 6.016   5.630   -17.290 1.00 18.45  ? 168 ALA A N      1 
ATOM   2599 C  CA     . ALA A 1 169 ? 7.451   5.383   -17.427 1.00 21.22  ? 168 ALA A CA     1 
ATOM   2600 C  C      . ALA A 1 169 ? 8.153   6.402   -18.308 1.00 21.74  ? 168 ALA A C      1 
ATOM   2601 O  O      . ALA A 1 169 ? 9.387   6.448   -18.298 1.00 20.90  ? 168 ALA A O      1 
ATOM   2602 C  CB     . ALA A 1 169 ? 7.690   3.976   -17.951 1.00 23.95  ? 168 ALA A CB     1 
ATOM   2603 H  H      . ALA A 1 169 ? 5.512   5.050   -17.677 1.00 22.16  ? 168 ALA A H      1 
ATOM   2604 H  HA     . ALA A 1 169 ? 7.854   5.436   -16.546 1.00 25.48  ? 168 ALA A HA     1 
ATOM   2605 H  HB1    . ALA A 1 169 ? 8.645   3.829   -18.036 1.00 28.76  ? 168 ALA A HB1    1 
ATOM   2606 H  HB2    . ALA A 1 169 ? 7.310   3.337   -17.327 1.00 28.76  ? 168 ALA A HB2    1 
ATOM   2607 H  HB3    . ALA A 1 169 ? 7.263   3.885   -18.818 1.00 28.76  ? 168 ALA A HB3    1 
ATOM   2608 N  N      . HIS A 1 170 ? 7.411   7.233   -19.034 1.00 20.73  ? 169 HIS A N      1 
ATOM   2609 C  CA     . HIS A 1 170 ? 8.008   8.329   -19.786 1.00 20.62  ? 169 HIS A CA     1 
ATOM   2610 C  C      . HIS A 1 170 ? 8.322   9.560   -18.944 1.00 19.77  ? 169 HIS A C      1 
ATOM   2611 O  O      . HIS A 1 170 ? 8.921   10.525  -19.480 1.00 20.59  ? 169 HIS A O      1 
ATOM   2612 C  CB     . HIS A 1 170 ? 7.103   8.734   -20.952 1.00 20.31  ? 169 HIS A CB     1 
ATOM   2613 C  CG     . HIS A 1 170 ? 5.706   9.112   -20.560 1.00 19.70  ? 169 HIS A CG     1 
ATOM   2614 N  ND1    . HIS A 1 170 ? 4.950   8.398   -19.655 1.00 20.35  ? 169 HIS A ND1    1 
ATOM   2615 C  CD2    . HIS A 1 170 ? 4.904   10.098  -21.028 1.00 22.08  ? 169 HIS A CD2    1 
ATOM   2616 C  CE1    . HIS A 1 170 ? 3.750   8.941   -19.565 1.00 21.27  ? 169 HIS A CE1    1 
ATOM   2617 N  NE2    . HIS A 1 170 ? 3.697   9.977   -20.387 1.00 21.42  ? 169 HIS A NE2    1 
ATOM   2618 H  H      . HIS A 1 170 ? 6.555   7.183   -19.107 1.00 24.90  ? 169 HIS A H      1 
ATOM   2619 H  HA     . HIS A 1 170 ? 8.845   8.017   -20.164 1.00 24.76  ? 169 HIS A HA     1 
ATOM   2620 H  HB2    . HIS A 1 170 ? 7.499   9.498   -21.400 1.00 24.39  ? 169 HIS A HB2    1 
ATOM   2621 H  HB3    . HIS A 1 170 ? 7.043   7.989   -21.570 1.00 24.39  ? 169 HIS A HB3    1 
ATOM   2622 H  HD2    . HIS A 1 170 ? 5.131   10.741  -21.661 1.00 26.52  ? 169 HIS A HD2    1 
ATOM   2623 H  HE1    . HIS A 1 170 ? 3.063   8.654   -19.008 1.00 25.55  ? 169 HIS A HE1    1 
ATOM   2624 H  HE2    . HIS A 1 170 ? 3.020   10.496  -20.495 1.00 25.72  ? 169 HIS A HE2    1 
ATOM   2625 N  N      . ARG A 1 171 ? 7.985   9.546   -17.659 1.00 18.18  ? 170 ARG A N      1 
ATOM   2626 C  CA     . ARG A 1 171 ? 8.171   10.702  -16.784 1.00 20.59  ? 170 ARG A CA     1 
ATOM   2627 C  C      . ARG A 1 171 ? 9.394   10.486  -15.904 1.00 21.82  ? 170 ARG A C      1 
ATOM   2628 O  O      . ARG A 1 171 ? 9.447   9.518   -15.142 1.00 21.35  ? 170 ARG A O      1 
ATOM   2629 C  CB     . ARG A 1 171 ? 6.962   10.928  -15.883 1.00 20.15  ? 170 ARG A CB     1 
ATOM   2630 C  CG     . ARG A 1 171 ? 5.677   11.122  -16.618 1.00 20.92  ? 170 ARG A CG     1 
ATOM   2631 C  CD     . ARG A 1 171 ? 5.759   12.273  -17.590 1.00 21.73  ? 170 ARG A CD     1 
ATOM   2632 N  NE     . ARG A 1 171 ? 4.427   12.638  -18.052 1.00 21.38  ? 170 ARG A NE     1 
ATOM   2633 C  CZ     . ARG A 1 171 ? 4.203   13.278  -19.194 1.00 22.19  ? 170 ARG A CZ     1 
ATOM   2634 N  NH1    . ARG A 1 171 ? 5.223   13.608  -19.989 1.00 23.75  1 170 ARG A NH1    1 
ATOM   2635 N  NH2    . ARG A 1 171 ? 2.969   13.595  -19.556 1.00 24.91  ? 170 ARG A NH2    1 
ATOM   2636 H  H      . ARG A 1 171 ? 7.640   8.866   -17.261 1.00 21.83  ? 170 ARG A H      1 
ATOM   2637 H  HA     . ARG A 1 171 ? 8.311   11.498  -17.321 1.00 24.73  ? 170 ARG A HA     1 
ATOM   2638 H  HB2    . ARG A 1 171 ? 6.857   10.156  -15.304 1.00 24.20  ? 170 ARG A HB2    1 
ATOM   2639 H  HB3    . ARG A 1 171 ? 7.117   11.721  -15.347 1.00 24.20  ? 170 ARG A HB3    1 
ATOM   2640 H  HG2    . ARG A 1 171 ? 5.470   10.316  -17.118 1.00 25.12  ? 170 ARG A HG2    1 
ATOM   2641 H  HG3    . ARG A 1 171 ? 4.970   11.312  -15.982 1.00 25.12  ? 170 ARG A HG3    1 
ATOM   2642 H  HD2    . ARG A 1 171 ? 6.154   13.041  -17.150 1.00 26.10  ? 170 ARG A HD2    1 
ATOM   2643 H  HD3    . ARG A 1 171 ? 6.290   12.011  -18.359 1.00 26.10  ? 170 ARG A HD3    1 
ATOM   2644 H  HE     . ARG A 1 171 ? 3.752   12.298  -17.642 1.00 25.68  ? 170 ARG A HE     1 
ATOM   2645 H  HH11   . ARG A 1 171 ? 6.028   13.409  -19.760 1.00 28.52  ? 170 ARG A HH11   1 
ATOM   2646 H  HH12   . ARG A 1 171 ? 5.076   14.020  -20.729 1.00 28.52  ? 170 ARG A HH12   1 
ATOM   2647 H  HH21   . ARG A 1 171 ? 2.305   13.384  -19.052 1.00 29.91  ? 170 ARG A HH21   1 
ATOM   2648 H  HH22   . ARG A 1 171 ? 2.830   14.005  -20.300 1.00 29.91  ? 170 ARG A HH22   1 
ATOM   2649 N  N      . ALA A 1 172 ? 10.343  11.411  -15.968 1.00 22.39  ? 171 ALA A N      1 
ATOM   2650 C  CA     . ALA A 1 172 ? 11.510  11.351  -15.085 1.00 25.82  ? 171 ALA A CA     1 
ATOM   2651 C  C      . ALA A 1 172 ? 11.215  12.030  -13.741 1.00 25.44  ? 171 ALA A C      1 
ATOM   2652 O  O      . ALA A 1 172 ? 11.871  12.981  -13.345 1.00 27.58  ? 171 ALA A O      1 
ATOM   2653 C  CB     . ALA A 1 172 ? 12.716  11.990  -15.767 1.00 28.56  ? 171 ALA A CB     1 
ATOM   2654 H  H      . ALA A 1 172 ? 10.339  12.081  -16.509 1.00 26.88  ? 171 ALA A H      1 
ATOM   2655 H  HA     . ALA A 1 172 ? 11.724  10.422  -14.910 1.00 31.00  ? 171 ALA A HA     1 
ATOM   2656 H  HB1    . ALA A 1 172 ? 13.479  11.941  -15.169 1.00 34.29  ? 171 ALA A HB1    1 
ATOM   2657 H  HB2    . ALA A 1 172 ? 12.907  11.508  -16.587 1.00 34.29  ? 171 ALA A HB2    1 
ATOM   2658 H  HB3    . ALA A 1 172 ? 12.511  12.916  -15.968 1.00 34.29  ? 171 ALA A HB3    1 
ATOM   2659 N  N      . HIS A 1 173 ? 10.210  11.519  -13.040 1.00 21.20  ? 172 HIS A N      1 
ATOM   2660 C  CA     . HIS A 1 173 ? 9.738   12.115  -11.800 1.00 22.44  ? 172 HIS A CA     1 
ATOM   2661 C  C      . HIS A 1 173 ? 10.399  11.411  -10.604 1.00 22.60  ? 172 HIS A C      1 
ATOM   2662 O  O      . HIS A 1 173 ? 10.974  10.332  -10.735 1.00 21.20  ? 172 HIS A O      1 
ATOM   2663 C  CB     . HIS A 1 173 ? 8.210   12.042  -11.743 1.00 22.42  ? 172 HIS A CB     1 
ATOM   2664 C  CG     . HIS A 1 173 ? 7.541   12.927  -12.755 1.00 22.06  ? 172 HIS A CG     1 
ATOM   2665 N  ND1    . HIS A 1 173 ? 6.179   12.919  -12.974 1.00 21.57  ? 172 HIS A ND1    1 
ATOM   2666 C  CD2    . HIS A 1 173 ? 8.058   13.827  -13.626 1.00 22.47  ? 172 HIS A CD2    1 
ATOM   2667 C  CE1    . HIS A 1 173 ? 5.884   13.815  -13.894 1.00 22.81  ? 172 HIS A CE1    1 
ATOM   2668 N  NE2    . HIS A 1 173 ? 7.008   14.362  -14.326 1.00 22.29  ? 172 HIS A NE2    1 
ATOM   2669 H  H      . HIS A 1 173 ? 9.777   10.811  -13.268 1.00 25.45  ? 172 HIS A H      1 
ATOM   2670 H  HA     . HIS A 1 173 ? 9.996   13.050  -11.779 1.00 26.95  ? 172 HIS A HA     1 
ATOM   2671 H  HB2    . HIS A 1 173 ? 7.931   11.128  -11.914 1.00 26.92  ? 172 HIS A HB2    1 
ATOM   2672 H  HB3    . HIS A 1 173 ? 7.913   12.318  -10.862 1.00 26.92  ? 172 HIS A HB3    1 
ATOM   2673 H  HD1    . HIS A 1 173 ? 5.609   12.442  -12.542 1.00 25.90  ? 172 HIS A HD1    1 
ATOM   2674 H  HD2    . HIS A 1 173 ? 8.956   14.052  -13.719 1.00 26.99  ? 172 HIS A HD2    1 
ATOM   2675 H  HE1    . HIS A 1 173 ? 5.033   13.994  -14.224 1.00 27.39  ? 172 HIS A HE1    1 
ATOM   2676 N  N      . SER A 1 174 ? 10.369  12.057  -9.440  1.00 23.66  ? 173 SER A N      1 
ATOM   2677 C  CA     . SER A 1 174 ? 11.130  11.534  -8.303  1.00 22.16  ? 173 SER A CA     1 
ATOM   2678 C  C      . SER A 1 174 ? 10.836  10.064  -8.020  1.00 22.85  ? 173 SER A C      1 
ATOM   2679 O  O      . SER A 1 174 ? 11.749  9.270   -7.785  1.00 22.90  ? 173 SER A O      1 
ATOM   2680 C  CB     . SER A 1 174 ? 10.853  12.358  -7.042  1.00 23.14  ? 173 SER A CB     1 
ATOM   2681 O  OG     . SER A 1 174 ? 11.463  13.611  -7.176  1.00 24.22  ? 173 SER A OG     1 
ATOM   2682 H  H      . SER A 1 174 ? 9.930   12.779  -9.284  1.00 28.42  ? 173 SER A H      1 
ATOM   2683 H  HA     . SER A 1 174 ? 12.076  11.611  -8.502  1.00 26.62  ? 173 SER A HA     1 
ATOM   2684 H  HB2    . SER A 1 174 ? 9.896   12.476  -6.939  1.00 27.78  ? 173 SER A HB2    1 
ATOM   2685 H  HB3    . SER A 1 174 ? 11.222  11.900  -6.271  1.00 27.78  ? 173 SER A HB3    1 
ATOM   2686 H  HG     . SER A 1 174 ? 11.320  14.075  -6.491  1.00 29.08  ? 173 SER A HG     1 
ATOM   2687 N  N      . SER A 1 175 ? 9.564   9.696   -7.966  1.00 21.63  ? 174 SER A N      1 
ATOM   2688 C  CA     . SER A 1 175 ? 9.199   8.324   -7.640  1.00 20.61  ? 174 SER A CA     1 
ATOM   2689 C  C      . SER A 1 175 ? 9.608   7.330   -8.722  1.00 23.93  ? 174 SER A C      1 
ATOM   2690 O  O      . SER A 1 175 ? 9.626   6.124   -8.454  1.00 23.59  ? 174 SER A O      1 
ATOM   2691 C  CB     . SER A 1 175 ? 7.698   8.222   -7.453  1.00 20.75  ? 174 SER A CB     1 
ATOM   2692 O  OG     . SER A 1 175 ? 7.018   8.421   -8.690  1.00 20.61  ? 174 SER A OG     1 
ATOM   2693 H  H      . SER A 1 175 ? 8.896   10.217  -8.113  1.00 25.97  ? 174 SER A H      1 
ATOM   2694 H  HA     . SER A 1 175 ? 9.629   8.066   -6.810  1.00 24.75  ? 174 SER A HA     1 
ATOM   2695 H  HB2    . SER A 1 175 ? 7.482   7.340   -7.113  1.00 24.92  ? 174 SER A HB2    1 
ATOM   2696 H  HB3    . SER A 1 175 ? 7.412   8.901   -6.822  1.00 24.92  ? 174 SER A HB3    1 
ATOM   2697 H  HG     . SER A 1 175 ? 7.197   9.183   -8.997  1.00 24.75  ? 174 SER A HG     1 
ATOM   2698 N  N      . MET A 1 176 ? 9.918   7.813   -9.926  1.00 22.25  ? 175 MET A N      1 
ATOM   2699 C  CA     . MET A 1 176 ? 10.216  6.971   -11.073 1.00 22.23  ? 175 MET A CA     1 
ATOM   2700 C  C      . MET A 1 176 ? 11.701  6.783   -11.316 1.00 25.76  ? 175 MET A C      1 
ATOM   2701 O  O      . MET A 1 176 ? 12.087  5.742   -11.854 1.00 29.55  ? 175 MET A O      1 
ATOM   2702 C  CB     . MET A 1 176 ? 9.581   7.588   -12.322 1.00 21.69  ? 175 MET A CB     1 
ATOM   2703 C  CG     . MET A 1 176 ? 8.061   7.680   -12.261 1.00 22.43  ? 175 MET A CG     1 
ATOM   2704 S  SD     . MET A 1 176 ? 7.216   6.069   -12.323 1.00 22.36  ? 175 MET A SD     1 
ATOM   2705 C  CE     . MET A 1 176 ? 7.750   5.549   -13.905 1.00 23.55  ? 175 MET A CE     1 
ATOM   2706 H  H      . MET A 1 176 ? 9.962   8.654   -10.102 1.00 26.72  ? 175 MET A H      1 
ATOM   2707 H  HA     . MET A 1 176 ? 9.811   6.100   -10.934 1.00 26.70  ? 175 MET A HA     1 
ATOM   2708 H  HB2    . MET A 1 176 ? 9.928   8.487   -12.437 1.00 26.04  ? 175 MET A HB2    1 
ATOM   2709 H  HB3    . MET A 1 176 ? 9.814   7.046   -13.092 1.00 26.04  ? 175 MET A HB3    1 
ATOM   2710 H  HG2    . MET A 1 176 ? 7.809   8.114   -11.431 1.00 26.93  ? 175 MET A HG2    1 
ATOM   2711 H  HG3    . MET A 1 176 ? 7.751   8.206   -13.014 1.00 26.93  ? 175 MET A HG3    1 
ATOM   2712 H  HE1    . MET A 1 176 ? 7.372   4.676   -14.094 1.00 28.28  ? 175 MET A HE1    1 
ATOM   2713 H  HE2    . MET A 1 176 ? 7.448   6.191   -14.567 1.00 28.28  ? 175 MET A HE2    1 
ATOM   2714 H  HE3    . MET A 1 176 ? 8.719   5.499   -13.910 1.00 28.28  ? 175 MET A HE3    1 
ATOM   2715 N  N      . VAL A 1 177 ? 12.546  7.762   -10.957 1.00 22.72  ? 176 VAL A N      1 
ATOM   2716 C  CA     . VAL A 1 177 ? 13.973  7.701   -11.278 1.00 25.06  ? 176 VAL A CA     1 
ATOM   2717 C  C      . VAL A 1 177 ? 14.835  8.029   -10.063 1.00 27.19  ? 176 VAL A C      1 
ATOM   2718 O  O      . VAL A 1 177 ? 16.064  7.889   -10.114 1.00 29.39  ? 176 VAL A O      1 
ATOM   2719 C  CB     . VAL A 1 177 ? 14.341  8.645   -12.454 1.00 26.56  ? 176 VAL A CB     1 
ATOM   2720 C  CG1    . VAL A 1 177 ? 13.523  8.301   -13.708 1.00 27.60  ? 176 VAL A CG1    1 
ATOM   2721 C  CG2    . VAL A 1 177 ? 14.184  10.120  -12.077 1.00 26.10  ? 176 VAL A CG2    1 
ATOM   2722 H  H      . VAL A 1 177 ? 12.313  8.469   -10.526 1.00 27.28  ? 176 VAL A H      1 
ATOM   2723 H  HA     . VAL A 1 177 ? 14.187  6.796   -11.553 1.00 30.09  ? 176 VAL A HA     1 
ATOM   2724 H  HB     . VAL A 1 177 ? 15.275  8.503   -12.674 1.00 31.89  ? 176 VAL A HB     1 
ATOM   2725 H  HG11   . VAL A 1 177 ? 13.775  8.906   -14.423 1.00 33.14  ? 176 VAL A HG11   1 
ATOM   2726 H  HG12   . VAL A 1 177 ? 13.712  7.385   -13.966 1.00 33.14  ? 176 VAL A HG12   1 
ATOM   2727 H  HG13   . VAL A 1 177 ? 12.580  8.401   -13.506 1.00 33.14  ? 176 VAL A HG13   1 
ATOM   2728 H  HG21   . VAL A 1 177 ? 14.424  10.668  -12.841 1.00 31.34  ? 176 VAL A HG21   1 
ATOM   2729 H  HG22   . VAL A 1 177 ? 13.261  10.285  -11.828 1.00 31.34  ? 176 VAL A HG22   1 
ATOM   2730 H  HG23   . VAL A 1 177 ? 14.769  10.318  -11.330 1.00 31.34  ? 176 VAL A HG23   1 
ATOM   2731 N  N      . GLY A 1 178 ? 14.212  8.477   -8.975  1.00 25.08  ? 177 GLY A N      1 
ATOM   2732 C  CA     . GLY A 1 178 ? 14.954  9.021   -7.853  1.00 26.76  ? 177 GLY A CA     1 
ATOM   2733 C  C      . GLY A 1 178 ? 15.045  8.171   -6.599  1.00 27.53  ? 177 GLY A C      1 
ATOM   2734 O  O      . GLY A 1 178 ? 15.603  8.636   -5.613  1.00 28.24  ? 177 GLY A O      1 
ATOM   2735 H  H      . GLY A 1 178 ? 13.359  8.475   -8.866  1.00 30.12  ? 177 GLY A H      1 
ATOM   2736 H  HA2    . GLY A 1 178 ? 15.860  9.204   -8.145  1.00 32.13  ? 177 GLY A HA2    1 
ATOM   2737 H  HA3    . GLY A 1 178 ? 14.551  9.867   -7.601  1.00 32.13  ? 177 GLY A HA3    1 
ATOM   2738 N  N      . VAL A 1 179 ? 14.513  6.947   -6.594  1.00 26.98  ? 178 VAL A N      1 
ATOM   2739 C  CA     . VAL A 1 179 ? 14.561  6.111   -5.400  1.00 27.94  ? 178 VAL A CA     1 
ATOM   2740 C  C      . VAL A 1 179 ? 15.938  5.468   -5.307  1.00 31.83  ? 178 VAL A C      1 
ATOM   2741 O  O      . VAL A 1 179 ? 16.418  4.845   -6.268  1.00 37.89  ? 178 VAL A O      1 
ATOM   2742 C  CB     . VAL A 1 179 ? 13.438  5.059   -5.429  1.00 27.25  ? 178 VAL A CB     1 
ATOM   2743 C  CG1    . VAL A 1 179 ? 13.595  4.066   -4.304  1.00 27.80  ? 178 VAL A CG1    1 
ATOM   2744 C  CG2    . VAL A 1 179 ? 12.086  5.726   -5.352  1.00 28.37  ? 178 VAL A CG2    1 
ATOM   2745 H  H      . VAL A 1 179 ? 14.122  6.582   -7.267  1.00 32.40  ? 178 VAL A H      1 
ATOM   2746 H  HA     . VAL A 1 179 ? 14.434  6.668   -4.616  1.00 33.54  ? 178 VAL A HA     1 
ATOM   2747 H  HB     . VAL A 1 179 ? 13.484  4.571   -6.266  1.00 32.71  ? 178 VAL A HB     1 
ATOM   2748 H  HG11   . VAL A 1 179 ? 12.873  3.419   -4.352  1.00 33.38  ? 178 VAL A HG11   1 
ATOM   2749 H  HG12   . VAL A 1 179 ? 14.449  3.616   -4.397  1.00 33.38  ? 178 VAL A HG12   1 
ATOM   2750 H  HG13   . VAL A 1 179 ? 13.560  4.540   -3.459  1.00 33.38  ? 178 VAL A HG13   1 
ATOM   2751 H  HG21   . VAL A 1 179 ? 11.397  5.044   -5.372  1.00 34.07  ? 178 VAL A HG21   1 
ATOM   2752 H  HG22   . VAL A 1 179 ? 12.030  6.230   -4.525  1.00 34.07  ? 178 VAL A HG22   1 
ATOM   2753 H  HG23   . VAL A 1 179 ? 11.985  6.321   -6.111  1.00 34.07  ? 178 VAL A HG23   1 
ATOM   2754 N  N      . ASN A 1 180 ? 16.586  5.639   -4.153  1.00 29.55  ? 179 ASN A N      1 
ATOM   2755 C  CA     . ASN A 1 180 ? 17.963  5.211   -3.933  1.00 34.82  ? 179 ASN A CA     1 
ATOM   2756 C  C      . ASN A 1 180 ? 17.941  3.958   -3.057  1.00 31.85  ? 179 ASN A C      1 
ATOM   2757 O  O      . ASN A 1 180 ? 18.034  4.034   -1.824  1.00 33.90  ? 179 ASN A O      1 
ATOM   2758 C  CB     . ASN A 1 180 ? 18.771  6.328   -3.278  1.00 48.30  ? 179 ASN A CB     1 
ATOM   2759 C  CG     . ASN A 1 180 ? 20.145  5.867   -2.834  1.00 61.85  ? 179 ASN A CG     1 
ATOM   2760 O  OD1    . ASN A 1 180 ? 20.695  4.905   -3.375  1.00 67.38  ? 179 ASN A OD1    1 
ATOM   2761 N  ND2    . ASN A 1 180 ? 20.703  6.548   -1.832  1.00 66.69  ? 179 ASN A ND2    1 
ATOM   2762 H  H      . ASN A 1 180 ? 16.235  6.013   -3.463  1.00 35.48  ? 179 ASN A H      1 
ATOM   2763 H  HA     . ASN A 1 180 ? 18.375  4.988   -4.782  1.00 41.81  ? 179 ASN A HA     1 
ATOM   2764 H  HB2    . ASN A 1 180 ? 18.887  7.050   -3.915  1.00 57.98  ? 179 ASN A HB2    1 
ATOM   2765 H  HB3    . ASN A 1 180 ? 18.293  6.647   -2.496  1.00 57.98  ? 179 ASN A HB3    1 
ATOM   2766 H  HD21   . ASN A 1 180 ? 21.482  6.326   -1.543  1.00 80.05  ? 179 ASN A HD21   1 
ATOM   2767 H  HD22   . ASN A 1 180 ? 20.284  7.209   -1.475  1.00 80.05  ? 179 ASN A HD22   1 
ATOM   2768 N  N      . LEU A 1 181 ? 17.768  2.816   -3.701  1.00 29.65  ? 180 LEU A N      1 
ATOM   2769 C  CA     . LEU A 1 181 ? 17.890  1.506   -3.094  1.00 28.93  ? 180 LEU A CA     1 
ATOM   2770 C  C      . LEU A 1 181 ? 18.785  0.639   -3.964  1.00 31.29  ? 180 LEU A C      1 
ATOM   2771 O  O      . LEU A 1 181 ? 18.872  0.863   -5.174  1.00 32.44  ? 180 LEU A O      1 
ATOM   2772 C  CB     . LEU A 1 181 ? 16.511  0.852   -2.933  1.00 27.82  ? 180 LEU A CB     1 
ATOM   2773 C  CG     . LEU A 1 181 ? 15.624  1.494   -1.845  1.00 29.52  ? 180 LEU A CG     1 
ATOM   2774 C  CD1    . LEU A 1 181 ? 14.190  0.932   -1.871  1.00 26.08  ? 180 LEU A CD1    1 
ATOM   2775 C  CD2    . LEU A 1 181 ? 16.260  1.352   -0.450  1.00 34.28  ? 180 LEU A CD2    1 
ATOM   2776 H  H      . LEU A 1 181 ? 17.569  2.776   -4.537  1.00 35.60  ? 180 LEU A H      1 
ATOM   2777 H  HA     . LEU A 1 181 ? 18.297  1.590   -2.217  1.00 34.73  ? 180 LEU A HA     1 
ATOM   2778 H  HB2    . LEU A 1 181 ? 16.036  0.917   -3.776  1.00 33.41  ? 180 LEU A HB2    1 
ATOM   2779 H  HB3    . LEU A 1 181 ? 16.635  -0.081  -2.699  1.00 33.41  ? 180 LEU A HB3    1 
ATOM   2780 H  HG     . LEU A 1 181 ? 15.560  2.443   -2.033  1.00 35.45  ? 180 LEU A HG     1 
ATOM   2781 H  HD11   . LEU A 1 181 ? 13.670  1.362   -1.174  1.00 31.32  ? 180 LEU A HD11   1 
ATOM   2782 H  HD12   . LEU A 1 181 ? 13.795  1.115   -2.738  1.00 31.32  ? 180 LEU A HD12   1 
ATOM   2783 H  HD13   . LEU A 1 181 ? 14.223  -0.025  -1.718  1.00 31.32  ? 180 LEU A HD13   1 
ATOM   2784 H  HD21   . LEU A 1 181 ? 15.676  1.766   0.206   1.00 41.16  ? 180 LEU A HD21   1 
ATOM   2785 H  HD22   . LEU A 1 181 ? 16.370  0.410   -0.248  1.00 41.16  ? 180 LEU A HD22   1 
ATOM   2786 H  HD23   . LEU A 1 181 ? 17.123  1.794   -0.450  1.00 41.16  ? 180 LEU A HD23   1 
ATOM   2787 N  N      . PRO A 1 182 ? 19.468  -0.354  -3.380  1.00 34.48  ? 181 PRO A N      1 
ATOM   2788 C  CA     . PRO A 1 182 ? 20.465  -1.110  -4.169  1.00 36.84  ? 181 PRO A CA     1 
ATOM   2789 C  C      . PRO A 1 182 ? 19.877  -1.938  -5.295  1.00 36.10  ? 181 PRO A C      1 
ATOM   2790 O  O      . PRO A 1 182 ? 20.567  -2.183  -6.293  1.00 37.60  ? 181 PRO A O      1 
ATOM   2791 C  CB     . PRO A 1 182 ? 21.131  -2.013  -3.126  1.00 40.01  ? 181 PRO A CB     1 
ATOM   2792 C  CG     . PRO A 1 182 ? 20.870  -1.353  -1.809  1.00 44.03  ? 181 PRO A CG     1 
ATOM   2793 C  CD     . PRO A 1 182 ? 19.552  -0.662  -1.940  1.00 39.19  ? 181 PRO A CD     1 
ATOM   2794 H  HA     . PRO A 1 182 ? 21.129  -0.504  -4.534  1.00 44.23  ? 181 PRO A HA     1 
ATOM   2795 H  HB2    . PRO A 1 182 ? 20.728  -2.895  -3.153  1.00 48.04  ? 181 PRO A HB2    1 
ATOM   2796 H  HB3    . PRO A 1 182 ? 22.084  -2.066  -3.300  1.00 48.04  ? 181 PRO A HB3    1 
ATOM   2797 H  HG2    . PRO A 1 182 ? 20.832  -2.026  -1.111  1.00 52.86  ? 181 PRO A HG2    1 
ATOM   2798 H  HG3    . PRO A 1 182 ? 21.573  -0.711  -1.624  1.00 52.86  ? 181 PRO A HG3    1 
ATOM   2799 H  HD2    . PRO A 1 182 ? 18.831  -1.256  -1.679  1.00 47.05  ? 181 PRO A HD2    1 
ATOM   2800 H  HD3    . PRO A 1 182 ? 19.546  0.156   -1.418  1.00 47.05  ? 181 PRO A HD3    1 
ATOM   2801 N  N      . GLN A 1 183 ? 18.643  -2.412  -5.160  1.00 29.08  ? 182 GLN A N      1 
ATOM   2802 C  CA     . GLN A 1 183 ? 18.003  -3.215  -6.191  1.00 26.13  ? 182 GLN A CA     1 
ATOM   2803 C  C      . GLN A 1 183 ? 16.764  -2.485  -6.651  1.00 28.41  ? 182 GLN A C      1 
ATOM   2804 O  O      . GLN A 1 183 ? 15.860  -2.231  -5.845  1.00 24.63  ? 182 GLN A O      1 
ATOM   2805 C  CB     . GLN A 1 183 ? 17.631  -4.607  -5.683  1.00 26.87  ? 182 GLN A CB     1 
ATOM   2806 C  CG     . GLN A 1 183 ? 18.835  -5.512  -5.477  1.00 34.45  ? 182 GLN A CG     1 
ATOM   2807 C  CD     . GLN A 1 183 ? 18.424  -6.873  -4.972  1.00 44.32  ? 182 GLN A CD     1 
ATOM   2808 O  OE1    . GLN A 1 183 ? 18.015  -7.022  -3.825  1.00 49.66  ? 182 GLN A OE1    1 
ATOM   2809 N  NE2    . GLN A 1 183 ? 18.517  -7.875  -5.836  1.00 45.95  ? 182 GLN A NE2    1 
ATOM   2810 H  H      . GLN A 1 183 ? 18.148  -2.278  -4.469  1.00 34.92  ? 182 GLN A H      1 
ATOM   2811 H  HA     . GLN A 1 183 ? 18.604  -3.312  -6.947  1.00 31.38  ? 182 GLN A HA     1 
ATOM   2812 H  HB2    . GLN A 1 183 ? 17.174  -4.519  -4.832  1.00 32.26  ? 182 GLN A HB2    1 
ATOM   2813 H  HB3    . GLN A 1 183 ? 17.046  -5.031  -6.330  1.00 32.26  ? 182 GLN A HB3    1 
ATOM   2814 H  HG2    . GLN A 1 183 ? 19.297  -5.628  -6.322  1.00 41.36  ? 182 GLN A HG2    1 
ATOM   2815 H  HG3    . GLN A 1 183 ? 19.428  -5.111  -4.822  1.00 41.36  ? 182 GLN A HG3    1 
ATOM   2816 H  HE21   . GLN A 1 183 ? 18.799  -7.729  -6.636  1.00 55.16  ? 182 GLN A HE21   1 
ATOM   2817 H  HE22   . GLN A 1 183 ? 18.295  -8.671  -5.598  1.00 55.16  ? 182 GLN A HE22   1 
ATOM   2818 N  N      . LYS A 1 184 ? 16.733  -2.172  -7.946  1.00 24.38  ? 183 LYS A N      1 
ATOM   2819 C  CA     . LYS A 1 184 ? 15.624  -1.490  -8.595  1.00 21.61  ? 183 LYS A CA     1 
ATOM   2820 C  C      . LYS A 1 184 ? 15.187  -2.333  -9.782  1.00 21.58  ? 183 LYS A C      1 
ATOM   2821 O  O      . LYS A 1 184 ? 15.894  -2.387  -10.800 1.00 22.60  ? 183 LYS A O      1 
ATOM   2822 C  CB     . LYS A 1 184 ? 16.048  -0.098  -9.048  1.00 22.76  ? 183 LYS A CB     1 
ATOM   2823 C  CG     . LYS A 1 184 ? 16.505  0.760   -7.836  1.00 25.28  ? 183 LYS A CG     1 
ATOM   2824 C  CD     . LYS A 1 184 ? 17.178  2.052   -8.246  1.00 33.04  ? 183 LYS A CD     1 
ATOM   2825 C  CE     . LYS A 1 184 ? 18.546  1.801   -8.840  1.00 43.84  ? 183 LYS A CE     1 
ATOM   2826 N  NZ     . LYS A 1 184 ? 19.218  3.055   -9.284  1.00 51.29  1 183 LYS A NZ     1 
ATOM   2827 H  H      . LYS A 1 184 ? 17.375  -2.355  -8.488  1.00 29.27  ? 183 LYS A H      1 
ATOM   2828 H  HA     . LYS A 1 184 ? 14.880  -1.407  -7.978  1.00 25.96  ? 183 LYS A HA     1 
ATOM   2829 H  HB2    . LYS A 1 184 ? 16.790  -0.173  -9.668  1.00 27.33  ? 183 LYS A HB2    1 
ATOM   2830 H  HB3    . LYS A 1 184 ? 15.297  0.346   -9.472  1.00 27.33  ? 183 LYS A HB3    1 
ATOM   2831 H  HG2    . LYS A 1 184 ? 15.730  0.985   -7.298  1.00 30.36  ? 183 LYS A HG2    1 
ATOM   2832 H  HG3    . LYS A 1 184 ? 17.137  0.248   -7.308  1.00 30.36  ? 183 LYS A HG3    1 
ATOM   2833 H  HD2    . LYS A 1 184 ? 16.634  2.498   -8.914  1.00 39.66  ? 183 LYS A HD2    1 
ATOM   2834 H  HD3    . LYS A 1 184 ? 17.284  2.619   -7.466  1.00 39.66  ? 183 LYS A HD3    1 
ATOM   2835 H  HE2    . LYS A 1 184 ? 19.109  1.380   -8.171  1.00 52.62  ? 183 LYS A HE2    1 
ATOM   2836 H  HE3    . LYS A 1 184 ? 18.455  1.220   -9.611  1.00 52.62  ? 183 LYS A HE3    1 
ATOM   2837 H  HZ1    . LYS A 1 184 ? 20.017  2.866   -9.626  1.00 61.57  ? 183 LYS A HZ1    1 
ATOM   2838 H  HZ2    . LYS A 1 184 ? 18.725  3.460   -9.905  1.00 61.57  ? 183 LYS A HZ2    1 
ATOM   2839 H  HZ3    . LYS A 1 184 ? 19.321  3.605   -8.592  1.00 61.57  ? 183 LYS A HZ3    1 
ATOM   2840 N  N      . ALA A 1 185 ? 14.009  -2.948  -9.681  1.00 21.54  ? 184 ALA A N      1 
ATOM   2841 C  CA     . ALA A 1 185 ? 13.595  -3.971  -10.635 1.00 20.55  ? 184 ALA A CA     1 
ATOM   2842 C  C      . ALA A 1 185 ? 12.330  -3.583  -11.379 1.00 18.98  ? 184 ALA A C      1 
ATOM   2843 O  O      . ALA A 1 185 ? 11.434  -2.947  -10.826 1.00 19.71  ? 184 ALA A O      1 
ATOM   2844 C  CB     . ALA A 1 185 ? 13.360  -5.313  -9.905  1.00 24.90  ? 184 ALA A CB     1 
ATOM   2845 H  H      . ALA A 1 185 ? 13.430  -2.789  -9.066  1.00 25.87  ? 184 ALA A H      1 
ATOM   2846 H  HA     . ALA A 1 185 ? 14.301  -4.102  -11.288 1.00 24.68  ? 184 ALA A HA     1 
ATOM   2847 H  HB1    . ALA A 1 185 ? 13.086  -5.981  -10.553 1.00 29.90  ? 184 ALA A HB1    1 
ATOM   2848 H  HB2    . ALA A 1 185 ? 14.186  -5.587  -9.476  1.00 29.90  ? 184 ALA A HB2    1 
ATOM   2849 H  HB3    . ALA A 1 185 ? 12.665  -5.192  -9.240  1.00 29.90  ? 184 ALA A HB3    1 
ATOM   2850 N  N      . GLY A 1 186 ? 12.236  -4.031  -12.631 1.00 19.79  ? 185 GLY A N      1 
ATOM   2851 C  CA     . GLY A 1 186 ? 11.018  -3.817  -13.392 1.00 20.12  ? 185 GLY A CA     1 
ATOM   2852 C  C      . GLY A 1 186 ? 9.988   -4.875  -13.042 1.00 20.83  ? 185 GLY A C      1 
ATOM   2853 O  O      . GLY A 1 186 ? 10.313  -6.043  -12.830 1.00 21.78  ? 185 GLY A O      1 
ATOM   2854 H  H      . GLY A 1 186 ? 12.854  -4.455  -13.052 1.00 23.77  ? 185 GLY A H      1 
ATOM   2855 H  HA2    . GLY A 1 186 ? 10.652  -2.942  -13.190 1.00 24.16  ? 185 GLY A HA2    1 
ATOM   2856 H  HA3    . GLY A 1 186 ? 11.210  -3.867  -14.342 1.00 24.16  ? 185 GLY A HA3    1 
ATOM   2857 N  N      . GLY A 1 187 ? 8.736   -4.436  -12.922 1.00 19.99  ? 186 GLY A N      1 
ATOM   2858 C  CA     . GLY A 1 187 ? 7.653   -5.342  -12.621 1.00 22.07  ? 186 GLY A CA     1 
ATOM   2859 C  C      . GLY A 1 187 ? 7.130   -6.054  -13.858 1.00 22.12  ? 186 GLY A C      1 
ATOM   2860 O  O      . GLY A 1 187 ? 7.581   -5.837  -14.986 1.00 19.60  ? 186 GLY A O      1 
ATOM   2861 H  H      . GLY A 1 187 ? 8.496   -3.615  -13.013 1.00 24.00  ? 186 GLY A H      1 
ATOM   2862 H  HA2    . GLY A 1 187 ? 7.958   -6.011  -11.988 1.00 26.50  ? 186 GLY A HA2    1 
ATOM   2863 H  HA3    . GLY A 1 187 ? 6.922   -4.849  -12.218 1.00 26.50  ? 186 GLY A HA3    1 
ATOM   2864 N  N      . PHE A 1 188 ? 6.135   -6.919  -13.634 1.00 20.80  ? 187 PHE A N      1 
ATOM   2865 C  CA     . PHE A 1 188 ? 5.680   -7.793  -14.713 1.00 22.60  ? 187 PHE A CA     1 
ATOM   2866 C  C      . PHE A 1 188 ? 4.835   -7.058  -15.757 1.00 21.54  ? 187 PHE A C      1 
ATOM   2867 O  O      . PHE A 1 188 ? 4.781   -7.494  -16.923 1.00 20.63  ? 187 PHE A O      1 
ATOM   2868 C  CB     . PHE A 1 188 ? 4.900   -8.953  -14.134 1.00 22.61  ? 187 PHE A CB     1 
ATOM   2869 C  CG     . PHE A 1 188 ? 5.732   -9.857  -13.267 1.00 23.94  ? 187 PHE A CG     1 
ATOM   2870 C  CD1    . PHE A 1 188 ? 7.033   -10.177 -13.615 1.00 28.26  ? 187 PHE A CD1    1 
ATOM   2871 C  CD2    . PHE A 1 188 ? 5.199   -10.407 -12.126 1.00 25.25  ? 187 PHE A CD2    1 
ATOM   2872 C  CE1    . PHE A 1 188 ? 7.791   -11.011 -12.792 1.00 31.31  ? 187 PHE A CE1    1 
ATOM   2873 C  CE2    . PHE A 1 188 ? 5.938   -11.244 -11.333 1.00 27.55  ? 187 PHE A CE2    1 
ATOM   2874 C  CZ     . PHE A 1 188 ? 7.237   -11.531 -11.666 1.00 27.33  ? 187 PHE A CZ     1 
ATOM   2875 H  H      . PHE A 1 188 ? 5.720   -7.017  -12.887 1.00 24.98  ? 187 PHE A H      1 
ATOM   2876 H  HA     . PHE A 1 188 ? 6.457   -8.156  -15.166 1.00 27.14  ? 187 PHE A HA     1 
ATOM   2877 H  HB2    . PHE A 1 188 ? 4.175   -8.605  -13.591 1.00 27.15  ? 187 PHE A HB2    1 
ATOM   2878 H  HB3    . PHE A 1 188 ? 4.541   -9.485  -14.861 1.00 27.15  ? 187 PHE A HB3    1 
ATOM   2879 H  HD1    . PHE A 1 188 ? 7.413   -9.811  -14.381 1.00 33.93  ? 187 PHE A HD1    1 
ATOM   2880 H  HD2    . PHE A 1 188 ? 4.322   -10.207 -11.889 1.00 30.32  ? 187 PHE A HD2    1 
ATOM   2881 H  HE1    . PHE A 1 188 ? 8.667   -11.222 -13.021 1.00 37.60  ? 187 PHE A HE1    1 
ATOM   2882 H  HE2    . PHE A 1 188 ? 5.567   -11.598 -10.557 1.00 33.08  ? 187 PHE A HE2    1 
ATOM   2883 H  HZ     . PHE A 1 188 ? 7.737   -12.099 -11.125 1.00 32.81  ? 187 PHE A HZ     1 
ATOM   2884 N  N      . LEU A 1 189 ? 4.138   -5.992  -15.359 1.00 20.01  ? 188 LEU A N      1 
ATOM   2885 C  CA     . LEU A 1 189 ? 3.416   -5.176  -16.335 1.00 21.84  ? 188 LEU A CA     1 
ATOM   2886 C  C      . LEU A 1 189 ? 4.394   -4.425  -17.233 1.00 20.42  ? 188 LEU A C      1 
ATOM   2887 O  O      . LEU A 1 189 ? 4.201   -4.328  -18.456 1.00 19.88  ? 188 LEU A O      1 
ATOM   2888 C  CB     . LEU A 1 189 ? 2.490   -4.210  -15.601 1.00 22.03  ? 188 LEU A CB     1 
ATOM   2889 C  CG     . LEU A 1 189 ? 1.700   -3.267  -16.506 1.00 23.44  ? 188 LEU A CG     1 
ATOM   2890 C  CD1    . LEU A 1 189 ? 0.814   -4.026  -17.500 1.00 25.21  ? 188 LEU A CD1    1 
ATOM   2891 C  CD2    . LEU A 1 189 ? 0.888   -2.307  -15.655 1.00 25.93  ? 188 LEU A CD2    1 
ATOM   2892 H  H      . LEU A 1 189 ? 4.069   -5.724  -14.545 1.00 24.03  ? 188 LEU A H      1 
ATOM   2893 H  HA     . LEU A 1 189 ? 2.872   -5.752  -16.894 1.00 26.22  ? 188 LEU A HA     1 
ATOM   2894 H  HB2    . LEU A 1 189 ? 1.850   -4.726  -15.086 1.00 26.46  ? 188 LEU A HB2    1 
ATOM   2895 H  HB3    . LEU A 1 189 ? 3.024   -3.663  -15.003 1.00 26.46  ? 188 LEU A HB3    1 
ATOM   2896 H  HG     . LEU A 1 189 ? 2.329   -2.738  -17.022 1.00 28.15  ? 188 LEU A HG     1 
ATOM   2897 H  HD11   . LEU A 1 189 ? 0.336   -3.386  -18.049 1.00 30.28  ? 188 LEU A HD11   1 
ATOM   2898 H  HD12   . LEU A 1 189 ? 1.375   -4.587  -18.058 1.00 30.28  ? 188 LEU A HD12   1 
ATOM   2899 H  HD13   . LEU A 1 189 ? 0.185   -4.574  -17.006 1.00 30.28  ? 188 LEU A HD13   1 
ATOM   2900 H  HD21   . LEU A 1 189 ? 0.390   -1.713  -16.237 1.00 31.13  ? 188 LEU A HD21   1 
ATOM   2901 H  HD22   . LEU A 1 189 ? 0.276   -2.817  -15.101 1.00 31.13  ? 188 LEU A HD22   1 
ATOM   2902 H  HD23   . LEU A 1 189 ? 1.492   -1.794  -15.095 1.00 31.13  ? 188 LEU A HD23   1 
ATOM   2903 N  N      . MET A 1 190 ? 5.438   -3.862  -16.625 1.00 20.36  ? 189 MET A N      1 
ATOM   2904 C  CA     . MET A 1 190 ? 6.480   -3.192  -17.382 1.00 21.72  ? 189 MET A CA     1 
ATOM   2905 C  C      . MET A 1 190 ? 7.091   -4.140  -18.394 1.00 22.87  ? 189 MET A C      1 
ATOM   2906 O  O      . MET A 1 190 ? 7.297   -3.775  -19.562 1.00 22.58  ? 189 MET A O      1 
ATOM   2907 C  CB     . MET A 1 190 ? 7.534   -2.660  -16.402 1.00 24.00  ? 189 MET A CB     1 
ATOM   2908 C  CG     . MET A 1 190 ? 8.565   -1.733  -16.991 1.00 25.80  ? 189 MET A CG     1 
ATOM   2909 S  SD     . MET A 1 190 ? 7.830   -0.079  -17.263 1.00 25.31  ? 189 MET A SD     1 
ATOM   2910 C  CE     . MET A 1 190 ? 7.846   0.634   -15.630 1.00 28.42  ? 189 MET A CE     1 
ATOM   2911 H  H      . MET A 1 190 ? 5.562   -3.858  -15.774 1.00 24.45  ? 189 MET A H      1 
ATOM   2912 H  HA     . MET A 1 190 ? 6.094   -2.434  -17.850 1.00 26.09  ? 189 MET A HA     1 
ATOM   2913 H  HB2    . MET A 1 190 ? 7.079   -2.176  -15.695 1.00 28.81  ? 189 MET A HB2    1 
ATOM   2914 H  HB3    . MET A 1 190 ? 8.008   -3.416  -16.022 1.00 28.81  ? 189 MET A HB3    1 
ATOM   2915 H  HG2    . MET A 1 190 ? 9.311   -1.643  -16.377 1.00 30.98  ? 189 MET A HG2    1 
ATOM   2916 H  HG3    . MET A 1 190 ? 8.866   -2.082  -17.844 1.00 30.98  ? 189 MET A HG3    1 
ATOM   2917 H  HE1    . MET A 1 190 ? 7.469   1.527   -15.672 1.00 34.13  ? 189 MET A HE1    1 
ATOM   2918 H  HE2    . MET A 1 190 ? 7.315   0.078   -15.038 1.00 34.13  ? 189 MET A HE2    1 
ATOM   2919 H  HE3    . MET A 1 190 ? 8.761   0.676   -15.313 1.00 34.13  ? 189 MET A HE3    1 
ATOM   2920 N  N      . LYS A 1 191 ? 7.378   -5.375  -17.969 1.00 21.07  ? 190 LYS A N      1 
ATOM   2921 C  CA     . LYS A 1 191 ? 7.957   -6.352  -18.886 1.00 22.18  ? 190 LYS A CA     1 
ATOM   2922 C  C      . LYS A 1 191 ? 6.986   -6.726  -20.003 1.00 24.02  ? 190 LYS A C      1 
ATOM   2923 O  O      . LYS A 1 191 ? 7.377   -6.805  -21.175 1.00 23.48  ? 190 LYS A O      1 
ATOM   2924 C  CB     . LYS A 1 191 ? 8.386   -7.594  -18.098 1.00 26.77  ? 190 LYS A CB     1 
ATOM   2925 C  CG     . LYS A 1 191 ? 8.830   -8.761  -18.978 1.00 37.84  ? 190 LYS A CG     1 
ATOM   2926 C  CD     . LYS A 1 191 ? 9.119   -10.017 -18.164 1.00 48.27  ? 190 LYS A CD     1 
ATOM   2927 C  CE     . LYS A 1 191 ? 10.311  -9.813  -17.271 1.00 48.81  ? 190 LYS A CE     1 
ATOM   2928 N  NZ     . LYS A 1 191 ? 10.799  -11.120 -16.747 1.00 54.62  1 190 LYS A NZ     1 
ATOM   2929 H  H      . LYS A 1 191 ? 7.248   -5.664  -17.169 1.00 25.30  ? 190 LYS A H      1 
ATOM   2930 H  HA     . LYS A 1 191 ? 8.749   -5.969  -19.295 1.00 26.63  ? 190 LYS A HA     1 
ATOM   2931 H  HB2    . LYS A 1 191 ? 9.129   -7.358  -17.522 1.00 32.14  ? 190 LYS A HB2    1 
ATOM   2932 H  HB3    . LYS A 1 191 ? 7.637   -7.897  -17.560 1.00 32.14  ? 190 LYS A HB3    1 
ATOM   2933 H  HG2    . LYS A 1 191 ? 8.126   -8.968  -19.612 1.00 45.43  ? 190 LYS A HG2    1 
ATOM   2934 H  HG3    . LYS A 1 191 ? 9.641   -8.514  -19.449 1.00 45.43  ? 190 LYS A HG3    1 
ATOM   2935 H  HD2    . LYS A 1 191 ? 8.351   -10.224 -17.608 1.00 57.94  ? 190 LYS A HD2    1 
ATOM   2936 H  HD3    . LYS A 1 191 ? 9.309   -10.754 -18.766 1.00 57.94  ? 190 LYS A HD3    1 
ATOM   2937 H  HE2    . LYS A 1 191 ? 11.027  -9.399  -17.778 1.00 58.59  ? 190 LYS A HE2    1 
ATOM   2938 H  HE3    . LYS A 1 191 ? 10.060  -9.255  -16.519 1.00 58.59  ? 190 LYS A HE3    1 
ATOM   2939 H  HZ1    . LYS A 1 191 ? 11.505  -10.991 -16.220 1.00 65.56  ? 190 LYS A HZ1    1 
ATOM   2940 H  HZ2    . LYS A 1 191 ? 10.156  -11.518 -16.278 1.00 65.56  ? 190 LYS A HZ2    1 
ATOM   2941 H  HZ3    . LYS A 1 191 ? 11.035  -11.649 -17.423 1.00 65.56  ? 190 LYS A HZ3    1 
ATOM   2942 N  N      . LYS A 1 192 ? 5.720   -6.973  -19.655 1.00 22.53  ? 191 LYS A N      1 
ATOM   2943 C  CA     . LYS A 1 192 ? 4.730   -7.391  -20.636 1.00 22.30  ? 191 LYS A CA     1 
ATOM   2944 C  C      . LYS A 1 192 ? 4.533   -6.322  -21.709 1.00 20.40  ? 191 LYS A C      1 
ATOM   2945 O  O      . LYS A 1 192 ? 4.488   -6.620  -22.908 1.00 20.63  ? 191 LYS A O      1 
ATOM   2946 C  CB     . LYS A 1 192 ? 3.410   -7.676  -19.915 1.00 28.55  ? 191 LYS A CB     1 
ATOM   2947 C  CG     . LYS A 1 192 ? 2.204   -7.886  -20.799 1.00 45.03  ? 191 LYS A CG     1 
ATOM   2948 C  CD     . LYS A 1 192 ? 0.945   -8.116  -19.952 1.00 60.84  ? 191 LYS A CD     1 
ATOM   2949 C  CE     . LYS A 1 192 ? -0.288  -8.236  -20.839 1.00 77.99  ? 191 LYS A CE     1 
ATOM   2950 N  NZ     . LYS A 1 192 ? -1.494  -8.675  -20.081 1.00 88.37  1 191 LYS A NZ     1 
ATOM   2951 H  H      . LYS A 1 192 ? 5.414   -6.905  -18.854 1.00 27.06  ? 191 LYS A H      1 
ATOM   2952 H  HA     . LYS A 1 192 ? 5.026   -8.207  -21.067 1.00 26.78  ? 191 LYS A HA     1 
ATOM   2953 H  HB2    . LYS A 1 192 ? 3.521   -8.478  -19.382 1.00 34.28  ? 191 LYS A HB2    1 
ATOM   2954 H  HB3    . LYS A 1 192 ? 3.213   -6.926  -19.332 1.00 34.28  ? 191 LYS A HB3    1 
ATOM   2955 H  HG2    . LYS A 1 192 ? 2.065   -7.099  -21.348 1.00 54.05  ? 191 LYS A HG2    1 
ATOM   2956 H  HG3    . LYS A 1 192 ? 2.345   -8.667  -21.357 1.00 54.05  ? 191 LYS A HG3    1 
ATOM   2957 H  HD2    . LYS A 1 192 ? 1.041   -8.940  -19.448 1.00 73.02  ? 191 LYS A HD2    1 
ATOM   2958 H  HD3    . LYS A 1 192 ? 0.819   -7.365  -19.351 1.00 73.02  ? 191 LYS A HD3    1 
ATOM   2959 H  HE2    . LYS A 1 192 ? -0.480  -7.370  -21.233 1.00 93.60  ? 191 LYS A HE2    1 
ATOM   2960 H  HE3    . LYS A 1 192 ? -0.116  -8.888  -21.535 1.00 93.60  ? 191 LYS A HE3    1 
ATOM   2961 H  HZ1    . LYS A 1 192 ? -2.193  -8.734  -20.628 1.00 106.07 ? 191 LYS A HZ1    1 
ATOM   2962 H  HZ2    . LYS A 1 192 ? -1.348  -9.472  -19.712 1.00 106.07 ? 191 LYS A HZ2    1 
ATOM   2963 H  HZ3    . LYS A 1 192 ? -1.679  -8.089  -19.437 1.00 106.07 ? 191 LYS A HZ3    1 
ATOM   2964 N  N      . GLU A 1 193 ? 4.409   -5.066  -21.285 1.00 20.06  ? 192 GLU A N      1 
ATOM   2965 C  CA     . GLU A 1 193 ? 4.162   -3.972  -22.214 1.00 20.51  ? 192 GLU A CA     1 
ATOM   2966 C  C      . GLU A 1 193 ? 5.379   -3.697  -23.085 1.00 20.67  ? 192 GLU A C      1 
ATOM   2967 O  O      . GLU A 1 193 ? 5.249   -3.518  -24.305 1.00 20.41  ? 192 GLU A O      1 
ATOM   2968 C  CB     . GLU A 1 193 ? 3.768   -2.721  -21.446 1.00 19.52  ? 192 GLU A CB     1 
ATOM   2969 C  CG     . GLU A 1 193 ? 2.461   -2.836  -20.686 1.00 24.17  ? 192 GLU A CG     1 
ATOM   2970 C  CD     . GLU A 1 193 ? 1.215   -2.304  -21.410 1.00 31.59  ? 192 GLU A CD     1 
ATOM   2971 O  OE1    . GLU A 1 193 ? 1.220   -2.192  -22.664 1.00 33.04  ? 192 GLU A OE1    1 
ATOM   2972 O  OE2    . GLU A 1 193 ? 0.202   -2.020  -20.697 1.00 30.80  1 192 GLU A OE2    1 
ATOM   2973 H  H      . GLU A 1 193 ? 4.466   -4.822  -20.462 1.00 24.09  ? 192 GLU A H      1 
ATOM   2974 H  HA     . GLU A 1 193 ? 3.424   -4.213  -22.796 1.00 24.63  ? 192 GLU A HA     1 
ATOM   2975 H  HB2    . GLU A 1 193 ? 4.466   -2.520  -20.803 1.00 23.44  ? 192 GLU A HB2    1 
ATOM   2976 H  HB3    . GLU A 1 193 ? 3.680   -1.986  -22.073 1.00 23.44  ? 192 GLU A HB3    1 
ATOM   2977 H  HG2    . GLU A 1 193 ? 2.304   -3.772  -20.490 1.00 29.02  ? 192 GLU A HG2    1 
ATOM   2978 H  HG3    . GLU A 1 193 ? 2.547   -2.342  -19.856 1.00 29.02  ? 192 GLU A HG3    1 
ATOM   2979 N  N      . LEU A 1 194 ? 6.566   -3.627  -22.478 1.00 18.55  ? 193 LEU A N      1 
ATOM   2980 C  CA     . LEU A 1 194 ? 7.774   -3.389  -23.261 1.00 20.33  ? 193 LEU A CA     1 
ATOM   2981 C  C      . LEU A 1 194 ? 8.029   -4.516  -24.250 1.00 23.20  ? 193 LEU A C      1 
ATOM   2982 O  O      . LEU A 1 194 ? 8.464   -4.267  -25.388 1.00 21.73  ? 193 LEU A O      1 
ATOM   2983 C  CB     . LEU A 1 194 ? 8.981   -3.198  -22.337 1.00 23.18  ? 193 LEU A CB     1 
ATOM   2984 C  CG     . LEU A 1 194 ? 8.992   -1.934  -21.491 1.00 32.05  ? 193 LEU A CG     1 
ATOM   2985 C  CD1    . LEU A 1 194 ? 10.145  -2.038  -20.523 1.00 40.12  ? 193 LEU A CD1    1 
ATOM   2986 C  CD2    . LEU A 1 194 ? 9.139   -0.683  -22.314 1.00 30.56  ? 193 LEU A CD2    1 
ATOM   2987 H  H      . LEU A 1 194 ? 6.695   -3.712  -21.632 1.00 22.28  ? 193 LEU A H      1 
ATOM   2988 H  HA     . LEU A 1 194 ? 7.658   -2.571  -23.769 1.00 24.41  ? 193 LEU A HA     1 
ATOM   2989 H  HB2    . LEU A 1 194 ? 9.019   -3.952  -21.728 1.00 27.83  ? 193 LEU A HB2    1 
ATOM   2990 H  HB3    . LEU A 1 194 ? 9.782   -3.185  -22.883 1.00 27.83  ? 193 LEU A HB3    1 
ATOM   2991 H  HG     . LEU A 1 194 ? 8.167   -1.876  -20.984 1.00 38.48  ? 193 LEU A HG     1 
ATOM   2992 H  HD11   . LEU A 1 194 ? 10.168  -1.239  -19.974 1.00 48.16  ? 193 LEU A HD11   1 
ATOM   2993 H  HD12   . LEU A 1 194 ? 10.019  -2.820  -19.964 1.00 48.16  ? 193 LEU A HD12   1 
ATOM   2994 H  HD13   . LEU A 1 194 ? 10.971  -2.119  -21.025 1.00 48.16  ? 193 LEU A HD13   1 
ATOM   2995 H  HD21   . LEU A 1 194 ? 9.140   0.086   -21.723 1.00 36.69  ? 193 LEU A HD21   1 
ATOM   2996 H  HD22   . LEU A 1 194 ? 9.975   -0.724  -22.804 1.00 36.69  ? 193 LEU A HD22   1 
ATOM   2997 H  HD23   . LEU A 1 194 ? 8.395   -0.624  -22.934 1.00 36.69  ? 193 LEU A HD23   1 
ATOM   2998 N  N      . ASN A 1 195 ? 7.757   -5.768  -23.853 1.00 24.50  ? 194 ASN A N      1 
ATOM   2999 C  CA     . ASN A 1 195 ? 7.982   -6.865  -24.781 1.00 26.18  ? 194 ASN A CA     1 
ATOM   3000 C  C      . ASN A 1 195 ? 6.991   -6.829  -25.939 1.00 25.54  ? 194 ASN A C      1 
ATOM   3001 O  O      . ASN A 1 195 ? 7.362   -7.094  -27.086 1.00 26.18  ? 194 ASN A O      1 
ATOM   3002 C  CB     . ASN A 1 195 ? 7.903   -8.202  -24.057 1.00 30.95  ? 194 ASN A CB     1 
ATOM   3003 C  CG     . ASN A 1 195 ? 9.169   -8.520  -23.295 1.00 41.38  ? 194 ASN A CG     1 
ATOM   3004 O  OD1    . ASN A 1 195 ? 10.238  -7.979  -23.588 1.00 45.21  ? 194 ASN A OD1    1 
ATOM   3005 N  ND2    . ASN A 1 195 ? 9.062   -9.414  -22.319 1.00 46.27  ? 194 ASN A ND2    1 
ATOM   3006 H  H      . ASN A 1 195 ? 7.453   -5.994  -23.081 1.00 29.42  ? 194 ASN A H      1 
ATOM   3007 H  HA     . ASN A 1 195 ? 8.874   -6.782  -25.152 1.00 31.44  ? 194 ASN A HA     1 
ATOM   3008 H  HB2    . ASN A 1 195 ? 7.169   -8.177  -23.424 1.00 37.16  ? 194 ASN A HB2    1 
ATOM   3009 H  HB3    . ASN A 1 195 ? 7.758   -8.907  -24.707 1.00 37.16  ? 194 ASN A HB3    1 
ATOM   3010 H  HD21   . ASN A 1 195 ? 9.753   -9.630  -21.855 1.00 55.54  ? 194 ASN A HD21   1 
ATOM   3011 H  HD22   . ASN A 1 195 ? 8.301   -9.778  -22.150 1.00 55.54  ? 194 ASN A HD22   1 
ATOM   3012 N  N      . TYR A 1 196 ? 5.730   -6.502  -25.662 1.00 21.89  ? 195 TYR A N      1 
ATOM   3013 C  CA     . TYR A 1 196 ? 4.748   -6.391  -26.726 1.00 21.39  ? 195 TYR A CA     1 
ATOM   3014 C  C      . TYR A 1 196 ? 5.171   -5.327  -27.732 1.00 22.05  ? 195 TYR A C      1 
ATOM   3015 O  O      . TYR A 1 196 ? 5.212   -5.576  -28.944 1.00 23.15  ? 195 TYR A O      1 
ATOM   3016 C  CB     . TYR A 1 196 ? 3.369   -6.063  -26.146 1.00 20.36  ? 195 TYR A CB     1 
ATOM   3017 C  CG     . TYR A 1 196 ? 2.385   -6.049  -27.216 1.00 23.77  ? 195 TYR A CG     1 
ATOM   3018 C  CD1    . TYR A 1 196 ? 1.788   -7.221  -27.648 1.00 27.27  ? 195 TYR A CD1    1 
ATOM   3019 C  CD2    . TYR A 1 196 ? 2.130   -4.886  -27.907 1.00 29.51  ? 195 TYR A CD2    1 
ATOM   3020 C  CE1    . TYR A 1 196 ? 0.934   -7.217  -28.732 1.00 32.72  ? 195 TYR A CE1    1 
ATOM   3021 C  CE2    . TYR A 1 196 ? 1.286   -4.873  -28.982 1.00 30.60  ? 195 TYR A CE2    1 
ATOM   3022 C  CZ     . TYR A 1 196 ? 0.690   -6.038  -29.387 1.00 34.01  ? 195 TYR A CZ     1 
ATOM   3023 O  OH     . TYR A 1 196 ? -0.162  -6.025  -30.446 1.00 39.05  ? 195 TYR A OH     1 
ATOM   3024 H  H      . TYR A 1 196 ? 5.425   -6.341  -24.875 1.00 26.28  ? 195 TYR A H      1 
ATOM   3025 H  HA     . TYR A 1 196 ? 4.686   -7.240  -27.192 1.00 25.69  ? 195 TYR A HA     1 
ATOM   3026 H  HB2    . TYR A 1 196 ? 3.117   -6.742  -25.501 1.00 24.45  ? 195 TYR A HB2    1 
ATOM   3027 H  HB3    . TYR A 1 196 ? 3.390   -5.187  -25.731 1.00 24.45  ? 195 TYR A HB3    1 
ATOM   3028 H  HD1    . TYR A 1 196 ? 1.973   -8.021  -27.210 1.00 32.74  ? 195 TYR A HD1    1 
ATOM   3029 H  HD2    . TYR A 1 196 ? 2.549   -4.098  -27.645 1.00 35.43  ? 195 TYR A HD2    1 
ATOM   3030 H  HE1    . TYR A 1 196 ? 0.521   -8.003  -29.009 1.00 39.28  ? 195 TYR A HE1    1 
ATOM   3031 H  HE2    . TYR A 1 196 ? 1.110   -4.077  -29.429 1.00 36.74  ? 195 TYR A HE2    1 
ATOM   3032 H  HH     . TYR A 1 196 ? -0.460  -6.798  -30.585 1.00 46.88  ? 195 TYR A HH     1 
ATOM   3033 N  N      . PHE A 1 197 ? 5.502   -4.126  -27.243 1.00 21.91  ? 196 PHE A N      1 
ATOM   3034 C  CA     . PHE A 1 197 ? 5.838   -3.045  -28.168 1.00 22.33  ? 196 PHE A CA     1 
ATOM   3035 C  C      . PHE A 1 197 ? 7.142   -3.317  -28.901 1.00 24.81  ? 196 PHE A C      1 
ATOM   3036 O  O      . PHE A 1 197 ? 7.268   -2.946  -30.073 1.00 24.53  ? 196 PHE A O      1 
ATOM   3037 C  CB     . PHE A 1 197 ? 5.898   -1.708  -27.433 1.00 22.33  ? 196 PHE A CB     1 
ATOM   3038 C  CG     . PHE A 1 197 ? 4.534   -1.106  -27.220 1.00 23.16  ? 196 PHE A CG     1 
ATOM   3039 C  CD1    . PHE A 1 197 ? 3.861   -0.535  -28.277 1.00 26.28  ? 196 PHE A CD1    1 
ATOM   3040 C  CD2    . PHE A 1 197 ? 3.917   -1.150  -25.980 1.00 22.55  ? 196 PHE A CD2    1 
ATOM   3041 C  CE1    . PHE A 1 197 ? 2.594   0.000   -28.111 1.00 26.68  ? 196 PHE A CE1    1 
ATOM   3042 C  CE2    . PHE A 1 197 ? 2.646   -0.615  -25.801 1.00 23.18  ? 196 PHE A CE2    1 
ATOM   3043 C  CZ     . PHE A 1 197 ? 1.986   -0.043  -26.893 1.00 25.39  ? 196 PHE A CZ     1 
ATOM   3044 H  H      . PHE A 1 197 ? 5.538   -3.918  -26.410 1.00 26.32  ? 196 PHE A H      1 
ATOM   3045 H  HA     . PHE A 1 197 ? 5.137   -2.981  -28.835 1.00 26.82  ? 196 PHE A HA     1 
ATOM   3046 H  HB2    . PHE A 1 197 ? 6.306   -1.842  -26.564 1.00 26.82  ? 196 PHE A HB2    1 
ATOM   3047 H  HB3    . PHE A 1 197 ? 6.424   -1.083  -27.956 1.00 26.82  ? 196 PHE A HB3    1 
ATOM   3048 H  HD1    . PHE A 1 197 ? 4.263   -0.509  -29.115 1.00 31.55  ? 196 PHE A HD1    1 
ATOM   3049 H  HD2    . PHE A 1 197 ? 4.357   -1.540  -25.260 1.00 27.08  ? 196 PHE A HD2    1 
ATOM   3050 H  HE1    . PHE A 1 197 ? 2.155   0.387   -28.834 1.00 32.03  ? 196 PHE A HE1    1 
ATOM   3051 H  HE2    . PHE A 1 197 ? 2.237   -0.642  -24.966 1.00 27.84  ? 196 PHE A HE2    1 
ATOM   3052 H  HZ     . PHE A 1 197 ? 1.140   0.327   -26.783 1.00 30.49  ? 196 PHE A HZ     1 
ATOM   3053 N  N      . ALA A 1 198 ? 8.113   -3.965  -28.248 1.00 24.76  ? 197 ALA A N      1 
ATOM   3054 C  CA     . ALA A 1 198 ? 9.345   -4.318  -28.944 1.00 28.44  ? 197 ALA A CA     1 
ATOM   3055 C  C      . ALA A 1 198 ? 9.058   -5.146  -30.183 1.00 29.06  ? 197 ALA A C      1 
ATOM   3056 O  O      . ALA A 1 198 ? 9.664   -4.934  -31.239 1.00 31.66  ? 197 ALA A O      1 
ATOM   3057 C  CB     . ALA A 1 198 ? 10.282  -5.075  -28.006 1.00 31.66  ? 197 ALA A CB     1 
ATOM   3058 H  H      . ALA A 1 198 ? 8.081   -4.206  -27.423 1.00 29.73  ? 197 ALA A H      1 
ATOM   3059 H  HA     . ALA A 1 198 ? 9.794   -3.505  -29.224 1.00 34.15  ? 197 ALA A HA     1 
ATOM   3060 H  HB1    . ALA A 1 198 ? 11.094  -5.301  -28.486 1.00 38.01  ? 197 ALA A HB1    1 
ATOM   3061 H  HB2    . ALA A 1 198 ? 10.492  -4.510  -27.246 1.00 38.01  ? 197 ALA A HB2    1 
ATOM   3062 H  HB3    . ALA A 1 198 ? 9.840   -5.885  -27.705 1.00 38.01  ? 197 ALA A HB3    1 
ATOM   3063 N  N      . LYS A 1 199 ? 8.152   -6.113  -30.059 1.00 27.03  ? 198 LYS A N      1 
ATOM   3064 C  CA     . LYS A 1 199 ? 7.812   -6.984  -31.162 1.00 30.60  ? 198 LYS A CA     1 
ATOM   3065 C  C      . LYS A 1 199 ? 6.981   -6.246  -32.202 1.00 28.78  ? 198 LYS A C      1 
ATOM   3066 O  O      . LYS A 1 199 ? 7.211   -6.393  -33.409 1.00 30.25  ? 198 LYS A O      1 
ATOM   3067 C  CB     . LYS A 1 199 ? 7.065   -8.206  -30.635 1.00 42.26  ? 198 LYS A CB     1 
ATOM   3068 C  CG     . LYS A 1 199 ? 6.636   -9.185  -31.715 1.00 66.95  ? 198 LYS A CG     1 
ATOM   3069 C  CD     . LYS A 1 199 ? 5.958   -10.421 -31.127 1.00 86.21  ? 198 LYS A CD     1 
ATOM   3070 C  CE     . LYS A 1 199 ? 5.433   -11.343 -32.228 1.00 97.89  ? 198 LYS A CE     1 
ATOM   3071 N  NZ     . LYS A 1 199 ? 4.814   -12.584 -31.678 1.00 103.10 1 198 LYS A NZ     1 
ATOM   3072 H  H      . LYS A 1 199 ? 7.720   -6.282  -29.335 1.00 32.46  ? 198 LYS A H      1 
ATOM   3073 H  HA     . LYS A 1 199 ? 8.627   -7.290  -31.589 1.00 36.74  ? 198 LYS A HA     1 
ATOM   3074 H  HB2    . LYS A 1 199 ? 7.642   -8.682  -30.018 1.00 50.73  ? 198 LYS A HB2    1 
ATOM   3075 H  HB3    . LYS A 1 199 ? 6.266   -7.908  -30.173 1.00 50.73  ? 198 LYS A HB3    1 
ATOM   3076 H  HG2    . LYS A 1 199 ? 6.006   -8.748  -32.310 1.00 80.36  ? 198 LYS A HG2    1 
ATOM   3077 H  HG3    . LYS A 1 199 ? 7.418   -9.475  -32.211 1.00 80.36  ? 198 LYS A HG3    1 
ATOM   3078 H  HD2    . LYS A 1 199 ? 6.600   -10.916 -30.595 1.00 103.47 ? 198 LYS A HD2    1 
ATOM   3079 H  HD3    . LYS A 1 199 ? 5.208   -10.144 -30.578 1.00 103.47 ? 198 LYS A HD3    1 
ATOM   3080 H  HE2    . LYS A 1 199 ? 4.758   -10.872 -32.742 1.00 117.49 ? 198 LYS A HE2    1 
ATOM   3081 H  HE3    . LYS A 1 199 ? 6.170   -11.602 -32.804 1.00 117.49 ? 198 LYS A HE3    1 
ATOM   3082 H  HZ1    . LYS A 1 199 ? 4.520   -13.097 -32.343 1.00 123.73 ? 198 LYS A HZ1    1 
ATOM   3083 H  HZ2    . LYS A 1 199 ? 5.416   -13.039 -31.205 1.00 123.73 ? 198 LYS A HZ2    1 
ATOM   3084 H  HZ3    . LYS A 1 199 ? 4.130   -12.374 -31.149 1.00 123.73 ? 198 LYS A HZ3    1 
ATOM   3085 N  N      . ALA A 1 200 ? 6.022   -5.434  -31.757 1.00 24.98  ? 199 ALA A N      1 
ATOM   3086 C  CA     . ALA A 1 200 ? 5.109   -4.774  -32.685 1.00 26.55  ? 199 ALA A CA     1 
ATOM   3087 C  C      . ALA A 1 200 ? 5.776   -3.628  -33.428 1.00 26.34  ? 199 ALA A C      1 
ATOM   3088 O  O      . ALA A 1 200 ? 5.346   -3.264  -34.540 1.00 29.59  ? 199 ALA A O      1 
ATOM   3089 C  CB     . ALA A 1 200 ? 3.902   -4.247  -31.909 1.00 28.30  ? 199 ALA A CB     1 
ATOM   3090 H  H      . ALA A 1 200 ? 5.881   -5.251  -30.929 1.00 30.00  ? 199 ALA A H      1 
ATOM   3091 H  HA     . ALA A 1 200 ? 4.794   -5.418  -33.338 1.00 31.88  ? 199 ALA A HA     1 
ATOM   3092 H  HB1    . ALA A 1 200 ? 3.297   -3.809  -32.527 1.00 33.98  ? 199 ALA A HB1    1 
ATOM   3093 H  HB2    . ALA A 1 200 ? 3.454   -4.992  -31.479 1.00 33.98  ? 199 ALA A HB2    1 
ATOM   3094 H  HB3    . ALA A 1 200 ? 4.208   -3.614  -31.241 1.00 33.98  ? 199 ALA A HB3    1 
ATOM   3095 N  N      . LEU A 1 201 ? 6.811   -3.039  -32.841 1.00 25.75  ? 200 LEU A N      1 
ATOM   3096 C  CA     . LEU A 1 201 ? 7.479   -1.901  -33.456 1.00 28.01  ? 200 LEU A CA     1 
ATOM   3097 C  C      . LEU A 1 201 ? 8.740   -2.267  -34.221 1.00 30.13  ? 200 LEU A C      1 
ATOM   3098 O  O      . LEU A 1 201 ? 9.272   -1.409  -34.940 1.00 31.36  ? 200 LEU A O      1 
ATOM   3099 C  CB     . LEU A 1 201 ? 7.833   -0.865  -32.399 1.00 28.13  ? 200 LEU A CB     1 
ATOM   3100 C  CG     . LEU A 1 201 ? 6.635   -0.216  -31.693 1.00 30.21  ? 200 LEU A CG     1 
ATOM   3101 C  CD1    . LEU A 1 201 ? 7.126   0.718   -30.625 1.00 28.97  ? 200 LEU A CD1    1 
ATOM   3102 C  CD2    . LEU A 1 201 ? 5.729   0.518   -32.723 1.00 35.48  ? 200 LEU A CD2    1 
ATOM   3103 H  H      . LEU A 1 201 ? 7.145   -3.280  -32.086 1.00 30.92  ? 200 LEU A H      1 
ATOM   3104 H  HA     . LEU A 1 201 ? 6.867   -1.485  -34.082 1.00 33.63  ? 200 LEU A HA     1 
ATOM   3105 H  HB2    . LEU A 1 201 ? 8.376   -1.292  -31.719 1.00 33.78  ? 200 LEU A HB2    1 
ATOM   3106 H  HB3    . LEU A 1 201 ? 8.341   -0.155  -32.822 1.00 33.78  ? 200 LEU A HB3    1 
ATOM   3107 H  HG     . LEU A 1 201 ? 6.106   -0.908  -31.267 1.00 36.27  ? 200 LEU A HG     1 
ATOM   3108 H  HD11   . LEU A 1 201 ? 6.363   1.123   -30.184 1.00 34.78  ? 200 LEU A HD11   1 
ATOM   3109 H  HD12   . LEU A 1 201 ? 7.651   0.214   -29.983 1.00 34.78  ? 200 LEU A HD12   1 
ATOM   3110 H  HD13   . LEU A 1 201 ? 7.675   1.404   -31.035 1.00 34.78  ? 200 LEU A HD13   1 
ATOM   3111 H  HD21   . LEU A 1 201 ? 4.980   0.919   -32.255 1.00 42.59  ? 200 LEU A HD21   1 
ATOM   3112 H  HD22   . LEU A 1 201 ? 6.249   1.206   -33.167 1.00 42.59  ? 200 LEU A HD22   1 
ATOM   3113 H  HD23   . LEU A 1 201 ? 5.407   -0.126  -33.374 1.00 42.59  ? 200 LEU A HD23   1 
ATOM   3114 N  N      . GLU A 1 202 ? 9.174   -3.525  -34.146 1.00 31.59  ? 201 GLU A N      1 
ATOM   3115 C  CA     A GLU A 1 202 ? 10.416  -3.926  -34.801 0.60 34.80  ? 201 GLU A CA     1 
ATOM   3116 C  CA     B GLU A 1 202 ? 10.410  -3.945  -34.804 0.40 34.86  ? 201 GLU A CA     1 
ATOM   3117 C  C      . GLU A 1 202 ? 10.300  -3.834  -36.322 1.00 35.07  ? 201 GLU A C      1 
ATOM   3118 O  O      . GLU A 1 202 ? 11.203  -3.322  -36.990 1.00 35.82  ? 201 GLU A O      1 
ATOM   3119 C  CB     A GLU A 1 202 ? 10.793  -5.344  -34.369 0.60 40.15  ? 201 GLU A CB     1 
ATOM   3120 C  CB     B GLU A 1 202 ? 10.746  -5.382  -34.398 0.40 40.17  ? 201 GLU A CB     1 
ATOM   3121 C  CG     A GLU A 1 202 ? 12.100  -5.881  -34.969 0.60 50.16  ? 201 GLU A CG     1 
ATOM   3122 C  CG     B GLU A 1 202 ? 12.021  -5.954  -35.042 0.40 50.25  ? 201 GLU A CG     1 
ATOM   3123 C  CD     A GLU A 1 202 ? 13.328  -5.076  -34.555 0.60 57.02  ? 201 GLU A CD     1 
ATOM   3124 C  CD     B GLU A 1 202 ? 11.756  -7.076  -36.042 0.40 61.75  ? 201 GLU A CD     1 
ATOM   3125 O  OE1    A GLU A 1 202 ? 13.277  -4.386  -33.513 0.60 59.06  ? 201 GLU A OE1    1 
ATOM   3126 O  OE1    B GLU A 1 202 ? 10.644  -7.648  -36.033 0.40 69.49  ? 201 GLU A OE1    1 
ATOM   3127 O  OE2    A GLU A 1 202 ? 14.348  -5.132  -35.284 0.60 63.70  1 201 GLU A OE2    1 
ATOM   3128 O  OE2    B GLU A 1 202 ? 12.671  -7.389  -36.840 0.40 70.02  1 201 GLU A OE2    1 
ATOM   3129 H  H      A GLU A 1 202 ? 8.772   -4.159  -33.727 0.60 37.92  ? 201 GLU A H      1 
ATOM   3130 H  H      B GLU A 1 202 ? 8.771   -4.154  -33.721 0.40 37.92  ? 201 GLU A H      1 
ATOM   3131 H  HA     A GLU A 1 202 ? 11.126  -3.329  -34.520 0.60 41.78  ? 201 GLU A HA     1 
ATOM   3132 H  HA     B GLU A 1 202 ? 11.136  -3.372  -34.513 0.40 41.85  ? 201 GLU A HA     1 
ATOM   3133 H  HB2    A GLU A 1 202 ? 10.887  -5.357  -33.404 0.60 48.20  ? 201 GLU A HB2    1 
ATOM   3134 H  HB2    B GLU A 1 202 ? 10.865  -5.411  -33.436 0.40 48.22  ? 201 GLU A HB2    1 
ATOM   3135 H  HB3    A GLU A 1 202 ? 10.080  -5.947  -34.634 0.60 48.20  ? 201 GLU A HB3    1 
ATOM   3136 H  HB3    B GLU A 1 202 ? 10.006  -5.956  -34.652 0.40 48.22  ? 201 GLU A HB3    1 
ATOM   3137 H  HG2    A GLU A 1 202 ? 12.230  -6.795  -34.672 0.60 60.21  ? 201 GLU A HG2    1 
ATOM   3138 H  HG2    B GLU A 1 202 ? 12.480  -5.240  -35.512 0.40 60.32  ? 201 GLU A HG2    1 
ATOM   3139 H  HG3    A GLU A 1 202 ? 12.037  -5.853  -35.936 0.60 60.21  ? 201 GLU A HG3    1 
ATOM   3140 H  HG3    B GLU A 1 202 ? 12.592  -6.308  -34.343 0.40 60.32  ? 201 GLU A HG3    1 
ATOM   3141 N  N      . SER A 1 203 ? 9.223   -4.357  -36.893 1.00 34.02  ? 202 SER A N      1 
ATOM   3142 C  CA     . SER A 1 203 ? 8.985   -4.256  -38.338 1.00 38.01  ? 202 SER A CA     1 
ATOM   3143 C  C      . SER A 1 203 ? 7.492   -4.127  -38.531 1.00 32.92  ? 202 SER A C      1 
ATOM   3144 O  O      . SER A 1 203 ? 6.803   -5.103  -38.853 1.00 35.01  ? 202 SER A O      1 
ATOM   3145 C  CB     . SER A 1 203 ? 9.532   -5.470  -39.088 1.00 51.53  ? 202 SER A CB     1 
ATOM   3146 O  OG     . SER A 1 203 ? 9.079   -6.671  -38.481 1.00 65.17  ? 202 SER A OG     1 
ATOM   3147 H  H      . SER A 1 203 ? 8.606   -4.780  -36.468 1.00 40.84  ? 202 SER A H      1 
ATOM   3148 H  HA     . SER A 1 203 ? 9.414   -3.457  -38.684 1.00 45.63  ? 202 SER A HA     1 
ATOM   3149 H  HB2    . SER A 1 203 ? 9.221   -5.442  -40.007 1.00 61.85  ? 202 SER A HB2    1 
ATOM   3150 H  HB3    . SER A 1 203 ? 10.502  -5.448  -39.064 1.00 61.85  ? 202 SER A HB3    1 
ATOM   3151 H  HG     . SER A 1 203 ? 9.341   -6.706  -37.683 1.00 78.22  ? 202 SER A HG     1 
ATOM   3152 N  N      . PRO A 1 204 ? 6.939   -2.945  -38.274 1.00 28.97  ? 203 PRO A N      1 
ATOM   3153 C  CA     . PRO A 1 204 ? 5.488   -2.798  -38.338 1.00 29.47  ? 203 PRO A CA     1 
ATOM   3154 C  C      . PRO A 1 204 ? 4.948   -3.218  -39.689 1.00 31.03  ? 203 PRO A C      1 
ATOM   3155 O  O      . PRO A 1 204 ? 5.620   -3.090  -40.727 1.00 32.59  ? 203 PRO A O      1 
ATOM   3156 C  CB     . PRO A 1 204 ? 5.270   -1.304  -38.104 1.00 31.97  ? 203 PRO A CB     1 
ATOM   3157 C  CG     . PRO A 1 204 ? 6.579   -0.786  -37.597 1.00 33.86  ? 203 PRO A CG     1 
ATOM   3158 C  CD     . PRO A 1 204 ? 7.612   -1.643  -38.180 1.00 30.39  ? 203 PRO A CD     1 
ATOM   3159 H  HA     . PRO A 1 204 ? 5.057   -3.309  -37.635 1.00 35.38  ? 203 PRO A HA     1 
ATOM   3160 H  HB2    . PRO A 1 204 ? 5.033   -0.874  -38.941 1.00 38.38  ? 203 PRO A HB2    1 
ATOM   3161 H  HB3    . PRO A 1 204 ? 4.571   -1.176  -37.443 1.00 38.38  ? 203 PRO A HB3    1 
ATOM   3162 H  HG2    . PRO A 1 204 ? 6.697   0.132   -37.884 1.00 40.65  ? 203 PRO A HG2    1 
ATOM   3163 H  HG3    . PRO A 1 204 ? 6.597   -0.844  -36.628 1.00 40.65  ? 203 PRO A HG3    1 
ATOM   3164 H  HD2    . PRO A 1 204 ? 7.860   -1.325  -39.062 1.00 36.48  ? 203 PRO A HD2    1 
ATOM   3165 H  HD3    . PRO A 1 204 ? 8.380   -1.700  -37.590 1.00 36.48  ? 203 PRO A HD3    1 
ATOM   3166 N  N      . GLU A 1 205 ? 3.720   -3.728  -39.664 1.00 31.00  ? 204 GLU A N      1 
ATOM   3167 C  CA     . GLU A 1 205 ? 2.983   -3.959  -40.896 1.00 35.79  ? 204 GLU A CA     1 
ATOM   3168 C  C      . GLU A 1 205 ? 2.618   -2.621  -41.523 1.00 32.98  ? 204 GLU A C      1 
ATOM   3169 O  O      . GLU A 1 205 ? 2.402   -1.629  -40.827 1.00 31.67  ? 204 GLU A O      1 
ATOM   3170 C  CB     . GLU A 1 205 ? 1.723   -4.787  -40.624 1.00 40.91  ? 204 GLU A CB     1 
ATOM   3171 C  CG     . GLU A 1 205 ? 2.006   -6.187  -40.092 1.00 47.82  ? 204 GLU A CG     1 
ATOM   3172 C  CD     . GLU A 1 205 ? 2.798   -7.039  -41.075 1.00 55.23  ? 204 GLU A CD     1 
ATOM   3173 O  OE1    . GLU A 1 205 ? 2.495   -7.017  -42.294 1.00 56.94  ? 204 GLU A OE1    1 
ATOM   3174 O  OE2    . GLU A 1 205 ? 3.738   -7.723  -40.621 1.00 58.09  1 204 GLU A OE2    1 
ATOM   3175 H  H      . GLU A 1 205 ? 3.295   -3.946  -38.950 1.00 37.22  ? 204 GLU A H      1 
ATOM   3176 H  HA     . GLU A 1 205 ? 3.543   -4.448  -41.520 1.00 42.97  ? 204 GLU A HA     1 
ATOM   3177 H  HB2    . GLU A 1 205 ? 1.181   -4.324  -39.966 1.00 49.12  ? 204 GLU A HB2    1 
ATOM   3178 H  HB3    . GLU A 1 205 ? 1.226   -4.880  -41.452 1.00 49.12  ? 204 GLU A HB3    1 
ATOM   3179 H  HG2    . GLU A 1 205 ? 2.521   -6.116  -39.273 1.00 57.40  ? 204 GLU A HG2    1 
ATOM   3180 H  HG3    . GLU A 1 205 ? 1.164   -6.636  -39.917 1.00 57.40  ? 204 GLU A HG3    1 
ATOM   3181 N  N      . ARG A 1 206 ? 2.564   -2.591  -42.851 1.00 31.14  ? 205 ARG A N      1 
ATOM   3182 C  CA     . ARG A 1 206 ? 2.455   -1.304  -43.525 1.00 33.96  ? 205 ARG A CA     1 
ATOM   3183 C  C      . ARG A 1 206 ? 1.344   -1.306  -44.564 1.00 33.99  ? 205 ARG A C      1 
ATOM   3184 O  O      . ARG A 1 206 ? 1.167   -2.298  -45.280 1.00 32.43  ? 205 ARG A O      1 
ATOM   3185 C  CB     . ARG A 1 206 ? 3.797   -0.956  -44.169 1.00 41.38  ? 205 ARG A CB     1 
ATOM   3186 C  CG     . ARG A 1 206 ? 4.842   -0.802  -43.073 1.00 48.94  ? 205 ARG A CG     1 
ATOM   3187 C  CD     . ARG A 1 206 ? 5.790   0.305   -43.318 1.00 46.40  ? 205 ARG A CD     1 
ATOM   3188 N  NE     . ARG A 1 206 ? 6.802   0.383   -42.273 1.00 37.37  ? 205 ARG A NE     1 
ATOM   3189 C  CZ     . ARG A 1 206 ? 6.929   1.379   -41.407 1.00 33.61  ? 205 ARG A CZ     1 
ATOM   3190 N  NH1    . ARG A 1 206 ? 7.906   1.342   -40.516 1.00 34.36  1 205 ARG A NH1    1 
ATOM   3191 N  NH2    . ARG A 1 206 ? 6.104   2.406   -41.428 1.00 29.81  ? 205 ARG A NH2    1 
ATOM   3192 H  H      . ARG A 1 206 ? 2.589   -3.276  -43.369 1.00 37.39  ? 205 ARG A H      1 
ATOM   3193 H  HA     . ARG A 1 206 ? 2.250   -0.619  -42.869 1.00 40.77  ? 205 ARG A HA     1 
ATOM   3194 H  HB2    . ARG A 1 206 ? 4.072   -1.671  -44.764 1.00 49.67  ? 205 ARG A HB2    1 
ATOM   3195 H  HB3    . ARG A 1 206 ? 3.724   -0.117  -44.650 1.00 49.67  ? 205 ARG A HB3    1 
ATOM   3196 H  HG2    . ARG A 1 206 ? 4.392   -0.628  -42.232 1.00 58.75  ? 205 ARG A HG2    1 
ATOM   3197 H  HG3    . ARG A 1 206 ? 5.354   -1.624  -43.009 1.00 58.75  ? 205 ARG A HG3    1 
ATOM   3198 H  HD2    . ARG A 1 206 ? 6.239   0.160   -44.165 1.00 55.70  ? 205 ARG A HD2    1 
ATOM   3199 H  HD3    . ARG A 1 206 ? 5.304   1.144   -43.334 1.00 55.70  ? 205 ARG A HD3    1 
ATOM   3200 H  HE     . ARG A 1 206 ? 7.361   -0.267  -42.214 1.00 44.87  ? 205 ARG A HE     1 
ATOM   3201 H  HH11   . ARG A 1 206 ? 8.445   0.672   -40.496 1.00 41.25  ? 205 ARG A HH11   1 
ATOM   3202 H  HH12   . ARG A 1 206 ? 7.992   1.980   -39.946 1.00 41.25  ? 205 ARG A HH12   1 
ATOM   3203 H  HH21   . ARG A 1 206 ? 5.471   2.437   -42.010 1.00 35.79  ? 205 ARG A HH21   1 
ATOM   3204 H  HH22   . ARG A 1 206 ? 6.197   3.044   -40.860 1.00 35.79  ? 205 ARG A HH22   1 
ATOM   3205 N  N      . PRO A 1 207 ? 0.586   -0.196  -44.693 1.00 33.30  ? 206 PRO A N      1 
ATOM   3206 C  CA     . PRO A 1 207 ? 0.725   1.105   -44.036 1.00 28.38  ? 206 PRO A CA     1 
ATOM   3207 C  C      . PRO A 1 207 ? 0.497   1.065   -42.516 1.00 25.59  ? 206 PRO A C      1 
ATOM   3208 O  O      . PRO A 1 207 ? -0.439  0.412   -42.056 1.00 27.03  ? 206 PRO A O      1 
ATOM   3209 C  CB     . PRO A 1 207 ? -0.367  1.950   -44.684 1.00 29.54  ? 206 PRO A CB     1 
ATOM   3210 C  CG     . PRO A 1 207 ? -0.706  1.265   -45.933 1.00 35.20  ? 206 PRO A CG     1 
ATOM   3211 C  CD     . PRO A 1 207 ? -0.510  -0.186  -45.675 1.00 37.15  ? 206 PRO A CD     1 
ATOM   3212 H  HA     . PRO A 1 207 ? 1.593   1.494   -44.226 1.00 34.08  ? 206 PRO A HA     1 
ATOM   3213 H  HB2    . PRO A 1 207 ? -1.138  1.991   -44.097 1.00 35.47  ? 206 PRO A HB2    1 
ATOM   3214 H  HB3    . PRO A 1 207 ? -0.026  2.840   -44.864 1.00 35.47  ? 206 PRO A HB3    1 
ATOM   3215 H  HG2    . PRO A 1 207 ? -1.631  1.448   -46.162 1.00 42.26  ? 206 PRO A HG2    1 
ATOM   3216 H  HG3    . PRO A 1 207 ? -0.115  1.568   -46.640 1.00 42.26  ? 206 PRO A HG3    1 
ATOM   3217 H  HD2    . PRO A 1 207 ? -1.312  -0.576  -45.293 1.00 44.60  ? 206 PRO A HD2    1 
ATOM   3218 H  HD3    . PRO A 1 207 ? -0.242  -0.643  -46.488 1.00 44.60  ? 206 PRO A HD3    1 
ATOM   3219 N  N      . PHE A 1 208 ? 1.321   1.817   -41.790 1.00 25.05  ? 207 PHE A N      1 
ATOM   3220 C  CA     . PHE A 1 208 ? 1.272   1.934   -40.323 1.00 23.18  ? 207 PHE A CA     1 
ATOM   3221 C  C      . PHE A 1 208 ? 0.641   3.282   -39.994 1.00 23.44  ? 207 PHE A C      1 
ATOM   3222 O  O      . PHE A 1 208 ? 1.210   4.327   -40.320 1.00 25.91  ? 207 PHE A O      1 
ATOM   3223 C  CB     . PHE A 1 208 ? 2.696   1.832   -39.769 1.00 23.31  ? 207 PHE A CB     1 
ATOM   3224 C  CG     . PHE A 1 208 ? 2.824   1.840   -38.239 1.00 23.30  ? 207 PHE A CG     1 
ATOM   3225 C  CD1    . PHE A 1 208 ? 1.734   1.721   -37.386 1.00 23.31  ? 207 PHE A CD1    1 
ATOM   3226 C  CD2    . PHE A 1 208 ? 4.088   1.970   -37.678 1.00 26.56  ? 207 PHE A CD2    1 
ATOM   3227 C  CE1    . PHE A 1 208 ? 1.922   1.744   -36.002 1.00 26.55  ? 207 PHE A CE1    1 
ATOM   3228 C  CE2    . PHE A 1 208 ? 4.277   1.978   -36.326 1.00 26.22  ? 207 PHE A CE2    1 
ATOM   3229 C  CZ     . PHE A 1 208 ? 3.200   1.861   -35.480 1.00 26.41  ? 207 PHE A CZ     1 
ATOM   3230 H  H      . PHE A 1 208 ? 1.948   2.293   -42.138 1.00 30.08  ? 207 PHE A H      1 
ATOM   3231 H  HA     . PHE A 1 208 ? 0.729   1.224   -39.946 1.00 27.84  ? 207 PHE A HA     1 
ATOM   3232 H  HB2    . PHE A 1 208 ? 3.088   1.004   -40.087 1.00 27.99  ? 207 PHE A HB2    1 
ATOM   3233 H  HB3    . PHE A 1 208 ? 3.209   2.582   -40.106 1.00 27.99  ? 207 PHE A HB3    1 
ATOM   3234 H  HD1    . PHE A 1 208 ? 0.877   1.638   -37.737 1.00 27.99  ? 207 PHE A HD1    1 
ATOM   3235 H  HD2    . PHE A 1 208 ? 4.827   2.045   -38.239 1.00 31.89  ? 207 PHE A HD2    1 
ATOM   3236 H  HE1    . PHE A 1 208 ? 1.192   1.661   -35.432 1.00 31.88  ? 207 PHE A HE1    1 
ATOM   3237 H  HE2    . PHE A 1 208 ? 5.135   2.066   -35.977 1.00 31.48  ? 207 PHE A HE2    1 
ATOM   3238 H  HZ     . PHE A 1 208 ? 3.328   1.875   -34.559 1.00 31.71  ? 207 PHE A HZ     1 
ATOM   3239 N  N      . LEU A 1 209 ? -0.552  3.251   -39.404 1.00 21.73  ? 208 LEU A N      1 
ATOM   3240 C  CA     . LEU A 1 209 ? -1.305  4.444   -39.040 1.00 21.35  ? 208 LEU A CA     1 
ATOM   3241 C  C      . LEU A 1 209 ? -1.183  4.730   -37.546 1.00 21.91  ? 208 LEU A C      1 
ATOM   3242 O  O      . LEU A 1 209 ? -1.386  3.835   -36.720 1.00 21.66  ? 208 LEU A O      1 
ATOM   3243 C  CB     . LEU A 1 209 ? -2.773  4.249   -39.409 1.00 21.69  ? 208 LEU A CB     1 
ATOM   3244 C  CG     . LEU A 1 209 ? -3.830  5.210   -38.869 1.00 24.97  ? 208 LEU A CG     1 
ATOM   3245 C  CD1    . LEU A 1 209 ? -3.700  6.590   -39.494 1.00 25.04  ? 208 LEU A CD1    1 
ATOM   3246 C  CD2    . LEU A 1 209 ? -5.190  4.621   -39.129 1.00 26.82  ? 208 LEU A CD2    1 
ATOM   3247 H  H      . LEU A 1 209 ? -0.958  2.521   -39.198 1.00 26.09  ? 208 LEU A H      1 
ATOM   3248 H  HA     . LEU A 1 209 ? -0.961  5.208   -39.530 1.00 25.64  ? 208 LEU A HA     1 
ATOM   3249 H  HB2    . LEU A 1 209 ? -2.837  4.285   -40.377 1.00 26.04  ? 208 LEU A HB2    1 
ATOM   3250 H  HB3    . LEU A 1 209 ? -3.032  3.362   -39.114 1.00 26.04  ? 208 LEU A HB3    1 
ATOM   3251 H  HG     . LEU A 1 209 ? -3.718  5.300   -37.910 1.00 29.98  ? 208 LEU A HG     1 
ATOM   3252 H  HD11   . LEU A 1 209 ? -4.386  7.169   -39.126 1.00 30.06  ? 208 LEU A HD11   1 
ATOM   3253 H  HD12   . LEU A 1 209 ? -2.821  6.947   -39.289 1.00 30.06  ? 208 LEU A HD12   1 
ATOM   3254 H  HD13   . LEU A 1 209 ? -3.811  6.514   -40.454 1.00 30.06  ? 208 LEU A HD13   1 
ATOM   3255 H  HD21   . LEU A 1 209 ? -5.866  5.227   -38.788 1.00 32.20  ? 208 LEU A HD21   1 
ATOM   3256 H  HD22   . LEU A 1 209 ? -5.304  4.501   -40.085 1.00 32.20  ? 208 LEU A HD22   1 
ATOM   3257 H  HD23   . LEU A 1 209 ? -5.255  3.765   -38.678 1.00 32.20  ? 208 LEU A HD23   1 
ATOM   3258 N  N      . ALA A 1 210 ? -0.899  5.987   -37.200 1.00 21.20  ? 209 ALA A N      1 
ATOM   3259 C  CA     . ALA A 1 210 ? -1.003  6.471   -35.829 1.00 23.17  ? 209 ALA A CA     1 
ATOM   3260 C  C      . ALA A 1 210 ? -2.225  7.371   -35.725 1.00 23.30  ? 209 ALA A C      1 
ATOM   3261 O  O      . ALA A 1 210 ? -2.450  8.213   -36.595 1.00 26.00  ? 209 ALA A O      1 
ATOM   3262 C  CB     . ALA A 1 210 ? 0.250   7.243   -35.397 1.00 26.00  ? 209 ALA A CB     1 
ATOM   3263 H  H      . ALA A 1 210 ? -0.638  6.589   -37.756 1.00 25.46  ? 209 ALA A H      1 
ATOM   3264 H  HA     . ALA A 1 210 ? -1.123  5.719   -35.229 1.00 27.82  ? 209 ALA A HA     1 
ATOM   3265 H  HB1    . ALA A 1 210 ? 0.135   7.544   -34.482 1.00 31.22  ? 209 ALA A HB1    1 
ATOM   3266 H  HB2    . ALA A 1 210 ? 1.019   6.655   -35.458 1.00 31.22  ? 209 ALA A HB2    1 
ATOM   3267 H  HB3    . ALA A 1 210 ? 0.369   8.006   -35.984 1.00 31.22  ? 209 ALA A HB3    1 
ATOM   3268 N  N      . ILE A 1 211 ? -3.049  7.136   -34.714 1.00 18.33  ? 210 ILE A N      1 
ATOM   3269 C  CA     . ILE A 1 211 ? -4.197  7.974   -34.418 1.00 17.98  ? 210 ILE A CA     1 
ATOM   3270 C  C      . ILE A 1 211 ? -3.894  8.708   -33.118 1.00 18.90  ? 210 ILE A C      1 
ATOM   3271 O  O      . ILE A 1 211 ? -3.738  8.082   -32.061 1.00 18.28  ? 210 ILE A O      1 
ATOM   3272 C  CB     . ILE A 1 211 ? -5.483  7.148   -34.300 1.00 20.53  ? 210 ILE A CB     1 
ATOM   3273 C  CG1    . ILE A 1 211 ? -5.664  6.290   -35.557 1.00 24.50  ? 210 ILE A CG1    1 
ATOM   3274 C  CG2    . ILE A 1 211 ? -6.672  8.060   -34.043 1.00 20.44  ? 210 ILE A CG2    1 
ATOM   3275 C  CD1    . ILE A 1 211 ? -6.872  5.406   -35.545 1.00 27.38  ? 210 ILE A CD1    1 
ATOM   3276 H  H      . ILE A 1 211 ? -2.959  6.476   -34.169 1.00 22.02  ? 210 ILE A H      1 
ATOM   3277 H  HA     . ILE A 1 211 ? -4.313  8.629   -35.124 1.00 21.59  ? 210 ILE A HA     1 
ATOM   3278 H  HB     . ILE A 1 211 ? -5.390  6.553   -33.540 1.00 24.65  ? 210 ILE A HB     1 
ATOM   3279 H  HG12   . ILE A 1 211 ? -5.738  6.878   -36.325 1.00 29.42  ? 210 ILE A HG12   1 
ATOM   3280 H  HG13   . ILE A 1 211 ? -4.885  5.720   -35.657 1.00 29.42  ? 210 ILE A HG13   1 
ATOM   3281 H  HG21   . ILE A 1 211 ? -7.474  7.519   -33.972 1.00 24.55  ? 210 ILE A HG21   1 
ATOM   3282 H  HG22   . ILE A 1 211 ? -6.524  8.545   -33.216 1.00 24.55  ? 210 ILE A HG22   1 
ATOM   3283 H  HG23   . ILE A 1 211 ? -6.757  8.683   -34.782 1.00 24.55  ? 210 ILE A HG23   1 
ATOM   3284 H  HD11   . ILE A 1 211 ? -6.903  4.904   -36.374 1.00 32.88  ? 210 ILE A HD11   1 
ATOM   3285 H  HD12   . ILE A 1 211 ? -6.810  4.798   -34.792 1.00 32.88  ? 210 ILE A HD12   1 
ATOM   3286 H  HD13   . ILE A 1 211 ? -7.665  5.958   -35.461 1.00 32.88  ? 210 ILE A HD13   1 
ATOM   3287 N  N      . LEU A 1 212 ? -3.831  10.033  -33.196 1.00 19.31  ? 211 LEU A N      1 
ATOM   3288 C  CA     . LEU A 1 212 ? -3.472  10.880  -32.069 1.00 21.50  ? 211 LEU A CA     1 
ATOM   3289 C  C      . LEU A 1 212 ? -4.632  11.822  -31.775 1.00 23.24  ? 211 LEU A C      1 
ATOM   3290 O  O      . LEU A 1 212 ? -4.974  12.669  -32.608 1.00 24.61  ? 211 LEU A O      1 
ATOM   3291 C  CB     . LEU A 1 212 ? -2.195  11.661  -32.382 1.00 30.58  ? 211 LEU A CB     1 
ATOM   3292 C  CG     . LEU A 1 212 ? -1.669  12.572  -31.272 1.00 50.05  ? 211 LEU A CG     1 
ATOM   3293 C  CD1    . LEU A 1 212 ? -1.610  11.868  -29.882 1.00 58.49  ? 211 LEU A CD1    1 
ATOM   3294 C  CD2    . LEU A 1 212 ? -0.297  13.102  -31.682 1.00 57.28  ? 211 LEU A CD2    1 
ATOM   3295 H  H      . LEU A 1 212 ? -3.997  10.475  -33.915 1.00 23.19  ? 211 LEU A H      1 
ATOM   3296 H  HA     . LEU A 1 212 ? -3.314  10.330  -31.286 1.00 25.82  ? 211 LEU A HA     1 
ATOM   3297 H  HB2    . LEU A 1 212 ? -1.492  11.025  -32.589 1.00 36.71  ? 211 LEU A HB2    1 
ATOM   3298 H  HB3    . LEU A 1 212 ? -2.362  12.219  -33.157 1.00 36.71  ? 211 LEU A HB3    1 
ATOM   3299 H  HG     . LEU A 1 212 ? -2.265  13.333  -31.189 1.00 60.08  ? 211 LEU A HG     1 
ATOM   3300 H  HD11   . LEU A 1 212 ? -1.270  12.496  -29.225 1.00 70.20  ? 211 LEU A HD11   1 
ATOM   3301 H  HD12   . LEU A 1 212 ? -2.503  11.582  -29.635 1.00 70.20  ? 211 LEU A HD12   1 
ATOM   3302 H  HD13   . LEU A 1 212 ? -1.021  11.100  -29.942 1.00 70.20  ? 211 LEU A HD13   1 
ATOM   3303 H  HD21   . LEU A 1 212 ? 0.040   13.681  -30.980 1.00 68.76  ? 211 LEU A HD21   1 
ATOM   3304 H  HD22   . LEU A 1 212 ? 0.305   12.352  -31.811 1.00 68.76  ? 211 LEU A HD22   1 
ATOM   3305 H  HD23   . LEU A 1 212 ? -0.386  13.601  -32.508 1.00 68.76  ? 211 LEU A HD23   1 
ATOM   3306 N  N      . GLY A 1 213 ? -5.256  11.646  -30.617 1.00 23.43  ? 212 GLY A N      1 
ATOM   3307 C  CA     . GLY A 1 213 ? -6.349  12.488  -30.169 1.00 24.22  ? 212 GLY A CA     1 
ATOM   3308 C  C      . GLY A 1 213 ? -6.102  12.973  -28.754 1.00 24.26  ? 212 GLY A C      1 
ATOM   3309 O  O      . GLY A 1 213 ? -4.977  13.275  -28.361 1.00 23.19  ? 212 GLY A O      1 
ATOM   3310 H  H      . GLY A 1 213 ? -5.055  11.024  -30.059 1.00 28.14  ? 212 GLY A H      1 
ATOM   3311 H  HA2    . GLY A 1 213 ? -6.434  13.257  -30.754 1.00 29.08  ? 212 GLY A HA2    1 
ATOM   3312 H  HA3    . GLY A 1 213 ? -7.180  11.987  -30.188 1.00 29.08  ? 212 GLY A HA3    1 
ATOM   3313 N  N      . GLY A 1 214 ? -7.186  13.041  -27.974 1.00 22.12  ? 213 GLY A N      1 
ATOM   3314 C  CA     . GLY A 1 214 ? -7.079  13.398  -26.571 1.00 22.44  ? 213 GLY A CA     1 
ATOM   3315 C  C      . GLY A 1 214 ? -6.987  14.889  -26.308 1.00 23.77  ? 213 GLY A C      1 
ATOM   3316 O  O      . GLY A 1 214 ? -7.283  15.736  -27.153 1.00 24.78  ? 213 GLY A O      1 
ATOM   3317 H  H      . GLY A 1 214 ? -7.989  12.885  -28.239 1.00 26.56  ? 213 GLY A H      1 
ATOM   3318 H  HA2    . GLY A 1 214 ? -7.854  13.056  -26.098 1.00 26.94  ? 213 GLY A HA2    1 
ATOM   3319 H  HA3    . GLY A 1 214 ? -6.289  12.977  -26.197 1.00 26.94  ? 213 GLY A HA3    1 
ATOM   3320 N  N      . ALA A 1 215 ? -6.533  15.192  -25.085 1.00 21.74  ? 214 ALA A N      1 
ATOM   3321 C  CA     . ALA A 1 215 ? -6.512  16.540  -24.549 1.00 24.05  ? 214 ALA A CA     1 
ATOM   3322 C  C      . ALA A 1 215 ? -5.150  16.998  -24.050 1.00 25.00  ? 214 ALA A C      1 
ATOM   3323 O  O      . ALA A 1 215 ? -5.024  18.149  -23.622 1.00 26.86  ? 214 ALA A O      1 
ATOM   3324 C  CB     . ALA A 1 215 ? -7.504  16.660  -23.390 1.00 27.26  ? 214 ALA A CB     1 
ATOM   3325 H  H      . ALA A 1 215 ? -6.224  14.606  -24.537 1.00 26.11  ? 214 ALA A H      1 
ATOM   3326 H  HA     . ALA A 1 215 ? -6.794  17.155  -25.244 1.00 28.88  ? 214 ALA A HA     1 
ATOM   3327 H  HB1    . ALA A 1 215 ? -7.477  17.566  -23.045 1.00 32.73  ? 214 ALA A HB1    1 
ATOM   3328 H  HB2    . ALA A 1 215 ? -8.395  16.456  -23.715 1.00 32.73  ? 214 ALA A HB2    1 
ATOM   3329 H  HB3    . ALA A 1 215 ? -7.254  16.032  -22.695 1.00 32.73  ? 214 ALA A HB3    1 
ATOM   3330 N  N      . LYS A 1 216 ? -4.131  16.149  -24.079 1.00 22.00  ? 215 LYS A N      1 
ATOM   3331 C  CA     . LYS A 1 216 ? -2.819  16.552  -23.563 1.00 23.16  ? 215 LYS A CA     1 
ATOM   3332 C  C      . LYS A 1 216 ? -2.002  17.132  -24.716 1.00 26.57  ? 215 LYS A C      1 
ATOM   3333 O  O      . LYS A 1 216 ? -0.990  16.587  -25.156 1.00 24.92  ? 215 LYS A O      1 
ATOM   3334 C  CB     . LYS A 1 216 ? -2.133  15.369  -22.904 1.00 23.04  ? 215 LYS A CB     1 
ATOM   3335 C  CG     . LYS A 1 216 ? -2.802  14.993  -21.587 1.00 24.63  ? 215 LYS A CG     1 
ATOM   3336 C  CD     . LYS A 1 216 ? -2.189  13.792  -20.895 1.00 23.50  ? 215 LYS A CD     1 
ATOM   3337 C  CE     . LYS A 1 216 ? -2.750  13.668  -19.490 1.00 25.45  ? 215 LYS A CE     1 
ATOM   3338 N  NZ     . LYS A 1 216 ? -2.292  12.441  -18.784 1.00 26.38  1 215 LYS A NZ     1 
ATOM   3339 H  H      . LYS A 1 216 ? -4.166  15.347  -24.386 1.00 26.41  ? 215 LYS A H      1 
ATOM   3340 H  HA     . LYS A 1 216 ? -2.936  17.246  -22.895 1.00 27.82  ? 215 LYS A HA     1 
ATOM   3341 H  HB2    . LYS A 1 216 ? -2.178  14.603  -23.497 1.00 27.66  ? 215 LYS A HB2    1 
ATOM   3342 H  HB3    . LYS A 1 216 ? -1.208  15.597  -22.720 1.00 27.66  ? 215 LYS A HB3    1 
ATOM   3343 H  HG2    . LYS A 1 216 ? -2.739  15.747  -20.980 1.00 29.58  ? 215 LYS A HG2    1 
ATOM   3344 H  HG3    . LYS A 1 216 ? -3.735  14.790  -21.760 1.00 29.58  ? 215 LYS A HG3    1 
ATOM   3345 H  HD2    . LYS A 1 216 ? -2.407  12.986  -21.388 1.00 28.21  ? 215 LYS A HD2    1 
ATOM   3346 H  HD3    . LYS A 1 216 ? -1.228  13.906  -20.836 1.00 28.21  ? 215 LYS A HD3    1 
ATOM   3347 H  HE2    . LYS A 1 216 ? -2.467  14.436  -18.969 1.00 30.56  ? 215 LYS A HE2    1 
ATOM   3348 H  HE3    . LYS A 1 216 ? -3.719  13.641  -19.539 1.00 30.56  ? 215 LYS A HE3    1 
ATOM   3349 H  HZ1    . LYS A 1 216 ? -2.645  12.410  -17.968 1.00 31.68  ? 215 LYS A HZ1    1 
ATOM   3350 H  HZ2    . LYS A 1 216 ? -2.546  11.718  -19.236 1.00 31.68  ? 215 LYS A HZ2    1 
ATOM   3351 H  HZ3    . LYS A 1 216 ? -1.405  12.443  -18.717 1.00 31.68  ? 215 LYS A HZ3    1 
ATOM   3352 N  N      . VAL A 1 217 ? -2.483  18.272  -25.216 1.00 26.94  ? 216 VAL A N      1 
ATOM   3353 C  CA     . VAL A 1 217 ? -1.979  18.797  -26.481 1.00 23.93  ? 216 VAL A CA     1 
ATOM   3354 C  C      . VAL A 1 217 ? -0.540  19.285  -26.327 1.00 24.01  ? 216 VAL A C      1 
ATOM   3355 O  O      . VAL A 1 217 ? 0.332   18.992  -27.156 1.00 26.05  ? 216 VAL A O      1 
ATOM   3356 C  CB     . VAL A 1 217 ? -2.896  19.919  -26.992 1.00 24.71  ? 216 VAL A CB     1 
ATOM   3357 C  CG1    . VAL A 1 217 ? -2.379  20.455  -28.310 1.00 25.65  ? 216 VAL A CG1    1 
ATOM   3358 C  CG2    . VAL A 1 217 ? -4.341  19.428  -27.158 1.00 24.61  ? 216 VAL A CG2    1 
ATOM   3359 H  H      . VAL A 1 217 ? -3.092  18.753  -24.847 1.00 32.35  ? 216 VAL A H      1 
ATOM   3360 H  HA     . VAL A 1 217 ? -1.983  18.085  -27.141 1.00 28.74  ? 216 VAL A HA     1 
ATOM   3361 H  HB     . VAL A 1 217 ? -2.897  20.646  -26.350 1.00 29.67  ? 216 VAL A HB     1 
ATOM   3362 H  HG11   . VAL A 1 217 ? -2.970  21.161  -28.617 1.00 30.80  ? 216 VAL A HG11   1 
ATOM   3363 H  HG12   . VAL A 1 217 ? -1.484  20.806  -28.179 1.00 30.80  ? 216 VAL A HG12   1 
ATOM   3364 H  HG13   . VAL A 1 217 ? -2.361  19.734  -28.959 1.00 30.80  ? 216 VAL A HG13   1 
ATOM   3365 H  HG21   . VAL A 1 217 ? -4.888  20.161  -27.480 1.00 29.55  ? 216 VAL A HG21   1 
ATOM   3366 H  HG22   . VAL A 1 217 ? -4.355  18.698  -27.796 1.00 29.55  ? 216 VAL A HG22   1 
ATOM   3367 H  HG23   . VAL A 1 217 ? -4.670  19.122  -26.298 1.00 29.55  ? 216 VAL A HG23   1 
ATOM   3368 N  N      . ALA A 1 218 ? -0.275  20.064  -25.287 1.00 24.21  ? 217 ALA A N      1 
ATOM   3369 C  CA     . ALA A 1 218 ? 1.071   20.617  -25.110 1.00 29.79  ? 217 ALA A CA     1 
ATOM   3370 C  C      . ALA A 1 218 ? 2.130   19.521  -25.080 1.00 30.29  ? 217 ALA A C      1 
ATOM   3371 O  O      . ALA A 1 218 ? 3.194   19.655  -25.701 1.00 30.42  ? 217 ALA A O      1 
ATOM   3372 C  CB     . ALA A 1 218 ? 1.133   21.438  -23.831 1.00 32.67  ? 217 ALA A CB     1 
ATOM   3373 H  H      . ALA A 1 218 ? -0.841  20.287  -24.678 1.00 29.07  ? 217 ALA A H      1 
ATOM   3374 H  HA     . ALA A 1 218 ? 1.270   21.206  -25.855 1.00 35.76  ? 217 ALA A HA     1 
ATOM   3375 H  HB1    . ALA A 1 218 ? 2.028   21.796  -23.729 1.00 39.22  ? 217 ALA A HB1    1 
ATOM   3376 H  HB2    . ALA A 1 218 ? 0.491   22.163  -23.890 1.00 39.22  ? 217 ALA A HB2    1 
ATOM   3377 H  HB3    . ALA A 1 218 ? 0.918   20.865  -23.078 1.00 39.22  ? 217 ALA A HB3    1 
ATOM   3378 N  N      . ASP A 1 219 ? 1.858   18.427  -24.364 1.00 25.79  ? 218 ASP A N      1 
ATOM   3379 C  CA     . ASP A 1 219 ? 2.807   17.314  -24.291 1.00 25.56  ? 218 ASP A CA     1 
ATOM   3380 C  C      . ASP A 1 219 ? 2.896   16.565  -25.605 1.00 24.82  ? 218 ASP A C      1 
ATOM   3381 O  O      . ASP A 1 219 ? 3.992   16.321  -26.133 1.00 26.36  ? 218 ASP A O      1 
ATOM   3382 C  CB     . ASP A 1 219 ? 2.381   16.315  -23.213 1.00 31.50  ? 218 ASP A CB     1 
ATOM   3383 C  CG     . ASP A 1 219 ? 2.600   16.810  -21.810 1.00 46.59  ? 218 ASP A CG     1 
ATOM   3384 O  OD1    . ASP A 1 219 ? 3.392   17.756  -21.592 1.00 49.85  ? 218 ASP A OD1    1 
ATOM   3385 O  OD2    . ASP A 1 219 ? 1.977   16.206  -20.909 1.00 49.60  1 218 ASP A OD2    1 
ATOM   3386 H  H      . ASP A 1 219 ? 1.135   18.305  -23.915 1.00 30.96  ? 218 ASP A H      1 
ATOM   3387 H  HA     . ASP A 1 219 ? 3.688   17.653  -24.069 1.00 30.69  ? 218 ASP A HA     1 
ATOM   3388 H  HB2    . ASP A 1 219 ? 1.435   16.126  -23.317 1.00 37.82  ? 218 ASP A HB2    1 
ATOM   3389 H  HB3    . ASP A 1 219 ? 2.893   15.498  -23.323 1.00 37.82  ? 218 ASP A HB3    1 
ATOM   3390 N  N      . LYS A 1 220 ? 1.756   16.144  -26.133 1.00 23.74  ? 219 LYS A N      1 
ATOM   3391 C  CA     . LYS A 1 220 ? 1.789   15.142  -27.179 1.00 24.69  ? 219 LYS A CA     1 
ATOM   3392 C  C      . LYS A 1 220 ? 2.075   15.734  -28.564 1.00 24.00  ? 219 LYS A C      1 
ATOM   3393 O  O      . LYS A 1 220 ? 2.619   15.030  -29.412 1.00 23.65  ? 219 LYS A O      1 
ATOM   3394 C  CB     . LYS A 1 220 ? 0.497   14.331  -27.116 1.00 26.10  ? 219 LYS A CB     1 
ATOM   3395 C  CG     . LYS A 1 220 ? 0.455   13.520  -25.762 1.00 28.86  ? 219 LYS A CG     1 
ATOM   3396 C  CD     . LYS A 1 220 ? -0.733  12.572  -25.633 1.00 30.78  ? 219 LYS A CD     1 
ATOM   3397 C  CE     . LYS A 1 220 ? -0.684  11.829  -24.281 1.00 32.31  ? 219 LYS A CE     1 
ATOM   3398 N  NZ     . LYS A 1 220 ? -1.899  10.968  -24.048 1.00 28.88  1 219 LYS A NZ     1 
ATOM   3399 H  H      . LYS A 1 220 ? 0.970   16.414  -25.909 1.00 28.50  ? 219 LYS A H      1 
ATOM   3400 H  HA     . LYS A 1 220 ? 2.516   14.530  -26.982 1.00 29.65  ? 219 LYS A HA     1 
ATOM   3401 H  HB2    . LYS A 1 220 ? -0.266  14.928  -27.144 1.00 31.34  ? 219 LYS A HB2    1 
ATOM   3402 H  HB3    . LYS A 1 220 ? 0.468   13.703  -27.855 1.00 31.34  ? 219 LYS A HB3    1 
ATOM   3403 H  HG2    . LYS A 1 220 ? 1.265   12.990  -25.693 1.00 34.65  ? 219 LYS A HG2    1 
ATOM   3404 H  HG3    . LYS A 1 220 ? 0.412   14.149  -25.025 1.00 34.65  ? 219 LYS A HG3    1 
ATOM   3405 H  HD2    . LYS A 1 220 ? -1.559  13.080  -25.675 1.00 36.95  ? 219 LYS A HD2    1 
ATOM   3406 H  HD3    . LYS A 1 220 ? -0.702  11.915  -26.346 1.00 36.95  ? 219 LYS A HD3    1 
ATOM   3407 H  HE2    . LYS A 1 220 ? 0.099   11.256  -24.263 1.00 38.79  ? 219 LYS A HE2    1 
ATOM   3408 H  HE3    . LYS A 1 220 ? -0.635  12.481  -23.564 1.00 38.79  ? 219 LYS A HE3    1 
ATOM   3409 H  HZ1    . LYS A 1 220 ? -1.835  10.557  -23.261 1.00 34.67  ? 219 LYS A HZ1    1 
ATOM   3410 H  HZ2    . LYS A 1 220 ? -2.634  11.470  -24.052 1.00 34.67  ? 219 LYS A HZ2    1 
ATOM   3411 H  HZ3    . LYS A 1 220 ? -1.965  10.354  -24.690 1.00 34.67  ? 219 LYS A HZ3    1 
ATOM   3412 N  N      . ILE A 1 221 ? 1.817   17.030  -28.788 1.00 23.24  ? 220 ILE A N      1 
ATOM   3413 C  CA     . ILE A 1 221 ? 2.177   17.625  -30.076 1.00 22.05  ? 220 ILE A CA     1 
ATOM   3414 C  C      . ILE A 1 221 ? 3.685   17.604  -30.249 1.00 23.35  ? 220 ILE A C      1 
ATOM   3415 O  O      . ILE A 1 221 ? 4.188   17.567  -31.373 1.00 24.78  ? 220 ILE A O      1 
ATOM   3416 C  CB     . ILE A 1 221 ? 1.600   19.059  -30.182 1.00 25.34  ? 220 ILE A CB     1 
ATOM   3417 C  CG1    . ILE A 1 221 ? 1.626   19.567  -31.620 1.00 33.75  ? 220 ILE A CG1    1 
ATOM   3418 C  CG2    . ILE A 1 221 ? 2.361   20.028  -29.280 1.00 26.73  ? 220 ILE A CG2    1 
ATOM   3419 C  CD1    . ILE A 1 221 ? 0.638   20.735  -31.819 1.00 37.74  ? 220 ILE A CD1    1 
ATOM   3420 H  H      . ILE A 1 221 ? 1.447   17.568  -28.228 1.00 27.90  ? 220 ILE A H      1 
ATOM   3421 H  HA     . ILE A 1 221 ? 1.787   17.094  -30.788 1.00 26.48  ? 220 ILE A HA     1 
ATOM   3422 H  HB     . ILE A 1 221 ? 0.676   19.034  -29.888 1.00 30.43  ? 220 ILE A HB     1 
ATOM   3423 H  HG12   . ILE A 1 221 ? 2.518   19.883  -31.833 1.00 40.52  ? 220 ILE A HG12   1 
ATOM   3424 H  HG13   . ILE A 1 221 ? 1.372   18.848  -32.220 1.00 40.52  ? 220 ILE A HG13   1 
ATOM   3425 H  HG21   . ILE A 1 221 ? 1.975   20.913  -29.371 1.00 32.10  ? 220 ILE A HG21   1 
ATOM   3426 H  HG22   . ILE A 1 221 ? 2.287   19.727  -28.360 1.00 32.10  ? 220 ILE A HG22   1 
ATOM   3427 H  HG23   . ILE A 1 221 ? 3.293   20.044  -29.549 1.00 32.10  ? 220 ILE A HG23   1 
ATOM   3428 H  HD11   . ILE A 1 221 ? 0.682   21.032  -32.742 1.00 45.30  ? 220 ILE A HD11   1 
ATOM   3429 H  HD12   . ILE A 1 221 ? -0.259  20.429  -31.612 1.00 45.30  ? 220 ILE A HD12   1 
ATOM   3430 H  HD13   . ILE A 1 221 ? 0.885   21.462  -31.226 1.00 45.30  ? 220 ILE A HD13   1 
ATOM   3431 N  N      . GLN A 1 222 ? 4.435   17.604  -29.144 1.00 22.78  ? 221 GLN A N      1 
ATOM   3432 C  CA     . GLN A 1 222 ? 5.891   17.583  -29.190 1.00 24.77  ? 221 GLN A CA     1 
ATOM   3433 C  C      . GLN A 1 222 ? 6.443   16.203  -29.520 1.00 21.40  ? 221 GLN A C      1 
ATOM   3434 O  O      . GLN A 1 222 ? 7.656   16.067  -29.700 1.00 24.81  ? 221 GLN A O      1 
ATOM   3435 C  CB     . GLN A 1 222 ? 6.467   18.069  -27.852 1.00 29.27  ? 221 GLN A CB     1 
ATOM   3436 C  CG     . GLN A 1 222 ? 6.137   19.538  -27.484 1.00 29.76  ? 221 GLN A CG     1 
ATOM   3437 C  CD     . GLN A 1 222 ? 6.806   20.549  -28.416 1.00 38.58  ? 221 GLN A CD     1 
ATOM   3438 O  OE1    . GLN A 1 222 ? 7.905   20.309  -28.922 1.00 41.02  ? 221 GLN A OE1    1 
ATOM   3439 N  NE2    . GLN A 1 222 ? 6.144   21.688  -28.641 1.00 42.99  ? 221 GLN A NE2    1 
ATOM   3440 H  H      . GLN A 1 222 ? 4.114   17.616  -28.346 1.00 27.36  ? 221 GLN A H      1 
ATOM   3441 H  HA     . GLN A 1 222 ? 6.190   18.194  -29.881 1.00 29.74  ? 221 GLN A HA     1 
ATOM   3442 H  HB2    . GLN A 1 222 ? 6.117   17.505  -27.144 1.00 35.14  ? 221 GLN A HB2    1 
ATOM   3443 H  HB3    . GLN A 1 222 ? 7.433   17.986  -27.885 1.00 35.14  ? 221 GLN A HB3    1 
ATOM   3444 H  HG2    . GLN A 1 222 ? 5.178   19.670  -27.538 1.00 35.73  ? 221 GLN A HG2    1 
ATOM   3445 H  HG3    . GLN A 1 222 ? 6.446   19.714  -26.581 1.00 35.73  ? 221 GLN A HG3    1 
ATOM   3446 H  HE21   . GLN A 1 222 ? 5.381   21.822  -28.269 1.00 51.60  ? 221 GLN A HE21   1 
ATOM   3447 H  HE22   . GLN A 1 222 ? 6.481   22.286  -29.159 1.00 51.60  ? 221 GLN A HE22   1 
ATOM   3448 N  N      . LEU A 1 223 ? 5.602   15.184  -29.587 1.00 20.34  ? 222 LEU A N      1 
ATOM   3449 C  CA     . LEU A 1 223 ? 6.032   13.842  -29.966 1.00 22.36  ? 222 LEU A CA     1 
ATOM   3450 C  C      . LEU A 1 223 ? 5.885   13.551  -31.473 1.00 23.04  ? 222 LEU A C      1 
ATOM   3451 O  O      . LEU A 1 223 ? 6.428   12.556  -31.963 1.00 22.06  ? 222 LEU A O      1 
ATOM   3452 C  CB     . LEU A 1 223 ? 5.218   12.812  -29.190 1.00 23.08  ? 222 LEU A CB     1 
ATOM   3453 C  CG     . LEU A 1 223 ? 5.213   13.002  -27.672 1.00 28.85  ? 222 LEU A CG     1 
ATOM   3454 C  CD1    . LEU A 1 223 ? 4.387   11.899  -27.042 1.00 32.77  ? 222 LEU A CD1    1 
ATOM   3455 C  CD2    . LEU A 1 223 ? 6.609   13.036  -27.097 1.00 31.08  ? 222 LEU A CD2    1 
ATOM   3456 H  H      . LEU A 1 223 ? 4.761   15.242  -29.416 1.00 24.42  ? 222 LEU A H      1 
ATOM   3457 H  HA     . LEU A 1 223 ? 6.965   13.730  -29.727 1.00 26.85  ? 222 LEU A HA     1 
ATOM   3458 H  HB2    . LEU A 1 223 ? 4.298   12.855  -29.493 1.00 27.71  ? 222 LEU A HB2    1 
ATOM   3459 H  HB3    . LEU A 1 223 ? 5.580   11.931  -29.373 1.00 27.71  ? 222 LEU A HB3    1 
ATOM   3460 H  HG     . LEU A 1 223 ? 4.786   13.848  -27.464 1.00 34.64  ? 222 LEU A HG     1 
ATOM   3461 H  HD11   . LEU A 1 223 ? 4.383   12.018  -26.079 1.00 39.34  ? 222 LEU A HD11   1 
ATOM   3462 H  HD12   . LEU A 1 223 ? 3.481   11.948  -27.385 1.00 39.34  ? 222 LEU A HD12   1 
ATOM   3463 H  HD13   . LEU A 1 223 ? 4.780   11.042  -27.268 1.00 39.34  ? 222 LEU A HD13   1 
ATOM   3464 H  HD21   . LEU A 1 223 ? 6.551   13.158  -26.136 1.00 37.32  ? 222 LEU A HD21   1 
ATOM   3465 H  HD22   . LEU A 1 223 ? 7.053   12.198  -27.298 1.00 37.32  ? 222 LEU A HD22   1 
ATOM   3466 H  HD23   . LEU A 1 223 ? 7.096   13.774  -27.495 1.00 37.32  ? 222 LEU A HD23   1 
ATOM   3467 N  N      . ILE A 1 224 ? 5.182   14.398  -32.218 1.00 23.26  ? 223 ILE A N      1 
ATOM   3468 C  CA     . ILE A 1 224 ? 4.844   14.097  -33.611 1.00 22.79  ? 223 ILE A CA     1 
ATOM   3469 C  C      . ILE A 1 224 ? 6.081   14.077  -34.492 1.00 23.45  ? 223 ILE A C      1 
ATOM   3470 O  O      . ILE A 1 224 ? 6.195   13.244  -35.398 1.00 24.16  ? 223 ILE A O      1 
ATOM   3471 C  CB     . ILE A 1 224 ? 3.810   15.114  -34.109 1.00 22.29  ? 223 ILE A CB     1 
ATOM   3472 C  CG1    . ILE A 1 224 ? 2.533   14.921  -33.305 1.00 24.25  ? 223 ILE A CG1    1 
ATOM   3473 C  CG2    . ILE A 1 224 ? 3.586   14.993  -35.662 1.00 21.75  ? 223 ILE A CG2    1 
ATOM   3474 C  CD1    . ILE A 1 224 ? 1.480   15.933  -33.632 1.00 27.89  ? 223 ILE A CD1    1 
ATOM   3475 H  H      . ILE A 1 224 ? 4.887   15.157  -31.942 1.00 27.93  ? 223 ILE A H      1 
ATOM   3476 H  HA     . ILE A 1 224 ? 4.438   13.217  -33.650 1.00 27.36  ? 223 ILE A HA     1 
ATOM   3477 H  HB     . ILE A 1 224 ? 4.150   16.003  -33.924 1.00 26.77  ? 223 ILE A HB     1 
ATOM   3478 H  HG12   . ILE A 1 224 ? 2.172   14.041  -33.494 1.00 29.11  ? 223 ILE A HG12   1 
ATOM   3479 H  HG13   . ILE A 1 224 ? 2.741   14.999  -32.361 1.00 29.11  ? 223 ILE A HG13   1 
ATOM   3480 H  HG21   . ILE A 1 224 ? 2.928   15.650  -35.938 1.00 26.12  ? 223 ILE A HG21   1 
ATOM   3481 H  HG22   . ILE A 1 224 ? 4.428   15.156  -36.116 1.00 26.12  ? 223 ILE A HG22   1 
ATOM   3482 H  HG23   . ILE A 1 224 ? 3.268   14.100  -35.866 1.00 26.12  ? 223 ILE A HG23   1 
ATOM   3483 H  HD11   . ILE A 1 224 ? 0.695   15.758  -33.089 1.00 33.48  ? 223 ILE A HD11   1 
ATOM   3484 H  HD12   . ILE A 1 224 ? 1.823   16.820  -33.440 1.00 33.48  ? 223 ILE A HD12   1 
ATOM   3485 H  HD13   . ILE A 1 224 ? 1.255   15.862  -34.573 1.00 33.48  ? 223 ILE A HD13   1 
ATOM   3486 N  N      . ASN A 1 225 ? 7.012   15.000  -34.259 1.00 23.97  ? 224 ASN A N      1 
ATOM   3487 C  CA     . ASN A 1 225 ? 8.188   15.100  -35.111 1.00 27.02  ? 224 ASN A CA     1 
ATOM   3488 C  C      . ASN A 1 225 ? 8.883   13.752  -35.242 1.00 28.75  ? 224 ASN A C      1 
ATOM   3489 O  O      . ASN A 1 225 ? 9.204   13.310  -36.347 1.00 30.16  ? 224 ASN A O      1 
ATOM   3490 C  CB     . ASN A 1 225 ? 9.145   16.154  -34.553 1.00 27.45  ? 224 ASN A CB     1 
ATOM   3491 C  CG     . ASN A 1 225 ? 10.396  16.286  -35.376 1.00 33.90  ? 224 ASN A CG     1 
ATOM   3492 O  OD1    . ASN A 1 225 ? 10.338  16.730  -36.505 1.00 34.91  ? 224 ASN A OD1    1 
ATOM   3493 N  ND2    . ASN A 1 225 ? 11.532  15.901  -34.815 1.00 43.54  ? 224 ASN A ND2    1 
ATOM   3494 H  H      . ASN A 1 225 ? 6.984   15.574  -33.620 1.00 28.78  ? 224 ASN A H      1 
ATOM   3495 H  HA     . ASN A 1 225 ? 7.914   15.384  -35.998 1.00 32.45  ? 224 ASN A HA     1 
ATOM   3496 H  HB2    . ASN A 1 225 ? 8.699   17.015  -34.543 1.00 32.96  ? 224 ASN A HB2    1 
ATOM   3497 H  HB3    . ASN A 1 225 ? 9.403   15.903  -33.652 1.00 32.96  ? 224 ASN A HB3    1 
ATOM   3498 H  HD21   . ASN A 1 225 ? 12.270  15.961  -35.254 1.00 52.27  ? 224 ASN A HD21   1 
ATOM   3499 H  HD22   . ASN A 1 225 ? 11.532  15.592  -34.013 1.00 52.27  ? 224 ASN A HD22   1 
ATOM   3500 N  N      . ASN A 1 226 ? 9.098   13.069  -34.123 1.00 24.45  ? 225 ASN A N      1 
ATOM   3501 C  CA     . ASN A 1 226 ? 9.804   11.799  -34.176 1.00 24.86  ? 225 ASN A CA     1 
ATOM   3502 C  C      . ASN A 1 226 ? 8.919   10.687  -34.705 1.00 24.21  ? 225 ASN A C      1 
ATOM   3503 O  O      . ASN A 1 226 ? 9.413   9.786   -35.400 1.00 29.25  ? 225 ASN A O      1 
ATOM   3504 C  CB     . ASN A 1 226 ? 10.338  11.419  -32.792 1.00 30.19  ? 225 ASN A CB     1 
ATOM   3505 C  CG     . ASN A 1 226 ? 11.538  12.238  -32.374 1.00 35.23  ? 225 ASN A CG     1 
ATOM   3506 O  OD1    . ASN A 1 226 ? 12.339  12.667  -33.191 1.00 34.28  ? 225 ASN A OD1    1 
ATOM   3507 N  ND2    . ASN A 1 226 ? 11.681  12.433  -31.070 1.00 40.36  ? 225 ASN A ND2    1 
ATOM   3508 H  H      . ASN A 1 226 ? 8.851   13.314  -33.336 1.00 29.36  ? 225 ASN A H      1 
ATOM   3509 H  HA     . ASN A 1 226 ? 10.563  11.886  -34.774 1.00 29.85  ? 225 ASN A HA     1 
ATOM   3510 H  HB2    . ASN A 1 226 ? 9.638   11.558  -32.135 1.00 36.25  ? 225 ASN A HB2    1 
ATOM   3511 H  HB3    . ASN A 1 226 ? 10.602  10.486  -32.802 1.00 36.25  ? 225 ASN A HB3    1 
ATOM   3512 H  HD21   . ASN A 1 226 ? 12.345  12.891  -30.774 1.00 48.45  ? 225 ASN A HD21   1 
ATOM   3513 H  HD22   . ASN A 1 226 ? 11.109  12.101  -30.520 1.00 48.45  ? 225 ASN A HD22   1 
ATOM   3514 N  N      . MET A 1 227 ? 7.612   10.753  -34.444 1.00 22.72  ? 226 MET A N      1 
ATOM   3515 C  CA     A MET A 1 227 ? 6.726   9.730   -34.978 0.48 24.99  ? 226 MET A CA     1 
ATOM   3516 C  CA     B MET A 1 227 ? 6.692   9.757   -34.980 0.52 24.98  ? 226 MET A CA     1 
ATOM   3517 C  C      . MET A 1 227 ? 6.658   9.775   -36.506 1.00 27.06  ? 226 MET A C      1 
ATOM   3518 O  O      . MET A 1 227 ? 6.390   8.750   -37.137 1.00 28.13  ? 226 MET A O      1 
ATOM   3519 C  CB     A MET A 1 227 ? 5.327   9.877   -34.379 0.48 27.37  ? 226 MET A CB     1 
ATOM   3520 C  CB     B MET A 1 227 ? 5.279   10.004  -34.458 0.52 27.36  ? 226 MET A CB     1 
ATOM   3521 C  CG     A MET A 1 227 ? 5.241   9.440   -32.917 0.48 33.71  ? 226 MET A CG     1 
ATOM   3522 C  CG     B MET A 1 227 ? 5.090   9.835   -32.965 0.52 33.71  ? 226 MET A CG     1 
ATOM   3523 S  SD     A MET A 1 227 ? 3.545   9.333   -32.300 0.48 38.78  ? 226 MET A SD     1 
ATOM   3524 S  SD     B MET A 1 227 ? 3.451   10.438  -32.475 0.52 40.06  ? 226 MET A SD     1 
ATOM   3525 C  CE     A MET A 1 227 ? 3.002   11.034  -32.477 0.48 41.07  ? 226 MET A CE     1 
ATOM   3526 C  CE     B MET A 1 227 ? 2.409   9.393   -33.486 0.52 41.03  ? 226 MET A CE     1 
ATOM   3527 H  H      A MET A 1 227 ? 7.227   11.361  -33.973 0.48 27.28  ? 226 MET A H      1 
ATOM   3528 H  H      B MET A 1 227 ? 7.238   11.359  -33.962 0.52 27.28  ? 226 MET A H      1 
ATOM   3529 H  HA     A MET A 1 227 ? 7.066   8.861   -34.713 0.48 30.00  ? 226 MET A HA     1 
ATOM   3530 H  HA     B MET A 1 227 ? 6.972   8.878   -34.682 0.52 30.00  ? 226 MET A HA     1 
ATOM   3531 H  HB2    A MET A 1 227 ? 5.061   10.809  -34.427 0.48 32.87  ? 226 MET A HB2    1 
ATOM   3532 H  HB2    B MET A 1 227 ? 5.025   10.913  -34.681 0.52 32.85  ? 226 MET A HB2    1 
ATOM   3533 H  HB3    A MET A 1 227 ? 4.708   9.332   -34.889 0.48 32.87  ? 226 MET A HB3    1 
ATOM   3534 H  HB3    B MET A 1 227 ? 4.678   9.384   -34.899 0.52 32.85  ? 226 MET A HB3    1 
ATOM   3535 H  HG2    A MET A 1 227 ? 5.647   8.564   -32.827 0.48 40.47  ? 226 MET A HG2    1 
ATOM   3536 H  HG2    B MET A 1 227 ? 5.155   8.895   -32.734 0.52 40.47  ? 226 MET A HG2    1 
ATOM   3537 H  HG3    A MET A 1 227 ? 5.718   10.083  -32.369 0.48 40.47  ? 226 MET A HG3    1 
ATOM   3538 H  HG3    B MET A 1 227 ? 5.763   10.349  -32.492 0.52 40.47  ? 226 MET A HG3    1 
ATOM   3539 H  HE1    A MET A 1 227 ? 2.084   11.105  -32.170 0.48 49.31  ? 226 MET A HE1    1 
ATOM   3540 H  HE1    B MET A 1 227 ? 1.480   9.617   -33.318 0.52 49.26  ? 226 MET A HE1    1 
ATOM   3541 H  HE2    A MET A 1 227 ? 3.575   11.605  -31.942 0.48 49.31  ? 226 MET A HE2    1 
ATOM   3542 H  HE2    B MET A 1 227 ? 2.622   9.544   -34.420 0.52 49.26  ? 226 MET A HE2    1 
ATOM   3543 H  HE3    A MET A 1 227 ? 3.060   11.288  -33.411 0.48 49.31  ? 226 MET A HE3    1 
ATOM   3544 H  HE3    B MET A 1 227 ? 2.573   8.465   -33.254 0.52 49.26  ? 226 MET A HE3    1 
ATOM   3545 N  N      . LEU A 1 228 ? 6.878   10.943  -37.120 1.00 26.94  ? 227 LEU A N      1 
ATOM   3546 C  CA     . LEU A 1 228 ? 6.771   11.040  -38.571 1.00 26.69  ? 227 LEU A CA     1 
ATOM   3547 C  C      . LEU A 1 228 ? 7.865   10.273  -39.292 1.00 28.32  ? 227 LEU A C      1 
ATOM   3548 O  O      . LEU A 1 228 ? 7.776   10.100  -40.501 1.00 30.02  ? 227 LEU A O      1 
ATOM   3549 C  CB     . LEU A 1 228 ? 6.807   12.490  -39.004 1.00 24.61  ? 227 LEU A CB     1 
ATOM   3550 C  CG     . LEU A 1 228 ? 5.574   13.253  -38.587 1.00 23.21  ? 227 LEU A CG     1 
ATOM   3551 C  CD1    . LEU A 1 228 ? 5.836   14.689  -38.903 1.00 22.24  ? 227 LEU A CD1    1 
ATOM   3552 C  CD2    . LEU A 1 228 ? 4.327   12.770  -39.277 1.00 29.18  ? 227 LEU A CD2    1 
ATOM   3553 H  H      . LEU A 1 228 ? 7.086   11.677  -36.725 1.00 32.34  ? 227 LEU A H      1 
ATOM   3554 H  HA     . LEU A 1 228 ? 5.919   10.669  -38.846 1.00 32.05  ? 227 LEU A HA     1 
ATOM   3555 H  HB2    . LEU A 1 228 ? 7.577   12.922  -38.601 1.00 29.55  ? 227 LEU A HB2    1 
ATOM   3556 H  HB3    . LEU A 1 228 ? 6.872   12.530  -39.971 1.00 29.55  ? 227 LEU A HB3    1 
ATOM   3557 H  HG     . LEU A 1 228 ? 5.448   13.167  -37.629 1.00 27.87  ? 227 LEU A HG     1 
ATOM   3558 H  HD11   . LEU A 1 228 ? 5.062   15.215  -38.649 1.00 26.70  ? 227 LEU A HD11   1 
ATOM   3559 H  HD12   . LEU A 1 228 ? 6.615   14.985  -38.406 1.00 26.70  ? 227 LEU A HD12   1 
ATOM   3560 H  HD13   . LEU A 1 228 ? 5.998   14.778  -39.856 1.00 26.70  ? 227 LEU A HD13   1 
ATOM   3561 H  HD21   . LEU A 1 228 ? 3.572   13.297  -38.970 1.00 35.04  ? 227 LEU A HD21   1 
ATOM   3562 H  HD22   . LEU A 1 228 ? 4.436   12.876  -40.235 1.00 35.04  ? 227 LEU A HD22   1 
ATOM   3563 H  HD23   . LEU A 1 228 ? 4.189   11.835  -39.061 1.00 35.04  ? 227 LEU A HD23   1 
ATOM   3564 N  N      . ASP A 1 229 ? 8.882   9.810   -38.582 1.00 28.90  ? 228 ASP A N      1 
ATOM   3565 C  CA     . ASP A 1 229 ? 9.895   8.954   -39.174 1.00 33.89  ? 228 ASP A CA     1 
ATOM   3566 C  C      . ASP A 1 229 ? 9.550   7.472   -39.112 1.00 31.65  ? 228 ASP A C      1 
ATOM   3567 O  O      . ASP A 1 229 ? 10.286  6.661   -39.682 1.00 30.53  ? 228 ASP A O      1 
ATOM   3568 C  CB     . ASP A 1 229 ? 11.216  9.194   -38.463 1.00 41.57  ? 228 ASP A CB     1 
ATOM   3569 C  CG     . ASP A 1 229 ? 11.770  10.560  -38.768 1.00 49.60  ? 228 ASP A CG     1 
ATOM   3570 O  OD1    . ASP A 1 229 ? 11.839  10.911  -39.973 1.00 52.35  ? 228 ASP A OD1    1 
ATOM   3571 O  OD2    . ASP A 1 229 ? 12.093  11.292  -37.812 1.00 43.27  1 228 ASP A OD2    1 
ATOM   3572 H  H      . ASP A 1 229 ? 9.008   9.979   -37.748 1.00 34.70  ? 228 ASP A H      1 
ATOM   3573 H  HA     . ASP A 1 229 ? 10.007  9.196   -40.107 1.00 40.69  ? 228 ASP A HA     1 
ATOM   3574 H  HB2    . ASP A 1 229 ? 11.081  9.127   -37.505 1.00 49.91  ? 228 ASP A HB2    1 
ATOM   3575 H  HB3    . ASP A 1 229 ? 11.862  8.532   -38.758 1.00 49.91  ? 228 ASP A HB3    1 
ATOM   3576 N  N      . LYS A 1 230 ? 8.465   7.105   -38.441 1.00 27.72  ? 229 LYS A N      1 
ATOM   3577 C  CA     . LYS A 1 230 ? 8.102   5.711   -38.206 1.00 27.82  ? 229 LYS A CA     1 
ATOM   3578 C  C      . LYS A 1 230 ? 6.817   5.288   -38.903 1.00 26.92  ? 229 LYS A C      1 
ATOM   3579 O  O      . LYS A 1 230 ? 6.688   4.124   -39.281 1.00 31.03  ? 229 LYS A O      1 
ATOM   3580 C  CB     . LYS A 1 230 ? 7.953   5.452   -36.689 1.00 28.65  ? 229 LYS A CB     1 
ATOM   3581 C  CG     . LYS A 1 230 ? 9.137   5.933   -35.853 1.00 28.36  ? 229 LYS A CG     1 
ATOM   3582 C  CD     . LYS A 1 230 ? 10.401  5.147   -36.069 1.00 33.24  ? 229 LYS A CD     1 
ATOM   3583 C  CE     . LYS A 1 230 ? 11.511  5.760   -35.201 1.00 44.39  ? 229 LYS A CE     1 
ATOM   3584 N  NZ     . LYS A 1 230 ? 12.755  4.944   -35.133 1.00 52.05  1 229 LYS A NZ     1 
ATOM   3585 H  H      . LYS A 1 230 ? 7.905   7.663   -38.101 1.00 33.28  ? 229 LYS A H      1 
ATOM   3586 H  HA     . LYS A 1 230 ? 8.817   5.144   -38.535 1.00 33.40  ? 229 LYS A HA     1 
ATOM   3587 H  HB2    . LYS A 1 230 ? 7.161   5.912   -36.371 1.00 34.40  ? 229 LYS A HB2    1 
ATOM   3588 H  HB3    . LYS A 1 230 ? 7.858   4.497   -36.544 1.00 34.40  ? 229 LYS A HB3    1 
ATOM   3589 H  HG2    . LYS A 1 230 ? 9.323   6.858   -36.079 1.00 34.05  ? 229 LYS A HG2    1 
ATOM   3590 H  HG3    . LYS A 1 230 ? 8.904   5.865   -34.914 1.00 34.05  ? 229 LYS A HG3    1 
ATOM   3591 H  HD2    . LYS A 1 230 ? 10.266  4.225   -35.800 1.00 39.91  ? 229 LYS A HD2    1 
ATOM   3592 H  HD3    . LYS A 1 230 ? 10.667  5.200   -37.000 1.00 39.91  ? 229 LYS A HD3    1 
ATOM   3593 H  HE2    . LYS A 1 230 ? 11.747  6.628   -35.564 1.00 53.28  ? 229 LYS A HE2    1 
ATOM   3594 H  HE3    . LYS A 1 230 ? 11.177  5.864   -34.296 1.00 53.28  ? 229 LYS A HE3    1 
ATOM   3595 H  HZ1    . LYS A 1 230 ? 13.357  5.349   -34.619 1.00 62.47  ? 229 LYS A HZ1    1 
ATOM   3596 H  HZ2    . LYS A 1 230 ? 12.574  4.142   -34.791 1.00 62.47  ? 229 LYS A HZ2    1 
ATOM   3597 H  HZ3    . LYS A 1 230 ? 13.095  4.840   -35.949 1.00 62.47  ? 229 LYS A HZ3    1 
ATOM   3598 N  N      . VAL A 1 231 ? 5.857   6.188   -39.074 1.00 23.39  ? 230 VAL A N      1 
ATOM   3599 C  CA     . VAL A 1 231 ? 4.529   5.823   -39.540 1.00 23.33  ? 230 VAL A CA     1 
ATOM   3600 C  C      . VAL A 1 231 ? 4.360   6.268   -41.008 1.00 26.36  ? 230 VAL A C      1 
ATOM   3601 O  O      . VAL A 1 231 ? 5.155   7.032   -41.549 1.00 28.82  ? 230 VAL A O      1 
ATOM   3602 C  CB     . VAL A 1 231 ? 3.424   6.423   -38.642 1.00 23.96  ? 230 VAL A CB     1 
ATOM   3603 C  CG1    . VAL A 1 231 ? 3.635   6.052   -37.126 1.00 28.02  ? 230 VAL A CG1    1 
ATOM   3604 C  CG2    . VAL A 1 231 ? 3.358   7.927   -38.837 1.00 25.15  ? 230 VAL A CG2    1 
ATOM   3605 H  H      . VAL A 1 231 ? 5.953   7.030   -38.925 1.00 28.09  ? 230 VAL A H      1 
ATOM   3606 H  HA     . VAL A 1 231 ? 4.443   4.858   -39.511 1.00 28.01  ? 230 VAL A HA     1 
ATOM   3607 H  HB     . VAL A 1 231 ? 2.570   6.055   -38.916 1.00 28.77  ? 230 VAL A HB     1 
ATOM   3608 H  HG11   . VAL A 1 231 ? 2.921   6.448   -36.602 1.00 33.65  ? 230 VAL A HG11   1 
ATOM   3609 H  HG12   . VAL A 1 231 ? 3.619   5.086   -37.033 1.00 33.65  ? 230 VAL A HG12   1 
ATOM   3610 H  HG13   . VAL A 1 231 ? 4.492   6.399   -36.833 1.00 33.65  ? 230 VAL A HG13   1 
ATOM   3611 H  HG21   . VAL A 1 231 ? 2.661   8.289   -38.267 1.00 30.20  ? 230 VAL A HG21   1 
ATOM   3612 H  HG22   . VAL A 1 231 ? 4.215   8.314   -38.598 1.00 30.20  ? 230 VAL A HG22   1 
ATOM   3613 H  HG23   . VAL A 1 231 ? 3.157   8.116   -39.767 1.00 30.20  ? 230 VAL A HG23   1 
ATOM   3614 N  N      . ASN A 1 232 ? 3.303   5.770   -41.649 1.00 25.48  ? 231 ASN A N      1 
ATOM   3615 C  CA     . ASN A 1 232 ? 2.951   6.137   -43.020 1.00 25.91  ? 231 ASN A CA     1 
ATOM   3616 C  C      . ASN A 1 232 ? 1.737   7.047   -43.116 1.00 25.91  ? 231 ASN A C      1 
ATOM   3617 O  O      . ASN A 1 232 ? 1.570   7.733   -44.137 1.00 25.74  ? 231 ASN A O      1 
ATOM   3618 C  CB     . ASN A 1 232 ? 2.688   4.869   -43.835 1.00 27.00  ? 231 ASN A CB     1 
ATOM   3619 C  CG     . ASN A 1 232 ? 3.831   3.906   -43.763 1.00 31.51  ? 231 ASN A CG     1 
ATOM   3620 O  OD1    . ASN A 1 232 ? 3.752   2.884   -43.080 1.00 31.26  ? 231 ASN A OD1    1 
ATOM   3621 N  ND2    . ASN A 1 232 ? 4.920   4.230   -44.453 1.00 32.91  ? 231 ASN A ND2    1 
ATOM   3622 H  H      . ASN A 1 232 ? 2.760   5.202   -41.299 1.00 30.59  ? 231 ASN A H      1 
ATOM   3623 H  HA     . ASN A 1 232 ? 3.702   6.600   -43.423 1.00 31.11  ? 231 ASN A HA     1 
ATOM   3624 H  HB2    . ASN A 1 232 ? 1.898   4.426   -43.488 1.00 32.42  ? 231 ASN A HB2    1 
ATOM   3625 H  HB3    . ASN A 1 232 ? 2.554   5.110   -44.765 1.00 32.42  ? 231 ASN A HB3    1 
ATOM   3626 H  HD21   . ASN A 1 232 ? 5.605   3.710   -44.444 1.00 39.51  ? 231 ASN A HD21   1 
ATOM   3627 H  HD22   . ASN A 1 232 ? 4.940   4.959   -44.908 1.00 39.51  ? 231 ASN A HD22   1 
ATOM   3628 N  N      . GLU A 1 233 ? 0.909   7.090   -42.068 1.00 25.83  ? 232 GLU A N      1 
ATOM   3629 C  CA     . GLU A 1 233 ? -0.295  7.906   -42.017 1.00 26.82  ? 232 GLU A CA     1 
ATOM   3630 C  C      . GLU A 1 233 ? -0.504  8.332   -40.576 1.00 24.76  ? 232 GLU A C      1 
ATOM   3631 O  O      . GLU A 1 233 ? -0.135  7.611   -39.646 1.00 24.05  ? 232 GLU A O      1 
ATOM   3632 C  CB     . GLU A 1 233 ? -1.553  7.159   -42.479 1.00 28.72  ? 232 GLU A CB     1 
ATOM   3633 C  CG     . GLU A 1 233 ? -1.590  6.783   -43.941 1.00 35.72  ? 232 GLU A CG     1 
ATOM   3634 C  CD     . GLU A 1 233 ? -3.013  6.640   -44.478 1.00 41.83  ? 232 GLU A CD     1 
ATOM   3635 O  OE1    . GLU A 1 233 ? -3.257  5.693   -45.276 1.00 43.45  ? 232 GLU A OE1    1 
ATOM   3636 O  OE2    . GLU A 1 233 ? -3.878  7.486   -44.140 1.00 37.44  1 232 GLU A OE2    1 
ATOM   3637 H  H      . GLU A 1 233 ? 1.036   6.636   -41.349 1.00 31.01  ? 232 GLU A H      1 
ATOM   3638 H  HA     . GLU A 1 233 ? -0.181  8.698   -42.565 1.00 32.21  ? 232 GLU A HA     1 
ATOM   3639 H  HB2    . GLU A 1 233 ? -1.627  6.338   -41.966 1.00 34.48  ? 232 GLU A HB2    1 
ATOM   3640 H  HB3    . GLU A 1 233 ? -2.325  7.720   -42.304 1.00 34.48  ? 232 GLU A HB3    1 
ATOM   3641 H  HG2    . GLU A 1 233 ? -1.143  7.473   -44.456 1.00 42.89  ? 232 GLU A HG2    1 
ATOM   3642 H  HG3    . GLU A 1 233 ? -1.137  5.934   -44.060 1.00 42.89  ? 232 GLU A HG3    1 
ATOM   3643 N  N      . MET A 1 234 ? -1.156  9.475   -40.388 1.00 23.06  ? 233 MET A N      1 
ATOM   3644 C  CA     . MET A 1 234 ? -1.518  9.904   -39.046 1.00 23.70  ? 233 MET A CA     1 
ATOM   3645 C  C      . MET A 1 234 ? -2.866  10.610  -39.094 1.00 24.86  ? 233 MET A C      1 
ATOM   3646 O  O      . MET A 1 234 ? -3.073  11.504  -39.921 1.00 27.76  ? 233 MET A O      1 
ATOM   3647 C  CB     . MET A 1 234 ? -0.434  10.821  -38.470 1.00 28.32  ? 233 MET A CB     1 
ATOM   3648 C  CG     . MET A 1 234 ? -0.553  11.203  -37.034 1.00 42.14  ? 233 MET A CG     1 
ATOM   3649 S  SD     . MET A 1 234 ? 0.866   12.271  -36.618 1.00 42.42  ? 233 MET A SD     1 
ATOM   3650 C  CE     . MET A 1 234 ? 2.243   11.190  -36.864 1.00 40.20  ? 233 MET A CE     1 
ATOM   3651 H  H      . MET A 1 234 ? -1.397  10.013  -41.014 1.00 27.69  ? 233 MET A H      1 
ATOM   3652 H  HA     . MET A 1 234 ? -1.589  9.124   -38.472 1.00 28.45  ? 233 MET A HA     1 
ATOM   3653 H  HB2    . MET A 1 234 ? 0.422   10.378  -38.577 1.00 34.01  ? 233 MET A HB2    1 
ATOM   3654 H  HB3    . MET A 1 234 ? -0.433  11.644  -38.984 1.00 34.01  ? 233 MET A HB3    1 
ATOM   3655 H  HG2    . MET A 1 234 ? -1.374  11.699  -36.889 1.00 50.59  ? 233 MET A HG2    1 
ATOM   3656 H  HG3    . MET A 1 234 ? -0.524  10.409  -36.476 1.00 50.59  ? 233 MET A HG3    1 
ATOM   3657 H  HE1    . MET A 1 234 ? 3.061   11.672  -36.666 1.00 48.26  ? 233 MET A HE1    1 
ATOM   3658 H  HE2    . MET A 1 234 ? 2.155   10.428  -36.272 1.00 48.26  ? 233 MET A HE2    1 
ATOM   3659 H  HE3    . MET A 1 234 ? 2.249   10.894  -37.788 1.00 48.26  ? 233 MET A HE3    1 
ATOM   3660 N  N      . ILE A 1 235 ? -3.785  10.169  -38.242 1.00 22.77  ? 234 ILE A N      1 
ATOM   3661 C  CA     . ILE A 1 235 ? -4.979  10.940  -37.918 1.00 23.47  ? 234 ILE A CA     1 
ATOM   3662 C  C      . ILE A 1 235 ? -4.636  11.824  -36.730 1.00 21.63  ? 234 ILE A C      1 
ATOM   3663 O  O      . ILE A 1 235 ? -4.137  11.347  -35.691 1.00 21.20  ? 234 ILE A O      1 
ATOM   3664 C  CB     . ILE A 1 235 ? -6.177  10.033  -37.582 1.00 23.11  ? 234 ILE A CB     1 
ATOM   3665 C  CG1    . ILE A 1 235 ? -6.697  9.300   -38.811 1.00 26.25  ? 234 ILE A CG1    1 
ATOM   3666 C  CG2    . ILE A 1 235 ? -7.310  10.847  -36.888 1.00 21.73  ? 234 ILE A CG2    1 
ATOM   3667 C  CD1    . ILE A 1 235 ? -7.656  8.166   -38.444 1.00 25.77  ? 234 ILE A CD1    1 
ATOM   3668 H  H      . ILE A 1 235 ? -3.739  9.414   -37.832 1.00 27.35  ? 234 ILE A H      1 
ATOM   3669 H  HA     . ILE A 1 235 ? -5.218  11.506  -38.669 1.00 28.19  ? 234 ILE A HA     1 
ATOM   3670 H  HB     . ILE A 1 235 ? -5.869  9.363   -36.951 1.00 27.75  ? 234 ILE A HB     1 
ATOM   3671 H  HG12   . ILE A 1 235 ? -7.174  9.927   -39.378 1.00 31.52  ? 234 ILE A HG12   1 
ATOM   3672 H  HG13   . ILE A 1 235 ? -5.948  8.917   -39.294 1.00 31.52  ? 234 ILE A HG13   1 
ATOM   3673 H  HG21   . ILE A 1 235 ? -8.050  10.252  -36.688 1.00 26.09  ? 234 ILE A HG21   1 
ATOM   3674 H  HG22   . ILE A 1 235 ? -6.965  11.233  -36.067 1.00 26.09  ? 234 ILE A HG22   1 
ATOM   3675 H  HG23   . ILE A 1 235 ? -7.604  11.552  -37.486 1.00 26.09  ? 234 ILE A HG23   1 
ATOM   3676 H  HD11   . ILE A 1 235 ? -7.958  7.732   -39.258 1.00 30.94  ? 234 ILE A HD11   1 
ATOM   3677 H  HD12   . ILE A 1 235 ? -7.190  7.528   -37.882 1.00 30.94  ? 234 ILE A HD12   1 
ATOM   3678 H  HD13   . ILE A 1 235 ? -8.414  8.537   -37.966 1.00 30.94  ? 234 ILE A HD13   1 
ATOM   3679 N  N      . ILE A 1 236 ? -4.927  13.106  -36.859 1.00 22.70  ? 235 ILE A N      1 
ATOM   3680 C  CA     . ILE A 1 236 ? -4.765  14.054  -35.762 1.00 24.48  ? 235 ILE A CA     1 
ATOM   3681 C  C      . ILE A 1 236 ? -6.152  14.550  -35.419 1.00 25.79  ? 235 ILE A C      1 
ATOM   3682 O  O      . ILE A 1 236 ? -6.737  15.315  -36.187 1.00 28.68  ? 235 ILE A O      1 
ATOM   3683 C  CB     . ILE A 1 236 ? -3.850  15.225  -36.137 1.00 27.26  ? 235 ILE A CB     1 
ATOM   3684 C  CG1    . ILE A 1 236 ? -2.463  14.680  -36.478 1.00 30.16  ? 235 ILE A CG1    1 
ATOM   3685 C  CG2    . ILE A 1 236 ? -3.775  16.260  -34.955 1.00 26.60  ? 235 ILE A CG2    1 
ATOM   3686 C  CD1    . ILE A 1 236 ? -1.459  15.736  -36.833 1.00 32.30  ? 235 ILE A CD1    1 
ATOM   3687 H  H      . ILE A 1 236 ? -5.225  13.462  -37.583 1.00 27.25  ? 235 ILE A H      1 
ATOM   3688 H  HA     . ILE A 1 236 ? -4.394  13.601  -34.989 1.00 29.39  ? 235 ILE A HA     1 
ATOM   3689 H  HB     . ILE A 1 236 ? -4.213  15.668  -36.919 1.00 32.73  ? 235 ILE A HB     1 
ATOM   3690 H  HG12   . ILE A 1 236 ? -2.122  14.195  -35.711 1.00 36.21  ? 235 ILE A HG12   1 
ATOM   3691 H  HG13   . ILE A 1 236 ? -2.542  14.081  -37.237 1.00 36.21  ? 235 ILE A HG13   1 
ATOM   3692 H  HG21   . ILE A 1 236 ? -3.192  16.991  -35.213 1.00 31.94  ? 235 ILE A HG21   1 
ATOM   3693 H  HG22   . ILE A 1 236 ? -4.667  16.596  -34.774 1.00 31.94  ? 235 ILE A HG22   1 
ATOM   3694 H  HG23   . ILE A 1 236 ? -3.422  15.816  -34.169 1.00 31.94  ? 235 ILE A HG23   1 
ATOM   3695 H  HD11   . ILE A 1 236 ? -0.611  15.310  -37.034 1.00 38.78  ? 235 ILE A HD11   1 
ATOM   3696 H  HD12   . ILE A 1 236 ? -1.776  16.225  -37.608 1.00 38.78  ? 235 ILE A HD12   1 
ATOM   3697 H  HD13   . ILE A 1 236 ? -1.356  16.339  -36.080 1.00 38.78  ? 235 ILE A HD13   1 
ATOM   3698 N  N      . GLY A 1 237 ? -6.669  14.133  -34.270 1.00 22.16  ? 236 GLY A N      1 
ATOM   3699 C  CA     . GLY A 1 237 ? -8.037  14.446  -33.912 1.00 23.19  ? 236 GLY A CA     1 
ATOM   3700 C  C      . GLY A 1 237 ? -8.197  14.899  -32.483 1.00 24.69  ? 236 GLY A C      1 
ATOM   3701 O  O      . GLY A 1 237 ? -7.237  15.314  -31.826 1.00 22.69  ? 236 GLY A O      1 
ATOM   3702 H  H      . GLY A 1 237 ? -6.246  13.669  -33.683 1.00 26.61  ? 236 GLY A H      1 
ATOM   3703 H  HA2    . GLY A 1 237 ? -8.366  15.151  -34.492 1.00 27.85  ? 236 GLY A HA2    1 
ATOM   3704 H  HA3    . GLY A 1 237 ? -8.590  13.660  -34.045 1.00 27.85  ? 236 GLY A HA3    1 
ATOM   3705 N  N      . GLY A 1 238 ? -9.418  14.788  -31.971 1.00 26.16  ? 237 GLY A N      1 
ATOM   3706 C  CA     . GLY A 1 238 ? -9.667  15.210  -30.612 1.00 24.76  ? 237 GLY A CA     1 
ATOM   3707 C  C      . GLY A 1 238 ? -9.249  16.645  -30.426 1.00 24.71  ? 237 GLY A C      1 
ATOM   3708 O  O      . GLY A 1 238 ? -9.367  17.483  -31.332 1.00 24.80  ? 237 GLY A O      1 
ATOM   3709 H  H      . GLY A 1 238 ? -10.105 14.478  -32.387 1.00 31.41  ? 237 GLY A H      1 
ATOM   3710 H  HA2    . GLY A 1 238 ? -10.612 15.129  -30.409 1.00 29.73  ? 237 GLY A HA2    1 
ATOM   3711 H  HA3    . GLY A 1 238 ? -9.165  14.653  -29.997 1.00 29.73  ? 237 GLY A HA3    1 
ATOM   3712 N  N      . GLY A 1 239 ? -8.672  16.915  -29.260 1.00 22.92  ? 238 GLY A N      1 
ATOM   3713 C  CA     . GLY A 1 239 ? -8.256  18.262  -28.925 1.00 24.08  ? 238 GLY A CA     1 
ATOM   3714 C  C      . GLY A 1 239 ? -7.018  18.710  -29.658 1.00 24.73  ? 238 GLY A C      1 
ATOM   3715 O  O      . GLY A 1 239 ? -6.776  19.916  -29.769 1.00 26.65  ? 238 GLY A O      1 
ATOM   3716 H  H      . GLY A 1 239 ? -8.511  16.332  -28.648 1.00 27.52  ? 238 GLY A H      1 
ATOM   3717 H  HA2    . GLY A 1 239 ? -8.974  18.880  -29.136 1.00 28.92  ? 238 GLY A HA2    1 
ATOM   3718 H  HA3    . GLY A 1 239 ? -8.080  18.315  -27.972 1.00 28.92  ? 238 GLY A HA3    1 
ATOM   3719 N  N      . MET A 1 240 ? -6.246  17.766  -30.195 1.00 24.35  ? 239 MET A N      1 
ATOM   3720 C  CA     A MET A 1 240 ? -5.028  18.185  -30.872 0.38 26.71  ? 239 MET A CA     1 
ATOM   3721 C  CA     B MET A 1 240 ? -5.021  18.071  -30.941 0.62 26.69  ? 239 MET A CA     1 
ATOM   3722 C  C      . MET A 1 240 ? -5.305  18.876  -32.206 1.00 25.46  ? 239 MET A C      1 
ATOM   3723 O  O      . MET A 1 240 ? -4.497  19.704  -32.628 1.00 24.20  ? 239 MET A O      1 
ATOM   3724 C  CB     A MET A 1 240 ? -4.103  16.998  -31.091 0.38 29.37  ? 239 MET A CB     1 
ATOM   3725 C  CB     B MET A 1 240 ? -4.335  16.761  -31.357 0.62 29.30  ? 239 MET A CB     1 
ATOM   3726 C  CG     A MET A 1 240 ? -2.742  17.437  -31.587 0.38 32.55  ? 239 MET A CG     1 
ATOM   3727 C  CG     B MET A 1 240 ? -3.896  15.830  -30.248 0.62 34.04  ? 239 MET A CG     1 
ATOM   3728 S  SD     A MET A 1 240 ? -1.537  16.126  -31.529 0.38 37.68  ? 239 MET A SD     1 
ATOM   3729 S  SD     B MET A 1 240 ? -2.423  16.363  -29.342 0.62 36.44  ? 239 MET A SD     1 
ATOM   3730 C  CE     A MET A 1 240 ? -1.428  15.819  -29.773 0.38 36.63  ? 239 MET A CE     1 
ATOM   3731 C  CE     B MET A 1 240 ? -1.501  17.277  -30.557 0.62 34.67  ? 239 MET A CE     1 
ATOM   3732 H  H      A MET A 1 240 ? -6.397  16.919  -30.182 0.38 29.24  ? 239 MET A H      1 
ATOM   3733 H  H      B MET A 1 240 ? -6.413  16.924  -30.140 0.62 29.24  ? 239 MET A H      1 
ATOM   3734 H  HA     A MET A 1 240 ? -4.561  18.811  -30.297 0.38 32.08  ? 239 MET A HA     1 
ATOM   3735 H  HA     B MET A 1 240 ? -4.413  18.568  -30.372 0.62 32.05  ? 239 MET A HA     1 
ATOM   3736 H  HB2    A MET A 1 240 ? -3.984  16.526  -30.252 0.38 35.27  ? 239 MET A HB2    1 
ATOM   3737 H  HB2    B MET A 1 240 ? -4.950  16.264  -31.919 0.62 35.18  ? 239 MET A HB2    1 
ATOM   3738 H  HB3    A MET A 1 240 ? -4.492  16.407  -31.755 0.38 35.27  ? 239 MET A HB3    1 
ATOM   3739 H  HB3    B MET A 1 240 ? -3.544  16.986  -31.871 0.62 35.18  ? 239 MET A HB3    1 
ATOM   3740 H  HG2    A MET A 1 240 ? -2.821  17.732  -32.507 0.38 39.08  ? 239 MET A HG2    1 
ATOM   3741 H  HG2    B MET A 1 240 ? -4.620  15.749  -29.608 0.62 40.86  ? 239 MET A HG2    1 
ATOM   3742 H  HG3    A MET A 1 240 ? -2.422  18.164  -31.030 0.38 39.08  ? 239 MET A HG3    1 
ATOM   3743 H  HG3    B MET A 1 240 ? -3.703  14.960  -30.633 0.62 40.86  ? 239 MET A HG3    1 
ATOM   3744 H  HE1    A MET A 1 240 ? -1.137  16.631  -29.329 0.38 43.98  ? 239 MET A HE1    1 
ATOM   3745 H  HE1    B MET A 1 240 ? -0.684  17.605  -30.152 0.62 41.62  ? 239 MET A HE1    1 
ATOM   3746 H  HE2    A MET A 1 240 ? -2.301  15.555  -29.444 0.38 43.98  ? 239 MET A HE2    1 
ATOM   3747 H  HE2    B MET A 1 240 ? -1.290  16.690  -31.300 0.62 41.62  ? 239 MET A HE2    1 
ATOM   3748 H  HE3    A MET A 1 240 ? -0.786  15.108  -29.617 0.38 43.98  ? 239 MET A HE3    1 
ATOM   3749 H  HE3    B MET A 1 240 ? -2.040  18.022  -30.867 0.62 41.62  ? 239 MET A HE3    1 
ATOM   3750 N  N      . ALA A 1 241 ? -6.430  18.582  -32.865 1.00 23.80  ? 240 ALA A N      1 
ATOM   3751 C  CA     . ALA A 1 241 ? -6.674  19.083  -34.214 1.00 23.90  ? 240 ALA A CA     1 
ATOM   3752 C  C      . ALA A 1 241 ? -6.723  20.597  -34.264 1.00 23.85  ? 240 ALA A C      1 
ATOM   3753 O  O      . ALA A 1 241 ? -6.338  21.193  -35.277 1.00 25.11  ? 240 ALA A O      1 
ATOM   3754 C  CB     . ALA A 1 241 ? -7.983  18.509  -34.742 1.00 22.99  ? 240 ALA A CB     1 
ATOM   3755 H  H      . ALA A 1 241 ? -7.064  18.094  -32.551 1.00 28.58  ? 240 ALA A H      1 
ATOM   3756 H  HA     . ALA A 1 241 ? -5.958  18.786  -34.797 1.00 28.70  ? 240 ALA A HA     1 
ATOM   3757 H  HB1    . ALA A 1 241 ? -8.137  18.847  -35.638 1.00 27.61  ? 240 ALA A HB1    1 
ATOM   3758 H  HB2    . ALA A 1 241 ? -7.918  17.541  -34.760 1.00 27.61  ? 240 ALA A HB2    1 
ATOM   3759 H  HB3    . ALA A 1 241 ? -8.706  18.782  -34.156 1.00 27.61  ? 240 ALA A HB3    1 
ATOM   3760 N  N      . PHE A 1 242 ? -7.214  21.248  -33.206 1.00 23.67  ? 241 PHE A N      1 
ATOM   3761 C  CA     . PHE A 1 242 ? -7.543  22.668  -33.342 1.00 26.03  ? 241 PHE A CA     1 
ATOM   3762 C  C      . PHE A 1 242 ? -6.300  23.539  -33.477 1.00 26.34  ? 241 PHE A C      1 
ATOM   3763 O  O      . PHE A 1 242 ? -6.338  24.556  -34.176 1.00 26.11  ? 241 PHE A O      1 
ATOM   3764 C  CB     . PHE A 1 242 ? -8.431  23.126  -32.177 1.00 23.94  ? 241 PHE A CB     1 
ATOM   3765 C  CG     . PHE A 1 242 ? -9.710  22.368  -32.114 1.00 24.45  ? 241 PHE A CG     1 
ATOM   3766 C  CD1    . PHE A 1 242 ? -10.714 22.600  -33.039 1.00 26.61  ? 241 PHE A CD1    1 
ATOM   3767 C  CD2    . PHE A 1 242 ? -9.886  21.362  -31.194 1.00 25.70  ? 241 PHE A CD2    1 
ATOM   3768 C  CE1    . PHE A 1 242 ? -11.870 21.856  -33.019 1.00 26.52  ? 241 PHE A CE1    1 
ATOM   3769 C  CE2    . PHE A 1 242 ? -11.036 20.617  -31.181 1.00 26.95  ? 241 PHE A CE2    1 
ATOM   3770 C  CZ     . PHE A 1 242 ? -12.031 20.874  -32.092 1.00 26.05  ? 241 PHE A CZ     1 
ATOM   3771 H  H      . PHE A 1 242 ? -7.360  20.907  -32.430 1.00 28.42  ? 241 PHE A H      1 
ATOM   3772 H  HA     . PHE A 1 242 ? -8.060  22.781  -34.155 1.00 31.25  ? 241 PHE A HA     1 
ATOM   3773 H  HB2    . PHE A 1 242 ? -7.956  22.988  -31.342 1.00 28.75  ? 241 PHE A HB2    1 
ATOM   3774 H  HB3    . PHE A 1 242 ? -8.642  24.066  -32.289 1.00 28.75  ? 241 PHE A HB3    1 
ATOM   3775 H  HD1    . PHE A 1 242 ? -10.605 23.265  -33.679 1.00 31.95  ? 241 PHE A HD1    1 
ATOM   3776 H  HD2    . PHE A 1 242 ? -9.212  21.177  -30.580 1.00 30.85  ? 241 PHE A HD2    1 
ATOM   3777 H  HE1    . PHE A 1 242 ? -12.546 22.031  -33.634 1.00 31.85  ? 241 PHE A HE1    1 
ATOM   3778 H  HE2    . PHE A 1 242 ? -11.151 19.951  -30.543 1.00 32.36  ? 241 PHE A HE2    1 
ATOM   3779 H  HZ     . PHE A 1 242 ? -12.819 20.380  -32.071 1.00 31.28  ? 241 PHE A HZ     1 
ATOM   3780 N  N      . THR A 1 243 ? -5.195  23.160  -32.845 1.00 24.89  ? 242 THR A N      1 
ATOM   3781 C  CA     . THR A 1 243 ? -3.950  23.884  -33.057 1.00 26.28  ? 242 THR A CA     1 
ATOM   3782 C  C      . THR A 1 243 ? -3.515  23.808  -34.525 1.00 26.90  ? 242 THR A C      1 
ATOM   3783 O  O      . THR A 1 243 ? -3.062  24.806  -35.090 1.00 27.06  ? 242 THR A O      1 
ATOM   3784 C  CB     . THR A 1 243 ? -2.863  23.339  -32.115 1.00 25.06  ? 242 THR A CB     1 
ATOM   3785 O  OG1    . THR A 1 243 ? -3.228  23.544  -30.725 1.00 23.13  ? 242 THR A OG1    1 
ATOM   3786 C  CG2    . THR A 1 243 ? -1.524  24.025  -32.381 1.00 27.40  ? 242 THR A CG2    1 
ATOM   3787 H  H      . THR A 1 243 ? -5.139  22.498  -32.298 1.00 29.88  ? 242 THR A H      1 
ATOM   3788 H  HA     . THR A 1 243 ? -4.091  24.818  -32.838 1.00 31.55  ? 242 THR A HA     1 
ATOM   3789 H  HB     . THR A 1 243 ? -2.751  22.389  -32.276 1.00 30.09  ? 242 THR A HB     1 
ATOM   3790 H  HG1    . THR A 1 243 ? -3.949  23.148  -30.556 1.00 27.77  ? 242 THR A HG1    1 
ATOM   3791 H  HG21   . THR A 1 243 ? -0.846  23.674  -31.782 1.00 32.90  ? 242 THR A HG21   1 
ATOM   3792 H  HG22   . THR A 1 243 ? -1.247  23.868  -33.297 1.00 32.90  ? 242 THR A HG22   1 
ATOM   3793 H  HG23   . THR A 1 243 ? -1.607  24.981  -32.237 1.00 32.90  ? 242 THR A HG23   1 
ATOM   3794 N  N      . PHE A 1 244 ? -3.652  22.634  -35.164 1.00 24.40  ? 243 PHE A N      1 
ATOM   3795 C  CA     . PHE A 1 244 ? -3.302  22.509  -36.571 1.00 25.26  ? 243 PHE A CA     1 
ATOM   3796 C  C      . PHE A 1 244 ? -4.232  23.313  -37.458 1.00 25.44  ? 243 PHE A C      1 
ATOM   3797 O  O      . PHE A 1 244 ? -3.776  23.969  -38.395 1.00 28.24  ? 243 PHE A O      1 
ATOM   3798 C  CB     . PHE A 1 244 ? -3.332  21.045  -37.008 1.00 23.52  ? 243 PHE A CB     1 
ATOM   3799 C  CG     . PHE A 1 244 ? -2.157  20.282  -36.535 1.00 24.82  ? 243 PHE A CG     1 
ATOM   3800 C  CD1    . PHE A 1 244 ? -2.069  19.856  -35.197 1.00 24.92  ? 243 PHE A CD1    1 
ATOM   3801 C  CD2    . PHE A 1 244 ? -1.095  20.059  -37.385 1.00 27.11  ? 243 PHE A CD2    1 
ATOM   3802 C  CE1    . PHE A 1 244 ? -0.939  19.169  -34.753 1.00 26.73  ? 243 PHE A CE1    1 
ATOM   3803 C  CE2    . PHE A 1 244 ? 0.034   19.378  -36.943 1.00 28.23  ? 243 PHE A CE2    1 
ATOM   3804 C  CZ     . PHE A 1 244 ? 0.114   18.940  -35.648 1.00 28.70  ? 243 PHE A CZ     1 
ATOM   3805 H  H      . PHE A 1 244 ? -3.941  21.909  -34.803 1.00 29.29  ? 243 PHE A H      1 
ATOM   3806 H  HA     . PHE A 1 244 ? -2.400  22.842  -36.702 1.00 30.33  ? 243 PHE A HA     1 
ATOM   3807 H  HB2    . PHE A 1 244 ? -4.128  20.624  -36.647 1.00 28.24  ? 243 PHE A HB2    1 
ATOM   3808 H  HB3    . PHE A 1 244 ? -3.345  21.004  -37.977 1.00 28.24  ? 243 PHE A HB3    1 
ATOM   3809 H  HD1    . PHE A 1 244 ? -2.775  20.014  -34.613 1.00 29.93  ? 243 PHE A HD1    1 
ATOM   3810 H  HD2    . PHE A 1 244 ? -1.141  20.352  -38.266 1.00 32.55  ? 243 PHE A HD2    1 
ATOM   3811 H  HE1    . PHE A 1 244 ? -0.883  18.871  -33.874 1.00 32.10  ? 243 PHE A HE1    1 
ATOM   3812 H  HE2    . PHE A 1 244 ? 0.737   19.218  -37.531 1.00 33.90  ? 243 PHE A HE2    1 
ATOM   3813 H  HZ     . PHE A 1 244 ? 0.870   18.481  -35.362 1.00 34.46  ? 243 PHE A HZ     1 
ATOM   3814 N  N      . LEU A 1 245 ? -5.538  23.239  -37.208 1.00 24.68  ? 244 LEU A N      1 
ATOM   3815 C  CA     . LEU A 1 245 ? -6.494  23.919  -38.081 1.00 27.37  ? 244 LEU A CA     1 
ATOM   3816 C  C      . LEU A 1 245 ? -6.380  25.429  -37.972 1.00 28.46  ? 244 LEU A C      1 
ATOM   3817 O  O      . LEU A 1 245 ? -6.561  26.137  -38.977 1.00 27.66  ? 244 LEU A O      1 
ATOM   3818 C  CB     . LEU A 1 245 ? -7.907  23.458  -37.746 1.00 28.88  ? 244 LEU A CB     1 
ATOM   3819 C  CG     . LEU A 1 245 ? -8.120  21.974  -38.079 1.00 30.03  ? 244 LEU A CG     1 
ATOM   3820 C  CD1    . LEU A 1 245 ? -9.384  21.477  -37.440 1.00 33.30  ? 244 LEU A CD1    1 
ATOM   3821 C  CD2    . LEU A 1 245 ? -8.152  21.761  -39.592 1.00 31.40  ? 244 LEU A CD2    1 
ATOM   3822 H  H      . LEU A 1 245 ? -5.892  22.810  -36.552 1.00 29.63  ? 244 LEU A H      1 
ATOM   3823 H  HA     . LEU A 1 245 ? -6.310  23.672  -39.001 1.00 32.86  ? 244 LEU A HA     1 
ATOM   3824 H  HB2    . LEU A 1 245 ? -8.066  23.581  -36.797 1.00 34.67  ? 244 LEU A HB2    1 
ATOM   3825 H  HB3    . LEU A 1 245 ? -8.543  23.978  -38.262 1.00 34.67  ? 244 LEU A HB3    1 
ATOM   3826 H  HG     . LEU A 1 245 ? -7.380  21.460  -37.720 1.00 36.05  ? 244 LEU A HG     1 
ATOM   3827 H  HD11   . LEU A 1 245 ? -9.501  20.540  -37.661 1.00 39.98  ? 244 LEU A HD11   1 
ATOM   3828 H  HD12   . LEU A 1 245 ? -9.314  21.584  -36.478 1.00 39.98  ? 244 LEU A HD12   1 
ATOM   3829 H  HD13   . LEU A 1 245 ? -10.132 21.993  -37.777 1.00 39.98  ? 244 LEU A HD13   1 
ATOM   3830 H  HD21   . LEU A 1 245 ? -8.288  20.818  -39.775 1.00 37.69  ? 244 LEU A HD21   1 
ATOM   3831 H  HD22   . LEU A 1 245 ? -8.881  22.279  -39.969 1.00 37.69  ? 244 LEU A HD22   1 
ATOM   3832 H  HD23   . LEU A 1 245 ? -7.308  22.053  -39.970 1.00 37.69  ? 244 LEU A HD23   1 
ATOM   3833 N  N      . LYS A 1 246 ? -6.064  25.941  -36.778 1.00 26.08  ? 245 LYS A N      1 
ATOM   3834 C  CA     . LYS A 1 246 ? -5.895  27.382  -36.638 1.00 25.89  ? 245 LYS A CA     1 
ATOM   3835 C  C      . LYS A 1 246 ? -4.701  27.871  -37.440 1.00 27.36  ? 245 LYS A C      1 
ATOM   3836 O  O      . LYS A 1 246 ? -4.781  28.897  -38.134 1.00 30.73  ? 245 LYS A O      1 
ATOM   3837 C  CB     . LYS A 1 246 ? -5.730  27.760  -35.159 1.00 27.24  ? 245 LYS A CB     1 
ATOM   3838 C  CG     . LYS A 1 246 ? -5.657  29.275  -34.951 1.00 37.69  ? 245 LYS A CG     1 
ATOM   3839 C  CD     . LYS A 1 246 ? -5.737  29.642  -33.493 1.00 52.52  ? 245 LYS A CD     1 
ATOM   3840 C  CE     . LYS A 1 246 ? -6.009  31.132  -33.292 1.00 63.21  ? 245 LYS A CE     1 
ATOM   3841 N  NZ     . LYS A 1 246 ? -6.005  31.462  -31.829 1.00 64.89  1 245 LYS A NZ     1 
ATOM   3842 H  H      . LYS A 1 246 ? -5.946  25.488  -36.057 1.00 31.32  ? 245 LYS A H      1 
ATOM   3843 H  HA     . LYS A 1 246 ? -6.687  27.828  -36.975 1.00 31.09  ? 245 LYS A HA     1 
ATOM   3844 H  HB2    . LYS A 1 246 ? -6.490  27.423  -34.659 1.00 32.70  ? 245 LYS A HB2    1 
ATOM   3845 H  HB3    . LYS A 1 246 ? -4.909  27.369  -34.821 1.00 32.70  ? 245 LYS A HB3    1 
ATOM   3846 H  HG2    . LYS A 1 246 ? -4.814  29.605  -35.301 1.00 45.25  ? 245 LYS A HG2    1 
ATOM   3847 H  HG3    . LYS A 1 246 ? -6.399  29.697  -35.411 1.00 45.25  ? 245 LYS A HG3    1 
ATOM   3848 H  HD2    . LYS A 1 246 ? -6.459  29.144  -33.079 1.00 63.04  ? 245 LYS A HD2    1 
ATOM   3849 H  HD3    . LYS A 1 246 ? -4.894  29.428  -33.064 1.00 63.04  ? 245 LYS A HD3    1 
ATOM   3850 H  HE2    . LYS A 1 246 ? -5.314  31.650  -33.727 1.00 75.87  ? 245 LYS A HE2    1 
ATOM   3851 H  HE3    . LYS A 1 246 ? -6.879  31.355  -33.657 1.00 75.87  ? 245 LYS A HE3    1 
ATOM   3852 H  HZ1    . LYS A 1 246 ? -6.164  32.330  -31.712 1.00 77.88  ? 245 LYS A HZ1    1 
ATOM   3853 H  HZ2    . LYS A 1 246 ? -6.636  30.994  -31.410 1.00 77.88  ? 245 LYS A HZ2    1 
ATOM   3854 H  HZ3    . LYS A 1 246 ? -5.213  31.262  -31.474 1.00 77.88  ? 245 LYS A HZ3    1 
ATOM   3855 N  N      . VAL A 1 247 ? -3.593  27.148  -37.374 1.00 27.27  ? 246 VAL A N      1 
ATOM   3856 C  CA     . VAL A 1 247 ? -2.378  27.566  -38.066 1.00 30.24  ? 246 VAL A CA     1 
ATOM   3857 C  C      . VAL A 1 247 ? -2.502  27.365  -39.575 1.00 32.30  ? 246 VAL A C      1 
ATOM   3858 O  O      . VAL A 1 247 ? -2.180  28.259  -40.365 1.00 32.64  ? 246 VAL A O      1 
ATOM   3859 C  CB     . VAL A 1 247 ? -1.167  26.807  -37.489 1.00 29.53  ? 246 VAL A CB     1 
ATOM   3860 C  CG1    . VAL A 1 247 ? 0.074   27.058  -38.326 1.00 35.81  ? 246 VAL A CG1    1 
ATOM   3861 C  CG2    . VAL A 1 247 ? -0.925  27.231  -36.040 1.00 25.75  ? 246 VAL A CG2    1 
ATOM   3862 H  H      . VAL A 1 247 ? -3.516  26.411  -36.937 1.00 32.75  ? 246 VAL A H      1 
ATOM   3863 H  HA     . VAL A 1 247 ? -2.238  28.513  -37.906 1.00 36.30  ? 246 VAL A HA     1 
ATOM   3864 H  HB     . VAL A 1 247 ? -1.352  25.855  -37.500 1.00 35.46  ? 246 VAL A HB     1 
ATOM   3865 H  HG11   . VAL A 1 247 ? 0.818   26.570  -37.941 1.00 42.99  ? 246 VAL A HG11   1 
ATOM   3866 H  HG12   . VAL A 1 247 ? -0.090  26.752  -39.232 1.00 42.99  ? 246 VAL A HG12   1 
ATOM   3867 H  HG13   . VAL A 1 247 ? 0.266   28.009  -38.328 1.00 42.99  ? 246 VAL A HG13   1 
ATOM   3868 H  HG21   . VAL A 1 247 ? -0.161  26.744  -35.693 1.00 30.92  ? 246 VAL A HG21   1 
ATOM   3869 H  HG22   . VAL A 1 247 ? -0.750  28.184  -36.015 1.00 30.92  ? 246 VAL A HG22   1 
ATOM   3870 H  HG23   . VAL A 1 247 ? -1.715  27.025  -35.516 1.00 30.92  ? 246 VAL A HG23   1 
ATOM   3871 N  N      . LEU A 1 248 ? -2.951  26.186  -40.001 1.00 28.92  ? 247 LEU A N      1 
ATOM   3872 C  CA     . LEU A 1 248 ? -2.937  25.841  -41.419 1.00 29.77  ? 247 LEU A CA     1 
ATOM   3873 C  C      . LEU A 1 248 ? -4.102  26.473  -42.173 1.00 31.77  ? 247 LEU A C      1 
ATOM   3874 O  O      . LEU A 1 248 ? -3.928  26.967  -43.293 1.00 35.08  ? 247 LEU A O      1 
ATOM   3875 C  CB     . LEU A 1 248 ? -2.974  24.324  -41.585 1.00 29.43  ? 247 LEU A CB     1 
ATOM   3876 C  CG     . LEU A 1 248 ? -1.793  23.588  -40.972 1.00 33.85  ? 247 LEU A CG     1 
ATOM   3877 C  CD1    . LEU A 1 248 ? -2.069  22.097  -40.941 1.00 33.26  ? 247 LEU A CD1    1 
ATOM   3878 C  CD2    . LEU A 1 248 ? -0.508  23.884  -41.723 1.00 37.72  ? 247 LEU A CD2    1 
ATOM   3879 H  H      . LEU A 1 248 ? -3.268  25.570  -39.490 1.00 34.72  ? 247 LEU A H      1 
ATOM   3880 H  HA     . LEU A 1 248 ? -2.113  26.166  -41.814 1.00 35.75  ? 247 LEU A HA     1 
ATOM   3881 H  HB2    . LEU A 1 248 ? -3.781  23.986  -41.165 1.00 35.33  ? 247 LEU A HB2    1 
ATOM   3882 H  HB3    . LEU A 1 248 ? -2.990  24.116  -42.533 1.00 35.33  ? 247 LEU A HB3    1 
ATOM   3883 H  HG     . LEU A 1 248 ? -1.678  23.887  -40.057 1.00 40.64  ? 247 LEU A HG     1 
ATOM   3884 H  HD11   . LEU A 1 248 ? -1.307  21.643  -40.548 1.00 39.93  ? 247 LEU A HD11   1 
ATOM   3885 H  HD12   . LEU A 1 248 ? -2.863  21.934  -40.408 1.00 39.93  ? 247 LEU A HD12   1 
ATOM   3886 H  HD13   . LEU A 1 248 ? -2.209  21.783  -41.849 1.00 39.93  ? 247 LEU A HD13   1 
ATOM   3887 H  HD21   . LEU A 1 248 ? 0.221   23.399  -41.304 1.00 45.28  ? 247 LEU A HD21   1 
ATOM   3888 H  HD22   . LEU A 1 248 ? -0.608  23.600  -42.645 1.00 45.28  ? 247 LEU A HD22   1 
ATOM   3889 H  HD23   . LEU A 1 248 ? -0.335  24.838  -41.687 1.00 45.28  ? 247 LEU A HD23   1 
ATOM   3890 N  N      . ASN A 1 249 ? -5.297  26.449  -41.590 1.00 28.67  ? 248 ASN A N      1 
ATOM   3891 C  CA     . ASN A 1 249 ? -6.498  26.923  -42.270 1.00 30.68  ? 248 ASN A CA     1 
ATOM   3892 C  C      . ASN A 1 249 ? -6.958  28.292  -41.794 1.00 32.31  ? 248 ASN A C      1 
ATOM   3893 O  O      . ASN A 1 249 ? -7.900  28.853  -42.372 1.00 35.02  ? 248 ASN A O      1 
ATOM   3894 C  CB     . ASN A 1 249 ? -7.632  25.915  -42.094 1.00 33.86  ? 248 ASN A CB     1 
ATOM   3895 C  CG     . ASN A 1 249 ? -7.377  24.618  -42.829 1.00 40.89  ? 248 ASN A CG     1 
ATOM   3896 O  OD1    . ASN A 1 249 ? -7.802  24.440  -43.973 1.00 51.35  ? 248 ASN A OD1    1 
ATOM   3897 N  ND2    . ASN A 1 249 ? -6.698  23.716  -42.186 1.00 35.96  ? 248 ASN A ND2    1 
ATOM   3898 H  H      . ASN A 1 249 ? -5.440  26.159  -40.793 1.00 34.42  ? 248 ASN A H      1 
ATOM   3899 H  HA     . ASN A 1 249 ? -6.309  26.991  -43.219 1.00 36.83  ? 248 ASN A HA     1 
ATOM   3900 H  HB2    . ASN A 1 249 ? -7.730  25.712  -41.151 1.00 40.66  ? 248 ASN A HB2    1 
ATOM   3901 H  HB3    . ASN A 1 249 ? -8.453  26.299  -42.439 1.00 40.66  ? 248 ASN A HB3    1 
ATOM   3902 H  HD21   . ASN A 1 249 ? -6.526  22.960  -42.559 1.00 43.17  ? 248 ASN A HD21   1 
ATOM   3903 H  HD22   . ASN A 1 249 ? -6.421  23.874  -41.388 1.00 43.17  ? 248 ASN A HD22   1 
ATOM   3904 N  N      . ASN A 1 250 ? -6.299  28.862  -40.793 1.00 30.55  ? 249 ASN A N      1 
ATOM   3905 C  CA     . ASN A 1 250 ? -6.777  30.093  -40.158 1.00 30.28  ? 249 ASN A CA     1 
ATOM   3906 C  C      . ASN A 1 250 ? -8.218  29.940  -39.668 1.00 30.19  ? 249 ASN A C      1 
ATOM   3907 O  O      . ASN A 1 250 ? -8.992  30.905  -39.611 1.00 32.91  ? 249 ASN A O      1 
ATOM   3908 C  CB     . ASN A 1 250 ? -6.631  31.283  -41.098 1.00 34.19  ? 249 ASN A CB     1 
ATOM   3909 C  CG     . ASN A 1 250 ? -5.172  31.654  -41.324 1.00 38.54  ? 249 ASN A CG     1 
ATOM   3910 O  OD1    . ASN A 1 250 ? -4.565  31.310  -42.355 1.00 39.23  ? 249 ASN A OD1    1 
ATOM   3911 N  ND2    . ASN A 1 250 ? -4.594  32.346  -40.347 1.00 37.58  ? 249 ASN A ND2    1 
ATOM   3912 H  H      . ASN A 1 250 ? -5.567  28.557  -40.459 1.00 36.68  ? 249 ASN A H      1 
ATOM   3913 H  HA     . ASN A 1 250 ? -6.224  30.269  -39.380 1.00 36.36  ? 249 ASN A HA     1 
ATOM   3914 H  HB2    . ASN A 1 250 ? -7.023  31.060  -41.957 1.00 41.05  ? 249 ASN A HB2    1 
ATOM   3915 H  HB3    . ASN A 1 250 ? -7.082  32.050  -40.713 1.00 41.05  ? 249 ASN A HB3    1 
ATOM   3916 H  HD21   . ASN A 1 250 ? -3.771  32.585  -40.419 1.00 45.12  ? 249 ASN A HD21   1 
ATOM   3917 H  HD22   . ASN A 1 250 ? -5.043  32.556  -39.645 1.00 45.12  ? 249 ASN A HD22   1 
ATOM   3918 N  N      . MET A 1 251 ? -8.575  28.718  -39.288 1.00 28.89  ? 250 MET A N      1 
ATOM   3919 C  CA     . MET A 1 251 ? -9.925  28.437  -38.828 1.00 31.54  ? 250 MET A CA     1 
ATOM   3920 C  C      . MET A 1 251 ? -10.180 29.106  -37.481 1.00 30.86  ? 250 MET A C      1 
ATOM   3921 O  O      . MET A 1 251 ? -9.311  29.106  -36.606 1.00 30.23  ? 250 MET A O      1 
ATOM   3922 C  CB     . MET A 1 251 ? -10.114 26.919  -38.699 1.00 31.70  ? 250 MET A CB     1 
ATOM   3923 C  CG     . MET A 1 251 ? -11.531 26.489  -38.312 1.00 34.39  ? 250 MET A CG     1 
ATOM   3924 S  SD     . MET A 1 251 ? -11.560 24.813  -37.658 1.00 38.80  ? 250 MET A SD     1 
ATOM   3925 C  CE     . MET A 1 251 ? -13.046 24.884  -36.670 1.00 44.64  ? 250 MET A CE     1 
ATOM   3926 H  H      . MET A 1 251 ? -8.053  28.035  -39.288 1.00 34.58  ? 250 MET A H      1 
ATOM   3927 H  HA     . MET A 1 251 ? -10.562 28.770  -39.479 1.00 37.87  ? 250 MET A HA     1 
ATOM   3928 H  HB2    . MET A 1 251 ? -9.904  26.506  -39.552 1.00 38.06  ? 250 MET A HB2    1 
ATOM   3929 H  HB3    . MET A 1 251 ? -9.509  26.587  -38.018 1.00 38.06  ? 250 MET A HB3    1 
ATOM   3930 H  HG2    . MET A 1 251 ? -11.871 27.088  -37.628 1.00 41.29  ? 250 MET A HG2    1 
ATOM   3931 H  HG3    . MET A 1 251 ? -12.100 26.519  -39.097 1.00 41.29  ? 250 MET A HG3    1 
ATOM   3932 H  HE1    . MET A 1 251 ? -13.186 24.022  -36.249 1.00 53.58  ? 250 MET A HE1    1 
ATOM   3933 H  HE2    . MET A 1 251 ? -12.942 25.571  -35.994 1.00 53.58  ? 250 MET A HE2    1 
ATOM   3934 H  HE3    . MET A 1 251 ? -13.797 25.097  -37.246 1.00 53.58  ? 250 MET A HE3    1 
ATOM   3935 N  N      . GLU A 1 252 ? -11.381 29.678  -37.328 1.00 29.87  ? 251 GLU A N      1 
ATOM   3936 C  CA     . GLU A 1 252 ? -11.885 30.115  -36.022 1.00 34.77  ? 251 GLU A CA     1 
ATOM   3937 C  C      . GLU A 1 252 ? -12.223 28.910  -35.159 1.00 33.27  ? 251 GLU A C      1 
ATOM   3938 O  O      . GLU A 1 252 ? -13.102 28.124  -35.518 1.00 32.08  ? 251 GLU A O      1 
ATOM   3939 C  CB     . GLU A 1 252 ? -13.137 30.982  -36.188 1.00 45.92  ? 251 GLU A CB     1 
ATOM   3940 C  CG     . GLU A 1 252 ? -12.883 32.463  -36.172 1.00 64.45  ? 251 GLU A CG     1 
ATOM   3941 C  CD     . GLU A 1 252 ? -12.215 32.906  -34.882 1.00 74.94  ? 251 GLU A CD     1 
ATOM   3942 O  OE1    . GLU A 1 252 ? -12.392 32.207  -33.856 1.00 76.72  ? 251 GLU A OE1    1 
ATOM   3943 O  OE2    . GLU A 1 252 ? -11.497 33.931  -34.897 1.00 80.99  1 251 GLU A OE2    1 
ATOM   3944 H  H      . GLU A 1 252 ? -11.928 29.824  -37.976 1.00 35.74  ? 251 GLU A H      1 
ATOM   3945 H  HA     . GLU A 1 252 ? -11.205 30.639  -35.570 1.00 41.75  ? 251 GLU A HA     1 
ATOM   3946 H  HB2    . GLU A 1 252 ? -13.554 30.765  -37.037 1.00 55.12  ? 251 GLU A HB2    1 
ATOM   3947 H  HB3    . GLU A 1 252 ? -13.751 30.781  -35.464 1.00 55.12  ? 251 GLU A HB3    1 
ATOM   3948 H  HG2    . GLU A 1 252 ? -12.299 32.695  -36.911 1.00 77.36  ? 251 GLU A HG2    1 
ATOM   3949 H  HG3    . GLU A 1 252 ? -13.728 32.933  -36.252 1.00 77.36  ? 251 GLU A HG3    1 
ATOM   3950 N  N      . ILE A 1 253 ? -11.569 28.786  -33.998 1.00 32.48  ? 252 ILE A N      1 
ATOM   3951 C  CA     . ILE A 1 253 ? -11.739 27.624  -33.137 1.00 30.52  ? 252 ILE A CA     1 
ATOM   3952 C  C      . ILE A 1 253 ? -12.441 27.949  -31.820 1.00 28.76  ? 252 ILE A C      1 
ATOM   3953 O  O      . ILE A 1 253 ? -12.582 27.052  -30.962 1.00 26.10  ? 252 ILE A O      1 
ATOM   3954 C  CB     . ILE A 1 253 ? -10.378 26.951  -32.863 1.00 31.63  ? 252 ILE A CB     1 
ATOM   3955 C  CG1    . ILE A 1 253 ? -9.481  27.886  -32.036 1.00 31.26  ? 252 ILE A CG1    1 
ATOM   3956 C  CG2    . ILE A 1 253 ? -9.743  26.550  -34.206 1.00 30.68  ? 252 ILE A CG2    1 
ATOM   3957 C  CD1    . ILE A 1 253 ? -8.201  27.235  -31.592 1.00 34.40  ? 252 ILE A CD1    1 
ATOM   3958 H  H      . ILE A 1 253 ? -11.018 29.370  -33.690 1.00 39.00  ? 252 ILE A H      1 
ATOM   3959 H  HA     . ILE A 1 253 ? -12.291 26.978  -33.604 1.00 36.64  ? 252 ILE A HA     1 
ATOM   3960 H  HB     . ILE A 1 253 ? -10.534 26.145  -32.348 1.00 37.98  ? 252 ILE A HB     1 
ATOM   3961 H  HG12   . ILE A 1 253 ? -9.252  28.660  -32.574 1.00 37.53  ? 252 ILE A HG12   1 
ATOM   3962 H  HG13   . ILE A 1 253 ? -9.964  28.165  -31.243 1.00 37.53  ? 252 ILE A HG13   1 
ATOM   3963 H  HG21   . ILE A 1 253 ? -8.887  26.127  -34.036 1.00 36.83  ? 252 ILE A HG21   1 
ATOM   3964 H  HG22   . ILE A 1 253 ? -10.334 25.931  -34.661 1.00 36.83  ? 252 ILE A HG22   1 
ATOM   3965 H  HG23   . ILE A 1 253 ? -9.617  27.346  -34.745 1.00 36.83  ? 252 ILE A HG23   1 
ATOM   3966 H  HD11   . ILE A 1 253 ? -7.684  27.875  -31.078 1.00 41.30  ? 252 ILE A HD11   1 
ATOM   3967 H  HD12   . ILE A 1 253 ? -8.412  26.464  -31.044 1.00 41.30  ? 252 ILE A HD12   1 
ATOM   3968 H  HD13   . ILE A 1 253 ? -7.700  26.958  -32.376 1.00 41.30  ? 252 ILE A HD13   1 
ATOM   3969 N  N      . GLY A 1 254 ? -12.864 29.189  -31.613 1.00 33.28  ? 253 GLY A N      1 
ATOM   3970 C  CA     . GLY A 1 254 ? -13.561 29.527  -30.386 1.00 39.22  ? 253 GLY A CA     1 
ATOM   3971 C  C      . GLY A 1 254 ? -12.697 29.245  -29.168 1.00 36.12  ? 253 GLY A C      1 
ATOM   3972 O  O      . GLY A 1 254 ? -11.517 29.604  -29.115 1.00 33.66  ? 253 GLY A O      1 
ATOM   3973 H  H      . GLY A 1 254 ? -12.760 29.844  -32.160 1.00 39.96  ? 253 GLY A H      1 
ATOM   3974 H  HA2    . GLY A 1 254 ? -13.794 30.469  -30.391 1.00 47.08  ? 253 GLY A HA2    1 
ATOM   3975 H  HA3    . GLY A 1 254 ? -14.375 29.005  -30.318 1.00 47.08  ? 253 GLY A HA3    1 
ATOM   3976 N  N      . THR A 1 255 ? -13.283 28.571  -28.184 1.00 32.38  ? 254 THR A N      1 
ATOM   3977 C  CA     . THR A 1 255 ? -12.591 28.233  -26.946 1.00 32.75  ? 254 THR A CA     1 
ATOM   3978 C  C      . THR A 1 255 ? -12.088 26.804  -26.939 1.00 30.29  ? 254 THR A C      1 
ATOM   3979 O  O      . THR A 1 255 ? -11.781 26.270  -25.871 1.00 28.50  ? 254 THR A O      1 
ATOM   3980 C  CB     . THR A 1 255 ? -13.504 28.475  -25.741 1.00 37.20  ? 254 THR A CB     1 
ATOM   3981 O  OG1    . THR A 1 255 ? -14.711 27.721  -25.893 1.00 36.55  ? 254 THR A OG1    1 
ATOM   3982 C  CG2    . THR A 1 255 ? -13.853 29.941  -25.629 1.00 43.77  ? 254 THR A CG2    1 
ATOM   3983 H  H      . THR A 1 255 ? -14.097 28.294  -28.210 1.00 38.88  ? 254 THR A H      1 
ATOM   3984 H  HA     . THR A 1 255 ? -11.821 28.816  -26.853 1.00 39.32  ? 254 THR A HA     1 
ATOM   3985 H  HB     . THR A 1 255 ? -13.050 28.203  -24.929 1.00 44.66  ? 254 THR A HB     1 
ATOM   3986 H  HG1    . THR A 1 255 ? -15.216 27.850  -25.234 1.00 43.87  ? 254 THR A HG1    1 
ATOM   3987 H  HG21   . THR A 1 255 ? -14.431 30.086  -24.864 1.00 52.55  ? 254 THR A HG21   1 
ATOM   3988 H  HG22   . THR A 1 255 ? -13.045 30.466  -25.518 1.00 52.55  ? 254 THR A HG22   1 
ATOM   3989 H  HG23   . THR A 1 255 ? -14.312 30.235  -26.432 1.00 52.55  ? 254 THR A HG23   1 
ATOM   3990 N  N      . SER A 1 256 ? -11.987 26.181  -28.114 1.00 28.32  ? 255 SER A N      1 
ATOM   3991 C  CA     . SER A 1 256 ? -11.439 24.842  -28.232 1.00 26.64  ? 255 SER A CA     1 
ATOM   3992 C  C      . SER A 1 256 ? -10.009 24.822  -27.704 1.00 26.81  ? 255 SER A C      1 
ATOM   3993 O  O      . SER A 1 256 ? -9.321  25.846  -27.664 1.00 26.69  ? 255 SER A O      1 
ATOM   3994 C  CB     . SER A 1 256 ? -11.459 24.384  -29.701 1.00 26.79  ? 255 SER A CB     1 
ATOM   3995 O  OG     . SER A 1 256 ? -12.760 24.510  -30.263 1.00 27.52  ? 255 SER A OG     1 
ATOM   3996 H  H      . SER A 1 256 ? -12.235 26.522  -28.863 1.00 34.00  ? 255 SER A H      1 
ATOM   3997 H  HA     . SER A 1 256 ? -11.971 24.223  -27.707 1.00 31.99  ? 255 SER A HA     1 
ATOM   3998 H  HB2    . SER A 1 256 ? -10.842 24.934  -30.210 1.00 32.17  ? 255 SER A HB2    1 
ATOM   3999 H  HB3    . SER A 1 256 ? -11.186 23.454  -29.745 1.00 32.17  ? 255 SER A HB3    1 
ATOM   4000 H  HG     . SER A 1 256 ? -13.009 25.312  -30.232 1.00 33.05  ? 255 SER A HG     1 
ATOM   4001 N  N      . LEU A 1 257 ? -9.540  23.629  -27.346 1.00 27.15  ? 256 LEU A N      1 
ATOM   4002 C  CA     . LEU A 1 257 ? -8.157  23.499  -26.888 1.00 28.93  ? 256 LEU A CA     1 
ATOM   4003 C  C      . LEU A 1 257 ? -7.166  24.031  -27.923 1.00 26.11  ? 256 LEU A C      1 
ATOM   4004 O  O      . LEU A 1 257 ? -7.247  23.713  -29.114 1.00 26.07  ? 256 LEU A O      1 
ATOM   4005 C  CB     . LEU A 1 257 ? -7.825  22.042  -26.565 1.00 30.25  ? 256 LEU A CB     1 
ATOM   4006 C  CG     . LEU A 1 257 ? -8.567  21.409  -25.398 1.00 32.89  ? 256 LEU A CG     1 
ATOM   4007 C  CD1    . LEU A 1 257 ? -8.089  19.988  -25.194 1.00 31.84  ? 256 LEU A CD1    1 
ATOM   4008 C  CD2    . LEU A 1 257 ? -8.386  22.203  -24.135 1.00 33.65  ? 256 LEU A CD2    1 
ATOM   4009 H  H      . LEU A 1 257 ? -9.989  22.895  -27.359 1.00 32.60  ? 256 LEU A H      1 
ATOM   4010 H  HA     . LEU A 1 257 ? -8.045  24.017  -26.076 1.00 34.73  ? 256 LEU A HA     1 
ATOM   4011 H  HB2    . LEU A 1 257 ? -8.019  21.507  -27.351 1.00 36.32  ? 256 LEU A HB2    1 
ATOM   4012 H  HB3    . LEU A 1 257 ? -6.877  21.985  -26.366 1.00 36.32  ? 256 LEU A HB3    1 
ATOM   4013 H  HG     . LEU A 1 257 ? -9.515  21.380  -25.602 1.00 39.49  ? 256 LEU A HG     1 
ATOM   4014 H  HD11   . LEU A 1 257 ? -8.569  19.598  -24.447 1.00 38.23  ? 256 LEU A HD11   1 
ATOM   4015 H  HD12   . LEU A 1 257 ? -8.260  19.479  -26.001 1.00 38.23  ? 256 LEU A HD12   1 
ATOM   4016 H  HD13   . LEU A 1 257 ? -7.137  20.000  -25.005 1.00 38.23  ? 256 LEU A HD13   1 
ATOM   4017 H  HD21   . LEU A 1 257 ? -8.873  21.768  -23.417 1.00 40.40  ? 256 LEU A HD21   1 
ATOM   4018 H  HD22   . LEU A 1 257 ? -7.441  22.241  -23.919 1.00 40.40  ? 256 LEU A HD22   1 
ATOM   4019 H  HD23   . LEU A 1 257 ? -8.731  23.099  -24.274 1.00 40.40  ? 256 LEU A HD23   1 
ATOM   4020 N  N      . PHE A 1 258 ? -6.209  24.823  -27.450 1.00 24.70  ? 257 PHE A N      1 
ATOM   4021 C  CA     . PHE A 1 258 ? -5.191  25.405  -28.307 1.00 27.00  ? 257 PHE A CA     1 
ATOM   4022 C  C      . PHE A 1 258 ? -3.863  25.479  -27.572 1.00 28.85  ? 257 PHE A C      1 
ATOM   4023 O  O      . PHE A 1 258 ? -3.816  25.906  -26.419 1.00 31.04  ? 257 PHE A O      1 
ATOM   4024 C  CB     . PHE A 1 258 ? -5.608  26.794  -28.764 1.00 27.63  ? 257 PHE A CB     1 
ATOM   4025 C  CG     . PHE A 1 258 ? -4.600  27.448  -29.637 1.00 28.60  ? 257 PHE A CG     1 
ATOM   4026 C  CD1    . PHE A 1 258 ? -4.425  27.024  -30.946 1.00 29.87  ? 257 PHE A CD1    1 
ATOM   4027 C  CD2    . PHE A 1 258 ? -3.818  28.472  -29.151 1.00 29.93  ? 257 PHE A CD2    1 
ATOM   4028 C  CE1    . PHE A 1 258 ? -3.483  27.613  -31.755 1.00 31.41  ? 257 PHE A CE1    1 
ATOM   4029 C  CE2    . PHE A 1 258 ? -2.876  29.072  -29.948 1.00 32.77  ? 257 PHE A CE2    1 
ATOM   4030 C  CZ     . PHE A 1 258 ? -2.705  28.649  -31.258 1.00 32.51  ? 257 PHE A CZ     1 
ATOM   4031 H  H      . PHE A 1 258 ? -6.130  25.040  -26.622 1.00 29.65  ? 257 PHE A H      1 
ATOM   4032 H  HA     . PHE A 1 258 ? -5.076  24.847  -29.092 1.00 32.42  ? 257 PHE A HA     1 
ATOM   4033 H  HB2    . PHE A 1 258 ? -6.436  26.726  -29.263 1.00 33.17  ? 257 PHE A HB2    1 
ATOM   4034 H  HB3    . PHE A 1 258 ? -5.736  27.356  -27.984 1.00 33.17  ? 257 PHE A HB3    1 
ATOM   4035 H  HD1    . PHE A 1 258 ? -4.946  26.329  -31.279 1.00 35.87  ? 257 PHE A HD1    1 
ATOM   4036 H  HD2    . PHE A 1 258 ? -3.929  28.759  -28.274 1.00 35.94  ? 257 PHE A HD2    1 
ATOM   4037 H  HE1    . PHE A 1 258 ? -3.374  27.326  -32.633 1.00 37.71  ? 257 PHE A HE1    1 
ATOM   4038 H  HE2    . PHE A 1 258 ? -2.355  29.765  -29.612 1.00 39.34  ? 257 PHE A HE2    1 
ATOM   4039 H  HZ     . PHE A 1 258 ? -2.068  29.056  -31.800 1.00 39.04  ? 257 PHE A HZ     1 
ATOM   4040 N  N      . ASP A 1 259 ? -2.786  25.075  -28.237 1.00 26.68  ? 258 ASP A N      1 
ATOM   4041 C  CA     . ASP A 1 259 ? -1.440  25.139  -27.667 1.00 25.13  ? 258 ASP A CA     1 
ATOM   4042 C  C      . ASP A 1 259 ? -0.571  26.155  -28.398 1.00 27.08  ? 258 ASP A C      1 
ATOM   4043 O  O      . ASP A 1 259 ? -0.150  25.914  -29.535 1.00 26.36  ? 258 ASP A O      1 
ATOM   4044 C  CB     . ASP A 1 259 ? -0.768  23.777  -27.736 1.00 27.43  ? 258 ASP A CB     1 
ATOM   4045 C  CG     . ASP A 1 259 ? 0.513   23.753  -26.944 1.00 39.10  ? 258 ASP A CG     1 
ATOM   4046 O  OD1    . ASP A 1 259 ? 0.451   24.016  -25.718 1.00 48.28  ? 258 ASP A OD1    1 
ATOM   4047 O  OD2    . ASP A 1 259 ? 1.569   23.499  -27.546 1.00 38.95  1 258 ASP A OD2    1 
ATOM   4048 H  H      . ASP A 1 259 ? -2.807  24.754  -29.035 1.00 32.04  ? 258 ASP A H      1 
ATOM   4049 H  HA     . ASP A 1 259 ? -1.499  25.403  -26.736 1.00 30.17  ? 258 ASP A HA     1 
ATOM   4050 H  HB2    . ASP A 1 259 ? -1.365  23.106  -27.369 1.00 32.94  ? 258 ASP A HB2    1 
ATOM   4051 H  HB3    . ASP A 1 259 ? -0.558  23.570  -28.660 1.00 32.94  ? 258 ASP A HB3    1 
ATOM   4052 N  N      . GLU A 1 260 ? -0.242  27.256  -27.714 1.00 30.75  ? 259 GLU A N      1 
ATOM   4053 C  CA     . GLU A 1 260 ? 0.505   28.345  -28.344 1.00 37.50  ? 259 GLU A CA     1 
ATOM   4054 C  C      . GLU A 1 260 ? 1.919   27.917  -28.749 1.00 33.75  ? 259 GLU A C      1 
ATOM   4055 O  O      . GLU A 1 260 ? 2.409   28.295  -29.825 1.00 31.99  ? 259 GLU A O      1 
ATOM   4056 C  CB     . GLU A 1 260 ? 0.542   29.538  -27.386 1.00 53.36  ? 259 GLU A CB     1 
ATOM   4057 C  CG     . GLU A 1 260 ? 1.140   30.798  -27.946 1.00 75.97  ? 259 GLU A CG     1 
ATOM   4058 C  CD     . GLU A 1 260 ? 1.019   31.949  -26.968 1.00 95.52  ? 259 GLU A CD     1 
ATOM   4059 O  OE1    . GLU A 1 260 ? 0.725   31.682  -25.782 1.00 100.66 ? 259 GLU A OE1    1 
ATOM   4060 O  OE2    . GLU A 1 260 ? 1.211   33.113  -27.381 1.00 103.51 1 259 GLU A OE2    1 
ATOM   4061 H  H      . GLU A 1 260 ? -0.438  27.394  -26.888 1.00 36.92  ? 259 GLU A H      1 
ATOM   4062 H  HA     . GLU A 1 260 ? 0.037   28.623  -29.147 1.00 45.02  ? 259 GLU A HA     1 
ATOM   4063 H  HB2    . GLU A 1 260 ? -0.366  29.743  -27.115 1.00 64.05  ? 259 GLU A HB2    1 
ATOM   4064 H  HB3    . GLU A 1 260 ? 1.064   29.290  -26.607 1.00 64.05  ? 259 GLU A HB3    1 
ATOM   4065 H  HG2    . GLU A 1 260 ? 2.081   30.653  -28.130 1.00 91.18  ? 259 GLU A HG2    1 
ATOM   4066 H  HG3    . GLU A 1 260 ? 0.672   31.041  -28.760 1.00 91.18  ? 259 GLU A HG3    1 
ATOM   4067 N  N      . GLU A 1 261 ? 2.600   27.133  -27.910 1.00 33.47  ? 260 GLU A N      1 
ATOM   4068 C  CA     . GLU A 1 261 ? 3.942   26.691  -28.277 1.00 38.20  ? 260 GLU A CA     1 
ATOM   4069 C  C      . GLU A 1 261 ? 3.887   25.696  -29.422 1.00 32.67  ? 260 GLU A C      1 
ATOM   4070 O  O      . GLU A 1 261 ? 4.657   25.796  -30.388 1.00 33.80  ? 260 GLU A O      1 
ATOM   4071 C  CB     . GLU A 1 261 ? 4.648   26.084  -27.063 1.00 51.79  ? 260 GLU A CB     1 
ATOM   4072 C  CG     . GLU A 1 261 ? 4.900   27.073  -25.949 1.00 63.78  ? 260 GLU A CG     1 
ATOM   4073 C  CD     . GLU A 1 261 ? 5.899   28.150  -26.333 1.00 74.43  ? 260 GLU A CD     1 
ATOM   4074 O  OE1    . GLU A 1 261 ? 6.851   27.841  -27.081 1.00 77.78  ? 260 GLU A OE1    1 
ATOM   4075 O  OE2    . GLU A 1 261 ? 5.731   29.306  -25.890 1.00 79.05  1 260 GLU A OE2    1 
ATOM   4076 H  H      . GLU A 1 261 ? 2.318   26.853  -27.147 1.00 40.19  ? 260 GLU A H      1 
ATOM   4077 H  HA     . GLU A 1 261 ? 4.458   27.458  -28.572 1.00 45.86  ? 260 GLU A HA     1 
ATOM   4078 H  HB2    . GLU A 1 261 ? 4.098   25.369  -26.707 1.00 62.17  ? 260 GLU A HB2    1 
ATOM   4079 H  HB3    . GLU A 1 261 ? 5.506   25.730  -27.345 1.00 62.17  ? 260 GLU A HB3    1 
ATOM   4080 H  HG2    . GLU A 1 261 ? 4.064   27.509  -25.718 1.00 76.56  ? 260 GLU A HG2    1 
ATOM   4081 H  HG3    . GLU A 1 261 ? 5.251   26.599  -25.179 1.00 76.56  ? 260 GLU A HG3    1 
ATOM   4082 N  N      . GLY A 1 262 ? 2.961   24.745  -29.351 1.00 29.29  ? 261 GLY A N      1 
ATOM   4083 C  CA     . GLY A 1 262 ? 2.826   23.788  -30.429 1.00 28.30  ? 261 GLY A CA     1 
ATOM   4084 C  C      . GLY A 1 262 ? 2.461   24.443  -31.744 1.00 28.33  ? 261 GLY A C      1 
ATOM   4085 O  O      . GLY A 1 262 ? 2.902   23.997  -32.807 1.00 26.40  ? 261 GLY A O      1 
ATOM   4086 H  H      . GLY A 1 262 ? 2.411   24.636  -28.699 1.00 35.16  ? 261 GLY A H      1 
ATOM   4087 H  HA2    . GLY A 1 262 ? 3.663   23.312  -30.545 1.00 33.98  ? 261 GLY A HA2    1 
ATOM   4088 H  HA3    . GLY A 1 262 ? 2.135   23.145  -30.205 1.00 33.98  ? 261 GLY A HA3    1 
ATOM   4089 N  N      . ALA A 1 263 ? 1.708   25.551  -31.689 1.00 27.07  ? 262 ALA A N      1 
ATOM   4090 C  CA     . ALA A 1 263 ? 1.327   26.251  -32.914 1.00 25.88  ? 262 ALA A CA     1 
ATOM   4091 C  C      . ALA A 1 263 ? 2.547   26.653  -33.713 1.00 27.64  ? 262 ALA A C      1 
ATOM   4092 O  O      . ALA A 1 263 ? 2.497   26.707  -34.949 1.00 30.39  ? 262 ALA A O      1 
ATOM   4093 C  CB     . ALA A 1 263 ? 0.495   27.490  -32.573 1.00 27.59  ? 262 ALA A CB     1 
ATOM   4094 H  H      . ALA A 1 263 ? 1.411   25.909  -30.966 1.00 32.50  ? 262 ALA A H      1 
ATOM   4095 H  HA     . ALA A 1 263 ? 0.785   25.662  -33.463 1.00 31.08  ? 262 ALA A HA     1 
ATOM   4096 H  HB1    . ALA A 1 263 ? 0.251   27.942  -33.396 1.00 33.12  ? 262 ALA A HB1    1 
ATOM   4097 H  HB2    . ALA A 1 263 ? -0.304  27.212  -32.098 1.00 33.12  ? 262 ALA A HB2    1 
ATOM   4098 H  HB3    . ALA A 1 263 ? 1.024   28.081  -32.015 1.00 33.12  ? 262 ALA A HB3    1 
ATOM   4099 N  N      . LYS A 1 264 ? 3.650   26.942  -33.023 1.00 26.17  ? 263 LYS A N      1 
ATOM   4100 C  CA     . LYS A 1 264 ? 4.857   27.419  -33.676 1.00 28.82  ? 263 LYS A CA     1 
ATOM   4101 C  C      . LYS A 1 264 ? 5.602   26.337  -34.441 1.00 29.19  ? 263 LYS A C      1 
ATOM   4102 O  O      . LYS A 1 264 ? 6.507   26.685  -35.208 1.00 32.89  ? 263 LYS A O      1 
ATOM   4103 C  CB     . LYS A 1 264 ? 5.808   28.041  -32.652 1.00 32.23  ? 263 LYS A CB     1 
ATOM   4104 C  CG     . LYS A 1 264 ? 5.276   29.278  -31.944 1.00 40.54  ? 263 LYS A CG     1 
ATOM   4105 C  CD     . LYS A 1 264 ? 6.227   29.676  -30.815 1.00 54.62  ? 263 LYS A CD     1 
ATOM   4106 C  CE     . LYS A 1 264 ? 5.706   30.837  -29.985 1.00 65.50  ? 263 LYS A CE     1 
ATOM   4107 N  NZ     . LYS A 1 264 ? 6.617   31.095  -28.831 1.00 72.20  1 263 LYS A NZ     1 
ATOM   4108 H  H      . LYS A 1 264 ? 3.720   26.869  -32.169 1.00 31.43  ? 263 LYS A H      1 
ATOM   4109 H  HA     . LYS A 1 264 ? 4.613   28.111  -34.310 1.00 34.61  ? 263 LYS A HA     1 
ATOM   4110 H  HB2    . LYS A 1 264 ? 6.005   27.378  -31.972 1.00 38.69  ? 263 LYS A HB2    1 
ATOM   4111 H  HB3    . LYS A 1 264 ? 6.627   28.294  -33.106 1.00 38.69  ? 263 LYS A HB3    1 
ATOM   4112 H  HG2    . LYS A 1 264 ? 5.218   30.014  -32.573 1.00 48.67  ? 263 LYS A HG2    1 
ATOM   4113 H  HG3    . LYS A 1 264 ? 4.405   29.085  -31.562 1.00 48.67  ? 263 LYS A HG3    1 
ATOM   4114 H  HD2    . LYS A 1 264 ? 6.350   28.917  -30.224 1.00 65.57  ? 263 LYS A HD2    1 
ATOM   4115 H  HD3    . LYS A 1 264 ? 7.079   29.939  -31.198 1.00 65.57  ? 263 LYS A HD3    1 
ATOM   4116 H  HE2    . LYS A 1 264 ? 5.669   31.636  -30.534 1.00 78.61  ? 263 LYS A HE2    1 
ATOM   4117 H  HE3    . LYS A 1 264 ? 4.826   30.620  -29.641 1.00 78.61  ? 263 LYS A HE3    1 
ATOM   4118 H  HZ1    . LYS A 1 264 ? 6.310   31.776  -28.347 1.00 86.66  ? 263 LYS A HZ1    1 
ATOM   4119 H  HZ2    . LYS A 1 264 ? 6.666   30.372  -28.315 1.00 86.66  ? 263 LYS A HZ2    1 
ATOM   4120 H  HZ3    . LYS A 1 264 ? 7.433   31.295  -29.126 1.00 86.66  ? 263 LYS A HZ3    1 
ATOM   4121 N  N      . ILE A 1 265 ? 5.264   25.058  -34.273 1.00 29.14  ? 264 ILE A N      1 
ATOM   4122 C  CA     . ILE A 1 265 ? 5.933   23.987  -35.013 1.00 26.38  ? 264 ILE A CA     1 
ATOM   4123 C  C      . ILE A 1 265 ? 5.011   23.277  -36.004 1.00 25.82  ? 264 ILE A C      1 
ATOM   4124 O  O      . ILE A 1 265 ? 5.470   22.373  -36.713 1.00 25.51  ? 264 ILE A O      1 
ATOM   4125 C  CB     . ILE A 1 265 ? 6.589   22.971  -34.052 1.00 28.24  ? 264 ILE A CB     1 
ATOM   4126 C  CG1    . ILE A 1 265 ? 5.531   22.182  -33.284 1.00 28.29  ? 264 ILE A CG1    1 
ATOM   4127 C  CG2    . ILE A 1 265 ? 7.560   23.715  -33.130 1.00 35.45  ? 264 ILE A CG2    1 
ATOM   4128 C  CD1    . ILE A 1 265 ? 6.073   21.006  -32.410 1.00 35.43  ? 264 ILE A CD1    1 
ATOM   4129 H  H      . ILE A 1 265 ? 4.650   24.785  -33.736 1.00 34.98  ? 264 ILE A H      1 
ATOM   4130 H  HA     . ILE A 1 265 ? 6.648   24.387  -35.532 1.00 31.67  ? 264 ILE A HA     1 
ATOM   4131 H  HB     . ILE A 1 265 ? 7.103   22.343  -34.585 1.00 33.91  ? 264 ILE A HB     1 
ATOM   4132 H  HG12   . ILE A 1 265 ? 5.064   22.793  -32.692 1.00 33.97  ? 264 ILE A HG12   1 
ATOM   4133 H  HG13   . ILE A 1 265 ? 4.905   21.807  -33.922 1.00 33.97  ? 264 ILE A HG13   1 
ATOM   4134 H  HG21   . ILE A 1 265 ? 7.973   23.078  -32.526 1.00 42.56  ? 264 ILE A HG21   1 
ATOM   4135 H  HG22   . ILE A 1 265 ? 8.240   24.148  -33.670 1.00 42.56  ? 264 ILE A HG22   1 
ATOM   4136 H  HG23   . ILE A 1 265 ? 7.067   24.380  -32.623 1.00 42.56  ? 264 ILE A HG23   1 
ATOM   4137 H  HD11   . ILE A 1 265 ? 5.327   20.573  -31.967 1.00 42.53  ? 264 ILE A HD11   1 
ATOM   4138 H  HD12   . ILE A 1 265 ? 6.531   20.372  -32.984 1.00 42.53  ? 264 ILE A HD12   1 
ATOM   4139 H  HD13   . ILE A 1 265 ? 6.690   21.360  -31.751 1.00 42.53  ? 264 ILE A HD13   1 
ATOM   4140 N  N      . VAL A 1 266 ? 3.752   23.700  -36.131 1.00 24.54  ? 265 VAL A N      1 
ATOM   4141 C  CA     . VAL A 1 266 ? 2.797   22.991  -36.982 1.00 26.90  ? 265 VAL A CA     1 
ATOM   4142 C  C      . VAL A 1 266 ? 3.273   22.963  -38.443 1.00 26.48  ? 265 VAL A C      1 
ATOM   4143 O  O      . VAL A 1 266 ? 3.211   21.926  -39.118 1.00 23.83  ? 265 VAL A O      1 
ATOM   4144 C  CB     . VAL A 1 266 ? 1.401   23.636  -36.842 1.00 28.72  ? 265 VAL A CB     1 
ATOM   4145 C  CG1    . VAL A 1 266 ? 0.494   23.292  -38.043 1.00 31.08  ? 265 VAL A CG1    1 
ATOM   4146 C  CG2    . VAL A 1 266 ? 0.760   23.186  -35.543 1.00 28.13  ? 265 VAL A CG2    1 
ATOM   4147 H  H      . VAL A 1 266 ? 3.428   24.393  -35.736 1.00 29.47  ? 265 VAL A H      1 
ATOM   4148 H  HA     . VAL A 1 266 ? 2.730   22.073  -36.676 1.00 32.30  ? 265 VAL A HA     1 
ATOM   4149 H  HB     . VAL A 1 266 ? 1.501   24.601  -36.809 1.00 34.48  ? 265 VAL A HB     1 
ATOM   4150 H  HG11   . VAL A 1 266 ? -0.370  23.715  -37.918 1.00 37.31  ? 265 VAL A HG11   1 
ATOM   4151 H  HG12   . VAL A 1 266 ? 0.909   23.621  -38.856 1.00 37.31  ? 265 VAL A HG12   1 
ATOM   4152 H  HG13   . VAL A 1 266 ? 0.388   22.329  -38.092 1.00 37.31  ? 265 VAL A HG13   1 
ATOM   4153 H  HG21   . VAL A 1 266 ? -0.116  23.596  -35.464 1.00 33.77  ? 265 VAL A HG21   1 
ATOM   4154 H  HG22   . VAL A 1 266 ? 0.673   22.220  -35.552 1.00 33.77  ? 265 VAL A HG22   1 
ATOM   4155 H  HG23   . VAL A 1 266 ? 1.322   23.461  -34.802 1.00 33.77  ? 265 VAL A HG23   1 
ATOM   4156 N  N      . LYS A 1 267 ? 3.731   24.101  -38.968 1.00 26.56  ? 266 LYS A N      1 
ATOM   4157 C  CA     . LYS A 1 267 ? 4.114   24.108  -40.378 1.00 31.68  ? 266 LYS A CA     1 
ATOM   4158 C  C      . LYS A 1 267 ? 5.358   23.263  -40.615 1.00 32.08  ? 266 LYS A C      1 
ATOM   4159 O  O      . LYS A 1 267 ? 5.463   22.588  -41.649 1.00 29.84  ? 266 LYS A O      1 
ATOM   4160 C  CB     . LYS A 1 267 ? 4.303   25.541  -40.874 1.00 33.51  ? 266 LYS A CB     1 
ATOM   4161 C  CG     . LYS A 1 267 ? 2.961   26.251  -41.066 1.00 40.33  ? 266 LYS A CG     1 
ATOM   4162 C  CD     . LYS A 1 267 ? 3.102   27.684  -41.567 1.00 54.55  ? 266 LYS A CD     1 
ATOM   4163 C  CE     . LYS A 1 267 ? 1.734   28.315  -41.846 1.00 63.00  ? 266 LYS A CE     1 
ATOM   4164 N  NZ     . LYS A 1 267 ? 1.849   29.700  -42.400 1.00 68.35  1 266 LYS A NZ     1 
ATOM   4165 H  H      . LYS A 1 267 ? 3.827   24.847  -38.552 1.00 31.89  ? 266 LYS A H      1 
ATOM   4166 H  HA     . LYS A 1 267 ? 3.392   23.715  -40.894 1.00 38.03  ? 266 LYS A HA     1 
ATOM   4167 H  HB2    . LYS A 1 267 ? 4.820   26.040  -40.222 1.00 40.23  ? 266 LYS A HB2    1 
ATOM   4168 H  HB3    . LYS A 1 267 ? 4.764   25.526  -41.727 1.00 40.23  ? 266 LYS A HB3    1 
ATOM   4169 H  HG2    . LYS A 1 267 ? 2.435   25.759  -41.716 1.00 48.41  ? 266 LYS A HG2    1 
ATOM   4170 H  HG3    . LYS A 1 267 ? 2.495   26.278  -40.216 1.00 48.41  ? 266 LYS A HG3    1 
ATOM   4171 H  HD2    . LYS A 1 267 ? 3.552   28.216  -40.893 1.00 65.48  ? 266 LYS A HD2    1 
ATOM   4172 H  HD3    . LYS A 1 267 ? 3.612   27.686  -42.392 1.00 65.48  ? 266 LYS A HD3    1 
ATOM   4173 H  HE2    . LYS A 1 267 ? 1.259   27.771  -42.493 1.00 75.62  ? 266 LYS A HE2    1 
ATOM   4174 H  HE3    . LYS A 1 267 ? 1.232   28.363  -41.018 1.00 75.62  ? 266 LYS A HE3    1 
ATOM   4175 H  HZ1    . LYS A 1 267 ? 1.039   30.035  -42.550 1.00 82.04  ? 266 LYS A HZ1    1 
ATOM   4176 H  HZ2    . LYS A 1 267 ? 2.277   30.224  -41.822 1.00 82.04  ? 266 LYS A HZ2    1 
ATOM   4177 H  HZ3    . LYS A 1 267 ? 2.302   29.684  -43.166 1.00 82.04  ? 266 LYS A HZ3    1 
ATOM   4178 N  N      . ASP A 1 268 ? 6.296   23.266  -39.659 1.00 29.44  ? 267 ASP A N      1 
ATOM   4179 C  CA     . ASP A 1 268 ? 7.459   22.395  -39.758 1.00 30.65  ? 267 ASP A CA     1 
ATOM   4180 C  C      . ASP A 1 268 ? 7.054   20.926  -39.729 1.00 29.89  ? 267 ASP A C      1 
ATOM   4181 O  O      . ASP A 1 268 ? 7.634   20.102  -40.446 1.00 29.01  ? 267 ASP A O      1 
ATOM   4182 C  CB     . ASP A 1 268 ? 8.437   22.683  -38.616 1.00 39.72  ? 267 ASP A CB     1 
ATOM   4183 C  CG     . ASP A 1 268 ? 9.239   23.953  -38.828 1.00 50.09  ? 267 ASP A CG     1 
ATOM   4184 O  OD1    . ASP A 1 268 ? 9.120   24.579  -39.909 1.00 49.36  ? 267 ASP A OD1    1 
ATOM   4185 O  OD2    . ASP A 1 268 ? 10.007  24.306  -37.902 1.00 55.56  1 267 ASP A OD2    1 
ATOM   4186 H  H      . ASP A 1 268 ? 6.277   23.758  -38.954 1.00 35.34  ? 267 ASP A H      1 
ATOM   4187 H  HA     . ASP A 1 268 ? 7.915   22.566  -40.597 1.00 36.79  ? 267 ASP A HA     1 
ATOM   4188 H  HB2    . ASP A 1 268 ? 7.937   22.779  -37.790 1.00 47.68  ? 267 ASP A HB2    1 
ATOM   4189 H  HB3    . ASP A 1 268 ? 9.061   21.944  -38.542 1.00 47.68  ? 267 ASP A HB3    1 
ATOM   4190 N  N      . LEU A 1 269 ? 6.061   20.573  -38.907 1.00 28.35  ? 268 LEU A N      1 
ATOM   4191 C  CA     . LEU A 1 269 ? 5.609   19.183  -38.897 1.00 25.90  ? 268 LEU A CA     1 
ATOM   4192 C  C      . LEU A 1 269 ? 4.965   18.804  -40.220 1.00 25.36  ? 268 LEU A C      1 
ATOM   4193 O  O      . LEU A 1 269 ? 5.185   17.695  -40.715 1.00 24.80  ? 268 LEU A O      1 
ATOM   4194 C  CB     . LEU A 1 269 ? 4.623   18.918  -37.752 1.00 22.09  ? 268 LEU A CB     1 
ATOM   4195 C  CG     . LEU A 1 269 ? 5.138   19.095  -36.336 1.00 22.51  ? 268 LEU A CG     1 
ATOM   4196 C  CD1    . LEU A 1 269 ? 4.014   18.962  -35.329 1.00 22.35  ? 268 LEU A CD1    1 
ATOM   4197 C  CD2    . LEU A 1 269 ? 6.182   18.022  -36.029 1.00 23.29  ? 268 LEU A CD2    1 
ATOM   4198 H  H      . LEU A 1 269 ? 5.649   21.098  -38.365 1.00 34.04  ? 268 LEU A H      1 
ATOM   4199 H  HA     . LEU A 1 269 ? 6.377   18.606  -38.765 1.00 31.10  ? 268 LEU A HA     1 
ATOM   4200 H  HB2    . LEU A 1 269 ? 3.870   19.521  -37.858 1.00 26.53  ? 268 LEU A HB2    1 
ATOM   4201 H  HB3    . LEU A 1 269 ? 4.311   18.003  -37.829 1.00 26.53  ? 268 LEU A HB3    1 
ATOM   4202 H  HG     . LEU A 1 269 ? 5.547   19.970  -36.239 1.00 27.04  ? 268 LEU A HG     1 
ATOM   4203 H  HD11   . LEU A 1 269 ? 4.375   19.080  -34.436 1.00 26.84  ? 268 LEU A HD11   1 
ATOM   4204 H  HD12   . LEU A 1 269 ? 3.347   19.642  -35.508 1.00 26.84  ? 268 LEU A HD12   1 
ATOM   4205 H  HD13   . LEU A 1 269 ? 3.619   18.080  -35.412 1.00 26.84  ? 268 LEU A HD13   1 
ATOM   4206 H  HD21   . LEU A 1 269 ? 6.503   18.146  -35.122 1.00 27.97  ? 268 LEU A HD21   1 
ATOM   4207 H  HD22   . LEU A 1 269 ? 5.771   17.148  -36.118 1.00 27.97  ? 268 LEU A HD22   1 
ATOM   4208 H  HD23   . LEU A 1 269 ? 6.917   18.108  -36.655 1.00 27.97  ? 268 LEU A HD23   1 
ATOM   4209 N  N      . MET A 1 270 ? 4.160   19.695  -40.808 1.00 26.02  ? 269 MET A N      1 
ATOM   4210 C  CA     . MET A 1 270 ? 3.514   19.354  -42.077 1.00 28.18  ? 269 MET A CA     1 
ATOM   4211 C  C      . MET A 1 270 ? 4.538   19.222  -43.188 1.00 28.53  ? 269 MET A C      1 
ATOM   4212 O  O      . MET A 1 270 ? 4.414   18.339  -44.037 1.00 29.97  ? 269 MET A O      1 
ATOM   4213 C  CB     . MET A 1 270 ? 2.458   20.389  -42.465 1.00 30.43  ? 269 MET A CB     1 
ATOM   4214 C  CG     . MET A 1 270 ? 1.285   20.490  -41.509 1.00 32.62  ? 269 MET A CG     1 
ATOM   4215 S  SD     . MET A 1 270 ? 0.387   18.943  -41.117 1.00 36.10  ? 269 MET A SD     1 
ATOM   4216 C  CE     . MET A 1 270 ? -0.472  18.686  -42.662 1.00 43.15  ? 269 MET A CE     1 
ATOM   4217 H  H      . MET A 1 270 ? 3.976   20.479  -40.504 1.00 31.25  ? 269 MET A H      1 
ATOM   4218 H  HA     . MET A 1 270 ? 3.063   18.502  -41.972 1.00 33.83  ? 269 MET A HA     1 
ATOM   4219 H  HB2    . MET A 1 270 ? 2.879   21.261  -42.506 1.00 36.53  ? 269 MET A HB2    1 
ATOM   4220 H  HB3    . MET A 1 270 ? 2.105   20.157  -43.338 1.00 36.53  ? 269 MET A HB3    1 
ATOM   4221 H  HG2    . MET A 1 270 ? 1.611   20.850  -40.670 1.00 39.16  ? 269 MET A HG2    1 
ATOM   4222 H  HG3    . MET A 1 270 ? 0.639   21.105  -41.890 1.00 39.16  ? 269 MET A HG3    1 
ATOM   4223 H  HE1    . MET A 1 270 ? -1.003  17.877  -42.597 1.00 51.79  ? 269 MET A HE1    1 
ATOM   4224 H  HE2    . MET A 1 270 ? -1.048  19.447  -42.832 1.00 51.79  ? 269 MET A HE2    1 
ATOM   4225 H  HE3    . MET A 1 270 ? 0.180   18.598  -43.374 1.00 51.79  ? 269 MET A HE3    1 
ATOM   4226 N  N      . SER A 1 271 ? 5.571   20.074  -43.194 1.00 29.51  ? 270 SER A N      1 
ATOM   4227 C  CA     . SER A 1 271 ? 6.623   19.944  -44.196 1.00 34.27  ? 270 SER A CA     1 
ATOM   4228 C  C      . SER A 1 271 ? 7.340   18.619  -44.068 1.00 31.68  ? 270 SER A C      1 
ATOM   4229 O  O      . SER A 1 271 ? 7.663   17.987  -45.084 1.00 29.45  ? 270 SER A O      1 
ATOM   4230 C  CB     . SER A 1 271 ? 7.629   21.082  -44.084 1.00 40.67  ? 270 SER A CB     1 
ATOM   4231 O  OG     . SER A 1 271 ? 7.043   22.299  -44.498 1.00 47.67  ? 270 SER A OG     1 
ATOM   4232 H  H      . SER A 1 271 ? 5.680   20.722  -42.639 1.00 35.43  ? 270 SER A H      1 
ATOM   4233 H  HA     . SER A 1 271 ? 6.223   19.984  -45.079 1.00 41.15  ? 270 SER A HA     1 
ATOM   4234 H  HB2    . SER A 1 271 ? 7.913   21.165  -43.160 1.00 48.82  ? 270 SER A HB2    1 
ATOM   4235 H  HB3    . SER A 1 271 ? 8.392   20.888  -44.651 1.00 48.82  ? 270 SER A HB3    1 
ATOM   4236 H  HG     . SER A 1 271 ? 6.379   22.477  -44.015 1.00 57.22  ? 270 SER A HG     1 
ATOM   4237 N  N      . LYS A 1 272 ? 7.612   18.190  -42.830 1.00 28.03  ? 271 LYS A N      1 
ATOM   4238 C  CA     . LYS A 1 272 ? 8.289   16.915  -42.619 1.00 27.79  ? 271 LYS A CA     1 
ATOM   4239 C  C      . LYS A 1 272 ? 7.397   15.747  -43.015 1.00 28.16  ? 271 LYS A C      1 
ATOM   4240 O  O      . LYS A 1 272 ? 7.881   14.753  -43.581 1.00 28.05  ? 271 LYS A O      1 
ATOM   4241 C  CB     . LYS A 1 272 ? 8.730   16.779  -41.167 1.00 28.22  ? 271 LYS A CB     1 
ATOM   4242 C  CG     . LYS A 1 272 ? 9.334   15.408  -40.839 1.00 31.27  ? 271 LYS A CG     1 
ATOM   4243 C  CD     . LYS A 1 272 ? 9.996   15.342  -39.462 1.00 33.20  ? 271 LYS A CD     1 
ATOM   4244 C  CE     . LYS A 1 272 ? 10.783  14.062  -39.285 1.00 36.02  ? 271 LYS A CE     1 
ATOM   4245 N  NZ     . LYS A 1 272 ? 11.452  14.060  -37.979 1.00 34.97  1 271 LYS A NZ     1 
ATOM   4246 H  H      . LYS A 1 272 ? 7.417   18.615  -42.108 1.00 33.65  ? 271 LYS A H      1 
ATOM   4247 H  HA     . LYS A 1 272 ? 9.083   16.886  -43.175 1.00 33.37  ? 271 LYS A HA     1 
ATOM   4248 H  HB2    . LYS A 1 272 ? 9.401   17.453  -40.979 1.00 33.88  ? 271 LYS A HB2    1 
ATOM   4249 H  HB3    . LYS A 1 272 ? 7.960   16.910  -40.592 1.00 33.88  ? 271 LYS A HB3    1 
ATOM   4250 H  HG2    . LYS A 1 272 ? 8.629   14.742  -40.862 1.00 37.54  ? 271 LYS A HG2    1 
ATOM   4251 H  HG3    . LYS A 1 272 ? 10.008  15.196  -41.503 1.00 37.54  ? 271 LYS A HG3    1 
ATOM   4252 H  HD2    . LYS A 1 272 ? 10.605  16.090  -39.364 1.00 39.86  ? 271 LYS A HD2    1 
ATOM   4253 H  HD3    . LYS A 1 272 ? 9.311   15.375  -38.776 1.00 39.86  ? 271 LYS A HD3    1 
ATOM   4254 H  HE2    . LYS A 1 272 ? 10.181  13.302  -39.325 1.00 43.24  ? 271 LYS A HE2    1 
ATOM   4255 H  HE3    . LYS A 1 272 ? 11.459  13.997  -39.978 1.00 43.24  ? 271 LYS A HE3    1 
ATOM   4256 H  HZ1    . LYS A 1 272 ? 11.915  13.307  -37.876 1.00 41.99  ? 271 LYS A HZ1    1 
ATOM   4257 H  HZ2    . LYS A 1 272 ? 12.008  14.752  -37.922 1.00 41.99  ? 271 LYS A HZ2    1 
ATOM   4258 H  HZ3    . LYS A 1 272 ? 10.848  14.120  -37.328 1.00 41.99  ? 271 LYS A HZ3    1 
ATOM   4259 N  N      . ALA A 1 273 ? 6.091   15.850  -42.749 1.00 26.80  ? 272 ALA A N      1 
ATOM   4260 C  CA     . ALA A 1 273 ? 5.185   14.799  -43.195 1.00 25.86  ? 272 ALA A CA     1 
ATOM   4261 C  C      . ALA A 1 273 ? 5.184   14.690  -44.720 1.00 27.18  ? 272 ALA A C      1 
ATOM   4262 O  O      . ALA A 1 273 ? 5.204   13.586  -45.270 1.00 30.56  ? 272 ALA A O      1 
ATOM   4263 C  CB     . ALA A 1 273 ? 3.775   15.059  -42.679 1.00 25.54  ? 272 ALA A CB     1 
ATOM   4264 H  H      . ALA A 1 273 ? 5.717   16.498  -42.325 1.00 32.18  ? 272 ALA A H      1 
ATOM   4265 H  HA     . ALA A 1 273 ? 5.484   13.950  -42.834 1.00 31.05  ? 272 ALA A HA     1 
ATOM   4266 H  HB1    . ALA A 1 273 ? 3.190   14.350  -42.987 1.00 30.67  ? 272 ALA A HB1    1 
ATOM   4267 H  HB2    . ALA A 1 273 ? 3.792   15.077  -41.710 1.00 30.67  ? 272 ALA A HB2    1 
ATOM   4268 H  HB3    . ALA A 1 273 ? 3.467   15.914  -43.020 1.00 30.67  ? 272 ALA A HB3    1 
ATOM   4269 N  N      . GLU A 1 274 ? 5.166   15.821  -45.417 1.00 26.09  ? 273 GLU A N      1 
ATOM   4270 C  CA     . GLU A 1 274 ? 5.245   15.790  -46.881 1.00 28.74  ? 273 GLU A CA     1 
ATOM   4271 C  C      . GLU A 1 274 ? 6.557   15.167  -47.343 1.00 30.11  ? 273 GLU A C      1 
ATOM   4272 O  O      . GLU A 1 274 ? 6.574   14.341  -48.265 1.00 31.51  ? 273 GLU A O      1 
ATOM   4273 C  CB     . GLU A 1 274 ? 5.087   17.207  -47.427 1.00 37.99  ? 273 GLU A CB     1 
ATOM   4274 C  CG     . GLU A 1 274 ? 5.009   17.254  -48.942 1.00 59.07  ? 273 GLU A CG     1 
ATOM   4275 C  CD     . GLU A 1 274 ? 4.454   18.564  -49.456 1.00 71.30  ? 273 GLU A CD     1 
ATOM   4276 O  OE1    . GLU A 1 274 ? 4.123   19.435  -48.620 1.00 75.84  ? 273 GLU A OE1    1 
ATOM   4277 O  OE2    . GLU A 1 274 ? 4.346   18.710  -50.692 1.00 74.16  1 273 GLU A OE2    1 
ATOM   4278 H  H      . GLU A 1 274 ? 5.110   16.608  -45.077 1.00 31.21  ? 273 GLU A H      1 
ATOM   4279 H  HA     . GLU A 1 274 ? 4.517   15.250  -47.227 1.00 34.51  ? 273 GLU A HA     1 
ATOM   4280 H  HB2    . GLU A 1 274 ? 4.271   17.592  -47.073 1.00 45.60  ? 273 GLU A HB2    1 
ATOM   4281 H  HB3    . GLU A 1 274 ? 5.851   17.738  -47.150 1.00 45.60  ? 273 GLU A HB3    1 
ATOM   4282 H  HG2    . GLU A 1 274 ? 5.899   17.140  -49.308 1.00 70.90  ? 273 GLU A HG2    1 
ATOM   4283 H  HG3    . GLU A 1 274 ? 4.429   16.540  -49.251 1.00 70.90  ? 273 GLU A HG3    1 
ATOM   4284 N  N      . LYS A 1 275 ? 7.667   15.522  -46.686 1.00 32.79  ? 274 LYS A N      1 
ATOM   4285 C  CA     . LYS A 1 275 ? 8.974   14.992  -47.076 1.00 35.47  ? 274 LYS A CA     1 
ATOM   4286 C  C      . LYS A 1 275 ? 9.058   13.489  -46.878 1.00 31.75  ? 274 LYS A C      1 
ATOM   4287 O  O      . LYS A 1 275 ? 9.758   12.803  -47.641 1.00 30.77  ? 274 LYS A O      1 
ATOM   4288 C  CB     . LYS A 1 275 ? 10.071  15.683  -46.260 1.00 41.52  ? 274 LYS A CB     1 
ATOM   4289 C  CG     . LYS A 1 275 ? 11.508  15.223  -46.535 1.00 46.49  ? 274 LYS A CG     1 
ATOM   4290 C  CD     . LYS A 1 275 ? 12.478  16.042  -45.687 1.00 56.06  ? 274 LYS A CD     1 
ATOM   4291 C  CE     . LYS A 1 275 ? 13.921  15.857  -46.098 1.00 71.00  ? 274 LYS A CE     1 
ATOM   4292 N  NZ     . LYS A 1 275 ? 14.405  14.483  -45.826 1.00 79.42  1 274 LYS A NZ     1 
ATOM   4293 H  H      . LYS A 1 275 ? 7.688   16.062  -46.017 1.00 39.36  ? 274 LYS A H      1 
ATOM   4294 H  HA     . LYS A 1 275 ? 9.129   15.183  -48.014 1.00 42.59  ? 274 LYS A HA     1 
ATOM   4295 H  HB2    . LYS A 1 275 ? 10.032  16.635  -46.443 1.00 49.85  ? 274 LYS A HB2    1 
ATOM   4296 H  HB3    . LYS A 1 275 ? 9.893   15.529  -45.319 1.00 49.85  ? 274 LYS A HB3    1 
ATOM   4297 H  HG2    . LYS A 1 275 ? 11.602  14.288  -46.297 1.00 55.81  ? 274 LYS A HG2    1 
ATOM   4298 H  HG3    . LYS A 1 275 ? 11.722  15.362  -47.471 1.00 55.81  ? 274 LYS A HG3    1 
ATOM   4299 H  HD2    . LYS A 1 275 ? 12.259  16.983  -45.777 1.00 67.29  ? 274 LYS A HD2    1 
ATOM   4300 H  HD3    . LYS A 1 275 ? 12.393  15.770  -44.760 1.00 67.29  ? 274 LYS A HD3    1 
ATOM   4301 H  HE2    . LYS A 1 275 ? 14.005  16.025  -47.049 1.00 85.22  ? 274 LYS A HE2    1 
ATOM   4302 H  HE3    . LYS A 1 275 ? 14.476  16.477  -45.599 1.00 85.22  ? 274 LYS A HE3    1 
ATOM   4303 H  HZ1    . LYS A 1 275 ? 15.255  14.405  -46.078 1.00 95.33  ? 274 LYS A HZ1    1 
ATOM   4304 H  HZ2    . LYS A 1 275 ? 14.343  14.306  -44.956 1.00 95.33  ? 274 LYS A HZ2    1 
ATOM   4305 H  HZ3    . LYS A 1 275 ? 13.914  13.893  -46.277 1.00 95.33  ? 274 LYS A HZ3    1 
ATOM   4306 N  N      . ASN A 1 276 ? 8.385   12.968  -45.848 1.00 31.00  ? 275 ASN A N      1 
ATOM   4307 C  CA     . ASN A 1 276 ? 8.445   11.563  -45.486 1.00 30.44  ? 275 ASN A CA     1 
ATOM   4308 C  C      . ASN A 1 276 ? 7.277   10.751  -46.029 1.00 31.55  ? 275 ASN A C      1 
ATOM   4309 O  O      . ASN A 1 276 ? 7.150   9.571   -45.689 1.00 33.05  ? 275 ASN A O      1 
ATOM   4310 C  CB     . ASN A 1 276 ? 8.493   11.413  -43.956 1.00 30.42  ? 275 ASN A CB     1 
ATOM   4311 C  CG     . ASN A 1 276 ? 9.835   11.798  -43.377 1.00 36.14  ? 275 ASN A CG     1 
ATOM   4312 O  OD1    . ASN A 1 276 ? 10.752  12.218  -44.093 1.00 38.28  ? 275 ASN A OD1    1 
ATOM   4313 N  ND2    . ASN A 1 276 ? 9.962   11.650  -42.076 1.00 41.93  ? 275 ASN A ND2    1 
ATOM   4314 H  H      . ASN A 1 276 ? 7.873   13.429  -45.333 1.00 37.22  ? 275 ASN A H      1 
ATOM   4315 H  HA     . ASN A 1 276 ? 9.262   11.183  -45.847 1.00 36.55  ? 275 ASN A HA     1 
ATOM   4316 H  HB2    . ASN A 1 276 ? 7.819   11.988  -43.561 1.00 36.53  ? 275 ASN A HB2    1 
ATOM   4317 H  HB3    . ASN A 1 276 ? 8.319   10.488  -43.723 1.00 36.53  ? 275 ASN A HB3    1 
ATOM   4318 H  HD21   . ASN A 1 276 ? 10.703  11.853  -41.690 1.00 50.34  ? 275 ASN A HD21   1 
ATOM   4319 H  HD22   . ASN A 1 276 ? 9.303   11.350  -41.611 1.00 50.34  ? 275 ASN A HD22   1 
ATOM   4320 N  N      . GLY A 1 277 ? 6.409   11.347  -46.840 1.00 31.43  ? 276 GLY A N      1 
ATOM   4321 C  CA     . GLY A 1 277 ? 5.289   10.608  -47.387 1.00 29.63  ? 276 GLY A CA     1 
ATOM   4322 C  C      . GLY A 1 277 ? 4.225   10.184  -46.397 1.00 29.75  ? 276 GLY A C      1 
ATOM   4323 O  O      . GLY A 1 277 ? 3.595   9.140   -46.591 1.00 33.16  ? 276 GLY A O      1 
ATOM   4324 H  H      . GLY A 1 277 ? 6.449   12.170  -47.085 1.00 37.73  ? 276 GLY A H      1 
ATOM   4325 H  HA2    . GLY A 1 277 ? 4.860   11.152  -48.066 1.00 35.58  ? 276 GLY A HA2    1 
ATOM   4326 H  HA3    . GLY A 1 277 ? 5.626   9.807   -47.818 1.00 35.58  ? 276 GLY A HA3    1 
ATOM   4327 N  N      . VAL A 1 278 ? 4.009   10.957  -45.333 1.00 27.79  ? 277 VAL A N      1 
ATOM   4328 C  CA     . VAL A 1 278 ? 3.014   10.631  -44.318 1.00 26.47  ? 277 VAL A CA     1 
ATOM   4329 C  C      . VAL A 1 278 ? 1.747   11.397  -44.639 1.00 27.51  ? 277 VAL A C      1 
ATOM   4330 O  O      . VAL A 1 278 ? 1.748   12.632  -44.638 1.00 31.06  ? 277 VAL A O      1 
ATOM   4331 C  CB     . VAL A 1 278 ? 3.521   10.976  -42.907 1.00 25.09  ? 277 VAL A CB     1 
ATOM   4332 C  CG1    . VAL A 1 278 ? 2.456   10.673  -41.853 1.00 24.82  ? 277 VAL A CG1    1 
ATOM   4333 C  CG2    . VAL A 1 278 ? 4.803   10.207  -42.612 1.00 28.06  ? 277 VAL A CG2    1 
ATOM   4334 H  H      . VAL A 1 278 ? 4.434   11.688  -45.177 1.00 33.37  ? 277 VAL A H      1 
ATOM   4335 H  HA     . VAL A 1 278 ? 2.817   9.681   -44.350 1.00 31.78  ? 277 VAL A HA     1 
ATOM   4336 H  HB     . VAL A 1 278 ? 3.723   11.924  -42.866 1.00 30.13  ? 277 VAL A HB     1 
ATOM   4337 H  HG11   . VAL A 1 278 ? 2.806   10.901  -40.977 1.00 29.80  ? 277 VAL A HG11   1 
ATOM   4338 H  HG12   . VAL A 1 278 ? 1.666   11.202  -42.042 1.00 29.80  ? 277 VAL A HG12   1 
ATOM   4339 H  HG13   . VAL A 1 278 ? 2.239   9.728   -41.887 1.00 29.80  ? 277 VAL A HG13   1 
ATOM   4340 H  HG21   . VAL A 1 278 ? 5.110   10.435  -41.721 1.00 33.69  ? 277 VAL A HG21   1 
ATOM   4341 H  HG22   . VAL A 1 278 ? 4.620   9.256   -42.666 1.00 33.69  ? 277 VAL A HG22   1 
ATOM   4342 H  HG23   . VAL A 1 278 ? 5.475   10.453  -43.267 1.00 33.69  ? 277 VAL A HG23   1 
ATOM   4343 N  N      . LYS A 1 279 ? 0.669   10.682  -44.927 1.00 27.45  ? 278 LYS A N      1 
ATOM   4344 C  CA     . LYS A 1 279 ? -0.621  11.328  -45.140 1.00 31.12  ? 278 LYS A CA     1 
ATOM   4345 C  C      . LYS A 1 279 ? -1.218  11.748  -43.802 1.00 29.88  ? 278 LYS A C      1 
ATOM   4346 O  O      . LYS A 1 279 ? -1.417  10.902  -42.921 1.00 25.79  ? 278 LYS A O      1 
ATOM   4347 C  CB     . LYS A 1 279 ? -1.592  10.395  -45.841 1.00 34.76  ? 278 LYS A CB     1 
ATOM   4348 C  CG     . LYS A 1 279 ? -2.951  11.061  -46.118 1.00 43.26  ? 278 LYS A CG     1 
ATOM   4349 C  CD     . LYS A 1 279 ? -3.800  10.236  -47.070 1.00 59.71  ? 278 LYS A CD     1 
ATOM   4350 C  CE     . LYS A 1 279 ? -5.174  10.872  -47.290 1.00 71.49  ? 278 LYS A CE     1 
ATOM   4351 N  NZ     . LYS A 1 279 ? -5.087  12.310  -47.661 1.00 73.74  1 278 LYS A NZ     1 
ATOM   4352 H  H      . LYS A 1 279 ? 0.655   9.825   -45.004 1.00 32.96  ? 278 LYS A H      1 
ATOM   4353 H  HA     . LYS A 1 279 ? -0.502  12.119  -45.689 1.00 37.36  ? 278 LYS A HA     1 
ATOM   4354 H  HB2    . LYS A 1 279 ? -1.212  10.121  -46.690 1.00 41.73  ? 278 LYS A HB2    1 
ATOM   4355 H  HB3    . LYS A 1 279 ? -1.746  9.618   -45.280 1.00 41.73  ? 278 LYS A HB3    1 
ATOM   4356 H  HG2    . LYS A 1 279 ? -3.436  11.154  -45.283 1.00 51.93  ? 278 LYS A HG2    1 
ATOM   4357 H  HG3    . LYS A 1 279 ? -2.804  11.931  -46.519 1.00 51.93  ? 278 LYS A HG3    1 
ATOM   4358 H  HD2    . LYS A 1 279 ? -3.352  10.177  -47.929 1.00 71.68  ? 278 LYS A HD2    1 
ATOM   4359 H  HD3    . LYS A 1 279 ? -3.931  9.350   -46.698 1.00 71.68  ? 278 LYS A HD3    1 
ATOM   4360 H  HE2    . LYS A 1 279 ? -5.629  10.403  -48.007 1.00 85.80  ? 278 LYS A HE2    1 
ATOM   4361 H  HE3    . LYS A 1 279 ? -5.689  10.804  -46.470 1.00 85.80  ? 278 LYS A HE3    1 
ATOM   4362 H  HZ1    . LYS A 1 279 ? -5.904  12.643  -47.780 1.00 88.50  ? 278 LYS A HZ1    1 
ATOM   4363 H  HZ2    . LYS A 1 279 ? -4.679  12.766  -47.015 1.00 88.50  ? 278 LYS A HZ2    1 
ATOM   4364 H  HZ3    . LYS A 1 279 ? -4.625  12.401  -48.416 1.00 88.50  ? 278 LYS A HZ3    1 
ATOM   4365 N  N      . ILE A 1 280 ? -1.527  13.041  -43.666 1.00 26.90  ? 279 ILE A N      1 
ATOM   4366 C  CA     . ILE A 1 280 ? -2.124  13.600  -42.453 1.00 28.14  ? 279 ILE A CA     1 
ATOM   4367 C  C      . ILE A 1 280 ? -3.614  13.792  -42.685 1.00 28.44  ? 279 ILE A C      1 
ATOM   4368 O  O      . ILE A 1 280 ? -4.022  14.479  -43.633 1.00 29.00  ? 279 ILE A O      1 
ATOM   4369 C  CB     . ILE A 1 280 ? -1.474  14.941  -42.068 1.00 31.47  ? 279 ILE A CB     1 
ATOM   4370 C  CG1    . ILE A 1 280 ? 0.049   14.808  -41.938 1.00 28.90  ? 279 ILE A CG1    1 
ATOM   4371 C  CG2    . ILE A 1 280 ? -2.058  15.472  -40.760 1.00 33.60  ? 279 ILE A CG2    1 
ATOM   4372 C  CD1    . ILE A 1 280 ? 0.505   13.810  -40.928 1.00 27.51  ? 279 ILE A CD1    1 
ATOM   4373 H  H      . ILE A 1 280 ? -1.397  13.628  -44.281 1.00 32.30  ? 279 ILE A H      1 
ATOM   4374 H  HA     . ILE A 1 280 ? -2.004  12.978  -41.718 1.00 33.79  ? 279 ILE A HA     1 
ATOM   4375 H  HB     . ILE A 1 280 ? -1.664  15.583  -42.769 1.00 37.78  ? 279 ILE A HB     1 
ATOM   4376 H  HG12   . ILE A 1 280 ? 0.411   14.541  -42.798 1.00 34.70  ? 279 ILE A HG12   1 
ATOM   4377 H  HG13   . ILE A 1 280 ? 0.414   15.670  -41.684 1.00 34.70  ? 279 ILE A HG13   1 
ATOM   4378 H  HG21   . ILE A 1 280 ? -1.631  16.315  -40.544 1.00 40.34  ? 279 ILE A HG21   1 
ATOM   4379 H  HG22   . ILE A 1 280 ? -3.012  15.603  -40.872 1.00 40.34  ? 279 ILE A HG22   1 
ATOM   4380 H  HG23   . ILE A 1 280 ? -1.892  14.826  -40.056 1.00 40.34  ? 279 ILE A HG23   1 
ATOM   4381 H  HD11   . ILE A 1 280 ? 1.475   13.795  -40.915 1.00 33.03  ? 279 ILE A HD11   1 
ATOM   4382 H  HD12   . ILE A 1 280 ? 0.166   14.067  -40.056 1.00 33.03  ? 279 ILE A HD12   1 
ATOM   4383 H  HD13   . ILE A 1 280 ? 0.163   12.936  -41.172 1.00 33.03  ? 279 ILE A HD13   1 
ATOM   4384 N  N      . THR A 1 281 ? -4.427  13.197  -41.824 1.00 26.71  ? 280 THR A N      1 
ATOM   4385 C  CA     . THR A 1 281 ? -5.874  13.356  -41.861 1.00 27.64  ? 280 THR A CA     1 
ATOM   4386 C  C      . THR A 1 281 ? -6.327  14.150  -40.643 1.00 25.23  ? 280 THR A C      1 
ATOM   4387 O  O      . THR A 1 281 ? -6.194  13.689  -39.503 1.00 23.58  ? 280 THR A O      1 
ATOM   4388 C  CB     . THR A 1 281 ? -6.573  12.003  -41.892 1.00 30.90  ? 280 THR A CB     1 
ATOM   4389 O  OG1    . THR A 1 281 ? -6.174  11.311  -43.079 1.00 34.15  ? 280 THR A OG1    1 
ATOM   4390 C  CG2    . THR A 1 281 ? -8.108  12.176  -41.870 1.00 29.48  ? 280 THR A CG2    1 
ATOM   4391 H  H      . THR A 1 281 ? -4.157  12.681  -41.190 1.00 32.07  ? 280 THR A H      1 
ATOM   4392 H  HA     . THR A 1 281 ? -6.124  13.848  -42.659 1.00 33.19  ? 280 THR A HA     1 
ATOM   4393 H  HB     . THR A 1 281 ? -6.311  11.487  -41.113 1.00 37.10  ? 280 THR A HB     1 
ATOM   4394 H  HG1    . THR A 1 281 ? -5.341  11.199  -43.080 1.00 41.00  ? 280 THR A HG1    1 
ATOM   4395 H  HG21   . THR A 1 281 ? -8.539  11.308  -41.889 1.00 35.40  ? 280 THR A HG21   1 
ATOM   4396 H  HG22   . THR A 1 281 ? -8.377  12.644  -41.064 1.00 35.40  ? 280 THR A HG22   1 
ATOM   4397 H  HG23   . THR A 1 281 ? -8.394  12.688  -42.642 1.00 35.40  ? 280 THR A HG23   1 
ATOM   4398 N  N      . LEU A 1 282 ? -6.873  15.322  -40.896 1.00 26.32  ? 281 LEU A N      1 
ATOM   4399 C  CA     . LEU A 1 282 ? -7.456  16.196  -39.898 1.00 25.83  ? 281 LEU A CA     1 
ATOM   4400 C  C      . LEU A 1 282 ? -8.974  16.220  -40.043 1.00 24.23  ? 281 LEU A C      1 
ATOM   4401 O  O      . LEU A 1 282 ? -9.497  15.947  -41.118 1.00 26.36  ? 281 LEU A O      1 
ATOM   4402 C  CB     . LEU A 1 282 ? -6.915  17.629  -40.027 1.00 27.62  ? 281 LEU A CB     1 
ATOM   4403 C  CG     . LEU A 1 282 ? -5.507  17.879  -39.461 1.00 31.30  ? 281 LEU A CG     1 
ATOM   4404 C  CD1    . LEU A 1 282 ? -4.868  19.065  -40.167 1.00 35.78  ? 281 LEU A CD1    1 
ATOM   4405 C  CD2    . LEU A 1 282 ? -5.526  18.104  -37.927 1.00 34.89  ? 281 LEU A CD2    1 
ATOM   4406 H  H      . LEU A 1 282 ? -6.920  15.652  -41.688 1.00 31.61  ? 281 LEU A H      1 
ATOM   4407 H  HA     . LEU A 1 282 ? -7.238  15.865  -39.012 1.00 31.01  ? 281 LEU A HA     1 
ATOM   4408 H  HB2    . LEU A 1 282 ? -6.892  17.861  -40.969 1.00 33.16  ? 281 LEU A HB2    1 
ATOM   4409 H  HB3    . LEU A 1 282 ? -7.522  18.226  -39.563 1.00 33.16  ? 281 LEU A HB3    1 
ATOM   4410 H  HG     . LEU A 1 282 ? -4.958  17.099  -39.638 1.00 37.58  ? 281 LEU A HG     1 
ATOM   4411 H  HD11   . LEU A 1 282 ? -3.982  19.210  -39.800 1.00 42.96  ? 281 LEU A HD11   1 
ATOM   4412 H  HD12   . LEU A 1 282 ? -4.806  18.871  -41.116 1.00 42.96  ? 281 LEU A HD12   1 
ATOM   4413 H  HD13   . LEU A 1 282 ? -5.419  19.851  -40.025 1.00 42.96  ? 281 LEU A HD13   1 
ATOM   4414 H  HD21   . LEU A 1 282 ? -4.619  18.257  -37.620 1.00 41.89  ? 281 LEU A HD21   1 
ATOM   4415 H  HD22   . LEU A 1 282 ? -6.078  18.877  -37.729 1.00 41.89  ? 281 LEU A HD22   1 
ATOM   4416 H  HD23   . LEU A 1 282 ? -5.893  17.316  -37.498 1.00 41.89  ? 281 LEU A HD23   1 
ATOM   4417 N  N      . PRO A 1 283 ? -9.707  16.512  -38.972 1.00 26.88  ? 282 PRO A N      1 
ATOM   4418 C  CA     . PRO A 1 283 ? -11.158 16.623  -39.088 1.00 26.88  ? 282 PRO A CA     1 
ATOM   4419 C  C      . PRO A 1 283 ? -11.551 17.816  -39.940 1.00 29.34  ? 282 PRO A C      1 
ATOM   4420 O  O      . PRO A 1 283 ? -10.819 18.795  -40.090 1.00 34.35  ? 282 PRO A O      1 
ATOM   4421 C  CB     . PRO A 1 283 ? -11.627 16.808  -37.641 1.00 29.17  ? 282 PRO A CB     1 
ATOM   4422 C  CG     . PRO A 1 283 ? -10.434 17.402  -36.938 1.00 28.75  ? 282 PRO A CG     1 
ATOM   4423 C  CD     . PRO A 1 283 ? -9.239  16.799  -37.599 1.00 29.35  ? 282 PRO A CD     1 
ATOM   4424 H  HA     . PRO A 1 283 ? -11.539 15.812  -39.458 1.00 32.28  ? 282 PRO A HA     1 
ATOM   4425 H  HB2    . PRO A 1 283 ? -12.382 17.417  -37.614 1.00 35.02  ? 282 PRO A HB2    1 
ATOM   4426 H  HB3    . PRO A 1 283 ? -11.861 15.948  -37.258 1.00 35.02  ? 282 PRO A HB3    1 
ATOM   4427 H  HG2    . PRO A 1 283 ? -10.437 18.366  -37.050 1.00 34.52  ? 282 PRO A HG2    1 
ATOM   4428 H  HG3    . PRO A 1 283 ? -10.460 17.167  -35.997 1.00 34.52  ? 282 PRO A HG3    1 
ATOM   4429 H  HD2    . PRO A 1 283 ? -8.507  17.435  -37.618 1.00 35.24  ? 282 PRO A HD2    1 
ATOM   4430 H  HD3    . PRO A 1 283 ? -8.984  15.978  -37.151 1.00 35.24  ? 282 PRO A HD3    1 
ATOM   4431 N  N      . VAL A 1 284 ? -12.759 17.714  -40.475 1.00 27.02  ? 283 VAL A N      1 
ATOM   4432 C  CA     . VAL A 1 284 ? -13.335 18.733  -41.347 1.00 29.90  ? 283 VAL A CA     1 
ATOM   4433 C  C      . VAL A 1 284 ? -14.663 19.241  -40.827 1.00 30.42  ? 283 VAL A C      1 
ATOM   4434 O  O      . VAL A 1 284 ? -15.223 20.180  -41.420 1.00 30.46  ? 283 VAL A O      1 
ATOM   4435 C  CB     . VAL A 1 284 ? -13.507 18.205  -42.785 1.00 33.94  ? 283 VAL A CB     1 
ATOM   4436 C  CG1    . VAL A 1 284 ? -12.165 17.794  -43.349 1.00 34.77  ? 283 VAL A CG1    1 
ATOM   4437 C  CG2    . VAL A 1 284 ? -14.487 17.041  -42.828 1.00 34.47  ? 283 VAL A CG2    1 
ATOM   4438 H  H      . VAL A 1 284 ? -13.282 17.044  -40.345 1.00 32.44  ? 283 VAL A H      1 
ATOM   4439 H  HA     . VAL A 1 284 ? -12.726 19.487  -41.383 1.00 35.90  ? 283 VAL A HA     1 
ATOM   4440 H  HB     . VAL A 1 284 ? -13.861 18.916  -43.342 1.00 40.75  ? 283 VAL A HB     1 
ATOM   4441 H  HG11   . VAL A 1 284 ? -12.291 17.464  -44.253 1.00 41.74  ? 283 VAL A HG11   1 
ATOM   4442 H  HG12   . VAL A 1 284 ? -11.576 18.564  -43.356 1.00 41.74  ? 283 VAL A HG12   1 
ATOM   4443 H  HG13   . VAL A 1 284 ? -11.790 17.095  -42.791 1.00 41.74  ? 283 VAL A HG13   1 
ATOM   4444 H  HG21   . VAL A 1 284 ? -14.572 16.734  -43.744 1.00 41.38  ? 283 VAL A HG21   1 
ATOM   4445 H  HG22   . VAL A 1 284 ? -14.150 16.324  -42.268 1.00 41.38  ? 283 VAL A HG22   1 
ATOM   4446 H  HG23   . VAL A 1 284 ? -15.348 17.342  -42.498 1.00 41.38  ? 283 VAL A HG23   1 
ATOM   4447 N  N      . ASP A 1 285 ? -15.212 18.619  -39.783 1.00 30.03  ? 284 ASP A N      1 
ATOM   4448 C  CA     . ASP A 1 285 ? -16.468 19.059  -39.186 1.00 31.19  ? 284 ASP A CA     1 
ATOM   4449 C  C      . ASP A 1 285 ? -16.506 18.602  -37.728 1.00 27.92  ? 284 ASP A C      1 
ATOM   4450 O  O      . ASP A 1 285 ? -15.703 17.769  -37.290 1.00 27.97  ? 284 ASP A O      1 
ATOM   4451 C  CB     . ASP A 1 285 ? -17.707 18.582  -39.966 1.00 33.78  ? 284 ASP A CB     1 
ATOM   4452 C  CG     . ASP A 1 285 ? -17.845 17.070  -40.052 1.00 36.00  ? 284 ASP A CG     1 
ATOM   4453 O  OD1    . ASP A 1 285 ? -16.946 16.325  -39.610 1.00 34.32  ? 284 ASP A OD1    1 
ATOM   4454 O  OD2    . ASP A 1 285 ? -18.889 16.624  -40.610 1.00 37.24  1 284 ASP A OD2    1 
ATOM   4455 H  H      . ASP A 1 285 ? -14.870 17.931  -39.399 1.00 36.06  ? 284 ASP A H      1 
ATOM   4456 H  HA     . ASP A 1 285 ? -16.483 20.029  -39.187 1.00 37.44  ? 284 ASP A HA     1 
ATOM   4457 H  HB2    . ASP A 1 285 ? -18.502 18.926  -39.529 1.00 40.56  ? 284 ASP A HB2    1 
ATOM   4458 H  HB3    . ASP A 1 285 ? -17.657 18.925  -40.872 1.00 40.56  ? 284 ASP A HB3    1 
ATOM   4459 N  N      . PHE A 1 286 ? -17.434 19.189  -36.969 1.00 28.90  ? 285 PHE A N      1 
ATOM   4460 C  CA     . PHE A 1 286 ? -17.361 19.135  -35.511 1.00 31.45  ? 285 PHE A CA     1 
ATOM   4461 C  C      . PHE A 1 286 ? -18.746 19.183  -34.884 1.00 32.18  ? 285 PHE A C      1 
ATOM   4462 O  O      . PHE A 1 286 ? -19.694 19.716  -35.467 1.00 33.38  ? 285 PHE A O      1 
ATOM   4463 C  CB     . PHE A 1 286 ? -16.543 20.314  -34.955 1.00 32.92  ? 285 PHE A CB     1 
ATOM   4464 C  CG     . PHE A 1 286 ? -15.236 20.481  -35.625 1.00 33.72  ? 285 PHE A CG     1 
ATOM   4465 C  CD1    . PHE A 1 286 ? -14.135 19.787  -35.176 1.00 32.63  ? 285 PHE A CD1    1 
ATOM   4466 C  CD2    . PHE A 1 286 ? -15.124 21.283  -36.755 1.00 39.95  ? 285 PHE A CD2    1 
ATOM   4467 C  CE1    . PHE A 1 286 ? -12.920 19.913  -35.831 1.00 32.42  ? 285 PHE A CE1    1 
ATOM   4468 C  CE2    . PHE A 1 286 ? -13.921 21.416  -37.415 1.00 40.87  ? 285 PHE A CE2    1 
ATOM   4469 C  CZ     . PHE A 1 286 ? -12.821 20.722  -36.958 1.00 35.60  ? 285 PHE A CZ     1 
ATOM   4470 H  H      . PHE A 1 286 ? -18.111 19.622  -37.274 1.00 34.69  ? 285 PHE A H      1 
ATOM   4471 H  HA     . PHE A 1 286 ? -16.930 18.309  -35.240 1.00 37.76  ? 285 PHE A HA     1 
ATOM   4472 H  HB2    . PHE A 1 286 ? -17.049 21.133  -35.078 1.00 39.52  ? 285 PHE A HB2    1 
ATOM   4473 H  HB3    . PHE A 1 286 ? -16.379 20.166  -34.011 1.00 39.52  ? 285 PHE A HB3    1 
ATOM   4474 H  HD1    . PHE A 1 286 ? -14.206 19.238  -34.428 1.00 39.18  ? 285 PHE A HD1    1 
ATOM   4475 H  HD2    . PHE A 1 286 ? -15.871 21.741  -37.068 1.00 47.96  ? 285 PHE A HD2    1 
ATOM   4476 H  HE1    . PHE A 1 286 ? -12.174 19.451  -35.521 1.00 38.92  ? 285 PHE A HE1    1 
ATOM   4477 H  HE2    . PHE A 1 286 ? -13.854 21.962  -38.165 1.00 49.06  ? 285 PHE A HE2    1 
ATOM   4478 H  HZ     . PHE A 1 286 ? -12.002 20.816  -37.390 1.00 42.74  ? 285 PHE A HZ     1 
ATOM   4479 N  N      . VAL A 1 287 ? -18.833 18.618  -33.673 1.00 28.79  ? 286 VAL A N      1 
ATOM   4480 C  CA     . VAL A 1 287 ? -19.918 18.880  -32.729 1.00 27.93  ? 286 VAL A CA     1 
ATOM   4481 C  C      . VAL A 1 287 ? -19.415 19.926  -31.740 1.00 26.37  ? 286 VAL A C      1 
ATOM   4482 O  O      . VAL A 1 287 ? -18.339 19.772  -31.160 1.00 26.85  ? 286 VAL A O      1 
ATOM   4483 C  CB     . VAL A 1 287 ? -20.354 17.597  -31.997 1.00 30.03  ? 286 VAL A CB     1 
ATOM   4484 C  CG1    . VAL A 1 287 ? -21.514 17.893  -31.032 1.00 34.00  ? 286 VAL A CG1    1 
ATOM   4485 C  CG2    . VAL A 1 287 ? -20.746 16.502  -33.023 1.00 32.49  ? 286 VAL A CG2    1 
ATOM   4486 H  H      . VAL A 1 287 ? -18.252 18.061  -33.369 1.00 34.57  ? 286 VAL A H      1 
ATOM   4487 H  HA     . VAL A 1 287 ? -20.683 19.242  -33.202 1.00 33.54  ? 286 VAL A HA     1 
ATOM   4488 H  HB     . VAL A 1 287 ? -19.608 17.263  -31.474 1.00 36.05  ? 286 VAL A HB     1 
ATOM   4489 H  HG11   . VAL A 1 287 ? -21.769 17.071  -30.585 1.00 40.82  ? 286 VAL A HG11   1 
ATOM   4490 H  HG12   . VAL A 1 287 ? -21.222 18.548  -30.380 1.00 40.82  ? 286 VAL A HG12   1 
ATOM   4491 H  HG13   . VAL A 1 287 ? -22.264 18.241  -31.539 1.00 40.82  ? 286 VAL A HG13   1 
ATOM   4492 H  HG21   . VAL A 1 287 ? -21.017 15.704  -32.544 1.00 39.01  ? 286 VAL A HG21   1 
ATOM   4493 H  HG22   . VAL A 1 287 ? -21.480 16.828  -33.566 1.00 39.01  ? 286 VAL A HG22   1 
ATOM   4494 H  HG23   . VAL A 1 287 ? -19.979 16.308  -33.584 1.00 39.01  ? 286 VAL A HG23   1 
ATOM   4495 N  N      . THR A 1 288 ? -20.173 20.992  -31.562 1.00 28.52  ? 287 THR A N      1 
ATOM   4496 C  CA     . THR A 1 288 ? -19.747 22.113  -30.742 1.00 31.90  ? 287 THR A CA     1 
ATOM   4497 C  C      . THR A 1 288 ? -20.574 22.174  -29.462 1.00 31.20  ? 287 THR A C      1 
ATOM   4498 O  O      . THR A 1 288 ? -21.645 21.573  -29.356 1.00 32.77  ? 287 THR A O      1 
ATOM   4499 C  CB     . THR A 1 288 ? -19.888 23.438  -31.493 1.00 34.77  ? 287 THR A CB     1 
ATOM   4500 O  OG1    . THR A 1 288 ? -21.252 23.598  -31.887 1.00 32.82  ? 287 THR A OG1    1 
ATOM   4501 C  CG2    . THR A 1 288 ? -19.010 23.456  -32.731 1.00 36.63  ? 287 THR A CG2    1 
ATOM   4502 H  H      . THR A 1 288 ? -20.952 21.093  -31.911 1.00 34.24  ? 287 THR A H      1 
ATOM   4503 H  HA     . THR A 1 288 ? -18.815 21.998  -30.498 1.00 38.30  ? 287 THR A HA     1 
ATOM   4504 H  HB     . THR A 1 288 ? -19.626 24.171  -30.915 1.00 41.74  ? 287 THR A HB     1 
ATOM   4505 H  HG1    . THR A 1 288 ? -21.348 24.322  -32.302 1.00 39.40  ? 287 THR A HG1    1 
ATOM   4506 H  HG21   . THR A 1 288 ? -19.111 24.301  -33.197 1.00 43.97  ? 287 THR A HG21   1 
ATOM   4507 H  HG22   . THR A 1 288 ? -18.080 23.343  -32.480 1.00 43.97  ? 287 THR A HG22   1 
ATOM   4508 H  HG23   . THR A 1 288 ? -19.264 22.735  -33.329 1.00 43.97  ? 287 THR A HG23   1 
ATOM   4509 N  N      . ALA A 1 289 ? -20.067 22.924  -28.491 1.00 30.70  ? 288 ALA A N      1 
ATOM   4510 C  CA     . ALA A 1 289 ? -20.715 23.061  -27.199 1.00 31.71  ? 288 ALA A CA     1 
ATOM   4511 C  C      . ALA A 1 289 ? -20.552 24.492  -26.729 1.00 32.07  ? 288 ALA A C      1 
ATOM   4512 O  O      . ALA A 1 289 ? -19.491 25.085  -26.927 1.00 32.54  ? 288 ALA A O      1 
ATOM   4513 C  CB     . ALA A 1 289 ? -20.105 22.105  -26.169 1.00 32.99  ? 288 ALA A CB     1 
ATOM   4514 H  H      . ALA A 1 289 ? -19.334 23.370  -28.560 1.00 36.86  ? 288 ALA A H      1 
ATOM   4515 H  HA     . ALA A 1 289 ? -21.662 22.865  -27.284 1.00 38.07  ? 288 ALA A HA     1 
ATOM   4516 H  HB1    . ALA A 1 289 ? -20.560 22.223  -25.321 1.00 39.61  ? 288 ALA A HB1    1 
ATOM   4517 H  HB2    . ALA A 1 289 ? -20.215 21.193  -26.480 1.00 39.61  ? 288 ALA A HB2    1 
ATOM   4518 H  HB3    . ALA A 1 289 ? -19.162 22.310  -26.070 1.00 39.61  ? 288 ALA A HB3    1 
ATOM   4519 N  N      . ASP A 1 290 ? -21.594 25.048  -26.105 1.00 33.35  ? 289 ASP A N      1 
ATOM   4520 C  CA     . ASP A 1 290 ? -21.496 26.413  -25.596 1.00 37.71  ? 289 ASP A CA     1 
ATOM   4521 C  C      . ASP A 1 290 ? -20.794 26.497  -24.245 1.00 40.49  ? 289 ASP A C      1 
ATOM   4522 O  O      . ASP A 1 290 ? -20.581 27.604  -23.747 1.00 45.56  ? 289 ASP A O      1 
ATOM   4523 C  CB     . ASP A 1 290 ? -22.887 27.075  -25.517 1.00 41.41  ? 289 ASP A CB     1 
ATOM   4524 C  CG     . ASP A 1 290 ? -23.764 26.520  -24.407 1.00 48.43  ? 289 ASP A CG     1 
ATOM   4525 O  OD1    . ASP A 1 290 ? -23.396 25.516  -23.762 1.00 46.62  ? 289 ASP A OD1    1 
ATOM   4526 O  OD2    . ASP A 1 290 ? -24.843 27.120  -24.179 1.00 52.24  1 289 ASP A OD2    1 
ATOM   4527 H  H      . ASP A 1 290 ? -22.352 24.665  -25.968 1.00 40.03  ? 289 ASP A H      1 
ATOM   4528 H  HA     . ASP A 1 290 ? -20.968 26.931  -26.224 1.00 45.28  ? 289 ASP A HA     1 
ATOM   4529 H  HB2    . ASP A 1 290 ? -22.773 28.025  -25.358 1.00 49.71  ? 289 ASP A HB2    1 
ATOM   4530 H  HB3    . ASP A 1 290 ? -23.348 26.935  -26.358 1.00 49.71  ? 289 ASP A HB3    1 
ATOM   4531 N  N      . LYS A 1 291 ? -20.406 25.371  -23.659 1.00 35.65  ? 290 LYS A N      1 
ATOM   4532 C  CA     . LYS A 1 291 ? -19.616 25.356  -22.441 1.00 36.41  ? 290 LYS A CA     1 
ATOM   4533 C  C      . LYS A 1 291 ? -19.086 23.943  -22.261 1.00 36.07  ? 290 LYS A C      1 
ATOM   4534 O  O      . LYS A 1 291 ? -19.559 22.996  -22.905 1.00 35.79  ? 290 LYS A O      1 
ATOM   4535 C  CB     . LYS A 1 291 ? -20.431 25.807  -21.217 1.00 42.38  ? 290 LYS A CB     1 
ATOM   4536 C  CG     . LYS A 1 291 ? -21.649 24.952  -20.915 1.00 56.82  ? 290 LYS A CG     1 
ATOM   4537 C  CD     . LYS A 1 291 ? -22.457 25.539  -19.760 1.00 76.11  ? 290 LYS A CD     1 
ATOM   4538 C  CE     . LYS A 1 291 ? -23.637 24.656  -19.380 1.00 92.69  ? 290 LYS A CE     1 
ATOM   4539 N  NZ     . LYS A 1 291 ? -24.324 25.143  -18.148 1.00 103.59 1 290 LYS A NZ     1 
ATOM   4540 H  H      . LYS A 1 291 ? -20.594 24.586  -23.956 1.00 42.80  ? 290 LYS A H      1 
ATOM   4541 H  HA     . LYS A 1 291 ? -18.860 25.955  -22.542 1.00 43.71  ? 290 LYS A HA     1 
ATOM   4542 H  HB2    . LYS A 1 291 ? -19.856 25.783  -20.436 1.00 50.87  ? 290 LYS A HB2    1 
ATOM   4543 H  HB3    . LYS A 1 291 ? -20.739 26.714  -21.367 1.00 50.87  ? 290 LYS A HB3    1 
ATOM   4544 H  HG2    . LYS A 1 291 ? -22.219 24.916  -21.699 1.00 68.20  ? 290 LYS A HG2    1 
ATOM   4545 H  HG3    . LYS A 1 291 ? -21.362 24.060  -20.665 1.00 68.20  ? 290 LYS A HG3    1 
ATOM   4546 H  HD2    . LYS A 1 291 ? -21.883 25.627  -18.982 1.00 91.35  ? 290 LYS A HD2    1 
ATOM   4547 H  HD3    . LYS A 1 291 ? -22.801 26.407  -20.021 1.00 91.35  ? 290 LYS A HD3    1 
ATOM   4548 H  HE2    . LYS A 1 291 ? -24.281 24.655  -20.105 1.00 111.25 ? 290 LYS A HE2    1 
ATOM   4549 H  HE3    . LYS A 1 291 ? -23.320 23.754  -19.213 1.00 111.25 ? 290 LYS A HE3    1 
ATOM   4550 H  HZ1    . LYS A 1 291 ? -25.008 24.610  -17.950 1.00 124.33 ? 290 LYS A HZ1    1 
ATOM   4551 H  HZ2    . LYS A 1 291 ? -23.754 25.149  -17.464 1.00 124.33 ? 290 LYS A HZ2    1 
ATOM   4552 H  HZ3    . LYS A 1 291 ? -24.629 25.969  -18.277 1.00 124.33 ? 290 LYS A HZ3    1 
ATOM   4553 N  N      . PHE A 1 292 ? -18.078 23.815  -21.401 1.00 34.73  ? 291 PHE A N      1 
ATOM   4554 C  CA     . PHE A 1 292 ? -17.430 22.525  -21.174 1.00 37.07  ? 291 PHE A CA     1 
ATOM   4555 C  C      . PHE A 1 292 ? -18.240 21.810  -20.100 1.00 37.67  ? 291 PHE A C      1 
ATOM   4556 O  O      . PHE A 1 292 ? -17.909 21.807  -18.911 1.00 39.75  ? 291 PHE A O      1 
ATOM   4557 C  CB     . PHE A 1 292 ? -15.966 22.706  -20.789 1.00 40.62  ? 291 PHE A CB     1 
ATOM   4558 C  CG     . PHE A 1 292 ? -15.186 21.427  -20.765 1.00 37.29  ? 291 PHE A CG     1 
ATOM   4559 C  CD1    . PHE A 1 292 ? -14.883 20.770  -21.933 1.00 31.84  ? 291 PHE A CD1    1 
ATOM   4560 C  CD2    . PHE A 1 292 ? -14.771 20.878  -19.568 1.00 41.05  ? 291 PHE A CD2    1 
ATOM   4561 C  CE1    . PHE A 1 292 ? -14.156 19.585  -21.921 1.00 32.82  ? 291 PHE A CE1    1 
ATOM   4562 C  CE2    . PHE A 1 292 ? -14.054 19.696  -19.548 1.00 39.73  ? 291 PHE A CE2    1 
ATOM   4563 C  CZ     . PHE A 1 292 ? -13.750 19.047  -20.725 1.00 37.99  ? 291 PHE A CZ     1 
ATOM   4564 H  H      . PHE A 1 292 ? -17.751 24.460  -20.935 1.00 41.70  ? 291 PHE A H      1 
ATOM   4565 H  HA     . PHE A 1 292 ? -17.469 21.998  -21.988 1.00 44.50  ? 291 PHE A HA     1 
ATOM   4566 H  HB2    . PHE A 1 292 ? -15.544 23.299  -21.430 1.00 48.76  ? 291 PHE A HB2    1 
ATOM   4567 H  HB3    . PHE A 1 292 ? -15.922 23.096  -19.902 1.00 48.76  ? 291 PHE A HB3    1 
ATOM   4568 H  HD1    . PHE A 1 292 ? -15.156 21.131  -22.745 1.00 38.22  ? 291 PHE A HD1    1 
ATOM   4569 H  HD2    . PHE A 1 292 ? -14.972 21.310  -18.769 1.00 49.28  ? 291 PHE A HD2    1 
ATOM   4570 H  HE1    . PHE A 1 292 ? -13.957 19.152  -22.719 1.00 39.40  ? 291 PHE A HE1    1 
ATOM   4571 H  HE2    . PHE A 1 292 ? -13.777 19.337  -18.736 1.00 47.69  ? 291 PHE A HE2    1 
ATOM   4572 H  HZ     . PHE A 1 292 ? -13.266 18.253  -20.710 1.00 45.61  ? 291 PHE A HZ     1 
ATOM   4573 N  N      . ASP A 1 293 ? -19.351 21.222  -20.542 1.00 33.97  ? 292 ASP A N      1 
ATOM   4574 C  CA     . ASP A 1 293 ? -20.305 20.599  -19.646 1.00 35.38  ? 292 ASP A CA     1 
ATOM   4575 C  C      . ASP A 1 293 ? -21.040 19.493  -20.378 1.00 33.25  ? 292 ASP A C      1 
ATOM   4576 O  O      . ASP A 1 293 ? -21.352 19.621  -21.565 1.00 33.49  ? 292 ASP A O      1 
ATOM   4577 C  CB     . ASP A 1 293 ? -21.311 21.622  -19.114 1.00 40.62  ? 292 ASP A CB     1 
ATOM   4578 C  CG     . ASP A 1 293 ? -22.172 21.067  -18.006 1.00 51.41  ? 292 ASP A CG     1 
ATOM   4579 O  OD1    . ASP A 1 293 ? -23.246 20.511  -18.307 1.00 54.79  ? 292 ASP A OD1    1 
ATOM   4580 O  OD2    . ASP A 1 293 ? -21.766 21.171  -16.830 1.00 57.77  1 292 ASP A OD2    1 
ATOM   4581 H  H      . ASP A 1 293 ? -19.572 21.172  -21.371 1.00 40.78  ? 292 ASP A H      1 
ATOM   4582 H  HA     . ASP A 1 293 ? -19.835 20.210  -18.892 1.00 42.48  ? 292 ASP A HA     1 
ATOM   4583 H  HB2    . ASP A 1 293 ? -20.828 22.387  -18.764 1.00 48.76  ? 292 ASP A HB2    1 
ATOM   4584 H  HB3    . ASP A 1 293 ? -21.893 21.899  -19.838 1.00 48.76  ? 292 ASP A HB3    1 
ATOM   4585 N  N      . GLU A 1 294 ? -21.316 18.417  -19.642 1.00 30.29  ? 293 GLU A N      1 
ATOM   4586 C  CA     . GLU A 1 294 ? -22.075 17.281  -20.155 1.00 34.11  ? 293 GLU A CA     1 
ATOM   4587 C  C      . GLU A 1 294 ? -23.402 17.712  -20.755 1.00 33.52  ? 293 GLU A C      1 
ATOM   4588 O  O      . GLU A 1 294 ? -23.876 17.116  -21.735 1.00 35.40  ? 293 GLU A O      1 
ATOM   4589 C  CB     . GLU A 1 294 ? -22.312 16.295  -19.011 1.00 47.61  ? 293 GLU A CB     1 
ATOM   4590 C  CG     . GLU A 1 294 ? -22.775 14.915  -19.416 1.00 59.61  ? 293 GLU A CG     1 
ATOM   4591 C  CD     . GLU A 1 294 ? -22.907 13.999  -18.206 1.00 68.44  ? 293 GLU A CD     1 
ATOM   4592 O  OE1    . GLU A 1 294 ? -22.912 12.762  -18.387 1.00 71.22  ? 293 GLU A OE1    1 
ATOM   4593 O  OE2    . GLU A 1 294 ? -22.994 14.524  -17.070 1.00 69.49  1 293 GLU A OE2    1 
ATOM   4594 H  H      . GLU A 1 294 ? -21.069 18.321  -18.824 1.00 36.37  ? 293 GLU A H      1 
ATOM   4595 H  HA     . GLU A 1 294 ? -21.558 16.834  -20.843 1.00 40.95  ? 293 GLU A HA     1 
ATOM   4596 H  HB2    . GLU A 1 294 ? -21.482 16.190  -18.521 1.00 57.16  ? 293 GLU A HB2    1 
ATOM   4597 H  HB3    . GLU A 1 294 ? -22.989 16.666  -18.423 1.00 57.16  ? 293 GLU A HB3    1 
ATOM   4598 H  HG2    . GLU A 1 294 ? -23.643 14.981  -19.845 1.00 71.55  ? 293 GLU A HG2    1 
ATOM   4599 H  HG3    . GLU A 1 294 ? -22.128 14.526  -20.024 1.00 71.55  ? 293 GLU A HG3    1 
ATOM   4600 N  N      . ASN A 1 295 ? -24.030 18.730  -20.168 1.00 31.58  ? 294 ASN A N      1 
ATOM   4601 C  CA     . ASN A 1 295 ? -25.360 19.165  -20.574 1.00 36.08  ? 294 ASN A CA     1 
ATOM   4602 C  C      . ASN A 1 295 ? -25.332 20.473  -21.348 1.00 35.08  ? 294 ASN A C      1 
ATOM   4603 O  O      . ASN A 1 295 ? -26.344 21.172  -21.412 1.00 35.79  ? 294 ASN A O      1 
ATOM   4604 C  CB     . ASN A 1 295 ? -26.262 19.284  -19.353 1.00 46.39  ? 294 ASN A CB     1 
ATOM   4605 C  CG     . ASN A 1 295 ? -26.392 17.973  -18.610 1.00 51.58  ? 294 ASN A CG     1 
ATOM   4606 O  OD1    . ASN A 1 295 ? -26.623 16.925  -19.221 1.00 47.92  ? 294 ASN A OD1    1 
ATOM   4607 N  ND2    . ASN A 1 295 ? -26.219 18.015  -17.293 1.00 55.91  ? 294 ASN A ND2    1 
ATOM   4608 H  H      . ASN A 1 295 ? -23.699 19.191  -19.521 1.00 37.91  ? 294 ASN A H      1 
ATOM   4609 H  HA     . ASN A 1 295 ? -25.741 18.489  -21.156 1.00 43.31  ? 294 ASN A HA     1 
ATOM   4610 H  HB2    . ASN A 1 295 ? -25.888 19.940  -18.744 1.00 55.68  ? 294 ASN A HB2    1 
ATOM   4611 H  HB3    . ASN A 1 295 ? -27.148 19.560  -19.637 1.00 55.68  ? 294 ASN A HB3    1 
ATOM   4612 H  HD21   . ASN A 1 295 ? -26.283 17.295  -16.827 1.00 67.11  ? 294 ASN A HD21   1 
ATOM   4613 H  HD22   . ASN A 1 295 ? -26.042 18.763  -16.906 1.00 67.11  ? 294 ASN A HD22   1 
ATOM   4614 N  N      . ALA A 1 296 ? -24.201 20.798  -21.958 1.00 37.16  ? 295 ALA A N      1 
ATOM   4615 C  CA     . ALA A 1 296 ? -24.086 22.009  -22.756 1.00 41.00  ? 295 ALA A CA     1 
ATOM   4616 C  C      . ALA A 1 296 ? -25.065 21.992  -23.927 1.00 41.00  ? 295 ALA A C      1 
ATOM   4617 O  O      . ALA A 1 296 ? -25.449 20.933  -24.426 1.00 41.10  ? 295 ALA A O      1 
ATOM   4618 C  CB     . ALA A 1 296 ? -22.658 22.139  -23.288 1.00 40.09  ? 295 ALA A CB     1 
ATOM   4619 H  H      . ALA A 1 296 ? -23.480 20.331  -21.925 1.00 44.61  ? 295 ALA A H      1 
ATOM   4620 H  HA     . ALA A 1 296 ? -24.281 22.781  -22.203 1.00 49.22  ? 295 ALA A HA     1 
ATOM   4621 H  HB1    . ALA A 1 296 ? -22.592 22.948  -23.819 1.00 48.12  ? 295 ALA A HB1    1 
ATOM   4622 H  HB2    . ALA A 1 296 ? -22.045 22.184  -22.538 1.00 48.12  ? 295 ALA A HB2    1 
ATOM   4623 H  HB3    . ALA A 1 296 ? -22.455 21.366  -23.837 1.00 48.12  ? 295 ALA A HB3    1 
ATOM   4624 N  N      . LYS A 1 297 ? -25.466 23.186  -24.369 1.00 40.43  ? 296 LYS A N      1 
ATOM   4625 C  CA     . LYS A 1 297 ? -26.095 23.312  -25.676 1.00 43.69  ? 296 LYS A CA     1 
ATOM   4626 C  C      . LYS A 1 297 ? -25.073 22.938  -26.738 1.00 39.78  ? 296 LYS A C      1 
ATOM   4627 O  O      . LYS A 1 297 ? -23.894 23.285  -26.626 1.00 39.00  ? 296 LYS A O      1 
ATOM   4628 C  CB     . LYS A 1 297 ? -26.606 24.739  -25.904 1.00 49.75  ? 296 LYS A CB     1 
ATOM   4629 C  CG     . LYS A 1 297 ? -27.597 25.191  -24.841 1.00 59.15  ? 296 LYS A CG     1 
ATOM   4630 C  CD     . LYS A 1 297 ? -28.128 26.597  -25.059 1.00 67.75  ? 296 LYS A CD     1 
ATOM   4631 C  CE     . LYS A 1 297 ? -29.094 26.967  -23.932 1.00 73.36  ? 296 LYS A CE     1 
ATOM   4632 N  NZ     . LYS A 1 297 ? -29.552 28.382  -24.001 1.00 76.65  1 296 LYS A NZ     1 
ATOM   4633 H  H      . LYS A 1 297 ? -25.386 23.924  -23.936 1.00 48.54  ? 296 LYS A H      1 
ATOM   4634 H  HA     . LYS A 1 297 ? -26.845 22.700  -25.738 1.00 52.45  ? 296 LYS A HA     1 
ATOM   4635 H  HB2    . LYS A 1 297 ? -25.852 25.350  -25.890 1.00 59.72  ? 296 LYS A HB2    1 
ATOM   4636 H  HB3    . LYS A 1 297 ? -27.050 24.782  -26.765 1.00 59.72  ? 296 LYS A HB3    1 
ATOM   4637 H  HG2    . LYS A 1 297 ? -28.354 24.584  -24.841 1.00 70.99  ? 296 LYS A HG2    1 
ATOM   4638 H  HG3    . LYS A 1 297 ? -27.159 25.170  -23.976 1.00 70.99  ? 296 LYS A HG3    1 
ATOM   4639 H  HD2    . LYS A 1 297 ? -27.392 27.228  -25.055 1.00 81.32  ? 296 LYS A HD2    1 
ATOM   4640 H  HD3    . LYS A 1 297 ? -28.607 26.637  -25.902 1.00 81.32  ? 296 LYS A HD3    1 
ATOM   4641 H  HE2    . LYS A 1 297 ? -29.876 26.396  -23.986 1.00 88.05  ? 296 LYS A HE2    1 
ATOM   4642 H  HE3    . LYS A 1 297 ? -28.648 26.838  -23.080 1.00 88.05  ? 296 LYS A HE3    1 
ATOM   4643 H  HZ1    . LYS A 1 297 ? -30.110 28.554  -23.329 1.00 92.00  ? 296 LYS A HZ1    1 
ATOM   4644 H  HZ2    . LYS A 1 297 ? -28.853 28.930  -23.944 1.00 92.00  ? 296 LYS A HZ2    1 
ATOM   4645 H  HZ3    . LYS A 1 297 ? -29.973 28.528  -24.771 1.00 92.00  ? 296 LYS A HZ3    1 
ATOM   4646 N  N      . THR A 1 298 ? -25.509 22.182  -27.737 1.00 36.51  ? 297 THR A N      1 
ATOM   4647 C  CA     . THR A 1 298 ? -24.600 21.703  -28.767 1.00 38.18  ? 297 THR A CA     1 
ATOM   4648 C  C      . THR A 1 298 ? -24.943 22.326  -30.109 1.00 38.21  ? 297 THR A C      1 
ATOM   4649 O  O      . THR A 1 298 ? -26.016 22.909  -30.295 1.00 40.69  ? 297 THR A O      1 
ATOM   4650 C  CB     . THR A 1 298 ? -24.624 20.173  -28.890 1.00 42.97  ? 297 THR A CB     1 
ATOM   4651 O  OG1    . THR A 1 298 ? -25.882 19.747  -29.418 1.00 48.19  ? 297 THR A OG1    1 
ATOM   4652 C  CG2    . THR A 1 298 ? -24.389 19.521  -27.514 1.00 44.30  ? 297 THR A CG2    1 
ATOM   4653 H  H      . THR A 1 298 ? -26.325 21.932  -27.842 1.00 43.83  ? 297 THR A H      1 
ATOM   4654 H  HA     . THR A 1 298 ? -23.696 21.969  -28.537 1.00 45.83  ? 297 THR A HA     1 
ATOM   4655 H  HB     . THR A 1 298 ? -23.914 19.888  -29.486 1.00 51.58  ? 297 THR A HB     1 
ATOM   4656 H  HG1    . THR A 1 298 ? -25.896 18.910  -29.485 1.00 57.84  ? 297 THR A HG1    1 
ATOM   4657 H  HG21   . THR A 1 298 ? -24.405 18.555  -27.598 1.00 53.18  ? 297 THR A HG21   1 
ATOM   4658 H  HG22   . THR A 1 298 ? -23.526 19.792  -27.162 1.00 53.18  ? 297 THR A HG22   1 
ATOM   4659 H  HG23   . THR A 1 298 ? -25.083 19.796  -26.895 1.00 53.18  ? 297 THR A HG23   1 
ATOM   4660 N  N      . GLY A 1 299 ? -23.997 22.210  -31.034 1.00 36.53  ? 298 GLY A N      1 
ATOM   4661 C  CA     . GLY A 1 299 ? -24.151 22.710  -32.381 1.00 38.68  ? 298 GLY A CA     1 
ATOM   4662 C  C      . GLY A 1 299 ? -23.309 21.923  -33.363 1.00 34.62  ? 298 GLY A C      1 
ATOM   4663 O  O      . GLY A 1 299 ? -22.713 20.894  -33.023 1.00 32.75  ? 298 GLY A O      1 
ATOM   4664 H  H      . GLY A 1 299 ? -23.237 21.833  -30.894 1.00 43.86  ? 298 GLY A H      1 
ATOM   4665 H  HA2    . GLY A 1 299 ? -25.081 22.646  -32.648 1.00 46.44  ? 298 GLY A HA2    1 
ATOM   4666 H  HA3    . GLY A 1 299 ? -23.880 23.641  -32.416 1.00 46.44  ? 298 GLY A HA3    1 
ATOM   4667 N  N      . GLN A 1 300 ? -23.256 22.403  -34.593 1.00 34.84  ? 299 GLN A N      1 
ATOM   4668 C  CA     . GLN A 1 300 ? -22.437 21.809  -35.633 1.00 37.14  ? 299 GLN A CA     1 
ATOM   4669 C  C      . GLN A 1 300 ? -21.595 22.903  -36.265 1.00 33.25  ? 299 GLN A C      1 
ATOM   4670 O  O      . GLN A 1 300 ? -21.994 24.070  -36.318 1.00 34.51  ? 299 GLN A O      1 
ATOM   4671 C  CB     . GLN A 1 300 ? -23.292 21.115  -36.717 1.00 48.08  ? 299 GLN A CB     1 
ATOM   4672 C  CG     . GLN A 1 300 ? -24.078 19.896  -36.240 1.00 63.61  ? 299 GLN A CG     1 
ATOM   4673 C  CD     . GLN A 1 300 ? -25.464 20.251  -35.738 1.00 84.14  ? 299 GLN A CD     1 
ATOM   4674 O  OE1    . GLN A 1 300 ? -26.067 21.226  -36.186 1.00 92.96  ? 299 GLN A OE1    1 
ATOM   4675 N  NE2    . GLN A 1 300 ? -25.976 19.460  -34.802 1.00 90.13  ? 299 GLN A NE2    1 
ATOM   4676 H  H      . GLN A 1 300 ? -23.697 23.093  -34.857 1.00 41.83  ? 299 GLN A H      1 
ATOM   4677 H  HA     . GLN A 1 300 ? -21.843 21.150  -35.241 1.00 44.59  ? 299 GLN A HA     1 
ATOM   4678 H  HB2    . GLN A 1 300 ? -23.931 21.758  -37.064 1.00 57.71  ? 299 GLN A HB2    1 
ATOM   4679 H  HB3    . GLN A 1 300 ? -22.705 20.823  -37.432 1.00 57.71  ? 299 GLN A HB3    1 
ATOM   4680 H  HG2    . GLN A 1 300 ? -24.177 19.275  -36.979 1.00 76.36  ? 299 GLN A HG2    1 
ATOM   4681 H  HG3    . GLN A 1 300 ? -23.595 19.473  -35.513 1.00 76.36  ? 299 GLN A HG3    1 
ATOM   4682 H  HE21   . GLN A 1 300 ? -25.524 18.788  -34.513 1.00 108.17 ? 299 GLN A HE21   1 
ATOM   4683 H  HE22   . GLN A 1 300 ? -26.759 19.620  -34.486 1.00 108.17 ? 299 GLN A HE22   1 
ATOM   4684 N  N      . ALA A 1 301 ? -20.422 22.511  -36.740 1.00 31.72  ? 300 ALA A N      1 
ATOM   4685 C  CA     . ALA A 1 301 ? -19.526 23.436  -37.408 1.00 33.92  ? 300 ALA A CA     1 
ATOM   4686 C  C      . ALA A 1 301 ? -18.667 22.666  -38.396 1.00 32.21  ? 300 ALA A C      1 
ATOM   4687 O  O      . ALA A 1 301 ? -18.445 21.460  -38.253 1.00 34.22  ? 300 ALA A O      1 
ATOM   4688 C  CB     . ALA A 1 301 ? -18.639 24.185  -36.407 1.00 36.08  ? 300 ALA A CB     1 
ATOM   4689 H  H      . ALA A 1 301 ? -20.121 21.707  -36.688 1.00 38.09  ? 300 ALA A H      1 
ATOM   4690 H  HA     . ALA A 1 301 ? -20.048 24.089  -37.902 1.00 40.72  ? 300 ALA A HA     1 
ATOM   4691 H  HB1    . ALA A 1 301 ? -18.057 24.790  -36.892 1.00 43.32  ? 300 ALA A HB1    1 
ATOM   4692 H  HB2    . ALA A 1 301 ? -19.204 24.685  -35.798 1.00 43.32  ? 300 ALA A HB2    1 
ATOM   4693 H  HB3    . ALA A 1 301 ? -18.108 23.541  -35.912 1.00 43.32  ? 300 ALA A HB3    1 
ATOM   4694 N  N      . THR A 1 302 ? -18.178 23.384  -39.405 1.00 34.19  ? 301 THR A N      1 
ATOM   4695 C  CA     . THR A 1 302 ? -17.172 22.860  -40.312 1.00 35.48  ? 301 THR A CA     1 
ATOM   4696 C  C      . THR A 1 302 ? -15.944 23.758  -40.259 1.00 35.34  ? 301 THR A C      1 
ATOM   4697 O  O      . THR A 1 302 ? -15.963 24.836  -39.661 1.00 34.08  ? 301 THR A O      1 
ATOM   4698 C  CB     . THR A 1 302 ? -17.707 22.763  -41.745 1.00 38.62  ? 301 THR A CB     1 
ATOM   4699 O  OG1    . THR A 1 302 ? -18.024 24.068  -42.228 1.00 36.25  ? 301 THR A OG1    1 
ATOM   4700 C  CG2    . THR A 1 302 ? -18.960 21.907  -41.772 1.00 43.90  ? 301 THR A CG2    1 
ATOM   4701 H  H      . THR A 1 302 ? -18.420 24.190  -39.584 1.00 41.05  ? 301 THR A H      1 
ATOM   4702 H  HA     . THR A 1 302 ? -16.912 21.972  -40.023 1.00 42.59  ? 301 THR A HA     1 
ATOM   4703 H  HB     . THR A 1 302 ? -17.039 22.355  -42.318 1.00 46.36  ? 301 THR A HB     1 
ATOM   4704 H  HG1    . THR A 1 302 ? -18.318 24.020  -43.013 1.00 43.52  ? 301 THR A HG1    1 
ATOM   4705 H  HG21   . THR A 1 302 ? -19.299 21.845  -42.678 1.00 52.70  ? 301 THR A HG21   1 
ATOM   4706 H  HG22   . THR A 1 302 ? -18.759 21.015  -41.448 1.00 52.70  ? 301 THR A HG22   1 
ATOM   4707 H  HG23   . THR A 1 302 ? -19.642 22.301  -41.206 1.00 52.70  ? 301 THR A HG23   1 
ATOM   4708 N  N      . VAL A 1 303 ? -14.872 23.316  -40.924 1.00 34.71  ? 302 VAL A N      1 
ATOM   4709 C  CA     . VAL A 1 303 ? -13.673 24.145  -40.998 1.00 37.90  ? 302 VAL A CA     1 
ATOM   4710 C  C      . VAL A 1 303 ? -13.977 25.444  -41.713 1.00 39.84  ? 302 VAL A C      1 
ATOM   4711 O  O      . VAL A 1 303 ? -13.471 26.506  -41.337 1.00 42.83  ? 302 VAL A O      1 
ATOM   4712 C  CB     . VAL A 1 303 ? -12.524 23.380  -41.683 1.00 44.79  ? 302 VAL A CB     1 
ATOM   4713 C  CG1    . VAL A 1 303 ? -11.317 24.291  -41.887 1.00 50.67  ? 302 VAL A CG1    1 
ATOM   4714 C  CG2    . VAL A 1 303 ? -12.121 22.198  -40.849 1.00 42.38  ? 302 VAL A CG2    1 
ATOM   4715 H  H      . VAL A 1 303 ? -14.816 22.560  -41.329 1.00 41.67  ? 302 VAL A H      1 
ATOM   4716 H  HA     . VAL A 1 303 ? -13.387 24.363  -40.097 1.00 45.50  ? 302 VAL A HA     1 
ATOM   4717 H  HB     . VAL A 1 303 ? -12.819 23.060  -42.550 1.00 53.77  ? 302 VAL A HB     1 
ATOM   4718 H  HG11   . VAL A 1 303 ? -10.611 23.786  -42.319 1.00 60.82  ? 302 VAL A HG11   1 
ATOM   4719 H  HG12   . VAL A 1 303 ? -11.578 25.040  -42.445 1.00 60.82  ? 302 VAL A HG12   1 
ATOM   4720 H  HG13   . VAL A 1 303 ? -11.015 24.611  -41.022 1.00 60.82  ? 302 VAL A HG13   1 
ATOM   4721 H  HG21   . VAL A 1 303 ? -11.398 21.729  -41.295 1.00 50.87  ? 302 VAL A HG21   1 
ATOM   4722 H  HG22   . VAL A 1 303 ? -11.825 22.511  -39.980 1.00 50.87  ? 302 VAL A HG22   1 
ATOM   4723 H  HG23   . VAL A 1 303 ? -12.884 21.608  -40.747 1.00 50.87  ? 302 VAL A HG23   1 
ATOM   4724 N  N      . ALA A 1 304 ? -14.794 25.375  -42.773 1.00 43.24  ? 303 ALA A N      1 
ATOM   4725 C  CA     . ALA A 1 304 ? -15.176 26.568  -43.529 1.00 45.06  ? 303 ALA A CA     1 
ATOM   4726 C  C      . ALA A 1 304 ? -16.005 27.539  -42.693 1.00 44.56  ? 303 ALA A C      1 
ATOM   4727 O  O      . ALA A 1 304 ? -15.855 28.761  -42.815 1.00 44.42  ? 303 ALA A O      1 
ATOM   4728 C  CB     . ALA A 1 304 ? -15.965 26.160  -44.769 1.00 47.61  ? 303 ALA A CB     1 
ATOM   4729 H  H      . ALA A 1 304 ? -15.140 24.646  -43.072 1.00 51.91  ? 303 ALA A H      1 
ATOM   4730 H  HA     . ALA A 1 304 ? -14.374 27.030  -43.820 1.00 54.09  ? 303 ALA A HA     1 
ATOM   4731 H  HB1    . ALA A 1 304 ? -16.212 26.958  -45.262 1.00 57.15  ? 303 ALA A HB1    1 
ATOM   4732 H  HB2    . ALA A 1 304 ? -15.410 25.588  -45.321 1.00 57.15  ? 303 ALA A HB2    1 
ATOM   4733 H  HB3    . ALA A 1 304 ? -16.762 25.681  -44.491 1.00 57.15  ? 303 ALA A HB3    1 
ATOM   4734 N  N      . SER A 1 305 ? -16.923 27.021  -41.877 1.00 39.06  ? 304 SER A N      1 
ATOM   4735 C  CA     . SER A 1 305 ? -17.784 27.889  -41.079 1.00 39.03  ? 304 SER A CA     1 
ATOM   4736 C  C      . SER A 1 305 ? -17.075 28.438  -39.850 1.00 40.08  ? 304 SER A C      1 
ATOM   4737 O  O      . SER A 1 305 ? -17.426 29.518  -39.365 1.00 43.79  ? 304 SER A O      1 
ATOM   4738 C  CB     . SER A 1 305 ? -19.031 27.130  -40.612 1.00 39.39  ? 304 SER A CB     1 
ATOM   4739 O  OG     . SER A 1 305 ? -18.751 26.354  -39.450 1.00 36.81  ? 304 SER A OG     1 
ATOM   4740 H  H      . SER A 1 305 ? -17.065 26.179  -41.769 1.00 46.89  ? 304 SER A H      1 
ATOM   4741 H  HA     . SER A 1 305 ? -18.071 28.639  -41.623 1.00 46.85  ? 304 SER A HA     1 
ATOM   4742 H  HB2    . SER A 1 305 ? -19.729 27.770  -40.404 1.00 47.28  ? 304 SER A HB2    1 
ATOM   4743 H  HB3    . SER A 1 305 ? -19.324 26.539  -41.323 1.00 47.28  ? 304 SER A HB3    1 
ATOM   4744 H  HG     . SER A 1 305 ? -19.442 25.944  -39.205 1.00 44.19  ? 304 SER A HG     1 
ATOM   4745 N  N      . GLY A 1 306 ? -16.108 27.708  -39.319 1.00 37.29  ? 305 GLY A N      1 
ATOM   4746 C  CA     . GLY A 1 306 ? -15.544 28.058  -38.037 1.00 42.78  ? 305 GLY A CA     1 
ATOM   4747 C  C      . GLY A 1 306 ? -16.447 27.702  -36.871 1.00 39.56  ? 305 GLY A C      1 
ATOM   4748 O  O      . GLY A 1 306 ? -17.637 27.424  -37.041 1.00 35.35  ? 305 GLY A O      1 
ATOM   4749 H  H      . GLY A 1 306 ? -15.765 27.008  -39.682 1.00 44.77  ? 305 GLY A H      1 
ATOM   4750 H  HA2    . GLY A 1 306 ? -14.699 27.594  -37.921 1.00 51.35  ? 305 GLY A HA2    1 
ATOM   4751 H  HA3    . GLY A 1 306 ? -15.374 29.012  -38.010 1.00 51.35  ? 305 GLY A HA3    1 
ATOM   4752 N  N      . ILE A 1 307 ? -15.873 27.707  -35.677 1.00 37.31  ? 306 ILE A N      1 
ATOM   4753 C  CA     . ILE A 1 307 ? -16.598 27.478  -34.428 1.00 34.03  ? 306 ILE A CA     1 
ATOM   4754 C  C      . ILE A 1 307 ? -16.959 28.855  -33.889 1.00 36.73  ? 306 ILE A C      1 
ATOM   4755 O  O      . ILE A 1 307 ? -16.080 29.722  -33.827 1.00 45.22  ? 306 ILE A O      1 
ATOM   4756 C  CB     . ILE A 1 307 ? -15.741 26.656  -33.453 1.00 33.25  ? 306 ILE A CB     1 
ATOM   4757 C  CG1    . ILE A 1 307 ? -15.497 25.278  -34.076 1.00 33.66  ? 306 ILE A CG1    1 
ATOM   4758 C  CG2    . ILE A 1 307 ? -16.399 26.528  -32.086 1.00 34.71  ? 306 ILE A CG2    1 
ATOM   4759 C  CD1    . ILE A 1 307 ? -14.537 24.425  -33.324 1.00 35.01  ? 306 ILE A CD1    1 
ATOM   4760 H  H      . ILE A 1 307 ? -15.032 27.845  -35.558 1.00 44.79  ? 306 ILE A H      1 
ATOM   4761 H  HA     . ILE A 1 307 ? -17.417 26.990  -34.610 1.00 40.86  ? 306 ILE A HA     1 
ATOM   4762 H  HB     . ILE A 1 307 ? -14.886 27.101  -33.343 1.00 39.92  ? 306 ILE A HB     1 
ATOM   4763 H  HG12   . ILE A 1 307 ? -16.341 24.803  -34.120 1.00 40.41  ? 306 ILE A HG12   1 
ATOM   4764 H  HG13   . ILE A 1 307 ? -15.144 25.401  -34.971 1.00 40.41  ? 306 ILE A HG13   1 
ATOM   4765 H  HG21   . ILE A 1 307 ? -15.824 26.004  -31.507 1.00 41.67  ? 306 ILE A HG21   1 
ATOM   4766 H  HG22   . ILE A 1 307 ? -16.526 27.414  -31.713 1.00 41.67  ? 306 ILE A HG22   1 
ATOM   4767 H  HG23   . ILE A 1 307 ? -17.257 26.086  -32.189 1.00 41.67  ? 306 ILE A HG23   1 
ATOM   4768 H  HD11   . ILE A 1 307 ? -14.441 23.577  -33.785 1.00 42.03  ? 306 ILE A HD11   1 
ATOM   4769 H  HD12   . ILE A 1 307 ? -13.680 24.877  -33.281 1.00 42.03  ? 306 ILE A HD12   1 
ATOM   4770 H  HD13   . ILE A 1 307 ? -14.879 24.278  -32.429 1.00 42.03  ? 306 ILE A HD13   1 
ATOM   4771 N  N      . PRO A 1 308 ? -18.217 29.123  -33.527 1.00 38.05  ? 307 PRO A N      1 
ATOM   4772 C  CA     . PRO A 1 308 ? -18.575 30.468  -33.055 1.00 45.93  ? 307 PRO A CA     1 
ATOM   4773 C  C      . PRO A 1 308 ? -17.826 30.854  -31.785 1.00 46.93  ? 307 PRO A C      1 
ATOM   4774 O  O      . PRO A 1 308 ? -17.394 30.011  -30.995 1.00 38.88  ? 307 PRO A O      1 
ATOM   4775 C  CB     . PRO A 1 308 ? -20.083 30.369  -32.777 1.00 49.56  ? 307 PRO A CB     1 
ATOM   4776 C  CG     . PRO A 1 308 ? -20.537 29.103  -33.394 1.00 46.34  ? 307 PRO A CG     1 
ATOM   4777 C  CD     . PRO A 1 308 ? -19.353 28.192  -33.422 1.00 38.43  ? 307 PRO A CD     1 
ATOM   4778 H  HA     . PRO A 1 308 ? -18.413 31.129  -33.746 1.00 55.14  ? 307 PRO A HA     1 
ATOM   4779 H  HB2    . PRO A 1 308 ? -20.235 30.354  -31.819 1.00 59.49  ? 307 PRO A HB2    1 
ATOM   4780 H  HB3    . PRO A 1 308 ? -20.536 31.126  -33.181 1.00 59.49  ? 307 PRO A HB3    1 
ATOM   4781 H  HG2    . PRO A 1 308 ? -21.247 28.719  -32.857 1.00 55.62  ? 307 PRO A HG2    1 
ATOM   4782 H  HG3    . PRO A 1 308 ? -20.851 29.278  -34.295 1.00 55.62  ? 307 PRO A HG3    1 
ATOM   4783 H  HD2    . PRO A 1 308 ? -19.299 27.681  -32.599 1.00 46.13  ? 307 PRO A HD2    1 
ATOM   4784 H  HD3    . PRO A 1 308 ? -19.390 27.612  -34.200 1.00 46.13  ? 307 PRO A HD3    1 
ATOM   4785 N  N      . ALA A 1 309 ? -17.705 32.162  -31.582 1.00 52.79  ? 308 ALA A N      1 
ATOM   4786 C  CA     . ALA A 1 309 ? -17.013 32.674  -30.408 1.00 53.18  ? 308 ALA A CA     1 
ATOM   4787 C  C      . ALA A 1 309 ? -17.672 32.167  -29.136 1.00 50.91  ? 308 ALA A C      1 
ATOM   4788 O  O      . ALA A 1 309 ? -18.900 32.169  -29.005 1.00 49.07  ? 308 ALA A O      1 
ATOM   4789 C  CB     . ALA A 1 309 ? -17.012 34.202  -30.418 1.00 56.21  ? 308 ALA A CB     1 
ATOM   4790 H  H      . ALA A 1 309 ? -18.012 32.770  -32.107 1.00 63.37  ? 308 ALA A H      1 
ATOM   4791 H  HA     . ALA A 1 309 ? -16.093 32.368  -30.418 1.00 63.83  ? 308 ALA A HA     1 
ATOM   4792 H  HB1    . ALA A 1 309 ? -16.547 34.522  -29.629 1.00 67.47  ? 308 ALA A HB1    1 
ATOM   4793 H  HB2    . ALA A 1 309 ? -16.559 34.511  -31.218 1.00 67.47  ? 308 ALA A HB2    1 
ATOM   4794 H  HB3    . ALA A 1 309 ? -17.929 34.518  -30.414 1.00 67.47  ? 308 ALA A HB3    1 
ATOM   4795 N  N      . GLY A 1 310 ? -16.846 31.743  -28.186 1.00 49.65  ? 309 GLY A N      1 
ATOM   4796 C  CA     . GLY A 1 310 ? -17.349 31.227  -26.936 1.00 50.33  ? 309 GLY A CA     1 
ATOM   4797 C  C      . GLY A 1 310 ? -17.815 29.790  -26.983 1.00 46.50  ? 309 GLY A C      1 
ATOM   4798 O  O      . GLY A 1 310 ? -18.215 29.259  -25.940 1.00 46.46  ? 309 GLY A O      1 
ATOM   4799 H  H      . GLY A 1 310 ? -15.988 31.748  -28.248 1.00 59.60  ? 309 GLY A H      1 
ATOM   4800 H  HA2    . GLY A 1 310 ? -16.652 31.293  -26.265 1.00 60.41  ? 309 GLY A HA2    1 
ATOM   4801 H  HA3    . GLY A 1 310 ? -18.096 31.774  -26.648 1.00 60.41  ? 309 GLY A HA3    1 
ATOM   4802 N  N      . TRP A 1 311 ? -17.790 29.148  -28.150 1.00 39.33  ? 310 TRP A N      1 
ATOM   4803 C  CA     . TRP A 1 311 ? -18.120 27.739  -28.273 1.00 33.55  ? 310 TRP A CA     1 
ATOM   4804 C  C      . TRP A 1 311 ? -16.846 26.944  -28.497 1.00 29.74  ? 310 TRP A C      1 
ATOM   4805 O  O      . TRP A 1 311 ? -15.801 27.490  -28.856 1.00 31.95  ? 310 TRP A O      1 
ATOM   4806 C  CB     . TRP A 1 311 ? -19.092 27.488  -29.426 1.00 36.08  ? 310 TRP A CB     1 
ATOM   4807 C  CG     . TRP A 1 311 ? -20.468 28.016  -29.195 1.00 40.14  ? 310 TRP A CG     1 
ATOM   4808 C  CD1    . TRP A 1 311 ? -20.822 29.310  -28.942 1.00 43.03  ? 310 TRP A CD1    1 
ATOM   4809 C  CD2    . TRP A 1 311 ? -21.687 27.260  -29.219 1.00 40.56  ? 310 TRP A CD2    1 
ATOM   4810 N  NE1    . TRP A 1 311 ? -22.185 29.405  -28.804 1.00 43.65  ? 310 TRP A NE1    1 
ATOM   4811 C  CE2    . TRP A 1 311 ? -22.741 28.163  -28.974 1.00 42.48  ? 310 TRP A CE2    1 
ATOM   4812 C  CE3    . TRP A 1 311 ? -21.988 25.908  -29.431 1.00 41.99  ? 310 TRP A CE3    1 
ATOM   4813 C  CZ2    . TRP A 1 311 ? -24.074 27.760  -28.930 1.00 44.82  ? 310 TRP A CZ2    1 
ATOM   4814 C  CZ3    . TRP A 1 311 ? -23.311 25.505  -29.383 1.00 49.33  ? 310 TRP A CZ3    1 
ATOM   4815 C  CH2    . TRP A 1 311 ? -24.341 26.431  -29.135 1.00 52.62  ? 310 TRP A CH2    1 
ATOM   4816 H  H      . TRP A 1 311 ? -17.580 29.518  -28.897 1.00 47.21  ? 310 TRP A H      1 
ATOM   4817 H  HA     . TRP A 1 311 ? -18.534 27.431  -27.451 1.00 40.27  ? 310 TRP A HA     1 
ATOM   4818 H  HB2    . TRP A 1 311 ? -18.743 27.914  -30.224 1.00 43.32  ? 310 TRP A HB2    1 
ATOM   4819 H  HB3    . TRP A 1 311 ? -19.163 26.532  -29.570 1.00 43.32  ? 310 TRP A HB3    1 
ATOM   4820 H  HD1    . TRP A 1 311 ? -20.228 30.022  -28.874 1.00 51.66  ? 310 TRP A HD1    1 
ATOM   4821 H  HE1    . TRP A 1 311 ? -22.620 30.128  -28.642 1.00 52.40  ? 310 TRP A HE1    1 
ATOM   4822 H  HE3    . TRP A 1 311 ? -21.311 25.293  -29.600 1.00 50.41  ? 310 TRP A HE3    1 
ATOM   4823 H  HZ2    . TRP A 1 311 ? -24.757 28.368  -28.759 1.00 53.80  ? 310 TRP A HZ2    1 
ATOM   4824 H  HZ3    . TRP A 1 311 ? -23.522 24.610  -29.522 1.00 59.21  ? 310 TRP A HZ3    1 
ATOM   4825 H  HH2    . TRP A 1 311 ? -25.222 26.134  -29.106 1.00 63.17  ? 310 TRP A HH2    1 
ATOM   4826 N  N      . MET A 1 312 ? -16.928 25.644  -28.255 1.00 30.44  ? 311 MET A N      1 
ATOM   4827 C  CA     . MET A 1 312 ? -15.763 24.785  -28.383 1.00 28.90  ? 311 MET A CA     1 
ATOM   4828 C  C      . MET A 1 312 ? -16.137 23.501  -29.107 1.00 27.13  ? 311 MET A C      1 
ATOM   4829 O  O      . MET A 1 312 ? -17.244 22.979  -28.950 1.00 28.03  ? 311 MET A O      1 
ATOM   4830 C  CB     . MET A 1 312 ? -15.134 24.438  -27.011 1.00 33.78  ? 311 MET A CB     1 
ATOM   4831 C  CG     . MET A 1 312 ? -16.090 23.907  -25.970 1.00 46.16  ? 311 MET A CG     1 
ATOM   4832 S  SD     . MET A 1 312 ? -15.303 23.703  -24.323 1.00 46.22  ? 311 MET A SD     1 
ATOM   4833 C  CE     . MET A 1 312 ? -15.275 25.383  -23.717 1.00 51.08  ? 311 MET A CE     1 
ATOM   4834 H  H      . MET A 1 312 ? -17.646 25.235  -28.016 1.00 36.54  ? 311 MET A H      1 
ATOM   4835 H  HA     . MET A 1 312 ? -15.091 25.251  -28.905 1.00 34.70  ? 311 MET A HA     1 
ATOM   4836 H  HB2    . MET A 1 312 ? -14.451 23.764  -27.148 1.00 40.56  ? 311 MET A HB2    1 
ATOM   4837 H  HB3    . MET A 1 312 ? -14.727 25.241  -26.648 1.00 40.56  ? 311 MET A HB3    1 
ATOM   4838 H  HG2    . MET A 1 312 ? -16.830 24.526  -25.874 1.00 55.41  ? 311 MET A HG2    1 
ATOM   4839 H  HG3    . MET A 1 312 ? -16.418 23.039  -26.256 1.00 55.41  ? 311 MET A HG3    1 
ATOM   4840 H  HE1    . MET A 1 312 ? -14.871 25.394  -22.835 1.00 61.32  ? 311 MET A HE1    1 
ATOM   4841 H  HE2    . MET A 1 312 ? -14.754 25.930  -24.327 1.00 61.32  ? 311 MET A HE2    1 
ATOM   4842 H  HE3    . MET A 1 312 ? -16.184 25.716  -23.669 1.00 61.32  ? 311 MET A HE3    1 
ATOM   4843 N  N      . GLY A 1 313 ? -15.193 22.985  -29.888 1.00 25.40  ? 312 GLY A N      1 
ATOM   4844 C  CA     . GLY A 1 313 ? -15.393 21.716  -30.565 1.00 26.21  ? 312 GLY A CA     1 
ATOM   4845 C  C      . GLY A 1 313 ? -15.042 20.568  -29.639 1.00 26.57  ? 312 GLY A C      1 
ATOM   4846 O  O      . GLY A 1 313 ? -13.899 20.490  -29.173 1.00 25.61  ? 312 GLY A O      1 
ATOM   4847 H  H      . GLY A 1 313 ? -14.431 23.353  -30.042 1.00 30.50  ? 312 GLY A H      1 
ATOM   4848 H  HA2    . GLY A 1 313 ? -16.320 21.628  -30.836 1.00 31.47  ? 312 GLY A HA2    1 
ATOM   4849 H  HA3    . GLY A 1 313 ? -14.829 21.669  -31.352 1.00 31.47  ? 312 GLY A HA3    1 
ATOM   4850 N  N      . LEU A 1 314 ? -16.010 19.692  -29.343 1.00 26.46  ? 313 LEU A N      1 
ATOM   4851 C  CA     . LEU A 1 314 ? -15.802 18.592  -28.392 1.00 27.14  ? 313 LEU A CA     1 
ATOM   4852 C  C      . LEU A 1 314 ? -15.927 17.216  -29.024 1.00 29.29  ? 313 LEU A C      1 
ATOM   4853 O  O      . LEU A 1 314 ? -15.724 16.213  -28.320 1.00 26.20  ? 313 LEU A O      1 
ATOM   4854 C  CB     . LEU A 1 314 ? -16.792 18.693  -27.221 1.00 25.27  ? 313 LEU A CB     1 
ATOM   4855 C  CG     . LEU A 1 314 ? -16.649 19.941  -26.350 1.00 25.68  ? 313 LEU A CG     1 
ATOM   4856 C  CD1    . LEU A 1 314 ? -17.537 19.807  -25.131 1.00 26.05  ? 313 LEU A CD1    1 
ATOM   4857 C  CD2    . LEU A 1 314 ? -15.194 20.144  -25.941 1.00 27.34  ? 313 LEU A CD2    1 
ATOM   4858 H  H      . LEU A 1 314 ? -16.800 19.713  -29.682 1.00 31.77  ? 313 LEU A H      1 
ATOM   4859 H  HA     . LEU A 1 314 ? -14.906 18.667  -28.027 1.00 32.59  ? 313 LEU A HA     1 
ATOM   4860 H  HB2    . LEU A 1 314 ? -17.693 18.689  -27.579 1.00 30.34  ? 313 LEU A HB2    1 
ATOM   4861 H  HB3    . LEU A 1 314 ? -16.668 17.921  -26.647 1.00 30.34  ? 313 LEU A HB3    1 
ATOM   4862 H  HG     . LEU A 1 314 ? -16.936 20.719  -26.853 1.00 30.83  ? 313 LEU A HG     1 
ATOM   4863 H  HD11   . LEU A 1 314 ? -17.442 20.601  -24.583 1.00 31.27  ? 313 LEU A HD11   1 
ATOM   4864 H  HD12   . LEU A 1 314 ? -18.458 19.712  -25.420 1.00 31.27  ? 313 LEU A HD12   1 
ATOM   4865 H  HD13   . LEU A 1 314 ? -17.265 19.023  -24.628 1.00 31.27  ? 313 LEU A HD13   1 
ATOM   4866 H  HD21   . LEU A 1 314 ? -15.130 20.940  -25.391 1.00 32.83  ? 313 LEU A HD21   1 
ATOM   4867 H  HD22   . LEU A 1 314 ? -14.897 19.369  -25.439 1.00 32.83  ? 313 LEU A HD22   1 
ATOM   4868 H  HD23   . LEU A 1 314 ? -14.654 20.248  -26.740 1.00 32.83  ? 313 LEU A HD23   1 
ATOM   4869 N  N      . ASP A 1 315 ? -16.245 17.144  -30.324 1.00 25.81  ? 314 ASP A N      1 
ATOM   4870 C  CA     . ASP A 1 315 ? -16.249 15.893  -31.071 1.00 24.36  ? 314 ASP A CA     1 
ATOM   4871 C  C      . ASP A 1 315 ? -16.120 16.228  -32.556 1.00 26.44  ? 314 ASP A C      1 
ATOM   4872 O  O      . ASP A 1 315 ? -16.398 17.353  -32.981 1.00 26.01  ? 314 ASP A O      1 
ATOM   4873 C  CB     . ASP A 1 315 ? -17.535 15.108  -30.785 1.00 26.84  ? 314 ASP A CB     1 
ATOM   4874 C  CG     . ASP A 1 315 ? -17.462 13.646  -31.210 1.00 34.39  ? 314 ASP A CG     1 
ATOM   4875 O  OD1    . ASP A 1 315 ? -16.337 13.091  -31.340 1.00 34.93  ? 314 ASP A OD1    1 
ATOM   4876 O  OD2    . ASP A 1 315 ? -18.562 13.057  -31.409 1.00 35.81  1 314 ASP A OD2    1 
ATOM   4877 H  H      . ASP A 1 315 ? -16.467 17.825  -30.800 1.00 30.99  ? 314 ASP A H      1 
ATOM   4878 H  HA     . ASP A 1 315 ? -15.489 15.352  -30.806 1.00 29.26  ? 314 ASP A HA     1 
ATOM   4879 H  HB2    . ASP A 1 315 ? -17.713 15.132  -29.832 1.00 32.23  ? 314 ASP A HB2    1 
ATOM   4880 H  HB3    . ASP A 1 315 ? -18.269 15.521  -31.268 1.00 32.23  ? 314 ASP A HB3    1 
ATOM   4881 N  N      . CYS A 1 316 ? -15.715 15.236  -33.340 1.00 27.16  ? 315 CYS A N      1 
ATOM   4882 C  CA     . CYS A 1 316 ? -15.745 15.411  -34.787 1.00 32.16  ? 315 CYS A CA     1 
ATOM   4883 C  C      . CYS A 1 316 ? -17.144 15.091  -35.325 1.00 33.43  ? 315 CYS A C      1 
ATOM   4884 O  O      . CYS A 1 316 ? -17.991 14.511  -34.640 1.00 37.73  ? 315 CYS A O      1 
ATOM   4885 C  CB     . CYS A 1 316 ? -14.686 14.533  -35.443 1.00 37.32  ? 315 CYS A CB     1 
ATOM   4886 S  SG     . CYS A 1 316 ? -15.081 12.769  -35.340 1.00 43.66  ? 315 CYS A SG     1 
ATOM   4887 H  H      . CYS A 1 316 ? -15.425 14.472  -33.069 1.00 32.61  ? 315 CYS A H      1 
ATOM   4888 H  HA     . CYS A 1 316 ? -15.544 16.335  -34.999 1.00 38.61  ? 315 CYS A HA     1 
ATOM   4889 H  HB2    . CYS A 1 316 ? -14.615 14.771  -36.380 1.00 44.81  ? 315 CYS A HB2    1 
ATOM   4890 H  HB3    . CYS A 1 316 ? -13.836 14.677  -34.998 1.00 44.81  ? 315 CYS A HB3    1 
ATOM   4891 H  HG     . CYS A 1 316 ? -14.208 12.141  -35.874 1.00 52.41  ? 315 CYS A HG     1 
ATOM   4892 N  N      . GLY A 1 317 ? -17.394 15.497  -36.569 1.00 31.14  ? 316 GLY A N      1 
ATOM   4893 C  CA     . GLY A 1 317 ? -18.681 15.287  -37.179 1.00 31.95  ? 316 GLY A CA     1 
ATOM   4894 C  C      . GLY A 1 317 ? -18.674 14.117  -38.145 1.00 30.85  ? 316 GLY A C      1 
ATOM   4895 O  O      . GLY A 1 317 ? -17.681 13.393  -38.268 1.00 29.88  ? 316 GLY A O      1 
ATOM   4896 H  H      . GLY A 1 317 ? -16.825 15.898  -37.075 1.00 37.39  ? 316 GLY A H      1 
ATOM   4897 H  HA2    . GLY A 1 317 ? -19.342 15.114  -36.491 1.00 38.36  ? 316 GLY A HA2    1 
ATOM   4898 H  HA3    . GLY A 1 317 ? -18.944 16.085  -37.665 1.00 38.36  ? 316 GLY A HA3    1 
ATOM   4899 N  N      . PRO A 1 318 ? -19.782 13.930  -38.866 1.00 35.43  ? 317 PRO A N      1 
ATOM   4900 C  CA     . PRO A 1 318 ? -19.895 12.757  -39.752 1.00 35.10  ? 317 PRO A CA     1 
ATOM   4901 C  C      . PRO A 1 318 ? -18.904 12.733  -40.914 1.00 31.73  ? 317 PRO A C      1 
ATOM   4902 O  O      . PRO A 1 318 ? -18.401 11.658  -41.269 1.00 31.39  ? 317 PRO A O      1 
ATOM   4903 C  CB     . PRO A 1 318 ? -21.347 12.849  -40.244 1.00 40.82  ? 317 PRO A CB     1 
ATOM   4904 C  CG     . PRO A 1 318 ? -21.704 14.287  -40.108 1.00 43.93  ? 317 PRO A CG     1 
ATOM   4905 C  CD     . PRO A 1 318 ? -20.996 14.766  -38.892 1.00 43.03  ? 317 PRO A CD     1 
ATOM   4906 H  HA     . PRO A 1 318 ? -19.791 11.943  -39.235 1.00 42.14  ? 317 PRO A HA     1 
ATOM   4907 H  HB2    . PRO A 1 318 ? -21.397 12.568  -41.171 1.00 49.01  ? 317 PRO A HB2    1 
ATOM   4908 H  HB3    . PRO A 1 318 ? -21.918 12.298  -39.685 1.00 49.01  ? 317 PRO A HB3    1 
ATOM   4909 H  HG2    . PRO A 1 318 ? -21.402 14.772  -40.892 1.00 52.73  ? 317 PRO A HG2    1 
ATOM   4910 H  HG3    . PRO A 1 318 ? -22.664 14.374  -40.000 1.00 52.73  ? 317 PRO A HG3    1 
ATOM   4911 H  HD2    . PRO A 1 318 ? -20.761 15.703  -38.983 1.00 51.66  ? 317 PRO A HD2    1 
ATOM   4912 H  HD3    . PRO A 1 318 ? -21.534 14.607  -38.101 1.00 51.66  ? 317 PRO A HD3    1 
ATOM   4913 N  N      . GLU A 1 319 ? -18.604 13.873  -41.535 1.00 29.29  ? 318 GLU A N      1 
ATOM   4914 C  CA     . GLU A 1 319 ? -17.661 13.824  -42.647 1.00 33.91  ? 318 GLU A CA     1 
ATOM   4915 C  C      . GLU A 1 319 ? -16.260 13.494  -42.159 1.00 30.68  ? 318 GLU A C      1 
ATOM   4916 O  O      . GLU A 1 319 ? -15.500 12.813  -42.861 1.00 28.64  ? 318 GLU A O      1 
ATOM   4917 C  CB     . GLU A 1 319 ? -17.681 15.143  -43.417 1.00 47.13  ? 318 GLU A CB     1 
ATOM   4918 C  CG     . GLU A 1 319 ? -18.981 15.373  -44.191 1.00 62.46  ? 318 GLU A CG     1 
ATOM   4919 C  CD     . GLU A 1 319 ? -19.221 14.340  -45.304 1.00 72.26  ? 318 GLU A CD     1 
ATOM   4920 O  OE1    . GLU A 1 319 ? -18.245 13.893  -45.952 1.00 72.21  ? 318 GLU A OE1    1 
ATOM   4921 O  OE2    . GLU A 1 319 ? -20.395 13.972  -45.530 1.00 76.24  1 318 GLU A OE2    1 
ATOM   4922 H  H      . GLU A 1 319 ? -18.916 14.651  -41.343 1.00 35.05  ? 318 GLU A H      1 
ATOM   4923 H  HA     . GLU A 1 319 ? -17.934 13.121  -43.256 1.00 40.71  ? 318 GLU A HA     1 
ATOM   4924 H  HB2    . GLU A 1 319 ? -17.575 15.875  -42.790 1.00 56.57  ? 318 GLU A HB2    1 
ATOM   4925 H  HB3    . GLU A 1 319 ? -16.950 15.145  -44.055 1.00 56.57  ? 318 GLU A HB3    1 
ATOM   4926 H  HG2    . GLU A 1 319 ? -19.727 15.324  -43.574 1.00 74.98  ? 318 GLU A HG2    1 
ATOM   4927 H  HG3    . GLU A 1 319 ? -18.950 16.251  -44.602 1.00 74.98  ? 318 GLU A HG3    1 
ATOM   4928 N  N      . SER A 1 320 ? -15.918 13.938  -40.948 1.00 29.37  ? 319 SER A N      1 
ATOM   4929 C  CA     . SER A 1 320 ? -14.641 13.559  -40.360 1.00 28.88  ? 319 SER A CA     1 
ATOM   4930 C  C      . SER A 1 320 ? -14.586 12.065  -40.114 1.00 28.43  ? 319 SER A C      1 
ATOM   4931 O  O      . SER A 1 320 ? -13.586 11.407  -40.430 1.00 28.75  ? 319 SER A O      1 
ATOM   4932 C  CB     . SER A 1 320 ? -14.420 14.307  -39.052 1.00 29.39  ? 319 SER A CB     1 
ATOM   4933 O  OG     . SER A 1 320 ? -14.454 15.710  -39.253 1.00 32.44  ? 319 SER A OG     1 
ATOM   4934 H  H      . SER A 1 320 ? -16.401 14.451  -40.455 1.00 35.27  ? 319 SER A H      1 
ATOM   4935 H  HA     . SER A 1 320 ? -13.925 13.794  -40.971 1.00 34.68  ? 319 SER A HA     1 
ATOM   4936 H  HB2    . SER A 1 320 ? -15.120 14.062  -38.427 1.00 35.28  ? 319 SER A HB2    1 
ATOM   4937 H  HB3    . SER A 1 320 ? -13.554 14.062  -38.691 1.00 35.28  ? 319 SER A HB3    1 
ATOM   4938 H  HG     . SER A 1 320 ? -15.200 15.938  -39.565 1.00 38.94  ? 319 SER A HG     1 
ATOM   4939 N  N      . SER A 1 321 ? -15.663 11.508  -39.565 1.00 28.09  ? 320 SER A N      1 
ATOM   4940 C  CA     . SER A 1 321 ? -15.678 10.079  -39.292 1.00 28.77  ? 320 SER A CA     1 
ATOM   4941 C  C      . SER A 1 321 ? -15.484 9.285   -40.572 1.00 30.52  ? 320 SER A C      1 
ATOM   4942 O  O      . SER A 1 321 ? -14.786 8.267   -40.582 1.00 31.31  ? 320 SER A O      1 
ATOM   4943 C  CB     . SER A 1 321 ? -16.982 9.710   -38.594 1.00 32.37  ? 320 SER A CB     1 
ATOM   4944 O  OG     . SER A 1 321 ? -17.009 10.292  -37.291 1.00 35.16  ? 320 SER A OG     1 
ATOM   4945 H  H      . SER A 1 321 ? -16.382 11.927  -39.347 1.00 33.73  ? 320 SER A H      1 
ATOM   4946 H  HA     . SER A 1 321 ? -14.946 9.864   -38.693 1.00 34.54  ? 320 SER A HA     1 
ATOM   4947 H  HB2    . SER A 1 321 ? -17.729 10.049  -39.111 1.00 38.86  ? 320 SER A HB2    1 
ATOM   4948 H  HB3    . SER A 1 321 ? -17.040 8.745   -38.514 1.00 38.86  ? 320 SER A HB3    1 
ATOM   4949 H  HG     . SER A 1 321 ? -17.726 10.092  -36.902 1.00 42.21  ? 320 SER A HG     1 
ATOM   4950 N  N      . LYS A 1 322 ? -16.063 9.757   -41.670 1.00 30.51  ? 321 LYS A N      1 
ATOM   4951 C  CA     . LYS A 1 322 ? -15.895 9.069   -42.939 1.00 29.57  ? 321 LYS A CA     1 
ATOM   4952 C  C      . LYS A 1 322 ? -14.428 9.065   -43.361 1.00 30.89  ? 321 LYS A C      1 
ATOM   4953 O  O      . LYS A 1 322 ? -13.914 8.044   -43.844 1.00 33.57  ? 321 LYS A O      1 
ATOM   4954 C  CB     . LYS A 1 322 ? -16.780 9.737   -44.000 1.00 32.64  ? 321 LYS A CB     1 
ATOM   4955 C  CG     . LYS A 1 322 ? -16.779 9.005   -45.318 1.00 42.26  ? 321 LYS A CG     1 
ATOM   4956 C  CD     . LYS A 1 322 ? -17.752 9.645   -46.314 1.00 55.41  ? 321 LYS A CD     1 
ATOM   4957 C  CE     . LYS A 1 322 ? -17.989 8.744   -47.528 1.00 69.55  ? 321 LYS A CE     1 
ATOM   4958 N  NZ     . LYS A 1 322 ? -16.762 8.541   -48.352 1.00 75.93  1 321 LYS A NZ     1 
ATOM   4959 H  H      . LYS A 1 322 ? -16.552 10.464  -41.705 1.00 36.63  ? 321 LYS A H      1 
ATOM   4960 H  HA     . LYS A 1 322 ? -16.184 8.148   -42.842 1.00 35.50  ? 321 LYS A HA     1 
ATOM   4961 H  HB2    . LYS A 1 322 ? -17.693 9.767   -43.675 1.00 39.19  ? 321 LYS A HB2    1 
ATOM   4962 H  HB3    . LYS A 1 322 ? -16.455 10.638  -44.158 1.00 39.19  ? 321 LYS A HB3    1 
ATOM   4963 H  HG2    . LYS A 1 322 ? -15.888 9.035   -45.701 1.00 50.73  ? 321 LYS A HG2    1 
ATOM   4964 H  HG3    . LYS A 1 322 ? -17.053 8.085   -45.174 1.00 50.73  ? 321 LYS A HG3    1 
ATOM   4965 H  HD2    . LYS A 1 322 ? -18.605 9.796   -45.877 1.00 66.52  ? 321 LYS A HD2    1 
ATOM   4966 H  HD3    . LYS A 1 322 ? -17.383 10.486  -46.627 1.00 66.52  ? 321 LYS A HD3    1 
ATOM   4967 H  HE2    . LYS A 1 322 ? -18.289 7.874   -47.221 1.00 83.48  ? 321 LYS A HE2    1 
ATOM   4968 H  HE3    . LYS A 1 322 ? -18.665 9.147   -48.093 1.00 83.48  ? 321 LYS A HE3    1 
ATOM   4969 H  HZ1    . LYS A 1 322 ? -16.945 8.012   -49.044 1.00 91.13  ? 321 LYS A HZ1    1 
ATOM   4970 H  HZ2    . LYS A 1 322 ? -16.467 9.324   -48.655 1.00 91.13  ? 321 LYS A HZ2    1 
ATOM   4971 H  HZ3    . LYS A 1 322 ? -16.124 8.163   -47.859 1.00 91.13  ? 321 LYS A HZ3    1 
ATOM   4972 N  N      . LYS A 1 323 ? -13.736 10.198  -43.185 1.00 32.47  ? 322 LYS A N      1 
ATOM   4973 C  CA     . LYS A 1 323 ? -12.314 10.285  -43.532 1.00 32.61  ? 322 LYS A CA     1 
ATOM   4974 C  C      . LYS A 1 323 ? -11.447 9.447   -42.601 1.00 29.87  ? 322 LYS A C      1 
ATOM   4975 O  O      . LYS A 1 323 ? -10.480 8.822   -43.050 1.00 31.30  ? 322 LYS A O      1 
ATOM   4976 C  CB     . LYS A 1 323 ? -11.847 11.739  -43.493 1.00 36.34  ? 322 LYS A CB     1 
ATOM   4977 C  CG     . LYS A 1 323 ? -12.555 12.632  -44.512 1.00 49.78  ? 322 LYS A CG     1 
ATOM   4978 C  CD     . LYS A 1 323 ? -12.130 14.095  -44.425 1.00 65.50  ? 322 LYS A CD     1 
ATOM   4979 C  CE     . LYS A 1 323 ? -10.711 14.338  -44.930 1.00 75.91  ? 322 LYS A CE     1 
ATOM   4980 N  NZ     . LYS A 1 323 ? -10.547 13.985  -46.363 1.00 79.21  ? 322 LYS A NZ     1 
ATOM   4981 H  H      . LYS A 1 323 ? -14.066 10.926  -42.868 1.00 38.98  ? 322 LYS A H      1 
ATOM   4982 H  HA     . LYS A 1 323 ? -12.189 9.955   -44.435 1.00 39.15  ? 322 LYS A HA     1 
ATOM   4983 H  HB2    . LYS A 1 323 ? -12.020 12.100  -42.609 1.00 43.63  ? 322 LYS A HB2    1 
ATOM   4984 H  HB3    . LYS A 1 323 ? -10.896 11.768  -43.681 1.00 43.63  ? 322 LYS A HB3    1 
ATOM   4985 H  HG2    . LYS A 1 323 ? -12.350 12.314  -45.405 1.00 59.76  ? 322 LYS A HG2    1 
ATOM   4986 H  HG3    . LYS A 1 323 ? -13.512 12.589  -44.358 1.00 59.76  ? 322 LYS A HG3    1 
ATOM   4987 H  HD2    . LYS A 1 323 ? -12.734 14.631  -44.963 1.00 78.62  ? 322 LYS A HD2    1 
ATOM   4988 H  HD3    . LYS A 1 323 ? -12.171 14.380  -43.499 1.00 78.62  ? 322 LYS A HD3    1 
ATOM   4989 H  HE2    . LYS A 1 323 ? -10.494 15.278  -44.825 1.00 91.11  ? 322 LYS A HE2    1 
ATOM   4990 H  HE3    . LYS A 1 323 ? -10.095 13.795  -44.414 1.00 91.11  ? 322 LYS A HE3    1 
ATOM   4991 H  HZ1    . LYS A 1 323 ? -9.709  14.140  -46.620 1.00 95.08  ? 322 LYS A HZ1    1 
ATOM   4992 H  HZ2    . LYS A 1 323 ? -10.733 13.124  -46.487 1.00 95.08  ? 322 LYS A HZ2    1 
ATOM   4993 H  HZ3    . LYS A 1 323 ? -11.098 14.475  -46.862 1.00 95.08  ? 322 LYS A HZ3    1 
ATOM   4994 N  N      . TYR A 1 324 ? -11.746 9.453   -41.294 1.00 27.90  ? 323 TYR A N      1 
ATOM   4995 C  CA     . TYR A 1 324 ? -11.015 8.588   -40.370 1.00 27.06  ? 323 TYR A CA     1 
ATOM   4996 C  C      . TYR A 1 324 ? -11.169 7.128   -40.771 1.00 29.17  ? 323 TYR A C      1 
ATOM   4997 O  O      . TYR A 1 324 ? -10.195 6.357   -40.781 1.00 28.68  ? 323 TYR A O      1 
ATOM   4998 C  CB     . TYR A 1 324 ? -11.519 8.791   -38.931 1.00 25.74  ? 323 TYR A CB     1 
ATOM   4999 C  CG     . TYR A 1 324 ? -11.271 10.141  -38.293 1.00 27.45  ? 323 TYR A CG     1 
ATOM   5000 C  CD1    . TYR A 1 324 ? -10.466 11.098  -38.883 1.00 28.25  ? 323 TYR A CD1    1 
ATOM   5001 C  CD2    . TYR A 1 324 ? -11.829 10.432  -37.058 1.00 31.96  ? 323 TYR A CD2    1 
ATOM   5002 C  CE1    . TYR A 1 324 ? -10.237 12.334  -38.257 1.00 29.26  ? 323 TYR A CE1    1 
ATOM   5003 C  CE2    . TYR A 1 324 ? -11.600 11.643  -36.430 1.00 33.89  ? 323 TYR A CE2    1 
ATOM   5004 C  CZ     . TYR A 1 324 ? -10.810 12.589  -37.043 1.00 32.48  ? 323 TYR A CZ     1 
ATOM   5005 O  OH     . TYR A 1 324 ? -10.587 13.783  -36.402 1.00 33.18  ? 323 TYR A OH     1 
ATOM   5006 H  H      . TYR A 1 324 ? -12.355 9.939   -40.929 1.00 33.50  ? 323 TYR A H      1 
ATOM   5007 H  HA     . TYR A 1 324 ? -10.072 8.814   -40.397 1.00 32.49  ? 323 TYR A HA     1 
ATOM   5008 H  HB2    . TYR A 1 324 ? -12.478 8.645   -38.925 1.00 30.91  ? 323 TYR A HB2    1 
ATOM   5009 H  HB3    . TYR A 1 324 ? -11.093 8.127   -38.367 1.00 30.91  ? 323 TYR A HB3    1 
ATOM   5010 H  HD1    . TYR A 1 324 ? -10.077 10.924  -39.710 1.00 33.92  ? 323 TYR A HD1    1 
ATOM   5011 H  HD2    . TYR A 1 324 ? -12.364 9.797   -36.639 1.00 38.37  ? 323 TYR A HD2    1 
ATOM   5012 H  HE1    . TYR A 1 324 ? -9.697  12.973  -38.664 1.00 35.13  ? 323 TYR A HE1    1 
ATOM   5013 H  HE2    . TYR A 1 324 ? -11.988 11.822  -35.604 1.00 40.68  ? 323 TYR A HE2    1 
ATOM   5014 H  HH     . TYR A 1 324 ? -10.080 14.268  -36.865 1.00 39.84  ? 323 TYR A HH     1 
ATOM   5015 N  N      . ALA A 1 325 ? -12.395 6.738   -41.128 1.00 30.78  ? 324 ALA A N      1 
ATOM   5016 C  CA     . ALA A 1 325 ? -12.654 5.362   -41.511 1.00 31.34  ? 324 ALA A CA     1 
ATOM   5017 C  C      . ALA A 1 325 ? -11.852 4.980   -42.749 1.00 32.00  ? 324 ALA A C      1 
ATOM   5018 O  O      . ALA A 1 325 ? -11.397 3.837   -42.867 1.00 35.77  ? 324 ALA A O      1 
ATOM   5019 C  CB     . ALA A 1 325 ? -14.148 5.169   -41.751 1.00 34.59  ? 324 ALA A CB     1 
ATOM   5020 H  H      . ALA A 1 325 ? -13.085 7.251   -41.154 1.00 36.96  ? 324 ALA A H      1 
ATOM   5021 H  HA     . ALA A 1 325 ? -12.386 4.776   -40.786 1.00 37.63  ? 324 ALA A HA     1 
ATOM   5022 H  HB1    . ALA A 1 325 ? -14.310 4.247   -42.007 1.00 41.52  ? 324 ALA A HB1    1 
ATOM   5023 H  HB2    . ALA A 1 325 ? -14.628 5.375   -40.934 1.00 41.52  ? 324 ALA A HB2    1 
ATOM   5024 H  HB3    . ALA A 1 325 ? -14.433 5.764   -42.462 1.00 41.52  ? 324 ALA A HB3    1 
ATOM   5025 N  N      . GLU A 1 326 ? -11.670 5.921   -43.684 1.00 31.38  ? 325 GLU A N      1 
ATOM   5026 C  CA     . GLU A 1 326 ? -10.922 5.632   -44.913 1.00 34.61  ? 325 GLU A CA     1 
ATOM   5027 C  C      . GLU A 1 326 ? -9.458  5.338   -44.603 1.00 35.51  ? 325 GLU A C      1 
ATOM   5028 O  O      . GLU A 1 326 ? -8.864  4.433   -45.198 1.00 34.39  ? 325 GLU A O      1 
ATOM   5029 C  CB     . GLU A 1 326 ? -11.051 6.797   -45.895 1.00 38.18  ? 325 GLU A CB     1 
ATOM   5030 C  CG     . GLU A 1 326 ? -12.429 6.813   -46.540 1.00 50.16  ? 325 GLU A CG     1 
ATOM   5031 C  CD     . GLU A 1 326 ? -12.744 8.081   -47.319 1.00 55.21  ? 325 GLU A CD     1 
ATOM   5032 O  OE1    . GLU A 1 326 ? -11.868 8.972   -47.406 1.00 54.69  ? 325 GLU A OE1    1 
ATOM   5033 O  OE2    . GLU A 1 326 ? -13.884 8.171   -47.839 1.00 55.31  1 325 GLU A OE2    1 
ATOM   5034 H  H      . GLU A 1 326 ? -11.967 6.726   -43.631 1.00 37.68  ? 325 GLU A H      1 
ATOM   5035 H  HA     . GLU A 1 326 ? -11.301 4.844   -45.334 1.00 41.55  ? 325 GLU A HA     1 
ATOM   5036 H  HB2    . GLU A 1 326 ? -10.925 7.633   -45.420 1.00 45.83  ? 325 GLU A HB2    1 
ATOM   5037 H  HB3    . GLU A 1 326 ? -10.386 6.703   -46.595 1.00 45.83  ? 325 GLU A HB3    1 
ATOM   5038 H  HG2    . GLU A 1 326 ? -12.492 6.066   -47.155 1.00 60.21  ? 325 GLU A HG2    1 
ATOM   5039 H  HG3    . GLU A 1 326 ? -13.098 6.721   -45.844 1.00 60.21  ? 325 GLU A HG3    1 
ATOM   5040 N  N      . ALA A 1 327 ? -8.871  6.069   -43.648 1.00 32.44  ? 326 ALA A N      1 
ATOM   5041 C  CA     . ALA A 1 327 ? -7.489  5.804   -43.280 1.00 30.41  ? 326 ALA A CA     1 
ATOM   5042 C  C      . ALA A 1 327 ? -7.367  4.480   -42.544 1.00 28.84  ? 326 ALA A C      1 
ATOM   5043 O  O      . ALA A 1 327 ? -6.415  3.727   -42.780 1.00 30.48  ? 326 ALA A O      1 
ATOM   5044 C  CB     . ALA A 1 327 ? -6.931  6.942   -42.427 1.00 30.84  ? 326 ALA A CB     1 
ATOM   5045 H  H      . ALA A 1 327 ? -9.246  6.708   -43.212 1.00 38.95  ? 326 ALA A H      1 
ATOM   5046 H  HA     . ALA A 1 327 ? -6.954  5.746   -44.087 1.00 36.51  ? 326 ALA A HA     1 
ATOM   5047 H  HB1    . ALA A 1 327 ? -6.010  6.741   -42.196 1.00 37.03  ? 326 ALA A HB1    1 
ATOM   5048 H  HB2    . ALA A 1 327 ? -6.971  7.767   -42.936 1.00 37.03  ? 326 ALA A HB2    1 
ATOM   5049 H  HB3    . ALA A 1 327 ? -7.464  7.024   -41.621 1.00 37.03  ? 326 ALA A HB3    1 
ATOM   5050 N  N      . VAL A 1 328 ? -8.307  4.188   -41.638 1.00 28.30  ? 327 VAL A N      1 
ATOM   5051 C  CA     . VAL A 1 328 ? -8.291  2.908   -40.933 1.00 26.96  ? 327 VAL A CA     1 
ATOM   5052 C  C      . VAL A 1 328 ? -8.389  1.757   -41.924 1.00 29.76  ? 327 VAL A C      1 
ATOM   5053 O  O      . VAL A 1 328 ? -7.748  0.721   -41.753 1.00 30.15  ? 327 VAL A O      1 
ATOM   5054 C  CB     . VAL A 1 328 ? -9.429  2.853   -39.897 1.00 26.48  ? 327 VAL A CB     1 
ATOM   5055 C  CG1    . VAL A 1 328 ? -9.584  1.439   -39.310 1.00 28.52  ? 327 VAL A CG1    1 
ATOM   5056 C  CG2    . VAL A 1 328 ? -9.190  3.864   -38.810 1.00 24.92  ? 327 VAL A CG2    1 
ATOM   5057 H  H      . VAL A 1 328 ? -8.956  4.708   -41.419 1.00 33.98  ? 327 VAL A H      1 
ATOM   5058 H  HA     . VAL A 1 328 ? -7.450  2.821   -40.458 1.00 32.38  ? 327 VAL A HA     1 
ATOM   5059 H  HB     . VAL A 1 328 ? -10.263 3.083   -40.337 1.00 31.80  ? 327 VAL A HB     1 
ATOM   5060 H  HG11   . VAL A 1 328 ? -10.307 1.443   -38.664 1.00 34.24  ? 327 VAL A HG11   1 
ATOM   5061 H  HG12   . VAL A 1 328 ? -9.785  0.819   -40.029 1.00 34.24  ? 327 VAL A HG12   1 
ATOM   5062 H  HG13   . VAL A 1 328 ? -8.754  1.185   -38.877 1.00 34.24  ? 327 VAL A HG13   1 
ATOM   5063 H  HG21   . VAL A 1 328 ? -9.915  3.815   -38.169 1.00 29.92  ? 327 VAL A HG21   1 
ATOM   5064 H  HG22   . VAL A 1 328 ? -8.347  3.664   -38.374 1.00 29.92  ? 327 VAL A HG22   1 
ATOM   5065 H  HG23   . VAL A 1 328 ? -9.156  4.750   -39.205 1.00 29.92  ? 327 VAL A HG23   1 
ATOM   5066 N  N      . THR A 1 329 ? -9.199  1.916   -42.971 1.00 34.00  ? 328 THR A N      1 
ATOM   5067 C  CA     . THR A 1 329 ? -9.368  0.856   -43.959 1.00 35.60  ? 328 THR A CA     1 
ATOM   5068 C  C      . THR A 1 329 ? -8.083  0.579   -44.725 1.00 32.93  ? 328 THR A C      1 
ATOM   5069 O  O      . THR A 1 329 ? -7.853  -0.555  -45.159 1.00 35.00  ? 328 THR A O      1 
ATOM   5070 C  CB     . THR A 1 329 ? -10.510 1.222   -44.922 1.00 44.43  ? 328 THR A CB     1 
ATOM   5071 O  OG1    . THR A 1 329 ? -11.751 0.983   -44.256 1.00 46.31  ? 328 THR A OG1    1 
ATOM   5072 C  CG2    . THR A 1 329 ? -10.472 0.397   -46.188 1.00 49.80  ? 328 THR A CG2    1 
ATOM   5073 H  H      . THR A 1 329 ? -9.659  2.625   -43.130 1.00 40.82  ? 328 THR A H      1 
ATOM   5074 H  HA     . THR A 1 329 ? -9.619  0.039   -43.500 1.00 42.74  ? 328 THR A HA     1 
ATOM   5075 H  HB     . THR A 1 329 ? -10.445 2.160   -45.162 1.00 53.34  ? 328 THR A HB     1 
ATOM   5076 H  HG1    . THR A 1 329 ? -11.800 1.454   -43.562 1.00 55.59  ? 328 THR A HG1    1 
ATOM   5077 H  HG21   . THR A 1 329 ? -11.203 0.652   -46.772 1.00 59.78  ? 328 THR A HG21   1 
ATOM   5078 H  HG22   . THR A 1 329 ? -9.632  0.541   -46.653 1.00 59.78  ? 328 THR A HG22   1 
ATOM   5079 H  HG23   . THR A 1 329 ? -10.555 -0.545  -45.972 1.00 59.78  ? 328 THR A HG23   1 
ATOM   5080 N  N      . ARG A 1 330 ? -7.252  1.595   -44.922 1.00 31.88  ? 329 ARG A N      1 
ATOM   5081 C  CA     . ARG A 1 330 ? -5.984  1.428   -45.620 1.00 32.63  ? 329 ARG A CA     1 
ATOM   5082 C  C      . ARG A 1 330 ? -4.886  0.793   -44.765 1.00 32.39  ? 329 ARG A C      1 
ATOM   5083 O  O      . ARG A 1 330 ? -3.901  0.295   -45.333 1.00 32.67  ? 329 ARG A O      1 
ATOM   5084 C  CB     . ARG A 1 330 ? -5.496  2.786   -46.118 1.00 34.99  ? 329 ARG A CB     1 
ATOM   5085 C  CG     . ARG A 1 330 ? -6.350  3.385   -47.257 1.00 40.68  ? 329 ARG A CG     1 
ATOM   5086 C  CD     . ARG A 1 330 ? -5.716  4.629   -47.824 1.00 40.36  ? 329 ARG A CD     1 
ATOM   5087 N  NE     . ARG A 1 330 ? -5.566  5.727   -46.878 1.00 39.24  ? 329 ARG A NE     1 
ATOM   5088 C  CZ     . ARG A 1 330 ? -6.452  6.707   -46.696 1.00 40.53  ? 329 ARG A CZ     1 
ATOM   5089 N  NH1    . ARG A 1 330 ? -7.583  6.733   -47.390 1.00 41.93  1 329 ARG A NH1    1 
ATOM   5090 N  NH2    . ARG A 1 330 ? -6.206  7.665   -45.799 1.00 41.31  ? 329 ARG A NH2    1 
ATOM   5091 H  H      . ARG A 1 330 ? -7.401  2.400   -44.658 1.00 38.27  ? 329 ARG A H      1 
ATOM   5092 H  HA     . ARG A 1 330 ? -6.124  0.859   -46.393 1.00 39.17  ? 329 ARG A HA     1 
ATOM   5093 H  HB2    . ARG A 1 330 ? -5.510  3.413   -45.377 1.00 42.00  ? 329 ARG A HB2    1 
ATOM   5094 H  HB3    . ARG A 1 330 ? -4.589  2.690   -46.448 1.00 42.00  ? 329 ARG A HB3    1 
ATOM   5095 H  HG2    . ARG A 1 330 ? -6.434  2.734   -47.971 1.00 48.83  ? 329 ARG A HG2    1 
ATOM   5096 H  HG3    . ARG A 1 330 ? -7.226  3.620   -46.911 1.00 48.83  ? 329 ARG A HG3    1 
ATOM   5097 H  HD2    . ARG A 1 330 ? -4.831  4.403   -48.153 1.00 48.46  ? 329 ARG A HD2    1 
ATOM   5098 H  HD3    . ARG A 1 330 ? -6.263  4.948   -48.559 1.00 48.46  ? 329 ARG A HD3    1 
ATOM   5099 H  HE     . ARG A 1 330 ? -4.851  5.744   -46.400 1.00 47.11  ? 329 ARG A HE     1 
ATOM   5100 H  HH11   . ARG A 1 330 ? -7.746  6.119   -47.969 1.00 50.33  ? 329 ARG A HH11   1 
ATOM   5101 H  HH12   . ARG A 1 330 ? -8.150  7.368   -47.265 1.00 50.33  ? 329 ARG A HH12   1 
ATOM   5102 H  HH21   . ARG A 1 330 ? -5.476  7.651   -45.345 1.00 49.59  ? 329 ARG A HH21   1 
ATOM   5103 H  HH22   . ARG A 1 330 ? -6.777  8.296   -45.677 1.00 49.59  ? 329 ARG A HH22   1 
ATOM   5104 N  N      . ALA A 1 331 ? -5.029  0.784   -43.432 1.00 29.26  ? 330 ALA A N      1 
ATOM   5105 C  CA     . ALA A 1 331 ? -3.929  0.398   -42.553 1.00 27.00  ? 330 ALA A CA     1 
ATOM   5106 C  C      . ALA A 1 331 ? -3.813  -1.117  -42.401 1.00 28.92  ? 330 ALA A C      1 
ATOM   5107 O  O      . ALA A 1 331 ? -4.801  -1.856  -42.421 1.00 32.42  ? 330 ALA A O      1 
ATOM   5108 C  CB     . ALA A 1 331 ? -4.098  1.030   -41.166 1.00 26.73  ? 330 ALA A CB     1 
ATOM   5109 H  H      . ALA A 1 331 ? -5.752  0.998   -43.018 1.00 35.13  ? 330 ALA A H      1 
ATOM   5110 H  HA     . ALA A 1 331 ? -3.097  0.724   -42.930 1.00 32.42  ? 330 ALA A HA     1 
ATOM   5111 H  HB1    . ALA A 1 331 ? -3.356  0.758   -40.603 1.00 32.10  ? 330 ALA A HB1    1 
ATOM   5112 H  HB2    . ALA A 1 331 ? -4.106  1.996   -41.258 1.00 32.10  ? 330 ALA A HB2    1 
ATOM   5113 H  HB3    . ALA A 1 331 ? -4.934  0.727   -40.780 1.00 32.10  ? 330 ALA A HB3    1 
ATOM   5114 N  N      . LYS A 1 332 ? -2.576  -1.577  -42.251 1.00 28.67  ? 331 LYS A N      1 
ATOM   5115 C  CA     . LYS A 1 332 ? -2.298  -2.927  -41.775 1.00 27.77  ? 331 LYS A CA     1 
ATOM   5116 C  C      . LYS A 1 332 ? -1.809  -2.971  -40.322 1.00 24.95  ? 331 LYS A C      1 
ATOM   5117 O  O      . LYS A 1 332 ? -1.738  -4.063  -39.728 1.00 27.67  ? 331 LYS A O      1 
ATOM   5118 C  CB     . LYS A 1 332 ? -1.267  -3.598  -42.676 1.00 27.42  ? 331 LYS A CB     1 
ATOM   5119 C  CG     . LYS A 1 332 ? -1.789  -3.775  -44.119 1.00 32.30  ? 331 LYS A CG     1 
ATOM   5120 C  CD     . LYS A 1 332 ? -0.903  -4.694  -44.927 1.00 41.28  ? 331 LYS A CD     1 
ATOM   5121 C  CE     . LYS A 1 332 ? -1.433  -4.816  -46.353 1.00 50.37  ? 331 LYS A CE     1 
ATOM   5122 N  NZ     . LYS A 1 332 ? -2.822  -5.378  -46.382 1.00 53.76  1 331 LYS A NZ     1 
ATOM   5123 H  H      . LYS A 1 332 ? -1.868  -1.118  -42.421 1.00 34.42  ? 331 LYS A H      1 
ATOM   5124 H  HA     . LYS A 1 332 ? -3.115  -3.447  -41.825 1.00 33.35  ? 331 LYS A HA     1 
ATOM   5125 H  HB2    . LYS A 1 332 ? -0.467  -3.050  -42.709 1.00 32.81  ? 331 LYS A HB2    1 
ATOM   5126 H  HB3    . LYS A 1 332 ? -1.056  -4.476  -42.321 1.00 32.81  ? 331 LYS A HB3    1 
ATOM   5127 H  HG2    . LYS A 1 332 ? -2.679  -4.159  -44.091 1.00 38.78  ? 331 LYS A HG2    1 
ATOM   5128 H  HG3    . LYS A 1 332 ? -1.811  -2.911  -44.558 1.00 38.78  ? 331 LYS A HG3    1 
ATOM   5129 H  HD2    . LYS A 1 332 ? -0.004  -4.330  -44.962 1.00 49.55  ? 331 LYS A HD2    1 
ATOM   5130 H  HD3    . LYS A 1 332 ? -0.897  -5.576  -44.524 1.00 49.55  ? 331 LYS A HD3    1 
ATOM   5131 H  HE2    . LYS A 1 332 ? -1.453  -3.937  -46.763 1.00 60.46  ? 331 LYS A HE2    1 
ATOM   5132 H  HE3    . LYS A 1 332 ? -0.855  -5.408  -46.859 1.00 60.46  ? 331 LYS A HE3    1 
ATOM   5133 H  HZ1    . LYS A 1 332 ? -3.108  -5.439  -47.223 1.00 64.53  ? 331 LYS A HZ1    1 
ATOM   5134 H  HZ2    . LYS A 1 332 ? -2.830  -6.189  -46.014 1.00 64.53  ? 331 LYS A HZ2    1 
ATOM   5135 H  HZ3    . LYS A 1 332 ? -3.374  -4.849  -45.927 1.00 64.53  ? 331 LYS A HZ3    1 
ATOM   5136 N  N      . GLN A 1 333 ? -1.433  -1.833  -39.752 1.00 24.33  ? 332 GLN A N      1 
ATOM   5137 C  CA     . GLN A 1 333 ? -1.114  -1.706  -38.330 1.00 23.92  ? 332 GLN A CA     1 
ATOM   5138 C  C      . GLN A 1 333 ? -1.559  -0.324  -37.875 1.00 23.65  ? 332 GLN A C      1 
ATOM   5139 O  O      . GLN A 1 333 ? -1.393  0.654   -38.609 1.00 24.69  ? 332 GLN A O      1 
ATOM   5140 C  CB     . GLN A 1 333 ? 0.388   -1.916  -38.066 1.00 23.87  ? 332 GLN A CB     1 
ATOM   5141 C  CG     . GLN A 1 333 ? 0.796   -1.936  -36.579 1.00 24.59  ? 332 GLN A CG     1 
ATOM   5142 C  CD     . GLN A 1 333 ? 2.138   -2.616  -36.322 1.00 27.43  ? 332 GLN A CD     1 
ATOM   5143 O  OE1    . GLN A 1 333 ? 2.456   -3.662  -36.913 1.00 29.14  ? 332 GLN A OE1    1 
ATOM   5144 N  NE2    . GLN A 1 333 ? 2.942   -2.017  -35.442 1.00 28.48  ? 332 GLN A NE2    1 
ATOM   5145 H  H      . GLN A 1 333 ? -1.352  -1.093  -40.183 1.00 29.22  ? 332 GLN A H      1 
ATOM   5146 H  HA     . GLN A 1 333 ? -1.610  -2.370  -37.827 1.00 28.72  ? 332 GLN A HA     1 
ATOM   5147 H  HB2    . GLN A 1 333 ? 0.653   -2.765  -38.453 1.00 28.67  ? 332 GLN A HB2    1 
ATOM   5148 H  HB3    . GLN A 1 333 ? 0.879   -1.197  -38.494 1.00 28.67  ? 332 GLN A HB3    1 
ATOM   5149 H  HG2    . GLN A 1 333 ? 0.861   -1.022  -36.259 1.00 29.53  ? 332 GLN A HG2    1 
ATOM   5150 H  HG3    . GLN A 1 333 ? 0.120   -2.414  -36.074 1.00 29.53  ? 332 GLN A HG3    1 
ATOM   5151 H  HE21   . GLN A 1 333 ? 2.692   -1.289  -35.057 1.00 34.19  ? 332 GLN A HE21   1 
ATOM   5152 H  HE22   . GLN A 1 333 ? 3.710   -2.358  -35.259 1.00 34.19  ? 332 GLN A HE22   1 
ATOM   5153 N  N      . ILE A 1 334 ? -2.160  -0.264  -36.683 1.00 20.73  ? 333 ILE A N      1 
ATOM   5154 C  CA     . ILE A 1 334 ? -2.679  0.973   -36.099 1.00 19.80  ? 333 ILE A CA     1 
ATOM   5155 C  C      . ILE A 1 334 ? -2.232  1.070   -34.634 1.00 19.00  ? 333 ILE A C      1 
ATOM   5156 O  O      . ILE A 1 334 ? -2.360  0.104   -33.868 1.00 19.84  ? 333 ILE A O      1 
ATOM   5157 C  CB     . ILE A 1 334 ? -4.218  1.019   -36.195 1.00 21.59  ? 333 ILE A CB     1 
ATOM   5158 C  CG1    . ILE A 1 334 ? -4.692  0.878   -37.645 1.00 26.92  ? 333 ILE A CG1    1 
ATOM   5159 C  CG2    . ILE A 1 334 ? -4.774  2.303   -35.538 1.00 20.94  ? 333 ILE A CG2    1 
ATOM   5160 C  CD1    . ILE A 1 334 ? -6.227  0.776   -37.780 1.00 28.90  ? 333 ILE A CD1    1 
ATOM   5161 H  H      . ILE A 1 334 ? -2.282  -0.951  -36.180 1.00 24.78  ? 333 ILE A H      1 
ATOM   5162 H  HA     . ILE A 1 334 ? -2.318  1.734   -36.581 1.00 23.67  ? 333 ILE A HA     1 
ATOM   5163 H  HB     . ILE A 1 334 ? -4.566  0.261   -35.699 1.00 25.92  ? 333 ILE A HB     1 
ATOM   5164 H  HG12   . ILE A 1 334 ? -4.399  1.653   -38.148 1.00 32.32  ? 333 ILE A HG12   1 
ATOM   5165 H  HG13   . ILE A 1 334 ? -4.305  0.073   -38.025 1.00 32.32  ? 333 ILE A HG13   1 
ATOM   5166 H  HG21   . ILE A 1 334 ? -5.741  2.304   -35.614 1.00 25.15  ? 333 ILE A HG21   1 
ATOM   5167 H  HG22   . ILE A 1 334 ? -4.515  2.316   -34.603 1.00 25.15  ? 333 ILE A HG22   1 
ATOM   5168 H  HG23   . ILE A 1 334 ? -4.405  3.076   -35.994 1.00 25.15  ? 333 ILE A HG23   1 
ATOM   5169 H  HD11   . ILE A 1 334 ? -6.456  0.690   -38.719 1.00 34.70  ? 333 ILE A HD11   1 
ATOM   5170 H  HD12   . ILE A 1 334 ? -6.536  -0.002  -37.291 1.00 34.70  ? 333 ILE A HD12   1 
ATOM   5171 H  HD13   . ILE A 1 334 ? -6.629  1.579   -37.414 1.00 34.70  ? 333 ILE A HD13   1 
ATOM   5172 N  N      . VAL A 1 335 ? -1.721  2.240   -34.233 1.00 21.53  ? 334 VAL A N      1 
ATOM   5173 C  CA     . VAL A 1 335 ? -1.562  2.601   -32.827 1.00 22.38  ? 334 VAL A CA     1 
ATOM   5174 C  C      . VAL A 1 335 ? -2.432  3.818   -32.584 1.00 21.66  ? 334 VAL A C      1 
ATOM   5175 O  O      . VAL A 1 335 ? -2.296  4.818   -33.288 1.00 23.68  ? 334 VAL A O      1 
ATOM   5176 C  CB     . VAL A 1 335 ? -0.101  2.908   -32.440 1.00 27.56  ? 334 VAL A CB     1 
ATOM   5177 C  CG1    . VAL A 1 335 ? -0.001  3.489   -31.008 1.00 26.12  ? 334 VAL A CG1    1 
ATOM   5178 C  CG2    . VAL A 1 335 ? 0.741   1.665   -32.522 1.00 33.20  ? 334 VAL A CG2    1 
ATOM   5179 H  H      . VAL A 1 335 ? -1.454  2.853   -34.774 1.00 25.86  ? 334 VAL A H      1 
ATOM   5180 H  HA     . VAL A 1 335 ? -1.883  1.876   -32.267 1.00 26.88  ? 334 VAL A HA     1 
ATOM   5181 H  HB     . VAL A 1 335 ? 0.262   3.562   -33.059 1.00 33.10  ? 334 VAL A HB     1 
ATOM   5182 H  HG11   . VAL A 1 335 ? 0.931   3.668   -30.804 1.00 31.36  ? 334 VAL A HG11   1 
ATOM   5183 H  HG12   . VAL A 1 335 ? -0.513  4.311   -30.964 1.00 31.36  ? 334 VAL A HG12   1 
ATOM   5184 H  HG13   . VAL A 1 335 ? -0.359  2.842   -30.379 1.00 31.36  ? 334 VAL A HG13   1 
ATOM   5185 H  HG21   . VAL A 1 335 ? 1.653   1.884   -32.275 1.00 39.85  ? 334 VAL A HG21   1 
ATOM   5186 H  HG22   . VAL A 1 335 ? 0.383   1.001   -31.912 1.00 39.85  ? 334 VAL A HG22   1 
ATOM   5187 H  HG23   . VAL A 1 335 ? 0.716   1.327   -33.431 1.00 39.85  ? 334 VAL A HG23   1 
ATOM   5188 N  N      . TRP A 1 336 ? -3.314  3.733   -31.584 1.00 19.69  ? 335 TRP A N      1 
ATOM   5189 C  CA     . TRP A 1 336 ? -4.278  4.789   -31.291 1.00 18.03  ? 335 TRP A CA     1 
ATOM   5190 C  C      . TRP A 1 336 ? -4.112  5.224   -29.841 1.00 18.85  ? 335 TRP A C      1 
ATOM   5191 O  O      . TRP A 1 336 ? -4.247  4.397   -28.928 1.00 18.49  ? 335 TRP A O      1 
ATOM   5192 C  CB     . TRP A 1 336 ? -5.696  4.268   -31.557 1.00 17.44  ? 335 TRP A CB     1 
ATOM   5193 C  CG     . TRP A 1 336 ? -6.817  5.207   -31.220 1.00 18.71  ? 335 TRP A CG     1 
ATOM   5194 C  CD1    . TRP A 1 336 ? -6.720  6.529   -30.921 1.00 19.33  ? 335 TRP A CD1    1 
ATOM   5195 C  CD2    . TRP A 1 336 ? -8.214  4.893   -31.228 1.00 20.30  ? 335 TRP A CD2    1 
ATOM   5196 N  NE1    . TRP A 1 336 ? -7.978  7.068   -30.744 1.00 20.23  ? 335 TRP A NE1    1 
ATOM   5197 C  CE2    . TRP A 1 336 ? -8.910  6.074   -30.918 1.00 22.38  ? 335 TRP A CE2    1 
ATOM   5198 C  CE3    . TRP A 1 336 ? -8.945  3.718   -31.468 1.00 24.21  ? 335 TRP A CE3    1 
ATOM   5199 C  CZ2    . TRP A 1 336 ? -10.306 6.113   -30.825 1.00 27.74  ? 335 TRP A CZ2    1 
ATOM   5200 C  CZ3    . TRP A 1 336 ? -10.312 3.753   -31.362 1.00 24.89  ? 335 TRP A CZ3    1 
ATOM   5201 C  CH2    . TRP A 1 336 ? -10.987 4.941   -31.053 1.00 27.10  ? 335 TRP A CH2    1 
ATOM   5202 H  H      . TRP A 1 336 ? -3.371  3.059   -31.053 1.00 23.65  ? 335 TRP A H      1 
ATOM   5203 H  HA     . TRP A 1 336 ? -4.114  5.552   -31.866 1.00 21.65  ? 335 TRP A HA     1 
ATOM   5204 H  HB2    . TRP A 1 336 ? -5.771  4.056   -32.501 1.00 20.95  ? 335 TRP A HB2    1 
ATOM   5205 H  HB3    . TRP A 1 336 ? -5.828  3.462   -31.034 1.00 20.95  ? 335 TRP A HB3    1 
ATOM   5206 H  HD1    . TRP A 1 336 ? -5.924  7.009   -30.876 1.00 23.22  ? 335 TRP A HD1    1 
ATOM   5207 H  HE1    . TRP A 1 336 ? -8.149  7.884   -30.535 1.00 24.30  ? 335 TRP A HE1    1 
ATOM   5208 H  HE3    . TRP A 1 336 ? -8.508  2.924   -31.677 1.00 29.07  ? 335 TRP A HE3    1 
ATOM   5209 H  HZ2    . TRP A 1 336 ? -10.754 6.898   -30.607 1.00 33.31  ? 335 TRP A HZ2    1 
ATOM   5210 H  HZ3    . TRP A 1 336 ? -10.802 2.979   -31.523 1.00 29.89  ? 335 TRP A HZ3    1 
ATOM   5211 H  HH2    . TRP A 1 336 ? -11.915 4.936   -30.995 1.00 32.54  ? 335 TRP A HH2    1 
ATOM   5212 N  N      . ASN A 1 337 ? -3.806  6.515   -29.630 1.00 20.15  ? 336 ASN A N      1 
ATOM   5213 C  CA     . ASN A 1 337 ? -3.771  7.126   -28.305 1.00 20.26  ? 336 ASN A CA     1 
ATOM   5214 C  C      . ASN A 1 337 ? -4.576  8.411   -28.363 1.00 21.47  ? 336 ASN A C      1 
ATOM   5215 O  O      . ASN A 1 337 ? -4.210  9.341   -29.092 1.00 22.92  ? 336 ASN A O      1 
ATOM   5216 C  CB     . ASN A 1 337 ? -2.362  7.450   -27.810 1.00 22.17  ? 336 ASN A CB     1 
ATOM   5217 C  CG     . ASN A 1 337 ? -2.390  8.225   -26.514 1.00 23.24  ? 336 ASN A CG     1 
ATOM   5218 O  OD1    . ASN A 1 337 ? -1.830  9.320   -26.407 1.00 24.20  ? 336 ASN A OD1    1 
ATOM   5219 N  ND2    . ASN A 1 337 ? -3.067  7.665   -25.512 1.00 20.50  ? 336 ASN A ND2    1 
ATOM   5220 H  H      . ASN A 1 337 ? -3.610  7.066   -30.261 1.00 24.20  ? 336 ASN A H      1 
ATOM   5221 H  HA     . ASN A 1 337 ? -4.191  6.530   -27.665 1.00 24.33  ? 336 ASN A HA     1 
ATOM   5222 H  HB2    . ASN A 1 337 ? -1.879  6.623   -27.659 1.00 26.63  ? 336 ASN A HB2    1 
ATOM   5223 H  HB3    . ASN A 1 337 ? -1.906  7.988   -28.476 1.00 26.63  ? 336 ASN A HB3    1 
ATOM   5224 H  HD21   . ASN A 1 337 ? -3.115  8.063   -24.751 1.00 24.61  ? 336 ASN A HD21   1 
ATOM   5225 H  HD22   . ASN A 1 337 ? -3.455  6.906   -25.626 1.00 24.61  ? 336 ASN A HD22   1 
ATOM   5226 N  N      . GLY A 1 338 ? -5.683  8.437   -27.627 1.00 23.77  ? 337 GLY A N      1 
ATOM   5227 C  CA     . GLY A 1 338 ? -6.429  9.656   -27.428 1.00 22.71  ? 337 GLY A CA     1 
ATOM   5228 C  C      . GLY A 1 338 ? -7.768  9.628   -28.141 1.00 20.95  ? 337 GLY A C      1 
ATOM   5229 O  O      . GLY A 1 338 ? -7.834  9.546   -29.370 1.00 23.28  ? 337 GLY A O      1 
ATOM   5230 H  H      . GLY A 1 338 ? -6.019  7.751   -27.232 1.00 28.54  ? 337 GLY A H      1 
ATOM   5231 H  HA2    . GLY A 1 338 ? -6.587  9.789   -26.481 1.00 27.27  ? 337 GLY A HA2    1 
ATOM   5232 H  HA3    . GLY A 1 338 ? -5.917  10.408  -27.764 1.00 27.27  ? 337 GLY A HA3    1 
ATOM   5233 N  N      . PRO A 1 339 ? -8.869  9.694   -27.387 1.00 21.03  ? 338 PRO A N      1 
ATOM   5234 C  CA     . PRO A 1 339 ? -10.187 9.729   -28.020 1.00 21.18  ? 338 PRO A CA     1 
ATOM   5235 C  C      . PRO A 1 339 ? -10.307 10.955  -28.892 1.00 22.34  ? 338 PRO A C      1 
ATOM   5236 O  O      . PRO A 1 339 ? -9.690  11.983  -28.610 1.00 24.42  ? 338 PRO A O      1 
ATOM   5237 C  CB     . PRO A 1 339 ? -11.162 9.806   -26.835 1.00 24.98  ? 338 PRO A CB     1 
ATOM   5238 C  CG     . PRO A 1 339 ? -10.369 9.451   -25.638 1.00 27.04  ? 338 PRO A CG     1 
ATOM   5239 C  CD     . PRO A 1 339 ? -8.967  9.847   -25.924 1.00 24.36  ? 338 PRO A CD     1 
ATOM   5240 H  HA     . PRO A 1 339 ? -10.351 8.926   -28.540 1.00 25.43  ? 338 PRO A HA     1 
ATOM   5241 H  HB2    . PRO A 1 339 ? -11.511 10.708  -26.759 1.00 30.00  ? 338 PRO A HB2    1 
ATOM   5242 H  HB3    . PRO A 1 339 ? -11.884 9.171   -26.966 1.00 30.00  ? 338 PRO A HB3    1 
ATOM   5243 H  HG2    . PRO A 1 339 ? -10.708 9.938   -24.871 1.00 32.46  ? 338 PRO A HG2    1 
ATOM   5244 H  HG3    . PRO A 1 339 ? -10.426 8.495   -25.485 1.00 32.46  ? 338 PRO A HG3    1 
ATOM   5245 H  HD2    . PRO A 1 339 ? -8.817  10.770  -25.669 1.00 29.25  ? 338 PRO A HD2    1 
ATOM   5246 H  HD3    . PRO A 1 339 ? -8.348  9.248   -25.478 1.00 29.25  ? 338 PRO A HD3    1 
ATOM   5247 N  N      . VAL A 1 340 ? -11.155 10.862  -29.926 1.00 22.21  ? 339 VAL A N      1 
ATOM   5248 C  CA     . VAL A 1 340 ? -11.293 11.948  -30.902 1.00 24.01  ? 339 VAL A CA     1 
ATOM   5249 C  C      . VAL A 1 340 ? -12.455 12.862  -30.531 1.00 25.25  ? 339 VAL A C      1 
ATOM   5250 O  O      . VAL A 1 340 ? -12.806 13.792  -31.272 1.00 27.21  ? 339 VAL A O      1 
ATOM   5251 C  CB     . VAL A 1 340 ? -11.425 11.394  -32.341 1.00 26.95  ? 339 VAL A CB     1 
ATOM   5252 C  CG1    . VAL A 1 340 ? -10.164 10.606  -32.690 1.00 27.10  ? 339 VAL A CG1    1 
ATOM   5253 C  CG2    . VAL A 1 340 ? -12.700 10.551  -32.528 1.00 26.58  ? 339 VAL A CG2    1 
ATOM   5254 H  H      . VAL A 1 340 ? -11.658 10.183  -30.083 1.00 26.67  ? 339 VAL A H      1 
ATOM   5255 H  HA     . VAL A 1 340 ? -10.485 12.485  -30.875 1.00 28.84  ? 339 VAL A HA     1 
ATOM   5256 H  HB     . VAL A 1 340 ? -11.480 12.143  -32.955 1.00 32.36  ? 339 VAL A HB     1 
ATOM   5257 H  HG11   . VAL A 1 340 ? -10.248 10.260  -33.592 1.00 32.54  ? 339 VAL A HG11   1 
ATOM   5258 H  HG12   . VAL A 1 340 ? -9.397  11.198  -32.632 1.00 32.54  ? 339 VAL A HG12   1 
ATOM   5259 H  HG13   . VAL A 1 340 ? -10.066 9.874   -32.061 1.00 32.54  ? 339 VAL A HG13   1 
ATOM   5260 H  HG21   . VAL A 1 340 ? -12.734 10.229  -33.442 1.00 31.92  ? 339 VAL A HG21   1 
ATOM   5261 H  HG22   . VAL A 1 340 ? -12.674 9.800   -31.914 1.00 31.92  ? 339 VAL A HG22   1 
ATOM   5262 H  HG23   . VAL A 1 340 ? -13.474 11.105  -32.342 1.00 31.92  ? 339 VAL A HG23   1 
ATOM   5263 N  N      . GLY A 1 341 ? -13.026 12.640  -29.356 1.00 21.85  ? 340 GLY A N      1 
ATOM   5264 C  CA     . GLY A 1 341 ? -13.972 13.564  -28.760 1.00 20.09  ? 340 GLY A CA     1 
ATOM   5265 C  C      . GLY A 1 341 ? -14.082 13.287  -27.273 1.00 21.69  ? 340 GLY A C      1 
ATOM   5266 O  O      . GLY A 1 341 ? -13.427 12.393  -26.731 1.00 21.55  ? 340 GLY A O      1 
ATOM   5267 H  H      . GLY A 1 341 ? -12.877 11.943  -28.874 1.00 26.24  ? 340 GLY A H      1 
ATOM   5268 H  HA2    . GLY A 1 341 ? -13.672 14.477  -28.891 1.00 24.12  ? 340 GLY A HA2    1 
ATOM   5269 H  HA3    . GLY A 1 341 ? -14.845 13.456  -29.168 1.00 24.12  ? 340 GLY A HA3    1 
ATOM   5270 N  N      . VAL A 1 342 ? -14.906 14.093  -26.594 1.00 22.68  ? 341 VAL A N      1 
ATOM   5271 C  CA     . VAL A 1 342 ? -15.121 13.935  -25.157 1.00 23.75  ? 341 VAL A CA     1 
ATOM   5272 C  C      . VAL A 1 342 ? -16.105 12.785  -24.944 1.00 24.21  ? 341 VAL A C      1 
ATOM   5273 O  O      . VAL A 1 342 ? -17.298 12.983  -24.670 1.00 24.61  ? 341 VAL A O      1 
ATOM   5274 C  CB     . VAL A 1 342 ? -15.601 15.249  -24.512 1.00 24.77  ? 341 VAL A CB     1 
ATOM   5275 C  CG1    . VAL A 1 342 ? -15.791 15.083  -22.986 1.00 26.79  ? 341 VAL A CG1    1 
ATOM   5276 C  CG2    . VAL A 1 342 ? -14.583 16.350  -24.793 1.00 22.43  ? 341 VAL A CG2    1 
ATOM   5277 H  H      . VAL A 1 342 ? -15.352 14.738  -26.946 1.00 27.24  ? 341 VAL A H      1 
ATOM   5278 H  HA     . VAL A 1 342 ? -14.281 13.689  -24.739 1.00 28.52  ? 341 VAL A HA     1 
ATOM   5279 H  HB     . VAL A 1 342 ? -16.451 15.509  -24.901 1.00 29.74  ? 341 VAL A HB     1 
ATOM   5280 H  HG11   . VAL A 1 342 ? -16.093 15.925  -22.612 1.00 32.17  ? 341 VAL A HG11   1 
ATOM   5281 H  HG12   . VAL A 1 342 ? -16.453 14.392  -22.824 1.00 32.17  ? 341 VAL A HG12   1 
ATOM   5282 H  HG13   . VAL A 1 342 ? -14.943 14.829  -22.589 1.00 32.17  ? 341 VAL A HG13   1 
ATOM   5283 H  HG21   . VAL A 1 342 ? -14.890 17.175  -24.385 1.00 26.94  ? 341 VAL A HG21   1 
ATOM   5284 H  HG22   . VAL A 1 342 ? -13.728 16.092  -24.416 1.00 26.94  ? 341 VAL A HG22   1 
ATOM   5285 H  HG23   . VAL A 1 342 ? -14.501 16.466  -25.753 1.00 26.94  ? 341 VAL A HG23   1 
ATOM   5286 N  N      . PHE A 1 343 ? -15.600 11.564  -25.088 1.00 25.63  ? 342 PHE A N      1 
ATOM   5287 C  CA     . PHE A 1 343 ? -16.442 10.380  -25.145 1.00 28.68  ? 342 PHE A CA     1 
ATOM   5288 C  C      . PHE A 1 343 ? -17.102 10.068  -23.809 1.00 31.33  ? 342 PHE A C      1 
ATOM   5289 O  O      . PHE A 1 343 ? -18.042 9.266   -23.789 1.00 30.71  ? 342 PHE A O      1 
ATOM   5290 C  CB     . PHE A 1 343 ? -15.602 9.180   -25.606 1.00 28.34  ? 342 PHE A CB     1 
ATOM   5291 C  CG     . PHE A 1 343 ? -14.813 8.567   -24.495 1.00 28.69  ? 342 PHE A CG     1 
ATOM   5292 C  CD1    . PHE A 1 343 ? -13.609 9.132   -24.082 1.00 30.43  ? 342 PHE A CD1    1 
ATOM   5293 C  CD2    . PHE A 1 343 ? -15.307 7.469   -23.790 1.00 32.38  ? 342 PHE A CD2    1 
ATOM   5294 C  CE1    . PHE A 1 343 ? -12.907 8.601   -23.007 1.00 34.72  ? 342 PHE A CE1    1 
ATOM   5295 C  CE2    . PHE A 1 343 ? -14.597 6.939   -22.717 1.00 32.43  ? 342 PHE A CE2    1 
ATOM   5296 C  CZ     . PHE A 1 343 ? -13.389 7.502   -22.335 1.00 32.61  ? 342 PHE A CZ     1 
ATOM   5297 H  H      . PHE A 1 343 ? -14.760 11.395  -25.156 1.00 30.78  ? 342 PHE A H      1 
ATOM   5298 H  HA     . PHE A 1 343 ? -17.143 10.524  -25.799 1.00 34.43  ? 342 PHE A HA     1 
ATOM   5299 H  HB2    . PHE A 1 343 ? -16.193 8.500   -25.966 1.00 34.03  ? 342 PHE A HB2    1 
ATOM   5300 H  HB3    . PHE A 1 343 ? -14.979 9.474   -26.289 1.00 34.03  ? 342 PHE A HB3    1 
ATOM   5301 H  HD1    . PHE A 1 343 ? -13.274 9.877   -24.527 1.00 36.54  ? 342 PHE A HD1    1 
ATOM   5302 H  HD2    . PHE A 1 343 ? -16.118 7.088   -24.039 1.00 38.87  ? 342 PHE A HD2    1 
ATOM   5303 H  HE1    . PHE A 1 343 ? -12.095 8.977   -22.755 1.00 41.69  ? 342 PHE A HE1    1 
ATOM   5304 H  HE2    . PHE A 1 343 ? -14.926 6.196   -22.266 1.00 38.94  ? 342 PHE A HE2    1 
ATOM   5305 H  HZ     . PHE A 1 343 ? -12.910 7.142   -21.624 1.00 39.15  ? 342 PHE A HZ     1 
ATOM   5306 N  N      . GLU A 1 344 ? -16.639 10.685  -22.705 1.00 26.27  ? 343 GLU A N      1 
ATOM   5307 C  CA     . GLU A 1 344 ? -17.256 10.507  -21.401 1.00 26.81  ? 343 GLU A CA     1 
ATOM   5308 C  C      . GLU A 1 344 ? -18.663 11.067  -21.368 1.00 27.02  ? 343 GLU A C      1 
ATOM   5309 O  O      . GLU A 1 344 ? -19.464 10.679  -20.512 1.00 27.89  ? 343 GLU A O      1 
ATOM   5310 C  CB     . GLU A 1 344 ? -16.447 11.217  -20.312 1.00 27.92  ? 343 GLU A CB     1 
ATOM   5311 C  CG     . GLU A 1 344 ? -15.042 10.632  -20.107 1.00 31.58  ? 343 GLU A CG     1 
ATOM   5312 C  CD     . GLU A 1 344 ? -13.958 11.293  -20.948 1.00 36.01  ? 343 GLU A CD     1 
ATOM   5313 O  OE1    . GLU A 1 344 ? -14.299 11.931  -21.964 1.00 31.28  ? 343 GLU A OE1    1 
ATOM   5314 O  OE2    . GLU A 1 344 ? -12.755 11.160  -20.571 1.00 33.01  1 343 GLU A OE2    1 
ATOM   5315 H  H      . GLU A 1 344 ? -15.961 11.214  -22.697 1.00 31.55  ? 343 GLU A H      1 
ATOM   5316 H  HA     . GLU A 1 344 ? -17.295 9.561   -21.187 1.00 32.19  ? 343 GLU A HA     1 
ATOM   5317 H  HB2    . GLU A 1 344 ? -16.347 12.151  -20.556 1.00 33.52  ? 343 GLU A HB2    1 
ATOM   5318 H  HB3    . GLU A 1 344 ? -16.924 11.146  -19.471 1.00 33.52  ? 343 GLU A HB3    1 
ATOM   5319 H  HG2    . GLU A 1 344 ? -14.796 10.736  -19.174 1.00 37.92  ? 343 GLU A HG2    1 
ATOM   5320 H  HG3    . GLU A 1 344 ? -15.061 9.690   -20.337 1.00 37.92  ? 343 GLU A HG3    1 
ATOM   5321 N  N      . TRP A 1 345 ? -18.953 11.999  -22.256 1.00 26.55  ? 344 TRP A N      1 
ATOM   5322 C  CA     . TRP A 1 345 ? -20.236 12.679  -22.318 1.00 27.45  ? 344 TRP A CA     1 
ATOM   5323 C  C      . TRP A 1 345 ? -20.945 12.272  -23.612 1.00 26.67  ? 344 TRP A C      1 
ATOM   5324 O  O      . TRP A 1 345 ? -20.419 12.485  -24.709 1.00 27.01  ? 344 TRP A O      1 
ATOM   5325 C  CB     . TRP A 1 345 ? -20.028 14.191  -22.269 1.00 31.20  ? 344 TRP A CB     1 
ATOM   5326 C  CG     . TRP A 1 345 ? -19.419 14.694  -21.009 1.00 33.87  ? 344 TRP A CG     1 
ATOM   5327 C  CD1    . TRP A 1 345 ? -19.372 14.056  -19.784 1.00 36.18  ? 344 TRP A CD1    1 
ATOM   5328 C  CD2    . TRP A 1 345 ? -18.780 15.958  -20.826 1.00 31.84  ? 344 TRP A CD2    1 
ATOM   5329 N  NE1    . TRP A 1 345 ? -18.723 14.853  -18.864 1.00 36.74  ? 344 TRP A NE1    1 
ATOM   5330 C  CE2    . TRP A 1 345 ? -18.348 16.022  -19.478 1.00 37.94  ? 344 TRP A CE2    1 
ATOM   5331 C  CE3    . TRP A 1 345 ? -18.526 17.042  -21.669 1.00 28.17  ? 344 TRP A CE3    1 
ATOM   5332 C  CZ2    . TRP A 1 345 ? -17.692 17.134  -18.960 1.00 36.13  ? 344 TRP A CZ2    1 
ATOM   5333 C  CZ3    . TRP A 1 345 ? -17.853 18.139  -21.160 1.00 33.81  ? 344 TRP A CZ3    1 
ATOM   5334 C  CH2    . TRP A 1 345 ? -17.444 18.175  -19.814 1.00 35.01  ? 344 TRP A CH2    1 
ATOM   5335 H  H      . TRP A 1 345 ? -18.401 12.267  -22.858 1.00 31.88  ? 344 TRP A H      1 
ATOM   5336 H  HA     . TRP A 1 345 ? -20.786 12.414  -21.563 1.00 32.96  ? 344 TRP A HA     1 
ATOM   5337 H  HB2    . TRP A 1 345 ? -19.442 14.447  -23.000 1.00 37.46  ? 344 TRP A HB2    1 
ATOM   5338 H  HB3    . TRP A 1 345 ? -20.888 14.626  -22.374 1.00 37.46  ? 344 TRP A HB3    1 
ATOM   5339 H  HD1    . TRP A 1 345 ? -19.714 13.209  -19.610 1.00 43.43  ? 344 TRP A HD1    1 
ATOM   5340 H  HE1    . TRP A 1 345 ? -18.579 14.652  -18.040 1.00 44.10  ? 344 TRP A HE1    1 
ATOM   5341 H  HE3    . TRP A 1 345 ? -18.789 17.021  -22.561 1.00 33.83  ? 344 TRP A HE3    1 
ATOM   5342 H  HZ2    . TRP A 1 345 ? -17.413 17.161  -18.073 1.00 43.38  ? 344 TRP A HZ2    1 
ATOM   5343 H  HZ3    . TRP A 1 345 ? -17.677 18.866  -21.712 1.00 40.60  ? 344 TRP A HZ3    1 
ATOM   5344 H  HH2    . TRP A 1 345 ? -17.000 18.927  -19.494 1.00 42.04  ? 344 TRP A HH2    1 
ATOM   5345 N  N      . GLU A 1 346 ? -22.166 11.746  -23.493 1.00 28.26  ? 345 GLU A N      1 
ATOM   5346 C  CA     . GLU A 1 346 ? -22.781 11.089  -24.648 1.00 31.64  ? 345 GLU A CA     1 
ATOM   5347 C  C      . GLU A 1 346 ? -22.972 12.032  -25.833 1.00 32.89  ? 345 GLU A C      1 
ATOM   5348 O  O      . GLU A 1 346 ? -22.880 11.598  -26.989 1.00 34.75  ? 345 GLU A O      1 
ATOM   5349 C  CB     . GLU A 1 346 ? -24.123 10.467  -24.241 1.00 35.67  ? 345 GLU A CB     1 
ATOM   5350 C  CG     . GLU A 1 346 ? -23.974 9.249   -23.363 1.00 42.84  ? 345 GLU A CG     1 
ATOM   5351 C  CD     . GLU A 1 346 ? -22.957 8.239   -23.930 1.00 51.14  ? 345 GLU A CD     1 
ATOM   5352 O  OE1    . GLU A 1 346 ? -22.971 7.961   -25.168 1.00 48.24  ? 345 GLU A OE1    1 
ATOM   5353 O  OE2    . GLU A 1 346 ? -22.129 7.749   -23.123 1.00 55.00  1 345 GLU A OE2    1 
ATOM   5354 H  H      . GLU A 1 346 ? -22.646 11.754  -22.779 1.00 33.93  ? 345 GLU A H      1 
ATOM   5355 H  HA     . GLU A 1 346 ? -22.199 10.368  -24.939 1.00 37.98  ? 345 GLU A HA     1 
ATOM   5356 H  HB2    . GLU A 1 346 ? -24.640 11.126  -23.752 1.00 42.83  ? 345 GLU A HB2    1 
ATOM   5357 H  HB3    . GLU A 1 346 ? -24.602 10.200  -25.042 1.00 42.83  ? 345 GLU A HB3    1 
ATOM   5358 H  HG2    . GLU A 1 346 ? -23.666 9.526   -22.486 1.00 51.43  ? 345 GLU A HG2    1 
ATOM   5359 H  HG3    . GLU A 1 346 ? -24.832 8.803   -23.290 1.00 51.43  ? 345 GLU A HG3    1 
ATOM   5360 N  N      . ALA A 1 347 ? -23.242 13.317  -25.581 1.00 30.95  ? 346 ALA A N      1 
ATOM   5361 C  CA     . ALA A 1 347 ? -23.406 14.252  -26.682 1.00 29.97  ? 346 ALA A CA     1 
ATOM   5362 C  C      . ALA A 1 347 ? -22.187 14.294  -27.588 1.00 29.79  ? 346 ALA A C      1 
ATOM   5363 O  O      . ALA A 1 347 ? -22.304 14.686  -28.758 1.00 30.74  ? 346 ALA A O      1 
ATOM   5364 C  CB     . ALA A 1 347 ? -23.684 15.648  -26.152 1.00 31.76  ? 346 ALA A CB     1 
ATOM   5365 H  H      . ALA A 1 347 ? -23.332 13.660  -24.798 1.00 37.16  ? 346 ALA A H      1 
ATOM   5366 H  HA     . ALA A 1 347 ? -24.167 13.978  -27.217 1.00 35.98  ? 346 ALA A HA     1 
ATOM   5367 H  HB1    . ALA A 1 347 ? -23.790 16.255  -26.901 1.00 38.13  ? 346 ALA A HB1    1 
ATOM   5368 H  HB2    . ALA A 1 347 ? -24.497 15.628  -25.624 1.00 38.13  ? 346 ALA A HB2    1 
ATOM   5369 H  HB3    . ALA A 1 347 ? -22.938 15.930  -25.600 1.00 38.13  ? 346 ALA A HB3    1 
ATOM   5370 N  N      . PHE A 1 348 ? -21.024 13.889  -27.071 1.00 26.14  ? 347 PHE A N      1 
ATOM   5371 C  CA     . PHE A 1 348 ? -19.750 14.108  -27.731 1.00 25.14  ? 347 PHE A CA     1 
ATOM   5372 C  C      . PHE A 1 348 ? -18.987 12.810  -27.913 1.00 25.23  ? 347 PHE A C      1 
ATOM   5373 O  O      . PHE A 1 348 ? -17.757 12.829  -28.056 1.00 24.72  ? 347 PHE A O      1 
ATOM   5374 C  CB     . PHE A 1 348 ? -18.921 15.107  -26.917 1.00 24.62  ? 347 PHE A CB     1 
ATOM   5375 C  CG     . PHE A 1 348 ? -19.685 16.346  -26.563 1.00 25.71  ? 347 PHE A CG     1 
ATOM   5376 C  CD1    . PHE A 1 348 ? -20.082 17.227  -27.546 1.00 25.39  ? 347 PHE A CD1    1 
ATOM   5377 C  CD2    . PHE A 1 348 ? -20.035 16.614  -25.247 1.00 29.05  ? 347 PHE A CD2    1 
ATOM   5378 C  CE1    . PHE A 1 348 ? -20.806 18.355  -27.237 1.00 28.52  ? 347 PHE A CE1    1 
ATOM   5379 C  CE2    . PHE A 1 348 ? -20.763 17.747  -24.921 1.00 30.61  ? 347 PHE A CE2    1 
ATOM   5380 C  CZ     . PHE A 1 348 ? -21.141 18.625  -25.920 1.00 31.89  ? 347 PHE A CZ     1 
ATOM   5381 H  H      . PHE A 1 348 ? -20.953 13.475  -26.320 1.00 31.39  ? 347 PHE A H      1 
ATOM   5382 H  HA     . PHE A 1 348 ? -19.908 14.491  -28.608 1.00 30.18  ? 347 PHE A HA     1 
ATOM   5383 H  HB2    . PHE A 1 348 ? -18.638 14.683  -26.091 1.00 29.56  ? 347 PHE A HB2    1 
ATOM   5384 H  HB3    . PHE A 1 348 ? -18.146 15.371  -27.437 1.00 29.56  ? 347 PHE A HB3    1 
ATOM   5385 H  HD1    . PHE A 1 348 ? -19.860 17.054  -28.432 1.00 30.37  ? 347 PHE A HD1    1 
ATOM   5386 H  HD2    . PHE A 1 348 ? -19.780 16.023  -24.575 1.00 34.87  ? 347 PHE A HD2    1 
ATOM   5387 H  HE1    . PHE A 1 348 ? -21.058 18.944  -27.911 1.00 34.24  ? 347 PHE A HE1    1 
ATOM   5388 H  HE2    . PHE A 1 348 ? -20.986 17.922  -24.035 1.00 36.76  ? 347 PHE A HE2    1 
ATOM   5389 H  HZ     . PHE A 1 348 ? -21.628 19.389  -25.710 1.00 38.29  ? 347 PHE A HZ     1 
ATOM   5390 N  N      . ALA A 1 349 ? -19.694 11.684  -27.911 1.00 24.77  ? 348 ALA A N      1 
ATOM   5391 C  CA     . ALA A 1 349 ? -19.061 10.375  -27.985 1.00 23.97  ? 348 ALA A CA     1 
ATOM   5392 C  C      . ALA A 1 349 ? -19.186 9.686   -29.340 1.00 24.44  ? 348 ALA A C      1 
ATOM   5393 O  O      . ALA A 1 349 ? -18.547 8.654   -29.540 1.00 25.85  ? 348 ALA A O      1 
ATOM   5394 C  CB     . ALA A 1 349 ? -19.668 9.443   -26.944 1.00 24.09  ? 348 ALA A CB     1 
ATOM   5395 H  H      . ALA A 1 349 ? -20.552 11.653  -27.867 1.00 29.74  ? 348 ALA A H      1 
ATOM   5396 H  HA     . ALA A 1 349 ? -18.117 10.472  -27.785 1.00 28.78  ? 348 ALA A HA     1 
ATOM   5397 H  HB1    . ALA A 1 349 ? -19.236 8.577   -27.006 1.00 28.93  ? 348 ALA A HB1    1 
ATOM   5398 H  HB2    . ALA A 1 349 ? -19.527 9.821   -26.062 1.00 28.93  ? 348 ALA A HB2    1 
ATOM   5399 H  HB3    . ALA A 1 349 ? -20.618 9.353   -27.117 1.00 28.93  ? 348 ALA A HB3    1 
ATOM   5400 N  N      . ARG A 1 350 ? -19.998 10.203  -30.261 1.00 25.98  ? 349 ARG A N      1 
ATOM   5401 C  CA     A ARG A 1 350 ? -20.298 9.462   -31.489 0.52 31.86  ? 349 ARG A CA     1 
ATOM   5402 C  CA     B ARG A 1 350 ? -20.299 9.463   -31.489 0.48 31.88  ? 349 ARG A CA     1 
ATOM   5403 C  C      . ARG A 1 350 ? -19.061 9.253   -32.356 1.00 27.10  ? 349 ARG A C      1 
ATOM   5404 O  O      . ARG A 1 350 ? -18.874 8.171   -32.933 1.00 25.89  ? 349 ARG A O      1 
ATOM   5405 C  CB     A ARG A 1 350 ? -21.375 10.194  -32.288 0.52 42.59  ? 349 ARG A CB     1 
ATOM   5406 C  CB     B ARG A 1 350 ? -21.379 10.195  -32.288 0.48 42.60  ? 349 ARG A CB     1 
ATOM   5407 C  CG     A ARG A 1 350 ? -22.632 10.474  -31.511 0.52 54.35  ? 349 ARG A CG     1 
ATOM   5408 C  CG     B ARG A 1 350 ? -22.663 10.456  -31.529 0.48 54.39  ? 349 ARG A CG     1 
ATOM   5409 C  CD     A ARG A 1 350 ? -23.653 11.193  -32.379 0.52 63.68  ? 349 ARG A CD     1 
ATOM   5410 C  CD     B ARG A 1 350 ? -23.766 10.937  -32.473 0.48 64.35  ? 349 ARG A CD     1 
ATOM   5411 N  NE     A ARG A 1 350 ? -24.110 10.360  -33.484 0.52 67.13  ? 349 ARG A NE     1 
ATOM   5412 N  NE     B ARG A 1 350 ? -24.131 12.342  -32.273 0.48 68.83  ? 349 ARG A NE     1 
ATOM   5413 C  CZ     A ARG A 1 350 ? -24.892 9.299   -33.333 0.52 69.97  ? 349 ARG A CZ     1 
ATOM   5414 C  CZ     B ARG A 1 350 ? -23.490 13.381  -32.804 0.48 67.74  ? 349 ARG A CZ     1 
ATOM   5415 N  NH1    A ARG A 1 350 ? -25.289 8.932   -32.118 0.52 72.06  1 349 ARG A NH1    1 
ATOM   5416 N  NH1    B ARG A 1 350 ? -22.426 13.196  -33.570 0.48 66.04  1 349 ARG A NH1    1 
ATOM   5417 N  NH2    A ARG A 1 350 ? -25.271 8.597   -34.392 0.52 71.38  ? 349 ARG A NH2    1 
ATOM   5418 N  NH2    B ARG A 1 350 ? -23.920 14.614  -32.566 0.48 66.93  ? 349 ARG A NH2    1 
ATOM   5419 H  H      . ARG A 1 350 ? -20.384 10.969  -30.204 1.00 31.19  ? 349 ARG A H      1 
ATOM   5420 H  HA     . ARG A 1 350 ? -20.646 8.589   -31.251 1.00 38.27  ? 349 ARG A HA     1 
ATOM   5421 H  HB2    A ARG A 1 350 ? -21.018 11.045  -32.587 0.52 51.13  ? 349 ARG A HB2    1 
ATOM   5422 H  HB2    B ARG A 1 350 ? -21.026 11.053  -32.571 0.48 51.14  ? 349 ARG A HB2    1 
ATOM   5423 H  HB3    A ARG A 1 350 ? -21.617 9.652   -33.055 0.52 51.13  ? 349 ARG A HB3    1 
ATOM   5424 H  HB3    B ARG A 1 350 ? -21.602 9.662   -33.067 0.48 51.14  ? 349 ARG A HB3    1 
ATOM   5425 H  HG2    A ARG A 1 350 ? -23.020 9.636   -31.212 0.52 65.23  ? 349 ARG A HG2    1 
ATOM   5426 H  HG2    B ARG A 1 350 ? -22.959 9.635   -31.106 0.48 65.29  ? 349 ARG A HG2    1 
ATOM   5427 H  HG3    A ARG A 1 350 ? -22.423 11.039  -30.751 0.52 65.23  ? 349 ARG A HG3    1 
ATOM   5428 H  HG3    B ARG A 1 350 ? -22.509 11.144  -30.863 0.48 65.29  ? 349 ARG A HG3    1 
ATOM   5429 H  HD2    A ARG A 1 350 ? -24.423 11.427  -31.837 0.52 76.44  ? 349 ARG A HD2    1 
ATOM   5430 H  HD2    B ARG A 1 350 ? -23.462 10.836  -33.389 0.48 77.23  ? 349 ARG A HD2    1 
ATOM   5431 H  HD3    A ARG A 1 350 ? -23.248 11.993  -32.749 0.52 76.44  ? 349 ARG A HD3    1 
ATOM   5432 H  HD3    B ARG A 1 350 ? -24.560 10.400  -32.328 0.48 77.23  ? 349 ARG A HD3    1 
ATOM   5433 H  HE     A ARG A 1 350 ? -23.774 10.505  -34.263 0.52 80.57  ? 349 ARG A HE     1 
ATOM   5434 H  HE     B ARG A 1 350 ? -24.811 12.508  -31.773 0.48 82.61  ? 349 ARG A HE     1 
ATOM   5435 H  HH11   A ARG A 1 350 ? -25.045 9.387   -31.431 0.52 86.50  ? 349 ARG A HH11   1 
ATOM   5436 H  HH11   B ARG A 1 350 ? -22.145 12.399  -33.731 0.48 79.26  ? 349 ARG A HH11   1 
ATOM   5437 H  HH12   A ARG A 1 350 ? -25.794 8.243   -32.021 0.52 86.50  ? 349 ARG A HH12   1 
ATOM   5438 H  HH12   B ARG A 1 350 ? -22.016 13.873  -33.908 0.48 79.26  ? 349 ARG A HH12   1 
ATOM   5439 H  HH21   A ARG A 1 350 ? -25.012 8.832   -35.178 0.52 85.67  ? 349 ARG A HH21   1 
ATOM   5440 H  HH21   B ARG A 1 350 ? -24.608 14.741  -32.067 0.48 80.33  ? 349 ARG A HH21   1 
ATOM   5441 H  HH22   A ARG A 1 350 ? -25.773 7.906   -34.293 0.52 85.67  ? 349 ARG A HH22   1 
ATOM   5442 H  HH22   B ARG A 1 350 ? -23.503 15.287  -32.903 0.48 80.33  ? 349 ARG A HH22   1 
ATOM   5443 N  N      . GLY A 1 351 ? -18.226 10.284  -32.511 1.00 28.02  ? 350 GLY A N      1 
ATOM   5444 C  CA     . GLY A 1 351 ? -17.022 10.133  -33.320 1.00 30.02  ? 350 GLY A CA     1 
ATOM   5445 C  C      . GLY A 1 351 ? -16.079 9.068   -32.797 1.00 27.70  ? 350 GLY A C      1 
ATOM   5446 O  O      . GLY A 1 351 ? -15.497 8.296   -33.573 1.00 25.01  ? 350 GLY A O      1 
ATOM   5447 H  H      . GLY A 1 351 ? -18.334 11.064  -32.165 1.00 33.65  ? 350 GLY A H      1 
ATOM   5448 H  HA2    . GLY A 1 351 ? -17.273 9.899   -34.227 1.00 36.04  ? 350 GLY A HA2    1 
ATOM   5449 H  HA3    . GLY A 1 351 ? -16.544 10.977  -33.344 1.00 36.04  ? 350 GLY A HA3    1 
ATOM   5450 N  N      . THR A 1 352 ? -15.890 9.015   -31.470 1.00 22.23  ? 351 THR A N      1 
ATOM   5451 C  CA     . THR A 1 352 ? -15.007 7.994   -30.927 1.00 20.66  ? 351 THR A CA     1 
ATOM   5452 C  C      . THR A 1 352 ? -15.623 6.610   -31.086 1.00 21.99  ? 351 THR A C      1 
ATOM   5453 O  O      . THR A 1 352 ? -14.920 5.643   -31.392 1.00 24.22  ? 351 THR A O      1 
ATOM   5454 C  CB     . THR A 1 352 ? -14.667 8.299   -29.460 1.00 22.81  ? 351 THR A CB     1 
ATOM   5455 O  OG1    . THR A 1 352 ? -14.012 9.570   -29.377 1.00 23.37  ? 351 THR A OG1    1 
ATOM   5456 C  CG2    . THR A 1 352 ? -13.700 7.299   -28.921 1.00 23.17  ? 351 THR A CG2    1 
ATOM   5457 H  H      . THR A 1 352 ? -16.249 9.540   -30.891 1.00 26.70  ? 351 THR A H      1 
ATOM   5458 H  HA     . THR A 1 352 ? -14.177 8.005   -31.428 1.00 24.70  ? 351 THR A HA     1 
ATOM   5459 H  HB     . THR A 1 352 ? -15.471 8.297   -28.917 1.00 27.40  ? 351 THR A HB     1 
ATOM   5460 H  HG1    . THR A 1 352 ? -14.516 10.173  -29.675 1.00 28.06  ? 351 THR A HG1    1 
ATOM   5461 H  HG21   . THR A 1 352 ? -13.494 7.503   -27.996 1.00 27.82  ? 351 THR A HG21   1 
ATOM   5462 H  HG22   . THR A 1 352 ? -14.083 6.409   -28.971 1.00 27.82  ? 351 THR A HG22   1 
ATOM   5463 H  HG23   . THR A 1 352 ? -12.880 7.319   -29.439 1.00 27.82  ? 351 THR A HG23   1 
ATOM   5464 N  N      . LYS A 1 353 ? -16.933 6.488   -30.899 1.00 23.80  ? 352 LYS A N      1 
ATOM   5465 C  CA     . LYS A 1 353 ? -17.576 5.185   -31.063 1.00 25.13  ? 352 LYS A CA     1 
ATOM   5466 C  C      . LYS A 1 353 ? -17.494 4.712   -32.512 1.00 27.94  ? 352 LYS A C      1 
ATOM   5467 O  O      . LYS A 1 353 ? -17.247 3.527   -32.778 1.00 27.26  ? 352 LYS A O      1 
ATOM   5468 C  CB     . LYS A 1 353 ? -19.024 5.287   -30.595 1.00 28.60  ? 352 LYS A CB     1 
ATOM   5469 C  CG     . LYS A 1 353 ? -19.907 4.066   -30.853 1.00 36.26  ? 352 LYS A CG     1 
ATOM   5470 C  CD     . LYS A 1 353 ? -19.292 2.811   -30.314 1.00 42.80  ? 352 LYS A CD     1 
ATOM   5471 C  CE     . LYS A 1 353 ? -20.308 1.657   -30.247 1.00 53.48  ? 352 LYS A CE     1 
ATOM   5472 N  NZ     . LYS A 1 353 ? -20.815 1.253   -31.590 1.00 59.78  1 352 LYS A NZ     1 
ATOM   5473 H  H      . LYS A 1 353 ? -17.464 7.128   -30.680 1.00 28.57  ? 352 LYS A H      1 
ATOM   5474 H  HA     . LYS A 1 353 ? -17.123 4.533   -30.506 1.00 30.17  ? 352 LYS A HA     1 
ATOM   5475 H  HB2    . LYS A 1 353 ? -19.024 5.445   -29.638 1.00 34.34  ? 352 LYS A HB2    1 
ATOM   5476 H  HB3    . LYS A 1 353 ? -19.437 6.041   -31.045 1.00 34.34  ? 352 LYS A HB3    1 
ATOM   5477 H  HG2    . LYS A 1 353 ? -20.765 4.195   -30.417 1.00 43.53  ? 352 LYS A HG2    1 
ATOM   5478 H  HG3    . LYS A 1 353 ? -20.030 3.958   -31.809 1.00 43.53  ? 352 LYS A HG3    1 
ATOM   5479 H  HD2    . LYS A 1 353 ? -18.563 2.539   -30.893 1.00 51.37  ? 352 LYS A HD2    1 
ATOM   5480 H  HD3    . LYS A 1 353 ? -18.963 2.977   -29.417 1.00 51.37  ? 352 LYS A HD3    1 
ATOM   5481 H  HE2    . LYS A 1 353 ? -19.882 0.885   -29.843 1.00 64.20  ? 352 LYS A HE2    1 
ATOM   5482 H  HE3    . LYS A 1 353 ? -21.067 1.936   -29.711 1.00 64.20  ? 352 LYS A HE3    1 
ATOM   5483 H  HZ1    . LYS A 1 353 ? -21.398 0.585   -31.506 1.00 71.76  ? 352 LYS A HZ1    1 
ATOM   5484 H  HZ2    . LYS A 1 353 ? -21.220 1.942   -31.982 1.00 71.76  ? 352 LYS A HZ2    1 
ATOM   5485 H  HZ3    . LYS A 1 353 ? -20.139 0.984   -32.102 1.00 71.76  ? 352 LYS A HZ3    1 
ATOM   5486 N  N      . ALA A 1 354 ? -17.696 5.630   -33.456 1.00 29.41  ? 353 ALA A N      1 
ATOM   5487 C  CA     . ALA A 1 354 ? -17.611 5.284   -34.875 1.00 32.24  ? 353 ALA A CA     1 
ATOM   5488 C  C      . ALA A 1 354 ? -16.212 4.809   -35.235 1.00 27.72  ? 353 ALA A C      1 
ATOM   5489 O  O      . ALA A 1 354 ? -16.050 3.825   -35.961 1.00 27.06  ? 353 ALA A O      1 
ATOM   5490 C  CB     . ALA A 1 354 ? -18.009 6.494   -35.722 1.00 34.12  ? 353 ALA A CB     1 
ATOM   5491 H  H      . ALA A 1 354 ? -17.882 6.455   -33.303 1.00 35.31  ? 353 ALA A H      1 
ATOM   5492 H  HA     . ALA A 1 354 ? -18.232 4.564   -35.064 1.00 38.71  ? 353 ALA A HA     1 
ATOM   5493 H  HB1    . ALA A 1 354 ? -17.950 6.255   -36.660 1.00 40.97  ? 353 ALA A HB1    1 
ATOM   5494 H  HB2    . ALA A 1 354 ? -18.920 6.747   -35.502 1.00 40.97  ? 353 ALA A HB2    1 
ATOM   5495 H  HB3    . ALA A 1 354 ? -17.406 7.227   -35.528 1.00 40.97  ? 353 ALA A HB3    1 
ATOM   5496 N  N      . LEU A 1 355 ? -15.194 5.477   -34.701 1.00 24.81  ? 354 LEU A N      1 
ATOM   5497 C  CA     . LEU A 1 355 ? -13.809 5.082   -34.949 1.00 25.03  ? 354 LEU A CA     1 
ATOM   5498 C  C      . LEU A 1 355 ? -13.483 3.735   -34.315 1.00 26.46  ? 354 LEU A C      1 
ATOM   5499 O  O      . LEU A 1 355 ? -12.810 2.890   -34.936 1.00 26.81  ? 354 LEU A O      1 
ATOM   5500 C  CB     . LEU A 1 355 ? -12.878 6.173   -34.438 1.00 25.18  ? 354 LEU A CB     1 
ATOM   5501 C  CG     . LEU A 1 355 ? -11.385 5.990   -34.735 1.00 31.89  ? 354 LEU A CG     1 
ATOM   5502 C  CD1    . LEU A 1 355 ? -11.137 5.731   -36.206 1.00 33.08  ? 354 LEU A CD1    1 
ATOM   5503 C  CD2    . LEU A 1 355 ? -10.625 7.219   -34.277 1.00 36.13  ? 354 LEU A CD2    1 
ATOM   5504 H  H      . LEU A 1 355 ? -15.278 6.164   -34.191 1.00 29.79  ? 354 LEU A H      1 
ATOM   5505 H  HA     . LEU A 1 355 ? -13.673 5.000   -35.906 1.00 30.05  ? 354 LEU A HA     1 
ATOM   5506 H  HB2    . LEU A 1 355 ? -13.149 7.015   -34.836 1.00 30.24  ? 354 LEU A HB2    1 
ATOM   5507 H  HB3    . LEU A 1 355 ? -12.975 6.228   -33.475 1.00 30.24  ? 354 LEU A HB3    1 
ATOM   5508 H  HG     . LEU A 1 355 ? -11.053 5.227   -34.235 1.00 38.28  ? 354 LEU A HG     1 
ATOM   5509 H  HD11   . LEU A 1 355 ? -10.185 5.621   -36.351 1.00 39.72  ? 354 LEU A HD11   1 
ATOM   5510 H  HD12   . LEU A 1 355 ? -11.607 4.924   -36.468 1.00 39.72  ? 354 LEU A HD12   1 
ATOM   5511 H  HD13   . LEU A 1 355 ? -11.466 6.486   -36.719 1.00 39.72  ? 354 LEU A HD13   1 
ATOM   5512 H  HD21   . LEU A 1 355 ? -9.682  7.096   -34.467 1.00 43.37  ? 354 LEU A HD21   1 
ATOM   5513 H  HD22   . LEU A 1 355 ? -10.962 7.993   -34.754 1.00 43.37  ? 354 LEU A HD22   1 
ATOM   5514 H  HD23   . LEU A 1 355 ? -10.758 7.334   -33.323 1.00 43.37  ? 354 LEU A HD23   1 
ATOM   5515 N  N      . MET A 1 356 ? -13.966 3.503   -33.091 1.00 26.18  ? 355 MET A N      1 
ATOM   5516 C  CA     . MET A 1 356 ? -13.784 2.201   -32.458 1.00 25.50  ? 355 MET A CA     1 
ATOM   5517 C  C      . MET A 1 356 ? -14.385 1.094   -33.306 1.00 24.98  ? 355 MET A C      1 
ATOM   5518 O  O      . MET A 1 356 ? -13.770 0.044   -33.500 1.00 26.85  ? 355 MET A O      1 
ATOM   5519 C  CB     . MET A 1 356 ? -14.411 2.223   -31.068 1.00 27.01  ? 355 MET A CB     1 
ATOM   5520 C  CG     . MET A 1 356 ? -14.260 0.952   -30.302 1.00 29.80  ? 355 MET A CG     1 
ATOM   5521 S  SD     . MET A 1 356 ? -12.557 0.598   -29.885 1.00 29.26  ? 355 MET A SD     1 
ATOM   5522 C  CE     . MET A 1 356 ? -12.322 1.776   -28.529 1.00 27.48  ? 355 MET A CE     1 
ATOM   5523 H  H      . MET A 1 356 ? -14.396 4.076   -32.615 1.00 31.44  ? 355 MET A H      1 
ATOM   5524 H  HA     . MET A 1 356 ? -12.835 2.034   -32.353 1.00 30.62  ? 355 MET A HA     1 
ATOM   5525 H  HB2    . MET A 1 356 ? -13.993 2.930   -30.551 1.00 32.43  ? 355 MET A HB2    1 
ATOM   5526 H  HB3    . MET A 1 356 ? -15.360 2.401   -31.158 1.00 32.43  ? 355 MET A HB3    1 
ATOM   5527 H  HG2    . MET A 1 356 ? -14.764 1.018   -29.476 1.00 35.78  ? 355 MET A HG2    1 
ATOM   5528 H  HG3    . MET A 1 356 ? -14.596 0.217   -30.838 1.00 35.78  ? 355 MET A HG3    1 
ATOM   5529 H  HE1    . MET A 1 356 ? -11.415 1.695   -28.194 1.00 32.99  ? 355 MET A HE1    1 
ATOM   5530 H  HE2    . MET A 1 356 ? -12.472 2.675   -28.863 1.00 32.99  ? 355 MET A HE2    1 
ATOM   5531 H  HE3    . MET A 1 356 ? -12.956 1.575   -27.823 1.00 32.99  ? 355 MET A HE3    1 
ATOM   5532 N  N      . ASP A 1 357 ? -15.599 1.309   -33.812 1.00 27.33  ? 356 ASP A N      1 
ATOM   5533 C  CA     . ASP A 1 357 ? -16.229 0.352   -34.729 1.00 29.00  ? 356 ASP A CA     1 
ATOM   5534 C  C      . ASP A 1 357 ? -15.344 0.024   -35.932 1.00 29.41  ? 356 ASP A C      1 
ATOM   5535 O  O      . ASP A 1 357 ? -15.277 -1.131  -36.362 1.00 32.04  ? 356 ASP A O      1 
ATOM   5536 C  CB     . ASP A 1 357 ? -17.568 0.897   -35.257 1.00 32.09  ? 356 ASP A CB     1 
ATOM   5537 C  CG     . ASP A 1 357 ? -18.641 1.023   -34.188 1.00 43.67  ? 356 ASP A CG     1 
ATOM   5538 O  OD1    . ASP A 1 357 ? -18.434 0.547   -33.042 1.00 49.13  ? 356 ASP A OD1    1 
ATOM   5539 O  OD2    . ASP A 1 357 ? -19.704 1.621   -34.503 1.00 45.18  1 356 ASP A OD2    1 
ATOM   5540 H  H      . ASP A 1 357 ? -16.081 2.001   -33.642 1.00 32.82  ? 356 ASP A H      1 
ATOM   5541 H  HA     . ASP A 1 357 ? -16.407 -0.474  -34.252 1.00 34.82  ? 356 ASP A HA     1 
ATOM   5542 H  HB2    . ASP A 1 357 ? -17.419 1.778   -35.634 1.00 38.53  ? 356 ASP A HB2    1 
ATOM   5543 H  HB3    . ASP A 1 357 ? -17.901 0.297   -35.942 1.00 38.53  ? 356 ASP A HB3    1 
ATOM   5544 N  N      . GLU A 1 358 ? -14.710 1.031   -36.527 1.00 27.73  ? 357 GLU A N      1 
ATOM   5545 C  CA     . GLU A 1 358 ? -13.849 0.792   -37.686 1.00 31.69  ? 357 GLU A CA     1 
ATOM   5546 C  C      . GLU A 1 358 ? -12.585 0.034   -37.300 1.00 30.37  ? 357 GLU A C      1 
ATOM   5547 O  O      . GLU A 1 358 ? -12.116 -0.836  -38.057 1.00 29.10  ? 357 GLU A O      1 
ATOM   5548 C  CB     . GLU A 1 358 ? -13.478 2.120   -38.339 1.00 34.23  ? 357 GLU A CB     1 
ATOM   5549 C  CG     . GLU A 1 358 ? -14.669 2.847   -38.901 1.00 41.46  ? 357 GLU A CG     1 
ATOM   5550 C  CD     . GLU A 1 358 ? -15.287 2.143   -40.124 1.00 48.47  ? 357 GLU A CD     1 
ATOM   5551 O  OE1    . GLU A 1 358 ? -14.553 1.465   -40.903 1.00 44.90  ? 357 GLU A OE1    1 
ATOM   5552 O  OE2    . GLU A 1 358 ? -16.522 2.272   -40.291 1.00 48.27  1 357 GLU A OE2    1 
ATOM   5553 H  H      . GLU A 1 358 ? -14.760 1.854   -36.284 1.00 33.29  ? 357 GLU A H      1 
ATOM   5554 H  HA     . GLU A 1 358 ? -14.333 0.260   -38.337 1.00 38.04  ? 357 GLU A HA     1 
ATOM   5555 H  HB2    . GLU A 1 358 ? -13.063 2.693   -37.676 1.00 41.09  ? 357 GLU A HB2    1 
ATOM   5556 H  HB3    . GLU A 1 358 ? -12.859 1.952   -39.067 1.00 41.09  ? 357 GLU A HB3    1 
ATOM   5557 H  HG2    . GLU A 1 358 ? -15.352 2.909   -38.215 1.00 49.77  ? 357 GLU A HG2    1 
ATOM   5558 H  HG3    . GLU A 1 358 ? -14.394 3.736   -39.175 1.00 49.77  ? 357 GLU A HG3    1 
ATOM   5559 N  N      . VAL A 1 359 ? -12.020 0.358   -36.135 1.00 27.18  ? 358 VAL A N      1 
ATOM   5560 C  CA     . VAL A 1 359 ? -10.824 -0.334  -35.668 1.00 25.86  ? 358 VAL A CA     1 
ATOM   5561 C  C      . VAL A 1 359 ? -11.138 -1.785  -35.373 1.00 26.37  ? 358 VAL A C      1 
ATOM   5562 O  O      . VAL A 1 359 ? -10.320 -2.678  -35.643 1.00 26.80  ? 358 VAL A O      1 
ATOM   5563 C  CB     . VAL A 1 359 ? -10.228 0.389   -34.447 1.00 26.79  ? 358 VAL A CB     1 
ATOM   5564 C  CG1    . VAL A 1 359 ? -9.077  -0.426  -33.827 1.00 29.38  ? 358 VAL A CG1    1 
ATOM   5565 C  CG2    . VAL A 1 359 ? -9.759  1.776   -34.867 1.00 25.33  ? 358 VAL A CG2    1 
ATOM   5566 H  H      . VAL A 1 359 ? -12.309 0.969   -35.602 1.00 32.63  ? 358 VAL A H      1 
ATOM   5567 H  HA     . VAL A 1 359 ? -10.159 -0.315  -36.375 1.00 31.05  ? 358 VAL A HA     1 
ATOM   5568 H  HB     . VAL A 1 359 ? -10.918 0.496   -33.774 1.00 32.16  ? 358 VAL A HB     1 
ATOM   5569 H  HG11   . VAL A 1 359 ? -8.726  0.057   -33.062 1.00 35.27  ? 358 VAL A HG11   1 
ATOM   5570 H  HG12   . VAL A 1 359 ? -9.419  -1.289  -33.545 1.00 35.27  ? 358 VAL A HG12   1 
ATOM   5571 H  HG13   . VAL A 1 359 ? -8.381  -0.546  -34.492 1.00 35.27  ? 358 VAL A HG13   1 
ATOM   5572 H  HG21   . VAL A 1 359 ? -9.384  2.229   -34.095 1.00 30.41  ? 358 VAL A HG21   1 
ATOM   5573 H  HG22   . VAL A 1 359 ? -9.085  1.686   -35.558 1.00 30.41  ? 358 VAL A HG22   1 
ATOM   5574 H  HG23   . VAL A 1 359 ? -10.518 2.276   -35.207 1.00 30.41  ? 358 VAL A HG23   1 
ATOM   5575 N  N      . VAL A 1 360 ? -12.333 -2.056  -34.841 1.00 26.76  ? 359 VAL A N      1 
ATOM   5576 C  CA     . VAL A 1 360 ? -12.711 -3.442  -34.575 1.00 29.18  ? 359 VAL A CA     1 
ATOM   5577 C  C      . VAL A 1 360 ? -12.886 -4.200  -35.880 1.00 30.32  ? 359 VAL A C      1 
ATOM   5578 O  O      . VAL A 1 360 ? -12.485 -5.367  -36.002 1.00 31.44  ? 359 VAL A O      1 
ATOM   5579 C  CB     . VAL A 1 360 ? -13.993 -3.494  -33.728 1.00 29.66  ? 359 VAL A CB     1 
ATOM   5580 C  CG1    . VAL A 1 360 ? -14.521 -4.907  -33.666 1.00 34.23  ? 359 VAL A CG1    1 
ATOM   5581 C  CG2    . VAL A 1 360 ? -13.687 -2.967  -32.319 1.00 26.52  ? 359 VAL A CG2    1 
ATOM   5582 H  H      . VAL A 1 360 ? -12.927 -1.471  -34.631 1.00 32.13  ? 359 VAL A H      1 
ATOM   5583 H  HA     . VAL A 1 360 ? -12.002 -3.872  -34.072 1.00 35.03  ? 359 VAL A HA     1 
ATOM   5584 H  HB     . VAL A 1 360 ? -14.670 -2.928  -34.129 1.00 35.62  ? 359 VAL A HB     1 
ATOM   5585 H  HG11   . VAL A 1 360 ? -15.328 -4.918  -33.128 1.00 41.09  ? 359 VAL A HG11   1 
ATOM   5586 H  HG12   . VAL A 1 360 ? -14.719 -5.210  -34.566 1.00 41.09  ? 359 VAL A HG12   1 
ATOM   5587 H  HG13   . VAL A 1 360 ? -13.847 -5.478  -33.264 1.00 41.09  ? 359 VAL A HG13   1 
ATOM   5588 H  HG21   . VAL A 1 360 ? -14.498 -3.001  -31.787 1.00 31.84  ? 359 VAL A HG21   1 
ATOM   5589 H  HG22   . VAL A 1 360 ? -13.003 -3.524  -31.916 1.00 31.84  ? 359 VAL A HG22   1 
ATOM   5590 H  HG23   . VAL A 1 360 ? -13.373 -2.052  -32.386 1.00 31.84  ? 359 VAL A HG23   1 
ATOM   5591 N  N      . LYS A 1 361 ? -13.492 -3.560  -36.875 1.00 30.97  ? 360 LYS A N      1 
ATOM   5592 C  CA     . LYS A 1 361 ? -13.641 -4.217  -38.171 1.00 31.71  ? 360 LYS A CA     1 
ATOM   5593 C  C      . LYS A 1 361 ? -12.281 -4.493  -38.788 1.00 31.09  ? 360 LYS A C      1 
ATOM   5594 O  O      . LYS A 1 361 ? -12.057 -5.558  -39.372 1.00 33.77  ? 360 LYS A O      1 
ATOM   5595 C  CB     . LYS A 1 361 ? -14.499 -3.363  -39.106 1.00 35.70  ? 360 LYS A CB     1 
ATOM   5596 C  CG     . LYS A 1 361 ? -15.981 -3.439  -38.796 1.00 47.73  ? 360 LYS A CG     1 
ATOM   5597 C  CD     . LYS A 1 361 ? -16.822 -2.762  -39.858 1.00 59.77  ? 360 LYS A CD     1 
ATOM   5598 C  CE     . LYS A 1 361 ? -16.660 -1.259  -39.815 1.00 67.05  ? 360 LYS A CE     1 
ATOM   5599 N  NZ     . LYS A 1 361 ? -17.642 -0.573  -40.700 1.00 68.62  1 360 LYS A NZ     1 
ATOM   5600 H  H      . LYS A 1 361 ? -13.818 -2.765  -36.830 1.00 37.19  ? 360 LYS A H      1 
ATOM   5601 H  HA     . LYS A 1 361 ? -14.090 -5.067  -38.044 1.00 38.07  ? 360 LYS A HA     1 
ATOM   5602 H  HB2    . LYS A 1 361 ? -14.224 -2.436  -39.025 1.00 42.85  ? 360 LYS A HB2    1 
ATOM   5603 H  HB3    . LYS A 1 361 ? -14.369 -3.668  -40.017 1.00 42.85  ? 360 LYS A HB3    1 
ATOM   5604 H  HG2    . LYS A 1 361 ? -16.248 -4.370  -38.747 1.00 57.30  ? 360 LYS A HG2    1 
ATOM   5605 H  HG3    . LYS A 1 361 ? -16.151 -2.997  -37.949 1.00 57.30  ? 360 LYS A HG3    1 
ATOM   5606 H  HD2    . LYS A 1 361 ? -16.545 -3.073  -40.733 1.00 71.74  ? 360 LYS A HD2    1 
ATOM   5607 H  HD3    . LYS A 1 361 ? -17.757 -2.971  -39.707 1.00 71.74  ? 360 LYS A HD3    1 
ATOM   5608 H  HE2    . LYS A 1 361 ? -16.802 -0.948  -38.907 1.00 80.48  ? 360 LYS A HE2    1 
ATOM   5609 H  HE3    . LYS A 1 361 ? -15.768 -1.025  -40.114 1.00 80.48  ? 360 LYS A HE3    1 
ATOM   5610 H  HZ1    . LYS A 1 361 ? -17.527 0.308   -40.658 1.00 82.36  ? 360 LYS A HZ1    1 
ATOM   5611 H  HZ2    . LYS A 1 361 ? -17.530 -0.839  -41.542 1.00 82.36  ? 360 LYS A HZ2    1 
ATOM   5612 H  HZ3    . LYS A 1 361 ? -18.472 -0.769  -40.443 1.00 82.36  ? 360 LYS A HZ3    1 
ATOM   5613 N  N      . ALA A 1 362 ? -11.356 -3.547  -38.647 1.00 30.45  ? 361 ALA A N      1 
ATOM   5614 C  CA     . ALA A 1 362 ? -10.007 -3.727  -39.171 1.00 32.32  ? 361 ALA A CA     1 
ATOM   5615 C  C      . ALA A 1 362 ? -9.313  -4.908  -38.517 1.00 32.21  ? 361 ALA A C      1 
ATOM   5616 O  O      . ALA A 1 362 ? -8.638  -5.699  -39.196 1.00 32.78  ? 361 ALA A O      1 
ATOM   5617 C  CB     . ALA A 1 362 ? -9.194  -2.454  -38.955 1.00 33.47  ? 361 ALA A CB     1 
ATOM   5618 H  H      . ALA A 1 362 ? -11.485 -2.793  -38.253 1.00 36.56  ? 361 ALA A H      1 
ATOM   5619 H  HA     . ALA A 1 362 ? -10.057 -3.896  -40.124 1.00 38.80  ? 361 ALA A HA     1 
ATOM   5620 H  HB1    . ALA A 1 362 ? -8.300  -2.587  -39.308 1.00 40.18  ? 361 ALA A HB1    1 
ATOM   5621 H  HB2    . ALA A 1 362 ? -9.627  -1.721  -39.420 1.00 40.18  ? 361 ALA A HB2    1 
ATOM   5622 H  HB3    . ALA A 1 362 ? -9.151  -2.264  -38.005 1.00 40.18  ? 361 ALA A HB3    1 
ATOM   5623 N  N      . THR A 1 363 ? -9.428  -5.023  -37.193 1.00 28.22  ? 362 THR A N      1 
ATOM   5624 C  CA     . THR A 1 363 ? -8.863  -6.183  -36.526 1.00 27.83  ? 362 THR A CA     1 
ATOM   5625 C  C      . THR A 1 363 ? -9.396  -7.467  -37.140 1.00 31.10  ? 362 THR A C      1 
ATOM   5626 O  O      . THR A 1 363 ? -8.656  -8.445  -37.307 1.00 32.76  ? 362 THR A O      1 
ATOM   5627 C  CB     . THR A 1 363 ? -9.172  -6.138  -35.025 1.00 27.42  ? 362 THR A CB     1 
ATOM   5628 O  OG1    . THR A 1 363 ? -8.890  -4.825  -34.509 1.00 26.72  ? 362 THR A OG1    1 
ATOM   5629 C  CG2    . THR A 1 363 ? -8.343  -7.148  -34.315 1.00 31.82  ? 362 THR A CG2    1 
ATOM   5630 H  H      . THR A 1 363 ? -9.819  -4.459  -36.676 1.00 33.88  ? 362 THR A H      1 
ATOM   5631 H  HA     . THR A 1 363 ? -7.899  -6.174  -36.636 1.00 33.42  ? 362 THR A HA     1 
ATOM   5632 H  HB     . THR A 1 363 ? -10.108 -6.349  -34.880 1.00 32.93  ? 362 THR A HB     1 
ATOM   5633 H  HG1    . THR A 1 363 ? -9.362  -4.253  -34.903 1.00 32.08  ? 362 THR A HG1    1 
ATOM   5634 H  HG21   . THR A 1 363 ? -8.535  -7.124  -33.364 1.00 38.20  ? 362 THR A HG21   1 
ATOM   5635 H  HG22   . THR A 1 363 ? -8.540  -8.035  -34.654 1.00 38.20  ? 362 THR A HG22   1 
ATOM   5636 H  HG23   . THR A 1 363 ? -7.402  -6.959  -34.451 1.00 38.20  ? 362 THR A HG23   1 
ATOM   5637 N  N      . SER A 1 364 ? -10.686 -7.489  -37.466 1.00 32.41  ? 363 SER A N      1 
ATOM   5638 C  CA     . SER A 1 364 ? -11.302 -8.714  -37.959 1.00 35.62  ? 363 SER A CA     1 
ATOM   5639 C  C      . SER A 1 364 ? -10.703 -9.166  -39.289 1.00 35.92  ? 363 SER A C      1 
ATOM   5640 O  O      . SER A 1 364 ? -10.720 -10.358 -39.598 1.00 40.22  ? 363 SER A O      1 
ATOM   5641 C  CB     . SER A 1 364 ? -12.810 -8.519  -38.117 1.00 42.31  ? 363 SER A CB     1 
ATOM   5642 O  OG     . SER A 1 364 ? -13.402 -8.310  -36.854 1.00 51.62  ? 363 SER A OG     1 
ATOM   5643 H  H      . SER A 1 364 ? -11.219 -6.816  -37.411 1.00 38.91  ? 363 SER A H      1 
ATOM   5644 H  HA     . SER A 1 364 ? -11.159 -9.422  -37.311 1.00 42.77  ? 363 SER A HA     1 
ATOM   5645 H  HB2    . SER A 1 364 ? -12.975 -7.745  -38.678 1.00 50.79  ? 363 SER A HB2    1 
ATOM   5646 H  HB3    . SER A 1 364 ? -13.194 -9.313  -38.521 1.00 50.79  ? 363 SER A HB3    1 
ATOM   5647 H  HG     . SER A 1 364 ? -13.074 -7.626  -36.493 1.00 61.96  ? 363 SER A HG     1 
ATOM   5648 N  N      . ARG A 1 365 ? -10.187 -8.247  -40.091 1.00 33.88  ? 364 ARG A N      1 
ATOM   5649 C  CA     . ARG A 1 365 ? -9.611  -8.611  -41.380 1.00 42.66  ? 364 ARG A CA     1 
ATOM   5650 C  C      . ARG A 1 365 ? -8.085  -8.662  -41.343 1.00 41.82  ? 364 ARG A C      1 
ATOM   5651 O  O      . ARG A 1 365 ? -7.446  -8.727  -42.404 1.00 39.36  ? 364 ARG A O      1 
ATOM   5652 C  CB     . ARG A 1 365 ? -10.095 -7.645  -42.463 1.00 51.97  ? 364 ARG A CB     1 
ATOM   5653 C  CG     . ARG A 1 365 ? -9.394  -6.326  -42.486 1.00 66.42  ? 364 ARG A CG     1 
ATOM   5654 C  CD     . ARG A 1 365 ? -10.308 -5.257  -43.026 1.00 87.54  ? 364 ARG A CD     1 
ATOM   5655 N  NE     . ARG A 1 365 ? -9.796  -3.933  -42.704 1.00 102.03 ? 364 ARG A NE     1 
ATOM   5656 C  CZ     . ARG A 1 365 ? -10.554 -2.871  -42.452 1.00 111.80 ? 364 ARG A CZ     1 
ATOM   5657 N  NH1    . ARG A 1 365 ? -11.879 -2.947  -42.473 1.00 109.72 1 364 ARG A NH1    1 
ATOM   5658 N  NH2    . ARG A 1 365 ? -9.976  -1.725  -42.153 1.00 120.28 ? 364 ARG A NH2    1 
ATOM   5659 H  H      . ARG A 1 365 ? -10.158 -7.405  -39.915 1.00 40.67  ? 364 ARG A H      1 
ATOM   5660 H  HA     . ARG A 1 365 ? -9.926  -9.497  -41.618 1.00 51.21  ? 364 ARG A HA     1 
ATOM   5661 H  HB2    . ARG A 1 365 ? -9.964  -8.061  -43.329 1.00 62.38  ? 364 ARG A HB2    1 
ATOM   5662 H  HB3    . ARG A 1 365 ? -11.039 -7.473  -42.324 1.00 62.38  ? 364 ARG A HB3    1 
ATOM   5663 H  HG2    . ARG A 1 365 ? -9.134  -6.081  -41.584 1.00 79.72  ? 364 ARG A HG2    1 
ATOM   5664 H  HG3    . ARG A 1 365 ? -8.614  -6.383  -43.060 1.00 79.72  ? 364 ARG A HG3    1 
ATOM   5665 H  HD2    . ARG A 1 365 ? -10.364 -5.338  -43.991 1.00 105.07 ? 364 ARG A HD2    1 
ATOM   5666 H  HD3    . ARG A 1 365 ? -11.187 -5.352  -42.627 1.00 105.07 ? 364 ARG A HD3    1 
ATOM   5667 H  HE     . ARG A 1 365 ? -8.942  -3.831  -42.674 1.00 122.45 ? 364 ARG A HE     1 
ATOM   5668 H  HH11   . ARG A 1 365 ? -12.263 -3.693  -42.661 1.00 131.68 ? 364 ARG A HH11   1 
ATOM   5669 H  HH12   . ARG A 1 365 ? -12.352 -2.249  -42.306 1.00 131.68 ? 364 ARG A HH12   1 
ATOM   5670 H  HH21   . ARG A 1 365 ? -9.118  -1.668  -42.138 1.00 144.36 ? 364 ARG A HH21   1 
ATOM   5671 H  HH22   . ARG A 1 365 ? -10.457 -1.031  -41.992 1.00 144.36 ? 364 ARG A HH22   1 
ATOM   5672 N  N      . GLY A 1 366 ? -7.488  -8.639  -40.146 1.00 39.10  ? 365 GLY A N      1 
ATOM   5673 C  CA     . GLY A 1 366 ? -6.072  -8.912  -39.986 1.00 39.01  ? 365 GLY A CA     1 
ATOM   5674 C  C      . GLY A 1 366 ? -5.206  -7.718  -39.670 1.00 39.00  ? 365 GLY A C      1 
ATOM   5675 O  O      . GLY A 1 366 ? -3.981  -7.868  -39.592 1.00 37.17  ? 365 GLY A O      1 
ATOM   5676 H  H      . GLY A 1 366 ? -7.894  -8.465  -39.408 1.00 46.94  ? 365 GLY A H      1 
ATOM   5677 H  HA2    . GLY A 1 366 ? -5.958  -9.558  -39.272 1.00 46.83  ? 365 GLY A HA2    1 
ATOM   5678 H  HA3    . GLY A 1 366 ? -5.737  -9.312  -40.805 1.00 46.83  ? 365 GLY A HA3    1 
ATOM   5679 N  N      . CYS A 1 367 ? -5.786  -6.543  -39.478 1.00 39.88  ? 366 CYS A N      1 
ATOM   5680 C  CA     . CYS A 1 367 ? -5.007  -5.400  -39.031 1.00 35.16  ? 366 CYS A CA     1 
ATOM   5681 C  C      . CYS A 1 367 ? -4.510  -5.623  -37.604 1.00 30.67  ? 366 CYS A C      1 
ATOM   5682 O  O      . CYS A 1 367 ? -5.224  -6.164  -36.753 1.00 30.14  ? 366 CYS A O      1 
ATOM   5683 C  CB     . CYS A 1 367 ? -5.858  -4.136  -39.112 1.00 33.77  ? 366 CYS A CB     1 
ATOM   5684 S  SG     . CYS A 1 367 ? -4.918  -2.584  -38.921 1.00 33.41  ? 366 CYS A SG     1 
ATOM   5685 H  H      . CYS A 1 367 ? -6.622  -6.382  -39.599 1.00 47.88  ? 366 CYS A H      1 
ATOM   5686 H  HA     . CYS A 1 367 ? -4.236  -5.288  -39.610 1.00 42.22  ? 366 CYS A HA     1 
ATOM   5687 H  HB2    . CYS A 1 367 ? -6.296  -4.111  -39.977 1.00 40.55  ? 366 CYS A HB2    1 
ATOM   5688 H  HB3    . CYS A 1 367 ? -6.526  -4.165  -38.408 1.00 40.55  ? 366 CYS A HB3    1 
ATOM   5689 H  HG     . CYS A 1 367 ? -5.675  -1.656  -38.999 1.00 40.11  ? 366 CYS A HG     1 
ATOM   5690 N  N      . ILE A 1 368 ? -3.274  -5.223  -37.334 1.00 28.57  ? 367 ILE A N      1 
ATOM   5691 C  CA     . ILE A 1 368 ? -2.761  -5.216  -35.967 1.00 28.74  ? 367 ILE A CA     1 
ATOM   5692 C  C      . ILE A 1 368 ? -3.181  -3.895  -35.334 1.00 26.69  ? 367 ILE A C      1 
ATOM   5693 O  O      . ILE A 1 368 ? -2.774  -2.830  -35.802 1.00 26.07  ? 367 ILE A O      1 
ATOM   5694 C  CB     . ILE A 1 368 ? -1.236  -5.382  -35.941 1.00 33.38  ? 367 ILE A CB     1 
ATOM   5695 C  CG1    . ILE A 1 368 ? -0.845  -6.730  -36.561 1.00 39.40  ? 367 ILE A CG1    1 
ATOM   5696 C  CG2    . ILE A 1 368 ? -0.700  -5.254  -34.520 1.00 35.65  ? 367 ILE A CG2    1 
ATOM   5697 C  CD1    . ILE A 1 368 ? 0.653   -6.947  -36.628 1.00 52.70  ? 367 ILE A CD1    1 
ATOM   5698 H  H      . ILE A 1 368 ? -2.711  -4.949  -37.923 1.00 34.31  ? 367 ILE A H      1 
ATOM   5699 H  HA     . ILE A 1 368 ? -3.161  -5.943  -35.464 1.00 34.51  ? 367 ILE A HA     1 
ATOM   5700 H  HB     . ILE A 1 368 ? -0.844  -4.676  -36.478 1.00 40.08  ? 367 ILE A HB     1 
ATOM   5701 H  HG12   . ILE A 1 368 ? -1.226  -7.444  -36.026 1.00 47.29  ? 367 ILE A HG12   1 
ATOM   5702 H  HG13   . ILE A 1 368 ? -1.193  -6.773  -37.465 1.00 47.29  ? 367 ILE A HG13   1 
ATOM   5703 H  HG21   . ILE A 1 368 ? 0.264   -5.363  -34.536 1.00 42.80  ? 367 ILE A HG21   1 
ATOM   5704 H  HG22   . ILE A 1 368 ? -0.928  -4.377  -34.175 1.00 42.80  ? 367 ILE A HG22   1 
ATOM   5705 H  HG23   . ILE A 1 368 ? -1.102  -5.942  -33.968 1.00 42.80  ? 367 ILE A HG23   1 
ATOM   5706 H  HD11   . ILE A 1 368 ? 0.829   -7.813  -37.027 1.00 63.26  ? 367 ILE A HD11   1 
ATOM   5707 H  HD12   . ILE A 1 368 ? 1.049   -6.246  -37.168 1.00 63.26  ? 367 ILE A HD12   1 
ATOM   5708 H  HD13   . ILE A 1 368 ? 1.016   -6.917  -35.729 1.00 63.26  ? 367 ILE A HD13   1 
ATOM   5709 N  N      . THR A 1 369 ? -4.014  -3.962  -34.296 1.00 25.29  ? 368 THR A N      1 
ATOM   5710 C  CA     . THR A 1 369 ? -4.608  -2.767  -33.697 1.00 22.61  ? 368 THR A CA     1 
ATOM   5711 C  C      . THR A 1 369 ? -4.222  -2.654  -32.223 1.00 23.53  ? 368 THR A C      1 
ATOM   5712 O  O      . THR A 1 369 ? -4.477  -3.563  -31.422 1.00 22.61  ? 368 THR A O      1 
ATOM   5713 C  CB     . THR A 1 369 ? -6.125  -2.786  -33.885 1.00 23.42  ? 368 THR A CB     1 
ATOM   5714 O  OG1    . THR A 1 369 ? -6.648  -3.989  -33.309 1.00 25.47  ? 368 THR A OG1    1 
ATOM   5715 C  CG2    . THR A 1 369 ? -6.484  -2.727  -35.409 1.00 25.85  ? 368 THR A CG2    1 
ATOM   5716 H  H      . THR A 1 369 ? -4.254  -4.696  -33.917 1.00 30.37  ? 368 THR A H      1 
ATOM   5717 H  HA     . THR A 1 369 ? -4.264  -1.984  -34.155 1.00 27.15  ? 368 THR A HA     1 
ATOM   5718 H  HB     . THR A 1 369 ? -6.518  -2.017  -33.444 1.00 28.12  ? 368 THR A HB     1 
ATOM   5719 H  HG1    . THR A 1 369 ? -7.483  -4.014  -33.405 1.00 30.59  ? 368 THR A HG1    1 
ATOM   5720 H  HG21   . THR A 1 369 ? -7.447  -2.739  -35.523 1.00 31.04  ? 368 THR A HG21   1 
ATOM   5721 H  HG22   . THR A 1 369 ? -6.130  -1.913  -35.801 1.00 31.04  ? 368 THR A HG22   1 
ATOM   5722 H  HG23   . THR A 1 369 ? -6.102  -3.490  -35.869 1.00 31.04  ? 368 THR A HG23   1 
ATOM   5723 N  N      . ILE A 1 370 ? -3.611  -1.528  -31.874 1.00 21.92  ? 369 ILE A N      1 
ATOM   5724 C  CA     . ILE A 1 370 ? -3.069  -1.287  -30.545 1.00 21.23  ? 369 ILE A CA     1 
ATOM   5725 C  C      . ILE A 1 370 ? -3.698  -0.006  -30.053 1.00 20.45  ? 369 ILE A C      1 
ATOM   5726 O  O      . ILE A 1 370 ? -3.568  1.033   -30.710 1.00 19.49  ? 369 ILE A O      1 
ATOM   5727 C  CB     . ILE A 1 370 ? -1.537  -1.170  -30.562 1.00 23.41  ? 369 ILE A CB     1 
ATOM   5728 C  CG1    . ILE A 1 370 ? -0.926  -2.438  -31.165 1.00 25.55  ? 369 ILE A CG1    1 
ATOM   5729 C  CG2    . ILE A 1 370 ? -1.003  -0.938  -29.166 1.00 23.72  ? 369 ILE A CG2    1 
ATOM   5730 C  CD1    . ILE A 1 370 ? 0.500   -2.264  -31.657 1.00 27.90  ? 369 ILE A CD1    1 
ATOM   5731 H  H      . ILE A 1 370 ? -3.495  -0.867  -32.411 1.00 26.32  ? 369 ILE A H      1 
ATOM   5732 H  HA     . ILE A 1 370 ? -3.322  -2.010  -29.950 1.00 25.50  ? 369 ILE A HA     1 
ATOM   5733 H  HB     . ILE A 1 370 ? -1.291  -0.414  -31.117 1.00 28.11  ? 369 ILE A HB     1 
ATOM   5734 H  HG12   . ILE A 1 370 ? -0.922  -3.134  -30.490 1.00 30.68  ? 369 ILE A HG12   1 
ATOM   5735 H  HG13   . ILE A 1 370 ? -1.467  -2.716  -31.920 1.00 30.68  ? 369 ILE A HG13   1 
ATOM   5736 H  HG21   . ILE A 1 370 ? -0.037  -0.868  -29.206 1.00 28.48  ? 369 ILE A HG21   1 
ATOM   5737 H  HG22   . ILE A 1 370 ? -1.381  -0.116  -28.817 1.00 28.48  ? 369 ILE A HG22   1 
ATOM   5738 H  HG23   . ILE A 1 370 ? -1.259  -1.685  -28.603 1.00 28.48  ? 369 ILE A HG23   1 
ATOM   5739 H  HD11   . ILE A 1 370 ? 0.813   -3.106  -32.022 1.00 33.49  ? 369 ILE A HD11   1 
ATOM   5740 H  HD12   . ILE A 1 370 ? 0.515   -1.579  -32.344 1.00 33.49  ? 369 ILE A HD12   1 
ATOM   5741 H  HD13   . ILE A 1 370 ? 1.060   -1.997  -30.912 1.00 33.49  ? 369 ILE A HD13   1 
ATOM   5742 N  N      . ILE A 1 371 ? -4.414  -0.092  -28.929 1.00 19.40  ? 370 ILE A N      1 
ATOM   5743 C  CA     . ILE A 1 371 ? -5.051  1.059   -28.316 1.00 20.57  ? 370 ILE A CA     1 
ATOM   5744 C  C      . ILE A 1 371 ? -4.397  1.245   -26.957 1.00 21.69  ? 370 ILE A C      1 
ATOM   5745 O  O      . ILE A 1 371 ? -4.230  0.270   -26.222 1.00 24.83  ? 370 ILE A O      1 
ATOM   5746 C  CB     . ILE A 1 371 ? -6.574  0.844   -28.199 1.00 30.42  ? 370 ILE A CB     1 
ATOM   5747 C  CG1    . ILE A 1 371 ? -7.191  0.707   -29.595 1.00 33.52  ? 370 ILE A CG1    1 
ATOM   5748 C  CG2    . ILE A 1 371 ? -7.223  2.004   -27.454 1.00 35.88  ? 370 ILE A CG2    1 
ATOM   5749 C  CD1    . ILE A 1 371 ? -8.705  0.489   -29.597 1.00 36.33  ? 370 ILE A CD1    1 
ATOM   5750 H  H      . ILE A 1 371 ? -4.543  -0.826  -28.499 1.00 23.29  ? 370 ILE A H      1 
ATOM   5751 H  HA     . ILE A 1 371 ? -4.888  1.850   -28.852 1.00 24.71  ? 370 ILE A HA     1 
ATOM   5752 H  HB     . ILE A 1 371 ? -6.736  0.025   -27.704 1.00 36.52  ? 370 ILE A HB     1 
ATOM   5753 H  HG12   . ILE A 1 371 ? -7.009  1.517   -30.096 1.00 40.25  ? 370 ILE A HG12   1 
ATOM   5754 H  HG13   . ILE A 1 371 ? -6.783  -0.052  -30.041 1.00 40.25  ? 370 ILE A HG13   1 
ATOM   5755 H  HG21   . ILE A 1 371 ? -8.178  1.846   -27.395 1.00 43.08  ? 370 ILE A HG21   1 
ATOM   5756 H  HG22   . ILE A 1 371 ? -6.841  2.062   -26.565 1.00 43.08  ? 370 ILE A HG22   1 
ATOM   5757 H  HG23   . ILE A 1 371 ? -7.054  2.826   -27.941 1.00 43.08  ? 370 ILE A HG23   1 
ATOM   5758 H  HD11   . ILE A 1 371 ? -9.011  0.414   -30.514 1.00 43.62  ? 370 ILE A HD11   1 
ATOM   5759 H  HD12   . ILE A 1 371 ? -8.907  -0.326  -29.112 1.00 43.62  ? 370 ILE A HD12   1 
ATOM   5760 H  HD13   . ILE A 1 371 ? -9.133  1.246   -29.167 1.00 43.62  ? 370 ILE A HD13   1 
ATOM   5761 N  N      . GLY A 1 372 ? -3.998  2.468   -26.635 1.00 19.44  ? 371 GLY A N      1 
ATOM   5762 C  CA     . GLY A 1 372 ? -3.320  2.726   -25.370 1.00 20.35  ? 371 GLY A CA     1 
ATOM   5763 C  C      . GLY A 1 372 ? -3.776  4.021   -24.735 1.00 21.82  ? 371 GLY A C      1 
ATOM   5764 O  O      . GLY A 1 372 ? -4.084  4.998   -25.417 1.00 23.41  ? 371 GLY A O      1 
ATOM   5765 H  H      . GLY A 1 372 ? -4.105  3.164   -27.128 1.00 23.35  ? 371 GLY A H      1 
ATOM   5766 H  HA2    . GLY A 1 372 ? -3.499  2.000   -24.752 1.00 24.44  ? 371 GLY A HA2    1 
ATOM   5767 H  HA3    . GLY A 1 372 ? -2.363  2.776   -25.518 1.00 24.44  ? 371 GLY A HA3    1 
ATOM   5768 N  N      . GLY A 1 373 ? -3.763  4.034   -23.407 1.00 24.39  ? 372 GLY A N      1 
ATOM   5769 C  CA     . GLY A 1 373 ? -3.977  5.252   -22.657 1.00 23.29  ? 372 GLY A CA     1 
ATOM   5770 C  C      . GLY A 1 373 ? -4.950  5.021   -21.524 1.00 24.10  ? 372 GLY A C      1 
ATOM   5771 O  O      . GLY A 1 373 ? -5.799  4.133   -21.601 1.00 26.14  ? 372 GLY A O      1 
ATOM   5772 H  H      . GLY A 1 373 ? -3.629  3.340   -22.917 1.00 29.28  ? 372 GLY A H      1 
ATOM   5773 H  HA2    . GLY A 1 373 ? -3.136  5.564   -22.289 1.00 27.96  ? 372 GLY A HA2    1 
ATOM   5774 H  HA3    . GLY A 1 373 ? -4.336  5.939   -23.241 1.00 27.96  ? 372 GLY A HA3    1 
ATOM   5775 N  N      . GLY A 1 374 ? -4.871  5.831   -20.482 1.00 22.07  ? 373 GLY A N      1 
ATOM   5776 C  CA     . GLY A 1 374 ? -5.819  5.686   -19.390 1.00 22.92  ? 373 GLY A CA     1 
ATOM   5777 C  C      . GLY A 1 374 ? -7.240  5.919   -19.858 1.00 25.04  ? 373 GLY A C      1 
ATOM   5778 O  O      . GLY A 1 374 ? -8.169  5.196   -19.474 1.00 25.54  ? 373 GLY A O      1 
ATOM   5779 H  H      . GLY A 1 374 ? -4.292  6.459   -20.382 1.00 26.51  ? 373 GLY A H      1 
ATOM   5780 H  HA2    . GLY A 1 374 ? -5.756  4.792   -19.020 1.00 27.53  ? 373 GLY A HA2    1 
ATOM   5781 H  HA3    . GLY A 1 374 ? -5.613  6.327   -18.692 1.00 27.53  ? 373 GLY A HA3    1 
ATOM   5782 N  N      . ASP A 1 375 ? -7.428  6.934   -20.694 1.00 22.86  ? 374 ASP A N      1 
ATOM   5783 C  CA     . ASP A 1 375 ? -8.745  7.300   -21.171 1.00 22.31  ? 374 ASP A CA     1 
ATOM   5784 C  C      . ASP A 1 375 ? -9.115  6.537   -22.440 1.00 23.37  ? 374 ASP A C      1 
ATOM   5785 O  O      . ASP A 1 375 ? -10.253 6.084   -22.576 1.00 27.56  ? 374 ASP A O      1 
ATOM   5786 C  CB     . ASP A 1 375 ? -8.784  8.825   -21.343 1.00 23.25  ? 374 ASP A CB     1 
ATOM   5787 C  CG     . ASP A 1 375 ? -8.552  9.558   -20.004 1.00 29.86  ? 374 ASP A CG     1 
ATOM   5788 O  OD1    . ASP A 1 375 ? -9.409  9.392   -19.122 1.00 29.95  ? 374 ASP A OD1    1 
ATOM   5789 O  OD2    . ASP A 1 375 ? -7.493  10.238  -19.795 1.00 30.93  1 374 ASP A OD2    1 
ATOM   5790 H  H      . ASP A 1 375 ? -6.796  7.431   -21.001 1.00 27.45  ? 374 ASP A H      1 
ATOM   5791 H  HA     . ASP A 1 375 ? -9.396  7.067   -20.491 1.00 26.79  ? 374 ASP A HA     1 
ATOM   5792 H  HB2    . ASP A 1 375 ? -8.086  9.095   -21.961 1.00 27.92  ? 374 ASP A HB2    1 
ATOM   5793 H  HB3    . ASP A 1 375 ? -9.653  9.086   -21.684 1.00 27.92  ? 374 ASP A HB3    1 
ATOM   5794 N  N      . THR A 1 376 ? -8.179  6.332   -23.367 1.00 20.71  ? 375 THR A N      1 
ATOM   5795 C  CA     . THR A 1 376 ? -8.527  5.593   -24.585 1.00 22.28  ? 375 THR A CA     1 
ATOM   5796 C  C      . THR A 1 376 ? -8.851  4.136   -24.284 1.00 23.47  ? 375 THR A C      1 
ATOM   5797 O  O      . THR A 1 376 ? -9.735  3.542   -24.927 1.00 20.95  ? 375 THR A O      1 
ATOM   5798 C  CB     . THR A 1 376 ? -7.395  5.693   -25.608 1.00 26.30  ? 375 THR A CB     1 
ATOM   5799 O  OG1    . THR A 1 376 ? -7.001  7.053   -25.729 1.00 23.79  ? 375 THR A OG1    1 
ATOM   5800 C  CG2    . THR A 1 376 ? -7.870  5.247   -26.971 1.00 32.06  ? 375 THR A CG2    1 
ATOM   5801 H  H      . THR A 1 376 ? -7.363  6.598   -23.320 1.00 24.87  ? 375 THR A H      1 
ATOM   5802 H  HA     . THR A 1 376 ? -9.317  5.996   -24.978 1.00 26.75  ? 375 THR A HA     1 
ATOM   5803 H  HB     . THR A 1 376 ? -6.642  5.147   -25.335 1.00 31.58  ? 375 THR A HB     1 
ATOM   5804 H  HG1    . THR A 1 376 ? -6.733  7.342   -24.987 1.00 28.57  ? 375 THR A HG1    1 
ATOM   5805 H  HG21   . THR A 1 376 ? -7.146  5.314   -27.613 1.00 38.49  ? 375 THR A HG21   1 
ATOM   5806 H  HG22   . THR A 1 376 ? -8.172  4.326   -26.932 1.00 38.49  ? 375 THR A HG22   1 
ATOM   5807 H  HG23   . THR A 1 376 ? -8.605  5.807   -27.266 1.00 38.49  ? 375 THR A HG23   1 
ATOM   5808 N  N      . ALA A 1 377 ? -8.166  3.535   -23.298 1.00 23.05  ? 376 ALA A N      1 
ATOM   5809 C  CA     . ALA A 1 377 ? -8.508  2.169   -22.910 1.00 23.56  ? 376 ALA A CA     1 
ATOM   5810 C  C      . ALA A 1 377 ? -9.890  2.097   -22.285 1.00 24.63  ? 376 ALA A C      1 
ATOM   5811 O  O      . ALA A 1 377 ? -10.529 1.039   -22.292 1.00 26.39  ? 376 ALA A O      1 
ATOM   5812 C  CB     . ALA A 1 377 ? -7.467  1.616   -21.924 1.00 26.59  ? 376 ALA A CB     1 
ATOM   5813 H  H      . ALA A 1 377 ? -7.520  3.889   -22.854 1.00 27.67  ? 376 ALA A H      1 
ATOM   5814 H  HA     . ALA A 1 377 ? -8.505  1.605   -23.699 1.00 28.29  ? 376 ALA A HA     1 
ATOM   5815 H  HB1    . ALA A 1 377 ? -7.714  0.710   -21.681 1.00 31.93  ? 376 ALA A HB1    1 
ATOM   5816 H  HB2    . ALA A 1 377 ? -6.596  1.619   -22.351 1.00 31.93  ? 376 ALA A HB2    1 
ATOM   5817 H  HB3    . ALA A 1 377 ? -7.451  2.179   -21.134 1.00 31.93  ? 376 ALA A HB3    1 
ATOM   5818 N  N      . THR A 1 378 ? -10.347 3.199   -21.702 1.00 21.57  ? 377 THR A N      1 
ATOM   5819 C  CA     . THR A 1 378 ? -11.679 3.272   -21.141 1.00 22.88  ? 377 THR A CA     1 
ATOM   5820 C  C      . THR A 1 378 ? -12.757 3.307   -22.223 1.00 26.04  ? 377 THR A C      1 
ATOM   5821 O  O      . THR A 1 378 ? -13.896 2.879   -21.970 1.00 27.01  ? 377 THR A O      1 
ATOM   5822 C  CB     . THR A 1 378 ? -11.734 4.487   -20.215 1.00 26.25  ? 377 THR A CB     1 
ATOM   5823 O  OG1    . THR A 1 378 ? -10.736 4.317   -19.181 1.00 24.97  ? 377 THR A OG1    1 
ATOM   5824 C  CG2    . THR A 1 378 ? -13.057 4.624   -19.567 1.00 30.06  ? 377 THR A CG2    1 
ATOM   5825 H  H      . THR A 1 378 ? -9.895  3.926   -21.621 1.00 25.90  ? 377 THR A H      1 
ATOM   5826 H  HA     . THR A 1 378 ? -11.832 2.482   -20.600 1.00 27.48  ? 377 THR A HA     1 
ATOM   5827 H  HB     . THR A 1 378 ? -11.548 5.294   -20.720 1.00 31.52  ? 377 THR A HB     1 
ATOM   5828 H  HG1    . THR A 1 378 ? -9.972  4.257   -19.526 1.00 29.98  ? 377 THR A HG1    1 
ATOM   5829 H  HG21   . THR A 1 378 ? -13.062 5.401   -18.986 1.00 36.09  ? 377 THR A HG21   1 
ATOM   5830 H  HG22   . THR A 1 378 ? -13.746 4.729   -20.241 1.00 36.09  ? 377 THR A HG22   1 
ATOM   5831 H  HG23   . THR A 1 378 ? -13.250 3.834   -19.038 1.00 36.09  ? 377 THR A HG23   1 
ATOM   5832 N  N      . CYS A 1 379 ? -12.428 3.799   -23.424 1.00 27.53  ? 378 CYS A N      1 
ATOM   5833 C  CA     . CYS A 1 379 ? -13.311 3.603   -24.579 1.00 27.42  ? 378 CYS A CA     1 
ATOM   5834 C  C      . CYS A 1 379 ? -13.519 2.132   -24.853 1.00 25.45  ? 378 CYS A C      1 
ATOM   5835 O  O      . CYS A 1 379 ? -14.646 1.702   -25.130 1.00 28.87  ? 378 CYS A O      1 
ATOM   5836 C  CB     . CYS A 1 379 ? -12.736 4.271   -25.831 1.00 30.37  ? 378 CYS A CB     1 
ATOM   5837 S  SG     . CYS A 1 379 ? -12.390 6.008   -25.616 1.00 33.21  ? 378 CYS A SG     1 
ATOM   5838 H  H      . CYS A 1 379 ? -11.711 4.242   -23.594 1.00 33.06  ? 378 CYS A H      1 
ATOM   5839 H  HA     . CYS A 1 379 ? -14.175 4.002   -24.392 1.00 32.93  ? 378 CYS A HA     1 
ATOM   5840 H  HB2    . CYS A 1 379 ? -11.905 3.829   -26.068 1.00 36.46  ? 378 CYS A HB2    1 
ATOM   5841 H  HB3    . CYS A 1 379 ? -13.375 4.183   -26.555 1.00 36.46  ? 378 CYS A HB3    1 
ATOM   5842 H  HG     . CYS A 1 379 ? -13.408 6.577   -25.334 1.00 39.88  ? 378 CYS A HG     1 
ATOM   5843 N  N      . CYS A 1 380 ? -12.437 1.341   -24.801 1.00 26.57  ? 379 CYS A N      1 
ATOM   5844 C  CA     . CYS A 1 380 ? -12.564 -0.103  -25.005 1.00 27.47  ? 379 CYS A CA     1 
ATOM   5845 C  C      . CYS A 1 380 ? -13.465 -0.727  -23.953 1.00 28.34  ? 379 CYS A C      1 
ATOM   5846 O  O      . CYS A 1 380 ? -14.276 -1.604  -24.259 1.00 31.66  ? 379 CYS A O      1 
ATOM   5847 C  CB     . CYS A 1 380 ? -11.191 -0.772  -24.975 1.00 31.41  ? 379 CYS A CB     1 
ATOM   5848 S  SG     . CYS A 1 380 ? -10.133 -0.277  -26.344 1.00 32.77  ? 379 CYS A SG     1 
ATOM   5849 H  H      . CYS A 1 380 ? -11.635 1.613   -24.652 1.00 31.91  ? 379 CYS A H      1 
ATOM   5850 H  HA     . CYS A 1 380 ? -12.959 -0.267  -25.876 1.00 32.98  ? 379 CYS A HA     1 
ATOM   5851 H  HB2    . CYS A 1 380 ? -10.743 -0.532  -24.149 1.00 37.71  ? 379 CYS A HB2    1 
ATOM   5852 H  HB3    . CYS A 1 380 ? -11.309 -1.734  -25.020 1.00 37.71  ? 379 CYS A HB3    1 
ATOM   5853 H  HG     . CYS A 1 380 ? -9.080  -0.843  -26.248 1.00 39.34  ? 379 CYS A HG     1 
ATOM   5854 N  N      . ALA A 1 381 ? -13.316 -0.313  -22.694 1.00 29.06  ? 380 ALA A N      1 
ATOM   5855 C  CA     . ALA A 1 381 ? -14.188 -0.849  -21.657 1.00 30.84  ? 380 ALA A CA     1 
ATOM   5856 C  C      . ALA A 1 381 ? -15.632 -0.409  -21.878 1.00 30.19  ? 380 ALA A C      1 
ATOM   5857 O  O      . ALA A 1 381 ? -16.569 -1.204  -21.730 1.00 31.04  ? 380 ALA A O      1 
ATOM   5858 C  CB     . ALA A 1 381 ? -13.663 -0.416  -20.285 1.00 30.14  ? 380 ALA A CB     1 
ATOM   5859 H  H      . ALA A 1 381 ? -12.735 0.261   -22.424 1.00 34.89  ? 380 ALA A H      1 
ATOM   5860 H  HA     . ALA A 1 381 ? -14.162 -1.818  -21.695 1.00 37.03  ? 380 ALA A HA     1 
ATOM   5861 H  HB1    . ALA A 1 381 ? -14.246 -0.775  -19.598 1.00 36.19  ? 380 ALA A HB1    1 
ATOM   5862 H  HB2    . ALA A 1 381 ? -12.763 -0.760  -20.169 1.00 36.19  ? 380 ALA A HB2    1 
ATOM   5863 H  HB3    . ALA A 1 381 ? -13.656 0.553   -20.241 1.00 36.19  ? 380 ALA A HB3    1 
ATOM   5864 N  N      . LYS A 1 382 ? -15.837 0.849   -22.246 1.00 29.33  ? 381 LYS A N      1 
ATOM   5865 C  CA     . LYS A 1 382 ? -17.193 1.381   -22.346 1.00 30.87  ? 381 LYS A CA     1 
ATOM   5866 C  C      . LYS A 1 382 ? -18.000 0.701   -23.450 1.00 29.38  ? 381 LYS A C      1 
ATOM   5867 O  O      . LYS A 1 382 ? -19.211 0.469   -23.290 1.00 30.94  ? 381 LYS A O      1 
ATOM   5868 C  CB     . LYS A 1 382 ? -17.120 2.889   -22.580 1.00 33.29  ? 381 LYS A CB     1 
ATOM   5869 C  CG     . LYS A 1 382 ? -18.454 3.538   -22.804 1.00 36.37  ? 381 LYS A CG     1 
ATOM   5870 C  CD     . LYS A 1 382 ? -18.310 5.035   -22.879 1.00 37.87  ? 381 LYS A CD     1 
ATOM   5871 C  CE     . LYS A 1 382 ? -19.668 5.696   -22.986 1.00 45.73  ? 381 LYS A CE     1 
ATOM   5872 N  NZ     . LYS A 1 382 ? -19.604 7.141   -22.646 1.00 48.59  1 381 LYS A NZ     1 
ATOM   5873 H  H      . LYS A 1 382 ? -15.217 1.412   -22.443 1.00 35.22  ? 381 LYS A H      1 
ATOM   5874 H  HA     . LYS A 1 382 ? -17.653 1.231   -21.505 1.00 37.07  ? 381 LYS A HA     1 
ATOM   5875 H  HB2    . LYS A 1 382 ? -16.716 3.306   -21.803 1.00 39.97  ? 381 LYS A HB2    1 
ATOM   5876 H  HB3    . LYS A 1 382 ? -16.574 3.057   -23.364 1.00 39.97  ? 381 LYS A HB3    1 
ATOM   5877 H  HG2    . LYS A 1 382 ? -18.829 3.224   -23.642 1.00 43.67  ? 381 LYS A HG2    1 
ATOM   5878 H  HG3    . LYS A 1 382 ? -19.046 3.323   -22.066 1.00 43.67  ? 381 LYS A HG3    1 
ATOM   5879 H  HD2    . LYS A 1 382 ? -17.874 5.358   -22.075 1.00 45.46  ? 381 LYS A HD2    1 
ATOM   5880 H  HD3    . LYS A 1 382 ? -17.791 5.271   -23.664 1.00 45.46  ? 381 LYS A HD3    1 
ATOM   5881 H  HE2    . LYS A 1 382 ? -19.992 5.613   -23.896 1.00 54.89  ? 381 LYS A HE2    1 
ATOM   5882 H  HE3    . LYS A 1 382 ? -20.282 5.266   -22.371 1.00 54.89  ? 381 LYS A HE3    1 
ATOM   5883 H  HZ1    . LYS A 1 382 ? -20.413 7.505   -22.716 1.00 58.33  ? 381 LYS A HZ1    1 
ATOM   5884 H  HZ2    . LYS A 1 382 ? -19.312 7.244   -21.811 1.00 58.33  ? 381 LYS A HZ2    1 
ATOM   5885 H  HZ3    . LYS A 1 382 ? -19.049 7.560   -23.200 1.00 58.33  ? 381 LYS A HZ3    1 
ATOM   5886 N  N      . TRP A 1 383 ? -17.365 0.394   -24.590 1.00 27.44  ? 382 TRP A N      1 
ATOM   5887 C  CA     . TRP A 1 383 ? -18.055 -0.232  -25.711 1.00 32.64  ? 382 TRP A CA     1 
ATOM   5888 C  C      . TRP A 1 383 ? -17.737 -1.718  -25.798 1.00 31.32  ? 382 TRP A C      1 
ATOM   5889 O  O      . TRP A 1 383 ? -18.102 -2.369  -26.776 1.00 30.50  ? 382 TRP A O      1 
ATOM   5890 C  CB     . TRP A 1 383 ? -17.718 0.507   -27.015 1.00 34.22  ? 382 TRP A CB     1 
ATOM   5891 C  CG     . TRP A 1 383 ? -18.292 1.889   -26.989 1.00 33.81  ? 382 TRP A CG     1 
ATOM   5892 C  CD1    . TRP A 1 383 ? -19.608 2.215   -26.824 1.00 41.91  ? 382 TRP A CD1    1 
ATOM   5893 C  CD2    . TRP A 1 383 ? -17.588 3.131   -27.095 1.00 29.62  ? 382 TRP A CD2    1 
ATOM   5894 N  NE1    . TRP A 1 383 ? -19.765 3.578   -26.808 1.00 39.97  ? 382 TRP A NE1    1 
ATOM   5895 C  CE2    . TRP A 1 383 ? -18.545 4.167   -26.975 1.00 33.10  ? 382 TRP A CE2    1 
ATOM   5896 C  CE3    . TRP A 1 383 ? -16.253 3.470   -27.287 1.00 30.85  ? 382 TRP A CE3    1 
ATOM   5897 C  CZ2    . TRP A 1 383 ? -18.201 5.514   -27.035 1.00 32.98  ? 382 TRP A CZ2    1 
ATOM   5898 C  CZ3    . TRP A 1 383 ? -15.919 4.816   -27.345 1.00 33.90  ? 382 TRP A CZ3    1 
ATOM   5899 C  CH2    . TRP A 1 383 ? -16.881 5.814   -27.206 1.00 32.38  ? 382 TRP A CH2    1 
ATOM   5900 H  H      . TRP A 1 383 ? -16.530 0.541   -24.733 1.00 32.95  ? 382 TRP A H      1 
ATOM   5901 H  HA     . TRP A 1 383 ? -19.010 -0.148  -25.568 1.00 39.18  ? 382 TRP A HA     1 
ATOM   5902 H  HB2    . TRP A 1 383 ? -16.755 0.575   -27.110 1.00 41.08  ? 382 TRP A HB2    1 
ATOM   5903 H  HB3    . TRP A 1 383 ? -18.101 0.028   -27.767 1.00 41.08  ? 382 TRP A HB3    1 
ATOM   5904 H  HD1    . TRP A 1 383 ? -20.296 1.600   -26.710 1.00 50.31  ? 382 TRP A HD1    1 
ATOM   5905 H  HE1    . TRP A 1 383 ? -20.512 3.994   -26.713 1.00 47.98  ? 382 TRP A HE1    1 
ATOM   5906 H  HE3    . TRP A 1 383 ? -15.599 2.813   -27.355 1.00 37.04  ? 382 TRP A HE3    1 
ATOM   5907 H  HZ2    . TRP A 1 383 ? -18.844 6.181   -26.963 1.00 39.60  ? 382 TRP A HZ2    1 
ATOM   5908 H  HZ3    . TRP A 1 383 ? -15.029 5.057   -27.459 1.00 40.70  ? 382 TRP A HZ3    1 
ATOM   5909 H  HH2    . TRP A 1 383 ? -16.622 6.706   -27.266 1.00 38.88  ? 382 TRP A HH2    1 
ATOM   5910 N  N      . ASN A 1 384 ? -17.071 -2.258  -24.776 1.00 30.11  ? 383 ASN A N      1 
ATOM   5911 C  CA     . ASN A 1 384 ? -16.830 -3.692  -24.646 1.00 31.64  ? 383 ASN A CA     1 
ATOM   5912 C  C      . ASN A 1 384 ? -16.068 -4.228  -25.859 1.00 30.18  ? 383 ASN A C      1 
ATOM   5913 O  O      . ASN A 1 384 ? -16.438 -5.228  -26.461 1.00 30.29  ? 383 ASN A O      1 
ATOM   5914 C  CB     . ASN A 1 384 ? -18.141 -4.448  -24.440 1.00 34.60  ? 383 ASN A CB     1 
ATOM   5915 C  CG     . ASN A 1 384 ? -17.915 -5.877  -24.023 1.00 40.25  ? 383 ASN A CG     1 
ATOM   5916 O  OD1    . ASN A 1 384 ? -16.942 -6.189  -23.342 1.00 40.83  ? 383 ASN A OD1    1 
ATOM   5917 N  ND2    . ASN A 1 384 ? -18.798 -6.760  -24.455 1.00 47.41  ? 383 ASN A ND2    1 
ATOM   5918 H  H      . ASN A 1 384 ? -16.740 -1.798  -24.129 1.00 36.16  ? 383 ASN A H      1 
ATOM   5919 H  HA     . ASN A 1 384 ? -16.278 -3.843  -23.863 1.00 37.99  ? 383 ASN A HA     1 
ATOM   5920 H  HB2    . ASN A 1 384 ? -18.655 -4.008  -23.745 1.00 41.54  ? 383 ASN A HB2    1 
ATOM   5921 H  HB3    . ASN A 1 384 ? -18.640 -4.451  -25.272 1.00 41.54  ? 383 ASN A HB3    1 
ATOM   5922 H  HD21   . ASN A 1 384 ? -18.714 -7.590  -24.245 1.00 56.91  ? 383 ASN A HD21   1 
ATOM   5923 H  HD22   . ASN A 1 384 ? -19.456 -6.505  -24.947 1.00 56.91  ? 383 ASN A HD22   1 
ATOM   5924 N  N      . THR A 1 385 ? -14.959 -3.567  -26.182 1.00 27.18  ? 384 THR A N      1 
ATOM   5925 C  CA     . THR A 1 385 ? -14.095 -3.979  -27.281 1.00 29.45  ? 384 THR A CA     1 
ATOM   5926 C  C      . THR A 1 385 ? -12.711 -4.416  -26.812 1.00 30.51  ? 384 THR A C      1 
ATOM   5927 O  O      . THR A 1 385 ? -11.817 -4.549  -27.649 1.00 28.90  ? 384 THR A O      1 
ATOM   5928 C  CB     . THR A 1 385 ? -13.958 -2.845  -28.296 1.00 30.33  ? 384 THR A CB     1 
ATOM   5929 O  OG1    . THR A 1 385 ? -13.416 -1.684  -27.636 1.00 32.81  ? 384 THR A OG1    1 
ATOM   5930 C  CG2    . THR A 1 385 ? -15.316 -2.504  -28.916 1.00 29.11  ? 384 THR A CG2    1 
ATOM   5931 H  H      . THR A 1 385 ? -14.682 -2.865  -25.770 1.00 32.63  ? 384 THR A H      1 
ATOM   5932 H  HA     . THR A 1 385 ? -14.505 -4.733  -27.733 1.00 35.36  ? 384 THR A HA     1 
ATOM   5933 H  HB     . THR A 1 385 ? -13.358 -3.120  -29.006 1.00 36.41  ? 384 THR A HB     1 
ATOM   5934 H  HG1    . THR A 1 385 ? -13.336 -1.053  -28.185 1.00 39.39  ? 384 THR A HG1    1 
ATOM   5935 H  HG21   . THR A 1 385 ? -15.216 -1.783  -29.557 1.00 34.95  ? 384 THR A HG21   1 
ATOM   5936 H  HG22   . THR A 1 385 ? -15.678 -3.281  -29.369 1.00 34.95  ? 384 THR A HG22   1 
ATOM   5937 H  HG23   . THR A 1 385 ? -15.936 -2.225  -28.224 1.00 34.95  ? 384 THR A HG23   1 
ATOM   5938 N  N      . GLU A 1 386 ? -12.517 -4.687  -25.503 1.00 30.51  ? 385 GLU A N      1 
ATOM   5939 C  CA     . GLU A 1 386 ? -11.165 -4.993  -25.018 1.00 31.14  ? 385 GLU A CA     1 
ATOM   5940 C  C      . GLU A 1 386 ? -10.608 -6.257  -25.672 1.00 34.89  ? 385 GLU A C      1 
ATOM   5941 O  O      . GLU A 1 386 ? -9.398  -6.345  -25.897 1.00 36.53  ? 385 GLU A O      1 
ATOM   5942 C  CB     . GLU A 1 386 ? -11.140 -5.139  -23.497 1.00 35.83  ? 385 GLU A CB     1 
ATOM   5943 C  CG     . GLU A 1 386 ? -11.282 -3.810  -22.748 1.00 46.18  ? 385 GLU A CG     1 
ATOM   5944 C  CD     . GLU A 1 386 ? -11.495 -3.961  -21.238 1.00 53.90  ? 385 GLU A CD     1 
ATOM   5945 O  OE1    . GLU A 1 386 ? -12.575 -4.439  -20.822 1.00 57.01  ? 385 GLU A OE1    1 
ATOM   5946 O  OE2    . GLU A 1 386 ? -10.581 -3.588  -20.467 1.00 55.72  1 385 GLU A OE2    1 
ATOM   5947 H  H      . GLU A 1 386 ? -13.131 -4.699  -24.901 1.00 36.63  ? 385 GLU A H      1 
ATOM   5948 H  HA     . GLU A 1 386 ? -10.578 -4.257  -25.252 1.00 37.38  ? 385 GLU A HA     1 
ATOM   5949 H  HB2    . GLU A 1 386 ? -11.874 -5.713  -23.225 1.00 43.02  ? 385 GLU A HB2    1 
ATOM   5950 H  HB3    . GLU A 1 386 ? -10.296 -5.539  -23.234 1.00 43.02  ? 385 GLU A HB3    1 
ATOM   5951 H  HG2    . GLU A 1 386 ? -10.475 -3.289  -22.882 1.00 55.44  ? 385 GLU A HG2    1 
ATOM   5952 H  HG3    . GLU A 1 386 ? -12.045 -3.330  -23.107 1.00 55.44  ? 385 GLU A HG3    1 
ATOM   5953 N  N      . ASP A 1 387 ? -11.465 -7.235  -25.988 1.00 34.04  ? 386 ASP A N      1 
ATOM   5954 C  CA     . ASP A 1 387 ? -11.054 -8.485  -26.627 1.00 36.82  ? 386 ASP A CA     1 
ATOM   5955 C  C      . ASP A 1 387 ? -11.247 -8.468  -28.144 1.00 37.26  ? 386 ASP A C      1 
ATOM   5956 O  O      . ASP A 1 387 ? -11.161 -9.521  -28.789 1.00 37.87  ? 386 ASP A O      1 
ATOM   5957 C  CB     . ASP A 1 387 ? -11.828 -9.666  -26.035 1.00 52.09  ? 386 ASP A CB     1 
ATOM   5958 C  CG     . ASP A 1 387 ? -11.558 -9.866  -24.542 1.00 78.65  ? 386 ASP A CG     1 
ATOM   5959 O  OD1    . ASP A 1 387 ? -10.416 -9.608  -24.096 1.00 87.86  ? 386 ASP A OD1    1 
ATOM   5960 O  OD2    . ASP A 1 387 ? -12.488 -10.286 -23.811 1.00 89.66  1 386 ASP A OD2    1 
ATOM   5961 H  H      . ASP A 1 387 ? -12.310 -7.192  -25.838 1.00 40.86  ? 386 ASP A H      1 
ATOM   5962 H  HA     . ASP A 1 387 ? -10.112 -8.630  -26.450 1.00 44.21  ? 386 ASP A HA     1 
ATOM   5963 H  HB2    . ASP A 1 387 ? -12.778 -9.510  -26.150 1.00 62.53  ? 386 ASP A HB2    1 
ATOM   5964 H  HB3    . ASP A 1 387 ? -11.567 -10.477 -26.498 1.00 62.53  ? 386 ASP A HB3    1 
ATOM   5965 N  N      . LYS A 1 388 ? -11.517 -7.307  -28.732 1.00 34.53  ? 387 LYS A N      1 
ATOM   5966 C  CA     . LYS A 1 388 ? -11.776 -7.220  -30.161 1.00 32.21  ? 387 LYS A CA     1 
ATOM   5967 C  C      . LYS A 1 388 ? -10.727 -6.393  -30.881 1.00 29.71  ? 387 LYS A C      1 
ATOM   5968 O  O      . LYS A 1 388 ? -10.902 -6.095  -32.061 1.00 32.55  ? 387 LYS A O      1 
ATOM   5969 C  CB     . LYS A 1 388 ? -13.169 -6.643  -30.404 1.00 29.49  ? 387 LYS A CB     1 
ATOM   5970 C  CG     . LYS A 1 388 ? -14.297 -7.532  -29.896 1.00 31.87  ? 387 LYS A CG     1 
ATOM   5971 C  CD     . LYS A 1 388 ? -15.648 -6.872  -30.111 1.00 42.32  ? 387 LYS A CD     1 
ATOM   5972 C  CE     . LYS A 1 388 ? -16.812 -7.780  -29.739 1.00 54.12  ? 387 LYS A CE     1 
ATOM   5973 N  NZ     . LYS A 1 388 ? -17.297 -7.493  -28.375 1.00 62.48  1 387 LYS A NZ     1 
ATOM   5974 H  H      . LYS A 1 388 ? -11.557 -6.552  -28.322 1.00 41.46  ? 387 LYS A H      1 
ATOM   5975 H  HA     . LYS A 1 388 ? -11.756 -8.115  -30.536 1.00 38.67  ? 387 LYS A HA     1 
ATOM   5976 H  HB2    . LYS A 1 388 ? -13.237 -5.789  -29.949 1.00 35.41  ? 387 LYS A HB2    1 
ATOM   5977 H  HB3    . LYS A 1 388 ? -13.295 -6.520  -31.357 1.00 35.41  ? 387 LYS A HB3    1 
ATOM   5978 H  HG2    . LYS A 1 388 ? -14.287 -8.372  -30.380 1.00 38.26  ? 387 LYS A HG2    1 
ATOM   5979 H  HG3    . LYS A 1 388 ? -14.181 -7.688  -28.946 1.00 38.26  ? 387 LYS A HG3    1 
ATOM   5980 H  HD2    . LYS A 1 388 ? -15.701 -6.075  -29.560 1.00 50.80  ? 387 LYS A HD2    1 
ATOM   5981 H  HD3    . LYS A 1 388 ? -15.739 -6.636  -31.047 1.00 50.80  ? 387 LYS A HD3    1 
ATOM   5982 H  HE2    . LYS A 1 388 ? -17.543 -7.634  -30.360 1.00 64.97  ? 387 LYS A HE2    1 
ATOM   5983 H  HE3    . LYS A 1 388 ? -16.521 -8.704  -29.772 1.00 64.97  ? 387 LYS A HE3    1 
ATOM   5984 H  HZ1    . LYS A 1 388 ? -16.643 -7.623  -27.786 1.00 74.99  ? 387 LYS A HZ1    1 
ATOM   5985 H  HZ2    . LYS A 1 388 ? -17.572 -6.649  -28.321 1.00 74.99  ? 387 LYS A HZ2    1 
ATOM   5986 H  HZ3    . LYS A 1 388 ? -17.977 -8.032  -28.175 1.00 74.99  ? 387 LYS A HZ3    1 
ATOM   5987 N  N      . VAL A 1 389 ? -9.659  -6.001  -30.192 1.00 26.58  ? 388 VAL A N      1 
ATOM   5988 C  CA     . VAL A 1 389 ? -8.507  -5.337  -30.782 1.00 25.87  ? 388 VAL A CA     1 
ATOM   5989 C  C      . VAL A 1 389 ? -7.295  -6.168  -30.421 1.00 27.06  ? 388 VAL A C      1 
ATOM   5990 O  O      . VAL A 1 389 ? -7.362  -7.051  -29.567 1.00 29.60  ? 388 VAL A O      1 
ATOM   5991 C  CB     . VAL A 1 389 ? -8.356  -3.881  -30.311 1.00 26.99  ? 388 VAL A CB     1 
ATOM   5992 C  CG1    . VAL A 1 389 ? -9.557  -3.067  -30.728 1.00 28.47  ? 388 VAL A CG1    1 
ATOM   5993 C  CG2    . VAL A 1 389 ? -8.217  -3.806  -28.835 1.00 26.81  ? 388 VAL A CG2    1 
ATOM   5994 H  H      . VAL A 1 389 ? -9.579  -6.116  -29.343 1.00 31.92  ? 388 VAL A H      1 
ATOM   5995 H  HA     . VAL A 1 389 ? -8.599  -5.335  -31.748 1.00 31.06  ? 388 VAL A HA     1 
ATOM   5996 H  HB     . VAL A 1 389 ? -7.565  -3.490  -30.714 1.00 32.41  ? 388 VAL A HB     1 
ATOM   5997 H  HG11   . VAL A 1 389 ? -9.441  -2.154  -30.422 1.00 34.18  ? 388 VAL A HG11   1 
ATOM   5998 H  HG12   . VAL A 1 389 ? -9.629  -3.085  -31.695 1.00 34.18  ? 388 VAL A HG12   1 
ATOM   5999 H  HG13   . VAL A 1 389 ? -10.353 -3.452  -30.329 1.00 34.18  ? 388 VAL A HG13   1 
ATOM   6000 H  HG21   . VAL A 1 389 ? -8.123  -2.876  -28.574 1.00 32.19  ? 388 VAL A HG21   1 
ATOM   6001 H  HG22   . VAL A 1 389 ? -9.008  -4.187  -28.424 1.00 32.19  ? 388 VAL A HG22   1 
ATOM   6002 H  HG23   . VAL A 1 389 ? -7.430  -4.306  -28.566 1.00 32.19  ? 388 VAL A HG23   1 
ATOM   6003 N  N      . SER A 1 390 ? -6.168  -5.889  -31.083 1.00 27.22  ? 389 SER A N      1 
ATOM   6004 C  CA     . SER A 1 390 ? -5.004  -6.755  -30.893 1.00 28.50  ? 389 SER A CA     1 
ATOM   6005 C  C      . SER A 1 390 ? -4.402  -6.598  -29.500 1.00 27.18  ? 389 SER A C      1 
ATOM   6006 O  O      . SER A 1 390 ? -3.970  -7.588  -28.891 1.00 30.68  ? 389 SER A O      1 
ATOM   6007 C  CB     . SER A 1 390 ? -3.940  -6.482  -31.953 1.00 28.30  ? 389 SER A CB     1 
ATOM   6008 O  OG     . SER A 1 390 ? -4.471  -6.619  -33.254 1.00 27.32  ? 389 SER A OG     1 
ATOM   6009 H  H      . SER A 1 390 ? -6.055  -5.232  -31.627 1.00 32.69  ? 389 SER A H      1 
ATOM   6010 H  HA     . SER A 1 390 ? -5.286  -7.679  -30.990 1.00 34.21  ? 389 SER A HA     1 
ATOM   6011 H  HB2    . SER A 1 390 ? -3.610  -5.576  -31.841 1.00 33.98  ? 389 SER A HB2    1 
ATOM   6012 H  HB3    . SER A 1 390 ? -3.214  -7.114  -31.840 1.00 33.98  ? 389 SER A HB3    1 
ATOM   6013 H  HG     . SER A 1 390 ? -4.760  -7.400  -33.365 1.00 32.80  ? 389 SER A HG     1 
ATOM   6014 N  N      . HIS A 1 391 ? -4.352  -5.375  -28.975 1.00 23.20  ? 390 HIS A N      1 
ATOM   6015 C  CA     . HIS A 1 391 ? -3.714  -5.136  -27.684 1.00 23.35  ? 390 HIS A CA     1 
ATOM   6016 C  C      . HIS A 1 391 ? -4.275  -3.852  -27.114 1.00 22.07  ? 390 HIS A C      1 
ATOM   6017 O  O      . HIS A 1 391 ? -4.396  -2.860  -27.839 1.00 24.29  ? 390 HIS A O      1 
ATOM   6018 C  CB     . HIS A 1 391 ? -2.189  -5.023  -27.850 1.00 26.12  ? 390 HIS A CB     1 
ATOM   6019 C  CG     . HIS A 1 391 ? -1.426  -4.801  -26.579 1.00 31.39  ? 390 HIS A CG     1 
ATOM   6020 N  ND1    . HIS A 1 391 ? -1.208  -5.801  -25.659 1.00 34.36  ? 390 HIS A ND1    1 
ATOM   6021 C  CD2    . HIS A 1 391 ? -0.757  -3.716  -26.119 1.00 32.96  ? 390 HIS A CD2    1 
ATOM   6022 C  CE1    . HIS A 1 391 ? -0.476  -5.331  -24.665 1.00 35.28  ? 390 HIS A CE1    1 
ATOM   6023 N  NE2    . HIS A 1 391 ? -0.186  -4.068  -24.920 1.00 33.61  ? 390 HIS A NE2    1 
ATOM   6024 H  H      . HIS A 1 391 ? -4.679  -4.670  -29.344 1.00 27.86  ? 390 HIS A H      1 
ATOM   6025 H  HA     . HIS A 1 391 ? -3.913  -5.865  -27.076 1.00 28.04  ? 390 HIS A HA     1 
ATOM   6026 H  HB2    . HIS A 1 391 ? -1.861  -5.844  -28.248 1.00 31.36  ? 390 HIS A HB2    1 
ATOM   6027 H  HB3    . HIS A 1 391 ? -1.998  -4.277  -28.439 1.00 31.36  ? 390 HIS A HB3    1 
ATOM   6028 H  HD2    . HIS A 1 391 ? -0.710  -2.883  -26.528 1.00 39.57  ? 390 HIS A HD2    1 
ATOM   6029 H  HE1    . HIS A 1 391 ? -0.207  -5.810  -23.915 1.00 42.35  ? 390 HIS A HE1    1 
ATOM   6030 H  HE2    . HIS A 1 391 ? 0.280   -3.550  -24.416 1.00 40.35  ? 390 HIS A HE2    1 
ATOM   6031 N  N      . VAL A 1 392 ? -4.640  -3.875  -25.835 1.00 22.01  ? 391 VAL A N      1 
ATOM   6032 C  CA     . VAL A 1 392 ? -5.021  -2.673  -25.104 1.00 21.45  ? 391 VAL A CA     1 
ATOM   6033 C  C      . VAL A 1 392 ? -3.916  -2.413  -24.080 1.00 22.06  ? 391 VAL A C      1 
ATOM   6034 O  O      . VAL A 1 392 ? -3.675  -3.244  -23.205 1.00 22.46  ? 391 VAL A O      1 
ATOM   6035 C  CB     . VAL A 1 392 ? -6.396  -2.822  -24.436 1.00 24.84  ? 391 VAL A CB     1 
ATOM   6036 C  CG1    . VAL A 1 392 ? -6.736  -1.571  -23.673 1.00 24.34  ? 391 VAL A CG1    1 
ATOM   6037 C  CG2    . VAL A 1 392 ? -7.464  -3.093  -25.505 1.00 27.49  ? 391 VAL A CG2    1 
ATOM   6038 H  H      . VAL A 1 392 ? -4.676  -4.591  -25.360 1.00 26.43  ? 391 VAL A H      1 
ATOM   6039 H  HA     . VAL A 1 392 ? -5.057  -1.921  -25.716 1.00 25.75  ? 391 VAL A HA     1 
ATOM   6040 H  HB     . VAL A 1 392 ? -6.379  -3.569  -23.817 1.00 29.83  ? 391 VAL A HB     1 
ATOM   6041 H  HG11   . VAL A 1 392 ? -7.605  -1.681  -23.258 1.00 29.23  ? 391 VAL A HG11   1 
ATOM   6042 H  HG12   . VAL A 1 392 ? -6.060  -1.423  -22.993 1.00 29.23  ? 391 VAL A HG12   1 
ATOM   6043 H  HG13   . VAL A 1 392 ? -6.755  -0.822  -24.289 1.00 29.23  ? 391 VAL A HG13   1 
ATOM   6044 H  HG21   . VAL A 1 392 ? -8.328  -3.185  -25.072 1.00 33.01  ? 391 VAL A HG21   1 
ATOM   6045 H  HG22   . VAL A 1 392 ? -7.484  -2.349  -26.127 1.00 33.01  ? 391 VAL A HG22   1 
ATOM   6046 H  HG23   . VAL A 1 392 ? -7.240  -3.912  -25.975 1.00 33.01  ? 391 VAL A HG23   1 
ATOM   6047 N  N      . SER A 1 393 ? -3.221  -1.289  -24.218 1.00 23.07  ? 392 SER A N      1 
ATOM   6048 C  CA     . SER A 1 393 ? -2.096  -0.935  -23.363 1.00 24.69  ? 392 SER A CA     1 
ATOM   6049 C  C      . SER A 1 393 ? -2.537  -0.004  -22.239 1.00 21.66  ? 392 SER A C      1 
ATOM   6050 O  O      . SER A 1 393 ? -3.425  0.831   -22.417 1.00 20.60  ? 392 SER A O      1 
ATOM   6051 C  CB     . SER A 1 393 ? -1.009  -0.243  -24.180 1.00 26.89  ? 392 SER A CB     1 
ATOM   6052 O  OG     . SER A 1 393 ? 0.086   0.108   -23.358 1.00 24.85  ? 392 SER A OG     1 
ATOM   6053 H  H      . SER A 1 393 ? -3.389  -0.698  -24.820 1.00 27.71  ? 392 SER A H      1 
ATOM   6054 H  HA     . SER A 1 393 ? -1.722  -1.738  -22.969 1.00 29.65  ? 392 SER A HA     1 
ATOM   6055 H  HB2    . SER A 1 393 ? -0.702  -0.847  -24.874 1.00 32.28  ? 392 SER A HB2    1 
ATOM   6056 H  HB3    . SER A 1 393 ? -1.376  0.562   -24.578 1.00 32.28  ? 392 SER A HB3    1 
ATOM   6057 H  HG     . SER A 1 393 ? 0.413   -0.581  -23.005 1.00 29.83  ? 392 SER A HG     1 
ATOM   6058 N  N      . THR A 1 394 ? -1.866  -0.127  -21.082 1.00 20.87  ? 393 THR A N      1 
ATOM   6059 C  CA     . THR A 1 394 ? -2.053  0.829   -20.002 1.00 24.45  ? 393 THR A CA     1 
ATOM   6060 C  C      . THR A 1 394 ? -1.312  2.132   -20.248 1.00 24.92  ? 393 THR A C      1 
ATOM   6061 O  O      . THR A 1 394 ? -1.496  3.084   -19.484 1.00 26.55  ? 393 THR A O      1 
ATOM   6062 C  CB     . THR A 1 394 ? -1.593  0.231   -18.674 1.00 23.49  ? 393 THR A CB     1 
ATOM   6063 O  OG1    . THR A 1 394 ? -0.208  -0.111  -18.739 1.00 21.12  ? 393 THR A OG1    1 
ATOM   6064 C  CG2    . THR A 1 394 ? -2.375  -1.045  -18.368 1.00 25.51  ? 393 THR A CG2    1 
ATOM   6065 H  H      . THR A 1 394 ? -1.303  -0.753  -20.908 1.00 25.06  ? 393 THR A H      1 
ATOM   6066 H  HA     . THR A 1 394 ? -2.998  1.034   -19.925 1.00 29.36  ? 393 THR A HA     1 
ATOM   6067 H  HB     . THR A 1 394 ? -1.741  0.868   -17.958 1.00 28.20  ? 393 THR A HB     1 
ATOM   6068 H  HG1    . THR A 1 394 ? -0.080  -0.675  -19.349 1.00 25.36  ? 393 THR A HG1    1 
ATOM   6069 H  HG21   . THR A 1 394 ? -2.079  -1.421  -17.524 1.00 30.64  ? 393 THR A HG21   1 
ATOM   6070 H  HG22   . THR A 1 394 ? -3.323  -0.847  -18.310 1.00 30.64  ? 393 THR A HG22   1 
ATOM   6071 H  HG23   . THR A 1 394 ? -2.232  -1.698  -19.071 1.00 30.64  ? 393 THR A HG23   1 
ATOM   6072 N  N      . GLY A 1 395 ? -0.484  2.203   -21.279 1.00 20.00  ? 394 GLY A N      1 
ATOM   6073 C  CA     . GLY A 1 395 ? 0.290   3.397   -21.566 1.00 22.95  ? 394 GLY A CA     1 
ATOM   6074 C  C      . GLY A 1 395 ? -0.263  4.167   -22.756 1.00 25.59  ? 394 GLY A C      1 
ATOM   6075 O  O      . GLY A 1 395 ? -0.570  3.583   -23.796 1.00 24.58  ? 394 GLY A O      1 
ATOM   6076 H  H      . GLY A 1 395 ? -0.352  1.561   -21.836 1.00 24.02  ? 394 GLY A H      1 
ATOM   6077 H  HA2    . GLY A 1 395 ? 0.284   3.981   -20.791 1.00 27.56  ? 394 GLY A HA2    1 
ATOM   6078 H  HA3    . GLY A 1 395 ? 1.208   3.150   -21.758 1.00 27.56  ? 394 GLY A HA3    1 
ATOM   6079 N  N      . GLY A 1 396 ? -0.366  5.482   -22.577 1.00 23.45  ? 395 GLY A N      1 
ATOM   6080 C  CA     . GLY A 1 396 ? -0.780  6.351   -23.653 1.00 19.88  ? 395 GLY A CA     1 
ATOM   6081 C  C      . GLY A 1 396 ? 0.412   7.143   -24.135 1.00 19.28  ? 395 GLY A C      1 
ATOM   6082 O  O      . GLY A 1 396 ? 1.101   6.729   -25.069 1.00 21.03  ? 395 GLY A O      1 
ATOM   6083 H  H      . GLY A 1 396 ? -0.199  5.888   -21.838 1.00 28.16  ? 395 GLY A H      1 
ATOM   6084 H  HA2    . GLY A 1 396 ? -1.133  5.827   -24.390 1.00 23.87  ? 395 GLY A HA2    1 
ATOM   6085 H  HA3    . GLY A 1 396 ? -1.465  6.964   -23.343 1.00 23.87  ? 395 GLY A HA3    1 
ATOM   6086 N  N      . GLY A 1 397 ? 0.688   8.264   -23.484 1.00 20.48  ? 396 GLY A N      1 
ATOM   6087 C  CA     . GLY A 1 397 ? 1.929   8.969   -23.759 1.00 23.70  ? 396 GLY A CA     1 
ATOM   6088 C  C      . GLY A 1 397 ? 3.134   8.055   -23.690 1.00 24.42  ? 396 GLY A C      1 
ATOM   6089 O  O      . GLY A 1 397 ? 4.066   8.171   -24.496 1.00 23.77  ? 396 GLY A O      1 
ATOM   6090 H  H      . GLY A 1 397 ? 0.186   8.631   -22.890 1.00 24.60  ? 396 GLY A H      1 
ATOM   6091 H  HA2    . GLY A 1 397 ? 1.890   9.360   -24.646 1.00 28.46  ? 396 GLY A HA2    1 
ATOM   6092 H  HA3    . GLY A 1 397 ? 2.047   9.683   -23.113 1.00 28.46  ? 396 GLY A HA3    1 
ATOM   6093 N  N      . ALA A 1 398 ? 3.142   7.127   -22.728 1.00 19.38  ? 397 ALA A N      1 
ATOM   6094 C  CA     . ALA A 1 398 ? 4.280   6.227   -22.635 1.00 19.63  ? 397 ALA A CA     1 
ATOM   6095 C  C      . ALA A 1 398 ? 4.430   5.386   -23.901 1.00 20.65  ? 397 ALA A C      1 
ATOM   6096 O  O      . ALA A 1 398 ? 5.548   5.124   -24.352 1.00 19.45  ? 397 ALA A O      1 
ATOM   6097 C  CB     . ALA A 1 398 ? 4.143   5.312   -21.433 1.00 19.69  ? 397 ALA A CB     1 
ATOM   6098 H  H      . ALA A 1 398 ? 2.525   7.005   -22.141 1.00 23.28  ? 397 ALA A H      1 
ATOM   6099 H  HA     . ALA A 1 398 ? 5.089   6.751   -22.524 1.00 23.57  ? 397 ALA A HA     1 
ATOM   6100 H  HB1    . ALA A 1 398 ? 4.913   4.723   -21.395 1.00 23.65  ? 397 ALA A HB1    1 
ATOM   6101 H  HB2    . ALA A 1 398 ? 4.099   5.852   -20.628 1.00 23.65  ? 397 ALA A HB2    1 
ATOM   6102 H  HB3    . ALA A 1 398 ? 3.331   4.789   -21.526 1.00 23.65  ? 397 ALA A HB3    1 
ATOM   6103 N  N      . SER A 1 399 ? 3.319   4.906   -24.459 1.00 21.40  ? 398 SER A N      1 
ATOM   6104 C  CA     . SER A 1 399 ? 3.394   4.120   -25.700 1.00 21.07  ? 398 SER A CA     1 
ATOM   6105 C  C      . SER A 1 399 ? 3.839   4.971   -26.887 1.00 20.53  ? 398 SER A C      1 
ATOM   6106 O  O      . SER A 1 399 ? 4.540   4.484   -27.776 1.00 23.27  ? 398 SER A O      1 
ATOM   6107 C  CB     . SER A 1 399 ? 2.041   3.461   -25.995 1.00 24.08  ? 398 SER A CB     1 
ATOM   6108 O  OG     . SER A 1 399 ? 1.668   2.652   -24.875 1.00 27.37  ? 398 SER A OG     1 
ATOM   6109 H  H      . SER A 1 399 ? 2.524   5.016   -24.150 1.00 25.70  ? 398 SER A H      1 
ATOM   6110 H  HA     . SER A 1 399 ? 4.048   3.413   -25.582 1.00 25.30  ? 398 SER A HA     1 
ATOM   6111 H  HB2    . SER A 1 399 ? 1.371   4.149   -26.133 1.00 28.91  ? 398 SER A HB2    1 
ATOM   6112 H  HB3    . SER A 1 399 ? 2.120   2.903   -26.784 1.00 28.91  ? 398 SER A HB3    1 
ATOM   6113 H  HG     . SER A 1 399 ? 0.927   2.283   -25.021 1.00 32.87  ? 398 SER A HG     1 
ATOM   6114 N  N      . LEU A 1 400 ? 3.421   6.232   -26.933 1.00 19.18  ? 399 LEU A N      1 
ATOM   6115 C  CA     . LEU A 1 400 ? 3.854   7.114   -28.006 1.00 21.80  ? 399 LEU A CA     1 
ATOM   6116 C  C      . LEU A 1 400 ? 5.349   7.364   -27.950 1.00 24.63  ? 399 LEU A C      1 
ATOM   6117 O  O      . LEU A 1 400 ? 6.007   7.462   -28.996 1.00 23.95  ? 399 LEU A O      1 
ATOM   6118 C  CB     . LEU A 1 400 ? 3.105   8.437   -27.949 1.00 24.76  ? 399 LEU A CB     1 
ATOM   6119 C  CG     . LEU A 1 400 ? 1.601   8.343   -28.215 1.00 26.62  ? 399 LEU A CG     1 
ATOM   6120 C  CD1    . LEU A 1 400 ? 1.037   9.730   -28.154 1.00 30.76  ? 399 LEU A CD1    1 
ATOM   6121 C  CD2    . LEU A 1 400 ? 1.288   7.726   -29.564 1.00 26.72  ? 399 LEU A CD2    1 
ATOM   6122 H  H      . LEU A 1 400 ? 2.892   6.597   -26.361 1.00 23.04  ? 399 LEU A H      1 
ATOM   6123 H  HA     . LEU A 1 400 ? 3.653   6.694   -28.857 1.00 26.18  ? 399 LEU A HA     1 
ATOM   6124 H  HB2    . LEU A 1 400 ? 3.222   8.819   -27.066 1.00 29.73  ? 399 LEU A HB2    1 
ATOM   6125 H  HB3    . LEU A 1 400 ? 3.482   9.033   -28.615 1.00 29.73  ? 399 LEU A HB3    1 
ATOM   6126 H  HG     . LEU A 1 400 ? 1.180   7.807   -27.524 1.00 31.96  ? 399 LEU A HG     1 
ATOM   6127 H  HD11   . LEU A 1 400 ? 0.082   9.691   -28.321 1.00 36.93  ? 399 LEU A HD11   1 
ATOM   6128 H  HD12   . LEU A 1 400 ? 1.205   10.100  -27.273 1.00 36.93  ? 399 LEU A HD12   1 
ATOM   6129 H  HD13   . LEU A 1 400 ? 1.469   10.276  -28.830 1.00 36.93  ? 399 LEU A HD13   1 
ATOM   6130 H  HD21   . LEU A 1 400 ? 0.326   7.691   -29.680 1.00 32.09  ? 399 LEU A HD21   1 
ATOM   6131 H  HD22   . LEU A 1 400 ? 1.686   8.272   -30.260 1.00 32.09  ? 399 LEU A HD22   1 
ATOM   6132 H  HD23   . LEU A 1 400 ? 1.658   6.830   -29.594 1.00 32.09  ? 399 LEU A HD23   1 
ATOM   6133 N  N      . GLU A 1 401 ? 5.914   7.490   -26.744 1.00 21.66  ? 400 GLU A N      1 
ATOM   6134 C  CA     . GLU A 1 401 ? 7.362   7.677   -26.656 1.00 21.81  ? 400 GLU A CA     1 
ATOM   6135 C  C      . GLU A 1 401 ? 8.123   6.433   -27.129 1.00 19.71  ? 400 GLU A C      1 
ATOM   6136 O  O      . GLU A 1 401 ? 9.189   6.564   -27.741 1.00 21.56  ? 400 GLU A O      1 
ATOM   6137 C  CB     . GLU A 1 401 ? 7.762   8.110   -25.231 1.00 26.31  ? 400 GLU A CB     1 
ATOM   6138 C  CG     . GLU A 1 401 ? 7.056   9.444   -24.870 1.00 35.58  ? 400 GLU A CG     1 
ATOM   6139 C  CD     . GLU A 1 401 ? 7.905   10.469  -24.096 1.00 45.19  ? 400 GLU A CD     1 
ATOM   6140 O  OE1    . GLU A 1 401 ? 9.150   10.370  -24.113 1.00 48.58  ? 400 GLU A OE1    1 
ATOM   6141 O  OE2    . GLU A 1 401 ? 7.308   11.391  -23.477 1.00 44.83  1 400 GLU A OE2    1 
ATOM   6142 H  H      . GLU A 1 401 ? 5.498   7.472   -25.991 1.00 26.01  ? 400 GLU A H      1 
ATOM   6143 H  HA     . GLU A 1 401 ? 7.607   8.402   -27.251 1.00 26.19  ? 400 GLU A HA     1 
ATOM   6144 H  HB2    . GLU A 1 401 ? 7.487   7.432   -24.595 1.00 31.59  ? 400 GLU A HB2    1 
ATOM   6145 H  HB3    . GLU A 1 401 ? 8.722   8.247   -25.190 1.00 31.59  ? 400 GLU A HB3    1 
ATOM   6146 H  HG2    . GLU A 1 401 ? 6.768   9.870   -25.692 1.00 42.71  ? 400 GLU A HG2    1 
ATOM   6147 H  HG3    . GLU A 1 401 ? 6.280   9.241   -24.324 1.00 42.71  ? 400 GLU A HG3    1 
ATOM   6148 N  N      . LEU A 1 402 ? 7.574   5.242   -26.950 1.00 21.70  ? 401 LEU A N      1 
ATOM   6149 C  CA     . LEU A 1 402 ? 8.203   4.057   -27.546 1.00 23.02  ? 401 LEU A CA     1 
ATOM   6150 C  C      . LEU A 1 402 ? 8.110   4.083   -29.071 1.00 24.99  ? 401 LEU A C      1 
ATOM   6151 O  O      . LEU A 1 402 ? 9.047   3.687   -29.779 1.00 26.32  ? 401 LEU A O      1 
ATOM   6152 C  CB     . LEU A 1 402 ? 7.538   2.786   -27.031 1.00 21.14  ? 401 LEU A CB     1 
ATOM   6153 C  CG     . LEU A 1 402 ? 7.823   2.409   -25.578 1.00 23.06  ? 401 LEU A CG     1 
ATOM   6154 C  CD1    . LEU A 1 402 ? 7.020   1.169   -25.235 1.00 25.68  ? 401 LEU A CD1    1 
ATOM   6155 C  CD2    . LEU A 1 402 ? 9.298   2.172   -25.332 1.00 24.38  ? 401 LEU A CD2    1 
ATOM   6156 H  H      . LEU A 1 402 ? 6.857   5.087   -26.502 1.00 26.06  ? 401 LEU A H      1 
ATOM   6157 H  HA     . LEU A 1 402 ? 9.140   4.032   -27.298 1.00 27.65  ? 401 LEU A HA     1 
ATOM   6158 H  HB2    . LEU A 1 402 ? 6.577   2.890   -27.118 1.00 25.38  ? 401 LEU A HB2    1 
ATOM   6159 H  HB3    . LEU A 1 402 ? 7.832   2.045   -27.584 1.00 25.38  ? 401 LEU A HB3    1 
ATOM   6160 H  HG     . LEU A 1 402 ? 7.530   3.129   -24.998 1.00 27.69  ? 401 LEU A HG     1 
ATOM   6161 H  HD11   . LEU A 1 402 ? 7.197   0.924   -24.313 1.00 30.83  ? 401 LEU A HD11   1 
ATOM   6162 H  HD12   . LEU A 1 402 ? 6.076   1.361   -25.351 1.00 30.83  ? 401 LEU A HD12   1 
ATOM   6163 H  HD13   . LEU A 1 402 ? 7.286   0.447   -25.826 1.00 30.83  ? 401 LEU A HD13   1 
ATOM   6164 H  HD21   . LEU A 1 402 ? 9.428   1.937   -24.400 1.00 29.27  ? 401 LEU A HD21   1 
ATOM   6165 H  HD22   . LEU A 1 402 ? 9.601   1.449   -25.902 1.00 29.27  ? 401 LEU A HD22   1 
ATOM   6166 H  HD23   . LEU A 1 402 ? 9.787   2.984   -25.539 1.00 29.27  ? 401 LEU A HD23   1 
ATOM   6167 N  N      . LEU A 1 403 ? 6.971   4.521   -29.596 1.00 22.14  ? 402 LEU A N      1 
ATOM   6168 C  CA     . LEU A 1 403 ? 6.832   4.642   -31.041 1.00 21.98  ? 402 LEU A CA     1 
ATOM   6169 C  C      . LEU A 1 403 ? 7.897   5.579   -31.604 1.00 24.98  ? 402 LEU A C      1 
ATOM   6170 O  O      . LEU A 1 403 ? 8.498   5.305   -32.650 1.00 28.89  ? 402 LEU A O      1 
ATOM   6171 C  CB     . LEU A 1 403 ? 5.418   5.115   -31.340 1.00 21.70  ? 402 LEU A CB     1 
ATOM   6172 C  CG     . LEU A 1 403 ? 5.063   5.455   -32.787 1.00 27.08  ? 402 LEU A CG     1 
ATOM   6173 C  CD1    . LEU A 1 403 ? 5.464   4.336   -33.686 1.00 32.55  ? 402 LEU A CD1    1 
ATOM   6174 C  CD2    . LEU A 1 403 ? 3.557   5.686   -32.804 1.00 27.94  ? 402 LEU A CD2    1 
ATOM   6175 H  H      . LEU A 1 403 ? 6.275   4.751   -29.147 1.00 26.59  ? 402 LEU A H      1 
ATOM   6176 H  HA     . LEU A 1 403 ? 6.952   3.769   -31.447 1.00 26.39  ? 402 LEU A HA     1 
ATOM   6177 H  HB2    . LEU A 1 403 ? 4.805   4.418   -31.056 1.00 26.07  ? 402 LEU A HB2    1 
ATOM   6178 H  HB3    . LEU A 1 403 ? 5.254   5.913   -30.814 1.00 26.07  ? 402 LEU A HB3    1 
ATOM   6179 H  HG     . LEU A 1 403 ? 5.515   6.268   -33.062 1.00 32.51  ? 402 LEU A HG     1 
ATOM   6180 H  HD11   . LEU A 1 403 ? 5.233   4.566   -34.600 1.00 39.07  ? 402 LEU A HD11   1 
ATOM   6181 H  HD12   . LEU A 1 403 ? 6.421   4.199   -33.612 1.00 39.07  ? 402 LEU A HD12   1 
ATOM   6182 H  HD13   . LEU A 1 403 ? 4.992   3.531   -33.418 1.00 39.07  ? 402 LEU A HD13   1 
ATOM   6183 H  HD21   . LEU A 1 403 ? 3.283   5.906   -33.708 1.00 33.55  ? 402 LEU A HD21   1 
ATOM   6184 H  HD22   . LEU A 1 403 ? 3.111   4.876   -32.511 1.00 33.55  ? 402 LEU A HD22   1 
ATOM   6185 H  HD23   . LEU A 1 403 ? 3.343   6.418   -32.205 1.00 33.55  ? 402 LEU A HD23   1 
ATOM   6186 N  N      . GLU A 1 404 ? 8.204   6.652   -30.878 1.00 23.93  ? 403 GLU A N      1 
ATOM   6187 C  CA     . GLU A 1 404 ? 9.271   7.564   -31.260 1.00 23.81  ? 403 GLU A CA     1 
ATOM   6188 C  C      . GLU A 1 404 ? 10.649  6.925   -31.250 1.00 24.43  ? 403 GLU A C      1 
ATOM   6189 O  O      . GLU A 1 404 ? 11.593  7.552   -31.721 1.00 27.33  ? 403 GLU A O      1 
ATOM   6190 C  CB     . GLU A 1 404 ? 9.367   8.748   -30.297 1.00 31.37  ? 403 GLU A CB     1 
ATOM   6191 C  CG     . GLU A 1 404 ? 8.299   9.804   -30.362 1.00 36.61  ? 403 GLU A CG     1 
ATOM   6192 C  CD     . GLU A 1 404 ? 8.646   10.936  -29.412 1.00 49.46  ? 403 GLU A CD     1 
ATOM   6193 O  OE1    . GLU A 1 404 ? 8.407   10.780  -28.191 1.00 55.39  ? 403 GLU A OE1    1 
ATOM   6194 O  OE2    . GLU A 1 404 ? 9.222   11.951  -29.856 1.00 55.35  1 403 GLU A OE2    1 
ATOM   6195 H  H      . GLU A 1 404 ? 7.802   6.874   -30.151 1.00 28.73  ? 403 GLU A H      1 
ATOM   6196 H  HA     . GLU A 1 404 ? 9.098   7.906   -32.151 1.00 28.59  ? 403 GLU A HA     1 
ATOM   6197 H  HB2    . GLU A 1 404 ? 9.361   8.398   -29.393 1.00 37.67  ? 403 GLU A HB2    1 
ATOM   6198 H  HB3    . GLU A 1 404 ? 10.213  9.194   -30.458 1.00 37.67  ? 403 GLU A HB3    1 
ATOM   6199 H  HG2    . GLU A 1 404 ? 8.246   10.160  -31.263 1.00 43.95  ? 403 GLU A HG2    1 
ATOM   6200 H  HG3    . GLU A 1 404 ? 7.448   9.425   -30.093 1.00 43.95  ? 403 GLU A HG3    1 
ATOM   6201 N  N      . GLY A 1 405 ? 10.822  5.771   -30.641 1.00 24.80  ? 404 GLY A N      1 
ATOM   6202 C  CA     . GLY A 1 405 ? 12.135  5.168   -30.570 1.00 28.88  ? 404 GLY A CA     1 
ATOM   6203 C  C      . GLY A 1 405 ? 12.907  5.481   -29.300 1.00 30.43  ? 404 GLY A C      1 
ATOM   6204 O  O      . GLY A 1 405 ? 14.116  5.220   -29.244 1.00 32.97  ? 404 GLY A O      1 
ATOM   6205 H  H      . GLY A 1 405 ? 10.198  5.316   -30.261 1.00 29.78  ? 404 GLY A H      1 
ATOM   6206 H  HA2    . GLY A 1 405 ? 12.044  4.205   -30.636 1.00 34.67  ? 404 GLY A HA2    1 
ATOM   6207 H  HA3    . GLY A 1 405 ? 12.663  5.473   -31.325 1.00 34.67  ? 404 GLY A HA3    1 
ATOM   6208 N  N      . LYS A 1 406 ? 12.252  6.026   -28.287 1.00 23.95  ? 405 LYS A N      1 
ATOM   6209 C  CA     . LYS A 1 406 ? 12.919  6.447   -27.062 1.00 26.01  ? 405 LYS A CA     1 
ATOM   6210 C  C      . LYS A 1 406 ? 13.033  5.316   -26.062 1.00 24.58  ? 405 LYS A C      1 
ATOM   6211 O  O      . LYS A 1 406 ? 12.187  4.422   -25.999 1.00 24.05  ? 405 LYS A O      1 
ATOM   6212 C  CB     . LYS A 1 406 ? 12.151  7.597   -26.410 1.00 31.09  ? 405 LYS A CB     1 
ATOM   6213 C  CG     . LYS A 1 406 ? 12.134  8.872   -27.241 1.00 37.24  ? 405 LYS A CG     1 
ATOM   6214 C  CD     . LYS A 1 406 ? 11.312  9.927   -26.553 1.00 44.50  ? 405 LYS A CD     1 
ATOM   6215 C  CE     . LYS A 1 406 ? 11.513  11.290  -27.192 1.00 56.63  ? 405 LYS A CE     1 
ATOM   6216 N  NZ     . LYS A 1 406 ? 10.759  12.323  -26.435 1.00 60.75  1 405 LYS A NZ     1 
ATOM   6217 H  H      . LYS A 1 406 ? 11.404  6.166   -28.283 1.00 28.76  ? 405 LYS A H      1 
ATOM   6218 H  HA     . LYS A 1 406 ? 13.813  6.758   -27.274 1.00 31.23  ? 405 LYS A HA     1 
ATOM   6219 H  HB2    . LYS A 1 406 ? 11.232  7.321   -26.271 1.00 37.33  ? 405 LYS A HB2    1 
ATOM   6220 H  HB3    . LYS A 1 406 ? 12.564  7.805   -25.557 1.00 37.33  ? 405 LYS A HB3    1 
ATOM   6221 H  HG2    . LYS A 1 406 ? 13.039  9.205   -27.344 1.00 44.71  ? 405 LYS A HG2    1 
ATOM   6222 H  HG3    . LYS A 1 406 ? 11.738  8.690   -28.108 1.00 44.71  ? 405 LYS A HG3    1 
ATOM   6223 H  HD2    . LYS A 1 406 ? 10.372  9.696   -26.619 1.00 53.42  ? 405 LYS A HD2    1 
ATOM   6224 H  HD3    . LYS A 1 406 ? 11.579  9.985   -25.622 1.00 53.42  ? 405 LYS A HD3    1 
ATOM   6225 H  HE2    . LYS A 1 406 ? 12.455  11.521  -27.175 1.00 67.98  ? 405 LYS A HE2    1 
ATOM   6226 H  HE3    . LYS A 1 406 ? 11.183  11.274  -28.104 1.00 67.98  ? 405 LYS A HE3    1 
ATOM   6227 H  HZ1    . LYS A 1 406 ? 10.878  13.121  -26.810 1.00 72.92  ? 405 LYS A HZ1    1 
ATOM   6228 H  HZ2    . LYS A 1 406 ? 9.891   12.128  -26.437 1.00 72.92  ? 405 LYS A HZ2    1 
ATOM   6229 H  HZ3    . LYS A 1 406 ? 11.047  12.353  -25.593 1.00 72.92  ? 405 LYS A HZ3    1 
ATOM   6230 N  N      . VAL A 1 407 ? 14.075  5.390   -25.244 1.00 24.59  ? 406 VAL A N      1 
ATOM   6231 C  CA     . VAL A 1 407 ? 14.126  4.613   -24.008 1.00 24.56  ? 406 VAL A CA     1 
ATOM   6232 C  C      . VAL A 1 407 ? 13.378  5.401   -22.939 1.00 25.38  ? 406 VAL A C      1 
ATOM   6233 O  O      . VAL A 1 407 ? 13.544  6.619   -22.816 1.00 31.12  ? 406 VAL A O      1 
ATOM   6234 C  CB     . VAL A 1 407 ? 15.583  4.343   -23.593 1.00 29.60  ? 406 VAL A CB     1 
ATOM   6235 C  CG1    . VAL A 1 407 ? 15.671  3.819   -22.147 1.00 30.79  ? 406 VAL A CG1    1 
ATOM   6236 C  CG2    . VAL A 1 407 ? 16.209  3.354   -24.542 1.00 31.87  ? 406 VAL A CG2    1 
ATOM   6237 H  H      . VAL A 1 407 ? 14.767  5.882   -25.380 1.00 29.53  ? 406 VAL A H      1 
ATOM   6238 H  HA     . VAL A 1 407 ? 13.678  3.763   -24.139 1.00 29.49  ? 406 VAL A HA     1 
ATOM   6239 H  HB     . VAL A 1 407 ? 16.086  5.170   -23.645 1.00 35.53  ? 406 VAL A HB     1 
ATOM   6240 H  HG11   . VAL A 1 407 ? 16.601  3.661   -21.925 1.00 36.97  ? 406 VAL A HG11   1 
ATOM   6241 H  HG12   . VAL A 1 407 ? 15.295  4.483   -21.548 1.00 36.97  ? 406 VAL A HG12   1 
ATOM   6242 H  HG13   . VAL A 1 407 ? 15.169  2.991   -22.081 1.00 36.97  ? 406 VAL A HG13   1 
ATOM   6243 H  HG21   . VAL A 1 407 ? 17.126  3.192   -24.269 1.00 38.26  ? 406 VAL A HG21   1 
ATOM   6244 H  HG22   . VAL A 1 407 ? 15.704  2.526   -24.514 1.00 38.26  ? 406 VAL A HG22   1 
ATOM   6245 H  HG23   . VAL A 1 407 ? 16.190  3.723   -25.439 1.00 38.26  ? 406 VAL A HG23   1 
ATOM   6246 N  N      . LEU A 1 408 ? 12.552  4.735   -22.197 1.00 20.51  ? 407 LEU A N      1 
ATOM   6247 C  CA     . LEU A 1 408 ? 11.752  5.435   -21.199 1.00 19.79  ? 407 LEU A CA     1 
ATOM   6248 C  C      . LEU A 1 408 ? 12.560  5.639   -19.908 1.00 20.42  ? 407 LEU A C      1 
ATOM   6249 O  O      . LEU A 1 408 ? 13.180  4.691   -19.414 1.00 20.58  ? 407 LEU A O      1 
ATOM   6250 C  CB     . LEU A 1 408 ? 10.493  4.629   -20.907 1.00 20.32  ? 407 LEU A CB     1 
ATOM   6251 C  CG     . LEU A 1 408 ? 9.599   4.333   -22.102 1.00 26.69  ? 407 LEU A CG     1 
ATOM   6252 C  CD1    . LEU A 1 408 ? 8.565   3.315   -21.738 1.00 26.70  ? 407 LEU A CD1    1 
ATOM   6253 C  CD2    . LEU A 1 408 ? 8.952   5.599   -22.545 1.00 32.79  ? 407 LEU A CD2    1 
ATOM   6254 H  H      . LEU A 1 408 ? 12.423  3.886   -22.236 1.00 24.63  ? 407 LEU A H      1 
ATOM   6255 H  HA     . LEU A 1 408 ? 11.491  6.304   -21.542 1.00 23.65  ? 407 LEU A HA     1 
ATOM   6256 H  HB2    . LEU A 1 408 ? 10.757  3.778   -20.526 1.00 24.40  ? 407 LEU A HB2    1 
ATOM   6257 H  HB3    . LEU A 1 408 ? 9.959   5.120   -20.262 1.00 24.40  ? 407 LEU A HB3    1 
ATOM   6258 H  HG     . LEU A 1 408 ? 10.134  3.986   -22.832 1.00 32.04  ? 407 LEU A HG     1 
ATOM   6259 H  HD11   . LEU A 1 408 ? 8.008   3.141   -22.512 1.00 32.05  ? 407 LEU A HD11   1 
ATOM   6260 H  HD12   . LEU A 1 408 ? 9.010   2.499   -21.460 1.00 32.05  ? 407 LEU A HD12   1 
ATOM   6261 H  HD13   . LEU A 1 408 ? 8.024   3.661   -21.011 1.00 32.05  ? 407 LEU A HD13   1 
ATOM   6262 H  HD21   . LEU A 1 408 ? 8.382   5.412   -23.307 1.00 39.37  ? 407 LEU A HD21   1 
ATOM   6263 H  HD22   . LEU A 1 408 ? 8.423   5.955   -21.814 1.00 39.37  ? 407 LEU A HD22   1 
ATOM   6264 H  HD23   . LEU A 1 408 ? 9.641   6.235   -22.794 1.00 39.37  ? 407 LEU A HD23   1 
ATOM   6265 N  N      . PRO A 1 409 ? 12.547  6.840   -19.324 1.00 20.96  ? 408 PRO A N      1 
ATOM   6266 C  CA     . PRO A 1 409 ? 13.328  7.077   -18.094 1.00 23.83  ? 408 PRO A CA     1 
ATOM   6267 C  C      . PRO A 1 409 ? 13.054  6.088   -16.972 1.00 21.93  ? 408 PRO A C      1 
ATOM   6268 O  O      . PRO A 1 409 ? 13.986  5.715   -16.264 1.00 22.93  ? 408 PRO A O      1 
ATOM   6269 C  CB     . PRO A 1 409 ? 12.910  8.489   -17.665 1.00 26.85  ? 408 PRO A CB     1 
ATOM   6270 C  CG     . PRO A 1 409 ? 12.431  9.159   -18.909 1.00 27.94  ? 408 PRO A CG     1 
ATOM   6271 C  CD     . PRO A 1 409 ? 11.946  8.074   -19.860 1.00 23.78  ? 408 PRO A CD     1 
ATOM   6272 H  HA     . PRO A 1 409 ? 14.277  7.073   -18.295 1.00 28.62  ? 408 PRO A HA     1 
ATOM   6273 H  HB2    . PRO A 1 409 ? 12.197  8.434   -17.010 1.00 32.24  ? 408 PRO A HB2    1 
ATOM   6274 H  HB3    . PRO A 1 409 ? 13.676  8.958   -17.298 1.00 32.24  ? 408 PRO A HB3    1 
ATOM   6275 H  HG2    . PRO A 1 409 ? 11.703  9.761   -18.687 1.00 33.55  ? 408 PRO A HG2    1 
ATOM   6276 H  HG3    . PRO A 1 409 ? 13.164  9.653   -19.309 1.00 33.55  ? 408 PRO A HG3    1 
ATOM   6277 H  HD2    . PRO A 1 409 ? 10.978  8.014   -19.838 1.00 28.55  ? 408 PRO A HD2    1 
ATOM   6278 H  HD3    . PRO A 1 409 ? 12.271  8.244   -20.758 1.00 28.55  ? 408 PRO A HD3    1 
ATOM   6279 N  N      . GLY A 1 410 ? 11.796  5.706   -16.745 1.00 22.91  ? 409 GLY A N      1 
ATOM   6280 C  CA     . GLY A 1 410 ? 11.502  4.762   -15.675 1.00 22.63  ? 409 GLY A CA     1 
ATOM   6281 C  C      . GLY A 1 410 ? 12.135  3.405   -15.902 1.00 24.55  ? 409 GLY A C      1 
ATOM   6282 O  O      . GLY A 1 410 ? 12.444  2.688   -14.944 1.00 25.78  ? 409 GLY A O      1 
ATOM   6283 H  H      . GLY A 1 410 ? 11.109  5.975   -17.187 1.00 27.51  ? 409 GLY A H      1 
ATOM   6284 H  HA2    . GLY A 1 410 ? 11.831  5.117   -14.834 1.00 27.17  ? 409 GLY A HA2    1 
ATOM   6285 H  HA3    . GLY A 1 410 ? 10.542  4.644   -15.604 1.00 27.17  ? 409 GLY A HA3    1 
ATOM   6286 N  N      . VAL A 1 411 ? 12.338  3.026   -17.171 1.00 21.14  ? 410 VAL A N      1 
ATOM   6287 C  CA     . VAL A 1 411 ? 13.075  1.803   -17.473 1.00 20.43  ? 410 VAL A CA     1 
ATOM   6288 C  C      . VAL A 1 411 ? 14.568  2.021   -17.316 1.00 21.59  ? 410 VAL A C      1 
ATOM   6289 O  O      . VAL A 1 411 ? 15.282  1.188   -16.748 1.00 22.59  ? 410 VAL A O      1 
ATOM   6290 C  CB     . VAL A 1 411 ? 12.728  1.345   -18.913 1.00 22.38  ? 410 VAL A CB     1 
ATOM   6291 C  CG1    . VAL A 1 411 ? 13.520  0.118   -19.303 1.00 25.96  ? 410 VAL A CG1    1 
ATOM   6292 C  CG2    . VAL A 1 411 ? 11.227  1.099   -19.031 1.00 23.81  ? 410 VAL A CG2    1 
ATOM   6293 H  H      . VAL A 1 411 ? 12.060  3.456   -17.862 1.00 25.38  ? 410 VAL A H      1 
ATOM   6294 H  HA     . VAL A 1 411 ? 12.803  1.104   -16.858 1.00 24.42  ? 410 VAL A HA     1 
ATOM   6295 H  HB     . VAL A 1 411 ? 12.960  2.055   -19.531 1.00 26.88  ? 410 VAL A HB     1 
ATOM   6296 H  HG11   . VAL A 1 411 ? 13.278  -0.140  -20.207 1.00 31.17  ? 410 VAL A HG11   1 
ATOM   6297 H  HG12   . VAL A 1 411 ? 14.466  0.327   -19.260 1.00 31.17  ? 410 VAL A HG12   1 
ATOM   6298 H  HG13   . VAL A 1 411 ? 13.311  -0.601  -18.687 1.00 31.17  ? 410 VAL A HG13   1 
ATOM   6299 H  HG21   . VAL A 1 411 ? 11.024  0.813   -19.936 1.00 28.59  ? 410 VAL A HG21   1 
ATOM   6300 H  HG22   . VAL A 1 411 ? 10.970  0.408   -18.400 1.00 28.59  ? 410 VAL A HG22   1 
ATOM   6301 H  HG23   . VAL A 1 411 ? 10.756  1.922   -18.831 1.00 28.59  ? 410 VAL A HG23   1 
ATOM   6302 N  N      . ASP A 1 412 ? 15.064  3.140   -17.836 1.00 22.46  ? 411 ASP A N      1 
ATOM   6303 C  CA     . ASP A 1 412 ? 16.498  3.424   -17.813 1.00 25.81  ? 411 ASP A CA     1 
ATOM   6304 C  C      . ASP A 1 412 ? 17.044  3.476   -16.392 1.00 25.80  ? 411 ASP A C      1 
ATOM   6305 O  O      . ASP A 1 412 ? 18.216  3.138   -16.147 1.00 25.26  ? 411 ASP A O      1 
ATOM   6306 C  CB     . ASP A 1 412 ? 16.712  4.757   -18.541 1.00 31.83  ? 411 ASP A CB     1 
ATOM   6307 C  CG     . ASP A 1 412 ? 18.169  5.139   -18.685 1.00 44.23  ? 411 ASP A CG     1 
ATOM   6308 O  OD1    . ASP A 1 412 ? 18.909  4.392   -19.353 1.00 42.35  ? 411 ASP A OD1    1 
ATOM   6309 O  OD2    . ASP A 1 412 ? 18.547  6.211   -18.159 1.00 54.51  1 411 ASP A OD2    1 
ATOM   6310 H  H      . ASP A 1 412 ? 14.591  3.753   -18.210 1.00 26.97  ? 411 ASP A H      1 
ATOM   6311 H  HA     . ASP A 1 412 ? 16.972  2.730   -18.297 1.00 30.99  ? 411 ASP A HA     1 
ATOM   6312 H  HB2    . ASP A 1 412 ? 16.332  4.692   -19.431 1.00 38.21  ? 411 ASP A HB2    1 
ATOM   6313 H  HB3    . ASP A 1 412 ? 16.268  5.461   -18.044 1.00 38.21  ? 411 ASP A HB3    1 
ATOM   6314 N  N      . ALA A 1 413 ? 16.212  3.910   -15.441 1.00 23.66  ? 412 ALA A N      1 
ATOM   6315 C  CA     . ALA A 1 413 ? 16.612  4.056   -14.046 1.00 24.57  ? 412 ALA A CA     1 
ATOM   6316 C  C      . ALA A 1 413 ? 16.685  2.735   -13.281 1.00 24.86  ? 412 ALA A C      1 
ATOM   6317 O  O      . ALA A 1 413 ? 17.178  2.723   -12.148 1.00 25.91  ? 412 ALA A O      1 
ATOM   6318 C  CB     . ALA A 1 413 ? 15.645  4.998   -13.329 1.00 24.57  ? 412 ALA A CB     1 
ATOM   6319 H  H      . ALA A 1 413 ? 15.394  4.130   -15.587 1.00 28.29  ? 412 ALA A H      1 
ATOM   6320 H  HA     . ALA A 1 413 ? 17.493  4.461   -14.017 1.00 29.39  ? 412 ALA A HA     1 
ATOM   6321 H  HB1    . ALA A 1 413 ? 15.920  5.088   -12.403 1.00 29.51  ? 412 ALA A HB1    1 
ATOM   6322 H  HB2    . ALA A 1 413 ? 15.666  5.864   -13.766 1.00 29.51  ? 412 ALA A HB2    1 
ATOM   6323 H  HB3    . ALA A 1 413 ? 14.750  4.626   -13.375 1.00 29.51  ? 412 ALA A HB3    1 
ATOM   6324 N  N      . LEU A 1 414 ? 16.216  1.636   -13.859 1.00 24.18  ? 413 LEU A N      1 
ATOM   6325 C  CA     . LEU A 1 414 ? 16.306  0.328   -13.209 1.00 24.77  ? 413 LEU A CA     1 
ATOM   6326 C  C      . LEU A 1 414 ? 17.749  -0.169  -13.095 1.00 27.62  ? 413 LEU A C      1 
ATOM   6327 O  O      . LEU A 1 414 ? 18.638  0.218   -13.864 1.00 30.47  ? 413 LEU A O      1 
ATOM   6328 C  CB     . LEU A 1 414 ? 15.478  -0.698  -13.994 1.00 23.94  ? 413 LEU A CB     1 
ATOM   6329 C  CG     . LEU A 1 414 ? 13.978  -0.426  -14.047 1.00 22.72  ? 413 LEU A CG     1 
ATOM   6330 C  CD1    . LEU A 1 414 ? 13.294  -1.437  -14.948 1.00 25.20  ? 413 LEU A CD1    1 
ATOM   6331 C  CD2    . LEU A 1 414 ? 13.358  -0.461  -12.624 1.00 23.17  ? 413 LEU A CD2    1 
ATOM   6332 H  H      . LEU A 1 414 ? 15.839  1.618   -14.632 1.00 28.93  ? 413 LEU A H      1 
ATOM   6333 H  HA     . LEU A 1 414 ? 15.937  0.392   -12.314 1.00 29.62  ? 413 LEU A HA     1 
ATOM   6334 H  HB2    . LEU A 1 414 ? 15.803  -0.720  -14.908 1.00 28.63  ? 413 LEU A HB2    1 
ATOM   6335 H  HB3    . LEU A 1 414 ? 15.602  -1.569  -13.585 1.00 28.63  ? 413 LEU A HB3    1 
ATOM   6336 H  HG     . LEU A 1 414 ? 13.829  0.457   -14.419 1.00 27.16  ? 413 LEU A HG     1 
ATOM   6337 H  HD11   . LEU A 1 414 ? 12.343  -1.247  -14.969 1.00 30.26  ? 413 LEU A HD11   1 
ATOM   6338 H  HD12   . LEU A 1 414 ? 13.666  -1.366  -15.841 1.00 30.26  ? 413 LEU A HD12   1 
ATOM   6339 H  HD13   . LEU A 1 414 ? 13.447  -2.327  -14.595 1.00 30.26  ? 413 LEU A HD13   1 
ATOM   6340 H  HD21   . LEU A 1 414 ? 12.406  -0.285  -12.691 1.00 27.71  ? 413 LEU A HD21   1 
ATOM   6341 H  HD22   . LEU A 1 414 ? 13.506  -1.338  -12.237 1.00 27.71  ? 413 LEU A HD22   1 
ATOM   6342 H  HD23   . LEU A 1 414 ? 13.783  0.218   -12.078 1.00 27.71  ? 413 LEU A HD23   1 
ATOM   6343 N  N      . SER A 1 415 ? 17.962  -1.100  -12.161 1.00 27.22  ? 414 SER A N      1 
ATOM   6344 C  CA     . SER A 1 415 ? 19.269  -1.723  -12.006 1.00 28.82  ? 414 SER A CA     1 
ATOM   6345 C  C      . SER A 1 415 ? 19.639  -2.540  -13.238 1.00 30.03  ? 414 SER A C      1 
ATOM   6346 O  O      . SER A 1 415 ? 18.794  -3.188  -13.869 1.00 29.17  ? 414 SER A O      1 
ATOM   6347 C  CB     . SER A 1 415 ? 19.300  -2.658  -10.799 1.00 31.06  ? 414 SER A CB     1 
ATOM   6348 O  OG     . SER A 1 415 ? 19.085  -1.995  -9.571  1.00 30.45  ? 414 SER A OG     1 
ATOM   6349 H  H      . SER A 1 415 ? 17.366  -1.385  -11.609 1.00 32.57  ? 414 SER A H      1 
ATOM   6350 H  HA     . SER A 1 415 ? 19.941  -1.036  -11.880 1.00 34.49  ? 414 SER A HA     1 
ATOM   6351 H  HB2    . SER A 1 415 ? 18.609  -3.329  -10.912 1.00 37.29  ? 414 SER A HB2    1 
ATOM   6352 H  HB3    . SER A 1 415 ? 20.169  -3.090  -10.767 1.00 37.29  ? 414 SER A HB3    1 
ATOM   6353 H  HG     . SER A 1 415 ? 19.679  -1.414  -9.450  1.00 36.45  ? 414 SER A HG     1 
ATOM   6354 N  N      . ASN A 1 416 ? 20.914  -2.535  -13.565 1.00 36.49  ? 415 ASN A N      1 
ATOM   6355 C  CA     . ASN A 1 416 ? 21.396  -3.356  -14.662 1.00 41.50  ? 415 ASN A CA     1 
ATOM   6356 C  C      . ASN A 1 416 ? 21.709  -4.746  -14.129 1.00 42.48  ? 415 ASN A C      1 
ATOM   6357 O  O      . ASN A 1 416 ? 22.168  -4.895  -12.995 1.00 44.99  ? 415 ASN A O      1 
ATOM   6358 C  CB     . ASN A 1 416 ? 22.635  -2.731  -15.299 1.00 50.38  ? 415 ASN A CB     1 
ATOM   6359 C  CG     . ASN A 1 416 ? 22.303  -1.530  -16.169 1.00 56.55  ? 415 ASN A CG     1 
ATOM   6360 O  OD1    . ASN A 1 416 ? 21.259  -1.488  -16.824 1.00 55.26  ? 415 ASN A OD1    1 
ATOM   6361 N  ND2    . ASN A 1 416 ? 23.197  -0.548  -16.186 1.00 61.02  ? 415 ASN A ND2    1 
ATOM   6362 H  H      . ASN A 1 416 ? 21.522  -2.070  -13.173 1.00 43.81  ? 415 ASN A H      1 
ATOM   6363 H  HA     . ASN A 1 416 ? 20.705  -3.432  -15.339 1.00 49.82  ? 415 ASN A HA     1 
ATOM   6364 H  HB2    . ASN A 1 416 ? 23.237  -2.437  -14.598 1.00 60.48  ? 415 ASN A HB2    1 
ATOM   6365 H  HB3    . ASN A 1 416 ? 23.072  -3.394  -15.856 1.00 60.48  ? 415 ASN A HB3    1 
ATOM   6366 H  HD21   . ASN A 1 416 ? 23.056  0.154   -16.663 1.00 73.24  ? 415 ASN A HD21   1 
ATOM   6367 H  HD22   . ASN A 1 416 ? 23.917  -0.614  -15.720 1.00 73.24  ? 415 ASN A HD22   1 
ATOM   6368 N  N      . ILE A 1 417 ? 21.421  -5.765  -14.930 1.00 45.80  ? 416 ILE A N      1 
ATOM   6369 C  CA     . ILE A 1 417 ? 21.851  -7.107  -14.578 1.00 58.70  ? 416 ILE A CA     1 
ATOM   6370 C  C      . ILE A 1 417 ? 23.369  -7.129  -14.627 1.00 70.98  ? 416 ILE A C      1 
ATOM   6371 O  O      . ILE A 1 417 ? 23.959  -6.820  -15.665 1.00 78.69  ? 416 ILE A O      1 
ATOM   6372 C  CB     . ILE A 1 417 ? 21.260  -8.162  -15.509 1.00 64.60  ? 416 ILE A CB     1 
ATOM   6373 C  CG1    . ILE A 1 417 ? 19.766  -8.315  -15.250 1.00 69.30  ? 416 ILE A CG1    1 
ATOM   6374 C  CG2    . ILE A 1 417 ? 21.954  -9.503  -15.300 1.00 69.11  ? 416 ILE A CG2    1 
ATOM   6375 C  CD1    . ILE A 1 417 ? 19.042  -9.062  -16.347 1.00 75.07  ? 416 ILE A CD1    1 
ATOM   6376 H  H      . ILE A 1 417 ? 20.985  -5.707  -15.669 1.00 54.98  ? 416 ILE A H      1 
ATOM   6377 H  HA     . ILE A 1 417 ? 21.571  -7.308  -13.671 1.00 70.46  ? 416 ILE A HA     1 
ATOM   6378 H  HB     . ILE A 1 417 ? 21.392  -7.879  -16.428 1.00 77.53  ? 416 ILE A HB     1 
ATOM   6379 H  HG12   . ILE A 1 417 ? 19.639  -8.804  -14.422 1.00 83.18  ? 416 ILE A HG12   1 
ATOM   6380 H  HG13   . ILE A 1 417 ? 19.368  -7.433  -15.177 1.00 83.18  ? 416 ILE A HG13   1 
ATOM   6381 H  HG21   . ILE A 1 417 ? 21.564  -10.157 -15.900 1.00 82.95  ? 416 ILE A HG21   1 
ATOM   6382 H  HG22   . ILE A 1 417 ? 22.900  -9.402  -15.490 1.00 82.95  ? 416 ILE A HG22   1 
ATOM   6383 H  HG23   . ILE A 1 417 ? 21.830  -9.782  -14.380 1.00 82.95  ? 416 ILE A HG23   1 
ATOM   6384 H  HD11   . ILE A 1 417 ? 18.101  -9.123  -16.119 1.00 90.10  ? 416 ILE A HD11   1 
ATOM   6385 H  HD12   . ILE A 1 417 ? 19.150  -8.579  -17.181 1.00 90.10  ? 416 ILE A HD12   1 
ATOM   6386 H  HD13   . ILE A 1 417 ? 19.422  -9.951  -16.426 1.00 90.10  ? 416 ILE A HD13   1 
HETATM 6387 P  PB     . ADP B 2 .   ? -5.145  8.985   -22.846 1.00 22.36  ? 501 ADP A PB     1 
HETATM 6388 O  O1B    . ADP B 2 .   ? -5.729  7.934   -23.736 1.00 21.51  ? 501 ADP A O1B    1 
HETATM 6389 O  O2B    . ADP B 2 .   ? -5.505  8.967   -21.413 1.00 20.43  ? 501 ADP A O2B    1 
HETATM 6390 O  O3B    . ADP B 2 .   ? -3.663  9.024   -23.135 1.00 23.89  ? 501 ADP A O3B    1 
HETATM 6391 P  PA     . ADP B 2 .   ? -5.405  11.814  -22.961 1.00 20.63  ? 501 ADP A PA     1 
HETATM 6392 O  O1A    . ADP B 2 .   ? -4.338  12.501  -23.753 1.00 23.30  ? 501 ADP A O1A    1 
HETATM 6393 O  O2A    . ADP B 2 .   ? -5.353  11.722  -21.487 1.00 18.31  ? 501 ADP A O2A    1 
HETATM 6394 O  O3A    . ADP B 2 .   ? -5.679  10.352  -23.533 1.00 17.84  ? 501 ADP A O3A    1 
HETATM 6395 O  "O5'"  . ADP B 2 .   ? -6.781  12.556  -23.398 1.00 21.59  ? 501 ADP A "O5'"  1 
HETATM 6396 C  "C5'"  . ADP B 2 .   ? -7.996  11.978  -22.964 1.00 23.45  ? 501 ADP A "C5'"  1 
HETATM 6397 C  "C4'"  . ADP B 2 .   ? -9.044  13.069  -22.902 1.00 23.97  ? 501 ADP A "C4'"  1 
HETATM 6398 O  "O4'"  . ADP B 2 .   ? -9.130  13.747  -24.149 1.00 22.17  ? 501 ADP A "O4'"  1 
HETATM 6399 C  "C3'"  . ADP B 2 .   ? -10.438 12.512  -22.658 1.00 23.94  ? 501 ADP A "C3'"  1 
HETATM 6400 O  "O3'"  . ADP B 2 .   ? -10.757 12.693  -21.298 1.00 23.42  ? 501 ADP A "O3'"  1 
HETATM 6401 C  "C2'"  . ADP B 2 .   ? -11.332 13.321  -23.590 1.00 22.28  ? 501 ADP A "C2'"  1 
HETATM 6402 O  "O2'"  . ADP B 2 .   ? -12.423 13.924  -22.921 1.00 23.33  ? 501 ADP A "O2'"  1 
HETATM 6403 C  "C1'"  . ADP B 2 .   ? -10.388 14.404  -24.092 1.00 21.41  ? 501 ADP A "C1'"  1 
HETATM 6404 N  N9     . ADP B 2 .   ? -10.789 14.998  -25.364 1.00 21.92  ? 501 ADP A N9     1 
HETATM 6405 C  C8     . ADP B 2 .   ? -10.978 14.386  -26.547 1.00 21.47  ? 501 ADP A C8     1 
HETATM 6406 N  N7     . ADP B 2 .   ? -11.330 15.284  -27.491 1.00 21.82  ? 501 ADP A N7     1 
HETATM 6407 C  C5     . ADP B 2 .   ? -11.374 16.479  -26.897 1.00 21.79  ? 501 ADP A C5     1 
HETATM 6408 C  C6     . ADP B 2 .   ? -11.717 17.838  -27.318 1.00 22.32  ? 501 ADP A C6     1 
HETATM 6409 N  N6     . ADP B 2 .   ? -12.056 18.056  -28.580 1.00 24.21  ? 501 ADP A N6     1 
HETATM 6410 N  N1     . ADP B 2 .   ? -11.636 18.817  -26.387 1.00 22.32  ? 501 ADP A N1     1 
HETATM 6411 C  C2     . ADP B 2 .   ? -11.266 18.587  -25.120 1.00 23.66  ? 501 ADP A C2     1 
HETATM 6412 N  N3     . ADP B 2 .   ? -10.977 17.352  -24.666 1.00 22.63  ? 501 ADP A N3     1 
HETATM 6413 C  C4     . ADP B 2 .   ? -11.010 16.301  -25.511 1.00 21.96  ? 501 ADP A C4     1 
HETATM 6414 H  "H5'1" . ADP B 2 .   ? -7.865  11.529  -21.977 1.00 28.16  ? 501 ADP A "H5'1" 1 
HETATM 6415 H  "H5'2" . ADP B 2 .   ? -8.309  11.198  -23.660 1.00 28.16  ? 501 ADP A "H5'2" 1 
HETATM 6416 H  "H4'"  . ADP B 2 .   ? -8.789  13.774  -22.099 1.00 28.78  ? 501 ADP A "H4'"  1 
HETATM 6417 H  "H3'"  . ADP B 2 .   ? -10.470 11.449  -22.935 1.00 28.74  ? 501 ADP A "H3'"  1 
HETATM 6418 H  "H2'"  . ADP B 2 .   ? -11.670 12.696  -24.428 1.00 26.75  ? 501 ADP A "H2'"  1 
HETATM 6419 H  "HO2'" . ADP B 2 .   ? -12.981 13.237  -22.530 1.00 28.01  ? 501 ADP A "HO2'" 1 
HETATM 6420 H  "H1'"  . ADP B 2 .   ? -10.345 15.193  -23.328 1.00 25.71  ? 501 ADP A "H1'"  1 
HETATM 6421 H  H8     . ADP B 2 .   ? -10.852 13.324  -26.721 1.00 25.79  ? 501 ADP A H8     1 
HETATM 6422 H  HN61   . ADP B 2 .   ? -12.271 18.992  -28.890 1.00 29.08  ? 501 ADP A HN61   1 
HETATM 6423 H  HN62   . ADP B 2 .   ? -12.089 17.287  -29.234 1.00 29.08  ? 501 ADP A HN62   1 
HETATM 6424 H  H2     . ADP B 2 .   ? -11.240 19.417  -24.425 1.00 28.42  ? 501 ADP A H2     1 
HETATM 6425 O  OAG    . X15 C 3 .   ? -1.172  9.667   -21.696 1.00 28.66  ? 502 X15 A OAG    1 
HETATM 6426 P  PAO    . X15 C 3 .   ? -2.157  9.083   -20.610 1.00 27.76  ? 502 X15 A PAO    1 
HETATM 6427 O  OAH    . X15 C 3 .   ? -3.230  10.229  -20.188 1.00 24.38  ? 502 X15 A OAH    1 
HETATM 6428 O  OAF    . X15 C 3 .   ? -2.511  7.561   -20.592 1.00 26.33  ? 502 X15 A OAF    1 
HETATM 6429 O  OAK    . X15 C 3 .   ? -0.960  9.267   -19.259 1.00 22.04  ? 502 X15 A OAK    1 
HETATM 6430 C  CAM    . X15 C 3 .   ? -1.186  8.919   -18.063 1.00 19.97  ? 502 X15 A CAM    1 
HETATM 6431 O  OAB    . X15 C 3 .   ? -2.350  8.760   -17.628 1.00 20.38  ? 502 X15 A OAB    1 
HETATM 6432 C  CAL    . X15 C 3 .   ? -0.039  8.631   -17.133 1.00 20.60  ? 502 X15 A CAL    1 
HETATM 6433 O  OAA    . X15 C 3 .   ? -0.508  8.300   -15.829 1.00 21.35  ? 502 X15 A OAA    1 
HETATM 6434 C  CAI    . X15 C 3 .   ? 0.850   9.855   -16.993 1.00 21.69  ? 502 X15 A CAI    1 
HETATM 6435 O  OAJ    . X15 C 3 .   ? 0.152   10.975  -16.455 1.00 20.65  ? 502 X15 A OAJ    1 
HETATM 6436 P  PAN    . X15 C 3 .   ? 0.683   12.429  -16.840 1.00 21.05  ? 502 X15 A PAN    1 
HETATM 6437 O  OAD    . X15 C 3 .   ? -0.226  13.312  -16.021 1.00 19.34  ? 502 X15 A OAD    1 
HETATM 6438 O  OAE    . X15 C 3 .   ? 0.537   12.633  -18.331 1.00 20.75  ? 502 X15 A OAE    1 
HETATM 6439 O  OAC    . X15 C 3 .   ? 2.148   12.466  -16.411 1.00 19.03  ? 502 X15 A OAC    1 
HETATM 6440 H  HAL    . X15 C 3 .   ? 0.553   7.799   -17.539 1.00 24.73  ? 502 X15 A HAL    1 
HETATM 6441 H  HAA    . X15 C 3 .   ? -1.009  9.044   -15.468 1.00 25.64  ? 502 X15 A HAA    1 
HETATM 6442 H  HAI1   . X15 C 3 .   ? 1.842   9.793   -16.542 1.00 26.05  ? 502 X15 A HAI1   1 
HETATM 6443 H  HAI2   . X15 C 3 .   ? 0.978   9.989   -18.069 1.00 26.05  ? 502 X15 A HAI2   1 
HETATM 6444 C  C1     . PEG D 4 .   ? -10.986 16.371  -19.713 1.00 47.78  ? 503 PEG A C1     1 
HETATM 6445 O  O1     . PEG D 4 .   ? -10.489 17.299  -20.682 1.00 50.73  ? 503 PEG A O1     1 
HETATM 6446 C  C2     . PEG D 4 .   ? -12.341 15.875  -20.131 1.00 49.21  ? 503 PEG A C2     1 
HETATM 6447 O  O2     . PEG D 4 .   ? -13.225 15.899  -19.002 1.00 52.57  ? 503 PEG A O2     1 
HETATM 6448 C  C3     . PEG D 4 .   ? -14.399 15.112  -19.257 1.00 50.78  ? 503 PEG A C3     1 
HETATM 6449 C  C4     . PEG D 4 .   ? -14.818 14.408  -17.997 1.00 48.92  ? 503 PEG A C4     1 
HETATM 6450 O  O4     . PEG D 4 .   ? -15.030 13.952  -16.650 1.00 57.15  ? 503 PEG A O4     1 
HETATM 6451 C  C1     . PEG E 4 .   ? -5.083  -6.946  -43.392 1.00 60.21  ? 504 PEG A C1     1 
HETATM 6452 O  O1     . PEG E 4 .   ? -3.693  -7.117  -43.687 1.00 62.73  ? 504 PEG A O1     1 
HETATM 6453 C  C2     . PEG E 4 .   ? -5.448  -5.493  -43.492 1.00 66.38  ? 504 PEG A C2     1 
HETATM 6454 O  O2     . PEG E 4 .   ? -5.420  -5.064  -44.860 1.00 69.05  ? 504 PEG A O2     1 
HETATM 6455 C  C3     . PEG E 4 .   ? -5.912  -3.721  -44.953 1.00 69.01  ? 504 PEG A C3     1 
HETATM 6456 C  C4     . PEG E 4 .   ? -6.019  -3.303  -46.388 1.00 68.96  ? 504 PEG A C4     1 
HETATM 6457 O  O4     . PEG E 4 .   ? -4.716  -2.943  -46.863 1.00 70.33  ? 504 PEG A O4     1 
HETATM 6458 CL CL     . CL  F 5 .   ? -0.351  18.350  -21.876 1.00 45.27  ? 505 CL  A CL     1 
HETATM 6459 MG MG     . MG  G 6 .   ? -5.281  10.336  -20.115 1.00 20.66  ? 506 MG  A MG     1 
HETATM 6460 NA NA     . NA  H 7 .   ? -1.083  0.376   -14.093 1.00 29.92  ? 507 NA  A NA     1 
HETATM 6461 O  O      . HOH I 8 .   ? -9.903  19.317  -20.800 1.00 54.38  ? 601 HOH A O      1 
HETATM 6462 O  O      . HOH I 8 .   ? 18.793  -5.669  -2.107  1.00 50.08  ? 602 HOH A O      1 
HETATM 6463 O  O      . HOH I 8 .   ? 13.130  10.548  -35.861 1.00 44.02  ? 603 HOH A O      1 
HETATM 6464 O  O      . HOH I 8 .   ? 3.421   18.813  -9.494  1.00 38.11  ? 604 HOH A O      1 
HETATM 6465 O  O      . HOH I 8 .   ? 2.098   17.514  -14.954 1.00 45.06  ? 605 HOH A O      1 
HETATM 6466 O  O      . HOH I 8 .   ? -16.083 11.289  -29.689 1.00 28.79  ? 606 HOH A O      1 
HETATM 6467 O  O      . HOH I 8 .   ? -11.866 11.302  -18.260 1.00 50.51  ? 607 HOH A O      1 
HETATM 6468 O  O      . HOH I 8 .   ? -5.053  14.401  -46.311 1.00 54.09  ? 608 HOH A O      1 
HETATM 6469 O  O      . HOH I 8 .   ? -19.864 12.835  -34.638 1.00 63.84  ? 609 HOH A O      1 
HETATM 6470 O  O      . HOH I 8 .   ? 7.885   -2.512  -41.656 1.00 40.10  ? 610 HOH A O      1 
HETATM 6471 O  O      . HOH I 8 .   ? 8.758   -3.127  14.686  1.00 50.51  ? 611 HOH A O      1 
HETATM 6472 O  O      . HOH I 8 .   ? 5.797   16.991  -21.765 1.00 50.96  ? 612 HOH A O      1 
HETATM 6473 O  O      . HOH I 8 .   ? -0.685  -8.252  -31.528 1.00 46.25  ? 613 HOH A O      1 
HETATM 6474 O  O      . HOH I 8 .   ? -4.173  9.772   -42.872 1.00 32.46  ? 614 HOH A O      1 
HETATM 6475 O  O      . HOH I 8 .   ? -2.783  -5.860  4.002   1.00 40.58  ? 615 HOH A O      1 
HETATM 6476 O  O      . HOH I 8 .   ? 0.496   17.784  -11.513 1.00 29.96  ? 616 HOH A O      1 
HETATM 6477 O  O      . HOH I 8 .   ? 19.529  1.923   -19.324 1.00 46.63  ? 617 HOH A O      1 
HETATM 6478 O  O      . HOH I 8 .   ? -24.479 16.845  -33.685 1.00 50.73  ? 618 HOH A O      1 
HETATM 6479 O  O      . HOH I 8 .   ? -8.824  32.981  -38.120 1.00 46.80  ? 619 HOH A O      1 
HETATM 6480 O  O      . HOH I 8 .   ? -8.470  10.294  -16.916 1.00 37.75  ? 620 HOH A O      1 
HETATM 6481 O  O      . HOH I 8 .   ? 14.422  -3.018  6.684   1.00 41.95  ? 621 HOH A O      1 
HETATM 6482 O  O      . HOH I 8 .   ? -7.338  -2.099  -42.068 1.00 39.59  ? 622 HOH A O      1 
HETATM 6483 O  O      . HOH I 8 .   ? -6.930  10.375  -13.633 1.00 40.19  ? 623 HOH A O      1 
HETATM 6484 O  O      . HOH I 8 .   ? 11.578  -3.224  -31.539 1.00 42.69  ? 624 HOH A O      1 
HETATM 6485 O  O      . HOH I 8 .   ? -20.656 18.001  -41.899 1.00 39.96  ? 625 HOH A O      1 
HETATM 6486 O  O      . HOH I 8 .   ? 10.654  1.703   -29.358 1.00 51.78  ? 626 HOH A O      1 
HETATM 6487 O  O      . HOH I 8 .   ? 4.622   13.585  -49.789 1.00 39.54  ? 627 HOH A O      1 
HETATM 6488 O  O      . HOH I 8 .   ? 16.748  -9.013  -2.370  1.00 43.30  ? 628 HOH A O      1 
HETATM 6489 O  O      . HOH I 8 .   ? -5.812  -8.683  -36.514 1.00 35.22  ? 629 HOH A O      1 
HETATM 6490 O  O      . HOH I 8 .   ? -5.390  22.075  -30.177 1.00 23.41  ? 630 HOH A O      1 
HETATM 6491 O  O      . HOH I 8 .   ? -4.989  -9.102  -33.871 1.00 36.74  ? 631 HOH A O      1 
HETATM 6492 O  O      . HOH I 8 .   ? 5.938   15.801  -24.471 1.00 32.57  ? 632 HOH A O      1 
HETATM 6493 O  O      . HOH I 8 .   ? -3.650  0.062   -47.925 1.00 39.66  ? 633 HOH A O      1 
HETATM 6494 O  O      . HOH I 8 .   ? 1.236   7.263   -46.699 1.00 47.22  ? 634 HOH A O      1 
HETATM 6495 O  O      . HOH I 8 .   ? -9.169  28.406  -28.236 1.00 39.30  ? 635 HOH A O      1 
HETATM 6496 O  O      . HOH I 8 .   ? -4.994  12.793  1.954   1.00 36.30  ? 636 HOH A O      1 
HETATM 6497 O  O      . HOH I 8 .   ? -24.853 18.376  -24.269 1.00 47.27  ? 637 HOH A O      1 
HETATM 6498 O  O      . HOH I 8 .   ? -23.535 12.260  -20.898 1.00 42.77  ? 638 HOH A O      1 
HETATM 6499 O  O      . HOH I 8 .   ? -7.557  3.115   -17.967 1.00 29.62  ? 639 HOH A O      1 
HETATM 6500 O  O      . HOH I 8 .   ? -8.080  -4.148  -21.106 1.00 44.70  ? 640 HOH A O      1 
HETATM 6501 O  O      . HOH I 8 .   ? 2.651   6.348   11.582  1.00 39.63  ? 641 HOH A O      1 
HETATM 6502 O  O      . HOH I 8 .   ? -1.787  -6.750  -40.554 1.00 38.93  ? 642 HOH A O      1 
HETATM 6503 O  O      . HOH I 8 .   ? 7.415   21.708  -0.703  1.00 55.25  ? 643 HOH A O      1 
HETATM 6504 O  O      . HOH I 8 .   ? -26.413 14.359  -18.605 1.00 53.98  ? 644 HOH A O      1 
HETATM 6505 O  O      . HOH I 8 .   ? -21.125 13.170  -30.755 1.00 31.60  ? 645 HOH A O      1 
HETATM 6506 O  O      . HOH I 8 .   ? 1.010   6.994   -20.546 1.00 22.62  ? 646 HOH A O      1 
HETATM 6507 O  O      . HOH I 8 .   ? 3.991   -9.017  -23.926 1.00 33.08  ? 647 HOH A O      1 
HETATM 6508 O  O      . HOH I 8 .   ? -13.939 10.336  -16.589 1.00 37.87  ? 648 HOH A O      1 
HETATM 6509 O  O      . HOH I 8 .   ? -5.205  -3.501  -20.621 1.00 40.37  ? 649 HOH A O      1 
HETATM 6510 O  O      . HOH I 8 .   ? 8.156   -13.797 4.683   1.00 35.56  ? 650 HOH A O      1 
HETATM 6511 O  O      . HOH I 8 .   ? 6.025   -0.044  10.949  1.00 33.88  ? 651 HOH A O      1 
HETATM 6512 O  O      . HOH I 8 .   ? -11.318 17.369  -33.155 1.00 28.91  ? 652 HOH A O      1 
HETATM 6513 O  O      . HOH I 8 .   ? -5.378  32.901  -3.978  1.00 32.89  ? 653 HOH A O      1 
HETATM 6514 O  O      . HOH I 8 .   ? 9.050   -8.791  -34.213 1.00 54.18  ? 654 HOH A O      1 
HETATM 6515 O  O      . HOH I 8 .   ? 10.430  10.705  -21.785 1.00 37.81  ? 655 HOH A O      1 
HETATM 6516 O  O      . HOH I 8 .   ? 12.887  -6.490  6.000   1.00 34.24  ? 656 HOH A O      1 
HETATM 6517 O  O      . HOH I 8 .   ? -4.775  20.702  -22.845 1.00 57.40  ? 657 HOH A O      1 
HETATM 6518 O  O      . HOH I 8 .   ? -8.546  15.769  -43.618 1.00 38.08  ? 658 HOH A O      1 
HETATM 6519 O  O      . HOH I 8 .   ? -11.954 8.593   -19.428 1.00 28.90  ? 659 HOH A O      1 
HETATM 6520 O  O      . HOH I 8 .   ? 16.630  7.386   2.624   1.00 38.29  ? 660 HOH A O      1 
HETATM 6521 O  O      . HOH I 8 .   ? 6.925   -5.820  -36.021 1.00 37.67  ? 661 HOH A O      1 
HETATM 6522 O  O      . HOH I 8 .   ? 1.588   -13.081 -9.754  1.00 35.91  ? 662 HOH A O      1 
HETATM 6523 O  O      . HOH I 8 .   ? 1.579   14.910  -46.065 1.00 36.45  ? 663 HOH A O      1 
HETATM 6524 O  O      . HOH I 8 .   ? -27.849 15.940  -21.421 1.00 59.31  ? 664 HOH A O      1 
HETATM 6525 O  O      . HOH I 8 .   ? -24.712 14.975  -29.959 1.00 44.31  ? 665 HOH A O      1 
HETATM 6526 O  O      . HOH I 8 .   ? 7.085   -1.056  4.248   1.00 24.50  ? 666 HOH A O      1 
HETATM 6527 O  O      . HOH I 8 .   ? 4.100   11.581  7.329   1.00 39.36  ? 667 HOH A O      1 
HETATM 6528 O  O      . HOH I 8 .   ? 18.098  9.609   -5.147  1.00 48.97  ? 668 HOH A O      1 
HETATM 6529 O  O      . HOH I 8 .   ? -18.583 7.471   -20.146 1.00 39.94  ? 669 HOH A O      1 
HETATM 6530 O  O      . HOH I 8 .   ? -2.850  12.589  -15.995 1.00 25.54  ? 670 HOH A O      1 
HETATM 6531 O  O      . HOH I 8 .   ? 12.497  3.076   -12.221 1.00 21.35  ? 671 HOH A O      1 
HETATM 6532 O  O      . HOH I 8 .   ? -3.695  13.936  -26.045 1.00 31.04  ? 672 HOH A O      1 
HETATM 6533 O  O      . HOH I 8 .   ? -4.830  29.205  -44.570 1.00 35.02  ? 673 HOH A O      1 
HETATM 6534 O  O      . HOH I 8 .   ? 4.631   17.031  -8.305  1.00 28.58  ? 674 HOH A O      1 
HETATM 6535 O  O      . HOH I 8 .   ? 13.112  -15.732 -14.741 1.00 34.52  ? 675 HOH A O      1 
HETATM 6536 O  O      . HOH I 8 .   ? -13.006 16.501  -30.965 1.00 25.16  ? 676 HOH A O      1 
HETATM 6537 O  O      . HOH I 8 .   ? -21.621 25.680  -33.625 1.00 51.85  ? 677 HOH A O      1 
HETATM 6538 O  O      . HOH I 8 .   ? 4.010   -12.068 2.259   1.00 35.01  ? 678 HOH A O      1 
HETATM 6539 O  O      . HOH I 8 .   ? 0.824   7.121   -3.689  1.00 22.64  ? 679 HOH A O      1 
HETATM 6540 O  O      . HOH I 8 .   ? 1.764   -6.593  -12.810 1.00 23.30  ? 680 HOH A O      1 
HETATM 6541 O  O      . HOH I 8 .   ? -1.613  24.177  -23.916 1.00 42.61  ? 681 HOH A O      1 
HETATM 6542 O  O      . HOH I 8 .   ? 5.384   -10.098 -17.547 1.00 36.52  ? 682 HOH A O      1 
HETATM 6543 O  O      . HOH I 8 .   ? -15.634 13.113  -45.616 1.00 35.02  ? 683 HOH A O      1 
HETATM 6544 O  O      . HOH I 8 .   ? 9.268   2.759   -33.358 1.00 30.32  ? 684 HOH A O      1 
HETATM 6545 O  O      . HOH I 8 .   ? -14.910 8.731   -36.229 1.00 29.88  ? 685 HOH A O      1 
HETATM 6546 O  O      . HOH I 8 .   ? -12.353 -0.798  -40.815 1.00 35.27  ? 686 HOH A O      1 
HETATM 6547 O  O      . HOH I 8 .   ? -13.625 3.128   -5.112  1.00 41.57  ? 687 HOH A O      1 
HETATM 6548 O  O      . HOH I 8 .   ? -5.069  9.020   -18.521 1.00 22.36  ? 688 HOH A O      1 
HETATM 6549 O  O      . HOH I 8 .   ? 0.605   1.089   -16.385 1.00 21.66  ? 689 HOH A O      1 
HETATM 6550 O  O      . HOH I 8 .   ? 3.868   22.191  -26.735 1.00 30.57  ? 690 HOH A O      1 
HETATM 6551 O  O      . HOH I 8 .   ? -14.114 32.118  -28.415 1.00 50.90  ? 691 HOH A O      1 
HETATM 6552 O  O      . HOH I 8 .   ? -14.367 -5.187  -23.186 1.00 39.35  ? 692 HOH A O      1 
HETATM 6553 O  O      . HOH I 8 .   ? -7.017  -7.399  -26.835 1.00 31.75  ? 693 HOH A O      1 
HETATM 6554 O  O      . HOH I 8 .   ? -8.961  10.922  1.134   1.00 41.53  ? 694 HOH A O      1 
HETATM 6555 O  O      . HOH I 8 .   ? -7.663  2.138   -15.323 1.00 21.01  ? 695 HOH A O      1 
HETATM 6556 O  O      . HOH I 8 .   ? 6.238   -17.129 -7.614  1.00 49.58  ? 696 HOH A O      1 
HETATM 6557 O  O      . HOH I 8 .   ? -6.010  33.494  -38.251 1.00 36.09  ? 697 HOH A O      1 
HETATM 6558 O  O      . HOH I 8 .   ? 17.742  -3.110  -2.591  1.00 39.13  ? 698 HOH A O      1 
HETATM 6559 O  O      . HOH I 8 .   ? 7.790   7.779   -42.029 1.00 38.71  ? 699 HOH A O      1 
HETATM 6560 O  O      . HOH I 8 .   ? 9.876   3.199   6.699   1.00 42.67  ? 700 HOH A O      1 
HETATM 6561 O  O      . HOH I 8 .   ? -0.207  -7.570  -42.656 1.00 46.60  ? 701 HOH A O      1 
HETATM 6562 O  O      . HOH I 8 .   ? 4.431   11.710  -11.177 1.00 19.90  ? 702 HOH A O      1 
HETATM 6563 O  O      . HOH I 8 .   ? 17.618  -10.555 -5.403  1.00 50.12  ? 703 HOH A O      1 
HETATM 6564 O  O      . HOH I 8 .   ? 12.853  -0.130  8.025   1.00 39.45  ? 704 HOH A O      1 
HETATM 6565 O  O      . HOH I 8 .   ? -23.142 9.016   -28.023 1.00 49.01  ? 705 HOH A O      1 
HETATM 6566 O  O      . HOH I 8 .   ? -9.881  31.231  -33.099 1.00 42.45  ? 706 HOH A O      1 
HETATM 6567 O  O      . HOH I 8 .   ? 16.846  5.391   -8.979  1.00 48.27  ? 707 HOH A O      1 
HETATM 6568 O  O      . HOH I 8 .   ? -19.519 10.828  -36.173 1.00 39.73  ? 708 HOH A O      1 
HETATM 6569 O  O      . HOH I 8 .   ? -11.635 14.708  -33.975 1.00 30.06  ? 709 HOH A O      1 
HETATM 6570 O  O      . HOH I 8 .   ? 21.450  -0.516  -9.271  1.00 38.96  ? 710 HOH A O      1 
HETATM 6571 O  O      . HOH I 8 .   ? 10.667  22.439  -2.881  1.00 56.21  ? 711 HOH A O      1 
HETATM 6572 O  O      . HOH I 8 .   ? 8.397   19.312  -47.446 1.00 49.38  ? 712 HOH A O      1 
HETATM 6573 O  O      . HOH I 8 .   ? 0.980   11.179  -20.710 1.00 22.72  ? 713 HOH A O      1 
HETATM 6574 O  O      . HOH I 8 .   ? 18.058  7.586   -12.070 1.00 50.95  ? 714 HOH A O      1 
HETATM 6575 O  O      . HOH I 8 .   ? -1.397  27.754  -25.200 1.00 44.64  ? 715 HOH A O      1 
HETATM 6576 O  O      . HOH I 8 .   ? 10.025  13.748  -17.504 1.00 34.43  ? 716 HOH A O      1 
HETATM 6577 O  O      . HOH I 8 .   ? -14.273 -7.426  -25.931 1.00 48.06  ? 717 HOH A O      1 
HETATM 6578 O  O      . HOH I 8 .   ? -6.598  8.037   -16.605 1.00 29.15  ? 718 HOH A O      1 
HETATM 6579 O  O      . HOH I 8 .   ? -13.934 7.834   -17.885 1.00 29.55  ? 719 HOH A O      1 
HETATM 6580 O  O      . HOH I 8 .   ? 15.268  1.627   3.236   1.00 34.92  ? 720 HOH A O      1 
HETATM 6581 O  O      . HOH I 8 .   ? -25.132 24.470  -35.026 1.00 43.34  ? 721 HOH A O      1 
HETATM 6582 O  O      . HOH I 8 .   ? 17.929  -1.768  1.245   1.00 35.80  ? 722 HOH A O      1 
HETATM 6583 O  O      . HOH I 8 .   ? -5.950  16.314  -13.477 1.00 32.11  ? 723 HOH A O      1 
HETATM 6584 O  O      . HOH I 8 .   ? -5.891  -4.768  -16.730 1.00 37.46  ? 724 HOH A O      1 
HETATM 6585 O  O      . HOH I 8 .   ? -21.061 6.551   -33.718 1.00 41.20  ? 725 HOH A O      1 
HETATM 6586 O  O      . HOH I 8 .   ? 8.492   1.251   -35.537 1.00 33.55  ? 726 HOH A O      1 
HETATM 6587 O  O      . HOH I 8 .   ? -9.582  -0.935  -20.363 1.00 33.22  ? 727 HOH A O      1 
HETATM 6588 O  O      . HOH I 8 .   ? 3.037   15.139  -16.063 1.00 32.97  ? 728 HOH A O      1 
HETATM 6589 O  O      . HOH I 8 .   ? 9.223   14.417  -31.398 1.00 28.69  ? 729 HOH A O      1 
HETATM 6590 O  O      . HOH I 8 .   ? 6.763   17.283  -32.547 1.00 26.53  ? 730 HOH A O      1 
HETATM 6591 O  O      . HOH I 8 .   ? 13.650  10.853  5.385   1.00 50.98  ? 731 HOH A O      1 
HETATM 6592 O  O      . HOH I 8 .   ? -17.599 2.758   -16.159 1.00 47.88  ? 732 HOH A O      1 
HETATM 6593 O  O      . HOH I 8 .   ? -11.743 21.453  -27.457 1.00 28.62  ? 733 HOH A O      1 
HETATM 6594 O  O      . HOH I 8 .   ? -19.189 -2.087  -29.393 1.00 46.57  ? 734 HOH A O      1 
HETATM 6595 O  O      . HOH I 8 .   ? -20.975 18.140  -37.467 1.00 35.18  ? 735 HOH A O      1 
HETATM 6596 O  O      . HOH I 8 .   ? 6.219   15.928  -16.579 1.00 58.91  ? 736 HOH A O      1 
HETATM 6597 O  O      . HOH I 8 .   ? -8.786  12.948  -19.247 1.00 33.68  ? 737 HOH A O      1 
HETATM 6598 O  O      . HOH I 8 .   ? -12.250 -7.754  -33.958 1.00 34.70  ? 738 HOH A O      1 
HETATM 6599 O  O      . HOH I 8 .   ? -8.314  9.721   -44.697 1.00 31.08  ? 739 HOH A O      1 
HETATM 6600 O  O      . HOH I 8 .   ? 4.254   -5.804  -36.282 1.00 38.16  ? 740 HOH A O      1 
HETATM 6601 O  O      . HOH I 8 .   ? -13.562 -1.472  -14.189 1.00 45.45  ? 741 HOH A O      1 
HETATM 6602 O  O      . HOH I 8 .   ? 1.153   -0.123  -12.497 1.00 23.28  ? 742 HOH A O      1 
HETATM 6603 O  O      . HOH I 8 .   ? 3.744   26.651  -37.536 1.00 29.30  ? 743 HOH A O      1 
HETATM 6604 O  O      . HOH I 8 .   ? 3.695   -4.801  -44.307 1.00 43.76  ? 744 HOH A O      1 
HETATM 6605 O  O      . HOH I 8 .   ? 4.564   20.706  -2.318  1.00 36.06  ? 745 HOH A O      1 
HETATM 6606 O  O      . HOH I 8 .   ? -3.562  3.712   -43.186 1.00 38.85  ? 746 HOH A O      1 
HETATM 6607 O  O      . HOH I 8 .   ? 18.083  11.859  -6.649  1.00 43.78  ? 747 HOH A O      1 
HETATM 6608 O  O      . HOH I 8 .   ? 21.556  2.216   -2.796  1.00 44.50  ? 748 HOH A O      1 
HETATM 6609 O  O      . HOH I 8 .   ? -20.406 18.242  -16.912 1.00 40.48  ? 749 HOH A O      1 
HETATM 6610 O  O      . HOH I 8 .   ? 9.761   -1.750  -25.962 1.00 31.97  ? 750 HOH A O      1 
HETATM 6611 O  O      . HOH I 8 .   ? -23.694 14.510  -22.969 1.00 33.91  ? 751 HOH A O      1 
HETATM 6612 O  O      . HOH I 8 .   ? 4.796   6.538   -46.207 1.00 33.51  ? 752 HOH A O      1 
HETATM 6613 O  O      . HOH I 8 .   ? 8.629   2.320   -37.885 1.00 41.74  ? 753 HOH A O      1 
HETATM 6614 O  O      . HOH I 8 .   ? -20.898 0.883   -20.968 1.00 35.50  ? 754 HOH A O      1 
HETATM 6615 O  O      . HOH I 8 .   ? 10.379  20.466  -41.310 1.00 46.18  ? 755 HOH A O      1 
HETATM 6616 O  O      . HOH I 8 .   ? -2.642  8.390   7.305   1.00 41.74  ? 756 HOH A O      1 
HETATM 6617 O  O      . HOH I 8 .   ? 20.375  2.543   -13.710 1.00 56.54  ? 757 HOH A O      1 
HETATM 6618 O  O      . HOH I 8 .   ? -2.279  20.828  -23.325 1.00 40.03  ? 758 HOH A O      1 
HETATM 6619 O  O      . HOH I 8 .   ? -6.600  14.002  -20.179 1.00 36.02  ? 759 HOH A O      1 
HETATM 6620 O  O      . HOH I 8 .   ? -19.813 9.125   -40.988 1.00 39.01  ? 760 HOH A O      1 
HETATM 6621 O  O      . HOH I 8 .   ? -14.973 6.695   -38.136 1.00 29.08  ? 761 HOH A O      1 
HETATM 6622 O  O      . HOH I 8 .   ? 16.305  7.486   -16.107 1.00 32.66  ? 762 HOH A O      1 
HETATM 6623 O  O      . HOH I 8 .   ? -16.929 26.020  -19.864 1.00 46.07  ? 763 HOH A O      1 
HETATM 6624 O  O      . HOH I 8 .   ? -0.865  -7.314  -16.101 1.00 29.17  ? 764 HOH A O      1 
HETATM 6625 O  O      . HOH I 8 .   ? 14.770  2.899   -10.488 1.00 32.42  ? 765 HOH A O      1 
HETATM 6626 O  O      . HOH I 8 .   ? -5.160  11.724  -18.563 1.00 22.43  ? 766 HOH A O      1 
HETATM 6627 O  O      . HOH I 8 .   ? 6.682   25.676  -38.017 1.00 32.20  ? 767 HOH A O      1 
HETATM 6628 O  O      . HOH I 8 .   ? -1.143  14.870  -45.941 1.00 29.70  ? 768 HOH A O      1 
HETATM 6629 O  O      . HOH I 8 .   ? -17.353 -3.011  -35.452 1.00 39.29  ? 769 HOH A O      1 
HETATM 6630 O  O      . HOH I 8 .   ? 16.637  -0.818  3.692   1.00 42.39  ? 770 HOH A O      1 
HETATM 6631 O  O      . HOH I 8 .   ? 1.545   19.615  -20.243 1.00 52.25  ? 771 HOH A O      1 
HETATM 6632 O  O      . HOH I 8 .   ? -9.276  26.431  -24.320 1.00 53.86  ? 772 HOH A O      1 
HETATM 6633 O  O      . HOH I 8 .   ? 0.673   12.920  -0.619  1.00 28.70  ? 773 HOH A O      1 
HETATM 6634 O  O      . HOH I 8 .   ? -14.945 3.964   -7.269  1.00 35.91  ? 774 HOH A O      1 
HETATM 6635 O  O      . HOH I 8 .   ? 7.579   26.074  -30.024 1.00 44.19  ? 775 HOH A O      1 
HETATM 6636 O  O      . HOH I 8 .   ? -5.113  -6.533  -24.626 1.00 26.95  ? 776 HOH A O      1 
HETATM 6637 O  O      . HOH I 8 .   ? -6.668  25.639  -24.622 1.00 44.79  ? 777 HOH A O      1 
HETATM 6638 O  O      . HOH I 8 .   ? 13.597  5.338   -8.937  1.00 33.53  ? 778 HOH A O      1 
HETATM 6639 O  O      . HOH I 8 .   ? 8.197   13.550  -19.720 1.00 42.25  ? 779 HOH A O      1 
HETATM 6640 O  O      . HOH I 8 .   ? 4.155   23.410  -44.207 1.00 43.68  ? 780 HOH A O      1 
HETATM 6641 O  O      . HOH I 8 .   ? -9.256  19.664  -42.496 1.00 34.22  ? 781 HOH A O      1 
HETATM 6642 O  O      . HOH I 8 .   ? 11.646  15.420  -11.600 1.00 50.24  ? 782 HOH A O      1 
HETATM 6643 O  O      . HOH I 8 .   ? -1.982  -6.301  -18.298 1.00 40.36  ? 783 HOH A O      1 
HETATM 6644 O  O      . HOH I 8 .   ? -1.070  14.344  1.296   1.00 38.45  ? 784 HOH A O      1 
HETATM 6645 O  O      . HOH I 8 .   ? 13.744  15.979  -37.576 1.00 53.13  ? 785 HOH A O      1 
HETATM 6646 O  O      . HOH I 8 .   ? 4.981   13.290  -23.150 1.00 36.08  ? 786 HOH A O      1 
HETATM 6647 O  O      . HOH I 8 .   ? 11.636  15.691  -9.362  1.00 39.89  ? 787 HOH A O      1 
HETATM 6648 O  O      . HOH I 8 .   ? 1.766   17.371  -45.158 1.00 37.97  ? 788 HOH A O      1 
HETATM 6649 O  O      . HOH I 8 .   ? -18.227 4.350   -11.851 1.00 109.51 ? 789 HOH A O      1 
HETATM 6650 O  O      . HOH I 8 .   ? -10.406 11.241  -14.833 1.00 29.91  ? 790 HOH A O      1 
HETATM 6651 O  O      . HOH I 8 .   ? 12.610  1.707   -22.605 1.00 30.34  ? 791 HOH A O      1 
HETATM 6652 O  O      . HOH I 8 .   ? 11.113  16.383  -31.816 1.00 47.27  ? 792 HOH A O      1 
HETATM 6653 O  O      . HOH I 8 .   ? -8.586  27.840  -45.184 1.00 50.02  ? 793 HOH A O      1 
HETATM 6654 O  O      . HOH I 8 .   ? -7.020  20.820  -43.174 1.00 53.26  ? 794 HOH A O      1 
HETATM 6655 O  O      . HOH I 8 .   ? -18.931 -4.869  -28.571 1.00 55.07  ? 795 HOH A O      1 
HETATM 6656 O  O      . HOH I 8 .   ? 3.810   21.510  -46.319 1.00 52.41  ? 796 HOH A O      1 
HETATM 6657 O  O      . HOH I 8 .   ? -15.057 12.892  -10.759 1.00 51.09  ? 797 HOH A O      1 
HETATM 6658 O  O      . HOH I 8 .   ? 18.535  7.845   0.024   1.00 50.15  ? 798 HOH A O      1 
HETATM 6659 O  O      . HOH I 8 .   ? 3.369   20.465  -13.033 1.00 58.73  ? 799 HOH A O      1 
HETATM 6660 O  O      . HOH I 8 .   ? -15.465 22.704  -44.280 1.00 72.87  ? 800 HOH A O      1 
HETATM 6661 O  O      . HOH I 8 .   ? -8.084  31.866  -35.675 1.00 58.14  ? 801 HOH A O      1 
HETATM 6662 O  O      . HOH I 8 .   ? -6.599  16.517  -43.820 1.00 37.86  ? 802 HOH A O      1 
HETATM 6663 O  O      . HOH I 8 .   ? 12.926  2.539   7.492   1.00 47.85  ? 803 HOH A O      1 
HETATM 6664 O  O      . HOH I 8 .   ? 10.969  -14.066 -5.200  1.00 65.23  ? 804 HOH A O      1 
HETATM 6665 O  O      . HOH I 8 .   ? 8.831   13.830  -21.953 1.00 55.17  ? 805 HOH A O      1 
HETATM 6666 O  O      . HOH I 8 .   ? 12.092  14.471  -28.505 1.00 51.92  ? 806 HOH A O      1 
HETATM 6667 O  O      . HOH I 8 .   ? 3.915   -10.063 11.721  1.00 51.19  ? 807 HOH A O      1 
HETATM 6668 O  O      . HOH I 8 .   ? 23.943  4.636   -3.081  1.00 45.04  ? 808 HOH A O      1 
HETATM 6669 O  O      . HOH I 8 .   ? 8.829   18.745  -31.646 1.00 41.61  ? 809 HOH A O      1 
HETATM 6670 O  O      . HOH I 8 .   ? 15.689  6.039   -32.046 1.00 66.68  ? 810 HOH A O      1 
HETATM 6671 O  O      . HOH I 8 .   ? 2.585   -15.051 -7.847  1.00 51.39  ? 811 HOH A O      1 
HETATM 6672 O  O      . HOH I 8 .   ? -12.948 12.806  -8.860  1.00 52.79  ? 812 HOH A O      1 
HETATM 6673 O  O      . HOH I 8 .   ? 2.329   12.518  -22.686 1.00 38.20  ? 813 HOH A O      1 
HETATM 6674 O  O      . HOH I 8 .   ? 1.528   -8.158  -15.431 1.00 31.63  ? 814 HOH A O      1 
HETATM 6675 O  O      . HOH I 8 .   ? 12.139  -0.043  -24.898 1.00 49.91  ? 815 HOH A O      1 
HETATM 6676 O  O      . HOH I 8 .   ? 2.725   2.476   -46.453 1.00 38.30  ? 816 HOH A O      1 
HETATM 6677 O  O      . HOH I 8 .   ? 14.924  2.240   6.043   1.00 41.09  ? 817 HOH A O      1 
HETATM 6678 O  O      . HOH I 8 .   ? -17.291 5.473   -39.122 1.00 37.75  ? 818 HOH A O      1 
HETATM 6679 O  O      . HOH I 8 .   ? -28.679 15.907  -15.856 1.00 47.42  ? 819 HOH A O      1 
HETATM 6680 O  O      . HOH I 8 .   ? -12.341 22.952  -24.702 1.00 53.11  ? 820 HOH A O      1 
HETATM 6681 O  O      . HOH I 8 .   ? -18.285 6.982   -41.170 1.00 45.53  ? 821 HOH A O      1 
HETATM 6682 O  O      . HOH I 8 .   ? 9.930   -0.882  -28.539 1.00 35.57  ? 822 HOH A O      1 
HETATM 6683 O  O      . HOH I 8 .   ? 10.262  16.701  1.265   1.00 54.04  ? 823 HOH A O      1 
HETATM 6684 O  O      . HOH I 8 .   ? 4.409   -9.829  -26.476 1.00 43.59  ? 824 HOH A O      1 
HETATM 6685 O  O      . HOH I 8 .   ? 11.268  18.479  -43.236 1.00 45.73  ? 825 HOH A O      1 
HETATM 6686 O  O      . HOH I 8 .   ? -1.888  -1.672  -48.882 1.00 50.92  ? 826 HOH A O      1 
HETATM 6687 O  O      . HOH I 8 .   ? -6.410  11.484  -16.265 1.00 44.12  ? 827 HOH A O      1 
HETATM 6688 O  O      . HOH I 8 .   ? 8.720   24.330  -2.619  1.00 55.74  ? 828 HOH A O      1 
HETATM 6689 O  O      . HOH I 8 .   ? 6.361   -11.112 -20.050 1.00 41.84  ? 829 HOH A O      1 
HETATM 6690 O  O      . HOH I 8 .   ? 16.096  16.929  -43.204 1.00 51.07  ? 830 HOH A O      1 
HETATM 6691 O  O      . HOH I 8 .   ? 2.001   0.389   -48.447 1.00 48.48  ? 831 HOH A O      1 
HETATM 6692 O  O      . HOH I 8 .   ? -4.751  14.529  -15.918 1.00 38.21  ? 832 HOH A O      1 
HETATM 6693 O  O      . HOH I 8 .   ? 8.111   -16.636 4.039   1.00 54.22  ? 833 HOH A O      1 
HETATM 6694 O  O      . HOH I 8 .   ? 13.409  17.438  -10.727 1.00 52.15  ? 834 HOH A O      1 
HETATM 6695 O  O      . HOH I 8 .   ? 1.883   4.675   -47.225 1.00 47.24  ? 835 HOH A O      1 
HETATM 6696 O  O      . HOH I 8 .   ? -22.919 16.601  -36.097 1.00 46.93  ? 836 HOH A O      1 
HETATM 6697 O  O      . HOH I 8 .   ? -26.113 12.319  -21.031 1.00 60.38  ? 837 HOH A O      1 
HETATM 6698 O  O      . HOH I 8 .   ? -22.031 19.170  -39.548 1.00 48.39  ? 838 HOH A O      1 
HETATM 6699 O  O      . HOH I 8 .   ? 22.607  7.119   -19.033 1.00 41.82  ? 839 HOH A O      1 
HETATM 6700 O  O      . HOH I 8 .   ? -4.260  -4.772  -18.903 1.00 48.90  ? 840 HOH A O      1 
HETATM 6701 O  O      . HOH I 8 .   ? 0.920   -9.130  -23.903 1.00 49.76  ? 841 HOH A O      1 
HETATM 6702 O  O      . HOH I 8 .   ? -19.643 19.141  -44.075 1.00 54.91  ? 842 HOH A O      1 
HETATM 6703 O  O      . HOH I 8 .   ? 13.203  16.768  -42.268 1.00 46.01  ? 843 HOH A O      1 
HETATM 6704 O  O      . HOH I 8 .   ? 1.752   -10.557 -15.868 1.00 42.61  ? 844 HOH A O      1 
HETATM 6705 O  O      . HOH I 8 .   ? -5.530  19.076  -44.030 1.00 46.17  ? 845 HOH A O      1 
HETATM 6706 O  O      . HOH I 8 .   ? -24.430 27.155  -32.806 1.00 59.80  ? 846 HOH A O      1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . SER A 2   ? 1.0930 1.0915 0.9473 0.1144  0.1636  0.0055  1   SER A N   
2    C CA  . SER A 2   ? 1.0334 1.0096 0.8771 0.1090  0.1370  -0.0063 1   SER A CA  
3    C C   . SER A 2   ? 0.9705 0.9653 0.8573 0.1053  0.1292  -0.0084 1   SER A C   
4    O O   . SER A 2   ? 0.9376 0.9641 0.8684 0.0994  0.1382  -0.0003 1   SER A O   
5    C CB  . SER A 2   ? 0.9875 0.9291 0.7808 0.1257  0.1306  -0.0191 1   SER A CB  
6    O OG  . SER A 2   ? 0.9161 0.8329 0.6970 0.1164  0.1043  -0.0280 1   SER A OG  
7    N N   . LEU A 3   ? 0.8719 0.8450 0.7452 0.1084  0.1109  -0.0190 2   LEU A N   
8    C CA  . LEU A 3   ? 0.7042 0.6877 0.6098 0.1041  0.0988  -0.0208 2   LEU A CA  
9    C C   . LEU A 3   ? 0.6416 0.6258 0.5517 0.1246  0.1024  -0.0271 2   LEU A C   
10   O O   . LEU A 3   ? 0.6447 0.6335 0.5770 0.1240  0.0904  -0.0290 2   LEU A O   
11   C CB  . LEU A 3   ? 0.7195 0.6783 0.6098 0.0909  0.0752  -0.0253 2   LEU A CB  
12   C CG  . LEU A 3   ? 0.7641 0.7273 0.6602 0.0707  0.0684  -0.0194 2   LEU A CG  
13   C CD1 . LEU A 3   ? 0.7518 0.6954 0.6373 0.0598  0.0480  -0.0230 2   LEU A CD1 
14   C CD2 . LEU A 3   ? 0.7391 0.7333 0.6765 0.0617  0.0741  -0.0117 2   LEU A CD2 
25   N N   . SER A 4   ? 0.6303 0.6086 0.5176 0.1446  0.1184  -0.0306 3   SER A N   
26   C CA  . SER A 4   ? 0.6643 0.6398 0.5521 0.1677  0.1214  -0.0381 3   SER A CA  
27   C C   . SER A 4   ? 0.6422 0.6588 0.5876 0.1693  0.1257  -0.0323 3   SER A C   
28   O O   . SER A 4   ? 0.6790 0.6923 0.6336 0.1824  0.1170  -0.0382 3   SER A O   
29   C CB  . SER A 4   ? 0.7517 0.7211 0.6085 0.1909  0.1432  -0.0415 3   SER A CB  
30   O OG  . SER A 4   ? 0.8231 0.7703 0.6399 0.1819  0.1420  -0.0408 3   SER A OG  
36   N N   . ASN A 5   ? 0.5736 0.6270 0.5586 0.1554  0.1364  -0.0209 4   ASN A N   
37   C CA  A ASN A 5   ? 0.5392 0.6355 0.5839 0.1541  0.1396  -0.0147 4   ASN A CA  
38   C CA  B ASN A 5   ? 0.5400 0.6351 0.5838 0.1552  0.1388  -0.0154 4   ASN A CA  
39   C C   . ASN A 5   ? 0.4229 0.5227 0.4919 0.1335  0.1165  -0.0133 4   ASN A C   
40   O O   . ASN A 5   ? 0.3784 0.5115 0.4964 0.1300  0.1142  -0.0091 4   ASN A O   
41   C CB  A ASN A 5   ? 0.5726 0.7067 0.6485 0.1501  0.1656  -0.0022 4   ASN A CB  
42   C CB  B ASN A 5   ? 0.5763 0.7114 0.6534 0.1547  0.1661  -0.0036 4   ASN A CB  
43   C CG  A ASN A 5   ? 0.5582 0.6835 0.6214 0.1276  0.1662  0.0055  4   ASN A CG  
44   C CG  B ASN A 5   ? 0.6002 0.7813 0.7382 0.1628  0.1729  0.0006  4   ASN A CG  
45   O OD1 A ASN A 5   ? 0.5081 0.5983 0.5225 0.1252  0.1601  0.0013  4   ASN A OD1 
46   O OD1 B ASN A 5   ? 0.6933 0.8749 0.8440 0.1738  0.1579  -0.0067 4   ASN A OD1 
47   N ND2 A ASN A 5   ? 0.5813 0.7380 0.6899 0.1112  0.1721  0.0166  4   ASN A ND2 
48   N ND2 B ASN A 5   ? 0.5541 0.7711 0.7288 0.1539  0.1912  0.0120  4   ASN A ND2 
61   N N   . LYS A 6   ? 0.3493 0.4171 0.3861 0.1200  0.0997  -0.0165 5   LYS A N   
62   C CA  . LYS A 6   ? 0.3212 0.3915 0.3747 0.1005  0.0815  -0.0144 5   LYS A CA  
63   C C   . LYS A 6   ? 0.3394 0.3821 0.3729 0.1024  0.0597  -0.0210 5   LYS A C   
64   O O   . LYS A 6   ? 0.4121 0.4237 0.4093 0.1118  0.0562  -0.0270 5   LYS A O   
65   C CB  . LYS A 6   ? 0.3623 0.4224 0.3989 0.0821  0.0818  -0.0102 5   LYS A CB  
66   C CG  . LYS A 6   ? 0.4245 0.5071 0.4788 0.0772  0.1019  -0.0012 5   LYS A CG  
67   C CD  . LYS A 6   ? 0.4042 0.5232 0.5135 0.0702  0.1035  0.0047  5   LYS A CD  
68   C CE  . LYS A 6   ? 0.4024 0.5370 0.5298 0.0573  0.1180  0.0153  5   LYS A CE  
69   N NZ  . LYS A 6   ? 0.3619 0.5287 0.5450 0.0469  0.1149  0.0202  5   LYS A NZ  
83   N N   . LEU A 7   ? 0.3040 0.3556 0.3590 0.0927  0.0444  -0.0195 6   LEU A N   
84   C CA  . LEU A 7   ? 0.3353 0.3598 0.3686 0.0907  0.0244  -0.0227 6   LEU A CA  
85   C C   . LEU A 7   ? 0.3322 0.3284 0.3289 0.0770  0.0203  -0.0225 6   LEU A C   
86   O O   . LEU A 7   ? 0.2932 0.2972 0.2924 0.0632  0.0247  -0.0190 6   LEU A O   
87   C CB  . LEU A 7   ? 0.3548 0.3961 0.4157 0.0834  0.0101  -0.0206 6   LEU A CB  
88   C CG  . LEU A 7   ? 0.3675 0.3844 0.4082 0.0828  -0.0099 -0.0217 6   LEU A CG  
89   C CD1 . LEU A 7   ? 0.3816 0.3855 0.4163 0.1030  -0.0156 -0.0249 6   LEU A CD1 
90   C CD2 . LEU A 7   ? 0.3616 0.3951 0.4244 0.0742  -0.0231 -0.0201 6   LEU A CD2 
102  N N   . THR A 8   ? 0.3569 0.3199 0.3217 0.0807  0.0111  -0.0259 7   THR A N   
103  C CA  . THR A 8   ? 0.3637 0.3025 0.2997 0.0667  0.0050  -0.0249 7   THR A CA  
104  C C   . THR A 8   ? 0.3686 0.2867 0.2927 0.0618  -0.0112 -0.0229 7   THR A C   
105  O O   . THR A 8   ? 0.3870 0.3013 0.3165 0.0723  -0.0189 -0.0235 7   THR A O   
106  C CB  . THR A 8   ? 0.4812 0.3955 0.3867 0.0722  0.0090  -0.0300 7   THR A CB  
107  O OG1 . THR A 8   ? 0.5848 0.4786 0.4782 0.0896  0.0052  -0.0357 7   THR A OG1 
108  C CG2 . THR A 8   ? 0.5129 0.4452 0.4228 0.0762  0.0262  -0.0300 7   THR A CG2 
116  N N   . LEU A 9   ? 0.3620 0.2682 0.2705 0.0460  -0.0157 -0.0194 8   LEU A N   
117  C CA  . LEU A 9   ? 0.3600 0.2513 0.2582 0.0383  -0.0273 -0.0143 8   LEU A CA  
118  C C   . LEU A 9   ? 0.4190 0.2769 0.2971 0.0466  -0.0372 -0.0151 8   LEU A C   
119  O O   . LEU A 9   ? 0.4559 0.3037 0.3297 0.0483  -0.0466 -0.0107 8   LEU A O   
120  C CB  . LEU A 9   ? 0.3467 0.2362 0.2354 0.0206  -0.0264 -0.0097 8   LEU A CB  
121  C CG  . LEU A 9   ? 0.4052 0.2802 0.2807 0.0098  -0.0341 -0.0021 8   LEU A CG  
122  C CD1 . LEU A 9   ? 0.4214 0.3070 0.3036 0.0130  -0.0380 0.0009  8   LEU A CD1 
123  C CD2 . LEU A 9   ? 0.3885 0.2712 0.2629 -0.0058 -0.0297 0.0019  8   LEU A CD2 
135  N N   . ASP A 10  ? 0.4665 0.3039 0.3291 0.0535  -0.0361 -0.0209 9   ASP A N   
136  C CA  . ASP A 10  ? 0.5075 0.3075 0.3491 0.0629  -0.0465 -0.0229 9   ASP A CA  
137  C C   . ASP A 10  ? 0.5278 0.3325 0.3811 0.0832  -0.0494 -0.0248 9   ASP A C   
138  O O   . ASP A 10  ? 0.5975 0.3699 0.4337 0.0920  -0.0600 -0.0248 9   ASP A O   
139  C CB  . ASP A 10  ? 0.5430 0.3180 0.3630 0.0689  -0.0454 -0.0316 9   ASP A CB  
140  C CG  . ASP A 10  ? 0.5774 0.3773 0.4077 0.0814  -0.0306 -0.0384 9   ASP A CG  
141  O OD1 . ASP A 10  ? 0.5555 0.3822 0.3982 0.0711  -0.0216 -0.0359 9   ASP A OD1 
142  O OD2 . ASP A 10  ? 0.6265 0.4177 0.4510 0.1024  -0.0271 -0.0457 9   ASP A OD2 
147  N N   . LYS A 11  ? 0.4453 0.2886 0.3288 0.0907  -0.0412 -0.0261 10  LYS A N   
148  C CA  . LYS A 11  ? 0.4632 0.3185 0.3658 0.1096  -0.0451 -0.0276 10  LYS A CA  
149  C C   . LYS A 11  ? 0.4857 0.3617 0.4069 0.1032  -0.0536 -0.0216 10  LYS A C   
150  O O   . LYS A 11  ? 0.5302 0.4227 0.4732 0.1171  -0.0594 -0.0225 10  LYS A O   
151  C CB  . LYS A 11  ? 0.4831 0.3684 0.4104 0.1246  -0.0301 -0.0335 10  LYS A CB  
152  C CG  . LYS A 11  ? 0.6282 0.4879 0.5305 0.1387  -0.0232 -0.0413 10  LYS A CG  
153  C CD  . LYS A 11  ? 0.7835 0.6754 0.7062 0.1513  -0.0033 -0.0451 10  LYS A CD  
154  C CE  . LYS A 11  ? 0.8232 0.6872 0.7115 0.1628  0.0048  -0.0535 10  LYS A CE  
155  N NZ  . LYS A 11  ? 0.7585 0.6017 0.6186 0.1426  0.0023  -0.0532 10  LYS A NZ  
169  N N   . LEU A 12  ? 0.4616 0.3371 0.3740 0.0837  -0.0553 -0.0160 11  LEU A N   
170  C CA  . LEU A 12  ? 0.4765 0.3704 0.4014 0.0776  -0.0624 -0.0121 11  LEU A CA  
171  C C   . LEU A 12  ? 0.5528 0.4162 0.4491 0.0754  -0.0759 -0.0051 11  LEU A C   
172  O O   . LEU A 12  ? 0.5904 0.4288 0.4608 0.0636  -0.0747 0.0001  11  LEU A O   
173  C CB  . LEU A 12  ? 0.4529 0.3664 0.3850 0.0605  -0.0532 -0.0111 11  LEU A CB  
174  C CG  . LEU A 12  ? 0.4907 0.4204 0.4314 0.0534  -0.0595 -0.0092 11  LEU A CG  
175  C CD1 . LEU A 12  ? 0.5344 0.4921 0.5097 0.0629  -0.0649 -0.0134 11  LEU A CD1 
176  C CD2 . LEU A 12  ? 0.4209 0.3610 0.3616 0.0384  -0.0496 -0.0085 11  LEU A CD2 
188  N N   . ASP A 13  ? 0.5605 0.4261 0.4619 0.0867  -0.0892 -0.0040 12  ASP A N   
189  C CA  . ASP A 13  ? 0.6583 0.4944 0.5291 0.0858  -0.1020 0.0044  12  ASP A CA  
190  C C   . ASP A 13  ? 0.6260 0.4710 0.4874 0.0703  -0.1005 0.0088  12  ASP A C   
191  O O   . ASP A 13  ? 0.6368 0.5089 0.5176 0.0707  -0.1037 0.0045  12  ASP A O   
192  C CB  . ASP A 13  ? 0.8284 0.6635 0.7057 0.1054  -0.1186 0.0038  12  ASP A CB  
193  C CG  . ASP A 13  ? 0.9936 0.7987 0.8358 0.1052  -0.1325 0.0136  12  ASP A CG  
194  O OD1 . ASP A 13  ? 1.0347 0.8136 0.8461 0.0914  -0.1273 0.0222  12  ASP A OD1 
195  O OD2 . ASP A 13  ? 1.0783 0.8873 0.9245 0.1189  -0.1488 0.0136  12  ASP A OD2 
200  N N   . VAL A 14  ? 0.5508 0.3739 0.3842 0.0565  -0.0953 0.0171  13  VAL A N   
201  C CA  . VAL A 14  ? 0.5026 0.3344 0.3251 0.0438  -0.0906 0.0216  13  VAL A CA  
202  C C   . VAL A 14  ? 0.4992 0.3047 0.2859 0.0435  -0.0980 0.0330  13  VAL A C   
203  O O   . VAL A 14  ? 0.5116 0.3218 0.2836 0.0352  -0.0928 0.0376  13  VAL A O   
204  C CB  . VAL A 14  ? 0.5217 0.3603 0.3467 0.0274  -0.0750 0.0228  13  VAL A CB  
205  C CG1 . VAL A 14  ? 0.5179 0.3819 0.3731 0.0285  -0.0675 0.0127  13  VAL A CG1 
206  C CG2 . VAL A 14  ? 0.5374 0.3459 0.3436 0.0199  -0.0732 0.0307  13  VAL A CG2 
216  N N   . LYS A 15  ? 0.5288 0.3055 0.2988 0.0535  -0.1092 0.0383  14  LYS A N   
217  C CA  . LYS A 15  ? 0.5930 0.3404 0.3244 0.0527  -0.1150 0.0519  14  LYS A CA  
218  C C   . LYS A 15  ? 0.6312 0.3909 0.3530 0.0602  -0.1244 0.0501  14  LYS A C   
219  O O   . LYS A 15  ? 0.6207 0.3932 0.3594 0.0745  -0.1388 0.0413  14  LYS A O   
220  C CB  . LYS A 15  ? 0.6153 0.3254 0.3298 0.0640  -0.1272 0.0579  14  LYS A CB  
221  C CG  . LYS A 15  ? 0.7021 0.3775 0.3726 0.0614  -0.1314 0.0751  14  LYS A CG  
222  C CD  . LYS A 15  ? 0.8671 0.4994 0.5183 0.0717  -0.1437 0.0826  14  LYS A CD  
223  C CE  . LYS A 15  ? 1.0229 0.6311 0.6435 0.0614  -0.1381 0.0983  14  LYS A CE  
224  N NZ  . LYS A 15  ? 1.1628 0.7356 0.7725 0.0697  -0.1475 0.1023  14  LYS A NZ  
238  N N   . GLY A 16  ? 0.6445 0.4005 0.3391 0.0512  -0.1167 0.0582  15  GLY A N   
239  C CA  . GLY A 16  ? 0.6373 0.4000 0.3142 0.0584  -0.1253 0.0556  15  GLY A CA  
240  C C   . GLY A 16  ? 0.5574 0.3552 0.2640 0.0573  -0.1246 0.0403  15  GLY A C   
241  O O   . GLY A 16  ? 0.5716 0.3732 0.2642 0.0635  -0.1346 0.0354  15  GLY A O   
245  N N   . LYS A 17  ? 0.5330 0.3531 0.2770 0.0499  -0.1140 0.0329  16  LYS A N   
246  C CA  . LYS A 17  ? 0.5156 0.3664 0.2898 0.0477  -0.1126 0.0200  16  LYS A CA  
247  C C   . LYS A 17  ? 0.4654 0.3254 0.2336 0.0354  -0.0948 0.0210  16  LYS A C   
248  O O   . LYS A 17  ? 0.4869 0.3400 0.2462 0.0259  -0.0805 0.0300  16  LYS A O   
249  C CB  . LYS A 17  ? 0.5106 0.3810 0.3284 0.0489  -0.1107 0.0122  16  LYS A CB  
250  C CG  . LYS A 17  ? 0.5980 0.4654 0.4292 0.0636  -0.1262 0.0102  16  LYS A CG  
251  C CD  . LYS A 17  ? 0.7550 0.6339 0.5941 0.0730  -0.1462 0.0036  16  LYS A CD  
252  C CE  . LYS A 17  ? 0.8784 0.7628 0.7411 0.0887  -0.1611 0.0010  16  LYS A CE  
253  N NZ  . LYS A 17  ? 0.8601 0.7653 0.7627 0.0891  -0.1484 -0.0033 16  LYS A NZ  
267  N N   . ARG A 18  ? 0.4332 0.3080 0.2068 0.0360  -0.0974 0.0117  17  ARG A N   
268  C CA  . ARG A 18  ? 0.4130 0.3012 0.1913 0.0271  -0.0817 0.0093  17  ARG A CA  
269  C C   . ARG A 18  ? 0.3826 0.2915 0.2026 0.0214  -0.0753 0.0030  17  ARG A C   
270  O O   . ARG A 18  ? 0.3871 0.3080 0.2344 0.0251  -0.0849 -0.0050 17  ARG A O   
271  C CB  . ARG A 18  ? 0.4180 0.3078 0.1818 0.0317  -0.0886 0.0006  17  ARG A CB  
272  C CG  . ARG A 18  ? 0.4656 0.3328 0.1809 0.0402  -0.0959 0.0059  17  ARG A CG  
273  C CD  . ARG A 18  ? 0.5061 0.3714 0.2054 0.0469  -0.1069 -0.0061 17  ARG A CD  
274  N NE  . ARG A 18  ? 0.5574 0.4331 0.2892 0.0490  -0.1271 -0.0189 17  ARG A NE  
275  C CZ  . ARG A 18  ? 0.5927 0.4782 0.3428 0.0464  -0.1319 -0.0317 17  ARG A CZ  
276  N NH1 . ARG A 18  ? 0.5717 0.4556 0.3069 0.0444  -0.1188 -0.0349 17  ARG A NH1 
277  N NH2 . ARG A 18  ? 0.5835 0.4806 0.3690 0.0459  -0.1503 -0.0409 17  ARG A NH2 
291  N N   . VAL A 19  ? 0.3895 0.3038 0.2148 0.0124  -0.0591 0.0074  18  VAL A N   
292  C CA  . VAL A 19  ? 0.3440 0.2744 0.2012 0.0075  -0.0516 0.0031  18  VAL A CA  
293  C C   . VAL A 19  ? 0.3589 0.3025 0.2221 0.0029  -0.0427 -0.0011 18  VAL A C   
294  O O   . VAL A 19  ? 0.4148 0.3573 0.2616 -0.0007 -0.0332 0.0039  18  VAL A O   
295  C CB  . VAL A 19  ? 0.3734 0.2968 0.2305 0.0017  -0.0434 0.0101  18  VAL A CB  
296  C CG1 . VAL A 19  ? 0.3681 0.3059 0.2518 -0.0013 -0.0362 0.0052  18  VAL A CG1 
297  C CG2 . VAL A 19  ? 0.4043 0.3082 0.2511 0.0077  -0.0529 0.0142  18  VAL A CG2 
307  N N   . VAL A 20  ? 0.3102 0.2665 0.1979 0.0033  -0.0453 -0.0092 19  VAL A N   
308  C CA  . VAL A 20  ? 0.2919 0.2577 0.1877 -0.0009 -0.0365 -0.0126 19  VAL A CA  
309  C C   . VAL A 20  ? 0.2985 0.2742 0.2160 -0.0056 -0.0269 -0.0107 19  VAL A C   
310  O O   . VAL A 20  ? 0.2610 0.2422 0.1983 -0.0043 -0.0290 -0.0123 19  VAL A O   
311  C CB  . VAL A 20  ? 0.3478 0.3149 0.2510 0.0015  -0.0466 -0.0221 19  VAL A CB  
312  C CG1 . VAL A 20  ? 0.3704 0.3464 0.3036 0.0018  -0.0564 -0.0260 19  VAL A CG1 
313  C CG2 . VAL A 20  ? 0.3643 0.3350 0.2710 -0.0013 -0.0380 -0.0254 19  VAL A CG2 
323  N N   . MET A 21  ? 0.2710 0.2498 0.1838 -0.0100 -0.0161 -0.0069 20  MET A N   
324  C CA  . MET A 21  ? 0.2957 0.2796 0.2197 -0.0138 -0.0088 -0.0041 20  MET A CA  
325  C C   . MET A 21  ? 0.2857 0.2784 0.2174 -0.0157 -0.0015 -0.0053 20  MET A C   
326  O O   . MET A 21  ? 0.3014 0.2968 0.2241 -0.0160 0.0027  -0.0037 20  MET A O   
327  C CB  . MET A 21  ? 0.2954 0.2725 0.2066 -0.0181 -0.0063 0.0029  20  MET A CB  
328  C CG  . MET A 21  ? 0.3206 0.2986 0.2396 -0.0212 -0.0027 0.0037  20  MET A CG  
329  S SD  . MET A 21  ? 0.3869 0.3543 0.2938 -0.0294 -0.0036 0.0111  20  MET A SD  
330  C CE  . MET A 21  ? 0.4166 0.3628 0.3100 -0.0255 -0.0122 0.0128  20  MET A CE  
340  N N   . ARG A 22  ? 0.2620 0.2594 0.2100 -0.0157 0.0008  -0.0073 21  ARG A N   
341  C CA  . ARG A 22  ? 0.2320 0.2343 0.1853 -0.0168 0.0074  -0.0065 21  ARG A CA  
342  C C   . ARG A 22  ? 0.2539 0.2576 0.2018 -0.0191 0.0115  -0.0019 21  ARG A C   
343  O O   . ARG A 22  ? 0.2730 0.2728 0.2201 -0.0192 0.0110  -0.0011 21  ARG A O   
344  C CB  . ARG A 22  ? 0.2478 0.2523 0.2183 -0.0169 0.0093  -0.0078 21  ARG A CB  
345  C CG  . ARG A 22  ? 0.2753 0.2780 0.2505 -0.0172 0.0111  -0.0090 21  ARG A CG  
346  C CD  . ARG A 22  ? 0.2701 0.2738 0.2370 -0.0158 0.0168  -0.0057 21  ARG A CD  
347  N NE  . ARG A 22  ? 0.2764 0.2745 0.2476 -0.0144 0.0179  -0.0066 21  ARG A NE  
348  C CZ  . ARG A 22  ? 0.2747 0.2722 0.2416 -0.0111 0.0216  -0.0038 21  ARG A CZ  
349  N NH1 . ARG A 22  ? 0.2813 0.2870 0.2422 -0.0099 0.0237  -0.0001 21  ARG A NH1 
350  N NH2 . ARG A 22  ? 0.2793 0.2667 0.2491 -0.0092 0.0216  -0.0046 21  ARG A NH2 
364  N N   . VAL A 23  ? 0.2596 0.2691 0.2046 -0.0200 0.0146  0.0003  22  VAL A N   
365  C CA  . VAL A 23  ? 0.2678 0.2813 0.2116 -0.0230 0.0156  0.0042  22  VAL A CA  
366  C C   . VAL A 23  ? 0.2759 0.2956 0.2250 -0.0198 0.0188  0.0047  22  VAL A C   
367  O O   . VAL A 23  ? 0.2716 0.2910 0.2234 -0.0157 0.0209  0.0025  22  VAL A O   
368  C CB  . VAL A 23  ? 0.2709 0.2896 0.2108 -0.0279 0.0152  0.0086  22  VAL A CB  
369  C CG1 . VAL A 23  ? 0.2965 0.3036 0.2281 -0.0311 0.0111  0.0097  22  VAL A CG1 
370  C CG2 . VAL A 23  ? 0.2873 0.3142 0.2258 -0.0245 0.0199  0.0090  22  VAL A CG2 
380  N N   . ASP A 24  ? 0.2478 0.2700 0.1963 -0.0210 0.0174  0.0074  23  ASP A N   
381  C CA  . ASP A 24  ? 0.2624 0.2907 0.2144 -0.0167 0.0185  0.0091  23  ASP A CA  
382  C C   . ASP A 24  ? 0.2748 0.3191 0.2337 -0.0189 0.0167  0.0122  23  ASP A C   
383  O O   . ASP A 24  ? 0.2796 0.3276 0.2398 -0.0239 0.0108  0.0144  23  ASP A O   
384  C CB  . ASP A 24  ? 0.3136 0.3344 0.2589 -0.0146 0.0171  0.0104  23  ASP A CB  
385  C CG  . ASP A 24  ? 0.3231 0.3467 0.2697 -0.0083 0.0174  0.0132  23  ASP A CG  
386  O OD1 . ASP A 24  ? 0.2754 0.3118 0.2305 -0.0062 0.0161  0.0140  23  ASP A OD1 
387  O OD2 . ASP A 24  ? 0.3143 0.3275 0.2532 -0.0045 0.0195  0.0154  23  ASP A OD2 
392  N N   . PHE A 25  ? 0.2579 0.3118 0.2219 -0.0149 0.0215  0.0121  24  PHE A N   
393  C CA  . PHE A 25  ? 0.2400 0.3148 0.2151 -0.0146 0.0237  0.0161  24  PHE A CA  
394  C C   . PHE A 25  ? 0.2239 0.3074 0.2061 -0.0040 0.0250  0.0159  24  PHE A C   
395  O O   . PHE A 25  ? 0.2382 0.3395 0.2299 0.0017  0.0302  0.0175  24  PHE A O   
396  C CB  . PHE A 25  ? 0.2469 0.3266 0.2186 -0.0146 0.0308  0.0167  24  PHE A CB  
397  C CG  . PHE A 25  ? 0.2634 0.3384 0.2303 -0.0253 0.0292  0.0202  24  PHE A CG  
398  C CD1 . PHE A 25  ? 0.3024 0.3691 0.2696 -0.0340 0.0211  0.0214  24  PHE A CD1 
399  C CD2 . PHE A 25  ? 0.3147 0.3892 0.2723 -0.0253 0.0351  0.0221  24  PHE A CD2 
400  C CE1 . PHE A 25  ? 0.3468 0.4042 0.3081 -0.0430 0.0185  0.0246  24  PHE A CE1 
401  C CE2 . PHE A 25  ? 0.3475 0.4139 0.2983 -0.0345 0.0332  0.0269  24  PHE A CE2 
402  C CZ  . PHE A 25  ? 0.3344 0.3917 0.2884 -0.0436 0.0246  0.0281  24  PHE A CZ  
412  N N   . ASN A 26  ? 0.2308 0.3009 0.2074 0.0001  0.0214  0.0146  25  ASN A N   
413  C CA  . ASN A 26  ? 0.2399 0.3128 0.2204 0.0111  0.0207  0.0155  25  ASN A CA  
414  C C   . ASN A 26  ? 0.2250 0.3169 0.2176 0.0107  0.0134  0.0201  25  ASN A C   
415  O O   . ASN A 26  ? 0.2539 0.3380 0.2401 0.0120  0.0060  0.0218  25  ASN A O   
416  C CB  . ASN A 26  ? 0.2832 0.3321 0.2515 0.0139  0.0199  0.0148  25  ASN A CB  
417  C CG  . ASN A 26  ? 0.2879 0.3330 0.2563 0.0257  0.0183  0.0170  25  ASN A CG  
418  O OD1 . ASN A 26  ? 0.2846 0.3418 0.2615 0.0350  0.0197  0.0161  25  ASN A OD1 
419  N ND2 . ASN A 26  ? 0.2998 0.3273 0.2575 0.0268  0.0163  0.0204  25  ASN A ND2 
426  N N   . VAL A 27  ? 0.2097 0.3277 0.2201 0.0091  0.0156  0.0226  26  VAL A N   
427  C CA  . VAL A 27  ? 0.2174 0.3591 0.2470 0.0052  0.0071  0.0272  26  VAL A CA  
428  C C   . VAL A 27  ? 0.2327 0.3902 0.2754 0.0199  0.0051  0.0288  26  VAL A C   
429  O O   . VAL A 27  ? 0.2456 0.4029 0.2874 0.0328  0.0140  0.0268  26  VAL A O   
430  C CB  . VAL A 27  ? 0.2312 0.3969 0.2796 -0.0056 0.0114  0.0315  26  VAL A CB  
431  C CG1 . VAL A 27  ? 0.2685 0.4155 0.3031 -0.0198 0.0100  0.0308  26  VAL A CG1 
432  C CG2 . VAL A 27  ? 0.2336 0.4157 0.2892 0.0034  0.0266  0.0324  26  VAL A CG2 
442  N N   . PRO A 28  ? 0.2070 0.3780 0.2619 0.0194  -0.0079 0.0319  27  PRO A N   
443  C CA  . PRO A 28  ? 0.2094 0.3982 0.2796 0.0351  -0.0116 0.0340  27  PRO A CA  
444  C C   . PRO A 28  ? 0.2289 0.4578 0.3322 0.0386  -0.0029 0.0372  27  PRO A C   
445  O O   . PRO A 28  ? 0.2040 0.4532 0.3246 0.0246  0.0004  0.0407  27  PRO A O   
446  C CB  . PRO A 28  ? 0.2872 0.4775 0.3585 0.0320  -0.0312 0.0360  27  PRO A CB  
447  C CG  . PRO A 28  ? 0.2946 0.4802 0.3627 0.0121  -0.0366 0.0352  27  PRO A CG  
448  C CD  . PRO A 28  ? 0.2490 0.4128 0.2983 0.0067  -0.0223 0.0322  27  PRO A CD  
456  N N   . MET A 29  ? 0.2776 0.5153 0.3876 0.0584  0.0026  0.0366  28  MET A N   
457  C CA  . MET A 29  ? 0.2941 0.5685 0.4315 0.0679  0.0154  0.0389  28  MET A CA  
458  C C   . MET A 29  ? 0.2806 0.5803 0.4425 0.0856  0.0074  0.0415  28  MET A C   
459  O O   . MET A 29  ? 0.2716 0.5486 0.4179 0.0965  -0.0040 0.0399  28  MET A O   
460  C CB  . MET A 29  ? 0.3067 0.5633 0.4233 0.0803  0.0325  0.0331  28  MET A CB  
461  C CG  . MET A 29  ? 0.3883 0.6159 0.4773 0.0670  0.0386  0.0293  28  MET A CG  
462  S SD  . MET A 29  ? 0.5322 0.7873 0.6347 0.0538  0.0524  0.0347  28  MET A SD  
463  C CE  . MET A 29  ? 0.6283 0.8485 0.6925 0.0580  0.0638  0.0266  28  MET A CE  
473  N N   . LYS A 30  ? 0.2667 0.6148 0.4681 0.0893  0.0144  0.0466  29  LYS A N   
474  C CA  . LYS A 30  ? 0.3368 0.7185 0.5701 0.1076  0.0077  0.0496  29  LYS A CA  
475  C C   . LYS A 30  ? 0.3675 0.7978 0.6366 0.1143  0.0274  0.0541  29  LYS A C   
476  O O   . LYS A 30  ? 0.2938 0.7453 0.5788 0.0953  0.0364  0.0595  29  LYS A O   
477  C CB  . LYS A 30  ? 0.3732 0.7718 0.6286 0.0961  -0.0169 0.0542  29  LYS A CB  
478  C CG  . LYS A 30  ? 0.4654 0.8943 0.7512 0.1156  -0.0302 0.0571  29  LYS A CG  
479  C CD  . LYS A 30  ? 0.5756 1.0117 0.8735 0.1016  -0.0586 0.0599  29  LYS A CD  
480  C CE  . LYS A 30  ? 0.7011 1.1712 1.0328 0.1198  -0.0762 0.0633  29  LYS A CE  
481  N NZ  . LYS A 30  ? 0.7483 1.2308 1.0963 0.1031  -0.1052 0.0653  29  LYS A NZ  
495  N N   . ASN A 31  ? 0.4605 0.9050 0.7387 0.1422  0.0360  0.0520  30  ASN A N   
496  C CA  . ASN A 31  ? 0.4745 0.9533 0.7757 0.1500  0.0581  0.0541  30  ASN A CA  
497  C C   . ASN A 31  ? 0.4953 0.9612 0.7726 0.1379  0.0782  0.0536  30  ASN A C   
498  O O   . ASN A 31  ? 0.4908 0.9808 0.7862 0.1263  0.0917  0.0594  30  ASN A O   
499  C CB  . ASN A 31  ? 0.3882 0.9149 0.7419 0.1376  0.0522  0.0625  30  ASN A CB  
500  C CG  . ASN A 31  ? 0.3855 0.9249 0.7625 0.1515  0.0311  0.0622  30  ASN A CG  
501  O OD1 . ASN A 31  ? 0.3759 0.9263 0.7722 0.1375  0.0081  0.0660  30  ASN A OD1 
502  N ND2 . ASN A 31  ? 0.4136 0.9480 0.7861 0.1794  0.0371  0.0571  30  ASN A ND2 
509  N N   . ASN A 32  ? 0.5363 0.9546 0.7680 0.1380  0.0779  0.0460  31  ASN A N   
510  C CA  . ASN A 32  ? 0.5785 0.9739 0.7783 0.1296  0.0934  0.0431  31  ASN A CA  
511  C C   . ASN A 32  ? 0.4642 0.8697 0.6735 0.0991  0.0927  0.0516  31  ASN A C   
512  O O   . ASN A 32  ? 0.4457 0.8407 0.6343 0.0917  0.1066  0.0522  31  ASN A O   
513  C CB  . ASN A 32  ? 0.6987 1.1035 0.8928 0.1470  0.1153  0.0405  31  ASN A CB  
514  C CG  . ASN A 32  ? 0.8074 1.1744 0.9544 0.1477  0.1268  0.0331  31  ASN A CG  
515  O OD1 . ASN A 32  ? 0.8297 1.1663 0.9517 0.1349  0.1195  0.0302  31  ASN A OD1 
516  N ND2 . ASN A 32  ? 0.8842 1.2479 1.0164 0.1616  0.1422  0.0290  31  ASN A ND2 
523  N N   . GLN A 33  ? 0.3101 0.7312 0.5466 0.0818  0.0752  0.0577  32  GLN A N   
524  C CA  . GLN A 33  ? 0.2636 0.6920 0.5116 0.0528  0.0712  0.0655  32  GLN A CA  
525  C C   . GLN A 33  ? 0.1934 0.5805 0.4169 0.0386  0.0491  0.0603  32  GLN A C   
526  O O   . GLN A 33  ? 0.1953 0.5681 0.4123 0.0480  0.0338  0.0554  32  GLN A O   
527  C CB  . GLN A 33  ? 0.3753 0.8608 0.6813 0.0432  0.0680  0.0772  32  GLN A CB  
528  C CG  . GLN A 33  ? 0.5422 1.0528 0.8667 0.0547  0.0874  0.0797  32  GLN A CG  
529  C CD  . GLN A 33  ? 0.6791 1.1976 1.0104 0.0343  0.1016  0.0885  32  GLN A CD  
530  O OE1 . GLN A 33  ? 0.8271 1.3744 1.1978 0.0188  0.0979  0.0964  32  GLN A OE1 
531  N NE2 . GLN A 33  ? 0.6700 1.1604 0.9619 0.0340  0.1165  0.0870  32  GLN A NE2 
540  N N   . ILE A 34  ? 0.1890 0.5577 0.3986 0.0171  0.0480  0.0623  33  ILE A N   
541  C CA  . ILE A 34  ? 0.1855 0.5170 0.3719 0.0041  0.0293  0.0575  33  ILE A CA  
542  C C   . ILE A 34  ? 0.1851 0.5363 0.4006 -0.0064 0.0086  0.0611  33  ILE A C   
543  O O   . ILE A 34  ? 0.1845 0.5717 0.4379 -0.0195 0.0081  0.0697  33  ILE A O   
544  C CB  . ILE A 34  ? 0.1849 0.4929 0.3505 -0.0137 0.0340  0.0588  33  ILE A CB  
545  C CG1 . ILE A 34  ? 0.2166 0.5022 0.3501 -0.0025 0.0504  0.0539  33  ILE A CG1 
546  C CG2 . ILE A 34  ? 0.1844 0.4576 0.3289 -0.0257 0.0159  0.0539  33  ILE A CG2 
547  C CD1 . ILE A 34  ? 0.3152 0.5865 0.4330 -0.0169 0.0575  0.0575  33  ILE A CD1 
559  N N   . THR A 35  ? 0.1891 0.5168 0.3872 -0.0009 -0.0091 0.0551  34  THR A N   
560  C CA  . THR A 35  ? 0.2106 0.5535 0.4308 -0.0088 -0.0322 0.0569  34  THR A CA  
561  C C   . THR A 35  ? 0.2141 0.5272 0.4146 -0.0287 -0.0473 0.0540  34  THR A C   
562  O O   . THR A 35  ? 0.2643 0.5893 0.4842 -0.0406 -0.0672 0.0554  34  THR A O   
563  C CB  . THR A 35  ? 0.2496 0.5853 0.4607 0.0107  -0.0453 0.0531  34  THR A CB  
564  O OG1 . THR A 35  ? 0.2482 0.5350 0.4113 0.0167  -0.0448 0.0465  34  THR A OG1 
565  C CG2 . THR A 35  ? 0.2633 0.6296 0.4976 0.0327  -0.0335 0.0555  34  THR A CG2 
573  N N   . ASN A 36  ? 0.2170 0.4922 0.3807 -0.0322 -0.0390 0.0497  35  ASN A N   
574  C CA  . ASN A 36  ? 0.2381 0.4815 0.3791 -0.0474 -0.0515 0.0458  35  ASN A CA  
575  C C   . ASN A 36  ? 0.2110 0.4304 0.3288 -0.0518 -0.0355 0.0448  35  ASN A C   
576  O O   . ASN A 36  ? 0.2294 0.4307 0.3236 -0.0392 -0.0244 0.0408  35  ASN A O   
577  C CB  . ASN A 36  ? 0.2783 0.4912 0.3871 -0.0380 -0.0664 0.0386  35  ASN A CB  
578  C CG  . ASN A 36  ? 0.3273 0.5077 0.4107 -0.0505 -0.0796 0.0333  35  ASN A CG  
579  O OD1 . ASN A 36  ? 0.3111 0.4905 0.4034 -0.0672 -0.0808 0.0349  35  ASN A OD1 
580  N ND2 . ASN A 36  ? 0.3429 0.4946 0.3925 -0.0414 -0.0893 0.0274  35  ASN A ND2 
587  N N   . ASN A 37  ? 0.2061 0.4241 0.3308 -0.0697 -0.0354 0.0487  36  ASN A N   
588  C CA  . ASN A 37  ? 0.2157 0.4101 0.3173 -0.0727 -0.0224 0.0483  36  ASN A CA  
589  C C   . ASN A 37  ? 0.2289 0.3819 0.2982 -0.0772 -0.0328 0.0410  36  ASN A C   
590  O O   . ASN A 37  ? 0.2439 0.3766 0.2963 -0.0812 -0.0257 0.0409  36  ASN A O   
591  C CB  . ASN A 37  ? 0.2880 0.5015 0.4113 -0.0872 -0.0126 0.0588  36  ASN A CB  
592  C CG  . ASN A 37  ? 0.3807 0.5974 0.5240 -0.1082 -0.0285 0.0633  36  ASN A CG  
593  O OD1 . ASN A 37  ? 0.3884 0.5836 0.5200 -0.1120 -0.0480 0.0562  36  ASN A OD1 
594  N ND2 . ASN A 37  ? 0.4351 0.6770 0.6074 -0.1224 -0.0203 0.0754  36  ASN A ND2 
601  N N   . GLN A 38  ? 0.2574 0.3968 0.3145 -0.0735 -0.0485 0.0347  37  GLN A N   
602  C CA  . GLN A 38  ? 0.3062 0.4070 0.3299 -0.0742 -0.0570 0.0270  37  GLN A CA  
603  C C   . GLN A 38  ? 0.2642 0.3436 0.2642 -0.0667 -0.0424 0.0241  37  GLN A C   
604  O O   . GLN A 38  ? 0.2732 0.3283 0.2568 -0.0718 -0.0439 0.0214  37  GLN A O   
605  C CB  . GLN A 38  ? 0.3875 0.4780 0.3943 -0.0640 -0.0698 0.0211  37  GLN A CB  
606  C CG  . GLN A 38  ? 0.4875 0.5391 0.4549 -0.0592 -0.0732 0.0131  37  GLN A CG  
607  C CD  . GLN A 38  ? 0.4922 0.5330 0.4357 -0.0426 -0.0708 0.0104  37  GLN A CD  
608  O OE1 . GLN A 38  ? 0.5174 0.5722 0.4689 -0.0332 -0.0612 0.0143  37  GLN A OE1 
609  N NE2 . GLN A 38  ? 0.4810 0.4941 0.3928 -0.0386 -0.0788 0.0042  37  GLN A NE2 
618  N N   . ARG A 39  ? 0.2420 0.3278 0.2396 -0.0536 -0.0303 0.0240  38  ARG A N   
619  C CA  . ARG A 39  ? 0.2614 0.3285 0.2402 -0.0472 -0.0192 0.0208  38  ARG A CA  
620  C C   . ARG A 39  ? 0.2701 0.3377 0.2524 -0.0536 -0.0110 0.0238  38  ARG A C   
621  O O   . ARG A 39  ? 0.3087 0.3574 0.2755 -0.0516 -0.0073 0.0207  38  ARG A O   
622  C CB  . ARG A 39  ? 0.3061 0.3777 0.2837 -0.0340 -0.0104 0.0201  38  ARG A CB  
623  C CG  . ARG A 39  ? 0.3206 0.3760 0.2802 -0.0261 -0.0147 0.0172  38  ARG A CG  
624  C CD  . ARG A 39  ? 0.2995 0.3566 0.2589 -0.0145 -0.0080 0.0184  38  ARG A CD  
625  N NE  . ARG A 39  ? 0.3040 0.3420 0.2427 -0.0081 -0.0090 0.0179  38  ARG A NE  
626  C CZ  . ARG A 39  ? 0.2978 0.3300 0.2317 0.0009  -0.0042 0.0205  38  ARG A CZ  
627  N NH1 . ARG A 39  ? 0.3041 0.3463 0.2519 0.0058  0.0002  0.0217  38  ARG A NH1 
628  N NH2 . ARG A 39  ? 0.2935 0.3076 0.2068 0.0056  -0.0029 0.0222  38  ARG A NH2 
642  N N   . ILE A 40  ? 0.2314 0.3216 0.2339 -0.0603 -0.0074 0.0306  39  ILE A N   
643  C CA  . ILE A 40  ? 0.2479 0.3373 0.2492 -0.0658 0.0013  0.0355  39  ILE A CA  
644  C C   . ILE A 40  ? 0.2616 0.3319 0.2569 -0.0792 -0.0074 0.0374  39  ILE A C   
645  O O   . ILE A 40  ? 0.3012 0.3510 0.2799 -0.0796 -0.0052 0.0369  39  ILE A O   
646  C CB  . ILE A 40  ? 0.2691 0.3906 0.2929 -0.0673 0.0114  0.0438  39  ILE A CB  
647  C CG1 . ILE A 40  ? 0.2746 0.4118 0.3030 -0.0515 0.0187  0.0405  39  ILE A CG1 
648  C CG2 . ILE A 40  ? 0.2802 0.3972 0.2951 -0.0715 0.0222  0.0499  39  ILE A CG2 
649  C CD1 . ILE A 40  ? 0.2880 0.4622 0.3428 -0.0497 0.0281  0.0479  39  ILE A CD1 
661  N N   . LYS A 41  ? 0.2590 0.3344 0.2678 -0.0900 -0.0195 0.0393  40  LYS A N   
662  C CA  . LYS A 41  ? 0.3249 0.3769 0.3272 -0.1036 -0.0308 0.0401  40  LYS A CA  
663  C C   . LYS A 41  ? 0.3488 0.3650 0.3205 -0.0955 -0.0364 0.0302  40  LYS A C   
664  O O   . LYS A 41  ? 0.3370 0.3276 0.2952 -0.1005 -0.0401 0.0302  40  LYS A O   
665  C CB  . LYS A 41  ? 0.4415 0.5041 0.4638 -0.1156 -0.0465 0.0413  40  LYS A CB  
666  C CG  . LYS A 41  ? 0.6687 0.7108 0.6920 -0.1340 -0.0586 0.0446  40  LYS A CG  
667  C CD  . LYS A 41  ? 0.8368 0.8990 0.8906 -0.1491 -0.0736 0.0482  40  LYS A CD  
668  C CE  . LYS A 41  ? 1.0075 1.0495 1.0674 -0.1712 -0.0849 0.0539  40  LYS A CE  
669  N NZ  . LYS A 41  ? 1.0962 1.1619 1.1937 -0.1894 -0.1006 0.0587  40  LYS A NZ  
683  N N   . ALA A 42  ? 0.3217 0.3358 0.2825 -0.0822 -0.0363 0.0225  41  ALA A N   
684  C CA  . ALA A 42  ? 0.3441 0.3292 0.2785 -0.0733 -0.0389 0.0140  41  ALA A CA  
685  C C   . ALA A 42  ? 0.3410 0.3156 0.2665 -0.0678 -0.0291 0.0141  41  ALA A C   
686  O O   . ALA A 42  ? 0.3557 0.3060 0.2636 -0.0628 -0.0321 0.0088  41  ALA A O   
687  C CB  . ALA A 42  ? 0.3338 0.3223 0.2601 -0.0606 -0.0369 0.0089  41  ALA A CB  
693  N N   . ALA A 43  ? 0.3344 0.3266 0.2704 -0.0665 -0.0183 0.0192  42  ALA A N   
694  C CA  . ALA A 43  ? 0.3235 0.3068 0.2509 -0.0610 -0.0118 0.0191  42  ALA A CA  
695  C C   . ALA A 43  ? 0.3426 0.3136 0.2656 -0.0700 -0.0141 0.0257  42  ALA A C   
696  O O   . ALA A 43  ? 0.3653 0.3234 0.2773 -0.0649 -0.0126 0.0255  42  ALA A O   
697  C CB  . ALA A 43  ? 0.3385 0.3410 0.2733 -0.0544 -0.0015 0.0202  42  ALA A CB  
703  N N   . VAL A 44  ? 0.3448 0.3196 0.2774 -0.0837 -0.0184 0.0325  43  VAL A N   
704  C CA  . VAL A 44  ? 0.3695 0.3326 0.2988 -0.0942 -0.0185 0.0420  43  VAL A CA  
705  C C   . VAL A 44  ? 0.4350 0.3616 0.3435 -0.0918 -0.0273 0.0383  43  VAL A C   
706  O O   . VAL A 44  ? 0.4506 0.3640 0.3481 -0.0917 -0.0248 0.0444  43  VAL A O   
707  C CB  . VAL A 44  ? 0.3795 0.3559 0.3291 -0.1119 -0.0216 0.0511  43  VAL A CB  
708  C CG1 . VAL A 44  ? 0.4183 0.3751 0.3630 -0.1256 -0.0234 0.0622  43  VAL A CG1 
709  C CG2 . VAL A 44  ? 0.4035 0.4186 0.3737 -0.1108 -0.0090 0.0568  43  VAL A CG2 
719  N N   . PRO A 45  ? 0.4180 0.3251 0.3171 -0.0880 -0.0374 0.0287  44  PRO A N   
720  C CA  . PRO A 45  ? 0.4300 0.3013 0.3084 -0.0823 -0.0449 0.0245  44  PRO A CA  
721  C C   . PRO A 45  ? 0.3890 0.2588 0.2593 -0.0675 -0.0383 0.0227  44  PRO A C   
722  O O   . PRO A 45  ? 0.3929 0.2403 0.2509 -0.0661 -0.0419 0.0264  44  PRO A O   
723  C CB  . PRO A 45  ? 0.4641 0.3212 0.3327 -0.0763 -0.0537 0.0126  44  PRO A CB  
724  C CG  . PRO A 45  ? 0.4687 0.3443 0.3531 -0.0890 -0.0582 0.0147  44  PRO A CG  
725  C CD  . PRO A 45  ? 0.4430 0.3560 0.3474 -0.0895 -0.0446 0.0222  44  PRO A CD  
733  N N   . SER A 46  ? 0.3686 0.2602 0.2460 -0.0567 -0.0304 0.0175  45  SER A N   
734  C CA  . SER A 46  ? 0.3705 0.2645 0.2458 -0.0447 -0.0263 0.0159  45  SER A CA  
735  C C   . SER A 46  ? 0.3789 0.2770 0.2520 -0.0491 -0.0234 0.0251  45  SER A C   
736  O O   . SER A 46  ? 0.3834 0.2684 0.2462 -0.0422 -0.0267 0.0263  45  SER A O   
737  C CB  . SER A 46  ? 0.3519 0.2688 0.2389 -0.0361 -0.0189 0.0099  45  SER A CB  
738  O OG  . SER A 46  ? 0.3633 0.2735 0.2471 -0.0286 -0.0197 0.0024  45  SER A OG  
744  N N   . ILE A 47  ? 0.3591 0.2765 0.2405 -0.0583 -0.0168 0.0317  46  ILE A N   
745  C CA  . ILE A 47  ? 0.3680 0.2901 0.2428 -0.0603 -0.0111 0.0406  46  ILE A CA  
746  C C   . ILE A 47  ? 0.4038 0.3002 0.2640 -0.0679 -0.0158 0.0506  46  ILE A C   
747  O O   . ILE A 47  ? 0.4257 0.3089 0.2691 -0.0622 -0.0170 0.0548  46  ILE A O   
748  C CB  . ILE A 47  ? 0.3645 0.3142 0.2522 -0.0669 -0.0009 0.0457  46  ILE A CB  
749  C CG1 . ILE A 47  ? 0.3421 0.3118 0.2407 -0.0577 0.0029  0.0363  46  ILE A CG1 
750  C CG2 . ILE A 47  ? 0.4005 0.3536 0.2766 -0.0680 0.0074  0.0559  46  ILE A CG2 
751  C CD1 . ILE A 47  ? 0.3624 0.3584 0.2761 -0.0616 0.0114  0.0397  46  ILE A CD1 
763  N N   . LYS A 48  ? 0.3964 0.2829 0.2619 -0.0810 -0.0202 0.0546  47  LYS A N   
764  C CA  . LYS A 48  ? 0.4373 0.2952 0.2905 -0.0912 -0.0255 0.0654  47  LYS A CA  
765  C C   . LYS A 48  ? 0.4678 0.2921 0.3009 -0.0791 -0.0358 0.0604  47  LYS A C   
766  O O   . LYS A 48  ? 0.5036 0.3048 0.3192 -0.0800 -0.0382 0.0701  47  LYS A O   
767  C CB  . LYS A 48  ? 0.5142 0.3669 0.3806 -0.1084 -0.0318 0.0679  47  LYS A CB  
768  C CG  . LYS A 48  ? 0.7650 0.5956 0.6270 -0.1258 -0.0344 0.0832  47  LYS A CG  
769  C CD  . LYS A 48  ? 0.9547 0.7924 0.8399 -0.1464 -0.0400 0.0867  47  LYS A CD  
770  C CE  . LYS A 48  ? 1.0256 0.9116 0.9390 -0.1537 -0.0265 0.0936  47  LYS A CE  
771  N NZ  . LYS A 48  ? 1.0547 0.9526 0.9969 -0.1746 -0.0337 0.0981  47  LYS A NZ  
785  N N   . PHE A 49  ? 0.4237 0.2451 0.2586 -0.0667 -0.0412 0.0463  48  PHE A N   
786  C CA  . PHE A 49  ? 0.4570 0.2528 0.2775 -0.0515 -0.0494 0.0406  48  PHE A CA  
787  C C   . PHE A 49  ? 0.4159 0.2178 0.2295 -0.0408 -0.0476 0.0439  48  PHE A C   
788  O O   . PHE A 49  ? 0.4391 0.2151 0.2359 -0.0342 -0.0551 0.0481  48  PHE A O   
789  C CB  . PHE A 49  ? 0.4682 0.2699 0.2956 -0.0385 -0.0505 0.0258  48  PHE A CB  
790  C CG  . PHE A 49  ? 0.4682 0.2502 0.2862 -0.0204 -0.0569 0.0192  48  PHE A CG  
791  C CD1 . PHE A 49  ? 0.4785 0.2787 0.3049 -0.0063 -0.0544 0.0160  48  PHE A CD1 
792  C CD2 . PHE A 49  ? 0.5198 0.2656 0.3224 -0.0164 -0.0662 0.0152  48  PHE A CD2 
793  C CE1 . PHE A 49  ? 0.5265 0.3144 0.3502 0.0117  -0.0602 0.0102  48  PHE A CE1 
794  C CE2 . PHE A 49  ? 0.5320 0.2616 0.3273 0.0036  -0.0711 0.0086  48  PHE A CE2 
795  C CZ  . PHE A 49  ? 0.5752 0.3288 0.3834 0.0178  -0.0675 0.0065  48  PHE A CZ  
805  N N   . CYS A 50  ? 0.4487 0.2820 0.2734 -0.0378 -0.0396 0.0412  49  CYS A N   
806  C CA  . CYS A 50  ? 0.4560 0.2933 0.2722 -0.0277 -0.0411 0.0426  49  CYS A CA  
807  C C   . CYS A 50  ? 0.4821 0.3020 0.2754 -0.0341 -0.0406 0.0572  49  CYS A C   
808  O O   . CYS A 50  ? 0.5033 0.3030 0.2781 -0.0250 -0.0489 0.0608  49  CYS A O   
809  C CB  . CYS A 50  ? 0.4137 0.2829 0.2434 -0.0251 -0.0338 0.0367  49  CYS A CB  
810  S SG  . CYS A 50  ? 0.4311 0.3178 0.2849 -0.0156 -0.0343 0.0223  49  CYS A SG  
816  N N   . LEU A 51  ? 0.4911 0.3193 0.2858 -0.0492 -0.0307 0.0670  50  LEU A N   
817  C CA  . LEU A 51  ? 0.5403 0.3546 0.3140 -0.0568 -0.0261 0.0838  50  LEU A CA  
818  C C   . LEU A 51  ? 0.5545 0.3283 0.3119 -0.0604 -0.0360 0.0923  50  LEU A C   
819  O O   . LEU A 51  ? 0.5817 0.3330 0.3128 -0.0561 -0.0390 0.1026  50  LEU A O   
820  C CB  . LEU A 51  ? 0.5416 0.3785 0.3288 -0.0731 -0.0119 0.0929  50  LEU A CB  
821  C CG  . LEU A 51  ? 0.5176 0.3908 0.3166 -0.0677 -0.0014 0.0859  50  LEU A CG  
822  C CD1 . LEU A 51  ? 0.5439 0.4414 0.3626 -0.0824 0.0114  0.0942  50  LEU A CD1 
823  C CD2 . LEU A 51  ? 0.5525 0.4251 0.3255 -0.0558 0.0021  0.0883  50  LEU A CD2 
835  N N   . ASP A 52  ? 0.5448 0.3051 0.3138 -0.0675 -0.0423 0.0879  51  ASP A N   
836  C CA  . ASP A 52  ? 0.5928 0.3091 0.3455 -0.0720 -0.0528 0.0953  51  ASP A CA  
837  C C   . ASP A 52  ? 0.5707 0.2613 0.3052 -0.0512 -0.0652 0.0897  51  ASP A C   
838  O O   . ASP A 52  ? 0.6312 0.2833 0.3432 -0.0508 -0.0731 0.0998  51  ASP A O   
839  C CB  . ASP A 52  ? 0.7056 0.4112 0.4726 -0.0823 -0.0592 0.0884  51  ASP A CB  
840  C CG  . ASP A 52  ? 0.8694 0.5934 0.6553 -0.1059 -0.0512 0.0977  51  ASP A CG  
841  O OD1 . ASP A 52  ? 0.8724 0.6151 0.6594 -0.1145 -0.0385 0.1119  51  ASP A OD1 
842  O OD2 . ASP A 52  ? 0.9518 0.6726 0.7515 -0.1148 -0.0580 0.0905  51  ASP A OD2 
847  N N   . ASN A 53  ? 0.5385 0.2502 0.2838 -0.0339 -0.0673 0.0749  52  ASN A N   
848  C CA  . ASN A 53  ? 0.5968 0.2928 0.3323 -0.0130 -0.0791 0.0693  52  ASN A CA  
849  C C   . ASN A 53  ? 0.6309 0.3394 0.3556 -0.0031 -0.0802 0.0729  52  ASN A C   
850  O O   . ASN A 53  ? 0.6097 0.3203 0.3367 0.0152  -0.0902 0.0651  52  ASN A O   
851  C CB  . ASN A 53  ? 0.5887 0.3003 0.3458 0.0003  -0.0812 0.0516  52  ASN A CB  
852  C CG  . ASN A 53  ? 0.6590 0.3428 0.4137 -0.0017 -0.0858 0.0465  52  ASN A CG  
853  O OD1 . ASN A 53  ? 0.7385 0.3850 0.4762 0.0068  -0.0964 0.0480  52  ASN A OD1 
854  N ND2 . ASN A 53  ? 0.6051 0.3034 0.3732 -0.0126 -0.0794 0.0409  52  ASN A ND2 
861  N N   . GLY A 54  ? 0.6164 0.3346 0.3300 -0.0140 -0.0705 0.0838  53  GLY A N   
862  C CA  . GLY A 54  ? 0.6424 0.3594 0.3328 -0.0042 -0.0739 0.0893  53  GLY A CA  
863  C C   . GLY A 54  ? 0.5981 0.3503 0.2999 0.0035  -0.0719 0.0779  53  GLY A C   
864  O O   . GLY A 54  ? 0.6054 0.3543 0.2883 0.0152  -0.0804 0.0781  53  GLY A O   
868  N N   . ALA A 55  ? 0.5533 0.3359 0.2829 -0.0027 -0.0626 0.0683  54  ALA A N   
869  C CA  . ALA A 55  ? 0.4965 0.3075 0.2355 0.0034  -0.0613 0.0581  54  ALA A CA  
870  C C   . ALA A 55  ? 0.5322 0.3412 0.2410 0.0030  -0.0559 0.0667  54  ALA A C   
871  O O   . ALA A 55  ? 0.5473 0.3493 0.2411 -0.0078 -0.0437 0.0804  54  ALA A O   
872  C CB  . ALA A 55  ? 0.4319 0.2712 0.2007 -0.0047 -0.0503 0.0497  54  ALA A CB  
878  N N   . LYS A 56  ? 0.5431 0.3577 0.2426 0.0151  -0.0655 0.0587  55  LYS A N   
879  C CA  . LYS A 56  ? 0.5716 0.3836 0.2374 0.0179  -0.0605 0.0638  55  LYS A CA  
880  C C   . LYS A 56  ? 0.5794 0.4155 0.2561 0.0089  -0.0414 0.0625  55  LYS A C   
881  O O   . LYS A 56  ? 0.5955 0.4303 0.2491 0.0051  -0.0269 0.0737  55  LYS A O   
882  C CB  . LYS A 56  ? 0.5698 0.3814 0.2242 0.0329  -0.0784 0.0523  55  LYS A CB  
883  C CG  . LYS A 56  ? 0.6327 0.4373 0.2440 0.0387  -0.0744 0.0554  55  LYS A CG  
884  C CD  . LYS A 56  ? 0.7150 0.5178 0.3179 0.0524  -0.0948 0.0424  55  LYS A CD  
885  C CE  . LYS A 56  ? 0.9005 0.6845 0.4948 0.0610  -0.1119 0.0468  55  LYS A CE  
886  N NZ  . LYS A 56  ? 1.0788 0.8633 0.6693 0.0730  -0.1324 0.0343  55  LYS A NZ  
900  N N   . SER A 57  ? 0.5455 0.4041 0.2578 0.0062  -0.0401 0.0502  56  SER A N   
901  C CA  . SER A 57  ? 0.5590 0.4403 0.2843 0.0001  -0.0244 0.0478  56  SER A CA  
902  C C   . SER A 57  ? 0.4705 0.3692 0.2352 -0.0045 -0.0247 0.0380  56  SER A C   
903  O O   . SER A 57  ? 0.4310 0.3274 0.2119 -0.0006 -0.0364 0.0308  56  SER A O   
904  C CB  . SER A 57  ? 0.6435 0.5296 0.3496 0.0100  -0.0246 0.0397  56  SER A CB  
905  O OG  . SER A 57  ? 0.5920 0.4802 0.3119 0.0172  -0.0414 0.0246  56  SER A OG  
911  N N   . VAL A 58  ? 0.4274 0.3444 0.2070 -0.0118 -0.0109 0.0388  57  VAL A N   
912  C CA  . VAL A 58  ? 0.4084 0.3419 0.2198 -0.0149 -0.0096 0.0302  57  VAL A CA  
913  C C   . VAL A 58  ? 0.4014 0.3513 0.2157 -0.0118 -0.0017 0.0243  57  VAL A C   
914  O O   . VAL A 58  ? 0.4254 0.3848 0.2338 -0.0145 0.0112  0.0310  57  VAL A O   
915  C CB  . VAL A 58  ? 0.4348 0.3713 0.2618 -0.0264 -0.0037 0.0369  57  VAL A CB  
916  C CG1 . VAL A 58  ? 0.4183 0.3690 0.2716 -0.0272 -0.0034 0.0280  57  VAL A CG1 
917  C CG2 . VAL A 58  ? 0.4718 0.3853 0.2904 -0.0288 -0.0119 0.0429  57  VAL A CG2 
927  N N   . VAL A 59  ? 0.3814 0.3347 0.2062 -0.0059 -0.0091 0.0123  58  VAL A N   
928  C CA  . VAL A 59  ? 0.3904 0.3537 0.2178 -0.0020 -0.0039 0.0052  58  VAL A CA  
929  C C   . VAL A 59  ? 0.3719 0.3487 0.2291 -0.0072 0.0004  0.0027  58  VAL A C   
930  O O   . VAL A 59  ? 0.3408 0.3174 0.2161 -0.0086 -0.0063 -0.0017 58  VAL A O   
931  C CB  . VAL A 59  ? 0.3918 0.3452 0.2092 0.0065  -0.0169 -0.0061 58  VAL A CB  
932  C CG1 . VAL A 59  ? 0.4145 0.3730 0.2362 0.0102  -0.0130 -0.0147 58  VAL A CG1 
933  C CG2 . VAL A 59  ? 0.3954 0.3325 0.1744 0.0140  -0.0223 -0.0037 58  VAL A CG2 
943  N N   . LEU A 60  ? 0.3297 0.3195 0.1920 -0.0092 0.0121  0.0064  59  LEU A N   
944  C CA  . LEU A 60  ? 0.3037 0.3050 0.1897 -0.0132 0.0155  0.0055  59  LEU A CA  
945  C C   . LEU A 60  ? 0.3022 0.3064 0.1927 -0.0065 0.0167  -0.0025 59  LEU A C   
946  O O   . LEU A 60  ? 0.3307 0.3359 0.2077 0.0005  0.0216  -0.0044 59  LEU A O   
947  C CB  . LEU A 60  ? 0.2957 0.3104 0.1882 -0.0197 0.0246  0.0149  59  LEU A CB  
948  C CG  . LEU A 60  ? 0.3516 0.3588 0.2390 -0.0281 0.0226  0.0235  59  LEU A CG  
949  C CD1 . LEU A 60  ? 0.4006 0.4221 0.2949 -0.0363 0.0316  0.0340  59  LEU A CD1 
950  C CD2 . LEU A 60  ? 0.3597 0.3576 0.2568 -0.0315 0.0141  0.0204  59  LEU A CD2 
962  N N   . MET A 61  ? 0.3123 0.3158 0.2195 -0.0079 0.0130  -0.0066 60  MET A N   
963  C CA  . MET A 61  ? 0.3018 0.3036 0.2138 -0.0028 0.0135  -0.0128 60  MET A CA  
964  C C   . MET A 61  ? 0.2662 0.2750 0.1951 -0.0055 0.0174  -0.0097 60  MET A C   
965  O O   . MET A 61  ? 0.2584 0.2678 0.1966 -0.0108 0.0159  -0.0069 60  MET A O   
966  C CB  . MET A 61  ? 0.3066 0.2954 0.2203 -0.0018 0.0032  -0.0209 60  MET A CB  
967  C CG  . MET A 61  ? 0.3086 0.2977 0.2387 -0.0076 -0.0024 -0.0201 60  MET A CG  
968  S SD  . MET A 61  ? 0.3803 0.3590 0.3169 -0.0074 -0.0172 -0.0293 60  MET A SD  
969  C CE  . MET A 61  ? 0.3384 0.3275 0.3011 -0.0128 -0.0183 -0.0251 60  MET A CE  
979  N N   . SER A 62  ? 0.2637 0.2756 0.1938 0.0001  0.0218  -0.0107 61  SER A N   
980  C CA  . SER A 62  ? 0.2697 0.2862 0.2119 -0.0005 0.0241  -0.0072 61  SER A CA  
981  C C   . SER A 62  ? 0.2968 0.3068 0.2380 0.0082  0.0253  -0.0110 61  SER A C   
982  O O   . SER A 62  ? 0.2901 0.2937 0.2205 0.0152  0.0251  -0.0170 61  SER A O   
983  C CB  . SER A 62  ? 0.2685 0.3016 0.2155 -0.0032 0.0277  -0.0002 61  SER A CB  
984  O OG  . SER A 62  ? 0.2638 0.2998 0.2189 -0.0022 0.0274  0.0026  61  SER A OG  
990  N N   . HIS A 63  ? 0.2716 0.2803 0.2207 0.0090  0.0259  -0.0077 62  HIS A N   
991  C CA  . HIS A 63  ? 0.2812 0.2846 0.2291 0.0191  0.0272  -0.0093 62  HIS A CA  
992  C C   . HIS A 63  ? 0.2926 0.3166 0.2465 0.0242  0.0310  -0.0039 62  HIS A C   
993  O O   . HIS A 63  ? 0.2831 0.3229 0.2430 0.0175  0.0312  0.0012  62  HIS A O   
994  C CB  . HIS A 63  ? 0.2830 0.2686 0.2346 0.0173  0.0246  -0.0077 62  HIS A CB  
995  C CG  . HIS A 63  ? 0.2693 0.2611 0.2257 0.0133  0.0260  0.0005  62  HIS A CG  
996  N ND1 . HIS A 63  ? 0.2636 0.2600 0.2223 0.0044  0.0264  0.0032  62  HIS A ND1 
997  C CD2 . HIS A 63  ? 0.2761 0.2692 0.2319 0.0188  0.0263  0.0061  62  HIS A CD2 
998  C CE1 . HIS A 63  ? 0.2844 0.2827 0.2410 0.0045  0.0272  0.0093  62  HIS A CE1 
999  N NE2 . HIS A 63  ? 0.2834 0.2798 0.2381 0.0127  0.0264  0.0115  62  HIS A NE2 
1007 N N   . LEU A 64  ? 0.2757 0.2987 0.2295 0.0366  0.0326  -0.0053 63  LEU A N   
1008 C CA  . LEU A 64  ? 0.2947 0.3387 0.2593 0.0435  0.0343  -0.0001 63  LEU A CA  
1009 C C   . LEU A 64  ? 0.3055 0.3336 0.2677 0.0554  0.0317  -0.0007 63  LEU A C   
1010 O O   . LEU A 64  ? 0.3174 0.3291 0.2705 0.0654  0.0328  -0.0074 63  LEU A O   
1011 C CB  . LEU A 64  ? 0.3321 0.4004 0.3015 0.0501  0.0419  -0.0005 63  LEU A CB  
1012 C CG  . LEU A 64  ? 0.3493 0.4474 0.3381 0.0569  0.0438  0.0055  63  LEU A CG  
1013 C CD1 . LEU A 64  ? 0.3354 0.4460 0.3361 0.0432  0.0372  0.0124  63  LEU A CD1 
1014 C CD2 . LEU A 64  ? 0.3964 0.5203 0.3913 0.0637  0.0554  0.0060  63  LEU A CD2 
1026 N N   . GLY A 65  ? 0.3012 0.3298 0.2677 0.0550  0.0272  0.0059  64  GLY A N   
1027 C CA  . GLY A 65  ? 0.3091 0.3209 0.2716 0.0673  0.0240  0.0076  64  GLY A CA  
1028 C C   . GLY A 65  ? 0.3190 0.2951 0.2694 0.0642  0.0230  0.0052  64  GLY A C   
1029 O O   . GLY A 65  ? 0.3032 0.2713 0.2519 0.0510  0.0237  0.0042  64  GLY A O   
1033 N N   . ARG A 66  ? 0.3495 0.3039 0.2936 0.0767  0.0208  0.0045  65  ARG A N   
1034 C CA  . ARG A 66  ? 0.3682 0.2850 0.3032 0.0731  0.0183  0.0033  65  ARG A CA  
1035 C C   . ARG A 66  ? 0.4373 0.3346 0.3641 0.0877  0.0165  -0.0068 65  ARG A C   
1036 O O   . ARG A 66  ? 0.4920 0.3663 0.4122 0.1000  0.0132  -0.0053 65  ARG A O   
1037 C CB  . ARG A 66  ? 0.3811 0.2790 0.3110 0.0726  0.0162  0.0148  65  ARG A CB  
1038 C CG  . ARG A 66  ? 0.3732 0.2823 0.3047 0.0583  0.0189  0.0234  65  ARG A CG  
1039 C CD  . ARG A 66  ? 0.4426 0.3323 0.3632 0.0592  0.0186  0.0359  65  ARG A CD  
1040 N NE  . ARG A 66  ? 0.4075 0.3058 0.3253 0.0474  0.0231  0.0425  65  ARG A NE  
1041 C CZ  . ARG A 66  ? 0.4231 0.3047 0.3281 0.0455  0.0263  0.0544  65  ARG A CZ  
1042 N NH1 . ARG A 66  ? 0.4814 0.3359 0.3757 0.0533  0.0244  0.0620  65  ARG A NH1 
1043 N NH2 . ARG A 66  ? 0.4098 0.2996 0.3096 0.0372  0.0319  0.0591  65  ARG A NH2 
1057 N N   . PRO A 67  ? 0.3827 0.2850 0.3059 0.0881  0.0182  -0.0175 66  PRO A N   
1058 C CA  . PRO A 67  ? 0.4173 0.2966 0.3263 0.1033  0.0161  -0.0295 66  PRO A CA  
1059 C C   . PRO A 67  ? 0.4611 0.2953 0.3608 0.0964  0.0072  -0.0345 66  PRO A C   
1060 O O   . PRO A 67  ? 0.5140 0.3204 0.3983 0.1093  0.0026  -0.0458 66  PRO A O   
1061 C CB  . PRO A 67  ? 0.4101 0.3108 0.3145 0.1042  0.0212  -0.0377 66  PRO A CB  
1062 C CG  . PRO A 67  ? 0.3637 0.2822 0.2788 0.0830  0.0216  -0.0315 66  PRO A CG  
1063 C CD  . PRO A 67  ? 0.3483 0.2768 0.2769 0.0766  0.0219  -0.0187 66  PRO A CD  
1071 N N   . ASP A 68  ? 0.4628 0.2897 0.3723 0.0765  0.0046  -0.0269 67  ASP A N   
1072 C CA  . ASP A 68  ? 0.5118 0.2989 0.4207 0.0666  -0.0032 -0.0268 67  ASP A CA  
1073 C C   . ASP A 68  ? 0.5105 0.2747 0.4108 0.0643  -0.0127 -0.0423 67  ASP A C   
1074 O O   . ASP A 68  ? 0.5472 0.2709 0.4408 0.0643  -0.0221 -0.0474 67  ASP A O   
1075 C CB  . ASP A 68  ? 0.6220 0.3794 0.5228 0.0786  -0.0054 -0.0214 67  ASP A CB  
1076 C CG  . ASP A 68  ? 0.7266 0.4956 0.6341 0.0748  0.0003  -0.0037 67  ASP A CG  
1077 O OD1 . ASP A 68  ? 0.7091 0.4987 0.6277 0.0588  0.0052  0.0041  67  ASP A OD1 
1078 O OD2 . ASP A 68  ? 0.7750 0.5313 0.6744 0.0895  -0.0007 0.0019  67  ASP A OD2 
1083 N N   . GLY A 69  ? 0.4893 0.2763 0.3882 0.0618  -0.0120 -0.0497 68  GLY A N   
1084 C CA  . GLY A 69  ? 0.5183 0.2849 0.4084 0.0572  -0.0236 -0.0636 68  GLY A CA  
1085 C C   . GLY A 69  ? 0.5863 0.3321 0.4480 0.0784  -0.0273 -0.0795 68  GLY A C   
1086 O O   . GLY A 69  ? 0.6513 0.3666 0.4994 0.0771  -0.0407 -0.0930 68  GLY A O   
1090 N N   . VAL A 70  ? 0.5866 0.3483 0.4392 0.0986  -0.0163 -0.0785 69  VAL A N   
1091 C CA  . VAL A 70  ? 0.6566 0.4059 0.4815 0.1227  -0.0152 -0.0929 69  VAL A CA  
1092 C C   . VAL A 70  ? 0.5956 0.3904 0.4195 0.1311  -0.0004 -0.0901 69  VAL A C   
1093 O O   . VAL A 70  ? 0.5381 0.3690 0.3836 0.1263  0.0094  -0.0763 69  VAL A O   
1094 C CB  . VAL A 70  ? 0.7781 0.5042 0.5959 0.1427  -0.0145 -0.0938 69  VAL A CB  
1095 C CG1 . VAL A 70  ? 0.7972 0.5148 0.5859 0.1712  -0.0103 -0.1091 69  VAL A CG1 
1096 C CG2 . VAL A 70  ? 0.8849 0.5615 0.7033 0.1321  -0.0292 -0.0946 69  VAL A CG2 
1106 N N   . PRO A 71  ? 0.6453 0.4389 0.4436 0.1430  0.0016  -0.1020 70  PRO A N   
1107 C CA  . PRO A 71  ? 0.5860 0.4229 0.3840 0.1512  0.0185  -0.0967 70  PRO A CA  
1108 C C   . PRO A 71  ? 0.5383 0.3964 0.3452 0.1715  0.0318  -0.0918 70  PRO A C   
1109 O O   . PRO A 71  ? 0.5978 0.4318 0.3884 0.1931  0.0312  -0.1014 70  PRO A O   
1110 C CB  . PRO A 71  ? 0.6932 0.5143 0.4543 0.1623  0.0171  -0.1114 70  PRO A CB  
1111 C CG  . PRO A 71  ? 0.7646 0.5436 0.5163 0.1489  -0.0046 -0.1217 70  PRO A CG  
1112 C CD  . PRO A 71  ? 0.7487 0.5035 0.5182 0.1445  -0.0127 -0.1192 70  PRO A CD  
1120 N N   . MET A 72  ? 0.5035 0.4064 0.3370 0.1651  0.0426  -0.0773 71  MET A N   
1121 C CA  . MET A 72  ? 0.5449 0.4776 0.3951 0.1823  0.0541  -0.0707 71  MET A CA  
1122 C C   . MET A 72  ? 0.5817 0.5657 0.4480 0.1781  0.0690  -0.0607 71  MET A C   
1123 O O   . MET A 72  ? 0.5535 0.5703 0.4498 0.1689  0.0713  -0.0478 71  MET A O   
1124 C CB  . MET A 72  ? 0.5422 0.4724 0.4155 0.1760  0.0464  -0.0609 71  MET A CB  
1125 C CG  . MET A 72  ? 0.6586 0.5367 0.5181 0.1786  0.0328  -0.0676 71  MET A CG  
1126 S SD  . MET A 72  ? 0.7114 0.5849 0.5921 0.1728  0.0258  -0.0530 71  MET A SD  
1127 C CE  . MET A 72  ? 0.7386 0.5460 0.6004 0.1672  0.0110  -0.0600 71  MET A CE  
1137 N N   . PRO A 73  ? 0.6676 0.6570 0.5126 0.1837  0.0784  -0.0658 72  PRO A N   
1138 C CA  . PRO A 73  ? 0.6728 0.7087 0.5330 0.1774  0.0936  -0.0540 72  PRO A CA  
1139 C C   . PRO A 73  ? 0.7090 0.7881 0.5983 0.1913  0.1073  -0.0455 72  PRO A C   
1140 O O   . PRO A 73  ? 0.6966 0.8172 0.6131 0.1795  0.1155  -0.0322 72  PRO A O   
1141 C CB  . PRO A 73  ? 0.6884 0.7128 0.5122 0.1851  0.1008  -0.0619 72  PRO A CB  
1142 C CG  . PRO A 73  ? 0.7169 0.7012 0.5151 0.2019  0.0924  -0.0768 72  PRO A CG  
1143 C CD  . PRO A 73  ? 0.7292 0.6824 0.5330 0.1989  0.0764  -0.0823 72  PRO A CD  
1151 N N   . ASP A 74  ? 0.7105 0.7793 0.5978 0.2136  0.1073  -0.0521 73  ASP A N   
1152 C CA  . ASP A 74  ? 0.8621 0.9703 0.7833 0.2245  0.1148  -0.0434 73  ASP A CA  
1153 C C   . ASP A 74  ? 0.9312 1.0738 0.8913 0.2113  0.1112  -0.0302 73  ASP A C   
1154 O O   . ASP A 74  ? 0.9425 1.1333 0.9352 0.2068  0.1202  -0.0187 73  ASP A O   
1155 C CB  . ASP A 74  ? 0.9884 1.0681 0.9003 0.2468  0.1080  -0.0526 73  ASP A CB  
1156 C CG  . ASP A 74  ? 1.0623 1.0849 0.9491 0.2456  0.0907  -0.0630 73  ASP A CG  
1157 O OD1 . ASP A 74  ? 1.0716 1.0635 0.9309 0.2354  0.0856  -0.0710 73  ASP A OD1 
1158 O OD2 . ASP A 74  ? 1.0856 1.0929 0.9811 0.2539  0.0813  -0.0623 73  ASP A OD2 
1163 N N   . LYS A 75  ? 0.9558 1.0691 0.9147 0.1966  0.0933  -0.0299 74  LYS A N   
1164 C CA  . LYS A 75  ? 0.8782 1.0142 0.8687 0.1821  0.0844  -0.0179 74  LYS A CA  
1165 C C   . LYS A 75  ? 0.5317 0.6562 0.5199 0.1532  0.0749  -0.0132 74  LYS A C   
1166 O O   . LYS A 75  ? 0.4607 0.6076 0.4723 0.1401  0.0691  -0.0036 74  LYS A O   
1167 C CB  . LYS A 75  ? 1.2051 1.3214 1.1986 0.1955  0.0725  -0.0187 74  LYS A CB  
1168 C CG  . LYS A 75  ? 1.5416 1.6020 1.5017 0.2059  0.0661  -0.0305 74  LYS A CG  
1169 C CD  . LYS A 75  ? 1.8307 1.8725 1.7942 0.2210  0.0560  -0.0289 74  LYS A CD  
1170 C CE  . LYS A 75  ? 2.0860 2.0897 2.0241 0.2466  0.0566  -0.0418 74  LYS A CE  
1171 N NZ  . LYS A 75  ? 2.2280 2.2179 2.1715 0.2656  0.0480  -0.0389 74  LYS A NZ  
1185 N N   . TYR A 76  ? 0.4415 0.5326 0.4026 0.1440  0.0722  -0.0203 75  TYR A N   
1186 C CA  . TYR A 76  ? 0.3761 0.4551 0.3355 0.1197  0.0635  -0.0167 75  TYR A CA  
1187 C C   . TYR A 76  ? 0.3550 0.4362 0.3019 0.1083  0.0688  -0.0179 75  TYR A C   
1188 O O   . TYR A 76  ? 0.3812 0.4429 0.3196 0.0927  0.0610  -0.0188 75  TYR A O   
1189 C CB  . TYR A 76  ? 0.4247 0.4600 0.3687 0.1166  0.0516  -0.0221 75  TYR A CB  
1190 C CG  . TYR A 76  ? 0.4683 0.4941 0.4202 0.1243  0.0447  -0.0183 75  TYR A CG  
1191 C CD1 . TYR A 76  ? 0.4950 0.5368 0.4636 0.1148  0.0395  -0.0080 75  TYR A CD1 
1192 C CD2 . TYR A 76  ? 0.5420 0.5382 0.4807 0.1418  0.0418  -0.0251 75  TYR A CD2 
1193 C CE1 . TYR A 76  ? 0.5573 0.5881 0.5284 0.1229  0.0322  -0.0034 75  TYR A CE1 
1194 C CE2 . TYR A 76  ? 0.6383 0.6220 0.5815 0.1494  0.0348  -0.0199 75  TYR A CE2 
1195 C CZ  . TYR A 76  ? 0.6475 0.6495 0.6063 0.1400  0.0302  -0.0085 75  TYR A CZ  
1196 O OH  . TYR A 76  ? 0.7221 0.7108 0.6813 0.1484  0.0225  -0.0022 75  TYR A OH  
1206 N N   . SER A 77  ? 0.3747 0.4798 0.3203 0.1162  0.0825  -0.0167 76  SER A N   
1207 C CA  . SER A 77  ? 0.3980 0.5039 0.3288 0.1057  0.0877  -0.0155 76  SER A CA  
1208 C C   . SER A 77  ? 0.3619 0.4878 0.3134 0.0836  0.0852  -0.0037 76  SER A C   
1209 O O   . SER A 77  ? 0.3470 0.5009 0.3273 0.0795  0.0854  0.0048  76  SER A O   
1210 C CB  . SER A 77  ? 0.4743 0.6000 0.3951 0.1210  0.1057  -0.0152 76  SER A CB  
1211 O OG  . SER A 77  ? 0.4488 0.5724 0.3517 0.1107  0.1103  -0.0120 76  SER A OG  
1217 N N   . LEU A 78  ? 0.3587 0.4684 0.2950 0.0699  0.0807  -0.0039 77  LEU A N   
1218 C CA  . LEU A 78  ? 0.3517 0.4755 0.3019 0.0507  0.0791  0.0063  77  LEU A CA  
1219 C C   . LEU A 78  ? 0.3320 0.4816 0.2851 0.0483  0.0934  0.0159  77  LEU A C   
1220 O O   . LEU A 78  ? 0.3630 0.5206 0.3257 0.0317  0.0920  0.0249  77  LEU A O   
1221 C CB  . LEU A 78  ? 0.3622 0.4578 0.2964 0.0389  0.0682  0.0027  77  LEU A CB  
1222 C CG  . LEU A 78  ? 0.3554 0.4340 0.2967 0.0336  0.0557  -0.0008 77  LEU A CG  
1223 C CD1 . LEU A 78  ? 0.3645 0.4178 0.2914 0.0260  0.0470  -0.0057 77  LEU A CD1 
1224 C CD2 . LEU A 78  ? 0.3646 0.4594 0.3279 0.0234  0.0520  0.0072  77  LEU A CD2 
1236 N N   . GLU A 79  ? 0.3426 0.5048 0.2876 0.0647  0.1080  0.0149  78  GLU A N   
1237 C CA  . GLU A 79  ? 0.3819 0.5692 0.3285 0.0618  0.1246  0.0263  78  GLU A CA  
1238 C C   . GLU A 79  ? 0.3590 0.5826 0.3467 0.0461  0.1268  0.0406  78  GLU A C   
1239 O O   . GLU A 79  ? 0.3422 0.5742 0.3323 0.0313  0.1326  0.0522  78  GLU A O   
1240 C CB  . GLU A 79  ? 0.5433 0.7412 0.4764 0.0846  0.1420  0.0229  78  GLU A CB  
1241 C CG  . GLU A 79  ? 0.7673 0.9787 0.6993 0.0783  0.1559  0.0338  78  GLU A CG  
1242 C CD  . GLU A 79  ? 1.0436 1.2447 0.9480 0.0977  0.1666  0.0265  78  GLU A CD  
1243 O OE1 . GLU A 79  ? 1.1308 1.3205 1.0261 0.1167  0.1637  0.0139  78  GLU A OE1 
1244 O OE2 . GLU A 79  ? 1.1479 1.3500 1.0379 0.0943  0.1774  0.0334  78  GLU A OE2 
1251 N N   . PRO A 80  ? 0.3963 0.6403 0.4161 0.0480  0.1212  0.0411  79  PRO A N   
1252 C CA  . PRO A 80  ? 0.3809 0.6583 0.4408 0.0312  0.1192  0.0537  79  PRO A CA  
1253 C C   . PRO A 80  ? 0.3261 0.5833 0.3840 0.0084  0.1039  0.0564  79  PRO A C   
1254 O O   . PRO A 80  ? 0.3338 0.6097 0.4145 -0.0091 0.1038  0.0678  79  PRO A O   
1255 C CB  . PRO A 80  ? 0.4371 0.7323 0.5238 0.0420  0.1116  0.0503  79  PRO A CB  
1256 C CG  . PRO A 80  ? 0.5111 0.7934 0.5757 0.0679  0.1190  0.0394  79  PRO A CG  
1257 C CD  . PRO A 80  ? 0.4514 0.6910 0.4728 0.0673  0.1171  0.0310  79  PRO A CD  
1265 N N   . VAL A 81  ? 0.2900 0.5094 0.3228 0.0084  0.0910  0.0463  80  VAL A N   
1266 C CA  . VAL A 81  ? 0.3102 0.5079 0.3367 -0.0094 0.0782  0.0475  80  VAL A CA  
1267 C C   . VAL A 81  ? 0.3243 0.5141 0.3351 -0.0190 0.0854  0.0547  80  VAL A C   
1268 O O   . VAL A 81  ? 0.3392 0.5262 0.3574 -0.0363 0.0797  0.0621  80  VAL A O   
1269 C CB  . VAL A 81  ? 0.3504 0.5141 0.3560 -0.0048 0.0662  0.0359  80  VAL A CB  
1270 C CG1 . VAL A 81  ? 0.3658 0.5065 0.3610 -0.0195 0.0560  0.0363  80  VAL A CG1 
1271 C CG2 . VAL A 81  ? 0.3912 0.5595 0.4111 0.0016  0.0579  0.0320  80  VAL A CG2 
1281 N N   . ALA A 82  ? 0.3530 0.5341 0.3377 -0.0073 0.0964  0.0521  81  ALA A N   
1282 C CA  . ALA A 82  ? 0.3918 0.5661 0.3579 -0.0142 0.1047  0.0610  81  ALA A CA  
1283 C C   . ALA A 82  ? 0.4004 0.6056 0.3939 -0.0281 0.1153  0.0779  81  ALA A C   
1284 O O   . ALA A 82  ? 0.4340 0.6291 0.4247 -0.0444 0.1131  0.0876  81  ALA A O   
1285 C CB  . ALA A 82  ? 0.4650 0.6306 0.3982 0.0038  0.1164  0.0559  81  ALA A CB  
1291 N N   . VAL A 83  ? 0.3947 0.6380 0.4170 -0.0222 0.1267  0.0825  82  VAL A N   
1292 C CA  . VAL A 83  ? 0.4067 0.6759 0.4588 -0.0365 0.1351  0.0973  82  VAL A CA  
1293 C C   . VAL A 83  ? 0.3625 0.6372 0.4440 -0.0593 0.1189  0.1035  82  VAL A C   
1294 O O   . VAL A 83  ? 0.3771 0.6478 0.4676 -0.0776 0.1181  0.1142  82  VAL A O   
1295 C CB  . VAL A 83  ? 0.5239 0.8281 0.6020 -0.0234 0.1485  0.0980  82  VAL A CB  
1296 C CG1 . VAL A 83  ? 0.4708 0.7645 0.5173 0.0029  0.1590  0.0865  82  VAL A CG1 
1297 C CG2 . VAL A 83  ? 0.6302 0.9652 0.7520 -0.0255 0.1383  0.0975  82  VAL A CG2 
1307 N N   . GLU A 84  ? 0.3529 0.6219 0.4430 -0.0568 0.1014  0.0925  83  GLU A N   
1308 C CA  . GLU A 84  ? 0.3875 0.6497 0.4959 -0.0756 0.0818  0.0935  83  GLU A CA  
1309 C C   . GLU A 84  ? 0.4073 0.6277 0.4868 -0.0872 0.0726  0.0928  83  GLU A C   
1310 O O   . GLU A 84  ? 0.4099 0.6249 0.5016 -0.1069 0.0639  0.1003  83  GLU A O   
1311 C CB  . GLU A 84  ? 0.3824 0.6416 0.4967 -0.0667 0.0658  0.0811  83  GLU A CB  
1312 C CG  . GLU A 84  ? 0.4713 0.7261 0.6031 -0.0831 0.0446  0.0809  83  GLU A CG  
1313 C CD  . GLU A 84  ? 0.5692 0.8661 0.7483 -0.0956 0.0429  0.0919  83  GLU A CD  
1314 O OE1 . GLU A 84  ? 0.6065 0.9423 0.8097 -0.0869 0.0586  0.0982  83  GLU A OE1 
1315 O OE2 . GLU A 84  ? 0.5849 0.8763 0.7781 -0.1138 0.0253  0.0937  83  GLU A OE2 
1322 N N   . LEU A 85  ? 0.3770 0.5666 0.4195 -0.0752 0.0727  0.0834  84  LEU A N   
1323 C CA  . LEU A 85  ? 0.4005 0.5523 0.4175 -0.0832 0.0632  0.0822  84  LEU A CA  
1324 C C   . LEU A 85  ? 0.4430 0.5918 0.4554 -0.0962 0.0721  0.0975  84  LEU A C   
1325 O O   . LEU A 85  ? 0.4527 0.5770 0.4592 -0.1099 0.0617  0.1012  84  LEU A O   
1326 C CB  . LEU A 85  ? 0.4155 0.5418 0.4002 -0.0673 0.0618  0.0702  84  LEU A CB  
1327 C CG  . LEU A 85  ? 0.4619 0.5517 0.4216 -0.0709 0.0517  0.0673  84  LEU A CG  
1328 C CD1 . LEU A 85  ? 0.5008 0.5759 0.4682 -0.0796 0.0358  0.0629  84  LEU A CD1 
1329 C CD2 . LEU A 85  ? 0.4502 0.5233 0.3856 -0.0552 0.0507  0.0561  84  LEU A CD2 
1341 N N   . LYS A 86  ? 0.4651 0.6369 0.4783 -0.0914 0.0920  0.1071  85  LYS A N   
1342 C CA  . LYS A 86  ? 0.5566 0.7258 0.5640 -0.1036 0.1032  0.1242  85  LYS A CA  
1343 C C   . LYS A 86  ? 0.5359 0.7089 0.5758 -0.1264 0.0943  0.1334  85  LYS A C   
1344 O O   . LYS A 86  ? 0.5554 0.6998 0.5834 -0.1395 0.0886  0.1407  85  LYS A O   
1345 C CB  . LYS A 86  ? 0.6517 0.8419 0.6582 -0.0901 0.1252  0.1277  85  LYS A CB  
1346 C CG  . LYS A 86  ? 0.8331 1.0030 0.7939 -0.0708 0.1331  0.1212  85  LYS A CG  
1347 C CD  . LYS A 86  ? 1.0329 1.2151 0.9855 -0.0611 0.1546  0.1260  85  LYS A CD  
1348 C CE  . LYS A 86  ? 1.1119 1.3209 1.0756 -0.0423 0.1629  0.1158  85  LYS A CE  
1349 N NZ  . LYS A 86  ? 1.1383 1.3267 1.0678 -0.0231 0.1567  0.1000  85  LYS A NZ  
1363 N N   . SER A 87  ? 0.4741 0.6806 0.5550 -0.1307 0.0915  0.1328  86  SER A N   
1364 C CA  . SER A 87  ? 0.5279 0.7388 0.6413 -0.1522 0.0812  0.1403  86  SER A CA  
1365 C C   . SER A 87  ? 0.5136 0.6925 0.6198 -0.1657 0.0563  0.1344  86  SER A C   
1366 O O   . SER A 87  ? 0.5278 0.6888 0.6423 -0.1834 0.0460  0.1399  86  SER A O   
1367 C CB  . SER A 87  ? 0.6484 0.9049 0.8075 -0.1515 0.0829  0.1405  86  SER A CB  
1368 O OG  . SER A 87  ? 0.7785 1.0468 0.9441 -0.1419 0.0715  0.1289  86  SER A OG  
1374 N N   . LEU A 88  ? 0.4839 0.6475 0.5704 -0.1532 0.0458  0.1194  87  LEU A N   
1375 C CA  . LEU A 88  ? 0.5239 0.6493 0.5954 -0.1580 0.0233  0.1085  87  LEU A CA  
1376 C C   . LEU A 88  ? 0.6196 0.7012 0.6558 -0.1600 0.0214  0.1103  87  LEU A C   
1377 O O   . LEU A 88  ? 0.6476 0.6966 0.6756 -0.1698 0.0046  0.1072  87  LEU A O   
1378 C CB  . LEU A 88  ? 0.4918 0.6130 0.5514 -0.1393 0.0158  0.0910  87  LEU A CB  
1379 C CG  . LEU A 88  ? 0.5699 0.7271 0.6596 -0.1349 0.0132  0.0877  87  LEU A CG  
1380 C CD1 . LEU A 88  ? 0.5884 0.7360 0.6591 -0.1149 0.0095  0.0728  87  LEU A CD1 
1381 C CD2 . LEU A 88  ? 0.6248 0.7859 0.7399 -0.1526 -0.0060 0.0890  87  LEU A CD2 
1393 N N   . LEU A 89  ? 0.5972 0.6750 0.6098 -0.1489 0.0368  0.1143  88  LEU A N   
1394 C CA  . LEU A 89  ? 0.6081 0.6463 0.5864 -0.1480 0.0347  0.1170  88  LEU A CA  
1395 C C   . LEU A 89  ? 0.6421 0.6743 0.6208 -0.1652 0.0430  0.1374  88  LEU A C   
1396 O O   . LEU A 89  ? 0.7444 0.7376 0.6988 -0.1694 0.0358  0.1413  88  LEU A O   
1397 C CB  . LEU A 89  ? 0.6261 0.6600 0.5749 -0.1268 0.0439  0.1106  88  LEU A CB  
1398 C CG  . LEU A 89  ? 0.5984 0.6209 0.5342 -0.1096 0.0344  0.0918  88  LEU A CG  
1399 C CD1 . LEU A 89  ? 0.5387 0.5555 0.4473 -0.0931 0.0421  0.0885  88  LEU A CD1 
1400 C CD2 . LEU A 89  ? 0.6468 0.6350 0.5724 -0.1123 0.0171  0.0847  88  LEU A CD2 
1412 N N   . GLY A 90  ? 0.5243 0.7175 0.6558 -0.0772 0.0963  0.0807  89  GLY A N   
1413 C CA  . GLY A 90  ? 0.6331 0.8178 0.7616 -0.0853 0.1112  0.0963  89  GLY A CA  
1414 C C   . GLY A 90  ? 0.6662 0.8223 0.7514 -0.0735 0.1168  0.1046  89  GLY A C   
1415 O O   . GLY A 90  ? 0.6822 0.8182 0.7557 -0.0798 0.1246  0.1176  89  GLY A O   
1419 N N   . LYS A 91  ? 0.6352 0.7871 0.6949 -0.0568 0.1119  0.0974  90  LYS A N   
1420 C CA  . LYS A 91  ? 0.6161 0.7404 0.6319 -0.0450 0.1129  0.1024  90  LYS A CA  
1421 C C   . LYS A 91  ? 0.5443 0.6793 0.5419 -0.0292 0.1189  0.0972  90  LYS A C   
1422 O O   . LYS A 91  ? 0.4824 0.6400 0.4996 -0.0253 0.1163  0.0875  90  LYS A O   
1423 C CB  . LYS A 91  ? 0.7169 0.8124 0.7183 -0.0424 0.0929  0.0959  90  LYS A CB  
1424 C CG  . LYS A 91  ? 0.8602 0.9405 0.8779 -0.0560 0.0878  0.1007  90  LYS A CG  
1425 C CD  . LYS A 91  ? 0.9406 0.9898 0.9407 -0.0509 0.0717  0.0988  90  LYS A CD  
1426 C CE  . LYS A 91  ? 0.9822 1.0123 0.9962 -0.0628 0.0697  0.1056  90  LYS A CE  
1427 N NZ  . LYS A 91  ? 0.9893 0.9904 0.9912 -0.0563 0.0542  0.1046  90  LYS A NZ  
1441 N N   . ASP A 92  ? 0.5901 0.7063 0.5474 -0.0194 0.1267  0.1036  91  ASP A N   
1442 C CA  A ASP A 92  ? 0.5956 0.7173 0.5324 -0.0038 0.1329  0.0973  91  ASP A CA  
1443 C CA  B ASP A 92  ? 0.5980 0.7175 0.5318 -0.0034 0.1329  0.0977  91  ASP A CA  
1444 C C   . ASP A 92  ? 0.5329 0.6384 0.4541 0.0052  0.1127  0.0830  91  ASP A C   
1445 O O   . ASP A 92  ? 0.4806 0.5662 0.3960 0.0019  0.0957  0.0804  91  ASP A O   
1446 C CB  A ASP A 92  ? 0.6539 0.7610 0.5498 0.0040  0.1503  0.1079  91  ASP A CB  
1447 C CB  B ASP A 92  ? 0.6578 0.7570 0.5458 0.0044  0.1468  0.1078  91  ASP A CB  
1448 C CG  A ASP A 92  ? 0.6796 0.8153 0.5961 0.0008  0.1773  0.1187  91  ASP A CG  
1449 C CG  B ASP A 92  ? 0.6498 0.7475 0.5088 0.0219  0.1536  0.0997  91  ASP A CG  
1450 O OD1 A ASP A 92  ? 0.6338 0.7949 0.5965 -0.0131 0.1802  0.1223  91  ASP A OD1 
1451 O OD1 B ASP A 92  ? 0.6004 0.7249 0.4851 0.0265  0.1611  0.0936  91  ASP A OD1 
1452 O OD2 A ASP A 92  ? 0.7266 0.8605 0.6144 0.0121  0.1958  0.1227  91  ASP A OD2 
1453 O OD2 B ASP A 92  ? 0.6602 0.7289 0.4702 0.0314  0.1509  0.0991  91  ASP A OD2 
1462 N N   . VAL A 93  ? 0.4888 0.6045 0.4076 0.0164  0.1153  0.0739  92  VAL A N   
1463 C CA  . VAL A 93  ? 0.4466 0.5492 0.3549 0.0239  0.0986  0.0605  92  VAL A CA  
1464 C C   . VAL A 93  ? 0.5087 0.5973 0.3794 0.0390  0.1050  0.0559  92  VAL A C   
1465 O O   . VAL A 93  ? 0.6084 0.7127 0.4809 0.0470  0.1222  0.0570  92  VAL A O   
1466 C CB  . VAL A 93  ? 0.4172 0.5424 0.3618 0.0221  0.0928  0.0523  92  VAL A CB  
1467 C CG1 . VAL A 93  ? 0.4458 0.5550 0.3781 0.0292  0.0783  0.0403  92  VAL A CG1 
1468 C CG2 . VAL A 93  ? 0.4389 0.5748 0.4161 0.0073  0.0859  0.0546  92  VAL A CG2 
1478 N N   . LEU A 94  ? 0.4822 0.5416 0.3199 0.0433  0.0908  0.0501  93  LEU A N   
1479 C CA  . LEU A 94  ? 0.5148 0.5551 0.3131 0.0570  0.0929  0.0425  93  LEU A CA  
1480 C C   . LEU A 94  ? 0.5102 0.5527 0.3220 0.0621  0.0845  0.0292  93  LEU A C   
1481 O O   . LEU A 94  ? 0.5072 0.5426 0.3305 0.0566  0.0661  0.0229  93  LEU A O   
1482 C CB  . LEU A 94  ? 0.5425 0.5500 0.2996 0.0583  0.0777  0.0411  93  LEU A CB  
1483 C CG  . LEU A 94  ? 0.6661 0.6494 0.3787 0.0715  0.0764  0.0302  93  LEU A CG  
1484 C CD1 . LEU A 94  ? 0.7406 0.7267 0.4280 0.0821  0.1029  0.0349  93  LEU A CD1 
1485 C CD2 . LEU A 94  ? 0.7652 0.7176 0.4402 0.0714  0.0556  0.0273  93  LEU A CD2 
1497 N N   . PHE A 95  ? 0.4614 0.5110 0.2696 0.0737  0.0987  0.0254  94  PHE A N   
1498 C CA  . PHE A 95  ? 0.4310 0.4776 0.2469 0.0805  0.0925  0.0140  94  PHE A CA  
1499 C C   . PHE A 95  ? 0.4904 0.5030 0.2615 0.0913  0.0883  0.0030  94  PHE A C   
1500 O O   . PHE A 95  ? 0.5444 0.5473 0.2827 0.1018  0.1027  0.0032  94  PHE A O   
1501 C CB  . PHE A 95  ? 0.4117 0.4864 0.2545 0.0881  0.1089  0.0165  94  PHE A CB  
1502 C CG  . PHE A 95  ? 0.4447 0.5146 0.2952 0.0959  0.1030  0.0071  94  PHE A CG  
1503 C CD1 . PHE A 95  ? 0.4367 0.5087 0.3104 0.0871  0.0870  0.0044  94  PHE A CD1 
1504 C CD2 . PHE A 95  ? 0.5077 0.5683 0.3404 0.1126  0.1143  0.0014  94  PHE A CD2 
1505 C CE1 . PHE A 95  ? 0.4442 0.5092 0.3233 0.0937  0.0825  -0.0023 94  PHE A CE1 
1506 C CE2 . PHE A 95  ? 0.5602 0.6125 0.3995 0.1200  0.1088  -0.0060 94  PHE A CE2 
1507 C CZ  . PHE A 95  ? 0.5089 0.5631 0.3711 0.1099  0.0927  -0.0071 94  PHE A CZ  
1517 N N   . LEU A 96  ? 0.4624 0.4565 0.2320 0.0884  0.0693  -0.0071 95  LEU A N   
1518 C CA  . LEU A 96  ? 0.5159 0.4760 0.2470 0.0962  0.0616  -0.0198 95  LEU A CA  
1519 C C   . LEU A 96  ? 0.5161 0.4728 0.2581 0.1043  0.0647  -0.0282 95  LEU A C   
1520 O O   . LEU A 96  ? 0.5272 0.5012 0.3063 0.0994  0.0616  -0.0258 95  LEU A O   
1521 C CB  . LEU A 96  ? 0.5522 0.4925 0.2756 0.0861  0.0366  -0.0254 95  LEU A CB  
1522 C CG  . LEU A 96  ? 0.5976 0.5377 0.3113 0.0787  0.0291  -0.0168 95  LEU A CG  
1523 C CD1 . LEU A 96  ? 0.5860 0.5112 0.3022 0.0701  0.0027  -0.0233 95  LEU A CD1 
1524 C CD2 . LEU A 96  ? 0.7442 0.6679 0.4087 0.0882  0.0397  -0.0147 95  LEU A CD2 
1536 N N   . LYS A 97  ? 0.5793 0.5099 0.2855 0.1173  0.0701  -0.0382 96  LYS A N   
1537 C CA  . LYS A 97  ? 0.6249 0.5488 0.3382 0.1281  0.0761  -0.0451 96  LYS A CA  
1538 C C   . LYS A 97  ? 0.6207 0.5180 0.3341 0.1218  0.0565  -0.0560 96  LYS A C   
1539 O O   . LYS A 97  ? 0.6769 0.5586 0.3889 0.1307  0.0598  -0.0628 96  LYS A O   
1540 C CB  . LYS A 97  ? 0.7502 0.6573 0.4261 0.1468  0.0940  -0.0513 96  LYS A CB  
1541 C CG  . LYS A 97  ? 0.9145 0.8499 0.5946 0.1525  0.1165  -0.0394 96  LYS A CG  
1542 C CD  . LYS A 97  ? 0.9844 0.9618 0.7152 0.1538  0.1280  -0.0284 96  LYS A CD  
1543 C CE  . LYS A 97  ? 1.0325 1.0375 0.7789 0.1563  0.1478  -0.0177 96  LYS A CE  
1544 N NZ  . LYS A 97  ? 1.0431 1.0366 0.7780 0.1710  0.1602  -0.0235 96  LYS A NZ  
1558 N N   . ASP A 98  ? 0.5813 0.4738 0.2997 0.1067  0.0369  -0.0569 97  ASP A N   
1559 C CA  . ASP A 98  ? 0.5395 0.4150 0.2701 0.0973  0.0192  -0.0647 97  ASP A CA  
1560 C C   . ASP A 98  ? 0.4988 0.3950 0.2613 0.0813  0.0065  -0.0574 97  ASP A C   
1561 O O   . ASP A 98  ? 0.5289 0.4475 0.2997 0.0784  0.0108  -0.0476 97  ASP A O   
1562 C CB  . ASP A 98  ? 0.6483 0.4834 0.3388 0.0984  0.0058  -0.0799 97  ASP A CB  
1563 C CG  . ASP A 98  ? 0.7471 0.5586 0.4476 0.0936  -0.0050 -0.0898 97  ASP A CG  
1564 O OD1 . ASP A 98  ? 0.7130 0.5401 0.4530 0.0844  -0.0078 -0.0838 97  ASP A OD1 
1565 O OD2 . ASP A 98  ? 0.8221 0.5972 0.4889 0.0987  -0.0101 -0.1038 97  ASP A OD2 
1570 N N   . CYS A 99  ? 0.4991 0.3876 0.2816 0.0709  -0.0075 -0.0619 98  CYS A N   
1571 C CA  . CYS A 99  ? 0.4912 0.3981 0.3050 0.0569  -0.0187 -0.0564 98  CYS A CA  
1572 C C   . CYS A 99  ? 0.5054 0.3945 0.3159 0.0471  -0.0406 -0.0648 98  CYS A C   
1573 O O   . CYS A 99  ? 0.5094 0.4137 0.3449 0.0372  -0.0505 -0.0606 98  CYS A O   
1574 C CB  . CYS A 99  ? 0.4745 0.3988 0.3263 0.0520  -0.0133 -0.0509 98  CYS A CB  
1575 S SG  . CYS A 99  ? 0.4752 0.3736 0.3298 0.0514  -0.0159 -0.0588 98  CYS A SG  
1581 N N   . VAL A 100 ? 0.5135 0.3712 0.2954 0.0497  -0.0490 -0.0772 99  VAL A N   
1582 C CA  . VAL A 100 ? 0.5654 0.4062 0.3449 0.0396  -0.0727 -0.0867 99  VAL A CA  
1583 C C   . VAL A 100 ? 0.6161 0.4238 0.3431 0.0473  -0.0800 -0.0988 99  VAL A C   
1584 O O   . VAL A 100 ? 0.6197 0.4168 0.3143 0.0609  -0.0642 -0.1001 99  VAL A O   
1585 C CB  . VAL A 100 ? 0.6061 0.4393 0.4162 0.0288  -0.0794 -0.0919 99  VAL A CB  
1586 C CG1 . VAL A 100 ? 0.5622 0.4269 0.4212 0.0197  -0.0752 -0.0809 99  VAL A CG1 
1587 C CG2 . VAL A 100 ? 0.6454 0.4564 0.4418 0.0368  -0.0665 -0.0969 99  VAL A CG2 
1597 N N   . GLY A 101 ? 0.6767 0.4685 0.3959 0.0387  -0.1044 -0.1083 100 GLY A N   
1598 C CA  . GLY A 101 ? 0.7431 0.4998 0.4096 0.0444  -0.1156 -0.1223 100 GLY A CA  
1599 C C   . GLY A 101 ? 0.7558 0.5145 0.3897 0.0484  -0.1246 -0.1183 100 GLY A C   
1600 O O   . GLY A 101 ? 0.7144 0.5009 0.3667 0.0480  -0.1194 -0.1036 100 GLY A O   
1604 N N   . PRO A 102 ? 0.8179 0.5437 0.3994 0.0527  -0.1386 -0.1313 101 PRO A N   
1605 C CA  . PRO A 102 ? 0.8482 0.5745 0.3996 0.0551  -0.1509 -0.1261 101 PRO A CA  
1606 C C   . PRO A 102 ? 0.8295 0.5672 0.3558 0.0674  -0.1276 -0.1119 101 PRO A C   
1607 O O   . PRO A 102 ? 0.8241 0.5742 0.3478 0.0663  -0.1348 -0.1003 101 PRO A O   
1608 C CB  . PRO A 102 ? 0.9846 0.6816 0.5015 0.0559  -0.1612 -0.1389 101 PRO A CB  
1609 C CG  . PRO A 102 ? 1.0339 0.7111 0.5452 0.0605  -0.1460 -0.1499 101 PRO A CG  
1610 C CD  . PRO A 102 ? 0.8897 0.5809 0.4472 0.0539  -0.1424 -0.1483 101 PRO A CD  
1618 N N   . GLU A 103 ? 0.8186 0.5541 0.3306 0.0790  -0.0991 -0.1110 102 GLU A N   
1619 C CA  . GLU A 103 ? 0.8542 0.6048 0.3497 0.0887  -0.0752 -0.0960 102 GLU A CA  
1620 C C   . GLU A 103 ? 0.7071 0.4964 0.2552 0.0817  -0.0676 -0.0786 102 GLU A C   
1621 O O   . GLU A 103 ? 0.7029 0.5043 0.2447 0.0822  -0.0634 -0.0649 102 GLU A O   
1622 C CB  . GLU A 103 ? 1.0740 0.8207 0.5560 0.1018  -0.0455 -0.0979 102 GLU A CB  
1623 C CG  . GLU A 103 ? 1.3809 1.0972 0.8257 0.1077  -0.0466 -0.1107 102 GLU A CG  
1624 C CD  . GLU A 103 ? 1.5721 1.2655 1.0254 0.1030  -0.0612 -0.1279 102 GLU A CD  
1625 O OE1 . GLU A 103 ? 1.5620 1.2636 1.0516 0.0948  -0.0698 -0.1294 102 GLU A OE1 
1626 O OE2 . GLU A 103 ? 1.7006 1.3668 1.1244 0.1071  -0.0634 -0.1398 102 GLU A OE2 
1633 N N   . VAL A 104 ? 0.6253 0.4326 0.2248 0.0748  -0.0648 -0.0786 103 VAL A N   
1634 C CA  . VAL A 104 ? 0.5688 0.4105 0.2183 0.0669  -0.0604 -0.0644 103 VAL A CA  
1635 C C   . VAL A 104 ? 0.5857 0.4316 0.2457 0.0579  -0.0838 -0.0602 103 VAL A C   
1636 O O   . VAL A 104 ? 0.5497 0.4134 0.2226 0.0562  -0.0798 -0.0467 103 VAL A O   
1637 C CB  . VAL A 104 ? 0.5444 0.4002 0.2408 0.0614  -0.0555 -0.0664 103 VAL A CB  
1638 C CG1 . VAL A 104 ? 0.4922 0.3788 0.2366 0.0520  -0.0557 -0.0550 103 VAL A CG1 
1639 C CG2 . VAL A 104 ? 0.5654 0.4233 0.2568 0.0724  -0.0310 -0.0663 103 VAL A CG2 
1649 N N   . GLU A 105 ? 0.6500 0.4794 0.3068 0.0520  -0.1091 -0.0717 104 GLU A N   
1650 C CA  . GLU A 105 ? 0.6833 0.5201 0.3567 0.0445  -0.1331 -0.0677 104 GLU A CA  
1651 C C   . GLU A 105 ? 0.6848 0.5133 0.3162 0.0516  -0.1364 -0.0584 104 GLU A C   
1652 O O   . GLU A 105 ? 0.6712 0.5144 0.3216 0.0490  -0.1428 -0.0463 104 GLU A O   
1653 C CB  . GLU A 105 ? 0.7759 0.5971 0.4534 0.0368  -0.1608 -0.0828 104 GLU A CB  
1654 C CG  . GLU A 105 ? 0.7960 0.6282 0.5244 0.0269  -0.1579 -0.0884 104 GLU A CG  
1655 C CD  . GLU A 105 ? 0.7918 0.6059 0.5242 0.0177  -0.1829 -0.1041 104 GLU A CD  
1656 O OE1 . GLU A 105 ? 0.7791 0.5754 0.4792 0.0182  -0.2064 -0.1113 104 GLU A OE1 
1657 O OE2 . GLU A 105 ? 0.7227 0.5396 0.4900 0.0095  -0.1793 -0.1090 104 GLU A OE2 
1664 N N   . LYS A 106 ? 0.6941 0.4971 0.2665 0.0614  -0.1304 -0.0632 105 LYS A N   
1665 C CA  . LYS A 106 ? 0.7176 0.5094 0.2430 0.0687  -0.1310 -0.0531 105 LYS A CA  
1666 C C   . LYS A 106 ? 0.6799 0.4939 0.2217 0.0704  -0.1054 -0.0340 105 LYS A C   
1667 O O   . LYS A 106 ? 0.7090 0.5259 0.2461 0.0701  -0.1109 -0.0203 105 LYS A O   
1668 C CB  . LYS A 106 ? 0.7877 0.5543 0.2617 0.0770  -0.1218 -0.0615 105 LYS A CB  
1669 C CG  . LYS A 106 ? 0.8730 0.6315 0.3079 0.0826  -0.1172 -0.0501 105 LYS A CG  
1670 C CD  . LYS A 106 ? 1.0170 0.7532 0.4066 0.0908  -0.1045 -0.0592 105 LYS A CD  
1671 C CE  . LYS A 106 ? 1.2055 0.9318 0.5533 0.0958  -0.1014 -0.0487 105 LYS A CE  
1672 N NZ  . LYS A 106 ? 1.3633 1.0846 0.7090 0.0906  -0.1332 -0.0465 105 LYS A NZ  
1686 N N   . ALA A 107 ? 0.6461 0.4751 0.2079 0.0721  -0.0784 -0.0328 106 ALA A N   
1687 C CA  . ALA A 107 ? 0.6702 0.5219 0.2516 0.0720  -0.0546 -0.0163 106 ALA A CA  
1688 C C   . ALA A 107 ? 0.6519 0.5260 0.2851 0.0619  -0.0631 -0.0070 106 ALA A C   
1689 O O   . ALA A 107 ? 0.6367 0.5208 0.2766 0.0604  -0.0530 0.0079  106 ALA A O   
1690 C CB  . ALA A 107 ? 0.6826 0.5493 0.2823 0.0755  -0.0285 -0.0187 106 ALA A CB  
1696 N N   . CYS A 108 ? 0.5913 0.4725 0.2618 0.0548  -0.0800 -0.0157 107 CYS A N   
1697 C CA  . CYS A 108 ? 0.5362 0.4381 0.2564 0.0465  -0.0866 -0.0088 107 CYS A CA  
1698 C C   . CYS A 108 ? 0.5603 0.4550 0.2804 0.0449  -0.1132 -0.0063 107 CYS A C   
1699 O O   . CYS A 108 ? 0.5276 0.4380 0.2873 0.0401  -0.1179 0.0002  107 CYS A O   
1700 C CB  . CYS A 108 ? 0.5063 0.4232 0.2710 0.0402  -0.0861 -0.0179 107 CYS A CB  
1701 S SG  . CYS A 108 ? 0.4938 0.4236 0.2666 0.0431  -0.0568 -0.0181 107 CYS A SG  
1707 N N   . ALA A 109 ? 0.6163 0.4876 0.2927 0.0495  -0.1312 -0.0115 108 ALA A N   
1708 C CA  . ALA A 109 ? 0.6257 0.4923 0.3072 0.0480  -0.1621 -0.0120 108 ALA A CA  
1709 C C   . ALA A 109 ? 0.6229 0.4928 0.3073 0.0504  -0.1646 0.0055  108 ALA A C   
1710 O O   . ALA A 109 ? 0.6023 0.4833 0.3236 0.0477  -0.1819 0.0084  108 ALA A O   
1711 C CB  . ALA A 109 ? 0.6991 0.5376 0.3265 0.0527  -0.1823 -0.0221 108 ALA A CB  
1717 N N   . ASN A 110 ? 0.6442 0.5038 0.2914 0.0558  -0.1469 0.0177  109 ASN A N   
1718 C CA  . ASN A 110 ? 0.6803 0.5361 0.3228 0.0583  -0.1489 0.0357  109 ASN A CA  
1719 C C   . ASN A 110 ? 0.6819 0.5368 0.3061 0.0592  -0.1175 0.0484  109 ASN A C   
1720 O O   . ASN A 110 ? 0.7358 0.5703 0.3073 0.0655  -0.1124 0.0580  109 ASN A O   
1721 C CB  . ASN A 110 ? 0.7682 0.5996 0.3631 0.0656  -0.1755 0.0392  109 ASN A CB  
1722 C CG  . ASN A 110 ? 0.8273 0.6557 0.4296 0.0685  -0.1851 0.0572  109 ASN A CG  
1723 O OD1 . ASN A 110 ? 0.8881 0.7345 0.5431 0.0641  -0.1810 0.0620  109 ASN A OD1 
1724 N ND2 . ASN A 110 ? 0.8791 0.6865 0.4344 0.0752  -0.1942 0.0663  109 ASN A ND2 
1731 N N   . PRO A 111 ? 0.5923 0.4691 0.2582 0.0529  -0.0963 0.0490  110 PRO A N   
1732 C CA  . PRO A 111 ? 0.5964 0.4772 0.2521 0.0522  -0.0664 0.0594  110 PRO A CA  
1733 C C   . PRO A 111 ? 0.6442 0.5180 0.2970 0.0507  -0.0615 0.0789  110 PRO A C   
1734 O O   . PRO A 111 ? 0.6515 0.5213 0.3213 0.0501  -0.0792 0.0843  110 PRO A O   
1735 C CB  . PRO A 111 ? 0.5687 0.4768 0.2763 0.0449  -0.0523 0.0522  110 PRO A CB  
1736 C CG  . PRO A 111 ? 0.5622 0.4755 0.2932 0.0436  -0.0709 0.0366  110 PRO A CG  
1737 C CD  . PRO A 111 ? 0.5322 0.4318 0.2542 0.0460  -0.0982 0.0379  110 PRO A CD  
1745 N N   . ALA A 112 ? 0.6765 0.5498 0.3112 0.0499  -0.0357 0.0900  111 ALA A N   
1746 C CA  . ALA A 112 ? 0.6903 0.5565 0.3264 0.0461  -0.0268 0.1095  111 ALA A CA  
1747 C C   . ALA A 112 ? 0.6018 0.4863 0.2985 0.0366  -0.0268 0.1091  111 ALA A C   
1748 O O   . ALA A 112 ? 0.5331 0.4406 0.2673 0.0316  -0.0210 0.0971  111 ALA A O   
1749 C CB  . ALA A 112 ? 0.7339 0.6003 0.3460 0.0450  0.0037  0.1209  111 ALA A CB  
1755 N N   . ALA A 113 ? 0.6216 0.4932 0.3249 0.0349  -0.0335 0.1224  112 ALA A N   
1756 C CA  . ALA A 113 ? 0.6376 0.5213 0.3944 0.0272  -0.0347 0.1209  112 ALA A CA  
1757 C C   . ALA A 113 ? 0.6174 0.5232 0.4038 0.0169  -0.0109 0.1182  112 ALA A C   
1758 O O   . ALA A 113 ? 0.5746 0.4800 0.3456 0.0130  0.0097  0.1286  112 ALA A O   
1759 C CB  . ALA A 113 ? 0.7242 0.5855 0.4777 0.0276  -0.0401 0.1382  112 ALA A CB  
1765 N N   . GLY A 114 ? 0.5478 0.4740 0.3774 0.0123  -0.0139 0.1043  113 GLY A N   
1766 C CA  . GLY A 114 ? 0.4664 0.4146 0.3269 0.0027  0.0036  0.1004  113 GLY A CA  
1767 C C   . GLY A 114 ? 0.4658 0.4331 0.3211 0.0043  0.0150  0.0917  113 GLY A C   
1768 O O   . GLY A 114 ? 0.5182 0.5047 0.3948 -0.0028 0.0307  0.0915  113 GLY A O   
1772 N N   . SER A 115 ? 0.4383 0.4003 0.2671 0.0136  0.0066  0.0843  114 SER A N   
1773 C CA  . SER A 115 ? 0.4472 0.4227 0.2678 0.0172  0.0181  0.0763  114 SER A CA  
1774 C C   . SER A 115 ? 0.4443 0.4413 0.3033 0.0139  0.0160  0.0629  114 SER A C   
1775 O O   . SER A 115 ? 0.4283 0.4241 0.3053 0.0132  0.0005  0.0553  114 SER A O   
1776 C CB  . SER A 115 ? 0.4756 0.4335 0.2536 0.0279  0.0082  0.0707  114 SER A CB  
1777 O OG  . SER A 115 ? 0.5655 0.5019 0.2987 0.0325  0.0115  0.0832  114 SER A OG  
1783 N N   . VAL A 116 ? 0.4068 0.4239 0.2782 0.0125  0.0321  0.0609  115 VAL A N   
1784 C CA  . VAL A 116 ? 0.3853 0.4210 0.2841 0.0119  0.0311  0.0492  115 VAL A CA  
1785 C C   . VAL A 116 ? 0.3847 0.4206 0.2617 0.0218  0.0370  0.0430  115 VAL A C   
1786 O O   . VAL A 116 ? 0.4138 0.4516 0.2720 0.0262  0.0523  0.0488  115 VAL A O   
1787 C CB  . VAL A 116 ? 0.3764 0.4356 0.3099 0.0030  0.0416  0.0514  115 VAL A CB  
1788 C CG1 . VAL A 116 ? 0.3548 0.4307 0.3122 0.0034  0.0382  0.0398  115 VAL A CG1 
1789 C CG2 . VAL A 116 ? 0.3831 0.4364 0.3340 -0.0066 0.0366  0.0568  115 VAL A CG2 
1799 N N   . ILE A 117 ? 0.3563 0.3868 0.2337 0.0255  0.0252  0.0317  116 ILE A N   
1800 C CA  . ILE A 117 ? 0.3740 0.3979 0.2303 0.0350  0.0274  0.0234  116 ILE A CA  
1801 C C   . ILE A 117 ? 0.3639 0.4023 0.2481 0.0345  0.0274  0.0156  116 ILE A C   
1802 O O   . ILE A 117 ? 0.3719 0.4134 0.2794 0.0282  0.0170  0.0119  116 ILE A O   
1803 C CB  . ILE A 117 ? 0.3822 0.3799 0.2095 0.0388  0.0102  0.0171  116 ILE A CB  
1804 C CG1 . ILE A 117 ? 0.4274 0.4083 0.2216 0.0404  0.0080  0.0262  116 ILE A CG1 
1805 C CG2 . ILE A 117 ? 0.4339 0.4205 0.2400 0.0475  0.0112  0.0062  116 ILE A CG2 
1806 C CD1 . ILE A 117 ? 0.4998 0.4580 0.2728 0.0420  -0.0154 0.0212  116 ILE A CD1 
1818 N N   . LEU A 118 ? 0.3638 0.4106 0.2451 0.0420  0.0398  0.0135  117 LEU A N   
1819 C CA  . LEU A 118 ? 0.3496 0.4055 0.2504 0.0441  0.0393  0.0071  117 LEU A CA  
1820 C C   . LEU A 118 ? 0.3637 0.3990 0.2388 0.0543  0.0379  -0.0017 117 LEU A C   
1821 O O   . LEU A 118 ? 0.3740 0.4022 0.2235 0.0638  0.0482  -0.0016 117 LEU A O   
1822 C CB  . LEU A 118 ? 0.3342 0.4181 0.2586 0.0453  0.0528  0.0122  117 LEU A CB  
1823 C CG  . LEU A 118 ? 0.3473 0.4405 0.2882 0.0497  0.0525  0.0076  117 LEU A CG  
1824 C CD1 . LEU A 118 ? 0.3370 0.4299 0.2963 0.0409  0.0405  0.0044  117 LEU A CD1 
1825 C CD2 . LEU A 118 ? 0.3802 0.5028 0.3423 0.0527  0.0644  0.0135  117 LEU A CD2 
1837 N N   . LEU A 119 ? 0.3304 0.3552 0.2125 0.0522  0.0265  -0.0092 118 LEU A N   
1838 C CA  . LEU A 119 ? 0.3725 0.3739 0.2329 0.0597  0.0232  -0.0187 118 LEU A CA  
1839 C C   . LEU A 119 ? 0.3743 0.3830 0.2441 0.0682  0.0340  -0.0194 118 LEU A C   
1840 O O   . LEU A 119 ? 0.3343 0.3666 0.2308 0.0664  0.0392  -0.0136 118 LEU A O   
1841 C CB  . LEU A 119 ? 0.3720 0.3582 0.2390 0.0516  0.0058  -0.0256 118 LEU A CB  
1842 C CG  . LEU A 119 ? 0.3880 0.3699 0.2535 0.0436  -0.0082 -0.0246 118 LEU A CG  
1843 C CD1 . LEU A 119 ? 0.4127 0.3860 0.2949 0.0357  -0.0239 -0.0313 118 LEU A CD1 
1844 C CD2 . LEU A 119 ? 0.4297 0.3936 0.2558 0.0494  -0.0105 -0.0257 118 LEU A CD2 
1856 N N   . GLU A 120 ? 0.4151 0.4016 0.2611 0.0784  0.0362  -0.0269 119 GLU A N   
1857 C CA  . GLU A 120 ? 0.4311 0.4200 0.2840 0.0889  0.0457  -0.0274 119 GLU A CA  
1858 C C   . GLU A 120 ? 0.4261 0.4111 0.2997 0.0824  0.0369  -0.0286 119 GLU A C   
1859 O O   . GLU A 120 ? 0.4089 0.3847 0.2880 0.0708  0.0242  -0.0317 119 GLU A O   
1860 C CB  . GLU A 120 ? 0.4604 0.4218 0.2788 0.1030  0.0517  -0.0360 119 GLU A CB  
1861 C CG  . GLU A 120 ? 0.4925 0.4502 0.3142 0.1174  0.0619  -0.0373 119 GLU A CG  
1862 C CD  . GLU A 120 ? 0.5055 0.4995 0.3520 0.1253  0.0763  -0.0268 119 GLU A CD  
1863 O OE1 . GLU A 120 ? 0.5269 0.5249 0.3623 0.1398  0.0916  -0.0267 119 GLU A OE1 
1864 O OE2 . GLU A 120 ? 0.4530 0.4716 0.3306 0.1174  0.0724  -0.0193 119 GLU A OE2 
1871 N N   . ASN A 121 ? 0.3721 0.3656 0.2582 0.0906  0.0444  -0.0250 120 ASN A N   
1872 C CA  . ASN A 121 ? 0.3302 0.3210 0.2333 0.0867  0.0398  -0.0232 120 ASN A CA  
1873 C C   . ASN A 121 ? 0.3514 0.3125 0.2482 0.0779  0.0287  -0.0306 120 ASN A C   
1874 O O   . ASN A 121 ? 0.4218 0.3532 0.2979 0.0835  0.0273  -0.0385 120 ASN A O   
1875 C CB  . ASN A 121 ? 0.3432 0.3329 0.2457 0.1026  0.0491  -0.0205 120 ASN A CB  
1876 C CG  . ASN A 121 ? 0.3252 0.3213 0.2461 0.1010  0.0470  -0.0138 120 ASN A CG  
1877 O OD1 . ASN A 121 ? 0.3079 0.2965 0.2358 0.0888  0.0398  -0.0138 120 ASN A OD1 
1878 N ND2 . ASN A 121 ? 0.3189 0.3287 0.2469 0.1146  0.0539  -0.0075 120 ASN A ND2 
1885 N N   . LEU A 122 ? 0.3166 0.2854 0.2326 0.0640  0.0211  -0.0286 121 LEU A N   
1886 C CA  . LEU A 122 ? 0.3204 0.2668 0.2389 0.0538  0.0112  -0.0344 121 LEU A CA  
1887 C C   . LEU A 122 ? 0.3623 0.2842 0.2760 0.0585  0.0141  -0.0355 121 LEU A C   
1888 O O   . LEU A 122 ? 0.3816 0.2761 0.2891 0.0528  0.0067  -0.0431 121 LEU A O   
1889 C CB  . LEU A 122 ? 0.2979 0.2615 0.2431 0.0403  0.0071  -0.0303 121 LEU A CB  
1890 C CG  . LEU A 122 ? 0.2993 0.2798 0.2515 0.0337  0.0014  -0.0301 121 LEU A CG  
1891 C CD1 . LEU A 122 ? 0.2741 0.2755 0.2525 0.0250  0.0023  -0.0251 121 LEU A CD1 
1892 C CD2 . LEU A 122 ? 0.3399 0.3027 0.2842 0.0280  -0.0120 -0.0382 121 LEU A CD2 
1904 N N   . ARG A 123 ? 0.3377 0.2680 0.2554 0.0680  0.0236  -0.0277 122 ARG A N   
1905 C CA  . ARG A 123 ? 0.3602 0.2652 0.2742 0.0721  0.0262  -0.0263 122 ARG A CA  
1906 C C   . ARG A 123 ? 0.3977 0.2744 0.2877 0.0864  0.0295  -0.0331 122 ARG A C   
1907 O O   . ARG A 123 ? 0.4221 0.2730 0.3071 0.0917  0.0321  -0.0320 122 ARG A O   
1908 C CB  . ARG A 123 ? 0.3452 0.2681 0.2711 0.0772  0.0330  -0.0142 122 ARG A CB  
1909 C CG  . ARG A 123 ? 0.3208 0.2591 0.2653 0.0626  0.0308  -0.0093 122 ARG A CG  
1910 C CD  . ARG A 123 ? 0.3138 0.2657 0.2630 0.0679  0.0363  0.0021  122 ARG A CD  
1911 N NE  . ARG A 123 ? 0.2931 0.2602 0.2563 0.0547  0.0359  0.0053  122 ARG A NE  
1912 C CZ  . ARG A 123 ? 0.2887 0.2673 0.2530 0.0562  0.0395  0.0140  122 ARG A CZ  
1913 N NH1 . ARG A 123 ? 0.3023 0.2802 0.2568 0.0702  0.0417  0.0214  122 ARG A NH1 
1914 N NH2 . ARG A 123 ? 0.2740 0.2643 0.2481 0.0449  0.0407  0.0152  122 ARG A NH2 
1928 N N   . PHE A 124 ? 0.4071 0.2853 0.2803 0.0931  0.0303  -0.0399 123 PHE A N   
1929 C CA  . PHE A 124 ? 0.4678 0.3127 0.3129 0.1047  0.0323  -0.0503 123 PHE A CA  
1930 C C   . PHE A 124 ? 0.4968 0.3047 0.3314 0.0928  0.0201  -0.0618 123 PHE A C   
1931 O O   . PHE A 124 ? 0.5235 0.2964 0.3328 0.1008  0.0200  -0.0723 123 PHE A O   
1932 C CB  . PHE A 124 ? 0.4747 0.3299 0.3008 0.1134  0.0372  -0.0548 123 PHE A CB  
1933 C CG  . PHE A 124 ? 0.4581 0.3458 0.2940 0.1275  0.0512  -0.0453 123 PHE A CG  
1934 C CD1 . PHE A 124 ? 0.4516 0.3558 0.3094 0.1334  0.0561  -0.0347 123 PHE A CD1 
1935 C CD2 . PHE A 124 ? 0.4943 0.3962 0.3176 0.1346  0.0593  -0.0465 123 PHE A CD2 
1936 C CE1 . PHE A 124 ? 0.4439 0.3802 0.3146 0.1457  0.0664  -0.0267 123 PHE A CE1 
1937 C CE2 . PHE A 124 ? 0.5170 0.4512 0.3548 0.1461  0.0725  -0.0377 123 PHE A CE2 
1938 C CZ  . PHE A 124 ? 0.4601 0.4131 0.3239 0.1514  0.0749  -0.0282 123 PHE A CZ  
1948 N N   . HIS A 125 ? 0.4698 0.2849 0.3245 0.0741  0.0098  -0.0605 124 HIS A N   
1949 C CA  . HIS A 125 ? 0.5095 0.2964 0.3643 0.0596  -0.0036 -0.0702 124 HIS A CA  
1950 C C   . HIS A 125 ? 0.4916 0.2757 0.3730 0.0485  -0.0023 -0.0623 124 HIS A C   
1951 O O   . HIS A 125 ? 0.4431 0.2571 0.3482 0.0425  0.0013  -0.0517 124 HIS A O   
1952 C CB  . HIS A 125 ? 0.5132 0.3148 0.3731 0.0470  -0.0172 -0.0750 124 HIS A CB  
1953 C CG  . HIS A 125 ? 0.5957 0.3944 0.4242 0.0563  -0.0193 -0.0825 124 HIS A CG  
1954 N ND1 . HIS A 125 ? 0.6556 0.4209 0.4542 0.0565  -0.0301 -0.0972 124 HIS A ND1 
1955 C CD2 . HIS A 125 ? 0.5995 0.4225 0.4194 0.0658  -0.0109 -0.0770 124 HIS A CD2 
1956 C CE1 . HIS A 125 ? 0.6710 0.4401 0.4408 0.0666  -0.0275 -0.0999 124 HIS A CE1 
1957 N NE2 . HIS A 125 ? 0.6346 0.4389 0.4184 0.0721  -0.0150 -0.0871 124 HIS A NE2 
1965 N N   . VAL A 126 ? 0.5211 0.2672 0.3972 0.0449  -0.0049 -0.0677 125 VAL A N   
1966 C CA  . VAL A 126 ? 0.5570 0.2961 0.4560 0.0342  -0.0013 -0.0588 125 VAL A CA  
1967 C C   . VAL A 126 ? 0.5281 0.2891 0.4584 0.0136  -0.0089 -0.0572 125 VAL A C   
1968 O O   . VAL A 126 ? 0.4851 0.2547 0.4381 0.0052  -0.0019 -0.0464 125 VAL A O   
1969 C CB  . VAL A 126 ? 0.6288 0.3176 0.5150 0.0334  -0.0030 -0.0659 125 VAL A CB  
1970 C CG1 . VAL A 126 ? 0.6506 0.3173 0.5333 0.0191  -0.0202 -0.0827 125 VAL A CG1 
1971 C CG2 . VAL A 126 ? 0.6898 0.3679 0.5952 0.0256  0.0053  -0.0528 125 VAL A CG2 
1981 N N   . GLU A 127 ? 0.4722 0.2433 0.4038 0.0065  -0.0225 -0.0669 126 GLU A N   
1982 C CA  . GLU A 127 ? 0.4498 0.2421 0.4147 -0.0115 -0.0308 -0.0660 126 GLU A CA  
1983 C C   . GLU A 127 ? 0.4041 0.2377 0.3886 -0.0108 -0.0224 -0.0544 126 GLU A C   
1984 O O   . GLU A 127 ? 0.3852 0.2373 0.4005 -0.0239 -0.0248 -0.0517 126 GLU A O   
1985 C CB  . GLU A 127 ? 0.4627 0.2515 0.4216 -0.0177 -0.0505 -0.0796 126 GLU A CB  
1986 C CG  . GLU A 127 ? 0.5267 0.2730 0.4697 -0.0229 -0.0625 -0.0936 126 GLU A CG  
1987 C CD  . GLU A 127 ? 0.6783 0.3957 0.5745 -0.0052 -0.0600 -0.1023 126 GLU A CD  
1988 O OE1 . GLU A 127 ? 0.7442 0.4225 0.6213 -0.0080 -0.0702 -0.1162 126 GLU A OE1 
1989 O OE2 . GLU A 127 ? 0.5839 0.3174 0.4633 0.0114  -0.0477 -0.0960 126 GLU A OE2 
1996 N N   . GLU A 128 ? 0.4188 0.2674 0.3878 0.0038  -0.0126 -0.0483 127 GLU A N   
1997 C CA  . GLU A 128 ? 0.3808 0.2648 0.3665 0.0036  -0.0057 -0.0389 127 GLU A CA  
1998 C C   . GLU A 128 ? 0.3469 0.2337 0.3497 -0.0016 0.0057  -0.0284 127 GLU A C   
1999 O O   . GLU A 128 ? 0.3254 0.2299 0.3532 -0.0123 0.0074  -0.0251 127 GLU A O   
2000 C CB  . GLU A 128 ? 0.3534 0.2522 0.3200 0.0190  0.0005  -0.0357 127 GLU A CB  
2001 C CG  . GLU A 128 ? 0.3055 0.2363 0.2848 0.0205  0.0090  -0.0258 127 GLU A CG  
2002 C CD  . GLU A 128 ? 0.2920 0.2459 0.2913 0.0107  0.0041  -0.0265 127 GLU A CD  
2003 O OE1 . GLU A 128 ? 0.3253 0.2742 0.3335 0.0022  -0.0065 -0.0330 127 GLU A OE1 
2004 O OE2 . GLU A 128 ? 0.2886 0.2655 0.2954 0.0118  0.0100  -0.0207 127 GLU A OE2 
2011 N N   . GLU A 129 ? 0.3692 0.2370 0.3574 0.0067  0.0143  -0.0227 128 GLU A N   
2012 C CA  . GLU A 129 ? 0.4002 0.2657 0.3979 0.0029  0.0256  -0.0111 128 GLU A CA  
2013 C C   . GLU A 129 ? 0.4524 0.2920 0.4642 -0.0115 0.0252  -0.0119 128 GLU A C   
2014 O O   . GLU A 129 ? 0.4414 0.2829 0.4676 -0.0196 0.0352  -0.0023 128 GLU A O   
2015 C CB  . GLU A 129 ? 0.4008 0.2569 0.3767 0.0191  0.0341  -0.0023 128 GLU A CB  
2016 C CG  . GLU A 129 ? 0.4490 0.3333 0.4157 0.0325  0.0351  -0.0001 128 GLU A CG  
2017 C CD  . GLU A 129 ? 0.6097 0.4878 0.5603 0.0487  0.0418  0.0097  128 GLU A CD  
2018 O OE1 . GLU A 129 ? 0.6289 0.5171 0.5804 0.0493  0.0476  0.0205  128 GLU A OE1 
2019 O OE2 . GLU A 129 ? 0.6744 0.5365 0.6104 0.0618  0.0410  0.0065  128 GLU A OE2 
2026 N N   . GLY A 130 ? 0.4320 0.2464 0.4391 -0.0153 0.0143  -0.0232 129 GLY A N   
2027 C CA  . GLY A 130 ? 0.4438 0.2313 0.4659 -0.0305 0.0122  -0.0253 129 GLY A CA  
2028 C C   . GLY A 130 ? 0.4835 0.2305 0.4863 -0.0243 0.0187  -0.0213 129 GLY A C   
2029 O O   . GLY A 130 ? 0.5305 0.2478 0.5428 -0.0372 0.0160  -0.0243 129 GLY A O   
2033 N N   . LYS A 131 ? 0.4856 0.2301 0.4633 -0.0049 0.0264  -0.0147 130 LYS A N   
2034 C CA  . LYS A 131 ? 0.5993 0.3064 0.5580 0.0050  0.0337  -0.0084 130 LYS A CA  
2035 C C   . LYS A 131 ? 0.6131 0.3266 0.5463 0.0293  0.0358  -0.0077 130 LYS A C   
2036 O O   . LYS A 131 ? 0.6124 0.3626 0.5463 0.0357  0.0350  -0.0077 130 LYS A O   
2037 C CB  . LYS A 131 ? 0.7365 0.4400 0.7038 -0.0001 0.0474  0.0096  130 LYS A CB  
2038 C CG  . LYS A 131 ? 0.8833 0.6255 0.8498 0.0079  0.0550  0.0211  130 LYS A CG  
2039 C CD  . LYS A 131 ? 1.0862 0.8223 1.0543 0.0036  0.0690  0.0390  130 LYS A CD  
2040 C CE  . LYS A 131 ? 1.1347 0.9107 1.1032 0.0072  0.0747  0.0469  130 LYS A CE  
2041 N NZ  . LYS A 131 ? 1.1330 0.9292 1.0838 0.0268  0.0694  0.0457  130 LYS A NZ  
2055 N N   . GLY A 132 ? 0.6079 0.2852 0.5209 0.0427  0.0390  -0.0071 131 GLY A N   
2056 C CA  . GLY A 132 ? 0.5737 0.2587 0.4676 0.0671  0.0427  -0.0050 131 GLY A CA  
2057 C C   . GLY A 132 ? 0.6209 0.2602 0.4951 0.0817  0.0466  -0.0048 131 GLY A C   
2058 O O   . GLY A 132 ? 0.6402 0.2448 0.5154 0.0748  0.0499  0.0017  131 GLY A O   
2062 N N   . LYS A 133 ? 0.7045 0.3420 0.5614 0.1022  0.0472  -0.0119 132 LYS A N   
2063 C CA  . LYS A 133 ? 0.7675 0.3607 0.6046 0.1198  0.0515  -0.0141 132 LYS A CA  
2064 C C   . LYS A 133 ? 0.7777 0.3571 0.5961 0.1274  0.0476  -0.0343 132 LYS A C   
2065 O O   . LYS A 133 ? 0.7845 0.3975 0.6037 0.1262  0.0444  -0.0415 132 LYS A O   
2066 C CB  . LYS A 133 ? 0.8247 0.4311 0.6585 0.1446  0.0599  0.0013  132 LYS A CB  
2067 C CG  . LYS A 133 ? 0.9430 0.5577 0.7870 0.1396  0.0634  0.0221  132 LYS A CG  
2068 C CD  . LYS A 133 ? 1.0666 0.6952 0.9062 0.1652  0.0680  0.0371  132 LYS A CD  
2069 C CE  . LYS A 133 ? 1.1393 0.7715 0.9815 0.1610  0.0705  0.0581  132 LYS A CE  
2070 N NZ  . LYS A 133 ? 1.1578 0.8349 1.0140 0.1438  0.0682  0.0611  132 LYS A NZ  
2084 N N   . ASP A 134 ? 0.7934 0.3203 0.5925 0.1349  0.0483  -0.0435 133 ASP A N   
2085 C CA  . ASP A 134 ? 0.8776 0.3875 0.6518 0.1468  0.0471  -0.0629 133 ASP A CA  
2086 C C   . ASP A 134 ? 0.9432 0.4692 0.7087 0.1780  0.0594  -0.0579 133 ASP A C   
2087 O O   . ASP A 134 ? 0.8777 0.4296 0.6583 0.1890  0.0657  -0.0401 133 ASP A O   
2088 C CB  . ASP A 134 ? 1.0013 0.4464 0.7568 0.1408  0.0417  -0.0779 133 ASP A CB  
2089 C CG  . ASP A 134 ? 1.1239 0.5353 0.8761 0.1553  0.0500  -0.0694 133 ASP A CG  
2090 O OD1 . ASP A 134 ? 1.1655 0.5968 0.9241 0.1745  0.0598  -0.0528 133 ASP A OD1 
2091 O OD2 . ASP A 134 ? 1.1959 0.5668 0.9432 0.1458  0.0449  -0.0789 133 ASP A OD2 
2096 N N   . ALA A 135 ? 1.0608 0.5729 0.8019 0.1928  0.0627  -0.0741 134 ALA A N   
2097 C CA  . ALA A 135 ? 1.0086 0.5517 0.7514 0.2177  0.0746  -0.0688 134 ALA A CA  
2098 C C   . ALA A 135 ? 0.9820 0.5101 0.7315 0.2340  0.0810  -0.0576 134 ALA A C   
2099 O O   . ALA A 135 ? 0.9767 0.5376 0.7382 0.2535  0.0893  -0.0471 134 ALA A O   
2100 C CB  . ALA A 135 ? 1.0568 0.5989 0.7773 0.2226  0.0767  -0.0865 134 ALA A CB  
2106 N N   . SER A 136 ? 0.9372 0.4178 0.6814 0.2257  0.0766  -0.0592 135 SER A N   
2107 C CA  . SER A 136 ? 0.9227 0.3845 0.6727 0.2394  0.0814  -0.0468 135 SER A CA  
2108 C C   . SER A 136 ? 1.0096 0.4805 0.7766 0.2357  0.0805  -0.0243 135 SER A C   
2109 O O   . SER A 136 ? 1.0371 0.4929 0.8079 0.2465  0.0832  -0.0115 135 SER A O   
2110 C CB  . SER A 136 ? 0.9706 0.3752 0.7068 0.2315  0.0775  -0.0588 135 SER A CB  
2111 O OG  . SER A 136 ? 1.0613 0.4562 0.7779 0.2364  0.0784  -0.0796 135 SER A OG  
2117 N N   . GLY A 137 ? 1.0882 0.5815 0.8638 0.2212  0.0770  -0.0188 136 GLY A N   
2118 C CA  . GLY A 137 ? 1.0468 0.5507 0.8353 0.2182  0.0774  0.0029  136 GLY A CA  
2119 C C   . GLY A 137 ? 1.0166 0.4800 0.8052 0.1962  0.0747  0.0086  136 GLY A C   
2120 O O   . GLY A 137 ? 1.0265 0.4948 0.8223 0.1942  0.0769  0.0287  136 GLY A O   
2124 N N   . ASN A 138 ? 0.9517 0.3794 0.7341 0.1778  0.0694  -0.0079 137 ASN A N   
2125 C CA  . ASN A 138 ? 0.9860 0.3819 0.7759 0.1524  0.0669  -0.0028 137 ASN A CA  
2126 C C   . ASN A 138 ? 0.9115 0.3477 0.7217 0.1265  0.0616  -0.0025 137 ASN A C   
2127 O O   . ASN A 138 ? 0.8246 0.2897 0.6373 0.1207  0.0550  -0.0169 137 ASN A O   
2128 C CB  . ASN A 138 ? 1.0750 0.4269 0.8590 0.1404  0.0603  -0.0211 137 ASN A CB  
2129 C CG  . ASN A 138 ? 1.2423 0.5704 1.0145 0.1621  0.0640  -0.0233 137 ASN A CG  
2130 O OD1 . ASN A 138 ? 1.3055 0.6101 1.0804 0.1661  0.0679  -0.0091 137 ASN A OD1 
2131 N ND2 . ASN A 138 ? 1.3225 0.6565 1.0809 0.1766  0.0635  -0.0406 137 ASN A ND2 
2138 N N   . LYS A 139 ? 0.9541 0.3945 0.7790 0.1113  0.0652  0.0148  138 LYS A N   
2139 C CA  . LYS A 139 ? 0.9907 0.4727 0.8384 0.0876  0.0620  0.0161  138 LYS A CA  
2140 C C   . LYS A 139 ? 0.8983 0.3638 0.7568 0.0626  0.0524  -0.0018 138 LYS A C   
2141 O O   . LYS A 139 ? 0.9477 0.3634 0.8035 0.0532  0.0510  -0.0066 138 LYS A O   
2142 C CB  . LYS A 139 ? 1.2051 0.6918 1.0628 0.0787  0.0708  0.0389  138 LYS A CB  
2143 C CG  . LYS A 139 ? 1.3903 0.9101 1.2405 0.0990  0.0760  0.0560  138 LYS A CG  
2144 C CD  . LYS A 139 ? 1.5166 1.0430 1.3719 0.0882  0.0843  0.0769  138 LYS A CD  
2145 C CE  . LYS A 139 ? 1.5364 1.1013 1.3834 0.1057  0.0858  0.0911  138 LYS A CE  
2146 N NZ  . LYS A 139 ? 1.5601 1.1333 1.4073 0.0940  0.0940  0.1093  138 LYS A NZ  
2160 N N   . VAL A 140 ? 0.8342 0.3410 0.7059 0.0516  0.0445  -0.0117 139 VAL A N   
2161 C CA  . VAL A 140 ? 0.8329 0.3304 0.7161 0.0293  0.0320  -0.0290 139 VAL A CA  
2162 C C   . VAL A 140 ? 0.8090 0.3548 0.7216 0.0105  0.0287  -0.0261 139 VAL A C   
2163 O O   . VAL A 140 ? 0.7724 0.3617 0.6897 0.0177  0.0338  -0.0168 139 VAL A O   
2164 C CB  . VAL A 140 ? 0.8326 0.3192 0.6924 0.0396  0.0216  -0.0510 139 VAL A CB  
2165 C CG1 . VAL A 140 ? 0.9225 0.3616 0.7529 0.0613  0.0273  -0.0544 139 VAL A CG1 
2166 C CG2 . VAL A 140 ? 0.7723 0.3096 0.6289 0.0509  0.0208  -0.0525 139 VAL A CG2 
2176 N N   . LYS A 141 ? 0.8280 0.3653 0.7620 -0.0137 0.0193  -0.0351 140 LYS A N   
2177 C CA  . LYS A 141 ? 0.8339 0.4135 0.8004 -0.0323 0.0149  -0.0342 140 LYS A CA  
2178 C C   . LYS A 141 ? 0.8197 0.4083 0.7866 -0.0386 -0.0043 -0.0546 140 LYS A C   
2179 O O   . LYS A 141 ? 0.8634 0.4150 0.8158 -0.0414 -0.0159 -0.0703 140 LYS A O   
2180 C CB  . LYS A 141 ? 0.9369 0.5050 0.9353 -0.0562 0.0202  -0.0255 140 LYS A CB  
2181 C CG  . LYS A 141 ? 1.0234 0.6382 1.0594 -0.0727 0.0212  -0.0207 140 LYS A CG  
2182 C CD  . LYS A 141 ? 1.1603 0.7664 1.2265 -0.0927 0.0339  -0.0071 140 LYS A CD  
2183 C CE  . LYS A 141 ? 1.2118 0.8128 1.2620 -0.0813 0.0554  0.0152  140 LYS A CE  
2184 N NZ  . LYS A 141 ? 1.2053 0.8002 1.2823 -0.1006 0.0712  0.0308  140 LYS A NZ  
2198 N N   . ALA A 142 ? 0.7328 0.3682 0.7134 -0.0402 -0.0082 -0.0546 141 ALA A N   
2199 C CA  . ALA A 142 ? 0.6873 0.3334 0.6668 -0.0452 -0.0270 -0.0713 141 ALA A CA  
2200 C C   . ALA A 142 ? 0.7485 0.3871 0.7600 -0.0707 -0.0410 -0.0793 141 ALA A C   
2201 O O   . ALA A 142 ? 0.7397 0.3848 0.7855 -0.0864 -0.0334 -0.0690 141 ALA A O   
2202 C CB  . ALA A 142 ? 0.6029 0.2991 0.5897 -0.0394 -0.0265 -0.0669 141 ALA A CB  
2208 N N   . GLU A 143 ? 0.8129 0.4384 0.8130 -0.0750 -0.0618 -0.0979 142 GLU A N   
2209 C CA  . GLU A 143 ? 0.8530 0.4736 0.8849 -0.0995 -0.0798 -0.1076 142 GLU A CA  
2210 C C   . GLU A 143 ? 0.6355 0.3072 0.7023 -0.1081 -0.0883 -0.1051 142 GLU A C   
2211 O O   . GLU A 143 ? 0.5806 0.2762 0.6299 -0.0951 -0.0926 -0.1068 142 GLU A O   
2212 C CB  . GLU A 143 ? 1.1657 0.7478 1.1668 -0.1002 -0.1014 -0.1299 142 GLU A CB  
2213 C CG  . GLU A 143 ? 1.4291 0.9561 1.3940 -0.0900 -0.0934 -0.1348 142 GLU A CG  
2214 C CD  . GLU A 143 ? 1.6149 1.1122 1.5369 -0.0820 -0.1084 -0.1561 142 GLU A CD  
2215 O OE1 . GLU A 143 ? 1.6660 1.1797 1.5949 -0.0934 -0.1273 -0.1672 142 GLU A OE1 
2216 O OE2 . GLU A 143 ? 1.6893 1.1544 1.5713 -0.0625 -0.0982 -0.1597 142 GLU A OE2 
2223 N N   . PRO A 144 ? 0.6070 0.4184 0.5844 -0.1528 -0.0757 -0.1084 143 PRO A N   
2224 C CA  . PRO A 144 ? 0.6080 0.4701 0.6158 -0.1524 -0.0804 -0.1040 143 PRO A CA  
2225 C C   . PRO A 144 ? 0.6018 0.4818 0.6025 -0.1448 -0.0960 -0.1130 143 PRO A C   
2226 O O   . PRO A 144 ? 0.5479 0.4570 0.5561 -0.1315 -0.0964 -0.1068 143 PRO A O   
2227 C CB  . PRO A 144 ? 0.6326 0.5110 0.6725 -0.1771 -0.0817 -0.1046 143 PRO A CB  
2228 C CG  . PRO A 144 ? 0.6691 0.5061 0.6972 -0.1871 -0.0705 -0.1020 143 PRO A CG  
2229 C CD  . PRO A 144 ? 0.6864 0.4786 0.6739 -0.1755 -0.0722 -0.1094 143 PRO A CD  
2237 N N   . ALA A 145 ? 0.6096 0.4715 0.5942 -0.1531 -0.1094 -0.1275 144 ALA A N   
2238 C CA  . ALA A 145 ? 0.5523 0.4290 0.5254 -0.1443 -0.1248 -0.1360 144 ALA A CA  
2239 C C   . ALA A 145 ? 0.5163 0.3852 0.4625 -0.1194 -0.1182 -0.1304 144 ALA A C   
2240 O O   . ALA A 145 ? 0.5346 0.4281 0.4804 -0.1078 -0.1242 -0.1286 144 ALA A O   
2241 C CB  . ALA A 145 ? 0.6078 0.4593 0.5618 -0.1565 -0.1398 -0.1537 144 ALA A CB  
2247 N N   . LYS A 146 ? 0.4964 0.3322 0.4205 -0.1104 -0.1052 -0.1270 145 LYS A N   
2248 C CA  . LYS A 146 ? 0.5861 0.4179 0.4878 -0.0880 -0.0977 -0.1215 145 LYS A CA  
2249 C C   . LYS A 146 ? 0.4831 0.3450 0.4061 -0.0795 -0.0880 -0.1066 145 LYS A C   
2250 O O   . LYS A 146 ? 0.4419 0.3165 0.3562 -0.0650 -0.0870 -0.1023 145 LYS A O   
2251 C CB  . LYS A 146 ? 0.9298 0.7207 0.8034 -0.0797 -0.0873 -0.1229 145 LYS A CB  
2252 C CG  . LYS A 146 ? 1.1448 0.9009 0.9896 -0.0843 -0.0971 -0.1388 145 LYS A CG  
2253 C CD  . LYS A 146 ? 1.2109 0.9333 1.0194 -0.0659 -0.0881 -0.1409 145 LYS A CD  
2254 C CE  . LYS A 146 ? 1.2182 0.9111 0.9927 -0.0657 -0.0998 -0.1580 145 LYS A CE  
2255 N NZ  . LYS A 146 ? 1.1588 0.8329 0.9394 -0.0878 -0.1090 -0.1683 145 LYS A NZ  
2269 N N   . ILE A 147 ? 0.4782 0.3504 0.4274 -0.0886 -0.0806 -0.0988 146 ILE A N   
2270 C CA  . ILE A 147 ? 0.4308 0.3310 0.3995 -0.0812 -0.0726 -0.0861 146 ILE A CA  
2271 C C   . ILE A 147 ? 0.4128 0.3466 0.3957 -0.0800 -0.0833 -0.0864 146 ILE A C   
2272 O O   . ILE A 147 ? 0.3929 0.3421 0.3762 -0.0676 -0.0800 -0.0790 146 ILE A O   
2273 C CB  . ILE A 147 ? 0.3949 0.2987 0.3864 -0.0913 -0.0631 -0.0785 146 ILE A CB  
2274 C CG1 . ILE A 147 ? 0.4238 0.2919 0.3979 -0.0894 -0.0522 -0.0764 146 ILE A CG1 
2275 C CG2 . ILE A 147 ? 0.3611 0.2924 0.3701 -0.0831 -0.0560 -0.0669 146 ILE A CG2 
2276 C CD1 . ILE A 147 ? 0.4980 0.3636 0.4898 -0.1009 -0.0430 -0.0692 146 ILE A CD1 
2288 N N   . GLU A 148 ? 0.4620 0.4076 0.4569 -0.0928 -0.0965 -0.0952 147 GLU A N   
2289 C CA  . GLU A 148 ? 0.4853 0.4641 0.4931 -0.0893 -0.1078 -0.0956 147 GLU A CA  
2290 C C   . GLU A 148 ? 0.4450 0.4170 0.4234 -0.0735 -0.1136 -0.0978 147 GLU A C   
2291 O O   . GLU A 148 ? 0.4388 0.4298 0.4194 -0.0621 -0.1146 -0.0912 147 GLU A O   
2292 C CB  . GLU A 148 ? 0.6261 0.6222 0.6544 -0.1065 -0.1222 -0.1055 147 GLU A CB  
2293 C CG  . GLU A 148 ? 0.8817 0.8993 0.9470 -0.1211 -0.1161 -0.1005 147 GLU A CG  
2294 C CD  . GLU A 148 ? 1.1187 1.1641 1.2030 -0.1102 -0.1073 -0.0878 147 GLU A CD  
2295 O OE1 . GLU A 148 ? 1.2060 1.2670 1.2855 -0.0956 -0.1128 -0.0855 147 GLU A OE1 
2296 O OE2 . GLU A 148 ? 1.1888 1.2375 1.2902 -0.1157 -0.0945 -0.0802 147 GLU A OE2 
2303 N N   . ALA A 149 ? 0.4662 0.4084 0.4147 -0.0718 -0.1160 -0.1063 148 ALA A N   
2304 C CA  . ALA A 149 ? 0.4811 0.4146 0.3979 -0.0566 -0.1199 -0.1084 148 ALA A CA  
2305 C C   . ALA A 149 ? 0.4323 0.3636 0.3402 -0.0416 -0.1048 -0.0962 148 ALA A C   
2306 O O   . ALA A 149 ? 0.4318 0.3701 0.3262 -0.0296 -0.1060 -0.0922 148 ALA A O   
2307 C CB  . ALA A 149 ? 0.5542 0.4543 0.4398 -0.0577 -0.1240 -0.1208 148 ALA A CB  
2313 N N   . PHE A 150 ? 0.4059 0.3262 0.3197 -0.0423 -0.0906 -0.0904 149 PHE A N   
2314 C CA  . PHE A 150 ? 0.3698 0.2923 0.2809 -0.0304 -0.0768 -0.0791 149 PHE A CA  
2315 C C   . PHE A 150 ? 0.3617 0.3115 0.2926 -0.0281 -0.0770 -0.0700 149 PHE A C   
2316 O O   . PHE A 150 ? 0.3712 0.3257 0.2920 -0.0176 -0.0737 -0.0638 149 PHE A O   
2317 C CB  . PHE A 150 ? 0.3785 0.2875 0.2959 -0.0328 -0.0644 -0.0755 149 PHE A CB  
2318 C CG  . PHE A 150 ? 0.4102 0.3214 0.3249 -0.0213 -0.0511 -0.0656 149 PHE A CG  
2319 C CD1 . PHE A 150 ? 0.3918 0.2897 0.2824 -0.0096 -0.0448 -0.0664 149 PHE A CD1 
2320 C CD2 . PHE A 150 ? 0.4132 0.3412 0.3501 -0.0224 -0.0447 -0.0561 149 PHE A CD2 
2321 C CE1 . PHE A 150 ? 0.3608 0.2656 0.2531 -0.0007 -0.0329 -0.0576 149 PHE A CE1 
2322 C CE2 . PHE A 150 ? 0.3981 0.3296 0.3341 -0.0135 -0.0338 -0.0481 149 PHE A CE2 
2323 C CZ  . PHE A 150 ? 0.3826 0.3044 0.2985 -0.0034 -0.0282 -0.0486 149 PHE A CZ  
2333 N N   . ARG A 151 ? 0.3500 0.3172 0.3085 -0.0379 -0.0805 -0.0691 150 ARG A N   
2334 C CA  . ARG A 151 ? 0.3456 0.3377 0.3226 -0.0343 -0.0807 -0.0613 150 ARG A CA  
2335 C C   . ARG A 151 ? 0.3260 0.3290 0.2934 -0.0271 -0.0927 -0.0632 150 ARG A C   
2336 O O   . ARG A 151 ? 0.3582 0.3687 0.3231 -0.0174 -0.0905 -0.0554 150 ARG A O   
2337 C CB  . ARG A 151 ? 0.3483 0.3577 0.3562 -0.0458 -0.0813 -0.0609 150 ARG A CB  
2338 C CG  . ARG A 151 ? 0.3373 0.3359 0.3523 -0.0499 -0.0676 -0.0558 150 ARG A CG  
2339 C CD  . ARG A 151 ? 0.3249 0.3366 0.3666 -0.0622 -0.0660 -0.0551 150 ARG A CD  
2340 N NE  . ARG A 151 ? 0.3457 0.3423 0.3874 -0.0642 -0.0531 -0.0497 150 ARG A NE  
2341 C CZ  . ARG A 151 ? 0.3696 0.3755 0.4312 -0.0715 -0.0465 -0.0451 150 ARG A CZ  
2342 N NH1 . ARG A 151 ? 0.4305 0.4631 0.5161 -0.0778 -0.0506 -0.0453 150 ARG A NH1 
2343 N NH2 . ARG A 151 ? 0.3655 0.3549 0.4223 -0.0714 -0.0354 -0.0399 150 ARG A NH2 
2357 N N   . ALA A 152 ? 0.3498 0.3524 0.3107 -0.0317 -0.1061 -0.0734 151 ALA A N   
2358 C CA  . ALA A 152 ? 0.4320 0.4434 0.3794 -0.0232 -0.1191 -0.0757 151 ALA A CA  
2359 C C   . ALA A 152 ? 0.4187 0.4125 0.3333 -0.0095 -0.1131 -0.0708 151 ALA A C   
2360 O O   . ALA A 152 ? 0.4249 0.4256 0.3310 0.0010  -0.1159 -0.0648 151 ALA A O   
2361 C CB  . ALA A 152 ? 0.5223 0.5342 0.4658 -0.0314 -0.1354 -0.0894 151 ALA A CB  
2367 N N   . SER A 153 ? 0.4100 0.3808 0.3057 -0.0088 -0.1040 -0.0727 152 SER A N   
2368 C CA  . SER A 153 ? 0.4544 0.4111 0.3206 0.0033  -0.0963 -0.0678 152 SER A CA  
2369 C C   . SER A 153 ? 0.4315 0.3952 0.3064 0.0086  -0.0838 -0.0543 152 SER A C   
2370 O O   . SER A 153 ? 0.4307 0.3933 0.2893 0.0177  -0.0826 -0.0478 152 SER A O   
2371 C CB  . SER A 153 ? 0.5075 0.4412 0.3547 0.0038  -0.0885 -0.0733 152 SER A CB  
2372 O OG  . SER A 153 ? 0.5354 0.4579 0.3531 0.0156  -0.0811 -0.0697 152 SER A OG  
2378 N N   . LEU A 154 ? 0.3918 0.3604 0.2900 0.0028  -0.0746 -0.0501 153 LEU A N   
2379 C CA  . LEU A 154 ? 0.3643 0.3400 0.2725 0.0061  -0.0649 -0.0389 153 LEU A CA  
2380 C C   . LEU A 154 ? 0.3559 0.3444 0.2696 0.0103  -0.0727 -0.0346 153 LEU A C   
2381 O O   . LEU A 154 ? 0.3628 0.3486 0.2685 0.0166  -0.0673 -0.0261 153 LEU A O   
2382 C CB  . LEU A 154 ? 0.3434 0.3242 0.2761 -0.0007 -0.0569 -0.0366 153 LEU A CB  
2383 C CG  . LEU A 154 ? 0.3663 0.3347 0.2954 -0.0024 -0.0474 -0.0383 153 LEU A CG  
2384 C CD1 . LEU A 154 ? 0.4200 0.3946 0.3721 -0.0076 -0.0407 -0.0344 153 LEU A CD1 
2385 C CD2 . LEU A 154 ? 0.3609 0.3214 0.2710 0.0056  -0.0379 -0.0341 153 LEU A CD2 
2397 N N   . SER A 155 ? 0.3697 0.3724 0.2980 0.0068  -0.0851 -0.0402 154 SER A N   
2398 C CA  . SER A 155 ? 0.3787 0.3962 0.3142 0.0131  -0.0930 -0.0364 154 SER A CA  
2399 C C   . SER A 155 ? 0.4215 0.4308 0.3280 0.0246  -0.0995 -0.0342 154 SER A C   
2400 O O   . SER A 155 ? 0.4550 0.4684 0.3595 0.0333  -0.1020 -0.0275 154 SER A O   
2401 C CB  . SER A 155 ? 0.4015 0.4408 0.3617 0.0066  -0.1049 -0.0437 154 SER A CB  
2402 O OG  . SER A 155 ? 0.4119 0.4574 0.3975 -0.0038 -0.0969 -0.0437 154 SER A OG  
2408 N N   . LYS A 156 ? 0.3847 0.3803 0.2661 0.0258  -0.1018 -0.0394 155 LYS A N   
2409 C CA  . LYS A 156 ? 0.4274 0.4130 0.2768 0.0373  -0.1070 -0.0368 155 LYS A CA  
2410 C C   . LYS A 156 ? 0.4236 0.3941 0.2557 0.0433  -0.0923 -0.0247 155 LYS A C   
2411 O O   . LYS A 156 ? 0.4229 0.3840 0.2290 0.0534  -0.0946 -0.0193 155 LYS A O   
2412 C CB  . LYS A 156 ? 0.4626 0.4366 0.2876 0.0371  -0.1129 -0.0468 155 LYS A CB  
2413 C CG  . LYS A 156 ? 0.5582 0.5457 0.3923 0.0326  -0.1319 -0.0591 155 LYS A CG  
2414 C CD  . LYS A 156 ? 0.7267 0.6984 0.5313 0.0333  -0.1386 -0.0698 155 LYS A CD  
2415 C CE  . LYS A 156 ? 0.8939 0.8790 0.7086 0.0262  -0.1589 -0.0835 155 LYS A CE  
2416 N NZ  . LYS A 156 ? 1.0312 0.9968 0.8139 0.0265  -0.1661 -0.0957 155 LYS A NZ  
2430 N N   . LEU A 157 ? 0.4052 0.3729 0.2504 0.0371  -0.0777 -0.0205 156 LEU A N   
2431 C CA  . LEU A 157 ? 0.4588 0.4134 0.2888 0.0398  -0.0631 -0.0106 156 LEU A CA  
2432 C C   . LEU A 157 ? 0.4609 0.4143 0.2953 0.0428  -0.0600 -0.0002 156 LEU A C   
2433 O O   . LEU A 157 ? 0.4621 0.4032 0.2826 0.0437  -0.0487 0.0086  156 LEU A O   
2434 C CB  . LEU A 157 ? 0.4438 0.3981 0.2857 0.0324  -0.0499 -0.0113 156 LEU A CB  
2435 C CG  . LEU A 157 ? 0.4437 0.3946 0.2797 0.0304  -0.0520 -0.0218 156 LEU A CG  
2436 C CD1 . LEU A 157 ? 0.4693 0.4200 0.3165 0.0261  -0.0383 -0.0207 156 LEU A CD1 
2437 C CD2 . LEU A 157 ? 0.4535 0.3917 0.2548 0.0381  -0.0547 -0.0252 156 LEU A CD2 
2449 N N   . GLY A 158 ? 0.4459 0.4109 0.2975 0.0446  -0.0697 -0.0012 157 GLY A N   
2450 C CA  . GLY A 158 ? 0.4711 0.4314 0.3229 0.0500  -0.0683 0.0076  157 GLY A CA  
2451 C C   . GLY A 158 ? 0.4138 0.3873 0.2733 0.0582  -0.0833 0.0049  157 GLY A C   
2452 O O   . GLY A 158 ? 0.4191 0.4097 0.2908 0.0565  -0.0944 -0.0042 157 GLY A O   
2456 N N   . ASP A 159 ? 0.3716 0.3369 0.2241 0.0672  -0.0837 0.0128  158 ASP A N   
2457 C CA  . ASP A 159 ? 0.3753 0.3548 0.2377 0.0776  -0.0964 0.0116  158 ASP A CA  
2458 C C   . ASP A 159 ? 0.3727 0.3661 0.2663 0.0745  -0.0931 0.0107  158 ASP A C   
2459 O O   . ASP A 159 ? 0.3645 0.3805 0.2776 0.0796  -0.1029 0.0064  158 ASP A O   
2460 C CB  . ASP A 159 ? 0.4215 0.3805 0.2545 0.0923  -0.0986 0.0212  158 ASP A CB  
2461 C CG  . ASP A 159 ? 0.5236 0.4665 0.3204 0.0972  -0.1010 0.0236  158 ASP A CG  
2462 O OD1 . ASP A 159 ? 0.5289 0.4850 0.3232 0.0976  -0.1119 0.0152  158 ASP A OD1 
2463 O OD2 . ASP A 159 ? 0.5471 0.4629 0.3165 0.1003  -0.0915 0.0340  158 ASP A OD2 
2468 N N   . VAL A 160 ? 0.3420 0.3233 0.2397 0.0668  -0.0795 0.0147  159 VAL A N   
2469 C CA  . VAL A 160 ? 0.3267 0.3170 0.2490 0.0637  -0.0746 0.0140  159 VAL A CA  
2470 C C   . VAL A 160 ? 0.3019 0.2903 0.2335 0.0495  -0.0634 0.0123  159 VAL A C   
2471 O O   . VAL A 160 ? 0.3254 0.3011 0.2418 0.0444  -0.0575 0.0143  159 VAL A O   
2472 C CB  . VAL A 160 ? 0.4077 0.3794 0.3193 0.0728  -0.0711 0.0216  159 VAL A CB  
2473 C CG1 . VAL A 160 ? 0.4827 0.4564 0.3847 0.0898  -0.0825 0.0236  159 VAL A CG1 
2474 C CG2 . VAL A 160 ? 0.4719 0.4142 0.3594 0.0683  -0.0610 0.0291  159 VAL A CG2 
2484 N N   . TYR A 161 ? 0.2794 0.2817 0.2357 0.0442  -0.0604 0.0089  160 TYR A N   
2485 C CA  . TYR A 161 ? 0.2651 0.2685 0.2321 0.0325  -0.0514 0.0068  160 TYR A CA  
2486 C C   . TYR A 161 ? 0.2533 0.2507 0.2267 0.0313  -0.0437 0.0099  160 TYR A C   
2487 O O   . TYR A 161 ? 0.2496 0.2518 0.2309 0.0378  -0.0457 0.0103  160 TYR A O   
2488 C CB  . TYR A 161 ? 0.2649 0.2885 0.2529 0.0265  -0.0549 -0.0003 160 TYR A CB  
2489 C CG  . TYR A 161 ? 0.2507 0.2764 0.2512 0.0169  -0.0466 -0.0022 160 TYR A CG  
2490 C CD1 . TYR A 161 ? 0.2581 0.2758 0.2507 0.0110  -0.0423 -0.0036 160 TYR A CD1 
2491 C CD2 . TYR A 161 ? 0.2394 0.2754 0.2585 0.0153  -0.0431 -0.0025 160 TYR A CD2 
2492 C CE1 . TYR A 161 ? 0.2590 0.2780 0.2615 0.0044  -0.0357 -0.0051 160 TYR A CE1 
2493 C CE2 . TYR A 161 ? 0.2494 0.2858 0.2771 0.0077  -0.0359 -0.0035 160 TYR A CE2 
2494 C CZ  . TYR A 161 ? 0.2757 0.3034 0.2952 0.0027  -0.0328 -0.0047 160 TYR A CZ  
2495 O OH  . TYR A 161 ? 0.2968 0.3242 0.3234 -0.0026 -0.0265 -0.0054 160 TYR A OH  
2505 N N   . VAL A 162 ? 0.2430 0.2310 0.2128 0.0237  -0.0351 0.0117  161 VAL A N   
2506 C CA  . VAL A 162 ? 0.2471 0.2305 0.2233 0.0205  -0.0287 0.0130  161 VAL A CA  
2507 C C   . VAL A 162 ? 0.2400 0.2326 0.2283 0.0122  -0.0237 0.0098  161 VAL A C   
2508 O O   . VAL A 162 ? 0.2500 0.2421 0.2335 0.0080  -0.0214 0.0094  161 VAL A O   
2509 C CB  . VAL A 162 ? 0.3171 0.2795 0.2765 0.0189  -0.0239 0.0186  161 VAL A CB  
2510 C CG1 . VAL A 162 ? 0.3425 0.2997 0.3079 0.0140  -0.0187 0.0183  161 VAL A CG1 
2511 C CG2 . VAL A 162 ? 0.3443 0.2920 0.2866 0.0290  -0.0288 0.0230  161 VAL A CG2 
2521 N N   . ASN A 163 ? 0.2347 0.2343 0.2362 0.0112  -0.0216 0.0079  162 ASN A N   
2522 C CA  . ASN A 163 ? 0.2374 0.2422 0.2470 0.0048  -0.0165 0.0062  162 ASN A CA  
2523 C C   . ASN A 163 ? 0.2286 0.2262 0.2364 0.0027  -0.0124 0.0076  162 ASN A C   
2524 O O   . ASN A 163 ? 0.2277 0.2235 0.2376 0.0060  -0.0127 0.0071  162 ASN A O   
2525 C CB  . ASN A 163 ? 0.2715 0.2893 0.2957 0.0046  -0.0171 0.0032  162 ASN A CB  
2526 C CG  . ASN A 163 ? 0.3056 0.3256 0.3340 -0.0006 -0.0126 0.0019  162 ASN A CG  
2527 O OD1 . ASN A 163 ? 0.2702 0.2860 0.2950 -0.0023 -0.0088 0.0031  162 ASN A OD1 
2528 N ND2 . ASN A 163 ? 0.3422 0.3684 0.3780 -0.0031 -0.0135 -0.0004 162 ASN A ND2 
2535 N N   . ASP A 164 ? 0.2297 0.2240 0.2332 -0.0027 -0.0087 0.0089  163 ASP A N   
2536 C CA  . ASP A 164 ? 0.2583 0.2495 0.2627 -0.0070 -0.0058 0.0091  163 ASP A CA  
2537 C C   . ASP A 164 ? 0.2490 0.2517 0.2622 -0.0098 -0.0031 0.0071  163 ASP A C   
2538 O O   . ASP A 164 ? 0.2547 0.2592 0.2699 -0.0141 -0.0016 0.0068  163 ASP A O   
2539 C CB  . ASP A 164 ? 0.2968 0.2771 0.2916 -0.0121 -0.0035 0.0125  163 ASP A CB  
2540 C CG  . ASP A 164 ? 0.3631 0.3311 0.3543 -0.0151 -0.0039 0.0123  163 ASP A CG  
2541 O OD1 . ASP A 164 ? 0.3806 0.3465 0.3733 -0.0103 -0.0065 0.0095  163 ASP A OD1 
2542 O OD2 . ASP A 164 ? 0.4002 0.3606 0.3868 -0.0230 -0.0011 0.0145  163 ASP A OD2 
2547 N N   . ALA A 165 ? 0.2025 0.2127 0.2206 -0.0075 -0.0031 0.0057  164 ALA A N   
2548 C CA  . ALA A 165 ? 0.2048 0.2225 0.2276 -0.0080 -0.0004 0.0047  164 ALA A CA  
2549 C C   . ALA A 165 ? 0.2222 0.2429 0.2500 -0.0061 -0.0003 0.0036  164 ALA A C   
2550 O O   . ALA A 165 ? 0.2068 0.2291 0.2372 -0.0041 0.0007  0.0032  164 ALA A O   
2551 C CB  . ALA A 165 ? 0.2006 0.2188 0.2219 -0.0065 0.0001  0.0037  164 ALA A CB  
2557 N N   . PHE A 166 ? 0.2294 0.2488 0.2564 -0.0071 -0.0012 0.0031  165 PHE A N   
2558 C CA  . PHE A 166 ? 0.2026 0.2237 0.2305 -0.0040 -0.0012 0.0019  165 PHE A CA  
2559 C C   . PHE A 166 ? 0.2097 0.2370 0.2396 -0.0018 0.0007  0.0023  165 PHE A C   
2560 O O   . PHE A 166 ? 0.2561 0.2825 0.2854 0.0015  0.0026  0.0032  165 PHE A O   
2561 C CB  . PHE A 166 ? 0.2047 0.2220 0.2288 -0.0056 -0.0035 -0.0002 165 PHE A CB  
2562 C CG  . PHE A 166 ? 0.2066 0.2250 0.2280 -0.0012 -0.0037 -0.0018 165 PHE A CG  
2563 C CD1 . PHE A 166 ? 0.2421 0.2569 0.2611 0.0039  -0.0017 -0.0016 165 PHE A CD1 
2564 C CD2 . PHE A 166 ? 0.2383 0.2630 0.2591 -0.0012 -0.0055 -0.0032 165 PHE A CD2 
2565 C CE1 . PHE A 166 ? 0.2610 0.2761 0.2748 0.0087  -0.0004 -0.0024 165 PHE A CE1 
2566 C CE2 . PHE A 166 ? 0.2684 0.2928 0.2829 0.0042  -0.0059 -0.0044 165 PHE A CE2 
2567 C CZ  . PHE A 166 ? 0.2673 0.2857 0.2771 0.0090  -0.0027 -0.0037 165 PHE A CZ  
2577 N N   . GLY A 167 ? 0.2239 0.2574 0.2555 -0.0029 0.0008  0.0023  166 GLY A N   
2578 C CA  . GLY A 167 ? 0.2194 0.2581 0.2513 0.0018  0.0021  0.0029  166 GLY A CA  
2579 C C   . GLY A 167 ? 0.2315 0.2634 0.2610 0.0047  0.0050  0.0042  166 GLY A C   
2580 O O   . GLY A 167 ? 0.2157 0.2462 0.2422 0.0098  0.0065  0.0054  166 GLY A O   
2584 N N   . THR A 168 ? 0.2242 0.2507 0.2539 0.0016  0.0052  0.0039  167 THR A N   
2585 C CA  . THR A 168 ? 0.1956 0.2146 0.2234 0.0018  0.0068  0.0038  167 THR A CA  
2586 C C   . THR A 168 ? 0.1953 0.2121 0.2269 -0.0011 0.0069  0.0042  167 THR A C   
2587 O O   . THR A 168 ? 0.2278 0.2393 0.2602 -0.0036 0.0078  0.0038  167 THR A O   
2588 C CB  . THR A 168 ? 0.2308 0.2475 0.2557 0.0005  0.0061  0.0020  167 THR A CB  
2589 O OG1 . THR A 168 ? 0.2618 0.2849 0.2854 0.0032  0.0076  0.0022  167 THR A OG1 
2590 C CG2 . THR A 168 ? 0.2350 0.2415 0.2555 0.0007  0.0070  0.0005  167 THR A CG2 
2598 N N   . ALA A 169 ? 0.2152 0.2363 0.2494 -0.0009 0.0062  0.0046  168 ALA A N   
2599 C CA  . ALA A 169 ? 0.2475 0.2711 0.2876 -0.0024 0.0064  0.0047  168 ALA A CA  
2600 C C   . ALA A 169 ? 0.2538 0.2762 0.2962 -0.0033 0.0112  0.0068  168 ALA A C   
2601 O O   . ALA A 169 ? 0.2386 0.2664 0.2893 -0.0061 0.0124  0.0069  168 ALA A O   
2602 C CB  . ALA A 169 ? 0.2814 0.3076 0.3211 0.0003  0.0051  0.0043  168 ALA A CB  
2608 N N   . HIS A 170 ? 0.2453 0.2614 0.2809 -0.0009 0.0143  0.0089  169 HIS A N   
2609 C CA  . HIS A 170 ? 0.2462 0.2563 0.2807 -0.0024 0.0201  0.0122  169 HIS A CA  
2610 C C   . HIS A 170 ? 0.2382 0.2392 0.2737 -0.0082 0.0207  0.0115  169 HIS A C   
2611 O O   . HIS A 170 ? 0.2514 0.2446 0.2862 -0.0120 0.0261  0.0146  169 HIS A O   
2612 C CB  . HIS A 170 ? 0.2483 0.2521 0.2712 0.0042  0.0228  0.0154  169 HIS A CB  
2613 C CG  . HIS A 170 ? 0.2439 0.2442 0.2604 0.0089  0.0196  0.0144  169 HIS A CG  
2614 N ND1 . HIS A 170 ? 0.2485 0.2561 0.2685 0.0089  0.0147  0.0108  169 HIS A ND1 
2615 C CD2 . HIS A 170 ? 0.2804 0.2718 0.2869 0.0150  0.0213  0.0170  169 HIS A CD2 
2616 C CE1 . HIS A 170 ? 0.2622 0.2689 0.2772 0.0143  0.0139  0.0109  169 HIS A CE1 
2617 N NE2 . HIS A 170 ? 0.2702 0.2670 0.2767 0.0191  0.0173  0.0144  169 HIS A NE2 
2625 N N   . ARG A 171 ? 0.2183 0.2184 0.2538 -0.0095 0.0157  0.0077  170 ARG A N   
2626 C CA  . ARG A 171 ? 0.2537 0.2421 0.2865 -0.0142 0.0151  0.0053  170 ARG A CA  
2627 C C   . ARG A 171 ? 0.2632 0.2594 0.3067 -0.0220 0.0109  0.0017  170 ARG A C   
2628 O O   . ARG A 171 ? 0.2530 0.2588 0.2993 -0.0204 0.0057  -0.0007 170 ARG A O   
2629 C CB  . ARG A 171 ? 0.2535 0.2356 0.2766 -0.0090 0.0126  0.0027  170 ARG A CB  
2630 C CG  . ARG A 171 ? 0.2667 0.2462 0.2818 -0.0001 0.0153  0.0055  170 ARG A CG  
2631 C CD  . ARG A 171 ? 0.2844 0.2491 0.2921 0.0015  0.0203  0.0094  170 ARG A CD  
2632 N NE  . ARG A 171 ? 0.2843 0.2458 0.2824 0.0125  0.0212  0.0113  170 ARG A NE  
2633 C CZ  . ARG A 171 ? 0.3005 0.2527 0.2899 0.0181  0.0248  0.0162  170 ARG A CZ  
2634 N NH1 . ARG A 171 ? 0.3233 0.2673 0.3118 0.0126  0.0293  0.0201  170 ARG A NH1 
2635 N NH2 . ARG A 171 ? 0.3377 0.2898 0.3190 0.0298  0.0242  0.0176  170 ARG A NH2 
2649 N N   . ALA A 172 ? 0.2701 0.2616 0.3189 -0.0305 0.0127  0.0014  171 ALA A N   
2650 C CA  . ALA A 172 ? 0.3062 0.3078 0.3670 -0.0387 0.0070  -0.0031 171 ALA A CA  
2651 C C   . ALA A 172 ? 0.3088 0.2976 0.3601 -0.0411 0.0009  -0.0093 171 ALA A C   
2652 O O   . ALA A 172 ? 0.3379 0.3189 0.3912 -0.0506 -0.0010 -0.0129 171 ALA A O   
2653 C CB  . ALA A 172 ? 0.3350 0.3412 0.4090 -0.0490 0.0117  -0.0012 171 ALA A CB  
2659 N N   . HIS A 173 ? 0.2596 0.2460 0.2998 -0.0329 -0.0019 -0.0107 172 HIS A N   
2660 C CA  . HIS A 173 ? 0.2842 0.2573 0.3111 -0.0322 -0.0062 -0.0162 172 HIS A CA  
2661 C C   . HIS A 173 ? 0.2816 0.2660 0.3111 -0.0336 -0.0151 -0.0208 172 HIS A C   
2662 O O   . HIS A 173 ? 0.2545 0.2563 0.2946 -0.0325 -0.0175 -0.0188 172 HIS A O   
2663 C CB  . HIS A 173 ? 0.2909 0.2567 0.3041 -0.0216 -0.0024 -0.0144 172 HIS A CB  
2664 C CG  . HIS A 173 ? 0.2925 0.2454 0.3001 -0.0182 0.0044  -0.0108 172 HIS A CG  
2665 N ND1 . HIS A 173 ? 0.2897 0.2408 0.2889 -0.0079 0.0079  -0.0086 172 HIS A ND1 
2666 C CD2 . HIS A 173 ? 0.3011 0.2428 0.3099 -0.0232 0.0084  -0.0085 172 HIS A CD2 
2667 C CE1 . HIS A 173 ? 0.3116 0.2498 0.3054 -0.0050 0.0127  -0.0054 172 HIS A CE1 
2668 N NE2 . HIS A 173 ? 0.3061 0.2366 0.3043 -0.0144 0.0136  -0.0047 172 HIS A NE2 
2676 N N   . SER A 174 ? 0.3028 0.2758 0.3206 -0.0352 -0.0204 -0.0273 173 SER A N   
2677 C CA  . SER A 174 ? 0.2803 0.2631 0.2987 -0.0367 -0.0303 -0.0322 173 SER A CA  
2678 C C   . SER A 174 ? 0.2851 0.2808 0.3023 -0.0281 -0.0313 -0.0281 173 SER A C   
2679 O O   . SER A 174 ? 0.2777 0.2886 0.3039 -0.0282 -0.0375 -0.0281 173 SER A O   
2680 C CB  . SER A 174 ? 0.3049 0.2702 0.3040 -0.0367 -0.0355 -0.0400 173 SER A CB  
2681 O OG  . SER A 174 ? 0.3220 0.2749 0.3234 -0.0472 -0.0372 -0.0452 173 SER A OG  
2687 N N   . SER A 175 ? 0.2757 0.2650 0.2810 -0.0205 -0.0256 -0.0246 174 SER A N   
2688 C CA  . SER A 175 ? 0.2613 0.2585 0.2633 -0.0143 -0.0256 -0.0204 174 SER A CA  
2689 C C   . SER A 175 ? 0.2943 0.3038 0.3110 -0.0139 -0.0237 -0.0153 174 SER A C   
2690 O O   . SER A 175 ? 0.2894 0.3033 0.3037 -0.0096 -0.0254 -0.0123 174 SER A O   
2691 C CB  . SER A 175 ? 0.2696 0.2596 0.2592 -0.0086 -0.0185 -0.0177 174 SER A CB  
2692 O OG  . SER A 175 ? 0.2648 0.2560 0.2622 -0.0082 -0.0116 -0.0142 174 SER A OG  
2698 N N   . MET A 176 ? 0.2680 0.2804 0.2970 -0.0177 -0.0198 -0.0140 175 MET A N   
2699 C CA  . MET A 176 ? 0.2607 0.2830 0.3008 -0.0161 -0.0166 -0.0097 175 MET A CA  
2700 C C   . MET A 176 ? 0.2955 0.3322 0.3510 -0.0189 -0.0204 -0.0107 175 MET A C   
2701 O O   . MET A 176 ? 0.3385 0.3841 0.3999 -0.0144 -0.0198 -0.0079 175 MET A O   
2702 C CB  . MET A 176 ? 0.2550 0.2724 0.2967 -0.0167 -0.0090 -0.0070 175 MET A CB  
2703 C CG  . MET A 176 ? 0.2710 0.2799 0.3012 -0.0124 -0.0053 -0.0057 175 MET A CG  
2704 S SD  . MET A 176 ? 0.2693 0.2835 0.2968 -0.0079 -0.0047 -0.0025 175 MET A SD  
2705 C CE  . MET A 176 ? 0.2792 0.2995 0.3161 -0.0074 -0.0024 0.0000  175 MET A CE  
2715 N N   . VAL A 177 ? 0.2536 0.2932 0.3162 -0.0262 -0.0240 -0.0149 176 VAL A N   
2716 C CA  . VAL A 177 ? 0.2705 0.3291 0.3525 -0.0304 -0.0266 -0.0158 176 VAL A CA  
2717 C C   . VAL A 177 ? 0.2937 0.3600 0.3794 -0.0348 -0.0375 -0.0221 176 VAL A C   
2718 O O   . VAL A 177 ? 0.3084 0.3958 0.4125 -0.0376 -0.0419 -0.0238 176 VAL A O   
2719 C CB  . VAL A 177 ? 0.2854 0.3448 0.3790 -0.0385 -0.0186 -0.0139 176 VAL A CB  
2720 C CG1 . VAL A 177 ? 0.3027 0.3553 0.3907 -0.0328 -0.0091 -0.0079 176 VAL A CG1 
2721 C CG2 . VAL A 177 ? 0.2867 0.3300 0.3749 -0.0483 -0.0189 -0.0176 176 VAL A CG2 
2731 N N   . GLY A 178 ? 0.2778 0.3289 0.3462 -0.0348 -0.0422 -0.0262 177 GLY A N   
2732 C CA  . GLY A 178 ? 0.2980 0.3526 0.3663 -0.0401 -0.0532 -0.0338 177 GLY A CA  
2733 C C   . GLY A 178 ? 0.3107 0.3688 0.3666 -0.0315 -0.0632 -0.0357 177 GLY A C   
2734 O O   . GLY A 178 ? 0.3200 0.3802 0.3727 -0.0350 -0.0738 -0.0428 177 GLY A O   
2738 N N   . VAL A 179 ? 0.3071 0.3639 0.3541 -0.0205 -0.0605 -0.0297 178 VAL A N   
2739 C CA  . VAL A 179 ? 0.3247 0.3807 0.3561 -0.0115 -0.0687 -0.0299 178 VAL A CA  
2740 C C   . VAL A 179 ? 0.3609 0.4406 0.4081 -0.0078 -0.0783 -0.0308 178 VAL A C   
2741 O O   . VAL A 179 ? 0.4275 0.5206 0.4914 -0.0051 -0.0742 -0.0268 178 VAL A O   
2742 C CB  . VAL A 179 ? 0.3259 0.3685 0.3409 -0.0029 -0.0612 -0.0225 178 VAL A CB  
2743 C CG1 . VAL A 179 ? 0.3393 0.3795 0.3373 0.0068  -0.0684 -0.0207 178 VAL A CG1 
2744 C CG2 . VAL A 179 ? 0.3508 0.3755 0.3518 -0.0054 -0.0530 -0.0223 178 VAL A CG2 
2754 N N   . ASN A 180 ? 0.3317 0.4177 0.3734 -0.0068 -0.0913 -0.0367 179 ASN A N   
2755 C CA  . ASN A 180 ? 0.3838 0.4968 0.4425 -0.0032 -0.1029 -0.0392 179 ASN A CA  
2756 C C   . ASN A 180 ? 0.3542 0.4632 0.3928 0.0129  -0.1094 -0.0351 179 ASN A C   
2757 O O   . ASN A 180 ? 0.3877 0.4924 0.4081 0.0168  -0.1203 -0.0390 179 ASN A O   
2758 C CB  . ASN A 180 ? 0.5476 0.6723 0.6153 -0.0141 -0.1150 -0.0496 179 ASN A CB  
2759 C CG  . ASN A 180 ? 0.7031 0.8593 0.7875 -0.0092 -0.1296 -0.0531 179 ASN A CG  
2760 O OD1 . ASN A 180 ? 0.7625 0.9369 0.8609 0.0005  -0.1283 -0.0477 179 ASN A OD1 
2761 N ND2 . ASN A 180 ? 0.7628 0.9261 0.8450 -0.0148 -0.1444 -0.0627 179 ASN A ND2 
2768 N N   . LEU A 181 ? 0.3271 0.4338 0.3657 0.0224  -0.1024 -0.0271 180 LEU A N   
2769 C CA  . LEU A 181 ? 0.3253 0.4269 0.3469 0.0383  -0.1073 -0.0217 180 LEU A CA  
2770 C C   . LEU A 181 ? 0.3424 0.4628 0.3839 0.0471  -0.1068 -0.0184 180 LEU A C   
2771 O O   . LEU A 181 ? 0.3472 0.4763 0.4092 0.0410  -0.0978 -0.0180 180 LEU A O   
2772 C CB  . LEU A 181 ? 0.3310 0.4012 0.3250 0.0417  -0.0970 -0.0144 180 LEU A CB  
2773 C CG  . LEU A 181 ? 0.3668 0.4187 0.3362 0.0378  -0.0973 -0.0166 180 LEU A CG  
2774 C CD1 . LEU A 181 ? 0.3386 0.3649 0.2874 0.0384  -0.0843 -0.0090 180 LEU A CD1 
2775 C CD2 . LEU A 181 ? 0.4322 0.4866 0.3838 0.0466  -0.1120 -0.0195 180 LEU A CD2 
2787 N N   . PRO A 182 ? 0.3832 0.5095 0.4174 0.0629  -0.1161 -0.0160 181 PRO A N   
2788 C CA  . PRO A 182 ? 0.3990 0.5470 0.4539 0.0735  -0.1165 -0.0141 181 PRO A CA  
2789 C C   . PRO A 182 ? 0.3966 0.5270 0.4479 0.0773  -0.1025 -0.0076 181 PRO A C   
2790 O O   . PRO A 182 ? 0.4023 0.5512 0.4751 0.0811  -0.0985 -0.0076 181 PRO A O   
2791 C CB  . PRO A 182 ? 0.4431 0.5942 0.4830 0.0921  -0.1300 -0.0123 181 PRO A CB  
2792 C CG  . PRO A 182 ? 0.5025 0.6466 0.5239 0.0875  -0.1401 -0.0164 181 PRO A CG  
2793 C CD  . PRO A 182 ? 0.4539 0.5723 0.4629 0.0724  -0.1283 -0.0162 181 PRO A CD  
2801 N N   . GLN A 183 ? 0.3280 0.4242 0.3528 0.0764  -0.0950 -0.0024 182 GLN A N   
2802 C CA  . GLN A 183 ? 0.2986 0.3760 0.3182 0.0783  -0.0831 0.0026  182 GLN A CA  
2803 C C   . GLN A 183 ? 0.3329 0.3964 0.3503 0.0626  -0.0728 0.0023  182 GLN A C   
2804 O O   . GLN A 183 ? 0.2966 0.3433 0.2958 0.0573  -0.0722 0.0034  182 GLN A O   
2805 C CB  . GLN A 183 ? 0.3272 0.3757 0.3178 0.0915  -0.0834 0.0096  182 GLN A CB  
2806 C CG  . GLN A 183 ? 0.4195 0.4786 0.4109 0.1111  -0.0922 0.0110  182 GLN A CG  
2807 C CD  . GLN A 183 ? 0.5672 0.5910 0.5256 0.1241  -0.0918 0.0188  182 GLN A CD  
2808 O OE1 . GLN A 183 ? 0.6487 0.6553 0.5829 0.1257  -0.0959 0.0224  182 GLN A OE1 
2809 N NE2 . GLN A 183 ? 0.5934 0.6036 0.5487 0.1332  -0.0861 0.0215  182 GLN A NE2 
2818 N N   . LYS A 184 ? 0.2734 0.3447 0.3082 0.0566  -0.0645 0.0011  183 LYS A N   
2819 C CA  . LYS A 184 ? 0.2419 0.3027 0.2767 0.0438  -0.0550 0.0008  183 LYS A CA  
2820 C C   . LYS A 184 ? 0.2462 0.2952 0.2785 0.0467  -0.0465 0.0038  183 LYS A C   
2821 O O   . LYS A 184 ? 0.2494 0.3123 0.2970 0.0499  -0.0436 0.0026  183 LYS A O   
2822 C CB  . LYS A 184 ? 0.2423 0.3234 0.2990 0.0330  -0.0540 -0.0040 183 LYS A CB  
2823 C CG  . LYS A 184 ? 0.2707 0.3615 0.3285 0.0289  -0.0640 -0.0087 183 LYS A CG  
2824 C CD  . LYS A 184 ? 0.3545 0.4653 0.4355 0.0176  -0.0643 -0.0138 183 LYS A CD  
2825 C CE  . LYS A 184 ? 0.4733 0.6131 0.5792 0.0217  -0.0663 -0.0147 183 LYS A CE  
2826 N NZ  . LYS A 184 ? 0.5531 0.7126 0.6832 0.0081  -0.0650 -0.0189 183 LYS A NZ  
2840 N N   . ALA A 185 ? 0.2603 0.2844 0.2737 0.0447  -0.0422 0.0072  184 ALA A N   
2841 C CA  . ALA A 185 ? 0.2554 0.2637 0.2618 0.0480  -0.0365 0.0093  184 ALA A CA  
2842 C C   . ALA A 185 ? 0.2383 0.2386 0.2443 0.0366  -0.0290 0.0089  184 ALA A C   
2843 O O   . ALA A 185 ? 0.2497 0.2471 0.2519 0.0282  -0.0276 0.0093  184 ALA A O   
2844 C CB  . ALA A 185 ? 0.3266 0.3098 0.3098 0.0558  -0.0387 0.0140  184 ALA A CB  
2850 N N   . GLY A 186 ? 0.2492 0.2456 0.2573 0.0379  -0.0246 0.0079  185 GLY A N   
2851 C CA  . GLY A 186 ? 0.2563 0.2455 0.2626 0.0287  -0.0191 0.0072  185 GLY A CA  
2852 C C   . GLY A 186 ? 0.2790 0.2444 0.2680 0.0255  -0.0183 0.0098  185 GLY A C   
2853 O O   . GLY A 186 ? 0.3008 0.2494 0.2773 0.0324  -0.0201 0.0116  185 GLY A O   
2857 N N   . GLY A 187 ? 0.2689 0.2330 0.2575 0.0151  -0.0152 0.0102  186 GLY A N   
2858 C CA  . GLY A 187 ? 0.3057 0.2512 0.2817 0.0088  -0.0131 0.0128  186 GLY A CA  
2859 C C   . GLY A 187 ? 0.3103 0.2459 0.2844 0.0055  -0.0118 0.0099  186 GLY A C   
2860 O O   . GLY A 187 ? 0.2739 0.2165 0.2542 0.0095  -0.0120 0.0061  186 GLY A O   
2864 N N   . PHE A 188 ? 0.3026 0.2210 0.2669 -0.0028 -0.0101 0.0117  187 PHE A N   
2865 C CA  . PHE A 188 ? 0.3318 0.2360 0.2910 -0.0067 -0.0105 0.0080  187 PHE A CA  
2866 C C   . PHE A 188 ? 0.3085 0.2299 0.2801 -0.0136 -0.0102 0.0034  187 PHE A C   
2867 O O   . PHE A 188 ? 0.3000 0.2151 0.2686 -0.0131 -0.0121 -0.0015 187 PHE A O   
2868 C CB  . PHE A 188 ? 0.3446 0.2242 0.2901 -0.0157 -0.0090 0.0113  187 PHE A CB  
2869 C CG  . PHE A 188 ? 0.3751 0.2313 0.3030 -0.0069 -0.0098 0.0162  187 PHE A CG  
2870 C CD1 . PHE A 188 ? 0.4334 0.2841 0.3561 0.0086  -0.0132 0.0146  187 PHE A CD1 
2871 C CD2 . PHE A 188 ? 0.4013 0.2412 0.3171 -0.0132 -0.0067 0.0229  187 PHE A CD2 
2872 C CE1 . PHE A 188 ? 0.4847 0.3146 0.3905 0.0191  -0.0148 0.0194  187 PHE A CE1 
2873 C CE2 . PHE A 188 ? 0.4447 0.2608 0.3412 -0.0036 -0.0077 0.0283  187 PHE A CE2 
2874 C CZ  . PHE A 188 ? 0.4451 0.2565 0.3367 0.0132  -0.0125 0.0263  187 PHE A CZ  
2884 N N   . LEU A 189 ? 0.2787 0.2198 0.2618 -0.0188 -0.0081 0.0048  188 LEU A N   
2885 C CA  . LEU A 189 ? 0.2923 0.2509 0.2865 -0.0220 -0.0084 0.0010  188 LEU A CA  
2886 C C   . LEU A 189 ? 0.2703 0.2376 0.2681 -0.0122 -0.0091 -0.0013 188 LEU A C   
2887 O O   . LEU A 189 ? 0.2622 0.2326 0.2604 -0.0112 -0.0104 -0.0051 188 LEU A O   
2888 C CB  . LEU A 189 ? 0.2857 0.2618 0.2897 -0.0272 -0.0054 0.0035  188 LEU A CB  
2889 C CG  . LEU A 189 ? 0.2937 0.2885 0.3084 -0.0281 -0.0060 0.0004  188 LEU A CG  
2890 C CD1 . LEU A 189 ? 0.3164 0.3100 0.3316 -0.0351 -0.0094 -0.0038 188 LEU A CD1 
2891 C CD2 . LEU A 189 ? 0.3172 0.3279 0.3400 -0.0300 -0.0024 0.0030  188 LEU A CD2 
2903 N N   . MET A 190 ? 0.2669 0.2393 0.2674 -0.0056 -0.0082 0.0011  189 MET A N   
2904 C CA  . MET A 190 ? 0.2794 0.2609 0.2851 0.0021  -0.0076 -0.0002 189 MET A CA  
2905 C C   . MET A 190 ? 0.3000 0.2711 0.2980 0.0084  -0.0082 -0.0031 189 MET A C   
2906 O O   . MET A 190 ? 0.2941 0.2707 0.2930 0.0120  -0.0067 -0.0054 189 MET A O   
2907 C CB  . MET A 190 ? 0.3042 0.2926 0.3149 0.0063  -0.0077 0.0022  189 MET A CB  
2908 C CG  . MET A 190 ? 0.3193 0.3214 0.3397 0.0108  -0.0060 0.0016  189 MET A CG  
2909 S SD  . MET A 190 ? 0.3070 0.3200 0.3348 0.0052  -0.0031 0.0019  189 MET A SD  
2910 C CE  . MET A 190 ? 0.3447 0.3605 0.3748 0.0019  -0.0049 0.0031  189 MET A CE  
2920 N N   . LYS A 191 ? 0.2866 0.2399 0.2741 0.0110  -0.0100 -0.0029 190 LYS A N   
2921 C CA  . LYS A 191 ? 0.3087 0.2482 0.2857 0.0188  -0.0105 -0.0063 190 LYS A CA  
2922 C C   . LYS A 191 ? 0.3372 0.2683 0.3071 0.0133  -0.0119 -0.0114 190 LYS A C   
2923 O O   . LYS A 191 ? 0.3323 0.2626 0.2971 0.0199  -0.0112 -0.0153 190 LYS A O   
2924 C CB  . LYS A 191 ? 0.3783 0.2962 0.3427 0.0234  -0.0124 -0.0046 190 LYS A CB  
2925 C CG  . LYS A 191 ? 0.5306 0.4273 0.4798 0.0321  -0.0130 -0.0088 190 LYS A CG  
2926 C CD  . LYS A 191 ? 0.6770 0.5466 0.6103 0.0369  -0.0149 -0.0064 190 LYS A CD  
2927 C CE  . LYS A 191 ? 0.6783 0.5592 0.6171 0.0488  -0.0154 -0.0019 190 LYS A CE  
2928 N NZ  . LYS A 191 ? 0.7678 0.6201 0.6874 0.0591  -0.0175 0.0001  190 LYS A NZ  
2942 N N   . LYS A 192 ? 0.3203 0.2463 0.2895 0.0011  -0.0139 -0.0115 191 LYS A N   
2943 C CA  . LYS A 192 ? 0.3211 0.2411 0.2851 -0.0059 -0.0172 -0.0172 191 LYS A CA  
2944 C C   . LYS A 192 ? 0.2885 0.2280 0.2588 -0.0031 -0.0172 -0.0195 191 LYS A C   
2945 O O   . LYS A 192 ? 0.2963 0.2302 0.2573 0.0001  -0.0195 -0.0250 191 LYS A O   
2946 C CB  . LYS A 192 ? 0.3993 0.3181 0.3674 -0.0208 -0.0185 -0.0159 191 LYS A CB  
2947 C CG  . LYS A 192 ? 0.6066 0.5284 0.5758 -0.0308 -0.0231 -0.0219 191 LYS A CG  
2948 C CD  . LYS A 192 ? 0.8023 0.7288 0.7804 -0.0465 -0.0227 -0.0196 191 LYS A CD  
2949 C CE  . LYS A 192 ? 1.0142 0.9507 0.9982 -0.0571 -0.0285 -0.0262 191 LYS A CE  
2950 N NZ  . LYS A 192 ? 1.1409 1.0821 1.1348 -0.0743 -0.0276 -0.0245 191 LYS A NZ  
2964 N N   . GLU A 193 ? 0.2728 0.2328 0.2565 -0.0036 -0.0146 -0.0153 192 GLU A N   
2965 C CA  . GLU A 193 ? 0.2719 0.2476 0.2597 -0.0006 -0.0141 -0.0160 192 GLU A CA  
2966 C C   . GLU A 193 ? 0.2758 0.2513 0.2584 0.0105  -0.0105 -0.0161 192 GLU A C   
2967 O O   . GLU A 193 ? 0.2747 0.2512 0.2497 0.0147  -0.0110 -0.0190 192 GLU A O   
2968 C CB  . GLU A 193 ? 0.2494 0.2419 0.2501 -0.0032 -0.0117 -0.0114 192 GLU A CB  
2969 C CG  . GLU A 193 ? 0.3043 0.3023 0.3116 -0.0130 -0.0137 -0.0111 192 GLU A CG  
2970 C CD  . GLU A 193 ? 0.3918 0.4045 0.4040 -0.0156 -0.0170 -0.0135 192 GLU A CD  
2971 O OE1 . GLU A 193 ? 0.4121 0.4253 0.4179 -0.0107 -0.0198 -0.0167 192 GLU A OE1 
2972 O OE2 . GLU A 193 ? 0.3744 0.3992 0.3965 -0.0216 -0.0167 -0.0120 192 GLU A OE2 
2979 N N   . LEU A 194 ? 0.2471 0.2236 0.2339 0.0158  -0.0066 -0.0128 193 LEU A N   
2980 C CA  . LEU A 194 ? 0.2688 0.2494 0.2541 0.0258  -0.0016 -0.0124 193 LEU A CA  
2981 C C   . LEU A 194 ? 0.3156 0.2811 0.2848 0.0328  -0.0025 -0.0177 193 LEU A C   
2982 O O   . LEU A 194 ? 0.2982 0.2665 0.2608 0.0402  0.0013  -0.0189 193 LEU A O   
2983 C CB  . LEU A 194 ? 0.2988 0.2871 0.2948 0.0293  0.0014  -0.0086 193 LEU A CB  
2984 C CG  . LEU A 194 ? 0.4018 0.4043 0.4118 0.0236  0.0026  -0.0044 193 LEU A CG  
2985 C CD1 . LEU A 194 ? 0.4989 0.5077 0.5177 0.0267  0.0027  -0.0025 193 LEU A CD1 
2986 C CD2 . LEU A 194 ? 0.3779 0.3910 0.3921 0.0239  0.0077  -0.0024 193 LEU A CD2 
2998 N N   . ASN A 195 ? 0.3414 0.2880 0.3015 0.0310  -0.0069 -0.0210 194 ASN A N   
2999 C CA  . ASN A 195 ? 0.3752 0.3026 0.3169 0.0381  -0.0081 -0.0272 194 ASN A CA  
3000 C C   . ASN A 195 ? 0.3717 0.2958 0.3028 0.0343  -0.0122 -0.0329 194 ASN A C   
3001 O O   . ASN A 195 ? 0.3869 0.3043 0.3034 0.0433  -0.0109 -0.0374 194 ASN A O   
3002 C CB  . ASN A 195 ? 0.4471 0.3500 0.3791 0.0363  -0.0119 -0.0290 194 ASN A CB  
3003 C CG  . ASN A 195 ? 0.5784 0.4807 0.5133 0.0470  -0.0085 -0.0250 194 ASN A CG  
3004 O OD1 . ASN A 195 ? 0.6187 0.5378 0.5612 0.0572  -0.0033 -0.0231 194 ASN A OD1 
3005 N ND2 . ASN A 195 ? 0.6486 0.5320 0.5773 0.0448  -0.0114 -0.0236 194 ASN A ND2 
3012 N N   . TYR A 196 ? 0.3212 0.2513 0.2591 0.0221  -0.0173 -0.0331 195 TYR A N   
3013 C CA  . TYR A 196 ? 0.3170 0.2487 0.2471 0.0189  -0.0229 -0.0386 195 TYR A CA  
3014 C C   . TYR A 196 ? 0.3217 0.2671 0.2490 0.0287  -0.0184 -0.0365 195 TYR A C   
3015 O O   . TYR A 196 ? 0.3437 0.2820 0.2538 0.0354  -0.0199 -0.0418 195 TYR A O   
3016 C CB  . TYR A 196 ? 0.2956 0.2391 0.2389 0.0052  -0.0282 -0.0380 195 TYR A CB  
3017 C CG  . TYR A 196 ? 0.3397 0.2871 0.2762 0.0026  -0.0357 -0.0444 195 TYR A CG  
3018 C CD1 . TYR A 196 ? 0.3934 0.3241 0.3185 -0.0045 -0.0436 -0.0532 195 TYR A CD1 
3019 C CD2 . TYR A 196 ? 0.4058 0.3712 0.3442 0.0083  -0.0355 -0.0423 195 TYR A CD2 
3020 C CE1 . TYR A 196 ? 0.4635 0.3988 0.3809 -0.0063 -0.0524 -0.0606 195 TYR A CE1 
3021 C CE2 . TYR A 196 ? 0.4213 0.3908 0.3507 0.0085  -0.0437 -0.0485 195 TYR A CE2 
3022 C CZ  . TYR A 196 ? 0.4721 0.4282 0.3918 0.0010  -0.0527 -0.0580 195 TYR A CZ  
3023 O OH  . TYR A 196 ? 0.5369 0.4990 0.4479 0.0008  -0.0626 -0.0652 195 TYR A OH  
3033 N N   . PHE A 197 ? 0.3092 0.2721 0.2513 0.0295  -0.0126 -0.0288 196 PHE A N   
3034 C CA  . PHE A 197 ? 0.3123 0.2854 0.2508 0.0371  -0.0074 -0.0255 196 PHE A CA  
3035 C C   . PHE A 197 ? 0.3488 0.3169 0.2770 0.0486  0.0003  -0.0255 196 PHE A C   
3036 O O   . PHE A 197 ? 0.3497 0.3181 0.2643 0.0561  0.0033  -0.0257 196 PHE A O   
3037 C CB  . PHE A 197 ? 0.3016 0.2901 0.2569 0.0340  -0.0029 -0.0176 196 PHE A CB  
3038 C CG  . PHE A 197 ? 0.3075 0.3042 0.2683 0.0277  -0.0088 -0.0174 196 PHE A CG  
3039 C CD1 . PHE A 197 ? 0.3489 0.3495 0.2999 0.0320  -0.0115 -0.0181 196 PHE A CD1 
3040 C CD2 . PHE A 197 ? 0.2935 0.2950 0.2682 0.0188  -0.0115 -0.0165 196 PHE A CD2 
3041 C CE1 . PHE A 197 ? 0.3483 0.3597 0.3056 0.0284  -0.0175 -0.0181 196 PHE A CE1 
3042 C CE2 . PHE A 197 ? 0.2958 0.3081 0.2769 0.0145  -0.0161 -0.0165 196 PHE A CE2 
3043 C CZ  . PHE A 197 ? 0.3244 0.3427 0.2977 0.0197  -0.0195 -0.0175 196 PHE A CZ  
3053 N N   . ALA A 198 ? 0.3477 0.3119 0.2810 0.0515  0.0038  -0.0250 197 ALA A N   
3054 C CA  . ALA A 198 ? 0.3979 0.3601 0.3228 0.0641  0.0115  -0.0255 197 ALA A CA  
3055 C C   . ALA A 198 ? 0.4199 0.3651 0.3191 0.0713  0.0086  -0.0335 197 ALA A C   
3056 O O   . ALA A 198 ? 0.4562 0.4033 0.3433 0.0818  0.0157  -0.0333 197 ALA A O   
3057 C CB  . ALA A 198 ? 0.4366 0.3966 0.3699 0.0677  0.0131  -0.0250 197 ALA A CB  
3063 N N   . LYS A 199 ? 0.4034 0.3308 0.2930 0.0653  -0.0015 -0.0408 198 LYS A N   
3064 C CA  . LYS A 199 ? 0.4637 0.3715 0.3274 0.0704  -0.0065 -0.0503 198 LYS A CA  
3065 C C   . LYS A 199 ? 0.4416 0.3566 0.2954 0.0697  -0.0102 -0.0518 198 LYS A C   
3066 O O   . LYS A 199 ? 0.4702 0.3778 0.3016 0.0802  -0.0086 -0.0561 198 LYS A O   
3067 C CB  . LYS A 199 ? 0.6206 0.5063 0.4787 0.0611  -0.0165 -0.0575 198 LYS A CB  
3068 C CG  . LYS A 199 ? 0.9508 0.8122 0.7809 0.0639  -0.0237 -0.0693 198 LYS A CG  
3069 C CD  . LYS A 199 ? 1.2047 1.0409 1.0298 0.0523  -0.0328 -0.0759 198 LYS A CD  
3070 C CE  . LYS A 199 ? 1.3707 1.1813 1.1675 0.0525  -0.0418 -0.0892 198 LYS A CE  
3071 N NZ  . LYS A 199 ? 1.4482 1.2300 1.2389 0.0394  -0.0499 -0.0958 198 LYS A NZ  
3085 N N   . ALA A 200 ? 0.3836 0.3132 0.2524 0.0592  -0.0151 -0.0481 199 ALA A N   
3086 C CA  . ALA A 200 ? 0.4042 0.3409 0.2636 0.0596  -0.0207 -0.0496 199 ALA A CA  
3087 C C   . ALA A 200 ? 0.4000 0.3469 0.2537 0.0703  -0.0104 -0.0419 199 ALA A C   
3088 O O   . ALA A 200 ? 0.4475 0.3940 0.2827 0.0766  -0.0132 -0.0436 199 ALA A O   
3089 C CB  . ALA A 200 ? 0.4151 0.3663 0.2940 0.0470  -0.0281 -0.0476 199 ALA A CB  
3095 N N   . LEU A 201 ? 0.3846 0.3405 0.2534 0.0721  0.0012  -0.0333 200 LEU A N   
3096 C CA  . LEU A 201 ? 0.4111 0.3761 0.2769 0.0794  0.0126  -0.0248 200 LEU A CA  
3097 C C   . LEU A 201 ? 0.4437 0.4047 0.2965 0.0914  0.0240  -0.0245 200 LEU A C   
3098 O O   . LEU A 201 ? 0.4595 0.4264 0.3056 0.0976  0.0346  -0.0176 200 LEU A O   
3099 C CB  . LEU A 201 ? 0.3996 0.3785 0.2908 0.0722  0.0187  -0.0154 200 LEU A CB  
3100 C CG  . LEU A 201 ? 0.4199 0.4049 0.3230 0.0629  0.0104  -0.0140 200 LEU A CG  
3101 C CD1 . LEU A 201 ? 0.3936 0.3884 0.3185 0.0568  0.0168  -0.0062 200 LEU A CD1 
3102 C CD2 . LEU A 201 ? 0.4920 0.4772 0.3788 0.0678  0.0065  -0.0130 200 LEU A CD2 
3114 N N   . GLU A 202 ? 0.4679 0.4176 0.3146 0.0957  0.0224  -0.0319 201 GLU A N   
3115 C CA  A GLU A 202 ? 0.5127 0.4609 0.3486 0.1092  0.0342  -0.0320 201 GLU A CA  
3116 C CA  B GLU A 202 ? 0.5137 0.4616 0.3494 0.1092  0.0340  -0.0322 201 GLU A CA  
3117 C C   . GLU A 202 ? 0.5293 0.4694 0.3339 0.1204  0.0371  -0.0345 201 GLU A C   
3118 O O   . GLU A 202 ? 0.5379 0.4860 0.3369 0.1295  0.0513  -0.0283 201 GLU A O   
3119 C CB  A GLU A 202 ? 0.5862 0.5200 0.4192 0.1132  0.0305  -0.0400 201 GLU A CB  
3120 C CB  B GLU A 202 ? 0.5872 0.5200 0.4190 0.1132  0.0300  -0.0405 201 GLU A CB  
3121 C CG  A GLU A 202 ? 0.7167 0.6498 0.5393 0.1299  0.0427  -0.0411 201 GLU A CG  
3122 C CG  B GLU A 202 ? 0.7195 0.6503 0.5394 0.1301  0.0418  -0.0420 201 GLU A CG  
3123 C CD  A GLU A 202 ? 0.7861 0.7461 0.6342 0.1317  0.0569  -0.0305 201 GLU A CD  
3124 C CD  B GLU A 202 ? 0.8857 0.7900 0.6707 0.1408  0.0368  -0.0539 201 GLU A CD  
3125 O OE1 A GLU A 202 ? 0.7984 0.7727 0.6730 0.1198  0.0554  -0.0242 201 GLU A OE1 
3126 O OE1 B GLU A 202 ? 0.9938 0.8793 0.7671 0.1329  0.0224  -0.0623 201 GLU A OE1 
3127 O OE2 A GLU A 202 ? 0.8704 0.8380 0.7118 0.1450  0.0699  -0.0290 201 GLU A OE2 
3128 O OE2 B GLU A 202 ? 0.9963 0.8988 0.7655 0.1569  0.0475  -0.0554 201 GLU A OE2 
3141 N N   . SER A 203 ? 0.4693 0.3900 0.4333 0.1291  0.0776  0.0028  202 SER A N   
3142 C CA  . SER A 203 ? 0.5339 0.4389 0.4716 0.1329  0.0828  -0.0082 202 SER A CA  
3143 C C   . SER A 203 ? 0.4793 0.3715 0.3999 0.1223  0.0703  -0.0188 202 SER A C   
3144 O O   . SER A 203 ? 0.5175 0.3867 0.4262 0.1221  0.0677  -0.0293 202 SER A O   
3145 C CB  . SER A 203 ? 0.7152 0.5990 0.6437 0.1460  0.0947  -0.0142 202 SER A CB  
3146 O OG  . SER A 203 ? 0.8919 0.7584 0.8258 0.1454  0.0908  -0.0172 202 SER A OG  
3152 N N   . PRO A 204 ? 0.4240 0.3310 0.3456 0.1130  0.0619  -0.0162 203 PRO A N   
3153 C CA  . PRO A 204 ? 0.4369 0.3356 0.3471 0.1032  0.0495  -0.0248 203 PRO A CA  
3154 C C   . PRO A 204 ? 0.4731 0.3503 0.3556 0.1062  0.0495  -0.0383 203 PRO A C   
3155 O O   . PRO A 204 ? 0.4997 0.3723 0.3664 0.1149  0.0588  -0.0404 203 PRO A O   
3156 C CB  . PRO A 204 ? 0.4609 0.3790 0.3747 0.0965  0.0444  -0.0190 203 PRO A CB  
3157 C CG  . PRO A 204 ? 0.4725 0.4096 0.4043 0.1002  0.0523  -0.0071 203 PRO A CG  
3158 C CD  . PRO A 204 ? 0.4317 0.3611 0.3618 0.1119  0.0646  -0.0069 203 PRO A CD  
3166 N N   . GLU A 205 ? 0.4789 0.3434 0.3555 0.0986  0.0388  -0.0475 204 GLU A N   
3167 C CA  . GLU A 205 ? 0.5544 0.4013 0.4042 0.0985  0.0342  -0.0614 204 GLU A CA  
3168 C C   . GLU A 205 ? 0.5191 0.3782 0.3560 0.0966  0.0296  -0.0602 204 GLU A C   
3169 O O   . GLU A 205 ? 0.4915 0.3693 0.3426 0.0909  0.0252  -0.0515 204 GLU A O   
3170 C CB  . GLU A 205 ? 0.6230 0.4567 0.4749 0.0890  0.0224  -0.0708 204 GLU A CB  
3171 C CG  . GLU A 205 ? 0.7124 0.5292 0.5752 0.0908  0.0272  -0.0723 204 GLU A CG  
3172 C CD  . GLU A 205 ? 0.8200 0.6144 0.6642 0.1024  0.0380  -0.0807 204 GLU A CD  
3173 O OE1 . GLU A 205 ? 0.8550 0.6367 0.6719 0.1044  0.0361  -0.0931 204 GLU A OE1 
3174 O OE2 . GLU A 205 ? 0.8536 0.6436 0.7100 0.1103  0.0487  -0.0748 204 GLU A OE2 
3181 N N   . ARG A 206 ? 0.5093 0.3565 0.3175 0.1019  0.0309  -0.0688 205 ARG A N   
3182 C CA  . ARG A 206 ? 0.5459 0.4040 0.3404 0.1028  0.0295  -0.0649 205 ARG A CA  
3183 C C   . ARG A 206 ? 0.5590 0.4060 0.3265 0.1004  0.0178  -0.0768 205 ARG A C   
3184 O O   . ARG A 206 ? 0.5524 0.3792 0.3005 0.1030  0.0168  -0.0898 205 ARG A O   
3185 C CB  . ARG A 206 ? 0.6421 0.5025 0.4275 0.1140  0.0459  -0.0585 205 ARG A CB  
3186 C CG  . ARG A 206 ? 0.7223 0.5988 0.5384 0.1148  0.0548  -0.0455 205 ARG A CG  
3187 C CD  . ARG A 206 ? 0.6840 0.5760 0.5032 0.1189  0.0650  -0.0339 205 ARG A CD  
3188 N NE  . ARG A 206 ? 0.5539 0.4624 0.4037 0.1190  0.0717  -0.0226 205 ARG A NE  
3189 C CZ  . ARG A 206 ? 0.4929 0.4205 0.3635 0.1120  0.0683  -0.0126 205 ARG A CZ  
3190 N NH1 . ARG A 206 ? 0.4888 0.4313 0.3854 0.1125  0.0736  -0.0034 205 ARG A NH1 
3191 N NH2 . ARG A 206 ? 0.4451 0.3770 0.3106 0.1050  0.0594  -0.0120 205 ARG A NH2 
3205 N N   . PRO A 207 ? 0.5470 0.4064 0.3121 0.0959  0.0083  -0.0730 206 PRO A N   
3206 C CA  . PRO A 207 ? 0.4720 0.3518 0.2547 0.0934  0.0092  -0.0594 206 PRO A CA  
3207 C C   . PRO A 207 ? 0.4217 0.3133 0.2373 0.0852  0.0057  -0.0538 206 PRO A C   
3208 O O   . PRO A 207 ? 0.4383 0.3265 0.2622 0.0782  -0.0040 -0.0601 206 PRO A O   
3209 C CB  . PRO A 207 ? 0.4902 0.3738 0.2584 0.0908  -0.0031 -0.0611 206 PRO A CB  
3210 C CG  . PRO A 207 ? 0.5780 0.4447 0.3148 0.0948  -0.0073 -0.0737 206 PRO A CG  
3211 C CD  . PRO A 207 ? 0.6064 0.4581 0.3471 0.0939  -0.0048 -0.0836 206 PRO A CD  
3219 N N   . PHE A 208 ? 0.4043 0.3101 0.2373 0.0857  0.0133  -0.0420 207 PHE A N   
3220 C CA  . PHE A 208 ? 0.3671 0.2855 0.2283 0.0789  0.0112  -0.0356 207 PHE A CA  
3221 C C   . PHE A 208 ? 0.3640 0.2954 0.2312 0.0740  0.0048  -0.0303 207 PHE A C   
3222 O O   . PHE A 208 ? 0.3944 0.3318 0.2583 0.0768  0.0102  -0.0233 207 PHE A O   
3223 C CB  . PHE A 208 ? 0.3617 0.2869 0.2371 0.0832  0.0232  -0.0271 207 PHE A CB  
3224 C CG  . PHE A 208 ? 0.3486 0.2865 0.2501 0.0773  0.0213  -0.0204 207 PHE A CG  
3225 C CD1 . PHE A 208 ? 0.3448 0.2851 0.2558 0.0694  0.0115  -0.0225 207 PHE A CD1 
3226 C CD2 . PHE A 208 ? 0.3813 0.3300 0.2978 0.0802  0.0297  -0.0115 207 PHE A CD2 
3227 C CE1 . PHE A 208 ? 0.3753 0.3269 0.3064 0.0651  0.0108  -0.0158 207 PHE A CE1 
3228 C CE2 . PHE A 208 ? 0.3662 0.3267 0.3032 0.0756  0.0272  -0.0054 207 PHE A CE2 
3229 C CZ  . PHE A 208 ? 0.3666 0.3278 0.3092 0.0683  0.0181  -0.0076 207 PHE A CZ  
3239 N N   . LEU A 209 ? 0.3382 0.2730 0.2143 0.0669  -0.0058 -0.0334 208 LEU A N   
3240 C CA  . LEU A 209 ? 0.3274 0.2734 0.2104 0.0630  -0.0119 -0.0294 208 LEU A CA  
3241 C C   . LEU A 209 ? 0.3230 0.2806 0.2290 0.0577  -0.0108 -0.0235 208 LEU A C   
3242 O O   . LEU A 209 ? 0.3160 0.2736 0.2335 0.0539  -0.0121 -0.0251 208 LEU A O   
3243 C CB  . LEU A 209 ? 0.3338 0.2780 0.2123 0.0595  -0.0243 -0.0368 208 LEU A CB  
3244 C CG  . LEU A 209 ? 0.3674 0.3236 0.2578 0.0553  -0.0318 -0.0339 208 LEU A CG  
3245 C CD1 . LEU A 209 ? 0.3705 0.3297 0.2511 0.0601  -0.0306 -0.0279 208 LEU A CD1 
3246 C CD2 . LEU A 209 ? 0.3905 0.3465 0.2820 0.0511  -0.0436 -0.0417 208 LEU A CD2 
3258 N N   . ALA A 210 ? 0.3091 0.2756 0.2207 0.0571  -0.0085 -0.0168 209 ALA A N   
3259 C CA  . ALA A 210 ? 0.3246 0.3016 0.2541 0.0518  -0.0094 -0.0129 209 ALA A CA  
3260 C C   . ALA A 210 ? 0.3244 0.3054 0.2555 0.0495  -0.0163 -0.0139 209 ALA A C   
3261 O O   . ALA A 210 ? 0.3628 0.3414 0.2838 0.0528  -0.0175 -0.0128 209 ALA A O   
3262 C CB  . ALA A 210 ? 0.3561 0.3394 0.2924 0.0520  -0.0021 -0.0057 209 ALA A CB  
3268 N N   . ILE A 211 ? 0.2553 0.2422 0.1990 0.0447  -0.0203 -0.0154 210 ILE A N   
3269 C CA  . ILE A 211 ? 0.2469 0.2399 0.1962 0.0431  -0.0254 -0.0158 210 ILE A CA  
3270 C C   . ILE A 211 ? 0.2526 0.2526 0.2128 0.0402  -0.0216 -0.0121 210 ILE A C   
3271 O O   . ILE A 211 ? 0.2407 0.2447 0.2093 0.0366  -0.0200 -0.0117 210 ILE A O   
3272 C CB  . ILE A 211 ? 0.2761 0.2717 0.2321 0.0398  -0.0323 -0.0207 210 ILE A CB  
3273 C CG1 . ILE A 211 ? 0.3335 0.3204 0.2772 0.0416  -0.0370 -0.0262 210 ILE A CG1 
3274 C CG2 . ILE A 211 ? 0.2695 0.2735 0.2336 0.0396  -0.0367 -0.0203 210 ILE A CG2 
3275 C CD1 . ILE A 211 ? 0.3667 0.3554 0.3182 0.0369  -0.0448 -0.0318 210 ILE A CD1 
3287 N N   . LEU A 212 ? 0.2582 0.2583 0.2170 0.0418  -0.0203 -0.0096 211 LEU A N   
3288 C CA  . LEU A 212 ? 0.2822 0.2862 0.2484 0.0389  -0.0170 -0.0077 211 LEU A CA  
3289 C C   . LEU A 212 ? 0.3022 0.3082 0.2727 0.0398  -0.0194 -0.0090 211 LEU A C   
3290 O O   . LEU A 212 ? 0.3225 0.3242 0.2882 0.0440  -0.0207 -0.0076 211 LEU A O   
3291 C CB  . LEU A 212 ? 0.3996 0.3999 0.3623 0.0393  -0.0120 -0.0037 211 LEU A CB  
3292 C CG  . LEU A 212 ? 0.6430 0.6460 0.6128 0.0349  -0.0096 -0.0029 211 LEU A CG  
3293 C CD1 . LEU A 212 ? 0.7449 0.7559 0.7215 0.0307  -0.0105 -0.0047 211 LEU A CD1 
3294 C CD2 . LEU A 212 ? 0.7353 0.7363 0.7049 0.0339  -0.0050 0.0015  211 LEU A CD2 
3306 N N   . GLY A 213 ? 0.2996 0.3121 0.2787 0.0370  -0.0195 -0.0110 212 GLY A N   
3307 C CA  . GLY A 213 ? 0.3065 0.3222 0.2914 0.0386  -0.0199 -0.0125 212 GLY A CA  
3308 C C   . GLY A 213 ? 0.3054 0.3231 0.2933 0.0356  -0.0156 -0.0138 212 GLY A C   
3309 O O   . GLY A 213 ? 0.2942 0.3087 0.2783 0.0328  -0.0132 -0.0132 212 GLY A O   
3313 N N   . GLY A 214 ? 0.2739 0.2978 0.2687 0.0361  -0.0146 -0.0158 213 GLY A N   
3314 C CA  . GLY A 214 ? 0.2773 0.3033 0.2719 0.0337  -0.0102 -0.0180 213 GLY A CA  
3315 C C   . GLY A 214 ? 0.2979 0.3160 0.2891 0.0358  -0.0073 -0.0207 213 GLY A C   
3316 O O   . GLY A 214 ? 0.3126 0.3244 0.3044 0.0402  -0.0081 -0.0199 213 GLY A O   
3320 N N   . ALA A 215 ? 0.2740 0.2915 0.2606 0.0324  -0.0043 -0.0239 214 ALA A N   
3321 C CA  . ALA A 215 ? 0.3076 0.3160 0.2901 0.0333  -0.0011 -0.0288 214 ALA A CA  
3322 C C   . ALA A 215 ? 0.3240 0.3265 0.2993 0.0271  -0.0019 -0.0311 214 ALA A C   
3323 O O   . ALA A 215 ? 0.3523 0.3447 0.3236 0.0266  0.0002  -0.0363 214 ALA A O   
3324 C CB  . ALA A 215 ? 0.3467 0.3598 0.3294 0.0356  0.0039  -0.0329 214 ALA A CB  
3330 N N   . LYS A 216 ? 0.2843 0.2925 0.2589 0.0225  -0.0050 -0.0278 215 LYS A N   
3331 C CA  . LYS A 216 ? 0.3010 0.3072 0.2719 0.0160  -0.0070 -0.0295 215 LYS A CA  
3332 C C   . LYS A 216 ? 0.3452 0.3442 0.3201 0.0150  -0.0075 -0.0262 215 LYS A C   
3333 O O   . LYS A 216 ? 0.3216 0.3255 0.2998 0.0124  -0.0092 -0.0215 215 LYS A O   
3334 C CB  . LYS A 216 ? 0.2958 0.3139 0.2656 0.0125  -0.0098 -0.0265 215 LYS A CB  
3335 C CG  . LYS A 216 ? 0.3164 0.3401 0.2794 0.0127  -0.0083 -0.0294 215 LYS A CG  
3336 C CD  . LYS A 216 ? 0.2990 0.3338 0.2600 0.0103  -0.0110 -0.0246 215 LYS A CD  
3337 C CE  . LYS A 216 ? 0.3258 0.3647 0.2765 0.0102  -0.0088 -0.0274 215 LYS A CE  
3338 N NZ  . LYS A 216 ? 0.3351 0.3843 0.2830 0.0090  -0.0108 -0.0209 215 LYS A NZ  
3352 N N   . VAL A 217 ? 0.3539 0.3408 0.3290 0.0180  -0.0050 -0.0278 216 VAL A N   
3353 C CA  . VAL A 217 ? 0.3174 0.2965 0.2954 0.0189  -0.0040 -0.0225 216 VAL A CA  
3354 C C   . VAL A 217 ? 0.3183 0.2951 0.2991 0.0107  -0.0046 -0.0223 216 VAL A C   
3355 O O   . VAL A 217 ? 0.3416 0.3215 0.3266 0.0094  -0.0041 -0.0159 216 VAL A O   
3356 C CB  . VAL A 217 ? 0.3317 0.2977 0.3093 0.0249  -0.0011 -0.0230 216 VAL A CB  
3357 C CG1 . VAL A 217 ? 0.3463 0.3036 0.3248 0.0263  0.0004  -0.0159 216 VAL A CG1 
3358 C CG2 . VAL A 217 ? 0.3282 0.3001 0.3067 0.0329  -0.0015 -0.0228 216 VAL A CG2 
3368 N N   . ALA A 218 ? 0.3230 0.2946 0.3021 0.0051  -0.0054 -0.0294 217 ALA A N   
3369 C CA  . ALA A 218 ? 0.3924 0.3625 0.3768 -0.0042 -0.0071 -0.0298 217 ALA A CA  
3370 C C   . ALA A 218 ? 0.3910 0.3785 0.3812 -0.0078 -0.0105 -0.0247 217 ALA A C   
3371 O O   . ALA A 218 ? 0.3889 0.3789 0.3882 -0.0119 -0.0098 -0.0194 217 ALA A O   
3372 C CB  . ALA A 218 ? 0.4329 0.3961 0.4122 -0.0103 -0.0094 -0.0404 217 ALA A CB  
3378 N N   . ASP A 219 ? 0.3314 0.3310 0.3174 -0.0059 -0.0134 -0.0255 218 ASP A N   
3379 C CA  . ASP A 219 ? 0.3213 0.3368 0.3131 -0.0077 -0.0163 -0.0199 218 ASP A CA  
3380 C C   . ASP A 219 ? 0.3098 0.3274 0.3060 -0.0018 -0.0126 -0.0118 218 ASP A C   
3381 O O   . ASP A 219 ? 0.3241 0.3484 0.3291 -0.0036 -0.0118 -0.0061 218 ASP A O   
3382 C CB  . ASP A 219 ? 0.3955 0.4209 0.3805 -0.0061 -0.0194 -0.0215 218 ASP A CB  
3383 C CG  . ASP A 219 ? 0.5883 0.6154 0.5665 -0.0121 -0.0241 -0.0288 218 ASP A CG  
3384 O OD1 . ASP A 219 ? 0.6296 0.6535 0.6111 -0.0195 -0.0271 -0.0327 218 ASP A OD1 
3385 O OD2 . ASP A 219 ? 0.6280 0.6598 0.5969 -0.0097 -0.0249 -0.0305 218 ASP A OD2 
3390 N N   . LYS A 220 ? 0.2995 0.3126 0.2898 0.0053  -0.0104 -0.0114 219 LYS A N   
3391 C CA  . LYS A 220 ? 0.3103 0.3265 0.3014 0.0107  -0.0085 -0.0056 219 LYS A CA  
3392 C C   . LYS A 220 ? 0.3040 0.3122 0.2956 0.0131  -0.0042 -0.0012 219 LYS A C   
3393 O O   . LYS A 220 ? 0.2982 0.3097 0.2907 0.0161  -0.0018 0.0038  219 LYS A O   
3394 C CB  . LYS A 220 ? 0.3298 0.3462 0.3156 0.0158  -0.0093 -0.0074 219 LYS A CB  
3395 C CG  . LYS A 220 ? 0.3617 0.3876 0.3472 0.0134  -0.0121 -0.0089 219 LYS A CG  
3396 C CD  . LYS A 220 ? 0.3863 0.4137 0.3695 0.0171  -0.0120 -0.0093 219 LYS A CD  
3397 C CE  . LYS A 220 ? 0.4033 0.4392 0.3853 0.0148  -0.0134 -0.0088 219 LYS A CE  
3398 N NZ  . LYS A 220 ? 0.3593 0.3967 0.3411 0.0172  -0.0120 -0.0085 219 LYS A NZ  
3412 N N   . ILE A 221 ? 0.2985 0.2955 0.2889 0.0121  -0.0025 -0.0024 220 ILE A N   
3413 C CA  . ILE A 221 ? 0.2862 0.2754 0.2763 0.0143  0.0023  0.0036  220 ILE A CA  
3414 C C   . ILE A 221 ? 0.2971 0.2932 0.2969 0.0091  0.0052  0.0087  220 ILE A C   
3415 O O   . ILE A 221 ? 0.3158 0.3105 0.3153 0.0121  0.0106  0.0154  220 ILE A O   
3416 C CB  . ILE A 221 ? 0.3336 0.3078 0.3216 0.0144  0.0039  0.0023  220 ILE A CB  
3417 C CG1 . ILE A 221 ? 0.4446 0.4094 0.4284 0.0194  0.0089  0.0101  220 ILE A CG1 
3418 C CG2 . ILE A 221 ? 0.3498 0.3204 0.3455 0.0050  0.0036  -0.0014 220 ILE A CG2 
3419 C CD1 . ILE A 221 ? 0.5015 0.4511 0.4811 0.0235  0.0096  0.0097  220 ILE A CD1 
3431 N N   . GLN A 222 ? 0.2840 0.2890 0.2927 0.0016  0.0016  0.0058  221 GLN A N   
3432 C CA  . GLN A 222 ? 0.3011 0.3166 0.3234 -0.0041 0.0032  0.0107  221 GLN A CA  
3433 C C   . GLN A 222 ? 0.2530 0.2818 0.2783 0.0008  0.0046  0.0156  221 GLN A C   
3434 O O   . GLN A 222 ? 0.2883 0.3279 0.3266 -0.0018 0.0072  0.0211  221 GLN A O   
3435 C CB  . GLN A 222 ? 0.3532 0.3750 0.3838 -0.0141 -0.0032 0.0053  221 GLN A CB  
3436 C CG  . GLN A 222 ? 0.3652 0.3715 0.3941 -0.0203 -0.0039 -0.0008 221 GLN A CG  
3437 C CD  . GLN A 222 ? 0.4766 0.4743 0.5148 -0.0242 0.0024  0.0052  221 GLN A CD  
3438 O OE1 . GLN A 222 ? 0.4996 0.5084 0.5507 -0.0268 0.0057  0.0126  221 GLN A OE1 
3439 N NE2 . GLN A 222 ? 0.5408 0.5190 0.5735 -0.0243 0.0051  0.0028  221 GLN A NE2 
3448 N N   . LEU A 223 ? 0.2431 0.2712 0.2584 0.0078  0.0033  0.0138  222 LEU A N   
3449 C CA  . LEU A 223 ? 0.2655 0.3019 0.2821 0.0134  0.0053  0.0177  222 LEU A CA  
3450 C C   . LEU A 223 ? 0.2796 0.3082 0.2875 0.0211  0.0122  0.0213  222 LEU A C   
3451 O O   . LEU A 223 ? 0.2653 0.2986 0.2742 0.0261  0.0159  0.0245  222 LEU A O   
3452 C CB  . LEU A 223 ? 0.2759 0.3143 0.2866 0.0159  0.0002  0.0137  222 LEU A CB  
3453 C CG  . LEU A 223 ? 0.3456 0.3910 0.3596 0.0098  -0.0064 0.0101  222 LEU A CG  
3454 C CD1 . LEU A 223 ? 0.3969 0.4436 0.4045 0.0131  -0.0092 0.0083  222 LEU A CD1 
3455 C CD2 . LEU A 223 ? 0.3646 0.4242 0.3923 0.0047  -0.0085 0.0137  222 LEU A CD2 
3467 N N   . ILE A 224 ? 0.2898 0.3059 0.2881 0.0227  0.0140  0.0210  223 ILE A N   
3468 C CA  . ILE A 224 ? 0.2908 0.2989 0.2760 0.0306  0.0186  0.0235  223 ILE A CA  
3469 C C   . ILE A 224 ? 0.2968 0.3084 0.2859 0.0325  0.0278  0.0309  223 ILE A C   
3470 O O   . ILE A 224 ? 0.3094 0.3194 0.2892 0.0397  0.0323  0.0323  223 ILE A O   
3471 C CB  . ILE A 224 ? 0.2922 0.2877 0.2671 0.0322  0.0174  0.0227  223 ILE A CB  
3472 C CG1 . ILE A 224 ? 0.3182 0.3126 0.2905 0.0321  0.0095  0.0156  223 ILE A CG1 
3473 C CG2 . ILE A 224 ? 0.2935 0.2808 0.2523 0.0404  0.0219  0.0267  223 ILE A CG2 
3474 C CD1 . ILE A 224 ? 0.3700 0.3540 0.3356 0.0344  0.0078  0.0149  223 ILE A CD1 
3486 N N   . ASN A 225 ? 0.2972 0.3134 0.3002 0.0259  0.0312  0.0356  224 ASN A N   
3487 C CA  . ASN A 225 ? 0.3320 0.3531 0.3416 0.0272  0.0415  0.0440  224 ASN A CA  
3488 C C   . ASN A 225 ? 0.3490 0.3810 0.3625 0.0329  0.0450  0.0453  224 ASN A C   
3489 O O   . ASN A 225 ? 0.3706 0.4000 0.3754 0.0405  0.0539  0.0491  224 ASN A O   
3490 C CB  . ASN A 225 ? 0.3282 0.3563 0.3585 0.0168  0.0428  0.0480  224 ASN A CB  
3491 C CG  . ASN A 225 ? 0.4036 0.4394 0.4451 0.0172  0.0545  0.0579  224 ASN A CG  
3492 O OD1 . ASN A 225 ? 0.4231 0.4493 0.4540 0.0214  0.0631  0.0637  224 ASN A OD1 
3493 N ND2 . ASN A 225 ? 0.5122 0.5667 0.5755 0.0132  0.0550  0.0606  224 ASN A ND2 
3500 N N   . ASN A 226 ? 0.2871 0.3301 0.3119 0.0302  0.0385  0.0421  225 ASN A N   
3501 C CA  . ASN A 226 ? 0.2870 0.3397 0.3177 0.0363  0.0420  0.0443  225 ASN A CA  
3502 C C   . ASN A 226 ? 0.2891 0.3303 0.3005 0.0450  0.0415  0.0391  225 ASN A C   
3503 O O   . ASN A 226 ? 0.3539 0.3951 0.3623 0.0530  0.0488  0.0409  225 ASN A O   
3504 C CB  . ASN A 226 ? 0.3434 0.4118 0.3921 0.0312  0.0346  0.0441  225 ASN A CB  
3505 C CG  . ASN A 226 ? 0.3942 0.4783 0.4660 0.0231  0.0354  0.0497  225 ASN A CG  
3506 O OD1 . ASN A 226 ? 0.3782 0.4661 0.4583 0.0235  0.0448  0.0563  225 ASN A OD1 
3507 N ND2 . ASN A 226 ? 0.4524 0.5464 0.5348 0.0154  0.0253  0.0472  225 ASN A ND2 
3514 N N   . MET A 227 ? 0.2779 0.3087 0.2765 0.0438  0.0336  0.0324  226 MET A N   
3515 C CA  A MET A 227 ? 0.3157 0.3358 0.2978 0.0504  0.0321  0.0269  226 MET A CA  
3516 C CA  B MET A 227 ? 0.3159 0.3357 0.2976 0.0503  0.0320  0.0268  226 MET A CA  
3517 C C   . MET A 227 ? 0.3515 0.3609 0.3157 0.0575  0.0393  0.0276  226 MET A C   
3518 O O   . MET A 227 ? 0.3719 0.3736 0.3234 0.0640  0.0406  0.0236  226 MET A O   
3519 C CB  A MET A 227 ? 0.3501 0.3643 0.3257 0.0469  0.0224  0.0204  226 MET A CB  
3520 C CB  B MET A 227 ? 0.3505 0.3639 0.3251 0.0468  0.0225  0.0205  226 MET A CB  
3521 C CG  A MET A 227 ? 0.4237 0.4462 0.4109 0.0421  0.0161  0.0188  226 MET A CG  
3522 C CG  B MET A 227 ? 0.4244 0.4458 0.4105 0.0410  0.0156  0.0186  226 MET A CG  
3523 S SD  A MET A 227 ? 0.4924 0.5088 0.4723 0.0397  0.0073  0.0117  226 MET A SD  
3524 S SD  B MET A 227 ? 0.5096 0.5243 0.4884 0.0376  0.0076  0.0123  226 MET A SD  
3525 C CE  A MET A 227 ? 0.5240 0.5360 0.5006 0.0364  0.0061  0.0112  226 MET A CE  
3526 C CE  B MET A 227 ? 0.5302 0.5345 0.4944 0.0438  0.0060  0.0077  226 MET A CE  
3545 N N   . LEU A 228 ? 0.3515 0.3590 0.3130 0.0562  0.0439  0.0327  227 LEU A N   
3546 C CA  . LEU A 228 ? 0.3586 0.3557 0.2998 0.0635  0.0506  0.0344  227 LEU A CA  
3547 C C   . LEU A 228 ? 0.3786 0.3787 0.3187 0.0706  0.0623  0.0378  227 LEU A C   
3548 O O   . LEU A 228 ? 0.4103 0.4008 0.3295 0.0780  0.0683  0.0377  227 LEU A O   
3549 C CB  . LEU A 228 ? 0.3338 0.3277 0.2735 0.0607  0.0539  0.0410  227 LEU A CB  
3550 C CG  . LEU A 228 ? 0.3196 0.3068 0.2554 0.0569  0.0438  0.0374  227 LEU A CG  
3551 C CD1 . LEU A 228 ? 0.3077 0.2911 0.2461 0.0539  0.0486  0.0452  227 LEU A CD1 
3552 C CD2 . LEU A 228 ? 0.4058 0.3831 0.3199 0.0629  0.0373  0.0314  227 LEU A CD2 
3564 N N   . ASP A 229 ? 0.3745 0.3878 0.3358 0.0693  0.0656  0.0408  228 ASP A N   
3565 C CA  . ASP A 229 ? 0.4359 0.4529 0.3988 0.0775  0.0772  0.0437  228 ASP A CA  
3566 C C   . ASP A 229 ? 0.4127 0.4224 0.3675 0.0839  0.0746  0.0360  228 ASP A C   
3567 O O   . ASP A 229 ? 0.3994 0.4085 0.3522 0.0926  0.0847  0.0369  228 ASP A O   
3568 C CB  . ASP A 229 ? 0.5165 0.5535 0.5096 0.0736  0.0820  0.0521  228 ASP A CB  
3569 C CG  . ASP A 229 ? 0.6133 0.6561 0.6152 0.0678  0.0879  0.0605  228 ASP A CG  
3570 O OD1 . ASP A 229 ? 0.6562 0.6908 0.6421 0.0730  0.0980  0.0642  228 ASP A OD1 
3571 O OD2 . ASP A 229 ? 0.5224 0.5763 0.5455 0.0578  0.0823  0.0632  228 ASP A OD2 
3576 N N   . LYS A 230 ? 0.3662 0.3699 0.3171 0.0800  0.0624  0.0287  229 LYS A N   
3577 C CA  . LYS A 230 ? 0.3712 0.3674 0.3183 0.0840  0.0592  0.0219  229 LYS A CA  
3578 C C   . LYS A 230 ? 0.3740 0.3524 0.2965 0.0856  0.0530  0.0120  229 LYS A C   
3579 O O   . LYS A 230 ? 0.4330 0.4002 0.3458 0.0911  0.0544  0.0058  229 LYS A O   
3580 C CB  . LYS A 230 ? 0.3722 0.3779 0.3386 0.0774  0.0502  0.0225  229 LYS A CB  
3581 C CG  . LYS A 230 ? 0.3536 0.3790 0.3450 0.0740  0.0526  0.0315  229 LYS A CG  
3582 C CD  . LYS A 230 ? 0.4089 0.4419 0.4121 0.0822  0.0627  0.0369  229 LYS A CD  
3583 C CE  . LYS A 230 ? 0.5333 0.5893 0.5639 0.0771  0.0626  0.0460  229 LYS A CE  
3584 N NZ  . LYS A 230 ? 0.6201 0.6886 0.6688 0.0849  0.0704  0.0527  229 LYS A NZ  
3598 N N   . VAL A 231 ? 0.3334 0.3088 0.2466 0.0810  0.0457  0.0103  230 VAL A N   
3599 C CA  . VAL A 231 ? 0.3428 0.3056 0.2379 0.0809  0.0368  0.0013  230 VAL A CA  
3600 C C   . VAL A 231 ? 0.3928 0.3463 0.2623 0.0867  0.0401  0.0004  230 VAL A C   
3601 O O   . VAL A 231 ? 0.4238 0.3807 0.2908 0.0896  0.0494  0.0079  230 VAL A O   
3602 C CB  . VAL A 231 ? 0.3464 0.3138 0.2501 0.0726  0.0252  0.0000  230 VAL A CB  
3603 C CG1 . VAL A 231 ? 0.3870 0.3644 0.3134 0.0671  0.0225  0.0019  230 VAL A CG1 
3604 C CG2 . VAL A 231 ? 0.3603 0.3320 0.2634 0.0705  0.0254  0.0058  230 VAL A CG2 
3614 N N   . ASN A 232 ? 0.3920 0.3339 0.2422 0.0880  0.0321  -0.0087 231 ASN A N   
3615 C CA  . ASN A 232 ? 0.4099 0.3426 0.2320 0.0935  0.0322  -0.0105 231 ASN A CA  
3616 C C   . ASN A 232 ? 0.4110 0.3453 0.2282 0.0897  0.0205  -0.0103 231 ASN A C   
3617 O O   . ASN A 232 ? 0.4170 0.3472 0.2140 0.0943  0.0211  -0.0074 231 ASN A O   
3618 C CB  . ASN A 232 ? 0.4358 0.3536 0.2364 0.0985  0.0310  -0.0220 231 ASN A CB  
3619 C CG  . ASN A 232 ? 0.4924 0.4068 0.2979 0.1038  0.0431  -0.0226 231 ASN A CG  
3620 O OD1 . ASN A 232 ? 0.4865 0.3975 0.3039 0.1017  0.0406  -0.0278 231 ASN A OD1 
3621 N ND2 . ASN A 232 ? 0.5124 0.4279 0.3101 0.1113  0.0574  -0.0162 231 ASN A ND2 
3628 N N   . GLU A 233 ? 0.4017 0.3424 0.2372 0.0824  0.0107  -0.0124 232 GLU A N   
3629 C CA  . GLU A 233 ? 0.4132 0.3572 0.2488 0.0794  -0.0002 -0.0121 232 GLU A CA  
3630 C C   . GLU A 233 ? 0.3747 0.3292 0.2368 0.0722  -0.0027 -0.0092 232 GLU A C   
3631 O O   . GLU A 233 ? 0.3596 0.3175 0.2367 0.0687  -0.0008 -0.0107 232 GLU A O   
3632 C CB  . GLU A 233 ? 0.4426 0.3814 0.2670 0.0787  -0.0129 -0.0224 232 GLU A CB  
3633 C CG  . GLU A 233 ? 0.5453 0.4730 0.3391 0.0854  -0.0138 -0.0275 232 GLU A CG  
3634 C CD  . GLU A 233 ? 0.6264 0.5532 0.4097 0.0840  -0.0298 -0.0349 232 GLU A CD  
3635 O OE1 . GLU A 233 ? 0.6568 0.5734 0.4208 0.0856  -0.0345 -0.0451 232 GLU A OE1 
3636 O OE2 . GLU A 233 ? 0.5639 0.5003 0.3582 0.0816  -0.0377 -0.0307 232 GLU A OE2 
3643 N N   . MET A 234 ? 0.3502 0.3091 0.2168 0.0707  -0.0071 -0.0052 233 MET A N   
3644 C CA  . MET A 234 ? 0.3482 0.3156 0.2365 0.0645  -0.0098 -0.0040 233 MET A CA  
3645 C C   . MET A 234 ? 0.3619 0.3317 0.2509 0.0646  -0.0190 -0.0047 233 MET A C   
3646 O O   . MET A 234 ? 0.4035 0.3699 0.2813 0.0692  -0.0197 -0.0003 233 MET A O   
3647 C CB  . MET A 234 ? 0.4020 0.3730 0.3012 0.0625  -0.0011 0.0036  233 MET A CB  
3648 C CG  . MET A 234 ? 0.5680 0.5465 0.4866 0.0561  -0.0027 0.0037  233 MET A CG  
3649 S SD  . MET A 234 ? 0.5672 0.5486 0.4961 0.0531  0.0065  0.0115  233 MET A SD  
3650 C CE  . MET A 234 ? 0.5376 0.5221 0.4677 0.0549  0.0142  0.0132  233 MET A CE  
3660 N N   . ILE A 235 ? 0.3290 0.3049 0.2314 0.0601  -0.0256 -0.0095 234 ILE A N   
3661 C CA  . ILE A 235 ? 0.3331 0.3149 0.2439 0.0598  -0.0322 -0.0089 234 ILE A CA  
3662 C C   . ILE A 235 ? 0.3036 0.2891 0.2290 0.0567  -0.0267 -0.0051 234 ILE A C   
3663 O O   . ILE A 235 ? 0.2936 0.2826 0.2293 0.0519  -0.0232 -0.0064 234 ILE A O   
3664 C CB  . ILE A 235 ? 0.3233 0.3115 0.2433 0.0563  -0.0410 -0.0156 234 ILE A CB  
3665 C CG1 . ILE A 235 ? 0.3692 0.3536 0.2745 0.0585  -0.0492 -0.0208 234 ILE A CG1 
3666 C CG2 . ILE A 235 ? 0.2974 0.2952 0.2329 0.0558  -0.0450 -0.0141 234 ILE A CG2 
3667 C CD1 . ILE A 235 ? 0.3577 0.3470 0.2744 0.0526  -0.0569 -0.0281 234 ILE A CD1 
3679 N N   . ILE A 236 ? 0.3176 0.3016 0.2432 0.0597  -0.0263 -0.0007 235 ILE A N   
3680 C CA  . ILE A 236 ? 0.3357 0.3207 0.2736 0.0569  -0.0220 0.0012  235 ILE A CA  
3681 C C   . ILE A 236 ? 0.3479 0.3378 0.2943 0.0590  -0.0274 -0.0002 235 ILE A C   
3682 O O   . ILE A 236 ? 0.3870 0.3741 0.3286 0.0650  -0.0303 0.0033  235 ILE A O   
3683 C CB  . ILE A 236 ? 0.3753 0.3518 0.3084 0.0583  -0.0152 0.0078  235 ILE A CB  
3684 C CG1 . ILE A 236 ? 0.4144 0.3892 0.3423 0.0564  -0.0090 0.0098  235 ILE A CG1 
3685 C CG2 . ILE A 236 ? 0.3633 0.3386 0.3088 0.0546  -0.0119 0.0076  235 ILE A CG2 
3686 C CD1 . ILE A 236 ? 0.4443 0.4124 0.3706 0.0563  -0.0012 0.0171  235 ILE A CD1 
3698 N N   . GLY A 237 ? 0.2949 0.2927 0.2542 0.0550  -0.0280 -0.0045 236 GLY A N   
3699 C CA  . GLY A 237 ? 0.3020 0.3071 0.2720 0.0574  -0.0320 -0.0059 236 GLY A CA  
3700 C C   . GLY A 237 ? 0.3163 0.3244 0.2974 0.0547  -0.0270 -0.0079 236 GLY A C   
3701 O O   . GLY A 237 ? 0.2935 0.2960 0.2726 0.0514  -0.0213 -0.0080 236 GLY A O   
3705 N N   . GLY A 238 ? 0.3276 0.3455 0.3207 0.0558  -0.0291 -0.0099 237 GLY A N   
3706 C CA  . GLY A 238 ? 0.3062 0.3269 0.3077 0.0544  -0.0233 -0.0123 237 GLY A CA  
3707 C C   . GLY A 238 ? 0.3107 0.3200 0.3081 0.0575  -0.0183 -0.0114 237 GLY A C   
3708 O O   . GLY A 238 ? 0.3154 0.3176 0.3093 0.0632  -0.0198 -0.0077 237 GLY A O   
3712 N N   . GLY A 239 ? 0.2895 0.2954 0.2858 0.0532  -0.0127 -0.0148 238 GLY A N   
3713 C CA  . GLY A 239 ? 0.3096 0.3028 0.3026 0.0545  -0.0080 -0.0159 238 GLY A CA  
3714 C C   . GLY A 239 ? 0.3244 0.3063 0.3092 0.0521  -0.0077 -0.0125 238 GLY A C   
3715 O O   . GLY A 239 ? 0.3535 0.3225 0.3365 0.0538  -0.0046 -0.0116 238 GLY A O   
3719 N N   . MET A 240 ? 0.3197 0.3054 0.3002 0.0485  -0.0101 -0.0101 239 MET A N   
3720 C CA  A MET A 240 ? 0.3546 0.3314 0.3291 0.0463  -0.0080 -0.0061 239 MET A CA  
3721 C CA  B MET A 240 ? 0.3541 0.3317 0.3283 0.0464  -0.0084 -0.0058 239 MET A CA  
3722 C C   . MET A 240 ? 0.3431 0.3117 0.3125 0.0531  -0.0086 0.0002  239 MET A C   
3723 O O   . MET A 240 ? 0.3318 0.2897 0.2978 0.0522  -0.0047 0.0044  239 MET A O   
3724 C CB  A MET A 240 ? 0.3870 0.3703 0.3588 0.0421  -0.0089 -0.0049 239 MET A CB  
3725 C CB  B MET A 240 ? 0.3859 0.3706 0.3569 0.0436  -0.0101 -0.0045 239 MET A CB  
3726 C CG  A MET A 240 ? 0.4303 0.4072 0.3992 0.0392  -0.0051 -0.0006 239 MET A CG  
3727 C CG  B MET A 240 ? 0.4417 0.4349 0.4166 0.0377  -0.0101 -0.0080 239 MET A CG  
3728 S SD  A MET A 240 ? 0.4921 0.4780 0.4615 0.0348  -0.0046 0.0004  239 MET A SD  
3729 S SD  B MET A 240 ? 0.4722 0.4636 0.4489 0.0301  -0.0068 -0.0087 239 MET A SD  
3730 C CE  A MET A 240 ? 0.4738 0.4677 0.4503 0.0284  -0.0061 -0.0053 239 MET A CE  
3731 C CE  B MET A 240 ? 0.4539 0.4352 0.4282 0.0308  -0.0033 -0.0026 239 MET A CE  
3750 N N   . ALA A 241 ? 0.3204 0.2943 0.2896 0.0597  -0.0135 0.0015  240 ALA A N   
3751 C CA  . ALA A 241 ? 0.3263 0.2942 0.2877 0.0668  -0.0156 0.0084  240 ALA A CA  
3752 C C   . ALA A 241 ? 0.3299 0.2842 0.2922 0.0709  -0.0113 0.0126  240 ALA A C   
3753 O O   . ALA A 241 ? 0.3519 0.2964 0.3057 0.0745  -0.0097 0.0203  240 ALA A O   
3754 C CB  . ALA A 241 ? 0.3105 0.2891 0.2738 0.0725  -0.0237 0.0080  240 ALA A CB  
3760 N N   . PHE A 242 ? 0.3253 0.2770 0.2969 0.0710  -0.0086 0.0080  241 PHE A N   
3761 C CA  . PHE A 242 ? 0.3595 0.2967 0.3328 0.0772  -0.0050 0.0118  241 PHE A CA  
3762 C C   . PHE A 242 ? 0.3706 0.2907 0.3394 0.0722  0.0013  0.0152  241 PHE A C   
3763 O O   . PHE A 242 ? 0.3733 0.2794 0.3394 0.0776  0.0040  0.0226  241 PHE A O   
3764 C CB  . PHE A 242 ? 0.3293 0.2673 0.3130 0.0796  -0.0027 0.0050  241 PHE A CB  
3765 C CG  . PHE A 242 ? 0.3272 0.2831 0.3188 0.0847  -0.0079 0.0035  241 PHE A CG  
3766 C CD1 . PHE A 242 ? 0.3519 0.3124 0.3467 0.0948  -0.0130 0.0099  241 PHE A CD1 
3767 C CD2 . PHE A 242 ? 0.3367 0.3064 0.3332 0.0791  -0.0085 -0.0033 241 PHE A CD2 
3768 C CE1 . PHE A 242 ? 0.3410 0.3206 0.3462 0.0982  -0.0188 0.0086  241 PHE A CE1 
3769 C CE2 . PHE A 242 ? 0.3437 0.3306 0.3499 0.0824  -0.0130 -0.0039 241 PHE A CE2 
3770 C CZ  . PHE A 242 ? 0.3286 0.3210 0.3402 0.0915  -0.0184 0.0016  241 PHE A CZ  
3780 N N   . THR A 243 ? 0.3516 0.2732 0.3208 0.0619  0.0036  0.0108  242 THR A N   
3781 C CA  . THR A 243 ? 0.3739 0.2826 0.3420 0.0557  0.0090  0.0146  242 THR A CA  
3782 C C   . THR A 243 ? 0.3854 0.2918 0.3448 0.0593  0.0102  0.0257  242 THR A C   
3783 O O   . THR A 243 ? 0.3929 0.2845 0.3508 0.0599  0.0155  0.0333  242 THR A O   
3784 C CB  . THR A 243 ? 0.3548 0.2705 0.3269 0.0442  0.0095  0.0082  242 THR A CB  
3785 O OG1 . THR A 243 ? 0.3289 0.2445 0.3054 0.0410  0.0089  -0.0020 242 THR A OG1 
3786 C CG2 . THR A 243 ? 0.3869 0.2927 0.3616 0.0366  0.0146  0.0127  242 THR A CG2 
3794 N N   . PHE A 244 ? 0.3515 0.2714 0.3040 0.0619  0.0059  0.0269  243 PHE A N   
3795 C CA  . PHE A 244 ? 0.3673 0.2849 0.3076 0.0665  0.0071  0.0364  243 PHE A CA  
3796 C C   . PHE A 244 ? 0.3747 0.2837 0.3081 0.0772  0.0054  0.0442  243 PHE A C   
3797 O O   . PHE A 244 ? 0.4167 0.3148 0.3417 0.0802  0.0101  0.0545  243 PHE A O   
3798 C CB  . PHE A 244 ? 0.3429 0.2748 0.2758 0.0672  0.0023  0.0336  243 PHE A CB  
3799 C CG  . PHE A 244 ? 0.3559 0.2944 0.2929 0.0588  0.0058  0.0303  243 PHE A CG  
3800 C CD1 . PHE A 244 ? 0.3508 0.2968 0.2993 0.0520  0.0041  0.0218  243 PHE A CD1 
3801 C CD2 . PHE A 244 ? 0.3877 0.3249 0.3174 0.0583  0.0115  0.0365  243 PHE A CD2 
3802 C CE1 . PHE A 244 ? 0.3698 0.3230 0.3230 0.0451  0.0066  0.0201  243 PHE A CE1 
3803 C CE2 . PHE A 244 ? 0.3971 0.3420 0.3335 0.0515  0.0151  0.0343  243 PHE A CE2 
3804 C CZ  . PHE A 244 ? 0.3964 0.3494 0.3448 0.0450  0.0120  0.0265  243 PHE A CZ  
3814 N N   . LEU A 245 ? 0.3617 0.2769 0.2992 0.0834  -0.0014 0.0406  244 LEU A N   
3815 C CA  . LEU A 245 ? 0.3991 0.3094 0.3313 0.0950  -0.0048 0.0489  244 LEU A CA  
3816 C C   . LEU A 245 ? 0.4181 0.3086 0.3547 0.0977  0.0023  0.0552  244 LEU A C   
3817 O O   . LEU A 245 ? 0.4142 0.2948 0.3421 0.1060  0.0031  0.0667  244 LEU A O   
3818 C CB  . LEU A 245 ? 0.4107 0.3354 0.3511 0.1005  -0.0136 0.0434  244 LEU A CB  
3819 C CG  . LEU A 245 ? 0.4212 0.3632 0.3564 0.0982  -0.0215 0.0384  244 LEU A CG  
3820 C CD1 . LEU A 245 ? 0.4529 0.4103 0.4020 0.0999  -0.0284 0.0317  244 LEU A CD1 
3821 C CD2 . LEU A 245 ? 0.4448 0.3867 0.3614 0.1046  -0.0265 0.0462  244 LEU A CD2 
3833 N N   . LYS A 246 ? 0.3865 0.2695 0.3350 0.0909  0.0074  0.0479  245 LYS A N   
3834 C CA  . LYS A 246 ? 0.3901 0.2508 0.3429 0.0922  0.0145  0.0524  245 LYS A CA  
3835 C C   . LYS A 246 ? 0.4154 0.2629 0.3612 0.0879  0.0216  0.0626  245 LYS A C   
3836 O O   . LYS A 246 ? 0.4649 0.2955 0.4073 0.0942  0.0258  0.0738  245 LYS A O   
3837 C CB  . LYS A 246 ? 0.4052 0.2600 0.3697 0.0844  0.0180  0.0402  245 LYS A CB  
3838 C CG  . LYS A 246 ? 0.5448 0.3734 0.5139 0.0859  0.0252  0.0428  245 LYS A CG  
3839 C CD  . LYS A 246 ? 0.7318 0.5541 0.7094 0.0803  0.0275  0.0288  245 LYS A CD  
3840 C CE  . LYS A 246 ? 0.8750 0.6697 0.8569 0.0849  0.0340  0.0298  245 LYS A CE  
3841 N NZ  . LYS A 246 ? 0.8972 0.6843 0.8838 0.0788  0.0365  0.0140  245 LYS A NZ  
3855 N N   . VAL A 247 ? 0.4120 0.2676 0.3566 0.0778  0.0235  0.0602  246 VAL A N   
3856 C CA  . VAL A 247 ? 0.4539 0.2998 0.3952 0.0726  0.0317  0.0699  246 VAL A CA  
3857 C C   . VAL A 247 ? 0.4854 0.3325 0.4093 0.0821  0.0319  0.0830  246 VAL A C   
3858 O O   . VAL A 247 ? 0.4967 0.3283 0.4151 0.0852  0.0388  0.0959  246 VAL A O   
3859 C CB  . VAL A 247 ? 0.4389 0.2963 0.3869 0.0598  0.0337  0.0633  246 VAL A CB  
3860 C CG1 . VAL A 247 ? 0.5206 0.3731 0.4667 0.0553  0.0427  0.0745  246 VAL A CG1 
3861 C CG2 . VAL A 247 ? 0.3875 0.2407 0.3503 0.0499  0.0336  0.0518  246 VAL A CG2 
3871 N N   . LEU A 248 ? 0.4403 0.3046 0.3538 0.0866  0.0245  0.0799  247 LEU A N   
3872 C CA  . LEU A 248 ? 0.4572 0.3236 0.3505 0.0945  0.0242  0.0901  247 LEU A CA  
3873 C C   . LEU A 248 ? 0.4876 0.3480 0.3714 0.1079  0.0188  0.0988  247 LEU A C   
3874 O O   . LEU A 248 ? 0.5379 0.3890 0.4062 0.1146  0.0226  0.1124  247 LEU A O   
3875 C CB  . LEU A 248 ? 0.4493 0.3344 0.3345 0.0938  0.0178  0.0819  247 LEU A CB  
3876 C CG  . LEU A 248 ? 0.5000 0.3926 0.3935 0.0826  0.0230  0.0752  247 LEU A CG  
3877 C CD1 . LEU A 248 ? 0.4889 0.3977 0.3772 0.0828  0.0156  0.0656  247 LEU A CD1 
3878 C CD2 . LEU A 248 ? 0.5530 0.4392 0.4407 0.0801  0.0347  0.0856  247 LEU A CD2 
3890 N N   . ASN A 249 ? 0.4432 0.3099 0.3360 0.1125  0.0101  0.0919  248 ASN A N   
3891 C CA  . ASN A 249 ? 0.4710 0.3368 0.3577 0.1261  0.0029  0.0998  248 ASN A CA  
3892 C C   . ASN A 249 ? 0.4931 0.3420 0.3928 0.1310  0.0071  0.1044  248 ASN A C   
3893 O O   . ASN A 249 ? 0.5293 0.3756 0.4257 0.1437  0.0023  0.1133  248 ASN A O   
3894 C CB  . ASN A 249 ? 0.5033 0.3904 0.3930 0.1295  -0.0103 0.0903  248 ASN A CB  
3895 C CG  . ASN A 249 ? 0.5934 0.4938 0.4664 0.1275  -0.0159 0.0870  248 ASN A CG  
3896 O OD1 . ASN A 249 ? 0.7307 0.6346 0.5857 0.1358  -0.0227 0.0936  248 ASN A OD1 
3897 N ND2 . ASN A 249 ? 0.5270 0.4343 0.4050 0.1170  -0.0135 0.0766  248 ASN A ND2 
3904 N N   . ASN A 250 ? 0.4702 0.3068 0.3839 0.1216  0.0156  0.0989  249 ASN A N   
3905 C CA  . ASN A 250 ? 0.4683 0.2872 0.3951 0.1256  0.0198  0.0995  249 ASN A CA  
3906 C C   . ASN A 250 ? 0.4598 0.2909 0.3964 0.1349  0.0113  0.0932  249 ASN A C   
3907 O O   . ASN A 250 ? 0.4958 0.3155 0.4393 0.1452  0.0125  0.0982  249 ASN A O   
3908 C CB  . ASN A 250 ? 0.5278 0.3243 0.4471 0.1333  0.0262  0.1170  249 ASN A CB  
3909 C CG  . ASN A 250 ? 0.5887 0.3706 0.5051 0.1222  0.0374  0.1228  249 ASN A CG  
3910 O OD1 . ASN A 250 ? 0.6015 0.3867 0.5025 0.1224  0.0397  0.1328  249 ASN A OD1 
3911 N ND2 . ASN A 250 ? 0.5768 0.3431 0.5082 0.1121  0.0446  0.1160  249 ASN A ND2 
3918 N N   . MET A 251 ? 0.4349 0.2893 0.3737 0.1314  0.0037  0.0825  250 MET A N   
3919 C CA  . MET A 251 ? 0.4594 0.3293 0.4098 0.1389  -0.0039 0.0768  250 MET A CA  
3920 C C   . MET A 251 ? 0.4484 0.3090 0.4152 0.1373  0.0026  0.0675  250 MET A C   
3921 O O   . MET A 251 ? 0.4422 0.2954 0.4112 0.1256  0.0089  0.0587  250 MET A O   
3922 C CB  . MET A 251 ? 0.4533 0.3484 0.4029 0.1330  -0.0124 0.0675  250 MET A CB  
3923 C CG  . MET A 251 ? 0.4761 0.3910 0.4397 0.1395  -0.0206 0.0625  250 MET A CG  
3924 S SD  . MET A 251 ? 0.5227 0.4611 0.4907 0.1284  -0.0262 0.0490  250 MET A SD  
3925 C CE  . MET A 251 ? 0.5836 0.5370 0.5754 0.1344  -0.0282 0.0431  250 MET A CE  
3935 N N   . GLU A 252 ? 0.4318 0.2935 0.4095 0.1496  0.0009  0.0694  251 GLU A N   
3936 C CA  . GLU A 252 ? 0.4902 0.3479 0.4831 0.1504  0.0065  0.0588  251 GLU A CA  
3937 C C   . GLU A 252 ? 0.4608 0.3427 0.4605 0.1435  0.0025  0.0462  251 GLU A C   
3938 O O   . GLU A 252 ? 0.4364 0.3415 0.4411 0.1483  -0.0062 0.0476  251 GLU A O   
3939 C CB  . GLU A 252 ? 0.6285 0.4834 0.6327 0.1675  0.0063  0.0657  251 GLU A CB  
3940 C CG  . GLU A 252 ? 0.8739 0.6965 0.8784 0.1732  0.0160  0.0714  251 GLU A CG  
3941 C CD  . GLU A 252 ? 1.0120 0.8160 1.0193 0.1627  0.0262  0.0574  251 GLU A CD  
3942 O OE1 . GLU A 252 ? 1.0280 0.8467 1.0403 0.1565  0.0259  0.0439  251 GLU A OE1 
3943 O OE2 . GLU A 252 ? 1.0997 0.8743 1.1033 0.1600  0.0341  0.0601  251 GLU A OE2 
3950 N N   . ILE A 253 ? 0.4523 0.3290 0.4530 0.1324  0.0086  0.0342  252 ILE A N   
3951 C CA  . ILE A 253 ? 0.4190 0.3165 0.4241 0.1250  0.0060  0.0235  252 ILE A CA  
3952 C C   . ILE A 253 ? 0.3929 0.2907 0.4090 0.1278  0.0122  0.0135  252 ILE A C   
3953 O O   . ILE A 253 ? 0.3530 0.2665 0.3722 0.1216  0.0118  0.0049  252 ILE A O   
3954 C CB  . ILE A 253 ? 0.4367 0.3332 0.4319 0.1099  0.0068  0.0184  252 ILE A CB  
3955 C CG1 . ILE A 253 ? 0.4402 0.3141 0.4334 0.1027  0.0153  0.0123  252 ILE A CG1 
3956 C CG2 . ILE A 253 ? 0.4279 0.3259 0.4118 0.1086  0.0021  0.0282  252 ILE A CG2 
3957 C CD1 . ILE A 253 ? 0.4812 0.3576 0.4684 0.0881  0.0153  0.0067  252 ILE A CD1 
3969 N N   . GLY A 254 ? 0.4547 0.3342 0.4756 0.1371  0.0188  0.0145  253 GLY A N   
3970 C CA  . GLY A 254 ? 0.5273 0.4059 0.5569 0.1412  0.0261  0.0045  253 GLY A CA  
3971 C C   . GLY A 254 ? 0.4926 0.3660 0.5139 0.1276  0.0307  -0.0089 253 GLY A C   
3972 O O   . GLY A 254 ? 0.4707 0.3263 0.4818 0.1177  0.0322  -0.0112 253 GLY A O   
3976 N N   . THR A 255 ? 0.4380 0.3284 0.4640 0.1269  0.0325  -0.0171 254 THR A N   
3977 C CA  . THR A 255 ? 0.4465 0.3347 0.4631 0.1154  0.0362  -0.0295 254 THR A CA  
3978 C C   . THR A 255 ? 0.4095 0.3188 0.4225 0.1044  0.0292  -0.0292 254 THR A C   
3979 O O   . THR A 255 ? 0.3868 0.3017 0.3942 0.0968  0.0313  -0.0378 254 THR A O   
3980 C CB  . THR A 255 ? 0.5008 0.3911 0.5216 0.1221  0.0449  -0.0387 254 THR A CB  
3981 O OG1 . THR A 255 ? 0.4785 0.3958 0.5143 0.1298  0.0432  -0.0337 254 THR A OG1 
3982 C CG2 . THR A 255 ? 0.5921 0.4566 0.6145 0.1326  0.0532  -0.0410 254 THR A CG2 
3990 N N   . SER A 256 ? 0.3803 0.3004 0.3952 0.1040  0.0212  -0.0196 255 SER A N   
3991 C CA  . SER A 256 ? 0.3548 0.2915 0.3659 0.0943  0.0150  -0.0191 255 SER A CA  
3992 C C   . SER A 256 ? 0.3645 0.2904 0.3640 0.0818  0.0162  -0.0244 255 SER A C   
3993 O O   . SER A 256 ? 0.3715 0.2767 0.3660 0.0797  0.0197  -0.0260 255 SER A O   
3994 C CB  . SER A 256 ? 0.3542 0.2981 0.3655 0.0967  0.0069  -0.0087 255 SER A CB  
3995 O OG  . SER A 256 ? 0.3562 0.3106 0.3790 0.1083  0.0039  -0.0032 255 SER A OG  
4001 N N   . LEU A 257 ? 0.3649 0.3053 0.3615 0.0735  0.0128  -0.0265 256 LEU A N   
4002 C CA  . LEU A 257 ? 0.3923 0.3268 0.3801 0.0620  0.0125  -0.0302 256 LEU A CA  
4003 C C   . LEU A 257 ? 0.3618 0.2837 0.3466 0.0592  0.0112  -0.0238 256 LEU A C   
4004 O O   . LEU A 257 ? 0.3597 0.2858 0.3451 0.0628  0.0079  -0.0153 256 LEU A O   
4005 C CB  . LEU A 257 ? 0.4033 0.3561 0.3899 0.0554  0.0085  -0.0305 256 LEU A CB  
4006 C CG  . LEU A 257 ? 0.4321 0.3974 0.4202 0.0557  0.0108  -0.0360 256 LEU A CG  
4007 C CD1 . LEU A 257 ? 0.4144 0.3944 0.4011 0.0489  0.0069  -0.0343 256 LEU A CD1 
4008 C CD2 . LEU A 257 ? 0.4477 0.4024 0.4285 0.0537  0.0162  -0.0453 256 LEU A CD2 
4020 N N   . PHE A 258 ? 0.3502 0.2569 0.3313 0.0520  0.0139  -0.0282 257 PHE A N   
4021 C CA  . PHE A 258 ? 0.3837 0.2781 0.3641 0.0478  0.0144  -0.0219 257 PHE A CA  
4022 C C   . PHE A 258 ? 0.4086 0.3000 0.3875 0.0348  0.0139  -0.0276 257 PHE A C   
4023 O O   . PHE A 258 ? 0.4393 0.3244 0.4157 0.0306  0.0150  -0.0378 257 PHE A O   
4024 C CB  . PHE A 258 ? 0.3983 0.2710 0.3804 0.0547  0.0190  -0.0188 257 PHE A CB  
4025 C CG  . PHE A 258 ? 0.4153 0.2740 0.3972 0.0502  0.0210  -0.0110 257 PHE A CG  
4026 C CD1 . PHE A 258 ? 0.4300 0.2950 0.4100 0.0536  0.0194  0.0009  257 PHE A CD1 
4027 C CD2 . PHE A 258 ? 0.4382 0.2775 0.4216 0.0421  0.0247  -0.0156 257 PHE A CD2 
4028 C CE1 . PHE A 258 ? 0.4536 0.3065 0.4332 0.0497  0.0229  0.0093  257 PHE A CE1 
4029 C CE2 . PHE A 258 ? 0.4774 0.3045 0.4632 0.0370  0.0275  -0.0073 257 PHE A CE2 
4030 C CZ  . PHE A 258 ? 0.4724 0.3067 0.4563 0.0411  0.0274  0.0059  257 PHE A CZ  
4040 N N   . ASP A 259 ? 0.3790 0.2755 0.3594 0.0287  0.0123  -0.0211 258 ASP A N   
4041 C CA  . ASP A 259 ? 0.3583 0.2552 0.3412 0.0161  0.0111  -0.0247 258 ASP A CA  
4042 C C   . ASP A 259 ? 0.3866 0.2677 0.3747 0.0112  0.0148  -0.0187 258 ASP A C   
4043 O O   . ASP A 259 ? 0.3758 0.2601 0.3656 0.0128  0.0166  -0.0080 258 ASP A O   
4044 C CB  . ASP A 259 ? 0.3801 0.2982 0.3641 0.0124  0.0071  -0.0215 258 ASP A CB  
4045 C CG  . ASP A 259 ? 0.5248 0.4478 0.5130 0.0002  0.0044  -0.0258 258 ASP A CG  
4046 O OD1 . ASP A 259 ? 0.6429 0.5639 0.6276 -0.0042 0.0019  -0.0360 258 ASP A OD1 
4047 O OD2 . ASP A 259 ? 0.5186 0.4479 0.5136 -0.0045 0.0046  -0.0190 258 ASP A OD2 
4052 N N   . GLU A 260 ? 0.4382 0.3020 0.4283 0.0044  0.0163  -0.0260 259 GLU A N   
4053 C CA  . GLU A 260 ? 0.5275 0.3731 0.5244 -0.0010 0.0208  -0.0204 259 GLU A CA  
4054 C C   . GLU A 260 ? 0.4728 0.3308 0.4787 -0.0113 0.0200  -0.0139 259 GLU A C   
4055 O O   . GLU A 260 ? 0.4509 0.3028 0.4618 -0.0115 0.0253  -0.0024 259 GLU A O   
4056 C CB  . GLU A 260 ? 0.7355 0.5591 0.7328 -0.0074 0.0218  -0.0321 259 GLU A CB  
4057 C CG  . GLU A 260 ? 1.0272 0.8269 1.0323 -0.0131 0.0271  -0.0272 259 GLU A CG  
4058 C CD  . GLU A 260 ? 1.2836 1.0584 1.2873 -0.0183 0.0280  -0.0408 259 GLU A CD  
4059 O OE1 . GLU A 260 ? 1.3497 1.1294 1.3456 -0.0198 0.0236  -0.0547 259 GLU A OE1 
4060 O OE2 . GLU A 260 ? 1.3915 1.1406 1.4007 -0.0208 0.0335  -0.0376 259 GLU A OE2 
4067 N N   . GLU A 261 ? 0.4624 0.3385 0.4709 -0.0193 0.0141  -0.0200 260 GLU A N   
4068 C CA  . GLU A 261 ? 0.5136 0.4043 0.5336 -0.0280 0.0136  -0.0132 260 GLU A CA  
4069 C C   . GLU A 261 ? 0.4398 0.3441 0.4575 -0.0191 0.0165  -0.0016 260 GLU A C   
4070 O O   . GLU A 261 ? 0.4515 0.3568 0.4760 -0.0208 0.0219  0.0090  260 GLU A O   
4071 C CB  . GLU A 261 ? 0.6788 0.5866 0.7023 -0.0373 0.0055  -0.0220 260 GLU A CB  
4072 C CG  . GLU A 261 ? 0.8347 0.7294 0.8593 -0.0480 0.0015  -0.0346 260 GLU A CG  
4073 C CD  . GLU A 261 ? 0.9687 0.8510 1.0083 -0.0597 0.0043  -0.0316 260 GLU A CD  
4074 O OE1 . GLU A 261 ? 1.0023 0.8973 1.0556 -0.0636 0.0067  -0.0207 260 GLU A OE1 
4075 O OE2 . GLU A 261 ? 1.0352 0.8945 1.0737 -0.0649 0.0048  -0.0400 260 GLU A OE2 
4082 N N   . GLY A 262 ? 0.3971 0.3109 0.4047 -0.0098 0.0137  -0.0034 261 GLY A N   
4083 C CA  . GLY A 262 ? 0.3826 0.3069 0.3859 -0.0015 0.0156  0.0056  261 GLY A CA  
4084 C C   . GLY A 262 ? 0.3892 0.2996 0.3876 0.0057  0.0217  0.0154  261 GLY A C   
4085 O O   . GLY A 262 ? 0.3636 0.2794 0.3600 0.0090  0.0256  0.0247  261 GLY A O   
4089 N N   . ALA A 263 ? 0.3804 0.2719 0.3762 0.0088  0.0234  0.0139  262 ALA A N   
4090 C CA  . ALA A 263 ? 0.3719 0.2491 0.3624 0.0167  0.0288  0.0247  262 ALA A CA  
4091 C C   . ALA A 263 ? 0.3933 0.2669 0.3900 0.0107  0.0358  0.0352  262 ALA A C   
4092 O O   . ALA A 263 ? 0.4317 0.3018 0.4210 0.0178  0.0408  0.0469  262 ALA A O   
4093 C CB  . ALA A 263 ? 0.4008 0.2565 0.3910 0.0201  0.0302  0.0215  262 ALA A CB  
4099 N N   . LYS A 264 ? 0.3695 0.2450 0.3799 -0.0025 0.0364  0.0316  263 LYS A N   
4100 C CA  . LYS A 264 ? 0.4003 0.2734 0.4214 -0.0100 0.0439  0.0417  263 LYS A CA  
4101 C C   . LYS A 264 ? 0.3983 0.2914 0.4194 -0.0080 0.0470  0.0496  263 LYS A C   
4102 O O   . LYS A 264 ? 0.4431 0.3351 0.4714 -0.0116 0.0555  0.0605  263 LYS A O   
4103 C CB  . LYS A 264 ? 0.4382 0.3095 0.4767 -0.0259 0.0420  0.0344  263 LYS A CB  
4104 C CG  . LYS A 264 ? 0.5516 0.3984 0.5905 -0.0294 0.0407  0.0261  263 LYS A CG  
4105 C CD  . LYS A 264 ? 0.7244 0.5727 0.7783 -0.0462 0.0360  0.0159  263 LYS A CD  
4106 C CE  . LYS A 264 ? 0.8714 0.6940 0.9232 -0.0501 0.0342  0.0044  263 LYS A CE  
4107 N NZ  . LYS A 264 ? 0.9512 0.7774 1.0148 -0.0668 0.0273  -0.0077 263 LYS A NZ  
4121 N N   . ILE A 265 ? 0.3945 0.3045 0.4082 -0.0023 0.0416  0.0449  264 ILE A N   
4122 C CA  . ILE A 265 ? 0.3544 0.2810 0.3667 0.0010  0.0452  0.0514  264 ILE A CA  
4123 C C   . ILE A 265 ? 0.3543 0.2805 0.3463 0.0147  0.0452  0.0547  264 ILE A C   
4124 O O   . ILE A 265 ? 0.3485 0.2853 0.3355 0.0189  0.0488  0.0591  264 ILE A O   
4125 C CB  . ILE A 265 ? 0.3675 0.3149 0.3905 -0.0048 0.0396  0.0443  264 ILE A CB  
4126 C CG1 . ILE A 265 ? 0.3701 0.3218 0.3832 0.0001  0.0304  0.0340  264 ILE A CG1 
4127 C CG2 . ILE A 265 ? 0.4515 0.4008 0.4946 -0.0191 0.0381  0.0411  264 ILE A CG2 
4128 C CD1 . ILE A 265 ? 0.4513 0.4231 0.4716 -0.0032 0.0250  0.0287  264 ILE A CD1 
4140 N N   . VAL A 266 ? 0.3460 0.2600 0.3264 0.0220  0.0415  0.0529  265 VAL A N   
4141 C CA  . VAL A 266 ? 0.3813 0.2971 0.3436 0.0340  0.0386  0.0545  265 VAL A CA  
4142 C C   . VAL A 266 ? 0.3809 0.2941 0.3313 0.0398  0.0468  0.0667  265 VAL A C   
4143 O O   . VAL A 266 ? 0.3487 0.2702 0.2865 0.0461  0.0463  0.0670  265 VAL A O   
4144 C CB  . VAL A 266 ? 0.4102 0.3147 0.3664 0.0405  0.0333  0.0518  265 VAL A CB  
4145 C CG1 . VAL A 266 ? 0.4465 0.3501 0.3843 0.0528  0.0310  0.0573  265 VAL A CG1 
4146 C CG2 . VAL A 266 ? 0.3980 0.3101 0.3606 0.0378  0.0255  0.0391  265 VAL A CG2 
4156 N N   . LYS A 267 ? 0.3855 0.2855 0.3382 0.0381  0.0551  0.0770  266 LYS A N   
4157 C CA  . LYS A 267 ? 0.4561 0.3530 0.3945 0.0447  0.0639  0.0898  266 LYS A CA  
4158 C C   . LYS A 267 ? 0.4545 0.3662 0.3981 0.0412  0.0711  0.0919  266 LYS A C   
4159 O O   . LYS A 267 ? 0.4306 0.3459 0.3571 0.0494  0.0755  0.0966  266 LYS A O   
4160 C CB  . LYS A 267 ? 0.4848 0.3632 0.4250 0.0437  0.0722  0.1021  266 LYS A CB  
4161 C CG  . LYS A 267 ? 0.5800 0.4433 0.5089 0.0526  0.0663  0.1034  266 LYS A CG  
4162 C CD  . LYS A 267 ? 0.7668 0.6088 0.6970 0.0528  0.0749  0.1167  266 LYS A CD  
4163 C CE  . LYS A 267 ? 0.8823 0.7106 0.8008 0.0643  0.0689  0.1194  266 LYS A CE  
4164 N NZ  . LYS A 267 ? 0.9578 0.7630 0.8763 0.0660  0.0778  0.1341  266 LYS A NZ  
4178 N N   . ASP A 268 ? 0.4102 0.3312 0.3771 0.0298  0.0720  0.0879  267 ASP A N   
4179 C CA  . ASP A 268 ? 0.4168 0.3549 0.3927 0.0272  0.0780  0.0895  267 ASP A CA  
4180 C C   . ASP A 268 ? 0.4074 0.3567 0.3718 0.0344  0.0718  0.0811  267 ASP A C   
4181 O O   . ASP A 268 ? 0.3957 0.3529 0.3536 0.0396  0.0786  0.0846  267 ASP A O   
4182 C CB  . ASP A 268 ? 0.5189 0.4668 0.5235 0.0134  0.0770  0.0862  267 ASP A CB  
4183 C CG  . ASP A 268 ? 0.6478 0.5875 0.6678 0.0045  0.0862  0.0961  267 ASP A CG  
4184 O OD1 . ASP A 268 ? 0.6469 0.5733 0.6551 0.0098  0.0953  0.1075  267 ASP A OD1 
4185 O OD2 . ASP A 268 ? 0.7068 0.6535 0.7509 -0.0082 0.0840  0.0927  267 ASP A OD2 
4190 N N   . LEU A 269 ? 0.3885 0.3379 0.3506 0.0348  0.0598  0.0701  268 LEU A N   
4191 C CA  . LEU A 269 ? 0.3581 0.3160 0.3100 0.0409  0.0541  0.0626  268 LEU A CA  
4192 C C   . LEU A 269 ? 0.3621 0.3130 0.2882 0.0522  0.0554  0.0656  268 LEU A C   
4193 O O   . LEU A 269 ? 0.3564 0.3130 0.2729 0.0574  0.0571  0.0635  268 LEU A O   
4194 C CB  . LEU A 269 ? 0.3081 0.2677 0.2636 0.0387  0.0420  0.0515  268 LEU A CB  
4195 C CG  . LEU A 269 ? 0.3040 0.2714 0.2801 0.0283  0.0385  0.0462  268 LEU A CG  
4196 C CD1 . LEU A 269 ? 0.3026 0.2691 0.2775 0.0278  0.0285  0.0364  268 LEU A CD1 
4197 C CD2 . LEU A 269 ? 0.3051 0.2886 0.2914 0.0262  0.0403  0.0457  268 LEU A CD2 
4209 N N   . MET A 270 ? 0.3790 0.3171 0.2928 0.0566  0.0541  0.0703  269 MET A N   
4210 C CA  . MET A 270 ? 0.4170 0.3494 0.3042 0.0675  0.0534  0.0731  269 MET A CA  
4211 C C   . MET A 270 ? 0.4252 0.3573 0.3014 0.0715  0.0665  0.0825  269 MET A C   
4212 O O   . MET A 270 ? 0.4502 0.3830 0.3056 0.0793  0.0670  0.0805  269 MET A O   
4213 C CB  . MET A 270 ? 0.4529 0.3730 0.3302 0.0724  0.0488  0.0778  269 MET A CB  
4214 C CG  . MET A 270 ? 0.4775 0.3983 0.3636 0.0710  0.0367  0.0688  269 MET A CG  
4215 S SD  . MET A 270 ? 0.5188 0.4518 0.4011 0.0728  0.0245  0.0548  269 MET A SD  
4216 C CE  . MET A 270 ? 0.6193 0.5477 0.4723 0.0846  0.0195  0.0583  269 MET A CE  
4226 N N   . SER A 271 ? 0.4334 0.3643 0.3234 0.0659  0.0778  0.0924  270 SER A N   
4227 C CA  . SER A 271 ? 0.4956 0.4284 0.3781 0.0694  0.0925  0.1023  270 SER A CA  
4228 C C   . SER A 271 ? 0.4569 0.4034 0.3434 0.0704  0.0955  0.0960  270 SER A C   
4229 O O   . SER A 271 ? 0.4351 0.3815 0.3023 0.0789  0.1036  0.0985  270 SER A O   
4230 C CB  . SER A 271 ? 0.5703 0.5016 0.4733 0.0611  0.1040  0.1140  270 SER A CB  
4231 O OG  . SER A 271 ? 0.6672 0.5821 0.5620 0.0626  0.1044  0.1226  270 SER A OG  
4237 N N   . LYS A 272 ? 0.3989 0.3566 0.3093 0.0626  0.0896  0.0879  271 LYS A N   
4238 C CA  . LYS A 272 ? 0.3896 0.3601 0.3061 0.0643  0.0920  0.0826  271 LYS A CA  
4239 C C   . LYS A 272 ? 0.4037 0.3698 0.2966 0.0729  0.0846  0.0727  271 LYS A C   
4240 O O   . LYS A 272 ? 0.4045 0.3732 0.2879 0.0795  0.0910  0.0711  271 LYS A O   
4241 C CB  . LYS A 272 ? 0.3810 0.3642 0.3270 0.0542  0.0859  0.0774  271 LYS A CB  
4242 C CG  . LYS A 272 ? 0.4128 0.4089 0.3663 0.0569  0.0868  0.0724  271 LYS A CG  
4243 C CD  . LYS A 272 ? 0.4222 0.4335 0.4057 0.0474  0.0819  0.0702  271 LYS A CD  
4244 C CE  . LYS A 272 ? 0.4505 0.4751 0.4430 0.0517  0.0854  0.0689  271 LYS A CE  
4245 N NZ  . LYS A 272 ? 0.4224 0.4632 0.4433 0.0428  0.0797  0.0683  271 LYS A NZ  
4259 N N   . ALA A 273 ? 0.3918 0.3508 0.2758 0.0731  0.0714  0.0660  272 ALA A N   
4260 C CA  . ALA A 273 ? 0.3884 0.3430 0.2510 0.0800  0.0634  0.0567  272 ALA A CA  
4261 C C   . ALA A 273 ? 0.4182 0.3640 0.2504 0.0901  0.0701  0.0608  272 ALA A C   
4262 O O   . ALA A 273 ? 0.4670 0.4111 0.2829 0.0961  0.0709  0.0543  272 ALA A O   
4263 C CB  . ALA A 273 ? 0.3859 0.3370 0.2476 0.0781  0.0488  0.0504  272 ALA A CB  
4269 N N   . GLU A 274 ? 0.4099 0.3488 0.2325 0.0922  0.0751  0.0716  273 GLU A N   
4270 C CA  . GLU A 274 ? 0.4567 0.3875 0.2478 0.1022  0.0826  0.0772  273 GLU A CA  
4271 C C   . GLU A 274 ? 0.4728 0.4084 0.2629 0.1056  0.0989  0.0803  273 GLU A C   
4272 O O   . GLU A 274 ? 0.5010 0.4317 0.2646 0.1144  0.1024  0.0762  273 GLU A O   
4273 C CB  . GLU A 274 ? 0.5788 0.5013 0.3631 0.1034  0.0866  0.0909  273 GLU A CB  
4274 C CG  . GLU A 274 ? 0.8611 0.7746 0.6086 0.1145  0.0927  0.0978  273 GLU A CG  
4275 C CD  . GLU A 274 ? 1.0228 0.9263 0.7600 0.1173  0.0916  0.1104  273 GLU A CD  
4276 O OE1 . GLU A 274 ? 1.0730 0.9755 0.8329 0.1106  0.0865  0.1128  273 GLU A OE1 
4277 O OE2 . GLU A 274 ? 1.0723 0.9682 0.7774 0.1269  0.0960  0.1179  273 GLU A OE2 
4284 N N   . LYS A 275 ? 0.4935 0.4391 0.3132 0.0986  0.1087  0.0868  274 LYS A N   
4285 C CA  . LYS A 275 ? 0.5233 0.4768 0.3477 0.1021  0.1252  0.0913  274 LYS A CA  
4286 C C   . LYS A 275 ? 0.4759 0.4329 0.2977 0.1064  0.1228  0.0788  274 LYS A C   
4287 O O   . LYS A 275 ? 0.4676 0.4247 0.2770 0.1148  0.1354  0.0795  274 LYS A O   
4288 C CB  . LYS A 275 ? 0.5829 0.5496 0.4452 0.0920  0.1330  0.1000  274 LYS A CB  
4289 C CG  . LYS A 275 ? 0.6370 0.6166 0.5129 0.0946  0.1506  0.1064  274 LYS A CG  
4290 C CD  . LYS A 275 ? 0.7401 0.7340 0.6560 0.0826  0.1550  0.1150  274 LYS A CD  
4291 C CE  . LYS A 275 ? 0.9189 0.9275 0.8513 0.0848  0.1742  0.1250  274 LYS A CE  
4292 N NZ  . LYS A 275 ? 1.0196 1.0394 0.9587 0.0909  0.1756  0.1173  274 LYS A NZ  
4306 N N   . ASN A 276 ? 0.4615 0.4208 0.2955 0.1012  0.1078  0.0680  275 ASN A N   
4307 C CA  . ASN A 276 ? 0.4530 0.4146 0.2890 0.1039  0.1048  0.0571  275 ASN A CA  
4308 C C   . ASN A 276 ? 0.4813 0.4294 0.2879 0.1094  0.0940  0.0449  275 ASN A C   
4309 O O   . ASN A 276 ? 0.5003 0.4472 0.3082 0.1107  0.0898  0.0348  275 ASN A O   
4310 C CB  . ASN A 276 ? 0.4382 0.4111 0.3067 0.0944  0.0959  0.0537  275 ASN A CB  
4311 C CG  . ASN A 276 ? 0.4950 0.4838 0.3942 0.0895  0.1058  0.0629  275 ASN A CG  
4312 O OD1 . ASN A 276 ? 0.5207 0.5130 0.4208 0.0925  0.1204  0.0727  275 ASN A OD1 
4313 N ND2 . ASN A 276 ? 0.5563 0.5557 0.4813 0.0818  0.0979  0.0602  275 ASN A ND2 
4320 N N   . GLY A 277 ? 0.4914 0.4298 0.2729 0.1123  0.0887  0.0460  276 GLY A N   
4321 C CA  . GLY A 277 ? 0.4812 0.4087 0.2359 0.1166  0.0767  0.0342  276 GLY A CA  
4322 C C   . GLY A 277 ? 0.4775 0.4069 0.2460 0.1096  0.0596  0.0242  276 GLY A C   
4323 O O   . GLY A 277 ? 0.5271 0.4499 0.2828 0.1113  0.0515  0.0124  276 GLY A O   
4327 N N   . VAL A 278 ? 0.4413 0.3790 0.2357 0.1014  0.0543  0.0284  277 VAL A N   
4328 C CA  . VAL A 278 ? 0.4186 0.3596 0.2274 0.0949  0.0400  0.0203  277 VAL A CA  
4329 C C   . VAL A 278 ? 0.4365 0.3740 0.2346 0.0951  0.0285  0.0206  277 VAL A C   
4330 O O   . VAL A 278 ? 0.4798 0.4180 0.2822 0.0942  0.0305  0.0299  277 VAL A O   
4331 C CB  . VAL A 278 ? 0.3867 0.3387 0.2281 0.0865  0.0412  0.0237  277 VAL A CB  
4332 C CG1 . VAL A 278 ? 0.3779 0.3331 0.2320 0.0805  0.0279  0.0161  277 VAL A CG1 
4333 C CG2 . VAL A 278 ? 0.4182 0.3760 0.2718 0.0873  0.0517  0.0247  277 VAL A CG2 
4343 N N   . LYS A 279 ? 0.4412 0.3751 0.2269 0.0962  0.0163  0.0108  278 LYS A N   
4344 C CA  . LYS A 279 ? 0.4894 0.4235 0.2694 0.0965  0.0037  0.0109  278 LYS A CA  
4345 C C   . LYS A 279 ? 0.4613 0.4041 0.2698 0.0890  -0.0027 0.0107  278 LYS A C   
4346 O O   . LYS A 279 ? 0.4031 0.3502 0.2267 0.0837  -0.0065 0.0032  278 LYS A O   
4347 C CB  . LYS A 279 ? 0.5434 0.4732 0.3040 0.0988  -0.0085 -0.0001 278 LYS A CB  
4348 C CG  . LYS A 279 ? 0.6513 0.5845 0.4080 0.0998  -0.0228 0.0009  278 LYS A CG  
4349 C CD  . LYS A 279 ? 0.8688 0.7981 0.6020 0.1026  -0.0354 -0.0092 278 LYS A CD  
4350 C CE  . LYS A 279 ? 1.0153 0.9519 0.7490 0.1037  -0.0510 -0.0076 278 LYS A CE  
4351 N NZ  . LYS A 279 ? 1.0456 0.9821 0.7740 0.1099  -0.0469 0.0068  278 LYS A NZ  
4365 N N   . ILE A 280 ? 0.4213 0.3652 0.2357 0.0892  -0.0033 0.0189  279 ILE A N   
4366 C CA  . ILE A 280 ? 0.4267 0.3772 0.2653 0.0835  -0.0081 0.0186  279 ILE A CA  
4367 C C   . ILE A 280 ? 0.4306 0.3837 0.2662 0.0861  -0.0214 0.0160  279 ILE A C   
4368 O O   . ILE A 280 ? 0.4442 0.3934 0.2642 0.0927  -0.0243 0.0219  279 ILE A O   
4369 C CB  . ILE A 280 ? 0.4659 0.4144 0.3154 0.0819  0.0005  0.0285  279 ILE A CB  
4370 C CG1 . ILE A 280 ? 0.4316 0.3803 0.2863 0.0791  0.0133  0.0322  279 ILE A CG1 
4371 C CG2 . ILE A 280 ? 0.4837 0.4372 0.3557 0.0764  -0.0038 0.0263  279 ILE A CG2 
4372 C CD1 . ILE A 280 ? 0.4062 0.3624 0.2765 0.0734  0.0136  0.0253  279 ILE A CD1 
4384 N N   . THR A 281 ? 0.4008 0.3617 0.2523 0.0812  -0.0293 0.0084  280 THR A N   
4385 C CA  . THR A 281 ? 0.4090 0.3763 0.2648 0.0827  -0.0416 0.0061  280 THR A CA  
4386 C C   . THR A 281 ? 0.3687 0.3419 0.2481 0.0797  -0.0408 0.0081  280 THR A C   
4387 O O   . THR A 281 ? 0.3407 0.3186 0.2364 0.0733  -0.0384 0.0037  280 THR A O   
4388 C CB  . THR A 281 ? 0.4485 0.4206 0.3049 0.0792  -0.0512 -0.0045 280 THR A CB  
4389 O OG1 . THR A 281 ? 0.5008 0.4648 0.3320 0.0827  -0.0520 -0.0079 280 THR A OG1 
4390 C CG2 . THR A 281 ? 0.4238 0.4064 0.2901 0.0798  -0.0644 -0.0064 280 THR A CG2 
4398 N N   . LEU A 282 ? 0.3827 0.3549 0.2625 0.0851  -0.0426 0.0149  281 LEU A N   
4399 C CA  . LEU A 282 ? 0.3687 0.3445 0.2681 0.0845  -0.0419 0.0165  281 LEU A CA  
4400 C C   . LEU A 282 ? 0.3425 0.3288 0.2493 0.0886  -0.0535 0.0151  281 LEU A C   
4401 O O   . LEU A 282 ? 0.3731 0.3618 0.2669 0.0932  -0.0625 0.0157  281 LEU A O   
4402 C CB  . LEU A 282 ? 0.3959 0.3606 0.2929 0.0882  -0.0339 0.0260  281 LEU A CB  
4403 C CG  . LEU A 282 ? 0.4439 0.4013 0.3440 0.0821  -0.0221 0.0274  281 LEU A CG  
4404 C CD1 . LEU A 282 ? 0.5079 0.4526 0.3991 0.0860  -0.0148 0.0382  281 LEU A CD1 
4405 C CD2 . LEU A 282 ? 0.4816 0.4422 0.4019 0.0756  -0.0193 0.0223  281 LEU A CD2 
4417 N N   . PRO A 283 ? 0.3666 0.3605 0.2944 0.0870  -0.0537 0.0130  282 PRO A N   
4418 C CA  . PRO A 283 ? 0.3586 0.3650 0.2978 0.0916  -0.0637 0.0130  282 PRO A CA  
4419 C C   . PRO A 283 ? 0.3936 0.3956 0.3256 0.1022  -0.0663 0.0225  282 PRO A C   
4420 O O   . PRO A 283 ? 0.4644 0.4525 0.3884 0.1054  -0.0581 0.0294  282 PRO A O   
4421 C CB  . PRO A 283 ? 0.3775 0.3909 0.3399 0.0883  -0.0589 0.0096  282 PRO A CB  
4422 C CG  . PRO A 283 ? 0.3776 0.3777 0.3370 0.0850  -0.0468 0.0107  282 PRO A CG  
4423 C CD  . PRO A 283 ? 0.3937 0.3858 0.3356 0.0815  -0.0445 0.0108  282 PRO A CD  
4431 N N   . VAL A 284 ? 0.3582 0.3731 0.2952 0.1073  -0.0784 0.0233  283 VAL A N   
4432 C CA  . VAL A 284 ? 0.3969 0.4110 0.3281 0.1188  -0.0838 0.0332  283 VAL A CA  
4433 C C   . VAL A 284 ? 0.3904 0.4189 0.3467 0.1245  -0.0886 0.0349  283 VAL A C   
4434 O O   . VAL A 284 ? 0.3911 0.4196 0.3467 0.1355  -0.0926 0.0442  283 VAL A O   
4435 C CB  . VAL A 284 ? 0.4547 0.4715 0.3633 0.1223  -0.0960 0.0344  283 VAL A CB  
4436 C CG1 . VAL A 284 ? 0.4789 0.4805 0.3616 0.1187  -0.0889 0.0336  283 VAL A CG1 
4437 C CG2 . VAL A 284 ? 0.4516 0.4873 0.3707 0.1173  -0.1099 0.0253  283 VAL A CG2 
4447 N N   . ASP A 285 ? 0.3736 0.4153 0.3522 0.1180  -0.0881 0.0271  284 ASP A N   
4448 C CA  . ASP A 285 ? 0.3741 0.4314 0.3794 0.1234  -0.0904 0.0285  284 ASP A CA  
4449 C C   . ASP A 285 ? 0.3248 0.3873 0.3488 0.1152  -0.0813 0.0208  284 ASP A C   
4450 O O   . ASP A 285 ? 0.3295 0.3867 0.3467 0.1051  -0.0768 0.0143  284 ASP A O   
4451 C CB  . ASP A 285 ? 0.3966 0.4758 0.4112 0.1268  -0.1073 0.0294  284 ASP A CB  
4452 C CG  . ASP A 285 ? 0.4205 0.5110 0.4364 0.1151  -0.1157 0.0196  284 ASP A CG  
4453 O OD1 . ASP A 285 ? 0.4055 0.4858 0.4128 0.1055  -0.1086 0.0130  284 ASP A OD1 
4454 O OD2 . ASP A 285 ? 0.4263 0.5360 0.4528 0.1158  -0.1305 0.0189  284 ASP A OD2 
4459 N N   . PHE A 286 ? 0.3261 0.3987 0.3731 0.1207  -0.0779 0.0222  285 PHE A N   
4460 C CA  . PHE A 286 ? 0.3541 0.4267 0.4142 0.1157  -0.0657 0.0165  285 PHE A CA  
4461 C C   . PHE A 286 ? 0.3464 0.4406 0.4356 0.1201  -0.0660 0.0166  285 PHE A C   
4462 O O   . PHE A 286 ? 0.3538 0.4594 0.4550 0.1301  -0.0731 0.0227  285 PHE A O   
4463 C CB  . PHE A 286 ? 0.3832 0.4336 0.4341 0.1192  -0.0529 0.0179  285 PHE A CB  
4464 C CG  . PHE A 286 ? 0.4081 0.4388 0.4344 0.1162  -0.0515 0.0200  285 PHE A CG  
4465 C CD1 . PHE A 286 ? 0.4002 0.4236 0.4160 0.1054  -0.0467 0.0143  285 PHE A CD1 
4466 C CD2 . PHE A 286 ? 0.4943 0.5152 0.5084 0.1247  -0.0552 0.0289  285 PHE A CD2 
4467 C CE1 . PHE A 286 ? 0.4094 0.4171 0.4051 0.1029  -0.0448 0.0170  285 PHE A CE1 
4468 C CE2 . PHE A 286 ? 0.5190 0.5228 0.5110 0.1220  -0.0527 0.0319  285 PHE A CE2 
4469 C CZ  . PHE A 286 ? 0.4570 0.4550 0.4408 0.1110  -0.0473 0.0257  285 PHE A CZ  
4479 N N   . VAL A 287 ? 0.2976 0.3980 0.3984 0.1129  -0.0578 0.0105  286 VAL A N   
4480 C CA  . VAL A 287 ? 0.2728 0.3891 0.3994 0.1175  -0.0513 0.0104  286 VAL A CA  
4481 C C   . VAL A 287 ? 0.2613 0.3593 0.3814 0.1219  -0.0361 0.0086  286 VAL A C   
4482 O O   . VAL A 287 ? 0.2782 0.3605 0.3815 0.1143  -0.0294 0.0037  286 VAL A O   
4483 C CB  . VAL A 287 ? 0.2882 0.4223 0.4303 0.1068  -0.0505 0.0057  286 VAL A CB  
4484 C CG1 . VAL A 287 ? 0.3232 0.4755 0.4931 0.1123  -0.0419 0.0066  286 VAL A CG1 
4485 C CG2 . VAL A 287 ? 0.3132 0.4615 0.4598 0.1003  -0.0664 0.0056  286 VAL A CG2 
4495 N N   . THR A 288 ? 0.2836 0.3833 0.4167 0.1344  -0.0313 0.0121  287 THR A N   
4496 C CA  . THR A 288 ? 0.3359 0.4149 0.4614 0.1398  -0.0177 0.0095  287 THR A CA  
4497 C C   . THR A 288 ? 0.3169 0.4077 0.4607 0.1430  -0.0060 0.0054  287 THR A C   
4498 O O   . THR A 288 ? 0.3204 0.4371 0.4876 0.1440  -0.0084 0.0073  287 THR A O   
4499 C CB  . THR A 288 ? 0.3773 0.4428 0.5008 0.1534  -0.0187 0.0167  287 THR A CB  
4500 O OG1 . THR A 288 ? 0.3369 0.4248 0.4852 0.1646  -0.0241 0.0232  287 THR A OG1 
4501 C CG2 . THR A 288 ? 0.4123 0.4645 0.5149 0.1508  -0.0280 0.0218  287 THR A CG2 
4509 N N   . ALA A 289 ? 0.3208 0.3921 0.4536 0.1444  0.0069  -0.0004 288 ALA A N   
4510 C CA  . ALA A 289 ? 0.3276 0.4058 0.4715 0.1479  0.0202  -0.0054 288 ALA A CA  
4511 C C   . ALA A 289 ? 0.3428 0.3968 0.4787 0.1581  0.0313  -0.0088 288 ALA A C   
4512 O O   . ALA A 289 ? 0.3644 0.3924 0.4796 0.1550  0.0310  -0.0111 288 ALA A O   
4513 C CB  . ALA A 289 ? 0.3471 0.4265 0.4798 0.1346  0.0254  -0.0125 288 ALA A CB  
4519 N N   . ASP A 290 ? 0.3507 0.4124 0.5038 0.1701  0.0416  -0.0094 289 ASP A N   
4520 C CA  . ASP A 290 ? 0.4171 0.4533 0.5625 0.1805  0.0534  -0.0141 289 ASP A CA  
4521 C C   . ASP A 290 ? 0.4649 0.4841 0.5896 0.1734  0.0653  -0.0266 289 ASP A C   
4522 O O   . ASP A 290 ? 0.5409 0.5351 0.6552 0.1799  0.0748  -0.0331 289 ASP A O   
4523 C CB  . ASP A 290 ? 0.4507 0.5001 0.6226 0.1986  0.0606  -0.0097 289 ASP A CB  
4524 C CG  . ASP A 290 ? 0.5268 0.5992 0.7143 0.2000  0.0721  -0.0135 289 ASP A CG  
4525 O OD1 . ASP A 290 ? 0.5039 0.5846 0.6830 0.1867  0.0731  -0.0181 289 ASP A OD1 
4526 O OD2 . ASP A 290 ? 0.5646 0.6468 0.7737 0.2154  0.0811  -0.0110 289 ASP A OD2 
4531 N N   . LYS A 291 ? 0.4022 0.4330 0.5195 0.1603  0.0643  -0.0303 290 LYS A N   
4532 C CA  . LYS A 291 ? 0.4244 0.4403 0.5188 0.1524  0.0727  -0.0413 290 LYS A CA  
4533 C C   . LYS A 291 ? 0.4171 0.4478 0.5055 0.1375  0.0663  -0.0405 290 LYS A C   
4534 O O   . LYS A 291 ? 0.4007 0.4539 0.5054 0.1346  0.0583  -0.0327 290 LYS A O   
4535 C CB  . LYS A 291 ? 0.4984 0.5158 0.5959 0.1620  0.0894  -0.0481 290 LYS A CB  
4536 C CG  . LYS A 291 ? 0.6619 0.7130 0.7839 0.1655  0.0942  -0.0425 290 LYS A CG  
4537 C CD  . LYS A 291 ? 0.9053 0.9565 1.0300 0.1771  0.1129  -0.0487 290 LYS A CD  
4538 C CE  . LYS A 291 ? 1.0950 1.1813 1.2456 0.1795  0.1195  -0.0424 290 LYS A CE  
4539 N NZ  . LYS A 291 ? 1.2333 1.3199 1.3829 0.1903  0.1400  -0.0488 290 LYS A NZ  
4553 N N   . PHE A 292 ? 0.4126 0.4296 0.4774 0.1280  0.0691  -0.0486 291 PHE A N   
4554 C CA  . PHE A 292 ? 0.4413 0.4689 0.4983 0.1145  0.0634  -0.0475 291 PHE A CA  
4555 C C   . PHE A 292 ? 0.4403 0.4872 0.5037 0.1151  0.0733  -0.0480 291 PHE A C   
4556 O O   . PHE A 292 ? 0.4746 0.5153 0.5203 0.1124  0.0816  -0.0550 291 PHE A O   
4557 C CB  . PHE A 292 ? 0.5018 0.5087 0.5328 0.1046  0.0606  -0.0543 291 PHE A CB  
4558 C CG  . PHE A 292 ? 0.4586 0.4751 0.4830 0.0920  0.0531  -0.0514 291 PHE A CG  
4559 C CD1 . PHE A 292 ? 0.3851 0.4078 0.4168 0.0876  0.0421  -0.0440 291 PHE A CD1 
4560 C CD2 . PHE A 292 ? 0.5105 0.5291 0.5202 0.0856  0.0575  -0.0560 291 PHE A CD2 
4561 C CE1 . PHE A 292 ? 0.3970 0.4268 0.4232 0.0771  0.0361  -0.0416 291 PHE A CE1 
4562 C CE2 . PHE A 292 ? 0.4926 0.5194 0.4973 0.0753  0.0509  -0.0522 291 PHE A CE2 
4563 C CZ  . PHE A 292 ? 0.4659 0.4978 0.4798 0.0713  0.0406  -0.0452 291 PHE A CZ  
4573 N N   . ASP A 293 ? 0.3767 0.4477 0.4662 0.1188  0.0725  -0.0400 292 ASP A N   
4574 C CA  . ASP A 293 ? 0.3834 0.4755 0.4855 0.1205  0.0833  -0.0383 292 ASP A CA  
4575 C C   . ASP A 293 ? 0.3386 0.4571 0.4676 0.1163  0.0756  -0.0287 292 ASP A C   
4576 O O   . ASP A 293 ? 0.3348 0.4586 0.4791 0.1192  0.0649  -0.0238 292 ASP A O   
4577 C CB  . ASP A 293 ? 0.4461 0.5390 0.5581 0.1354  0.0974  -0.0412 292 ASP A CB  
4578 C CG  . ASP A 293 ? 0.5734 0.6858 0.6940 0.1373  0.1119  -0.0402 292 ASP A CG  
4579 O OD1 . ASP A 293 ? 0.5972 0.7363 0.7482 0.1396  0.1128  -0.0319 292 ASP A OD1 
4580 O OD2 . ASP A 293 ? 0.6656 0.7672 0.7622 0.1360  0.1223  -0.0475 292 ASP A OD2 
4585 N N   . GLU A 294 ? 0.2944 0.4286 0.4278 0.1094  0.0809  -0.0260 293 GLU A N   
4586 C CA  . GLU A 294 ? 0.3254 0.4847 0.4858 0.1038  0.0752  -0.0176 293 GLU A CA  
4587 C C   . GLU A 294 ? 0.3003 0.4795 0.4937 0.1139  0.0751  -0.0128 293 GLU A C   
4588 O O   . GLU A 294 ? 0.3116 0.5068 0.5267 0.1102  0.0631  -0.0071 293 GLU A O   
4589 C CB  . GLU A 294 ? 0.4923 0.6637 0.6532 0.0972  0.0861  -0.0152 293 GLU A CB  
4590 C CG  . GLU A 294 ? 0.6300 0.8214 0.8133 0.0870  0.0797  -0.0073 293 GLU A CG  
4591 C CD  . GLU A 294 ? 0.7400 0.9396 0.9207 0.0807  0.0923  -0.0037 293 GLU A CD  
4592 O OE1 . GLU A 294 ? 0.7692 0.9771 0.9598 0.0697  0.0872  0.0020  293 GLU A OE1 
4593 O OE2 . GLU A 294 ? 0.7589 0.9551 0.9262 0.0870  0.1075  -0.0065 293 GLU A OE2 
4600 N N   . ASN A 295 ? 0.2743 0.4533 0.4723 0.1270  0.0883  -0.0152 294 ASN A N   
4601 C CA  . ASN A 295 ? 0.3126 0.5133 0.5449 0.1386  0.0906  -0.0098 294 ASN A CA  
4602 C C   . ASN A 295 ? 0.3052 0.4914 0.5360 0.1512  0.0858  -0.0112 294 ASN A C   
4603 O O   . ASN A 295 ? 0.3026 0.5009 0.5565 0.1650  0.0919  -0.0081 294 ASN A O   
4604 C CB  . ASN A 295 ? 0.4344 0.6495 0.6786 0.1460  0.1111  -0.0097 294 ASN A CB  
4605 C CG  . ASN A 295 ? 0.4935 0.7245 0.7417 0.1338  0.1169  -0.0059 294 ASN A CG  
4606 O OD1 . ASN A 295 ? 0.4352 0.6830 0.7024 0.1234  0.1060  0.0005  294 ASN A OD1 
4607 N ND2 . ASN A 295 ? 0.5573 0.7813 0.7858 0.1350  0.1338  -0.0099 294 ASN A ND2 
4614 N N   . ALA A 296 ? 0.3483 0.5094 0.5541 0.1472  0.0753  -0.0146 295 ALA A N   
4615 C CA  . ALA A 296 ? 0.4035 0.5482 0.6063 0.1581  0.0705  -0.0144 295 ALA A CA  
4616 C C   . ALA A 296 ? 0.3857 0.5529 0.6192 0.1648  0.0591  -0.0048 295 ALA A C   
4617 O O   . ALA A 296 ? 0.3738 0.5637 0.6240 0.1565  0.0489  0.0002  295 ALA A O   
4618 C CB  . ALA A 296 ? 0.4109 0.5283 0.5838 0.1497  0.0606  -0.0179 295 ALA A CB  
4624 N N   . LYS A 297 ? 0.3786 0.5385 0.6192 0.1801  0.0602  -0.0024 296 LYS A N   
4625 C CA  . LYS A 297 ? 0.4078 0.5829 0.6693 0.1866  0.0455  0.0071  296 LYS A CA  
4626 C C   . LYS A 297 ? 0.3700 0.5314 0.6101 0.1762  0.0288  0.0081  296 LYS A C   
4627 O O   . LYS A 297 ? 0.3797 0.5120 0.5900 0.1714  0.0305  0.0028  296 LYS A O   
4628 C CB  . LYS A 297 ? 0.4849 0.6506 0.7549 0.2062  0.0508  0.0104  296 LYS A CB  
4629 C CG  . LYS A 297 ? 0.5932 0.7706 0.8835 0.2186  0.0695  0.0087  296 LYS A CG  
4630 C CD  . LYS A 297 ? 0.7042 0.8689 1.0011 0.2361  0.0740  0.0107  296 LYS A CD  
4631 C CE  . LYS A 297 ? 0.7682 0.9413 1.0780 0.2426  0.0909  0.0058  296 LYS A CE  
4632 N NZ  . LYS A 297 ? 0.8153 0.9709 1.1263 0.2572  0.0958  0.0052  296 LYS A NZ  
4646 N N   . THR A 298 ? 0.3164 0.4994 0.5715 0.1719  0.0128  0.0144  297 THR A N   
4647 C CA  . THR A 298 ? 0.3482 0.5200 0.5824 0.1622  -0.0024 0.0150  297 THR A CA  
4648 C C   . THR A 298 ? 0.3462 0.5203 0.5853 0.1725  -0.0159 0.0234  297 THR A C   
4649 O O   . THR A 298 ? 0.3638 0.5544 0.6279 0.1859  -0.0163 0.0297  297 THR A O   
4650 C CB  . THR A 298 ? 0.4010 0.5909 0.6409 0.1465  -0.0112 0.0136  297 THR A CB  
4651 O OG1 . THR A 298 ? 0.4453 0.6675 0.7180 0.1489  -0.0208 0.0195  297 THR A OG1 
4652 C CG2 . THR A 298 ? 0.4188 0.6086 0.6557 0.1373  0.0028  0.0075  297 THR A CG2 
4660 N N   . GLY A 299 ? 0.3389 0.4962 0.5531 0.1668  -0.0265 0.0241  298 GLY A N   
4661 C CA  . GLY A 299 ? 0.3671 0.5240 0.5788 0.1753  -0.0401 0.0325  298 GLY A CA  
4662 C C   . GLY A 299 ? 0.3255 0.4756 0.5141 0.1641  -0.0535 0.0319  298 GLY A C   
4663 O O   . GLY A 299 ? 0.3054 0.4543 0.4846 0.1499  -0.0531 0.0250  298 GLY A O   
4667 N N   . GLN A 300 ? 0.3333 0.4786 0.5119 0.1714  -0.0648 0.0395  299 GLN A N   
4668 C CA  . GLN A 300 ? 0.3738 0.5104 0.5270 0.1634  -0.0763 0.0394  299 GLN A CA  
4669 C C   . GLN A 300 ? 0.3421 0.4506 0.4706 0.1711  -0.0735 0.0457  299 GLN A C   
4670 O O   . GLN A 300 ? 0.3578 0.4601 0.4931 0.1851  -0.0694 0.0529  299 GLN A O   
4671 C CB  . GLN A 300 ? 0.5004 0.6626 0.6637 0.1634  -0.0960 0.0430  299 GLN A CB  
4672 C CG  . GLN A 300 ? 0.6796 0.8694 0.8680 0.1529  -0.1006 0.0369  299 GLN A CG  
4673 C CD  . GLN A 300 ? 0.9178 1.1347 1.1445 0.1620  -0.0990 0.0412  299 GLN A CD  
4674 O OE1 . GLN A 300 ? 1.0245 1.2466 1.2608 0.1771  -0.1022 0.0500  299 GLN A OE1 
4675 N NE2 . GLN A 300 ? 0.9800 1.2147 1.2298 0.1534  -0.0931 0.0360  299 GLN A NE2 
4684 N N   . ALA A 301 ? 0.3377 0.4291 0.4386 0.1622  -0.0750 0.0433  300 ALA A N   
4685 C CA  . ALA A 301 ? 0.3822 0.4474 0.4592 0.1674  -0.0719 0.0500  300 ALA A CA  
4686 C C   . ALA A 301 ? 0.3709 0.4307 0.4221 0.1593  -0.0801 0.0495  300 ALA A C   
4687 O O   . ALA A 301 ? 0.3942 0.4627 0.4433 0.1476  -0.0837 0.0414  300 ALA A O   
4688 C CB  . ALA A 301 ? 0.4200 0.4602 0.4908 0.1651  -0.0549 0.0460  300 ALA A CB  
4694 N N   . THR A 302 ? 0.4081 0.4521 0.4390 0.1663  -0.0819 0.0589  301 THR A N   
4695 C CA  . THR A 302 ? 0.4373 0.4708 0.4398 0.1600  -0.0854 0.0592  301 THR A CA  
4696 C C   . THR A 302 ? 0.4506 0.4556 0.4366 0.1598  -0.0720 0.0635  301 THR A C   
4697 O O   . THR A 302 ? 0.4358 0.4280 0.4309 0.1653  -0.0623 0.0667  301 THR A O   
4698 C CB  . THR A 302 ? 0.4780 0.5212 0.4682 0.1679  -0.1012 0.0672  301 THR A CB  
4699 O OG1 . THR A 302 ? 0.4512 0.4857 0.4405 0.1826  -0.1004 0.0806  301 THR A OG1 
4700 C CG2 . THR A 302 ? 0.5281 0.6012 0.5386 0.1668  -0.1157 0.0624  301 THR A CG2 
4708 N N   . VAL A 303 ? 0.4542 0.4487 0.4160 0.1536  -0.0714 0.0637  302 VAL A N   
4709 C CA  . VAL A 303 ? 0.5077 0.4771 0.4553 0.1526  -0.0590 0.0692  302 VAL A CA  
4710 C C   . VAL A 303 ? 0.5379 0.4951 0.4809 0.1661  -0.0584 0.0836  302 VAL A C   
4711 O O   . VAL A 303 ? 0.5819 0.5185 0.5268 0.1677  -0.0469 0.0880  302 VAL A O   
4712 C CB  . VAL A 303 ? 0.6047 0.5684 0.5286 0.1447  -0.0581 0.0679  302 VAL A CB  
4713 C CG1 . VAL A 303 ? 0.6913 0.6312 0.6027 0.1440  -0.0454 0.0757  302 VAL A CG1 
4714 C CG2 . VAL A 303 ? 0.5693 0.5414 0.4994 0.1320  -0.0567 0.0546  302 VAL A CG2 
4724 N N   . ALA A 304 ? 0.5792 0.5483 0.5155 0.1760  -0.0714 0.0913  303 ALA A N   
4725 C CA  . ALA A 304 ? 0.6072 0.5663 0.5386 0.1907  -0.0723 0.1071  303 ALA A CA  
4726 C C   . ALA A 304 ? 0.5927 0.5502 0.5504 0.1995  -0.0677 0.1091  303 ALA A C   
4727 O O   . ALA A 304 ? 0.5981 0.5350 0.5546 0.2081  -0.0597 0.1198  303 ALA A O   
4728 C CB  . ALA A 304 ? 0.6377 0.6142 0.5570 0.1992  -0.0897 0.1137  303 ALA A CB  
4734 N N   . SER A 305 ? 0.5080 0.4865 0.4897 0.1981  -0.0720 0.0996  304 SER A N   
4735 C CA  . SER A 305 ? 0.4989 0.4779 0.5061 0.2078  -0.0667 0.1010  304 SER A CA  
4736 C C   . SER A 305 ? 0.5175 0.4750 0.5304 0.2013  -0.0496 0.0931  304 SER A C   
4737 O O   . SER A 305 ? 0.5648 0.5093 0.5899 0.2105  -0.0413 0.0963  304 SER A O   
4738 C CB  . SER A 305 ? 0.4843 0.4953 0.5169 0.2086  -0.0759 0.0940  304 SER A CB  
4739 O OG  . SER A 305 ? 0.4470 0.4629 0.4886 0.1951  -0.0690 0.0793  304 SER A OG  
4745 N N   . GLY A 306 ? 0.4862 0.4400 0.4907 0.1858  -0.0446 0.0823  305 GLY A N   
4746 C CA  . GLY A 306 ? 0.5584 0.4974 0.5696 0.1784  -0.0312 0.0726  305 GLY A CA  
4747 C C   . GLY A 306 ? 0.5043 0.4606 0.5381 0.1783  -0.0296 0.0623  305 GLY A C   
4748 O O   . GLY A 306 ? 0.4383 0.4170 0.4877 0.1863  -0.0376 0.0646  305 GLY A O   
4752 N N   . ILE A 307 ? 0.4785 0.4251 0.5139 0.1691  -0.0192 0.0513  306 ILE A N   
4753 C CA  . ILE A 307 ? 0.4270 0.3858 0.4803 0.1689  -0.0143 0.0415  306 ILE A CA  
4754 C C   . ILE A 307 ? 0.4647 0.4045 0.5263 0.1800  -0.0037 0.0424  306 ILE A C   
4755 O O   . ILE A 307 ? 0.5856 0.4971 0.6356 0.1779  0.0038  0.0427  306 ILE A O   
4756 C CB  . ILE A 307 ? 0.4192 0.3782 0.4660 0.1531  -0.0097 0.0293  306 ILE A CB  
4757 C CG1 . ILE A 307 ? 0.4205 0.3975 0.4608 0.1442  -0.0201 0.0292  306 ILE A CG1 
4758 C CG2 . ILE A 307 ? 0.4297 0.3979 0.4911 0.1531  -0.0023 0.0196  306 ILE A CG2 
4759 C CD1 . ILE A 307 ? 0.4405 0.4169 0.4728 0.1297  -0.0167 0.0199  306 ILE A CD1 
4771 N N   . PRO A 308 ? 0.4702 0.4234 0.5523 0.1921  -0.0024 0.0431  307 PRO A N   
4772 C CA  . PRO A 308 ? 0.5744 0.5070 0.6639 0.2045  0.0087  0.0439  307 PRO A CA  
4773 C C   . PRO A 308 ? 0.5972 0.5074 0.6786 0.1960  0.0218  0.0303  307 PRO A C   
4774 O O   . PRO A 308 ? 0.4940 0.4126 0.5706 0.1831  0.0231  0.0197  307 PRO A O   
4775 C CB  . PRO A 308 ? 0.6028 0.5616 0.7186 0.2174  0.0078  0.0454  307 PRO A CB  
4776 C CG  . PRO A 308 ? 0.5488 0.5408 0.6710 0.2124  -0.0064 0.0484  307 PRO A CG  
4777 C CD  . PRO A 308 ? 0.4570 0.4447 0.5585 0.1942  -0.0095 0.0422  307 PRO A CD  
4785 N N   . ALA A 309 ? 0.6818 0.5626 0.7616 0.2038  0.0313  0.0308  308 ALA A N   
4786 C CA  . ALA A 309 ? 0.6978 0.5541 0.7686 0.1962  0.0430  0.0170  308 ALA A CA  
4787 C C   . ALA A 309 ? 0.6606 0.5337 0.7401 0.1961  0.0492  0.0046  308 ALA A C   
4788 O O   . ALA A 309 ? 0.6251 0.5161 0.7232 0.2092  0.0511  0.0072  308 ALA A O   
4789 C CB  . ALA A 309 ? 0.7477 0.5693 0.8186 0.2069  0.0524  0.0193  308 ALA A CB  
4795 N N   . GLY A 310 ? 0.6507 0.5188 0.7171 0.1815  0.0527  -0.0081 309 GLY A N   
4796 C CA  . GLY A 310 ? 0.6533 0.5356 0.7233 0.1802  0.0593  -0.0195 309 GLY A CA  
4797 C C   . GLY A 310 ? 0.5897 0.5085 0.6686 0.1752  0.0519  -0.0171 309 GLY A C   
4798 O O   . GLY A 310 ? 0.5837 0.5160 0.6656 0.1732  0.0579  -0.0251 309 GLY A O   
4802 N N   . TRP A 311 ? 0.4925 0.4267 0.5749 0.1731  0.0396  -0.0064 310 TRP A N   
4803 C CA  . TRP A 311 ? 0.4065 0.3719 0.4961 0.1662  0.0315  -0.0049 310 TRP A CA  
4804 C C   . TRP A 311 ? 0.3655 0.3274 0.4372 0.1500  0.0251  -0.0069 310 TRP A C   
4805 O O   . TRP A 311 ? 0.4058 0.3453 0.4627 0.1454  0.0248  -0.0062 310 TRP A O   
4806 C CB  . TRP A 311 ? 0.4257 0.4128 0.5324 0.1756  0.0211  0.0071  310 TRP A CB  
4807 C CG  . TRP A 311 ? 0.4651 0.4648 0.5954 0.1915  0.0261  0.0102  310 TRP A CG  
4808 C CD1 . TRP A 311 ? 0.5064 0.4875 0.6411 0.2054  0.0359  0.0107  310 TRP A CD1 
4809 C CD2 . TRP A 311 ? 0.4504 0.4850 0.6055 0.1957  0.0218  0.0138  310 TRP A CD2 
4810 N NE1 . TRP A 311 ? 0.4981 0.5014 0.6591 0.2191  0.0385  0.0146  310 TRP A NE1 
4811 C CE2 . TRP A 311 ? 0.4672 0.5047 0.6422 0.2129  0.0297  0.0169  310 TRP A CE2 
4812 C CE3 . TRP A 311 ? 0.4562 0.5192 0.6202 0.1862  0.0123  0.0146  310 TRP A CE3 
4813 C CZ2 . TRP A 311 ? 0.4756 0.5466 0.6806 0.2208  0.0283  0.0214  310 TRP A CZ2 
4814 C CZ3 . TRP A 311 ? 0.5289 0.6233 0.7221 0.1926  0.0104  0.0186  310 TRP A CZ3 
4815 C CH2 . TRP A 311 ? 0.5618 0.6616 0.7762 0.2098  0.0183  0.0222  310 TRP A CH2 
4826 N N   . MET A 312 ? 0.3660 0.3500 0.4404 0.1414  0.0207  -0.0089 311 MET A N   
4827 C CA  . MET A 312 ? 0.3521 0.3345 0.4113 0.1271  0.0154  -0.0109 311 MET A CA  
4828 C C   . MET A 312 ? 0.3194 0.3257 0.3857 0.1233  0.0048  -0.0061 311 MET A C   
4829 O O   . MET A 312 ? 0.3177 0.3459 0.4016 0.1269  0.0035  -0.0050 311 MET A O   
4830 C CB  . MET A 312 ? 0.4184 0.3971 0.4680 0.1173  0.0226  -0.0215 311 MET A CB  
4831 C CG  . MET A 312 ? 0.5654 0.5623 0.6262 0.1192  0.0287  -0.0258 311 MET A CG  
4832 S SD  . MET A 312 ? 0.5746 0.5633 0.6183 0.1094  0.0376  -0.0377 311 MET A SD  
4833 C CE  . MET A 312 ? 0.6480 0.6090 0.6839 0.1177  0.0481  -0.0454 311 MET A CE  
4843 N N   . GLY A 313 ? 0.3033 0.3052 0.3565 0.1156  -0.0022 -0.0036 312 GLY A N   
4844 C CA  . GLY A 313 ? 0.3064 0.3268 0.3626 0.1107  -0.0122 -0.0010 312 GLY A CA  
4845 C C   . GLY A 313 ? 0.3085 0.3375 0.3636 0.0995  -0.0099 -0.0074 312 GLY A C   
4846 O O   . GLY A 313 ? 0.3050 0.3218 0.3462 0.0918  -0.0064 -0.0112 312 GLY A O   
4850 N N   . LEU A 314 ? 0.2948 0.3449 0.3656 0.0985  -0.0119 -0.0079 313 LEU A N   
4851 C CA  . LEU A 314 ? 0.3006 0.3588 0.3718 0.0888  -0.0086 -0.0125 313 LEU A CA  
4852 C C   . LEU A 314 ? 0.3220 0.3933 0.3975 0.0818  -0.0179 -0.0109 313 LEU A C   
4853 O O   . LEU A 314 ? 0.2809 0.3576 0.3569 0.0736  -0.0155 -0.0134 313 LEU A O   
4854 C CB  . LEU A 314 ? 0.2679 0.3381 0.3542 0.0922  0.0006  -0.0148 313 LEU A CB  
4855 C CG  . LEU A 314 ? 0.2802 0.3355 0.3598 0.0984  0.0116  -0.0190 313 LEU A CG  
4856 C CD1 . LEU A 314 ? 0.2769 0.3448 0.3679 0.1009  0.0220  -0.0219 313 LEU A CD1 
4857 C CD2 . LEU A 314 ? 0.3156 0.3508 0.3725 0.0910  0.0138  -0.0238 313 LEU A CD2 
4869 N N   . ASP A 315 ? 0.2761 0.3513 0.3532 0.0849  -0.0285 -0.0070 314 ASP A N   
4870 C CA  . ASP A 315 ? 0.2553 0.3383 0.3321 0.0780  -0.0383 -0.0072 314 ASP A CA  
4871 C C   . ASP A 315 ? 0.2868 0.3646 0.3532 0.0830  -0.0485 -0.0035 314 ASP A C   
4872 O O   . ASP A 315 ? 0.2828 0.3566 0.3490 0.0925  -0.0487 0.0008  314 ASP A O   
4873 C CB  . ASP A 315 ? 0.2710 0.3767 0.3721 0.0758  -0.0413 -0.0073 314 ASP A CB  
4874 C CG  . ASP A 315 ? 0.3647 0.4757 0.4663 0.0657  -0.0492 -0.0096 314 ASP A CG  
4875 O OD1 . ASP A 315 ? 0.3822 0.4794 0.4655 0.0600  -0.0489 -0.0119 314 ASP A OD1 
4876 O OD2 . ASP A 315 ? 0.3696 0.4992 0.4918 0.0636  -0.0557 -0.0092 314 ASP A OD2 
4881 N N   . CYS A 316 ? 0.2996 0.3764 0.3561 0.0770  -0.0563 -0.0051 315 CYS A N   
4882 C CA  . CYS A 316 ? 0.3675 0.4419 0.4126 0.0818  -0.0669 -0.0020 315 CYS A CA  
4883 C C   . CYS A 316 ? 0.3709 0.4658 0.4337 0.0841  -0.0787 -0.0012 315 CYS A C   
4884 O O   . CYS A 316 ? 0.4125 0.5237 0.4974 0.0799  -0.0787 -0.0034 315 CYS A O   
4885 C CB  . CYS A 316 ? 0.4435 0.5067 0.4679 0.0755  -0.0695 -0.0050 315 CYS A CB  
4886 S SG  . CYS A 316 ? 0.5173 0.5911 0.5506 0.0646  -0.0760 -0.0119 315 CYS A SG  
4892 N N   . GLY A 317 ? 0.3448 0.4400 0.3986 0.0910  -0.0891 0.0028  316 GLY A N   
4893 C CA  . GLY A 317 ? 0.3426 0.4586 0.4127 0.0937  -0.1027 0.0042  316 GLY A CA  
4894 C C   . GLY A 317 ? 0.3313 0.4500 0.3907 0.0865  -0.1161 -0.0012 316 GLY A C   
4895 O O   . GLY A 317 ? 0.3303 0.4343 0.3708 0.0796  -0.1132 -0.0062 316 GLY A O   
4899 N N   . PRO A 318 ? 0.3791 0.5166 0.4506 0.0883  -0.1313 -0.0006 317 PRO A N   
4900 C CA  . PRO A 318 ? 0.3770 0.5173 0.4393 0.0802  -0.1456 -0.0078 317 PRO A CA  
4901 C C   . PRO A 318 ? 0.3537 0.4741 0.3779 0.0828  -0.1493 -0.0088 317 PRO A C   
4902 O O   . PRO A 318 ? 0.3573 0.4686 0.3667 0.0744  -0.1524 -0.0171 317 PRO A O   
4903 C CB  . PRO A 318 ? 0.4329 0.5998 0.5184 0.0832  -0.1617 -0.0055 317 PRO A CB  
4904 C CG  . PRO A 318 ? 0.4680 0.6395 0.5616 0.0975  -0.1571 0.0052  317 PRO A CG  
4905 C CD  . PRO A 318 ? 0.4607 0.6183 0.5560 0.0979  -0.1366 0.0063  317 PRO A CD  
4913 N N   . GLU A 319 ? 0.3311 0.4434 0.3384 0.0945  -0.1483 -0.0003 318 GLU A N   
4914 C CA  . GLU A 319 ? 0.4080 0.5021 0.3784 0.0970  -0.1503 -0.0004 318 GLU A CA  
4915 C C   . GLU A 319 ? 0.3789 0.4523 0.3345 0.0916  -0.1347 -0.0037 318 GLU A C   
4916 O O   . GLU A 319 ? 0.3655 0.4264 0.2962 0.0887  -0.1357 -0.0086 318 GLU A O   
4917 C CB  . GLU A 319 ? 0.5813 0.6715 0.5378 0.1109  -0.1518 0.0115  318 GLU A CB  
4918 C CG  . GLU A 319 ? 0.7657 0.8766 0.7309 0.1176  -0.1705 0.0153  318 GLU A CG  
4919 C CD  . GLU A 319 ? 0.8946 1.0100 0.8412 0.1127  -0.1882 0.0071  318 GLU A CD  
4920 O OE1 . GLU A 319 ? 0.9110 1.0078 0.8249 0.1106  -0.1857 0.0029  318 GLU A OE1 
4921 O OE2 . GLU A 319 ? 0.9312 1.0691 0.8965 0.1108  -0.2048 0.0044  318 GLU A OE2 
4928 N N   . SER A 320 ? 0.3583 0.4286 0.3292 0.0904  -0.1205 -0.0014 319 SER A N   
4929 C CA  . SER A 320 ? 0.3605 0.4150 0.3218 0.0844  -0.1072 -0.0046 319 SER A CA  
4930 C C   . SER A 320 ? 0.3531 0.4093 0.3178 0.0735  -0.1099 -0.0145 319 SER A C   
4931 O O   . SER A 320 ? 0.3681 0.4105 0.3140 0.0703  -0.1060 -0.0184 319 SER A O   
4932 C CB  . SER A 320 ? 0.3620 0.4150 0.3396 0.0846  -0.0939 -0.0013 319 SER A CB  
4933 O OG  . SER A 320 ? 0.4031 0.4512 0.3781 0.0945  -0.0906 0.0074  319 SER A OG  
4939 N N   . SER A 321 ? 0.3350 0.4077 0.3248 0.0681  -0.1158 -0.0181 320 SER A N   
4940 C CA  . SER A 321 ? 0.3416 0.4145 0.3371 0.0571  -0.1179 -0.0268 320 SER A CA  
4941 C C   . SER A 321 ? 0.3742 0.4388 0.3465 0.0554  -0.1288 -0.0336 320 SER A C   
4942 O O   . SER A 321 ? 0.3918 0.4440 0.3539 0.0493  -0.1256 -0.0402 320 SER A O   
4943 C CB  . SER A 321 ? 0.3693 0.4630 0.3975 0.0516  -0.1229 -0.0281 320 SER A CB  
4944 O OG  . SER A 321 ? 0.3973 0.4955 0.4431 0.0528  -0.1100 -0.0232 320 SER A OG  
4950 N N   . LYS A 322 ? 0.3755 0.4461 0.3377 0.0617  -0.1414 -0.0319 321 LYS A N   
4951 C CA  . LYS A 322 ? 0.3753 0.4373 0.3110 0.0610  -0.1523 -0.0391 321 LYS A CA  
4952 C C   . LYS A 322 ? 0.4099 0.4493 0.3143 0.0647  -0.1410 -0.0389 321 LYS A C   
4953 O O   . LYS A 322 ? 0.4539 0.4807 0.3408 0.0605  -0.1420 -0.0478 321 LYS A O   
4954 C CB  . LYS A 322 ? 0.4125 0.4865 0.3414 0.0686  -0.1682 -0.0354 321 LYS A CB  
4955 C CG  . LYS A 322 ? 0.5460 0.6133 0.4464 0.0675  -0.1821 -0.0441 321 LYS A CG  
4956 C CD  . LYS A 322 ? 0.7094 0.7917 0.6044 0.0750  -0.2000 -0.0399 321 LYS A CD  
4957 C CE  . LYS A 322 ? 0.8980 0.9769 0.7676 0.0713  -0.2175 -0.0515 321 LYS A CE  
4958 N NZ  . LYS A 322 ? 1.0016 1.0554 0.8277 0.0757  -0.2099 -0.0547 321 LYS A NZ  
4972 N N   . LYS A 323 ? 0.4339 0.4675 0.3321 0.0725  -0.1295 -0.0289 322 LYS A N   
4973 C CA  . LYS A 323 ? 0.4504 0.4652 0.3233 0.0758  -0.1173 -0.0270 322 LYS A CA  
4974 C C   . LYS A 323 ? 0.4157 0.4226 0.2965 0.0683  -0.1056 -0.0316 322 LYS A C   
4975 O O   . LYS A 323 ? 0.4449 0.4380 0.3062 0.0683  -0.1000 -0.0355 322 LYS A O   
4976 C CB  . LYS A 323 ? 0.5000 0.5114 0.3692 0.0843  -0.1082 -0.0146 322 LYS A CB  
4977 C CG  . LYS A 323 ? 0.6725 0.6889 0.5301 0.0938  -0.1184 -0.0076 322 LYS A CG  
4978 C CD  . LYS A 323 ? 0.8740 0.8845 0.7302 0.1020  -0.1085 0.0054  322 LYS A CD  
4979 C CE  . LYS A 323 ? 1.0200 1.0128 0.8515 0.1046  -0.0957 0.0099  322 LYS A CE  
4980 N NZ  . LYS A 323 ? 1.0751 1.0615 0.8731 0.1096  -0.1019 0.0091  322 LYS A NZ  
4994 N N   . TYR A 324 ? 0.3788 0.3943 0.2871 0.0631  -0.1009 -0.0305 323 TYR A N   
4995 C CA  . TYR A 324 ? 0.3675 0.3770 0.2837 0.0563  -0.0913 -0.0341 323 TYR A CA  
4996 C C   . TYR A 324 ? 0.3977 0.4017 0.3091 0.0500  -0.0978 -0.0445 323 TYR A C   
4997 O O   . TYR A 324 ? 0.3993 0.3902 0.3002 0.0485  -0.0906 -0.0480 323 TYR A O   
4998 C CB  . TYR A 324 ? 0.3374 0.3584 0.2822 0.0518  -0.0869 -0.0314 323 TYR A CB  
4999 C CG  . TYR A 324 ? 0.3563 0.3795 0.3071 0.0568  -0.0786 -0.0232 323 TYR A CG  
5000 C CD1 . TYR A 324 ? 0.3753 0.3892 0.3090 0.0636  -0.0737 -0.0174 323 TYR A CD1 
5001 C CD2 . TYR A 324 ? 0.4025 0.4359 0.3759 0.0543  -0.0748 -0.0214 323 TYR A CD2 
5002 C CE1 . TYR A 324 ? 0.3860 0.3994 0.3264 0.0669  -0.0661 -0.0108 323 TYR A CE1 
5003 C CE2 . TYR A 324 ? 0.4257 0.4586 0.4032 0.0584  -0.0671 -0.0158 323 TYR A CE2 
5004 C CZ  . TYR A 324 ? 0.4168 0.4390 0.3783 0.0644  -0.0633 -0.0108 323 TYR A CZ  
5005 O OH  . TYR A 324 ? 0.4250 0.4443 0.3914 0.0674  -0.0558 -0.0062 323 TYR A OH  
5015 N N   . ALA A 325 ? 0.4119 0.4259 0.3318 0.0463  -0.1117 -0.0497 324 ALA A N   
5016 C CA  . ALA A 325 ? 0.4222 0.4298 0.3390 0.0389  -0.1193 -0.0607 324 ALA A CA  
5017 C C   . ALA A 325 ? 0.4479 0.4377 0.3302 0.0434  -0.1200 -0.0666 324 ALA A C   
5018 O O   . ALA A 325 ? 0.5029 0.4788 0.3776 0.0392  -0.1180 -0.0751 324 ALA A O   
5019 C CB  . ALA A 325 ? 0.4522 0.4761 0.3859 0.0337  -0.1356 -0.0648 324 ALA A CB  
5025 N N   . GLU A 326 ? 0.4476 0.4367 0.3081 0.0526  -0.1221 -0.0619 325 GLU A N   
5026 C CA  . GLU A 326 ? 0.5058 0.4787 0.3304 0.0582  -0.1216 -0.0667 325 GLU A CA  
5027 C C   . GLU A 326 ? 0.5250 0.4830 0.3412 0.0604  -0.1039 -0.0651 325 GLU A C   
5028 O O   . GLU A 326 ? 0.5226 0.4651 0.3189 0.0610  -0.1014 -0.0734 325 GLU A O   
5029 C CB  . GLU A 326 ? 0.5567 0.5331 0.3607 0.0681  -0.1261 -0.0592 325 GLU A CB  
5030 C CG  . GLU A 326 ? 0.7038 0.6932 0.5088 0.0669  -0.1465 -0.0632 325 GLU A CG  
5031 C CD  . GLU A 326 ? 0.7701 0.7666 0.5610 0.0774  -0.1521 -0.0528 325 GLU A CD  
5032 O OE1 . GLU A 326 ? 0.7699 0.7591 0.5488 0.0853  -0.1391 -0.0424 325 GLU A OE1 
5033 O OE2 . GLU A 326 ? 0.7661 0.7760 0.5595 0.0775  -0.1698 -0.0546 325 GLU A OE2 
5040 N N   . ALA A 327 ? 0.4793 0.4419 0.3114 0.0616  -0.0918 -0.0550 326 ALA A N   
5041 C CA  . ALA A 327 ? 0.4582 0.4104 0.2867 0.0633  -0.0762 -0.0526 326 ALA A CA  
5042 C C   . ALA A 327 ? 0.4356 0.3824 0.2777 0.0561  -0.0741 -0.0598 326 ALA A C   
5043 O O   . ALA A 327 ? 0.4647 0.3982 0.2951 0.0582  -0.0659 -0.0634 326 ALA A O   
5044 C CB  . ALA A 327 ? 0.4565 0.4160 0.2994 0.0652  -0.0659 -0.0408 326 ALA A CB  
5050 N N   . VAL A 328 ? 0.4170 0.3739 0.2845 0.0482  -0.0802 -0.0611 327 VAL A N   
5051 C CA  . VAL A 328 ? 0.3975 0.3485 0.2785 0.0409  -0.0783 -0.0666 327 VAL A CA  
5052 C C   . VAL A 328 ? 0.4442 0.3794 0.3071 0.0395  -0.0846 -0.0792 327 VAL A C   
5053 O O   . VAL A 328 ? 0.4545 0.3756 0.3156 0.0383  -0.0780 -0.0836 327 VAL A O   
5054 C CB  . VAL A 328 ? 0.3767 0.3423 0.2872 0.0327  -0.0839 -0.0651 327 VAL A CB  
5055 C CG1 . VAL A 328 ? 0.4006 0.3586 0.3243 0.0243  -0.0833 -0.0707 327 VAL A CG1 
5056 C CG2 . VAL A 328 ? 0.3478 0.3253 0.2735 0.0344  -0.0756 -0.0543 327 VAL A CG2 
5066 N N   . THR A 329 ? 0.5021 0.4390 0.3509 0.0399  -0.0978 -0.0853 328 THR A N   
5067 C CA  . THR A 329 ? 0.5343 0.4554 0.3630 0.0378  -0.1057 -0.0993 328 THR A CA  
5068 C C   . THR A 329 ? 0.5169 0.4188 0.3156 0.0467  -0.0946 -0.1021 328 THR A C   
5069 O O   . THR A 329 ? 0.5535 0.4370 0.3395 0.0452  -0.0946 -0.1136 328 THR A O   
5070 C CB  . THR A 329 ? 0.6465 0.5764 0.4652 0.0369  -0.1238 -0.1044 328 THR A CB  
5071 O OG1 . THR A 329 ? 0.6549 0.5999 0.5046 0.0265  -0.1346 -0.1057 328 THR A OG1 
5072 C CG2 . THR A 329 ? 0.7310 0.6430 0.5181 0.0375  -0.1317 -0.1190 328 THR A CG2 
5080 N N   . ARG A 330 ? 0.5061 0.4114 0.2936 0.0558  -0.0847 -0.0920 329 ARG A N   
5081 C CA  . ARG A 330 ? 0.5292 0.4195 0.2909 0.0649  -0.0720 -0.0926 329 ARG A CA  
5082 C C   . ARG A 330 ? 0.5239 0.4072 0.2994 0.0655  -0.0567 -0.0897 329 ARG A C   
5083 O O   . ARG A 330 ? 0.5385 0.4074 0.2954 0.0725  -0.0464 -0.0929 329 ARG A O   
5084 C CB  . ARG A 330 ? 0.5612 0.4589 0.3092 0.0737  -0.0662 -0.0812 329 ARG A CB  
5085 C CG  . ARG A 330 ? 0.6399 0.5408 0.3648 0.0768  -0.0798 -0.0832 329 ARG A CG  
5086 C CD  . ARG A 330 ? 0.6404 0.5443 0.3488 0.0864  -0.0714 -0.0708 329 ARG A CD  
5087 N NE  . ARG A 330 ? 0.6131 0.5306 0.3471 0.0856  -0.0653 -0.0570 329 ARG A NE  
5088 C CZ  . ARG A 330 ? 0.6214 0.5520 0.3665 0.0850  -0.0742 -0.0503 329 ARG A CZ  
5089 N NH1 . ARG A 330 ? 0.6410 0.5760 0.3762 0.0850  -0.0905 -0.0549 329 ARG A NH1 
5090 N NH2 . ARG A 330 ? 0.6211 0.5606 0.3880 0.0844  -0.0669 -0.0392 329 ARG A NH2 
5104 N N   . ALA A 331 ? 0.4704 0.3641 0.2772 0.0593  -0.0549 -0.0833 330 ALA A N   
5105 C CA  . ALA A 331 ? 0.4380 0.3292 0.2586 0.0610  -0.0410 -0.0774 330 ALA A CA  
5106 C C   . ALA A 331 ? 0.4672 0.3413 0.2901 0.0584  -0.0394 -0.0864 330 ALA A C   
5107 O O   . ALA A 331 ? 0.5120 0.3805 0.3392 0.0506  -0.0500 -0.0955 330 ALA A O   
5108 C CB  . ALA A 331 ? 0.4191 0.3278 0.2688 0.0560  -0.0398 -0.0667 330 ALA A CB  
5114 N N   . LYS A 332 ? 0.4672 0.3331 0.2889 0.0649  -0.0258 -0.0835 331 LYS A N   
5115 C CA  . LYS A 332 ? 0.4578 0.3088 0.2886 0.0635  -0.0215 -0.0879 331 LYS A CA  
5116 C C   . LYS A 332 ? 0.4091 0.2709 0.2680 0.0617  -0.0147 -0.0759 331 LYS A C   
5117 O O   . LYS A 332 ? 0.4432 0.2945 0.3137 0.0595  -0.0123 -0.0771 331 LYS A O   
5118 C CB  . LYS A 332 ? 0.4671 0.2990 0.2759 0.0739  -0.0108 -0.0940 331 LYS A CB  
5119 C CG  . LYS A 332 ? 0.5445 0.3618 0.3209 0.0755  -0.0181 -0.1083 331 LYS A CG  
5120 C CD  . LYS A 332 ? 0.6734 0.4673 0.4276 0.0852  -0.0072 -0.1172 331 LYS A CD  
5121 C CE  . LYS A 332 ? 0.8054 0.5849 0.5235 0.0869  -0.0152 -0.1321 331 LYS A CE  
5122 N NZ  . LYS A 332 ? 0.8494 0.6227 0.5703 0.0744  -0.0336 -0.1443 331 LYS A NZ  
5136 N N   . GLN A 333 ? 0.3915 0.2726 0.2604 0.0628  -0.0116 -0.0644 332 GLN A N   
5137 C CA  . GLN A 333 ? 0.3738 0.2678 0.2673 0.0599  -0.0079 -0.0535 332 GLN A CA  
5138 C C   . GLN A 333 ? 0.3614 0.2749 0.2625 0.0562  -0.0124 -0.0468 332 GLN A C   
5139 O O   . GLN A 333 ? 0.3771 0.2951 0.2659 0.0599  -0.0120 -0.0457 332 GLN A O   
5140 C CB  . GLN A 333 ? 0.3718 0.2660 0.2693 0.0682  0.0049  -0.0461 332 GLN A CB  
5141 C CG  . GLN A 333 ? 0.3687 0.2757 0.2899 0.0657  0.0075  -0.0351 332 GLN A CG  
5142 C CD  . GLN A 333 ? 0.4035 0.3077 0.3311 0.0739  0.0182  -0.0293 332 GLN A CD  
5143 O OE1 . GLN A 333 ? 0.4337 0.3199 0.3535 0.0797  0.0231  -0.0350 332 GLN A OE1 
5144 N NE2 . GLN A 333 ? 0.4060 0.3279 0.3482 0.0749  0.0216  -0.0182 332 GLN A NE2 
5153 N N   . ILE A 334 ? 0.3146 0.2382 0.2350 0.0492  -0.0159 -0.0423 333 ILE A N   
5154 C CA  . ILE A 334 ? 0.2943 0.2348 0.2233 0.0457  -0.0197 -0.0369 333 ILE A CA  
5155 C C   . ILE A 334 ? 0.2747 0.2259 0.2213 0.0434  -0.0152 -0.0279 333 ILE A C   
5156 O O   . ILE A 334 ? 0.2831 0.2310 0.2399 0.0404  -0.0144 -0.0267 333 ILE A O   
5157 C CB  . ILE A 334 ? 0.3146 0.2582 0.2474 0.0390  -0.0304 -0.0423 333 ILE A CB  
5158 C CG1 . ILE A 334 ? 0.3916 0.3255 0.3056 0.0408  -0.0371 -0.0517 333 ILE A CG1 
5159 C CG2 . ILE A 334 ? 0.2975 0.2579 0.2403 0.0368  -0.0328 -0.0366 333 ILE A CG2 
5160 C CD1 . ILE A 334 ? 0.4129 0.3516 0.3337 0.0337  -0.0494 -0.0575 333 ILE A CD1 
5172 N N   . VAL A 335 ? 0.3019 0.2650 0.2513 0.0446  -0.0126 -0.0216 334 VAL A N   
5173 C CA  . VAL A 335 ? 0.3039 0.2791 0.2674 0.0412  -0.0113 -0.0148 334 VAL A CA  
5174 C C   . VAL A 335 ? 0.2910 0.2754 0.2566 0.0379  -0.0157 -0.0149 334 VAL A C   
5175 O O   . VAL A 335 ? 0.3188 0.3042 0.2768 0.0405  -0.0158 -0.0151 334 VAL A O   
5176 C CB  . VAL A 335 ? 0.3665 0.3477 0.3331 0.0448  -0.0047 -0.0079 334 VAL A CB  
5177 C CG1 . VAL A 335 ? 0.3401 0.3345 0.3179 0.0407  -0.0054 -0.0021 334 VAL A CG1 
5178 C CG2 . VAL A 335 ? 0.4399 0.4135 0.4079 0.0493  0.0003  -0.0064 334 VAL A CG2 
5188 N N   . TRP A 336 ? 0.2605 0.2513 0.2365 0.0329  -0.0182 -0.0141 335 TRP A N   
5189 C CA  . TRP A 336 ? 0.2353 0.2346 0.2151 0.0307  -0.0215 -0.0147 335 TRP A CA  
5190 C C   . TRP A 336 ? 0.2399 0.2486 0.2276 0.0282  -0.0185 -0.0100 335 TRP A C   
5191 O O   . TRP A 336 ? 0.2326 0.2431 0.2268 0.0254  -0.0170 -0.0074 335 TRP A O   
5192 C CB  . TRP A 336 ? 0.2261 0.2254 0.2112 0.0272  -0.0274 -0.0193 335 TRP A CB  
5193 C CG  . TRP A 336 ? 0.2361 0.2459 0.2287 0.0259  -0.0304 -0.0194 335 TRP A CG  
5194 C CD1 . TRP A 336 ? 0.2426 0.2579 0.2342 0.0283  -0.0286 -0.0173 335 TRP A CD1 
5195 C CD2 . TRP A 336 ? 0.2507 0.2662 0.2542 0.0222  -0.0354 -0.0221 335 TRP A CD2 
5196 N NE1 . TRP A 336 ? 0.2483 0.2718 0.2486 0.0277  -0.0316 -0.0183 335 TRP A NE1 
5197 C CE2 . TRP A 336 ? 0.2718 0.2975 0.2809 0.0239  -0.0359 -0.0209 335 TRP A CE2 
5198 C CE3 . TRP A 336 ? 0.2986 0.3118 0.3096 0.0172  -0.0396 -0.0255 335 TRP A CE3 
5199 C CZ2 . TRP A 336 ? 0.3317 0.3677 0.3547 0.0217  -0.0399 -0.0221 335 TRP A CZ2 
5200 C CZ3 . TRP A 336 ? 0.2989 0.3226 0.3244 0.0134  -0.0442 -0.0269 335 TRP A CZ3 
5201 C CH2 . TRP A 336 ? 0.3205 0.3567 0.3525 0.0161  -0.0443 -0.0248 335 TRP A CH2 
5212 N N   . ASN A 337 ? 0.2556 0.2688 0.2412 0.0292  -0.0174 -0.0089 336 ASN A N   
5213 C CA  . ASN A 337 ? 0.2530 0.2740 0.2429 0.0267  -0.0154 -0.0066 336 ASN A CA  
5214 C C   . ASN A 337 ? 0.2675 0.2907 0.2574 0.0274  -0.0166 -0.0092 336 ASN A C   
5215 O O   . ASN A 337 ? 0.2889 0.3082 0.2737 0.0298  -0.0167 -0.0096 336 ASN A O   
5216 C CB  . ASN A 337 ? 0.2770 0.3004 0.2651 0.0267  -0.0129 -0.0031 336 ASN A CB  
5217 C CG  . ASN A 337 ? 0.2880 0.3181 0.2771 0.0238  -0.0124 -0.0029 336 ASN A CG  
5218 O OD1 . ASN A 337 ? 0.3006 0.3312 0.2876 0.0230  -0.0122 -0.0037 336 ASN A OD1 
5219 N ND2 . ASN A 337 ? 0.2509 0.2854 0.2425 0.0219  -0.0118 -0.0019 336 ASN A ND2 
5226 N N   . GLY A 338 ? 0.2926 0.3215 0.2889 0.0258  -0.0165 -0.0102 337 GLY A N   
5227 C CA  . GLY A 338 ? 0.2778 0.3093 0.2756 0.0275  -0.0160 -0.0123 337 GLY A CA  
5228 C C   . GLY A 338 ? 0.2523 0.2867 0.2569 0.0294  -0.0196 -0.0141 337 GLY A C   
5229 O O   . GLY A 338 ? 0.2843 0.3146 0.2856 0.0316  -0.0241 -0.0150 337 GLY A O   
5233 N N   . PRO A 339 ? 0.2473 0.2901 0.2616 0.0288  -0.0178 -0.0145 338 PRO A N   
5234 C CA  . PRO A 339 ? 0.2435 0.2927 0.2684 0.0305  -0.0219 -0.0157 338 PRO A CA  
5235 C C   . PRO A 339 ? 0.2608 0.3064 0.2814 0.0365  -0.0247 -0.0164 338 PRO A C   
5236 O O   . PRO A 339 ? 0.2916 0.3312 0.3051 0.0389  -0.0210 -0.0162 338 PRO A O   
5237 C CB  . PRO A 339 ? 0.2842 0.3442 0.3208 0.0297  -0.0165 -0.0150 338 PRO A CB  
5238 C CG  . PRO A 339 ? 0.3131 0.3712 0.3429 0.0265  -0.0106 -0.0133 338 PRO A CG  
5239 C CD  . PRO A 339 ? 0.2873 0.3352 0.3031 0.0271  -0.0117 -0.0137 338 PRO A CD  
5247 N N   . VAL A 340 ? 0.2563 0.3057 0.2819 0.0388  -0.0316 -0.0169 339 VAL A N   
5248 C CA  . VAL A 340 ? 0.2821 0.3278 0.3025 0.0455  -0.0352 -0.0159 339 VAL A CA  
5249 C C   . VAL A 340 ? 0.2904 0.3450 0.3238 0.0506  -0.0341 -0.0150 339 VAL A C   
5250 O O   . VAL A 340 ? 0.3162 0.3692 0.3484 0.0574  -0.0372 -0.0130 339 VAL A O   
5251 C CB  . VAL A 340 ? 0.3220 0.3660 0.3360 0.0463  -0.0444 -0.0166 339 VAL A CB  
5252 C CG1 . VAL A 340 ? 0.3322 0.3654 0.3320 0.0431  -0.0431 -0.0176 339 VAL A CG1 
5253 C CG2 . VAL A 340 ? 0.3082 0.3648 0.3372 0.0434  -0.0517 -0.0188 339 VAL A CG2 
5263 N N   . GLY A 341 ? 0.2404 0.3040 0.2858 0.0483  -0.0285 -0.0157 340 GLY A N   
5264 C CA  . GLY A 341 ? 0.2117 0.2827 0.2688 0.0539  -0.0240 -0.0152 340 GLY A CA  
5265 C C   . GLY A 341 ? 0.2289 0.3048 0.2905 0.0506  -0.0146 -0.0164 340 GLY A C   
5266 O O   . GLY A 341 ? 0.2298 0.3035 0.2855 0.0439  -0.0126 -0.0166 340 GLY A O   
5270 N N   . VAL A 342 ? 0.2364 0.3183 0.3072 0.0562  -0.0081 -0.0167 341 VAL A N   
5271 C CA  . VAL A 342 ? 0.2475 0.3345 0.3204 0.0544  0.0021  -0.0178 341 VAL A CA  
5272 C C   . VAL A 342 ? 0.2411 0.3456 0.3329 0.0500  0.0022  -0.0148 341 VAL A C   
5273 O O   . VAL A 342 ? 0.2352 0.3542 0.3455 0.0539  0.0062  -0.0133 341 VAL A O   
5274 C CB  . VAL A 342 ? 0.2608 0.3456 0.3346 0.0629  0.0105  -0.0202 341 VAL A CB  
5275 C CG1 . VAL A 342 ? 0.2858 0.3750 0.3572 0.0616  0.0221  -0.0220 341 VAL A CG1 
5276 C CG2 . VAL A 342 ? 0.2437 0.3087 0.2999 0.0655  0.0097  -0.0232 341 VAL A CG2 
5286 N N   . PHE A 343 ? 0.2607 0.3638 0.3495 0.0418  -0.0017 -0.0136 342 PHE A N   
5287 C CA  . PHE A 343 ? 0.2886 0.4050 0.3959 0.0359  -0.0037 -0.0108 342 PHE A CA  
5288 C C   . PHE A 343 ? 0.3150 0.4427 0.4326 0.0343  0.0079  -0.0078 342 PHE A C   
5289 O O   . PHE A 343 ? 0.2955 0.4373 0.4341 0.0298  0.0080  -0.0046 342 PHE A O   
5290 C CB  . PHE A 343 ? 0.2902 0.3975 0.3891 0.0281  -0.0098 -0.0107 342 PHE A CB  
5291 C CG  . PHE A 343 ? 0.3002 0.4015 0.3883 0.0239  -0.0022 -0.0086 342 PHE A CG  
5292 C CD1 . PHE A 343 ? 0.3331 0.4226 0.4006 0.0260  0.0003  -0.0100 342 PHE A CD1 
5293 C CD2 . PHE A 343 ? 0.3406 0.4494 0.4402 0.0177  0.0025  -0.0043 342 PHE A CD2 
5294 C CE1 . PHE A 343 ? 0.3919 0.4781 0.4493 0.0228  0.0061  -0.0074 342 PHE A CE1 
5295 C CE2 . PHE A 343 ? 0.3469 0.4505 0.4350 0.0150  0.0096  -0.0008 342 PHE A CE2 
5296 C CZ  . PHE A 343 ? 0.3599 0.4528 0.4264 0.0179  0.0106  -0.0024 342 PHE A CZ  
5306 N N   . GLU A 344 ? 0.2578 0.3797 0.3608 0.0375  0.0177  -0.0089 343 GLU A N   
5307 C CA  . GLU A 344 ? 0.2594 0.3913 0.3678 0.0375  0.0302  -0.0061 343 GLU A CA  
5308 C C   . GLU A 344 ? 0.2488 0.3976 0.3802 0.0437  0.0354  -0.0051 343 GLU A C   
5309 O O   . GLU A 344 ? 0.2510 0.4133 0.3952 0.0428  0.0457  -0.0011 343 GLU A O   
5310 C CB  . GLU A 344 ? 0.2853 0.4061 0.3693 0.0407  0.0382  -0.0093 343 GLU A CB  
5311 C CG  . GLU A 344 ? 0.3430 0.4508 0.4061 0.0349  0.0341  -0.0090 343 GLU A CG  
5312 C CD  . GLU A 344 ? 0.4084 0.5017 0.4582 0.0360  0.0252  -0.0136 343 GLU A CD  
5313 O OE1 . GLU A 344 ? 0.3461 0.4386 0.4037 0.0400  0.0200  -0.0156 343 GLU A OE1 
5314 O OE2 . GLU A 344 ? 0.3794 0.4633 0.4116 0.0330  0.0237  -0.0142 343 GLU A OE2 
5321 N N   . TRP A 345 ? 0.2412 0.3895 0.3780 0.0506  0.0293  -0.0078 344 TRP A N   
5322 C CA  . TRP A 345 ? 0.2397 0.4041 0.3993 0.0587  0.0333  -0.0065 344 TRP A CA  
5323 C C   . TRP A 345 ? 0.2180 0.3952 0.4000 0.0568  0.0200  -0.0041 344 TRP A C   
5324 O O   . TRP A 345 ? 0.2287 0.3959 0.4015 0.0573  0.0081  -0.0060 344 TRP A O   
5325 C CB  . TRP A 345 ? 0.2952 0.4478 0.4426 0.0698  0.0369  -0.0111 344 TRP A CB  
5326 C CG  . TRP A 345 ? 0.3406 0.4806 0.4656 0.0717  0.0489  -0.0154 344 TRP A CG  
5327 C CD1 . TRP A 345 ? 0.3710 0.5146 0.4891 0.0674  0.0592  -0.0143 344 TRP A CD1 
5328 C CD2 . TRP A 345 ? 0.3279 0.4488 0.4331 0.0783  0.0515  -0.0218 344 TRP A CD2 
5329 N NE1 . TRP A 345 ? 0.3913 0.5199 0.4846 0.0711  0.0670  -0.0204 344 TRP A NE1 
5330 C CE2 . TRP A 345 ? 0.4139 0.5279 0.4998 0.0771  0.0623  -0.0257 344 TRP A CE2 
5331 C CE3 . TRP A 345 ? 0.2870 0.3950 0.3884 0.0848  0.0458  -0.0243 344 TRP A CE3 
5332 C CZ2 . TRP A 345 ? 0.4046 0.4995 0.4686 0.0814  0.0665  -0.0336 344 TRP A CZ2 
5333 C CZ3 . TRP A 345 ? 0.3719 0.4598 0.4531 0.0888  0.0510  -0.0311 344 TRP A CZ3 
5334 C CH2 . TRP A 345 ? 0.3953 0.4768 0.4583 0.0866  0.0608  -0.0365 344 TRP A CH2 
5345 N N   . GLU A 346 ? 0.2206 0.4208 0.4324 0.0548  0.0221  0.0003  345 GLU A N   
5346 C CA  . GLU A 346 ? 0.2520 0.4651 0.4849 0.0496  0.0076  0.0019  345 GLU A CA  
5347 C C   . GLU A 346 ? 0.2674 0.4806 0.5017 0.0584  -0.0040 0.0006  345 GLU A C   
5348 O O   . GLU A 346 ? 0.2913 0.5037 0.5254 0.0542  -0.0192 -0.0005 345 GLU A O   
5349 C CB  . GLU A 346 ? 0.2820 0.5225 0.5510 0.0457  0.0125  0.0072  345 GLU A CB  
5350 C CG  . GLU A 346 ? 0.3724 0.6128 0.6424 0.0343  0.0208  0.0102  345 GLU A CG  
5351 C CD  . GLU A 346 ? 0.4899 0.7117 0.7417 0.0238  0.0102  0.0076  345 GLU A CD  
5352 O OE1 . GLU A 346 ? 0.4522 0.6730 0.7076 0.0205  -0.0057 0.0045  345 GLU A OE1 
5353 O OE2 . GLU A 346 ? 0.5497 0.7577 0.7823 0.0199  0.0181  0.0086  345 GLU A OE2 
5360 N N   . ALA A 347 ? 0.2430 0.4558 0.4772 0.0712  0.0029  0.0007  346 ALA A N   
5361 C CA  . ALA A 347 ? 0.2309 0.4422 0.4656 0.0807  -0.0074 0.0012  346 ALA A CA  
5362 C C   . ALA A 347 ? 0.2460 0.4342 0.4515 0.0781  -0.0178 -0.0018 346 ALA A C   
5363 O O   . ALA A 347 ? 0.2583 0.4464 0.4632 0.0828  -0.0299 -0.0003 346 ALA A O   
5364 C CB  . ALA A 347 ? 0.2547 0.4624 0.4894 0.0950  0.0039  0.0015  346 ALA A CB  
5370 N N   . PHE A 348 ? 0.2140 0.3836 0.3956 0.0712  -0.0130 -0.0051 347 PHE A N   
5371 C CA  . PHE A 348 ? 0.2180 0.3651 0.3718 0.0702  -0.0188 -0.0076 347 PHE A CA  
5372 C C   . PHE A 348 ? 0.2248 0.3657 0.3682 0.0584  -0.0237 -0.0094 347 PHE A C   
5373 O O   . PHE A 348 ? 0.2322 0.3546 0.3523 0.0563  -0.0240 -0.0115 347 PHE A O   
5374 C CB  . PHE A 348 ? 0.2241 0.3529 0.3585 0.0749  -0.0077 -0.0103 347 PHE A CB  
5375 C CG  . PHE A 348 ? 0.2334 0.3656 0.3778 0.0869  -0.0003 -0.0095 347 PHE A CG  
5376 C CD1 . PHE A 348 ? 0.2277 0.3595 0.3773 0.0964  -0.0069 -0.0065 347 PHE A CD1 
5377 C CD2 . PHE A 348 ? 0.2733 0.4088 0.4215 0.0894  0.0139  -0.0114 347 PHE A CD2 
5378 C CE1 . PHE A 348 ? 0.2631 0.3970 0.4234 0.1087  0.0004  -0.0053 347 PHE A CE1 
5379 C CE2 . PHE A 348 ? 0.2895 0.4267 0.4470 0.1016  0.0220  -0.0115 347 PHE A CE2 
5380 C CZ  . PHE A 348 ? 0.3037 0.4397 0.4683 0.1114  0.0152  -0.0083 347 PHE A CZ  
5390 N N   . ALA A 349 ? 0.2079 0.3637 0.3696 0.0507  -0.0272 -0.0085 348 ALA A N   
5391 C CA  . ALA A 349 ? 0.2027 0.3512 0.3568 0.0398  -0.0305 -0.0101 348 ALA A CA  
5392 C C   . ALA A 349 ? 0.2081 0.3572 0.3634 0.0354  -0.0458 -0.0123 348 ALA A C   
5393 O O   . ALA A 349 ? 0.2325 0.3714 0.3781 0.0275  -0.0487 -0.0147 348 ALA A O   
5394 C CB  . ALA A 349 ? 0.1942 0.3550 0.3663 0.0324  -0.0224 -0.0075 348 ALA A CB  
5400 N N   . ARG A 350 ? 0.2202 0.3806 0.3862 0.0407  -0.0558 -0.0117 349 ARG A N   
5401 C CA  A ARG A 350 ? 0.2928 0.4566 0.4610 0.0356  -0.0715 -0.0147 349 ARG A CA  
5402 C CA  B ARG A 350 ? 0.2930 0.4569 0.4612 0.0356  -0.0715 -0.0147 349 ARG A CA  
5403 C C   . ARG A 350 ? 0.2504 0.3917 0.3875 0.0350  -0.0768 -0.0185 349 ARG A C   
5404 O O   . ARG A 350 ? 0.2385 0.3744 0.3708 0.0271  -0.0844 -0.0229 349 ARG A O   
5405 C CB  A ARG A 350 ? 0.4176 0.5992 0.6015 0.0431  -0.0820 -0.0123 349 ARG A CB  
5406 C CB  B ARG A 350 ? 0.4177 0.5993 0.6017 0.0431  -0.0820 -0.0123 349 ARG A CB  
5407 C CG  A ARG A 350 ? 0.5471 0.7533 0.7645 0.0454  -0.0764 -0.0079 349 ARG A CG  
5408 C CG  B ARG A 350 ? 0.5472 0.7540 0.7653 0.0452  -0.0767 -0.0080 349 ARG A CG  
5409 C CD  A ARG A 350 ? 0.6536 0.8785 0.8875 0.0539  -0.0881 -0.0048 349 ARG A CD  
5410 C CD  B ARG A 350 ? 0.6601 0.8876 0.8972 0.0514  -0.0906 -0.0054 349 ARG A CD  
5411 N NE  A ARG A 350 ? 0.6922 0.9262 0.9322 0.0465  -0.1067 -0.0081 349 ARG A NE  
5412 N NE  B ARG A 350 ? 0.7134 0.9460 0.9558 0.0662  -0.0845 0.0000  349 ARG A NE  
5413 C CZ  A ARG A 350 ? 0.7138 0.9648 0.9798 0.0349  -0.1115 -0.0099 349 ARG A CZ  
5414 C CZ  B ARG A 350 ? 0.7129 0.9290 0.9320 0.0766  -0.0852 0.0016  349 ARG A CZ  
5415 N NH1 A ARG A 350 ? 0.7299 0.9906 1.0177 0.0299  -0.0977 -0.0073 349 ARG A NH1 
5416 N NH1 B ARG A 350 ? 0.7086 0.9035 0.8971 0.0741  -0.0910 -0.0015 349 ARG A NH1 
5417 N NH2 A ARG A 350 ? 0.7285 0.9858 0.9977 0.0278  -0.1298 -0.0145 349 ARG A NH2 
5418 N NH2 B ARG A 350 ? 0.6985 0.9187 0.9258 0.0899  -0.0791 0.0066  349 ARG A NH2 
5443 N N   . GLY A 351 ? 0.2734 0.4013 0.3900 0.0434  -0.0726 -0.0169 350 GLY A N   
5444 C CA  . GLY A 351 ? 0.3146 0.4227 0.4032 0.0433  -0.0756 -0.0193 350 GLY A CA  
5445 C C   . GLY A 351 ? 0.2924 0.3883 0.3719 0.0351  -0.0697 -0.0222 350 GLY A C   
5446 O O   . GLY A 351 ? 0.2665 0.3517 0.3319 0.0317  -0.0752 -0.0260 350 GLY A O   
5450 N N   . THR A 352 ? 0.2205 0.3175 0.3067 0.0328  -0.0582 -0.0201 351 THR A N   
5451 C CA  . THR A 352 ? 0.2067 0.2931 0.2852 0.0260  -0.0529 -0.0212 351 THR A CA  
5452 C C   . THR A 352 ? 0.2176 0.3084 0.3093 0.0170  -0.0583 -0.0237 351 THR A C   
5453 O O   . THR A 352 ? 0.2536 0.3316 0.3350 0.0124  -0.0597 -0.0265 351 THR A O   
5454 C CB  . THR A 352 ? 0.2334 0.3202 0.3133 0.0261  -0.0402 -0.0180 351 THR A CB  
5455 O OG1 . THR A 352 ? 0.2471 0.3270 0.3138 0.0332  -0.0362 -0.0172 351 THR A OG1 
5456 C CG2 . THR A 352 ? 0.2442 0.3208 0.3154 0.0205  -0.0357 -0.0176 351 THR A CG2 
5464 N N   . LYS A 353 ? 0.2265 0.3351 0.3425 0.0142  -0.0611 -0.0228 352 LYS A N   
5465 C CA  . LYS A 353 ? 0.2367 0.3496 0.3684 0.0040  -0.0668 -0.0253 352 LYS A CA  
5466 C C   . LYS A 353 ? 0.2787 0.3836 0.3993 0.0021  -0.0809 -0.0323 352 LYS A C   
5467 O O   . LYS A 353 ? 0.2747 0.3686 0.3924 -0.0057 -0.0840 -0.0367 352 LYS A O   
5468 C CB  . LYS A 353 ? 0.2623 0.3990 0.4255 0.0016  -0.0667 -0.0222 352 LYS A CB  
5469 C CG  . LYS A 353 ? 0.3490 0.4940 0.5345 -0.0102 -0.0743 -0.0246 352 LYS A CG  
5470 C CD  . LYS A 353 ? 0.4384 0.5680 0.6197 -0.0190 -0.0681 -0.0247 352 LYS A CD  
5471 C CE  . LYS A 353 ? 0.5611 0.7001 0.7708 -0.0319 -0.0720 -0.0253 352 LYS A CE  
5472 N NZ  . LYS A 353 ? 0.6393 0.7795 0.8527 -0.0371 -0.0899 -0.0339 352 LYS A NZ  
5486 N N   . ALA A 354 ? 0.2986 0.4074 0.4114 0.0096  -0.0894 -0.0332 353 ALA A N   
5487 C CA  . ALA A 354 ? 0.3421 0.4434 0.4395 0.0091  -0.1031 -0.0398 353 ALA A CA  
5488 C C   . ALA A 354 ? 0.3024 0.3795 0.3714 0.0098  -0.0991 -0.0432 353 ALA A C   
5489 O O   . ALA A 354 ? 0.3007 0.3669 0.3605 0.0046  -0.1060 -0.0504 353 ALA A O   
5490 C CB  . ALA A 354 ? 0.3649 0.4748 0.4568 0.0191  -0.1111 -0.0376 353 ALA A CB  
5496 N N   . LEU A 355 ? 0.2725 0.3412 0.3287 0.0158  -0.0878 -0.0385 354 LEU A N   
5497 C CA  . LEU A 355 ? 0.2898 0.3385 0.3227 0.0171  -0.0825 -0.0403 354 LEU A CA  
5498 C C   . LEU A 355 ? 0.3089 0.3492 0.3475 0.0091  -0.0777 -0.0422 354 LEU A C   
5499 O O   . LEU A 355 ? 0.3233 0.3478 0.3473 0.0078  -0.0791 -0.0474 354 LEU A O   
5500 C CB  . LEU A 355 ? 0.2962 0.3414 0.3192 0.0243  -0.0723 -0.0343 354 LEU A CB  
5501 C CG  . LEU A 355 ? 0.3940 0.4222 0.3954 0.0270  -0.0664 -0.0345 354 LEU A CG  
5502 C CD1 . LEU A 355 ? 0.4190 0.4373 0.4006 0.0298  -0.0738 -0.0396 354 LEU A CD1 
5503 C CD2 . LEU A 355 ? 0.4498 0.4774 0.4454 0.0327  -0.0583 -0.0287 354 LEU A CD2 
5515 N N   . MET A 356 ? 0.2954 0.3451 0.3543 0.0044  -0.0713 -0.0378 355 MET A N   
5516 C CA  . MET A 356 ? 0.2870 0.3289 0.3531 -0.0033 -0.0667 -0.0378 355 MET A CA  
5517 C C   . MET A 356 ? 0.2806 0.3169 0.3515 -0.0110 -0.0769 -0.0457 355 MET A C   
5518 O O   . MET A 356 ? 0.3129 0.3317 0.3755 -0.0141 -0.0757 -0.0494 355 MET A O   
5519 C CB  . MET A 356 ? 0.2945 0.3498 0.3819 -0.0069 -0.0585 -0.0309 355 MET A CB  
5520 C CG  . MET A 356 ? 0.3298 0.3775 0.4251 -0.0143 -0.0524 -0.0283 355 MET A CG  
5521 S SD  . MET A 356 ? 0.3362 0.3652 0.4102 -0.0097 -0.0437 -0.0251 355 MET A SD  
5522 C CE  . MET A 356 ? 0.3094 0.3514 0.3832 -0.0043 -0.0336 -0.0168 355 MET A CE  
5532 N N   . ASP A 357 ? 0.3008 0.3518 0.3859 -0.0141 -0.0875 -0.0487 356 ASP A N   
5533 C CA  . ASP A 357 ? 0.3220 0.3688 0.4110 -0.0222 -0.1001 -0.0578 356 ASP A CA  
5534 C C   . ASP A 357 ? 0.3443 0.3700 0.4031 -0.0185 -0.1053 -0.0664 356 ASP A C   
5535 O O   . ASP A 357 ? 0.3839 0.3943 0.4390 -0.0252 -0.1094 -0.0743 356 ASP A O   
5536 C CB  . ASP A 357 ? 0.3481 0.4171 0.4541 -0.0237 -0.1129 -0.0594 356 ASP A CB  
5537 C CG  . ASP A 357 ? 0.4757 0.5673 0.6161 -0.0286 -0.1083 -0.0522 356 ASP A CG  
5538 O OD1 . ASP A 357 ? 0.5425 0.6314 0.6928 -0.0324 -0.0957 -0.0465 356 ASP A OD1 
5539 O OD2 . ASP A 357 ? 0.4821 0.5951 0.6394 -0.0278 -0.1171 -0.0515 356 ASP A OD2 
5544 N N   . GLU A 358 ? 0.3309 0.3549 0.3678 -0.0080 -0.1051 -0.0651 357 GLU A N   
5545 C CA  . GLU A 358 ? 0.3974 0.4025 0.4040 -0.0032 -0.1082 -0.0723 357 GLU A CA  
5546 C C   . GLU A 358 ? 0.3911 0.3761 0.3866 -0.0021 -0.0962 -0.0720 357 GLU A C   
5547 O O   . GLU A 358 ? 0.3868 0.3531 0.3658 -0.0027 -0.0982 -0.0805 357 GLU A O   
5548 C CB  . GLU A 358 ? 0.4344 0.4437 0.4224 0.0079  -0.1089 -0.0685 357 GLU A CB  
5549 C CG  . GLU A 358 ? 0.5174 0.5448 0.5132 0.0089  -0.1220 -0.0684 357 GLU A CG  
5550 C CD  . GLU A 358 ? 0.6105 0.6345 0.5967 0.0044  -0.1384 -0.0797 357 GLU A CD  
5551 O OE1 . GLU A 358 ? 0.5805 0.5842 0.5413 0.0051  -0.1390 -0.0877 357 GLU A OE1 
5552 O OE2 . GLU A 358 ? 0.5957 0.6380 0.6004 0.0002  -0.1509 -0.0807 357 GLU A OE2 
5559 N N   . VAL A 359 ? 0.3466 0.3354 0.3505 0.0001  -0.0839 -0.0626 358 VAL A N   
5560 C CA  . VAL A 359 ? 0.3376 0.3107 0.3342 0.0018  -0.0730 -0.0605 358 VAL A CA  
5561 C C   . VAL A 359 ? 0.3439 0.3058 0.3521 -0.0070 -0.0733 -0.0644 358 VAL A C   
5562 O O   . VAL A 359 ? 0.3598 0.3020 0.3565 -0.0056 -0.0692 -0.0681 358 VAL A O   
5563 C CB  . VAL A 359 ? 0.3441 0.3262 0.3474 0.0056  -0.0619 -0.0495 358 VAL A CB  
5564 C CG1 . VAL A 359 ? 0.3823 0.3515 0.3824 0.0068  -0.0519 -0.0460 358 VAL A CG1 
5565 C CG2 . VAL A 359 ? 0.3281 0.3161 0.3181 0.0140  -0.0611 -0.0466 358 VAL A CG2 
5575 N N   . VAL A 360 ? 0.3370 0.3107 0.3690 -0.0161 -0.0775 -0.0635 359 VAL A N   
5576 C CA  . VAL A 360 ? 0.3670 0.3292 0.4124 -0.0261 -0.0778 -0.0667 359 VAL A CA  
5577 C C   . VAL A 360 ? 0.3912 0.3369 0.4238 -0.0296 -0.0886 -0.0807 359 VAL A C   
5578 O O   . VAL A 360 ? 0.4141 0.3378 0.4428 -0.0328 -0.0862 -0.0858 359 VAL A O   
5579 C CB  . VAL A 360 ? 0.3567 0.3376 0.4328 -0.0355 -0.0791 -0.0616 359 VAL A CB  
5580 C CG1 . VAL A 360 ? 0.4135 0.3821 0.5048 -0.0476 -0.0813 -0.0659 359 VAL A CG1 
5581 C CG2 . VAL A 360 ? 0.3103 0.3024 0.3949 -0.0319 -0.0662 -0.0485 359 VAL A CG2 
5591 N N   . LYS A 361 ? 0.3989 0.3540 0.4240 -0.0287 -0.1010 -0.0872 360 LYS A N   
5592 C CA  . LYS A 361 ? 0.4190 0.3584 0.4272 -0.0315 -0.1126 -0.1017 360 LYS A CA  
5593 C C   . LYS A 361 ? 0.4294 0.3451 0.4067 -0.0220 -0.1053 -0.1061 360 LYS A C   
5594 O O   . LYS A 361 ? 0.4748 0.3675 0.4407 -0.0249 -0.1073 -0.1169 360 LYS A O   
5595 C CB  . LYS A 361 ? 0.4654 0.4218 0.4690 -0.0305 -0.1277 -0.1062 360 LYS A CB  
5596 C CG  . LYS A 361 ? 0.6001 0.5777 0.6358 -0.0419 -0.1382 -0.1060 360 LYS A CG  
5597 C CD  . LYS A 361 ? 0.7491 0.7423 0.7796 -0.0408 -0.1556 -0.1115 360 LYS A CD  
5598 C CE  . LYS A 361 ? 0.8378 0.8479 0.8618 -0.0283 -0.1524 -0.1012 360 LYS A CE  
5599 N NZ  . LYS A 361 ? 0.8511 0.8801 0.8759 -0.0270 -0.1695 -0.1036 360 LYS A NZ  
5613 N N   . ALA A 362 ? 0.4239 0.3444 0.3885 -0.0107 -0.0962 -0.0977 361 ALA A N   
5614 C CA  . ALA A 362 ? 0.4625 0.3642 0.4012 -0.0009 -0.0874 -0.0998 361 ALA A CA  
5615 C C   . ALA A 362 ? 0.4652 0.3484 0.4101 -0.0023 -0.0770 -0.0988 361 ALA A C   
5616 O O   . ALA A 362 ? 0.4861 0.3465 0.4129 0.0015  -0.0740 -0.1071 361 ALA A O   
5617 C CB  . ALA A 362 ? 0.4757 0.3893 0.4068 0.0095  -0.0791 -0.0890 361 ALA A CB  
5623 N N   . THR A 363 ? 0.4037 0.2958 0.3726 -0.0063 -0.0704 -0.0882 362 THR A N   
5624 C CA  . THR A 363 ? 0.4022 0.2769 0.3783 -0.0076 -0.0612 -0.0856 362 THR A CA  
5625 C C   . THR A 363 ? 0.4511 0.3039 0.4269 -0.0158 -0.0677 -0.0985 362 THR A C   
5626 O O   . THR A 363 ? 0.4830 0.3114 0.4502 -0.0127 -0.0612 -0.1024 362 THR A O   
5627 C CB  . THR A 363 ? 0.3838 0.2727 0.3855 -0.0123 -0.0553 -0.0723 362 THR A CB  
5628 O OG1 . THR A 363 ? 0.3677 0.2780 0.3694 -0.0063 -0.0518 -0.0629 362 THR A OG1 
5629 C CG2 . THR A 363 ? 0.4436 0.3161 0.4492 -0.0102 -0.0445 -0.0664 362 THR A CG2 
5637 N N   . SER A 364 ? 0.4614 0.3223 0.4478 -0.0266 -0.0806 -0.1054 363 SER A N   
5638 C CA  . SER A 364 ? 0.5076 0.3484 0.4975 -0.0372 -0.0882 -0.1181 363 SER A CA  
5639 C C   . SER A 364 ? 0.5303 0.3461 0.4882 -0.0314 -0.0913 -0.1335 363 SER A C   
5640 O O   . SER A 364 ? 0.5944 0.3840 0.5497 -0.0368 -0.0922 -0.1440 363 SER A O   
5641 C CB  . SER A 364 ? 0.5798 0.4390 0.5888 -0.0499 -0.1031 -0.1224 363 SER A CB  
5642 O OG  . SER A 364 ? 0.6808 0.5600 0.7205 -0.0557 -0.0982 -0.1089 363 SER A OG  
5648 N N   . ARG A 365 ? 0.5108 0.3328 0.4436 -0.0207 -0.0923 -0.1352 364 ARG A N   
5649 C CA  . ARG A 365 ? 0.6408 0.4400 0.5400 -0.0140 -0.0940 -0.1494 364 ARG A CA  
5650 C C   . ARG A 365 ? 0.6399 0.4261 0.5228 0.0004  -0.0770 -0.1442 364 ARG A C   
5651 O O   . ARG A 365 ? 0.6240 0.3950 0.4767 0.0092  -0.0751 -0.1535 364 ARG A O   
5652 C CB  . ARG A 365 ? 0.7608 0.5738 0.6399 -0.0116 -0.1068 -0.1555 364 ARG A CB  
5653 C CG  . ARG A 365 ? 0.9417 0.7719 0.8098 0.0008  -0.0996 -0.1438 364 ARG A CG  
5654 C CD  . ARG A 365 ? 1.2028 1.0554 1.0680 -0.0004 -0.1136 -0.1435 364 ARG A CD  
5655 N NE  . ARG A 365 ? 1.3802 1.2514 1.2450 0.0090  -0.1059 -0.1292 364 ARG A NE  
5656 C CZ  . ARG A 365 ? 1.4913 1.3871 1.3695 0.0078  -0.1126 -0.1214 364 ARG A CZ  
5657 N NH1 . ARG A 365 ? 1.4550 1.3636 1.3502 -0.0019 -0.1273 -0.1254 364 ARG A NH1 
5658 N NH2 . ARG A 365 ? 1.5953 1.5031 1.4718 0.0163  -0.1042 -0.1093 364 ARG A NH2 
5672 N N   . GLY A 366 ? 0.5535 0.4900 0.4423 0.0040  -0.0849 -0.1115 365 GLY A N   
5673 C CA  . GLY A 366 ? 0.5556 0.4892 0.4374 0.0147  -0.0748 -0.1176 365 GLY A CA  
5674 C C   . GLY A 366 ? 0.5510 0.5018 0.4292 0.0177  -0.0594 -0.1007 365 GLY A C   
5675 O O   . GLY A 366 ? 0.5282 0.4824 0.4016 0.0265  -0.0505 -0.1055 365 GLY A O   
5679 N N   . CYS A 367 ? 0.5571 0.5188 0.4396 0.0111  -0.0570 -0.0819 366 CYS A N   
5680 C CA  . CYS A 367 ? 0.4935 0.4659 0.3767 0.0122  -0.0445 -0.0653 366 CYS A CA  
5681 C C   . CYS A 367 ? 0.4355 0.3927 0.3373 0.0118  -0.0378 -0.0607 366 CYS A C   
5682 O O   . CYS A 367 ? 0.4288 0.3700 0.3465 0.0060  -0.0426 -0.0603 366 CYS A O   
5683 C CB  . CYS A 367 ? 0.4715 0.4536 0.3581 0.0062  -0.0473 -0.0481 366 CYS A CB  
5684 S SG  . CYS A 367 ? 0.4637 0.4579 0.3477 0.0066  -0.0360 -0.0277 366 CYS A SG  
5690 N N   . ILE A 368 ? 0.4073 0.3716 0.3069 0.0169  -0.0269 -0.0565 367 ILE A N   
5691 C CA  . ILE A 368 ? 0.4077 0.3611 0.3233 0.0165  -0.0210 -0.0498 367 ILE A CA  
5692 C C   . ILE A 368 ? 0.3767 0.3355 0.3018 0.0103  -0.0177 -0.0323 367 ILE A C   
5693 O O   . ILE A 368 ? 0.3664 0.3392 0.2850 0.0103  -0.0134 -0.0232 367 ILE A O   
5694 C CB  . ILE A 368 ? 0.4652 0.4260 0.3772 0.0252  -0.0122 -0.0547 367 ILE A CB  
5695 C CG1 . ILE A 368 ? 0.5458 0.5005 0.4506 0.0345  -0.0171 -0.0759 367 ILE A CG1 
5696 C CG2 . ILE A 368 ? 0.4919 0.4434 0.4194 0.0246  -0.0074 -0.0464 367 ILE A CG2 
5697 C CD1 . ILE A 368 ? 0.7104 0.6780 0.6139 0.0457  -0.0089 -0.0840 367 ILE A CD1 
5709 N N   . THR A 369 ? 0.3572 0.3059 0.2979 0.0047  -0.0203 -0.0278 368 THR A N   
5710 C CA  . THR A 369 ? 0.3175 0.2723 0.2693 0.0008  -0.0191 -0.0157 368 THR A CA  
5711 C C   . THR A 369 ? 0.3267 0.2763 0.2912 -0.0002 -0.0130 -0.0109 368 THR A C   
5712 O O   . THR A 369 ? 0.3160 0.2560 0.2869 -0.0033 -0.0140 -0.0135 368 THR A O   
5713 C CB  . THR A 369 ? 0.3244 0.2816 0.2838 -0.0045 -0.0279 -0.0162 368 THR A CB  
5714 O OG1 . THR A 369 ? 0.3511 0.2981 0.3186 -0.0097 -0.0311 -0.0223 368 THR A OG1 
5715 C CG2 . THR A 369 ? 0.3576 0.3224 0.3022 -0.0031 -0.0355 -0.0199 368 THR A CG2 
5723 N N   . ILE A 370 ? 0.3034 0.2589 0.2706 0.0016  -0.0079 -0.0033 369 ILE A N   
5724 C CA  . ILE A 370 ? 0.2923 0.2455 0.2689 0.0018  -0.0025 -0.0001 369 ILE A CA  
5725 C C   . ILE A 370 ? 0.2767 0.2357 0.2644 0.0007  -0.0035 0.0056  369 ILE A C   
5726 O O   . ILE A 370 ? 0.2640 0.2264 0.2502 0.0018  -0.0055 0.0109  369 ILE A O   
5727 C CB  . ILE A 370 ? 0.3209 0.2761 0.2926 0.0060  0.0034  0.0006  369 ILE A CB  
5728 C CG1 . ILE A 370 ? 0.3523 0.3038 0.3147 0.0104  0.0033  -0.0085 369 ILE A CG1 
5729 C CG2 . ILE A 370 ? 0.3223 0.2756 0.3033 0.0062  0.0071  0.0032  369 ILE A CG2 
5730 C CD1 . ILE A 370 ? 0.3799 0.3428 0.3372 0.0156  0.0093  -0.0099 369 ILE A CD1 
5742 N N   . ILE A 371 ? 0.2591 0.2200 0.2578 -0.0016 -0.0029 0.0045  370 ILE A N   
5743 C CA  . ILE A 371 ? 0.2671 0.2359 0.2787 -0.0002 -0.0040 0.0055  370 ILE A CA  
5744 C C   . ILE A 371 ? 0.2796 0.2493 0.2952 0.0007  0.0015  0.0049  370 ILE A C   
5745 O O   . ILE A 371 ? 0.3209 0.2893 0.3334 -0.0024 0.0048  0.0043  370 ILE A O   
5746 C CB  . ILE A 371 ? 0.3848 0.3639 0.4070 -0.0029 -0.0077 0.0021  370 ILE A CB  
5747 C CG1 . ILE A 371 ? 0.4258 0.4046 0.4435 -0.0033 -0.0152 0.0023  370 ILE A CG1 
5748 C CG2 . ILE A 371 ? 0.4448 0.4356 0.4829 0.0014  -0.0086 -0.0005 370 ILE A CG2 
5749 C CD1 . ILE A 371 ? 0.4525 0.4445 0.4834 -0.0064 -0.0203 -0.0014 370 ILE A CD1 
5761 N N   . GLY A 372 ? 0.2487 0.2192 0.2707 0.0043  0.0008  0.0054  371 GLY A N   
5762 C CA  . GLY A 372 ? 0.2587 0.2310 0.2836 0.0055  0.0046  0.0031  371 GLY A CA  
5763 C C   . GLY A 372 ? 0.2711 0.2487 0.3092 0.0100  0.0014  -0.0022 371 GLY A C   
5764 O O   . GLY A 372 ? 0.2905 0.2636 0.3355 0.0129  -0.0051 -0.0011 371 GLY A O   
5768 N N   . GLY A 373 ? 0.2997 0.2863 0.3405 0.0110  0.0049  -0.0082 372 GLY A N   
5769 C CA  . GLY A 373 ? 0.2800 0.2720 0.3328 0.0171  0.0016  -0.0172 372 GLY A CA  
5770 C C   . GLY A 373 ? 0.2817 0.2955 0.3386 0.0184  0.0061  -0.0263 372 GLY A C   
5771 O O   . GLY A 373 ? 0.3043 0.3292 0.3597 0.0138  0.0098  -0.0238 372 GLY A O   
5775 N N   . GLY A 374 ? 0.2510 0.2736 0.3140 0.0242  0.0054  -0.0374 373 GLY A N   
5776 C CA  . GLY A 374 ? 0.2514 0.3019 0.3177 0.0259  0.0109  -0.0475 373 GLY A CA  
5777 C C   . GLY A 374 ? 0.2683 0.3334 0.3497 0.0297  0.0093  -0.0529 373 GLY A C   
5778 O O   . GLY A 374 ? 0.2661 0.3559 0.3485 0.0250  0.0160  -0.0533 373 GLY A O   
5782 N N   . ASP A 375 ? 0.2410 0.2922 0.3355 0.0376  -0.0007 -0.0560 374 ASP A N   
5783 C CA  . ASP A 375 ? 0.2238 0.2883 0.3356 0.0439  -0.0053 -0.0623 374 ASP A CA  
5784 C C   . ASP A 375 ? 0.2412 0.2979 0.3488 0.0366  -0.0071 -0.0488 374 ASP A C   
5785 O O   . ASP A 375 ? 0.2843 0.3621 0.4008 0.0351  -0.0055 -0.0510 374 ASP A O   
5786 C CB  . ASP A 375 ? 0.2345 0.2857 0.3632 0.0574  -0.0182 -0.0727 374 ASP A CB  
5787 C CG  . ASP A 375 ? 0.3127 0.3748 0.4470 0.0660  -0.0174 -0.0911 374 ASP A CG  
5788 O OD1 . ASP A 375 ? 0.3004 0.3967 0.4410 0.0704  -0.0104 -0.1047 374 ASP A OD1 
5789 O OD2 . ASP A 375 ? 0.3347 0.3745 0.4662 0.0673  -0.0232 -0.0922 374 ASP A OD2 
5794 N N   . THR A 376 ? 0.2206 0.2510 0.3151 0.0314  -0.0100 -0.0359 375 THR A N   
5795 C CA  . THR A 376 ? 0.2444 0.2693 0.3329 0.0254  -0.0123 -0.0259 375 THR A CA  
5796 C C   . THR A 376 ? 0.2580 0.2954 0.3385 0.0151  -0.0037 -0.0229 375 THR A C   
5797 O O   . THR A 376 ? 0.2223 0.2672 0.3063 0.0110  -0.0058 -0.0211 375 THR A O   
5798 C CB  . THR A 376 ? 0.3084 0.3078 0.3830 0.0225  -0.0159 -0.0143 375 THR A CB  
5799 O OG1 . THR A 376 ? 0.2785 0.2646 0.3609 0.0289  -0.0242 -0.0146 375 THR A OG1 
5800 C CG2 . THR A 376 ? 0.3845 0.3802 0.4535 0.0194  -0.0209 -0.0071 375 THR A CG2 
5808 N N   . ALA A 377 ? 0.2554 0.2943 0.3259 0.0103  0.0045  -0.0217 376 ALA A N   
5809 C CA  . ALA A 377 ? 0.2611 0.3090 0.3249 -0.0006 0.0106  -0.0168 376 ALA A CA  
5810 C C   . ALA A 377 ? 0.2592 0.3392 0.3375 -0.0031 0.0142  -0.0228 376 ALA A C   
5811 O O   . ALA A 377 ? 0.2783 0.3675 0.3567 -0.0142 0.0166  -0.0173 376 ALA A O   
5812 C CB  . ALA A 377 ? 0.3061 0.3483 0.3559 -0.0045 0.0165  -0.0125 376 ALA A CB  
5818 N N   . THR A 378 ? 0.2096 0.3083 0.3017 0.0069  0.0142  -0.0348 377 THR A N   
5819 C CA  . THR A 378 ? 0.2079 0.3443 0.3172 0.0071  0.0181  -0.0436 377 THR A CA  
5820 C C   . THR A 378 ? 0.2403 0.3833 0.3658 0.0082  0.0107  -0.0445 377 THR A C   
5821 O O   . THR A 378 ? 0.2373 0.4125 0.3765 0.0024  0.0145  -0.0473 377 THR A O   
5822 C CB  . THR A 378 ? 0.2415 0.3950 0.3610 0.0208  0.0191  -0.0599 377 THR A CB  
5823 O OG1 . THR A 378 ? 0.2323 0.3819 0.3346 0.0179  0.0255  -0.0585 377 THR A OG1 
5824 C CG2 . THR A 378 ? 0.2682 0.4672 0.4066 0.0232  0.0246  -0.0721 377 THR A CG2 
5832 N N   . CYS A 379 ? 0.2687 0.3847 0.3927 0.0144  0.0000  -0.0414 378 CYS A N   
5833 C CA  . CYS A 379 ? 0.2634 0.3818 0.3967 0.0132  -0.0085 -0.0393 378 CYS A CA  
5834 C C   . CYS A 379 ? 0.2412 0.3600 0.3659 -0.0031 -0.0052 -0.0304 378 CYS A C   
5835 O O   . CYS A 379 ? 0.2727 0.4128 0.4116 -0.0087 -0.0075 -0.0320 378 CYS A O   
5836 C CB  . CYS A 379 ? 0.3134 0.4010 0.4394 0.0201  -0.0202 -0.0339 378 CYS A CB  
5837 S SG  . CYS A 379 ? 0.3494 0.4265 0.4861 0.0370  -0.0281 -0.0412 378 CYS A SG  
5843 N N   . CYS A 380 ? 0.2706 0.3651 0.3740 -0.0106 -0.0013 -0.0215 379 CYS A N   
5844 C CA  . CYS A 380 ? 0.2863 0.3752 0.3820 -0.0255 -0.0004 -0.0139 379 CYS A CA  
5845 C C   . CYS A 380 ? 0.2834 0.4030 0.3902 -0.0372 0.0072  -0.0130 379 CYS A C   
5846 O O   . CYS A 380 ? 0.3201 0.4484 0.4343 -0.0496 0.0047  -0.0096 379 CYS A O   
5847 C CB  . CYS A 380 ? 0.3537 0.4123 0.4273 -0.0283 0.0017  -0.0066 379 CYS A CB  
5848 S SG  . CYS A 380 ? 0.3854 0.4147 0.4451 -0.0185 -0.0055 -0.0060 379 CYS A SG  
5854 N N   . ALA A 381 ? 0.2863 0.4242 0.3937 -0.0350 0.0163  -0.0157 380 ALA A N   
5855 C CA  . ALA A 381 ? 0.2939 0.4678 0.4102 -0.0472 0.0252  -0.0138 380 ALA A CA  
5856 C C   . ALA A 381 ? 0.2637 0.4761 0.4072 -0.0453 0.0240  -0.0233 380 ALA A C   
5857 O O   . ALA A 381 ? 0.2624 0.4997 0.4172 -0.0607 0.0266  -0.0186 380 ALA A O   
5858 C CB  . ALA A 381 ? 0.2831 0.4712 0.3910 -0.0435 0.0350  -0.0163 380 ALA A CB  
5864 N N   . LYS A 382 ? 0.2468 0.4645 0.4030 -0.0270 0.0188  -0.0363 381 LYS A N   
5865 C CA  . LYS A 382 ? 0.2433 0.5012 0.4285 -0.0214 0.0168  -0.0479 381 LYS A CA  
5866 C C   . LYS A 382 ? 0.2208 0.4790 0.4166 -0.0308 0.0078  -0.0431 381 LYS A C   
5867 O O   . LYS A 382 ? 0.2190 0.5183 0.4382 -0.0375 0.0097  -0.0470 381 LYS A O   
5868 C CB  . LYS A 382 ? 0.2717 0.5255 0.4676 0.0021  0.0092  -0.0621 381 LYS A CB  
5869 C CG  . LYS A 382 ? 0.2877 0.5786 0.5157 0.0125  0.0037  -0.0757 381 LYS A CG  
5870 C CD  . LYS A 382 ? 0.3060 0.5882 0.5447 0.0365  -0.0054 -0.0897 381 LYS A CD  
5871 C CE  . LYS A 382 ? 0.3803 0.7028 0.6544 0.0498  -0.0118 -0.1057 381 LYS A CE  
5872 N NZ  . LYS A 382 ? 0.4124 0.7332 0.7007 0.0743  -0.0191 -0.1236 381 LYS A NZ  
5886 N N   . TRP A 383 ? 0.2153 0.4321 0.3953 -0.0313 -0.0023 -0.0359 382 TRP A N   
5887 C CA  . TRP A 383 ? 0.2795 0.4940 0.4665 -0.0391 -0.0129 -0.0333 382 TRP A CA  
5888 C C   . TRP A 383 ? 0.2744 0.4691 0.4465 -0.0593 -0.0119 -0.0218 382 TRP A C   
5889 O O   . TRP A 383 ? 0.2671 0.4517 0.4402 -0.0665 -0.0220 -0.0204 382 TRP A O   
5890 C CB  . TRP A 383 ? 0.3109 0.4982 0.4910 -0.0249 -0.0267 -0.0353 382 TRP A CB  
5891 C CG  . TRP A 383 ? 0.2923 0.4992 0.4930 -0.0064 -0.0319 -0.0459 382 TRP A CG  
5892 C CD1 . TRP A 383 ? 0.3707 0.6194 0.6022 -0.0025 -0.0344 -0.0557 382 TRP A CD1 
5893 C CD2 . TRP A 383 ? 0.2481 0.4341 0.4431 0.0110  -0.0364 -0.0486 382 TRP A CD2 
5894 N NE1 . TRP A 383 ? 0.3399 0.5933 0.5854 0.0184  -0.0410 -0.0656 382 TRP A NE1 
5895 C CE2 . TRP A 383 ? 0.2738 0.4868 0.4970 0.0261  -0.0430 -0.0607 382 TRP A CE2 
5896 C CE3 . TRP A 383 ? 0.2843 0.4326 0.4555 0.0149  -0.0364 -0.0419 382 TRP A CE3 
5897 C CZ2 . TRP A 383 ? 0.2761 0.4736 0.5034 0.0446  -0.0512 -0.0658 382 TRP A CZ2 
5898 C CZ3 . TRP A 383 ? 0.3255 0.4615 0.5009 0.0309  -0.0433 -0.0456 382 TRP A CZ3 
5899 C CH2 . TRP A 383 ? 0.2900 0.4477 0.4927 0.0454  -0.0513 -0.0573 382 TRP A CH2 
5910 N N   . ASN A 384 ? 0.2658 0.4540 0.4244 -0.0677 -0.0015 -0.0142 383 ASN A N   
5911 C CA  . ASN A 384 ? 0.2951 0.4647 0.4426 -0.0872 -0.0015 -0.0022 383 ASN A CA  
5912 C C   . ASN A 384 ? 0.2973 0.4223 0.4273 -0.0851 -0.0128 -0.0012 383 ASN A C   
5913 O O   . ASN A 384 ? 0.3018 0.4157 0.4335 -0.0975 -0.0211 0.0012  383 ASN A O   
5914 C CB  . ASN A 384 ? 0.3142 0.5168 0.4836 -0.1067 -0.0014 0.0013  383 ASN A CB  
5915 C CG  . ASN A 384 ? 0.3953 0.5792 0.5551 -0.1289 -0.0013 0.0161  383 ASN A CG  
5916 O OD1 . ASN A 384 ? 0.4165 0.5784 0.5565 -0.1300 0.0036  0.0245  383 ASN A OD1 
5917 N ND2 . ASN A 384 ? 0.4789 0.6690 0.6535 -0.1469 -0.0089 0.0197  383 ASN A ND2 
5924 N N   . THR A 385 ? 0.2731 0.3736 0.3860 -0.0696 -0.0131 -0.0037 384 THR A N   
5925 C CA  . THR A 385 ? 0.3202 0.3841 0.4145 -0.0656 -0.0213 -0.0041 384 THR A CA  
5926 C C   . THR A 385 ? 0.3498 0.3855 0.4238 -0.0641 -0.0166 0.0013  384 THR A C   
5927 O O   . THR A 385 ? 0.3429 0.3533 0.4016 -0.0569 -0.0211 -0.0011 384 THR A O   
5928 C CB  . THR A 385 ? 0.3329 0.3947 0.4248 -0.0497 -0.0271 -0.0104 384 THR A CB  
5929 O OG1 . THR A 385 ? 0.3629 0.4295 0.4543 -0.0379 -0.0201 -0.0109 384 THR A OG1 
5930 C CG2 . THR A 385 ? 0.3026 0.3893 0.4143 -0.0498 -0.0354 -0.0157 384 THR A CG2 
5938 N N   . GLU A 386 ? 0.3478 0.3902 0.4212 -0.0707 -0.0080 0.0084  385 GLU A N   
5939 C CA  . GLU A 386 ? 0.3700 0.3876 0.4255 -0.0671 -0.0050 0.0133  385 GLU A CA  
5940 C C   . GLU A 386 ? 0.4324 0.4163 0.4771 -0.0717 -0.0137 0.0151  385 GLU A C   
5941 O O   . GLU A 386 ? 0.4651 0.4267 0.4961 -0.0624 -0.0144 0.0136  385 GLU A O   
5942 C CB  . GLU A 386 ? 0.4247 0.4570 0.4797 -0.0747 0.0038  0.0217  385 GLU A CB  
5943 C CG  . GLU A 386 ? 0.5442 0.6054 0.6052 -0.0651 0.0126  0.0158  385 GLU A CG  
5944 C CD  . GLU A 386 ? 0.6341 0.7196 0.6942 -0.0738 0.0219  0.0224  385 GLU A CD  
5945 O OE1 . GLU A 386 ? 0.6612 0.7726 0.7323 -0.0878 0.0250  0.0271  385 GLU A OE1 
5946 O OE2 . GLU A 386 ? 0.6625 0.7440 0.7107 -0.0672 0.0262  0.0230  385 GLU A OE2 
5953 N N   . ASP A 387 ? 0.4199 0.4008 0.4726 -0.0854 -0.0210 0.0168  386 ASP A N   
5954 C CA  . ASP A 387 ? 0.4690 0.4159 0.5142 -0.0894 -0.0320 0.0155  386 ASP A CA  
5955 C C   . ASP A 387 ? 0.4774 0.4173 0.5210 -0.0828 -0.0412 0.0025  386 ASP A C   
5956 O O   . ASP A 387 ? 0.4945 0.4098 0.5346 -0.0865 -0.0522 -0.0026 386 ASP A O   
5957 C CB  . ASP A 387 ? 0.6606 0.6033 0.7155 -0.1108 -0.0371 0.0260  386 ASP A CB  
5958 C CG  . ASP A 387 ? 0.9963 0.9439 1.0480 -0.1192 -0.0293 0.0416  386 ASP A CG  
5959 O OD1 . ASP A 387 ? 1.1215 1.0573 1.1595 -0.1077 -0.0252 0.0430  386 ASP A OD1 
5960 O OD2 . ASP A 387 ? 1.1262 1.0919 1.1887 -0.1382 -0.0274 0.0531  386 ASP A OD2 
5965 N N   . LYS A 388 ? 0.4355 0.3956 0.4809 -0.0729 -0.0386 -0.0033 387 LYS A N   
5966 C CA  . LYS A 388 ? 0.4082 0.3659 0.4496 -0.0675 -0.0478 -0.0137 387 LYS A CA  
5967 C C   . LYS A 388 ? 0.3838 0.3365 0.4085 -0.0510 -0.0449 -0.0181 387 LYS A C   
5968 O O   . LYS A 388 ? 0.4209 0.3767 0.4391 -0.0456 -0.0513 -0.0248 387 LYS A O   
5969 C CB  . LYS A 388 ? 0.3580 0.3452 0.4173 -0.0721 -0.0509 -0.0150 387 LYS A CB  
5970 C CG  . LYS A 388 ? 0.3784 0.3758 0.4567 -0.0911 -0.0547 -0.0112 387 LYS A CG  
5971 C CD  . LYS A 388 ? 0.4918 0.5249 0.5912 -0.0937 -0.0572 -0.0139 387 LYS A CD  
5972 C CE  . LYS A 388 ? 0.6291 0.6773 0.7500 -0.1149 -0.0614 -0.0103 387 LYS A CE  
5973 N NZ  . LYS A 388 ? 0.7195 0.7985 0.8558 -0.1230 -0.0487 -0.0012 387 LYS A NZ  
5987 N N   . VAL A 389 ? 0.3483 0.2957 0.3659 -0.0442 -0.0359 -0.0135 388 VAL A N   
5988 C CA  . VAL A 389 ? 0.3457 0.2885 0.3487 -0.0313 -0.0324 -0.0159 388 VAL A CA  
5989 C C   . VAL A 389 ? 0.3707 0.2932 0.3644 -0.0282 -0.0303 -0.0169 388 VAL A C   
5990 O O   . VAL A 389 ? 0.4050 0.3162 0.4036 -0.0354 -0.0315 -0.0131 388 VAL A O   
5991 C CB  . VAL A 389 ? 0.3533 0.3116 0.3606 -0.0253 -0.0251 -0.0100 388 VAL A CB  
5992 C CG1 . VAL A 389 ? 0.3622 0.3388 0.3806 -0.0257 -0.0297 -0.0103 388 VAL A CG1 
5993 C CG2 . VAL A 389 ? 0.3472 0.3093 0.3623 -0.0284 -0.0175 -0.0043 388 VAL A CG2 
6003 N N   . SER A 390 ? 0.3780 0.2975 0.3590 -0.0175 -0.0277 -0.0213 389 SER A N   
6004 C CA  . SER A 390 ? 0.4019 0.3045 0.3764 -0.0120 -0.0274 -0.0255 389 SER A CA  
6005 C C   . SER A 390 ? 0.3841 0.2848 0.3638 -0.0124 -0.0210 -0.0162 389 SER A C   
6006 O O   . SER A 390 ? 0.4341 0.3174 0.4143 -0.0131 -0.0244 -0.0154 389 SER A O   
6007 C CB  . SER A 390 ? 0.4021 0.3099 0.3634 -0.0005 -0.0248 -0.0335 389 SER A CB  
6008 O OG  . SER A 390 ? 0.3910 0.3033 0.3438 0.0001  -0.0310 -0.0423 389 SER A OG  
6014 N N   . HIS A 391 ? 0.3271 0.2438 0.3105 -0.0116 -0.0135 -0.0094 390 HIS A N   
6015 C CA  . HIS A 391 ? 0.3278 0.2453 0.3141 -0.0111 -0.0080 -0.0026 390 HIS A CA  
6016 C C   . HIS A 391 ? 0.3030 0.2387 0.2968 -0.0129 -0.0029 0.0020  390 HIS A C   
6017 O O   . HIS A 391 ? 0.3280 0.2726 0.3224 -0.0092 -0.0024 0.0005  390 HIS A O   
6018 C CB  . HIS A 391 ? 0.3657 0.2806 0.3460 -0.0010 -0.0049 -0.0054 390 HIS A CB  
6019 C CG  . HIS A 391 ? 0.4312 0.3472 0.4141 0.0003  -0.0011 0.0004  390 HIS A CG  
6020 N ND1 . HIS A 391 ? 0.4734 0.3762 0.4560 -0.0017 -0.0048 0.0043  390 HIS A ND1 
6021 C CD2 . HIS A 391 ? 0.4464 0.3741 0.4318 0.0035  0.0044  0.0029  390 HIS A CD2 
6022 C CE1 . HIS A 391 ? 0.4827 0.3916 0.4661 0.0007  -0.0013 0.0088  390 HIS A CE1 
6023 N NE2 . HIS A 391 ? 0.4557 0.3798 0.4416 0.0038  0.0043  0.0069  390 HIS A NE2 
6031 N N   . VAL A 392 ? 0.2984 0.2400 0.2977 -0.0183 0.0000  0.0072  391 VAL A N   
6032 C CA  . VAL A 392 ? 0.2827 0.2426 0.2895 -0.0174 0.0049  0.0081  391 VAL A CA  
6033 C C   . VAL A 392 ? 0.2921 0.2511 0.2950 -0.0137 0.0088  0.0103  391 VAL A C   
6034 O O   . VAL A 392 ? 0.3002 0.2544 0.2987 -0.0177 0.0089  0.0152  391 VAL A O   
6035 C CB  . VAL A 392 ? 0.3170 0.2933 0.3334 -0.0262 0.0060  0.0097  391 VAL A CB  
6036 C CG1 . VAL A 392 ? 0.3009 0.2981 0.3259 -0.0220 0.0107  0.0064  391 VAL A CG1 
6037 C CG2 . VAL A 392 ? 0.3479 0.3264 0.3703 -0.0301 0.0004  0.0068  391 VAL A CG2 
6047 N N   . SER A 393 ? 0.3032 0.2658 0.3077 -0.0067 0.0104  0.0078  392 SER A N   
6048 C CA  . SER A 393 ? 0.3243 0.2871 0.3268 -0.0031 0.0127  0.0084  392 SER A CA  
6049 C C   . SER A 393 ? 0.2788 0.2566 0.2874 -0.0029 0.0151  0.0056  392 SER A C   
6050 O O   . SER A 393 ? 0.2593 0.2466 0.2767 -0.0017 0.0147  0.0013  392 SER A O   
6051 C CB  . SER A 393 ? 0.3532 0.3125 0.3558 0.0025  0.0125  0.0072  392 SER A CB  
6052 O OG  . SER A 393 ? 0.3264 0.2878 0.3298 0.0051  0.0136  0.0073  392 SER A OG  
6058 N N   . THR A 394 ? 0.2693 0.2502 0.2733 -0.0027 0.0165  0.0067  393 THR A N   
6059 C CA  . THR A 394 ? 0.3082 0.3046 0.3161 -0.0006 0.0183  0.0008  393 THR A CA  
6060 C C   . THR A 394 ? 0.3127 0.3060 0.3281 0.0057  0.0156  -0.0052 393 THR A C   
6061 O O   . THR A 394 ? 0.3282 0.3315 0.3492 0.0090  0.0149  -0.0134 393 THR A O   
6062 C CB  . THR A 394 ? 0.2975 0.2997 0.2951 -0.0032 0.0196  0.0044  393 THR A CB  
6063 O OG1 . THR A 394 ? 0.2735 0.2626 0.2665 -0.0001 0.0163  0.0079  393 THR A OG1 
6064 C CG2 . THR A 394 ? 0.3250 0.3288 0.3155 -0.0124 0.0211  0.0136  393 THR A CG2 
6072 N N   . GLY A 395 ? 0.2543 0.2353 0.2703 0.0068  0.0136  -0.0016 394 GLY A N   
6073 C CA  . GLY A 395 ? 0.2902 0.2677 0.3141 0.0093  0.0105  -0.0038 394 GLY A CA  
6074 C C   . GLY A 395 ? 0.3233 0.2953 0.3538 0.0095  0.0074  -0.0022 394 GLY A C   
6075 O O   . GLY A 395 ? 0.3133 0.2818 0.3388 0.0079  0.0081  0.0026  394 GLY A O   
6079 N N   . GLY A 396 ? 0.2933 0.2633 0.3346 0.0118  0.0022  -0.0066 395 GLY A N   
6080 C CA  . GLY A 396 ? 0.2485 0.2101 0.2966 0.0120  -0.0036 -0.0027 395 GLY A CA  
6081 C C   . GLY A 396 ? 0.2427 0.1954 0.2944 0.0080  -0.0071 0.0041  395 GLY A C   
6082 O O   . GLY A 396 ? 0.2671 0.2201 0.3117 0.0034  -0.0039 0.0133  395 GLY A O   
6086 N N   . GLY A 397 ? 0.2559 0.2029 0.3195 0.0091  -0.0138 -0.0012 396 GLY A N   
6087 C CA  . GLY A 397 ? 0.2970 0.2373 0.3663 0.0025  -0.0173 0.0058  396 GLY A CA  
6088 C C   . GLY A 397 ? 0.3048 0.2564 0.3667 -0.0013 -0.0092 0.0094  396 GLY A C   
6089 O O   . GLY A 397 ? 0.2956 0.2496 0.3580 -0.0082 -0.0077 0.0194  396 GLY A O   
6093 N N   . ALA A 398 ? 0.2402 0.2008 0.2955 0.0031  -0.0044 0.0019  397 ALA A N   
6094 C CA  . ALA A 398 ? 0.2419 0.2118 0.2921 0.0018  0.0009  0.0046  397 ALA A CA  
6095 C C   . ALA A 398 ? 0.2565 0.2296 0.2984 0.0006  0.0067  0.0124  397 ALA A C   
6096 O O   . ALA A 398 ? 0.2379 0.2200 0.2810 -0.0015 0.0099  0.0161  397 ALA A O   
6097 C CB  . ALA A 398 ? 0.2433 0.2191 0.2859 0.0066  0.0031  -0.0021 397 ALA A CB  
6103 N N   . SER A 399 ? 0.2702 0.2389 0.3041 0.0025  0.0079  0.0129  398 SER A N   
6104 C CA  . SER A 399 ? 0.2680 0.2398 0.2926 0.0021  0.0121  0.0175  398 SER A CA  
6105 C C   . SER A 399 ? 0.2597 0.2345 0.2858 -0.0038 0.0116  0.0267  398 SER A C   
6106 O O   . SER A 399 ? 0.2928 0.2785 0.3128 -0.0049 0.0167  0.0297  398 SER A O   
6107 C CB  . SER A 399 ? 0.3104 0.2769 0.3275 0.0043  0.0116  0.0153  398 SER A CB  
6108 O OG  . SER A 399 ? 0.3530 0.3187 0.3684 0.0068  0.0125  0.0099  398 SER A OG  
6114 N N   . LEU A 400 ? 0.2430 0.2089 0.2769 -0.0075 0.0049  0.0312  399 LEU A N   
6115 C CA  . LEU A 400 ? 0.2756 0.2422 0.3105 -0.0157 0.0027  0.0438  399 LEU A CA  
6116 C C   . LEU A 400 ? 0.3049 0.2840 0.3469 -0.0224 0.0063  0.0483  399 LEU A C   
6117 O O   . LEU A 400 ? 0.2933 0.2854 0.3311 -0.0295 0.0105  0.0585  399 LEU A O   
6118 C CB  . LEU A 400 ? 0.3157 0.2649 0.3602 -0.0175 -0.0085 0.0479  399 LEU A CB  
6119 C CG  . LEU A 400 ? 0.3431 0.2844 0.3837 -0.0111 -0.0132 0.0448  399 LEU A CG  
6120 C CD1 . LEU A 400 ? 0.3971 0.3209 0.4507 -0.0111 -0.0262 0.0480  399 LEU A CD1 
6121 C CD2 . LEU A 400 ? 0.3475 0.2957 0.3722 -0.0128 -0.0103 0.0523  399 LEU A CD2 
6133 N N   . GLU A 401 ? 0.2636 0.2426 0.3167 -0.0209 0.0048  0.0408  400 GLU A N   
6134 C CA  . GLU A 401 ? 0.2572 0.2515 0.3200 -0.0274 0.0075  0.0440  400 GLU A CA  
6135 C C   . GLU A 401 ? 0.2256 0.2422 0.2812 -0.0232 0.0178  0.0415  400 GLU A C   
6136 O O   . GLU A 401 ? 0.2404 0.2776 0.3012 -0.0298 0.0228  0.0476  400 GLU A O   
6137 C CB  . GLU A 401 ? 0.3114 0.3009 0.3873 -0.0262 0.0014  0.0351  400 GLU A CB  
6138 C CG  . GLU A 401 ? 0.4330 0.4006 0.5182 -0.0291 -0.0102 0.0348  400 GLU A CG  
6139 C CD  . GLU A 401 ? 0.5500 0.5139 0.6533 -0.0360 -0.0189 0.0324  400 GLU A CD  
6140 O OE1 . GLU A 401 ? 0.5846 0.5655 0.6957 -0.0429 -0.0158 0.0361  400 GLU A OE1 
6141 O OE2 . GLU A 401 ? 0.5491 0.4939 0.6605 -0.0341 -0.0297 0.0254  400 GLU A OE2 
6148 N N   . LEU A 402 ? 0.2554 0.2691 0.3000 -0.0127 0.0206  0.0327  401 LEU A N   
6149 C CA  . LEU A 402 ? 0.2686 0.2994 0.3069 -0.0068 0.0281  0.0284  401 LEU A CA  
6150 C C   . LEU A 402 ? 0.2931 0.3354 0.3210 -0.0107 0.0332  0.0349  401 LEU A C   
6151 O O   . LEU A 402 ? 0.3018 0.3687 0.3294 -0.0102 0.0405  0.0339  401 LEU A O   
6152 C CB  . LEU A 402 ? 0.2515 0.2706 0.2809 0.0039  0.0271  0.0187  401 LEU A CB  
6153 C CG  . LEU A 402 ? 0.2757 0.2895 0.3109 0.0089  0.0231  0.0130  401 LEU A CG  
6154 C CD1 . LEU A 402 ? 0.3170 0.3171 0.3416 0.0160  0.0215  0.0080  401 LEU A CD1 
6155 C CD2 . LEU A 402 ? 0.2824 0.3151 0.3287 0.0116  0.0247  0.0104  401 LEU A CD2 
6167 N N   . LEU A 403 ? 0.2649 0.2926 0.2837 -0.0137 0.0293  0.0405  402 LEU A N   
6168 C CA  . LEU A 403 ? 0.2634 0.3022 0.2694 -0.0184 0.0326  0.0483  402 LEU A CA  
6169 C C   . LEU A 403 ? 0.2927 0.3514 0.3051 -0.0309 0.0361  0.0617  402 LEU A C   
6170 O O   . LEU A 403 ? 0.3363 0.4212 0.3401 -0.0335 0.0442  0.0647  402 LEU A O   
6171 C CB  . LEU A 403 ? 0.2693 0.2874 0.2679 -0.0196 0.0247  0.0533  402 LEU A CB  
6172 C CG  . LEU A 403 ? 0.3400 0.3653 0.3235 -0.0255 0.0243  0.0644  402 LEU A CG  
6173 C CD1 . LEU A 403 ? 0.4068 0.4542 0.3755 -0.0204 0.0329  0.0564  402 LEU A CD1 
6174 C CD2 . LEU A 403 ? 0.3593 0.3629 0.3393 -0.0226 0.0146  0.0648  402 LEU A CD2 
6186 N N   . GLU A 404 ? 0.2772 0.3264 0.3056 -0.0391 0.0302  0.0688  403 GLU A N   
6187 C CA  . GLU A 404 ? 0.2665 0.3331 0.3051 -0.0538 0.0322  0.0827  403 GLU A CA  
6188 C C   . GLU A 404 ? 0.2600 0.3614 0.3067 -0.0527 0.0427  0.0766  403 GLU A C   
6189 O O   . GLU A 404 ? 0.2861 0.4110 0.3414 -0.0662 0.0468  0.0885  403 GLU A O   
6190 C CB  . GLU A 404 ? 0.3628 0.4088 0.4204 -0.0616 0.0214  0.0874  403 GLU A CB  
6191 C CG  . GLU A 404 ? 0.4397 0.4542 0.4970 -0.0657 0.0087  0.0963  403 GLU A CG  
6192 C CD  . GLU A 404 ? 0.6011 0.5982 0.6798 -0.0728 -0.0023 0.0975  403 GLU A CD  
6193 O OE1 . GLU A 404 ? 0.6776 0.6633 0.7637 -0.0629 -0.0063 0.0815  403 GLU A OE1 
6194 O OE2 . GLU A 404 ? 0.6728 0.6694 0.7610 -0.0890 -0.0072 0.1141  403 GLU A OE2 
6201 N N   . GLY A 405 ? 0.2633 0.3684 0.3107 -0.0379 0.0457  0.0594  404 GLY A N   
6202 C CA  . GLY A 405 ? 0.3002 0.4382 0.3589 -0.0341 0.0536  0.0519  404 GLY A CA  
6203 C C   . GLY A 405 ? 0.3129 0.4504 0.3931 -0.0351 0.0484  0.0484  404 GLY A C   
6204 O O   . GLY A 405 ? 0.3298 0.4986 0.4244 -0.0346 0.0536  0.0445  404 GLY A O   
6208 N N   . LYS A 406 ? 0.2401 0.3465 0.3234 -0.0359 0.0380  0.0482  405 LYS A N   
6209 C CA  . LYS A 406 ? 0.2604 0.3655 0.3621 -0.0378 0.0313  0.0443  405 LYS A CA  
6210 C C   . LYS A 406 ? 0.2434 0.3463 0.3441 -0.0218 0.0296  0.0296  405 LYS A C   
6211 O O   . LYS A 406 ? 0.2469 0.3345 0.3324 -0.0108 0.0298  0.0234  405 LYS A O   
6212 C CB  . LYS A 406 ? 0.3341 0.4082 0.4389 -0.0447 0.0200  0.0482  405 LYS A CB  
6213 C CG  . LYS A 406 ? 0.4118 0.4818 0.5215 -0.0620 0.0172  0.0650  405 LYS A CG  
6214 C CD  . LYS A 406 ? 0.5135 0.5492 0.6280 -0.0647 0.0037  0.0649  405 LYS A CD  
6215 C CE  . LYS A 406 ? 0.6665 0.6939 0.7914 -0.0831 -0.0033 0.0825  405 LYS A CE  
6216 N NZ  . LYS A 406 ? 0.7278 0.7196 0.8608 -0.0829 -0.0190 0.0785  405 LYS A NZ  
6230 N N   . VAL A 407 ? 0.2330 0.3506 0.3508 -0.0219 0.0262  0.0253  406 VAL A N   
6231 C CA  . VAL A 407 ? 0.2355 0.3450 0.3525 -0.0093 0.0200  0.0144  406 VAL A CA  
6232 C C   . VAL A 407 ? 0.2555 0.3388 0.3699 -0.0129 0.0104  0.0134  406 VAL A C   
6233 O O   . VAL A 407 ? 0.3254 0.4057 0.4512 -0.0247 0.0055  0.0175  406 VAL A O   
6234 C CB  . VAL A 407 ? 0.2828 0.4221 0.4196 -0.0065 0.0190  0.0095  406 VAL A CB  
6235 C CG1 . VAL A 407 ? 0.3017 0.4305 0.4377 0.0038  0.0089  0.0013  406 VAL A CG1 
6236 C CG2 . VAL A 407 ? 0.3020 0.4681 0.4407 0.0025  0.0282  0.0056  406 VAL A CG2 
6246 N N   . LEU A 408 ? 0.2046 0.2699 0.3047 -0.0033 0.0074  0.0077  407 LEU A N   
6247 C CA  . LEU A 408 ? 0.2033 0.2492 0.2994 -0.0050 -0.0002 0.0043  407 LEU A CA  
6248 C C   . LEU A 408 ? 0.2056 0.2593 0.3108 -0.0040 -0.0086 -0.0026 407 LEU A C   
6249 O O   . LEU A 408 ? 0.2046 0.2689 0.3086 0.0041  -0.0098 -0.0054 407 LEU A O   
6250 C CB  . LEU A 408 ? 0.2220 0.2512 0.2988 0.0030  0.0012  0.0019  407 LEU A CB  
6251 C CG  . LEU A 408 ? 0.3086 0.3298 0.3756 0.0028  0.0076  0.0068  407 LEU A CG  
6252 C CD1 . LEU A 408 ? 0.3180 0.3270 0.3694 0.0098  0.0083  0.0044  407 LEU A CD1 
6253 C CD2 . LEU A 408 ? 0.3880 0.3990 0.4588 -0.0053 0.0055  0.0107  407 LEU A CD2 
6265 N N   . PRO A 409 ? 0.2118 0.2591 0.3257 -0.0112 -0.0164 -0.0062 408 PRO A N   
6266 C CA  . PRO A 409 ? 0.2425 0.2986 0.3644 -0.0106 -0.0260 -0.0145 408 PRO A CA  
6267 C C   . PRO A 409 ? 0.2242 0.2801 0.3290 0.0008  -0.0285 -0.0201 408 PRO A C   
6268 O O   . PRO A 409 ? 0.2305 0.3007 0.3401 0.0043  -0.0343 -0.0231 408 PRO A O   
6269 C CB  . PRO A 409 ? 0.2834 0.3245 0.4123 -0.0179 -0.0348 -0.0205 408 PRO A CB  
6270 C CG  . PRO A 409 ? 0.2995 0.3288 0.4333 -0.0262 -0.0308 -0.0109 408 PRO A CG  
6271 C CD  . PRO A 409 ? 0.2507 0.2826 0.3701 -0.0205 -0.0188 -0.0028 408 PRO A CD  
6279 N N   . GLY A 410 ? 0.2478 0.2892 0.3335 0.0057  -0.0254 -0.0208 409 GLY A N   
6280 C CA  . GLY A 410 ? 0.2499 0.2920 0.3178 0.0136  -0.0277 -0.0227 409 GLY A CA  
6281 C C   . GLY A 410 ? 0.2732 0.3211 0.3384 0.0205  -0.0263 -0.0159 409 GLY A C   
6282 O O   . GLY A 410 ? 0.2905 0.3422 0.3469 0.0261  -0.0325 -0.0156 409 GLY A O   
6286 N N   . VAL A 411 ? 0.2273 0.2761 0.2997 0.0208  -0.0192 -0.0110 410 VAL A N   
6287 C CA  . VAL A 411 ? 0.2154 0.2710 0.2900 0.0296  -0.0192 -0.0084 410 VAL A CA  
6288 C C   . VAL A 411 ? 0.2155 0.2944 0.3106 0.0307  -0.0242 -0.0116 410 VAL A C   
6289 O O   . VAL A 411 ? 0.2252 0.3112 0.3220 0.0398  -0.0312 -0.0124 410 VAL A O   
6290 C CB  . VAL A 411 ? 0.2415 0.2932 0.3156 0.0306  -0.0097 -0.0055 410 VAL A CB  
6291 C CG1 . VAL A 411 ? 0.2827 0.3421 0.3616 0.0419  -0.0104 -0.0068 410 VAL A CG1 
6292 C CG2 . VAL A 411 ? 0.2728 0.3031 0.3287 0.0290  -0.0063 -0.0026 410 VAL A CG2 
6302 N N   . ASP A 412 ? 0.2165 0.3079 0.3289 0.0208  -0.0218 -0.0126 411 ASP A N   
6303 C CA  . ASP A 412 ? 0.2419 0.3606 0.3782 0.0190  -0.0255 -0.0151 411 ASP A CA  
6304 C C   . ASP A 412 ? 0.2395 0.3635 0.3773 0.0221  -0.0386 -0.0204 411 ASP A C   
6305 O O   . ASP A 412 ? 0.2197 0.3663 0.3738 0.0269  -0.0443 -0.0230 411 ASP A O   
6306 C CB  . ASP A 412 ? 0.3103 0.4364 0.4627 0.0034  -0.0217 -0.0122 411 ASP A CB  
6307 C CG  . ASP A 412 ? 0.4471 0.6059 0.6275 -0.0026 -0.0237 -0.0130 411 ASP A CG  
6308 O OD1 . ASP A 412 ? 0.4120 0.5948 0.6024 0.0038  -0.0176 -0.0128 411 ASP A OD1 
6309 O OD2 . ASP A 412 ? 0.5720 0.7333 0.7659 -0.0139 -0.0317 -0.0148 411 ASP A OD2 
6314 N N   . ALA A 413 ? 0.2235 0.3304 0.3450 0.0199  -0.0439 -0.0232 412 ALA A N   
6315 C CA  . ALA A 413 ? 0.2342 0.3470 0.3524 0.0220  -0.0567 -0.0294 412 ALA A CA  
6316 C C   . ALA A 413 ? 0.2437 0.3552 0.3456 0.0345  -0.0627 -0.0258 412 ALA A C   
6317 O O   . ALA A 413 ? 0.2552 0.3755 0.3537 0.0372  -0.0746 -0.0293 412 ALA A O   
6318 C CB  . ALA A 413 ? 0.2435 0.3417 0.3485 0.0163  -0.0594 -0.0360 412 ALA A CB  
6324 N N   . LEU A 414 ? 0.2425 0.3421 0.3343 0.0416  -0.0565 -0.0186 413 LEU A N   
6325 C CA  . LEU A 414 ? 0.2565 0.3498 0.3346 0.0528  -0.0644 -0.0127 413 LEU A CA  
6326 C C   . LEU A 414 ? 0.2792 0.3928 0.3773 0.0623  -0.0741 -0.0147 413 LEU A C   
6327 O O   . LEU A 414 ? 0.2996 0.4344 0.4239 0.0615  -0.0705 -0.0199 413 LEU A O   
6328 C CB  . LEU A 414 ? 0.2567 0.3294 0.3233 0.0571  -0.0569 -0.0058 413 LEU A CB  
6329 C CG  . LEU A 414 ? 0.2539 0.3083 0.3009 0.0491  -0.0486 -0.0028 413 LEU A CG  
6330 C CD1 . LEU A 414 ? 0.2936 0.3299 0.3340 0.0526  -0.0425 0.0028  413 LEU A CD1 
6331 C CD2 . LEU A 414 ? 0.2688 0.3190 0.2927 0.0466  -0.0550 0.0004  413 LEU A CD2 
6343 N N   . SER A 415 ? 0.2798 0.3884 0.3660 0.0717  -0.0868 -0.0094 414 SER A N   
6344 C CA  . SER A 415 ? 0.2879 0.4140 0.3932 0.0839  -0.0985 -0.0111 414 SER A CA  
6345 C C   . SER A 415 ? 0.2970 0.4246 0.4195 0.0945  -0.0926 -0.0130 414 SER A C   
6346 O O   . SER A 415 ? 0.2980 0.4025 0.4079 0.0964  -0.0855 -0.0089 414 SER A O   
6347 C CB  . SER A 415 ? 0.3266 0.4413 0.4123 0.0924  -0.1151 -0.0020 414 SER A CB  
6348 O OG  . SER A 415 ? 0.3232 0.4426 0.3912 0.0846  -0.1221 -0.0017 414 SER A OG  
6354 N N   . ASN A 416 ? 0.3590 0.5163 0.5112 0.1020  -0.0960 -0.0206 415 ASN A N   
6355 C CA  . ASN A 416 ? 0.4137 0.5793 0.5840 0.1152  -0.0914 -0.0260 415 ASN A CA  
6356 C C   . ASN A 416 ? 0.4321 0.5826 0.5993 0.1344  -0.1082 -0.0229 415 ASN A C   
6357 O O   . ASN A 416 ? 0.4641 0.6166 0.6286 0.1386  -0.1246 -0.0186 415 ASN A O   
6358 C CB  . ASN A 416 ? 0.4992 0.7099 0.7053 0.1145  -0.0862 -0.0363 415 ASN A CB  
6359 C CG  . ASN A 416 ? 0.5722 0.7938 0.7826 0.0957  -0.0688 -0.0369 415 ASN A CG  
6360 O OD1 . ASN A 416 ? 0.5694 0.7685 0.7617 0.0899  -0.0576 -0.0332 415 ASN A OD1 
6361 N ND2 . ASN A 416 ? 0.6091 0.8648 0.8445 0.0854  -0.0678 -0.0406 415 ASN A ND2 
6368 N N   . ILE A 417 ? 0.4803 0.6133 0.6465 0.1460  -0.1060 -0.0248 416 ILE A N   
6369 C CA  . ILE A 417 ? 0.6477 0.7653 0.8173 0.1664  -0.1240 -0.0236 416 ILE A CA  
6370 C C   . ILE A 417 ? 0.7776 0.9363 0.9831 0.1810  -0.1316 -0.0357 416 ILE A C   
6371 O O   . ILE A 417 ? 0.8557 1.0479 1.0863 0.1838  -0.1189 -0.0491 416 ILE A O   
6372 C CB  . ILE A 417 ? 0.7334 0.8230 0.8980 0.1763  -0.1212 -0.0266 416 ILE A CB  
6373 C CG1 . ILE A 417 ? 0.8183 0.8663 0.9484 0.1623  -0.1181 -0.0124 416 ILE A CG1 
6374 C CG2 . ILE A 417 ? 0.7904 0.8676 0.9678 0.2007  -0.1418 -0.0296 416 ILE A CG2 
6375 C CD1 . ILE A 417 ? 0.9008 0.9249 1.0265 0.1664  -0.1116 -0.0172 416 ILE A CD1 
# 
