data_8TF5
# 
_entry.id   8TF5 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8TF5         pdb_00008tf5 10.2210/pdb8tf5/pdb 
WWPDB D_1000275785 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2024-12-04 
2 'Structure model' 1 1 2024-12-18 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
5 2 'Structure model' '_citation.title'                   
6 2 'Structure model' '_citation_author.identifier_ORCID' 
7 2 'Structure model' '_citation_author.name'             
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8TF5 
_pdbx_database_status.recvd_initial_deposition_date   2023-07-07 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              cherezov@usc.edu 
_pdbx_contact_author.name_first         Vadim 
_pdbx_contact_author.name_last          Cherezov 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-5265-3914 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Barekatain, M.'   1  ? 
'Johansson, L.'    2  ? 
'Lam, J.H.'        3  ? 
'Sadybekov, A.V.'  4  ? 
'Han, G.W.'        5  ? 
'Popov, P.'        6  ? 
'Russo, J.'        7  ? 
'Bliesath, J.'     8  ? 
'Brice, N.'        9  ? 
'Beresford, M.'    10 ? 
'Carlson, L.'      11 ? 
'Saikatendu, K.S.' 12 ? 
'Sun, H.'          13 ? 
'Murphy, S.'       14 ? 
'Monenschein, H.'  15 ? 
'Schiffer, H.H.'   16 ? 
'Lutomski, C.'     17 ? 
'Robinson, C.V.'   18 ? 
'Liu, Z.'          19 ? 
'Hua, T.'          20 ? 
'Katritch, V.'     21 ? 
'Cherezov, V.'     22 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Sci.Signal. 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1937-9145 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            17 
_citation.language                  ? 
_citation.page_first                eado8741 
_citation.page_last                 eado8741 
_citation.title                     
;Structural insights into the high basal activity and inverse agonism of the orphan receptor GPR6 implicated in Parkinson's disease.
;
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1126/scisignal.ado8741 
_citation.pdbx_database_id_PubMed   39626010 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Barekatain, M.'   1  0000-0003-4178-684X 
primary 'Johansson, L.C.'  2  ?                   
primary 'Lam, J.H.'        3  0000-0002-5496-6228 
primary 'Chang, H.'        4  0000-0003-1684-8201 
primary 'Sadybekov, A.V.'  5  0000-0003-3925-983X 
primary 'Han, G.W.'        6  0000-0003-4107-835X 
primary 'Russo, J.'        7  ?                   
primary 'Bliesath, J.'     8  ?                   
primary 'Brice, N.L.'      9  ?                   
primary 'Carlton, M.B.L.'  10 ?                   
primary 'Saikatendu, K.S.' 11 0000-0001-6734-237X 
primary 'Sun, H.'          12 ?                   
primary 'Murphy, S.T.'     13 0009-0000-5404-6512 
primary 'Monenschein, H.'  14 ?                   
primary 'Schiffer, H.H.'   15 ?                   
primary 'Popov, P.'        16 ?                   
primary 'Lutomski, C.A.'   17 0000-0001-7509-103X 
primary 'Robinson, C.V.'   18 0000-0001-7829-5505 
primary 'Liu, Z.J.'        19 0000-0001-7279-2893 
primary 'Hua, T.'          20 0000-0002-6132-2068 
primary 'Katritch, V.'     21 0000-0003-3883-4505 
primary 'Cherezov, V.'     22 0000-0002-5265-3914 
# 
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 
'G-protein coupled receptor 6,Soluble cytochrome b562 chimera,Soluble cytochrome b562,G-protein coupled receptor 6' 47664.312 1  ? 
C92L,A142P,M232W,H327I,R331L,G342R,S354C,Y383L,C408D ? ? 
2 non-polymer syn '(2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate' 356.540   5  ? ? ? ? 
3 non-polymer syn 2,5,8,11,14,17-HEXAOXANONADECAN-19-OL 296.357   2  ? ?                                                    ? ? 
4 non-polymer syn 'OLEIC ACID' 282.461   12 ? ?                                                    ? ? 
5 non-polymer syn CHOLESTEROL 386.654   1  ? ?                                                    ? ? 
6 water       nat water 18.015    74 ? ?                                                    ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Cytochrome b-562' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   yes 
_entity_poly.pdbx_seq_one_letter_code       
;MKTIIALSYIFCLVFAGGANGSLELSSQLSAGPPGLLLPAVNPWDVLLCVSGTVIAGENALVVALIASTPALRTPMFVLV
GSLATADLLAGLGLILHFVFQYLVPSETVSLLTVGFLVASFAASVSSLLAITVDRYLSLYNPLTYYSRRTLLGVHLLLAA
TWTVSLGLGLLPVLGWNCLAERAACSVVRPLARSHVALLSAAFFMVFGIMLHLYVRI(YCM)QVVWRHAADLEDNWETLN
DNLKVIEKADNAAQVKDALTKMRAAALDAQKATPPKLEDKSPDSPEMKDFRHGFDILVGQIDDALKLANEGKVKEAQAAA
EQLKTTRNAYIQKYLAHLAATRKGVRTLAVVLGTFGACWLPFAIYCVVGSHEDPAVYTYATLLPATLNSMINPIIYAFRN
QEIQRALWLLLDGCFQSKVPFRSRSPSEVEFHHHHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MKTIIALSYIFCLVFAGGANGSLELSSQLSAGPPGLLLPAVNPWDVLLCVSGTVIAGENALVVALIASTPALRTPMFVLV
GSLATADLLAGLGLILHFVFQYLVPSETVSLLTVGFLVASFAASVSSLLAITVDRYLSLYNPLTYYSRRTLLGVHLLLAA
TWTVSLGLGLLPVLGWNCLAERAACSVVRPLARSHVALLSAAFFMVFGIMLHLYVRICQVVWRHAADLEDNWETLNDNLK
VIEKADNAAQVKDALTKMRAAALDAQKATPPKLEDKSPDSPEMKDFRHGFDILVGQIDDALKLANEGKVKEAQAAAEQLK
TTRNAYIQKYLAHLAATRKGVRTLAVVLGTFGACWLPFAIYCVVGSHEDPAVYTYATLLPATLNSMINPIIYAFRNQEIQ
RALWLLLDGCFQSKVPFRSRSPSEVEFHHHHHHHHH
;
_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 '(2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate' OLC 
3 2,5,8,11,14,17-HEXAOXANONADECAN-19-OL            P15 
4 'OLEIC ACID'                                     OLA 
5 CHOLESTEROL                                      CLR 
6 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   LYS n 
1 3   THR n 
1 4   ILE n 
1 5   ILE n 
1 6   ALA n 
1 7   LEU n 
1 8   SER n 
1 9   TYR n 
1 10  ILE n 
1 11  PHE n 
1 12  CYS n 
1 13  LEU n 
1 14  VAL n 
1 15  PHE n 
1 16  ALA n 
1 17  GLY n 
1 18  GLY n 
1 19  ALA n 
1 20  ASN n 
1 21  GLY n 
1 22  SER n 
1 23  LEU n 
1 24  GLU n 
1 25  LEU n 
1 26  SER n 
1 27  SER n 
1 28  GLN n 
1 29  LEU n 
1 30  SER n 
1 31  ALA n 
1 32  GLY n 
1 33  PRO n 
1 34  PRO n 
1 35  GLY n 
1 36  LEU n 
1 37  LEU n 
1 38  LEU n 
1 39  PRO n 
1 40  ALA n 
1 41  VAL n 
1 42  ASN n 
1 43  PRO n 
1 44  TRP n 
1 45  ASP n 
1 46  VAL n 
1 47  LEU n 
1 48  LEU n 
1 49  CYS n 
1 50  VAL n 
1 51  SER n 
1 52  GLY n 
1 53  THR n 
1 54  VAL n 
1 55  ILE n 
1 56  ALA n 
1 57  GLY n 
1 58  GLU n 
1 59  ASN n 
1 60  ALA n 
1 61  LEU n 
1 62  VAL n 
1 63  VAL n 
1 64  ALA n 
1 65  LEU n 
1 66  ILE n 
1 67  ALA n 
1 68  SER n 
1 69  THR n 
1 70  PRO n 
1 71  ALA n 
1 72  LEU n 
1 73  ARG n 
1 74  THR n 
1 75  PRO n 
1 76  MET n 
1 77  PHE n 
1 78  VAL n 
1 79  LEU n 
1 80  VAL n 
1 81  GLY n 
1 82  SER n 
1 83  LEU n 
1 84  ALA n 
1 85  THR n 
1 86  ALA n 
1 87  ASP n 
1 88  LEU n 
1 89  LEU n 
1 90  ALA n 
1 91  GLY n 
1 92  LEU n 
1 93  GLY n 
1 94  LEU n 
1 95  ILE n 
1 96  LEU n 
1 97  HIS n 
1 98  PHE n 
1 99  VAL n 
1 100 PHE n 
1 101 GLN n 
1 102 TYR n 
1 103 LEU n 
1 104 VAL n 
1 105 PRO n 
1 106 SER n 
1 107 GLU n 
1 108 THR n 
1 109 VAL n 
1 110 SER n 
1 111 LEU n 
1 112 LEU n 
1 113 THR n 
1 114 VAL n 
1 115 GLY n 
1 116 PHE n 
1 117 LEU n 
1 118 VAL n 
1 119 ALA n 
1 120 SER n 
1 121 PHE n 
1 122 ALA n 
1 123 ALA n 
1 124 SER n 
1 125 VAL n 
1 126 SER n 
1 127 SER n 
1 128 LEU n 
1 129 LEU n 
1 130 ALA n 
1 131 ILE n 
1 132 THR n 
1 133 VAL n 
1 134 ASP n 
1 135 ARG n 
1 136 TYR n 
1 137 LEU n 
1 138 SER n 
1 139 LEU n 
1 140 TYR n 
1 141 ASN n 
1 142 PRO n 
1 143 LEU n 
1 144 THR n 
1 145 TYR n 
1 146 TYR n 
1 147 SER n 
1 148 ARG n 
1 149 ARG n 
1 150 THR n 
1 151 LEU n 
1 152 LEU n 
1 153 GLY n 
1 154 VAL n 
1 155 HIS n 
1 156 LEU n 
1 157 LEU n 
1 158 LEU n 
1 159 ALA n 
1 160 ALA n 
1 161 THR n 
1 162 TRP n 
1 163 THR n 
1 164 VAL n 
1 165 SER n 
1 166 LEU n 
1 167 GLY n 
1 168 LEU n 
1 169 GLY n 
1 170 LEU n 
1 171 LEU n 
1 172 PRO n 
1 173 VAL n 
1 174 LEU n 
1 175 GLY n 
1 176 TRP n 
1 177 ASN n 
1 178 CYS n 
1 179 LEU n 
1 180 ALA n 
1 181 GLU n 
1 182 ARG n 
1 183 ALA n 
1 184 ALA n 
1 185 CYS n 
1 186 SER n 
1 187 VAL n 
1 188 VAL n 
1 189 ARG n 
1 190 PRO n 
1 191 LEU n 
1 192 ALA n 
1 193 ARG n 
1 194 SER n 
1 195 HIS n 
1 196 VAL n 
1 197 ALA n 
1 198 LEU n 
1 199 LEU n 
1 200 SER n 
1 201 ALA n 
1 202 ALA n 
1 203 PHE n 
1 204 PHE n 
1 205 MET n 
1 206 VAL n 
1 207 PHE n 
1 208 GLY n 
1 209 ILE n 
1 210 MET n 
1 211 LEU n 
1 212 HIS n 
1 213 LEU n 
1 214 TYR n 
1 215 VAL n 
1 216 ARG n 
1 217 ILE n 
1 218 YCM n 
1 219 GLN n 
1 220 VAL n 
1 221 VAL n 
1 222 TRP n 
1 223 ARG n 
1 224 HIS n 
1 225 ALA n 
1 226 ALA n 
1 227 ASP n 
1 228 LEU n 
1 229 GLU n 
1 230 ASP n 
1 231 ASN n 
1 232 TRP n 
1 233 GLU n 
1 234 THR n 
1 235 LEU n 
1 236 ASN n 
1 237 ASP n 
1 238 ASN n 
1 239 LEU n 
1 240 LYS n 
1 241 VAL n 
1 242 ILE n 
1 243 GLU n 
1 244 LYS n 
1 245 ALA n 
1 246 ASP n 
1 247 ASN n 
1 248 ALA n 
1 249 ALA n 
1 250 GLN n 
1 251 VAL n 
1 252 LYS n 
1 253 ASP n 
1 254 ALA n 
1 255 LEU n 
1 256 THR n 
1 257 LYS n 
1 258 MET n 
1 259 ARG n 
1 260 ALA n 
1 261 ALA n 
1 262 ALA n 
1 263 LEU n 
1 264 ASP n 
1 265 ALA n 
1 266 GLN n 
1 267 LYS n 
1 268 ALA n 
1 269 THR n 
1 270 PRO n 
1 271 PRO n 
1 272 LYS n 
1 273 LEU n 
1 274 GLU n 
1 275 ASP n 
1 276 LYS n 
1 277 SER n 
1 278 PRO n 
1 279 ASP n 
1 280 SER n 
1 281 PRO n 
1 282 GLU n 
1 283 MET n 
1 284 LYS n 
1 285 ASP n 
1 286 PHE n 
1 287 ARG n 
1 288 HIS n 
1 289 GLY n 
1 290 PHE n 
1 291 ASP n 
1 292 ILE n 
1 293 LEU n 
1 294 VAL n 
1 295 GLY n 
1 296 GLN n 
1 297 ILE n 
1 298 ASP n 
1 299 ASP n 
1 300 ALA n 
1 301 LEU n 
1 302 LYS n 
1 303 LEU n 
1 304 ALA n 
1 305 ASN n 
1 306 GLU n 
1 307 GLY n 
1 308 LYS n 
1 309 VAL n 
1 310 LYS n 
1 311 GLU n 
1 312 ALA n 
1 313 GLN n 
1 314 ALA n 
1 315 ALA n 
1 316 ALA n 
1 317 GLU n 
1 318 GLN n 
1 319 LEU n 
1 320 LYS n 
1 321 THR n 
1 322 THR n 
1 323 ARG n 
1 324 ASN n 
1 325 ALA n 
1 326 TYR n 
1 327 ILE n 
1 328 GLN n 
1 329 LYS n 
1 330 TYR n 
1 331 LEU n 
1 332 ALA n 
1 333 HIS n 
1 334 LEU n 
1 335 ALA n 
1 336 ALA n 
1 337 THR n 
1 338 ARG n 
1 339 LYS n 
1 340 GLY n 
1 341 VAL n 
1 342 ARG n 
1 343 THR n 
1 344 LEU n 
1 345 ALA n 
1 346 VAL n 
1 347 VAL n 
1 348 LEU n 
1 349 GLY n 
1 350 THR n 
1 351 PHE n 
1 352 GLY n 
1 353 ALA n 
1 354 CYS n 
1 355 TRP n 
1 356 LEU n 
1 357 PRO n 
1 358 PHE n 
1 359 ALA n 
1 360 ILE n 
1 361 TYR n 
1 362 CYS n 
1 363 VAL n 
1 364 VAL n 
1 365 GLY n 
1 366 SER n 
1 367 HIS n 
1 368 GLU n 
1 369 ASP n 
1 370 PRO n 
1 371 ALA n 
1 372 VAL n 
1 373 TYR n 
1 374 THR n 
1 375 TYR n 
1 376 ALA n 
1 377 THR n 
1 378 LEU n 
1 379 LEU n 
1 380 PRO n 
1 381 ALA n 
1 382 THR n 
1 383 LEU n 
1 384 ASN n 
1 385 SER n 
1 386 MET n 
1 387 ILE n 
1 388 ASN n 
1 389 PRO n 
1 390 ILE n 
1 391 ILE n 
1 392 TYR n 
1 393 ALA n 
1 394 PHE n 
1 395 ARG n 
1 396 ASN n 
1 397 GLN n 
1 398 GLU n 
1 399 ILE n 
1 400 GLN n 
1 401 ARG n 
1 402 ALA n 
1 403 LEU n 
1 404 TRP n 
1 405 LEU n 
1 406 LEU n 
1 407 LEU n 
1 408 ASP n 
1 409 GLY n 
1 410 CYS n 
1 411 PHE n 
1 412 GLN n 
1 413 SER n 
1 414 LYS n 
1 415 VAL n 
1 416 PRO n 
1 417 PHE n 
1 418 ARG n 
1 419 SER n 
1 420 ARG n 
1 421 SER n 
1 422 PRO n 
1 423 SER n 
1 424 GLU n 
1 425 VAL n 
1 426 GLU n 
1 427 PHE n 
1 428 HIS n 
1 429 HIS n 
1 430 HIS n 
1 431 HIS n 
1 432 HIS n 
1 433 HIS n 
1 434 HIS n 
1 435 HIS n 
1 436 HIS n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1   225 human ? GPR6 ? ? ? ? ? ? 'Homo sapiens'     9606 ? ? ? ? ? ? ? 'fall armyworm' 
'Spodoptera frugiperda' 7108 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
1 2 sample 'Biological sequence' 226 331 ?     ? cybC ? ? ? ? ? ? 'Escherichia coli' 562  ? ? ? ? ? ? ? 'fall armyworm' 
'Spodoptera frugiperda' 7108 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
1 3 sample 'Biological sequence' 332 436 human ? GPR6 ? ? ? ? ? ? 'Homo sapiens'     9606 ? ? ? ? ? ? ? 'fall armyworm' 
'Spodoptera frugiperda' 7108 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                          ?                    'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                                         ?                    'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                                       ?                    'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                  ?                    'C4 H7 N O4'     133.103 
CLR non-polymer         . CHOLESTEROL                                      ?                    'C27 H46 O'      386.654 
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 
OLA non-polymer         . 'OLEIC ACID'                                     ?                    'C18 H34 O2'     282.461 
OLC non-polymer         . '(2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate' 1-Oleoyl-R-glycerol  'C21 H40 O4'     356.540 
P15 non-polymer         . 2,5,8,11,14,17-HEXAOXANONADECAN-19-OL            ?                    'C13 H28 O7'     296.357 
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 
YCM 'L-peptide linking' n 'S-(2-AMINO-2-OXOETHYL)-L-CYSTEINE'              CYSTEINE-S-ACETAMIDE 'C5 H10 N2 O3 S' 178.209 
# 
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   32   ?    ?   ?   A . n 
A 1 2   LYS 2   33   ?    ?   ?   A . n 
A 1 3   THR 3   34   ?    ?   ?   A . n 
A 1 4   ILE 4   35   ?    ?   ?   A . n 
A 1 5   ILE 5   36   ?    ?   ?   A . n 
A 1 6   ALA 6   37   ?    ?   ?   A . n 
A 1 7   LEU 7   38   ?    ?   ?   A . n 
A 1 8   SER 8   39   ?    ?   ?   A . n 
A 1 9   TYR 9   40   ?    ?   ?   A . n 
A 1 10  ILE 10  41   ?    ?   ?   A . n 
A 1 11  PHE 11  42   ?    ?   ?   A . n 
A 1 12  CYS 12  43   ?    ?   ?   A . n 
A 1 13  LEU 13  44   ?    ?   ?   A . n 
A 1 14  VAL 14  45   ?    ?   ?   A . n 
A 1 15  PHE 15  46   ?    ?   ?   A . n 
A 1 16  ALA 16  47   ?    ?   ?   A . n 
A 1 17  GLY 17  48   ?    ?   ?   A . n 
A 1 18  GLY 18  49   ?    ?   ?   A . n 
A 1 19  ALA 19  50   ?    ?   ?   A . n 
A 1 20  ASN 20  51   ?    ?   ?   A . n 
A 1 21  GLY 21  52   ?    ?   ?   A . n 
A 1 22  SER 22  53   ?    ?   ?   A . n 
A 1 23  LEU 23  54   ?    ?   ?   A . n 
A 1 24  GLU 24  55   ?    ?   ?   A . n 
A 1 25  LEU 25  56   ?    ?   ?   A . n 
A 1 26  SER 26  57   ?    ?   ?   A . n 
A 1 27  SER 27  58   ?    ?   ?   A . n 
A 1 28  GLN 28  59   ?    ?   ?   A . n 
A 1 29  LEU 29  60   ?    ?   ?   A . n 
A 1 30  SER 30  61   ?    ?   ?   A . n 
A 1 31  ALA 31  62   ?    ?   ?   A . n 
A 1 32  GLY 32  63   ?    ?   ?   A . n 
A 1 33  PRO 33  64   ?    ?   ?   A . n 
A 1 34  PRO 34  65   ?    ?   ?   A . n 
A 1 35  GLY 35  66   ?    ?   ?   A . n 
A 1 36  LEU 36  67   ?    ?   ?   A . n 
A 1 37  LEU 37  68   ?    ?   ?   A . n 
A 1 38  LEU 38  69   ?    ?   ?   A . n 
A 1 39  PRO 39  70   70   PRO PRO A . n 
A 1 40  ALA 40  71   71   ALA ALA A . n 
A 1 41  VAL 41  72   72   VAL VAL A . n 
A 1 42  ASN 42  73   73   ASN ASN A . n 
A 1 43  PRO 43  74   74   PRO PRO A . n 
A 1 44  TRP 44  75   75   TRP TRP A . n 
A 1 45  ASP 45  76   76   ASP ASP A . n 
A 1 46  VAL 46  77   77   VAL VAL A . n 
A 1 47  LEU 47  78   78   LEU LEU A . n 
A 1 48  LEU 48  79   79   LEU LEU A . n 
A 1 49  CYS 49  80   80   CYS CYS A . n 
A 1 50  VAL 50  81   81   VAL VAL A . n 
A 1 51  SER 51  82   82   SER SER A . n 
A 1 52  GLY 52  83   83   GLY GLY A . n 
A 1 53  THR 53  84   84   THR THR A . n 
A 1 54  VAL 54  85   85   VAL VAL A . n 
A 1 55  ILE 55  86   86   ILE ILE A . n 
A 1 56  ALA 56  87   87   ALA ALA A . n 
A 1 57  GLY 57  88   88   GLY GLY A . n 
A 1 58  GLU 58  89   89   GLU GLU A . n 
A 1 59  ASN 59  90   90   ASN ASN A . n 
A 1 60  ALA 60  91   91   ALA ALA A . n 
A 1 61  LEU 61  92   92   LEU LEU A . n 
A 1 62  VAL 62  93   93   VAL VAL A . n 
A 1 63  VAL 63  94   94   VAL VAL A . n 
A 1 64  ALA 64  95   95   ALA ALA A . n 
A 1 65  LEU 65  96   96   LEU LEU A . n 
A 1 66  ILE 66  97   97   ILE ILE A . n 
A 1 67  ALA 67  98   98   ALA ALA A . n 
A 1 68  SER 68  99   99   SER SER A . n 
A 1 69  THR 69  100  100  THR THR A . n 
A 1 70  PRO 70  101  101  PRO PRO A . n 
A 1 71  ALA 71  102  102  ALA ALA A . n 
A 1 72  LEU 72  103  103  LEU LEU A . n 
A 1 73  ARG 73  104  104  ARG ARG A . n 
A 1 74  THR 74  105  105  THR THR A . n 
A 1 75  PRO 75  106  106  PRO PRO A . n 
A 1 76  MET 76  107  107  MET MET A . n 
A 1 77  PHE 77  108  108  PHE PHE A . n 
A 1 78  VAL 78  109  109  VAL VAL A . n 
A 1 79  LEU 79  110  110  LEU LEU A . n 
A 1 80  VAL 80  111  111  VAL VAL A . n 
A 1 81  GLY 81  112  112  GLY GLY A . n 
A 1 82  SER 82  113  113  SER SER A . n 
A 1 83  LEU 83  114  114  LEU LEU A . n 
A 1 84  ALA 84  115  115  ALA ALA A . n 
A 1 85  THR 85  116  116  THR THR A . n 
A 1 86  ALA 86  117  117  ALA ALA A . n 
A 1 87  ASP 87  118  118  ASP ASP A . n 
A 1 88  LEU 88  119  119  LEU LEU A . n 
A 1 89  LEU 89  120  120  LEU LEU A . n 
A 1 90  ALA 90  121  121  ALA ALA A . n 
A 1 91  GLY 91  122  122  GLY GLY A . n 
A 1 92  LEU 92  123  123  LEU LEU A . n 
A 1 93  GLY 93  124  124  GLY GLY A . n 
A 1 94  LEU 94  125  125  LEU LEU A . n 
A 1 95  ILE 95  126  126  ILE ILE A . n 
A 1 96  LEU 96  127  127  LEU LEU A . n 
A 1 97  HIS 97  128  128  HIS HIS A . n 
A 1 98  PHE 98  129  129  PHE PHE A . n 
A 1 99  VAL 99  130  130  VAL VAL A . n 
A 1 100 PHE 100 131  131  PHE PHE A . n 
A 1 101 GLN 101 132  132  GLN GLN A . n 
A 1 102 TYR 102 133  133  TYR TYR A . n 
A 1 103 LEU 103 134  134  LEU LEU A . n 
A 1 104 VAL 104 135  135  VAL VAL A . n 
A 1 105 PRO 105 136  136  PRO PRO A . n 
A 1 106 SER 106 137  137  SER SER A . n 
A 1 107 GLU 107 138  138  GLU GLU A . n 
A 1 108 THR 108 139  139  THR THR A . n 
A 1 109 VAL 109 140  140  VAL VAL A . n 
A 1 110 SER 110 141  141  SER SER A . n 
A 1 111 LEU 111 142  142  LEU LEU A . n 
A 1 112 LEU 112 143  143  LEU LEU A . n 
A 1 113 THR 113 144  144  THR THR A . n 
A 1 114 VAL 114 145  145  VAL VAL A . n 
A 1 115 GLY 115 146  146  GLY GLY A . n 
A 1 116 PHE 116 147  147  PHE PHE A . n 
A 1 117 LEU 117 148  148  LEU LEU A . n 
A 1 118 VAL 118 149  149  VAL VAL A . n 
A 1 119 ALA 119 150  150  ALA ALA A . n 
A 1 120 SER 120 151  151  SER SER A . n 
A 1 121 PHE 121 152  152  PHE PHE A . n 
A 1 122 ALA 122 153  153  ALA ALA A . n 
A 1 123 ALA 123 154  154  ALA ALA A . n 
A 1 124 SER 124 155  155  SER SER A . n 
A 1 125 VAL 125 156  156  VAL VAL A . n 
A 1 126 SER 126 157  157  SER SER A . n 
A 1 127 SER 127 158  158  SER SER A . n 
A 1 128 LEU 128 159  159  LEU LEU A . n 
A 1 129 LEU 129 160  160  LEU LEU A . n 
A 1 130 ALA 130 161  161  ALA ALA A . n 
A 1 131 ILE 131 162  162  ILE ILE A . n 
A 1 132 THR 132 163  163  THR THR A . n 
A 1 133 VAL 133 164  164  VAL VAL A . n 
A 1 134 ASP 134 165  165  ASP ASP A . n 
A 1 135 ARG 135 166  166  ARG ARG A . n 
A 1 136 TYR 136 167  167  TYR TYR A . n 
A 1 137 LEU 137 168  168  LEU LEU A . n 
A 1 138 SER 138 169  169  SER SER A . n 
A 1 139 LEU 139 170  170  LEU LEU A . n 
A 1 140 TYR 140 171  171  TYR TYR A . n 
A 1 141 ASN 141 172  172  ASN ASN A . n 
A 1 142 PRO 142 173  173  PRO PRO A . n 
A 1 143 LEU 143 174  174  LEU LEU A . n 
A 1 144 THR 144 175  175  THR THR A . n 
A 1 145 TYR 145 176  176  TYR TYR A . n 
A 1 146 TYR 146 177  177  TYR TYR A . n 
A 1 147 SER 147 178  178  SER SER A . n 
A 1 148 ARG 148 179  179  ARG ARG A . n 
A 1 149 ARG 149 180  180  ARG ARG A . n 
A 1 150 THR 150 181  181  THR THR A . n 
A 1 151 LEU 151 182  182  LEU LEU A . n 
A 1 152 LEU 152 183  183  LEU LEU A . n 
A 1 153 GLY 153 184  184  GLY GLY A . n 
A 1 154 VAL 154 185  185  VAL VAL A . n 
A 1 155 HIS 155 186  186  HIS HIS A . n 
A 1 156 LEU 156 187  187  LEU LEU A . n 
A 1 157 LEU 157 188  188  LEU LEU A . n 
A 1 158 LEU 158 189  189  LEU LEU A . n 
A 1 159 ALA 159 190  190  ALA ALA A . n 
A 1 160 ALA 160 191  191  ALA ALA A . n 
A 1 161 THR 161 192  192  THR THR A . n 
A 1 162 TRP 162 193  193  TRP TRP A . n 
A 1 163 THR 163 194  194  THR THR A . n 
A 1 164 VAL 164 195  195  VAL VAL A . n 
A 1 165 SER 165 196  196  SER SER A . n 
A 1 166 LEU 166 197  197  LEU LEU A . n 
A 1 167 GLY 167 198  198  GLY GLY A . n 
A 1 168 LEU 168 199  199  LEU LEU A . n 
A 1 169 GLY 169 200  200  GLY GLY A . n 
A 1 170 LEU 170 201  201  LEU LEU A . n 
A 1 171 LEU 171 202  202  LEU LEU A . n 
A 1 172 PRO 172 203  203  PRO PRO A . n 
A 1 173 VAL 173 204  204  VAL VAL A . n 
A 1 174 LEU 174 205  205  LEU LEU A . n 
A 1 175 GLY 175 206  206  GLY GLY A . n 
A 1 176 TRP 176 207  207  TRP TRP A . n 
A 1 177 ASN 177 208  208  ASN ASN A . n 
A 1 178 CYS 178 209  209  CYS CYS A . n 
A 1 179 LEU 179 210  210  LEU LEU A . n 
A 1 180 ALA 180 211  211  ALA ALA A . n 
A 1 181 GLU 181 212  212  GLU GLU A . n 
A 1 182 ARG 182 213  213  ARG ARG A . n 
A 1 183 ALA 183 214  214  ALA ALA A . n 
A 1 184 ALA 184 215  215  ALA ALA A . n 
A 1 185 CYS 185 216  216  CYS CYS A . n 
A 1 186 SER 186 217  217  SER SER A . n 
A 1 187 VAL 187 218  218  VAL VAL A . n 
A 1 188 VAL 188 219  219  VAL VAL A . n 
A 1 189 ARG 189 220  220  ARG ARG A . n 
A 1 190 PRO 190 221  221  PRO PRO A . n 
A 1 191 LEU 191 222  222  LEU LEU A . n 
A 1 192 ALA 192 223  223  ALA ALA A . n 
A 1 193 ARG 193 224  224  ARG ARG A . n 
A 1 194 SER 194 225  225  SER SER A . n 
A 1 195 HIS 195 226  226  HIS HIS A . n 
A 1 196 VAL 196 227  227  VAL VAL A . n 
A 1 197 ALA 197 228  228  ALA ALA A . n 
A 1 198 LEU 198 229  229  LEU LEU A . n 
A 1 199 LEU 199 230  230  LEU LEU A . n 
A 1 200 SER 200 231  231  SER SER A . n 
A 1 201 ALA 201 232  232  ALA ALA A . n 
A 1 202 ALA 202 233  233  ALA ALA A . n 
A 1 203 PHE 203 234  234  PHE PHE A . n 
A 1 204 PHE 204 235  235  PHE PHE A . n 
A 1 205 MET 205 236  236  MET MET A . n 
A 1 206 VAL 206 237  237  VAL VAL A . n 
A 1 207 PHE 207 238  238  PHE PHE A . n 
A 1 208 GLY 208 239  239  GLY GLY A . n 
A 1 209 ILE 209 240  240  ILE ILE A . n 
A 1 210 MET 210 241  241  MET MET A . n 
A 1 211 LEU 211 242  242  LEU LEU A . n 
A 1 212 HIS 212 243  243  HIS HIS A . n 
A 1 213 LEU 213 244  244  LEU LEU A . n 
A 1 214 TYR 214 245  245  TYR TYR A . n 
A 1 215 VAL 215 246  246  VAL VAL A . n 
A 1 216 ARG 216 247  247  ARG ARG A . n 
A 1 217 ILE 217 248  248  ILE ILE A . n 
A 1 218 YCM 218 249  249  YCM YCM A . n 
A 1 219 GLN 219 250  250  GLN GLN A . n 
A 1 220 VAL 220 251  251  VAL VAL A . n 
A 1 221 VAL 221 252  252  VAL VAL A . n 
A 1 222 TRP 222 253  253  TRP TRP A . n 
A 1 223 ARG 223 254  254  ARG ARG A . n 
A 1 224 HIS 224 255  255  HIS HIS A . n 
A 1 225 ALA 225 256  256  ALA ALA A . n 
A 1 226 ALA 226 1001 1001 ALA ALA A . n 
A 1 227 ASP 227 1002 1002 ASP ASP A . n 
A 1 228 LEU 228 1003 1003 LEU LEU A . n 
A 1 229 GLU 229 1004 1004 GLU GLU A . n 
A 1 230 ASP 230 1005 1005 ASP ASP A . n 
A 1 231 ASN 231 1006 1006 ASN ASN A . n 
A 1 232 TRP 232 1007 1007 TRP TRP A . n 
A 1 233 GLU 233 1008 1008 GLU GLU A . n 
A 1 234 THR 234 1009 1009 THR THR A . n 
A 1 235 LEU 235 1010 1010 LEU LEU A . n 
A 1 236 ASN 236 1011 1011 ASN ASN A . n 
A 1 237 ASP 237 1012 1012 ASP ASP A . n 
A 1 238 ASN 238 1013 1013 ASN ASN A . n 
A 1 239 LEU 239 1014 1014 LEU LEU A . n 
A 1 240 LYS 240 1015 1015 LYS LYS A . n 
A 1 241 VAL 241 1016 1016 VAL VAL A . n 
A 1 242 ILE 242 1017 1017 ILE ILE A . n 
A 1 243 GLU 243 1018 1018 GLU GLU A . n 
A 1 244 LYS 244 1019 1019 LYS LYS A . n 
A 1 245 ALA 245 1020 1020 ALA ALA A . n 
A 1 246 ASP 246 1021 1021 ASP ASP A . n 
A 1 247 ASN 247 1022 1022 ASN ASN A . n 
A 1 248 ALA 248 1023 1023 ALA ALA A . n 
A 1 249 ALA 249 1024 1024 ALA ALA A . n 
A 1 250 GLN 250 1025 1025 GLN GLN A . n 
A 1 251 VAL 251 1026 1026 VAL VAL A . n 
A 1 252 LYS 252 1027 1027 LYS LYS A . n 
A 1 253 ASP 253 1028 1028 ASP ASP A . n 
A 1 254 ALA 254 1029 1029 ALA ALA A . n 
A 1 255 LEU 255 1030 1030 LEU LEU A . n 
A 1 256 THR 256 1031 1031 THR THR A . n 
A 1 257 LYS 257 1032 1032 LYS LYS A . n 
A 1 258 MET 258 1033 1033 MET MET A . n 
A 1 259 ARG 259 1034 1034 ARG ARG A . n 
A 1 260 ALA 260 1035 1035 ALA ALA A . n 
A 1 261 ALA 261 1036 1036 ALA ALA A . n 
A 1 262 ALA 262 1037 1037 ALA ALA A . n 
A 1 263 LEU 263 1038 1038 LEU LEU A . n 
A 1 264 ASP 264 1039 1039 ASP ASP A . n 
A 1 265 ALA 265 1040 1040 ALA ALA A . n 
A 1 266 GLN 266 1041 1041 GLN GLN A . n 
A 1 267 LYS 267 1042 1042 LYS LYS A . n 
A 1 268 ALA 268 1043 1043 ALA ALA A . n 
A 1 269 THR 269 1044 1044 THR THR A . n 
A 1 270 PRO 270 1045 1045 PRO PRO A . n 
A 1 271 PRO 271 1046 1046 PRO PRO A . n 
A 1 272 LYS 272 1047 1047 LYS LYS A . n 
A 1 273 LEU 273 1048 1048 LEU LEU A . n 
A 1 274 GLU 274 1049 1049 GLU GLU A . n 
A 1 275 ASP 275 1050 ?    ?   ?   A . n 
A 1 276 LYS 276 1051 ?    ?   ?   A . n 
A 1 277 SER 277 1052 ?    ?   ?   A . n 
A 1 278 PRO 278 1053 ?    ?   ?   A . n 
A 1 279 ASP 279 1054 ?    ?   ?   A . n 
A 1 280 SER 280 1055 ?    ?   ?   A . n 
A 1 281 PRO 281 1056 ?    ?   ?   A . n 
A 1 282 GLU 282 1057 ?    ?   ?   A . n 
A 1 283 MET 283 1058 1058 MET MET A . n 
A 1 284 LYS 284 1059 1059 LYS LYS A . n 
A 1 285 ASP 285 1060 1060 ASP ASP A . n 
A 1 286 PHE 286 1061 1061 PHE PHE A . n 
A 1 287 ARG 287 1062 1062 ARG ARG A . n 
A 1 288 HIS 288 1063 1063 HIS HIS A . n 
A 1 289 GLY 289 1064 1064 GLY GLY A . n 
A 1 290 PHE 290 1065 1065 PHE PHE A . n 
A 1 291 ASP 291 1066 1066 ASP ASP A . n 
A 1 292 ILE 292 1067 1067 ILE ILE A . n 
A 1 293 LEU 293 1068 1068 LEU LEU A . n 
A 1 294 VAL 294 1069 1069 VAL VAL A . n 
A 1 295 GLY 295 1070 1070 GLY GLY A . n 
A 1 296 GLN 296 1071 1071 GLN GLN A . n 
A 1 297 ILE 297 1072 1072 ILE ILE A . n 
A 1 298 ASP 298 1073 1073 ASP ASP A . n 
A 1 299 ASP 299 1074 1074 ASP ASP A . n 
A 1 300 ALA 300 1075 1075 ALA ALA A . n 
A 1 301 LEU 301 1076 1076 LEU LEU A . n 
A 1 302 LYS 302 1077 1077 LYS LYS A . n 
A 1 303 LEU 303 1078 1078 LEU LEU A . n 
A 1 304 ALA 304 1079 1079 ALA ALA A . n 
A 1 305 ASN 305 1080 1080 ASN ASN A . n 
A 1 306 GLU 306 1081 1081 GLU GLU A . n 
A 1 307 GLY 307 1082 1082 GLY GLY A . n 
A 1 308 LYS 308 1083 1083 LYS LYS A . n 
A 1 309 VAL 309 1084 1084 VAL VAL A . n 
A 1 310 LYS 310 1085 1085 LYS LYS A . n 
A 1 311 GLU 311 1086 1086 GLU GLU A . n 
A 1 312 ALA 312 1087 1087 ALA ALA A . n 
A 1 313 GLN 313 1088 1088 GLN GLN A . n 
A 1 314 ALA 314 1089 1089 ALA ALA A . n 
A 1 315 ALA 315 1090 1090 ALA ALA A . n 
A 1 316 ALA 316 1091 1091 ALA ALA A . n 
A 1 317 GLU 317 1092 1092 GLU GLU A . n 
A 1 318 GLN 318 1093 1093 GLN GLN A . n 
A 1 319 LEU 319 1094 1094 LEU LEU A . n 
A 1 320 LYS 320 1095 1095 LYS LYS A . n 
A 1 321 THR 321 1096 1096 THR THR A . n 
A 1 322 THR 322 1097 1097 THR THR A . n 
A 1 323 ARG 323 1098 1098 ARG ARG A . n 
A 1 324 ASN 324 1099 1099 ASN ASN A . n 
A 1 325 ALA 325 1100 1100 ALA ALA A . n 
A 1 326 TYR 326 1101 1101 TYR TYR A . n 
A 1 327 ILE 327 1102 1102 ILE ILE A . n 
A 1 328 GLN 328 1103 1103 GLN GLN A . n 
A 1 329 LYS 329 1104 1104 LYS LYS A . n 
A 1 330 TYR 330 1105 1105 TYR TYR A . n 
A 1 331 LEU 331 1106 1106 LEU LEU A . n 
A 1 332 ALA 332 900  900  ALA ALA A . n 
A 1 333 HIS 333 270  270  HIS HIS A . n 
A 1 334 LEU 334 271  271  LEU LEU A . n 
A 1 335 ALA 335 272  272  ALA ALA A . n 
A 1 336 ALA 336 273  273  ALA ALA A . n 
A 1 337 THR 337 274  274  THR THR A . n 
A 1 338 ARG 338 275  275  ARG ARG A . n 
A 1 339 LYS 339 276  276  LYS LYS A . n 
A 1 340 GLY 340 277  277  GLY GLY A . n 
A 1 341 VAL 341 278  278  VAL VAL A . n 
A 1 342 ARG 342 279  279  ARG ARG A . n 
A 1 343 THR 343 280  280  THR THR A . n 
A 1 344 LEU 344 281  281  LEU LEU A . n 
A 1 345 ALA 345 282  282  ALA ALA A . n 
A 1 346 VAL 346 283  283  VAL VAL A . n 
A 1 347 VAL 347 284  284  VAL VAL A . n 
A 1 348 LEU 348 285  285  LEU LEU A . n 
A 1 349 GLY 349 286  286  GLY GLY A . n 
A 1 350 THR 350 287  287  THR THR A . n 
A 1 351 PHE 351 288  288  PHE PHE A . n 
A 1 352 GLY 352 289  289  GLY GLY A . n 
A 1 353 ALA 353 290  290  ALA ALA A . n 
A 1 354 CYS 354 291  291  CYS CYS A . n 
A 1 355 TRP 355 292  292  TRP TRP A . n 
A 1 356 LEU 356 293  293  LEU LEU A . n 
A 1 357 PRO 357 294  294  PRO PRO A . n 
A 1 358 PHE 358 295  295  PHE PHE A . n 
A 1 359 ALA 359 296  296  ALA ALA A . n 
A 1 360 ILE 360 297  297  ILE ILE A . n 
A 1 361 TYR 361 298  298  TYR TYR A . n 
A 1 362 CYS 362 299  299  CYS CYS A . n 
A 1 363 VAL 363 300  300  VAL VAL A . n 
A 1 364 VAL 364 301  301  VAL VAL A . n 
A 1 365 GLY 365 302  302  GLY GLY A . n 
A 1 366 SER 366 303  303  SER SER A . n 
A 1 367 HIS 367 304  304  HIS HIS A . n 
A 1 368 GLU 368 305  305  GLU GLU A . n 
A 1 369 ASP 369 306  306  ASP ASP A . n 
A 1 370 PRO 370 307  307  PRO PRO A . n 
A 1 371 ALA 371 308  308  ALA ALA A . n 
A 1 372 VAL 372 309  309  VAL VAL A . n 
A 1 373 TYR 373 310  310  TYR TYR A . n 
A 1 374 THR 374 311  311  THR THR A . n 
A 1 375 TYR 375 312  312  TYR TYR A . n 
A 1 376 ALA 376 313  313  ALA ALA A . n 
A 1 377 THR 377 314  314  THR THR A . n 
A 1 378 LEU 378 315  315  LEU LEU A . n 
A 1 379 LEU 379 316  316  LEU LEU A . n 
A 1 380 PRO 380 317  317  PRO PRO A . n 
A 1 381 ALA 381 318  318  ALA ALA A . n 
A 1 382 THR 382 319  319  THR THR A . n 
A 1 383 LEU 383 320  320  LEU LEU A . n 
A 1 384 ASN 384 321  321  ASN ASN A . n 
A 1 385 SER 385 322  322  SER SER A . n 
A 1 386 MET 386 323  323  MET MET A . n 
A 1 387 ILE 387 324  324  ILE ILE A . n 
A 1 388 ASN 388 325  325  ASN ASN A . n 
A 1 389 PRO 389 326  326  PRO PRO A . n 
A 1 390 ILE 390 327  327  ILE ILE A . n 
A 1 391 ILE 391 328  328  ILE ILE A . n 
A 1 392 TYR 392 329  329  TYR TYR A . n 
A 1 393 ALA 393 330  330  ALA ALA A . n 
A 1 394 PHE 394 331  331  PHE PHE A . n 
A 1 395 ARG 395 332  332  ARG ARG A . n 
A 1 396 ASN 396 333  333  ASN ASN A . n 
A 1 397 GLN 397 334  334  GLN GLN A . n 
A 1 398 GLU 398 335  335  GLU GLU A . n 
A 1 399 ILE 399 336  336  ILE ILE A . n 
A 1 400 GLN 400 337  337  GLN GLN A . n 
A 1 401 ARG 401 338  338  ARG ARG A . n 
A 1 402 ALA 402 339  339  ALA ALA A . n 
A 1 403 LEU 403 340  340  LEU LEU A . n 
A 1 404 TRP 404 341  341  TRP TRP A . n 
A 1 405 LEU 405 342  342  LEU LEU A . n 
A 1 406 LEU 406 343  343  LEU LEU A . n 
A 1 407 LEU 407 344  344  LEU LEU A . n 
A 1 408 ASP 408 345  345  ASP ASP A . n 
A 1 409 GLY 409 346  346  GLY GLY A . n 
A 1 410 CYS 410 347  347  CYS CYS A . n 
A 1 411 PHE 411 348  ?    ?   ?   A . n 
A 1 412 GLN 412 349  ?    ?   ?   A . n 
A 1 413 SER 413 350  ?    ?   ?   A . n 
A 1 414 LYS 414 351  ?    ?   ?   A . n 
A 1 415 VAL 415 352  ?    ?   ?   A . n 
A 1 416 PRO 416 353  ?    ?   ?   A . n 
A 1 417 PHE 417 354  ?    ?   ?   A . n 
A 1 418 ARG 418 355  ?    ?   ?   A . n 
A 1 419 SER 419 356  ?    ?   ?   A . n 
A 1 420 ARG 420 357  ?    ?   ?   A . n 
A 1 421 SER 421 358  ?    ?   ?   A . n 
A 1 422 PRO 422 359  ?    ?   ?   A . n 
A 1 423 SER 423 360  ?    ?   ?   A . n 
A 1 424 GLU 424 361  ?    ?   ?   A . n 
A 1 425 VAL 425 362  ?    ?   ?   A . n 
A 1 426 GLU 426 363  ?    ?   ?   A . n 
A 1 427 PHE 427 364  ?    ?   ?   A . n 
A 1 428 HIS 428 365  ?    ?   ?   A . n 
A 1 429 HIS 429 366  ?    ?   ?   A . n 
A 1 430 HIS 430 367  ?    ?   ?   A . n 
A 1 431 HIS 431 368  ?    ?   ?   A . n 
A 1 432 HIS 432 369  ?    ?   ?   A . n 
A 1 433 HIS 433 370  ?    ?   ?   A . n 
A 1 434 HIS 434 371  ?    ?   ?   A . n 
A 1 435 HIS 435 372  ?    ?   ?   A . n 
A 1 436 HIS 436 373  ?    ?   ?   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 OLA ? ? OLA ? ? 'SUBJECT OF INVESTIGATION' ? 
2 OLC ? ? OLC ? ? 'SUBJECT OF INVESTIGATION' ? 
3 P15 ? ? P15 ? ? '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 OLC 1  1201 501  OLC OLC A . 
C 2 OLC 1  1202 1901 OLC OLC A . 
D 3 P15 1  1203 2001 P15 P15 A . 
E 4 OLA 1  1204 2101 OLA OLA A . 
F 3 P15 1  1205 2301 P15 P15 A . 
G 4 OLA 1  1206 2401 OLA OLA A . 
H 4 OLA 1  1207 2501 OLA OLA A . 
I 4 OLA 1  1208 2801 OLA OLA A . 
J 4 OLA 1  1209 2901 OLA OLA A . 
K 4 OLA 1  1210 3001 OLA OLA A . 
L 2 OLC 1  1211 3002 OLC OLC A . 
M 2 OLC 1  1212 3003 OLC OLC A . 
N 4 OLA 1  1213 3004 OLA OLA A . 
O 2 OLC 1  1214 3005 OLC OLC A . 
P 4 OLA 1  1215 3006 OLA OLA A . 
Q 4 OLA 1  1216 3007 OLA OLA A . 
R 4 OLA 1  1217 3008 OLA OLA A . 
S 4 OLA 1  1218 2101 OLA OLA A . 
T 4 OLA 1  1219 2201 OLA OLA A . 
U 5 CLR 1  1220 2901 CLR CLR A . 
V 6 HOH 1  1301 95   HOH HOH A . 
V 6 HOH 2  1302 157  HOH HOH A . 
V 6 HOH 3  1303 123  HOH HOH A . 
V 6 HOH 4  1304 145  HOH HOH A . 
V 6 HOH 5  1305 147  HOH HOH A . 
V 6 HOH 6  1306 10   HOH HOH A . 
V 6 HOH 7  1307 109  HOH HOH A . 
V 6 HOH 8  1308 132  HOH HOH A . 
V 6 HOH 9  1309 2    HOH HOH A . 
V 6 HOH 10 1310 156  HOH HOH A . 
V 6 HOH 11 1311 154  HOH HOH A . 
V 6 HOH 12 1312 1    HOH HOH A . 
V 6 HOH 13 1313 22   HOH HOH A . 
V 6 HOH 14 1314 153  HOH HOH A . 
V 6 HOH 15 1315 12   HOH HOH A . 
V 6 HOH 16 1316 138  HOH HOH A . 
V 6 HOH 17 1317 124  HOH HOH A . 
V 6 HOH 18 1318 7    HOH HOH A . 
V 6 HOH 19 1319 9    HOH HOH A . 
V 6 HOH 20 1320 122  HOH HOH A . 
V 6 HOH 21 1321 135  HOH HOH A . 
V 6 HOH 22 1322 3    HOH HOH A . 
V 6 HOH 23 1323 6    HOH HOH A . 
V 6 HOH 24 1324 143  HOH HOH A . 
V 6 HOH 25 1325 119  HOH HOH A . 
V 6 HOH 26 1326 151  HOH HOH A . 
V 6 HOH 27 1327 96   HOH HOH A . 
V 6 HOH 28 1328 158  HOH HOH A . 
V 6 HOH 29 1329 137  HOH HOH A . 
V 6 HOH 30 1330 58   HOH HOH A . 
V 6 HOH 31 1331 75   HOH HOH A . 
V 6 HOH 32 1332 148  HOH HOH A . 
V 6 HOH 33 1333 146  HOH HOH A . 
V 6 HOH 34 1334 163  HOH HOH A . 
V 6 HOH 35 1335 11   HOH HOH A . 
V 6 HOH 36 1336 121  HOH HOH A . 
V 6 HOH 37 1337 128  HOH HOH A . 
V 6 HOH 38 1338 82   HOH HOH A . 
V 6 HOH 39 1339 65   HOH HOH A . 
V 6 HOH 40 1340 160  HOH HOH A . 
V 6 HOH 41 1341 130  HOH HOH A . 
V 6 HOH 42 1342 159  HOH HOH A . 
V 6 HOH 43 1343 149  HOH HOH A . 
V 6 HOH 44 1344 94   HOH HOH A . 
V 6 HOH 45 1345 161  HOH HOH A . 
V 6 HOH 46 1346 144  HOH HOH A . 
V 6 HOH 47 1347 140  HOH HOH A . 
V 6 HOH 48 1348 120  HOH HOH A . 
V 6 HOH 49 1349 29   HOH HOH A . 
V 6 HOH 50 1350 4    HOH HOH A . 
V 6 HOH 51 1351 136  HOH HOH A . 
V 6 HOH 52 1352 127  HOH HOH A . 
V 6 HOH 53 1353 74   HOH HOH A . 
V 6 HOH 54 1354 19   HOH HOH A . 
V 6 HOH 55 1355 150  HOH HOH A . 
V 6 HOH 56 1356 101  HOH HOH A . 
V 6 HOH 57 1357 125  HOH HOH A . 
V 6 HOH 58 1358 116  HOH HOH A . 
V 6 HOH 59 1359 142  HOH HOH A . 
V 6 HOH 60 1360 48   HOH HOH A . 
V 6 HOH 61 1361 111  HOH HOH A . 
V 6 HOH 62 1362 83   HOH HOH A . 
V 6 HOH 63 1363 162  HOH HOH A . 
V 6 HOH 64 1364 152  HOH HOH A . 
V 6 HOH 65 1365 133  HOH HOH A . 
V 6 HOH 66 1366 105  HOH HOH A . 
V 6 HOH 67 1367 98   HOH HOH A . 
V 6 HOH 68 1368 118  HOH HOH A . 
V 6 HOH 69 1369 80   HOH HOH A . 
V 6 HOH 70 1370 41   HOH HOH A . 
V 6 HOH 71 1371 155  HOH HOH A . 
V 6 HOH 72 1372 141  HOH HOH A . 
V 6 HOH 73 1373 117  HOH HOH A . 
V 6 HOH 74 1374 139  HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 1042 ? CG  ? A LYS 267 CG  
2  1 Y 1 A LYS 1042 ? CD  ? A LYS 267 CD  
3  1 Y 1 A LYS 1042 ? CE  ? A LYS 267 CE  
4  1 Y 1 A LYS 1042 ? NZ  ? A LYS 267 NZ  
5  1 Y 1 A LYS 1047 ? CG  ? A LYS 272 CG  
6  1 Y 1 A LYS 1047 ? CD  ? A LYS 272 CD  
7  1 Y 1 A LYS 1047 ? CE  ? A LYS 272 CE  
8  1 Y 1 A LYS 1047 ? NZ  ? A LYS 272 NZ  
9  1 Y 1 A LEU 1048 ? CG  ? A LEU 273 CG  
10 1 Y 1 A LEU 1048 ? CD1 ? A LEU 273 CD1 
11 1 Y 1 A LEU 1048 ? CD2 ? A LEU 273 CD2 
12 1 Y 1 A GLU 1049 ? CG  ? A GLU 274 CG  
13 1 Y 1 A GLU 1049 ? CD  ? A GLU 274 CD  
14 1 Y 1 A GLU 1049 ? OE1 ? A GLU 274 OE1 
15 1 Y 1 A GLU 1049 ? OE2 ? A GLU 274 OE2 
16 1 Y 1 A ARG 279  ? NE  ? A ARG 342 NE  
17 1 Y 1 A ARG 279  ? CZ  ? A ARG 342 CZ  
18 1 Y 1 A ARG 279  ? NH1 ? A ARG 342 NH1 
19 1 Y 1 A ARG 279  ? NH2 ? A ARG 342 NH2 
20 1 N 1 A OLC 1201 ? C18 ? B OLC 1   C18 
21 1 N 1 A OLC 1201 ? C10 ? B OLC 1   C10 
22 1 N 1 A OLC 1201 ? C17 ? B OLC 1   C17 
23 1 N 1 A OLC 1201 ? C11 ? B OLC 1   C11 
24 1 N 1 A OLC 1201 ? C16 ? B OLC 1   C16 
25 1 N 1 A OLC 1201 ? C12 ? B OLC 1   C12 
26 1 N 1 A OLC 1201 ? C15 ? B OLC 1   C15 
27 1 N 1 A OLC 1201 ? C13 ? B OLC 1   C13 
28 1 N 1 A OLC 1201 ? C14 ? B OLC 1   C14 
29 1 N 1 A P15 1205 ? C13 ? F P15 1   C13 
30 1 N 1 A P15 1205 ? O6  ? F P15 1   O6  
31 1 N 1 A P15 1205 ? C12 ? F P15 1   C12 
32 1 N 1 A P15 1205 ? C11 ? F P15 1   C11 
33 1 N 1 A P15 1205 ? O5  ? F P15 1   O5  
34 1 N 1 A P15 1205 ? C10 ? F P15 1   C10 
35 1 N 1 A OLA 1213 ? C1  ? N OLA 1   C1  
36 1 N 1 A OLA 1213 ? O1  ? N OLA 1   O1  
37 1 N 1 A OLA 1213 ? O2  ? N OLA 1   O2  
38 1 N 1 A OLA 1213 ? C2  ? N OLA 1   C2  
39 1 N 1 A OLA 1213 ? C3  ? N OLA 1   C3  
40 1 N 1 A OLA 1213 ? C4  ? N OLA 1   C4  
41 1 N 1 A OLA 1213 ? C5  ? N OLA 1   C5  
42 1 N 1 A OLA 1215 ? C13 ? P OLA 1   C13 
43 1 N 1 A OLA 1215 ? C14 ? P OLA 1   C14 
44 1 N 1 A OLA 1215 ? C15 ? P OLA 1   C15 
45 1 N 1 A OLA 1215 ? C16 ? P OLA 1   C16 
46 1 N 1 A OLA 1215 ? C17 ? P OLA 1   C17 
47 1 N 1 A OLA 1215 ? C18 ? P OLA 1   C18 
48 1 N 1 A OLA 1216 ? C1  ? Q OLA 1   C1  
49 1 N 1 A OLA 1216 ? O1  ? Q OLA 1   O1  
50 1 N 1 A OLA 1216 ? O2  ? Q OLA 1   O2  
51 1 N 1 A OLA 1216 ? C2  ? Q OLA 1   C2  
52 1 N 1 A OLA 1216 ? C3  ? Q OLA 1   C3  
53 1 N 1 A OLA 1216 ? C4  ? Q OLA 1   C4  
54 1 N 1 A OLA 1216 ? C5  ? Q OLA 1   C5  
55 1 N 1 A OLA 1216 ? C6  ? Q OLA 1   C6  
56 1 N 1 A OLA 1216 ? C7  ? Q OLA 1   C7  
57 1 N 1 A OLA 1216 ? C8  ? Q OLA 1   C8  
58 1 N 1 A OLA 1216 ? C9  ? Q OLA 1   C9  
59 1 N 1 A OLA 1219 ? C12 ? T OLA 1   C12 
60 1 N 1 A OLA 1219 ? C13 ? T OLA 1   C13 
61 1 N 1 A OLA 1219 ? C14 ? T OLA 1   C14 
62 1 N 1 A OLA 1219 ? C15 ? T OLA 1   C15 
63 1 N 1 A OLA 1219 ? C16 ? T OLA 1   C16 
64 1 N 1 A OLA 1219 ? C17 ? T OLA 1   C17 
65 1 N 1 A OLA 1219 ? C18 ? T OLA 1   C18 
# 
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   ? ? ? '(1.20.1_4487: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .                    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                     8TF5 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     57.033 
_cell.length_a_esd                 ? 
_cell.length_b                     96.867 
_cell.length_b_esd                 ? 
_cell.length_c                     97.563 
_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                         8TF5 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8TF5 
_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             2.83 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          56.49 
_exptl_crystal.description                  'orthorhombic crystals' 
_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          'LIPIDIC CUBIC PHASE' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    'NaCH3COO, PEG 400, NaCl, PPG P40' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     123 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2020-02-27 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0332 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'APS BEAMLINE 23-ID-B' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0332 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   23-ID-B 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8TF5 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.1 
_reflns.d_resolution_low                               30.0 
_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                                     31292 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           96.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.2 
_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                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.930 
_reflns.pdbx_CC_star                                   0.982 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.191 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.1 
_reflns_shell.d_res_low                                     2.18 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.2 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2492 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.677 
_reflns_shell.pdbx_CC_star                                  0.898 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.638 
_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                                 8TF5 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.10 
_refine.ls_d_res_low                             29.44 
_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                     30995 
_refine.ls_number_reflns_R_free                  1677 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    96.03 
_refine.ls_percent_reflns_R_free                 5.41 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1861 
_refine.ls_R_factor_R_free                       0.2141 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1845 
_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                          1.35 
_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                 21.44 
_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                            0.22 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.10 
_refine_hist.d_res_low                        29.44 
_refine_hist.number_atoms_solvent             74 
_refine_hist.number_atoms_total               3238 
_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        2777 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         387 
_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' ? 0.003  ? 3294 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.695  ? 4398 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 13.722 ? 1321 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.038  ? 504  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.004  ? 527  ? 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' 2.10 2.16  . . 101 1886 75.00  . . . . 0.2898 . . . . . . . . . . . 0.2802 
'X-RAY DIFFRACTION' 2.16 2.23  . . 105 2220 88.00  . . . . 0.2577 . . . . . . . . . . . 0.2544 
'X-RAY DIFFRACTION' 2.23 2.31  . . 128 2416 95.00  . . . . 0.2293 . . . . . . . . . . . 0.2465 
'X-RAY DIFFRACTION' 2.31 2.40  . . 138 2463 98.00  . . . . 0.2107 . . . . . . . . . . . 0.2865 
'X-RAY DIFFRACTION' 2.40 2.51  . . 158 2454 99.00  . . . . 0.2000 . . . . . . . . . . . 0.2493 
'X-RAY DIFFRACTION' 2.51 2.65  . . 143 2485 99.00  . . . . 0.1782 . . . . . . . . . . . 0.2183 
'X-RAY DIFFRACTION' 2.65 2.81  . . 168 2503 100.00 . . . . 0.1638 . . . . . . . . . . . 0.1706 
'X-RAY DIFFRACTION' 2.81 3.03  . . 152 2519 100.00 . . . . 0.1701 . . . . . . . . . . . 0.1871 
'X-RAY DIFFRACTION' 3.03 3.33  . . 132 2541 99.00  . . . . 0.1864 . . . . . . . . . . . 0.2485 
'X-RAY DIFFRACTION' 3.33 3.81  . . 150 2558 100.00 . . . . 0.1732 . . . . . . . . . . . 0.2310 
'X-RAY DIFFRACTION' 3.81 4.80  . . 145 2586 100.00 . . . . 0.1587 . . . . . . . . . . . 0.1772 
'X-RAY DIFFRACTION' 4.80 29.44 . . 157 2687 99.00  . . . . 0.1961 . . . . . . . . . . . 0.2176 
# 
_struct.entry_id                     8TF5 
_struct.title                        'Crystal structure of orphan G protein-coupled receptor 6, pseudoapo form' 
_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        8TF5 
_struct_keywords.text            
;Orphan GPCR, GPR6, pseudoapo form, BRIL, LCP, membrane protein, Parkinson's disease, active-like conformation
;
_struct_keywords.pdbx_keywords   'MEMBRANE PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 3 ? 
G N N 4 ? 
H N N 4 ? 
I N N 4 ? 
J N N 4 ? 
K N N 4 ? 
L N N 2 ? 
M N N 2 ? 
N N N 4 ? 
O N N 2 ? 
P N N 4 ? 
Q N N 4 ? 
R N N 4 ? 
S N N 4 ? 
T N N 4 ? 
U N N 5 ? 
V N N 6 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP GPR6_HUMAN P46095 ? 1 
;GGANGSLELSSQLSAGPPGLLLPAVNPWDVLLCVSGTVIAGENALVVALIASTPALRTPMFVLVGSLATADLLAGCGLIL
HFVFQYLVPSETVSLLTVGFLVASFAASVSSLLAITVDRYLSLYNALTYYSRRTLLGVHLLLAATWTVSLGLGLLPVLGW
NCLAERAACSVVRPLARSHVALLSAAFFMVFGIMLHLYVRICQVVWRHA
;
48  
2 UNP C562_ECOLX P0ABE7 ? 1 
;ADLEDNMETLNDNLKVIEKADNAAQVKDALTKMRAAALDAQKATPPKLEDKSPDSPEMKDFRHGFDILVGQIDDALKLAN
EGKVKEAQAAAEQLKTTRNAYHQKYR
;
23  
3 UNP GPR6_HUMAN P46095 ? 1 
;HLAATRKGVGTLAVVLGTFGASWLPFAIYCVVGSHEDPAVYTYATLLPATYNSMINPIIYAFRNQEIQRALWLLLCGCFQ
SKVPFRSRSPSEV
;
270 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8TF5 A 17  ? 225 ? P46095 48  ? 256 ? 48   256  
2 2 8TF5 A 226 ? 331 ? P0ABE7 23  ? 128 ? 1001 1106 
3 3 8TF5 A 333 ? 425 ? P46095 270 ? 362 ? 270  362  
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8TF5 MET A 1   ? UNP P46095 ?   ?   'initiating methionine' 32   1  
1 8TF5 LYS A 2   ? UNP P46095 ?   ?   'expression tag'        33   2  
1 8TF5 THR A 3   ? UNP P46095 ?   ?   'expression tag'        34   3  
1 8TF5 ILE A 4   ? UNP P46095 ?   ?   'expression tag'        35   4  
1 8TF5 ILE A 5   ? UNP P46095 ?   ?   'expression tag'        36   5  
1 8TF5 ALA A 6   ? UNP P46095 ?   ?   'expression tag'        37   6  
1 8TF5 LEU A 7   ? UNP P46095 ?   ?   'expression tag'        38   7  
1 8TF5 SER A 8   ? UNP P46095 ?   ?   'expression tag'        39   8  
1 8TF5 TYR A 9   ? UNP P46095 ?   ?   'expression tag'        40   9  
1 8TF5 ILE A 10  ? UNP P46095 ?   ?   'expression tag'        41   10 
1 8TF5 PHE A 11  ? UNP P46095 ?   ?   'expression tag'        42   11 
1 8TF5 CYS A 12  ? UNP P46095 ?   ?   'expression tag'        43   12 
1 8TF5 LEU A 13  ? UNP P46095 ?   ?   'expression tag'        44   13 
1 8TF5 VAL A 14  ? UNP P46095 ?   ?   'expression tag'        45   14 
1 8TF5 PHE A 15  ? UNP P46095 ?   ?   'expression tag'        46   15 
1 8TF5 ALA A 16  ? UNP P46095 ?   ?   'expression tag'        47   16 
1 8TF5 LEU A 92  ? UNP P46095 CYS 123 'engineered mutation'   123  17 
1 8TF5 PRO A 142 ? UNP P46095 ALA 173 'engineered mutation'   173  18 
2 8TF5 TRP A 232 ? UNP P0ABE7 MET 29  'engineered mutation'   1007 19 
2 8TF5 ILE A 327 ? UNP P0ABE7 HIS 124 'engineered mutation'   1102 20 
2 8TF5 LEU A 331 ? UNP P0ABE7 ARG 128 'engineered mutation'   1106 21 
2 8TF5 ALA A 332 ? UNP P0ABE7 ?   ?   linker                  900  22 
3 8TF5 ARG A 342 ? UNP P46095 GLY 279 'engineered mutation'   279  23 
3 8TF5 CYS A 354 ? UNP P46095 SER 291 'engineered mutation'   291  24 
3 8TF5 LEU A 383 ? UNP P46095 TYR 320 'engineered mutation'   320  25 
3 8TF5 ASP A 408 ? UNP P46095 CYS 345 'engineered mutation'   345  26 
3 8TF5 GLU A 426 ? UNP P46095 ?   ?   'expression tag'        363  27 
3 8TF5 PHE A 427 ? UNP P46095 ?   ?   'expression tag'        364  28 
3 8TF5 HIS A 428 ? UNP P46095 ?   ?   'expression tag'        365  29 
3 8TF5 HIS A 429 ? UNP P46095 ?   ?   'expression tag'        366  30 
3 8TF5 HIS A 430 ? UNP P46095 ?   ?   'expression tag'        367  31 
3 8TF5 HIS A 431 ? UNP P46095 ?   ?   'expression tag'        368  32 
3 8TF5 HIS A 432 ? UNP P46095 ?   ?   'expression tag'        369  33 
3 8TF5 HIS A 433 ? UNP P46095 ?   ?   'expression tag'        370  34 
3 8TF5 HIS A 434 ? UNP P46095 ?   ?   'expression tag'        371  35 
3 8TF5 HIS A 435 ? UNP P46095 ?   ?   'expression tag'        372  36 
3 8TF5 HIS A 436 ? UNP P46095 ?   ?   'expression tag'        373  37 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V 
# 
_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 
# 
_struct_biol.id        1 
_struct_biol.details   'THE AUTHOR STATES THAT THE BIOLOGICAL UNIT OF THIS PROTEIN IS UNKNOWN.' 
# 
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 ASN A 42  ? SER A 68  ? ASN A 73   SER A 99   1 ? 27 
HELX_P HELX_P2  AA2 THR A 74  ? LEU A 103 ? THR A 105  LEU A 134  1 ? 30 
HELX_P HELX_P3  AA3 SER A 106 ? ASN A 141 ? SER A 137  ASN A 172  1 ? 36 
HELX_P HELX_P4  AA4 SER A 147 ? GLY A 175 ? SER A 178  GLY A 206  1 ? 29 
HELX_P HELX_P5  AA5 GLU A 181 ? CYS A 185 ? GLU A 212  CYS A 216  5 ? 5  
HELX_P HELX_P6  AA6 ALA A 192 ? ALA A 245 ? ALA A 223  ALA A 1020 1 ? 54 
HELX_P HELX_P7  AA7 ASN A 247 ? THR A 269 ? ASN A 1022 THR A 1044 1 ? 23 
HELX_P HELX_P8  AA8 ASP A 285 ? GLU A 306 ? ASP A 1060 GLU A 1081 1 ? 22 
HELX_P HELX_P9  AA9 LYS A 308 ? ALA A 315 ? LYS A 1083 ALA A 1090 1 ? 8  
HELX_P HELX_P10 AB1 ALA A 315 ? TYR A 326 ? ALA A 1090 TYR A 1101 1 ? 12 
HELX_P HELX_P11 AB2 TYR A 326 ? GLY A 365 ? TYR A 1101 GLY A 302  1 ? 40 
HELX_P HELX_P12 AB3 ALA A 371 ? ALA A 393 ? ALA A 308  ALA A 330  1 ? 23 
HELX_P HELX_P13 AB4 ASN A 396 ? ASP A 408 ? ASN A 333  ASP A 345  1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ?    ? A CYS 178 SG ? ? ? 1_555 A CYS 185 SG ? ? A CYS 209 A CYS 216 1_555 ? ? ? ? ? ? ? 2.049 ? ? 
covale1 covale both ? A ILE 217 C  ? ? ? 1_555 A YCM 218 N  ? ? A ILE 248 A YCM 249 1_555 ? ? ? ? ? ? ? 1.328 ? ? 
covale2 covale both ? A YCM 218 C  ? ? ? 1_555 A GLN 219 N  ? ? A YCM 249 A GLN 250 1_555 ? ? ? ? ? ? ? 1.331 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 YCM A 218 ? .   . .   . YCM A 249 ? 1_555 .   . .   . .     .  .  CYS 1 YCM Acetamidation 'Named protein modification' 
2 CYS A 178 ? CYS A 185 ? CYS A 209 ? 1_555 CYS A 216 ? 1_555 SG SG .   . .   None          'Disulfide bridge'           
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 ARG 189 A . ? ARG 220 A PRO 190 A ? PRO 221 A 1 -2.92 
2 ARG 189 A . ? ARG 220 A PRO 190 A ? PRO 221 A 1 -2.48 
# 
_pdbx_entry_details.entry_id                   8TF5 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 PRO A 221  ? ? -98.50  33.73   
2 1 LEU A 1048 ? ? 177.81  -172.66 
3 1 LYS A 1083 ? ? -101.22 66.17   
# 
_pdbx_struct_mod_residue.id               1 
_pdbx_struct_mod_residue.label_asym_id    A 
_pdbx_struct_mod_residue.label_comp_id    YCM 
_pdbx_struct_mod_residue.label_seq_id     218 
_pdbx_struct_mod_residue.auth_asym_id     A 
_pdbx_struct_mod_residue.auth_comp_id     YCM 
_pdbx_struct_mod_residue.auth_seq_id      249 
_pdbx_struct_mod_residue.PDB_ins_code     ? 
_pdbx_struct_mod_residue.parent_comp_id   CYS 
_pdbx_struct_mod_residue.details          'modified residue' 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.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[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
'X-RAY DIFFRACTION' 1 ? refined 29.455 17.968 46.658 0.2364 0.1863 0.2796 0.0081 0.0036  -0.0066 1.6428 1.3469 0.2843 0.1541  
0.0145 -0.2911 -0.0201 -0.0578 -0.0001 0.0035 -0.0209 -0.0447 0.0596  0.0446 -0.0194 
'X-RAY DIFFRACTION' 2 ? refined 14.175 16.846 21.635 0.5243 0.5137 0.4067 0.0190 -0.0332 -0.0319 0.5176 0.0373 0.6995 -0.0526 
0.0998 -0.4571 0.0143  -0.0211 0.0001  0.2998 -0.0498 0.0610  -0.1949 0.2014 -0.2202 
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.selection_details 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
'X-RAY DIFFRACTION' 1 1 A 70  A 223 '( CHAIN A AND RESID 70:223 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 2 2 A 224 A 347 
;( chain 'A' and (resid 224 through 256 or resid 1001 through 1106 or resid 900 or resid 270 through 347 ))
;
? ? ? ? ? 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 32   ? A MET 1   
2  1 Y 1 A LYS 33   ? A LYS 2   
3  1 Y 1 A THR 34   ? A THR 3   
4  1 Y 1 A ILE 35   ? A ILE 4   
5  1 Y 1 A ILE 36   ? A ILE 5   
6  1 Y 1 A ALA 37   ? A ALA 6   
7  1 Y 1 A LEU 38   ? A LEU 7   
8  1 Y 1 A SER 39   ? A SER 8   
9  1 Y 1 A TYR 40   ? A TYR 9   
10 1 Y 1 A ILE 41   ? A ILE 10  
11 1 Y 1 A PHE 42   ? A PHE 11  
12 1 Y 1 A CYS 43   ? A CYS 12  
13 1 Y 1 A LEU 44   ? A LEU 13  
14 1 Y 1 A VAL 45   ? A VAL 14  
15 1 Y 1 A PHE 46   ? A PHE 15  
16 1 Y 1 A ALA 47   ? A ALA 16  
17 1 Y 1 A GLY 48   ? A GLY 17  
18 1 Y 1 A GLY 49   ? A GLY 18  
19 1 Y 1 A ALA 50   ? A ALA 19  
20 1 Y 1 A ASN 51   ? A ASN 20  
21 1 Y 1 A GLY 52   ? A GLY 21  
22 1 Y 1 A SER 53   ? A SER 22  
23 1 Y 1 A LEU 54   ? A LEU 23  
24 1 Y 1 A GLU 55   ? A GLU 24  
25 1 Y 1 A LEU 56   ? A LEU 25  
26 1 Y 1 A SER 57   ? A SER 26  
27 1 Y 1 A SER 58   ? A SER 27  
28 1 Y 1 A GLN 59   ? A GLN 28  
29 1 Y 1 A LEU 60   ? A LEU 29  
30 1 Y 1 A SER 61   ? A SER 30  
31 1 Y 1 A ALA 62   ? A ALA 31  
32 1 Y 1 A GLY 63   ? A GLY 32  
33 1 Y 1 A PRO 64   ? A PRO 33  
34 1 Y 1 A PRO 65   ? A PRO 34  
35 1 Y 1 A GLY 66   ? A GLY 35  
36 1 Y 1 A LEU 67   ? A LEU 36  
37 1 Y 1 A LEU 68   ? A LEU 37  
38 1 Y 1 A LEU 69   ? A LEU 38  
39 1 Y 1 A ASP 1050 ? A ASP 275 
40 1 Y 1 A LYS 1051 ? A LYS 276 
41 1 Y 1 A SER 1052 ? A SER 277 
42 1 Y 1 A PRO 1053 ? A PRO 278 
43 1 Y 1 A ASP 1054 ? A ASP 279 
44 1 Y 1 A SER 1055 ? A SER 280 
45 1 Y 1 A PRO 1056 ? A PRO 281 
46 1 Y 1 A GLU 1057 ? A GLU 282 
47 1 Y 1 A PHE 348  ? A PHE 411 
48 1 Y 1 A GLN 349  ? A GLN 412 
49 1 Y 1 A SER 350  ? A SER 413 
50 1 Y 1 A LYS 351  ? A LYS 414 
51 1 Y 1 A VAL 352  ? A VAL 415 
52 1 Y 1 A PRO 353  ? A PRO 416 
53 1 Y 1 A PHE 354  ? A PHE 417 
54 1 Y 1 A ARG 355  ? A ARG 418 
55 1 Y 1 A SER 356  ? A SER 419 
56 1 Y 1 A ARG 357  ? A ARG 420 
57 1 Y 1 A SER 358  ? A SER 421 
58 1 Y 1 A PRO 359  ? A PRO 422 
59 1 Y 1 A SER 360  ? A SER 423 
60 1 Y 1 A GLU 361  ? A GLU 424 
61 1 Y 1 A VAL 362  ? A VAL 425 
62 1 Y 1 A GLU 363  ? A GLU 426 
63 1 Y 1 A PHE 364  ? A PHE 427 
64 1 Y 1 A HIS 365  ? A HIS 428 
65 1 Y 1 A HIS 366  ? A HIS 429 
66 1 Y 1 A HIS 367  ? A HIS 430 
67 1 Y 1 A HIS 368  ? A HIS 431 
68 1 Y 1 A HIS 369  ? A HIS 432 
69 1 Y 1 A HIS 370  ? A HIS 433 
70 1 Y 1 A HIS 371  ? A HIS 434 
71 1 Y 1 A HIS 372  ? A HIS 435 
72 1 Y 1 A HIS 373  ? A HIS 436 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CLR C1   C N N 74  
CLR C2   C N N 75  
CLR C3   C N S 76  
CLR C4   C N N 77  
CLR C5   C N N 78  
CLR C6   C N N 79  
CLR C7   C N N 80  
CLR C8   C N S 81  
CLR C9   C N S 82  
CLR C10  C N R 83  
CLR C11  C N N 84  
CLR C12  C N N 85  
CLR C13  C N R 86  
CLR C14  C N S 87  
CLR C15  C N N 88  
CLR C16  C N N 89  
CLR C17  C N R 90  
CLR C18  C N N 91  
CLR C19  C N N 92  
CLR C20  C N R 93  
CLR C21  C N N 94  
CLR C22  C N N 95  
CLR C23  C N N 96  
CLR C24  C N N 97  
CLR C25  C N N 98  
CLR C26  C N N 99  
CLR C27  C N N 100 
CLR O1   O N N 101 
CLR H11  H N N 102 
CLR H12  H N N 103 
CLR H21  H N N 104 
CLR H22  H N N 105 
CLR H3   H N N 106 
CLR H41  H N N 107 
CLR H42  H N N 108 
CLR H6   H N N 109 
CLR H71  H N N 110 
CLR H72  H N N 111 
CLR H8   H N N 112 
CLR H9   H N N 113 
CLR H111 H N N 114 
CLR H112 H N N 115 
CLR H121 H N N 116 
CLR H122 H N N 117 
CLR H14  H N N 118 
CLR H151 H N N 119 
CLR H152 H N N 120 
CLR H161 H N N 121 
CLR H162 H N N 122 
CLR H17  H N N 123 
CLR H181 H N N 124 
CLR H182 H N N 125 
CLR H183 H N N 126 
CLR H191 H N N 127 
CLR H192 H N N 128 
CLR H193 H N N 129 
CLR H20  H N N 130 
CLR H211 H N N 131 
CLR H212 H N N 132 
CLR H213 H N N 133 
CLR H221 H N N 134 
CLR H222 H N N 135 
CLR H231 H N N 136 
CLR H232 H N N 137 
CLR H241 H N N 138 
CLR H242 H N N 139 
CLR H25  H N N 140 
CLR H261 H N N 141 
CLR H262 H N N 142 
CLR H263 H N N 143 
CLR H271 H N N 144 
CLR H272 H N N 145 
CLR H273 H N N 146 
CLR H1   H N N 147 
CYS N    N N N 148 
CYS CA   C N R 149 
CYS C    C N N 150 
CYS O    O N N 151 
CYS CB   C N N 152 
CYS SG   S N N 153 
CYS OXT  O N N 154 
CYS H    H N N 155 
CYS H2   H N N 156 
CYS HA   H N N 157 
CYS HB2  H N N 158 
CYS HB3  H N N 159 
CYS HG   H N N 160 
CYS HXT  H N N 161 
GLN N    N N N 162 
GLN CA   C N S 163 
GLN C    C N N 164 
GLN O    O N N 165 
GLN CB   C N N 166 
GLN CG   C N N 167 
GLN CD   C N N 168 
GLN OE1  O N N 169 
GLN NE2  N N N 170 
GLN OXT  O N N 171 
GLN H    H N N 172 
GLN H2   H N N 173 
GLN HA   H N N 174 
GLN HB2  H N N 175 
GLN HB3  H N N 176 
GLN HG2  H N N 177 
GLN HG3  H N N 178 
GLN HE21 H N N 179 
GLN HE22 H N N 180 
GLN HXT  H N N 181 
GLU N    N N N 182 
GLU CA   C N S 183 
GLU C    C N N 184 
GLU O    O N N 185 
GLU CB   C N N 186 
GLU CG   C N N 187 
GLU CD   C N N 188 
GLU OE1  O N N 189 
GLU OE2  O N N 190 
GLU OXT  O N N 191 
GLU H    H N N 192 
GLU H2   H N N 193 
GLU HA   H N N 194 
GLU HB2  H N N 195 
GLU HB3  H N N 196 
GLU HG2  H N N 197 
GLU HG3  H N N 198 
GLU HE2  H N N 199 
GLU HXT  H N N 200 
GLY N    N N N 201 
GLY CA   C N N 202 
GLY C    C N N 203 
GLY O    O N N 204 
GLY OXT  O N N 205 
GLY H    H N N 206 
GLY H2   H N N 207 
GLY HA2  H N N 208 
GLY HA3  H N N 209 
GLY HXT  H N N 210 
HIS N    N N N 211 
HIS CA   C N S 212 
HIS C    C N N 213 
HIS O    O N N 214 
HIS CB   C N N 215 
HIS CG   C Y N 216 
HIS ND1  N Y N 217 
HIS CD2  C Y N 218 
HIS CE1  C Y N 219 
HIS NE2  N Y N 220 
HIS OXT  O N N 221 
HIS H    H N N 222 
HIS H2   H N N 223 
HIS HA   H N N 224 
HIS HB2  H N N 225 
HIS HB3  H N N 226 
HIS HD1  H N N 227 
HIS HD2  H N N 228 
HIS HE1  H N N 229 
HIS HE2  H N N 230 
HIS HXT  H N N 231 
HOH O    O N N 232 
HOH H1   H N N 233 
HOH H2   H N N 234 
ILE N    N N N 235 
ILE CA   C N S 236 
ILE C    C N N 237 
ILE O    O N N 238 
ILE CB   C N S 239 
ILE CG1  C N N 240 
ILE CG2  C N N 241 
ILE CD1  C N N 242 
ILE OXT  O N N 243 
ILE H    H N N 244 
ILE H2   H N N 245 
ILE HA   H N N 246 
ILE HB   H N N 247 
ILE HG12 H N N 248 
ILE HG13 H N N 249 
ILE HG21 H N N 250 
ILE HG22 H N N 251 
ILE HG23 H N N 252 
ILE HD11 H N N 253 
ILE HD12 H N N 254 
ILE HD13 H N N 255 
ILE HXT  H N N 256 
LEU N    N N N 257 
LEU CA   C N S 258 
LEU C    C N N 259 
LEU O    O N N 260 
LEU CB   C N N 261 
LEU CG   C N N 262 
LEU CD1  C N N 263 
LEU CD2  C N N 264 
LEU OXT  O N N 265 
LEU H    H N N 266 
LEU H2   H N N 267 
LEU HA   H N N 268 
LEU HB2  H N N 269 
LEU HB3  H N N 270 
LEU HG   H N N 271 
LEU HD11 H N N 272 
LEU HD12 H N N 273 
LEU HD13 H N N 274 
LEU HD21 H N N 275 
LEU HD22 H N N 276 
LEU HD23 H N N 277 
LEU HXT  H N N 278 
LYS N    N N N 279 
LYS CA   C N S 280 
LYS C    C N N 281 
LYS O    O N N 282 
LYS CB   C N N 283 
LYS CG   C N N 284 
LYS CD   C N N 285 
LYS CE   C N N 286 
LYS NZ   N N N 287 
LYS OXT  O N N 288 
LYS H    H N N 289 
LYS H2   H N N 290 
LYS HA   H N N 291 
LYS HB2  H N N 292 
LYS HB3  H N N 293 
LYS HG2  H N N 294 
LYS HG3  H N N 295 
LYS HD2  H N N 296 
LYS HD3  H N N 297 
LYS HE2  H N N 298 
LYS HE3  H N N 299 
LYS HZ1  H N N 300 
LYS HZ2  H N N 301 
LYS HZ3  H N N 302 
LYS HXT  H N N 303 
MET N    N N N 304 
MET CA   C N S 305 
MET C    C N N 306 
MET O    O N N 307 
MET CB   C N N 308 
MET CG   C N N 309 
MET SD   S N N 310 
MET CE   C N N 311 
MET OXT  O N N 312 
MET H    H N N 313 
MET H2   H N N 314 
MET HA   H N N 315 
MET HB2  H N N 316 
MET HB3  H N N 317 
MET HG2  H N N 318 
MET HG3  H N N 319 
MET HE1  H N N 320 
MET HE2  H N N 321 
MET HE3  H N N 322 
MET HXT  H N N 323 
OLA C1   C N N 324 
OLA O1   O N N 325 
OLA O2   O N N 326 
OLA C2   C N N 327 
OLA C3   C N N 328 
OLA C4   C N N 329 
OLA C5   C N N 330 
OLA C6   C N N 331 
OLA C7   C N N 332 
OLA C8   C N N 333 
OLA C9   C N N 334 
OLA C10  C N N 335 
OLA C11  C N N 336 
OLA C12  C N N 337 
OLA C13  C N N 338 
OLA C14  C N N 339 
OLA C15  C N N 340 
OLA C16  C N N 341 
OLA C17  C N N 342 
OLA C18  C N N 343 
OLA HO2  H N N 344 
OLA H21  H N N 345 
OLA H22  H N N 346 
OLA H31  H N N 347 
OLA H32  H N N 348 
OLA H41  H N N 349 
OLA H42  H N N 350 
OLA H51  H N N 351 
OLA H52  H N N 352 
OLA H61  H N N 353 
OLA H62  H N N 354 
OLA H71  H N N 355 
OLA H72  H N N 356 
OLA H81  H N N 357 
OLA H82  H N N 358 
OLA H9   H N N 359 
OLA H10  H N N 360 
OLA H111 H N N 361 
OLA H112 H N N 362 
OLA H121 H N N 363 
OLA H122 H N N 364 
OLA H131 H N N 365 
OLA H132 H N N 366 
OLA H141 H N N 367 
OLA H142 H N N 368 
OLA H151 H N N 369 
OLA H152 H N N 370 
OLA H161 H N N 371 
OLA H162 H N N 372 
OLA H171 H N N 373 
OLA H172 H N N 374 
OLA H181 H N N 375 
OLA H182 H N N 376 
OLA H183 H N N 377 
OLC C18  C N N 378 
OLC C10  C N N 379 
OLC C9   C N N 380 
OLC C17  C N N 381 
OLC C11  C N N 382 
OLC C8   C N N 383 
OLC C24  C N N 384 
OLC C16  C N N 385 
OLC C12  C N N 386 
OLC C7   C N N 387 
OLC C15  C N N 388 
OLC C13  C N N 389 
OLC C6   C N N 390 
OLC C14  C N N 391 
OLC C5   C N N 392 
OLC C4   C N N 393 
OLC C3   C N N 394 
OLC C2   C N N 395 
OLC C21  C N N 396 
OLC C1   C N N 397 
OLC C22  C N R 398 
OLC O19  O N N 399 
OLC O25  O N N 400 
OLC O23  O N N 401 
OLC O20  O N N 402 
OLC H18  H N N 403 
OLC H18A H N N 404 
OLC H18B H N N 405 
OLC H10  H N N 406 
OLC H9   H N N 407 
OLC H17  H N N 408 
OLC H17A H N N 409 
OLC H11  H N N 410 
OLC H11A H N N 411 
OLC H8   H N N 412 
OLC H8A  H N N 413 
OLC H24  H N N 414 
OLC H24A H N N 415 
OLC H16  H N N 416 
OLC H16A H N N 417 
OLC H12  H N N 418 
OLC H12A H N N 419 
OLC H7   H N N 420 
OLC H7A  H N N 421 
OLC H15  H N N 422 
OLC H15A H N N 423 
OLC H13  H N N 424 
OLC H13A H N N 425 
OLC H6   H N N 426 
OLC H6A  H N N 427 
OLC H14  H N N 428 
OLC H14A H N N 429 
OLC H5   H N N 430 
OLC H5A  H N N 431 
OLC H4   H N N 432 
OLC H4A  H N N 433 
OLC H3   H N N 434 
OLC H3A  H N N 435 
OLC H2   H N N 436 
OLC H2A  H N N 437 
OLC H21  H N N 438 
OLC H21A H N N 439 
OLC H22  H N N 440 
OLC HO25 H N N 441 
OLC HO23 H N N 442 
P15 C13  C N N 443 
P15 O6   O N N 444 
P15 C12  C N N 445 
P15 C11  C N N 446 
P15 O5   O N N 447 
P15 C10  C N N 448 
P15 C9   C N N 449 
P15 O4   O N N 450 
P15 C8   C N N 451 
P15 C7   C N N 452 
P15 O3   O N N 453 
P15 C6   C N N 454 
P15 C5   C N N 455 
P15 O2   O N N 456 
P15 C4   C N N 457 
P15 C3   C N N 458 
P15 O1   O N N 459 
P15 C2   C N N 460 
P15 C1   C N N 461 
P15 OXT  O N N 462 
P15 H131 H N N 463 
P15 H132 H N N 464 
P15 H133 H N N 465 
P15 H121 H N N 466 
P15 H122 H N N 467 
P15 H111 H N N 468 
P15 H112 H N N 469 
P15 H101 H N N 470 
P15 H102 H N N 471 
P15 H91  H N N 472 
P15 H92  H N N 473 
P15 H81  H N N 474 
P15 H82  H N N 475 
P15 H71  H N N 476 
P15 H72  H N N 477 
P15 H61  H N N 478 
P15 H62  H N N 479 
P15 H51  H N N 480 
P15 H52  H N N 481 
P15 H41  H N N 482 
P15 H42  H N N 483 
P15 H31  H N N 484 
P15 H32  H N N 485 
P15 H21  H N N 486 
P15 H22  H N N 487 
P15 H11  H N N 488 
P15 H12  H N N 489 
P15 HOXT H N N 490 
PHE N    N N N 491 
PHE CA   C N S 492 
PHE C    C N N 493 
PHE O    O N N 494 
PHE CB   C N N 495 
PHE CG   C Y N 496 
PHE CD1  C Y N 497 
PHE CD2  C Y N 498 
PHE CE1  C Y N 499 
PHE CE2  C Y N 500 
PHE CZ   C Y N 501 
PHE OXT  O N N 502 
PHE H    H N N 503 
PHE H2   H N N 504 
PHE HA   H N N 505 
PHE HB2  H N N 506 
PHE HB3  H N N 507 
PHE HD1  H N N 508 
PHE HD2  H N N 509 
PHE HE1  H N N 510 
PHE HE2  H N N 511 
PHE HZ   H N N 512 
PHE HXT  H N N 513 
PRO N    N N N 514 
PRO CA   C N S 515 
PRO C    C N N 516 
PRO O    O N N 517 
PRO CB   C N N 518 
PRO CG   C N N 519 
PRO CD   C N N 520 
PRO OXT  O N N 521 
PRO H    H N N 522 
PRO HA   H N N 523 
PRO HB2  H N N 524 
PRO HB3  H N N 525 
PRO HG2  H N N 526 
PRO HG3  H N N 527 
PRO HD2  H N N 528 
PRO HD3  H N N 529 
PRO HXT  H N N 530 
SER N    N N N 531 
SER CA   C N S 532 
SER C    C N N 533 
SER O    O N N 534 
SER CB   C N N 535 
SER OG   O N N 536 
SER OXT  O N N 537 
SER H    H N N 538 
SER H2   H N N 539 
SER HA   H N N 540 
SER HB2  H N N 541 
SER HB3  H N N 542 
SER HG   H N N 543 
SER HXT  H N N 544 
THR N    N N N 545 
THR CA   C N S 546 
THR C    C N N 547 
THR O    O N N 548 
THR CB   C N R 549 
THR OG1  O N N 550 
THR CG2  C N N 551 
THR OXT  O N N 552 
THR H    H N N 553 
THR H2   H N N 554 
THR HA   H N N 555 
THR HB   H N N 556 
THR HG1  H N N 557 
THR HG21 H N N 558 
THR HG22 H N N 559 
THR HG23 H N N 560 
THR HXT  H N N 561 
TRP N    N N N 562 
TRP CA   C N S 563 
TRP C    C N N 564 
TRP O    O N N 565 
TRP CB   C N N 566 
TRP CG   C Y N 567 
TRP CD1  C Y N 568 
TRP CD2  C Y N 569 
TRP NE1  N Y N 570 
TRP CE2  C Y N 571 
TRP CE3  C Y N 572 
TRP CZ2  C Y N 573 
TRP CZ3  C Y N 574 
TRP CH2  C Y N 575 
TRP OXT  O N N 576 
TRP H    H N N 577 
TRP H2   H N N 578 
TRP HA   H N N 579 
TRP HB2  H N N 580 
TRP HB3  H N N 581 
TRP HD1  H N N 582 
TRP HE1  H N N 583 
TRP HE3  H N N 584 
TRP HZ2  H N N 585 
TRP HZ3  H N N 586 
TRP HH2  H N N 587 
TRP HXT  H N N 588 
TYR N    N N N 589 
TYR CA   C N S 590 
TYR C    C N N 591 
TYR O    O N N 592 
TYR CB   C N N 593 
TYR CG   C Y N 594 
TYR CD1  C Y N 595 
TYR CD2  C Y N 596 
TYR CE1  C Y N 597 
TYR CE2  C Y N 598 
TYR CZ   C Y N 599 
TYR OH   O N N 600 
TYR OXT  O N N 601 
TYR H    H N N 602 
TYR H2   H N N 603 
TYR HA   H N N 604 
TYR HB2  H N N 605 
TYR HB3  H N N 606 
TYR HD1  H N N 607 
TYR HD2  H N N 608 
TYR HE1  H N N 609 
TYR HE2  H N N 610 
TYR HH   H N N 611 
TYR HXT  H N N 612 
VAL N    N N N 613 
VAL CA   C N S 614 
VAL C    C N N 615 
VAL O    O N N 616 
VAL CB   C N N 617 
VAL CG1  C N N 618 
VAL CG2  C N N 619 
VAL OXT  O N N 620 
VAL H    H N N 621 
VAL H2   H N N 622 
VAL HA   H N N 623 
VAL HB   H N N 624 
VAL HG11 H N N 625 
VAL HG12 H N N 626 
VAL HG13 H N N 627 
VAL HG21 H N N 628 
VAL HG22 H N N 629 
VAL HG23 H N N 630 
VAL HXT  H N N 631 
YCM N    N N N 632 
YCM CA   C N R 633 
YCM CB   C N N 634 
YCM SG   S N N 635 
YCM CD   C N N 636 
YCM CE   C N N 637 
YCM OZ1  O N N 638 
YCM NZ2  N N N 639 
YCM C    C N N 640 
YCM O    O N N 641 
YCM OXT  O N N 642 
YCM H    H N N 643 
YCM H2   H N N 644 
YCM HA   H N N 645 
YCM HB2  H N N 646 
YCM HB3  H N N 647 
YCM HD2  H N N 648 
YCM HD3  H N N 649 
YCM HZ21 H N N 650 
YCM HZ22 H N N 651 
YCM HXT  H N N 652 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CLR C1  C2   sing N N 70  
CLR C1  C10  sing N N 71  
CLR C1  H11  sing N N 72  
CLR C1  H12  sing N N 73  
CLR C2  C3   sing N N 74  
CLR C2  H21  sing N N 75  
CLR C2  H22  sing N N 76  
CLR C3  C4   sing N N 77  
CLR C3  O1   sing N N 78  
CLR C3  H3   sing N N 79  
CLR C4  C5   sing N N 80  
CLR C4  H41  sing N N 81  
CLR C4  H42  sing N N 82  
CLR C5  C6   doub N N 83  
CLR C5  C10  sing N N 84  
CLR C6  C7   sing N N 85  
CLR C6  H6   sing N N 86  
CLR C7  C8   sing N N 87  
CLR C7  H71  sing N N 88  
CLR C7  H72  sing N N 89  
CLR C8  C9   sing N N 90  
CLR C8  C14  sing N N 91  
CLR C8  H8   sing N N 92  
CLR C9  C10  sing N N 93  
CLR C9  C11  sing N N 94  
CLR C9  H9   sing N N 95  
CLR C10 C19  sing N N 96  
CLR C11 C12  sing N N 97  
CLR C11 H111 sing N N 98  
CLR C11 H112 sing N N 99  
CLR C12 C13  sing N N 100 
CLR C12 H121 sing N N 101 
CLR C12 H122 sing N N 102 
CLR C13 C14  sing N N 103 
CLR C13 C17  sing N N 104 
CLR C13 C18  sing N N 105 
CLR C14 C15  sing N N 106 
CLR C14 H14  sing N N 107 
CLR C15 C16  sing N N 108 
CLR C15 H151 sing N N 109 
CLR C15 H152 sing N N 110 
CLR C16 C17  sing N N 111 
CLR C16 H161 sing N N 112 
CLR C16 H162 sing N N 113 
CLR C17 C20  sing N N 114 
CLR C17 H17  sing N N 115 
CLR C18 H181 sing N N 116 
CLR C18 H182 sing N N 117 
CLR C18 H183 sing N N 118 
CLR C19 H191 sing N N 119 
CLR C19 H192 sing N N 120 
CLR C19 H193 sing N N 121 
CLR C20 C21  sing N N 122 
CLR C20 C22  sing N N 123 
CLR C20 H20  sing N N 124 
CLR C21 H211 sing N N 125 
CLR C21 H212 sing N N 126 
CLR C21 H213 sing N N 127 
CLR C22 C23  sing N N 128 
CLR C22 H221 sing N N 129 
CLR C22 H222 sing N N 130 
CLR C23 C24  sing N N 131 
CLR C23 H231 sing N N 132 
CLR C23 H232 sing N N 133 
CLR C24 C25  sing N N 134 
CLR C24 H241 sing N N 135 
CLR C24 H242 sing N N 136 
CLR C25 C26  sing N N 137 
CLR C25 C27  sing N N 138 
CLR C25 H25  sing N N 139 
CLR C26 H261 sing N N 140 
CLR C26 H262 sing N N 141 
CLR C26 H263 sing N N 142 
CLR C27 H271 sing N N 143 
CLR C27 H272 sing N N 144 
CLR C27 H273 sing N N 145 
CLR O1  H1   sing N N 146 
CYS N   CA   sing N N 147 
CYS N   H    sing N N 148 
CYS N   H2   sing N N 149 
CYS CA  C    sing N N 150 
CYS CA  CB   sing N N 151 
CYS CA  HA   sing N N 152 
CYS C   O    doub N N 153 
CYS C   OXT  sing N N 154 
CYS CB  SG   sing N N 155 
CYS CB  HB2  sing N N 156 
CYS CB  HB3  sing N N 157 
CYS SG  HG   sing N N 158 
CYS OXT HXT  sing N N 159 
GLN N   CA   sing N N 160 
GLN N   H    sing N N 161 
GLN N   H2   sing N N 162 
GLN CA  C    sing N N 163 
GLN CA  CB   sing N N 164 
GLN CA  HA   sing N N 165 
GLN C   O    doub N N 166 
GLN C   OXT  sing N N 167 
GLN CB  CG   sing N N 168 
GLN CB  HB2  sing N N 169 
GLN CB  HB3  sing N N 170 
GLN CG  CD   sing N N 171 
GLN CG  HG2  sing N N 172 
GLN CG  HG3  sing N N 173 
GLN CD  OE1  doub N N 174 
GLN CD  NE2  sing N N 175 
GLN NE2 HE21 sing N N 176 
GLN NE2 HE22 sing N N 177 
GLN OXT HXT  sing N N 178 
GLU N   CA   sing N N 179 
GLU N   H    sing N N 180 
GLU N   H2   sing N N 181 
GLU CA  C    sing N N 182 
GLU CA  CB   sing N N 183 
GLU CA  HA   sing N N 184 
GLU C   O    doub N N 185 
GLU C   OXT  sing N N 186 
GLU CB  CG   sing N N 187 
GLU CB  HB2  sing N N 188 
GLU CB  HB3  sing N N 189 
GLU CG  CD   sing N N 190 
GLU CG  HG2  sing N N 191 
GLU CG  HG3  sing N N 192 
GLU CD  OE1  doub N N 193 
GLU CD  OE2  sing N N 194 
GLU OE2 HE2  sing N N 195 
GLU OXT HXT  sing N N 196 
GLY N   CA   sing N N 197 
GLY N   H    sing N N 198 
GLY N   H2   sing N N 199 
GLY CA  C    sing N N 200 
GLY CA  HA2  sing N N 201 
GLY CA  HA3  sing N N 202 
GLY C   O    doub N N 203 
GLY C   OXT  sing N N 204 
GLY OXT HXT  sing N N 205 
HIS N   CA   sing N N 206 
HIS N   H    sing N N 207 
HIS N   H2   sing N N 208 
HIS CA  C    sing N N 209 
HIS CA  CB   sing N N 210 
HIS CA  HA   sing N N 211 
HIS C   O    doub N N 212 
HIS C   OXT  sing N N 213 
HIS CB  CG   sing N N 214 
HIS CB  HB2  sing N N 215 
HIS CB  HB3  sing N N 216 
HIS CG  ND1  sing Y N 217 
HIS CG  CD2  doub Y N 218 
HIS ND1 CE1  doub Y N 219 
HIS ND1 HD1  sing N N 220 
HIS CD2 NE2  sing Y N 221 
HIS CD2 HD2  sing N N 222 
HIS CE1 NE2  sing Y N 223 
HIS CE1 HE1  sing N N 224 
HIS NE2 HE2  sing N N 225 
HIS OXT HXT  sing N N 226 
HOH O   H1   sing N N 227 
HOH O   H2   sing N N 228 
ILE N   CA   sing N N 229 
ILE N   H    sing N N 230 
ILE N   H2   sing N N 231 
ILE CA  C    sing N N 232 
ILE CA  CB   sing N N 233 
ILE CA  HA   sing N N 234 
ILE C   O    doub N N 235 
ILE C   OXT  sing N N 236 
ILE CB  CG1  sing N N 237 
ILE CB  CG2  sing N N 238 
ILE CB  HB   sing N N 239 
ILE CG1 CD1  sing N N 240 
ILE CG1 HG12 sing N N 241 
ILE CG1 HG13 sing N N 242 
ILE CG2 HG21 sing N N 243 
ILE CG2 HG22 sing N N 244 
ILE CG2 HG23 sing N N 245 
ILE CD1 HD11 sing N N 246 
ILE CD1 HD12 sing N N 247 
ILE CD1 HD13 sing N N 248 
ILE OXT HXT  sing N N 249 
LEU N   CA   sing N N 250 
LEU N   H    sing N N 251 
LEU N   H2   sing N N 252 
LEU CA  C    sing N N 253 
LEU CA  CB   sing N N 254 
LEU CA  HA   sing N N 255 
LEU C   O    doub N N 256 
LEU C   OXT  sing N N 257 
LEU CB  CG   sing N N 258 
LEU CB  HB2  sing N N 259 
LEU CB  HB3  sing N N 260 
LEU CG  CD1  sing N N 261 
LEU CG  CD2  sing N N 262 
LEU CG  HG   sing N N 263 
LEU CD1 HD11 sing N N 264 
LEU CD1 HD12 sing N N 265 
LEU CD1 HD13 sing N N 266 
LEU CD2 HD21 sing N N 267 
LEU CD2 HD22 sing N N 268 
LEU CD2 HD23 sing N N 269 
LEU OXT HXT  sing N N 270 
LYS N   CA   sing N N 271 
LYS N   H    sing N N 272 
LYS N   H2   sing N N 273 
LYS CA  C    sing N N 274 
LYS CA  CB   sing N N 275 
LYS CA  HA   sing N N 276 
LYS C   O    doub N N 277 
LYS C   OXT  sing N N 278 
LYS CB  CG   sing N N 279 
LYS CB  HB2  sing N N 280 
LYS CB  HB3  sing N N 281 
LYS CG  CD   sing N N 282 
LYS CG  HG2  sing N N 283 
LYS CG  HG3  sing N N 284 
LYS CD  CE   sing N N 285 
LYS CD  HD2  sing N N 286 
LYS CD  HD3  sing N N 287 
LYS CE  NZ   sing N N 288 
LYS CE  HE2  sing N N 289 
LYS CE  HE3  sing N N 290 
LYS NZ  HZ1  sing N N 291 
LYS NZ  HZ2  sing N N 292 
LYS NZ  HZ3  sing N N 293 
LYS OXT HXT  sing N N 294 
MET N   CA   sing N N 295 
MET N   H    sing N N 296 
MET N   H2   sing N N 297 
MET CA  C    sing N N 298 
MET CA  CB   sing N N 299 
MET CA  HA   sing N N 300 
MET C   O    doub N N 301 
MET C   OXT  sing N N 302 
MET CB  CG   sing N N 303 
MET CB  HB2  sing N N 304 
MET CB  HB3  sing N N 305 
MET CG  SD   sing N N 306 
MET CG  HG2  sing N N 307 
MET CG  HG3  sing N N 308 
MET SD  CE   sing N N 309 
MET CE  HE1  sing N N 310 
MET CE  HE2  sing N N 311 
MET CE  HE3  sing N N 312 
MET OXT HXT  sing N N 313 
OLA C1  O1   doub N N 314 
OLA C1  O2   sing N N 315 
OLA C1  C2   sing N N 316 
OLA O2  HO2  sing N N 317 
OLA C2  C3   sing N N 318 
OLA C2  H21  sing N N 319 
OLA C2  H22  sing N N 320 
OLA C3  C4   sing N N 321 
OLA C3  H31  sing N N 322 
OLA C3  H32  sing N N 323 
OLA C4  C5   sing N N 324 
OLA C4  H41  sing N N 325 
OLA C4  H42  sing N N 326 
OLA C5  C6   sing N N 327 
OLA C5  H51  sing N N 328 
OLA C5  H52  sing N N 329 
OLA C6  C7   sing N N 330 
OLA C6  H61  sing N N 331 
OLA C6  H62  sing N N 332 
OLA C7  C8   sing N N 333 
OLA C7  H71  sing N N 334 
OLA C7  H72  sing N N 335 
OLA C8  C9   sing N N 336 
OLA C8  H81  sing N N 337 
OLA C8  H82  sing N N 338 
OLA C9  C10  doub N Z 339 
OLA C9  H9   sing N N 340 
OLA C10 C11  sing N N 341 
OLA C10 H10  sing N N 342 
OLA C11 C12  sing N N 343 
OLA C11 H111 sing N N 344 
OLA C11 H112 sing N N 345 
OLA C12 C13  sing N N 346 
OLA C12 H121 sing N N 347 
OLA C12 H122 sing N N 348 
OLA C13 C14  sing N N 349 
OLA C13 H131 sing N N 350 
OLA C13 H132 sing N N 351 
OLA C14 C15  sing N N 352 
OLA C14 H141 sing N N 353 
OLA C14 H142 sing N N 354 
OLA C15 C16  sing N N 355 
OLA C15 H151 sing N N 356 
OLA C15 H152 sing N N 357 
OLA C16 C17  sing N N 358 
OLA C16 H161 sing N N 359 
OLA C16 H162 sing N N 360 
OLA C17 C18  sing N N 361 
OLA C17 H171 sing N N 362 
OLA C17 H172 sing N N 363 
OLA C18 H181 sing N N 364 
OLA C18 H182 sing N N 365 
OLA C18 H183 sing N N 366 
OLC C18 C17  sing N N 367 
OLC C10 C9   doub N N 368 
OLC C10 C11  sing N N 369 
OLC C9  C8   sing N N 370 
OLC C17 C16  sing N Z 371 
OLC C11 C12  sing N N 372 
OLC C8  C7   sing N N 373 
OLC C24 C22  sing N N 374 
OLC C24 O25  sing N N 375 
OLC C16 C15  sing N N 376 
OLC C12 C13  sing N N 377 
OLC C7  C6   sing N N 378 
OLC C15 C14  sing N N 379 
OLC C13 C14  sing N N 380 
OLC C6  C5   sing N N 381 
OLC C5  C4   sing N N 382 
OLC C4  C3   sing N N 383 
OLC C3  C2   sing N N 384 
OLC C2  C1   sing N N 385 
OLC C21 C22  sing N N 386 
OLC C21 O20  sing N N 387 
OLC C1  O19  doub N N 388 
OLC C1  O20  sing N N 389 
OLC C22 O23  sing N N 390 
OLC C18 H18  sing N N 391 
OLC C18 H18A sing N N 392 
OLC C18 H18B sing N N 393 
OLC C10 H10  sing N N 394 
OLC C9  H9   sing N N 395 
OLC C17 H17  sing N N 396 
OLC C17 H17A sing N N 397 
OLC C11 H11  sing N N 398 
OLC C11 H11A sing N N 399 
OLC C8  H8   sing N N 400 
OLC C8  H8A  sing N N 401 
OLC C24 H24  sing N N 402 
OLC C24 H24A sing N N 403 
OLC C16 H16  sing N N 404 
OLC C16 H16A sing N N 405 
OLC C12 H12  sing N N 406 
OLC C12 H12A sing N N 407 
OLC C7  H7   sing N N 408 
OLC C7  H7A  sing N N 409 
OLC C15 H15  sing N N 410 
OLC C15 H15A sing N N 411 
OLC C13 H13  sing N N 412 
OLC C13 H13A sing N N 413 
OLC C6  H6   sing N N 414 
OLC C6  H6A  sing N N 415 
OLC C14 H14  sing N N 416 
OLC C14 H14A sing N N 417 
OLC C5  H5   sing N N 418 
OLC C5  H5A  sing N N 419 
OLC C4  H4   sing N N 420 
OLC C4  H4A  sing N N 421 
OLC C3  H3   sing N N 422 
OLC C3  H3A  sing N N 423 
OLC C2  H2   sing N N 424 
OLC C2  H2A  sing N N 425 
OLC C21 H21  sing N N 426 
OLC C21 H21A sing N N 427 
OLC C22 H22  sing N N 428 
OLC O25 HO25 sing N N 429 
OLC O23 HO23 sing N N 430 
P15 C13 O6   sing N N 431 
P15 C13 H131 sing N N 432 
P15 C13 H132 sing N N 433 
P15 C13 H133 sing N N 434 
P15 O6  C12  sing N N 435 
P15 C12 C11  sing N N 436 
P15 C12 H121 sing N N 437 
P15 C12 H122 sing N N 438 
P15 C11 O5   sing N N 439 
P15 C11 H111 sing N N 440 
P15 C11 H112 sing N N 441 
P15 O5  C10  sing N N 442 
P15 C10 C9   sing N N 443 
P15 C10 H101 sing N N 444 
P15 C10 H102 sing N N 445 
P15 C9  O4   sing N N 446 
P15 C9  H91  sing N N 447 
P15 C9  H92  sing N N 448 
P15 O4  C8   sing N N 449 
P15 C8  C7   sing N N 450 
P15 C8  H81  sing N N 451 
P15 C8  H82  sing N N 452 
P15 C7  O3   sing N N 453 
P15 C7  H71  sing N N 454 
P15 C7  H72  sing N N 455 
P15 O3  C6   sing N N 456 
P15 C6  C5   sing N N 457 
P15 C6  H61  sing N N 458 
P15 C6  H62  sing N N 459 
P15 C5  O2   sing N N 460 
P15 C5  H51  sing N N 461 
P15 C5  H52  sing N N 462 
P15 O2  C4   sing N N 463 
P15 C4  C3   sing N N 464 
P15 C4  H41  sing N N 465 
P15 C4  H42  sing N N 466 
P15 C3  O1   sing N N 467 
P15 C3  H31  sing N N 468 
P15 C3  H32  sing N N 469 
P15 O1  C2   sing N N 470 
P15 C2  C1   sing N N 471 
P15 C2  H21  sing N N 472 
P15 C2  H22  sing N N 473 
P15 C1  OXT  sing N N 474 
P15 C1  H11  sing N N 475 
P15 C1  H12  sing N N 476 
P15 OXT HOXT sing N N 477 
PHE N   CA   sing N N 478 
PHE N   H    sing N N 479 
PHE N   H2   sing N N 480 
PHE CA  C    sing N N 481 
PHE CA  CB   sing N N 482 
PHE CA  HA   sing N N 483 
PHE C   O    doub N N 484 
PHE C   OXT  sing N N 485 
PHE CB  CG   sing N N 486 
PHE CB  HB2  sing N N 487 
PHE CB  HB3  sing N N 488 
PHE CG  CD1  doub Y N 489 
PHE CG  CD2  sing Y N 490 
PHE CD1 CE1  sing Y N 491 
PHE CD1 HD1  sing N N 492 
PHE CD2 CE2  doub Y N 493 
PHE CD2 HD2  sing N N 494 
PHE CE1 CZ   doub Y N 495 
PHE CE1 HE1  sing N N 496 
PHE CE2 CZ   sing Y N 497 
PHE CE2 HE2  sing N N 498 
PHE CZ  HZ   sing N N 499 
PHE OXT HXT  sing N N 500 
PRO N   CA   sing N N 501 
PRO N   CD   sing N N 502 
PRO N   H    sing N N 503 
PRO CA  C    sing N N 504 
PRO CA  CB   sing N N 505 
PRO CA  HA   sing N N 506 
PRO C   O    doub N N 507 
PRO C   OXT  sing N N 508 
PRO CB  CG   sing N N 509 
PRO CB  HB2  sing N N 510 
PRO CB  HB3  sing N N 511 
PRO CG  CD   sing N N 512 
PRO CG  HG2  sing N N 513 
PRO CG  HG3  sing N N 514 
PRO CD  HD2  sing N N 515 
PRO CD  HD3  sing N N 516 
PRO OXT HXT  sing N N 517 
SER N   CA   sing N N 518 
SER N   H    sing N N 519 
SER N   H2   sing N N 520 
SER CA  C    sing N N 521 
SER CA  CB   sing N N 522 
SER CA  HA   sing N N 523 
SER C   O    doub N N 524 
SER C   OXT  sing N N 525 
SER CB  OG   sing N N 526 
SER CB  HB2  sing N N 527 
SER CB  HB3  sing N N 528 
SER OG  HG   sing N N 529 
SER OXT HXT  sing N N 530 
THR N   CA   sing N N 531 
THR N   H    sing N N 532 
THR N   H2   sing N N 533 
THR CA  C    sing N N 534 
THR CA  CB   sing N N 535 
THR CA  HA   sing N N 536 
THR C   O    doub N N 537 
THR C   OXT  sing N N 538 
THR CB  OG1  sing N N 539 
THR CB  CG2  sing N N 540 
THR CB  HB   sing N N 541 
THR OG1 HG1  sing N N 542 
THR CG2 HG21 sing N N 543 
THR CG2 HG22 sing N N 544 
THR CG2 HG23 sing N N 545 
THR OXT HXT  sing N N 546 
TRP N   CA   sing N N 547 
TRP N   H    sing N N 548 
TRP N   H2   sing N N 549 
TRP CA  C    sing N N 550 
TRP CA  CB   sing N N 551 
TRP CA  HA   sing N N 552 
TRP C   O    doub N N 553 
TRP C   OXT  sing N N 554 
TRP CB  CG   sing N N 555 
TRP CB  HB2  sing N N 556 
TRP CB  HB3  sing N N 557 
TRP CG  CD1  doub Y N 558 
TRP CG  CD2  sing Y N 559 
TRP CD1 NE1  sing Y N 560 
TRP CD1 HD1  sing N N 561 
TRP CD2 CE2  doub Y N 562 
TRP CD2 CE3  sing Y N 563 
TRP NE1 CE2  sing Y N 564 
TRP NE1 HE1  sing N N 565 
TRP CE2 CZ2  sing Y N 566 
TRP CE3 CZ3  doub Y N 567 
TRP CE3 HE3  sing N N 568 
TRP CZ2 CH2  doub Y N 569 
TRP CZ2 HZ2  sing N N 570 
TRP CZ3 CH2  sing Y N 571 
TRP CZ3 HZ3  sing N N 572 
TRP CH2 HH2  sing N N 573 
TRP OXT HXT  sing N N 574 
TYR N   CA   sing N N 575 
TYR N   H    sing N N 576 
TYR N   H2   sing N N 577 
TYR CA  C    sing N N 578 
TYR CA  CB   sing N N 579 
TYR CA  HA   sing N N 580 
TYR C   O    doub N N 581 
TYR C   OXT  sing N N 582 
TYR CB  CG   sing N N 583 
TYR CB  HB2  sing N N 584 
TYR CB  HB3  sing N N 585 
TYR CG  CD1  doub Y N 586 
TYR CG  CD2  sing Y N 587 
TYR CD1 CE1  sing Y N 588 
TYR CD1 HD1  sing N N 589 
TYR CD2 CE2  doub Y N 590 
TYR CD2 HD2  sing N N 591 
TYR CE1 CZ   doub Y N 592 
TYR CE1 HE1  sing N N 593 
TYR CE2 CZ   sing Y N 594 
TYR CE2 HE2  sing N N 595 
TYR CZ  OH   sing N N 596 
TYR OH  HH   sing N N 597 
TYR OXT HXT  sing N N 598 
VAL N   CA   sing N N 599 
VAL N   H    sing N N 600 
VAL N   H2   sing N N 601 
VAL CA  C    sing N N 602 
VAL CA  CB   sing N N 603 
VAL CA  HA   sing N N 604 
VAL C   O    doub N N 605 
VAL C   OXT  sing N N 606 
VAL CB  CG1  sing N N 607 
VAL CB  CG2  sing N N 608 
VAL CB  HB   sing N N 609 
VAL CG1 HG11 sing N N 610 
VAL CG1 HG12 sing N N 611 
VAL CG1 HG13 sing N N 612 
VAL CG2 HG21 sing N N 613 
VAL CG2 HG22 sing N N 614 
VAL CG2 HG23 sing N N 615 
VAL OXT HXT  sing N N 616 
YCM N   CA   sing N N 617 
YCM N   H    sing N N 618 
YCM N   H2   sing N N 619 
YCM CA  CB   sing N N 620 
YCM CA  C    sing N N 621 
YCM CA  HA   sing N N 622 
YCM CB  SG   sing N N 623 
YCM CB  HB2  sing N N 624 
YCM CB  HB3  sing N N 625 
YCM SG  CD   sing N N 626 
YCM CD  CE   sing N N 627 
YCM CD  HD2  sing N N 628 
YCM CD  HD3  sing N N 629 
YCM CE  OZ1  doub N N 630 
YCM CE  NZ2  sing N N 631 
YCM NZ2 HZ21 sing N N 632 
YCM NZ2 HZ22 sing N N 633 
YCM C   O    doub N N 634 
YCM C   OXT  sing N N 635 
YCM OXT HXT  sing N N 636 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           'R35 GM127086' 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8T1V 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8TF5 
_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.fract_transf_matrix[1][1]   0.017534 
_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]   0.010323 
_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]   0.010250 
_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 
N 
O 
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   . PRO A 1 39  ? 22.822 -2.903 71.131  1.00 77.27  ? 70   PRO A N   1 
ATOM   2    C CA  . PRO A 1 39  ? 22.492 -2.151 69.916  1.00 78.12  ? 70   PRO A CA  1 
ATOM   3    C C   . PRO A 1 39  ? 22.752 -0.652 70.065  1.00 82.44  ? 70   PRO A C   1 
ATOM   4    O O   . PRO A 1 39  ? 21.809 0.132  70.189  1.00 87.82  ? 70   PRO A O   1 
ATOM   5    C CB  . PRO A 1 39  ? 21.001 -2.436 69.731  1.00 86.56  ? 70   PRO A CB  1 
ATOM   6    C CG  . PRO A 1 39  ? 20.494 -2.602 71.121  1.00 101.64 ? 70   PRO A CG  1 
ATOM   7    C CD  . PRO A 1 39  ? 21.613 -3.264 71.895  1.00 94.46  ? 70   PRO A CD  1 
ATOM   8    N N   . ALA A 1 40  ? 24.028 -0.265 70.061  1.00 70.83  ? 71   ALA A N   1 
ATOM   9    C CA  . ALA A 1 40  ? 24.402 1.140  70.145  1.00 86.30  ? 71   ALA A CA  1 
ATOM   10   C C   . ALA A 1 40  ? 24.575 1.785  68.779  1.00 71.26  ? 71   ALA A C   1 
ATOM   11   O O   . ALA A 1 40  ? 24.559 3.019  68.685  1.00 66.55  ? 71   ALA A O   1 
ATOM   12   C CB  . ALA A 1 40  ? 25.701 1.296  70.944  1.00 82.27  ? 71   ALA A CB  1 
ATOM   13   N N   . VAL A 1 41  ? 24.740 0.991  67.725  1.00 49.76  ? 72   VAL A N   1 
ATOM   14   C CA  . VAL A 1 41  ? 24.823 1.531  66.373  1.00 52.51  ? 72   VAL A CA  1 
ATOM   15   C C   . VAL A 1 41  ? 23.417 1.851  65.886  1.00 34.81  ? 72   VAL A C   1 
ATOM   16   O O   . VAL A 1 41  ? 22.512 1.012  65.951  1.00 37.85  ? 72   VAL A O   1 
ATOM   17   C CB  . VAL A 1 41  ? 25.533 0.546  65.430  1.00 51.31  ? 72   VAL A CB  1 
ATOM   18   C CG1 . VAL A 1 41  ? 25.480 1.044  63.993  1.00 44.63  ? 72   VAL A CG1 1 
ATOM   19   C CG2 . VAL A 1 41  ? 26.973 0.366  65.850  1.00 59.07  ? 72   VAL A CG2 1 
ATOM   20   N N   . ASN A 1 42  ? 23.234 3.063  65.407  1.00 40.01  ? 73   ASN A N   1 
ATOM   21   C CA  . ASN A 1 42  ? 21.946 3.486  64.877  1.00 36.05  ? 73   ASN A CA  1 
ATOM   22   C C   . ASN A 1 42  ? 21.755 2.934  63.467  1.00 36.70  ? 73   ASN A C   1 
ATOM   23   O O   . ASN A 1 42  ? 22.619 3.137  62.608  1.00 35.55  ? 73   ASN A O   1 
ATOM   24   C CB  . ASN A 1 42  ? 21.870 5.006  64.859  1.00 36.93  ? 73   ASN A CB  1 
ATOM   25   C CG  . ASN A 1 42  ? 20.497 5.516  64.484  1.00 40.41  ? 73   ASN A CG  1 
ATOM   26   O OD1 . ASN A 1 42  ? 20.041 5.326  63.361  1.00 47.73  ? 73   ASN A OD1 1 
ATOM   27   N ND2 . ASN A 1 42  ? 19.834 6.175  65.424  1.00 51.69  ? 73   ASN A ND2 1 
ATOM   28   N N   . PRO A 1 43  ? 20.645 2.239  63.190  1.00 36.13  ? 74   PRO A N   1 
ATOM   29   C CA  . PRO A 1 43  ? 20.448 1.668  61.844  1.00 36.10  ? 74   PRO A CA  1 
ATOM   30   C C   . PRO A 1 43  ? 20.588 2.676  60.720  1.00 37.88  ? 74   PRO A C   1 
ATOM   31   O O   . PRO A 1 43  ? 21.099 2.346  59.642  1.00 34.28  ? 74   PRO A O   1 
ATOM   32   C CB  . PRO A 1 43  ? 19.015 1.121  61.903  1.00 43.01  ? 74   PRO A CB  1 
ATOM   33   C CG  . PRO A 1 43  ? 18.718 0.934  63.337  1.00 46.24  ? 74   PRO A CG  1 
ATOM   34   C CD  . PRO A 1 43  ? 19.515 1.951  64.089  1.00 34.56  ? 74   PRO A CD  1 
ATOM   35   N N   . TRP A 1 44  ? 20.111 3.900  60.941  1.00 33.04  ? 75   TRP A N   1 
ATOM   36   C CA  . TRP A 1 44  ? 20.183 4.919  59.905  1.00 31.87  ? 75   TRP A CA  1 
ATOM   37   C C   . TRP A 1 44  ? 21.620 5.253  59.545  1.00 33.73  ? 75   TRP A C   1 
ATOM   38   O O   . TRP A 1 44  ? 21.915 5.546  58.382  1.00 35.96  ? 75   TRP A O   1 
ATOM   39   C CB  . TRP A 1 44  ? 19.446 6.172  60.366  1.00 37.44  ? 75   TRP A CB  1 
ATOM   40   C CG  . TRP A 1 44  ? 17.987 5.944  60.571  1.00 34.82  ? 75   TRP A CG  1 
ATOM   41   C CD1 . TRP A 1 44  ? 17.355 5.693  61.750  1.00 38.37  ? 75   TRP A CD1 1 
ATOM   42   C CD2 . TRP A 1 44  ? 16.973 5.942  59.562  1.00 35.99  ? 75   TRP A CD2 1 
ATOM   43   N NE1 . TRP A 1 44  ? 16.009 5.537  61.540  1.00 40.52  ? 75   TRP A NE1 1 
ATOM   44   C CE2 . TRP A 1 44  ? 15.748 5.686  60.204  1.00 37.61  ? 75   TRP A CE2 1 
ATOM   45   C CE3 . TRP A 1 44  ? 16.983 6.138  58.177  1.00 39.70  ? 75   TRP A CE3 1 
ATOM   46   C CZ2 . TRP A 1 44  ? 14.541 5.618  59.510  1.00 44.08  ? 75   TRP A CZ2 1 
ATOM   47   C CZ3 . TRP A 1 44  ? 15.786 6.070  57.490  1.00 51.39  ? 75   TRP A CZ3 1 
ATOM   48   C CH2 . TRP A 1 44  ? 14.581 5.812  58.157  1.00 45.02  ? 75   TRP A CH2 1 
ATOM   49   N N   . ASP A 1 45  ? 22.529 5.230  60.526  1.00 33.51  ? 76   ASP A N   1 
ATOM   50   C CA  . ASP A 1 45  ? 23.931 5.491  60.218  1.00 35.59  ? 76   ASP A CA  1 
ATOM   51   C C   . ASP A 1 45  ? 24.489 4.416  59.296  1.00 31.78  ? 76   ASP A C   1 
ATOM   52   O O   . ASP A 1 45  ? 25.277 4.712  58.391  1.00 29.60  ? 76   ASP A O   1 
ATOM   53   C CB  . ASP A 1 45  ? 24.748 5.579  61.505  1.00 33.85  ? 76   ASP A CB  1 
ATOM   54   C CG  . ASP A 1 45  ? 24.443 6.831  62.302  1.00 39.10  ? 76   ASP A CG  1 
ATOM   55   O OD1 . ASP A 1 45  ? 24.244 7.892  61.677  1.00 44.89  ? 76   ASP A OD1 1 
ATOM   56   O OD2 . ASP A 1 45  ? 24.400 6.757  63.549  1.00 47.05  ? 76   ASP A OD2 1 
ATOM   57   N N   . VAL A 1 46  ? 24.077 3.164  59.497  1.00 31.53  ? 77   VAL A N   1 
ATOM   58   C CA  . VAL A 1 46  ? 24.500 2.104  58.591  1.00 32.28  ? 77   VAL A CA  1 
ATOM   59   C C   . VAL A 1 46  ? 23.916 2.330  57.202  1.00 32.43  ? 77   VAL A C   1 
ATOM   60   O O   . VAL A 1 46  ? 24.593 2.119  56.190  1.00 33.70  ? 77   VAL A O   1 
ATOM   61   C CB  . VAL A 1 46  ? 24.106 0.729  59.154  1.00 35.05  ? 77   VAL A CB  1 
ATOM   62   C CG1 . VAL A 1 46  ? 24.495 -0.367 58.175  1.00 34.96  ? 77   VAL A CG1 1 
ATOM   63   C CG2 . VAL A 1 46  ? 24.770 0.502  60.506  1.00 43.32  ? 77   VAL A CG2 1 
ATOM   64   N N   . LEU A 1 47  ? 22.656 2.767  57.126  1.00 40.43  ? 78   LEU A N   1 
ATOM   65   C CA  A LEU A 1 47  ? 22.046 3.022  55.825  0.50 38.69  ? 78   LEU A CA  1 
ATOM   66   C CA  B LEU A 1 47  ? 22.042 3.024  55.828  0.50 38.69  ? 78   LEU A CA  1 
ATOM   67   C C   . LEU A 1 47  ? 22.780 4.129  55.080  1.00 40.81  ? 78   LEU A C   1 
ATOM   68   O O   . LEU A 1 47  ? 22.985 4.036  53.864  1.00 34.23  ? 78   LEU A O   1 
ATOM   69   C CB  A LEU A 1 47  ? 20.571 3.382  55.990  0.50 46.20  ? 78   LEU A CB  1 
ATOM   70   C CB  B LEU A 1 47  ? 20.573 3.393  56.017  0.50 46.19  ? 78   LEU A CB  1 
ATOM   71   C CG  A LEU A 1 47  ? 19.599 2.215  56.172  0.50 41.65  ? 78   LEU A CG  1 
ATOM   72   C CG  B LEU A 1 47  ? 19.578 2.933  54.953  0.50 50.56  ? 78   LEU A CG  1 
ATOM   73   C CD1 A LEU A 1 47  ? 18.197 2.743  56.409  0.50 45.54  ? 78   LEU A CD1 1 
ATOM   74   C CD1 B LEU A 1 47  ? 19.619 1.427  54.772  0.50 51.43  ? 78   LEU A CD1 1 
ATOM   75   C CD2 A LEU A 1 47  ? 19.622 1.285  54.965  0.50 51.51  ? 78   LEU A CD2 1 
ATOM   76   C CD2 B LEU A 1 47  ? 18.194 3.372  55.370  0.50 61.14  ? 78   LEU A CD2 1 
ATOM   77   N N   . LEU A 1 48  ? 23.179 5.188  55.789  1.00 34.70  ? 79   LEU A N   1 
ATOM   78   C CA  . LEU A 1 48  ? 23.940 6.255  55.146  1.00 35.07  ? 79   LEU A CA  1 
ATOM   79   C C   . LEU A 1 48  ? 25.300 5.759  54.680  1.00 39.77  ? 79   LEU A C   1 
ATOM   80   O O   . LEU A 1 48  ? 25.789 6.176  53.626  1.00 34.06  ? 79   LEU A O   1 
ATOM   81   C CB  . LEU A 1 48  ? 24.122 7.430  56.101  1.00 31.80  ? 79   LEU A CB  1 
ATOM   82   C CG  . LEU A 1 48  ? 22.877 8.241  56.447  1.00 37.61  ? 79   LEU A CG  1 
ATOM   83   C CD1 . LEU A 1 48  ? 23.181 9.194  57.590  1.00 32.89  ? 79   LEU A CD1 1 
ATOM   84   C CD2 . LEU A 1 48  ? 22.397 9.000  55.225  1.00 38.09  ? 79   LEU A CD2 1 
ATOM   85   N N   . CYS A 1 49  ? 25.929 4.876  55.457  1.00 30.30  ? 80   CYS A N   1 
ATOM   86   C CA  . CYS A 1 49  ? 27.218 4.335  55.049  1.00 34.63  ? 80   CYS A CA  1 
ATOM   87   C C   . CYS A 1 49  ? 27.070 3.488  53.794  1.00 32.42  ? 80   CYS A C   1 
ATOM   88   O O   . CYS A 1 49  ? 27.879 3.589  52.866  1.00 32.08  ? 80   CYS A O   1 
ATOM   89   C CB  . CYS A 1 49  ? 27.820 3.519  56.191  1.00 40.56  ? 80   CYS A CB  1 
ATOM   90   S SG  . CYS A 1 49  ? 29.490 2.924  55.868  1.00 42.49  ? 80   CYS A SG  1 
ATOM   91   N N   . VAL A 1 50  ? 26.032 2.652  53.753  1.00 34.96  ? 81   VAL A N   1 
ATOM   92   C CA  . VAL A 1 50  ? 25.724 1.880  52.554  1.00 37.69  ? 81   VAL A CA  1 
ATOM   93   C C   . VAL A 1 50  ? 25.456 2.813  51.381  1.00 30.44  ? 81   VAL A C   1 
ATOM   94   O O   . VAL A 1 50  ? 25.977 2.623  50.275  1.00 32.41  ? 81   VAL A O   1 
ATOM   95   C CB  . VAL A 1 50  ? 24.523 0.955  52.823  1.00 30.91  ? 81   VAL A CB  1 
ATOM   96   C CG1 . VAL A 1 50  ? 24.018 0.335  51.535  1.00 38.93  ? 81   VAL A CG1 1 
ATOM   97   C CG2 . VAL A 1 50  ? 24.898 -0.121 53.827  1.00 36.37  ? 81   VAL A CG2 1 
ATOM   98   N N   . SER A 1 51  ? 24.616 3.825  51.601  1.00 36.38  ? 82   SER A N   1 
ATOM   99   C CA  . SER A 1 51  ? 24.322 4.787  50.546  1.00 30.87  ? 82   SER A CA  1 
ATOM   100  C C   . SER A 1 51  ? 25.596 5.457  50.051  1.00 34.30  ? 82   SER A C   1 
ATOM   101  O O   . SER A 1 51  ? 25.822 5.576  48.840  1.00 32.82  ? 82   SER A O   1 
ATOM   102  C CB  . SER A 1 51  ? 23.324 5.826  51.058  1.00 37.24  ? 82   SER A CB  1 
ATOM   103  O OG  . SER A 1 51  ? 23.025 6.787  50.062  1.00 46.60  ? 82   SER A OG  1 
ATOM   104  N N   . GLY A 1 52  ? 26.450 5.893  50.978  1.00 29.75  ? 83   GLY A N   1 
ATOM   105  C CA  . GLY A 1 52  ? 27.692 6.533  50.579  1.00 28.32  ? 83   GLY A CA  1 
ATOM   106  C C   . GLY A 1 52  ? 28.590 5.620  49.768  1.00 27.63  ? 83   GLY A C   1 
ATOM   107  O O   . GLY A 1 52  ? 29.266 6.064  48.838  1.00 30.27  ? 83   GLY A O   1 
ATOM   108  N N   . THR A 1 53  ? 28.619 4.332  50.115  1.00 30.67  ? 84   THR A N   1 
ATOM   109  C CA  . THR A 1 53  ? 29.433 3.381  49.365  1.00 32.90  ? 84   THR A CA  1 
ATOM   110  C C   . THR A 1 53  ? 28.973 3.296  47.915  1.00 29.70  ? 84   THR A C   1 
ATOM   111  O O   . THR A 1 53  ? 29.785 3.376  46.986  1.00 29.52  ? 84   THR A O   1 
ATOM   112  C CB  . THR A 1 53  ? 29.370 2.006  50.032  1.00 35.95  ? 84   THR A CB  1 
ATOM   113  O OG1 . THR A 1 53  ? 29.917 2.094  51.352  1.00 35.38  ? 84   THR A OG1 1 
ATOM   114  C CG2 . THR A 1 53  ? 30.156 0.976  49.229  1.00 30.25  ? 84   THR A CG2 1 
ATOM   115  N N   . VAL A 1 54  ? 27.668 3.117  47.704  1.00 32.61  ? 85   VAL A N   1 
ATOM   116  C CA  . VAL A 1 54  ? 27.132 3.065  46.346  1.00 30.91  ? 85   VAL A CA  1 
ATOM   117  C C   . VAL A 1 54  ? 27.435 4.365  45.611  1.00 30.43  ? 85   VAL A C   1 
ATOM   118  O O   . VAL A 1 54  ? 27.884 4.356  44.460  1.00 30.59  ? 85   VAL A O   1 
ATOM   119  C CB  . VAL A 1 54  ? 25.622 2.770  46.381  1.00 29.57  ? 85   VAL A CB  1 
ATOM   120  C CG1 . VAL A 1 54  ? 25.024 2.811  44.980  1.00 37.70  ? 85   VAL A CG1 1 
ATOM   121  C CG2 . VAL A 1 54  ? 25.371 1.418  47.019  1.00 37.93  ? 85   VAL A CG2 1 
ATOM   122  N N   . ILE A 1 55  ? 27.204 5.502  46.272  1.00 34.74  ? 86   ILE A N   1 
ATOM   123  C CA  . ILE A 1 55  ? 27.479 6.795  45.649  1.00 26.88  ? 86   ILE A CA  1 
ATOM   124  C C   . ILE A 1 55  ? 28.947 6.897  45.262  1.00 28.36  ? 86   ILE A C   1 
ATOM   125  O O   . ILE A 1 55  ? 29.285 7.293  44.140  1.00 26.97  ? 86   ILE A O   1 
ATOM   126  C CB  . ILE A 1 55  ? 27.079 7.945  46.588  1.00 24.70  ? 86   ILE A CB  1 
ATOM   127  C CG1 . ILE A 1 55  ? 25.564 7.992  46.768  1.00 30.06  ? 86   ILE A CG1 1 
ATOM   128  C CG2 . ILE A 1 55  ? 27.598 9.274  46.045  1.00 33.80  ? 86   ILE A CG2 1 
ATOM   129  C CD1 . ILE A 1 55  ? 25.141 8.804  47.968  1.00 36.08  ? 86   ILE A CD1 1 
ATOM   130  N N   . ALA A 1 56  ? 29.843 6.561  46.192  1.00 27.56  ? 87   ALA A N   1 
ATOM   131  C CA  . ALA A 1 56  ? 31.268 6.680  45.908  1.00 26.16  ? 87   ALA A CA  1 
ATOM   132  C C   . ALA A 1 56  ? 31.673 5.778  44.750  1.00 31.39  ? 87   ALA A C   1 
ATOM   133  O O   . ALA A 1 56  ? 32.429 6.195  43.864  1.00 31.89  ? 87   ALA A O   1 
ATOM   134  C CB  . ALA A 1 56  ? 32.084 6.350  47.158  1.00 32.61  ? 87   ALA A CB  1 
ATOM   135  N N   . GLY A 1 57  ? 31.178 4.540  44.734  1.00 31.07  ? 88   GLY A N   1 
ATOM   136  C CA  . GLY A 1 57  ? 31.562 3.621  43.675  1.00 31.16  ? 88   GLY A CA  1 
ATOM   137  C C   . GLY A 1 57  ? 31.085 4.077  42.310  1.00 37.35  ? 88   GLY A C   1 
ATOM   138  O O   . GLY A 1 57  ? 31.842 4.065  41.336  1.00 34.35  ? 88   GLY A O   1 
ATOM   139  N N   . GLU A 1 58  ? 29.816 4.481  42.220  1.00 34.48  ? 89   GLU A N   1 
ATOM   140  C CA  . GLU A 1 58  ? 29.277 4.972  40.956  1.00 29.77  ? 89   GLU A CA  1 
ATOM   141  C C   . GLU A 1 58  ? 30.074 6.159  40.446  1.00 34.36  ? 89   GLU A C   1 
ATOM   142  O O   . GLU A 1 58  ? 30.497 6.193  39.286  1.00 33.54  ? 89   GLU A O   1 
ATOM   143  C CB  . GLU A 1 58  ? 27.825 5.395  41.133  1.00 37.41  ? 89   GLU A CB  1 
ATOM   144  C CG  . GLU A 1 58  ? 26.791 4.342  40.911  1.00 38.89  ? 89   GLU A CG  1 
ATOM   145  C CD  . GLU A 1 58  ? 25.405 4.921  41.084  1.00 43.53  ? 89   GLU A CD  1 
ATOM   146  O OE1 . GLU A 1 58  ? 25.027 5.218  42.233  1.00 43.76  ? 89   GLU A OE1 1 
ATOM   147  O OE2 . GLU A 1 58  ? 24.716 5.125  40.067  1.00 47.00  ? 89   GLU A OE2 1 
ATOM   148  N N   . ASN A 1 59  ? 30.263 7.160  41.302  1.00 27.25  ? 90   ASN A N   1 
ATOM   149  C CA  . ASN A 1 59  ? 30.842 8.414  40.851  1.00 34.49  ? 90   ASN A CA  1 
ATOM   150  C C   . ASN A 1 59  ? 32.355 8.338  40.721  1.00 31.12  ? 90   ASN A C   1 
ATOM   151  O O   . ASN A 1 59  ? 32.932 9.081  39.919  1.00 33.35  ? 90   ASN A O   1 
ATOM   152  C CB  . ASN A 1 59  ? 30.421 9.530  41.797  1.00 29.09  ? 90   ASN A CB  1 
ATOM   153  C CG  . ASN A 1 59  ? 28.971 9.909  41.614  1.00 29.61  ? 90   ASN A CG  1 
ATOM   154  O OD1 . ASN A 1 59  ? 28.623 10.600 40.657  1.00 32.33  ? 90   ASN A OD1 1 
ATOM   155  N ND2 . ASN A 1 59  ? 28.111 9.439  42.514  1.00 28.09  ? 90   ASN A ND2 1 
ATOM   156  N N   . ALA A 1 60  ? 33.012 7.450  41.472  1.00 34.58  ? 91   ALA A N   1 
ATOM   157  C CA  . ALA A 1 60  ? 34.435 7.222  41.240  1.00 36.76  ? 91   ALA A CA  1 
ATOM   158  C C   . ALA A 1 60  ? 34.669 6.691  39.835  1.00 38.27  ? 91   ALA A C   1 
ATOM   159  O O   . ALA A 1 60  ? 35.657 7.046  39.182  1.00 35.70  ? 91   ALA A O   1 
ATOM   160  C CB  . ALA A 1 60  ? 34.999 6.250  42.274  1.00 33.74  ? 91   ALA A CB  1 
ATOM   161  N N   . LEU A 1 61  ? 33.768 5.833  39.353  1.00 35.92  ? 92   LEU A N   1 
ATOM   162  C CA  . LEU A 1 61  ? 33.904 5.301  38.004  1.00 33.18  ? 92   LEU A CA  1 
ATOM   163  C C   . LEU A 1 61  ? 33.765 6.409  36.968  1.00 36.79  ? 92   LEU A C   1 
ATOM   164  O O   . LEU A 1 61  ? 34.553 6.489  36.020  1.00 32.87  ? 92   LEU A O   1 
ATOM   165  C CB  . LEU A 1 61  ? 32.865 4.202  37.775  1.00 35.12  ? 92   LEU A CB  1 
ATOM   166  C CG  . LEU A 1 61  ? 32.806 3.590  36.374  1.00 35.97  ? 92   LEU A CG  1 
ATOM   167  C CD1 . LEU A 1 61  ? 34.149 3.001  35.993  1.00 39.78  ? 92   LEU A CD1 1 
ATOM   168  C CD2 . LEU A 1 61  ? 31.714 2.531  36.299  1.00 37.33  ? 92   LEU A CD2 1 
ATOM   169  N N   . VAL A 1 62  ? 32.764 7.277  37.138  1.00 30.02  ? 93   VAL A N   1 
ATOM   170  C CA  . VAL A 1 62  ? 32.597 8.408  36.231  1.00 30.64  ? 93   VAL A CA  1 
ATOM   171  C C   . VAL A 1 62  ? 33.847 9.278  36.238  1.00 38.43  ? 93   VAL A C   1 
ATOM   172  O O   . VAL A 1 62  ? 34.367 9.660  35.183  1.00 32.57  ? 93   VAL A O   1 
ATOM   173  C CB  . VAL A 1 62  ? 31.346 9.221  36.613  1.00 33.48  ? 93   VAL A CB  1 
ATOM   174  C CG1 . VAL A 1 62  ? 31.224 10.448 35.725  1.00 37.95  ? 93   VAL A CG1 1 
ATOM   175  C CG2 . VAL A 1 62  ? 30.098 8.356  36.517  1.00 30.37  ? 93   VAL A CG2 1 
ATOM   176  N N   . VAL A 1 63  ? 34.347 9.606  37.432  1.00 30.30  ? 94   VAL A N   1 
ATOM   177  C CA  . VAL A 1 63  ? 35.538 10.446 37.522  1.00 38.83  ? 94   VAL A CA  1 
ATOM   178  C C   . VAL A 1 63  ? 36.703 9.788  36.794  1.00 38.23  ? 94   VAL A C   1 
ATOM   179  O O   . VAL A 1 63  ? 37.436 10.443 36.042  1.00 31.20  ? 94   VAL A O   1 
ATOM   180  C CB  . VAL A 1 63  ? 35.881 10.740 38.996  1.00 39.40  ? 94   VAL A CB  1 
ATOM   181  C CG1 . VAL A 1 63  ? 37.261 11.360 39.102  1.00 43.75  ? 94   VAL A CG1 1 
ATOM   182  C CG2 . VAL A 1 63  ? 34.842 11.668 39.618  1.00 37.76  ? 94   VAL A CG2 1 
ATOM   183  N N   . ALA A 1 64  ? 36.883 8.480  36.988  1.00 32.30  ? 95   ALA A N   1 
ATOM   184  C CA  . ALA A 1 64  ? 37.983 7.779  36.333  1.00 31.29  ? 95   ALA A CA  1 
ATOM   185  C C   . ALA A 1 64  ? 37.822 7.779  34.817  1.00 36.37  ? 95   ALA A C   1 
ATOM   186  O O   . ALA A 1 64  ? 38.809 7.907  34.083  1.00 44.94  ? 95   ALA A O   1 
ATOM   187  C CB  . ALA A 1 64  ? 38.074 6.346  36.856  1.00 37.50  ? 95   ALA A CB  1 
ATOM   188  N N   . LEU A 1 65  ? 36.591 7.621  34.328  1.00 40.06  ? 96   LEU A N   1 
ATOM   189  C CA  . LEU A 1 65  ? 36.370 7.570  32.886  1.00 37.89  ? 96   LEU A CA  1 
ATOM   190  C C   . LEU A 1 65  ? 36.704 8.906  32.236  1.00 35.64  ? 96   LEU A C   1 
ATOM   191  O O   . LEU A 1 65  ? 37.409 8.959  31.221  1.00 37.77  ? 96   LEU A O   1 
ATOM   192  C CB  . LEU A 1 65  ? 34.919 7.178  32.593  1.00 31.95  ? 96   LEU A CB  1 
ATOM   193  C CG  . LEU A 1 65  ? 34.517 5.746  32.961  1.00 38.36  ? 96   LEU A CG  1 
ATOM   194  C CD1 . LEU A 1 65  ? 33.031 5.506  32.726  1.00 37.45  ? 96   LEU A CD1 1 
ATOM   195  C CD2 . LEU A 1 65  ? 35.334 4.743  32.180  1.00 34.71  ? 96   LEU A CD2 1 
ATOM   196  N N   . ILE A 1 66  ? 36.204 10.000 32.810  1.00 35.61  ? 97   ILE A N   1 
ATOM   197  C CA  . ILE A 1 66  ? 36.445 11.317 32.232  1.00 45.09  ? 97   ILE A CA  1 
ATOM   198  C C   . ILE A 1 66  ? 37.922 11.675 32.319  1.00 48.86  ? 97   ILE A C   1 
ATOM   199  O O   . ILE A 1 66  ? 38.496 12.236 31.378  1.00 61.03  ? 97   ILE A O   1 
ATOM   200  C CB  . ILE A 1 66  ? 35.557 12.365 32.928  1.00 44.91  ? 97   ILE A CB  1 
ATOM   201  C CG1 . ILE A 1 66  ? 34.083 12.092 32.599  1.00 40.21  ? 97   ILE A CG1 1 
ATOM   202  C CG2 . ILE A 1 66  ? 35.978 13.772 32.519  1.00 59.67  ? 97   ILE A CG2 1 
ATOM   203  C CD1 . ILE A 1 66  ? 33.089 12.998 33.302  1.00 43.93  ? 97   ILE A CD1 1 
ATOM   204  N N   . ALA A 1 67  ? 38.569 11.327 33.433  1.00 52.08  ? 98   ALA A N   1 
ATOM   205  C CA  . ALA A 1 67  ? 39.962 11.709 33.638  1.00 44.37  ? 98   ALA A CA  1 
ATOM   206  C C   . ALA A 1 67  ? 40.890 11.015 32.648  1.00 51.43  ? 98   ALA A C   1 
ATOM   207  O O   . ALA A 1 67  ? 41.843 11.626 32.150  1.00 50.41  ? 98   ALA A O   1 
ATOM   208  C CB  . ALA A 1 67  ? 40.382 11.390 35.072  1.00 39.53  ? 98   ALA A CB  1 
ATOM   209  N N   . SER A 1 68  ? 40.643 9.741  32.361  1.00 59.93  ? 99   SER A N   1 
ATOM   210  C CA  . SER A 1 68  ? 41.522 8.957  31.506  1.00 48.51  ? 99   SER A CA  1 
ATOM   211  C C   . SER A 1 68  ? 41.108 8.987  30.040  1.00 48.24  ? 99   SER A C   1 
ATOM   212  O O   . SER A 1 68  ? 41.623 8.190  29.251  1.00 50.56  ? 99   SER A O   1 
ATOM   213  C CB  . SER A 1 68  ? 41.573 7.508  31.997  1.00 43.00  ? 99   SER A CB  1 
ATOM   214  O OG  . SER A 1 68  ? 40.283 6.923  31.981  1.00 58.08  ? 99   SER A OG  1 
ATOM   215  N N   . THR A 1 69  ? 40.203 9.884  29.657  1.00 50.80  ? 100  THR A N   1 
ATOM   216  C CA  . THR A 1 69  ? 39.692 9.953  28.288  1.00 59.53  ? 100  THR A CA  1 
ATOM   217  C C   . THR A 1 69  ? 39.884 11.371 27.764  1.00 59.28  ? 100  THR A C   1 
ATOM   218  O O   . THR A 1 69  ? 39.078 12.265 28.075  1.00 58.30  ? 100  THR A O   1 
ATOM   219  C CB  . THR A 1 69  ? 38.222 9.549  28.227  1.00 60.20  ? 100  THR A CB  1 
ATOM   220  O OG1 . THR A 1 69  ? 38.044 8.286  28.881  1.00 49.64  ? 100  THR A OG1 1 
ATOM   221  C CG2 . THR A 1 69  ? 37.757 9.436  26.781  1.00 51.79  ? 100  THR A CG2 1 
ATOM   222  N N   . PRO A 1 70  ? 40.930 11.619 26.969  1.00 62.68  ? 101  PRO A N   1 
ATOM   223  C CA  . PRO A 1 70  ? 41.164 12.989 26.482  1.00 70.45  ? 101  PRO A CA  1 
ATOM   224  C C   . PRO A 1 70  ? 39.992 13.580 25.711  1.00 63.63  ? 101  PRO A C   1 
ATOM   225  O O   . PRO A 1 70  ? 39.830 14.807 25.689  1.00 67.31  ? 101  PRO A O   1 
ATOM   226  C CB  . PRO A 1 70  ? 42.404 12.833 25.590  1.00 85.13  ? 101  PRO A CB  1 
ATOM   227  C CG  . PRO A 1 70  ? 43.093 11.609 26.101  1.00 60.70  ? 101  PRO A CG  1 
ATOM   228  C CD  . PRO A 1 70  ? 42.001 10.692 26.560  1.00 66.83  ? 101  PRO A CD  1 
ATOM   229  N N   . ALA A 1 71  ? 39.166 12.748 25.074  1.00 53.59  ? 102  ALA A N   1 
ATOM   230  C CA  . ALA A 1 71  ? 38.039 13.263 24.305  1.00 60.36  ? 102  ALA A CA  1 
ATOM   231  C C   . ALA A 1 71  ? 36.993 13.950 25.177  1.00 80.98  ? 102  ALA A C   1 
ATOM   232  O O   . ALA A 1 71  ? 36.208 14.752 24.660  1.00 72.28  ? 102  ALA A O   1 
ATOM   233  C CB  . ALA A 1 71  ? 37.378 12.130 23.518  1.00 58.99  ? 102  ALA A CB  1 
ATOM   234  N N   . LEU A 1 72  ? 36.961 13.659 26.474  1.00 59.99  ? 103  LEU A N   1 
ATOM   235  C CA  . LEU A 1 72  ? 35.923 14.186 27.361  1.00 51.68  ? 103  LEU A CA  1 
ATOM   236  C C   . LEU A 1 72  ? 36.429 15.428 28.094  1.00 47.17  ? 103  LEU A C   1 
ATOM   237  O O   . LEU A 1 72  ? 36.557 15.461 29.319  1.00 54.62  ? 103  LEU A O   1 
ATOM   238  C CB  . LEU A 1 72  ? 35.470 13.102 28.337  1.00 47.00  ? 103  LEU A CB  1 
ATOM   239  C CG  . LEU A 1 72  ? 35.079 11.769 27.687  1.00 54.64  ? 103  LEU A CG  1 
ATOM   240  C CD1 . LEU A 1 72  ? 34.669 10.730 28.719  1.00 51.88  ? 103  LEU A CD1 1 
ATOM   241  C CD2 . LEU A 1 72  ? 33.961 11.968 26.687  1.00 70.20  ? 103  LEU A CD2 1 
ATOM   242  N N   . ARG A 1 73  ? 36.709 16.470 27.305  1.00 40.37  ? 104  ARG A N   1 
ATOM   243  C CA  . ARG A 1 73  ? 37.258 17.719 27.820  1.00 53.99  ? 104  ARG A CA  1 
ATOM   244  C C   . ARG A 1 73  ? 36.458 18.937 27.365  1.00 51.11  ? 104  ARG A C   1 
ATOM   245  O O   . ARG A 1 73  ? 36.920 20.070 27.545  1.00 48.27  ? 104  ARG A O   1 
ATOM   246  C CB  . ARG A 1 73  ? 38.726 17.873 27.398  1.00 56.69  ? 104  ARG A CB  1 
ATOM   247  C CG  . ARG A 1 73  ? 39.653 16.787 27.942  1.00 55.91  ? 104  ARG A CG  1 
ATOM   248  C CD  . ARG A 1 73  ? 39.849 16.900 29.445  1.00 64.18  ? 104  ARG A CD  1 
ATOM   249  N NE  . ARG A 1 73  ? 39.778 15.596 30.094  1.00 76.68  ? 104  ARG A NE  1 
ATOM   250  C CZ  . ARG A 1 73  ? 40.781 14.731 30.155  1.00 72.28  ? 104  ARG A CZ  1 
ATOM   251  N NH1 . ARG A 1 73  ? 41.965 15.002 29.628  1.00 83.61  ? 104  ARG A NH1 1 
ATOM   252  N NH2 . ARG A 1 73  ? 40.591 13.561 30.756  1.00 69.93  ? 104  ARG A NH2 1 
ATOM   253  N N   . THR A 1 74  ? 35.278 18.737 26.785  1.00 42.13  ? 105  THR A N   1 
ATOM   254  C CA  . THR A 1 74  ? 34.416 19.849 26.431  1.00 43.94  ? 105  THR A CA  1 
ATOM   255  C C   . THR A 1 74  ? 33.784 20.448 27.686  1.00 41.19  ? 105  THR A C   1 
ATOM   256  O O   . THR A 1 74  ? 33.778 19.824 28.750  1.00 40.12  ? 105  THR A O   1 
ATOM   257  C CB  . THR A 1 74  ? 33.319 19.389 25.477  1.00 40.35  ? 105  THR A CB  1 
ATOM   258  O OG1 . THR A 1 74  ? 32.468 18.453 26.152  1.00 36.34  ? 105  THR A OG1 1 
ATOM   259  C CG2 . THR A 1 74  ? 33.920 18.725 24.244  1.00 41.61  ? 105  THR A CG2 1 
ATOM   260  N N   . PRO A 1 75  ? 33.245 21.666 27.586  1.00 38.86  ? 106  PRO A N   1 
ATOM   261  C CA  . PRO A 1 75  ? 32.530 22.239 28.738  1.00 39.46  ? 106  PRO A CA  1 
ATOM   262  C C   . PRO A 1 75  ? 31.521 21.284 29.350  1.00 36.30  ? 106  PRO A C   1 
ATOM   263  O O   . PRO A 1 75  ? 31.476 21.130 30.576  1.00 34.26  ? 106  PRO A O   1 
ATOM   264  C CB  . PRO A 1 75  ? 31.859 23.480 28.136  1.00 43.09  ? 106  PRO A CB  1 
ATOM   265  C CG  . PRO A 1 75  ? 32.761 23.884 27.026  1.00 41.51  ? 106  PRO A CG  1 
ATOM   266  C CD  . PRO A 1 75  ? 33.322 22.609 26.455  1.00 51.31  ? 106  PRO A CD  1 
ATOM   267  N N   . MET A 1 76  ? 30.706 20.633 28.519  1.00 35.43  ? 107  MET A N   1 
ATOM   268  C CA  . MET A 1 76  ? 29.723 19.682 29.024  1.00 41.90  ? 107  MET A CA  1 
ATOM   269  C C   . MET A 1 76  ? 30.369 18.648 29.942  1.00 33.07  ? 107  MET A C   1 
ATOM   270  O O   . MET A 1 76  ? 29.853 18.354 31.026  1.00 34.68  ? 107  MET A O   1 
ATOM   271  C CB  . MET A 1 76  ? 29.023 18.994 27.850  1.00 48.95  ? 107  MET A CB  1 
ATOM   272  C CG  . MET A 1 76  ? 27.861 18.101 28.253  1.00 58.43  ? 107  MET A CG  1 
ATOM   273  S SD  . MET A 1 76  ? 27.569 16.763 27.079  1.00 83.33  ? 107  MET A SD  1 
ATOM   274  C CE  . MET A 1 76  ? 27.410 17.660 25.536  1.00 62.68  ? 107  MET A CE  1 
ATOM   275  N N   . PHE A 1 77  ? 31.499 18.075 29.525  1.00 32.61  ? 108  PHE A N   1 
ATOM   276  C CA  . PHE A 1 77  ? 32.103 17.014 30.328  1.00 37.68  ? 108  PHE A CA  1 
ATOM   277  C C   . PHE A 1 77  ? 32.898 17.559 31.507  1.00 35.20  ? 108  PHE A C   1 
ATOM   278  O O   . PHE A 1 77  ? 33.028 16.877 32.531  1.00 32.64  ? 108  PHE A O   1 
ATOM   279  C CB  . PHE A 1 77  ? 32.978 16.124 29.448  1.00 40.54  ? 108  PHE A CB  1 
ATOM   280  C CG  . PHE A 1 77  ? 32.187 15.269 28.513  1.00 42.89  ? 108  PHE A CG  1 
ATOM   281  C CD1 . PHE A 1 77  ? 31.366 14.268 29.005  1.00 53.41  ? 108  PHE A CD1 1 
ATOM   282  C CD2 . PHE A 1 77  ? 32.237 15.481 27.148  1.00 40.57  ? 108  PHE A CD2 1 
ATOM   283  C CE1 . PHE A 1 77  ? 30.620 13.486 28.151  1.00 56.45  ? 108  PHE A CE1 1 
ATOM   284  C CE2 . PHE A 1 77  ? 31.493 14.702 26.289  1.00 46.95  ? 108  PHE A CE2 1 
ATOM   285  C CZ  . PHE A 1 77  ? 30.683 13.702 26.791  1.00 47.82  ? 108  PHE A CZ  1 
ATOM   286  N N   . VAL A 1 78  ? 33.430 18.775 31.397  1.00 28.51  ? 109  VAL A N   1 
ATOM   287  C CA  . VAL A 1 78  ? 34.000 19.417 32.575  1.00 25.91  ? 109  VAL A CA  1 
ATOM   288  C C   . VAL A 1 78  ? 32.928 19.576 33.641  1.00 28.45  ? 109  VAL A C   1 
ATOM   289  O O   . VAL A 1 78  ? 33.196 19.448 34.842  1.00 29.33  ? 109  VAL A O   1 
ATOM   290  C CB  . VAL A 1 78  ? 34.636 20.768 32.196  1.00 34.79  ? 109  VAL A CB  1 
ATOM   291  C CG1 . VAL A 1 78  ? 35.097 21.502 33.439  1.00 40.50  ? 109  VAL A CG1 1 
ATOM   292  C CG2 . VAL A 1 78  ? 35.810 20.549 31.260  1.00 41.68  ? 109  VAL A CG2 1 
ATOM   293  N N   . LEU A 1 79  ? 31.692 19.846 33.219  1.00 28.76  ? 110  LEU A N   1 
ATOM   294  C CA  . LEU A 1 79  ? 30.606 20.002 34.179  1.00 29.81  ? 110  LEU A CA  1 
ATOM   295  C C   . LEU A 1 79  ? 30.174 18.658 34.747  1.00 27.85  ? 110  LEU A C   1 
ATOM   296  O O   . LEU A 1 79  ? 29.920 18.545 35.950  1.00 29.96  ? 110  LEU A O   1 
ATOM   297  C CB  . LEU A 1 79  ? 29.427 20.713 33.522  1.00 32.35  ? 110  LEU A CB  1 
ATOM   298  C CG  . LEU A 1 79  ? 29.712 22.170 33.155  1.00 33.45  ? 110  LEU A CG  1 
ATOM   299  C CD1 . LEU A 1 79  ? 28.686 22.702 32.173  1.00 40.08  ? 110  LEU A CD1 1 
ATOM   300  C CD2 . LEU A 1 79  ? 29.734 23.011 34.415  1.00 31.44  ? 110  LEU A CD2 1 
ATOM   301  N N   . VAL A 1 80  ? 30.091 17.625 33.908  1.00 26.92  ? 111  VAL A N   1 
ATOM   302  C CA  . VAL A 1 80  ? 29.744 16.303 34.422  1.00 30.92  ? 111  VAL A CA  1 
ATOM   303  C C   . VAL A 1 80  ? 30.808 15.825 35.400  1.00 26.72  ? 111  VAL A C   1 
ATOM   304  O O   . VAL A 1 80  ? 30.497 15.226 36.436  1.00 35.43  ? 111  VAL A O   1 
ATOM   305  C CB  . VAL A 1 80  ? 29.545 15.314 33.261  1.00 33.92  ? 111  VAL A CB  1 
ATOM   306  C CG1 . VAL A 1 80  ? 29.365 13.898 33.783  1.00 32.93  ? 111  VAL A CG1 1 
ATOM   307  C CG2 . VAL A 1 80  ? 28.341 15.725 32.445  1.00 38.38  ? 111  VAL A CG2 1 
ATOM   308  N N   . GLY A 1 81  ? 32.076 16.103 35.100  1.00 29.57  ? 112  GLY A N   1 
ATOM   309  C CA  . GLY A 1 81  ? 33.144 15.700 35.999  1.00 29.37  ? 112  GLY A CA  1 
ATOM   310  C C   . GLY A 1 81  ? 33.081 16.408 37.337  1.00 29.37  ? 112  GLY A C   1 
ATOM   311  O O   . GLY A 1 81  ? 33.401 15.820 38.374  1.00 28.34  ? 112  GLY A O   1 
ATOM   312  N N   . SER A 1 82  ? 32.662 17.674 37.333  1.00 32.12  ? 113  SER A N   1 
ATOM   313  C CA  . SER A 1 82  ? 32.470 18.398 38.583  1.00 26.53  ? 113  SER A CA  1 
ATOM   314  C C   . SER A 1 82  ? 31.343 17.780 39.401  1.00 33.28  ? 113  SER A C   1 
ATOM   315  O O   . SER A 1 82  ? 31.495 17.548 40.605  1.00 30.33  ? 113  SER A O   1 
ATOM   316  C CB  . SER A 1 82  ? 32.189 19.872 38.288  1.00 31.18  ? 113  SER A CB  1 
ATOM   317  O OG  . SER A 1 82  ? 31.831 20.576 39.463  1.00 28.12  ? 113  SER A OG  1 
ATOM   318  N N   . LEU A 1 83  ? 30.203 17.499 38.763  1.00 24.89  ? 114  LEU A N   1 
ATOM   319  C CA  . LEU A 1 83  ? 29.099 16.866 39.478  1.00 27.38  ? 114  LEU A CA  1 
ATOM   320  C C   . LEU A 1 83  ? 29.528 15.527 40.066  1.00 29.87  ? 114  LEU A C   1 
ATOM   321  O O   . LEU A 1 83  ? 29.254 15.231 41.236  1.00 27.91  ? 114  LEU A O   1 
ATOM   322  C CB  . LEU A 1 83  ? 27.903 16.680 38.543  1.00 27.75  ? 114  LEU A CB  1 
ATOM   323  C CG  . LEU A 1 83  ? 26.659 16.017 39.147  1.00 30.69  ? 114  LEU A CG  1 
ATOM   324  C CD1 . LEU A 1 83  ? 26.051 16.879 40.246  1.00 29.39  ? 114  LEU A CD1 1 
ATOM   325  C CD2 . LEU A 1 83  ? 25.625 15.729 38.076  1.00 39.09  ? 114  LEU A CD2 1 
ATOM   326  N N   . ALA A 1 84  ? 30.201 14.702 39.260  1.00 26.82  ? 115  ALA A N   1 
ATOM   327  C CA  . ALA A 1 84  ? 30.622 13.384 39.721  1.00 29.00  ? 115  ALA A CA  1 
ATOM   328  C C   . ALA A 1 84  ? 31.631 13.484 40.857  1.00 31.54  ? 115  ALA A C   1 
ATOM   329  O O   . ALA A 1 84  ? 31.606 12.671 41.787  1.00 30.27  ? 115  ALA A O   1 
ATOM   330  C CB  . ALA A 1 84  ? 31.212 12.590 38.556  1.00 25.41  ? 115  ALA A CB  1 
ATOM   331  N N   . THR A 1 85  ? 32.540 14.461 40.793  1.00 29.19  ? 116  THR A N   1 
ATOM   332  C CA  . THR A 1 85  ? 33.509 14.629 41.871  1.00 24.61  ? 116  THR A CA  1 
ATOM   333  C C   . THR A 1 85  ? 32.812 15.022 43.163  1.00 31.07  ? 116  THR A C   1 
ATOM   334  O O   . THR A 1 85  ? 33.124 14.489 44.234  1.00 27.66  ? 116  THR A O   1 
ATOM   335  C CB  . THR A 1 85  ? 34.552 15.681 41.491  1.00 31.77  ? 116  THR A CB  1 
ATOM   336  O OG1 . THR A 1 85  ? 35.276 15.247 40.334  1.00 32.58  ? 116  THR A OG1 1 
ATOM   337  C CG2 . THR A 1 85  ? 35.528 15.921 42.639  1.00 31.03  ? 116  THR A CG2 1 
ATOM   338  N N   . ALA A 1 86  ? 31.865 15.956 43.075  1.00 28.32  ? 117  ALA A N   1 
ATOM   339  C CA  . ALA A 1 86  ? 31.122 16.388 44.251  1.00 28.55  ? 117  ALA A CA  1 
ATOM   340  C C   . ALA A 1 86  ? 30.345 15.230 44.865  1.00 29.12  ? 117  ALA A C   1 
ATOM   341  O O   . ALA A 1 86  ? 30.355 15.040 46.087  1.00 31.28  ? 117  ALA A O   1 
ATOM   342  C CB  . ALA A 1 86  ? 30.181 17.529 43.869  1.00 26.19  ? 117  ALA A CB  1 
ATOM   343  N N   . ASP A 1 87  ? 29.661 14.443 44.032  1.00 26.43  ? 118  ASP A N   1 
ATOM   344  C CA  . ASP A 1 87  ? 28.929 13.293 44.553  1.00 25.56  ? 118  ASP A CA  1 
ATOM   345  C C   . ASP A 1 87  ? 29.882 12.243 45.111  1.00 29.93  ? 118  ASP A C   1 
ATOM   346  O O   . ASP A 1 87  ? 29.616 11.660 46.168  1.00 28.41  ? 118  ASP A O   1 
ATOM   347  C CB  . ASP A 1 87  ? 28.034 12.701 43.467  1.00 28.29  ? 118  ASP A CB  1 
ATOM   348  C CG  . ASP A 1 87  ? 26.849 13.602 43.130  1.00 48.05  ? 118  ASP A CG  1 
ATOM   349  O OD1 . ASP A 1 87  ? 26.429 14.393 44.007  1.00 42.07  ? 118  ASP A OD1 1 
ATOM   350  O OD2 . ASP A 1 87  ? 26.333 13.521 41.992  1.00 45.56  ? 118  ASP A OD2 1 
ATOM   351  N N   . LEU A 1 88  ? 31.004 11.997 44.430  1.00 31.00  ? 119  LEU A N   1 
ATOM   352  C CA  . LEU A 1 88  ? 32.032 11.132 45.002  1.00 26.58  ? 119  LEU A CA  1 
ATOM   353  C C   . LEU A 1 88  ? 32.446 11.619 46.384  1.00 30.48  ? 119  LEU A C   1 
ATOM   354  O O   . LEU A 1 88  ? 32.487 10.842 47.343  1.00 28.67  ? 119  LEU A O   1 
ATOM   355  C CB  . LEU A 1 88  ? 33.248 11.067 44.081  1.00 32.05  ? 119  LEU A CB  1 
ATOM   356  C CG  . LEU A 1 88  ? 34.476 10.366 44.669  1.00 34.81  ? 119  LEU A CG  1 
ATOM   357  C CD1 . LEU A 1 88  ? 34.163 8.935  45.090  1.00 31.48  ? 119  LEU A CD1 1 
ATOM   358  C CD2 . LEU A 1 88  ? 35.593 10.393 43.655  1.00 37.71  ? 119  LEU A CD2 1 
ATOM   359  N N   . LEU A 1 89  ? 32.754 12.912 46.505  1.00 27.38  ? 120  LEU A N   1 
ATOM   360  C CA  . LEU A 1 89  ? 33.175 13.441 47.796  1.00 28.48  ? 120  LEU A CA  1 
ATOM   361  C C   . LEU A 1 89  ? 32.076 13.285 48.837  1.00 28.73  ? 120  LEU A C   1 
ATOM   362  O O   . LEU A 1 89  ? 32.352 12.955 49.995  1.00 29.57  ? 120  LEU A O   1 
ATOM   363  C CB  . LEU A 1 89  ? 33.583 14.904 47.656  1.00 22.24  ? 120  LEU A CB  1 
ATOM   364  C CG  . LEU A 1 89  ? 34.885 15.124 46.888  1.00 28.37  ? 120  LEU A CG  1 
ATOM   365  C CD1 . LEU A 1 89  ? 35.091 16.602 46.624  1.00 31.08  ? 120  LEU A CD1 1 
ATOM   366  C CD2 . LEU A 1 89  ? 36.062 14.546 47.658  1.00 33.41  ? 120  LEU A CD2 1 
ATOM   367  N N   . ALA A 1 90  ? 30.821 13.505 48.444  1.00 28.57  ? 121  ALA A N   1 
ATOM   368  C CA  . ALA A 1 90  ? 29.722 13.353 49.391  1.00 28.11  ? 121  ALA A CA  1 
ATOM   369  C C   . ALA A 1 90  ? 29.565 11.900 49.827  1.00 33.53  ? 121  ALA A C   1 
ATOM   370  O O   . ALA A 1 90  ? 29.286 11.623 51.001  1.00 30.06  ? 121  ALA A O   1 
ATOM   371  C CB  . ALA A 1 90  ? 28.425 13.872 48.774  1.00 24.99  ? 121  ALA A CB  1 
ATOM   372  N N   . GLY A 1 91  ? 29.728 10.960 48.895  1.00 28.79  ? 122  GLY A N   1 
ATOM   373  C CA  . GLY A 1 91  ? 29.667 9.553  49.263  1.00 26.70  ? 122  GLY A CA  1 
ATOM   374  C C   . GLY A 1 91  ? 30.731 9.173  50.275  1.00 25.96  ? 122  GLY A C   1 
ATOM   375  O O   . GLY A 1 91  ? 30.430 8.621  51.335  1.00 30.35  ? 122  GLY A O   1 
ATOM   376  N N   . LEU A 1 92  ? 31.997 9.461  49.956  1.00 30.32  ? 123  LEU A N   1 
ATOM   377  C CA  . LEU A 1 92  ? 33.079 9.217  50.903  1.00 32.80  ? 123  LEU A CA  1 
ATOM   378  C C   . LEU A 1 92  ? 32.796 9.885  52.240  1.00 30.78  ? 123  LEU A C   1 
ATOM   379  O O   . LEU A 1 92  ? 33.092 9.324  53.300  1.00 31.58  ? 123  LEU A O   1 
ATOM   380  C CB  . LEU A 1 92  ? 34.402 9.730  50.335  1.00 34.79  ? 123  LEU A CB  1 
ATOM   381  C CG  . LEU A 1 92  ? 34.845 9.142  48.998  1.00 33.15  ? 123  LEU A CG  1 
ATOM   382  C CD1 . LEU A 1 92  ? 36.072 9.876  48.480  1.00 34.24  ? 123  LEU A CD1 1 
ATOM   383  C CD2 . LEU A 1 92  ? 35.121 7.661  49.157  1.00 36.93  ? 123  LEU A CD2 1 
ATOM   384  N N   . GLY A 1 93  ? 32.226 11.090 52.204  1.00 30.41  ? 124  GLY A N   1 
ATOM   385  C CA  . GLY A 1 93  ? 31.935 11.799 53.436  1.00 33.19  ? 124  GLY A CA  1 
ATOM   386  C C   . GLY A 1 93  ? 30.946 11.069 54.325  1.00 29.56  ? 124  GLY A C   1 
ATOM   387  O O   . GLY A 1 93  ? 31.080 11.080 55.549  1.00 31.35  ? 124  GLY A O   1 
ATOM   388  N N   . LEU A 1 94  ? 29.929 10.437 53.728  1.00 25.26  ? 125  LEU A N   1 
ATOM   389  C CA  . LEU A 1 94  ? 28.992 9.653  54.530  1.00 22.33  ? 125  LEU A CA  1 
ATOM   390  C C   . LEU A 1 94  ? 29.696 8.480  55.198  1.00 27.66  ? 125  LEU A C   1 
ATOM   391  O O   . LEU A 1 94  ? 29.421 8.160  56.360  1.00 32.32  ? 125  LEU A O   1 
ATOM   392  C CB  . LEU A 1 94  ? 27.837 9.161  53.664  1.00 27.79  ? 125  LEU A CB  1 
ATOM   393  C CG  . LEU A 1 94  ? 26.949 10.273 53.112  1.00 32.62  ? 125  LEU A CG  1 
ATOM   394  C CD1 . LEU A 1 94  ? 25.973 9.713  52.097  1.00 27.27  ? 125  LEU A CD1 1 
ATOM   395  C CD2 . LEU A 1 94  ? 26.224 10.964 54.259  1.00 32.02  ? 125  LEU A CD2 1 
ATOM   396  N N   . ILE A 1 95  ? 30.616 7.835  54.479  1.00 24.93  ? 126  ILE A N   1 
ATOM   397  C CA  . ILE A 1 95  ? 31.411 6.758  55.063  1.00 31.84  ? 126  ILE A CA  1 
ATOM   398  C C   . ILE A 1 95  ? 32.297 7.303  56.176  1.00 31.74  ? 126  ILE A C   1 
ATOM   399  O O   . ILE A 1 95  ? 32.384 6.729  57.268  1.00 30.94  ? 126  ILE A O   1 
ATOM   400  C CB  . ILE A 1 95  ? 32.252 6.066  53.974  1.00 34.79  ? 126  ILE A CB  1 
ATOM   401  C CG1 . ILE A 1 95  ? 31.348 5.511  52.866  1.00 37.76  ? 126  ILE A CG1 1 
ATOM   402  C CG2 . ILE A 1 95  ? 33.117 4.976  54.591  1.00 40.20  ? 126  ILE A CG2 1 
ATOM   403  C CD1 . ILE A 1 95  ? 32.110 5.003  51.649  1.00 36.73  ? 126  ILE A CD1 1 
ATOM   404  N N   . LEU A 1 96  ? 32.978 8.417  55.910  1.00 28.55  ? 127  LEU A N   1 
ATOM   405  C CA  . LEU A 1 96  ? 33.854 9.003  56.918  1.00 37.03  ? 127  LEU A CA  1 
ATOM   406  C C   . LEU A 1 96  ? 33.076 9.391  58.167  1.00 32.28  ? 127  LEU A C   1 
ATOM   407  O O   . LEU A 1 96  ? 33.551 9.196  59.292  1.00 36.58  ? 127  LEU A O   1 
ATOM   408  C CB  . LEU A 1 96  ? 34.570 10.222 56.340  1.00 37.66  ? 127  LEU A CB  1 
ATOM   409  C CG  . LEU A 1 96  ? 35.695 9.937  55.344  1.00 43.94  ? 127  LEU A CG  1 
ATOM   410  C CD1 . LEU A 1 96  ? 36.165 11.224 54.683  1.00 55.10  ? 127  LEU A CD1 1 
ATOM   411  C CD2 . LEU A 1 96  ? 36.853 9.241  56.038  1.00 53.73  ? 127  LEU A CD2 1 
ATOM   412  N N   . HIS A 1 97  ? 31.879 9.947  57.988  1.00 38.03  ? 128  HIS A N   1 
ATOM   413  C CA  . HIS A 1 97  ? 31.054 10.300 59.136  1.00 33.20  ? 128  HIS A CA  1 
ATOM   414  C C   . HIS A 1 97  ? 30.785 9.083  60.011  1.00 33.43  ? 128  HIS A C   1 
ATOM   415  O O   . HIS A 1 97  ? 30.837 9.171  61.242  1.00 32.06  ? 128  HIS A O   1 
ATOM   416  C CB  . HIS A 1 97  ? 29.745 10.926 58.657  1.00 33.85  ? 128  HIS A CB  1 
ATOM   417  C CG  . HIS A 1 97  ? 28.890 11.454 59.764  1.00 40.86  ? 128  HIS A CG  1 
ATOM   418  N ND1 . HIS A 1 97  ? 27.823 10.750 60.281  1.00 47.11  ? 128  HIS A ND1 1 
ATOM   419  C CD2 . HIS A 1 97  ? 28.949 12.613 60.460  1.00 44.58  ? 128  HIS A CD2 1 
ATOM   420  C CE1 . HIS A 1 97  ? 27.262 11.454 61.247  1.00 47.46  ? 128  HIS A CE1 1 
ATOM   421  N NE2 . HIS A 1 97  ? 27.925 12.589 61.375  1.00 48.99  ? 128  HIS A NE2 1 
ATOM   422  N N   . PHE A 1 98  ? 30.493 7.935  59.395  1.00 31.88  ? 129  PHE A N   1 
ATOM   423  C CA  . PHE A 1 98  ? 30.302 6.717  60.175  1.00 32.59  ? 129  PHE A CA  1 
ATOM   424  C C   . PHE A 1 98  ? 31.584 6.318  60.895  1.00 31.89  ? 129  PHE A C   1 
ATOM   425  O O   . PHE A 1 98  ? 31.553 5.946  62.074  1.00 35.42  ? 129  PHE A O   1 
ATOM   426  C CB  . PHE A 1 98  ? 29.829 5.581  59.269  1.00 38.27  ? 129  PHE A CB  1 
ATOM   427  C CG  . PHE A 1 98  ? 29.468 4.330  60.014  1.00 36.08  ? 129  PHE A CG  1 
ATOM   428  C CD1 . PHE A 1 98  ? 30.449 3.435  60.414  1.00 35.07  ? 129  PHE A CD1 1 
ATOM   429  C CD2 . PHE A 1 98  ? 28.147 4.051  60.318  1.00 33.98  ? 129  PHE A CD2 1 
ATOM   430  C CE1 . PHE A 1 98  ? 30.119 2.288  61.106  1.00 34.84  ? 129  PHE A CE1 1 
ATOM   431  C CE2 . PHE A 1 98  ? 27.809 2.901  61.012  1.00 34.96  ? 129  PHE A CE2 1 
ATOM   432  C CZ  . PHE A 1 98  ? 28.796 2.020  61.406  1.00 48.02  ? 129  PHE A CZ  1 
ATOM   433  N N   . VAL A 1 99  ? 32.720 6.393  60.198  1.00 35.77  ? 130  VAL A N   1 
ATOM   434  C CA  . VAL A 1 99  ? 33.992 5.953  60.768  1.00 33.34  ? 130  VAL A CA  1 
ATOM   435  C C   . VAL A 1 99  ? 34.311 6.732  62.037  1.00 35.43  ? 130  VAL A C   1 
ATOM   436  O O   . VAL A 1 99  ? 34.673 6.155  63.068  1.00 34.33  ? 130  VAL A O   1 
ATOM   437  C CB  . VAL A 1 99  ? 35.119 6.101  59.729  1.00 42.66  ? 130  VAL A CB  1 
ATOM   438  C CG1 . VAL A 1 99  ? 36.489 6.004  60.395  1.00 39.11  ? 130  VAL A CG1 1 
ATOM   439  C CG2 . VAL A 1 99  ? 34.977 5.049  58.650  1.00 37.11  ? 130  VAL A CG2 1 
ATOM   440  N N   . PHE A 1 100 ? 34.206 8.054  61.975  1.00 36.96  ? 131  PHE A N   1 
ATOM   441  C CA  . PHE A 1 100 ? 34.591 8.894  63.099  1.00 33.57  ? 131  PHE A CA  1 
ATOM   442  C C   . PHE A 1 100 ? 33.463 9.084  64.093  1.00 42.61  ? 131  PHE A C   1 
ATOM   443  O O   . PHE A 1 100 ? 33.625 9.832  65.062  1.00 43.56  ? 131  PHE A O   1 
ATOM   444  C CB  . PHE A 1 100 ? 35.098 10.237 62.589  1.00 33.92  ? 131  PHE A CB  1 
ATOM   445  C CG  . PHE A 1 100 ? 36.426 10.135 61.918  1.00 34.42  ? 131  PHE A CG  1 
ATOM   446  C CD1 . PHE A 1 100 ? 37.580 10.008 62.671  1.00 45.70  ? 131  PHE A CD1 1 
ATOM   447  C CD2 . PHE A 1 100 ? 36.526 10.125 60.540  1.00 37.50  ? 131  PHE A CD2 1 
ATOM   448  C CE1 . PHE A 1 100 ? 38.811 9.898  62.062  1.00 51.13  ? 131  PHE A CE1 1 
ATOM   449  C CE2 . PHE A 1 100 ? 37.755 10.017 59.925  1.00 46.01  ? 131  PHE A CE2 1 
ATOM   450  C CZ  . PHE A 1 100 ? 38.899 9.901  60.688  1.00 45.23  ? 131  PHE A CZ  1 
ATOM   451  N N   . GLN A 1 101 ? 32.334 8.421  63.876  1.00 41.44  ? 132  GLN A N   1 
ATOM   452  C CA  . GLN A 1 101 ? 31.311 8.293  64.900  1.00 38.35  ? 132  GLN A CA  1 
ATOM   453  C C   . GLN A 1 101 ? 31.476 7.009  65.707  1.00 38.79  ? 132  GLN A C   1 
ATOM   454  O O   . GLN A 1 101 ? 31.357 7.034  66.936  1.00 39.77  ? 132  GLN A O   1 
ATOM   455  C CB  . GLN A 1 101 ? 29.929 8.337  64.248  1.00 41.09  ? 132  GLN A CB  1 
ATOM   456  C CG  . GLN A 1 101 ? 28.774 8.291  65.215  1.00 51.75  ? 132  GLN A CG  1 
ATOM   457  C CD  . GLN A 1 101 ? 27.470 8.671  64.550  1.00 66.58  ? 132  GLN A CD  1 
ATOM   458  O OE1 . GLN A 1 101 ? 27.411 8.855  63.332  1.00 68.79  ? 132  GLN A OE1 1 
ATOM   459  N NE2 . GLN A 1 101 ? 26.415 8.798  65.346  1.00 82.50  ? 132  GLN A NE2 1 
ATOM   460  N N   . TYR A 1 102 ? 31.788 5.891  65.045  1.00 32.41  ? 133  TYR A N   1 
ATOM   461  C CA  . TYR A 1 102 ? 31.782 4.581  65.687  1.00 33.98  ? 133  TYR A CA  1 
ATOM   462  C C   . TYR A 1 102 ? 33.143 3.905  65.782  1.00 38.99  ? 133  TYR A C   1 
ATOM   463  O O   . TYR A 1 102 ? 33.342 3.096  66.689  1.00 37.98  ? 133  TYR A O   1 
ATOM   464  C CB  . TYR A 1 102 ? 30.831 3.636  64.942  1.00 36.31  ? 133  TYR A CB  1 
ATOM   465  C CG  . TYR A 1 102 ? 29.376 4.016  65.051  1.00 34.65  ? 133  TYR A CG  1 
ATOM   466  C CD1 . TYR A 1 102 ? 28.664 3.771  66.215  1.00 33.45  ? 133  TYR A CD1 1 
ATOM   467  C CD2 . TYR A 1 102 ? 28.710 4.610  63.987  1.00 34.97  ? 133  TYR A CD2 1 
ATOM   468  C CE1 . TYR A 1 102 ? 27.330 4.114  66.319  1.00 37.80  ? 133  TYR A CE1 1 
ATOM   469  C CE2 . TYR A 1 102 ? 27.378 4.954  64.081  1.00 40.77  ? 133  TYR A CE2 1 
ATOM   470  C CZ  . TYR A 1 102 ? 26.691 4.703  65.247  1.00 38.69  ? 133  TYR A CZ  1 
ATOM   471  O OH  . TYR A 1 102 ? 25.362 5.044  65.341  1.00 39.34  ? 133  TYR A OH  1 
ATOM   472  N N   . LEU A 1 103 ? 34.077 4.186  64.877  1.00 40.42  ? 134  LEU A N   1 
ATOM   473  C CA  . LEU A 1 103 ? 35.360 3.488  64.870  1.00 41.95  ? 134  LEU A CA  1 
ATOM   474  C C   . LEU A 1 103 ? 36.471 4.296  65.511  1.00 39.41  ? 134  LEU A C   1 
ATOM   475  O O   . LEU A 1 103 ? 37.363 3.725  66.143  1.00 41.67  ? 134  LEU A O   1 
ATOM   476  C CB  . LEU A 1 103 ? 35.771 3.138  63.437  1.00 36.95  ? 134  LEU A CB  1 
ATOM   477  C CG  . LEU A 1 103 ? 34.770 2.285  62.661  1.00 40.07  ? 134  LEU A CG  1 
ATOM   478  C CD1 . LEU A 1 103 ? 35.335 1.929  61.299  1.00 41.43  ? 134  LEU A CD1 1 
ATOM   479  C CD2 . LEU A 1 103 ? 34.419 1.029  63.450  1.00 40.82  ? 134  LEU A CD2 1 
ATOM   480  N N   . VAL A 1 104 ? 36.434 5.611  65.335  1.00 38.84  ? 135  VAL A N   1 
ATOM   481  C CA  . VAL A 1 104 ? 37.366 6.539  65.961  1.00 39.10  ? 135  VAL A CA  1 
ATOM   482  C C   . VAL A 1 104 ? 36.515 7.642  66.575  1.00 49.39  ? 135  VAL A C   1 
ATOM   483  O O   . VAL A 1 104 ? 36.446 8.748  66.018  1.00 44.98  ? 135  VAL A O   1 
ATOM   484  C CB  . VAL A 1 104 ? 38.367 7.110  64.946  1.00 51.79  ? 135  VAL A CB  1 
ATOM   485  C CG1 . VAL A 1 104 ? 39.333 8.060  65.638  1.00 60.63  ? 135  VAL A CG1 1 
ATOM   486  C CG2 . VAL A 1 104 ? 39.108 5.990  64.226  1.00 59.02  ? 135  VAL A CG2 1 
ATOM   487  N N   . PRO A 1 105 ? 35.823 7.382  67.687  1.00 47.19  ? 136  PRO A N   1 
ATOM   488  C CA  . PRO A 1 105 ? 34.958 8.415  68.272  1.00 48.88  ? 136  PRO A CA  1 
ATOM   489  C C   . PRO A 1 105 ? 35.701 9.720  68.490  1.00 58.46  ? 136  PRO A C   1 
ATOM   490  O O   . PRO A 1 105 ? 36.648 9.780  69.281  1.00 54.86  ? 136  PRO A O   1 
ATOM   491  C CB  . PRO A 1 105 ? 34.512 7.791  69.600  1.00 59.35  ? 136  PRO A CB  1 
ATOM   492  C CG  . PRO A 1 105 ? 34.647 6.321  69.394  1.00 48.10  ? 136  PRO A CG  1 
ATOM   493  C CD  . PRO A 1 105 ? 35.817 6.139  68.478  1.00 51.14  ? 136  PRO A CD  1 
ATOM   494  N N   . SER A 1 106 ? 35.290 10.768 67.784  1.00 51.97  ? 137  SER A N   1 
ATOM   495  C CA  . SER A 1 106 ? 35.975 12.054 67.867  1.00 61.30  ? 137  SER A CA  1 
ATOM   496  C C   . SER A 1 106 ? 34.962 13.147 67.567  1.00 70.91  ? 137  SER A C   1 
ATOM   497  O O   . SER A 1 106 ? 34.463 13.243 66.441  1.00 57.55  ? 137  SER A O   1 
ATOM   498  C CB  . SER A 1 106 ? 37.150 12.114 66.894  1.00 53.07  ? 137  SER A CB  1 
ATOM   499  O OG  . SER A 1 106 ? 37.830 13.353 66.992  1.00 66.74  ? 137  SER A OG  1 
ATOM   500  N N   . GLU A 1 107 ? 34.654 13.964 68.575  1.00 49.87  ? 138  GLU A N   1 
ATOM   501  C CA  . GLU A 1 107 ? 33.781 15.108 68.341  1.00 69.51  ? 138  GLU A CA  1 
ATOM   502  C C   . GLU A 1 107 ? 34.416 16.076 67.352  1.00 63.13  ? 138  GLU A C   1 
ATOM   503  O O   . GLU A 1 107 ? 33.748 16.571 66.436  1.00 49.77  ? 138  GLU A O   1 
ATOM   504  C CB  . GLU A 1 107 ? 33.469 15.806 69.667  1.00 64.99  ? 138  GLU A CB  1 
ATOM   505  C CG  . GLU A 1 107 ? 32.730 14.929 70.676  1.00 87.09  ? 138  GLU A CG  1 
ATOM   506  C CD  . GLU A 1 107 ? 31.319 14.576 70.235  1.00 104.04 ? 138  GLU A CD  1 
ATOM   507  O OE1 . GLU A 1 107 ? 30.873 15.079 69.180  1.00 94.68  ? 138  GLU A OE1 1 
ATOM   508  O OE2 . GLU A 1 107 ? 30.654 13.792 70.948  1.00 104.29 ? 138  GLU A OE2 1 
ATOM   509  N N   . THR A 1 108 ? 35.717 16.337 67.503  1.00 47.64  ? 139  THR A N   1 
ATOM   510  C CA  . THR A 1 108 ? 36.387 17.286 66.621  1.00 56.88  ? 139  THR A CA  1 
ATOM   511  C C   . THR A 1 108 ? 36.309 16.832 65.167  1.00 59.48  ? 139  THR A C   1 
ATOM   512  O O   . THR A 1 108 ? 35.917 17.604 64.285  1.00 49.38  ? 139  THR A O   1 
ATOM   513  C CB  . THR A 1 108 ? 37.845 17.473 67.049  1.00 52.22  ? 139  THR A CB  1 
ATOM   514  O OG1 . THR A 1 108 ? 38.576 16.257 66.839  1.00 72.50  ? 139  THR A OG1 1 
ATOM   515  C CG2 . THR A 1 108 ? 37.929 17.870 68.518  1.00 61.96  ? 139  THR A CG2 1 
ATOM   516  N N   . VAL A 1 109 ? 36.676 15.576 64.894  1.00 49.84  ? 140  VAL A N   1 
ATOM   517  C CA  . VAL A 1 109 ? 36.652 15.094 63.518  1.00 60.37  ? 140  VAL A CA  1 
ATOM   518  C C   . VAL A 1 109 ? 35.225 14.930 63.005  1.00 49.10  ? 140  VAL A C   1 
ATOM   519  O O   . VAL A 1 109 ? 35.005 14.952 61.789  1.00 43.96  ? 140  VAL A O   1 
ATOM   520  C CB  . VAL A 1 109 ? 37.441 13.775 63.391  1.00 57.42  ? 140  VAL A CB  1 
ATOM   521  C CG1 . VAL A 1 109 ? 37.493 13.318 61.934  1.00 60.40  ? 140  VAL A CG1 1 
ATOM   522  C CG2 . VAL A 1 109 ? 38.854 13.947 63.927  1.00 55.62  ? 140  VAL A CG2 1 
ATOM   523  N N   . SER A 1 110 ? 34.239 14.778 63.893  1.00 50.13  ? 141  SER A N   1 
ATOM   524  C CA  . SER A 1 110 ? 32.852 14.753 63.438  1.00 46.86  ? 141  SER A CA  1 
ATOM   525  C C   . SER A 1 110 ? 32.401 16.133 62.975  1.00 42.03  ? 141  SER A C   1 
ATOM   526  O O   . SER A 1 110 ? 31.615 16.250 62.029  1.00 43.69  ? 141  SER A O   1 
ATOM   527  C CB  . SER A 1 110 ? 31.933 14.239 64.546  1.00 46.01  ? 141  SER A CB  1 
ATOM   528  O OG  . SER A 1 110 ? 31.980 12.824 64.629  1.00 57.60  ? 141  SER A OG  1 
ATOM   529  N N   . LEU A 1 111 ? 32.864 17.191 63.645  1.00 40.52  ? 142  LEU A N   1 
ATOM   530  C CA  . LEU A 1 111 ? 32.626 18.536 63.135  1.00 32.56  ? 142  LEU A CA  1 
ATOM   531  C C   . LEU A 1 111 ? 33.213 18.686 61.738  1.00 36.92  ? 142  LEU A C   1 
ATOM   532  O O   . LEU A 1 111 ? 32.572 19.249 60.841  1.00 33.21  ? 142  LEU A O   1 
ATOM   533  C CB  . LEU A 1 111 ? 33.220 19.576 64.088  1.00 39.96  ? 142  LEU A CB  1 
ATOM   534  C CG  . LEU A 1 111 ? 33.239 21.033 63.609  1.00 38.79  ? 142  LEU A CG  1 
ATOM   535  C CD1 . LEU A 1 111 ? 31.834 21.545 63.360  1.00 37.53  ? 142  LEU A CD1 1 
ATOM   536  C CD2 . LEU A 1 111 ? 33.956 21.932 64.611  1.00 37.69  ? 142  LEU A CD2 1 
ATOM   537  N N   . LEU A 1 112 ? 34.422 18.158 61.529  1.00 34.06  ? 143  LEU A N   1 
ATOM   538  C CA  . LEU A 1 112 ? 35.046 18.222 60.212  1.00 28.45  ? 143  LEU A CA  1 
ATOM   539  C C   . LEU A 1 112 ? 34.248 17.436 59.181  1.00 31.28  ? 143  LEU A C   1 
ATOM   540  O O   . LEU A 1 112 ? 34.090 17.881 58.039  1.00 33.17  ? 143  LEU A O   1 
ATOM   541  C CB  . LEU A 1 112 ? 36.476 17.688 60.284  1.00 37.91  ? 143  LEU A CB  1 
ATOM   542  C CG  . LEU A 1 112 ? 37.405 18.346 61.301  1.00 44.93  ? 143  LEU A CG  1 
ATOM   543  C CD1 . LEU A 1 112 ? 38.737 17.624 61.334  1.00 43.26  ? 143  LEU A CD1 1 
ATOM   544  C CD2 . LEU A 1 112 ? 37.594 19.805 60.957  1.00 37.92  ? 143  LEU A CD2 1 
ATOM   545  N N   . THR A 1 113 ? 33.739 16.261 59.563  1.00 29.33  ? 144  THR A N   1 
ATOM   546  C CA  . THR A 1 113 ? 33.015 15.432 58.604  1.00 35.32  ? 144  THR A CA  1 
ATOM   547  C C   . THR A 1 113 ? 31.706 16.090 58.181  1.00 31.69  ? 144  THR A C   1 
ATOM   548  O O   . THR A 1 113 ? 31.334 16.039 57.003  1.00 30.57  ? 144  THR A O   1 
ATOM   549  C CB  . THR A 1 113 ? 32.750 14.042 59.188  1.00 34.25  ? 144  THR A CB  1 
ATOM   550  O OG1 . THR A 1 113 ? 32.014 14.161 60.411  1.00 46.77  ? 144  THR A OG1 1 
ATOM   551  C CG2 . THR A 1 113 ? 34.061 13.299 59.441  1.00 34.83  ? 144  THR A CG2 1 
ATOM   552  N N   . VAL A 1 114 ? 30.988 16.711 59.121  1.00 30.85  ? 145  VAL A N   1 
ATOM   553  C CA  . VAL A 1 114 ? 29.751 17.393 58.749  1.00 32.10  ? 145  VAL A CA  1 
ATOM   554  C C   . VAL A 1 114 ? 30.055 18.608 57.880  1.00 27.47  ? 145  VAL A C   1 
ATOM   555  O O   . VAL A 1 114 ? 29.358 18.872 56.893  1.00 29.25  ? 145  VAL A O   1 
ATOM   556  C CB  . VAL A 1 114 ? 28.944 17.781 60.000  1.00 36.10  ? 145  VAL A CB  1 
ATOM   557  C CG1 . VAL A 1 114 ? 27.724 18.602 59.606  1.00 33.70  ? 145  VAL A CG1 1 
ATOM   558  C CG2 . VAL A 1 114 ? 28.522 16.536 60.764  1.00 40.03  ? 145  VAL A CG2 1 
ATOM   559  N N   . GLY A 1 115 ? 31.084 19.375 58.235  1.00 27.11  ? 146  GLY A N   1 
ATOM   560  C CA  . GLY A 1 115 ? 31.503 20.463 57.367  1.00 34.45  ? 146  GLY A CA  1 
ATOM   561  C C   . GLY A 1 115 ? 31.913 19.964 55.997  1.00 36.04  ? 146  GLY A C   1 
ATOM   562  O O   . GLY A 1 115 ? 31.619 20.595 54.978  1.00 27.21  ? 146  GLY A O   1 
ATOM   563  N N   . PHE A 1 116 ? 32.600 18.820 55.958  1.00 31.29  ? 147  PHE A N   1 
ATOM   564  C CA  . PHE A 1 116 ? 32.942 18.181 54.693  1.00 26.42  ? 147  PHE A CA  1 
ATOM   565  C C   . PHE A 1 116 ? 31.694 17.870 53.875  1.00 26.97  ? 147  PHE A C   1 
ATOM   566  O O   . PHE A 1 116 ? 31.664 18.106 52.661  1.00 26.70  ? 147  PHE A O   1 
ATOM   567  C CB  . PHE A 1 116 ? 33.741 16.908 54.988  1.00 33.64  ? 147  PHE A CB  1 
ATOM   568  C CG  . PHE A 1 116 ? 34.282 16.223 53.773  1.00 36.71  ? 147  PHE A CG  1 
ATOM   569  C CD1 . PHE A 1 116 ? 35.535 16.550 53.283  1.00 36.71  ? 147  PHE A CD1 1 
ATOM   570  C CD2 . PHE A 1 116 ? 33.553 15.232 53.136  1.00 34.51  ? 147  PHE A CD2 1 
ATOM   571  C CE1 . PHE A 1 116 ? 36.044 15.915 52.167  1.00 52.18  ? 147  PHE A CE1 1 
ATOM   572  C CE2 . PHE A 1 116 ? 34.057 14.594 52.015  1.00 41.01  ? 147  PHE A CE2 1 
ATOM   573  C CZ  . PHE A 1 116 ? 35.305 14.935 51.532  1.00 40.22  ? 147  PHE A CZ  1 
ATOM   574  N N   . LEU A 1 117 ? 30.644 17.359 54.525  1.00 29.06  ? 148  LEU A N   1 
ATOM   575  C CA  . LEU A 1 117 ? 29.442 16.967 53.794  1.00 26.80  ? 148  LEU A CA  1 
ATOM   576  C C   . LEU A 1 117 ? 28.668 18.182 53.307  1.00 26.96  ? 148  LEU A C   1 
ATOM   577  O O   . LEU A 1 117 ? 28.093 18.159 52.213  1.00 28.46  ? 148  LEU A O   1 
ATOM   578  C CB  . LEU A 1 117 ? 28.565 16.083 54.678  1.00 27.74  ? 148  LEU A CB  1 
ATOM   579  C CG  . LEU A 1 117 ? 29.100 14.657 54.820  1.00 30.94  ? 148  LEU A CG  1 
ATOM   580  C CD1 . LEU A 1 117 ? 28.425 13.920 55.956  1.00 25.43  ? 148  LEU A CD1 1 
ATOM   581  C CD2 . LEU A 1 117 ? 28.912 13.907 53.515  1.00 33.21  ? 148  LEU A CD2 1 
ATOM   582  N N   . VAL A 1 118 ? 28.629 19.246 54.109  1.00 27.33  ? 149  VAL A N   1 
ATOM   583  C CA  . VAL A 1 118 ? 27.989 20.485 53.673  1.00 28.32  ? 149  VAL A CA  1 
ATOM   584  C C   . VAL A 1 118 ? 28.626 20.982 52.379  1.00 24.61  ? 149  VAL A C   1 
ATOM   585  O O   . VAL A 1 118 ? 27.934 21.317 51.408  1.00 26.86  ? 149  VAL A O   1 
ATOM   586  C CB  . VAL A 1 118 ? 28.070 21.537 54.796  1.00 29.34  ? 149  VAL A CB  1 
ATOM   587  C CG1 . VAL A 1 118 ? 27.686 22.918 54.291  1.00 29.47  ? 149  VAL A CG1 1 
ATOM   588  C CG2 . VAL A 1 118 ? 27.175 21.128 55.965  1.00 26.08  ? 149  VAL A CG2 1 
ATOM   589  N N   . ALA A 1 119 ? 29.958 21.024 52.342  1.00 28.40  ? 150  ALA A N   1 
ATOM   590  C CA  . ALA A 1 119 ? 30.653 21.488 51.145  1.00 29.94  ? 150  ALA A CA  1 
ATOM   591  C C   . ALA A 1 119 ? 30.420 20.557 49.961  1.00 31.03  ? 150  ALA A C   1 
ATOM   592  O O   . ALA A 1 119 ? 30.251 21.017 48.826  1.00 29.74  ? 150  ALA A O   1 
ATOM   593  C CB  . ALA A 1 119 ? 32.148 21.616 51.427  1.00 28.35  ? 150  ALA A CB  1 
ATOM   594  N N   . SER A 1 120 ? 30.433 19.243 50.198  1.00 29.96  ? 151  SER A N   1 
ATOM   595  C CA  . SER A 1 120 ? 30.254 18.298 49.099  1.00 29.93  ? 151  SER A CA  1 
ATOM   596  C C   . SER A 1 120 ? 28.853 18.387 48.505  1.00 30.78  ? 151  SER A C   1 
ATOM   597  O O   . SER A 1 120 ? 28.693 18.386 47.279  1.00 25.48  ? 151  SER A O   1 
ATOM   598  C CB  . SER A 1 120 ? 30.530 16.873 49.577  1.00 37.32  ? 151  SER A CB  1 
ATOM   599  O OG  . SER A 1 120 ? 31.847 16.752 50.076  1.00 37.98  ? 151  SER A OG  1 
ATOM   600  N N   . PHE A 1 121 ? 27.822 18.448 49.350  1.00 26.98  ? 152  PHE A N   1 
ATOM   601  C CA  . PHE A 1 121 ? 26.470 18.543 48.814  1.00 30.22  ? 152  PHE A CA  1 
ATOM   602  C C   . PHE A 1 121 ? 26.208 19.919 48.218  1.00 33.87  ? 152  PHE A C   1 
ATOM   603  O O   . PHE A 1 121 ? 25.503 20.028 47.210  1.00 30.36  ? 152  PHE A O   1 
ATOM   604  C CB  . PHE A 1 121 ? 25.452 18.194 49.898  1.00 26.76  ? 152  PHE A CB  1 
ATOM   605  C CG  . PHE A 1 121 ? 25.310 16.710 50.124  1.00 33.98  ? 152  PHE A CG  1 
ATOM   606  C CD1 . PHE A 1 121 ? 24.912 15.875 49.090  1.00 39.43  ? 152  PHE A CD1 1 
ATOM   607  C CD2 . PHE A 1 121 ? 25.578 16.150 51.361  1.00 35.01  ? 152  PHE A CD2 1 
ATOM   608  C CE1 . PHE A 1 121 ? 24.782 14.511 49.286  1.00 36.12  ? 152  PHE A CE1 1 
ATOM   609  C CE2 . PHE A 1 121 ? 25.447 14.785 51.563  1.00 35.18  ? 152  PHE A CE2 1 
ATOM   610  C CZ  . PHE A 1 121 ? 25.051 13.968 50.523  1.00 49.23  ? 152  PHE A CZ  1 
ATOM   611  N N   . ALA A 1 122 ? 26.781 20.976 48.800  1.00 20.57  ? 153  ALA A N   1 
ATOM   612  C CA  . ALA A 1 122 ? 26.706 22.279 48.151  1.00 29.80  ? 153  ALA A CA  1 
ATOM   613  C C   . ALA A 1 122 ? 27.313 22.218 46.755  1.00 29.10  ? 153  ALA A C   1 
ATOM   614  O O   . ALA A 1 122 ? 26.731 22.732 45.794  1.00 26.46  ? 153  ALA A O   1 
ATOM   615  C CB  . ALA A 1 122 ? 27.408 23.341 48.997  1.00 27.22  ? 153  ALA A CB  1 
ATOM   616  N N   . ALA A 1 123 ? 28.473 21.568 46.622  1.00 25.86  ? 154  ALA A N   1 
ATOM   617  C CA  . ALA A 1 123 ? 29.134 21.487 45.326  1.00 27.72  ? 154  ALA A CA  1 
ATOM   618  C C   . ALA A 1 123 ? 28.329 20.654 44.339  1.00 34.88  ? 154  ALA A C   1 
ATOM   619  O O   . ALA A 1 123 ? 28.352 20.930 43.135  1.00 27.24  ? 154  ALA A O   1 
ATOM   620  C CB  . ALA A 1 123 ? 30.538 20.903 45.493  1.00 26.53  ? 154  ALA A CB  1 
ATOM   621  N N   . SER A 1 124 ? 27.625 19.630 44.826  1.00 28.08  ? 155  SER A N   1 
ATOM   622  C CA  . SER A 1 124 ? 26.808 18.799 43.949  1.00 32.76  ? 155  SER A CA  1 
ATOM   623  C C   . SER A 1 124 ? 25.599 19.570 43.434  1.00 26.39  ? 155  SER A C   1 
ATOM   624  O O   . SER A 1 124 ? 25.291 19.541 42.236  1.00 25.60  ? 155  SER A O   1 
ATOM   625  C CB  . SER A 1 124 ? 26.358 17.546 44.698  1.00 29.82  ? 155  SER A CB  1 
ATOM   626  O OG  . SER A 1 124 ? 25.534 16.741 43.881  1.00 40.03  ? 155  SER A OG  1 
ATOM   627  N N   . VAL A 1 125 ? 24.892 20.254 44.333  1.00 24.80  ? 156  VAL A N   1 
ATOM   628  C CA  . VAL A 1 125 ? 23.715 21.012 43.925  1.00 37.41  ? 156  VAL A CA  1 
ATOM   629  C C   . VAL A 1 125 ? 24.112 22.162 43.011  1.00 29.07  ? 156  VAL A C   1 
ATOM   630  O O   . VAL A 1 125 ? 23.420 22.463 42.031  1.00 25.86  ? 156  VAL A O   1 
ATOM   631  C CB  . VAL A 1 125 ? 22.949 21.510 45.162  1.00 30.09  ? 156  VAL A CB  1 
ATOM   632  C CG1 . VAL A 1 125 ? 21.869 22.492 44.749  1.00 37.61  ? 156  VAL A CG1 1 
ATOM   633  C CG2 . VAL A 1 125 ? 22.340 20.339 45.898  1.00 34.00  ? 156  VAL A CG2 1 
ATOM   634  N N   . SER A 1 126 ? 25.223 22.832 43.316  1.00 24.09  ? 157  SER A N   1 
ATOM   635  C CA  . SER A 1 126 ? 25.658 23.922 42.453  1.00 27.70  ? 157  SER A CA  1 
ATOM   636  C C   . SER A 1 126 ? 26.192 23.398 41.123  1.00 30.17  ? 157  SER A C   1 
ATOM   637  O O   . SER A 1 126 ? 26.077 24.084 40.100  1.00 29.03  ? 157  SER A O   1 
ATOM   638  C CB  . SER A 1 126 ? 26.701 24.774 43.175  1.00 26.14  ? 157  SER A CB  1 
ATOM   639  O OG  . SER A 1 126 ? 27.841 24.015 43.536  1.00 29.21  ? 157  SER A OG  1 
ATOM   640  N N   . SER A 1 127 ? 26.741 22.178 41.104  1.00 30.27  ? 158  SER A N   1 
ATOM   641  C CA  . SER A 1 127 ? 27.160 21.585 39.836  1.00 28.13  ? 158  SER A CA  1 
ATOM   642  C C   . SER A 1 127 ? 25.962 21.260 38.954  1.00 24.10  ? 158  SER A C   1 
ATOM   643  O O   . SER A 1 127 ? 26.046 21.367 37.726  1.00 26.44  ? 158  SER A O   1 
ATOM   644  C CB  . SER A 1 127 ? 27.979 20.317 40.074  1.00 32.04  ? 158  SER A CB  1 
ATOM   645  O OG  . SER A 1 127 ? 29.295 20.610 40.496  1.00 28.84  ? 158  SER A OG  1 
ATOM   646  N N   . LEU A 1 128 ? 24.846 20.844 39.561  1.00 28.31  ? 159  LEU A N   1 
ATOM   647  C CA  . LEU A 1 128 ? 23.633 20.610 38.786  1.00 32.14  ? 159  LEU A CA  1 
ATOM   648  C C   . LEU A 1 128 ? 23.127 21.905 38.178  1.00 32.47  ? 159  LEU A C   1 
ATOM   649  O O   . LEU A 1 128 ? 22.656 21.927 37.035  1.00 27.11  ? 159  LEU A O   1 
ATOM   650  C CB  . LEU A 1 128 ? 22.553 19.991 39.669  1.00 30.90  ? 159  LEU A CB  1 
ATOM   651  C CG  . LEU A 1 128 ? 22.749 18.528 40.055  1.00 34.68  ? 159  LEU A CG  1 
ATOM   652  C CD1 . LEU A 1 128 ? 21.674 18.130 41.052  1.00 44.58  ? 159  LEU A CD1 1 
ATOM   653  C CD2 . LEU A 1 128 ? 22.717 17.630 38.828  1.00 41.89  ? 159  LEU A CD2 1 
ATOM   654  N N   . LEU A 1 129 ? 23.200 22.995 38.939  1.00 27.70  ? 160  LEU A N   1 
ATOM   655  C CA  . LEU A 1 129 ? 22.866 24.302 38.392  1.00 31.45  ? 160  LEU A CA  1 
ATOM   656  C C   . LEU A 1 129 ? 23.728 24.615 37.178  1.00 27.75  ? 160  LEU A C   1 
ATOM   657  O O   . LEU A 1 129 ? 23.216 24.994 36.118  1.00 27.20  ? 160  LEU A O   1 
ATOM   658  C CB  . LEU A 1 129 ? 23.040 25.365 39.471  1.00 30.58  ? 160  LEU A CB  1 
ATOM   659  C CG  . LEU A 1 129 ? 22.865 26.810 39.020  1.00 43.34  ? 160  LEU A CG  1 
ATOM   660  C CD1 . LEU A 1 129 ? 21.476 27.006 38.435  1.00 40.05  ? 160  LEU A CD1 1 
ATOM   661  C CD2 . LEU A 1 129 ? 23.115 27.735 40.198  1.00 39.94  ? 160  LEU A CD2 1 
ATOM   662  N N   . ALA A 1 130 ? 25.046 24.444 37.310  1.00 31.36  ? 161  ALA A N   1 
ATOM   663  C CA  . ALA A 1 130 ? 25.948 24.766 36.210  1.00 25.76  ? 161  ALA A CA  1 
ATOM   664  C C   . ALA A 1 130 ? 25.652 23.911 34.985  1.00 29.04  ? 161  ALA A C   1 
ATOM   665  O O   . ALA A 1 130 ? 25.684 24.406 33.854  1.00 30.21  ? 161  ALA A O   1 
ATOM   666  C CB  . ALA A 1 130 ? 27.399 24.581 36.652  1.00 26.41  ? 161  ALA A CB  1 
ATOM   667  N N   . ILE A 1 131 ? 25.376 22.621 35.189  1.00 32.95  ? 162  ILE A N   1 
ATOM   668  C CA  . ILE A 1 131 ? 24.999 21.756 34.074  1.00 31.98  ? 162  ILE A CA  1 
ATOM   669  C C   . ILE A 1 131 ? 23.751 22.291 33.388  1.00 34.00  ? 162  ILE A C   1 
ATOM   670  O O   . ILE A 1 131 ? 23.676 22.362 32.155  1.00 35.66  ? 162  ILE A O   1 
ATOM   671  C CB  . ILE A 1 131 ? 24.799 20.310 34.565  1.00 38.04  ? 162  ILE A CB  1 
ATOM   672  C CG1 . ILE A 1 131 ? 26.159 19.659 34.801  1.00 28.66  ? 162  ILE A CG1 1 
ATOM   673  C CG2 . ILE A 1 131 ? 23.979 19.502 33.562  1.00 39.91  ? 162  ILE A CG2 1 
ATOM   674  C CD1 . ILE A 1 131 ? 26.088 18.363 35.557  1.00 39.43  ? 162  ILE A CD1 1 
ATOM   675  N N   . THR A 1 132 ? 22.748 22.671 34.178  1.00 28.80  ? 163  THR A N   1 
ATOM   676  C CA  . THR A 1 132 ? 21.505 23.164 33.598  1.00 29.92  ? 163  THR A CA  1 
ATOM   677  C C   . THR A 1 132 ? 21.732 24.462 32.836  1.00 34.07  ? 163  THR A C   1 
ATOM   678  O O   . THR A 1 132 ? 21.151 24.671 31.764  1.00 32.19  ? 163  THR A O   1 
ATOM   679  C CB  . THR A 1 132 ? 20.462 23.361 34.696  1.00 29.27  ? 163  THR A CB  1 
ATOM   680  O OG1 . THR A 1 132 ? 20.445 22.211 35.550  1.00 35.85  ? 163  THR A OG1 1 
ATOM   681  C CG2 . THR A 1 132 ? 19.090 23.557 34.086  1.00 36.19  ? 163  THR A CG2 1 
ATOM   682  N N   . VAL A 1 133 ? 22.561 25.356 33.379  1.00 27.12  ? 164  VAL A N   1 
ATOM   683  C CA  . VAL A 1 133 ? 22.907 26.580 32.659  1.00 29.92  ? 164  VAL A CA  1 
ATOM   684  C C   . VAL A 1 133 ? 23.505 26.234 31.301  1.00 30.72  ? 164  VAL A C   1 
ATOM   685  O O   . VAL A 1 133 ? 23.115 26.787 30.267  1.00 29.33  ? 164  VAL A O   1 
ATOM   686  C CB  . VAL A 1 133 ? 23.873 27.439 33.497  1.00 35.51  ? 164  VAL A CB  1 
ATOM   687  C CG1 . VAL A 1 133 ? 24.499 28.539 32.647  1.00 32.43  ? 164  VAL A CG1 1 
ATOM   688  C CG2 . VAL A 1 133 ? 23.152 28.045 34.691  1.00 31.26  ? 164  VAL A CG2 1 
ATOM   689  N N   . ASP A 1 134 ? 24.468 25.311 31.293  1.00 31.41  ? 165  ASP A N   1 
ATOM   690  C CA  . ASP A 1 134 ? 25.114 24.888 30.055  1.00 31.79  ? 165  ASP A CA  1 
ATOM   691  C C   . ASP A 1 134 ? 24.103 24.342 29.050  1.00 36.36  ? 165  ASP A C   1 
ATOM   692  O O   . ASP A 1 134 ? 24.147 24.684 27.862  1.00 34.50  ? 165  ASP A O   1 
ATOM   693  C CB  . ASP A 1 134 ? 26.176 23.844 30.396  1.00 30.39  ? 165  ASP A CB  1 
ATOM   694  C CG  . ASP A 1 134 ? 26.955 23.377 29.191  1.00 43.92  ? 165  ASP A CG  1 
ATOM   695  O OD1 . ASP A 1 134 ? 27.843 24.127 28.719  1.00 30.86  ? 165  ASP A OD1 1 
ATOM   696  O OD2 . ASP A 1 134 ? 26.689 22.242 28.737  1.00 38.34  ? 165  ASP A OD2 1 
ATOM   697  N N   . ARG A 1 135 ? 23.179 23.489 29.504  1.00 32.15  ? 166  ARG A N   1 
ATOM   698  C CA  . ARG A 1 135 ? 22.187 22.939 28.585  1.00 34.71  ? 166  ARG A CA  1 
ATOM   699  C C   . ARG A 1 135 ? 21.308 24.041 28.013  1.00 35.20  ? 166  ARG A C   1 
ATOM   700  O O   . ARG A 1 135 ? 20.993 24.038 26.818  1.00 35.29  ? 166  ARG A O   1 
ATOM   701  C CB  . ARG A 1 135 ? 21.353 21.870 29.295  1.00 36.72  ? 166  ARG A CB  1 
ATOM   702  C CG  . ARG A 1 135 ? 22.197 20.653 29.667  1.00 58.22  ? 166  ARG A CG  1 
ATOM   703  C CD  . ARG A 1 135 ? 21.540 19.716 30.669  1.00 50.77  ? 166  ARG A CD  1 
ATOM   704  N NE  . ARG A 1 135 ? 20.560 18.839 30.041  1.00 73.49  ? 166  ARG A NE  1 
ATOM   705  C CZ  . ARG A 1 135 ? 19.299 18.698 30.431  1.00 71.06  ? 166  ARG A CZ  1 
ATOM   706  N NH1 . ARG A 1 135 ? 18.824 19.333 31.491  1.00 83.65  ? 166  ARG A NH1 1 
ATOM   707  N NH2 . ARG A 1 135 ? 18.496 17.894 29.743  1.00 84.70  ? 166  ARG A NH2 1 
ATOM   708  N N   . TYR A 1 136 ? 20.920 25.008 28.846  1.00 33.49  ? 167  TYR A N   1 
ATOM   709  C CA  . TYR A 1 136 ? 20.182 26.163 28.346  1.00 32.21  ? 167  TYR A CA  1 
ATOM   710  C C   . TYR A 1 136 ? 20.965 26.888 27.256  1.00 31.66  ? 167  TYR A C   1 
ATOM   711  O O   . TYR A 1 136 ? 20.428 27.172 26.180  1.00 32.94  ? 167  TYR A O   1 
ATOM   712  C CB  . TYR A 1 136 ? 19.855 27.108 29.504  1.00 31.83  ? 167  TYR A CB  1 
ATOM   713  C CG  . TYR A 1 136 ? 19.374 28.476 29.079  1.00 32.17  ? 167  TYR A CG  1 
ATOM   714  C CD1 . TYR A 1 136 ? 18.048 28.698 28.751  1.00 39.49  ? 167  TYR A CD1 1 
ATOM   715  C CD2 . TYR A 1 136 ? 20.249 29.549 29.018  1.00 41.26  ? 167  TYR A CD2 1 
ATOM   716  C CE1 . TYR A 1 136 ? 17.609 29.947 28.368  1.00 49.02  ? 167  TYR A CE1 1 
ATOM   717  C CE2 . TYR A 1 136 ? 19.818 30.803 28.631  1.00 44.35  ? 167  TYR A CE2 1 
ATOM   718  C CZ  . TYR A 1 136 ? 18.498 30.997 28.308  1.00 47.58  ? 167  TYR A CZ  1 
ATOM   719  O OH  . TYR A 1 136 ? 18.065 32.246 27.924  1.00 66.14  ? 167  TYR A OH  1 
ATOM   720  N N   . LEU A 1 137 ? 22.239 27.198 27.511  1.00 33.15  ? 168  LEU A N   1 
ATOM   721  C CA  . LEU A 1 137 ? 22.995 28.002 26.554  1.00 37.89  ? 168  LEU A CA  1 
ATOM   722  C C   . LEU A 1 137 ? 23.197 27.265 25.235  1.00 36.53  ? 168  LEU A C   1 
ATOM   723  O O   . LEU A 1 137 ? 23.135 27.878 24.164  1.00 37.78  ? 168  LEU A O   1 
ATOM   724  C CB  . LEU A 1 137 ? 24.339 28.411 27.151  1.00 34.49  ? 168  LEU A CB  1 
ATOM   725  C CG  . LEU A 1 137 ? 24.261 29.468 28.255  1.00 45.28  ? 168  LEU A CG  1 
ATOM   726  C CD1 . LEU A 1 137 ? 25.596 29.600 28.949  1.00 46.73  ? 168  LEU A CD1 1 
ATOM   727  C CD2 . LEU A 1 137 ? 23.822 30.820 27.710  1.00 50.28  ? 168  LEU A CD2 1 
ATOM   728  N N   . SER A 1 138 ? 23.428 25.952 25.285  1.00 37.15  ? 169  SER A N   1 
ATOM   729  C CA  . SER A 1 138 ? 23.609 25.206 24.045  1.00 38.27  ? 169  SER A CA  1 
ATOM   730  C C   . SER A 1 138 ? 22.327 25.160 23.222  1.00 38.52  ? 169  SER A C   1 
ATOM   731  O O   . SER A 1 138 ? 22.388 25.091 21.989  1.00 44.51  ? 169  SER A O   1 
ATOM   732  C CB  . SER A 1 138 ? 24.098 23.790 24.351  1.00 38.05  ? 169  SER A CB  1 
ATOM   733  O OG  . SER A 1 138 ? 23.103 23.026 25.004  1.00 45.27  ? 169  SER A OG  1 
ATOM   734  N N   . LEU A 1 139 ? 21.162 25.200 23.875  1.00 38.58  ? 170  LEU A N   1 
ATOM   735  C CA  . LEU A 1 139 ? 19.901 25.180 23.143  1.00 35.54  ? 170  LEU A CA  1 
ATOM   736  C C   . LEU A 1 139 ? 19.529 26.551 22.598  1.00 36.50  ? 170  LEU A C   1 
ATOM   737  O O   . LEU A 1 139 ? 18.944 26.642 21.513  1.00 38.26  ? 170  LEU A O   1 
ATOM   738  C CB  . LEU A 1 139 ? 18.770 24.670 24.036  1.00 40.04  ? 170  LEU A CB  1 
ATOM   739  C CG  . LEU A 1 139 ? 18.779 23.177 24.366  1.00 41.80  ? 170  LEU A CG  1 
ATOM   740  C CD1 . LEU A 1 139 ? 17.632 22.842 25.304  1.00 49.03  ? 170  LEU A CD1 1 
ATOM   741  C CD2 . LEU A 1 139 ? 18.698 22.329 23.101  1.00 52.33  ? 170  LEU A CD2 1 
ATOM   742  N N   . TYR A 1 140 ? 19.848 27.621 23.320  1.00 38.83  ? 171  TYR A N   1 
ATOM   743  C CA  . TYR A 1 140 ? 19.468 28.953 22.871  1.00 41.97  ? 171  TYR A CA  1 
ATOM   744  C C   . TYR A 1 140 ? 20.490 29.586 21.939  1.00 49.41  ? 171  TYR A C   1 
ATOM   745  O O   . TYR A 1 140 ? 20.162 30.570 21.268  1.00 45.91  ? 171  TYR A O   1 
ATOM   746  C CB  . TYR A 1 140 ? 19.218 29.857 24.082  1.00 43.72  ? 171  TYR A CB  1 
ATOM   747  C CG  . TYR A 1 140 ? 17.792 29.746 24.565  1.00 49.11  ? 171  TYR A CG  1 
ATOM   748  C CD1 . TYR A 1 140 ? 17.404 28.717 25.413  1.00 56.23  ? 171  TYR A CD1 1 
ATOM   749  C CD2 . TYR A 1 140 ? 16.821 30.642 24.138  1.00 51.11  ? 171  TYR A CD2 1 
ATOM   750  C CE1 . TYR A 1 140 ? 16.096 28.599 25.845  1.00 53.29  ? 171  TYR A CE1 1 
ATOM   751  C CE2 . TYR A 1 140 ? 15.511 30.532 24.563  1.00 59.53  ? 171  TYR A CE2 1 
ATOM   752  C CZ  . TYR A 1 140 ? 15.155 29.509 25.418  1.00 59.59  ? 171  TYR A CZ  1 
ATOM   753  O OH  . TYR A 1 140 ? 13.853 29.385 25.845  1.00 52.87  ? 171  TYR A OH  1 
ATOM   754  N N   . ASN A 1 141 ? 21.698 29.033 21.857  1.00 48.95  ? 172  ASN A N   1 
ATOM   755  C CA  . ASN A 1 141 ? 22.765 29.566 21.011  1.00 46.61  ? 172  ASN A CA  1 
ATOM   756  C C   . ASN A 1 141 ? 23.388 28.426 20.217  1.00 45.15  ? 172  ASN A C   1 
ATOM   757  O O   . ASN A 1 141 ? 24.510 27.991 20.501  1.00 50.51  ? 172  ASN A O   1 
ATOM   758  C CB  . ASN A 1 141 ? 23.813 30.287 21.858  1.00 38.45  ? 172  ASN A CB  1 
ATOM   759  C CG  . ASN A 1 141 ? 23.203 31.343 22.756  1.00 48.61  ? 172  ASN A CG  1 
ATOM   760  O OD1 . ASN A 1 141 ? 22.822 32.418 22.297  1.00 53.38  ? 172  ASN A OD1 1 
ATOM   761  N ND2 . ASN A 1 141 ? 23.104 31.038 24.047  1.00 49.66  ? 172  ASN A ND2 1 
ATOM   762  N N   . PRO A 1 142 ? 22.684 27.927 19.197  1.00 45.16  ? 173  PRO A N   1 
ATOM   763  C CA  . PRO A 1 142 ? 23.192 26.764 18.450  1.00 62.11  ? 173  PRO A CA  1 
ATOM   764  C C   . PRO A 1 142 ? 24.535 26.996 17.783  1.00 57.38  ? 173  PRO A C   1 
ATOM   765  O O   . PRO A 1 142 ? 25.186 26.019 17.390  1.00 57.77  ? 173  PRO A O   1 
ATOM   766  C CB  . PRO A 1 142 ? 22.095 26.506 17.404  1.00 58.14  ? 173  PRO A CB  1 
ATOM   767  C CG  . PRO A 1 142 ? 20.890 27.231 17.896  1.00 63.58  ? 173  PRO A CG  1 
ATOM   768  C CD  . PRO A 1 142 ? 21.389 28.400 18.681  1.00 53.22  ? 173  PRO A CD  1 
ATOM   769  N N   . LEU A 1 143 ? 24.963 28.246 17.612  1.00 38.08  ? 174  LEU A N   1 
ATOM   770  C CA  . LEU A 1 143 ? 26.272 28.541 17.044  1.00 56.90  ? 174  LEU A CA  1 
ATOM   771  C C   . LEU A 1 143 ? 27.217 29.144 18.076  1.00 46.77  ? 174  LEU A C   1 
ATOM   772  O O   . LEU A 1 143 ? 28.260 28.556 18.369  1.00 48.53  ? 174  LEU A O   1 
ATOM   773  C CB  . LEU A 1 143 ? 26.121 29.474 15.836  1.00 53.14  ? 174  LEU A CB  1 
ATOM   774  C CG  . LEU A 1 143 ? 27.372 29.635 14.970  1.00 56.01  ? 174  LEU A CG  1 
ATOM   775  C CD1 . LEU A 1 143 ? 26.978 29.998 13.553  1.00 57.35  ? 174  LEU A CD1 1 
ATOM   776  C CD2 . LEU A 1 143 ? 28.311 30.684 15.541  1.00 50.79  ? 174  LEU A CD2 1 
ATOM   777  N N   . THR A 1 144 ? 26.871 30.298 18.654  1.00 46.28  ? 175  THR A N   1 
ATOM   778  C CA  . THR A 1 144 ? 27.783 30.993 19.554  1.00 51.18  ? 175  THR A CA  1 
ATOM   779  C C   . THR A 1 144 ? 28.052 30.229 20.847  1.00 45.83  ? 175  THR A C   1 
ATOM   780  O O   . THR A 1 144 ? 28.957 30.615 21.594  1.00 43.65  ? 175  THR A O   1 
ATOM   781  C CB  . THR A 1 144 ? 27.236 32.387 19.875  1.00 60.92  ? 175  THR A CB  1 
ATOM   782  O OG1 . THR A 1 144 ? 25.985 32.273 20.562  1.00 57.67  ? 175  THR A OG1 1 
ATOM   783  C CG2 . THR A 1 144 ? 27.039 33.186 18.590  1.00 55.98  ? 175  THR A CG2 1 
ATOM   784  N N   . TYR A 1 145 ? 27.298 29.168 21.138  1.00 39.93  ? 176  TYR A N   1 
ATOM   785  C CA  . TYR A 1 145 ? 27.676 28.298 22.247  1.00 44.17  ? 176  TYR A CA  1 
ATOM   786  C C   . TYR A 1 145 ? 29.083 27.747 22.047  1.00 44.43  ? 176  TYR A C   1 
ATOM   787  O O   . TYR A 1 145 ? 29.841 27.588 23.011  1.00 38.17  ? 176  TYR A O   1 
ATOM   788  C CB  . TYR A 1 145 ? 26.668 27.157 22.390  1.00 41.10  ? 176  TYR A CB  1 
ATOM   789  C CG  . TYR A 1 145 ? 27.083 26.110 23.394  1.00 36.52  ? 176  TYR A CG  1 
ATOM   790  C CD1 . TYR A 1 145 ? 26.897 26.312 24.755  1.00 41.46  ? 176  TYR A CD1 1 
ATOM   791  C CD2 . TYR A 1 145 ? 27.667 24.923 22.982  1.00 34.95  ? 176  TYR A CD2 1 
ATOM   792  C CE1 . TYR A 1 145 ? 27.283 25.357 25.675  1.00 36.44  ? 176  TYR A CE1 1 
ATOM   793  C CE2 . TYR A 1 145 ? 28.055 23.964 23.890  1.00 35.68  ? 176  TYR A CE2 1 
ATOM   794  C CZ  . TYR A 1 145 ? 27.863 24.184 25.235  1.00 39.88  ? 176  TYR A CZ  1 
ATOM   795  O OH  . TYR A 1 145 ? 28.253 23.224 26.138  1.00 34.82  ? 176  TYR A OH  1 
ATOM   796  N N   . TYR A 1 146 ? 29.452 27.463 20.799  1.00 40.03  ? 177  TYR A N   1 
ATOM   797  C CA  . TYR A 1 146 ? 30.777 26.943 20.464  1.00 46.71  ? 177  TYR A CA  1 
ATOM   798  C C   . TYR A 1 146 ? 31.714 28.127 20.270  1.00 44.54  ? 177  TYR A C   1 
ATOM   799  O O   . TYR A 1 146 ? 31.926 28.608 19.157  1.00 41.76  ? 177  TYR A O   1 
ATOM   800  C CB  . TYR A 1 146 ? 30.699 26.056 19.229  1.00 45.68  ? 177  TYR A CB  1 
ATOM   801  C CG  . TYR A 1 146 ? 29.783 24.876 19.437  1.00 51.38  ? 177  TYR A CG  1 
ATOM   802  C CD1 . TYR A 1 146 ? 30.202 23.768 20.160  1.00 46.38  ? 177  TYR A CD1 1 
ATOM   803  C CD2 . TYR A 1 146 ? 28.490 24.881 18.937  1.00 55.19  ? 177  TYR A CD2 1 
ATOM   804  C CE1 . TYR A 1 146 ? 29.364 22.692 20.364  1.00 54.85  ? 177  TYR A CE1 1 
ATOM   805  C CE2 . TYR A 1 146 ? 27.645 23.810 19.135  1.00 45.34  ? 177  TYR A CE2 1 
ATOM   806  C CZ  . TYR A 1 146 ? 28.085 22.719 19.849  1.00 50.57  ? 177  TYR A CZ  1 
ATOM   807  O OH  . TYR A 1 146 ? 27.244 21.649 20.049  1.00 62.37  ? 177  TYR A OH  1 
ATOM   808  N N   . SER A 1 147 ? 32.291 28.593 21.375  1.00 37.10  ? 178  SER A N   1 
ATOM   809  C CA  . SER A 1 147 ? 33.137 29.778 21.376  1.00 45.57  ? 178  SER A CA  1 
ATOM   810  C C   . SER A 1 147 ? 34.044 29.712 22.595  1.00 45.60  ? 178  SER A C   1 
ATOM   811  O O   . SER A 1 147 ? 33.837 28.906 23.504  1.00 42.00  ? 178  SER A O   1 
ATOM   812  C CB  . SER A 1 147 ? 32.301 31.061 21.393  1.00 46.46  ? 178  SER A CB  1 
ATOM   813  O OG  . SER A 1 147 ? 31.613 31.198 22.628  1.00 53.28  ? 178  SER A OG  1 
ATOM   814  N N   . ARG A 1 148 ? 35.054 30.584 22.607  1.00 45.47  ? 179  ARG A N   1 
ATOM   815  C CA  A ARG A 1 148 ? 35.955 30.635 23.753  0.50 43.25  ? 179  ARG A CA  1 
ATOM   816  C CA  B ARG A 1 148 ? 35.958 30.649 23.751  0.50 43.26  ? 179  ARG A CA  1 
ATOM   817  C C   . ARG A 1 148 ? 35.218 31.092 25.006  1.00 40.80  ? 179  ARG A C   1 
ATOM   818  O O   . ARG A 1 148 ? 35.497 30.606 26.109  1.00 44.47  ? 179  ARG A O   1 
ATOM   819  C CB  A ARG A 1 148 ? 37.141 31.558 23.454  0.50 49.39  ? 179  ARG A CB  1 
ATOM   820  C CB  B ARG A 1 148 ? 37.114 31.604 23.448  0.50 49.38  ? 179  ARG A CB  1 
ATOM   821  C CG  A ARG A 1 148 ? 38.316 30.857 22.770  0.50 60.54  ? 179  ARG A CG  1 
ATOM   822  C CG  B ARG A 1 148 ? 37.940 31.209 22.233  0.50 62.38  ? 179  ARG A CG  1 
ATOM   823  C CD  A ARG A 1 148 ? 39.540 31.765 22.621  0.50 70.31  ? 179  ARG A CD  1 
ATOM   824  C CD  B ARG A 1 148 ? 38.986 32.258 21.883  0.50 71.93  ? 179  ARG A CD  1 
ATOM   825  N NE  A ARG A 1 148 ? 39.417 32.705 21.510  0.50 72.68  ? 179  ARG A NE  1 
ATOM   826  N NE  B ARG A 1 148 ? 39.868 32.558 23.005  0.50 69.42  ? 179  ARG A NE  1 
ATOM   827  C CZ  A ARG A 1 148 ? 39.981 32.557 20.317  0.50 53.08  ? 179  ARG A CZ  1 
ATOM   828  C CZ  B ARG A 1 148 ? 40.919 31.827 23.354  0.50 68.47  ? 179  ARG A CZ  1 
ATOM   829  N NH1 A ARG A 1 148 ? 40.729 31.505 20.025  0.50 56.05  ? 179  ARG A NH1 1 
ATOM   830  N NH1 B ARG A 1 148 ? 41.243 30.724 22.699  0.50 64.05  ? 179  ARG A NH1 1 
ATOM   831  N NH2 A ARG A 1 148 ? 39.793 33.493 19.392  0.50 50.70  ? 179  ARG A NH2 1 
ATOM   832  N NH2 B ARG A 1 148 ? 41.662 32.212 24.387  0.50 61.70  ? 179  ARG A NH2 1 
ATOM   833  N N   . ARG A 1 149 ? 34.266 32.012 24.853  1.00 42.64  ? 180  ARG A N   1 
ATOM   834  C CA  . ARG A 1 149 ? 33.530 32.534 25.998  1.00 41.70  ? 180  ARG A CA  1 
ATOM   835  C C   . ARG A 1 149 ? 32.843 31.420 26.779  1.00 51.95  ? 180  ARG A C   1 
ATOM   836  O O   . ARG A 1 149 ? 32.775 31.468 28.013  1.00 44.57  ? 180  ARG A O   1 
ATOM   837  C CB  . ARG A 1 149 ? 32.509 33.563 25.518  1.00 38.11  ? 180  ARG A CB  1 
ATOM   838  C CG  . ARG A 1 149 ? 31.873 34.377 26.630  1.00 65.72  ? 180  ARG A CG  1 
ATOM   839  C CD  . ARG A 1 149 ? 30.596 35.061 26.161  1.00 81.08  ? 180  ARG A CD  1 
ATOM   840  N NE  . ARG A 1 149 ? 29.920 35.746 27.257  1.00 98.29  ? 180  ARG A NE  1 
ATOM   841  C CZ  . ARG A 1 149 ? 28.700 36.259 27.186  1.00 104.82 ? 180  ARG A CZ  1 
ATOM   842  N NH1 . ARG A 1 149 ? 27.980 36.183 26.078  1.00 117.33 ? 180  ARG A NH1 1 
ATOM   843  N NH2 . ARG A 1 149 ? 28.186 36.861 28.255  1.00 111.33 ? 180  ARG A NH2 1 
ATOM   844  N N   . THR A 1 150 ? 32.319 30.408 26.083  1.00 39.21  ? 181  THR A N   1 
ATOM   845  C CA  . THR A 1 150 ? 31.625 29.338 26.791  1.00 40.72  ? 181  THR A CA  1 
ATOM   846  C C   . THR A 1 150 ? 32.585 28.560 27.678  1.00 36.86  ? 181  THR A C   1 
ATOM   847  O O   . THR A 1 150 ? 32.239 28.197 28.807  1.00 33.74  ? 181  THR A O   1 
ATOM   848  C CB  . THR A 1 150 ? 30.929 28.397 25.808  1.00 37.23  ? 181  THR A CB  1 
ATOM   849  O OG1 . THR A 1 150 ? 29.904 29.107 25.106  1.00 36.25  ? 181  THR A OG1 1 
ATOM   850  C CG2 . THR A 1 150 ? 30.309 27.218 26.557  1.00 35.94  ? 181  THR A CG2 1 
ATOM   851  N N   . LEU A 1 151 ? 33.796 28.292 27.191  1.00 38.34  ? 182  LEU A N   1 
ATOM   852  C CA  . LEU A 1 151 ? 34.750 27.562 28.019  1.00 42.42  ? 182  LEU A CA  1 
ATOM   853  C C   . LEU A 1 151 ? 35.226 28.419 29.186  1.00 31.96  ? 182  LEU A C   1 
ATOM   854  O O   . LEU A 1 151 ? 35.324 27.939 30.321  1.00 32.12  ? 182  LEU A O   1 
ATOM   855  C CB  . LEU A 1 151 ? 35.935 27.091 27.179  1.00 45.57  ? 182  LEU A CB  1 
ATOM   856  C CG  . LEU A 1 151 ? 36.947 26.245 27.959  1.00 48.42  ? 182  LEU A CG  1 
ATOM   857  C CD1 . LEU A 1 151 ? 36.309 24.968 28.502  1.00 48.29  ? 182  LEU A CD1 1 
ATOM   858  C CD2 . LEU A 1 151 ? 38.152 25.918 27.095  1.00 68.70  ? 182  LEU A CD2 1 
ATOM   859  N N   . LEU A 1 152 ? 35.533 29.691 28.930  1.00 31.38  ? 183  LEU A N   1 
ATOM   860  C CA  . LEU A 1 152 ? 35.833 30.599 30.030  1.00 36.52  ? 183  LEU A CA  1 
ATOM   861  C C   . LEU A 1 152 ? 34.701 30.606 31.048  1.00 34.08  ? 183  LEU A C   1 
ATOM   862  O O   . LEU A 1 152 ? 34.942 30.585 32.261  1.00 30.58  ? 183  LEU A O   1 
ATOM   863  C CB  . LEU A 1 152 ? 36.073 32.008 29.491  1.00 33.44  ? 183  LEU A CB  1 
ATOM   864  C CG  . LEU A 1 152 ? 36.244 33.109 30.535  1.00 40.64  ? 183  LEU A CG  1 
ATOM   865  C CD1 . LEU A 1 152 ? 37.410 32.796 31.464  1.00 45.87  ? 183  LEU A CD1 1 
ATOM   866  C CD2 . LEU A 1 152 ? 36.441 34.437 29.827  1.00 37.34  ? 183  LEU A CD2 1 
ATOM   867  N N   . GLY A 1 153 ? 33.456 30.614 30.568  1.00 34.76  ? 184  GLY A N   1 
ATOM   868  C CA  . GLY A 1 153 ? 32.320 30.719 31.468  1.00 28.41  ? 184  GLY A CA  1 
ATOM   869  C C   . GLY A 1 153 ? 32.202 29.542 32.416  1.00 36.07  ? 184  GLY A C   1 
ATOM   870  O O   . GLY A 1 153 ? 31.844 29.711 33.584  1.00 34.73  ? 184  GLY A O   1 
ATOM   871  N N   . VAL A 1 154 ? 32.479 28.331 31.927  1.00 29.90  ? 185  VAL A N   1 
ATOM   872  C CA  A VAL A 1 154 ? 32.429 27.158 32.793  0.50 30.37  ? 185  VAL A CA  1 
ATOM   873  C CA  B VAL A 1 154 ? 32.423 27.162 32.800  0.50 30.41  ? 185  VAL A CA  1 
ATOM   874  C C   . VAL A 1 154 ? 33.541 27.218 33.833  1.00 32.06  ? 185  VAL A C   1 
ATOM   875  O O   . VAL A 1 154 ? 33.337 26.879 35.005  1.00 35.75  ? 185  VAL A O   1 
ATOM   876  C CB  A VAL A 1 154 ? 32.508 25.875 31.944  0.50 33.09  ? 185  VAL A CB  1 
ATOM   877  C CB  B VAL A 1 154 ? 32.468 25.858 31.977  0.50 33.06  ? 185  VAL A CB  1 
ATOM   878  C CG1 A VAL A 1 154 ? 32.683 24.646 32.826  0.50 37.74  ? 185  VAL A CG1 1 
ATOM   879  C CG1 B VAL A 1 154 ? 33.682 25.809 31.065  0.50 38.40  ? 185  VAL A CG1 1 
ATOM   880  C CG2 A VAL A 1 154 ? 31.264 25.743 31.077  0.50 30.56  ? 185  VAL A CG2 1 
ATOM   881  C CG2 B VAL A 1 154 ? 32.467 24.646 32.898  0.50 37.82  ? 185  VAL A CG2 1 
ATOM   882  N N   . HIS A 1 155 ? 34.733 27.656 33.424  1.00 31.97  ? 186  HIS A N   1 
ATOM   883  C CA  . HIS A 1 155 ? 35.846 27.766 34.360  1.00 35.80  ? 186  HIS A CA  1 
ATOM   884  C C   . HIS A 1 155 ? 35.522 28.735 35.487  1.00 31.36  ? 186  HIS A C   1 
ATOM   885  O O   . HIS A 1 155 ? 35.760 28.446 36.665  1.00 28.91  ? 186  HIS A O   1 
ATOM   886  C CB  . HIS A 1 155 ? 37.101 28.220 33.619  1.00 40.43  ? 186  HIS A CB  1 
ATOM   887  C CG  . HIS A 1 155 ? 37.641 27.196 32.676  1.00 34.54  ? 186  HIS A CG  1 
ATOM   888  N ND1 . HIS A 1 155 ? 38.501 27.509 31.645  1.00 38.13  ? 186  HIS A ND1 1 
ATOM   889  C CD2 . HIS A 1 155 ? 37.444 25.859 32.610  1.00 33.90  ? 186  HIS A CD2 1 
ATOM   890  C CE1 . HIS A 1 155 ? 38.813 26.407 30.987  1.00 43.99  ? 186  HIS A CE1 1 
ATOM   891  N NE2 . HIS A 1 155 ? 38.185 25.391 31.553  1.00 38.29  ? 186  HIS A NE2 1 
ATOM   892  N N   . LEU A 1 156 ? 35.001 29.908 35.136  1.00 28.49  ? 187  LEU A N   1 
ATOM   893  C CA  . LEU A 1 156 ? 34.696 30.908 36.146  1.00 32.55  ? 187  LEU A CA  1 
ATOM   894  C C   . LEU A 1 156 ? 33.523 30.469 37.008  1.00 37.39  ? 187  LEU A C   1 
ATOM   895  O O   . LEU A 1 156 ? 33.541 30.663 38.229  1.00 33.13  ? 187  LEU A O   1 
ATOM   896  C CB  . LEU A 1 156 ? 34.406 32.247 35.475  1.00 30.68  ? 187  LEU A CB  1 
ATOM   897  C CG  . LEU A 1 156 ? 35.534 32.835 34.622  1.00 34.81  ? 187  LEU A CG  1 
ATOM   898  C CD1 . LEU A 1 156 ? 35.087 34.159 34.017  1.00 31.93  ? 187  LEU A CD1 1 
ATOM   899  C CD2 . LEU A 1 156 ? 36.819 33.019 35.425  1.00 41.16  ? 187  LEU A CD2 1 
ATOM   900  N N   . LEU A 1 157 ? 32.504 29.860 36.396  1.00 30.15  ? 188  LEU A N   1 
ATOM   901  C CA  . LEU A 1 157 ? 31.331 29.442 37.157  1.00 23.32  ? 188  LEU A CA  1 
ATOM   902  C C   . LEU A 1 157 ? 31.676 28.334 38.146  1.00 33.01  ? 188  LEU A C   1 
ATOM   903  O O   . LEU A 1 157 ? 31.199 28.343 39.286  1.00 29.33  ? 188  LEU A O   1 
ATOM   904  C CB  . LEU A 1 157 ? 30.223 28.989 36.206  1.00 29.04  ? 188  LEU A CB  1 
ATOM   905  C CG  . LEU A 1 157 ? 28.918 28.546 36.870  1.00 42.36  ? 188  LEU A CG  1 
ATOM   906  C CD1 . LEU A 1 157 ? 28.396 29.624 37.807  1.00 35.92  ? 188  LEU A CD1 1 
ATOM   907  C CD2 . LEU A 1 157 ? 27.881 28.203 35.811  1.00 38.99  ? 188  LEU A CD2 1 
ATOM   908  N N   . LEU A 1 158 ? 32.500 27.369 37.732  1.00 26.97  ? 189  LEU A N   1 
ATOM   909  C CA  . LEU A 1 158 ? 32.872 26.290 38.642  1.00 30.97  ? 189  LEU A CA  1 
ATOM   910  C C   . LEU A 1 158 ? 33.812 26.779 39.735  1.00 32.34  ? 189  LEU A C   1 
ATOM   911  O O   . LEU A 1 158 ? 33.696 26.359 40.890  1.00 30.21  ? 189  LEU A O   1 
ATOM   912  C CB  . LEU A 1 158 ? 33.521 25.144 37.876  1.00 24.73  ? 189  LEU A CB  1 
ATOM   913  C CG  . LEU A 1 158 ? 32.592 24.272 37.039  1.00 32.46  ? 189  LEU A CG  1 
ATOM   914  C CD1 . LEU A 1 158 ? 33.385 23.106 36.466  1.00 35.88  ? 189  LEU A CD1 1 
ATOM   915  C CD2 . LEU A 1 158 ? 31.404 23.786 37.864  1.00 32.01  ? 189  LEU A CD2 1 
ATOM   916  N N   . ALA A 1 159 ? 34.768 27.643 39.394  1.00 30.23  ? 190  ALA A N   1 
ATOM   917  C CA  . ALA A 1 159 ? 35.602 28.235 40.434  1.00 30.03  ? 190  ALA A CA  1 
ATOM   918  C C   . ALA A 1 159 ? 34.743 28.941 41.476  1.00 28.06  ? 190  ALA A C   1 
ATOM   919  O O   . ALA A 1 159 ? 35.009 28.850 42.680  1.00 29.45  ? 190  ALA A O   1 
ATOM   920  C CB  . ALA A 1 159 ? 36.611 29.203 39.815  1.00 31.77  ? 190  ALA A CB  1 
ATOM   921  N N   . ALA A 1 160 ? 33.682 29.620 41.036  1.00 27.98  ? 191  ALA A N   1 
ATOM   922  C CA  . ALA A 1 160 ? 32.831 30.339 41.978  1.00 28.59  ? 191  ALA A CA  1 
ATOM   923  C C   . ALA A 1 160 ? 31.955 29.389 42.784  1.00 32.17  ? 191  ALA A C   1 
ATOM   924  O O   . ALA A 1 160 ? 31.811 29.557 44.000  1.00 32.81  ? 191  ALA A O   1 
ATOM   925  C CB  . ALA A 1 160 ? 31.958 31.354 41.243  1.00 28.72  ? 191  ALA A CB  1 
ATOM   926  N N   . THR A 1 161 ? 31.350 28.391 42.137  1.00 26.07  ? 192  THR A N   1 
ATOM   927  C CA  . THR A 1 161 ? 30.475 27.496 42.885  1.00 36.95  ? 192  THR A CA  1 
ATOM   928  C C   . THR A 1 161 ? 31.269 26.662 43.877  1.00 25.10  ? 192  THR A C   1 
ATOM   929  O O   . THR A 1 161 ? 30.816 26.430 45.002  1.00 24.70  ? 192  THR A O   1 
ATOM   930  C CB  . THR A 1 161 ? 29.687 26.577 41.953  1.00 34.11  ? 192  THR A CB  1 
ATOM   931  O OG1 . THR A 1 161 ? 30.588 25.798 41.159  1.00 32.73  ? 192  THR A OG1 1 
ATOM   932  C CG2 . THR A 1 161 ? 28.776 27.382 41.066  1.00 32.50  ? 192  THR A CG2 1 
ATOM   933  N N   . TRP A 1 162 ? 32.454 26.197 43.483  1.00 26.90  ? 193  TRP A N   1 
ATOM   934  C CA  . TRP A 1 162 ? 33.250 25.410 44.414  1.00 21.56  ? 193  TRP A CA  1 
ATOM   935  C C   . TRP A 1 162 ? 33.824 26.281 45.524  1.00 30.25  ? 193  TRP A C   1 
ATOM   936  O O   . TRP A 1 162 ? 33.914 25.837 46.672  1.00 27.67  ? 193  TRP A O   1 
ATOM   937  C CB  . TRP A 1 162 ? 34.360 24.671 43.676  1.00 24.25  ? 193  TRP A CB  1 
ATOM   938  C CG  . TRP A 1 162 ? 33.906 23.389 43.036  1.00 26.03  ? 193  TRP A CG  1 
ATOM   939  C CD1 . TRP A 1 162 ? 33.403 23.235 41.775  1.00 28.83  ? 193  TRP A CD1 1 
ATOM   940  C CD2 . TRP A 1 162 ? 33.921 22.082 43.623  1.00 27.40  ? 193  TRP A CD2 1 
ATOM   941  N NE1 . TRP A 1 162 ? 33.101 21.915 41.545  1.00 25.97  ? 193  TRP A NE1 1 
ATOM   942  C CE2 . TRP A 1 162 ? 33.406 21.188 42.665  1.00 32.25  ? 193  TRP A CE2 1 
ATOM   943  C CE3 . TRP A 1 162 ? 34.316 21.582 44.868  1.00 29.82  ? 193  TRP A CE3 1 
ATOM   944  C CZ2 . TRP A 1 162 ? 33.287 19.823 42.908  1.00 29.31  ? 193  TRP A CZ2 1 
ATOM   945  C CZ3 . TRP A 1 162 ? 34.192 20.226 45.108  1.00 23.67  ? 193  TRP A CZ3 1 
ATOM   946  C CH2 . TRP A 1 162 ? 33.684 19.363 44.133  1.00 25.97  ? 193  TRP A CH2 1 
ATOM   947  N N   . THR A 1 163 ? 34.192 27.528 45.214  1.00 25.41  ? 194  THR A N   1 
ATOM   948  C CA  . THR A 1 163 ? 34.670 28.427 46.262  1.00 33.21  ? 194  THR A CA  1 
ATOM   949  C C   . THR A 1 163 ? 33.579 28.686 47.292  1.00 30.51  ? 194  THR A C   1 
ATOM   950  O O   . THR A 1 163 ? 33.840 28.692 48.501  1.00 27.32  ? 194  THR A O   1 
ATOM   951  C CB  . THR A 1 163 ? 35.151 29.748 45.659  1.00 31.20  ? 194  THR A CB  1 
ATOM   952  O OG1 . THR A 1 163 ? 36.242 29.502 44.767  1.00 33.52  ? 194  THR A OG1 1 
ATOM   953  C CG2 . THR A 1 163 ? 35.615 30.701 46.753  1.00 37.13  ? 194  THR A CG2 1 
ATOM   954  N N   . VAL A 1 164 ? 32.346 28.896 46.829  1.00 27.08  ? 195  VAL A N   1 
ATOM   955  C CA  . VAL A 1 164 ? 31.244 29.165 47.742  1.00 28.91  ? 195  VAL A CA  1 
ATOM   956  C C   . VAL A 1 164 ? 30.871 27.907 48.511  1.00 30.46  ? 195  VAL A C   1 
ATOM   957  O O   . VAL A 1 164 ? 30.606 27.955 49.718  1.00 27.63  ? 195  VAL A O   1 
ATOM   958  C CB  . VAL A 1 164 ? 30.046 29.729 46.961  1.00 32.49  ? 195  VAL A CB  1 
ATOM   959  C CG1 . VAL A 1 164 ? 28.798 29.745 47.834  1.00 35.83  ? 195  VAL A CG1 1 
ATOM   960  C CG2 . VAL A 1 164 ? 30.376 31.120 46.431  1.00 30.67  ? 195  VAL A CG2 1 
ATOM   961  N N   . SER A 1 165 ? 30.851 26.763 47.826  1.00 26.29  ? 196  SER A N   1 
ATOM   962  C CA  . SER A 1 165 ? 30.539 25.499 48.483  1.00 25.78  ? 196  SER A CA  1 
ATOM   963  C C   . SER A 1 165 ? 31.502 25.225 49.630  1.00 28.78  ? 196  SER A C   1 
ATOM   964  O O   . SER A 1 165 ? 31.082 24.934 50.757  1.00 30.97  ? 196  SER A O   1 
ATOM   965  C CB  . SER A 1 165 ? 30.582 24.367 47.455  1.00 27.90  ? 196  SER A CB  1 
ATOM   966  O OG  . SER A 1 165 ? 29.534 24.507 46.509  1.00 28.14  ? 196  SER A OG  1 
ATOM   967  N N   . LEU A 1 166 ? 32.804 25.319 49.363  1.00 30.43  ? 197  LEU A N   1 
ATOM   968  C CA  . LEU A 1 166 ? 33.792 25.099 50.413  1.00 33.04  ? 197  LEU A CA  1 
ATOM   969  C C   . LEU A 1 166 ? 33.597 26.080 51.561  1.00 27.87  ? 197  LEU A C   1 
ATOM   970  O O   . LEU A 1 166 ? 33.622 25.697 52.736  1.00 26.00  ? 197  LEU A O   1 
ATOM   971  C CB  . LEU A 1 166 ? 35.203 25.218 49.839  1.00 26.93  ? 197  LEU A CB  1 
ATOM   972  C CG  . LEU A 1 166 ? 35.843 23.898 49.406  1.00 33.73  ? 197  LEU A CG  1 
ATOM   973  C CD1 . LEU A 1 166 ? 35.049 23.288 48.262  1.00 44.59  ? 197  LEU A CD1 1 
ATOM   974  C CD2 . LEU A 1 166 ? 37.306 24.092 49.031  1.00 44.14  ? 197  LEU A CD2 1 
ATOM   975  N N   . GLY A 1 167 ? 33.414 27.359 51.238  1.00 33.07  ? 198  GLY A N   1 
ATOM   976  C CA  . GLY A 1 167 ? 33.161 28.340 52.280  1.00 31.23  ? 198  GLY A CA  1 
ATOM   977  C C   . GLY A 1 167 ? 31.977 27.975 53.155  1.00 36.47  ? 198  GLY A C   1 
ATOM   978  O O   . GLY A 1 167 ? 32.022 28.143 54.376  1.00 27.39  ? 198  GLY A O   1 
ATOM   979  N N   . LEU A 1 168 ? 30.904 27.463 52.547  1.00 29.45  ? 199  LEU A N   1 
ATOM   980  C CA  . LEU A 1 168 ? 29.716 27.115 53.322  1.00 33.62  ? 199  LEU A CA  1 
ATOM   981  C C   . LEU A 1 168 ? 29.997 25.986 54.305  1.00 32.20  ? 199  LEU A C   1 
ATOM   982  O O   . LEU A 1 168 ? 29.437 25.963 55.406  1.00 28.02  ? 199  LEU A O   1 
ATOM   983  C CB  . LEU A 1 168 ? 28.576 26.718 52.392  1.00 25.92  ? 199  LEU A CB  1 
ATOM   984  C CG  . LEU A 1 168 ? 27.929 27.865 51.627  1.00 32.85  ? 199  LEU A CG  1 
ATOM   985  C CD1 . LEU A 1 168 ? 26.946 27.296 50.627  1.00 31.70  ? 199  LEU A CD1 1 
ATOM   986  C CD2 . LEU A 1 168 ? 27.256 28.826 52.588  1.00 32.47  ? 199  LEU A CD2 1 
ATOM   987  N N   . GLY A 1 169 ? 30.834 25.022 53.916  1.00 31.98  ? 200  GLY A N   1 
ATOM   988  C CA  . GLY A 1 169 ? 31.219 23.970 54.838  1.00 25.89  ? 200  GLY A CA  1 
ATOM   989  C C   . GLY A 1 169 ? 32.315 24.367 55.799  1.00 34.74  ? 200  GLY A C   1 
ATOM   990  O O   . GLY A 1 169 ? 32.466 23.729 56.845  1.00 32.61  ? 200  GLY A O   1 
ATOM   991  N N   . LEU A 1 170 ? 33.073 25.416 55.471  1.00 28.31  ? 201  LEU A N   1 
ATOM   992  C CA  . LEU A 1 170 ? 34.158 25.866 56.332  1.00 28.39  ? 201  LEU A CA  1 
ATOM   993  C C   . LEU A 1 170 ? 33.650 26.700 57.496  1.00 32.80  ? 201  LEU A C   1 
ATOM   994  O O   . LEU A 1 170 ? 34.278 26.720 58.559  1.00 30.36  ? 201  LEU A O   1 
ATOM   995  C CB  . LEU A 1 170 ? 35.157 26.690 55.523  1.00 35.10  ? 201  LEU A CB  1 
ATOM   996  C CG  . LEU A 1 170 ? 36.608 26.683 55.986  1.00 67.70  ? 201  LEU A CG  1 
ATOM   997  C CD1 . LEU A 1 170 ? 37.214 25.323 55.701  1.00 65.76  ? 201  LEU A CD1 1 
ATOM   998  C CD2 . LEU A 1 170 ? 37.374 27.798 55.291  1.00 62.15  ? 201  LEU A CD2 1 
ATOM   999  N N   . LEU A 1 171 ? 32.539 27.406 57.308  1.00 34.69  ? 202  LEU A N   1 
ATOM   1000 C CA  . LEU A 1 171 ? 32.031 28.274 58.368  1.00 40.24  ? 202  LEU A CA  1 
ATOM   1001 C C   . LEU A 1 171 ? 31.777 27.515 59.661  1.00 30.11  ? 202  LEU A C   1 
ATOM   1002 O O   . LEU A 1 171 ? 32.219 27.985 60.724  1.00 31.66  ? 202  LEU A O   1 
ATOM   1003 C CB  . LEU A 1 171 ? 30.769 28.986 57.873  1.00 33.94  ? 202  LEU A CB  1 
ATOM   1004 C CG  . LEU A 1 171 ? 31.046 30.084 56.842  1.00 39.36  ? 202  LEU A CG  1 
ATOM   1005 C CD1 . LEU A 1 171 ? 29.755 30.522 56.166  1.00 35.12  ? 202  LEU A CD1 1 
ATOM   1006 C CD2 . LEU A 1 171 ? 31.750 31.274 57.482  1.00 40.08  ? 202  LEU A CD2 1 
ATOM   1007 N N   . PRO A 1 172 ? 31.090 26.370 59.661  1.00 32.01  ? 203  PRO A N   1 
ATOM   1008 C CA  . PRO A 1 172 ? 30.919 25.640 60.928  1.00 36.79  ? 203  PRO A CA  1 
ATOM   1009 C C   . PRO A 1 172 ? 32.227 25.151 61.521  1.00 30.81  ? 203  PRO A C   1 
ATOM   1010 O O   . PRO A 1 172 ? 32.366 25.128 62.749  1.00 36.53  ? 203  PRO A O   1 
ATOM   1011 C CB  . PRO A 1 172 ? 29.994 24.475 60.546  1.00 34.37  ? 203  PRO A CB  1 
ATOM   1012 C CG  . PRO A 1 172 ? 30.054 24.383 59.059  1.00 33.27  ? 203  PRO A CG  1 
ATOM   1013 C CD  . PRO A 1 172 ? 30.311 25.768 58.566  1.00 35.48  ? 203  PRO A CD  1 
ATOM   1014 N N   . VAL A 1 173 ? 33.195 24.764 60.688  1.00 31.86  ? 204  VAL A N   1 
ATOM   1015 C CA  . VAL A 1 173 ? 34.484 24.321 61.210  1.00 34.14  ? 204  VAL A CA  1 
ATOM   1016 C C   . VAL A 1 173 ? 35.206 25.468 61.902  1.00 33.38  ? 204  VAL A C   1 
ATOM   1017 O O   . VAL A 1 173 ? 35.903 25.266 62.904  1.00 29.27  ? 204  VAL A O   1 
ATOM   1018 C CB  . VAL A 1 173 ? 35.337 23.722 60.078  1.00 33.34  ? 204  VAL A CB  1 
ATOM   1019 C CG1 . VAL A 1 173 ? 36.720 23.344 60.591  1.00 39.82  ? 204  VAL A CG1 1 
ATOM   1020 C CG2 . VAL A 1 173 ? 34.632 22.517 59.478  1.00 29.71  ? 204  VAL A CG2 1 
ATOM   1021 N N   . LEU A 1 174 ? 35.051 26.687 61.386  1.00 29.81  ? 205  LEU A N   1 
ATOM   1022 C CA  . LEU A 1 174 ? 35.720 27.835 61.983  1.00 32.43  ? 205  LEU A CA  1 
ATOM   1023 C C   . LEU A 1 174 ? 35.007 28.339 63.227  1.00 32.86  ? 205  LEU A C   1 
ATOM   1024 O O   . LEU A 1 174 ? 35.598 29.110 63.991  1.00 45.10  ? 205  LEU A O   1 
ATOM   1025 C CB  . LEU A 1 174 ? 35.839 28.963 60.956  1.00 29.40  ? 205  LEU A CB  1 
ATOM   1026 C CG  . LEU A 1 174 ? 36.749 28.673 59.755  1.00 38.99  ? 205  LEU A CG  1 
ATOM   1027 C CD1 . LEU A 1 174 ? 36.687 29.809 58.743  1.00 53.27  ? 205  LEU A CD1 1 
ATOM   1028 C CD2 . LEU A 1 174 ? 38.192 28.433 60.193  1.00 43.91  ? 205  LEU A CD2 1 
ATOM   1029 N N   . GLY A 1 175 ? 33.759 27.929 63.446  1.00 43.44  ? 206  GLY A N   1 
ATOM   1030 C CA  . GLY A 1 175 ? 33.095 28.207 64.704  1.00 36.87  ? 206  GLY A CA  1 
ATOM   1031 C C   . GLY A 1 175 ? 31.632 28.585 64.598  1.00 38.49  ? 206  GLY A C   1 
ATOM   1032 O O   . GLY A 1 175 ? 30.982 28.774 65.628  1.00 40.58  ? 206  GLY A O   1 
ATOM   1033 N N   . TRP A 1 176 ? 31.087 28.695 63.384  1.00 38.75  ? 207  TRP A N   1 
ATOM   1034 C CA  . TRP A 1 176 ? 29.663 28.998 63.226  1.00 41.46  ? 207  TRP A CA  1 
ATOM   1035 C C   . TRP A 1 176 ? 28.900 27.684 63.357  1.00 34.81  ? 207  TRP A C   1 
ATOM   1036 O O   . TRP A 1 176 ? 28.433 27.086 62.384  1.00 30.77  ? 207  TRP A O   1 
ATOM   1037 C CB  . TRP A 1 176 ? 29.378 29.690 61.902  1.00 40.18  ? 207  TRP A CB  1 
ATOM   1038 C CG  . TRP A 1 176 ? 27.955 30.183 61.790  1.00 38.13  ? 207  TRP A CG  1 
ATOM   1039 C CD1 . TRP A 1 176 ? 27.011 30.197 62.776  1.00 50.66  ? 207  TRP A CD1 1 
ATOM   1040 C CD2 . TRP A 1 176 ? 27.320 30.727 60.624  1.00 38.22  ? 207  TRP A CD2 1 
ATOM   1041 N NE1 . TRP A 1 176 ? 25.830 30.712 62.296  1.00 41.53  ? 207  TRP A NE1 1 
ATOM   1042 C CE2 . TRP A 1 176 ? 25.994 31.045 60.978  1.00 37.43  ? 207  TRP A CE2 1 
ATOM   1043 C CE3 . TRP A 1 176 ? 27.744 30.970 59.315  1.00 39.73  ? 207  TRP A CE3 1 
ATOM   1044 C CZ2 . TRP A 1 176 ? 25.092 31.599 60.073  1.00 40.26  ? 207  TRP A CZ2 1 
ATOM   1045 C CZ3 . TRP A 1 176 ? 26.848 31.520 58.420  1.00 41.66  ? 207  TRP A CZ3 1 
ATOM   1046 C CH2 . TRP A 1 176 ? 25.537 31.828 58.802  1.00 41.96  ? 207  TRP A CH2 1 
ATOM   1047 N N   . ASN A 1 177 ? 28.776 27.236 64.599  1.00 34.22  ? 208  ASN A N   1 
ATOM   1048 C CA  . ASN A 1 177 ? 28.158 25.963 64.922  1.00 35.34  ? 208  ASN A CA  1 
ATOM   1049 C C   . ASN A 1 177 ? 27.483 26.117 66.275  1.00 38.68  ? 208  ASN A C   1 
ATOM   1050 O O   . ASN A 1 177 ? 27.460 27.209 66.852  1.00 37.69  ? 208  ASN A O   1 
ATOM   1051 C CB  . ASN A 1 177 ? 29.197 24.838 64.929  1.00 38.32  ? 208  ASN A CB  1 
ATOM   1052 C CG  . ASN A 1 177 ? 30.309 25.087 65.925  1.00 38.61  ? 208  ASN A CG  1 
ATOM   1053 O OD1 . ASN A 1 177 ? 30.078 25.108 67.128  1.00 37.42  ? 208  ASN A OD1 1 
ATOM   1054 N ND2 . ASN A 1 177 ? 31.524 25.266 65.428  1.00 38.83  ? 208  ASN A ND2 1 
ATOM   1055 N N   . CYS A 1 178 ? 26.946 25.017 66.797  1.00 37.33  ? 209  CYS A N   1 
ATOM   1056 C CA  . CYS A 1 178 ? 26.190 25.048 68.041  1.00 47.25  ? 209  CYS A CA  1 
ATOM   1057 C C   . CYS A 1 178 ? 26.888 24.309 69.179  1.00 50.27  ? 209  CYS A C   1 
ATOM   1058 O O   . CYS A 1 178 ? 26.257 24.025 70.202  1.00 48.58  ? 209  CYS A O   1 
ATOM   1059 C CB  . CYS A 1 178 ? 24.793 24.470 67.814  1.00 39.17  ? 209  CYS A CB  1 
ATOM   1060 S SG  . CYS A 1 178 ? 24.706 22.671 67.632  1.00 46.47  ? 209  CYS A SG  1 
ATOM   1061 N N   . LEU A 1 179 ? 28.181 24.007 69.034  1.00 46.16  ? 210  LEU A N   1 
ATOM   1062 C CA  . LEU A 1 179 ? 28.885 23.265 70.076  1.00 56.67  ? 210  LEU A CA  1 
ATOM   1063 C C   . LEU A 1 179 ? 28.827 23.986 71.418  1.00 50.30  ? 210  LEU A C   1 
ATOM   1064 O O   . LEU A 1 179 ? 28.705 23.346 72.469  1.00 59.34  ? 210  LEU A O   1 
ATOM   1065 C CB  . LEU A 1 179 ? 30.336 23.033 69.662  1.00 48.67  ? 210  LEU A CB  1 
ATOM   1066 C CG  . LEU A 1 179 ? 30.507 22.071 68.490  1.00 50.41  ? 210  LEU A CG  1 
ATOM   1067 C CD1 . LEU A 1 179 ? 31.933 22.101 67.972  1.00 58.94  ? 210  LEU A CD1 1 
ATOM   1068 C CD2 . LEU A 1 179 ? 30.106 20.664 68.910  1.00 48.76  ? 210  LEU A CD2 1 
ATOM   1069 N N   . ALA A 1 180 ? 28.906 25.317 71.405  1.00 45.61  ? 211  ALA A N   1 
ATOM   1070 C CA  . ALA A 1 180 ? 28.869 26.069 72.655  1.00 72.34  ? 211  ALA A CA  1 
ATOM   1071 C C   . ALA A 1 180 ? 27.441 26.252 73.155  1.00 70.10  ? 211  ALA A C   1 
ATOM   1072 O O   . ALA A 1 180 ? 27.160 26.047 74.341  1.00 82.86  ? 211  ALA A O   1 
ATOM   1073 C CB  . ALA A 1 180 ? 29.545 27.428 72.468  1.00 71.99  ? 211  ALA A CB  1 
ATOM   1074 N N   . GLU A 1 181 ? 26.529 26.634 72.266  1.00 68.42  ? 212  GLU A N   1 
ATOM   1075 C CA  . GLU A 1 181 ? 25.140 26.929 72.612  1.00 68.28  ? 212  GLU A CA  1 
ATOM   1076 C C   . GLU A 1 181 ? 24.263 25.835 72.010  1.00 71.41  ? 212  GLU A C   1 
ATOM   1077 O O   . GLU A 1 181 ? 23.933 25.875 70.821  1.00 65.63  ? 212  GLU A O   1 
ATOM   1078 C CB  . GLU A 1 181 ? 24.749 28.315 72.103  1.00 74.66  ? 212  GLU A CB  1 
ATOM   1079 C CG  . GLU A 1 181 ? 23.371 28.791 72.539  1.00 89.76  ? 212  GLU A CG  1 
ATOM   1080 C CD  . GLU A 1 181 ? 23.003 30.135 71.935  1.00 102.00 ? 212  GLU A CD  1 
ATOM   1081 O OE1 . GLU A 1 181 ? 23.897 30.800 71.370  1.00 97.96  ? 212  GLU A OE1 1 
ATOM   1082 O OE2 . GLU A 1 181 ? 21.818 30.523 72.022  1.00 103.79 ? 212  GLU A OE2 1 
ATOM   1083 N N   . ARG A 1 182 ? 23.888 24.854 72.836  1.00 64.28  ? 213  ARG A N   1 
ATOM   1084 C CA  . ARG A 1 182 ? 23.083 23.740 72.350  1.00 74.49  ? 213  ARG A CA  1 
ATOM   1085 C C   . ARG A 1 182 ? 21.655 24.160 72.023  1.00 71.47  ? 213  ARG A C   1 
ATOM   1086 O O   . ARG A 1 182 ? 20.984 23.481 71.237  1.00 51.44  ? 213  ARG A O   1 
ATOM   1087 C CB  . ARG A 1 182 ? 23.070 22.609 73.382  1.00 71.60  ? 213  ARG A CB  1 
ATOM   1088 C CG  . ARG A 1 182 ? 22.684 21.250 72.804  1.00 95.27  ? 213  ARG A CG  1 
ATOM   1089 C CD  . ARG A 1 182 ? 22.396 20.237 73.901  1.00 102.46 ? 213  ARG A CD  1 
ATOM   1090 N NE  . ARG A 1 182 ? 21.285 20.668 74.743  1.00 118.28 ? 213  ARG A NE  1 
ATOM   1091 C CZ  . ARG A 1 182 ? 20.005 20.506 74.437  1.00 103.70 ? 213  ARG A CZ  1 
ATOM   1092 N NH1 . ARG A 1 182 ? 19.630 19.897 73.323  1.00 111.30 ? 213  ARG A NH1 1 
ATOM   1093 N NH2 . ARG A 1 182 ? 19.076 20.973 75.267  1.00 79.31  ? 213  ARG A NH2 1 
ATOM   1094 N N   . ALA A 1 183 ? 21.173 25.260 72.606  1.00 51.00  ? 214  ALA A N   1 
ATOM   1095 C CA  . ALA A 1 183 ? 19.853 25.767 72.253  1.00 66.05  ? 214  ALA A CA  1 
ATOM   1096 C C   . ALA A 1 183 ? 19.796 26.264 70.814  1.00 67.62  ? 214  ALA A C   1 
ATOM   1097 O O   . ALA A 1 183 ? 18.699 26.413 70.266  1.00 60.17  ? 214  ALA A O   1 
ATOM   1098 C CB  . ALA A 1 183 ? 19.449 26.896 73.204  1.00 52.03  ? 214  ALA A CB  1 
ATOM   1099 N N   . ALA A 1 184 ? 20.947 26.522 70.196  1.00 62.20  ? 215  ALA A N   1 
ATOM   1100 C CA  . ALA A 1 184 ? 21.015 27.023 68.833  1.00 51.53  ? 215  ALA A CA  1 
ATOM   1101 C C   . ALA A 1 184 ? 21.228 25.913 67.815  1.00 42.81  ? 215  ALA A C   1 
ATOM   1102 O O   . ALA A 1 184 ? 21.405 26.206 66.630  1.00 42.21  ? 215  ALA A O   1 
ATOM   1103 C CB  . ALA A 1 184 ? 22.133 28.061 68.714  1.00 48.08  ? 215  ALA A CB  1 
ATOM   1104 N N   . CYS A 1 185 ? 21.208 24.652 68.244  1.00 37.78  ? 216  CYS A N   1 
ATOM   1105 C CA  . CYS A 1 185 ? 21.471 23.547 67.333  1.00 36.78  ? 216  CYS A CA  1 
ATOM   1106 C C   . CYS A 1 185 ? 20.316 23.342 66.362  1.00 40.33  ? 216  CYS A C   1 
ATOM   1107 O O   . CYS A 1 185 ? 19.141 23.465 66.720  1.00 43.17  ? 216  CYS A O   1 
ATOM   1108 C CB  . CYS A 1 185 ? 21.716 22.251 68.109  1.00 58.17  ? 216  CYS A CB  1 
ATOM   1109 S SG  . CYS A 1 185 ? 23.285 22.178 69.023  1.00 63.70  ? 216  CYS A SG  1 
ATOM   1110 N N   . SER A 1 186 ? 20.667 23.017 65.127  1.00 41.46  ? 217  SER A N   1 
ATOM   1111 C CA  . SER A 1 186 ? 19.693 22.596 64.135  1.00 32.25  ? 217  SER A CA  1 
ATOM   1112 C C   . SER A 1 186 ? 19.408 21.107 64.303  1.00 43.00  ? 217  SER A C   1 
ATOM   1113 O O   . SER A 1 186 ? 19.888 20.454 65.235  1.00 35.72  ? 217  SER A O   1 
ATOM   1114 C CB  . SER A 1 186 ? 20.209 22.902 62.735  1.00 38.98  ? 217  SER A CB  1 
ATOM   1115 O OG  . SER A 1 186 ? 21.244 22.002 62.381  1.00 34.93  ? 217  SER A OG  1 
ATOM   1116 N N   . VAL A 1 187 ? 18.616 20.555 63.381  1.00 35.61  ? 218  VAL A N   1 
ATOM   1117 C CA  . VAL A 1 187 ? 18.322 19.129 63.394  1.00 37.53  ? 218  VAL A CA  1 
ATOM   1118 C C   . VAL A 1 187 ? 19.497 18.288 62.926  1.00 36.06  ? 218  VAL A C   1 
ATOM   1119 O O   . VAL A 1 187 ? 19.468 17.065 63.081  1.00 40.11  ? 218  VAL A O   1 
ATOM   1120 C CB  . VAL A 1 187 ? 17.089 18.826 62.518  1.00 36.87  ? 218  VAL A CB  1 
ATOM   1121 C CG1 . VAL A 1 187 ? 15.878 19.579 63.039  1.00 36.22  ? 218  VAL A CG1 1 
ATOM   1122 C CG2 . VAL A 1 187 ? 17.371 19.176 61.058  1.00 31.72  ? 218  VAL A CG2 1 
ATOM   1123 N N   . VAL A 1 188 ? 20.517 18.908 62.341  1.00 29.90  ? 219  VAL A N   1 
ATOM   1124 C CA  . VAL A 1 188 ? 21.740 18.227 61.929  1.00 39.88  ? 219  VAL A CA  1 
ATOM   1125 C C   . VAL A 1 188 ? 22.850 18.745 62.837  1.00 37.35  ? 219  VAL A C   1 
ATOM   1126 O O   . VAL A 1 188 ? 23.354 19.854 62.635  1.00 36.19  ? 219  VAL A O   1 
ATOM   1127 C CB  . VAL A 1 188 ? 22.065 18.475 60.450  1.00 42.77  ? 219  VAL A CB  1 
ATOM   1128 C CG1 . VAL A 1 188 ? 23.431 17.909 60.097  1.00 47.35  ? 219  VAL A CG1 1 
ATOM   1129 C CG2 . VAL A 1 188 ? 20.987 17.878 59.549  1.00 43.55  ? 219  VAL A CG2 1 
ATOM   1130 N N   . ARG A 1 189 ? 23.242 17.955 63.851  1.00 38.81  ? 220  ARG A N   1 
ATOM   1131 C CA  A ARG A 1 189 ? 24.293 18.396 64.756  0.50 40.28  ? 220  ARG A CA  1 
ATOM   1132 C CA  B ARG A 1 189 ? 24.291 18.406 64.751  0.50 40.28  ? 220  ARG A CA  1 
ATOM   1133 C C   . ARG A 1 189 ? 25.655 18.303 64.069  1.00 37.89  ? 220  ARG A C   1 
ATOM   1134 O O   . ARG A 1 189 ? 25.880 17.416 63.240  1.00 39.31  ? 220  ARG A O   1 
ATOM   1135 C CB  A ARG A 1 189 ? 24.323 17.548 66.023  0.50 51.00  ? 220  ARG A CB  1 
ATOM   1136 C CB  B ARG A 1 189 ? 24.303 17.576 66.031  0.50 51.00  ? 220  ARG A CB  1 
ATOM   1137 C CG  A ARG A 1 189 ? 22.982 17.305 66.684  0.50 59.71  ? 220  ARG A CG  1 
ATOM   1138 C CG  B ARG A 1 189 ? 22.941 17.352 66.670  0.50 59.72  ? 220  ARG A CG  1 
ATOM   1139 C CD  A ARG A 1 189 ? 22.398 18.558 67.306  0.50 63.02  ? 220  ARG A CD  1 
ATOM   1140 C CD  B ARG A 1 189 ? 22.256 18.653 67.053  0.50 62.63  ? 220  ARG A CD  1 
ATOM   1141 N NE  A ARG A 1 189 ? 21.356 18.203 68.260  0.50 69.00  ? 220  ARG A NE  1 
ATOM   1142 N NE  B ARG A 1 189 ? 21.142 18.408 67.963  0.50 69.39  ? 220  ARG A NE  1 
ATOM   1143 C CZ  A ARG A 1 189 ? 20.151 17.765 67.921  0.50 62.28  ? 220  ARG A CZ  1 
ATOM   1144 C CZ  B ARG A 1 189 ? 21.262 18.277 69.278  0.50 63.98  ? 220  ARG A CZ  1 
ATOM   1145 N NH1 A ARG A 1 189 ? 19.784 17.667 66.653  0.50 47.08  ? 220  ARG A NH1 1 
ATOM   1146 N NH1 B ARG A 1 189 ? 22.434 18.396 69.882  0.50 67.60  ? 220  ARG A NH1 1 
ATOM   1147 N NH2 A ARG A 1 189 ? 19.297 17.410 68.875  0.50 57.39  ? 220  ARG A NH2 1 
ATOM   1148 N NH2 B ARG A 1 189 ? 20.180 18.017 70.005  0.50 67.06  ? 220  ARG A NH2 1 
ATOM   1149 N N   . PRO A 1 190 ? 26.594 19.209 64.403  1.00 36.11  ? 221  PRO A N   1 
ATOM   1150 C CA  . PRO A 1 190 ? 26.519 20.356 65.313  1.00 37.04  ? 221  PRO A CA  1 
ATOM   1151 C C   . PRO A 1 190 ? 26.280 21.673 64.575  1.00 40.40  ? 221  PRO A C   1 
ATOM   1152 O O   . PRO A 1 190 ? 26.782 22.715 64.989  1.00 37.79  ? 221  PRO A O   1 
ATOM   1153 C CB  . PRO A 1 190 ? 27.895 20.348 65.983  1.00 47.83  ? 221  PRO A CB  1 
ATOM   1154 C CG  . PRO A 1 190 ? 28.819 19.695 64.963  1.00 45.07  ? 221  PRO A CG  1 
ATOM   1155 C CD  . PRO A 1 190 ? 27.965 19.039 63.895  1.00 39.44  ? 221  PRO A CD  1 
ATOM   1156 N N   . LEU A 1 191 ? 25.527 21.624 63.481  1.00 32.00  ? 222  LEU A N   1 
ATOM   1157 C CA  . LEU A 1 191 ? 25.269 22.832 62.712  1.00 37.71  ? 222  LEU A CA  1 
ATOM   1158 C C   . LEU A 1 191 ? 24.300 23.745 63.451  1.00 33.23  ? 222  LEU A C   1 
ATOM   1159 O O   . LEU A 1 191 ? 23.311 23.289 64.031  1.00 36.41  ? 222  LEU A O   1 
ATOM   1160 C CB  . LEU A 1 191 ? 24.704 22.481 61.337  1.00 35.58  ? 222  LEU A CB  1 
ATOM   1161 C CG  . LEU A 1 191 ? 25.613 21.611 60.474  1.00 37.93  ? 222  LEU A CG  1 
ATOM   1162 C CD1 . LEU A 1 191 ? 24.965 21.365 59.134  1.00 31.08  ? 222  LEU A CD1 1 
ATOM   1163 C CD2 . LEU A 1 191 ? 26.983 22.257 60.304  1.00 36.53  ? 222  LEU A CD2 1 
ATOM   1164 N N   . ALA A 1 192 ? 24.588 25.044 63.411  1.00 34.56  ? 223  ALA A N   1 
ATOM   1165 C CA  . ALA A 1 192 ? 23.712 26.045 64.000  1.00 30.44  ? 223  ALA A CA  1 
ATOM   1166 C C   . ALA A 1 192 ? 22.504 26.295 63.106  1.00 35.20  ? 223  ALA A C   1 
ATOM   1167 O O   . ALA A 1 192 ? 22.611 26.288 61.876  1.00 32.75  ? 223  ALA A O   1 
ATOM   1168 C CB  . ALA A 1 192 ? 24.474 27.351 64.218  1.00 35.90  ? 223  ALA A CB  1 
ATOM   1169 N N   . ARG A 1 193 ? 21.350 26.529 63.739  1.00 31.04  ? 224  ARG A N   1 
ATOM   1170 C CA  A ARG A 1 193 ? 20.123 26.749 62.980  0.50 39.15  ? 224  ARG A CA  1 
ATOM   1171 C CA  B ARG A 1 193 ? 20.121 26.750 62.985  0.50 39.15  ? 224  ARG A CA  1 
ATOM   1172 C C   . ARG A 1 193 ? 20.269 27.907 62.003  1.00 33.99  ? 224  ARG A C   1 
ATOM   1173 O O   . ARG A 1 193 ? 19.711 27.869 60.899  1.00 31.88  ? 224  ARG A O   1 
ATOM   1174 C CB  A ARG A 1 193 ? 18.949 27.009 63.924  0.50 40.20  ? 224  ARG A CB  1 
ATOM   1175 C CB  B ARG A 1 193 ? 18.963 27.007 63.952  0.50 40.22  ? 224  ARG A CB  1 
ATOM   1176 C CG  A ARG A 1 193 ? 18.296 25.748 64.454  0.50 42.44  ? 224  ARG A CG  1 
ATOM   1177 C CG  B ARG A 1 193 ? 17.604 26.839 63.308  0.50 45.29  ? 224  ARG A CG  1 
ATOM   1178 C CD  A ARG A 1 193 ? 16.921 26.031 65.037  0.50 48.67  ? 224  ARG A CD  1 
ATOM   1179 C CD  B ARG A 1 193 ? 16.471 26.720 64.311  0.50 54.48  ? 224  ARG A CD  1 
ATOM   1180 N NE  A ARG A 1 193 ? 16.958 27.113 66.012  0.50 50.14  ? 224  ARG A NE  1 
ATOM   1181 N NE  B ARG A 1 193 ? 15.229 26.351 63.641  0.50 56.13  ? 224  ARG A NE  1 
ATOM   1182 C CZ  A ARG A 1 193 ? 17.400 26.984 67.255  0.50 50.16  ? 224  ARG A CZ  1 
ATOM   1183 C CZ  B ARG A 1 193 ? 14.075 26.130 64.256  0.50 58.80  ? 224  ARG A CZ  1 
ATOM   1184 N NH1 A ARG A 1 193 ? 17.862 25.829 67.708  0.50 44.61  ? 224  ARG A NH1 1 
ATOM   1185 N NH1 B ARG A 1 193 ? 13.959 26.236 65.569  0.50 54.00  ? 224  ARG A NH1 1 
ATOM   1186 N NH2 A ARG A 1 193 ? 17.383 28.041 68.062  0.50 46.70  ? 224  ARG A NH2 1 
ATOM   1187 N NH2 B ARG A 1 193 ? 13.010 25.794 63.534  0.50 46.91  ? 224  ARG A NH2 1 
ATOM   1188 N N   . SER A 1 194 ? 21.004 28.952 62.390  1.00 34.32  ? 225  SER A N   1 
ATOM   1189 C CA  . SER A 1 194 ? 21.146 30.110 61.511  1.00 34.08  ? 225  SER A CA  1 
ATOM   1190 C C   . SER A 1 194 ? 22.000 29.786 60.291  1.00 34.58  ? 225  SER A C   1 
ATOM   1191 O O   . SER A 1 194 ? 21.749 30.306 59.197  1.00 37.47  ? 225  SER A O   1 
ATOM   1192 C CB  . SER A 1 194 ? 21.752 31.280 62.283  1.00 31.91  ? 225  SER A CB  1 
ATOM   1193 O OG  . SER A 1 194 ? 23.017 30.926 62.815  1.00 42.08  ? 225  SER A OG  1 
ATOM   1194 N N   . HIS A 1 195 ? 23.012 28.937 60.460  1.00 33.04  ? 226  HIS A N   1 
ATOM   1195 C CA  . HIS A 1 195 ? 23.809 28.492 59.323  1.00 32.57  ? 226  HIS A CA  1 
ATOM   1196 C C   . HIS A 1 195 ? 22.996 27.590 58.401  1.00 36.14  ? 226  HIS A C   1 
ATOM   1197 O O   . HIS A 1 195 ? 23.072 27.713 57.172  1.00 29.50  ? 226  HIS A O   1 
ATOM   1198 C CB  . HIS A 1 195 ? 25.051 27.765 59.828  1.00 31.23  ? 226  HIS A CB  1 
ATOM   1199 C CG  . HIS A 1 195 ? 25.870 27.139 58.743  1.00 31.49  ? 226  HIS A CG  1 
ATOM   1200 N ND1 . HIS A 1 195 ? 26.039 25.776 58.631  1.00 33.75  ? 226  HIS A ND1 1 
ATOM   1201 C CD2 . HIS A 1 195 ? 26.569 27.690 57.724  1.00 28.28  ? 226  HIS A CD2 1 
ATOM   1202 C CE1 . HIS A 1 195 ? 26.804 25.514 57.587  1.00 31.27  ? 226  HIS A CE1 1 
ATOM   1203 N NE2 . HIS A 1 195 ? 27.140 26.659 57.019  1.00 29.19  ? 226  HIS A NE2 1 
ATOM   1204 N N   . VAL A 1 196 ? 22.215 26.675 58.979  1.00 38.62  ? 227  VAL A N   1 
ATOM   1205 C CA  . VAL A 1 196 ? 21.380 25.784 58.183  1.00 29.67  ? 227  VAL A CA  1 
ATOM   1206 C C   . VAL A 1 196 ? 20.306 26.566 57.442  1.00 35.67  ? 227  VAL A C   1 
ATOM   1207 O O   . VAL A 1 196 ? 19.941 26.220 56.311  1.00 31.85  ? 227  VAL A O   1 
ATOM   1208 C CB  . VAL A 1 196 ? 20.773 24.701 59.093  1.00 38.09  ? 227  VAL A CB  1 
ATOM   1209 C CG1 . VAL A 1 196 ? 19.691 23.924 58.364  1.00 44.38  ? 227  VAL A CG1 1 
ATOM   1210 C CG2 . VAL A 1 196 ? 21.870 23.773 59.590  1.00 34.96  ? 227  VAL A CG2 1 
ATOM   1211 N N   . ALA A 1 197 ? 19.790 27.631 58.055  1.00 32.46  ? 228  ALA A N   1 
ATOM   1212 C CA  . ALA A 1 197 ? 18.835 28.492 57.368  1.00 35.56  ? 228  ALA A CA  1 
ATOM   1213 C C   . ALA A 1 197 ? 19.443 29.083 56.105  1.00 31.34  ? 228  ALA A C   1 
ATOM   1214 O O   . ALA A 1 197 ? 18.784 29.159 55.062  1.00 33.34  ? 228  ALA A O   1 
ATOM   1215 C CB  . ALA A 1 197 ? 18.375 29.605 58.308  1.00 36.22  ? 228  ALA A CB  1 
ATOM   1216 N N   . LEU A 1 198 ? 20.696 29.532 56.194  1.00 37.57  ? 229  LEU A N   1 
ATOM   1217 C CA  . LEU A 1 198 ? 21.407 30.024 55.021  1.00 39.55  ? 229  LEU A CA  1 
ATOM   1218 C C   . LEU A 1 198 ? 21.538 28.938 53.962  1.00 35.11  ? 229  LEU A C   1 
ATOM   1219 O O   . LEU A 1 198 ? 21.329 29.193 52.771  1.00 32.04  ? 229  LEU A O   1 
ATOM   1220 C CB  . LEU A 1 198 ? 22.784 30.532 55.441  1.00 41.18  ? 229  LEU A CB  1 
ATOM   1221 C CG  . LEU A 1 198 ? 23.757 30.883 54.320  1.00 41.69  ? 229  LEU A CG  1 
ATOM   1222 C CD1 . LEU A 1 198 ? 23.189 32.010 53.485  1.00 44.48  ? 229  LEU A CD1 1 
ATOM   1223 C CD2 . LEU A 1 198 ? 25.113 31.250 54.901  1.00 38.15  ? 229  LEU A CD2 1 
ATOM   1224 N N   . LEU A 1 199 ? 21.898 27.721 54.378  1.00 32.92  ? 230  LEU A N   1 
ATOM   1225 C CA  . LEU A 1 199 ? 22.011 26.620 53.430  1.00 27.16  ? 230  LEU A CA  1 
ATOM   1226 C C   . LEU A 1 199 ? 20.695 26.378 52.706  1.00 38.28  ? 230  LEU A C   1 
ATOM   1227 O O   . LEU A 1 199 ? 20.678 26.180 51.485  1.00 28.95  ? 230  LEU A O   1 
ATOM   1228 C CB  . LEU A 1 199 ? 22.455 25.350 54.151  1.00 26.61  ? 230  LEU A CB  1 
ATOM   1229 C CG  . LEU A 1 199 ? 23.865 25.359 54.743  1.00 30.67  ? 230  LEU A CG  1 
ATOM   1230 C CD1 . LEU A 1 199 ? 24.200 23.998 55.356  1.00 32.56  ? 230  LEU A CD1 1 
ATOM   1231 C CD2 . LEU A 1 199 ? 24.890 25.736 53.692  1.00 32.10  ? 230  LEU A CD2 1 
ATOM   1232 N N   . SER A 1 200 ? 19.581 26.384 53.446  1.00 32.04  ? 231  SER A N   1 
ATOM   1233 C CA  . SER A 1 200 ? 18.282 26.151 52.828  1.00 34.49  ? 231  SER A CA  1 
ATOM   1234 C C   . SER A 1 200 ? 17.905 27.302 51.913  1.00 32.28  ? 231  SER A C   1 
ATOM   1235 O O   . SER A 1 200 ? 17.323 27.086 50.846  1.00 32.57  ? 231  SER A O   1 
ATOM   1236 C CB  . SER A 1 200 ? 17.207 25.954 53.897  1.00 36.27  ? 231  SER A CB  1 
ATOM   1237 O OG  . SER A 1 200 ? 17.297 24.668 54.484  1.00 51.90  ? 231  SER A OG  1 
ATOM   1238 N N   . ALA A 1 201 ? 18.217 28.534 52.321  1.00 32.97  ? 232  ALA A N   1 
ATOM   1239 C CA  . ALA A 1 201 ? 17.968 29.676 51.451  1.00 38.99  ? 232  ALA A CA  1 
ATOM   1240 C C   . ALA A 1 201 ? 18.735 29.537 50.147  1.00 31.59  ? 232  ALA A C   1 
ATOM   1241 O O   . ALA A 1 201 ? 18.200 29.819 49.069  1.00 35.82  ? 232  ALA A O   1 
ATOM   1242 C CB  . ALA A 1 201 ? 18.353 30.974 52.160  1.00 34.70  ? 232  ALA A CB  1 
ATOM   1243 N N   . ALA A 1 202 ? 19.992 29.093 50.224  1.00 35.93  ? 233  ALA A N   1 
ATOM   1244 C CA  . ALA A 1 202 ? 20.782 28.915 49.012  1.00 31.53  ? 233  ALA A CA  1 
ATOM   1245 C C   . ALA A 1 202 ? 20.195 27.817 48.143  1.00 34.87  ? 233  ALA A C   1 
ATOM   1246 O O   . ALA A 1 202 ? 20.148 27.946 46.914  1.00 33.47  ? 233  ALA A O   1 
ATOM   1247 C CB  . ALA A 1 202 ? 22.233 28.594 49.365  1.00 37.99  ? 233  ALA A CB  1 
ATOM   1248 N N   . PHE A 1 203 ? 19.740 26.728 48.765  1.00 31.13  ? 234  PHE A N   1 
ATOM   1249 C CA  . PHE A 1 203 ? 19.119 25.659 47.996  1.00 28.25  ? 234  PHE A CA  1 
ATOM   1250 C C   . PHE A 1 203 ? 17.867 26.153 47.278  1.00 36.80  ? 234  PHE A C   1 
ATOM   1251 O O   . PHE A 1 203 ? 17.682 25.892 46.084  1.00 28.96  ? 234  PHE A O   1 
ATOM   1252 C CB  . PHE A 1 203 ? 18.776 24.474 48.891  1.00 28.03  ? 234  PHE A CB  1 
ATOM   1253 C CG  . PHE A 1 203 ? 17.980 23.438 48.185  1.00 36.79  ? 234  PHE A CG  1 
ATOM   1254 C CD1 . PHE A 1 203 ? 18.607 22.449 47.449  1.00 36.17  ? 234  PHE A CD1 1 
ATOM   1255 C CD2 . PHE A 1 203 ? 16.600 23.486 48.207  1.00 36.03  ? 234  PHE A CD2 1 
ATOM   1256 C CE1 . PHE A 1 203 ? 17.867 21.510 46.769  1.00 38.34  ? 234  PHE A CE1 1 
ATOM   1257 C CE2 . PHE A 1 203 ? 15.857 22.554 47.530  1.00 46.59  ? 234  PHE A CE2 1 
ATOM   1258 C CZ  . PHE A 1 203 ? 16.488 21.566 46.809  1.00 37.41  ? 234  PHE A CZ  1 
ATOM   1259 N N   . PHE A 1 204 ? 16.983 26.858 47.994  1.00 29.14  ? 235  PHE A N   1 
ATOM   1260 C CA  . PHE A 1 204 ? 15.739 27.309 47.375  1.00 34.64  ? 235  PHE A CA  1 
ATOM   1261 C C   . PHE A 1 204 ? 16.011 28.248 46.210  1.00 32.07  ? 235  PHE A C   1 
ATOM   1262 O O   . PHE A 1 204 ? 15.326 28.191 45.182  1.00 30.06  ? 235  PHE A O   1 
ATOM   1263 C CB  . PHE A 1 204 ? 14.841 27.993 48.408  1.00 29.68  ? 235  PHE A CB  1 
ATOM   1264 C CG  . PHE A 1 204 ? 14.204 27.041 49.369  1.00 38.20  ? 235  PHE A CG  1 
ATOM   1265 C CD1 . PHE A 1 204 ? 13.355 26.049 48.915  1.00 43.89  ? 235  PHE A CD1 1 
ATOM   1266 C CD2 . PHE A 1 204 ? 14.454 27.134 50.724  1.00 33.80  ? 235  PHE A CD2 1 
ATOM   1267 C CE1 . PHE A 1 204 ? 12.772 25.162 49.797  1.00 33.67  ? 235  PHE A CE1 1 
ATOM   1268 C CE2 . PHE A 1 204 ? 13.872 26.254 51.610  1.00 35.22  ? 235  PHE A CE2 1 
ATOM   1269 C CZ  . PHE A 1 204 ? 13.030 25.267 51.144  1.00 36.25  ? 235  PHE A CZ  1 
ATOM   1270 N N   . MET A 1 205 ? 16.991 29.137 46.358  1.00 34.74  ? 236  MET A N   1 
ATOM   1271 C CA  . MET A 1 205 ? 17.329 30.037 45.263  1.00 36.51  ? 236  MET A CA  1 
ATOM   1272 C C   . MET A 1 205 ? 17.887 29.260 44.078  1.00 35.52  ? 236  MET A C   1 
ATOM   1273 O O   . MET A 1 205 ? 17.484 29.483 42.930  1.00 34.01  ? 236  MET A O   1 
ATOM   1274 C CB  . MET A 1 205 ? 18.328 31.091 45.741  1.00 38.99  ? 236  MET A CB  1 
ATOM   1275 C CG  . MET A 1 205 ? 17.691 32.215 46.544  1.00 57.56  ? 236  MET A CG  1 
ATOM   1276 S SD  . MET A 1 205 ? 18.865 33.494 47.038  1.00 79.02  ? 236  MET A SD  1 
ATOM   1277 C CE  . MET A 1 205 ? 19.696 32.697 48.409  1.00 74.76  ? 236  MET A CE  1 
ATOM   1278 N N   . VAL A 1 206 ? 18.808 28.331 44.338  1.00 29.35  ? 237  VAL A N   1 
ATOM   1279 C CA  . VAL A 1 206 ? 19.359 27.523 43.255  1.00 29.81  ? 237  VAL A CA  1 
ATOM   1280 C C   . VAL A 1 206 ? 18.252 26.744 42.564  1.00 33.52  ? 237  VAL A C   1 
ATOM   1281 O O   . VAL A 1 206 ? 18.201 26.665 41.331  1.00 29.85  ? 237  VAL A O   1 
ATOM   1282 C CB  . VAL A 1 206 ? 20.458 26.584 43.783  1.00 33.87  ? 237  VAL A CB  1 
ATOM   1283 C CG1 . VAL A 1 206 ? 20.778 25.511 42.756  1.00 39.08  ? 237  VAL A CG1 1 
ATOM   1284 C CG2 . VAL A 1 206 ? 21.706 27.369 44.107  1.00 38.82  ? 237  VAL A CG2 1 
ATOM   1285 N N   . PHE A 1 207 ? 17.347 26.160 43.347  1.00 34.98  ? 238  PHE A N   1 
ATOM   1286 C CA  . PHE A 1 207 ? 16.277 25.362 42.766  1.00 33.39  ? 238  PHE A CA  1 
ATOM   1287 C C   . PHE A 1 207 ? 15.351 26.228 41.928  1.00 30.72  ? 238  PHE A C   1 
ATOM   1288 O O   . PHE A 1 207 ? 14.934 25.826 40.836  1.00 30.70  ? 238  PHE A O   1 
ATOM   1289 C CB  . PHE A 1 207 ? 15.509 24.649 43.879  1.00 34.80  ? 238  PHE A CB  1 
ATOM   1290 C CG  . PHE A 1 207 ? 14.523 23.636 43.385  1.00 44.05  ? 238  PHE A CG  1 
ATOM   1291 C CD1 . PHE A 1 207 ? 14.946 22.541 42.656  1.00 49.97  ? 238  PHE A CD1 1 
ATOM   1292 C CD2 . PHE A 1 207 ? 13.177 23.765 43.667  1.00 46.86  ? 238  PHE A CD2 1 
ATOM   1293 C CE1 . PHE A 1 207 ? 14.044 21.600 42.204  1.00 49.64  ? 238  PHE A CE1 1 
ATOM   1294 C CE2 . PHE A 1 207 ? 12.268 22.825 43.219  1.00 60.87  ? 238  PHE A CE2 1 
ATOM   1295 C CZ  . PHE A 1 207 ? 12.703 21.741 42.487  1.00 43.65  ? 238  PHE A CZ  1 
ATOM   1296 N N   . GLY A 1 208 ? 15.028 27.425 42.420  1.00 36.10  ? 239  GLY A N   1 
ATOM   1297 C CA  . GLY A 1 208 ? 14.207 28.337 41.639  1.00 31.36  ? 239  GLY A CA  1 
ATOM   1298 C C   . GLY A 1 208 ? 14.834 28.693 40.304  1.00 31.16  ? 239  GLY A C   1 
ATOM   1299 O O   . GLY A 1 208 ? 14.138 28.813 39.294  1.00 31.58  ? 239  GLY A O   1 
ATOM   1300 N N   . ILE A 1 209 ? 16.156 28.875 40.277  1.00 32.08  ? 240  ILE A N   1 
ATOM   1301 C CA  . ILE A 1 209 ? 16.823 29.175 39.013  1.00 36.39  ? 240  ILE A CA  1 
ATOM   1302 C C   . ILE A 1 209 ? 16.752 27.976 38.074  1.00 34.94  ? 240  ILE A C   1 
ATOM   1303 O O   . ILE A 1 209 ? 16.506 28.129 36.871  1.00 31.42  ? 240  ILE A O   1 
ATOM   1304 C CB  . ILE A 1 209 ? 18.278 29.614 39.258  1.00 34.55  ? 240  ILE A CB  1 
ATOM   1305 C CG1 . ILE A 1 209 ? 18.307 30.942 40.016  1.00 36.62  ? 240  ILE A CG1 1 
ATOM   1306 C CG2 . ILE A 1 209 ? 19.038 29.741 37.929  1.00 38.17  ? 240  ILE A CG2 1 
ATOM   1307 C CD1 . ILE A 1 209 ? 19.666 31.276 40.593  1.00 41.02  ? 240  ILE A CD1 1 
ATOM   1308 N N   . MET A 1 210 ? 16.964 26.767 38.602  1.00 31.87  ? 241  MET A N   1 
ATOM   1309 C CA  . MET A 1 210 ? 16.855 25.578 37.764  1.00 36.19  ? 241  MET A CA  1 
ATOM   1310 C C   . MET A 1 210 ? 15.468 25.475 37.144  1.00 32.45  ? 241  MET A C   1 
ATOM   1311 O O   . MET A 1 210 ? 15.329 25.120 35.969  1.00 31.74  ? 241  MET A O   1 
ATOM   1312 C CB  . MET A 1 210 ? 17.169 24.323 38.578  1.00 32.38  ? 241  MET A CB  1 
ATOM   1313 C CG  . MET A 1 210 ? 18.592 24.259 39.102  1.00 42.56  ? 241  MET A CG  1 
ATOM   1314 S SD  . MET A 1 210 ? 18.904 22.789 40.114  1.00 50.69  ? 241  MET A SD  1 
ATOM   1315 C CE  . MET A 1 210 ? 19.347 21.614 38.845  1.00 64.30  ? 241  MET A CE  1 
ATOM   1316 N N   . LEU A 1 211 ? 14.428 25.799 37.917  1.00 32.43  ? 242  LEU A N   1 
ATOM   1317 C CA  . LEU A 1 211 ? 13.070 25.756 37.385  1.00 36.92  ? 242  LEU A CA  1 
ATOM   1318 C C   . LEU A 1 211 ? 12.882 26.759 36.256  1.00 32.42  ? 242  LEU A C   1 
ATOM   1319 O O   . LEU A 1 211 ? 12.183 26.478 35.275  1.00 32.86  ? 242  LEU A O   1 
ATOM   1320 C CB  . LEU A 1 211 ? 12.062 26.026 38.500  1.00 33.80  ? 242  LEU A CB  1 
ATOM   1321 C CG  . LEU A 1 211 ? 11.939 24.918 39.541  1.00 35.79  ? 242  LEU A CG  1 
ATOM   1322 C CD1 . LEU A 1 211 ? 11.229 25.459 40.774  1.00 41.00  ? 242  LEU A CD1 1 
ATOM   1323 C CD2 . LEU A 1 211 ? 11.193 23.726 38.950  1.00 40.25  ? 242  LEU A CD2 1 
ATOM   1324 N N   . HIS A 1 212 ? 13.475 27.946 36.386  1.00 33.32  ? 243  HIS A N   1 
ATOM   1325 C CA  . HIS A 1 212 ? 13.389 28.930 35.313  1.00 35.55  ? 243  HIS A CA  1 
ATOM   1326 C C   . HIS A 1 212 ? 14.070 28.411 34.053  1.00 32.78  ? 243  HIS A C   1 
ATOM   1327 O O   . HIS A 1 212 ? 13.498 28.445 32.957  1.00 33.23  ? 243  HIS A O   1 
ATOM   1328 C CB  . HIS A 1 212 ? 14.017 30.248 35.770  1.00 36.59  ? 243  HIS A CB  1 
ATOM   1329 C CG  . HIS A 1 212 ? 14.105 31.284 34.693  1.00 42.66  ? 243  HIS A CG  1 
ATOM   1330 N ND1 . HIS A 1 212 ? 13.059 31.567 33.841  1.00 61.73  ? 243  HIS A ND1 1 
ATOM   1331 C CD2 . HIS A 1 212 ? 15.115 32.112 34.335  1.00 59.81  ? 243  HIS A CD2 1 
ATOM   1332 C CE1 . HIS A 1 212 ? 13.422 32.521 33.003  1.00 54.75  ? 243  HIS A CE1 1 
ATOM   1333 N NE2 . HIS A 1 212 ? 14.665 32.870 33.282  1.00 59.55  ? 243  HIS A NE2 1 
ATOM   1334 N N   . LEU A 1 213 ? 15.299 27.915 34.199  1.00 32.38  ? 244  LEU A N   1 
ATOM   1335 C CA  . LEU A 1 213 ? 16.004 27.337 33.064  1.00 32.47  ? 244  LEU A CA  1 
ATOM   1336 C C   . LEU A 1 213 ? 15.244 26.148 32.495  1.00 32.77  ? 244  LEU A C   1 
ATOM   1337 O O   . LEU A 1 213 ? 15.187 25.959 31.274  1.00 33.14  ? 244  LEU A O   1 
ATOM   1338 C CB  . LEU A 1 213 ? 17.408 26.917 33.493  1.00 31.99  ? 244  LEU A CB  1 
ATOM   1339 C CG  . LEU A 1 213 ? 18.337 28.048 33.930  1.00 36.36  ? 244  LEU A CG  1 
ATOM   1340 C CD1 . LEU A 1 213 ? 19.586 27.484 34.575  1.00 38.09  ? 244  LEU A CD1 1 
ATOM   1341 C CD2 . LEU A 1 213 ? 18.710 28.915 32.748  1.00 39.16  ? 244  LEU A CD2 1 
ATOM   1342 N N   . TYR A 1 214 ? 14.650 25.335 33.367  1.00 32.65  ? 245  TYR A N   1 
ATOM   1343 C CA  . TYR A 1 214 ? 13.928 24.157 32.904  1.00 36.40  ? 245  TYR A CA  1 
ATOM   1344 C C   . TYR A 1 214 ? 12.786 24.548 31.974  1.00 33.57  ? 245  TYR A C   1 
ATOM   1345 O O   . TYR A 1 214 ? 12.606 23.953 30.905  1.00 33.96  ? 245  TYR A O   1 
ATOM   1346 C CB  . TYR A 1 214 ? 13.413 23.371 34.107  1.00 36.14  ? 245  TYR A CB  1 
ATOM   1347 C CG  . TYR A 1 214 ? 12.378 22.336 33.761  1.00 40.70  ? 245  TYR A CG  1 
ATOM   1348 C CD1 . TYR A 1 214 ? 11.031 22.666 33.712  1.00 33.60  ? 245  TYR A CD1 1 
ATOM   1349 C CD2 . TYR A 1 214 ? 12.746 21.027 33.488  1.00 50.43  ? 245  TYR A CD2 1 
ATOM   1350 C CE1 . TYR A 1 214 ? 10.082 21.723 33.391  1.00 42.68  ? 245  TYR A CE1 1 
ATOM   1351 C CE2 . TYR A 1 214 ? 11.806 20.077 33.173  1.00 61.17  ? 245  TYR A CE2 1 
ATOM   1352 C CZ  . TYR A 1 214 ? 10.476 20.429 33.130  1.00 54.59  ? 245  TYR A CZ  1 
ATOM   1353 O OH  . TYR A 1 214 ? 9.535  19.482 32.812  1.00 60.57  ? 245  TYR A OH  1 
ATOM   1354 N N   . VAL A 1 215 ? 12.007 25.559 32.361  1.00 33.68  ? 246  VAL A N   1 
ATOM   1355 C CA  . VAL A 1 215 ? 10.867 25.964 31.547  1.00 34.27  ? 246  VAL A CA  1 
ATOM   1356 C C   . VAL A 1 215 ? 11.339 26.519 30.209  1.00 36.53  ? 246  VAL A C   1 
ATOM   1357 O O   . VAL A 1 215 ? 10.717 26.284 29.167  1.00 39.61  ? 246  VAL A O   1 
ATOM   1358 C CB  . VAL A 1 215 ? 10.004 26.988 32.307  1.00 34.35  ? 246  VAL A CB  1 
ATOM   1359 C CG1 . VAL A 1 215 ? 8.900  27.509 31.406  1.00 48.31  ? 246  VAL A CG1 1 
ATOM   1360 C CG2 . VAL A 1 215 ? 9.414  26.362 33.566  1.00 39.04  ? 246  VAL A CG2 1 
ATOM   1361 N N   . ARG A 1 216 ? 12.433 27.276 30.217  1.00 34.24  ? 247  ARG A N   1 
ATOM   1362 C CA  . ARG A 1 216 ? 12.971 27.800 28.967  1.00 38.44  ? 247  ARG A CA  1 
ATOM   1363 C C   . ARG A 1 216 ? 13.443 26.668 28.061  1.00 34.62  ? 247  ARG A C   1 
ATOM   1364 O O   . ARG A 1 216 ? 13.161 26.663 26.856  1.00 39.28  ? 247  ARG A O   1 
ATOM   1365 C CB  . ARG A 1 216 ? 14.110 28.771 29.270  1.00 38.50  ? 247  ARG A CB  1 
ATOM   1366 C CG  . ARG A 1 216 ? 13.705 29.912 30.199  1.00 46.26  ? 247  ARG A CG  1 
ATOM   1367 C CD  . ARG A 1 216 ? 13.938 31.254 29.549  1.00 60.15  ? 247  ARG A CD  1 
ATOM   1368 N NE  . ARG A 1 216 ? 13.113 31.416 28.359  1.00 67.49  ? 247  ARG A NE  1 
ATOM   1369 C CZ  . ARG A 1 216 ? 13.423 32.190 27.328  1.00 89.81  ? 247  ARG A CZ  1 
ATOM   1370 N NH1 . ARG A 1 216 ? 14.548 32.888 27.300  1.00 71.12  ? 247  ARG A NH1 1 
ATOM   1371 N NH2 . ARG A 1 216 ? 12.588 32.257 26.295  1.00 85.78  ? 247  ARG A NH2 1 
ATOM   1372 N N   . ILE A 1 217 ? 14.156 25.698 28.624  1.00 35.35  ? 248  ILE A N   1 
ATOM   1373 C CA  . ILE A 1 217 ? 14.618 24.538 27.869  1.00 34.40  ? 248  ILE A CA  1 
ATOM   1374 C C   . ILE A 1 217 ? 13.422 23.802 27.289  1.00 39.65  ? 248  ILE A C   1 
ATOM   1375 O O   . ILE A 1 217 ? 13.390 23.487 26.100  1.00 35.40  ? 248  ILE A O   1 
ATOM   1376 C CB  . ILE A 1 217 ? 15.460 23.599 28.748  1.00 33.92  ? 248  ILE A CB  1 
ATOM   1377 C CG1 . ILE A 1 217 ? 16.819 24.228 29.047  1.00 33.47  ? 248  ILE A CG1 1 
ATOM   1378 C CG2 . ILE A 1 217 ? 15.642 22.249 28.070  1.00 36.44  ? 248  ILE A CG2 1 
ATOM   1379 C CD1 . ILE A 1 217 ? 17.529 23.595 30.210  1.00 36.07  ? 248  ILE A CD1 1 
HETATM 1380 N N   . YCM A 1 218 ? 12.444 23.520 28.142  1.00 39.47  ? 249  YCM A N   1 
HETATM 1381 C CA  . YCM A 1 218 ? 11.241 22.855 27.717  1.00 35.48  ? 249  YCM A CA  1 
HETATM 1382 C CB  . YCM A 1 218 ? 10.282 22.688 28.897  1.00 57.72  ? 249  YCM A CB  1 
HETATM 1383 S SG  . YCM A 1 218 ? 8.602  22.293 28.494  1.00 94.03  ? 249  YCM A SG  1 
HETATM 1384 C CD  . YCM A 1 218 ? 8.504  20.526 28.476  1.00 78.87  ? 249  YCM A CD  1 
HETATM 1385 C CE  . YCM A 1 218 ? 8.777  19.868 29.811  1.00 88.63  ? 249  YCM A CE  1 
HETATM 1386 O OZ1 . YCM A 1 218 ? 9.819  20.121 30.447  1.00 80.72  ? 249  YCM A OZ1 1 
HETATM 1387 N NZ2 . YCM A 1 218 ? 7.868  18.977 30.316  1.00 76.87  ? 249  YCM A NZ2 1 
HETATM 1388 C C   . YCM A 1 218 ? 10.558 23.575 26.558  1.00 42.47  ? 249  YCM A C   1 
HETATM 1389 O O   . YCM A 1 218 ? 10.080 22.984 25.588  1.00 45.35  ? 249  YCM A O   1 
ATOM   1390 N N   . GLN A 1 219 ? 10.534 24.902 26.662  1.00 40.07  ? 250  GLN A N   1 
ATOM   1391 C CA  . GLN A 1 219 ? 9.982  25.765 25.616  1.00 41.00  ? 250  GLN A CA  1 
ATOM   1392 C C   . GLN A 1 219 ? 10.661 25.566 24.252  1.00 47.97  ? 250  GLN A C   1 
ATOM   1393 O O   . GLN A 1 219 ? 9.983  25.409 23.237  1.00 50.87  ? 250  GLN A O   1 
ATOM   1394 C CB  . GLN A 1 219 ? 10.093 27.236 26.043  1.00 44.81  ? 250  GLN A CB  1 
ATOM   1395 C CG  . GLN A 1 219 ? 9.464  28.234 25.072  1.00 63.79  ? 250  GLN A CG  1 
ATOM   1396 C CD  . GLN A 1 219 ? 9.158  29.571 25.725  1.00 86.46  ? 250  GLN A CD  1 
ATOM   1397 O OE1 . GLN A 1 219 ? 10.042 30.218 26.289  1.00 93.81  ? 250  GLN A OE1 1 
ATOM   1398 N NE2 . GLN A 1 219 ? 7.897  29.987 25.659  1.00 79.09  ? 250  GLN A NE2 1 
ATOM   1399 N N   . VAL A 1 220 ? 11.996 25.577 24.227  1.00 49.81  ? 251  VAL A N   1 
ATOM   1400 C CA  . VAL A 1 220 ? 12.711 25.436 22.960  1.00 38.58  ? 251  VAL A CA  1 
ATOM   1401 C C   . VAL A 1 220 ? 12.481 24.056 22.359  1.00 54.41  ? 251  VAL A C   1 
ATOM   1402 O O   . VAL A 1 220 ? 12.279 23.918 21.147  1.00 54.20  ? 251  VAL A O   1 
ATOM   1403 C CB  . VAL A 1 220 ? 14.214 25.710 23.151  1.00 55.31  ? 251  VAL A CB  1 
ATOM   1404 C CG1 . VAL A 1 220 ? 14.991 25.347 21.885  1.00 58.91  ? 251  VAL A CG1 1 
ATOM   1405 C CG2 . VAL A 1 220 ? 14.443 27.151 23.491  1.00 65.00  ? 251  VAL A CG2 1 
ATOM   1406 N N   . VAL A 1 221 ? 12.536 23.010 23.186  1.00 41.35  ? 252  VAL A N   1 
ATOM   1407 C CA  . VAL A 1 221 ? 12.359 21.656 22.670  1.00 42.07  ? 252  VAL A CA  1 
ATOM   1408 C C   . VAL A 1 221 ? 10.959 21.488 22.095  1.00 61.70  ? 252  VAL A C   1 
ATOM   1409 O O   . VAL A 1 221 ? 10.776 20.871 21.039  1.00 55.73  ? 252  VAL A O   1 
ATOM   1410 C CB  . VAL A 1 221 ? 12.649 20.621 23.771  1.00 46.28  ? 252  VAL A CB  1 
ATOM   1411 C CG1 . VAL A 1 221 ? 12.241 19.230 23.317  1.00 58.33  ? 252  VAL A CG1 1 
ATOM   1412 C CG2 . VAL A 1 221 ? 14.124 20.649 24.147  1.00 48.14  ? 252  VAL A CG2 1 
ATOM   1413 N N   . TRP A 1 222 ? 9.951  22.050 22.770  1.00 46.41  ? 253  TRP A N   1 
ATOM   1414 C CA  . TRP A 1 222 ? 8.583  21.957 22.269  1.00 58.43  ? 253  TRP A CA  1 
ATOM   1415 C C   . TRP A 1 222 ? 8.424  22.702 20.950  1.00 57.58  ? 253  TRP A C   1 
ATOM   1416 O O   . TRP A 1 222 ? 7.794  22.193 20.017  1.00 63.59  ? 253  TRP A O   1 
ATOM   1417 C CB  . TRP A 1 222 ? 7.604  22.506 23.305  1.00 64.55  ? 253  TRP A CB  1 
ATOM   1418 C CG  . TRP A 1 222 ? 6.882  21.441 24.066  1.00 84.21  ? 253  TRP A CG  1 
ATOM   1419 C CD1 . TRP A 1 222 ? 7.270  20.858 25.238  1.00 82.42  ? 253  TRP A CD1 1 
ATOM   1420 C CD2 . TRP A 1 222 ? 5.638  20.831 23.707  1.00 74.53  ? 253  TRP A CD2 1 
ATOM   1421 N NE1 . TRP A 1 222 ? 6.343  19.921 25.630  1.00 85.00  ? 253  TRP A NE1 1 
ATOM   1422 C CE2 . TRP A 1 222 ? 5.332  19.885 24.706  1.00 87.75  ? 253  TRP A CE2 1 
ATOM   1423 C CE3 . TRP A 1 222 ? 4.754  20.992 22.637  1.00 72.54  ? 253  TRP A CE3 1 
ATOM   1424 C CZ2 . TRP A 1 222 ? 4.179  19.105 24.665  1.00 80.92  ? 253  TRP A CZ2 1 
ATOM   1425 C CZ3 . TRP A 1 222 ? 3.611  20.217 22.599  1.00 86.77  ? 253  TRP A CZ3 1 
ATOM   1426 C CH2 . TRP A 1 222 ? 3.334  19.285 23.605  1.00 80.02  ? 253  TRP A CH2 1 
ATOM   1427 N N   . ARG A 1 223 ? 8.978  23.913 20.859  1.00 61.85  ? 254  ARG A N   1 
ATOM   1428 C CA  . ARG A 1 223 ? 8.855  24.703 19.639  1.00 56.14  ? 254  ARG A CA  1 
ATOM   1429 C C   . ARG A 1 223 ? 9.390  23.937 18.435  1.00 70.05  ? 254  ARG A C   1 
ATOM   1430 O O   . ARG A 1 223 ? 8.695  23.775 17.425  1.00 61.99  ? 254  ARG A O   1 
ATOM   1431 C CB  . ARG A 1 223 ? 9.604  26.027 19.802  1.00 68.80  ? 254  ARG A CB  1 
ATOM   1432 C CG  . ARG A 1 223 ? 9.342  27.051 18.698  1.00 91.41  ? 254  ARG A CG  1 
ATOM   1433 C CD  . ARG A 1 223 ? 10.528 27.996 18.491  1.00 94.65  ? 254  ARG A CD  1 
ATOM   1434 N NE  . ARG A 1 223 ? 11.349 28.155 19.687  1.00 97.90  ? 254  ARG A NE  1 
ATOM   1435 C CZ  . ARG A 1 223 ? 11.003 28.869 20.751  1.00 98.33  ? 254  ARG A CZ  1 
ATOM   1436 N NH1 . ARG A 1 223 ? 9.836  29.489 20.821  1.00 103.60 ? 254  ARG A NH1 1 
ATOM   1437 N NH2 . ARG A 1 223 ? 11.848 28.958 21.774  1.00 87.45  ? 254  ARG A NH2 1 
ATOM   1438 N N   . HIS A 1 224 ? 10.631 23.453 18.531  1.00 54.30  ? 255  HIS A N   1 
ATOM   1439 C CA  . HIS A 1 224 ? 11.251 22.764 17.405  1.00 60.27  ? 255  HIS A CA  1 
ATOM   1440 C C   . HIS A 1 224 ? 10.457 21.527 17.007  1.00 62.32  ? 255  HIS A C   1 
ATOM   1441 O O   . HIS A 1 224 ? 10.252 21.269 15.816  1.00 61.07  ? 255  HIS A O   1 
ATOM   1442 C CB  . HIS A 1 224 ? 12.690 22.391 17.756  1.00 60.12  ? 255  HIS A CB  1 
ATOM   1443 C CG  . HIS A 1 224 ? 13.578 23.574 17.982  1.00 75.56  ? 255  HIS A CG  1 
ATOM   1444 N ND1 . HIS A 1 224 ? 13.185 24.863 17.690  1.00 79.99  ? 255  HIS A ND1 1 
ATOM   1445 C CD2 . HIS A 1 224 ? 14.837 23.666 18.471  1.00 64.20  ? 255  HIS A CD2 1 
ATOM   1446 C CE1 . HIS A 1 224 ? 14.165 25.698 17.988  1.00 74.26  ? 255  HIS A CE1 1 
ATOM   1447 N NE2 . HIS A 1 224 ? 15.179 24.997 18.463  1.00 62.28  ? 255  HIS A NE2 1 
ATOM   1448 N N   . ALA A 1 225 ? 10.001 20.746 17.989  1.00 48.44  ? 256  ALA A N   1 
ATOM   1449 C CA  . ALA A 1 225 ? 9.192  19.574 17.671  1.00 64.66  ? 256  ALA A CA  1 
ATOM   1450 C C   . ALA A 1 225 ? 7.896  19.977 16.977  1.00 70.89  ? 256  ALA A C   1 
ATOM   1451 O O   . ALA A 1 225 ? 7.443  19.298 16.046  1.00 61.05  ? 256  ALA A O   1 
ATOM   1452 C CB  . ALA A 1 225 ? 8.898  18.778 18.942  1.00 54.11  ? 256  ALA A CB  1 
ATOM   1453 N N   . ALA A 1 226 ? 7.293  21.089 17.406  1.00 57.89  ? 1001 ALA A N   1 
ATOM   1454 C CA  . ALA A 1 226 ? 6.049  21.544 16.794  1.00 60.00  ? 1001 ALA A CA  1 
ATOM   1455 C C   . ALA A 1 226 ? 6.277  22.035 15.371  1.00 60.71  ? 1001 ALA A C   1 
ATOM   1456 O O   . ALA A 1 226 ? 5.428  21.831 14.496  1.00 68.40  ? 1001 ALA A O   1 
ATOM   1457 C CB  . ALA A 1 226 ? 5.422  22.650 17.640  1.00 58.27  ? 1001 ALA A CB  1 
ATOM   1458 N N   . ASP A 1 227 ? 7.410  22.694 15.122  1.00 61.59  ? 1002 ASP A N   1 
ATOM   1459 C CA  . ASP A 1 227 ? 7.695  23.180 13.776  1.00 64.27  ? 1002 ASP A CA  1 
ATOM   1460 C C   . ASP A 1 227 ? 8.039  22.029 12.841  1.00 64.33  ? 1002 ASP A C   1 
ATOM   1461 O O   . ASP A 1 227 ? 7.642  22.032 11.670  1.00 55.06  ? 1002 ASP A O   1 
ATOM   1462 C CB  . ASP A 1 227 ? 8.832  24.199 13.819  1.00 53.20  ? 1002 ASP A CB  1 
ATOM   1463 C CG  . ASP A 1 227 ? 8.433  25.486 14.511  1.00 64.33  ? 1002 ASP A CG  1 
ATOM   1464 O OD1 . ASP A 1 227 ? 7.242  25.629 14.862  1.00 65.29  ? 1002 ASP A OD1 1 
ATOM   1465 O OD2 . ASP A 1 227 ? 9.311  26.354 14.704  1.00 67.96  ? 1002 ASP A OD2 1 
ATOM   1466 N N   . LEU A 1 228 ? 8.777  21.037 13.340  1.00 52.40  ? 1003 LEU A N   1 
ATOM   1467 C CA  . LEU A 1 228 ? 9.077  19.859 12.535  1.00 57.30  ? 1003 LEU A CA  1 
ATOM   1468 C C   . LEU A 1 228 ? 7.798  19.145 12.118  1.00 57.98  ? 1003 LEU A C   1 
ATOM   1469 O O   . LEU A 1 228 ? 7.606  18.825 10.939  1.00 60.37  ? 1003 LEU A O   1 
ATOM   1470 C CB  . LEU A 1 228 ? 9.993  18.919 13.321  1.00 51.86  ? 1003 LEU A CB  1 
ATOM   1471 C CG  . LEU A 1 228 ? 10.315 17.576 12.669  1.00 61.77  ? 1003 LEU A CG  1 
ATOM   1472 C CD1 . LEU A 1 228 ? 10.942 17.780 11.297  1.00 55.20  ? 1003 LEU A CD1 1 
ATOM   1473 C CD2 . LEU A 1 228 ? 11.229 16.765 13.576  1.00 63.87  ? 1003 LEU A CD2 1 
ATOM   1474 N N   . GLU A 1 229 ? 6.903  18.894 13.077  1.00 56.62  ? 1004 GLU A N   1 
ATOM   1475 C CA  . GLU A 1 229 ? 5.658  18.199 12.771  1.00 63.19  ? 1004 GLU A CA  1 
ATOM   1476 C C   . GLU A 1 229 ? 4.771  19.022 11.845  1.00 67.24  ? 1004 GLU A C   1 
ATOM   1477 O O   . GLU A 1 229 ? 4.067  18.455 11.002  1.00 65.45  ? 1004 GLU A O   1 
ATOM   1478 C CB  . GLU A 1 229 ? 4.922  17.863 14.071  1.00 61.50  ? 1004 GLU A CB  1 
ATOM   1479 C CG  . GLU A 1 229 ? 3.864  16.770 13.948  1.00 80.73  ? 1004 GLU A CG  1 
ATOM   1480 C CD  . GLU A 1 229 ? 3.349  16.303 15.301  1.00 96.80  ? 1004 GLU A CD  1 
ATOM   1481 O OE1 . GLU A 1 229 ? 3.671  16.956 16.317  1.00 70.15  ? 1004 GLU A OE1 1 
ATOM   1482 O OE2 . GLU A 1 229 ? 2.628  15.282 15.350  1.00 75.66  ? 1004 GLU A OE2 1 
ATOM   1483 N N   . ASP A 1 230 ? 4.794  20.351 11.975  1.00 63.05  ? 1005 ASP A N   1 
ATOM   1484 C CA  . ASP A 1 230 ? 4.030  21.198 11.065  1.00 58.02  ? 1005 ASP A CA  1 
ATOM   1485 C C   . ASP A 1 230 ? 4.548  21.068 9.639   1.00 60.20  ? 1005 ASP A C   1 
ATOM   1486 O O   . ASP A 1 230 ? 3.813  20.670 8.729   1.00 68.88  ? 1005 ASP A O   1 
ATOM   1487 C CB  . ASP A 1 230 ? 4.089  22.659 11.516  1.00 51.62  ? 1005 ASP A CB  1 
ATOM   1488 C CG  . ASP A 1 230 ? 3.272  22.920 12.767  1.00 87.64  ? 1005 ASP A CG  1 
ATOM   1489 O OD1 . ASP A 1 230 ? 2.303  22.172 13.016  1.00 99.41  ? 1005 ASP A OD1 1 
ATOM   1490 O OD2 . ASP A 1 230 ? 3.597  23.881 13.499  1.00 97.86  ? 1005 ASP A OD2 1 
ATOM   1491 N N   . ASN A 1 231 ? 5.823  21.405 9.426   1.00 59.48  ? 1006 ASN A N   1 
ATOM   1492 C CA  . ASN A 1 231 ? 6.372  21.398 8.074   1.00 62.25  ? 1006 ASN A CA  1 
ATOM   1493 C C   . ASN A 1 231 ? 6.317  20.011 7.451   1.00 57.98  ? 1006 ASN A C   1 
ATOM   1494 O O   . ASN A 1 231 ? 6.164  19.887 6.230   1.00 51.20  ? 1006 ASN A O   1 
ATOM   1495 C CB  . ASN A 1 231 ? 7.810  21.914 8.091   1.00 62.80  ? 1006 ASN A CB  1 
ATOM   1496 C CG  . ASN A 1 231 ? 7.898  23.375 8.473   1.00 67.15  ? 1006 ASN A CG  1 
ATOM   1497 O OD1 . ASN A 1 231 ? 8.629  23.744 9.390   1.00 83.62  ? 1006 ASN A OD1 1 
ATOM   1498 N ND2 . ASN A 1 231 ? 7.152  24.218 7.767   1.00 68.94  ? 1006 ASN A ND2 1 
ATOM   1499 N N   . TRP A 1 232 ? 6.457  18.962 8.262   1.00 48.40  ? 1007 TRP A N   1 
ATOM   1500 C CA  . TRP A 1 232 ? 6.340  17.607 7.735   1.00 58.63  ? 1007 TRP A CA  1 
ATOM   1501 C C   . TRP A 1 232 ? 4.923  17.332 7.249   1.00 63.55  ? 1007 TRP A C   1 
ATOM   1502 O O   . TRP A 1 232 ? 4.730  16.694 6.207   1.00 60.20  ? 1007 TRP A O   1 
ATOM   1503 C CB  . TRP A 1 232 ? 6.754  16.600 8.807   1.00 53.72  ? 1007 TRP A CB  1 
ATOM   1504 C CG  . TRP A 1 232 ? 6.718  15.169 8.361   1.00 64.09  ? 1007 TRP A CG  1 
ATOM   1505 C CD1 . TRP A 1 232 ? 5.679  14.292 8.498   1.00 64.61  ? 1007 TRP A CD1 1 
ATOM   1506 C CD2 . TRP A 1 232 ? 7.773  14.443 7.719   1.00 55.14  ? 1007 TRP A CD2 1 
ATOM   1507 N NE1 . TRP A 1 232 ? 6.021  13.067 7.978   1.00 56.14  ? 1007 TRP A NE1 1 
ATOM   1508 C CE2 . TRP A 1 232 ? 7.301  13.133 7.493   1.00 52.82  ? 1007 TRP A CE2 1 
ATOM   1509 C CE3 . TRP A 1 232 ? 9.070  14.772 7.312   1.00 68.05  ? 1007 TRP A CE3 1 
ATOM   1510 C CZ2 . TRP A 1 232 ? 8.080  12.154 6.878   1.00 59.06  ? 1007 TRP A CZ2 1 
ATOM   1511 C CZ3 . TRP A 1 232 ? 9.842  13.799 6.701   1.00 55.31  ? 1007 TRP A CZ3 1 
ATOM   1512 C CH2 . TRP A 1 232 ? 9.345  12.506 6.491   1.00 61.79  ? 1007 TRP A CH2 1 
ATOM   1513 N N   . GLU A 1 233 ? 3.918  17.822 7.981   1.00 58.83  ? 1008 GLU A N   1 
ATOM   1514 C CA  . GLU A 1 233 ? 2.532  17.619 7.571   1.00 66.18  ? 1008 GLU A CA  1 
ATOM   1515 C C   . GLU A 1 233 ? 2.207  18.415 6.314   1.00 64.52  ? 1008 GLU A C   1 
ATOM   1516 O O   . GLU A 1 233 ? 1.543  17.904 5.405   1.00 60.08  ? 1008 GLU A O   1 
ATOM   1517 C CB  . GLU A 1 233 ? 1.586  18.012 8.705   1.00 74.21  ? 1008 GLU A CB  1 
ATOM   1518 C CG  . GLU A 1 233 ? 0.214  17.361 8.618   1.00 95.54  ? 1008 GLU A CG  1 
ATOM   1519 C CD  . GLU A 1 233 ? 0.244  15.887 8.983   1.00 113.72 ? 1008 GLU A CD  1 
ATOM   1520 O OE1 . GLU A 1 233 ? 1.223  15.452 9.629   1.00 100.15 ? 1008 GLU A OE1 1 
ATOM   1521 O OE2 . GLU A 1 233 ? -0.711 15.166 8.623   1.00 113.12 ? 1008 GLU A OE2 1 
ATOM   1522 N N   . THR A 1 234 ? 2.651  19.673 6.248   1.00 62.96  ? 1009 THR A N   1 
ATOM   1523 C CA  . THR A 1 234 ? 2.423  20.467 5.045   1.00 78.45  ? 1009 THR A CA  1 
ATOM   1524 C C   . THR A 1 234 ? 3.160  19.866 3.856   1.00 62.61  ? 1009 THR A C   1 
ATOM   1525 O O   . THR A 1 234 ? 2.659  19.889 2.726   1.00 64.60  ? 1009 THR A O   1 
ATOM   1526 C CB  . THR A 1 234 ? 2.867  21.912 5.271   1.00 67.10  ? 1009 THR A CB  1 
ATOM   1527 O OG1 . THR A 1 234 ? 4.286  21.953 5.463   1.00 87.78  ? 1009 THR A OG1 1 
ATOM   1528 C CG2 . THR A 1 234 ? 2.171  22.508 6.489   1.00 67.56  ? 1009 THR A CG2 1 
ATOM   1529 N N   . LEU A 1 235 ? 4.353  19.321 4.098   1.00 58.57  ? 1010 LEU A N   1 
ATOM   1530 C CA  . LEU A 1 235 ? 5.077  18.599 3.059   1.00 55.61  ? 1010 LEU A CA  1 
ATOM   1531 C C   . LEU A 1 235 ? 4.220  17.487 2.466   1.00 55.26  ? 1010 LEU A C   1 
ATOM   1532 O O   . LEU A 1 235 ? 4.141  17.331 1.243   1.00 53.14  ? 1010 LEU A O   1 
ATOM   1533 C CB  . LEU A 1 235 ? 6.370  18.034 3.644   1.00 65.91  ? 1010 LEU A CB  1 
ATOM   1534 C CG  . LEU A 1 235 ? 7.307  17.289 2.697   1.00 58.67  ? 1010 LEU A CG  1 
ATOM   1535 C CD1 . LEU A 1 235 ? 7.901  18.254 1.687   1.00 68.18  ? 1010 LEU A CD1 1 
ATOM   1536 C CD2 . LEU A 1 235 ? 8.397  16.590 3.496   1.00 72.20  ? 1010 LEU A CD2 1 
ATOM   1537 N N   . ASN A 1 236 ? 3.568  16.698 3.325   1.00 50.98  ? 1011 ASN A N   1 
ATOM   1538 C CA  . ASN A 1 236 ? 2.724  15.614 2.830   1.00 57.77  ? 1011 ASN A CA  1 
ATOM   1539 C C   . ASN A 1 236 ? 1.472  16.154 2.151   1.00 61.17  ? 1011 ASN A C   1 
ATOM   1540 O O   . ASN A 1 236 ? 1.056  15.637 1.109   1.00 62.17  ? 1011 ASN A O   1 
ATOM   1541 C CB  . ASN A 1 236 ? 2.341  14.673 3.971   1.00 61.93  ? 1011 ASN A CB  1 
ATOM   1542 C CG  . ASN A 1 236 ? 3.546  14.030 4.629   1.00 85.63  ? 1011 ASN A CG  1 
ATOM   1543 O OD1 . ASN A 1 236 ? 4.574  13.807 3.988   1.00 87.87  ? 1011 ASN A OD1 1 
ATOM   1544 N ND2 . ASN A 1 236 ? 3.425  13.724 5.917   1.00 86.53  ? 1011 ASN A ND2 1 
ATOM   1545 N N   . ASP A 1 237 ? 0.857  17.193 2.722   1.00 53.38  ? 1012 ASP A N   1 
ATOM   1546 C CA  . ASP A 1 237 ? -0.343 17.765 2.120   1.00 60.44  ? 1012 ASP A CA  1 
ATOM   1547 C C   . ASP A 1 237 ? -0.097 18.163 0.670   1.00 61.85  ? 1012 ASP A C   1 
ATOM   1548 O O   . ASP A 1 237 ? -0.848 17.772 -0.231  1.00 57.99  ? 1012 ASP A O   1 
ATOM   1549 C CB  . ASP A 1 237 ? -0.816 18.975 2.927   1.00 52.07  ? 1012 ASP A CB  1 
ATOM   1550 C CG  . ASP A 1 237 ? -1.328 18.595 4.303   1.00 71.35  ? 1012 ASP A CG  1 
ATOM   1551 O OD1 . ASP A 1 237 ? -1.714 17.422 4.491   1.00 83.66  ? 1012 ASP A OD1 1 
ATOM   1552 O OD2 . ASP A 1 237 ? -1.350 19.470 5.194   1.00 66.38  ? 1012 ASP A OD2 1 
ATOM   1553 N N   . ASN A 1 238 ? 0.952  18.952 0.428   1.00 52.87  ? 1013 ASN A N   1 
ATOM   1554 C CA  . ASN A 1 238 ? 1.218  19.424 -0.926  1.00 60.50  ? 1013 ASN A CA  1 
ATOM   1555 C C   . ASN A 1 238 ? 1.600  18.280 -1.851  1.00 58.80  ? 1013 ASN A C   1 
ATOM   1556 O O   . ASN A 1 238 ? 1.268  18.311 -3.040  1.00 60.41  ? 1013 ASN A O   1 
ATOM   1557 C CB  . ASN A 1 238 ? 2.318  20.482 -0.905  1.00 55.06  ? 1013 ASN A CB  1 
ATOM   1558 C CG  . ASN A 1 238 ? 1.825  21.817 -0.390  1.00 54.53  ? 1013 ASN A CG  1 
ATOM   1559 O OD1 . ASN A 1 238 ? 1.353  22.655 -1.158  1.00 61.61  ? 1013 ASN A OD1 1 
ATOM   1560 N ND2 . ASN A 1 238 ? 1.927  22.020 0.917   1.00 59.41  ? 1013 ASN A ND2 1 
ATOM   1561 N N   . LEU A 1 239 ? 2.286  17.263 -1.329  1.00 57.73  ? 1014 LEU A N   1 
ATOM   1562 C CA  . LEU A 1 239 ? 2.612  16.103 -2.149  1.00 63.79  ? 1014 LEU A CA  1 
ATOM   1563 C C   . LEU A 1 239 ? 1.349  15.440 -2.688  1.00 72.37  ? 1014 LEU A C   1 
ATOM   1564 O O   . LEU A 1 239 ? 1.328  14.969 -3.831  1.00 60.75  ? 1014 LEU A O   1 
ATOM   1565 C CB  . LEU A 1 239 ? 3.446  15.118 -1.333  1.00 58.49  ? 1014 LEU A CB  1 
ATOM   1566 C CG  . LEU A 1 239 ? 4.021  13.909 -2.065  1.00 80.59  ? 1014 LEU A CG  1 
ATOM   1567 C CD1 . LEU A 1 239 ? 4.873  14.348 -3.241  1.00 78.64  ? 1014 LEU A CD1 1 
ATOM   1568 C CD2 . LEU A 1 239 ? 4.835  13.069 -1.098  1.00 70.46  ? 1014 LEU A CD2 1 
ATOM   1569 N N   . LYS A 1 240 ? 0.278  15.405 -1.888  1.00 66.79  ? 1015 LYS A N   1 
ATOM   1570 C CA  . LYS A 1 240 ? -0.988 14.878 -2.387  1.00 68.34  ? 1015 LYS A CA  1 
ATOM   1571 C C   . LYS A 1 240 ? -1.627 15.822 -3.393  1.00 62.60  ? 1015 LYS A C   1 
ATOM   1572 O O   . LYS A 1 240 ? -2.286 15.372 -4.335  1.00 73.60  ? 1015 LYS A O   1 
ATOM   1573 C CB  . LYS A 1 240 ? -1.962 14.627 -1.240  1.00 76.37  ? 1015 LYS A CB  1 
ATOM   1574 C CG  . LYS A 1 240 ? -1.591 13.468 -0.346  1.00 77.68  ? 1015 LYS A CG  1 
ATOM   1575 C CD  . LYS A 1 240 ? -2.693 13.185 0.667   1.00 104.87 ? 1015 LYS A CD  1 
ATOM   1576 C CE  . LYS A 1 240 ? -2.922 14.372 1.595   1.00 106.43 ? 1015 LYS A CE  1 
ATOM   1577 N NZ  . LYS A 1 240 ? -3.934 14.081 2.647   1.00 111.00 ? 1015 LYS A NZ  1 
ATOM   1578 N N   . VAL A 1 241 ? -1.478 17.134 -3.192  1.00 56.80  ? 1016 VAL A N   1 
ATOM   1579 C CA  . VAL A 1 241 ? -1.977 18.085 -4.180  1.00 66.06  ? 1016 VAL A CA  1 
ATOM   1580 C C   . VAL A 1 241 ? -1.364 17.791 -5.543  1.00 60.29  ? 1016 VAL A C   1 
ATOM   1581 O O   . VAL A 1 241 ? -2.058 17.799 -6.567  1.00 64.17  ? 1016 VAL A O   1 
ATOM   1582 C CB  . VAL A 1 241 ? -1.690 19.528 -3.725  1.00 58.41  ? 1016 VAL A CB  1 
ATOM   1583 C CG1 . VAL A 1 241 ? -2.022 20.508 -4.835  1.00 59.14  ? 1016 VAL A CG1 1 
ATOM   1584 C CG2 . VAL A 1 241 ? -2.482 19.850 -2.465  1.00 58.24  ? 1016 VAL A CG2 1 
ATOM   1585 N N   . ILE A 1 242 ? -0.060 17.502 -5.574  1.00 57.65  ? 1017 ILE A N   1 
ATOM   1586 C CA  A ILE A 1 242 ? 0.600  17.195 -6.840  0.50 61.61  ? 1017 ILE A CA  1 
ATOM   1587 C CA  B ILE A 1 242 ? 0.608  17.188 -6.836  0.50 61.60  ? 1017 ILE A CA  1 
ATOM   1588 C C   . ILE A 1 242 ? -0.031 15.966 -7.481  1.00 65.72  ? 1017 ILE A C   1 
ATOM   1589 O O   . ILE A 1 242 ? -0.408 15.983 -8.659  1.00 66.29  ? 1017 ILE A O   1 
ATOM   1590 C CB  A ILE A 1 242 ? 2.112  17.002 -6.627  0.50 59.45  ? 1017 ILE A CB  1 
ATOM   1591 C CB  B ILE A 1 242 ? 2.115  16.965 -6.611  0.50 59.45  ? 1017 ILE A CB  1 
ATOM   1592 C CG1 A ILE A 1 242 ? 2.742  18.294 -6.101  0.50 56.65  ? 1017 ILE A CG1 1 
ATOM   1593 C CG1 B ILE A 1 242 ? 2.764  18.188 -5.959  0.50 56.59  ? 1017 ILE A CG1 1 
ATOM   1594 C CG2 A ILE A 1 242 ? 2.769  16.566 -7.934  0.50 60.74  ? 1017 ILE A CG2 1 
ATOM   1595 C CG2 B ILE A 1 242 ? 2.798  16.636 -7.935  0.50 60.68  ? 1017 ILE A CG2 1 
ATOM   1596 C CD1 A ILE A 1 242 ? 4.175  18.137 -5.634  0.50 57.83  ? 1017 ILE A CD1 1 
ATOM   1597 C CD1 B ILE A 1 242 ? 2.765  19.422 -6.822  0.50 71.07  ? 1017 ILE A CD1 1 
ATOM   1598 N N   . GLU A 1 243 ? -0.153 14.880 -6.716  1.00 70.79  ? 1018 GLU A N   1 
ATOM   1599 C CA  . GLU A 1 243 ? -0.670 13.638 -7.277  1.00 76.89  ? 1018 GLU A CA  1 
ATOM   1600 C C   . GLU A 1 243 ? -2.093 13.800 -7.790  1.00 75.27  ? 1018 GLU A C   1 
ATOM   1601 O O   . GLU A 1 243 ? -2.472 13.163 -8.779  1.00 76.54  ? 1018 GLU A O   1 
ATOM   1602 C CB  . GLU A 1 243 ? -0.592 12.530 -6.226  1.00 74.58  ? 1018 GLU A CB  1 
ATOM   1603 C CG  . GLU A 1 243 ? 0.835  12.208 -5.818  1.00 88.72  ? 1018 GLU A CG  1 
ATOM   1604 C CD  . GLU A 1 243 ? 0.918  11.303 -4.604  1.00 116.19 ? 1018 GLU A CD  1 
ATOM   1605 O OE1 . GLU A 1 243 ? -0.143 10.930 -4.059  1.00 110.10 ? 1018 GLU A OE1 1 
ATOM   1606 O OE2 . GLU A 1 243 ? 2.051  10.969 -4.196  1.00 92.05  ? 1018 GLU A OE2 1 
ATOM   1607 N N   . LYS A 1 244 ? -2.884 14.659 -7.153  1.00 77.01  ? 1019 LYS A N   1 
ATOM   1608 C CA  A LYS A 1 244 ? -4.278 14.861 -7.516  0.50 83.88  ? 1019 LYS A CA  1 
ATOM   1609 C CA  B LYS A 1 244 ? -4.278 14.857 -7.522  0.50 83.88  ? 1019 LYS A CA  1 
ATOM   1610 C C   . LYS A 1 244 ? -4.494 16.125 -8.341  1.00 81.19  ? 1019 LYS A C   1 
ATOM   1611 O O   . LYS A 1 244 ? -5.644 16.474 -8.633  1.00 72.69  ? 1019 LYS A O   1 
ATOM   1612 C CB  A LYS A 1 244 ? -5.138 14.909 -6.251  0.50 83.25  ? 1019 LYS A CB  1 
ATOM   1613 C CB  B LYS A 1 244 ? -5.149 14.893 -6.263  0.50 83.25  ? 1019 LYS A CB  1 
ATOM   1614 C CG  A LYS A 1 244 ? -5.045 13.645 -5.405  0.50 82.99  ? 1019 LYS A CG  1 
ATOM   1615 C CG  B LYS A 1 244 ? -4.915 13.725 -5.308  0.50 83.01  ? 1019 LYS A CG  1 
ATOM   1616 C CD  A LYS A 1 244 ? -5.919 13.703 -4.159  0.50 76.56  ? 1019 LYS A CD  1 
ATOM   1617 C CD  B LYS A 1 244 ? -5.138 12.374 -5.980  0.50 79.12  ? 1019 LYS A CD  1 
ATOM   1618 C CE  A LYS A 1 244 ? -5.564 14.883 -3.271  0.50 74.85  ? 1019 LYS A CE  1 
ATOM   1619 C CE  B LYS A 1 244 ? -4.714 11.227 -5.076  0.50 82.69  ? 1019 LYS A CE  1 
ATOM   1620 N NZ  A LYS A 1 244 ? -6.381 16.086 -3.593  0.50 64.68  ? 1019 LYS A NZ  1 
ATOM   1621 N NZ  B LYS A 1 244 ? -3.241 11.213 -4.853  0.50 84.43  ? 1019 LYS A NZ  1 
ATOM   1622 N N   . ALA A 1 245 ? -3.422 16.815 -8.722  1.00 67.26  ? 1020 ALA A N   1 
ATOM   1623 C CA  . ALA A 1 245 ? -3.562 18.066 -9.454  1.00 76.72  ? 1020 ALA A CA  1 
ATOM   1624 C C   . ALA A 1 245 ? -4.319 17.851 -10.757 1.00 76.07  ? 1020 ALA A C   1 
ATOM   1625 O O   . ALA A 1 245 ? -4.165 16.825 -11.426 1.00 64.65  ? 1020 ALA A O   1 
ATOM   1626 C CB  . ALA A 1 245 ? -2.187 18.668 -9.745  1.00 75.46  ? 1020 ALA A CB  1 
ATOM   1627 N N   . ASP A 1 246 ? -5.148 18.835 -11.114 1.00 65.27  ? 1021 ASP A N   1 
ATOM   1628 C CA  . ASP A 1 246 ? -5.854 18.829 -12.386 1.00 88.78  ? 1021 ASP A CA  1 
ATOM   1629 C C   . ASP A 1 246 ? -5.424 19.949 -13.322 1.00 72.66  ? 1021 ASP A C   1 
ATOM   1630 O O   . ASP A 1 246 ? -5.712 19.870 -14.519 1.00 66.52  ? 1021 ASP A O   1 
ATOM   1631 C CB  . ASP A 1 246 ? -7.371 18.921 -12.159 1.00 74.91  ? 1021 ASP A CB  1 
ATOM   1632 C CG  . ASP A 1 246 ? -7.772 20.150 -11.367 1.00 97.50  ? 1021 ASP A CG  1 
ATOM   1633 O OD1 . ASP A 1 246 ? -7.688 21.269 -11.917 1.00 99.26  ? 1021 ASP A OD1 1 
ATOM   1634 O OD2 . ASP A 1 246 ? -8.175 19.998 -10.194 1.00 112.54 ? 1021 ASP A OD2 1 
ATOM   1635 N N   . ASN A 1 247 ? -4.748 20.980 -12.815 1.00 70.29  ? 1022 ASN A N   1 
ATOM   1636 C CA  . ASN A 1 247 ? -4.229 22.056 -13.646 1.00 76.25  ? 1022 ASN A CA  1 
ATOM   1637 C C   . ASN A 1 247 ? -2.783 22.345 -13.266 1.00 76.14  ? 1022 ASN A C   1 
ATOM   1638 O O   . ASN A 1 247 ? -2.303 21.948 -12.202 1.00 65.81  ? 1022 ASN A O   1 
ATOM   1639 C CB  . ASN A 1 247 ? -5.070 23.334 -13.518 1.00 74.94  ? 1022 ASN A CB  1 
ATOM   1640 C CG  . ASN A 1 247 ? -5.026 23.925 -12.125 1.00 77.24  ? 1022 ASN A CG  1 
ATOM   1641 O OD1 . ASN A 1 247 ? -4.075 24.616 -11.762 1.00 84.54  ? 1022 ASN A OD1 1 
ATOM   1642 N ND2 . ASN A 1 247 ? -6.065 23.666 -11.340 1.00 102.71 ? 1022 ASN A ND2 1 
ATOM   1643 N N   . ALA A 1 248 ? -2.094 23.058 -14.159 1.00 68.69  ? 1023 ALA A N   1 
ATOM   1644 C CA  . ALA A 1 248 ? -0.668 23.299 -13.977 1.00 70.22  ? 1023 ALA A CA  1 
ATOM   1645 C C   . ALA A 1 248 ? -0.394 24.284 -12.848 1.00 68.67  ? 1023 ALA A C   1 
ATOM   1646 O O   . ALA A 1 248 ? 0.658  24.205 -12.202 1.00 59.26  ? 1023 ALA A O   1 
ATOM   1647 C CB  . ALA A 1 248 ? -0.058 23.810 -15.282 1.00 73.17  ? 1023 ALA A CB  1 
ATOM   1648 N N   . ALA A 1 249 ? -1.314 25.217 -12.599 1.00 69.05  ? 1024 ALA A N   1 
ATOM   1649 C CA  . ALA A 1 249 ? -1.092 26.203 -11.546 1.00 66.96  ? 1024 ALA A CA  1 
ATOM   1650 C C   . ALA A 1 249 ? -0.965 25.536 -10.183 1.00 71.94  ? 1024 ALA A C   1 
ATOM   1651 O O   . ALA A 1 249 ? -0.151 25.955 -9.350  1.00 72.91  ? 1024 ALA A O   1 
ATOM   1652 C CB  . ALA A 1 249 ? -2.228 27.225 -11.539 1.00 91.31  ? 1024 ALA A CB  1 
ATOM   1653 N N   . GLN A 1 250 ? -1.760 24.492 -9.935  1.00 81.63  ? 1025 GLN A N   1 
ATOM   1654 C CA  . GLN A 1 250 ? -1.700 23.811 -8.646  1.00 72.79  ? 1025 GLN A CA  1 
ATOM   1655 C C   . GLN A 1 250 ? -0.343 23.157 -8.428  1.00 57.47  ? 1025 GLN A C   1 
ATOM   1656 O O   . GLN A 1 250 ? 0.191  23.171 -7.313  1.00 56.54  ? 1025 GLN A O   1 
ATOM   1657 C CB  . GLN A 1 250 ? -2.800 22.757 -8.555  1.00 68.91  ? 1025 GLN A CB  1 
ATOM   1658 C CG  . GLN A 1 250 ? -4.202 23.299 -8.624  1.00 85.80  ? 1025 GLN A CG  1 
ATOM   1659 C CD  . GLN A 1 250 ? -5.223 22.188 -8.721  1.00 102.82 ? 1025 GLN A CD  1 
ATOM   1660 O OE1 . GLN A 1 250 ? -5.229 21.421 -9.685  1.00 89.10  ? 1025 GLN A OE1 1 
ATOM   1661 N NE2 . GLN A 1 250 ? -6.083 22.082 -7.714  1.00 110.78 ? 1025 GLN A NE2 1 
ATOM   1662 N N   . VAL A 1 251 ? 0.225  22.565 -9.481  1.00 61.97  ? 1026 VAL A N   1 
ATOM   1663 C CA  . VAL A 1 251 ? 1.479  21.832 -9.333  1.00 57.87  ? 1026 VAL A CA  1 
ATOM   1664 C C   . VAL A 1 251 ? 2.593  22.775 -8.901  1.00 62.33  ? 1026 VAL A C   1 
ATOM   1665 O O   . VAL A 1 251 ? 3.318  22.511 -7.934  1.00 58.60  ? 1026 VAL A O   1 
ATOM   1666 C CB  . VAL A 1 251 ? 1.829  21.101 -10.642 1.00 58.92  ? 1026 VAL A CB  1 
ATOM   1667 C CG1 . VAL A 1 251 ? 3.229  20.511 -10.563 1.00 58.63  ? 1026 VAL A CG1 1 
ATOM   1668 C CG2 . VAL A 1 251 ? 0.800  20.016 -10.932 1.00 59.93  ? 1026 VAL A CG2 1 
ATOM   1669 N N   . LYS A 1 252 ? 2.746  23.893 -9.612  1.00 63.74  ? 1027 LYS A N   1 
ATOM   1670 C CA  A LYS A 1 252 ? 3.786  24.853 -9.258  0.50 65.85  ? 1027 LYS A CA  1 
ATOM   1671 C CA  B LYS A 1 252 ? 3.787  24.850 -9.255  0.50 65.85  ? 1027 LYS A CA  1 
ATOM   1672 C C   . LYS A 1 252 ? 3.569  25.405 -7.854  1.00 64.90  ? 1027 LYS A C   1 
ATOM   1673 O O   . LYS A 1 252 ? 4.522  25.540 -7.079  1.00 66.62  ? 1027 LYS A O   1 
ATOM   1674 C CB  A LYS A 1 252 ? 3.818  25.985 -10.287 0.50 72.43  ? 1027 LYS A CB  1 
ATOM   1675 C CB  B LYS A 1 252 ? 3.832  25.982 -10.279 0.50 72.43  ? 1027 LYS A CB  1 
ATOM   1676 C CG  A LYS A 1 252 ? 4.893  27.034 -10.041 0.50 74.93  ? 1027 LYS A CG  1 
ATOM   1677 C CG  B LYS A 1 252 ? 4.412  25.568 -11.619 0.50 70.61  ? 1027 LYS A CG  1 
ATOM   1678 C CD  A LYS A 1 252 ? 6.294  26.464 -10.191 0.50 70.17  ? 1027 LYS A CD  1 
ATOM   1679 C CD  B LYS A 1 252 ? 4.571  26.752 -12.555 0.50 79.33  ? 1027 LYS A CD  1 
ATOM   1680 C CE  A LYS A 1 252 ? 7.345  27.497 -9.829  0.50 69.31  ? 1027 LYS A CE  1 
ATOM   1681 C CE  B LYS A 1 252 ? 3.233  27.360 -12.927 0.50 77.63  ? 1027 LYS A CE  1 
ATOM   1682 N NZ  A LYS A 1 252 ? 7.200  28.745 -10.626 0.50 67.97  ? 1027 LYS A NZ  1 
ATOM   1683 N NZ  B LYS A 1 252 ? 3.409  28.559 -13.785 0.50 72.96  ? 1027 LYS A NZ  1 
ATOM   1684 N N   . ASP A 1 253 ? 2.320  25.729 -7.509  1.00 66.89  ? 1028 ASP A N   1 
ATOM   1685 C CA  . ASP A 1 253 ? 2.030  26.240 -6.173  1.00 62.92  ? 1028 ASP A CA  1 
ATOM   1686 C C   . ASP A 1 253 ? 2.439  25.236 -5.104  1.00 61.80  ? 1028 ASP A C   1 
ATOM   1687 O O   . ASP A 1 253 ? 3.090  25.591 -4.115  1.00 66.83  ? 1028 ASP A O   1 
ATOM   1688 C CB  . ASP A 1 253 ? 0.543  26.572 -6.045  1.00 72.87  ? 1028 ASP A CB  1 
ATOM   1689 C CG  . ASP A 1 253 ? 0.133  27.762 -6.891  1.00 111.20 ? 1028 ASP A CG  1 
ATOM   1690 O OD1 . ASP A 1 253 ? 1.022  28.395 -7.501  1.00 110.07 ? 1028 ASP A OD1 1 
ATOM   1691 O OD2 . ASP A 1 253 ? -1.080 28.065 -6.944  1.00 107.09 ? 1028 ASP A OD2 1 
ATOM   1692 N N   . ALA A 1 254 ? 2.063  23.969 -5.288  1.00 58.10  ? 1029 ALA A N   1 
ATOM   1693 C CA  . ALA A 1 254 ? 2.350  22.960 -4.276  1.00 53.91  ? 1029 ALA A CA  1 
ATOM   1694 C C   . ALA A 1 254 ? 3.845  22.696 -4.167  1.00 58.06  ? 1029 ALA A C   1 
ATOM   1695 O O   . ALA A 1 254 ? 4.360  22.464 -3.068  1.00 56.10  ? 1029 ALA A O   1 
ATOM   1696 C CB  . ALA A 1 254 ? 1.594  21.673 -4.596  1.00 65.51  ? 1029 ALA A CB  1 
ATOM   1697 N N   . LEU A 1 255 ? 4.561  22.727 -5.293  1.00 57.95  ? 1030 LEU A N   1 
ATOM   1698 C CA  . LEU A 1 255 ? 6.007  22.544 -5.242  1.00 59.46  ? 1030 LEU A CA  1 
ATOM   1699 C C   . LEU A 1 255 ? 6.682  23.700 -4.518  1.00 52.43  ? 1030 LEU A C   1 
ATOM   1700 O O   . LEU A 1 255 ? 7.685  23.503 -3.823  1.00 55.62  ? 1030 LEU A O   1 
ATOM   1701 C CB  . LEU A 1 255 ? 6.575  22.403 -6.651  1.00 55.50  ? 1030 LEU A CB  1 
ATOM   1702 C CG  . LEU A 1 255 ? 6.313  21.072 -7.352  1.00 59.15  ? 1030 LEU A CG  1 
ATOM   1703 C CD1 . LEU A 1 255 ? 6.749  21.151 -8.808  1.00 56.06  ? 1030 LEU A CD1 1 
ATOM   1704 C CD2 . LEU A 1 255 ? 7.031  19.941 -6.628  1.00 54.96  ? 1030 LEU A CD2 1 
ATOM   1705 N N   . THR A 1 256 ? 6.154  24.914 -4.677  1.00 64.66  ? 1031 THR A N   1 
ATOM   1706 C CA  . THR A 1 256 ? 6.740  26.064 -4.000  1.00 58.74  ? 1031 THR A CA  1 
ATOM   1707 C C   . THR A 1 256 ? 6.590  25.945 -2.490  1.00 56.85  ? 1031 THR A C   1 
ATOM   1708 O O   . THR A 1 256 ? 7.519  26.268 -1.740  1.00 65.74  ? 1031 THR A O   1 
ATOM   1709 C CB  . THR A 1 256 ? 6.092  27.354 -4.499  1.00 72.95  ? 1031 THR A CB  1 
ATOM   1710 O OG1 . THR A 1 256 ? 6.337  27.502 -5.903  1.00 69.33  ? 1031 THR A OG1 1 
ATOM   1711 C CG2 . THR A 1 256 ? 6.657  28.556 -3.756  1.00 62.46  ? 1031 THR A CG2 1 
ATOM   1712 N N   . LYS A 1 257 ? 5.431  25.477 -2.024  1.00 59.90  ? 1032 LYS A N   1 
ATOM   1713 C CA  . LYS A 1 257 ? 5.240  25.289 -0.592  1.00 52.97  ? 1032 LYS A CA  1 
ATOM   1714 C C   . LYS A 1 257 ? 6.064  24.120 -0.068  1.00 57.73  ? 1032 LYS A C   1 
ATOM   1715 O O   . LYS A 1 257 ? 6.562  24.175 1.062   1.00 57.94  ? 1032 LYS A O   1 
ATOM   1716 C CB  . LYS A 1 257 ? 3.755  25.085 -0.288  1.00 58.52  ? 1032 LYS A CB  1 
ATOM   1717 C CG  . LYS A 1 257 ? 2.894  26.286 -0.656  1.00 66.73  ? 1032 LYS A CG  1 
ATOM   1718 C CD  . LYS A 1 257 ? 1.418  25.932 -0.733  1.00 80.47  ? 1032 LYS A CD  1 
ATOM   1719 C CE  . LYS A 1 257 ? 0.603  27.099 -1.279  1.00 85.34  ? 1032 LYS A CE  1 
ATOM   1720 N NZ  . LYS A 1 257 ? -0.789 26.704 -1.637  1.00 96.03  ? 1032 LYS A NZ  1 
ATOM   1721 N N   . MET A 1 258 ? 6.232  23.062 -0.865  1.00 52.54  ? 1033 MET A N   1 
ATOM   1722 C CA  . MET A 1 258 ? 7.044  21.938 -0.410  1.00 54.95  ? 1033 MET A CA  1 
ATOM   1723 C C   . MET A 1 258 ? 8.488  22.362 -0.189  1.00 57.59  ? 1033 MET A C   1 
ATOM   1724 O O   . MET A 1 258 ? 9.138  21.910 0.761   1.00 67.80  ? 1033 MET A O   1 
ATOM   1725 C CB  . MET A 1 258 ? 6.983  20.789 -1.413  1.00 60.37  ? 1033 MET A CB  1 
ATOM   1726 C CG  . MET A 1 258 ? 5.687  20.014 -1.391  1.00 65.15  ? 1033 MET A CG  1 
ATOM   1727 S SD  . MET A 1 258 ? 5.724  18.611 -2.527  1.00 68.98  ? 1033 MET A SD  1 
ATOM   1728 C CE  . MET A 1 258 ? 7.018  17.610 -1.798  1.00 62.31  ? 1033 MET A CE  1 
ATOM   1729 N N   . ARG A 1 259 ? 9.010  23.230 -1.057  1.00 62.64  ? 1034 ARG A N   1 
ATOM   1730 C CA  . ARG A 1 259 ? 10.386 23.685 -0.900  1.00 63.71  ? 1034 ARG A CA  1 
ATOM   1731 C C   . ARG A 1 259 ? 10.562 24.427 0.418   1.00 60.83  ? 1034 ARG A C   1 
ATOM   1732 O O   . ARG A 1 259 ? 11.525 24.188 1.155   1.00 69.27  ? 1034 ARG A O   1 
ATOM   1733 C CB  . ARG A 1 259 ? 10.785 24.579 -2.073  1.00 56.99  ? 1034 ARG A CB  1 
ATOM   1734 C CG  . ARG A 1 259 ? 12.266 24.921 -2.074  1.00 80.11  ? 1034 ARG A CG  1 
ATOM   1735 C CD  . ARG A 1 259 ? 12.647 25.845 -3.217  1.00 72.48  ? 1034 ARG A CD  1 
ATOM   1736 N NE  . ARG A 1 259 ? 14.091 26.045 -3.283  1.00 92.47  ? 1034 ARG A NE  1 
ATOM   1737 C CZ  . ARG A 1 259 ? 14.767 26.906 -2.533  1.00 90.26  ? 1034 ARG A CZ  1 
ATOM   1738 N NH1 . ARG A 1 259 ? 14.162 27.669 -1.638  1.00 100.50 ? 1034 ARG A NH1 1 
ATOM   1739 N NH2 . ARG A 1 259 ? 16.085 27.002 -2.685  1.00 99.11  ? 1034 ARG A NH2 1 
ATOM   1740 N N   . ALA A 1 260 ? 9.633  25.331 0.733   1.00 60.65  ? 1035 ALA A N   1 
ATOM   1741 C CA  . ALA A 1 260 ? 9.732  26.092 1.973   1.00 62.75  ? 1035 ALA A CA  1 
ATOM   1742 C C   . ALA A 1 260 ? 9.581  25.180 3.184   1.00 66.70  ? 1035 ALA A C   1 
ATOM   1743 O O   . ALA A 1 260 ? 10.345 25.280 4.151   1.00 72.96  ? 1035 ALA A O   1 
ATOM   1744 C CB  . ALA A 1 260 ? 8.674  27.195 1.994   1.00 59.65  ? 1035 ALA A CB  1 
ATOM   1745 N N   . ALA A 1 261 ? 8.593  24.284 3.147   1.00 61.80  ? 1036 ALA A N   1 
ATOM   1746 C CA  . ALA A 1 261 ? 8.385  23.366 4.261   1.00 62.03  ? 1036 ALA A CA  1 
ATOM   1747 C C   . ALA A 1 261 ? 9.600  22.471 4.471   1.00 75.13  ? 1036 ALA A C   1 
ATOM   1748 O O   . ALA A 1 261 ? 9.990  22.199 5.612   1.00 71.98  ? 1036 ALA A O   1 
ATOM   1749 C CB  . ALA A 1 261 ? 7.135  22.523 4.014   1.00 60.99  ? 1036 ALA A CB  1 
ATOM   1750 N N   . ALA A 1 262 ? 10.210 22.001 3.382   1.00 63.47  ? 1037 ALA A N   1 
ATOM   1751 C CA  . ALA A 1 262 ? 11.387 21.150 3.514   1.00 73.48  ? 1037 ALA A CA  1 
ATOM   1752 C C   . ALA A 1 262 ? 12.510 21.881 4.238   1.00 81.41  ? 1037 ALA A C   1 
ATOM   1753 O O   . ALA A 1 262 ? 13.155 21.318 5.131   1.00 77.00  ? 1037 ALA A O   1 
ATOM   1754 C CB  . ALA A 1 262 ? 11.852 20.680 2.135   1.00 76.33  ? 1037 ALA A CB  1 
ATOM   1755 N N   . LEU A 1 263 ? 12.756 23.139 3.870   1.00 79.67  ? 1038 LEU A N   1 
ATOM   1756 C CA  . LEU A 1 263 ? 13.813 23.904 4.523   1.00 86.53  ? 1038 LEU A CA  1 
ATOM   1757 C C   . LEU A 1 263 ? 13.471 24.191 5.980   1.00 83.58  ? 1038 LEU A C   1 
ATOM   1758 O O   . LEU A 1 263 ? 14.326 24.046 6.863   1.00 84.27  ? 1038 LEU A O   1 
ATOM   1759 C CB  . LEU A 1 263 ? 14.059 25.202 3.754   1.00 78.86  ? 1038 LEU A CB  1 
ATOM   1760 C CG  . LEU A 1 263 ? 14.697 25.006 2.378   1.00 75.58  ? 1038 LEU A CG  1 
ATOM   1761 C CD1 . LEU A 1 263 ? 14.670 26.292 1.571   1.00 97.89  ? 1038 LEU A CD1 1 
ATOM   1762 C CD2 . LEU A 1 263 ? 16.125 24.498 2.518   1.00 80.87  ? 1038 LEU A CD2 1 
ATOM   1763 N N   . ASP A 1 264 ? 12.227 24.591 6.256   1.00 80.54  ? 1039 ASP A N   1 
ATOM   1764 C CA  . ASP A 1 264 ? 11.831 24.859 7.635   1.00 81.02  ? 1039 ASP A CA  1 
ATOM   1765 C C   . ASP A 1 264 ? 11.917 23.600 8.487   1.00 85.74  ? 1039 ASP A C   1 
ATOM   1766 O O   . ASP A 1 264 ? 12.357 23.651 9.642   1.00 95.37  ? 1039 ASP A O   1 
ATOM   1767 C CB  . ASP A 1 264 ? 10.417 25.436 7.675   1.00 64.85  ? 1039 ASP A CB  1 
ATOM   1768 C CG  . ASP A 1 264 ? 10.335 26.818 7.059   1.00 94.23  ? 1039 ASP A CG  1 
ATOM   1769 O OD1 . ASP A 1 264 ? 11.359 27.536 7.070   1.00 89.78  ? 1039 ASP A OD1 1 
ATOM   1770 O OD2 . ASP A 1 264 ? 9.247  27.188 6.564   1.00 96.55  ? 1039 ASP A OD2 1 
ATOM   1771 N N   . ALA A 1 265 ? 11.496 22.457 7.939   1.00 74.32  ? 1040 ALA A N   1 
ATOM   1772 C CA  . ALA A 1 265 ? 11.635 21.203 8.670   1.00 83.52  ? 1040 ALA A CA  1 
ATOM   1773 C C   . ALA A 1 265 ? 13.096 20.886 8.950   1.00 85.01  ? 1040 ALA A C   1 
ATOM   1774 O O   . ALA A 1 265 ? 13.418 20.312 9.997   1.00 86.63  ? 1040 ALA A O   1 
ATOM   1775 C CB  . ALA A 1 265 ? 10.986 20.060 7.889   1.00 67.01  ? 1040 ALA A CB  1 
ATOM   1776 N N   . GLN A 1 266 ? 13.993 21.254 8.033   1.00 76.23  ? 1041 GLN A N   1 
ATOM   1777 C CA  . GLN A 1 266 ? 15.418 21.034 8.256   1.00 77.98  ? 1041 GLN A CA  1 
ATOM   1778 C C   . GLN A 1 266 ? 15.923 21.880 9.419   1.00 89.34  ? 1041 GLN A C   1 
ATOM   1779 O O   . GLN A 1 266 ? 16.643 21.383 10.294  1.00 92.45  ? 1041 GLN A O   1 
ATOM   1780 C CB  . GLN A 1 266 ? 16.196 21.349 6.978   1.00 76.94  ? 1041 GLN A CB  1 
ATOM   1781 C CG  . GLN A 1 266 ? 17.677 21.024 7.050   1.00 81.13  ? 1041 GLN A CG  1 
ATOM   1782 C CD  . GLN A 1 266 ? 18.387 21.274 5.735   1.00 80.63  ? 1041 GLN A CD  1 
ATOM   1783 O OE1 . GLN A 1 266 ? 18.128 22.267 5.056   1.00 91.79  ? 1041 GLN A OE1 1 
ATOM   1784 N NE2 . GLN A 1 266 ? 19.281 20.366 5.363   1.00 86.13  ? 1041 GLN A NE2 1 
ATOM   1785 N N   . LYS A 1 267 ? 15.548 23.161 9.451   1.00 87.76  ? 1042 LYS A N   1 
ATOM   1786 C CA  . LYS A 1 267 ? 16.014 24.044 10.516  1.00 82.43  ? 1042 LYS A CA  1 
ATOM   1787 C C   . LYS A 1 267 ? 15.549 23.556 11.884  1.00 93.21  ? 1042 LYS A C   1 
ATOM   1788 O O   . LYS A 1 267 ? 16.309 23.601 12.858  1.00 90.70  ? 1042 LYS A O   1 
ATOM   1789 C CB  . LYS A 1 267 ? 15.525 25.471 10.262  1.00 76.51  ? 1042 LYS A CB  1 
ATOM   1790 N N   . ALA A 1 268 ? 14.302 23.085 11.978  1.00 100.67 ? 1043 ALA A N   1 
ATOM   1791 C CA  . ALA A 1 268 ? 13.778 22.613 13.255  1.00 98.37  ? 1043 ALA A CA  1 
ATOM   1792 C C   . ALA A 1 268 ? 14.494 21.365 13.757  1.00 94.04  ? 1043 ALA A C   1 
ATOM   1793 O O   . ALA A 1 268 ? 14.391 21.046 14.946  1.00 93.99  ? 1043 ALA A O   1 
ATOM   1794 C CB  . ALA A 1 268 ? 12.280 22.328 13.136  1.00 95.25  ? 1043 ALA A CB  1 
ATOM   1795 N N   . THR A 1 269 ? 15.201 20.653 12.887  1.00 87.41  ? 1044 THR A N   1 
ATOM   1796 C CA  . THR A 1 269 ? 15.965 19.487 13.321  1.00 98.63  ? 1044 THR A CA  1 
ATOM   1797 C C   . THR A 1 269 ? 17.271 19.944 13.964  1.00 110.03 ? 1044 THR A C   1 
ATOM   1798 O O   . THR A 1 269 ? 18.000 20.742 13.367  1.00 110.99 ? 1044 THR A O   1 
ATOM   1799 C CB  . THR A 1 269 ? 16.260 18.565 12.138  1.00 108.17 ? 1044 THR A CB  1 
ATOM   1800 O OG1 . THR A 1 269 ? 15.029 18.068 11.596  1.00 107.33 ? 1044 THR A OG1 1 
ATOM   1801 C CG2 . THR A 1 269 ? 17.133 17.389 12.567  1.00 106.44 ? 1044 THR A CG2 1 
ATOM   1802 N N   . PRO A 1 270 ? 17.599 19.473 15.168  1.00 120.18 ? 1045 PRO A N   1 
ATOM   1803 C CA  . PRO A 1 270 ? 18.847 19.897 15.793  1.00 109.46 ? 1045 PRO A CA  1 
ATOM   1804 C C   . PRO A 1 270 ? 20.032 19.542 14.915  1.00 122.30 ? 1045 PRO A C   1 
ATOM   1805 O O   . PRO A 1 270 ? 19.984 18.563 14.146  1.00 129.01 ? 1045 PRO A O   1 
ATOM   1806 C CB  . PRO A 1 270 ? 18.864 19.118 17.116  1.00 108.79 ? 1045 PRO A CB  1 
ATOM   1807 C CG  . PRO A 1 270 ? 17.927 17.978 16.911  1.00 102.19 ? 1045 PRO A CG  1 
ATOM   1808 C CD  . PRO A 1 270 ? 16.865 18.510 16.009  1.00 108.77 ? 1045 PRO A CD  1 
ATOM   1809 N N   . PRO A 1 271 ? 21.112 20.309 14.994  1.00 139.35 ? 1046 PRO A N   1 
ATOM   1810 C CA  . PRO A 1 271 ? 22.236 20.113 14.071  1.00 141.88 ? 1046 PRO A CA  1 
ATOM   1811 C C   . PRO A 1 271 ? 23.069 18.887 14.427  1.00 149.77 ? 1046 PRO A C   1 
ATOM   1812 O O   . PRO A 1 271 ? 22.886 18.244 15.461  1.00 149.58 ? 1046 PRO A O   1 
ATOM   1813 C CB  . PRO A 1 271 ? 23.045 21.404 14.234  1.00 140.96 ? 1046 PRO A CB  1 
ATOM   1814 C CG  . PRO A 1 271 ? 22.771 21.827 15.639  1.00 137.29 ? 1046 PRO A CG  1 
ATOM   1815 C CD  . PRO A 1 271 ? 21.340 21.445 15.906  1.00 126.63 ? 1046 PRO A CD  1 
ATOM   1816 N N   . LYS A 1 272 ? 24.013 18.578 13.533  1.00 146.46 ? 1047 LYS A N   1 
ATOM   1817 C CA  . LYS A 1 272 ? 24.857 17.398 13.706  1.00 148.11 ? 1047 LYS A CA  1 
ATOM   1818 C C   . LYS A 1 272 ? 25.796 17.558 14.895  1.00 147.09 ? 1047 LYS A C   1 
ATOM   1819 O O   . LYS A 1 272 ? 25.780 16.748 15.829  1.00 142.57 ? 1047 LYS A O   1 
ATOM   1820 C CB  . LYS A 1 272 ? 25.660 17.134 12.430  1.00 137.15 ? 1047 LYS A CB  1 
ATOM   1821 N N   . LEU A 1 273 ? 26.631 18.597 14.874  1.00 146.89 ? 1048 LEU A N   1 
ATOM   1822 C CA  . LEU A 1 273 ? 27.665 18.760 15.889  1.00 135.60 ? 1048 LEU A CA  1 
ATOM   1823 C C   . LEU A 1 273 ? 28.516 19.993 15.610  1.00 117.58 ? 1048 LEU A C   1 
ATOM   1824 O O   . LEU A 1 273 ? 28.210 20.776 14.705  1.00 114.23 ? 1048 LEU A O   1 
ATOM   1825 C CB  . LEU A 1 273 ? 28.550 17.513 15.948  1.00 116.23 ? 1048 LEU A CB  1 
ATOM   1826 N N   . GLU A 1 274 ? 29.587 20.166 16.380  1.00 107.17 ? 1049 GLU A N   1 
ATOM   1827 C CA  . GLU A 1 274 ? 30.462 21.326 16.242  1.00 86.54  ? 1049 GLU A CA  1 
ATOM   1828 C C   . GLU A 1 274 ? 31.918 20.941 16.482  1.00 92.49  ? 1049 GLU A C   1 
ATOM   1829 O O   . GLU A 1 274 ? 32.481 21.221 17.540  1.00 78.39  ? 1049 GLU A O   1 
ATOM   1830 C CB  . GLU A 1 274 ? 30.048 22.429 17.215  1.00 73.99  ? 1049 GLU A CB  1 
ATOM   1831 N N   . MET A 1 283 ? 23.693 14.400 14.864  1.00 120.76 ? 1058 MET A N   1 
ATOM   1832 C CA  . MET A 1 283 ? 23.785 13.760 13.556  1.00 138.90 ? 1058 MET A CA  1 
ATOM   1833 C C   . MET A 1 283 ? 23.078 14.606 12.496  1.00 140.07 ? 1058 MET A C   1 
ATOM   1834 O O   . MET A 1 283 ? 22.180 15.387 12.812  1.00 135.38 ? 1058 MET A O   1 
ATOM   1835 C CB  . MET A 1 283 ? 23.181 12.353 13.613  1.00 125.97 ? 1058 MET A CB  1 
ATOM   1836 C CG  . MET A 1 283 ? 23.302 11.561 12.317  1.00 129.83 ? 1058 MET A CG  1 
ATOM   1837 S SD  . MET A 1 283 ? 25.019 11.250 11.853  1.00 148.10 ? 1058 MET A SD  1 
ATOM   1838 C CE  . MET A 1 283 ? 25.008 11.667 10.108  1.00 123.10 ? 1058 MET A CE  1 
ATOM   1839 N N   . LYS A 1 284 ? 23.496 14.453 11.239  1.00 140.05 ? 1059 LYS A N   1 
ATOM   1840 C CA  . LYS A 1 284 ? 22.899 15.150 10.102  1.00 135.77 ? 1059 LYS A CA  1 
ATOM   1841 C C   . LYS A 1 284 ? 22.636 14.176 8.958   1.00 124.91 ? 1059 LYS A C   1 
ATOM   1842 O O   . LYS A 1 284 ? 23.022 14.400 7.808   1.00 124.02 ? 1059 LYS A O   1 
ATOM   1843 C CB  . LYS A 1 284 ? 23.788 16.304 9.641   1.00 138.26 ? 1059 LYS A CB  1 
ATOM   1844 C CG  . LYS A 1 284 ? 23.435 17.644 10.269  1.00 137.90 ? 1059 LYS A CG  1 
ATOM   1845 C CD  . LYS A 1 284 ? 24.443 18.725 9.898   1.00 131.27 ? 1059 LYS A CD  1 
ATOM   1846 C CE  . LYS A 1 284 ? 24.239 19.207 8.468   1.00 126.47 ? 1059 LYS A CE  1 
ATOM   1847 N NZ  . LYS A 1 284 ? 25.215 20.262 8.073   1.00 112.46 ? 1059 LYS A NZ  1 
ATOM   1848 N N   . ASP A 1 285 ? 21.971 13.063 9.269   1.00 124.35 ? 1060 ASP A N   1 
ATOM   1849 C CA  . ASP A 1 285 ? 21.490 12.124 8.262   1.00 108.06 ? 1060 ASP A CA  1 
ATOM   1850 C C   . ASP A 1 285 ? 20.002 12.304 7.997   1.00 114.41 ? 1060 ASP A C   1 
ATOM   1851 O O   . ASP A 1 285 ? 19.579 12.392 6.840   1.00 107.90 ? 1060 ASP A O   1 
ATOM   1852 C CB  . ASP A 1 285 ? 21.764 10.680 8.695   1.00 112.90 ? 1060 ASP A CB  1 
ATOM   1853 C CG  . ASP A 1 285 ? 21.192 9.665  7.722   1.00 104.03 ? 1060 ASP A CG  1 
ATOM   1854 O OD1 . ASP A 1 285 ? 21.743 9.529  6.609   1.00 115.80 ? 1060 ASP A OD1 1 
ATOM   1855 O OD2 . ASP A 1 285 ? 20.187 9.009  8.068   1.00 92.89  ? 1060 ASP A OD2 1 
ATOM   1856 N N   . PHE A 1 286 ? 19.196 12.348 9.060   1.00 99.96  ? 1061 PHE A N   1 
ATOM   1857 C CA  . PHE A 1 286 ? 17.813 12.783 8.919   1.00 94.11  ? 1061 PHE A CA  1 
ATOM   1858 C C   . PHE A 1 286 ? 17.751 14.154 8.259   1.00 98.72  ? 1061 PHE A C   1 
ATOM   1859 O O   . PHE A 1 286 ? 16.871 14.417 7.431   1.00 90.26  ? 1061 PHE A O   1 
ATOM   1860 C CB  . PHE A 1 286 ? 17.139 12.806 10.292  1.00 100.72 ? 1061 PHE A CB  1 
ATOM   1861 C CG  . PHE A 1 286 ? 15.681 13.162 10.252  1.00 93.99  ? 1061 PHE A CG  1 
ATOM   1862 C CD1 . PHE A 1 286 ? 14.768 12.327 9.630   1.00 94.36  ? 1061 PHE A CD1 1 
ATOM   1863 C CD2 . PHE A 1 286 ? 15.220 14.322 10.856  1.00 94.28  ? 1061 PHE A CD2 1 
ATOM   1864 C CE1 . PHE A 1 286 ? 13.424 12.649 9.598   1.00 87.45  ? 1061 PHE A CE1 1 
ATOM   1865 C CE2 . PHE A 1 286 ? 13.878 14.647 10.829  1.00 89.08  ? 1061 PHE A CE2 1 
ATOM   1866 C CZ  . PHE A 1 286 ? 12.979 13.809 10.199  1.00 84.96  ? 1061 PHE A CZ  1 
ATOM   1867 N N   . ARG A 1 287 ? 18.697 15.034 8.601   1.00 102.06 ? 1062 ARG A N   1 
ATOM   1868 C CA  . ARG A 1 287 ? 18.746 16.357 7.987   1.00 99.73  ? 1062 ARG A CA  1 
ATOM   1869 C C   . ARG A 1 287 ? 19.068 16.263 6.501   1.00 89.49  ? 1062 ARG A C   1 
ATOM   1870 O O   . ARG A 1 287 ? 18.388 16.877 5.671   1.00 104.73 ? 1062 ARG A O   1 
ATOM   1871 C CB  . ARG A 1 287 ? 19.781 17.229 8.698   1.00 113.12 ? 1062 ARG A CB  1 
ATOM   1872 C CG  . ARG A 1 287 ? 19.207 18.147 9.766   1.00 107.40 ? 1062 ARG A CG  1 
ATOM   1873 C CD  . ARG A 1 287 ? 20.099 19.361 9.968   1.00 108.79 ? 1062 ARG A CD  1 
ATOM   1874 N NE  . ARG A 1 287 ? 19.426 20.433 10.689  1.00 110.07 ? 1062 ARG A NE  1 
ATOM   1875 C CZ  . ARG A 1 287 ? 19.841 21.693 10.713  1.00 120.45 ? 1062 ARG A CZ  1 
ATOM   1876 N NH1 . ARG A 1 287 ? 20.916 22.080 10.045  1.00 117.39 ? 1062 ARG A NH1 1 
ATOM   1877 N NH2 . ARG A 1 287 ? 19.158 22.588 11.421  1.00 116.55 ? 1062 ARG A NH2 1 
ATOM   1878 N N   . HIS A 1 288 ? 20.111 15.508 6.147   1.00 93.56  ? 1063 HIS A N   1 
ATOM   1879 C CA  . HIS A 1 288 ? 20.484 15.370 4.743   1.00 95.33  ? 1063 HIS A CA  1 
ATOM   1880 C C   . HIS A 1 288 ? 19.371 14.734 3.918   1.00 95.10  ? 1063 HIS A C   1 
ATOM   1881 O O   . HIS A 1 288 ? 19.370 14.865 2.689   1.00 84.43  ? 1063 HIS A O   1 
ATOM   1882 C CB  . HIS A 1 288 ? 21.774 14.554 4.625   1.00 86.05  ? 1063 HIS A CB  1 
ATOM   1883 C CG  . HIS A 1 288 ? 22.302 14.446 3.228   1.00 80.71  ? 1063 HIS A CG  1 
ATOM   1884 N ND1 . HIS A 1 288 ? 22.080 13.342 2.432   1.00 84.25  ? 1063 HIS A ND1 1 
ATOM   1885 C CD2 . HIS A 1 288 ? 23.048 15.300 2.487   1.00 82.04  ? 1063 HIS A CD2 1 
ATOM   1886 C CE1 . HIS A 1 288 ? 22.663 13.523 1.260   1.00 87.08  ? 1063 HIS A CE1 1 
ATOM   1887 N NE2 . HIS A 1 288 ? 23.257 14.703 1.267   1.00 83.39  ? 1063 HIS A NE2 1 
ATOM   1888 N N   . GLY A 1 289 ? 18.426 14.047 4.563   1.00 86.35  ? 1064 GLY A N   1 
ATOM   1889 C CA  . GLY A 1 289 ? 17.235 13.616 3.855   1.00 83.61  ? 1064 GLY A CA  1 
ATOM   1890 C C   . GLY A 1 289 ? 16.442 14.780 3.296   1.00 82.61  ? 1064 GLY A C   1 
ATOM   1891 O O   . GLY A 1 289 ? 15.838 14.670 2.225   1.00 71.04  ? 1064 GLY A O   1 
ATOM   1892 N N   . PHE A 1 290 ? 16.431 15.910 4.008   1.00 76.90  ? 1065 PHE A N   1 
ATOM   1893 C CA  . PHE A 1 290 ? 15.792 17.108 3.478   1.00 82.47  ? 1065 PHE A CA  1 
ATOM   1894 C C   . PHE A 1 290 ? 16.638 17.757 2.390   1.00 79.20  ? 1065 PHE A C   1 
ATOM   1895 O O   . PHE A 1 290 ? 16.097 18.422 1.499   1.00 79.68  ? 1065 PHE A O   1 
ATOM   1896 C CB  . PHE A 1 290 ? 15.530 18.112 4.602   1.00 69.82  ? 1065 PHE A CB  1 
ATOM   1897 C CG  . PHE A 1 290 ? 14.497 17.660 5.595   1.00 71.39  ? 1065 PHE A CG  1 
ATOM   1898 C CD1 . PHE A 1 290 ? 13.150 17.718 5.286   1.00 62.98  ? 1065 PHE A CD1 1 
ATOM   1899 C CD2 . PHE A 1 290 ? 14.872 17.190 6.842   1.00 87.82  ? 1065 PHE A CD2 1 
ATOM   1900 C CE1 . PHE A 1 290 ? 12.195 17.308 6.197   1.00 62.48  ? 1065 PHE A CE1 1 
ATOM   1901 C CE2 . PHE A 1 290 ? 13.921 16.779 7.759   1.00 89.92  ? 1065 PHE A CE2 1 
ATOM   1902 C CZ  . PHE A 1 290 ? 12.581 16.839 7.435   1.00 81.30  ? 1065 PHE A CZ  1 
ATOM   1903 N N   . ASP A 1 291 ? 17.961 17.579 2.447   1.00 90.85  ? 1066 ASP A N   1 
ATOM   1904 C CA  . ASP A 1 291 ? 18.830 18.167 1.433   1.00 80.27  ? 1066 ASP A CA  1 
ATOM   1905 C C   . ASP A 1 291 ? 18.509 17.621 0.049   1.00 86.24  ? 1066 ASP A C   1 
ATOM   1906 O O   . ASP A 1 291 ? 18.456 18.377 -0.928  1.00 76.60  ? 1066 ASP A O   1 
ATOM   1907 C CB  . ASP A 1 291 ? 20.296 17.906 1.782   1.00 79.87  ? 1066 ASP A CB  1 
ATOM   1908 C CG  . ASP A 1 291 ? 20.802 18.812 2.889   1.00 91.49  ? 1066 ASP A CG  1 
ATOM   1909 O OD1 . ASP A 1 291 ? 20.433 20.006 2.897   1.00 83.22  ? 1066 ASP A OD1 1 
ATOM   1910 O OD2 . ASP A 1 291 ? 21.568 18.332 3.751   1.00 91.16  ? 1066 ASP A OD2 1 
ATOM   1911 N N   . ILE A 1 292 ? 18.294 16.309 -0.058  1.00 73.76  ? 1067 ILE A N   1 
ATOM   1912 C CA  . ILE A 1 292 ? 17.968 15.727 -1.353  1.00 86.27  ? 1067 ILE A CA  1 
ATOM   1913 C C   . ILE A 1 292 ? 16.495 15.909 -1.700  1.00 79.28  ? 1067 ILE A C   1 
ATOM   1914 O O   . ILE A 1 292 ? 16.133 15.821 -2.879  1.00 73.99  ? 1067 ILE A O   1 
ATOM   1915 C CB  . ILE A 1 292 ? 18.367 14.242 -1.392  1.00 99.24  ? 1067 ILE A CB  1 
ATOM   1916 C CG1 . ILE A 1 292 ? 17.541 13.430 -0.399  1.00 88.67  ? 1067 ILE A CG1 1 
ATOM   1917 C CG2 . ILE A 1 292 ? 19.855 14.081 -1.096  1.00 93.14  ? 1067 ILE A CG2 1 
ATOM   1918 C CD1 . ILE A 1 292 ? 16.436 12.665 -1.054  1.00 87.69  ? 1067 ILE A CD1 1 
ATOM   1919 N N   . LEU A 1 293 ? 15.634 16.172 -0.711  1.00 69.72  ? 1068 LEU A N   1 
ATOM   1920 C CA  . LEU A 1 293 ? 14.257 16.551 -1.016  1.00 68.42  ? 1068 LEU A CA  1 
ATOM   1921 C C   . LEU A 1 293 ? 14.207 17.924 -1.673  1.00 71.12  ? 1068 LEU A C   1 
ATOM   1922 O O   . LEU A 1 293 ? 13.551 18.107 -2.704  1.00 60.03  ? 1068 LEU A O   1 
ATOM   1923 C CB  . LEU A 1 293 ? 13.404 16.545 0.251   1.00 65.91  ? 1068 LEU A CB  1 
ATOM   1924 C CG  . LEU A 1 293 ? 12.768 15.216 0.656   1.00 79.51  ? 1068 LEU A CG  1 
ATOM   1925 C CD1 . LEU A 1 293 ? 12.036 15.378 1.976   1.00 89.12  ? 1068 LEU A CD1 1 
ATOM   1926 C CD2 . LEU A 1 293 ? 11.821 14.715 -0.424  1.00 78.60  ? 1068 LEU A CD2 1 
ATOM   1927 N N   . VAL A 1 294 ? 14.887 18.907 -1.080  1.00 60.28  ? 1069 VAL A N   1 
ATOM   1928 C CA  . VAL A 1 294 ? 14.980 20.220 -1.709  1.00 77.38  ? 1069 VAL A CA  1 
ATOM   1929 C C   . VAL A 1 294 ? 15.550 20.089 -3.115  1.00 65.52  ? 1069 VAL A C   1 
ATOM   1930 O O   . VAL A 1 294 ? 15.083 20.744 -4.054  1.00 68.42  ? 1069 VAL A O   1 
ATOM   1931 C CB  . VAL A 1 294 ? 15.823 21.172 -0.843  1.00 67.52  ? 1069 VAL A CB  1 
ATOM   1932 C CG1 . VAL A 1 294 ? 16.047 22.490 -1.569  1.00 70.50  ? 1069 VAL A CG1 1 
ATOM   1933 C CG2 . VAL A 1 294 ? 15.144 21.406 0.496   1.00 63.27  ? 1069 VAL A CG2 1 
ATOM   1934 N N   . GLY A 1 295 ? 16.561 19.234 -3.284  1.00 68.90  ? 1070 GLY A N   1 
ATOM   1935 C CA  . GLY A 1 295 ? 17.116 19.023 -4.611  1.00 72.88  ? 1070 GLY A CA  1 
ATOM   1936 C C   . GLY A 1 295 ? 16.087 18.479 -5.582  1.00 74.00  ? 1070 GLY A C   1 
ATOM   1937 O O   . GLY A 1 295 ? 15.924 18.995 -6.690  1.00 75.50  ? 1070 GLY A O   1 
ATOM   1938 N N   . GLN A 1 296 ? 15.373 17.428 -5.173  1.00 67.02  ? 1071 GLN A N   1 
ATOM   1939 C CA  . GLN A 1 296 ? 14.330 16.869 -6.027  1.00 66.07  ? 1071 GLN A CA  1 
ATOM   1940 C C   . GLN A 1 296 ? 13.218 17.882 -6.273  1.00 62.75  ? 1071 GLN A C   1 
ATOM   1941 O O   . GLN A 1 296 ? 12.687 17.973 -7.386  1.00 69.23  ? 1071 GLN A O   1 
ATOM   1942 C CB  . GLN A 1 296 ? 13.768 15.594 -5.399  1.00 67.42  ? 1071 GLN A CB  1 
ATOM   1943 C CG  . GLN A 1 296 ? 14.761 14.447 -5.354  1.00 75.91  ? 1071 GLN A CG  1 
ATOM   1944 C CD  . GLN A 1 296 ? 14.195 13.207 -4.692  1.00 73.84  ? 1071 GLN A CD  1 
ATOM   1945 O OE1 . GLN A 1 296 ? 13.112 13.238 -4.112  1.00 87.12  ? 1071 GLN A OE1 1 
ATOM   1946 N NE2 . GLN A 1 296 ? 14.928 12.106 -4.778  1.00 84.11  ? 1071 GLN A NE2 1 
ATOM   1947 N N   . ILE A 1 297 ? 12.845 18.650 -5.246  1.00 63.18  ? 1072 ILE A N   1 
ATOM   1948 C CA  . ILE A 1 297 ? 11.819 19.671 -5.436  1.00 63.49  ? 1072 ILE A CA  1 
ATOM   1949 C C   . ILE A 1 297 ? 12.306 20.728 -6.419  1.00 60.97  ? 1072 ILE A C   1 
ATOM   1950 O O   . ILE A 1 297 ? 11.538 21.221 -7.254  1.00 66.41  ? 1072 ILE A O   1 
ATOM   1951 C CB  . ILE A 1 297 ? 11.418 20.293 -4.086  1.00 61.18  ? 1072 ILE A CB  1 
ATOM   1952 C CG1 . ILE A 1 297 ? 10.712 19.251 -3.215  1.00 60.25  ? 1072 ILE A CG1 1 
ATOM   1953 C CG2 . ILE A 1 297 ? 10.510 21.497 -4.309  1.00 63.13  ? 1072 ILE A CG2 1 
ATOM   1954 C CD1 . ILE A 1 297 ? 10.541 19.663 -1.769  1.00 63.87  ? 1072 ILE A CD1 1 
ATOM   1955 N N   . ASP A 1 298 ? 13.591 21.087 -6.341  1.00 63.52  ? 1073 ASP A N   1 
ATOM   1956 C CA  . ASP A 1 298 ? 14.148 22.042 -7.294  1.00 74.69  ? 1073 ASP A CA  1 
ATOM   1957 C C   . ASP A 1 298 ? 14.161 21.468 -8.705  1.00 54.02  ? 1073 ASP A C   1 
ATOM   1958 O O   . ASP A 1 298 ? 13.910 22.192 -9.676  1.00 68.27  ? 1073 ASP A O   1 
ATOM   1959 C CB  . ASP A 1 298 ? 15.561 22.447 -6.873  1.00 73.94  ? 1073 ASP A CB  1 
ATOM   1960 C CG  . ASP A 1 298 ? 15.576 23.276 -5.604  1.00 87.32  ? 1073 ASP A CG  1 
ATOM   1961 O OD1 . ASP A 1 298 ? 14.628 24.063 -5.394  1.00 92.29  ? 1073 ASP A OD1 1 
ATOM   1962 O OD2 . ASP A 1 298 ? 16.536 23.140 -4.816  1.00 102.97 ? 1073 ASP A OD2 1 
ATOM   1963 N N   . ASP A 1 299 ? 14.457 20.172 -8.840  1.00 55.40  ? 1074 ASP A N   1 
ATOM   1964 C CA  . ASP A 1 299 ? 14.367 19.530 -10.148 1.00 55.75  ? 1074 ASP A CA  1 
ATOM   1965 C C   . ASP A 1 299 ? 12.952 19.630 -10.699 1.00 58.27  ? 1074 ASP A C   1 
ATOM   1966 O O   . ASP A 1 299 ? 12.752 19.978 -11.868 1.00 58.46  ? 1074 ASP A O   1 
ATOM   1967 C CB  . ASP A 1 299 ? 14.792 18.063 -10.055 1.00 70.77  ? 1074 ASP A CB  1 
ATOM   1968 C CG  . ASP A 1 299 ? 16.234 17.896 -9.619  1.00 90.39  ? 1074 ASP A CG  1 
ATOM   1969 O OD1 . ASP A 1 299 ? 16.986 18.893 -9.646  1.00 89.04  ? 1074 ASP A OD1 1 
ATOM   1970 O OD2 . ASP A 1 299 ? 16.614 16.764 -9.246  1.00 80.39  ? 1074 ASP A OD2 1 
ATOM   1971 N N   . ALA A 1 300 ? 11.953 19.322 -9.866  1.00 56.16  ? 1075 ALA A N   1 
ATOM   1972 C CA  . ALA A 1 300 ? 10.571 19.385 -10.325 1.00 58.02  ? 1075 ALA A CA  1 
ATOM   1973 C C   . ALA A 1 300 ? 10.152 20.816 -10.624 1.00 56.53  ? 1075 ALA A C   1 
ATOM   1974 O O   . ALA A 1 300 ? 9.375  21.049 -11.556 1.00 60.22  ? 1075 ALA A O   1 
ATOM   1975 C CB  . ALA A 1 300 ? 9.636  18.763 -9.287  1.00 56.55  ? 1075 ALA A CB  1 
ATOM   1976 N N   . LEU A 1 301 ? 10.659 21.784 -9.858  1.00 56.87  ? 1076 LEU A N   1 
ATOM   1977 C CA  . LEU A 1 301 ? 10.331 23.179 -10.131 1.00 61.88  ? 1076 LEU A CA  1 
ATOM   1978 C C   . LEU A 1 301 ? 10.966 23.648 -11.434 1.00 67.37  ? 1076 LEU A C   1 
ATOM   1979 O O   . LEU A 1 301 ? 10.355 24.417 -12.186 1.00 70.16  ? 1076 LEU A O   1 
ATOM   1980 C CB  . LEU A 1 301 ? 10.777 24.062 -8.967  1.00 59.60  ? 1076 LEU A CB  1 
ATOM   1981 C CG  . LEU A 1 301 ? 9.869  24.015 -7.737  1.00 62.70  ? 1076 LEU A CG  1 
ATOM   1982 C CD1 . LEU A 1 301 ? 10.556 24.636 -6.531  1.00 79.30  ? 1076 LEU A CD1 1 
ATOM   1983 C CD2 . LEU A 1 301 ? 8.547  24.721 -8.016  1.00 68.56  ? 1076 LEU A CD2 1 
ATOM   1984 N N   . LYS A 1 302 ? 12.189 23.199 -11.722 1.00 61.16  ? 1077 LYS A N   1 
ATOM   1985 C CA  . LYS A 1 302 ? 12.813 23.560 -12.990 1.00 75.29  ? 1077 LYS A CA  1 
ATOM   1986 C C   . LYS A 1 302 ? 11.962 23.083 -14.159 1.00 65.91  ? 1077 LYS A C   1 
ATOM   1987 O O   . LYS A 1 302 ? 11.687 23.843 -15.094 1.00 66.54  ? 1077 LYS A O   1 
ATOM   1988 C CB  . LYS A 1 302 ? 14.224 22.976 -13.077 1.00 67.49  ? 1077 LYS A CB  1 
ATOM   1989 C CG  . LYS A 1 302 ? 15.072 23.616 -14.166 1.00 88.34  ? 1077 LYS A CG  1 
ATOM   1990 C CD  . LYS A 1 302 ? 16.479 23.041 -14.203 1.00 103.91 ? 1077 LYS A CD  1 
ATOM   1991 C CE  . LYS A 1 302 ? 16.510 21.663 -14.846 1.00 116.13 ? 1077 LYS A CE  1 
ATOM   1992 N NZ  . LYS A 1 302 ? 16.167 21.705 -16.297 1.00 97.63  ? 1077 LYS A NZ  1 
ATOM   1993 N N   . LEU A 1 303 ? 11.530 21.820 -14.119 1.00 60.04  ? 1078 LEU A N   1 
ATOM   1994 C CA  . LEU A 1 303 ? 10.658 21.308 -15.170 1.00 67.65  ? 1078 LEU A CA  1 
ATOM   1995 C C   . LEU A 1 303 ? 9.376  22.123 -15.263 1.00 62.66  ? 1078 LEU A C   1 
ATOM   1996 O O   . LEU A 1 303 ? 8.931  22.469 -16.363 1.00 68.50  ? 1078 LEU A O   1 
ATOM   1997 C CB  . LEU A 1 303 ? 10.330 19.839 -14.913 1.00 64.21  ? 1078 LEU A CB  1 
ATOM   1998 C CG  . LEU A 1 303 ? 11.496 18.857 -14.990 1.00 67.75  ? 1078 LEU A CG  1 
ATOM   1999 C CD1 . LEU A 1 303 ? 11.083 17.520 -14.398 1.00 61.40  ? 1078 LEU A CD1 1 
ATOM   2000 C CD2 . LEU A 1 303 ? 11.951 18.697 -16.430 1.00 62.50  ? 1078 LEU A CD2 1 
ATOM   2001 N N   . ALA A 1 304 ? 8.771  22.445 -14.118 1.00 64.28  ? 1079 ALA A N   1 
ATOM   2002 C CA  . ALA A 1 304 ? 7.502  23.163 -14.141 1.00 70.23  ? 1079 ALA A CA  1 
ATOM   2003 C C   . ALA A 1 304 ? 7.665  24.555 -14.736 1.00 61.68  ? 1079 ALA A C   1 
ATOM   2004 O O   . ALA A 1 304 ? 6.765  25.052 -15.422 1.00 66.97  ? 1079 ALA A O   1 
ATOM   2005 C CB  . ALA A 1 304 ? 6.922  23.248 -12.731 1.00 58.67  ? 1079 ALA A CB  1 
ATOM   2006 N N   . ASN A 1 305 ? 8.807  25.201 -14.487 1.00 78.00  ? 1080 ASN A N   1 
ATOM   2007 C CA  . ASN A 1 305 ? 9.021  26.550 -14.999 1.00 76.41  ? 1080 ASN A CA  1 
ATOM   2008 C C   . ASN A 1 305 ? 9.334  26.557 -16.491 1.00 76.17  ? 1080 ASN A C   1 
ATOM   2009 O O   . ASN A 1 305 ? 9.049  27.551 -17.168 1.00 86.70  ? 1080 ASN A O   1 
ATOM   2010 C CB  . ASN A 1 305 ? 10.141 27.234 -14.216 1.00 72.61  ? 1080 ASN A CB  1 
ATOM   2011 C CG  . ASN A 1 305 ? 9.752  27.520 -12.778 1.00 97.64  ? 1080 ASN A CG  1 
ATOM   2012 O OD1 . ASN A 1 305 ? 8.605  27.864 -12.490 1.00 90.72  ? 1080 ASN A OD1 1 
ATOM   2013 N ND2 . ASN A 1 305 ? 10.706 27.372 -11.865 1.00 95.74  ? 1080 ASN A ND2 1 
ATOM   2014 N N   . GLU A 1 306 ? 9.906  25.476 -17.021 1.00 65.25  ? 1081 GLU A N   1 
ATOM   2015 C CA  . GLU A 1 306 ? 10.133 25.354 -18.458 1.00 66.57  ? 1081 GLU A CA  1 
ATOM   2016 C C   . GLU A 1 306 ? 8.872  24.985 -19.233 1.00 64.12  ? 1081 GLU A C   1 
ATOM   2017 O O   . GLU A 1 306 ? 8.930  24.879 -20.463 1.00 71.72  ? 1081 GLU A O   1 
ATOM   2018 C CB  . GLU A 1 306 ? 11.217 24.308 -18.735 1.00 63.02  ? 1081 GLU A CB  1 
ATOM   2019 C CG  . GLU A 1 306 ? 12.555 24.629 -18.085 1.00 78.50  ? 1081 GLU A CG  1 
ATOM   2020 C CD  . GLU A 1 306 ? 13.545 23.482 -18.167 1.00 77.46  ? 1081 GLU A CD  1 
ATOM   2021 O OE1 . GLU A 1 306 ? 13.236 22.468 -18.827 1.00 80.56  ? 1081 GLU A OE1 1 
ATOM   2022 O OE2 . GLU A 1 306 ? 14.634 23.598 -17.568 1.00 87.24  ? 1081 GLU A OE2 1 
ATOM   2023 N N   . GLY A 1 307 ? 7.743  24.788 -18.558 1.00 72.02  ? 1082 GLY A N   1 
ATOM   2024 C CA  . GLY A 1 307 ? 6.525  24.358 -19.208 1.00 62.35  ? 1082 GLY A CA  1 
ATOM   2025 C C   . GLY A 1 307 ? 6.280  22.867 -19.161 1.00 62.98  ? 1082 GLY A C   1 
ATOM   2026 O O   . GLY A 1 307 ? 5.312  22.399 -19.768 1.00 63.93  ? 1082 GLY A O   1 
ATOM   2027 N N   . LYS A 1 308 ? 7.124  22.110 -18.463 1.00 62.54  ? 1083 LYS A N   1 
ATOM   2028 C CA  . LYS A 1 308 ? 6.989  20.656 -18.389 1.00 64.53  ? 1083 LYS A CA  1 
ATOM   2029 C C   . LYS A 1 308 ? 6.345  20.274 -17.056 1.00 62.50  ? 1083 LYS A C   1 
ATOM   2030 O O   . LYS A 1 308 ? 6.949  19.648 -16.182 1.00 61.95  ? 1083 LYS A O   1 
ATOM   2031 C CB  . LYS A 1 308 ? 8.352  19.991 -18.571 1.00 65.27  ? 1083 LYS A CB  1 
ATOM   2032 C CG  . LYS A 1 308 ? 9.066  20.368 -19.872 1.00 68.08  ? 1083 LYS A CG  1 
ATOM   2033 C CD  . LYS A 1 308 ? 10.498 19.843 -19.895 1.00 70.56  ? 1083 LYS A CD  1 
ATOM   2034 C CE  . LYS A 1 308 ? 11.254 20.289 -21.146 1.00 75.37  ? 1083 LYS A CE  1 
ATOM   2035 N NZ  . LYS A 1 308 ? 11.445 21.764 -21.204 1.00 94.77  ? 1083 LYS A NZ  1 
ATOM   2036 N N   . VAL A 1 309 ? 5.082  20.679 -16.915 1.00 62.58  ? 1084 VAL A N   1 
ATOM   2037 C CA  . VAL A 1 309 ? 4.371  20.462 -15.660 1.00 61.95  ? 1084 VAL A CA  1 
ATOM   2038 C C   . VAL A 1 309 ? 3.950  19.006 -15.520 1.00 62.64  ? 1084 VAL A C   1 
ATOM   2039 O O   . VAL A 1 309 ? 3.964  18.450 -14.418 1.00 62.07  ? 1084 VAL A O   1 
ATOM   2040 C CB  . VAL A 1 309 ? 3.169  21.417 -15.561 1.00 64.05  ? 1084 VAL A CB  1 
ATOM   2041 C CG1 . VAL A 1 309 ? 2.460  21.239 -14.222 1.00 61.18  ? 1084 VAL A CG1 1 
ATOM   2042 C CG2 . VAL A 1 309 ? 3.628  22.855 -15.743 1.00 61.24  ? 1084 VAL A CG2 1 
ATOM   2043 N N   . LYS A 1 310 ? 3.565  18.364 -16.625 1.00 63.91  ? 1085 LYS A N   1 
ATOM   2044 C CA  . LYS A 1 310 ? 3.319  16.926 -16.590 1.00 64.69  ? 1085 LYS A CA  1 
ATOM   2045 C C   . LYS A 1 310 ? 4.534  16.198 -16.030 1.00 64.25  ? 1085 LYS A C   1 
ATOM   2046 O O   . LYS A 1 310 ? 4.417  15.358 -15.129 1.00 64.03  ? 1085 LYS A O   1 
ATOM   2047 C CB  . LYS A 1 310 ? 2.980  16.424 -17.995 1.00 66.17  ? 1085 LYS A CB  1 
ATOM   2048 C CG  . LYS A 1 310 ? 2.654  14.941 -18.099 1.00 67.18  ? 1085 LYS A CG  1 
ATOM   2049 C CD  . LYS A 1 310 ? 2.736  14.485 -19.552 1.00 71.29  ? 1085 LYS A CD  1 
ATOM   2050 C CE  . LYS A 1 310 ? 2.383  13.017 -19.715 1.00 81.50  ? 1085 LYS A CE  1 
ATOM   2051 N NZ  . LYS A 1 310 ? 0.923  12.813 -19.913 1.00 100.70 ? 1085 LYS A NZ  1 
ATOM   2052 N N   . GLU A 1 311 ? 5.719  16.527 -16.549 1.00 64.12  ? 1086 GLU A N   1 
ATOM   2053 C CA  . GLU A 1 311 ? 6.949  15.941 -16.031 1.00 63.66  ? 1086 GLU A CA  1 
ATOM   2054 C C   . GLU A 1 311 ? 7.183  16.342 -14.578 1.00 62.28  ? 1086 GLU A C   1 
ATOM   2055 O O   . GLU A 1 311 ? 7.709  15.552 -13.785 1.00 64.52  ? 1086 GLU A O   1 
ATOM   2056 C CB  . GLU A 1 311 ? 8.134  16.366 -16.901 1.00 63.80  ? 1086 GLU A CB  1 
ATOM   2057 C CG  . GLU A 1 311 ? 8.197  15.703 -18.280 1.00 65.24  ? 1086 GLU A CG  1 
ATOM   2058 C CD  . GLU A 1 311 ? 7.160  16.221 -19.267 1.00 66.04  ? 1086 GLU A CD  1 
ATOM   2059 O OE1 . GLU A 1 311 ? 6.408  17.157 -18.930 1.00 65.47  ? 1086 GLU A OE1 1 
ATOM   2060 O OE2 . GLU A 1 311 ? 7.106  15.685 -20.393 1.00 67.27  ? 1086 GLU A OE2 1 
ATOM   2061 N N   . ALA A 1 312 ? 6.804  17.569 -14.211 1.00 65.11  ? 1087 ALA A N   1 
ATOM   2062 C CA  . ALA A 1 312 ? 6.977  18.010 -12.831 1.00 60.18  ? 1087 ALA A CA  1 
ATOM   2063 C C   . ALA A 1 312 ? 6.058  17.241 -11.892 1.00 60.12  ? 1087 ALA A C   1 
ATOM   2064 O O   . ALA A 1 312 ? 6.465  16.865 -10.787 1.00 59.37  ? 1087 ALA A O   1 
ATOM   2065 C CB  . ALA A 1 312 ? 6.715  19.511 -12.721 1.00 59.50  ? 1087 ALA A CB  1 
ATOM   2066 N N   . GLN A 1 313 ? 4.814  17.005 -12.313 1.00 60.93  ? 1088 GLN A N   1 
ATOM   2067 C CA  . GLN A 1 313 ? 3.893  16.214 -11.506 1.00 61.01  ? 1088 GLN A CA  1 
ATOM   2068 C C   . GLN A 1 313 ? 4.406  14.791 -11.332 1.00 61.44  ? 1088 GLN A C   1 
ATOM   2069 O O   . GLN A 1 313 ? 4.459  14.268 -10.213 1.00 63.26  ? 1088 GLN A O   1 
ATOM   2070 C CB  . GLN A 1 313 ? 2.507  16.209 -12.150 1.00 61.96  ? 1088 GLN A CB  1 
ATOM   2071 C CG  . GLN A 1 313 ? 1.497  15.334 -11.436 1.00 62.23  ? 1088 GLN A CG  1 
ATOM   2072 C CD  . GLN A 1 313 ? 0.168  15.271 -12.152 1.00 63.27  ? 1088 GLN A CD  1 
ATOM   2073 O OE1 . GLN A 1 313 ? 0.110  15.292 -13.382 1.00 68.91  ? 1088 GLN A OE1 1 
ATOM   2074 N NE2 . GLN A 1 313 ? -0.913 15.198 -11.383 1.00 71.65  ? 1088 GLN A NE2 1 
ATOM   2075 N N   . ALA A 1 314 ? 4.789  14.146 -12.436 1.00 62.49  ? 1089 ALA A N   1 
ATOM   2076 C CA  . ALA A 1 314 ? 5.252  12.766 -12.365 1.00 71.75  ? 1089 ALA A CA  1 
ATOM   2077 C C   . ALA A 1 314 ? 6.442  12.609 -11.429 1.00 66.18  ? 1089 ALA A C   1 
ATOM   2078 O O   . ALA A 1 314 ? 6.664  11.512 -10.906 1.00 77.46  ? 1089 ALA A O   1 
ATOM   2079 C CB  . ALA A 1 314 ? 5.610  12.264 -13.765 1.00 64.33  ? 1089 ALA A CB  1 
ATOM   2080 N N   . ALA A 1 315 ? 7.209  13.679 -11.203 1.00 69.00  ? 1090 ALA A N   1 
ATOM   2081 C CA  . ALA A 1 315 ? 8.335  13.624 -10.280 1.00 72.80  ? 1090 ALA A CA  1 
ATOM   2082 C C   . ALA A 1 315 ? 7.908  13.450 -8.828  1.00 78.50  ? 1090 ALA A C   1 
ATOM   2083 O O   . ALA A 1 315 ? 8.774  13.246 -7.971  1.00 77.98  ? 1090 ALA A O   1 
ATOM   2084 C CB  . ALA A 1 315 ? 9.183  14.891 -10.410 1.00 65.33  ? 1090 ALA A CB  1 
ATOM   2085 N N   . ALA A 1 316 ? 6.608  13.531 -8.527  1.00 76.98  ? 1091 ALA A N   1 
ATOM   2086 C CA  . ALA A 1 316 ? 6.166  13.344 -7.149  1.00 87.38  ? 1091 ALA A CA  1 
ATOM   2087 C C   . ALA A 1 316 ? 6.353  11.904 -6.694  1.00 83.95  ? 1091 ALA A C   1 
ATOM   2088 O O   . ALA A 1 316 ? 6.613  11.662 -5.511  1.00 88.59  ? 1091 ALA A O   1 
ATOM   2089 C CB  . ALA A 1 316 ? 4.703  13.754 -6.996  1.00 79.19  ? 1091 ALA A CB  1 
ATOM   2090 N N   . GLU A 1 317 ? 6.216  10.939 -7.606  1.00 67.19  ? 1092 GLU A N   1 
ATOM   2091 C CA  . GLU A 1 317 ? 6.488  9.552  -7.244  1.00 84.80  ? 1092 GLU A CA  1 
ATOM   2092 C C   . GLU A 1 317 ? 7.866  9.423  -6.607  1.00 75.32  ? 1092 GLU A C   1 
ATOM   2093 O O   . GLU A 1 317 ? 8.035  8.715  -5.608  1.00 77.41  ? 1092 GLU A O   1 
ATOM   2094 C CB  . GLU A 1 317 ? 6.375  8.653  -8.477  1.00 92.71  ? 1092 GLU A CB  1 
ATOM   2095 C CG  . GLU A 1 317 ? 5.141  7.760  -8.475  1.00 88.64  ? 1092 GLU A CG  1 
ATOM   2096 C CD  . GLU A 1 317 ? 5.008  6.934  -9.742  1.00 134.92 ? 1092 GLU A CD  1 
ATOM   2097 O OE1 . GLU A 1 317 ? 5.878  7.056  -10.630 1.00 142.12 ? 1092 GLU A OE1 1 
ATOM   2098 O OE2 . GLU A 1 317 ? 4.031  6.161  -9.848  1.00 136.76 ? 1092 GLU A OE2 1 
ATOM   2099 N N   . GLN A 1 318 ? 8.860  10.121 -7.161  1.00 69.69  ? 1093 GLN A N   1 
ATOM   2100 C CA  . GLN A 1 318 ? 10.202 10.079 -6.592  1.00 68.07  ? 1093 GLN A CA  1 
ATOM   2101 C C   . GLN A 1 318 ? 10.276 10.850 -5.281  1.00 77.38  ? 1093 GLN A C   1 
ATOM   2102 O O   . GLN A 1 318 ? 11.040 10.472 -4.385  1.00 78.70  ? 1093 GLN A O   1 
ATOM   2103 C CB  . GLN A 1 318 ? 11.209 10.635 -7.599  1.00 70.58  ? 1093 GLN A CB  1 
ATOM   2104 C CG  . GLN A 1 318 ? 12.652 10.634 -7.115  1.00 96.58  ? 1093 GLN A CG  1 
ATOM   2105 C CD  . GLN A 1 318 ? 13.630 11.032 -8.206  1.00 109.07 ? 1093 GLN A CD  1 
ATOM   2106 O OE1 . GLN A 1 318 ? 13.239 11.285 -9.348  1.00 114.27 ? 1093 GLN A OE1 1 
ATOM   2107 N NE2 . GLN A 1 318 ? 14.911 11.087 -7.858  1.00 99.50  ? 1093 GLN A NE2 1 
ATOM   2108 N N   . LEU A 1 319 ? 9.501  11.929 -5.152  1.00 70.79  ? 1094 LEU A N   1 
ATOM   2109 C CA  . LEU A 1 319 ? 9.445  12.651 -3.886  1.00 74.50  ? 1094 LEU A CA  1 
ATOM   2110 C C   . LEU A 1 319 ? 8.743  11.826 -2.817  1.00 73.99  ? 1094 LEU A C   1 
ATOM   2111 O O   . LEU A 1 319 ? 9.130  11.859 -1.644  1.00 71.10  ? 1094 LEU A O   1 
ATOM   2112 C CB  . LEU A 1 319 ? 8.734  13.990 -4.076  1.00 73.70  ? 1094 LEU A CB  1 
ATOM   2113 C CG  . LEU A 1 319 ? 9.451  15.013 -4.956  1.00 77.60  ? 1094 LEU A CG  1 
ATOM   2114 C CD1 . LEU A 1 319 ? 8.497  16.122 -5.369  1.00 88.00  ? 1094 LEU A CD1 1 
ATOM   2115 C CD2 . LEU A 1 319 ? 10.653 15.586 -4.228  1.00 76.97  ? 1094 LEU A CD2 1 
ATOM   2116 N N   . LYS A 1 320 ? 7.702  11.085 -3.203  1.00 68.42  ? 1095 LYS A N   1 
ATOM   2117 C CA  . LYS A 1 320 ? 7.033  10.211 -2.248  1.00 73.23  ? 1095 LYS A CA  1 
ATOM   2118 C C   . LYS A 1 320 ? 7.938  9.057  -1.838  1.00 80.17  ? 1095 LYS A C   1 
ATOM   2119 O O   . LYS A 1 320 ? 7.930  8.637  -0.675  1.00 75.03  ? 1095 LYS A O   1 
ATOM   2120 C CB  . LYS A 1 320 ? 5.725  9.690  -2.841  1.00 73.66  ? 1095 LYS A CB  1 
ATOM   2121 C CG  . LYS A 1 320 ? 4.915  8.850  -1.872  1.00 91.52  ? 1095 LYS A CG  1 
ATOM   2122 C CD  . LYS A 1 320 ? 3.504  8.599  -2.376  1.00 75.91  ? 1095 LYS A CD  1 
ATOM   2123 C CE  . LYS A 1 320 ? 3.487  7.690  -3.591  1.00 91.46  ? 1095 LYS A CE  1 
ATOM   2124 N NZ  . LYS A 1 320 ? 2.094  7.328  -3.974  1.00 112.20 ? 1095 LYS A NZ  1 
ATOM   2125 N N   . THR A 1 321 ? 8.727  8.532  -2.778  1.00 78.00  ? 1096 THR A N   1 
ATOM   2126 C CA  . THR A 1 321 ? 9.694  7.494  -2.435  1.00 81.75  ? 1096 THR A CA  1 
ATOM   2127 C C   . THR A 1 321 ? 10.701 8.012  -1.418  1.00 76.22  ? 1096 THR A C   1 
ATOM   2128 O O   . THR A 1 321 ? 10.968 7.363  -0.401  1.00 74.79  ? 1096 THR A O   1 
ATOM   2129 C CB  . THR A 1 321 ? 10.408 7.004  -3.696  1.00 81.23  ? 1096 THR A CB  1 
ATOM   2130 O OG1 . THR A 1 321 ? 9.494  6.249  -4.503  1.00 73.20  ? 1096 THR A OG1 1 
ATOM   2131 C CG2 . THR A 1 321 ? 11.612 6.137  -3.338  1.00 66.52  ? 1096 THR A CG2 1 
ATOM   2132 N N   . THR A 1 322 ? 11.275 9.187  -1.683  1.00 72.82  ? 1097 THR A N   1 
ATOM   2133 C CA  . THR A 1 322 ? 12.212 9.789  -0.743  1.00 69.30  ? 1097 THR A CA  1 
ATOM   2134 C C   . THR A 1 322 ? 11.564 9.992  0.622   1.00 73.92  ? 1097 THR A C   1 
ATOM   2135 O O   . THR A 1 322 ? 12.123 9.603  1.654   1.00 71.23  ? 1097 THR A O   1 
ATOM   2136 C CB  . THR A 1 322 ? 12.715 11.121 -1.300  1.00 71.85  ? 1097 THR A CB  1 
ATOM   2137 O OG1 . THR A 1 322 ? 13.627 10.879 -2.377  1.00 85.28  ? 1097 THR A OG1 1 
ATOM   2138 C CG2 . THR A 1 322 ? 13.404 11.935 -0.216  1.00 71.25  ? 1097 THR A CG2 1 
ATOM   2139 N N   . ARG A 1 323 ? 10.382 10.609 0.643   1.00 69.20  ? 1098 ARG A N   1 
ATOM   2140 C CA  . ARG A 1 323 ? 9.718  10.899 1.908   1.00 63.90  ? 1098 ARG A CA  1 
ATOM   2141 C C   . ARG A 1 323 ? 9.466  9.625  2.705   1.00 82.97  ? 1098 ARG A C   1 
ATOM   2142 O O   . ARG A 1 323 ? 9.654  9.603  3.928   1.00 73.07  ? 1098 ARG A O   1 
ATOM   2143 C CB  . ARG A 1 323 ? 8.408  11.642 1.639   1.00 69.86  ? 1098 ARG A CB  1 
ATOM   2144 C CG  . ARG A 1 323 ? 7.703  12.183 2.878   1.00 72.97  ? 1098 ARG A CG  1 
ATOM   2145 C CD  . ARG A 1 323 ? 6.872  11.126 3.605   1.00 77.29  ? 1098 ARG A CD  1 
ATOM   2146 N NE  . ARG A 1 323 ? 6.035  10.342 2.704   1.00 79.52  ? 1098 ARG A NE  1 
ATOM   2147 C CZ  . ARG A 1 323 ? 4.874  10.751 2.210   1.00 71.06  ? 1098 ARG A CZ  1 
ATOM   2148 N NH1 . ARG A 1 323 ? 4.392  11.953 2.481   1.00 83.63  ? 1098 ARG A NH1 1 
ATOM   2149 N NH2 . ARG A 1 323 ? 4.178  9.933  1.426   1.00 68.28  ? 1098 ARG A NH2 1 
ATOM   2150 N N   . ASN A 1 324 ? 9.041  8.552  2.034   1.00 67.19  ? 1099 ASN A N   1 
ATOM   2151 C CA  . ASN A 1 324 ? 8.763  7.308  2.745   1.00 81.31  ? 1099 ASN A CA  1 
ATOM   2152 C C   . ASN A 1 324 ? 10.033 6.683  3.307   1.00 83.53  ? 1099 ASN A C   1 
ATOM   2153 O O   . ASN A 1 324 ? 9.974  5.963  4.310   1.00 82.40  ? 1099 ASN A O   1 
ATOM   2154 C CB  . ASN A 1 324 ? 8.058  6.314  1.822   1.00 73.29  ? 1099 ASN A CB  1 
ATOM   2155 C CG  . ASN A 1 324 ? 6.690  6.795  1.379   1.00 76.55  ? 1099 ASN A CG  1 
ATOM   2156 O OD1 . ASN A 1 324 ? 6.035  7.572  2.074   1.00 88.08  ? 1099 ASN A OD1 1 
ATOM   2157 N ND2 . ASN A 1 324 ? 6.249  6.329  0.217   1.00 87.09  ? 1099 ASN A ND2 1 
ATOM   2158 N N   . ALA A 1 325 ? 11.184 6.942  2.683   1.00 69.22  ? 1100 ALA A N   1 
ATOM   2159 C CA  . ALA A 1 325 ? 12.432 6.366  3.171   1.00 61.05  ? 1100 ALA A CA  1 
ATOM   2160 C C   . ALA A 1 325 ? 12.824 6.931  4.529   1.00 78.62  ? 1100 ALA A C   1 
ATOM   2161 O O   . ALA A 1 325 ? 13.493 6.247  5.311   1.00 82.36  ? 1100 ALA A O   1 
ATOM   2162 C CB  . ALA A 1 325 ? 13.555 6.609  2.164   1.00 64.58  ? 1100 ALA A CB  1 
ATOM   2163 N N   . TYR A 1 326 ? 12.427 8.169  4.827   1.00 76.15  ? 1101 TYR A N   1 
ATOM   2164 C CA  . TYR A 1 326 ? 12.802 8.842  6.065   1.00 67.84  ? 1101 TYR A CA  1 
ATOM   2165 C C   . TYR A 1 326 ? 11.636 8.945  7.044   1.00 71.85  ? 1101 TYR A C   1 
ATOM   2166 O O   . TYR A 1 326 ? 11.704 9.716  8.007   1.00 66.23  ? 1101 TYR A O   1 
ATOM   2167 C CB  . TYR A 1 326 ? 13.359 10.232 5.754   1.00 72.88  ? 1101 TYR A CB  1 
ATOM   2168 C CG  . TYR A 1 326 ? 14.732 10.212 5.118   1.00 69.43  ? 1101 TYR A CG  1 
ATOM   2169 C CD1 . TYR A 1 326 ? 14.895 9.929  3.767   1.00 76.81  ? 1101 TYR A CD1 1 
ATOM   2170 C CD2 . TYR A 1 326 ? 15.867 10.482 5.872   1.00 76.00  ? 1101 TYR A CD2 1 
ATOM   2171 C CE1 . TYR A 1 326 ? 16.152 9.912  3.188   1.00 76.09  ? 1101 TYR A CE1 1 
ATOM   2172 C CE2 . TYR A 1 326 ? 17.123 10.468 5.303   1.00 76.76  ? 1101 TYR A CE2 1 
ATOM   2173 C CZ  . TYR A 1 326 ? 17.262 10.183 3.963   1.00 75.84  ? 1101 TYR A CZ  1 
ATOM   2174 O OH  . TYR A 1 326 ? 18.518 10.172 3.405   1.00 85.80  ? 1101 TYR A OH  1 
ATOM   2175 N N   . ILE A 1 327 ? 10.570 8.173  6.823   1.00 76.59  ? 1102 ILE A N   1 
ATOM   2176 C CA  . ILE A 1 327 ? 9.394  8.276  7.680   1.00 71.34  ? 1102 ILE A CA  1 
ATOM   2177 C C   . ILE A 1 327 ? 9.671  7.686  9.056   1.00 90.78  ? 1102 ILE A C   1 
ATOM   2178 O O   . ILE A 1 327 ? 9.109  8.143  10.059  1.00 83.88  ? 1102 ILE A O   1 
ATOM   2179 C CB  . ILE A 1 327 ? 8.191  7.592  7.006   1.00 78.44  ? 1102 ILE A CB  1 
ATOM   2180 C CG1 . ILE A 1 327 ? 6.888  8.025  7.677   1.00 90.13  ? 1102 ILE A CG1 1 
ATOM   2181 C CG2 . ILE A 1 327 ? 8.337  6.075  7.061   1.00 85.40  ? 1102 ILE A CG2 1 
ATOM   2182 C CD1 . ILE A 1 327 ? 5.673  7.819  6.802   1.00 99.31  ? 1102 ILE A CD1 1 
ATOM   2183 N N   . GLN A 1 328 ? 10.532 6.672  9.136   1.00 81.93  ? 1103 GLN A N   1 
ATOM   2184 C CA  . GLN A 1 328 ? 10.857 6.081  10.430  1.00 79.87  ? 1103 GLN A CA  1 
ATOM   2185 C C   . GLN A 1 328 ? 11.785 6.987  11.228  1.00 72.25  ? 1103 GLN A C   1 
ATOM   2186 O O   . GLN A 1 328 ? 11.559 7.226  12.420  1.00 74.61  ? 1103 GLN A O   1 
ATOM   2187 C CB  . GLN A 1 328 ? 11.485 4.701  10.232  1.00 80.04  ? 1103 GLN A CB  1 
ATOM   2188 C CG  . GLN A 1 328 ? 10.562 3.702  9.551   1.00 91.97  ? 1103 GLN A CG  1 
ATOM   2189 C CD  . GLN A 1 328 ? 9.249  3.516  10.293  1.00 91.46  ? 1103 GLN A CD  1 
ATOM   2190 O OE1 . GLN A 1 328 ? 8.177  3.527  9.691   1.00 92.49  ? 1103 GLN A OE1 1 
ATOM   2191 N NE2 . GLN A 1 328 ? 9.330  3.343  11.607  1.00 99.45  ? 1103 GLN A NE2 1 
ATOM   2192 N N   . LYS A 1 329 ? 12.838 7.502  10.588  1.00 64.63  ? 1104 LYS A N   1 
ATOM   2193 C CA  . LYS A 1 329 ? 13.719 8.444  11.270  1.00 70.82  ? 1104 LYS A CA  1 
ATOM   2194 C C   . LYS A 1 329 ? 12.943 9.643  11.794  1.00 69.12  ? 1104 LYS A C   1 
ATOM   2195 O O   . LYS A 1 329 ? 13.306 10.217 12.828  1.00 71.14  ? 1104 LYS A O   1 
ATOM   2196 C CB  . LYS A 1 329 ? 14.833 8.891  10.324  1.00 56.22  ? 1104 LYS A CB  1 
ATOM   2197 C CG  . LYS A 1 329 ? 15.938 7.860  10.168  1.00 78.02  ? 1104 LYS A CG  1 
ATOM   2198 C CD  . LYS A 1 329 ? 16.789 8.109  8.934   1.00 93.15  ? 1104 LYS A CD  1 
ATOM   2199 C CE  . LYS A 1 329 ? 17.844 7.023  8.776   1.00 97.47  ? 1104 LYS A CE  1 
ATOM   2200 N NZ  . LYS A 1 329 ? 18.474 7.035  7.428   1.00 91.89  ? 1104 LYS A NZ  1 
ATOM   2201 N N   . TYR A 1 330 ? 11.866 10.025 11.104  1.00 69.57  ? 1105 TYR A N   1 
ATOM   2202 C CA  . TYR A 1 330 ? 11.026 11.122 11.571  1.00 66.66  ? 1105 TYR A CA  1 
ATOM   2203 C C   . TYR A 1 330 ? 10.218 10.716 12.799  1.00 65.44  ? 1105 TYR A C   1 
ATOM   2204 O O   . TYR A 1 330 ? 10.115 11.484 13.763  1.00 61.74  ? 1105 TYR A O   1 
ATOM   2205 C CB  . TYR A 1 330 ? 10.105 11.573 10.440  1.00 60.26  ? 1105 TYR A CB  1 
ATOM   2206 C CG  . TYR A 1 330 ? 8.948  12.438 10.876  1.00 59.16  ? 1105 TYR A CG  1 
ATOM   2207 C CD1 . TYR A 1 330 ? 9.109  13.804 11.067  1.00 54.47  ? 1105 TYR A CD1 1 
ATOM   2208 C CD2 . TYR A 1 330 ? 7.689  11.891 11.080  1.00 58.83  ? 1105 TYR A CD2 1 
ATOM   2209 C CE1 . TYR A 1 330 ? 8.048  14.599 11.457  1.00 57.74  ? 1105 TYR A CE1 1 
ATOM   2210 C CE2 . TYR A 1 330 ? 6.623  12.677 11.470  1.00 62.32  ? 1105 TYR A CE2 1 
ATOM   2211 C CZ  . TYR A 1 330 ? 6.808  14.029 11.656  1.00 56.88  ? 1105 TYR A CZ  1 
ATOM   2212 O OH  . TYR A 1 330 ? 5.748  14.815 12.043  1.00 66.38  ? 1105 TYR A OH  1 
ATOM   2213 N N   . LEU A 1 331 ? 9.631  9.518  12.781  1.00 60.81  ? 1106 LEU A N   1 
ATOM   2214 C CA  . LEU A 1 331 ? 8.891  9.040  13.944  1.00 66.44  ? 1106 LEU A CA  1 
ATOM   2215 C C   . LEU A 1 331 ? 9.825  8.776  15.118  1.00 67.80  ? 1106 LEU A C   1 
ATOM   2216 O O   . LEU A 1 331 ? 9.473  9.040  16.274  1.00 58.10  ? 1106 LEU A O   1 
ATOM   2217 C CB  . LEU A 1 331 ? 8.121  7.771  13.586  1.00 67.38  ? 1106 LEU A CB  1 
ATOM   2218 C CG  . LEU A 1 331 ? 7.053  7.925  12.506  1.00 78.33  ? 1106 LEU A CG  1 
ATOM   2219 C CD1 . LEU A 1 331 ? 6.648  6.561  11.970  1.00 79.09  ? 1106 LEU A CD1 1 
ATOM   2220 C CD2 . LEU A 1 331 ? 5.848  8.673  13.053  1.00 74.79  ? 1106 LEU A CD2 1 
ATOM   2221 N N   . ALA A 1 332 ? 11.017 8.246  14.838  1.00 59.22  ? 900  ALA A N   1 
ATOM   2222 C CA  . ALA A 1 332 ? 11.987 8.002  15.898  1.00 51.68  ? 900  ALA A CA  1 
ATOM   2223 C C   . ALA A 1 332 ? 12.448 9.307  16.530  1.00 69.04  ? 900  ALA A C   1 
ATOM   2224 O O   . ALA A 1 332 ? 12.633 9.384  17.751  1.00 70.30  ? 900  ALA A O   1 
ATOM   2225 C CB  . ALA A 1 332 ? 13.182 7.229  15.345  1.00 56.09  ? 900  ALA A CB  1 
ATOM   2226 N N   . HIS A 1 333 ? 12.646 10.345 15.714  1.00 60.17  ? 270  HIS A N   1 
ATOM   2227 C CA  . HIS A 1 333 ? 13.056 11.634 16.260  1.00 56.42  ? 270  HIS A CA  1 
ATOM   2228 C C   . HIS A 1 333 ? 11.964 12.225 17.141  1.00 55.56  ? 270  HIS A C   1 
ATOM   2229 O O   . HIS A 1 333 ? 12.247 12.739 18.229  1.00 61.19  ? 270  HIS A O   1 
ATOM   2230 C CB  . HIS A 1 333 ? 13.409 12.599 15.131  1.00 61.79  ? 270  HIS A CB  1 
ATOM   2231 C CG  . HIS A 1 333 ? 13.816 13.956 15.610  1.00 69.34  ? 270  HIS A CG  1 
ATOM   2232 N ND1 . HIS A 1 333 ? 15.121 14.276 15.919  1.00 82.21  ? 270  HIS A ND1 1 
ATOM   2233 C CD2 . HIS A 1 333 ? 13.089 15.074 15.847  1.00 60.07  ? 270  HIS A CD2 1 
ATOM   2234 C CE1 . HIS A 1 333 ? 15.181 15.533 16.318  1.00 80.47  ? 270  HIS A CE1 1 
ATOM   2235 N NE2 . HIS A 1 333 ? 13.962 16.040 16.283  1.00 66.73  ? 270  HIS A NE2 1 
ATOM   2236 N N   . LEU A 1 334 ? 10.711 12.163 16.688  1.00 63.43  ? 271  LEU A N   1 
ATOM   2237 C CA  . LEU A 1 334 ? 9.611  12.633 17.522  1.00 66.38  ? 271  LEU A CA  1 
ATOM   2238 C C   . LEU A 1 334 ? 9.480  11.783 18.779  1.00 66.26  ? 271  LEU A C   1 
ATOM   2239 O O   . LEU A 1 334 ? 9.137  12.291 19.854  1.00 55.40  ? 271  LEU A O   1 
ATOM   2240 C CB  . LEU A 1 334 ? 8.306  12.622 16.725  1.00 64.21  ? 271  LEU A CB  1 
ATOM   2241 C CG  . LEU A 1 334 ? 8.203  13.606 15.555  1.00 73.37  ? 271  LEU A CG  1 
ATOM   2242 C CD1 . LEU A 1 334 ? 6.815  13.533 14.941  1.00 75.23  ? 271  LEU A CD1 1 
ATOM   2243 C CD2 . LEU A 1 334 ? 8.529  15.036 15.978  1.00 67.37  ? 271  LEU A CD2 1 
ATOM   2244 N N   . ALA A 1 335 ? 9.751  10.481 18.664  1.00 74.92  ? 272  ALA A N   1 
ATOM   2245 C CA  . ALA A 1 335 ? 9.707  9.613  19.833  1.00 55.87  ? 272  ALA A CA  1 
ATOM   2246 C C   . ALA A 1 335 ? 10.833 9.931  20.809  1.00 73.99  ? 272  ALA A C   1 
ATOM   2247 O O   . ALA A 1 335 ? 10.649 9.808  22.025  1.00 65.21  ? 272  ALA A O   1 
ATOM   2248 C CB  . ALA A 1 335 ? 9.777  8.149  19.399  1.00 63.46  ? 272  ALA A CB  1 
ATOM   2249 N N   . ALA A 1 336 ? 11.996 10.348 20.300  1.00 65.53  ? 273  ALA A N   1 
ATOM   2250 C CA  . ALA A 1 336 ? 13.117 10.656 21.183  1.00 61.72  ? 273  ALA A CA  1 
ATOM   2251 C C   . ALA A 1 336 ? 12.902 11.976 21.913  1.00 65.38  ? 273  ALA A C   1 
ATOM   2252 O O   . ALA A 1 336 ? 13.164 12.073 23.117  1.00 54.91  ? 273  ALA A O   1 
ATOM   2253 C CB  . ALA A 1 336 ? 14.421 10.699 20.388  1.00 47.65  ? 273  ALA A CB  1 
ATOM   2254 N N   . THR A 1 337 ? 12.441 13.008 21.203  1.00 53.61  ? 274  THR A N   1 
ATOM   2255 C CA  . THR A 1 337 ? 12.171 14.280 21.866  1.00 70.17  ? 274  THR A CA  1 
ATOM   2256 C C   . THR A 1 337 ? 11.085 14.117 22.925  1.00 64.04  ? 274  THR A C   1 
ATOM   2257 O O   . THR A 1 337 ? 11.208 14.640 24.039  1.00 52.71  ? 274  THR A O   1 
ATOM   2258 C CB  . THR A 1 337 ? 11.774 15.342 20.838  1.00 65.63  ? 274  THR A CB  1 
ATOM   2259 O OG1 . THR A 1 337 ? 10.633 14.896 20.097  1.00 74.69  ? 274  THR A OG1 1 
ATOM   2260 C CG2 . THR A 1 337 ? 12.926 15.619 19.873  1.00 59.90  ? 274  THR A CG2 1 
ATOM   2261 N N   . ARG A 1 338 ? 10.023 13.376 22.598  1.00 53.95  ? 275  ARG A N   1 
ATOM   2262 C CA  . ARG A 1 338 ? 8.980  13.081 23.576  1.00 57.33  ? 275  ARG A CA  1 
ATOM   2263 C C   . ARG A 1 338 ? 9.576  12.454 24.832  1.00 60.66  ? 275  ARG A C   1 
ATOM   2264 O O   . ARG A 1 338 ? 9.309  12.897 25.954  1.00 54.64  ? 275  ARG A O   1 
ATOM   2265 C CB  . ARG A 1 338 ? 7.937  12.150 22.947  1.00 62.74  ? 275  ARG A CB  1 
ATOM   2266 C CG  . ARG A 1 338 ? 6.621  12.051 23.709  1.00 82.89  ? 275  ARG A CG  1 
ATOM   2267 C CD  . ARG A 1 338 ? 5.647  11.058 23.063  1.00 86.10  ? 275  ARG A CD  1 
ATOM   2268 N NE  . ARG A 1 338 ? 5.458  11.296 21.633  1.00 100.11 ? 275  ARG A NE  1 
ATOM   2269 C CZ  . ARG A 1 338 ? 5.796  10.452 20.663  1.00 92.00  ? 275  ARG A CZ  1 
ATOM   2270 N NH1 . ARG A 1 338 ? 6.332  9.269  20.921  1.00 91.42  ? 275  ARG A NH1 1 
ATOM   2271 N NH2 . ARG A 1 338 ? 5.580  10.801 19.398  1.00 69.20  ? 275  ARG A NH2 1 
ATOM   2272 N N   . LYS A 1 339 ? 10.391 11.414 24.653  1.00 60.78  ? 276  LYS A N   1 
ATOM   2273 C CA  . LYS A 1 339 ? 11.019 10.753 25.791  1.00 55.33  ? 276  LYS A CA  1 
ATOM   2274 C C   . LYS A 1 339 ? 11.946 11.707 26.533  1.00 61.06  ? 276  LYS A C   1 
ATOM   2275 O O   . LYS A 1 339 ? 12.001 11.695 27.769  1.00 53.66  ? 276  LYS A O   1 
ATOM   2276 C CB  . LYS A 1 339 ? 11.774 9.518  25.300  1.00 70.07  ? 276  LYS A CB  1 
ATOM   2277 C CG  . LYS A 1 339 ? 12.374 8.641  26.382  1.00 74.13  ? 276  LYS A CG  1 
ATOM   2278 C CD  . LYS A 1 339 ? 12.805 7.298  25.801  1.00 78.95  ? 276  LYS A CD  1 
ATOM   2279 C CE  . LYS A 1 339 ? 13.742 6.551  26.733  1.00 91.01  ? 276  LYS A CE  1 
ATOM   2280 N NZ  . LYS A 1 339 ? 15.076 7.205  26.810  1.00 92.16  ? 276  LYS A NZ  1 
ATOM   2281 N N   . GLY A 1 340 ? 12.666 12.558 25.799  1.00 49.77  ? 277  GLY A N   1 
ATOM   2282 C CA  . GLY A 1 340 ? 13.556 13.508 26.447  1.00 49.75  ? 277  GLY A CA  1 
ATOM   2283 C C   . GLY A 1 340 ? 12.817 14.496 27.328  1.00 56.19  ? 277  GLY A C   1 
ATOM   2284 O O   . GLY A 1 340 ? 13.271 14.822 28.429  1.00 49.19  ? 277  GLY A O   1 
ATOM   2285 N N   . VAL A 1 341 ? 11.669 14.988 26.857  1.00 51.30  ? 278  VAL A N   1 
ATOM   2286 C CA  . VAL A 1 341 ? 10.860 15.898 27.663  1.00 58.96  ? 278  VAL A CA  1 
ATOM   2287 C C   . VAL A 1 341 ? 10.433 15.216 28.955  1.00 49.24  ? 278  VAL A C   1 
ATOM   2288 O O   . VAL A 1 341 ? 10.524 15.794 30.044  1.00 52.90  ? 278  VAL A O   1 
ATOM   2289 C CB  . VAL A 1 341 ? 9.646  16.392 26.857  1.00 54.31  ? 278  VAL A CB  1 
ATOM   2290 C CG1 . VAL A 1 341 ? 8.659  17.106 27.766  1.00 65.56  ? 278  VAL A CG1 1 
ATOM   2291 C CG2 . VAL A 1 341 ? 10.096 17.309 25.730  1.00 59.29  ? 278  VAL A CG2 1 
ATOM   2292 N N   . ARG A 1 342 ? 9.958  13.973 28.851  1.00 54.26  ? 279  ARG A N   1 
ATOM   2293 C CA  . ARG A 1 342 ? 9.590  13.217 30.044  1.00 53.63  ? 279  ARG A CA  1 
ATOM   2294 C C   . ARG A 1 342 ? 10.766 13.122 31.011  1.00 47.37  ? 279  ARG A C   1 
ATOM   2295 O O   . ARG A 1 342 ? 10.621 13.384 32.210  1.00 44.43  ? 279  ARG A O   1 
ATOM   2296 C CB  . ARG A 1 342 ? 9.098  11.825 29.639  1.00 58.26  ? 279  ARG A CB  1 
ATOM   2297 C CG  . ARG A 1 342 ? 8.692  10.925 30.798  1.00 80.47  ? 279  ARG A CG  1 
ATOM   2298 C CD  . ARG A 1 342 ? 8.138  9.597  30.299  1.00 66.86  ? 279  ARG A CD  1 
ATOM   2299 N N   . THR A 1 343 ? 11.944 12.756 30.500  1.00 44.96  ? 280  THR A N   1 
ATOM   2300 C CA  . THR A 1 343 ? 13.126 12.638 31.348  1.00 52.24  ? 280  THR A CA  1 
ATOM   2301 C C   . THR A 1 343 ? 13.425 13.951 32.060  1.00 43.41  ? 280  THR A C   1 
ATOM   2302 O O   . THR A 1 343 ? 13.693 13.968 33.267  1.00 38.43  ? 280  THR A O   1 
ATOM   2303 C CB  . THR A 1 343 ? 14.325 12.194 30.505  1.00 41.24  ? 280  THR A CB  1 
ATOM   2304 O OG1 . THR A 1 343 ? 14.039 10.927 29.903  1.00 49.97  ? 280  THR A OG1 1 
ATOM   2305 C CG2 . THR A 1 343 ? 15.580 12.072 31.361  1.00 45.79  ? 280  THR A CG2 1 
ATOM   2306 N N   . LEU A 1 344 ? 13.407 15.061 31.319  1.00 41.37  ? 281  LEU A N   1 
ATOM   2307 C CA  . LEU A 1 344 ? 13.601 16.380 31.913  1.00 47.41  ? 281  LEU A CA  1 
ATOM   2308 C C   . LEU A 1 344 ? 12.759 16.550 33.170  1.00 39.25  ? 281  LEU A C   1 
ATOM   2309 O O   . LEU A 1 344 ? 13.276 16.847 34.254  1.00 35.05  ? 281  LEU A O   1 
ATOM   2310 C CB  . LEU A 1 344 ? 13.235 17.462 30.896  1.00 55.05  ? 281  LEU A CB  1 
ATOM   2311 C CG  . LEU A 1 344 ? 14.305 17.914 29.912  1.00 59.40  ? 281  LEU A CG  1 
ATOM   2312 C CD1 . LEU A 1 344 ? 13.698 18.826 28.857  1.00 66.16  ? 281  LEU A CD1 1 
ATOM   2313 C CD2 . LEU A 1 344 ? 15.406 18.622 30.665  1.00 64.20  ? 281  LEU A CD2 1 
ATOM   2314 N N   . ALA A 1 345 ? 11.444 16.375 33.028  1.00 34.86  ? 282  ALA A N   1 
ATOM   2315 C CA  . ALA A 1 345 ? 10.533 16.630 34.135  1.00 42.01  ? 282  ALA A CA  1 
ATOM   2316 C C   . ALA A 1 345 ? 10.724 15.616 35.250  1.00 34.65  ? 282  ALA A C   1 
ATOM   2317 O O   . ALA A 1 345 ? 10.659 15.967 36.433  1.00 37.53  ? 282  ALA A O   1 
ATOM   2318 C CB  . ALA A 1 345 ? 9.087  16.597 33.641  1.00 40.46  ? 282  ALA A CB  1 
ATOM   2319 N N   . VAL A 1 346 ? 10.942 14.351 34.893  1.00 34.30  ? 283  VAL A N   1 
ATOM   2320 C CA  . VAL A 1 346 ? 11.072 13.317 35.910  1.00 33.94  ? 283  VAL A CA  1 
ATOM   2321 C C   . VAL A 1 346 ? 12.328 13.545 36.732  1.00 35.04  ? 283  VAL A C   1 
ATOM   2322 O O   . VAL A 1 346 ? 12.316 13.413 37.962  1.00 36.20  ? 283  VAL A O   1 
ATOM   2323 C CB  . VAL A 1 346 ? 11.069 11.924 35.261  1.00 36.61  ? 283  VAL A CB  1 
ATOM   2324 C CG1 . VAL A 1 346 ? 11.474 10.875 36.277  1.00 47.90  ? 283  VAL A CG1 1 
ATOM   2325 C CG2 . VAL A 1 346 ? 9.699  11.611 34.696  1.00 52.25  ? 283  VAL A CG2 1 
ATOM   2326 N N   . VAL A 1 347 ? 13.425 13.912 36.071  1.00 33.05  ? 284  VAL A N   1 
ATOM   2327 C CA  . VAL A 1 347 ? 14.681 14.113 36.779  1.00 32.42  ? 284  VAL A CA  1 
ATOM   2328 C C   . VAL A 1 347 ? 14.594 15.328 37.694  1.00 31.95  ? 284  VAL A C   1 
ATOM   2329 O O   . VAL A 1 347 ? 15.044 15.288 38.845  1.00 31.46  ? 284  VAL A O   1 
ATOM   2330 C CB  . VAL A 1 347 ? 15.831 14.235 35.766  1.00 36.24  ? 284  VAL A CB  1 
ATOM   2331 C CG1 . VAL A 1 347 ? 17.063 14.762 36.438  1.00 41.06  ? 284  VAL A CG1 1 
ATOM   2332 C CG2 . VAL A 1 347 ? 16.100 12.884 35.115  1.00 35.32  ? 284  VAL A CG2 1 
ATOM   2333 N N   . LEU A 1 348 ? 14.010 16.424 37.210  1.00 36.04  ? 285  LEU A N   1 
ATOM   2334 C CA  . LEU A 1 348 ? 13.885 17.602 38.059  1.00 31.76  ? 285  LEU A CA  1 
ATOM   2335 C C   . LEU A 1 348 ? 12.892 17.354 39.187  1.00 34.61  ? 285  LEU A C   1 
ATOM   2336 O O   . LEU A 1 348 ? 13.130 17.758 40.330  1.00 33.60  ? 285  LEU A O   1 
ATOM   2337 C CB  . LEU A 1 348 ? 13.467 18.812 37.228  1.00 33.33  ? 285  LEU A CB  1 
ATOM   2338 C CG  . LEU A 1 348 ? 13.429 20.148 37.975  1.00 43.81  ? 285  LEU A CG  1 
ATOM   2339 C CD1 . LEU A 1 348 ? 14.693 20.379 38.803  1.00 44.40  ? 285  LEU A CD1 1 
ATOM   2340 C CD2 . LEU A 1 348 ? 13.225 21.275 36.977  1.00 44.66  ? 285  LEU A CD2 1 
ATOM   2341 N N   . GLY A 1 349 ? 11.779 16.683 38.889  1.00 32.24  ? 286  GLY A N   1 
ATOM   2342 C CA  . GLY A 1 349 ? 10.843 16.334 39.944  1.00 36.23  ? 286  GLY A CA  1 
ATOM   2343 C C   . GLY A 1 349 ? 11.464 15.434 40.997  1.00 36.53  ? 286  GLY A C   1 
ATOM   2344 O O   . GLY A 1 349 ? 11.200 15.584 42.192  1.00 35.21  ? 286  GLY A O   1 
ATOM   2345 N N   . THR A 1 350 ? 12.294 14.483 40.567  1.00 32.81  ? 287  THR A N   1 
ATOM   2346 C CA  . THR A 1 350 ? 12.955 13.597 41.518  1.00 31.49  ? 287  THR A CA  1 
ATOM   2347 C C   . THR A 1 350 ? 13.942 14.369 42.380  1.00 30.83  ? 287  THR A C   1 
ATOM   2348 O O   . THR A 1 350 ? 14.008 14.163 43.597  1.00 30.49  ? 287  THR A O   1 
ATOM   2349 C CB  . THR A 1 350 ? 13.652 12.464 40.765  1.00 36.17  ? 287  THR A CB  1 
ATOM   2350 O OG1 . THR A 1 350 ? 12.674 11.706 40.041  1.00 37.85  ? 287  THR A OG1 1 
ATOM   2351 C CG2 . THR A 1 350 ? 14.403 11.544 41.721  1.00 40.65  ? 287  THR A CG2 1 
ATOM   2352 N N   . PHE A 1 351 ? 14.708 15.273 41.767  1.00 31.33  ? 288  PHE A N   1 
ATOM   2353 C CA  . PHE A 1 351 ? 15.561 16.176 42.530  1.00 37.47  ? 288  PHE A CA  1 
ATOM   2354 C C   . PHE A 1 351 ? 14.763 16.914 43.601  1.00 30.12  ? 288  PHE A C   1 
ATOM   2355 O O   . PHE A 1 351 ? 15.188 17.008 44.759  1.00 29.59  ? 288  PHE A O   1 
ATOM   2356 C CB  . PHE A 1 351 ? 16.233 17.163 41.574  1.00 39.84  ? 288  PHE A CB  1 
ATOM   2357 C CG  . PHE A 1 351 ? 17.148 18.143 42.247  1.00 32.18  ? 288  PHE A CG  1 
ATOM   2358 C CD1 . PHE A 1 351 ? 18.365 17.733 42.761  1.00 39.01  ? 288  PHE A CD1 1 
ATOM   2359 C CD2 . PHE A 1 351 ? 16.802 19.477 42.343  1.00 50.08  ? 288  PHE A CD2 1 
ATOM   2360 C CE1 . PHE A 1 351 ? 19.215 18.633 43.370  1.00 38.53  ? 288  PHE A CE1 1 
ATOM   2361 C CE2 . PHE A 1 351 ? 17.646 20.382 42.950  1.00 43.80  ? 288  PHE A CE2 1 
ATOM   2362 C CZ  . PHE A 1 351 ? 18.855 19.961 43.464  1.00 46.97  ? 288  PHE A CZ  1 
ATOM   2363 N N   . GLY A 1 352 ? 13.599 17.450 43.229  1.00 30.41  ? 289  GLY A N   1 
ATOM   2364 C CA  . GLY A 1 352 ? 12.783 18.160 44.202  1.00 34.67  ? 289  GLY A CA  1 
ATOM   2365 C C   . GLY A 1 352 ? 12.234 17.249 45.285  1.00 30.34  ? 289  GLY A C   1 
ATOM   2366 O O   . GLY A 1 352 ? 12.264 17.589 46.470  1.00 30.04  ? 289  GLY A O   1 
ATOM   2367 N N   . ALA A 1 353 ? 11.733 16.075 44.897  1.00 34.76  ? 290  ALA A N   1 
ATOM   2368 C CA  . ALA A 1 353 ? 11.206 15.146 45.892  1.00 33.47  ? 290  ALA A CA  1 
ATOM   2369 C C   . ALA A 1 353 ? 12.290 14.689 46.862  1.00 33.68  ? 290  ALA A C   1 
ATOM   2370 O O   . ALA A 1 353 ? 12.004 14.451 48.041  1.00 30.68  ? 290  ALA A O   1 
ATOM   2371 C CB  . ALA A 1 353 ? 10.567 13.941 45.200  1.00 33.33  ? 290  ALA A CB  1 
ATOM   2372 N N   . CYS A 1 354 ? 13.538 14.580 46.395  1.00 32.56  ? 291  CYS A N   1 
ATOM   2373 C CA  . CYS A 1 354 ? 14.630 14.125 47.251  1.00 34.15  ? 291  CYS A CA  1 
ATOM   2374 C C   . CYS A 1 354 ? 15.131 15.213 48.195  1.00 36.29  ? 291  CYS A C   1 
ATOM   2375 O O   . CYS A 1 354 ? 15.502 14.915 49.336  1.00 32.88  ? 291  CYS A O   1 
ATOM   2376 C CB  . CYS A 1 354 ? 15.801 13.629 46.402  1.00 32.76  ? 291  CYS A CB  1 
ATOM   2377 S SG  . CYS A 1 354 ? 15.552 12.025 45.651  1.00 40.38  ? 291  CYS A SG  1 
ATOM   2378 N N   . TRP A 1 355 ? 15.177 16.469 47.743  1.00 30.70  ? 292  TRP A N   1 
ATOM   2379 C CA  . TRP A 1 355 ? 15.817 17.528 48.516  1.00 30.36  ? 292  TRP A CA  1 
ATOM   2380 C C   . TRP A 1 355 ? 14.849 18.450 49.243  1.00 29.78  ? 292  TRP A C   1 
ATOM   2381 O O   . TRP A 1 355 ? 15.215 19.010 50.282  1.00 28.34  ? 292  TRP A O   1 
ATOM   2382 C CB  . TRP A 1 355 ? 16.708 18.387 47.614  1.00 28.46  ? 292  TRP A CB  1 
ATOM   2383 C CG  . TRP A 1 355 ? 18.087 17.848 47.446  1.00 42.31  ? 292  TRP A CG  1 
ATOM   2384 C CD1 . TRP A 1 355 ? 18.562 17.129 46.391  1.00 37.09  ? 292  TRP A CD1 1 
ATOM   2385 C CD2 . TRP A 1 355 ? 19.179 17.987 48.362  1.00 36.34  ? 292  TRP A CD2 1 
ATOM   2386 N NE1 . TRP A 1 355 ? 19.882 16.808 46.593  1.00 41.88  ? 292  TRP A NE1 1 
ATOM   2387 C CE2 . TRP A 1 355 ? 20.285 17.322 47.797  1.00 36.45  ? 292  TRP A CE2 1 
ATOM   2388 C CE3 . TRP A 1 355 ? 19.327 18.605 49.608  1.00 34.87  ? 292  TRP A CE3 1 
ATOM   2389 C CZ2 . TRP A 1 355 ? 21.523 17.262 48.429  1.00 36.63  ? 292  TRP A CZ2 1 
ATOM   2390 C CZ3 . TRP A 1 355 ? 20.561 18.543 50.235  1.00 41.68  ? 292  TRP A CZ3 1 
ATOM   2391 C CH2 . TRP A 1 355 ? 21.640 17.876 49.645  1.00 31.22  ? 292  TRP A CH2 1 
ATOM   2392 N N   . LEU A 1 356 ? 13.641 18.640 48.735  1.00 33.28  ? 293  LEU A N   1 
ATOM   2393 C CA  . LEU A 1 356 ? 12.760 19.653 49.308  1.00 34.83  ? 293  LEU A CA  1 
ATOM   2394 C C   . LEU A 1 356 ? 12.278 19.269 50.703  1.00 29.18  ? 293  LEU A C   1 
ATOM   2395 O O   . LEU A 1 356 ? 12.274 20.128 51.592  1.00 30.41  ? 293  LEU A O   1 
ATOM   2396 C CB  . LEU A 1 356 ? 11.566 19.915 48.388  1.00 35.61  ? 293  LEU A CB  1 
ATOM   2397 C CG  . LEU A 1 356 ? 11.894 20.839 47.213  1.00 53.24  ? 293  LEU A CG  1 
ATOM   2398 C CD1 . LEU A 1 356 ? 10.790 20.811 46.167  1.00 47.92  ? 293  LEU A CD1 1 
ATOM   2399 C CD2 . LEU A 1 356 ? 12.138 22.268 47.698  1.00 42.92  ? 293  LEU A CD2 1 
ATOM   2400 N N   . PRO A 1 357 ? 11.861 18.020 50.948  1.00 30.60  ? 294  PRO A N   1 
ATOM   2401 C CA  . PRO A 1 357 ? 11.470 17.665 52.325  1.00 32.26  ? 294  PRO A CA  1 
ATOM   2402 C C   . PRO A 1 357 ? 12.579 17.926 53.328  1.00 31.09  ? 294  PRO A C   1 
ATOM   2403 O O   . PRO A 1 357 ? 12.328 18.471 54.409  1.00 28.54  ? 294  PRO A O   1 
ATOM   2404 C CB  . PRO A 1 357 ? 11.123 16.172 52.220  1.00 34.46  ? 294  PRO A CB  1 
ATOM   2405 C CG  . PRO A 1 357 ? 10.774 15.963 50.776  1.00 35.66  ? 294  PRO A CG  1 
ATOM   2406 C CD  . PRO A 1 357 ? 11.662 16.900 50.010  1.00 32.19  ? 294  PRO A CD  1 
ATOM   2407 N N   . PHE A 1 358 ? 13.813 17.568 52.975  1.00 31.19  ? 295  PHE A N   1 
ATOM   2408 C CA  . PHE A 1 358 ? 14.959 17.836 53.837  1.00 31.83  ? 295  PHE A CA  1 
ATOM   2409 C C   . PHE A 1 358 ? 15.185 19.335 54.010  1.00 30.15  ? 295  PHE A C   1 
ATOM   2410 O O   . PHE A 1 358 ? 15.318 19.831 55.135  1.00 27.57  ? 295  PHE A O   1 
ATOM   2411 C CB  . PHE A 1 358 ? 16.194 17.158 53.241  1.00 27.50  ? 295  PHE A CB  1 
ATOM   2412 C CG  . PHE A 1 358 ? 17.425 17.244 54.101  1.00 34.92  ? 295  PHE A CG  1 
ATOM   2413 C CD1 . PHE A 1 358 ? 17.408 16.805 55.411  1.00 31.53  ? 295  PHE A CD1 1 
ATOM   2414 C CD2 . PHE A 1 358 ? 18.610 17.734 53.582  1.00 34.47  ? 295  PHE A CD2 1 
ATOM   2415 C CE1 . PHE A 1 358 ? 18.546 16.874 56.193  1.00 34.34  ? 295  PHE A CE1 1 
ATOM   2416 C CE2 . PHE A 1 358 ? 19.746 17.806 54.357  1.00 49.29  ? 295  PHE A CE2 1 
ATOM   2417 C CZ  . PHE A 1 358 ? 19.715 17.374 55.664  1.00 38.69  ? 295  PHE A CZ  1 
ATOM   2418 N N   . ALA A 1 359 ? 15.232 20.075 52.901  1.00 29.37  ? 296  ALA A N   1 
ATOM   2419 C CA  . ALA A 1 359 ? 15.474 21.513 52.981  1.00 27.97  ? 296  ALA A CA  1 
ATOM   2420 C C   . ALA A 1 359 ? 14.414 22.207 53.825  1.00 33.68  ? 296  ALA A C   1 
ATOM   2421 O O   . ALA A 1 359 ? 14.719 23.154 54.560  1.00 30.34  ? 296  ALA A O   1 
ATOM   2422 C CB  . ALA A 1 359 ? 15.512 22.118 51.581  1.00 28.22  ? 296  ALA A CB  1 
ATOM   2423 N N   . ILE A 1 360 ? 13.163 21.752 53.733  1.00 28.59  ? 297  ILE A N   1 
ATOM   2424 C CA  . ILE A 1 360 ? 12.094 22.367 54.513  1.00 28.90  ? 297  ILE A CA  1 
ATOM   2425 C C   . ILE A 1 360 ? 12.211 21.972 55.980  1.00 28.72  ? 297  ILE A C   1 
ATOM   2426 O O   . ILE A 1 360 ? 12.125 22.818 56.877  1.00 32.82  ? 297  ILE A O   1 
ATOM   2427 C CB  . ILE A 1 360 ? 10.721 21.983 53.933  1.00 29.40  ? 297  ILE A CB  1 
ATOM   2428 C CG1 . ILE A 1 360 ? 10.519 22.660 52.577  1.00 30.73  ? 297  ILE A CG1 1 
ATOM   2429 C CG2 . ILE A 1 360 ? 9.611  22.378 54.889  1.00 29.72  ? 297  ILE A CG2 1 
ATOM   2430 C CD1 . ILE A 1 360 ? 9.345  22.117 51.781  1.00 30.18  ? 297  ILE A CD1 1 
ATOM   2431 N N   . TYR A 1 361 ? 12.403 20.679 56.248  1.00 32.43  ? 298  TYR A N   1 
ATOM   2432 C CA  . TYR A 1 361 ? 12.466 20.232 57.635  1.00 28.20  ? 298  TYR A CA  1 
ATOM   2433 C C   . TYR A 1 361 ? 13.650 20.851 58.362  1.00 31.04  ? 298  TYR A C   1 
ATOM   2434 O O   . TYR A 1 361 ? 13.589 21.069 59.578  1.00 30.31  ? 298  TYR A O   1 
ATOM   2435 C CB  . TYR A 1 361 ? 12.539 18.705 57.697  1.00 33.54  ? 298  TYR A CB  1 
ATOM   2436 C CG  . TYR A 1 361 ? 12.685 18.185 59.104  1.00 28.09  ? 298  TYR A CG  1 
ATOM   2437 C CD1 . TYR A 1 361 ? 11.647 18.305 60.018  1.00 32.85  ? 298  TYR A CD1 1 
ATOM   2438 C CD2 . TYR A 1 361 ? 13.862 17.592 59.524  1.00 31.26  ? 298  TYR A CD2 1 
ATOM   2439 C CE1 . TYR A 1 361 ? 11.781 17.844 61.313  1.00 34.06  ? 298  TYR A CE1 1 
ATOM   2440 C CE2 . TYR A 1 361 ? 14.006 17.129 60.810  1.00 34.73  ? 298  TYR A CE2 1 
ATOM   2441 C CZ  . TYR A 1 361 ? 12.961 17.255 61.701  1.00 33.87  ? 298  TYR A CZ  1 
ATOM   2442 O OH  . TYR A 1 361 ? 13.105 16.794 62.987  1.00 36.96  ? 298  TYR A OH  1 
ATOM   2443 N N   . CYS A 1 362 ? 14.723 21.165 57.630  1.00 27.58  ? 299  CYS A N   1 
ATOM   2444 C CA  . CYS A 1 362 ? 15.909 21.751 58.239  1.00 27.24  ? 299  CYS A CA  1 
ATOM   2445 C C   . CYS A 1 362 ? 15.662 23.164 58.756  1.00 28.61  ? 299  CYS A C   1 
ATOM   2446 O O   . CYS A 1 362 ? 16.375 23.610 59.662  1.00 38.64  ? 299  CYS A O   1 
ATOM   2447 C CB  . CYS A 1 362 ? 17.067 21.748 57.238  1.00 27.01  ? 299  CYS A CB  1 
ATOM   2448 S SG  . CYS A 1 362 ? 17.997 20.184 57.213  1.00 37.31  ? 299  CYS A SG  1 
ATOM   2449 N N   . VAL A 1 363 ? 14.685 23.884 58.205  1.00 31.20  ? 300  VAL A N   1 
ATOM   2450 C CA  . VAL A 1 363 ? 14.350 25.208 58.721  1.00 33.92  ? 300  VAL A CA  1 
ATOM   2451 C C   . VAL A 1 363 ? 13.134 25.183 59.647  1.00 41.08  ? 300  VAL A C   1 
ATOM   2452 O O   . VAL A 1 363 ? 12.942 26.136 60.418  1.00 42.11  ? 300  VAL A O   1 
ATOM   2453 C CB  . VAL A 1 363 ? 14.113 26.224 57.580  1.00 38.37  ? 300  VAL A CB  1 
ATOM   2454 C CG1 . VAL A 1 363 ? 15.398 26.501 56.828  1.00 42.09  ? 300  VAL A CG1 1 
ATOM   2455 C CG2 . VAL A 1 363 ? 13.062 25.730 56.622  1.00 33.56  ? 300  VAL A CG2 1 
ATOM   2456 N N   . VAL A 1 364 ? 12.317 24.133 59.598  1.00 30.66  ? 301  VAL A N   1 
ATOM   2457 C CA  . VAL A 1 364 ? 11.126 24.044 60.442  1.00 31.68  ? 301  VAL A CA  1 
ATOM   2458 C C   . VAL A 1 364 ? 11.407 23.275 61.727  1.00 38.65  ? 301  VAL A C   1 
ATOM   2459 O O   . VAL A 1 364 ? 10.939 23.662 62.801  1.00 36.93  ? 301  VAL A O   1 
ATOM   2460 C CB  . VAL A 1 364 ? 9.968  23.398 59.652  1.00 30.06  ? 301  VAL A CB  1 
ATOM   2461 C CG1 . VAL A 1 364 ? 8.812  23.068 60.580  1.00 45.62  ? 301  VAL A CG1 1 
ATOM   2462 C CG2 . VAL A 1 364 ? 9.505  24.314 58.535  1.00 40.09  ? 301  VAL A CG2 1 
ATOM   2463 N N   . GLY A 1 365 ? 12.153 22.178 61.639  1.00 32.62  ? 302  GLY A N   1 
ATOM   2464 C CA  . GLY A 1 365 ? 12.421 21.362 62.804  1.00 36.50  ? 302  GLY A CA  1 
ATOM   2465 C C   . GLY A 1 365 ? 13.392 22.024 63.762  1.00 35.72  ? 302  GLY A C   1 
ATOM   2466 O O   . GLY A 1 365 ? 13.967 23.080 63.493  1.00 39.33  ? 302  GLY A O   1 
ATOM   2467 N N   . SER A 1 366 ? 13.576 21.379 64.914  1.00 36.49  ? 303  SER A N   1 
ATOM   2468 C CA  . SER A 1 366 ? 14.509 21.857 65.925  1.00 40.49  ? 303  SER A CA  1 
ATOM   2469 C C   . SER A 1 366 ? 15.217 20.670 66.560  1.00 39.97  ? 303  SER A C   1 
ATOM   2470 O O   . SER A 1 366 ? 14.836 19.511 66.368  1.00 40.64  ? 303  SER A O   1 
ATOM   2471 C CB  . SER A 1 366 ? 13.811 22.681 67.010  1.00 54.03  ? 303  SER A CB  1 
ATOM   2472 O OG  . SER A 1 366 ? 13.232 21.839 67.993  1.00 71.68  ? 303  SER A OG  1 
ATOM   2473 N N   . HIS A 1 367 ? 16.251 20.981 67.345  1.00 41.22  ? 304  HIS A N   1 
ATOM   2474 C CA  . HIS A 1 367 ? 17.120 19.949 67.897  1.00 44.85  ? 304  HIS A CA  1 
ATOM   2475 C C   . HIS A 1 367 ? 16.386 19.008 68.843  1.00 37.41  ? 304  HIS A C   1 
ATOM   2476 O O   . HIS A 1 367 ? 16.860 17.890 69.075  1.00 39.91  ? 304  HIS A O   1 
ATOM   2477 C CB  . HIS A 1 367 ? 18.307 20.597 68.617  1.00 48.72  ? 304  HIS A CB  1 
ATOM   2478 C CG  . HIS A 1 367 ? 17.919 21.479 69.762  1.00 51.40  ? 304  HIS A CG  1 
ATOM   2479 N ND1 . HIS A 1 367 ? 17.786 21.009 71.052  1.00 58.27  ? 304  HIS A ND1 1 
ATOM   2480 C CD2 . HIS A 1 367 ? 17.642 22.804 69.814  1.00 49.50  ? 304  HIS A CD2 1 
ATOM   2481 C CE1 . HIS A 1 367 ? 17.438 22.005 71.847  1.00 54.58  ? 304  HIS A CE1 1 
ATOM   2482 N NE2 . HIS A 1 367 ? 17.344 23.104 71.122  1.00 64.65  ? 304  HIS A NE2 1 
ATOM   2483 N N   . GLU A 1 368 ? 15.241 19.423 69.386  1.00 39.98  ? 305  GLU A N   1 
ATOM   2484 C CA  . GLU A 1 368 ? 14.478 18.543 70.261  1.00 44.35  ? 305  GLU A CA  1 
ATOM   2485 C C   . GLU A 1 368 ? 13.830 17.386 69.511  1.00 52.60  ? 305  GLU A C   1 
ATOM   2486 O O   . GLU A 1 368 ? 13.515 16.367 70.134  1.00 39.73  ? 305  GLU A O   1 
ATOM   2487 C CB  . GLU A 1 368 ? 13.393 19.331 70.992  1.00 41.33  ? 305  GLU A CB  1 
ATOM   2488 C CG  . GLU A 1 368 ? 13.914 20.419 71.916  1.00 62.36  ? 305  GLU A CG  1 
ATOM   2489 C CD  . GLU A 1 368 ? 12.801 21.073 72.715  1.00 77.44  ? 305  GLU A CD  1 
ATOM   2490 O OE1 . GLU A 1 368 ? 11.859 20.359 73.120  1.00 76.92  ? 305  GLU A OE1 1 
ATOM   2491 O OE2 . GLU A 1 368 ? 12.860 22.301 72.927  1.00 94.75  ? 305  GLU A OE2 1 
ATOM   2492 N N   . ASP A 1 369 ? 13.614 17.517 68.203  1.00 36.56  ? 306  ASP A N   1 
ATOM   2493 C CA  . ASP A 1 369 ? 12.978 16.444 67.454  1.00 41.72  ? 306  ASP A CA  1 
ATOM   2494 C C   . ASP A 1 369 ? 13.824 15.172 67.540  1.00 29.52  ? 306  ASP A C   1 
ATOM   2495 O O   . ASP A 1 369 ? 15.055 15.238 67.579  1.00 33.56  ? 306  ASP A O   1 
ATOM   2496 C CB  . ASP A 1 369 ? 12.800 16.826 65.983  1.00 35.27  ? 306  ASP A CB  1 
ATOM   2497 C CG  . ASP A 1 369 ? 11.920 18.047 65.784  1.00 43.57  ? 306  ASP A CG  1 
ATOM   2498 O OD1 . ASP A 1 369 ? 11.203 18.445 66.729  1.00 32.56  ? 306  ASP A OD1 1 
ATOM   2499 O OD2 . ASP A 1 369 ? 11.938 18.602 64.662  1.00 37.49  ? 306  ASP A OD2 1 
ATOM   2500 N N   . PRO A 1 370 ? 13.192 13.996 67.554  1.00 33.50  ? 307  PRO A N   1 
ATOM   2501 C CA  . PRO A 1 370 ? 13.964 12.753 67.453  1.00 38.63  ? 307  PRO A CA  1 
ATOM   2502 C C   . PRO A 1 370 ? 14.741 12.711 66.147  1.00 36.23  ? 307  PRO A C   1 
ATOM   2503 O O   . PRO A 1 370 ? 14.287 13.210 65.116  1.00 37.39  ? 307  PRO A O   1 
ATOM   2504 C CB  . PRO A 1 370 ? 12.893 11.656 67.504  1.00 37.85  ? 307  PRO A CB  1 
ATOM   2505 C CG  . PRO A 1 370 ? 11.682 12.306 68.073  1.00 48.44  ? 307  PRO A CG  1 
ATOM   2506 C CD  . PRO A 1 370 ? 11.747 13.742 67.658  1.00 30.54  ? 307  PRO A CD  1 
ATOM   2507 N N   . ALA A 1 371 ? 15.923 12.092 66.199  1.00 34.70  ? 308  ALA A N   1 
ATOM   2508 C CA  . ALA A 1 371 ? 16.834 12.133 65.061  1.00 38.03  ? 308  ALA A CA  1 
ATOM   2509 C C   . ALA A 1 371 ? 16.281 11.416 63.839  1.00 33.59  ? 308  ALA A C   1 
ATOM   2510 O O   . ALA A 1 371 ? 16.753 11.670 62.726  1.00 34.76  ? 308  ALA A O   1 
ATOM   2511 C CB  . ALA A 1 371 ? 18.183 11.520 65.440  1.00 39.77  ? 308  ALA A CB  1 
ATOM   2512 N N   . VAL A 1 372 ? 15.294 10.533 64.015  1.00 27.46  ? 309  VAL A N   1 
ATOM   2513 C CA  . VAL A 1 372 ? 14.798 9.738  62.896  1.00 31.86  ? 309  VAL A CA  1 
ATOM   2514 C C   . VAL A 1 372 ? 14.223 10.626 61.802  1.00 38.03  ? 309  VAL A C   1 
ATOM   2515 O O   . VAL A 1 372 ? 14.256 10.268 60.619  1.00 34.51  ? 309  VAL A O   1 
ATOM   2516 C CB  . VAL A 1 372 ? 13.751 8.718  63.386  1.00 35.13  ? 309  VAL A CB  1 
ATOM   2517 C CG1 . VAL A 1 372 ? 12.570 9.423  64.048  1.00 39.03  ? 309  VAL A CG1 1 
ATOM   2518 C CG2 . VAL A 1 372 ? 13.272 7.854  62.227  1.00 41.17  ? 309  VAL A CG2 1 
ATOM   2519 N N   . TYR A 1 373 ? 13.675 11.783 62.168  1.00 32.97  ? 310  TYR A N   1 
ATOM   2520 C CA  . TYR A 1 373 ? 13.042 12.630 61.166  1.00 33.23  ? 310  TYR A CA  1 
ATOM   2521 C C   . TYR A 1 373 ? 14.084 13.321 60.302  1.00 31.99  ? 310  TYR A C   1 
ATOM   2522 O O   . TYR A 1 373 ? 13.840 13.573 59.117  1.00 32.37  ? 310  TYR A O   1 
ATOM   2523 C CB  . TYR A 1 373 ? 12.113 13.623 61.856  1.00 32.12  ? 310  TYR A CB  1 
ATOM   2524 C CG  . TYR A 1 373 ? 10.995 12.910 62.584  1.00 35.71  ? 310  TYR A CG  1 
ATOM   2525 C CD1 . TYR A 1 373 ? 9.975  12.292 61.876  1.00 38.53  ? 310  TYR A CD1 1 
ATOM   2526 C CD2 . TYR A 1 373 ? 10.976 12.824 63.970  1.00 43.09  ? 310  TYR A CD2 1 
ATOM   2527 C CE1 . TYR A 1 373 ? 8.956  11.625 62.522  1.00 44.38  ? 310  TYR A CE1 1 
ATOM   2528 C CE2 . TYR A 1 373 ? 9.953  12.156 64.631  1.00 39.16  ? 310  TYR A CE2 1 
ATOM   2529 C CZ  . TYR A 1 373 ? 8.948  11.557 63.900  1.00 45.69  ? 310  TYR A CZ  1 
ATOM   2530 O OH  . TYR A 1 373 ? 7.925  10.888 64.534  1.00 52.59  ? 310  TYR A OH  1 
ATOM   2531 N N   . THR A 1 374 ? 15.255 13.600 60.871  1.00 30.66  ? 311  THR A N   1 
ATOM   2532 C CA  . THR A 1 374 ? 16.377 14.089 60.082  1.00 30.99  ? 311  THR A CA  1 
ATOM   2533 C C   . THR A 1 374 ? 16.907 12.997 59.164  1.00 37.56  ? 311  THR A C   1 
ATOM   2534 O O   . THR A 1 374 ? 17.144 13.233 57.974  1.00 29.31  ? 311  THR A O   1 
ATOM   2535 C CB  . THR A 1 374 ? 17.474 14.593 61.017  1.00 33.54  ? 311  THR A CB  1 
ATOM   2536 O OG1 . THR A 1 374 ? 16.981 15.710 61.765  1.00 36.68  ? 311  THR A OG1 1 
ATOM   2537 C CG2 . THR A 1 374 ? 18.719 15.006 60.244  1.00 37.94  ? 311  THR A CG2 1 
ATOM   2538 N N   . TYR A 1 375 ? 17.092 11.788 59.704  1.00 31.30  ? 312  TYR A N   1 
ATOM   2539 C CA  . TYR A 1 375 ? 17.538 10.668 58.885  1.00 32.47  ? 312  TYR A CA  1 
ATOM   2540 C C   . TYR A 1 375 ? 16.558 10.375 57.760  1.00 31.07  ? 312  TYR A C   1 
ATOM   2541 O O   . TYR A 1 375 ? 16.967 10.124 56.621  1.00 30.22  ? 312  TYR A O   1 
ATOM   2542 C CB  . TYR A 1 375 ? 17.705 9.417  59.742  1.00 35.34  ? 312  TYR A CB  1 
ATOM   2543 C CG  . TYR A 1 375 ? 18.924 9.409  60.619  1.00 32.69  ? 312  TYR A CG  1 
ATOM   2544 C CD1 . TYR A 1 375 ? 20.200 9.477  60.073  1.00 33.99  ? 312  TYR A CD1 1 
ATOM   2545 C CD2 . TYR A 1 375 ? 18.802 9.300  61.998  1.00 39.48  ? 312  TYR A CD2 1 
ATOM   2546 C CE1 . TYR A 1 375 ? 21.320 9.455  60.881  1.00 40.01  ? 312  TYR A CE1 1 
ATOM   2547 C CE2 . TYR A 1 375 ? 19.916 9.278  62.813  1.00 36.50  ? 312  TYR A CE2 1 
ATOM   2548 C CZ  . TYR A 1 375 ? 21.170 9.351  62.251  1.00 36.28  ? 312  TYR A CZ  1 
ATOM   2549 O OH  . TYR A 1 375 ? 22.278 9.328  63.059  1.00 39.94  ? 312  TYR A OH  1 
ATOM   2550 N N   . ALA A 1 376 ? 15.258 10.382 58.065  1.00 29.89  ? 313  ALA A N   1 
ATOM   2551 C CA  . ALA A 1 376 ? 14.271 9.967  57.080  1.00 28.81  ? 313  ALA A CA  1 
ATOM   2552 C C   . ALA A 1 376 ? 14.185 10.952 55.926  1.00 33.47  ? 313  ALA A C   1 
ATOM   2553 O O   . ALA A 1 376 ? 13.839 10.560 54.807  1.00 34.25  ? 313  ALA A O   1 
ATOM   2554 C CB  . ALA A 1 376 ? 12.901 9.804  57.738  1.00 38.58  ? 313  ALA A CB  1 
ATOM   2555 N N   . THR A 1 377 ? 14.483 12.225 56.174  1.00 31.85  ? 314  THR A N   1 
ATOM   2556 C CA  . THR A 1 377 ? 14.494 13.209 55.103  1.00 32.29  ? 314  THR A CA  1 
ATOM   2557 C C   . THR A 1 377 ? 15.869 13.349 54.469  1.00 34.66  ? 314  THR A C   1 
ATOM   2558 O O   . THR A 1 377 ? 15.966 13.736 53.297  1.00 34.76  ? 314  THR A O   1 
ATOM   2559 C CB  . THR A 1 377 ? 14.021 14.571 55.622  1.00 27.77  ? 314  THR A CB  1 
ATOM   2560 O OG1 . THR A 1 377 ? 14.856 15.001 56.703  1.00 30.14  ? 314  THR A OG1 1 
ATOM   2561 C CG2 . THR A 1 377 ? 12.584 14.491 56.093  1.00 29.74  ? 314  THR A CG2 1 
ATOM   2562 N N   . LEU A 1 378 ? 16.930 13.016 55.207  1.00 34.87  ? 315  LEU A N   1 
ATOM   2563 C CA  . LEU A 1 378 ? 18.276 13.101 54.656  1.00 26.86  ? 315  LEU A CA  1 
ATOM   2564 C C   . LEU A 1 378 ? 18.558 11.962 53.687  1.00 35.80  ? 315  LEU A C   1 
ATOM   2565 O O   . LEU A 1 378 ? 19.210 12.170 52.658  1.00 30.22  ? 315  LEU A O   1 
ATOM   2566 C CB  . LEU A 1 378 ? 19.307 13.092 55.781  1.00 37.20  ? 315  LEU A CB  1 
ATOM   2567 C CG  . LEU A 1 378 ? 20.769 12.954 55.350  1.00 43.87  ? 315  LEU A CG  1 
ATOM   2568 C CD1 . LEU A 1 378 ? 21.209 14.121 54.469  1.00 42.83  ? 315  LEU A CD1 1 
ATOM   2569 C CD2 . LEU A 1 378 ? 21.651 12.842 56.579  1.00 44.01  ? 315  LEU A CD2 1 
ATOM   2570 N N   . LEU A 1 379 ? 18.088 10.756 53.997  1.00 29.17  ? 316  LEU A N   1 
ATOM   2571 C CA  . LEU A 1 379 ? 18.432 9.607  53.163  1.00 34.46  ? 316  LEU A CA  1 
ATOM   2572 C C   . LEU A 1 379 ? 18.004 9.803  51.714  1.00 35.81  ? 316  LEU A C   1 
ATOM   2573 O O   . LEU A 1 379 ? 18.811 9.521  50.812  1.00 33.47  ? 316  LEU A O   1 
ATOM   2574 C CB  . LEU A 1 379 ? 17.830 8.332  53.762  1.00 37.61  ? 316  LEU A CB  1 
ATOM   2575 C CG  . LEU A 1 379 ? 18.231 7.040  53.050  1.00 61.81  ? 316  LEU A CG  1 
ATOM   2576 C CD1 . LEU A 1 379 ? 19.723 6.751  53.229  1.00 43.76  ? 316  LEU A CD1 1 
ATOM   2577 C CD2 . LEU A 1 379 ? 17.384 5.890  53.554  1.00 63.23  ? 316  LEU A CD2 1 
ATOM   2578 N N   . PRO A 1 380 ? 16.790 10.275 51.413  1.00 36.91  ? 317  PRO A N   1 
ATOM   2579 C CA  . PRO A 1 380 ? 16.439 10.508 50.001  1.00 39.11  ? 317  PRO A CA  1 
ATOM   2580 C C   . PRO A 1 380 ? 17.339 11.520 49.316  1.00 35.48  ? 317  PRO A C   1 
ATOM   2581 O O   . PRO A 1 380 ? 17.658 11.361 48.131  1.00 34.51  ? 317  PRO A O   1 
ATOM   2582 C CB  . PRO A 1 380 ? 14.988 11.004 50.080  1.00 43.58  ? 317  PRO A CB  1 
ATOM   2583 C CG  . PRO A 1 380 ? 14.478 10.480 51.379  1.00 43.39  ? 317  PRO A CG  1 
ATOM   2584 C CD  . PRO A 1 380 ? 15.647 10.516 52.310  1.00 40.91  ? 317  PRO A CD  1 
ATOM   2585 N N   . ALA A 1 381 ? 17.753 12.567 50.031  1.00 31.02  ? 318  ALA A N   1 
ATOM   2586 C CA  . ALA A 1 381 ? 18.662 13.543 49.444  1.00 32.97  ? 318  ALA A CA  1 
ATOM   2587 C C   . ALA A 1 381 ? 19.954 12.879 48.985  1.00 37.36  ? 318  ALA A C   1 
ATOM   2588 O O   . ALA A 1 381 ? 20.504 13.233 47.935  1.00 36.66  ? 318  ALA A O   1 
ATOM   2589 C CB  . ALA A 1 381 ? 18.952 14.656 50.449  1.00 33.30  ? 318  ALA A CB  1 
ATOM   2590 N N   . THR A 1 382 ? 20.451 11.904 49.751  1.00 34.10  ? 319  THR A N   1 
ATOM   2591 C CA  . THR A 1 382 ? 21.653 11.193 49.330  1.00 36.23  ? 319  THR A CA  1 
ATOM   2592 C C   . THR A 1 382 ? 21.378 10.300 48.127  1.00 34.09  ? 319  THR A C   1 
ATOM   2593 O O   . THR A 1 382 ? 22.264 10.106 47.286  1.00 39.46  ? 319  THR A O   1 
ATOM   2594 C CB  . THR A 1 382 ? 22.214 10.357 50.483  1.00 31.11  ? 319  THR A CB  1 
ATOM   2595 O OG1 . THR A 1 382 ? 21.388 9.205  50.698  1.00 30.82  ? 319  THR A OG1 1 
ATOM   2596 C CG2 . THR A 1 382 ? 22.268 11.177 51.746  1.00 28.73  ? 319  THR A CG2 1 
ATOM   2597 N N   . LEU A 1 383 ? 20.165 9.745  48.032  1.00 33.96  ? 320  LEU A N   1 
ATOM   2598 C CA  . LEU A 1 383 ? 19.832 8.887  46.900  1.00 39.53  ? 320  LEU A CA  1 
ATOM   2599 C C   . LEU A 1 383 ? 19.938 9.640  45.584  1.00 30.04  ? 320  LEU A C   1 
ATOM   2600 O O   . LEU A 1 383 ? 20.199 9.033  44.540  1.00 32.63  ? 320  LEU A O   1 
ATOM   2601 C CB  . LEU A 1 383 ? 18.422 8.319  47.065  1.00 39.71  ? 320  LEU A CB  1 
ATOM   2602 C CG  . LEU A 1 383 ? 18.186 7.413  48.276  1.00 60.60  ? 320  LEU A CG  1 
ATOM   2603 C CD1 . LEU A 1 383 ? 16.750 6.895  48.285  1.00 46.79  ? 320  LEU A CD1 1 
ATOM   2604 C CD2 . LEU A 1 383 ? 19.176 6.253  48.316  1.00 47.50  ? 320  LEU A CD2 1 
ATOM   2605 N N   . ASN A 1 384 ? 19.730 10.956 45.611  1.00 34.18  ? 321  ASN A N   1 
ATOM   2606 C CA  . ASN A 1 384 ? 19.858 11.738 44.392  1.00 32.97  ? 321  ASN A CA  1 
ATOM   2607 C C   . ASN A 1 384 ? 21.282 11.696 43.861  1.00 37.76  ? 321  ASN A C   1 
ATOM   2608 O O   . ASN A 1 384 ? 21.492 11.726 42.643  1.00 34.35  ? 321  ASN A O   1 
ATOM   2609 C CB  . ASN A 1 384 ? 19.420 13.179 44.648  1.00 33.88  ? 321  ASN A CB  1 
ATOM   2610 C CG  . ASN A 1 384 ? 19.260 13.974 43.366  1.00 38.37  ? 321  ASN A CG  1 
ATOM   2611 O OD1 . ASN A 1 384 ? 20.015 14.910 43.099  1.00 51.45  ? 321  ASN A OD1 1 
ATOM   2612 N ND2 . ASN A 1 384 ? 18.282 13.591 42.557  1.00 34.17  ? 321  ASN A ND2 1 
ATOM   2613 N N   . SER A 1 385 ? 22.273 11.619 44.753  1.00 28.44  ? 322  SER A N   1 
ATOM   2614 C CA  . SER A 1 385 ? 23.652 11.467 44.312  1.00 30.58  ? 322  SER A CA  1 
ATOM   2615 C C   . SER A 1 385 ? 23.911 10.100 43.689  1.00 31.64  ? 322  SER A C   1 
ATOM   2616 O O   . SER A 1 385 ? 24.924 9.934  43.005  1.00 32.99  ? 322  SER A O   1 
ATOM   2617 C CB  . SER A 1 385 ? 24.604 11.709 45.486  1.00 36.62  ? 322  SER A CB  1 
ATOM   2618 O OG  . SER A 1 385 ? 24.577 13.069 45.889  1.00 38.50  ? 322  SER A OG  1 
ATOM   2619 N N   . MET A 1 386 ? 23.028 9.118  43.911  1.00 34.07  ? 323  MET A N   1 
ATOM   2620 C CA  . MET A 1 386 ? 23.117 7.858  43.181  1.00 39.52  ? 323  MET A CA  1 
ATOM   2621 C C   . MET A 1 386 ? 22.500 7.953  41.800  1.00 34.91  ? 323  MET A C   1 
ATOM   2622 O O   . MET A 1 386 ? 22.866 7.181  40.910  1.00 39.21  ? 323  MET A O   1 
ATOM   2623 C CB  . MET A 1 386 ? 22.387 6.732  43.908  1.00 44.73  ? 323  MET A CB  1 
ATOM   2624 C CG  . MET A 1 386 ? 22.930 6.344  45.230  1.00 40.15  ? 323  MET A CG  1 
ATOM   2625 S SD  . MET A 1 386 ? 21.880 5.036  45.899  1.00 48.95  ? 323  MET A SD  1 
ATOM   2626 C CE  . MET A 1 386 ? 22.460 5.063  47.586  1.00 50.31  ? 323  MET A CE  1 
ATOM   2627 N N   . ILE A 1 387 ? 21.534 8.852  41.629  1.00 37.85  ? 324  ILE A N   1 
ATOM   2628 C CA  . ILE A 1 387 ? 20.829 8.995  40.363  1.00 33.55  ? 324  ILE A CA  1 
ATOM   2629 C C   . ILE A 1 387 ? 21.607 9.891  39.417  1.00 30.97  ? 324  ILE A C   1 
ATOM   2630 O O   . ILE A 1 387 ? 21.669 9.626  38.211  1.00 33.57  ? 324  ILE A O   1 
ATOM   2631 C CB  . ILE A 1 387 ? 19.418 9.553  40.629  1.00 38.48  ? 324  ILE A CB  1 
ATOM   2632 C CG1 . ILE A 1 387 ? 18.621 8.615  41.533  1.00 50.11  ? 324  ILE A CG1 1 
ATOM   2633 C CG2 . ILE A 1 387 ? 18.668 9.773  39.337  1.00 36.90  ? 324  ILE A CG2 1 
ATOM   2634 C CD1 . ILE A 1 387 ? 17.315 9.218  42.000  1.00 62.50  ? 324  ILE A CD1 1 
ATOM   2635 N N   . ASN A 1 388 ? 22.189 10.969 39.946  1.00 31.06  ? 325  ASN A N   1 
ATOM   2636 C CA  . ASN A 1 388 ? 22.955 11.915 39.138  1.00 36.77  ? 325  ASN A CA  1 
ATOM   2637 C C   . ASN A 1 388 ? 23.911 11.252 38.157  1.00 37.68  ? 325  ASN A C   1 
ATOM   2638 O O   . ASN A 1 388 ? 23.851 11.575 36.961  1.00 35.99  ? 325  ASN A O   1 
ATOM   2639 C CB  . ASN A 1 388 ? 23.737 12.856 40.066  1.00 33.92  ? 325  ASN A CB  1 
ATOM   2640 C CG  . ASN A 1 388 ? 22.861 13.909 40.704  1.00 34.91  ? 325  ASN A CG  1 
ATOM   2641 O OD1 . ASN A 1 388 ? 21.763 14.182 40.229  1.00 35.50  ? 325  ASN A OD1 1 
ATOM   2642 N ND2 . ASN A 1 388 ? 23.351 14.518 41.776  1.00 35.38  ? 325  ASN A ND2 1 
ATOM   2643 N N   . PRO A 1 389 ? 24.800 10.345 38.568  1.00 30.80  ? 326  PRO A N   1 
ATOM   2644 C CA  . PRO A 1 389 ? 25.739 9.769  37.591  1.00 36.29  ? 326  PRO A CA  1 
ATOM   2645 C C   . PRO A 1 389 ? 25.050 8.996  36.485  1.00 31.37  ? 326  PRO A C   1 
ATOM   2646 O O   . PRO A 1 389 ? 25.568 8.937  35.363  1.00 35.80  ? 326  PRO A O   1 
ATOM   2647 C CB  . PRO A 1 389 ? 26.633 8.863  38.451  1.00 32.63  ? 326  PRO A CB  1 
ATOM   2648 C CG  . PRO A 1 389 ? 25.862 8.611  39.699  1.00 37.75  ? 326  PRO A CG  1 
ATOM   2649 C CD  . PRO A 1 389 ? 25.029 9.829  39.929  1.00 29.86  ? 326  PRO A CD  1 
ATOM   2650 N N   . ILE A 1 390 ? 23.889 8.405  36.759  1.00 32.57  ? 327  ILE A N   1 
ATOM   2651 C CA  . ILE A 1 390 ? 23.178 7.672  35.718  1.00 32.37  ? 327  ILE A CA  1 
ATOM   2652 C C   . ILE A 1 390 ? 22.590 8.640  34.701  1.00 32.62  ? 327  ILE A C   1 
ATOM   2653 O O   . ILE A 1 390 ? 22.697 8.432  33.488  1.00 34.47  ? 327  ILE A O   1 
ATOM   2654 C CB  . ILE A 1 390 ? 22.097 6.776  36.350  1.00 35.63  ? 327  ILE A CB  1 
ATOM   2655 C CG1 . ILE A 1 390 ? 22.753 5.733  37.256  1.00 42.93  ? 327  ILE A CG1 1 
ATOM   2656 C CG2 . ILE A 1 390 ? 21.255 6.100  35.270  1.00 43.32  ? 327  ILE A CG2 1 
ATOM   2657 C CD1 . ILE A 1 390 ? 21.795 5.037  38.188  1.00 46.25  ? 327  ILE A CD1 1 
ATOM   2658 N N   . ILE A 1 391 ? 21.993 9.730  35.179  1.00 34.48  ? 328  ILE A N   1 
ATOM   2659 C CA  A ILE A 1 391 ? 21.336 10.672 34.280  0.50 38.69  ? 328  ILE A CA  1 
ATOM   2660 C CA  B ILE A 1 391 ? 21.337 10.675 34.281  0.50 38.69  ? 328  ILE A CA  1 
ATOM   2661 C C   . ILE A 1 391 ? 22.365 11.455 33.474  1.00 32.41  ? 328  ILE A C   1 
ATOM   2662 O O   . ILE A 1 391 ? 22.238 11.603 32.254  1.00 32.89  ? 328  ILE A O   1 
ATOM   2663 C CB  A ILE A 1 391 ? 20.415 11.613 35.078  0.50 42.29  ? 328  ILE A CB  1 
ATOM   2664 C CB  B ILE A 1 391 ? 20.430 11.625 35.081  0.50 42.28  ? 328  ILE A CB  1 
ATOM   2665 C CG1 A ILE A 1 391 ? 19.282 10.818 35.735  0.50 34.77  ? 328  ILE A CG1 1 
ATOM   2666 C CG1 B ILE A 1 391 ? 19.258 10.852 35.676  0.50 34.72  ? 328  ILE A CG1 1 
ATOM   2667 C CG2 A ILE A 1 391 ? 19.869 12.717 34.179  0.50 43.55  ? 328  ILE A CG2 1 
ATOM   2668 C CG2 B ILE A 1 391 ? 19.949 12.770 34.194  0.50 43.48  ? 328  ILE A CG2 1 
ATOM   2669 C CD1 A ILE A 1 391 ? 18.407 10.057 34.758  0.50 39.85  ? 328  ILE A CD1 1 
ATOM   2670 C CD1 B ILE A 1 391 ? 18.601 11.578 36.802  0.50 45.54  ? 328  ILE A CD1 1 
ATOM   2671 N N   . TYR A 1 392 ? 23.392 11.976 34.141  1.00 37.70  ? 329  TYR A N   1 
ATOM   2672 C CA  . TYR A 1 392 ? 24.292 12.914 33.489  1.00 34.73  ? 329  TYR A CA  1 
ATOM   2673 C C   . TYR A 1 392 ? 25.563 12.286 32.942  1.00 33.57  ? 329  TYR A C   1 
ATOM   2674 O O   . TYR A 1 392 ? 26.221 12.913 32.108  1.00 38.78  ? 329  TYR A O   1 
ATOM   2675 C CB  . TYR A 1 392 ? 24.643 14.046 34.461  1.00 31.52  ? 329  TYR A CB  1 
ATOM   2676 C CG  . TYR A 1 392 ? 23.436 14.901 34.781  1.00 31.02  ? 329  TYR A CG  1 
ATOM   2677 C CD1 . TYR A 1 392 ? 22.949 15.810 33.857  1.00 40.32  ? 329  TYR A CD1 1 
ATOM   2678 C CD2 . TYR A 1 392 ? 22.766 14.775 35.987  1.00 30.72  ? 329  TYR A CD2 1 
ATOM   2679 C CE1 . TYR A 1 392 ? 21.839 16.585 34.128  1.00 36.59  ? 329  TYR A CE1 1 
ATOM   2680 C CE2 . TYR A 1 392 ? 21.652 15.546 36.268  1.00 35.65  ? 329  TYR A CE2 1 
ATOM   2681 C CZ  . TYR A 1 392 ? 21.195 16.452 35.333  1.00 37.94  ? 329  TYR A CZ  1 
ATOM   2682 O OH  . TYR A 1 392 ? 20.087 17.225 35.600  1.00 39.42  ? 329  TYR A OH  1 
ATOM   2683 N N   . ALA A 1 393 ? 25.919 11.070 33.353  1.00 33.72  ? 330  ALA A N   1 
ATOM   2684 C CA  . ALA A 1 393 ? 27.145 10.443 32.867  1.00 33.86  ? 330  ALA A CA  1 
ATOM   2685 C C   . ALA A 1 393 ? 26.882 9.143  32.117  1.00 38.79  ? 330  ALA A C   1 
ATOM   2686 O O   . ALA A 1 393 ? 27.205 9.051  30.927  1.00 38.60  ? 330  ALA A O   1 
ATOM   2687 C CB  . ALA A 1 393 ? 28.109 10.210 34.040  1.00 38.28  ? 330  ALA A CB  1 
ATOM   2688 N N   . PHE A 1 394 ? 26.307 8.130  32.766  1.00 36.57  ? 331  PHE A N   1 
ATOM   2689 C CA  . PHE A 1 394 ? 26.244 6.806  32.151  1.00 35.21  ? 331  PHE A CA  1 
ATOM   2690 C C   . PHE A 1 394 ? 25.276 6.736  30.975  1.00 43.50  ? 331  PHE A C   1 
ATOM   2691 O O   . PHE A 1 394 ? 25.405 5.829  30.145  1.00 39.56  ? 331  PHE A O   1 
ATOM   2692 C CB  . PHE A 1 394 ? 25.872 5.764  33.206  1.00 37.84  ? 331  PHE A CB  1 
ATOM   2693 C CG  . PHE A 1 394 ? 26.936 5.555  34.251  1.00 39.09  ? 331  PHE A CG  1 
ATOM   2694 C CD1 . PHE A 1 394 ? 28.241 5.273  33.884  1.00 47.22  ? 331  PHE A CD1 1 
ATOM   2695 C CD2 . PHE A 1 394 ? 26.631 5.651  35.598  1.00 43.70  ? 331  PHE A CD2 1 
ATOM   2696 C CE1 . PHE A 1 394 ? 29.218 5.084  34.840  1.00 46.78  ? 331  PHE A CE1 1 
ATOM   2697 C CE2 . PHE A 1 394 ? 27.608 5.464  36.561  1.00 49.01  ? 331  PHE A CE2 1 
ATOM   2698 C CZ  . PHE A 1 394 ? 28.902 5.181  36.181  1.00 39.61  ? 331  PHE A CZ  1 
ATOM   2699 N N   . ARG A 1 395 ? 24.322 7.662  30.871  1.00 37.16  ? 332  ARG A N   1 
ATOM   2700 C CA  . ARG A 1 395 ? 23.442 7.694  29.707  1.00 47.05  ? 332  ARG A CA  1 
ATOM   2701 C C   . ARG A 1 395 ? 24.073 8.399  28.515  1.00 44.49  ? 332  ARG A C   1 
ATOM   2702 O O   . ARG A 1 395 ? 23.487 8.390  27.429  1.00 48.38  ? 332  ARG A O   1 
ATOM   2703 C CB  . ARG A 1 395 ? 22.113 8.368  30.064  1.00 47.80  ? 332  ARG A CB  1 
ATOM   2704 C CG  . ARG A 1 395 ? 21.174 7.451  30.842  1.00 60.11  ? 332  ARG A CG  1 
ATOM   2705 C CD  . ARG A 1 395 ? 19.898 8.146  31.293  1.00 49.51  ? 332  ARG A CD  1 
ATOM   2706 N NE  . ARG A 1 395 ? 19.225 8.845  30.204  1.00 66.73  ? 332  ARG A NE  1 
ATOM   2707 C CZ  . ARG A 1 395 ? 19.250 10.159 30.012  1.00 79.21  ? 332  ARG A CZ  1 
ATOM   2708 N NH1 . ARG A 1 395 ? 19.886 10.972 30.842  1.00 57.43  ? 332  ARG A NH1 1 
ATOM   2709 N NH2 . ARG A 1 395 ? 18.616 10.673 28.962  1.00 73.43  ? 332  ARG A NH2 1 
ATOM   2710 N N   . ASN A 1 396 ? 25.249 8.993  28.689  1.00 48.70  ? 333  ASN A N   1 
ATOM   2711 C CA  . ASN A 1 396 ? 25.944 9.656  27.595  1.00 41.82  ? 333  ASN A CA  1 
ATOM   2712 C C   . ASN A 1 396 ? 26.728 8.631  26.780  1.00 46.99  ? 333  ASN A C   1 
ATOM   2713 O O   . ASN A 1 396 ? 27.470 7.818  27.340  1.00 39.14  ? 333  ASN A O   1 
ATOM   2714 C CB  . ASN A 1 396 ? 26.872 10.733 28.155  1.00 45.06  ? 333  ASN A CB  1 
ATOM   2715 C CG  . ASN A 1 396 ? 27.594 11.505 27.074  1.00 46.44  ? 333  ASN A CG  1 
ATOM   2716 O OD1 . ASN A 1 396 ? 28.659 11.099 26.611  1.00 52.21  ? 333  ASN A OD1 1 
ATOM   2717 N ND2 . ASN A 1 396 ? 27.025 12.635 26.676  1.00 60.54  ? 333  ASN A ND2 1 
ATOM   2718 N N   . GLN A 1 397 ? 26.563 8.673  25.454  1.00 46.06  ? 334  GLN A N   1 
ATOM   2719 C CA  . GLN A 1 397 ? 27.172 7.655  24.601  1.00 50.97  ? 334  GLN A CA  1 
ATOM   2720 C C   . GLN A 1 397 ? 28.694 7.686  24.675  1.00 40.27  ? 334  GLN A C   1 
ATOM   2721 O O   . GLN A 1 397 ? 29.341 6.637  24.582  1.00 42.84  ? 334  GLN A O   1 
ATOM   2722 C CB  . GLN A 1 397 ? 26.714 7.834  23.149  1.00 57.43  ? 334  GLN A CB  1 
ATOM   2723 C CG  . GLN A 1 397 ? 27.222 9.111  22.474  1.00 87.30  ? 334  GLN A CG  1 
ATOM   2724 C CD  . GLN A 1 397 ? 27.036 9.102  20.967  1.00 101.60 ? 334  GLN A CD  1 
ATOM   2725 O OE1 . GLN A 1 397 ? 26.294 8.282  20.423  1.00 88.16  ? 334  GLN A OE1 1 
ATOM   2726 N NE2 . GLN A 1 397 ? 27.724 10.012 20.284  1.00 94.30  ? 334  GLN A NE2 1 
ATOM   2727 N N   . GLU A 1 398 ? 29.285 8.873  24.829  1.00 42.30  ? 335  GLU A N   1 
ATOM   2728 C CA  . GLU A 1 398 ? 30.740 8.963  24.893  1.00 49.50  ? 335  GLU A CA  1 
ATOM   2729 C C   . GLU A 1 398 ? 31.271 8.384  26.200  1.00 40.59  ? 335  GLU A C   1 
ATOM   2730 O O   . GLU A 1 398 ? 32.350 7.779  26.225  1.00 43.82  ? 335  GLU A O   1 
ATOM   2731 C CB  . GLU A 1 398 ? 31.177 10.419 24.721  1.00 47.26  ? 335  GLU A CB  1 
ATOM   2732 C CG  . GLU A 1 398 ? 31.539 10.795 23.289  1.00 74.28  ? 335  GLU A CG  1 
ATOM   2733 C CD  . GLU A 1 398 ? 31.713 12.291 23.100  1.00 84.56  ? 335  GLU A CD  1 
ATOM   2734 O OE1 . GLU A 1 398 ? 30.724 13.035 23.279  1.00 80.59  ? 335  GLU A OE1 1 
ATOM   2735 O OE2 . GLU A 1 398 ? 32.842 12.724 22.778  1.00 80.97  ? 335  GLU A OE2 1 
ATOM   2736 N N   . ILE A 1 399 ? 30.528 8.556  27.295  1.00 38.29  ? 336  ILE A N   1 
ATOM   2737 C CA  . ILE A 1 399 ? 30.907 7.926  28.557  1.00 38.62  ? 336  ILE A CA  1 
ATOM   2738 C C   . ILE A 1 399 ? 30.828 6.409  28.434  1.00 36.63  ? 336  ILE A C   1 
ATOM   2739 O O   . ILE A 1 399 ? 31.715 5.684  28.899  1.00 37.21  ? 336  ILE A O   1 
ATOM   2740 C CB  . ILE A 1 399 ? 30.015 8.443  29.700  1.00 39.78  ? 336  ILE A CB  1 
ATOM   2741 C CG1 . ILE A 1 399 ? 30.294 9.922  29.983  1.00 45.83  ? 336  ILE A CG1 1 
ATOM   2742 C CG2 . ILE A 1 399 ? 30.229 7.608  30.958  1.00 37.71  ? 336  ILE A CG2 1 
ATOM   2743 C CD1 . ILE A 1 399 ? 31.586 10.173 30.723  1.00 54.37  ? 336  ILE A CD1 1 
ATOM   2744 N N   . GLN A 1 400 ? 29.759 5.907  27.812  1.00 37.92  ? 337  GLN A N   1 
ATOM   2745 C CA  . GLN A 1 400 ? 29.631 4.470  27.594  1.00 49.20  ? 337  GLN A CA  1 
ATOM   2746 C C   . GLN A 1 400 ? 30.799 3.925  26.785  1.00 40.95  ? 337  GLN A C   1 
ATOM   2747 O O   . GLN A 1 400 ? 31.320 2.847  27.090  1.00 37.96  ? 337  GLN A O   1 
ATOM   2748 C CB  . GLN A 1 400 ? 28.307 4.170  26.894  1.00 41.49  ? 337  GLN A CB  1 
ATOM   2749 C CG  . GLN A 1 400 ? 27.091 4.594  27.706  1.00 44.64  ? 337  GLN A CG  1 
ATOM   2750 C CD  . GLN A 1 400 ? 25.798 4.512  26.918  1.00 42.63  ? 337  GLN A CD  1 
ATOM   2751 O OE1 . GLN A 1 400 ? 25.800 4.219  25.722  1.00 48.59  ? 337  GLN A OE1 1 
ATOM   2752 N NE2 . GLN A 1 400 ? 24.683 4.773  27.590  1.00 43.64  ? 337  GLN A NE2 1 
ATOM   2753 N N   . ARG A 1 401 ? 31.227 4.654  25.750  1.00 45.58  ? 338  ARG A N   1 
ATOM   2754 C CA  A ARG A 1 401 ? 32.361 4.209  24.947  0.50 44.41  ? 338  ARG A CA  1 
ATOM   2755 C CA  B ARG A 1 401 ? 32.362 4.199  24.952  0.50 44.41  ? 338  ARG A CA  1 
ATOM   2756 C C   . ARG A 1 401 ? 33.619 4.101  25.801  1.00 43.51  ? 338  ARG A C   1 
ATOM   2757 O O   . ARG A 1 401 ? 34.343 3.101  25.744  1.00 42.50  ? 338  ARG A O   1 
ATOM   2758 C CB  A ARG A 1 401 ? 32.572 5.177  23.781  0.50 48.07  ? 338  ARG A CB  1 
ATOM   2759 C CB  B ARG A 1 401 ? 32.599 5.135  23.769  0.50 48.07  ? 338  ARG A CB  1 
ATOM   2760 C CG  A ARG A 1 401 ? 33.745 4.844  22.875  0.50 52.10  ? 338  ARG A CG  1 
ATOM   2761 C CG  B ARG A 1 401 ? 31.438 5.195  22.822  0.50 55.89  ? 338  ARG A CG  1 
ATOM   2762 C CD  A ARG A 1 401 ? 34.099 6.027  21.988  0.50 58.77  ? 338  ARG A CD  1 
ATOM   2763 C CD  B ARG A 1 401 ? 31.863 5.431  21.392  0.50 62.94  ? 338  ARG A CD  1 
ATOM   2764 N NE  A ARG A 1 401 ? 35.463 5.935  21.484  0.50 62.02  ? 338  ARG A NE  1 
ATOM   2765 N NE  B ARG A 1 401 ? 30.679 5.574  20.557  0.50 63.31  ? 338  ARG A NE  1 
ATOM   2766 C CZ  A ARG A 1 401 ? 36.546 6.174  22.212  0.50 61.49  ? 338  ARG A CZ  1 
ATOM   2767 C CZ  B ARG A 1 401 ? 29.904 6.649  20.546  0.50 68.00  ? 338  ARG A CZ  1 
ATOM   2768 N NH1 A ARG A 1 401 ? 36.461 6.503  23.492  0.50 60.24  ? 338  ARG A NH1 1 
ATOM   2769 N NH1 B ARG A 1 401 ? 30.201 7.723  21.261  0.50 61.66  ? 338  ARG A NH1 1 
ATOM   2770 N NH2 A ARG A 1 401 ? 37.744 6.076  21.644  0.50 63.63  ? 338  ARG A NH2 1 
ATOM   2771 N NH2 B ARG A 1 401 ? 28.799 6.643  19.807  0.50 83.97  ? 338  ARG A NH2 1 
ATOM   2772 N N   . ALA A 1 402 ? 33.897 5.133  26.597  1.00 36.82  ? 339  ALA A N   1 
ATOM   2773 C CA  . ALA A 1 402 ? 35.041 5.071  27.497  1.00 38.41  ? 339  ALA A CA  1 
ATOM   2774 C C   . ALA A 1 402 ? 34.933 3.873  28.433  1.00 35.85  ? 339  ALA A C   1 
ATOM   2775 O O   . ALA A 1 402 ? 35.930 3.192  28.697  1.00 38.94  ? 339  ALA A O   1 
ATOM   2776 C CB  . ALA A 1 402 ? 35.150 6.370  28.292  1.00 40.25  ? 339  ALA A CB  1 
ATOM   2777 N N   . LEU A 1 403 ? 33.727 3.591  28.935  1.00 44.35  ? 340  LEU A N   1 
ATOM   2778 C CA  . LEU A 1 403 ? 33.542 2.421  29.790  1.00 41.33  ? 340  LEU A CA  1 
ATOM   2779 C C   . LEU A 1 403 ? 33.848 1.133  29.033  1.00 37.93  ? 340  LEU A C   1 
ATOM   2780 O O   . LEU A 1 403 ? 34.467 0.214  29.581  1.00 41.67  ? 340  LEU A O   1 
ATOM   2781 C CB  . LEU A 1 403 ? 32.118 2.398  30.348  1.00 37.53  ? 340  LEU A CB  1 
ATOM   2782 C CG  . LEU A 1 403 ? 31.785 1.258  31.317  1.00 45.55  ? 340  LEU A CG  1 
ATOM   2783 C CD1 . LEU A 1 403 ? 32.762 1.213  32.485  1.00 37.82  ? 340  LEU A CD1 1 
ATOM   2784 C CD2 . LEU A 1 403 ? 30.364 1.401  31.833  1.00 47.85  ? 340  LEU A CD2 1 
ATOM   2785 N N   . TRP A 1 404 ? 33.424 1.046  27.770  1.00 45.65  ? 341  TRP A N   1 
ATOM   2786 C CA  A TRP A 1 404 ? 33.728 -0.147 26.989  0.50 49.74  ? 341  TRP A CA  1 
ATOM   2787 C CA  B TRP A 1 404 ? 33.727 -0.127 26.950  0.50 49.73  ? 341  TRP A CA  1 
ATOM   2788 C C   . TRP A 1 404 ? 35.231 -0.309 26.789  1.00 56.74  ? 341  TRP A C   1 
ATOM   2789 O O   . TRP A 1 404 ? 35.754 -1.425 26.901  1.00 55.32  ? 341  TRP A O   1 
ATOM   2790 C CB  A TRP A 1 404 ? 33.001 -0.097 25.648  0.50 49.92  ? 341  TRP A CB  1 
ATOM   2791 C CB  B TRP A 1 404 ? 33.049 0.021  25.583  0.50 49.94  ? 341  TRP A CB  1 
ATOM   2792 C CG  A TRP A 1 404 ? 31.499 0.021  25.765  0.50 52.24  ? 341  TRP A CG  1 
ATOM   2793 C CG  B TRP A 1 404 ? 33.527 -0.936 24.521  0.50 56.05  ? 341  TRP A CG  1 
ATOM   2794 C CD1 A TRP A 1 404 ? 30.658 0.549  24.837  0.50 57.36  ? 341  TRP A CD1 1 
ATOM   2795 C CD1 B TRP A 1 404 ? 33.256 -2.270 24.437  0.50 62.38  ? 341  TRP A CD1 1 
ATOM   2796 C CD2 A TRP A 1 404 ? 30.668 -0.391 26.868  0.50 52.86  ? 341  TRP A CD2 1 
ATOM   2797 C CD2 B TRP A 1 404 ? 34.338 -0.620 23.379  0.50 57.56  ? 341  TRP A CD2 1 
ATOM   2798 N NE1 A TRP A 1 404 ? 29.359 0.492  25.281  0.50 51.43  ? 341  TRP A NE1 1 
ATOM   2799 N NE1 B TRP A 1 404 ? 33.853 -2.807 23.323  0.50 55.50  ? 341  TRP A NE1 1 
ATOM   2800 C CE2 A TRP A 1 404 ? 29.338 -0.081 26.525  0.50 53.46  ? 341  TRP A CE2 1 
ATOM   2801 C CE2 B TRP A 1 404 ? 34.523 -1.815 22.656  0.50 46.80  ? 341  TRP A CE2 1 
ATOM   2802 C CE3 A TRP A 1 404 ? 30.919 -0.992 28.106  0.50 45.37  ? 341  TRP A CE3 1 
ATOM   2803 C CE3 B TRP A 1 404 ? 34.927 0.555  22.902  0.50 57.95  ? 341  TRP A CE3 1 
ATOM   2804 C CZ2 A TRP A 1 404 ? 28.266 -0.350 27.376  0.50 53.82  ? 341  TRP A CZ2 1 
ATOM   2805 C CZ2 B TRP A 1 404 ? 35.274 -1.871 21.483  0.50 65.55  ? 341  TRP A CZ2 1 
ATOM   2806 C CZ3 A TRP A 1 404 ? 29.857 -1.256 28.945  0.50 48.07  ? 341  TRP A CZ3 1 
ATOM   2807 C CZ3 B TRP A 1 404 ? 35.673 0.497  21.735  0.50 66.41  ? 341  TRP A CZ3 1 
ATOM   2808 C CH2 A TRP A 1 404 ? 28.547 -0.937 28.578  0.50 43.95  ? 341  TRP A CH2 1 
ATOM   2809 C CH2 B TRP A 1 404 ? 35.840 -0.707 21.040  0.50 53.87  ? 341  TRP A CH2 1 
ATOM   2810 N N   . LEU A 1 405 ? 35.944 0.783  26.511  1.00 46.13  ? 342  LEU A N   1 
ATOM   2811 C CA  . LEU A 1 405 ? 37.393 0.688  26.377  1.00 52.00  ? 342  LEU A CA  1 
ATOM   2812 C C   . LEU A 1 405 ? 38.052 0.323  27.699  1.00 55.79  ? 342  LEU A C   1 
ATOM   2813 O O   . LEU A 1 405 ? 39.107 -0.320 27.709  1.00 62.01  ? 342  LEU A O   1 
ATOM   2814 C CB  . LEU A 1 405 ? 37.964 2.006  25.858  1.00 48.37  ? 342  LEU A CB  1 
ATOM   2815 C CG  . LEU A 1 405 ? 37.649 2.346  24.404  1.00 63.72  ? 342  LEU A CG  1 
ATOM   2816 C CD1 . LEU A 1 405 ? 38.135 3.749  24.089  1.00 60.37  ? 342  LEU A CD1 1 
ATOM   2817 C CD2 . LEU A 1 405 ? 38.280 1.328  23.463  1.00 58.75  ? 342  LEU A CD2 1 
ATOM   2818 N N   . LEU A 1 406 ? 37.450 0.723  28.819  1.00 51.56  ? 343  LEU A N   1 
ATOM   2819 C CA  . LEU A 1 406 ? 38.029 0.408  30.120  1.00 50.77  ? 343  LEU A CA  1 
ATOM   2820 C C   . LEU A 1 406 ? 37.862 -1.069 30.452  1.00 58.13  ? 343  LEU A C   1 
ATOM   2821 O O   . LEU A 1 406 ? 38.804 -1.720 30.918  1.00 59.79  ? 343  LEU A O   1 
ATOM   2822 C CB  . LEU A 1 406 ? 37.387 1.274  31.200  1.00 53.28  ? 343  LEU A CB  1 
ATOM   2823 C CG  . LEU A 1 406 ? 37.716 0.879  32.639  1.00 58.21  ? 343  LEU A CG  1 
ATOM   2824 C CD1 . LEU A 1 406 ? 39.218 0.892  32.864  1.00 65.67  ? 343  LEU A CD1 1 
ATOM   2825 C CD2 . LEU A 1 406 ? 37.012 1.809  33.605  1.00 49.64  ? 343  LEU A CD2 1 
ATOM   2826 N N   . LEU A 1 407 ? 36.665 -1.613 30.229  1.00 54.30  ? 344  LEU A N   1 
ATOM   2827 C CA  . LEU A 1 407 ? 36.431 -3.020 30.535  1.00 69.06  ? 344  LEU A CA  1 
ATOM   2828 C C   . LEU A 1 407 ? 37.267 -3.926 29.640  1.00 69.45  ? 344  LEU A C   1 
ATOM   2829 O O   . LEU A 1 407 ? 37.786 -4.951 30.096  1.00 81.21  ? 344  LEU A O   1 
ATOM   2830 C CB  . LEU A 1 407 ? 34.942 -3.339 30.394  1.00 58.07  ? 344  LEU A CB  1 
ATOM   2831 C CG  . LEU A 1 407 ? 34.028 -2.587 31.368  1.00 53.96  ? 344  LEU A CG  1 
ATOM   2832 C CD1 . LEU A 1 407 ? 32.559 -2.756 31.008  1.00 51.00  ? 344  LEU A CD1 1 
ATOM   2833 C CD2 . LEU A 1 407 ? 34.275 -3.038 32.803  1.00 64.55  ? 344  LEU A CD2 1 
ATOM   2834 N N   . ASP A 1 408 ? 37.422 -3.560 28.370  1.00 67.43  ? 345  ASP A N   1 
ATOM   2835 C CA  . ASP A 1 408 ? 38.146 -4.378 27.408  1.00 76.65  ? 345  ASP A CA  1 
ATOM   2836 C C   . ASP A 1 408 ? 39.657 -4.165 27.459  1.00 89.69  ? 345  ASP A C   1 
ATOM   2837 O O   . ASP A 1 408 ? 40.338 -4.415 26.457  1.00 113.28 ? 345  ASP A O   1 
ATOM   2838 C CB  . ASP A 1 408 ? 37.630 -4.098 25.994  1.00 79.72  ? 345  ASP A CB  1 
ATOM   2839 C CG  . ASP A 1 408 ? 36.138 -4.346 25.857  1.00 87.12  ? 345  ASP A CG  1 
ATOM   2840 O OD1 . ASP A 1 408 ? 35.506 -4.751 26.857  1.00 69.92  ? 345  ASP A OD1 1 
ATOM   2841 O OD2 . ASP A 1 408 ? 35.598 -4.137 24.749  1.00 89.22  ? 345  ASP A OD2 1 
ATOM   2842 N N   . GLY A 1 409 ? 40.191 -3.720 28.592  1.00 82.56  ? 346  GLY A N   1 
ATOM   2843 C CA  . GLY A 1 409 ? 41.631 -3.507 28.697  1.00 77.04  ? 346  GLY A CA  1 
ATOM   2844 C C   . GLY A 1 409 ? 42.192 -2.611 27.617  1.00 102.02 ? 346  GLY A C   1 
ATOM   2845 O O   . GLY A 1 409 ? 43.322 -2.821 27.157  1.00 117.45 ? 346  GLY A O   1 
ATOM   2846 N N   . CYS A 1 410 ? 41.424 -1.609 27.198  1.00 92.64  ? 347  CYS A N   1 
ATOM   2847 C CA  . CYS A 1 410 ? 41.851 -0.690 26.148  1.00 108.62 ? 347  CYS A CA  1 
ATOM   2848 C C   . CYS A 1 410 ? 42.063 -1.439 24.836  1.00 109.45 ? 347  CYS A C   1 
ATOM   2849 O O   . CYS A 1 410 ? 41.146 -2.081 24.322  1.00 97.67  ? 347  CYS A O   1 
ATOM   2850 C CB  . CYS A 1 410 ? 43.136 0.038  26.552  1.00 112.77 ? 347  CYS A CB  1 
ATOM   2851 S SG  . CYS A 1 410 ? 43.094 0.750  28.214  1.00 113.06 ? 347  CYS A SG  1 
HETATM 2852 C C9  . OLC B 2 .   ? 33.546 35.030 39.041  1.00 57.38  ? 1201 OLC A C9  1 
HETATM 2853 C C8  . OLC B 2 .   ? 32.125 34.667 38.782  1.00 62.49  ? 1201 OLC A C8  1 
HETATM 2854 C C24 . OLC B 2 .   ? 28.015 27.564 29.976  1.00 57.19  ? 1201 OLC A C24 1 
HETATM 2855 C C7  . OLC B 2 .   ? 32.030 33.810 37.529  1.00 61.54  ? 1201 OLC A C7  1 
HETATM 2856 C C6  . OLC B 2 .   ? 30.594 33.779 37.023  1.00 56.56  ? 1201 OLC A C6  1 
HETATM 2857 C C5  . OLC B 2 .   ? 30.531 32.965 35.736  1.00 59.49  ? 1201 OLC A C5  1 
HETATM 2858 C C4  . OLC B 2 .   ? 29.321 33.368 34.908  1.00 66.62  ? 1201 OLC A C4  1 
HETATM 2859 C C3  . OLC B 2 .   ? 29.370 32.624 33.583  1.00 63.71  ? 1201 OLC A C3  1 
HETATM 2860 C C2  . OLC B 2 .   ? 28.679 31.263 33.684  1.00 66.68  ? 1201 OLC A C2  1 
HETATM 2861 C C21 . OLC B 2 .   ? 29.232 28.730 31.888  1.00 53.51  ? 1201 OLC A C21 1 
HETATM 2862 C C1  . OLC B 2 .   ? 28.354 30.870 32.285  1.00 58.88  ? 1201 OLC A C1  1 
HETATM 2863 C C22 . OLC B 2 .   ? 29.267 28.418 30.348  1.00 49.72  ? 1201 OLC A C22 1 
HETATM 2864 O O19 . OLC B 2 .   ? 28.304 31.617 31.318  1.00 95.00  ? 1201 OLC A O19 1 
HETATM 2865 O O25 . OLC B 2 .   ? 28.491 26.257 29.844  1.00 43.27  ? 1201 OLC A O25 1 
HETATM 2866 O O23 . OLC B 2 .   ? 29.341 29.576 29.592  1.00 54.09  ? 1201 OLC A O23 1 
HETATM 2867 O O20 . OLC B 2 .   ? 28.089 29.543 32.100  1.00 63.51  ? 1201 OLC A O20 1 
HETATM 2868 C C18 . OLC C 2 .   ? 25.733 31.766 50.035  1.00 50.21  ? 1202 OLC A C18 1 
HETATM 2869 C C10 . OLC C 2 .   ? 23.450 32.449 42.258  1.00 84.43  ? 1202 OLC A C10 1 
HETATM 2870 C C9  . OLC C 2 .   ? 24.172 32.362 41.128  1.00 78.50  ? 1202 OLC A C9  1 
HETATM 2871 C C17 . OLC C 2 .   ? 25.549 31.981 48.547  1.00 60.39  ? 1202 OLC A C17 1 
HETATM 2872 C C11 . OLC C 2 .   ? 22.333 31.516 42.603  1.00 89.32  ? 1202 OLC A C11 1 
HETATM 2873 C C8  . OLC C 2 .   ? 23.956 31.321 40.073  1.00 82.55  ? 1202 OLC A C8  1 
HETATM 2874 C C24 . OLC C 2 .   ? 24.943 34.134 28.896  1.00 106.08 ? 1202 OLC A C24 1 
HETATM 2875 C C16 . OLC C 2 .   ? 24.242 31.353 48.098  1.00 81.65  ? 1202 OLC A C16 1 
HETATM 2876 C C12 . OLC C 2 .   ? 22.575 30.904 43.968  1.00 82.28  ? 1202 OLC A C12 1 
HETATM 2877 C C7  . OLC C 2 .   ? 24.013 31.966 38.696  1.00 66.30  ? 1202 OLC A C7  1 
HETATM 2878 C C15 . OLC C 2 .   ? 23.908 31.718 46.661  1.00 73.24  ? 1202 OLC A C15 1 
HETATM 2879 C C13 . OLC C 2 .   ? 22.026 31.837 45.031  1.00 63.52  ? 1202 OLC A C13 1 
HETATM 2880 C C6  . OLC C 2 .   ? 23.950 30.884 37.629  1.00 70.94  ? 1202 OLC A C6  1 
HETATM 2881 C C14 . OLC C 2 .   ? 22.454 31.346 46.397  1.00 77.44  ? 1202 OLC A C14 1 
HETATM 2882 C C5  . OLC C 2 .   ? 23.744 31.518 36.262  1.00 70.82  ? 1202 OLC A C5  1 
HETATM 2883 C C4  . OLC C 2 .   ? 22.321 32.047 36.130  1.00 80.14  ? 1202 OLC A C4  1 
HETATM 2884 C C3  . OLC C 2 .   ? 21.880 31.891 34.687  1.00 76.19  ? 1202 OLC A C3  1 
HETATM 2885 C C2  . OLC C 2 .   ? 22.736 32.739 33.756  1.00 73.56  ? 1202 OLC A C2  1 
HETATM 2886 C C21 . OLC C 2 .   ? 23.649 33.410 30.902  1.00 96.72  ? 1202 OLC A C21 1 
HETATM 2887 C C1  . OLC C 2 .   ? 22.029 32.736 32.445  1.00 98.14  ? 1202 OLC A C1  1 
HETATM 2888 C C22 . OLC C 2 .   ? 23.741 34.492 29.810  1.00 98.97  ? 1202 OLC A C22 1 
HETATM 2889 O O19 . OLC C 2 .   ? 21.137 31.977 32.093  1.00 90.84  ? 1202 OLC A O19 1 
HETATM 2890 O O25 . OLC C 2 .   ? 24.833 35.009 27.812  1.00 101.16 ? 1202 OLC A O25 1 
HETATM 2891 O O23 . OLC C 2 .   ? 22.557 34.568 29.095  1.00 100.04 ? 1202 OLC A O23 1 
HETATM 2892 O O20 . OLC C 2 .   ? 22.441 33.703 31.580  1.00 110.59 ? 1202 OLC A O20 1 
HETATM 2893 C C13 . P15 D 3 .   ? 18.486 19.077 25.809  1.00 77.86  ? 1203 P15 A C13 1 
HETATM 2894 O O6  . P15 D 3 .   ? 17.701 18.305 26.675  1.00 90.09  ? 1203 P15 A O6  1 
HETATM 2895 C C12 . P15 D 3 .   ? 17.445 17.007 26.216  1.00 94.38  ? 1203 P15 A C12 1 
HETATM 2896 C C11 . P15 D 3 .   ? 16.668 16.222 27.274  1.00 73.65  ? 1203 P15 A C11 1 
HETATM 2897 O O5  . P15 D 3 .   ? 17.550 15.711 28.237  1.00 75.93  ? 1203 P15 A O5  1 
HETATM 2898 C C10 . P15 D 3 .   ? 16.932 14.982 29.262  1.00 60.36  ? 1203 P15 A C10 1 
HETATM 2899 C C9  . P15 D 3 .   ? 17.860 14.894 30.473  1.00 64.68  ? 1203 P15 A C9  1 
HETATM 2900 O O4  . P15 D 3 .   ? 17.234 15.500 31.570  1.00 63.24  ? 1203 P15 A O4  1 
HETATM 2901 C C8  . P15 D 3 .   ? 18.082 15.818 32.639  1.00 69.15  ? 1203 P15 A C8  1 
HETATM 2902 C C7  . P15 D 3 .   ? 17.324 16.677 33.652  1.00 61.89  ? 1203 P15 A C7  1 
HETATM 2903 O O3  . P15 D 3 .   ? 17.359 18.018 33.251  1.00 75.39  ? 1203 P15 A O3  1 
HETATM 2904 C C6  . P15 D 3 .   ? 16.295 18.802 33.713  1.00 55.26  ? 1203 P15 A C6  1 
HETATM 2905 C C5  . P15 D 3 .   ? 16.397 18.955 35.225  1.00 71.68  ? 1203 P15 A C5  1 
HETATM 2906 O O2  . P15 D 3 .   ? 17.745 19.076 35.570  1.00 77.33  ? 1203 P15 A O2  1 
HETATM 2907 C C4  . P15 D 3 .   ? 17.989 19.470 36.888  1.00 59.43  ? 1203 P15 A C4  1 
HETATM 2908 C C3  . P15 D 3 .   ? 17.792 18.288 37.837  1.00 66.83  ? 1203 P15 A C3  1 
HETATM 2909 O O1  . P15 D 3 .   ? 18.997 17.589 38.002  1.00 48.63  ? 1203 P15 A O1  1 
HETATM 2910 C C2  . P15 D 3 .   ? 18.828 16.258 38.397  1.00 49.32  ? 1203 P15 A C2  1 
HETATM 2911 C C1  . P15 D 3 .   ? 19.570 15.962 39.690  1.00 53.38  ? 1203 P15 A C1  1 
HETATM 2912 O OXT . P15 D 3 .   ? 19.332 14.621 40.021  1.00 57.79  ? 1203 P15 A OXT 1 
HETATM 2913 C C1  . OLA E 4 .   ? 14.520 29.672 60.873  1.00 83.14  ? 1204 OLA A C1  1 
HETATM 2914 O O1  . OLA E 4 .   ? 15.396 28.981 61.450  1.00 68.25  ? 1204 OLA A O1  1 
HETATM 2915 O O2  . OLA E 4 .   ? 13.333 29.604 61.276  1.00 84.57  ? 1204 OLA A O2  1 
HETATM 2916 C C2  . OLA E 4 .   ? 14.904 30.593 59.707  1.00 67.55  ? 1204 OLA A C2  1 
HETATM 2917 C C3  . OLA E 4 .   ? 14.373 30.098 58.360  1.00 49.88  ? 1204 OLA A C3  1 
HETATM 2918 C C4  . OLA E 4 .   ? 14.670 31.103 57.246  1.00 52.66  ? 1204 OLA A C4  1 
HETATM 2919 C C5  . OLA E 4 .   ? 14.584 30.461 55.858  1.00 56.94  ? 1204 OLA A C5  1 
HETATM 2920 C C6  . OLA E 4 .   ? 14.713 31.498 54.739  1.00 50.07  ? 1204 OLA A C6  1 
HETATM 2921 C C7  . OLA E 4 .   ? 14.686 30.832 53.362  1.00 54.30  ? 1204 OLA A C7  1 
HETATM 2922 C C8  . OLA E 4 .   ? 14.046 31.714 52.302  1.00 58.61  ? 1204 OLA A C8  1 
HETATM 2923 C C9  . OLA E 4 .   ? 15.054 32.556 51.554  1.00 66.68  ? 1204 OLA A C9  1 
HETATM 2924 C C10 . OLA E 4 .   ? 15.138 32.623 50.217  1.00 64.03  ? 1204 OLA A C10 1 
HETATM 2925 C C11 . OLA E 4 .   ? 14.244 31.871 49.257  1.00 64.57  ? 1204 OLA A C11 1 
HETATM 2926 C C12 . OLA E 4 .   ? 13.722 32.804 48.178  1.00 84.93  ? 1204 OLA A C12 1 
HETATM 2927 C C13 . OLA E 4 .   ? 12.517 32.214 47.443  1.00 72.00  ? 1204 OLA A C13 1 
HETATM 2928 C C14 . OLA E 4 .   ? 12.965 31.136 46.457  1.00 55.45  ? 1204 OLA A C14 1 
HETATM 2929 C C15 . OLA E 4 .   ? 11.776 30.444 45.793  1.00 51.70  ? 1204 OLA A C15 1 
HETATM 2930 C C16 . OLA E 4 .   ? 12.195 29.081 45.247  1.00 52.32  ? 1204 OLA A C16 1 
HETATM 2931 C C17 . OLA E 4 .   ? 11.002 28.138 45.130  1.00 52.72  ? 1204 OLA A C17 1 
HETATM 2932 C C18 . OLA E 4 .   ? 11.441 26.694 44.996  1.00 52.01  ? 1204 OLA A C18 1 
HETATM 2933 C C9  . P15 F 3 .   ? 29.660 4.238  14.698  1.00 80.81  ? 1205 P15 A C9  1 
HETATM 2934 O O4  . P15 F 3 .   ? 29.348 3.026  15.327  1.00 111.22 ? 1205 P15 A O4  1 
HETATM 2935 C C8  . P15 F 3 .   ? 28.120 3.015  16.002  1.00 119.16 ? 1205 P15 A C8  1 
HETATM 2936 C C7  . P15 F 3 .   ? 28.297 3.557  17.421  1.00 114.67 ? 1205 P15 A C7  1 
HETATM 2937 O O3  . P15 F 3 .   ? 28.301 2.505  18.348  1.00 116.86 ? 1205 P15 A O3  1 
HETATM 2938 C C6  . P15 F 3 .   ? 27.033 2.036  18.719  1.00 110.35 ? 1205 P15 A C6  1 
HETATM 2939 C C5  . P15 F 3 .   ? 26.435 2.928  19.807  1.00 103.98 ? 1205 P15 A C5  1 
HETATM 2940 O O2  . P15 F 3 .   ? 26.977 2.576  21.048  1.00 102.48 ? 1205 P15 A O2  1 
HETATM 2941 C C4  . P15 F 3 .   ? 27.026 3.625  21.973  1.00 90.47  ? 1205 P15 A C4  1 
HETATM 2942 C C3  . P15 F 3 .   ? 27.447 3.084  23.338  1.00 64.23  ? 1205 P15 A C3  1 
HETATM 2943 O O1  . P15 F 3 .   ? 28.293 1.984  23.161  1.00 80.61  ? 1205 P15 A O1  1 
HETATM 2944 C C2  . P15 F 3 .   ? 29.468 2.290  22.467  1.00 91.18  ? 1205 P15 A C2  1 
HETATM 2945 C C1  . P15 F 3 .   ? 29.977 1.043  21.748  1.00 94.32  ? 1205 P15 A C1  1 
HETATM 2946 O OXT . P15 F 3 .   ? 31.351 1.178  21.504  1.00 78.32  ? 1205 P15 A OXT 1 
HETATM 2947 C C1  . OLA G 4 .   ? 34.093 32.225 66.643  1.00 84.80  ? 1206 OLA A C1  1 
HETATM 2948 O O1  . OLA G 4 .   ? 33.809 31.738 67.762  1.00 88.46  ? 1206 OLA A O1  1 
HETATM 2949 O O2  . OLA G 4 .   ? 35.112 32.944 66.528  1.00 91.41  ? 1206 OLA A O2  1 
HETATM 2950 C C2  . OLA G 4 .   ? 33.206 31.944 65.430  1.00 71.23  ? 1206 OLA A C2  1 
HETATM 2951 C C3  . OLA G 4 .   ? 33.714 32.675 64.190  1.00 71.42  ? 1206 OLA A C3  1 
HETATM 2952 C C4  . OLA G 4 .   ? 32.904 32.255 62.966  1.00 61.48  ? 1206 OLA A C4  1 
HETATM 2953 C C5  . OLA G 4 .   ? 33.342 32.996 61.704  1.00 70.90  ? 1206 OLA A C5  1 
HETATM 2954 C C6  . OLA G 4 .   ? 34.701 32.489 61.227  1.00 61.99  ? 1206 OLA A C6  1 
HETATM 2955 C C7  . OLA G 4 .   ? 34.952 32.837 59.761  1.00 69.26  ? 1206 OLA A C7  1 
HETATM 2956 C C8  . OLA G 4 .   ? 35.223 34.320 59.585  1.00 70.47  ? 1206 OLA A C8  1 
HETATM 2957 C C9  . OLA G 4 .   ? 36.643 34.562 59.123  1.00 52.24  ? 1206 OLA A C9  1 
HETATM 2958 C C10 . OLA G 4 .   ? 36.977 35.143 57.962  1.00 63.07  ? 1206 OLA A C10 1 
HETATM 2959 C C11 . OLA G 4 .   ? 35.983 35.644 56.940  1.00 85.32  ? 1206 OLA A C11 1 
HETATM 2960 C C12 . OLA G 4 .   ? 35.940 34.731 55.727  1.00 83.62  ? 1206 OLA A C12 1 
HETATM 2961 C C13 . OLA G 4 .   ? 34.905 33.616 55.885  1.00 87.07  ? 1206 OLA A C13 1 
HETATM 2962 C C14 . OLA G 4 .   ? 34.983 32.629 54.720  1.00 63.71  ? 1206 OLA A C14 1 
HETATM 2963 C C15 . OLA G 4 .   ? 36.240 31.767 54.836  1.00 63.17  ? 1206 OLA A C15 1 
HETATM 2964 C C16 . OLA G 4 .   ? 36.356 30.754 53.700  1.00 63.61  ? 1206 OLA A C16 1 
HETATM 2965 C C17 . OLA G 4 .   ? 36.389 31.441 52.337  1.00 49.17  ? 1206 OLA A C17 1 
HETATM 2966 C C18 . OLA G 4 .   ? 36.578 30.434 51.220  1.00 61.28  ? 1206 OLA A C18 1 
HETATM 2967 C C1  . OLA H 4 .   ? 28.618 32.282 65.949  1.00 86.25  ? 1207 OLA A C1  1 
HETATM 2968 O O1  . OLA H 4 .   ? 27.377 32.245 65.765  1.00 87.22  ? 1207 OLA A O1  1 
HETATM 2969 O O2  . OLA H 4 .   ? 29.082 31.920 67.055  1.00 82.43  ? 1207 OLA A O2  1 
HETATM 2970 C C2  . OLA H 4 .   ? 29.554 32.762 64.838  1.00 69.19  ? 1207 OLA A C2  1 
HETATM 2971 C C3  . OLA H 4 .   ? 28.771 33.398 63.692  1.00 69.47  ? 1207 OLA A C3  1 
HETATM 2972 C C4  . OLA H 4 .   ? 29.663 33.554 62.465  1.00 74.01  ? 1207 OLA A C4  1 
HETATM 2973 C C5  . OLA H 4 .   ? 28.905 34.176 61.297  1.00 54.69  ? 1207 OLA A C5  1 
HETATM 2974 C C6  . OLA H 4 .   ? 29.781 34.179 60.047  1.00 70.47  ? 1207 OLA A C6  1 
HETATM 2975 C C7  . OLA H 4 .   ? 29.183 35.077 58.965  1.00 68.34  ? 1207 OLA A C7  1 
HETATM 2976 C C8  . OLA H 4 .   ? 30.042 35.111 57.710  1.00 74.14  ? 1207 OLA A C8  1 
HETATM 2977 C C9  . OLA H 4 .   ? 31.397 35.711 57.996  1.00 80.18  ? 1207 OLA A C9  1 
HETATM 2978 C C10 . OLA H 4 .   ? 32.226 36.073 57.016  1.00 71.99  ? 1207 OLA A C10 1 
HETATM 2979 C C11 . OLA H 4 .   ? 31.865 35.908 55.561  1.00 83.88  ? 1207 OLA A C11 1 
HETATM 2980 C C12 . OLA H 4 .   ? 32.841 36.689 54.698  1.00 87.06  ? 1207 OLA A C12 1 
HETATM 2981 C C13 . OLA H 4 .   ? 32.443 36.654 53.225  1.00 98.65  ? 1207 OLA A C13 1 
HETATM 2982 C C14 . OLA H 4 .   ? 33.555 37.226 52.348  1.00 88.06  ? 1207 OLA A C14 1 
HETATM 2983 C C15 . OLA H 4 .   ? 33.372 36.807 50.891  1.00 94.22  ? 1207 OLA A C15 1 
HETATM 2984 C C16 . OLA H 4 .   ? 32.132 37.452 50.274  1.00 91.23  ? 1207 OLA A C16 1 
HETATM 2985 C C17 . OLA H 4 .   ? 31.996 37.069 48.801  1.00 76.96  ? 1207 OLA A C17 1 
HETATM 2986 C C18 . OLA H 4 .   ? 30.888 37.856 48.126  1.00 91.34  ? 1207 OLA A C18 1 
HETATM 2987 C C1  . OLA I 4 .   ? 40.473 15.905 34.755  1.00 89.28  ? 1208 OLA A C1  1 
HETATM 2988 O O1  . OLA I 4 .   ? 39.321 16.396 34.731  1.00 82.11  ? 1208 OLA A O1  1 
HETATM 2989 O O2  . OLA I 4 .   ? 41.234 16.067 33.771  1.00 80.02  ? 1208 OLA A O2  1 
HETATM 2990 C C2  . OLA I 4 .   ? 40.936 15.117 35.980  1.00 75.14  ? 1208 OLA A C2  1 
HETATM 2991 C C3  . OLA I 4 .   ? 39.792 14.997 36.980  1.00 62.89  ? 1208 OLA A C3  1 
HETATM 2992 C C4  . OLA I 4 .   ? 40.223 14.234 38.228  1.00 65.29  ? 1208 OLA A C4  1 
HETATM 2993 C C5  . OLA I 4 .   ? 39.404 14.692 39.430  1.00 60.45  ? 1208 OLA A C5  1 
HETATM 2994 C C6  . OLA I 4 .   ? 39.754 13.892 40.679  1.00 63.21  ? 1208 OLA A C6  1 
HETATM 2995 C C7  . OLA I 4 .   ? 38.654 14.063 41.719  1.00 61.38  ? 1208 OLA A C7  1 
HETATM 2996 C C8  . OLA I 4 .   ? 38.970 13.287 42.981  1.00 53.39  ? 1208 OLA A C8  1 
HETATM 2997 C C9  . OLA I 4 .   ? 39.526 14.208 44.033  1.00 60.73  ? 1208 OLA A C9  1 
HETATM 2998 C C10 . OLA I 4 .   ? 39.616 13.835 45.309  1.00 58.96  ? 1208 OLA A C10 1 
HETATM 2999 C C11 . OLA I 4 .   ? 39.169 12.473 45.777  1.00 63.92  ? 1208 OLA A C11 1 
HETATM 3000 C C12 . OLA I 4 .   ? 40.033 12.009 46.933  1.00 66.03  ? 1208 OLA A C12 1 
HETATM 3001 C C13 . OLA I 4 .   ? 39.791 12.858 48.180  1.00 59.86  ? 1208 OLA A C13 1 
HETATM 3002 C C14 . OLA I 4 .   ? 39.198 12.019 49.309  1.00 83.54  ? 1208 OLA A C14 1 
HETATM 3003 C C15 . OLA I 4 .   ? 38.513 12.894 50.356  1.00 78.73  ? 1208 OLA A C15 1 
HETATM 3004 C C16 . OLA I 4 .   ? 38.318 12.122 51.660  1.00 70.46  ? 1208 OLA A C16 1 
HETATM 3005 C C17 . OLA I 4 .   ? 39.514 12.305 52.591  1.00 68.99  ? 1208 OLA A C17 1 
HETATM 3006 C C18 . OLA I 4 .   ? 39.884 11.002 53.273  1.00 74.84  ? 1208 OLA A C18 1 
HETATM 3007 C C1  . OLA J 4 .   ? 15.162 4.307  64.529  1.00 74.93  ? 1209 OLA A C1  1 
HETATM 3008 O O1  . OLA J 4 .   ? 16.294 4.659  64.933  1.00 73.96  ? 1209 OLA A O1  1 
HETATM 3009 O O2  . OLA J 4 .   ? 14.354 5.182  64.141  1.00 54.82  ? 1209 OLA A O2  1 
HETATM 3010 C C2  . OLA J 4 .   ? 14.771 2.828  64.506  1.00 74.94  ? 1209 OLA A C2  1 
HETATM 3011 C C3  . OLA J 4 .   ? 14.125 2.468  63.171  1.00 64.81  ? 1209 OLA A C3  1 
HETATM 3012 C C4  . OLA J 4 .   ? 15.171 1.949  62.190  1.00 56.36  ? 1209 OLA A C4  1 
HETATM 3013 C C5  . OLA J 4 .   ? 14.682 2.087  60.750  1.00 73.23  ? 1209 OLA A C5  1 
HETATM 3014 C C6  . OLA J 4 .   ? 15.391 1.096  59.831  1.00 71.62  ? 1209 OLA A C6  1 
HETATM 3015 C C7  . OLA J 4 .   ? 15.983 1.779  58.598  1.00 70.27  ? 1209 OLA A C7  1 
HETATM 3016 C C8  . OLA J 4 .   ? 14.921 2.322  57.653  1.00 85.98  ? 1209 OLA A C8  1 
HETATM 3017 C C9  . OLA J 4 .   ? 14.151 1.214  56.974  1.00 92.21  ? 1209 OLA A C9  1 
HETATM 3018 C C10 . OLA J 4 .   ? 13.543 1.383  55.794  1.00 95.08  ? 1209 OLA A C10 1 
HETATM 3019 C C11 . OLA J 4 .   ? 13.576 2.693  55.044  1.00 77.22  ? 1209 OLA A C11 1 
HETATM 3020 C C12 . OLA J 4 .   ? 14.851 2.821  54.227  1.00 80.24  ? 1209 OLA A C12 1 
HETATM 3021 C C13 . OLA J 4 .   ? 14.775 2.038  52.914  1.00 76.37  ? 1209 OLA A C13 1 
HETATM 3022 C C14 . OLA J 4 .   ? 16.143 1.482  52.511  1.00 90.87  ? 1209 OLA A C14 1 
HETATM 3023 C C15 . OLA J 4 .   ? 16.237 -0.035 52.688  1.00 87.53  ? 1209 OLA A C15 1 
HETATM 3024 C C16 . OLA J 4 .   ? 15.802 -0.480 54.085  1.00 80.29  ? 1209 OLA A C16 1 
HETATM 3025 C C17 . OLA J 4 .   ? 16.266 -1.905 54.381  1.00 88.35  ? 1209 OLA A C17 1 
HETATM 3026 C C18 . OLA J 4 .   ? 15.449 -2.513 55.505  1.00 80.27  ? 1209 OLA A C18 1 
HETATM 3027 C C1  . OLA K 4 .   ? 21.525 13.922 63.430  1.00 68.45  ? 1210 OLA A C1  1 
HETATM 3028 O O1  . OLA K 4 .   ? 21.095 13.070 64.242  1.00 78.84  ? 1210 OLA A O1  1 
HETATM 3029 O O2  . OLA K 4 .   ? 21.956 15.015 63.865  1.00 63.71  ? 1210 OLA A O2  1 
HETATM 3030 C C2  . OLA K 4 .   ? 21.523 13.633 61.925  1.00 61.82  ? 1210 OLA A C2  1 
HETATM 3031 C C3  . OLA K 4 .   ? 22.869 13.083 61.457  1.00 69.78  ? 1210 OLA A C3  1 
HETATM 3032 C C4  . OLA K 4 .   ? 23.013 13.225 59.941  1.00 56.58  ? 1210 OLA A C4  1 
HETATM 3033 C C5  . OLA K 4 .   ? 24.462 13.036 59.494  1.00 63.13  ? 1210 OLA A C5  1 
HETATM 3034 C C6  . OLA K 4 .   ? 25.107 14.356 59.069  1.00 52.49  ? 1210 OLA A C6  1 
HETATM 3035 C C7  . OLA K 4 .   ? 24.768 14.700 57.619  1.00 50.47  ? 1210 OLA A C7  1 
HETATM 3036 C C8  . OLA K 4 .   ? 25.270 16.080 57.234  1.00 42.34  ? 1210 OLA A C8  1 
HETATM 3037 C C9  . OLA K 4 .   ? 25.171 16.265 55.741  1.00 63.25  ? 1210 OLA A C9  1 
HETATM 3038 C C10 . OLA K 4 .   ? 24.646 17.350 55.170  1.00 60.83  ? 1210 OLA A C10 1 
HETATM 3039 C C11 . OLA K 4 .   ? 24.094 18.514 55.954  1.00 59.45  ? 1210 OLA A C11 1 
HETATM 3040 C C12 . OLA K 4 .   ? 23.590 19.571 54.986  1.00 52.05  ? 1210 OLA A C12 1 
HETATM 3041 C C13 . OLA K 4 .   ? 22.477 20.423 55.594  1.00 54.59  ? 1210 OLA A C13 1 
HETATM 3042 C C14 . OLA K 4 .   ? 21.664 21.092 54.487  1.00 70.40  ? 1210 OLA A C14 1 
HETATM 3043 C C15 . OLA K 4 .   ? 20.537 21.942 55.066  1.00 51.88  ? 1210 OLA A C15 1 
HETATM 3044 C C16 . OLA K 4 .   ? 19.280 21.857 54.201  1.00 61.75  ? 1210 OLA A C16 1 
HETATM 3045 C C17 . OLA K 4 .   ? 19.426 22.636 52.895  1.00 54.11  ? 1210 OLA A C17 1 
HETATM 3046 C C18 . OLA K 4 .   ? 19.607 21.699 51.715  1.00 70.34  ? 1210 OLA A C18 1 
HETATM 3047 C C18 . OLC L 2 .   ? 12.410 9.897  45.473  1.00 65.48  ? 1211 OLC A C18 1 
HETATM 3048 C C10 . OLC L 2 .   ? 9.623  12.295 54.779  1.00 84.03  ? 1211 OLC A C10 1 
HETATM 3049 C C9  . OLC L 2 .   ? 9.003  11.964 55.922  1.00 92.17  ? 1211 OLC A C9  1 
HETATM 3050 C C17 . OLC L 2 .   ? 12.224 9.397  46.897  1.00 65.80  ? 1211 OLC A C17 1 
HETATM 3051 C C11 . OLC L 2 .   ? 10.335 11.308 53.913  1.00 67.77  ? 1211 OLC A C11 1 
HETATM 3052 C C8  . OLC L 2 .   ? 8.953  10.572 56.469  1.00 81.89  ? 1211 OLC A C8  1 
HETATM 3053 C C24 . OLC L 2 .   ? 8.439  9.038  67.407  1.00 82.14  ? 1211 OLC A C24 1 
HETATM 3054 C C16 . OLC L 2 .   ? 11.643 10.506 47.781  1.00 64.84  ? 1211 OLC A C16 1 
HETATM 3055 C C12 . OLC L 2 .   ? 10.401 11.839 52.476  1.00 54.22  ? 1211 OLC A C12 1 
HETATM 3056 C C7  . OLC L 2 .   ? 8.922  10.624 58.000  1.00 64.49  ? 1211 OLC A C7  1 
HETATM 3057 C C15 . OLC L 2 .   ? 11.458 10.028 49.224  1.00 78.90  ? 1211 OLC A C15 1 
HETATM 3058 C C13 . OLC L 2 .   ? 10.814 10.700 51.547  1.00 72.71  ? 1211 OLC A C13 1 
HETATM 3059 C C6  . OLC L 2 .   ? 9.054  9.211  58.562  1.00 75.44  ? 1211 OLC A C6  1 
HETATM 3060 C C14 . OLC L 2 .   ? 10.937 11.176 50.097  1.00 85.24  ? 1211 OLC A C14 1 
HETATM 3061 C C5  . OLC L 2 .   ? 9.054  9.256  60.086  1.00 82.92  ? 1211 OLC A C5  1 
HETATM 3062 C C4  . OLC L 2 .   ? 9.018  7.843  60.663  1.00 72.09  ? 1211 OLC A C4  1 
HETATM 3063 C C3  . OLC L 2 .   ? 8.827  7.940  62.166  1.00 74.59  ? 1211 OLC A C3  1 
HETATM 3064 C C2  . OLC L 2 .   ? 8.497  6.577  62.766  1.00 92.49  ? 1211 OLC A C2  1 
HETATM 3065 C C21 . OLC L 2 .   ? 9.314  7.060  66.198  1.00 87.24  ? 1211 OLC A C21 1 
HETATM 3066 C C1  . OLC L 2 .   ? 8.124  6.833  64.185  1.00 84.88  ? 1211 OLC A C1  1 
HETATM 3067 C C22 . OLC L 2 .   ? 9.741  8.318  66.971  1.00 75.48  ? 1211 OLC A C22 1 
HETATM 3068 O O19 . OLC L 2 .   ? 7.094  6.487  64.748  1.00 105.94 ? 1211 OLC A O19 1 
HETATM 3069 O O25 . OLC L 2 .   ? 8.739  10.394 67.293  1.00 61.93  ? 1211 OLC A O25 1 
HETATM 3070 O O23 . OLC L 2 .   ? 10.546 8.000  68.051  1.00 81.20  ? 1211 OLC A O23 1 
HETATM 3071 O O20 . OLC L 2 .   ? 9.049  7.539  64.887  1.00 93.24  ? 1211 OLC A O20 1 
HETATM 3072 C C18 . OLC M 2 .   ? 34.745 21.255 54.632  1.00 57.14  ? 1212 OLC A C18 1 
HETATM 3073 C C10 . OLC M 2 .   ? 42.247 16.670 56.806  1.00 77.35  ? 1212 OLC A C10 1 
HETATM 3074 C C9  . OLC M 2 .   ? 43.096 15.848 57.445  1.00 71.63  ? 1212 OLC A C9  1 
HETATM 3075 C C17 . OLC M 2 .   ? 35.944 21.855 55.313  1.00 52.69  ? 1212 OLC A C17 1 
HETATM 3076 C C11 . OLC M 2 .   ? 40.780 16.402 56.621  1.00 90.29  ? 1212 OLC A C11 1 
HETATM 3077 C C8  . OLC M 2 .   ? 42.705 14.546 58.054  1.00 72.97  ? 1212 OLC A C8  1 
HETATM 3078 C C24 . OLC M 2 .   ? 39.603 11.347 69.269  1.00 83.26  ? 1212 OLC A C24 1 
HETATM 3079 C C16 . OLC M 2 .   ? 36.463 20.883 56.348  1.00 58.77  ? 1212 OLC A C16 1 
HETATM 3080 C C12 . OLC M 2 .   ? 39.957 17.587 57.155  1.00 66.05  ? 1212 OLC A C12 1 
HETATM 3081 C C7  . OLC M 2 .   ? 42.646 14.663 59.569  1.00 92.10  ? 1212 OLC A C7  1 
HETATM 3082 C C15 . OLC M 2 .   ? 37.139 19.684 55.712  1.00 50.15  ? 1212 OLC A C15 1 
HETATM 3083 C C13 . OLC M 2 .   ? 38.738 17.819 56.250  1.00 46.30  ? 1212 OLC A C13 1 
HETATM 3084 C C6  . OLC M 2 .   ? 42.464 13.265 60.143  1.00 100.08 ? 1212 OLC A C6  1 
HETATM 3085 C C14 . OLC M 2 .   ? 37.911 18.973 56.807  1.00 40.69  ? 1212 OLC A C14 1 
HETATM 3086 C C5  . OLC M 2 .   ? 42.416 13.317 61.655  1.00 85.27  ? 1212 OLC A C5  1 
HETATM 3087 C C4  . OLC M 2 .   ? 42.552 11.913 62.226  1.00 77.28  ? 1212 OLC A C4  1 
HETATM 3088 C C3  . OLC M 2 .   ? 42.521 12.016 63.731  1.00 82.46  ? 1212 OLC A C3  1 
HETATM 3089 C C2  . OLC M 2 .   ? 42.796 10.671 64.382  1.00 89.18  ? 1212 OLC A C2  1 
HETATM 3090 C C21 . OLC M 2 .   ? 40.855 10.572 67.246  1.00 95.29  ? 1212 OLC A C21 1 
HETATM 3091 C C1  . OLC M 2 .   ? 42.690 10.911 65.848  1.00 90.19  ? 1212 OLC A C1  1 
HETATM 3092 C C22 . OLC M 2 .   ? 40.981 11.384 68.550  1.00 92.06  ? 1212 OLC A C22 1 
HETATM 3093 O O19 . OLC M 2 .   ? 43.568 10.738 66.682  1.00 108.07 ? 1212 OLC A O19 1 
HETATM 3094 O O25 . OLC M 2 .   ? 39.902 11.545 70.620  1.00 91.05  ? 1212 OLC A O25 1 
HETATM 3095 O O23 . OLC M 2 .   ? 41.991 10.873 69.348  1.00 119.67 ? 1212 OLC A O23 1 
HETATM 3096 O O20 . OLC M 2 .   ? 41.480 11.378 66.261  1.00 102.42 ? 1212 OLC A O20 1 
HETATM 3097 C C6  . OLA N 4 .   ? 27.616 30.037 42.912  1.00 73.09  ? 1213 OLA A C6  1 
HETATM 3098 C C7  . OLA N 4 .   ? 26.208 29.806 43.454  1.00 74.00  ? 1213 OLA A C7  1 
HETATM 3099 C C8  . OLA N 4 .   ? 26.243 29.348 44.900  1.00 57.17  ? 1213 OLA A C8  1 
HETATM 3100 C C9  . OLA N 4 .   ? 26.912 28.002 45.040  1.00 53.03  ? 1213 OLA A C9  1 
HETATM 3101 C C10 . OLA N 4 .   ? 26.475 27.049 45.869  1.00 50.84  ? 1213 OLA A C10 1 
HETATM 3102 C C11 . OLA N 4 .   ? 25.268 27.195 46.763  1.00 51.46  ? 1213 OLA A C11 1 
HETATM 3103 C C12 . OLA N 4 .   ? 24.498 25.890 46.808  1.00 41.31  ? 1213 OLA A C12 1 
HETATM 3104 C C13 . OLA N 4 .   ? 23.681 25.821 48.088  1.00 46.13  ? 1213 OLA A C13 1 
HETATM 3105 C C14 . OLA N 4 .   ? 22.527 24.843 47.927  1.00 57.37  ? 1213 OLA A C14 1 
HETATM 3106 C C15 . OLA N 4 .   ? 22.968 23.438 48.318  1.00 46.40  ? 1213 OLA A C15 1 
HETATM 3107 C C16 . OLA N 4 .   ? 23.179 23.337 49.818  1.00 41.98  ? 1213 OLA A C16 1 
HETATM 3108 C C17 . OLA N 4 .   ? 23.039 21.885 50.278  1.00 62.72  ? 1213 OLA A C17 1 
HETATM 3109 C C18 . OLA N 4 .   ? 23.731 21.671 51.615  1.00 55.71  ? 1213 OLA A C18 1 
HETATM 3110 C C18 . OLC O 2 .   ? 36.857 -2.546 50.558  1.00 57.99  ? 1214 OLC A C18 1 
HETATM 3111 C C10 . OLC O 2 .   ? 35.650 1.984  43.473  1.00 78.95  ? 1214 OLC A C10 1 
HETATM 3112 C C9  . OLC O 2 .   ? 35.927 2.494  42.264  1.00 75.10  ? 1214 OLC A C9  1 
HETATM 3113 C C17 . OLC O 2 .   ? 35.739 -1.958 49.714  1.00 56.52  ? 1214 OLC A C17 1 
HETATM 3114 C C11 . OLC O 2 .   ? 35.662 0.514  43.760  1.00 77.70  ? 1214 OLC A C11 1 
HETATM 3115 C C8  . OLC O 2 .   ? 36.275 1.646  41.088  1.00 76.48  ? 1214 OLC A C8  1 
HETATM 3116 C C24 . OLC O 2 .   ? 42.180 -0.799 34.677  1.00 99.89  ? 1214 OLC A C24 1 
HETATM 3117 C C16 . OLC O 2 .   ? 36.052 -2.121 48.230  1.00 74.73  ? 1214 OLC A C16 1 
HETATM 3118 C C12 . OLC O 2 .   ? 36.355 0.250  45.098  1.00 95.89  ? 1214 OLC A C12 1 
HETATM 3119 C C7  . OLC O 2 .   ? 36.129 2.447  39.795  1.00 65.01  ? 1214 OLC A C7  1 
HETATM 3120 C C15 . OLC O 2 .   ? 37.084 -1.113 47.749  1.00 80.09  ? 1214 OLC A C15 1 
HETATM 3121 C C13 . OLC O 2 .   ? 36.528 -1.253 45.289  1.00 77.71  ? 1214 OLC A C13 1 
HETATM 3122 C C6  . OLC O 2 .   ? 37.335 3.371  39.608  1.00 69.29  ? 1214 OLC A C6  1 
HETATM 3123 C C14 . OLC O 2 .   ? 37.577 -1.537 46.361  1.00 83.96  ? 1214 OLC A C14 1 
HETATM 3124 C C5  . OLC O 2 .   ? 38.531 2.598  39.051  1.00 76.67  ? 1214 OLC A C5  1 
HETATM 3125 C C4  . OLC O 2 .   ? 38.378 2.382  37.545  1.00 68.24  ? 1214 OLC A C4  1 
HETATM 3126 C C3  . OLC O 2 .   ? 39.711 1.904  36.961  1.00 81.46  ? 1214 OLC A C3  1 
HETATM 3127 C C2  . OLC O 2 .   ? 40.789 2.995  37.010  1.00 86.43  ? 1214 OLC A C2  1 
HETATM 3128 C C21 . OLC O 2 .   ? 42.595 1.610  34.113  1.00 97.09  ? 1214 OLC A C21 1 
HETATM 3129 C C1  . OLC O 2 .   ? 41.522 2.945  35.711  1.00 100.67 ? 1214 OLC A C1  1 
HETATM 3130 C C22 . OLC O 2 .   ? 43.202 0.188  34.045  1.00 89.57  ? 1214 OLC A C22 1 
HETATM 3131 O O19 . OLC O 2 .   ? 41.605 3.844  34.886  1.00 80.91  ? 1214 OLC A O19 1 
HETATM 3132 O O25 . OLC O 2 .   ? 42.693 -1.072 35.947  1.00 100.63 ? 1214 OLC A O25 1 
HETATM 3133 O O23 . OLC O 2 .   ? 43.504 -0.157 32.738  1.00 85.83  ? 1214 OLC A O23 1 
HETATM 3134 O O20 . OLC O 2 .   ? 42.158 1.763  35.458  1.00 116.29 ? 1214 OLC A O20 1 
HETATM 3135 C C1  . OLA P 4 .   ? 16.427 34.046 30.299  1.00 78.41  ? 1215 OLA A C1  1 
HETATM 3136 O O1  . OLA P 4 .   ? 15.928 33.464 29.310  1.00 76.17  ? 1215 OLA A O1  1 
HETATM 3137 O O2  . OLA P 4 .   ? 16.230 35.274 30.442  1.00 92.49  ? 1215 OLA A O2  1 
HETATM 3138 C C2  . OLA P 4 .   ? 17.262 33.271 31.321  1.00 83.30  ? 1215 OLA A C2  1 
HETATM 3139 C C3  . OLA P 4 .   ? 17.562 34.153 32.530  1.00 81.46  ? 1215 OLA A C3  1 
HETATM 3140 C C4  . OLA P 4 .   ? 18.242 33.375 33.654  1.00 80.01  ? 1215 OLA A C4  1 
HETATM 3141 C C5  . OLA P 4 .   ? 18.049 34.105 34.982  1.00 90.94  ? 1215 OLA A C5  1 
HETATM 3142 C C6  . OLA P 4 .   ? 19.117 33.717 36.001  1.00 95.98  ? 1215 OLA A C6  1 
HETATM 3143 C C7  . OLA P 4 .   ? 18.981 34.548 37.276  1.00 79.55  ? 1215 OLA A C7  1 
HETATM 3144 C C8  . OLA P 4 .   ? 20.064 34.182 38.276  1.00 90.45  ? 1215 OLA A C8  1 
HETATM 3145 C C9  . OLA P 4 .   ? 20.530 35.367 39.088  1.00 75.58  ? 1215 OLA A C9  1 
HETATM 3146 C C10 . OLA P 4 .   ? 19.756 35.921 40.021  1.00 79.36  ? 1215 OLA A C10 1 
HETATM 3147 C C11 . OLA P 4 .   ? 18.375 35.389 40.310  1.00 89.84  ? 1215 OLA A C11 1 
HETATM 3148 C C12 . OLA P 4 .   ? 17.765 36.082 41.515  1.00 69.82  ? 1215 OLA A C12 1 
HETATM 3149 C C10 . OLA Q 4 .   ? 36.720 33.654 39.366  1.00 66.46  ? 1216 OLA A C10 1 
HETATM 3150 C C11 . OLA Q 4 .   ? 37.467 32.562 40.088  1.00 59.08  ? 1216 OLA A C11 1 
HETATM 3151 C C12 . OLA Q 4 .   ? 36.756 32.177 41.376  1.00 54.26  ? 1216 OLA A C12 1 
HETATM 3152 C C13 . OLA Q 4 .   ? 36.102 33.392 42.027  1.00 54.59  ? 1216 OLA A C13 1 
HETATM 3153 C C14 . OLA Q 4 .   ? 36.062 33.233 43.539  1.00 48.02  ? 1216 OLA A C14 1 
HETATM 3154 C C15 . OLA Q 4 .   ? 34.641 32.988 44.037  1.00 65.92  ? 1216 OLA A C15 1 
HETATM 3155 C C16 . OLA Q 4 .   ? 33.869 34.301 44.143  1.00 79.28  ? 1216 OLA A C16 1 
HETATM 3156 C C17 . OLA Q 4 .   ? 32.495 34.077 44.775  1.00 61.59  ? 1216 OLA A C17 1 
HETATM 3157 C C18 . OLA Q 4 .   ? 31.536 35.184 44.375  1.00 76.20  ? 1216 OLA A C18 1 
HETATM 3158 C C1  . OLA R 4 .   ? 43.965 7.120  64.653  1.00 94.35  ? 1217 OLA A C1  1 
HETATM 3159 O O1  . OLA R 4 .   ? 45.105 7.434  64.240  1.00 84.48  ? 1217 OLA A O1  1 
HETATM 3160 O O2  . OLA R 4 .   ? 43.784 6.980  65.885  1.00 89.72  ? 1217 OLA A O2  1 
HETATM 3161 C C2  . OLA R 4 .   ? 42.809 6.908  63.671  1.00 82.74  ? 1217 OLA A C2  1 
HETATM 3162 C C3  . OLA R 4 .   ? 43.246 7.160  62.228  1.00 71.97  ? 1217 OLA A C3  1 
HETATM 3163 C C4  . OLA R 4 .   ? 42.086 6.945  61.255  1.00 82.24  ? 1217 OLA A C4  1 
HETATM 3164 C C5  . OLA R 4 .   ? 42.504 7.245  59.816  1.00 75.02  ? 1217 OLA A C5  1 
HETATM 3165 C C6  . OLA R 4 .   ? 41.297 7.364  58.883  1.00 78.66  ? 1217 OLA A C6  1 
HETATM 3166 C C7  . OLA R 4 .   ? 40.599 6.017  58.699  1.00 85.81  ? 1217 OLA A C7  1 
HETATM 3167 C C8  . OLA R 4 .   ? 39.588 6.046  57.563  1.00 70.38  ? 1217 OLA A C8  1 
HETATM 3168 C C9  . OLA R 4 .   ? 40.265 6.194  56.224  1.00 82.31  ? 1217 OLA A C9  1 
HETATM 3169 C C10 . OLA R 4 .   ? 39.560 6.146  55.094  1.00 92.29  ? 1217 OLA A C10 1 
HETATM 3170 C C11 . OLA R 4 .   ? 38.065 5.944  55.122  1.00 75.11  ? 1217 OLA A C11 1 
HETATM 3171 C C12 . OLA R 4 .   ? 37.491 5.784  53.722  1.00 82.48  ? 1217 OLA A C12 1 
HETATM 3172 C C13 . OLA R 4 .   ? 37.120 7.123  53.082  1.00 76.39  ? 1217 OLA A C13 1 
HETATM 3173 C C14 . OLA R 4 .   ? 38.334 7.981  52.713  1.00 89.13  ? 1217 OLA A C14 1 
HETATM 3174 C C15 . OLA R 4 .   ? 39.280 7.304  51.719  1.00 82.38  ? 1217 OLA A C15 1 
HETATM 3175 C C16 . OLA R 4 .   ? 38.583 6.972  50.400  1.00 91.12  ? 1217 OLA A C16 1 
HETATM 3176 C C17 . OLA R 4 .   ? 39.572 6.425  49.369  1.00 88.20  ? 1217 OLA A C17 1 
HETATM 3177 C C18 . OLA R 4 .   ? 40.489 7.513  48.842  1.00 85.10  ? 1217 OLA A C18 1 
HETATM 3178 C C1  . OLA S 4 .   ? 15.908 -2.020 64.700  1.00 86.60  ? 1218 OLA A C1  1 
HETATM 3179 O O1  . OLA S 4 .   ? 16.423 -1.501 65.718  1.00 89.93  ? 1218 OLA A O1  1 
HETATM 3180 O O2  . OLA S 4 .   ? 14.789 -2.574 64.799  1.00 97.33  ? 1218 OLA A O2  1 
HETATM 3181 C C2  . OLA S 4 .   ? 16.630 -1.983 63.351  1.00 57.87  ? 1218 OLA A C2  1 
HETATM 3182 C C3  . OLA S 4 .   ? 16.011 -3.000 62.398  1.00 64.22  ? 1218 OLA A C3  1 
HETATM 3183 C C4  . OLA S 4 .   ? 16.917 -3.260 61.200  1.00 61.22  ? 1218 OLA A C4  1 
HETATM 3184 C C5  . OLA S 4 .   ? 17.063 -2.006 60.343  1.00 77.73  ? 1218 OLA A C5  1 
HETATM 3185 C C6  . OLA S 4 .   ? 17.659 -2.339 58.977  1.00 81.29  ? 1218 OLA A C6  1 
HETATM 3186 C C7  . OLA S 4 .   ? 19.020 -1.677 58.780  1.00 66.04  ? 1218 OLA A C7  1 
HETATM 3187 C C8  . OLA S 4 .   ? 19.324 -1.558 57.299  1.00 59.00  ? 1218 OLA A C8  1 
HETATM 3188 C C9  . OLA S 4 .   ? 20.808 -1.499 57.040  1.00 64.02  ? 1218 OLA A C9  1 
HETATM 3189 C C10 . OLA S 4 .   ? 21.314 -1.835 55.850  1.00 53.80  ? 1218 OLA A C10 1 
HETATM 3190 C C11 . OLA S 4 .   ? 20.427 -2.286 54.714  1.00 74.13  ? 1218 OLA A C11 1 
HETATM 3191 C C12 . OLA S 4 .   ? 21.172 -2.260 53.391  1.00 56.13  ? 1218 OLA A C12 1 
HETATM 3192 C C13 . OLA S 4 .   ? 20.230 -2.515 52.215  1.00 73.93  ? 1218 OLA A C13 1 
HETATM 3193 C C14 . OLA S 4 .   ? 20.893 -3.354 51.119  1.00 68.09  ? 1218 OLA A C14 1 
HETATM 3194 C C15 . OLA S 4 .   ? 21.621 -2.495 50.083  1.00 75.90  ? 1218 OLA A C15 1 
HETATM 3195 C C16 . OLA S 4 .   ? 22.453 -3.366 49.139  1.00 64.30  ? 1218 OLA A C16 1 
HETATM 3196 C C17 . OLA S 4 .   ? 23.447 -2.544 48.314  1.00 52.85  ? 1218 OLA A C17 1 
HETATM 3197 C C18 . OLA S 4 .   ? 23.005 -2.400 46.869  1.00 52.99  ? 1218 OLA A C18 1 
HETATM 3198 C C1  . OLA T 4 .   ? 39.222 -3.857 33.646  1.00 82.45  ? 1219 OLA A C1  1 
HETATM 3199 O O1  . OLA T 4 .   ? 38.210 -4.253 33.024  1.00 78.88  ? 1219 OLA A O1  1 
HETATM 3200 O O2  . OLA T 4 .   ? 40.351 -3.999 33.122  1.00 90.72  ? 1219 OLA A O2  1 
HETATM 3201 C C2  . OLA T 4 .   ? 39.081 -3.213 35.027  1.00 74.20  ? 1219 OLA A C2  1 
HETATM 3202 C C3  . OLA T 4 .   ? 38.169 -1.989 34.968  1.00 72.31  ? 1219 OLA A C3  1 
HETATM 3203 C C4  . OLA T 4 .   ? 37.038 -2.073 35.995  1.00 75.89  ? 1219 OLA A C4  1 
HETATM 3204 C C5  . OLA T 4 .   ? 36.071 -0.898 35.835  1.00 91.56  ? 1219 OLA A C5  1 
HETATM 3205 C C6  . OLA T 4 .   ? 34.991 -0.885 36.920  1.00 63.65  ? 1219 OLA A C6  1 
HETATM 3206 C C7  . OLA T 4 .   ? 33.883 -1.902 36.633  1.00 73.59  ? 1219 OLA A C7  1 
HETATM 3207 C C8  . OLA T 4 .   ? 32.583 -1.232 36.216  1.00 71.29  ? 1219 OLA A C8  1 
HETATM 3208 C C9  . OLA T 4 .   ? 31.449 -2.227 36.171  1.00 68.08  ? 1219 OLA A C9  1 
HETATM 3209 C C10 . OLA T 4 .   ? 30.225 -1.839 35.823  1.00 63.15  ? 1219 OLA A C10 1 
HETATM 3210 C C11 . OLA T 4 .   ? 29.949 -0.401 35.467  1.00 65.10  ? 1219 OLA A C11 1 
HETATM 3211 C C1  . CLR U 5 .   ? 37.109 17.824 39.064  1.00 33.31  ? 1220 CLR A C1  1 
HETATM 3212 C C2  . CLR U 5 .   ? 36.938 17.746 37.550  1.00 36.00  ? 1220 CLR A C2  1 
HETATM 3213 C C3  . CLR U 5 .   ? 35.908 18.765 37.087  1.00 34.68  ? 1220 CLR A C3  1 
HETATM 3214 C C4  . CLR U 5 .   ? 36.387 20.164 37.441  1.00 35.80  ? 1220 CLR A C4  1 
HETATM 3215 C C5  . CLR U 5 .   ? 36.721 20.254 38.914  1.00 38.84  ? 1220 CLR A C5  1 
HETATM 3216 C C6  . CLR U 5 .   ? 36.250 21.309 39.597  1.00 35.25  ? 1220 CLR A C6  1 
HETATM 3217 C C7  . CLR U 5 .   ? 36.626 21.623 41.026  1.00 35.83  ? 1220 CLR A C7  1 
HETATM 3218 C C8  . CLR U 5 .   ? 37.678 20.684 41.594  1.00 32.51  ? 1220 CLR A C8  1 
HETATM 3219 C C9  . CLR U 5 .   ? 37.505 19.264 41.064  1.00 31.76  ? 1220 CLR A C9  1 
HETATM 3220 C C10 . CLR U 5 .   ? 37.598 19.194 39.537  1.00 34.08  ? 1220 CLR A C10 1 
HETATM 3221 C C11 . CLR U 5 .   ? 38.483 18.313 41.759  1.00 30.22  ? 1220 CLR A C11 1 
HETATM 3222 C C12 . CLR U 5 .   ? 38.370 18.365 43.287  1.00 33.54  ? 1220 CLR A C12 1 
HETATM 3223 C C13 . CLR U 5 .   ? 38.569 19.779 43.818  1.00 29.62  ? 1220 CLR A C13 1 
HETATM 3224 C C14 . CLR U 5 .   ? 37.550 20.657 43.108  1.00 30.66  ? 1220 CLR A C14 1 
HETATM 3225 C C15 . CLR U 5 .   ? 37.633 21.985 43.851  1.00 39.85  ? 1220 CLR A C15 1 
HETATM 3226 C C16 . CLR U 5 .   ? 37.892 21.557 45.299  1.00 39.08  ? 1220 CLR A C16 1 
HETATM 3227 C C17 . CLR U 5 .   ? 38.185 20.047 45.273  1.00 28.78  ? 1220 CLR A C17 1 
HETATM 3228 C C18 . CLR U 5 .   ? 39.999 20.270 43.565  1.00 33.02  ? 1220 CLR A C18 1 
HETATM 3229 C C19 . CLR U 5 .   ? 39.017 19.429 39.030  1.00 35.36  ? 1220 CLR A C19 1 
HETATM 3230 C C20 . CLR U 5 .   ? 39.178 19.636 46.362  1.00 31.94  ? 1220 CLR A C20 1 
HETATM 3231 C C21 . CLR U 5 .   ? 39.481 18.140 46.307  1.00 30.02  ? 1220 CLR A C21 1 
HETATM 3232 C C22 . CLR U 5 .   ? 38.704 20.011 47.774  1.00 30.26  ? 1220 CLR A C22 1 
HETATM 3233 C C23 . CLR U 5 .   ? 37.304 19.491 48.114  1.00 32.89  ? 1220 CLR A C23 1 
HETATM 3234 C C24 . CLR U 5 .   ? 36.939 19.781 49.569  1.00 31.86  ? 1220 CLR A C24 1 
HETATM 3235 C C25 . CLR U 5 .   ? 35.647 19.108 50.024  1.00 34.78  ? 1220 CLR A C25 1 
HETATM 3236 C C26 . CLR U 5 .   ? 35.360 19.439 51.485  1.00 40.03  ? 1220 CLR A C26 1 
HETATM 3237 C C27 . CLR U 5 .   ? 34.455 19.506 49.162  1.00 42.30  ? 1220 CLR A C27 1 
HETATM 3238 O O1  . CLR U 5 .   ? 35.714 18.665 35.673  1.00 38.92  ? 1220 CLR A O1  1 
HETATM 3239 O O   . HOH V 6 .   ? 7.269  8.668  16.891  1.00 63.86  ? 1301 HOH A O   1 
HETATM 3240 O O   . HOH V 6 .   ? 12.149 5.341  64.969  1.00 69.06  ? 1302 HOH A O   1 
HETATM 3241 O O   . HOH V 6 .   ? 19.107 22.141 2.904   1.00 70.41  ? 1303 HOH A O   1 
HETATM 3242 O O   . HOH V 6 .   ? 12.061 30.396 23.703  1.00 67.81  ? 1304 HOH A O   1 
HETATM 3243 O O   . HOH V 6 .   ? 14.674 20.443 -18.911 1.00 90.28  ? 1305 HOH A O   1 
HETATM 3244 O O   . HOH V 6 .   ? 20.151 19.728 33.582  1.00 52.04  ? 1306 HOH A O   1 
HETATM 3245 O O   . HOH V 6 .   ? 17.010 13.663 39.955  1.00 38.26  ? 1307 HOH A O   1 
HETATM 3246 O O   . HOH V 6 .   ? 20.217 11.826 4.476   1.00 87.22  ? 1308 HOH A O   1 
HETATM 3247 O O   . HOH V 6 .   ? 27.382 8.307  60.875  1.00 67.29  ? 1309 HOH A O   1 
HETATM 3248 O O   . HOH V 6 .   ? 25.437 -1.761 68.604  1.00 61.07  ? 1310 HOH A O   1 
HETATM 3249 O O   . HOH V 6 .   ? 27.170 29.822 66.431  1.00 61.79  ? 1311 HOH A O   1 
HETATM 3250 O O   . HOH V 6 .   ? 25.654 14.986 62.552  1.00 72.64  ? 1312 HOH A O   1 
HETATM 3251 O O   . HOH V 6 .   ? 30.078 23.498 42.120  1.00 42.23  ? 1313 HOH A O   1 
HETATM 3252 O O   . HOH V 6 .   ? 36.029 14.287 70.705  1.00 73.81  ? 1314 HOH A O   1 
HETATM 3253 O O   . HOH V 6 .   ? 27.124 12.424 39.575  1.00 35.11  ? 1315 HOH A O   1 
HETATM 3254 O O   . HOH V 6 .   ? 36.810 16.679 34.131  1.00 51.52  ? 1316 HOH A O   1 
HETATM 3255 O O   . HOH V 6 .   ? 31.619 11.615 62.352  1.00 53.88  ? 1317 HOH A O   1 
HETATM 3256 O O   . HOH V 6 .   ? 15.154 15.358 63.771  1.00 30.90  ? 1318 HOH A O   1 
HETATM 3257 O O   . HOH V 6 .   ? 14.128 14.792 51.585  1.00 37.46  ? 1319 HOH A O   1 
HETATM 3258 O O   . HOH V 6 .   ? 23.240 32.918 19.737  1.00 59.16  ? 1320 HOH A O   1 
HETATM 3259 O O   . HOH V 6 .   ? 38.569 21.091 29.342  1.00 49.26  ? 1321 HOH A O   1 
HETATM 3260 O O   . HOH V 6 .   ? 17.120 22.771 62.059  1.00 40.74  ? 1322 HOH A O   1 
HETATM 3261 O O   . HOH V 6 .   ? 26.577 25.395 61.544  1.00 29.16  ? 1323 HOH A O   1 
HETATM 3262 O O   . HOH V 6 .   ? 18.231 15.226 -4.395  1.00 71.46  ? 1324 HOH A O   1 
HETATM 3263 O O   . HOH V 6 .   ? 34.661 8.123  24.630  1.00 52.49  ? 1325 HOH A O   1 
HETATM 3264 O O   . HOH V 6 .   ? 24.005 7.960  66.165  1.00 72.49  ? 1326 HOH A O   1 
HETATM 3265 O O   . HOH V 6 .   ? 10.523 19.149 69.234  1.00 46.68  ? 1327 HOH A O   1 
HETATM 3266 O O   . HOH V 6 .   ? 12.856 7.212  66.909  1.00 66.56  ? 1328 HOH A O   1 
HETATM 3267 O O   . HOH V 6 .   ? 10.077 26.046 63.751  1.00 49.00  ? 1329 HOH A O   1 
HETATM 3268 O O   . HOH V 6 .   ? 30.135 21.307 25.797  1.00 37.02  ? 1330 HOH A O   1 
HETATM 3269 O O   . HOH V 6 .   ? 30.392 17.682 24.593  1.00 54.29  ? 1331 HOH A O   1 
HETATM 3270 O O   . HOH V 6 .   ? 24.814 10.415 24.329  1.00 49.82  ? 1332 HOH A O   1 
HETATM 3271 O O   . HOH V 6 .   ? -5.896 17.530 -15.888 1.00 66.73  ? 1333 HOH A O   1 
HETATM 3272 O O   . HOH V 6 .   ? 2.591  24.973 15.786  1.00 74.35  ? 1334 HOH A O   1 
HETATM 3273 O O   . HOH V 6 .   ? 25.284 20.755 30.647  1.00 47.76  ? 1335 HOH A O   1 
HETATM 3274 O O   . HOH V 6 .   ? 24.559 22.110 20.218  1.00 77.63  ? 1336 HOH A O   1 
HETATM 3275 O O   . HOH V 6 .   ? 15.456 11.202 24.333  1.00 66.95  ? 1337 HOH A O   1 
HETATM 3276 O O   . HOH V 6 .   ? 16.963 7.334  65.174  1.00 47.07  ? 1338 HOH A O   1 
HETATM 3277 O O   . HOH V 6 .   ? 36.880 17.052 31.573  1.00 42.39  ? 1339 HOH A O   1 
HETATM 3278 O O   . HOH V 6 .   ? 19.053 19.062 -7.785  1.00 70.04  ? 1340 HOH A O   1 
HETATM 3279 O O   . HOH V 6 .   ? 31.052 17.276 66.486  1.00 51.44  ? 1341 HOH A O   1 
HETATM 3280 O O   . HOH V 6 .   ? 13.212 28.887 66.085  1.00 68.93  ? 1342 HOH A O   1 
HETATM 3281 O O   . HOH V 6 .   ? 2.170  13.778 -14.554 1.00 57.70  ? 1343 HOH A O   1 
HETATM 3282 O O   . HOH V 6 .   ? 13.580 7.023  18.987  1.00 57.03  ? 1344 HOH A O   1 
HETATM 3283 O O   . HOH V 6 .   ? 14.768 24.888 -9.765  1.00 69.22  ? 1345 HOH A O   1 
HETATM 3284 O O   . HOH V 6 .   ? 12.741 18.571 16.698  1.00 59.28  ? 1346 HOH A O   1 
HETATM 3285 O O   . HOH V 6 .   ? 16.440 14.730 70.008  1.00 63.51  ? 1347 HOH A O   1 
HETATM 3286 O O   . HOH V 6 .   ? 28.240 13.933 24.388  1.00 66.27  ? 1348 HOH A O   1 
HETATM 3287 O O   . HOH V 6 .   ? 16.163 10.523 68.584  1.00 53.80  ? 1349 HOH A O   1 
HETATM 3288 O O   . HOH V 6 .   ? 17.164 26.556 60.554  1.00 45.99  ? 1350 HOH A O   1 
HETATM 3289 O O   . HOH V 6 .   ? 38.653 22.554 31.284  1.00 49.82  ? 1351 HOH A O   1 
HETATM 3290 O O   . HOH V 6 .   ? 27.621 14.475 63.590  1.00 57.90  ? 1352 HOH A O   1 
HETATM 3291 O O   . HOH V 6 .   ? 25.029 21.077 26.614  1.00 51.72  ? 1353 HOH A O   1 
HETATM 3292 O O   . HOH V 6 .   ? 24.008 30.991 18.107  1.00 47.25  ? 1354 HOH A O   1 
HETATM 3293 O O   . HOH V 6 .   ? 26.944 18.762 31.328  1.00 62.72  ? 1355 HOH A O   1 
HETATM 3294 O O   . HOH V 6 .   ? 18.010 15.039 67.655  1.00 75.17  ? 1356 HOH A O   1 
HETATM 3295 O O   . HOH V 6 .   ? 26.963 7.149  58.674  1.00 60.39  ? 1357 HOH A O   1 
HETATM 3296 O O   . HOH V 6 .   ? 22.165 14.813 45.948  1.00 62.27  ? 1358 HOH A O   1 
HETATM 3297 O O   . HOH V 6 .   ? 18.441 16.182 -6.963  1.00 63.91  ? 1359 HOH A O   1 
HETATM 3298 O O   . HOH V 6 .   ? 15.053 9.049  66.591  1.00 43.29  ? 1360 HOH A O   1 
HETATM 3299 O O   . HOH V 6 .   ? 34.096 25.442 66.945  1.00 63.37  ? 1361 HOH A O   1 
HETATM 3300 O O   . HOH V 6 .   ? 27.735 26.359 32.872  1.00 44.79  ? 1362 HOH A O   1 
HETATM 3301 O O   . HOH V 6 .   ? 5.084  14.500 -22.316 1.00 52.47  ? 1363 HOH A O   1 
HETATM 3302 O O   . HOH V 6 .   ? 24.768 6.007  68.192  1.00 67.78  ? 1364 HOH A O   1 
HETATM 3303 O O   . HOH V 6 .   ? 10.383 10.963 -10.383 1.00 74.92  ? 1365 HOH A O   1 
HETATM 3304 O O   . HOH V 6 .   ? 38.267 19.730 34.354  1.00 53.53  ? 1366 HOH A O   1 
HETATM 3305 O O   . HOH V 6 .   ? 22.512 16.348 44.233  1.00 42.68  ? 1367 HOH A O   1 
HETATM 3306 O O   . HOH V 6 .   ? 16.967 16.584 65.526  1.00 57.37  ? 1368 HOH A O   1 
HETATM 3307 O O   . HOH V 6 .   ? 10.517 15.872 70.904  1.00 58.10  ? 1369 HOH A O   1 
HETATM 3308 O O   . HOH V 6 .   ? 21.827 29.399 65.437  1.00 43.84  ? 1370 HOH A O   1 
HETATM 3309 O O   . HOH V 6 .   ? 24.636 30.560 65.586  1.00 55.29  ? 1371 HOH A O   1 
HETATM 3310 O O   . HOH V 6 .   ? 17.442 13.010 69.012  1.00 69.87  ? 1372 HOH A O   1 
HETATM 3311 O O   . HOH V 6 .   ? 27.772 13.052 36.841  1.00 44.28  ? 1373 HOH A O   1 
HETATM 3312 O O   . HOH V 6 .   ? 39.243 18.796 31.784  1.00 64.89  ? 1374 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   . PRO A 39  ? 0.9870 0.9671 0.9819 -0.0483 0.0555  0.2378  70   PRO A N   
2    C CA  . PRO A 39  ? 0.9971 0.9715 0.9997 -0.0447 0.0573  0.2156  70   PRO A CA  
3    C C   . PRO A 39  ? 1.0618 1.0376 1.0331 -0.0434 0.0554  0.2002  70   PRO A C   
4    O O   . PRO A 39  ? 1.1334 1.1122 1.0910 -0.0431 0.0643  0.1901  70   PRO A O   
5    C CB  . PRO A 39  ? 1.0990 1.0754 1.1147 -0.0453 0.0701  0.2141  70   PRO A CB  
6    C CG  . PRO A 39  ? 1.2935 1.2790 1.2893 -0.0488 0.0771  0.2293  70   PRO A CG  
7    C CD  . PRO A 39  ? 1.2038 1.1908 1.1946 -0.0510 0.0676  0.2478  70   PRO A CD  
8    N N   . ALA A 40  ? 0.9185 0.8921 0.8808 -0.0427 0.0440  0.1986  71   ALA A N   
9    C CA  . ALA A 40  ? 1.1231 1.0970 1.0590 -0.0415 0.0406  0.1838  71   ALA A CA  
10   C C   . ALA A 40  ? 0.9303 0.8974 0.8799 -0.0376 0.0384  0.1654  71   ALA A C   
11   O O   . ALA A 40  ? 0.8765 0.8436 0.8086 -0.0363 0.0384  0.1511  71   ALA A O   
12   C CB  . ALA A 40  ? 1.0774 1.0533 0.9952 -0.0433 0.0287  0.1922  71   ALA A CB  
13   N N   . VAL A 41  ? 0.6496 0.6111 0.6298 -0.0358 0.0367  0.1655  72   VAL A N   
14   C CA  . VAL A 41  ? 0.6822 0.6379 0.6750 -0.0323 0.0354  0.1487  72   VAL A CA  
15   C C   . VAL A 41  ? 0.4564 0.4129 0.4534 -0.0316 0.0457  0.1384  72   VAL A C   
16   O O   . VAL A 41  ? 0.4898 0.4475 0.5010 -0.0330 0.0526  0.1452  72   VAL A O   
17   C CB  . VAL A 41  ? 0.6591 0.6086 0.6816 -0.0306 0.0303  0.1518  72   VAL A CB  
18   C CG1 . VAL A 41  ? 0.5724 0.5167 0.6067 -0.0273 0.0304  0.1346  72   VAL A CG1 
19   C CG2 . VAL A 41  ? 0.7584 0.7075 0.7787 -0.0308 0.0197  0.1610  72   VAL A CG2 
20   N N   . ASN A 42  ? 0.5259 0.4819 0.5125 -0.0296 0.0464  0.1228  73   ASN A N   
21   C CA  . ASN A 42  ? 0.4736 0.4305 0.4655 -0.0287 0.0551  0.1125  73   ASN A CA  
22   C C   . ASN A 42  ? 0.4744 0.4260 0.4941 -0.0270 0.0542  0.1065  73   ASN A C   
23   O O   . ASN A 42  ? 0.4594 0.4065 0.4847 -0.0249 0.0473  0.1000  73   ASN A O   
24   C CB  . ASN A 42  ? 0.4908 0.4488 0.4634 -0.0271 0.0555  0.0984  73   ASN A CB  
25   C CG  . ASN A 42  ? 0.5326 0.4928 0.5100 -0.0263 0.0648  0.0891  73   ASN A CG  
26   O OD1 . ASN A 42  ? 0.6195 0.5771 0.6171 -0.0249 0.0653  0.0831  73   ASN A OD1 
27   N ND2 . ASN A 42  ? 0.6799 0.6451 0.6389 -0.0271 0.0721  0.0877  73   ASN A ND2 
28   N N   . PRO A 43  ? 0.4611 0.4133 0.4983 -0.0281 0.0609  0.1084  74   PRO A N   
29   C CA  . PRO A 43  ? 0.4539 0.4009 0.5167 -0.0270 0.0593  0.1019  74   PRO A CA  
30   C C   . PRO A 43  ? 0.4780 0.4227 0.5388 -0.0242 0.0560  0.0859  74   PRO A C   
31   O O   . PRO A 43  ? 0.4295 0.3692 0.5039 -0.0228 0.0512  0.0806  74   PRO A O   
32   C CB  . PRO A 43  ? 0.5357 0.4856 0.6128 -0.0290 0.0677  0.1047  74   PRO A CB  
33   C CG  . PRO A 43  ? 0.5790 0.5348 0.6431 -0.0313 0.0735  0.1178  74   PRO A CG  
34   C CD  . PRO A 43  ? 0.4401 0.3981 0.4749 -0.0305 0.0704  0.1163  74   PRO A CD  
35   N N   . TRP A 44  ? 0.4208 0.3692 0.4654 -0.0234 0.0590  0.0782  75   TRP A N   
36   C CA  . TRP A 44  ? 0.4069 0.3538 0.4503 -0.0209 0.0560  0.0644  75   TRP A CA  
37   C C   . TRP A 44  ? 0.4337 0.3769 0.4710 -0.0190 0.0476  0.0619  75   TRP A C   
38   O O   . TRP A 44  ? 0.4605 0.4009 0.5051 -0.0171 0.0440  0.0533  75   TRP A O   
39   C CB  . TRP A 44  ? 0.4808 0.4324 0.5093 -0.0203 0.0611  0.0579  75   TRP A CB  
40   C CG  . TRP A 44  ? 0.4432 0.3989 0.4807 -0.0217 0.0700  0.0591  75   TRP A CG  
41   C CD1 . TRP A 44  ? 0.4890 0.4493 0.5196 -0.0236 0.0778  0.0673  75   TRP A CD1 
42   C CD2 . TRP A 44  ? 0.4518 0.4079 0.5077 -0.0214 0.0719  0.0524  75   TRP A CD2 
43   N NE1 . TRP A 44  ? 0.5102 0.4739 0.5556 -0.0244 0.0851  0.0662  75   TRP A NE1 
44   C CE2 . TRP A 44  ? 0.4689 0.4299 0.5303 -0.0231 0.0810  0.0571  75   TRP A CE2 
45   C CE3 . TRP A 44  ? 0.4958 0.4491 0.5634 -0.0201 0.0666  0.0432  75   TRP A CE3 
46   C CZ2 . TRP A 44  ? 0.5437 0.5069 0.6242 -0.0236 0.0844  0.0530  75   TRP A CZ2 
47   C CZ3 . TRP A 44  ? 0.6377 0.5931 0.7219 -0.0208 0.0693  0.0391  75   TRP A CZ3 
48   C CH2 . TRP A 44  ? 0.5530 0.5132 0.6445 -0.0225 0.0778  0.0440  75   TRP A CH2 
49   N N   . ASP A 45  ? 0.4352 0.3790 0.4592 -0.0197 0.0443  0.0698  76   ASP A N   
50   C CA  . ASP A 45  ? 0.4635 0.4042 0.4845 -0.0181 0.0361  0.0687  76   ASP A CA  
51   C C   . ASP A 45  ? 0.4097 0.3456 0.4523 -0.0172 0.0330  0.0707  76   ASP A C   
52   O O   . ASP A 45  ? 0.3815 0.3145 0.4286 -0.0150 0.0286  0.0643  76   ASP A O   
53   C CB  . ASP A 45  ? 0.4465 0.3893 0.4505 -0.0196 0.0323  0.0779  76   ASP A CB  
54   C CG  . ASP A 45  ? 0.5195 0.4661 0.5000 -0.0201 0.0341  0.0725  76   ASP A CG  
55   O OD1 . ASP A 45  ? 0.5938 0.5399 0.5718 -0.0182 0.0344  0.0606  76   ASP A OD1 
56   O OD2 . ASP A 45  ? 0.6244 0.5744 0.5890 -0.0224 0.0354  0.0802  76   ASP A OD2 
57   N N   . VAL A 46  ? 0.4021 0.3369 0.4591 -0.0189 0.0358  0.0792  77   VAL A N   
58   C CA  . VAL A 46  ? 0.4058 0.3353 0.4853 -0.0181 0.0338  0.0795  77   VAL A CA  
59   C C   . VAL A 46  ? 0.4053 0.3326 0.4943 -0.0168 0.0353  0.0661  77   VAL A C   
60   O O   . VAL A 46  ? 0.4196 0.3428 0.5182 -0.0149 0.0323  0.0603  77   VAL A O   
61   C CB  . VAL A 46  ? 0.4360 0.3648 0.5308 -0.0205 0.0367  0.0919  77   VAL A CB  
62   C CG1 . VAL A 46  ? 0.4287 0.3509 0.5487 -0.0196 0.0351  0.0903  77   VAL A CG1 
63   C CG2 . VAL A 46  ? 0.5434 0.4749 0.6278 -0.0220 0.0342  0.1066  77   VAL A CG2 
64   N N   . LEU A 47  ? 0.5064 0.4369 0.5928 -0.0178 0.0400  0.0610  78   LEU A N   
65   C CA  A LEU A 47  ? 0.4821 0.4114 0.5767 -0.0169 0.0403  0.0490  78   LEU A CA  
66   C CA  B LEU A 47  ? 0.4821 0.4114 0.5766 -0.0169 0.0403  0.0490  78   LEU A CA  
67   C C   . LEU A 47  ? 0.5125 0.4416 0.5967 -0.0142 0.0362  0.0399  78   LEU A C   
68   O O   . LEU A 47  ? 0.4274 0.3538 0.5195 -0.0130 0.0341  0.0320  78   LEU A O   
69   C CB  A LEU A 47  ? 0.5757 0.5094 0.6702 -0.0185 0.0457  0.0467  78   LEU A CB  
70   C CB  B LEU A 47  ? 0.5757 0.5095 0.6699 -0.0185 0.0457  0.0468  78   LEU A CB  
71   C CG  A LEU A 47  ? 0.5122 0.4458 0.6247 -0.0212 0.0499  0.0525  78   LEU A CG  
72   C CG  B LEU A 47  ? 0.6256 0.5584 0.7372 -0.0195 0.0467  0.0400  78   LEU A CG  
73   C CD1 A LEU A 47  ? 0.5598 0.4989 0.6717 -0.0225 0.0556  0.0505  78   LEU A CD1 
74   C CD1 B LEU A 47  ? 0.6315 0.5595 0.7632 -0.0212 0.0466  0.0448  78   LEU A CD1 
75   C CD2 A LEU A 47  ? 0.6322 0.5602 0.7647 -0.0215 0.0471  0.0469  78   LEU A CD2 
76   C CD2 B LEU A 47  ? 0.7576 0.6960 0.8692 -0.0210 0.0522  0.0400  78   LEU A CD2 
77   N N   . LEU A 48  ? 0.4399 0.3720 0.5065 -0.0135 0.0350  0.0406  79   LEU A N   
78   C CA  . LEU A 48  ? 0.4474 0.3794 0.5059 -0.0110 0.0309  0.0333  79   LEU A CA  
79   C C   . LEU A 48  ? 0.5060 0.4340 0.5709 -0.0095 0.0264  0.0350  79   LEU A C   
80   O O   . LEU A 48  ? 0.4334 0.3604 0.5003 -0.0075 0.0243  0.0279  79   LEU A O   
81   C CB  . LEU A 48  ? 0.4110 0.3463 0.4510 -0.0109 0.0303  0.0338  79   LEU A CB  
82   C CG  . LEU A 48  ? 0.4856 0.4248 0.5186 -0.0115 0.0353  0.0296  79   LEU A CG  
83   C CD1 . LEU A 48  ? 0.4313 0.3728 0.4455 -0.0117 0.0350  0.0305  79   LEU A CD1 
84   C CD2 . LEU A 48  ? 0.4897 0.4297 0.5280 -0.0100 0.0348  0.0196  79   LEU A CD2 
85   N N   . CYS A 49  ? 0.3853 0.3117 0.4543 -0.0103 0.0252  0.0450  80   CYS A N   
86   C CA  . CYS A 49  ? 0.4382 0.3610 0.5167 -0.0086 0.0215  0.0473  80   CYS A CA  
87   C C   . CYS A 49  ? 0.4058 0.3244 0.5018 -0.0077 0.0234  0.0411  80   CYS A C   
88   O O   . CYS A 49  ? 0.4007 0.3173 0.5011 -0.0054 0.0219  0.0356  80   CYS A O   
89   C CB  . CYS A 49  ? 0.5125 0.4349 0.5938 -0.0099 0.0195  0.0607  80   CYS A CB  
90   S SG  . CYS A 49  ? 0.5335 0.4523 0.6286 -0.0076 0.0145  0.0653  80   CYS A SG  
91   N N   . VAL A 50  ? 0.4350 0.3524 0.5410 -0.0097 0.0270  0.0415  81   VAL A N   
92   C CA  . VAL A 50  ? 0.4658 0.3791 0.5873 -0.0095 0.0285  0.0337  81   VAL A CA  
93   C C   . VAL A 50  ? 0.3759 0.2908 0.4900 -0.0082 0.0280  0.0214  81   VAL A C   
94   O O   . VAL A 50  ? 0.3999 0.3121 0.5193 -0.0066 0.0274  0.0141  81   VAL A O   
95   C CB  . VAL A 50  ? 0.3762 0.2887 0.5097 -0.0124 0.0318  0.0365  81   VAL A CB  
96   C CG1 . VAL A 50  ? 0.4744 0.3830 0.6216 -0.0128 0.0325  0.0261  81   VAL A CG1 
97   C CG2 . VAL A 50  ? 0.4424 0.3528 0.5867 -0.0136 0.0322  0.0497  81   VAL A CG2 
98   N N   . SER A 51  ? 0.4535 0.3733 0.5555 -0.0090 0.0285  0.0191  82   SER A N   
99   C CA  . SER A 51  ? 0.3851 0.3072 0.4805 -0.0080 0.0274  0.0092  82   SER A CA  
100  C C   . SER A 51  ? 0.4308 0.3528 0.5197 -0.0052 0.0247  0.0069  82   SER A C   
101  O O   . SER A 51  ? 0.4118 0.3332 0.5022 -0.0039 0.0241  -0.0006 82   SER A O   
102  C CB  . SER A 51  ? 0.4674 0.3948 0.5528 -0.0089 0.0286  0.0089  82   SER A CB  
103  O OG  . SER A 51  ? 0.5866 0.5166 0.6674 -0.0080 0.0270  0.0007  82   SER A OG  
104  N N   . GLY A 52  ? 0.3753 0.2981 0.4571 -0.0043 0.0230  0.0136  83   GLY A N   
105  C CA  . GLY A 52  ? 0.3583 0.2813 0.4363 -0.0018 0.0203  0.0125  83   GLY A CA  
106  C C   . GLY A 52  ? 0.3468 0.2657 0.4372 -0.0001 0.0208  0.0110  83   GLY A C   
107  O O   . GLY A 52  ? 0.3804 0.2998 0.4700 0.0020  0.0205  0.0060  83   GLY A O   
108  N N   . THR A 53  ? 0.3825 0.2975 0.4855 -0.0010 0.0222  0.0154  84   THR A N   
109  C CA  . THR A 53  ? 0.4074 0.3179 0.5249 0.0008  0.0236  0.0132  84   THR A CA  
110  C C   . THR A 53  ? 0.3668 0.2762 0.4856 0.0012  0.0260  0.0011  84   THR A C   
111  O O   . THR A 53  ? 0.3641 0.2728 0.4845 0.0036  0.0271  -0.0042 84   THR A O   
112  C CB  . THR A 53  ? 0.4423 0.3484 0.5753 -0.0005 0.0247  0.0204  84   THR A CB  
113  O OG1 . THR A 53  ? 0.4354 0.3432 0.5656 -0.0010 0.0217  0.0326  84   THR A OG1 
114  C CG2 . THR A 53  ? 0.3660 0.2667 0.5167 0.0015  0.0269  0.0169  84   THR A CG2 
115  N N   . VAL A 54  ? 0.4037 0.3134 0.5220 -0.0013 0.0267  -0.0033 85   VAL A N   
116  C CA  . VAL A 54  ? 0.3824 0.2917 0.5003 -0.0016 0.0276  -0.0148 85   VAL A CA  
117  C C   . VAL A 54  ? 0.3795 0.2937 0.4832 0.0000  0.0263  -0.0191 85   VAL A C   
118  O O   . VAL A 54  ? 0.3819 0.2958 0.4844 0.0014  0.0275  -0.0264 85   VAL A O   
119  C CB  . VAL A 54  ? 0.3643 0.2742 0.4849 -0.0050 0.0273  -0.0172 85   VAL A CB  
120  C CG1 . VAL A 54  ? 0.4679 0.3783 0.5863 -0.0059 0.0266  -0.0290 85   VAL A CG1 
121  C CG2 . VAL A 54  ? 0.4663 0.3712 0.6036 -0.0067 0.0290  -0.0124 85   VAL A CG2 
122  N N   . ILE A 55  ? 0.4360 0.3550 0.5291 -0.0001 0.0242  -0.0146 86   ILE A N   
123  C CA  . ILE A 55  ? 0.3387 0.2623 0.4204 0.0013  0.0227  -0.0174 86   ILE A CA  
124  C C   . ILE A 55  ? 0.3572 0.2801 0.4401 0.0043  0.0235  -0.0166 86   ILE A C   
125  O O   . ILE A 55  ? 0.3404 0.2652 0.4193 0.0056  0.0244  -0.0220 86   ILE A O   
126  C CB  . ILE A 55  ? 0.3126 0.2403 0.3855 0.0008  0.0206  -0.0126 86   ILE A CB  
127  C CG1 . ILE A 55  ? 0.3800 0.3096 0.4526 -0.0017 0.0208  -0.0143 86   ILE A CG1 
128  C CG2 . ILE A 55  ? 0.4293 0.3611 0.4938 0.0026  0.0189  -0.0140 86   ILE A CG2 
129  C CD1 . ILE A 55  ? 0.4574 0.3897 0.5237 -0.0023 0.0206  -0.0093 86   ILE A CD1 
130  N N   . ALA A 56  ? 0.3460 0.2667 0.4346 0.0052  0.0232  -0.0092 87   ALA A N   
131  C CA  . ALA A 56  ? 0.3270 0.2475 0.4195 0.0081  0.0238  -0.0073 87   ALA A CA  
132  C C   . ALA A 56  ? 0.3914 0.3088 0.4924 0.0096  0.0282  -0.0143 87   ALA A C   
133  O O   . ALA A 56  ? 0.3977 0.3171 0.4969 0.0118  0.0302  -0.0175 87   ALA A O   
134  C CB  . ALA A 56  ? 0.4070 0.3258 0.5061 0.0083  0.0216  0.0026  87   ALA A CB  
135  N N   . GLY A 57  ? 0.3858 0.2983 0.4965 0.0084  0.0301  -0.0169 88   GLY A N   
136  C CA  . GLY A 57  ? 0.3853 0.2939 0.5048 0.0098  0.0346  -0.0250 88   GLY A CA  
137  C C   . GLY A 57  ? 0.4666 0.3779 0.5745 0.0095  0.0359  -0.0356 88   GLY A C   
138  O O   . GLY A 57  ? 0.4288 0.3404 0.5360 0.0117  0.0398  -0.0410 88   GLY A O   
139  N N   . GLU A 58  ? 0.4324 0.3462 0.5313 0.0066  0.0328  -0.0382 89   GLU A N   
140  C CA  . GLU A 58  ? 0.3755 0.2930 0.4627 0.0058  0.0325  -0.0469 89   GLU A CA  
141  C C   . GLU A 58  ? 0.4351 0.3583 0.5121 0.0081  0.0330  -0.0450 89   GLU A C   
142  O O   . GLU A 58  ? 0.4260 0.3507 0.4977 0.0093  0.0361  -0.0513 89   GLU A O   
143  C CB  . GLU A 58  ? 0.4731 0.3936 0.5546 0.0025  0.0281  -0.0472 89   GLU A CB  
144  C CG  . GLU A 58  ? 0.4908 0.4074 0.5794 -0.0005 0.0275  -0.0535 89   GLU A CG  
145  C CD  . GLU A 58  ? 0.5495 0.4705 0.6338 -0.0035 0.0231  -0.0526 89   GLU A CD  
146  O OE1 . GLU A 58  ? 0.5513 0.4732 0.6382 -0.0041 0.0223  -0.0448 89   GLU A OE1 
147  O OE2 . GLU A 58  ? 0.5947 0.5186 0.6726 -0.0053 0.0206  -0.0596 89   GLU A OE2 
148  N N   . ASN A 59  ? 0.3449 0.2714 0.4189 0.0086  0.0301  -0.0364 90   ASN A N   
149  C CA  . ASN A 59  ? 0.4374 0.3698 0.5031 0.0103  0.0297  -0.0340 90   ASN A CA  
150  C C   . ASN A 59  ? 0.3929 0.3248 0.4649 0.0135  0.0335  -0.0313 90   ASN A C   
151  O O   . ASN A 59  ? 0.4214 0.3578 0.4879 0.0151  0.0352  -0.0315 90   ASN A O   
152  C CB  . ASN A 59  ? 0.3694 0.3050 0.4309 0.0094  0.0250  -0.0273 90   ASN A CB  
153  C CG  . ASN A 59  ? 0.3771 0.3154 0.4324 0.0067  0.0221  -0.0302 90   ASN A CG  
154  O OD1 . ASN A 59  ? 0.4126 0.3555 0.4605 0.0064  0.0210  -0.0330 90   ASN A OD1 
155  N ND2 . ASN A 59  ? 0.3575 0.2932 0.4166 0.0047  0.0208  -0.0290 90   ASN A ND2 
156  N N   . ALA A 60  ? 0.4341 0.3610 0.5187 0.0146  0.0349  -0.0279 91   ALA A N   
157  C CA  . ALA A 60  ? 0.4588 0.3852 0.5528 0.0178  0.0390  -0.0258 91   ALA A CA  
158  C C   . ALA A 60  ? 0.4785 0.4045 0.5712 0.0192  0.0456  -0.0354 91   ALA A C   
159  O O   . ALA A 60  ? 0.4446 0.3737 0.5381 0.0218  0.0500  -0.0352 91   ALA A O   
160  C CB  . ALA A 60  ? 0.4170 0.3381 0.5268 0.0184  0.0388  -0.0202 91   ALA A CB  
161  N N   . LEU A 61  ? 0.4506 0.3729 0.5415 0.0173  0.0466  -0.0442 92   LEU A N   
162  C CA  . LEU A 61  ? 0.4173 0.3390 0.5046 0.0182  0.0526  -0.0551 92   LEU A CA  
163  C C   . LEU A 61  ? 0.4663 0.3956 0.5360 0.0180  0.0526  -0.0572 92   LEU A C   
164  O O   . LEU A 61  ? 0.4169 0.3488 0.4833 0.0203  0.0588  -0.0607 92   LEU A O   
165  C CB  . LEU A 61  ? 0.4431 0.3591 0.5323 0.0155  0.0520  -0.0644 92   LEU A CB  
166  C CG  . LEU A 61  ? 0.4564 0.3709 0.5394 0.0155  0.0571  -0.0781 92   LEU A CG  
167  C CD1 . LEU A 61  ? 0.5020 0.4138 0.5957 0.0196  0.0659  -0.0808 92   LEU A CD1 
168  C CD2 . LEU A 61  ? 0.4743 0.3828 0.5614 0.0122  0.0548  -0.0868 92   LEU A CD2 
169  N N   . VAL A 62  ? 0.3826 0.3160 0.4418 0.0154  0.0462  -0.0545 93   VAL A N   
170  C CA  . VAL A 62  ? 0.3929 0.3341 0.4372 0.0150  0.0452  -0.0542 93   VAL A CA  
171  C C   . VAL A 62  ? 0.4893 0.4349 0.5360 0.0181  0.0481  -0.0464 93   VAL A C   
172  O O   . VAL A 62  ? 0.4159 0.3663 0.4551 0.0194  0.0525  -0.0480 93   VAL A O   
173  C CB  . VAL A 62  ? 0.4300 0.3744 0.4675 0.0120  0.0374  -0.0509 93   VAL A CB  
174  C CG1 . VAL A 62  ? 0.4881 0.4409 0.5129 0.0117  0.0358  -0.0487 93   VAL A CG1 
175  C CG2 . VAL A 62  ? 0.3920 0.3329 0.4289 0.0087  0.0346  -0.0584 93   VAL A CG2 
176  N N   . VAL A 63  ? 0.3833 0.3275 0.4404 0.0190  0.0454  -0.0376 94   VAL A N   
177  C CA  . VAL A 63  ? 0.4884 0.4367 0.5504 0.0216  0.0471  -0.0299 94   VAL A CA  
178  C C   . VAL A 63  ? 0.4786 0.4264 0.5475 0.0247  0.0558  -0.0328 94   VAL A C   
179  O O   . VAL A 63  ? 0.3885 0.3420 0.4549 0.0265  0.0600  -0.0306 94   VAL A O   
180  C CB  . VAL A 63  ? 0.4929 0.4390 0.5651 0.0216  0.0419  -0.0212 94   VAL A CB  
181  C CG1 . VAL A 63  ? 0.5439 0.4931 0.6251 0.0241  0.0436  -0.0138 94   VAL A CG1 
182  C CG2 . VAL A 63  ? 0.4742 0.4221 0.5385 0.0189  0.0347  -0.0183 94   VAL A CG2 
183  N N   . ALA A 64  ? 0.4024 0.3436 0.4814 0.0255  0.0592  -0.0378 95   ALA A N   
184  C CA  . ALA A 64  ? 0.3870 0.3270 0.4751 0.0289  0.0685  -0.0415 95   ALA A CA  
185  C C   . ALA A 64  ? 0.4550 0.3986 0.5282 0.0291  0.0749  -0.0509 95   ALA A C   
186  O O   . ALA A 64  ? 0.5618 0.5091 0.6368 0.0319  0.0829  -0.0511 95   ALA A O   
187  C CB  . ALA A 64  ? 0.4632 0.3947 0.5668 0.0295  0.0704  -0.0453 95   ALA A CB  
188  N N   . LEU A 65  ? 0.5069 0.4499 0.5654 0.0259  0.0716  -0.0586 96   LEU A N   
189  C CA  . LEU A 65  ? 0.4837 0.4303 0.5256 0.0254  0.0766  -0.0681 96   LEU A CA  
190  C C   . LEU A 65  ? 0.4557 0.4123 0.4860 0.0259  0.0773  -0.0611 96   LEU A C   
191  O O   . LEU A 65  ? 0.4834 0.4442 0.5076 0.0279  0.0856  -0.0640 96   LEU A O   
192  C CB  . LEU A 65  ? 0.4131 0.3576 0.4431 0.0212  0.0707  -0.0766 96   LEU A CB  
193  C CG  . LEU A 65  ? 0.4940 0.4287 0.5349 0.0203  0.0710  -0.0854 96   LEU A CG  
194  C CD1 . LEU A 65  ? 0.4863 0.4198 0.5170 0.0158  0.0639  -0.0922 96   LEU A CD1 
195  C CD2 . LEU A 65  ? 0.4475 0.3782 0.4930 0.0230  0.0814  -0.0958 96   LEU A CD2 
196  N N   . ILE A 66  ? 0.4549 0.4153 0.4826 0.0242  0.0690  -0.0519 97   ILE A N   
197  C CA  . ILE A 66  ? 0.5749 0.5445 0.5938 0.0244  0.0687  -0.0443 97   ILE A CA  
198  C C   . ILE A 66  ? 0.6176 0.5899 0.6491 0.0281  0.0753  -0.0369 97   ILE A C   
199  O O   . ILE A 66  ? 0.7715 0.7509 0.7965 0.0294  0.0811  -0.0344 97   ILE A O   
200  C CB  . ILE A 66  ? 0.5724 0.5443 0.5896 0.0219  0.0584  -0.0367 97   ILE A CB  
201  C CG1 . ILE A 66  ? 0.5173 0.4885 0.5220 0.0182  0.0526  -0.0437 97   ILE A CG1 
202  C CG2 . ILE A 66  ? 0.7576 0.7381 0.7717 0.0225  0.0580  -0.0269 97   ILE A CG2 
203  C CD1 . ILE A 66  ? 0.5638 0.5366 0.5687 0.0158  0.0432  -0.0375 97   ILE A CD1 
204  N N   . ALA A 67  ? 0.6539 0.6210 0.7040 0.0297  0.0745  -0.0327 98   ALA A N   
205  C CA  . ALA A 67  ? 0.5503 0.5202 0.6154 0.0329  0.0791  -0.0245 98   ALA A CA  
206  C C   . ALA A 67  ? 0.6384 0.6095 0.7061 0.0362  0.0916  -0.0300 98   ALA A C   
207  O O   . ALA A 67  ? 0.6220 0.5996 0.6937 0.0384  0.0977  -0.0241 98   ALA A O   
208  C CB  . ALA A 67  ? 0.4846 0.4487 0.5686 0.0335  0.0742  -0.0191 98   ALA A CB  
209  N N   . SER A 68  ? 0.7484 0.7133 0.8153 0.0365  0.0962  -0.0415 99   SER A N   
210  C CA  . SER A 68  ? 0.6024 0.5671 0.6737 0.0399  0.1089  -0.0485 99   SER A CA  
211  C C   . SER A 68  ? 0.6052 0.5747 0.6529 0.0390  0.1151  -0.0578 99   SER A C   
212  O O   . SER A 68  ? 0.6352 0.6035 0.6825 0.0413  0.1262  -0.0672 99   SER A O   
213  C CB  . SER A 68  ? 0.5311 0.4857 0.6171 0.0409  0.1111  -0.0565 99   SER A CB  
214  O OG  . SER A 68  ? 0.7278 0.6771 0.8020 0.0375  0.1055  -0.0657 99   SER A OG  
215  N N   . THR A 69  ? 0.6422 0.6173 0.6705 0.0357  0.1083  -0.0553 100  THR A N   
216  C CA  . THR A 69  ? 0.7594 0.7398 0.7628 0.0340  0.1120  -0.0631 100  THR A CA  
217  C C   . THR A 69  ? 0.7556 0.7472 0.7495 0.0336  0.1113  -0.0514 100  THR A C   
218  O O   . THR A 69  ? 0.7441 0.7386 0.7324 0.0308  0.1009  -0.0444 100  THR A O   
219  C CB  . THR A 69  ? 0.7739 0.7504 0.7631 0.0297  0.1030  -0.0718 100  THR A CB  
220  O OG1 . THR A 69  ? 0.6394 0.6051 0.6416 0.0299  0.1027  -0.0804 100  THR A OG1 
221  C CG2 . THR A 69  ? 0.6743 0.6557 0.6376 0.0277  0.1066  -0.0815 100  THR A CG2 
222  N N   . PRO A 70  ? 0.7968 0.7950 0.7899 0.0365  0.1227  -0.0488 101  PRO A N   
223  C CA  . PRO A 70  ? 0.8937 0.9030 0.8802 0.0361  0.1223  -0.0359 101  PRO A CA  
224  C C   . PRO A 70  ? 0.8138 0.8289 0.7749 0.0320  0.1153  -0.0362 101  PRO A C   
225  O O   . PRO A 70  ? 0.8586 0.8809 0.8182 0.0307  0.1098  -0.0238 101  PRO A O   
226  C CB  . PRO A 70  ? 1.0773 1.0922 1.0649 0.0399  0.1381  -0.0363 101  PRO A CB  
227  C CG  . PRO A 70  ? 0.7646 0.7706 0.7712 0.0432  0.1449  -0.0446 101  PRO A CG  
228  C CD  . PRO A 70  ? 0.8470 0.8431 0.8490 0.0406  0.1368  -0.0561 101  PRO A CD  
229  N N   . ALA A 71  ? 0.6938 0.7062 0.6363 0.0297  0.1149  -0.0498 102  ALA A N   
230  C CA  . ALA A 71  ? 0.7854 0.8039 0.7041 0.0254  0.1073  -0.0499 102  ALA A CA  
231  C C   . ALA A 71  ? 1.0451 1.0621 0.9696 0.0224  0.0925  -0.0427 102  ALA A C   
232  O O   . ALA A 71  ? 0.9371 0.9612 0.8478 0.0194  0.0853  -0.0372 102  ALA A O   
233  C CB  . ALA A 71  ? 0.7758 0.7906 0.6752 0.0232  0.1089  -0.0674 102  ALA A CB  
234  N N   . LEU A 72  ? 0.7754 0.7839 0.7200 0.0233  0.0879  -0.0422 103  LEU A N   
235  C CA  . LEU A 72  ? 0.6691 0.6753 0.6191 0.0206  0.0751  -0.0373 103  LEU A CA  
236  C C   . LEU A 72  ? 0.6058 0.6154 0.5710 0.0219  0.0720  -0.0224 103  LEU A C   
237  O O   . LEU A 72  ? 0.6965 0.7001 0.6786 0.0227  0.0681  -0.0194 103  LEU A O   
238  C CB  . LEU A 72  ? 0.6100 0.6051 0.5705 0.0201  0.0718  -0.0460 103  LEU A CB  
239  C CG  . LEU A 72  ? 0.7120 0.7021 0.6619 0.0190  0.0753  -0.0617 103  LEU A CG  
240  C CD1 . LEU A 72  ? 0.6760 0.6552 0.6400 0.0185  0.0721  -0.0683 103  LEU A CD1 
241  C CD2 . LEU A 72  ? 0.9146 0.9102 0.8423 0.0148  0.0695  -0.0660 103  LEU A CD2 
242  N N   . ARG A 73  ? 0.5187 0.5381 0.4770 0.0219  0.0736  -0.0130 104  ARG A N   
243  C CA  . ARG A 73  ? 0.6849 0.7083 0.6580 0.0231  0.0713  0.0012  104  ARG A CA  
244  C C   . ARG A 73  ? 0.6484 0.6797 0.6139 0.0204  0.0636  0.0104  104  ARG A C   
245  O O   . ARG A 73  ? 0.6071 0.6430 0.5839 0.0212  0.0624  0.0227  104  ARG A O   
246  C CB  . ARG A 73  ? 0.7152 0.7432 0.6957 0.0265  0.0825  0.0067  104  ARG A CB  
247  C CG  . ARG A 73  ? 0.7033 0.7238 0.6971 0.0296  0.0900  -0.0002 104  ARG A CG  
248  C CD  . ARG A 73  ? 0.8033 0.8167 0.8187 0.0302  0.0832  0.0036  104  ARG A CD  
249  N NE  . ARG A 73  ? 0.9631 0.9667 0.9837 0.0308  0.0839  -0.0066 104  ARG A NE  
250  C CZ  . ARG A 73  ? 0.9047 0.9051 0.9364 0.0339  0.0926  -0.0102 104  ARG A CZ  
251  N NH1 . ARG A 73  ? 1.0439 1.0500 1.0829 0.0367  0.1019  -0.0049 104  ARG A NH1 
252  N NH2 . ARG A 73  ? 0.8761 0.8675 0.9134 0.0341  0.0921  -0.0189 104  ARG A NH2 
253  N N   . THR A 74  ? 0.5396 0.5727 0.4883 0.0172  0.0581  0.0053  105  THR A N   
254  C CA  . THR A 74  ? 0.5617 0.6020 0.5059 0.0146  0.0495  0.0145  105  THR A CA  
255  C C   . THR A 74  ? 0.5228 0.5580 0.4842 0.0140  0.0401  0.0183  105  THR A C   
256  O O   . THR A 74  ? 0.5089 0.5350 0.4803 0.0148  0.0393  0.0119  105  THR A O   
257  C CB  . THR A 74  ? 0.5224 0.5662 0.4446 0.0111  0.0453  0.0075  105  THR A CB  
258  O OG1 . THR A 74  ? 0.4740 0.5087 0.3979 0.0097  0.0403  -0.0040 105  THR A OG1 
259  C CG2 . THR A 74  ? 0.5434 0.5916 0.4458 0.0115  0.0551  0.0015  105  THR A CG2 
260  N N   . PRO A 75  ? 0.4900 0.5311 0.4554 0.0127  0.0332  0.0289  106  PRO A N   
261  C CA  . PRO A 75  ? 0.4941 0.5302 0.4750 0.0121  0.0248  0.0311  106  PRO A CA  
262  C C   . PRO A 75  ? 0.4575 0.4861 0.4356 0.0105  0.0206  0.0197  106  PRO A C   
263  O O   . PRO A 75  ? 0.4300 0.4510 0.4206 0.0113  0.0189  0.0169  106  PRO A O   
264  C CB  . PRO A 75  ? 0.5371 0.5820 0.5182 0.0103  0.0183  0.0423  106  PRO A CB  
265  C CG  . PRO A 75  ? 0.5166 0.5705 0.4903 0.0111  0.0246  0.0506  106  PRO A CG  
266  C CD  . PRO A 75  ? 0.6464 0.6989 0.6041 0.0118  0.0333  0.0402  106  PRO A CD  
267  N N   . MET A 76  ? 0.4511 0.4822 0.4130 0.0080  0.0186  0.0132  107  MET A N   
268  C CA  . MET A 76  ? 0.5357 0.5600 0.4964 0.0061  0.0146  0.0027  107  MET A CA  
269  C C   . MET A 76  ? 0.4247 0.4392 0.3925 0.0082  0.0202  -0.0054 107  MET A C   
270  O O   . MET A 76  ? 0.4441 0.4519 0.4217 0.0079  0.0169  -0.0086 107  MET A O   
271  C CB  . MET A 76  ? 0.6300 0.6583 0.5714 0.0031  0.0127  -0.0043 107  MET A CB  
272  C CG  . MET A 76  ? 0.7520 0.7746 0.6936 0.0005  0.0072  -0.0142 107  MET A CG  
273  S SD  . MET A 76  ? 1.0743 1.0969 0.9947 -0.0022 0.0086  -0.0280 107  MET A SD  
274  C CE  . MET A 76  ? 0.8147 0.8510 0.7159 -0.0045 0.0052  -0.0200 107  MET A CE  
275  N N   . PHE A 77  ? 0.4205 0.4344 0.3843 0.0103  0.0289  -0.0083 108  PHE A N   
276  C CA  . PHE A 77  ? 0.4850 0.4897 0.4568 0.0122  0.0339  -0.0155 108  PHE A CA  
277  C C   . PHE A 77  ? 0.4488 0.4502 0.4384 0.0146  0.0343  -0.0085 108  PHE A C   
278  O O   . PHE A 77  ? 0.4159 0.4095 0.4147 0.0153  0.0345  -0.0123 108  PHE A O   
279  C CB  . PHE A 77  ? 0.5242 0.5291 0.4872 0.0137  0.0434  -0.0223 108  PHE A CB  
280  C CG  . PHE A 77  ? 0.5595 0.5647 0.5055 0.0110  0.0427  -0.0331 108  PHE A CG  
281  C CD1 . PHE A 77  ? 0.6944 0.6921 0.6427 0.0092  0.0391  -0.0427 108  PHE A CD1 
282  C CD2 . PHE A 77  ? 0.5335 0.5468 0.4611 0.0100  0.0453  -0.0334 108  PHE A CD2 
283  C CE1 . PHE A 77  ? 0.7378 0.7354 0.6718 0.0063  0.0376  -0.0533 108  PHE A CE1 
284  C CE2 . PHE A 77  ? 0.6198 0.6335 0.5306 0.0071  0.0436  -0.0443 108  PHE A CE2 
285  C CZ  . PHE A 77  ? 0.6323 0.6378 0.5469 0.0052  0.0394  -0.0546 108  PHE A CZ  
286  N N   . VAL A 78  ? 0.3605 0.3675 0.3554 0.0156  0.0340  0.0021  109  VAL A N   
287  C CA  . VAL A 78  ? 0.3229 0.3267 0.3347 0.0171  0.0321  0.0082  109  VAL A CA  
288  C C   . VAL A 78  ? 0.3552 0.3541 0.3719 0.0154  0.0244  0.0065  109  VAL A C   
289  O O   . VAL A 78  ? 0.3650 0.3577 0.3918 0.0161  0.0232  0.0060  109  VAL A O   
290  C CB  . VAL A 78  ? 0.4310 0.4419 0.4490 0.0180  0.0322  0.0198  109  VAL A CB  
291  C CG1 . VAL A 78  ? 0.4989 0.5059 0.5342 0.0189  0.0285  0.0250  109  VAL A CG1 
292  C CG2 . VAL A 78  ? 0.5177 0.5334 0.5325 0.0200  0.0414  0.0220  109  VAL A CG2 
293  N N   . LEU A 79  ? 0.3604 0.3624 0.3701 0.0130  0.0193  0.0056  110  LEU A N   
294  C CA  . LEU A 79  ? 0.3731 0.3712 0.3884 0.0115  0.0131  0.0039  110  LEU A CA  
295  C C   . LEU A 79  ? 0.3513 0.3423 0.3646 0.0107  0.0140  -0.0054 110  LEU A C   
296  O O   . LEU A 79  ? 0.3773 0.3628 0.3983 0.0107  0.0122  -0.0065 110  LEU A O   
297  C CB  . LEU A 79  ? 0.4044 0.4088 0.4159 0.0094  0.0073  0.0068  110  LEU A CB  
298  C CG  . LEU A 79  ? 0.4141 0.4250 0.4317 0.0100  0.0052  0.0176  110  LEU A CG  
299  C CD1 . LEU A 79  ? 0.4974 0.5161 0.5094 0.0078  0.0000  0.0215  110  LEU A CD1 
300  C CD2 . LEU A 79  ? 0.3848 0.3916 0.4180 0.0109  0.0025  0.0207  110  LEU A CD2 
301  N N   . VAL A 80  ? 0.3429 0.3338 0.3461 0.0100  0.0170  -0.0123 111  VAL A N   
302  C CA  . VAL A 80  ? 0.3957 0.3794 0.3996 0.0092  0.0181  -0.0208 111  VAL A CA  
303  C C   . VAL A 80  ? 0.3414 0.3189 0.3550 0.0116  0.0222  -0.0202 111  VAL A C   
304  O O   . VAL A 80  ? 0.4517 0.4231 0.4715 0.0111  0.0210  -0.0224 111  VAL A O   
305  C CB  . VAL A 80  ? 0.4374 0.4219 0.4294 0.0079  0.0206  -0.0293 111  VAL A CB  
306  C CG1 . VAL A 80  ? 0.4264 0.4025 0.4224 0.0074  0.0225  -0.0379 111  VAL A CG1 
307  C CG2 . VAL A 80  ? 0.4949 0.4854 0.4779 0.0049  0.0144  -0.0296 111  VAL A CG2 
308  N N   . GLY A 81  ? 0.3760 0.3554 0.3919 0.0140  0.0269  -0.0163 112  GLY A N   
309  C CA  . GLY A 81  ? 0.3716 0.3459 0.3984 0.0162  0.0299  -0.0146 112  GLY A CA  
310  C C   . GLY A 81  ? 0.3695 0.3414 0.4051 0.0160  0.0248  -0.0092 112  GLY A C   
311  O O   . GLY A 81  ? 0.3559 0.3222 0.3985 0.0164  0.0246  -0.0095 112  GLY A O   
312  N N   . SER A 82  ? 0.4029 0.3792 0.4385 0.0153  0.0205  -0.0043 113  SER A N   
313  C CA  . SER A 82  ? 0.3306 0.3043 0.3732 0.0149  0.0157  -0.0009 113  SER A CA  
314  C C   . SER A 82  ? 0.4181 0.3873 0.4589 0.0130  0.0133  -0.0058 113  SER A C   
315  O O   . SER A 82  ? 0.3810 0.3455 0.4260 0.0130  0.0121  -0.0055 113  SER A O   
316  C CB  . SER A 82  ? 0.3870 0.3660 0.4316 0.0146  0.0122  0.0046  113  SER A CB  
317  O OG  . SER A 82  ? 0.3472 0.3234 0.3979 0.0140  0.0078  0.0057  113  SER A OG  
318  N N   . LEU A 83  ? 0.3133 0.2844 0.3479 0.0114  0.0124  -0.0098 114  LEU A N   
319  C CA  . LEU A 83  ? 0.3461 0.3134 0.3808 0.0095  0.0107  -0.0139 114  LEU A CA  
320  C C   . LEU A 83  ? 0.3790 0.3401 0.4159 0.0097  0.0137  -0.0170 114  LEU A C   
321  O O   . LEU A 83  ? 0.3544 0.3114 0.3946 0.0091  0.0129  -0.0166 114  LEU A O   
322  C CB  . LEU A 83  ? 0.3514 0.3222 0.3806 0.0074  0.0089  -0.0177 114  LEU A CB  
323  C CG  . LEU A 83  ? 0.3890 0.3569 0.4203 0.0053  0.0072  -0.0217 114  LEU A CG  
324  C CD1 . LEU A 83  ? 0.3706 0.3384 0.4077 0.0051  0.0050  -0.0185 114  LEU A CD1 
325  C CD2 . LEU A 83  ? 0.4955 0.4672 0.5224 0.0030  0.0047  -0.0256 114  LEU A CD2 
326  N N   . ALA A 84  ? 0.3412 0.3016 0.3764 0.0107  0.0177  -0.0200 115  ALA A N   
327  C CA  . ALA A 84  ? 0.3692 0.3235 0.4092 0.0111  0.0208  -0.0228 115  ALA A CA  
328  C C   . ALA A 84  ? 0.3998 0.3512 0.4475 0.0126  0.0207  -0.0170 115  ALA A C   
329  O O   . ALA A 84  ? 0.3836 0.3301 0.4362 0.0121  0.0206  -0.0166 115  ALA A O   
330  C CB  . ALA A 84  ? 0.3245 0.2787 0.3623 0.0122  0.0258  -0.0279 115  ALA A CB  
331  N N   . THR A 85  ? 0.3683 0.3229 0.4178 0.0142  0.0202  -0.0120 116  THR A N   
332  C CA  . THR A 85  ? 0.3086 0.2609 0.3657 0.0151  0.0187  -0.0064 116  THR A CA  
333  C C   . THR A 85  ? 0.3916 0.3418 0.4471 0.0134  0.0140  -0.0048 116  THR A C   
334  O O   . THR A 85  ? 0.3485 0.2951 0.4075 0.0130  0.0127  -0.0025 116  THR A O   
335  C CB  . THR A 85  ? 0.3965 0.3531 0.4574 0.0168  0.0186  -0.0014 116  THR A CB  
336  O OG1 . THR A 85  ? 0.4056 0.3644 0.4678 0.0187  0.0244  -0.0027 116  THR A OG1 
337  C CG2 . THR A 85  ? 0.3851 0.3395 0.4544 0.0173  0.0154  0.0042  116  THR A CG2 
338  N N   . ALA A 86  ? 0.3574 0.3105 0.4081 0.0122  0.0116  -0.0058 117  ALA A N   
339  C CA  . ALA A 86  ? 0.3614 0.3129 0.4103 0.0108  0.0085  -0.0055 117  ALA A CA  
340  C C   . ALA A 86  ? 0.3703 0.3181 0.4179 0.0092  0.0098  -0.0078 117  ALA A C   
341  O O   . ALA A 86  ? 0.3988 0.3438 0.4459 0.0084  0.0086  -0.0056 117  ALA A O   
342  C CB  . ALA A 86  ? 0.3310 0.2864 0.3777 0.0102  0.0067  -0.0066 117  ALA A CB  
343  N N   . ASP A 87  ? 0.3365 0.2845 0.3834 0.0086  0.0121  -0.0119 118  ASP A N   
344  C CA  . ASP A 87  ? 0.3262 0.2706 0.3745 0.0070  0.0134  -0.0137 118  ASP A CA  
345  C C   . ASP A 87  ? 0.3812 0.3211 0.4349 0.0077  0.0149  -0.0109 118  ASP A C   
346  O O   . ASP A 87  ? 0.3624 0.2995 0.4176 0.0065  0.0147  -0.0083 118  ASP A O   
347  C CB  . ASP A 87  ? 0.3606 0.3059 0.4083 0.0058  0.0147  -0.0194 118  ASP A CB  
348  C CG  . ASP A 87  ? 0.6104 0.5602 0.6550 0.0046  0.0124  -0.0209 118  ASP A CG  
349  O OD1 . ASP A 87  ? 0.5343 0.4851 0.5789 0.0043  0.0110  -0.0184 118  ASP A OD1 
350  O OD2 . ASP A 87  ? 0.5786 0.5312 0.6212 0.0038  0.0117  -0.0247 118  ASP A OD2 
351  N N   . LEU A 88  ? 0.3936 0.3332 0.4511 0.0097  0.0166  -0.0107 119  LEU A N   
352  C CA  . LEU A 88  ? 0.3361 0.2720 0.4017 0.0107  0.0175  -0.0069 119  LEU A CA  
353  C C   . LEU A 88  ? 0.3859 0.3215 0.4509 0.0102  0.0134  -0.0002 119  LEU A C   
354  O O   . LEU A 88  ? 0.3630 0.2955 0.4311 0.0092  0.0127  0.0037  119  LEU A O   
355  C CB  . LEU A 88  ? 0.4033 0.3401 0.4742 0.0133  0.0204  -0.0072 119  LEU A CB  
356  C CG  . LEU A 88  ? 0.4354 0.3693 0.5178 0.0148  0.0208  -0.0018 119  LEU A CG  
357  C CD1 . LEU A 88  ? 0.3925 0.3212 0.4822 0.0140  0.0224  -0.0022 119  LEU A CD1 
358  C CD2 . LEU A 88  ? 0.4694 0.4052 0.5580 0.0176  0.0250  -0.0027 119  LEU A CD2 
359  N N   . LEU A 89  ? 0.3470 0.2856 0.4079 0.0105  0.0105  0.0014  120  LEU A N   
360  C CA  . LEU A 89  ? 0.3617 0.2999 0.4207 0.0097  0.0060  0.0063  120  LEU A CA  
361  C C   . LEU A 89  ? 0.3677 0.3046 0.4195 0.0074  0.0053  0.0061  120  LEU A C   
362  O O   . LEU A 89  ? 0.3794 0.3146 0.4296 0.0062  0.0030  0.0107  120  LEU A O   
363  C CB  . LEU A 89  ? 0.2821 0.2234 0.3393 0.0103  0.0030  0.0066  120  LEU A CB  
364  C CG  . LEU A 89  ? 0.3563 0.2995 0.4221 0.0124  0.0034  0.0091  120  LEU A CG  
365  C CD1 . LEU A 89  ? 0.3897 0.3362 0.4551 0.0127  0.0008  0.0094  120  LEU A CD1 
366  C CD2 . LEU A 89  ? 0.4182 0.3595 0.4919 0.0127  0.0008  0.0150  120  LEU A CD2 
367  N N   . ALA A 90  ? 0.3666 0.3047 0.4142 0.0066  0.0075  0.0013  121  ALA A N   
368  C CA  . ALA A 90  ? 0.3628 0.3003 0.4050 0.0046  0.0082  0.0011  121  ALA A CA  
369  C C   . ALA A 90  ? 0.4310 0.3655 0.4774 0.0035  0.0102  0.0041  121  ALA A C   
370  O O   . ALA A 90  ? 0.3887 0.3223 0.4311 0.0019  0.0099  0.0080  121  ALA A O   
371  C CB  . ALA A 90  ? 0.3230 0.2631 0.3635 0.0041  0.0100  -0.0042 121  ALA A CB  
372  N N   . GLY A 91  ? 0.3689 0.3017 0.4234 0.0042  0.0125  0.0023  122  GLY A N   
373  C CA  . GLY A 91  ? 0.3411 0.2704 0.4029 0.0034  0.0143  0.0053  122  GLY A CA  
374  C C   . GLY A 91  ? 0.3315 0.2591 0.3959 0.0035  0.0117  0.0135  122  GLY A C   
375  O O   . GLY A 91  ? 0.3878 0.3143 0.4512 0.0017  0.0114  0.0190  122  GLY A O   
376  N N   . LEU A 92  ? 0.3852 0.3130 0.4536 0.0055  0.0097  0.0150  123  LEU A N   
377  C CA  . LEU A 92  ? 0.4158 0.3428 0.4878 0.0055  0.0059  0.0234  123  LEU A CA  
378  C C   . LEU A 92  ? 0.3938 0.3225 0.4533 0.0033  0.0019  0.0272  123  LEU A C   
379  O O   . LEU A 92  ? 0.4042 0.3321 0.4635 0.0018  -0.0008 0.0348  123  LEU A O   
380  C CB  . LEU A 92  ? 0.4384 0.3667 0.5167 0.0079  0.0041  0.0240  123  LEU A CB  
381  C CG  . LEU A 92  ? 0.4143 0.3414 0.5038 0.0104  0.0090  0.0198  123  LEU A CG  
382  C CD1 . LEU A 92  ? 0.4256 0.3553 0.5199 0.0126  0.0079  0.0209  123  LEU A CD1 
383  C CD2 . LEU A 92  ? 0.4591 0.3821 0.5620 0.0107  0.0110  0.0233  123  LEU A CD2 
384  N N   . GLY A 93  ? 0.3918 0.3228 0.4407 0.0029  0.0015  0.0220  124  GLY A N   
385  C CA  . GLY A 93  ? 0.4309 0.3632 0.4670 0.0009  -0.0014 0.0236  124  GLY A CA  
386  C C   . GLY A 93  ? 0.3868 0.3187 0.4176 -0.0013 0.0014  0.0265  124  GLY A C   
387  O O   . GLY A 93  ? 0.4123 0.3447 0.4340 -0.0032 -0.0013 0.0316  124  GLY A O   
388  N N   . LEU A 94  ? 0.3308 0.2621 0.3667 -0.0013 0.0066  0.0235  125  LEU A N   
389  C CA  . LEU A 94  ? 0.2945 0.2257 0.3283 -0.0035 0.0099  0.0273  125  LEU A CA  
390  C C   . LEU A 94  ? 0.3606 0.2899 0.4005 -0.0044 0.0080  0.0372  125  LEU A C   
391  O O   . LEU A 94  ? 0.4216 0.3519 0.4545 -0.0065 0.0080  0.0439  125  LEU A O   
392  C CB  . LEU A 94  ? 0.3612 0.2920 0.4027 -0.0036 0.0150  0.0222  125  LEU A CB  
393  C CG  . LEU A 94  ? 0.4232 0.3566 0.4596 -0.0031 0.0166  0.0141  125  LEU A CG  
394  C CD1 . LEU A 94  ? 0.3523 0.2856 0.3982 -0.0034 0.0199  0.0094  125  LEU A CD1 
395  C CD2 . LEU A 94  ? 0.4187 0.3546 0.4435 -0.0046 0.0183  0.0146  125  LEU A CD2 
396  N N   . ILE A 95  ? 0.3224 0.2491 0.3758 -0.0026 0.0067  0.0386  126  ILE A N   
397  C CA  . ILE A 95  ? 0.4074 0.3323 0.4702 -0.0030 0.0044  0.0486  126  ILE A CA  
398  C C   . ILE A 95  ? 0.4086 0.3358 0.4617 -0.0041 -0.0023 0.0556  126  ILE A C   
399  O O   . ILE A 95  ? 0.3991 0.3270 0.4494 -0.0062 -0.0045 0.0653  126  ILE A O   
400  C CB  . ILE A 95  ? 0.4397 0.3615 0.5207 -0.0004 0.0051  0.0471  126  ILE A CB  
401  C CG1 . ILE A 95  ? 0.4755 0.3950 0.5643 0.0001  0.0110  0.0389  126  ILE A CG1 
402  C CG2 . ILE A 95  ? 0.5046 0.4245 0.5985 -0.0006 0.0025  0.0581  126  ILE A CG2 
403  C CD1 . ILE A 95  ? 0.4586 0.3751 0.5618 0.0028  0.0129  0.0342  126  ILE A CD1 
404  N N   . LEU A 96  ? 0.3694 0.2979 0.4175 -0.0029 -0.0059 0.0513  127  LEU A N   
405  C CA  . LEU A 96  ? 0.4791 0.4096 0.5184 -0.0042 -0.0134 0.0567  127  LEU A CA  
406  C C   . LEU A 96  ? 0.4248 0.3573 0.4445 -0.0073 -0.0138 0.0580  127  LEU A C   
407  O O   . LEU A 96  ? 0.4812 0.4152 0.4935 -0.0095 -0.0191 0.0664  127  LEU A O   
408  C CB  . LEU A 96  ? 0.4869 0.4183 0.5257 -0.0026 -0.0166 0.0506  127  LEU A CB  
409  C CG  . LEU A 96  ? 0.5607 0.4912 0.6177 0.0002  -0.0173 0.0516  127  LEU A CG  
410  C CD1 . LEU A 96  ? 0.7018 0.6338 0.7579 0.0016  -0.0190 0.0452  127  LEU A CD1 
411  C CD2 . LEU A 96  ? 0.6816 0.6121 0.7480 -0.0004 -0.0234 0.0626  127  LEU A CD2 
412  N N   . HIS A 97  ? 0.5002 0.4334 0.5113 -0.0074 -0.0082 0.0500  128  HIS A N   
413  C CA  . HIS A 97  ? 0.4444 0.3797 0.4374 -0.0099 -0.0066 0.0503  128  HIS A CA  
414  C C   . HIS A 97  ? 0.4472 0.3832 0.4397 -0.0122 -0.0052 0.0612  128  HIS A C   
415  O O   . HIS A 97  ? 0.4342 0.3725 0.4113 -0.0147 -0.0078 0.0667  128  HIS A O   
416  C CB  . HIS A 97  ? 0.4536 0.3895 0.4431 -0.0093 0.0005  0.0405  128  HIS A CB  
417  C CG  . HIS A 97  ? 0.5475 0.4858 0.5192 -0.0113 0.0036  0.0389  128  HIS A CG  
418  N ND1 . HIS A 97  ? 0.6270 0.5667 0.5961 -0.0128 0.0102  0.0425  128  HIS A ND1 
419  C CD2 . HIS A 97  ? 0.5996 0.5389 0.5555 -0.0121 0.0015  0.0336  128  HIS A CD2 
420  C CE1 . HIS A 97  ? 0.6365 0.5786 0.5882 -0.0143 0.0128  0.0397  128  HIS A CE1 
421  N NE2 . HIS A 97  ? 0.6590 0.6005 0.6021 -0.0139 0.0075  0.0336  128  HIS A NE2 
422  N N   . PHE A 98  ? 0.4228 0.3568 0.4319 -0.0114 -0.0012 0.0645  129  PHE A N   
423  C CA  . PHE A 98  ? 0.4304 0.3648 0.4431 -0.0134 -0.0002 0.0763  129  PHE A CA  
424  C C   . PHE A 98  ? 0.4210 0.3560 0.4348 -0.0144 -0.0084 0.0876  129  PHE A C   
425  O O   . PHE A 98  ? 0.4682 0.4058 0.4720 -0.0172 -0.0104 0.0978  129  PHE A O   
426  C CB  . PHE A 98  ? 0.4963 0.4276 0.5300 -0.0123 0.0050  0.0765  129  PHE A CB  
427  C CG  . PHE A 98  ? 0.4664 0.3979 0.5066 -0.0145 0.0070  0.0886  129  PHE A CG  
428  C CD1 . PHE A 98  ? 0.4503 0.3807 0.5014 -0.0149 0.0020  0.1006  129  PHE A CD1 
429  C CD2 . PHE A 98  ? 0.4402 0.3732 0.4777 -0.0163 0.0140  0.0890  129  PHE A CD2 
430  C CE1 . PHE A 98  ? 0.4447 0.3756 0.5034 -0.0170 0.0037  0.1131  129  PHE A CE1 
431  C CE2 . PHE A 98  ? 0.4500 0.3836 0.4948 -0.0185 0.0162  0.1013  129  PHE A CE2 
432  C CZ  . PHE A 98  ? 0.6124 0.5448 0.6676 -0.0189 0.0109  0.1136  129  PHE A CZ  
433  N N   . VAL A 99  ? 0.4665 0.3995 0.4930 -0.0122 -0.0133 0.0867  130  VAL A N   
434  C CA  . VAL A 99  ? 0.4335 0.3672 0.4662 -0.0128 -0.0216 0.0980  130  VAL A CA  
435  C C   . VAL A 99  ? 0.4662 0.4038 0.4763 -0.0159 -0.0287 0.1017  130  VAL A C   
436  O O   . VAL A 99  ? 0.4527 0.3927 0.4588 -0.0184 -0.0338 0.1142  130  VAL A O   
437  C CB  . VAL A 99  ? 0.5463 0.4779 0.5965 -0.0096 -0.0245 0.0945  130  VAL A CB  
438  C CG1 . VAL A 99  ? 0.4992 0.4326 0.5541 -0.0104 -0.0345 0.1051  130  VAL A CG1 
439  C CG2 . VAL A 99  ? 0.4698 0.3974 0.5427 -0.0070 -0.0183 0.0931  130  VAL A CG2 
440  N N   . PHE A 100 ? 0.4901 0.4284 0.4857 -0.0157 -0.0296 0.0909  131  PHE A N   
441  C CA  . PHE A 100 ? 0.4533 0.3945 0.4276 -0.0186 -0.0370 0.0918  131  PHE A CA  
442  C C   . PHE A 100 ? 0.5747 0.5184 0.5259 -0.0214 -0.0321 0.0908  131  PHE A C   
443  O O   . PHE A 100 ? 0.5930 0.5390 0.5230 -0.0240 -0.0370 0.0894  131  PHE A O   
444  C CB  . PHE A 100 ? 0.4588 0.3992 0.4309 -0.0173 -0.0406 0.0806  131  PHE A CB  
445  C CG  . PHE A 100 ? 0.4588 0.3982 0.4507 -0.0154 -0.0469 0.0839  131  PHE A CG  
446  C CD1 . PHE A 100 ? 0.6007 0.5422 0.5935 -0.0174 -0.0577 0.0935  131  PHE A CD1 
447  C CD2 . PHE A 100 ? 0.4925 0.4296 0.5028 -0.0117 -0.0419 0.0780  131  PHE A CD2 
448  C CE1 . PHE A 100 ? 0.6627 0.6038 0.6764 -0.0155 -0.0629 0.0971  131  PHE A CE1 
449  C CE2 . PHE A 100 ? 0.5942 0.5309 0.6232 -0.0097 -0.0464 0.0812  131  PHE A CE2 
450  C CZ  . PHE A 100 ? 0.5825 0.5213 0.6146 -0.0115 -0.0566 0.0908  131  PHE A CZ  
451  N N   . GLN A 101 ? 0.5587 0.5021 0.5139 -0.0209 -0.0225 0.0911  132  GLN A N   
452  C CA  . GLN A 101 ? 0.5247 0.4712 0.4614 -0.0236 -0.0170 0.0940  132  GLN A CA  
453  C C   . GLN A 101 ? 0.5286 0.4774 0.4679 -0.0261 -0.0188 0.1110  132  GLN A C   
454  O O   . GLN A 101 ? 0.5466 0.4994 0.4650 -0.0294 -0.0204 0.1176  132  GLN A O   
455  C CB  . GLN A 101 ? 0.5580 0.5037 0.4994 -0.0220 -0.0056 0.0855  132  GLN A CB  
456  C CG  . GLN A 101 ? 0.6975 0.6468 0.6219 -0.0244 0.0021  0.0873  132  GLN A CG  
457  C CD  . GLN A 101 ? 0.8839 0.8328 0.8129 -0.0226 0.0123  0.0767  132  GLN A CD  
458  O OE1 . GLN A 101 ? 0.9077 0.8535 0.8527 -0.0199 0.0131  0.0690  132  GLN A OE1 
459  N NE2 . GLN A 101 ? 1.0891 1.0415 1.0042 -0.0242 0.0203  0.0765  132  GLN A NE2 
460  N N   . TYR A 102 ? 0.4402 0.3865 0.4047 -0.0245 -0.0187 0.1184  133  TYR A N   
461  C CA  . TYR A 102 ? 0.4571 0.4050 0.4292 -0.0266 -0.0190 0.1349  133  TYR A CA  
462  C C   . TYR A 102 ? 0.5156 0.4630 0.5030 -0.0266 -0.0290 0.1471  133  TYR A C   
463  O O   . TYR A 102 ? 0.5020 0.4524 0.4886 -0.0292 -0.0324 0.1628  133  TYR A O   
464  C CB  . TYR A 102 ? 0.4807 0.4258 0.4731 -0.0251 -0.0094 0.1349  133  TYR A CB  
465  C CG  . TYR A 102 ? 0.4630 0.4099 0.4435 -0.0258 0.0008  0.1274  133  TYR A CG  
466  C CD1 . TYR A 102 ? 0.4516 0.4032 0.4160 -0.0290 0.0048  0.1361  133  TYR A CD1 
467  C CD2 . TYR A 102 ? 0.4662 0.4104 0.4521 -0.0233 0.0064  0.1125  133  TYR A CD2 
468  C CE1 . TYR A 102 ? 0.5090 0.4627 0.4647 -0.0294 0.0150  0.1296  133  TYR A CE1 
469  C CE2 . TYR A 102 ? 0.5417 0.4879 0.5196 -0.0238 0.0155  0.1063  133  TYR A CE2 
470  C CZ  . TYR A 102 ? 0.5185 0.4693 0.4822 -0.0268 0.0201  0.1147  133  TYR A CZ  
471  O OH  . TYR A 102 ? 0.5278 0.4811 0.4857 -0.0271 0.0300  0.1087  133  TYR A OH  
472  N N   . LEU A 103 ? 0.5296 0.4739 0.5324 -0.0237 -0.0334 0.1414  134  LEU A N   
473  C CA  . LEU A 103 ? 0.5426 0.4864 0.5649 -0.0231 -0.0419 0.1529  134  LEU A CA  
474  C C   . LEU A 103 ? 0.5135 0.4605 0.5236 -0.0248 -0.0537 0.1552  134  LEU A C   
475  O O   . LEU A 103 ? 0.5391 0.4884 0.5559 -0.0264 -0.0627 0.1695  134  LEU A O   
476  C CB  . LEU A 103 ? 0.4715 0.4101 0.5222 -0.0187 -0.0386 0.1462  134  LEU A CB  
477  C CG  . LEU A 103 ? 0.5073 0.4419 0.5732 -0.0171 -0.0280 0.1426  134  LEU A CG  
478  C CD1 . LEU A 103 ? 0.5176 0.4472 0.6094 -0.0130 -0.0257 0.1359  134  LEU A CD1 
479  C CD2 . LEU A 103 ? 0.5140 0.4495 0.5875 -0.0195 -0.0271 0.1583  134  LEU A CD2 
480  N N   . VAL A 104 ? 0.5116 0.4586 0.5057 -0.0245 -0.0545 0.1415  135  VAL A N   
481  C CA  . VAL A 104 ? 0.5185 0.4682 0.4989 -0.0266 -0.0657 0.1412  135  VAL A CA  
482  C C   . VAL A 104 ? 0.6587 0.6099 0.6081 -0.0288 -0.0630 0.1304  135  VAL A C   
483  O O   . VAL A 104 ? 0.6048 0.5541 0.5502 -0.0272 -0.0616 0.1162  135  VAL A O   
484  C CB  . VAL A 104 ? 0.6740 0.6212 0.6725 -0.0234 -0.0695 0.1342  135  VAL A CB  
485  C CG1 . VAL A 104 ? 0.7891 0.7391 0.7754 -0.0260 -0.0821 0.1342  135  VAL A CG1 
486  C CG2 . VAL A 104 ? 0.7554 0.7007 0.7864 -0.0205 -0.0695 0.1430  135  VAL A CG2 
487  N N   . PRO A 105 ? 0.6368 0.5915 0.5648 -0.0322 -0.0613 0.1365  136  PRO A N   
488  C CA  . PRO A 105 ? 0.6674 0.6234 0.5663 -0.0340 -0.0569 0.1251  136  PRO A CA  
489  C C   . PRO A 105 ? 0.7930 0.7489 0.6791 -0.0351 -0.0660 0.1154  136  PRO A C   
490  O O   . PRO A 105 ? 0.7493 0.7079 0.6273 -0.0382 -0.0781 0.1229  136  PRO A O   
491  C CB  . PRO A 105 ? 0.8051 0.7662 0.6837 -0.0381 -0.0566 0.1375  136  PRO A CB  
492  C CG  . PRO A 105 ? 0.6548 0.6160 0.5569 -0.0375 -0.0557 0.1535  136  PRO A CG  
493  C CD  . PRO A 105 ? 0.6851 0.6430 0.6150 -0.0347 -0.0629 0.1546  136  PRO A CD  
494  N N   . SER A 106 ? 0.7121 0.6648 0.5977 -0.0327 -0.0609 0.0992  137  SER A N   
495  C CA  . SER A 106 ? 0.8332 0.7849 0.7108 -0.0334 -0.0690 0.0891  137  SER A CA  
496  C C   . SER A 106 ? 0.9591 0.9086 0.8265 -0.0319 -0.0599 0.0722  137  SER A C   
497  O O   . SER A 106 ? 0.7855 0.7322 0.6691 -0.0282 -0.0520 0.0657  137  SER A O   
498  C CB  . SER A 106 ? 0.7209 0.6705 0.6248 -0.0309 -0.0758 0.0903  137  SER A CB  
499  O OG  . SER A 106 ? 0.8962 0.8451 0.7946 -0.0320 -0.0840 0.0814  137  SER A OG  
500  N N   . GLU A 107 ? 0.7012 0.6518 0.5418 -0.0349 -0.0612 0.0650  138  GLU A N   
501  C CA  . GLU A 107 ? 0.9533 0.9015 0.7861 -0.0334 -0.0533 0.0484  138  GLU A CA  
502  C C   . GLU A 107 ? 0.8681 0.8125 0.7181 -0.0309 -0.0576 0.0391  138  GLU A C   
503  O O   . GLU A 107 ? 0.6961 0.6381 0.5570 -0.0276 -0.0495 0.0301  138  GLU A O   
504  C CB  . GLU A 107 ? 0.9063 0.8561 0.7071 -0.0372 -0.0543 0.0418  138  GLU A CB  
505  C CG  . GLU A 107 ? 1.1911 1.1455 0.9724 -0.0398 -0.0482 0.0509  138  GLU A CG  
506  C CD  . GLU A 107 ? 1.4038 1.3584 1.1910 -0.0370 -0.0322 0.0486  138  GLU A CD  
507  O OE1 . GLU A 107 ? 1.2806 1.2318 1.0848 -0.0332 -0.0264 0.0390  138  GLU A OE1 
508  O OE2 . GLU A 107 ? 1.4095 1.3681 1.1848 -0.0387 -0.0258 0.0571  138  GLU A OE2 
509  N N   . THR A 108 ? 0.6706 0.6149 0.5247 -0.0326 -0.0707 0.0423  139  THR A N   
510  C CA  . THR A 108 ? 0.7829 0.7242 0.6541 -0.0306 -0.0750 0.0346  139  THR A CA  
511  C C   . THR A 108 ? 0.8073 0.7474 0.7054 -0.0259 -0.0684 0.0369  139  THR A C   
512  O O   . THR A 108 ? 0.6771 0.6149 0.5844 -0.0232 -0.0631 0.0274  139  THR A O   
513  C CB  . THR A 108 ? 0.7225 0.6648 0.5966 -0.0334 -0.0905 0.0400  139  THR A CB  
514  O OG1 . THR A 108 ? 0.9733 0.9180 0.8632 -0.0330 -0.0945 0.0555  139  THR A OG1 
515  C CG2 . THR A 108 ? 0.8553 0.7991 0.7000 -0.0386 -0.0982 0.0376  139  THR A CG2 
516  N N   . VAL A 109 ? 0.6803 0.6219 0.5915 -0.0251 -0.0686 0.0496  140  VAL A N   
517  C CA  . VAL A 109 ? 0.8060 0.7463 0.7415 -0.0209 -0.0624 0.0509  140  VAL A CA  
518  C C   . VAL A 109 ? 0.6641 0.6034 0.5981 -0.0189 -0.0495 0.0450  140  VAL A C   
519  O O   . VAL A 109 ? 0.5941 0.5321 0.5442 -0.0156 -0.0440 0.0413  140  VAL A O   
520  C CB  . VAL A 109 ? 0.7629 0.7044 0.7144 -0.0206 -0.0658 0.0651  140  VAL A CB  
521  C CG1 . VAL A 109 ? 0.7931 0.7328 0.7690 -0.0162 -0.0592 0.0646  140  VAL A CG1 
522  C CG2 . VAL A 109 ? 0.7384 0.6816 0.6935 -0.0228 -0.0794 0.0718  140  VAL A CG2 
523  N N   . SER A 110 ? 0.6830 0.6235 0.5980 -0.0208 -0.0445 0.0442  141  SER A N   
524  C CA  . SER A 110 ? 0.6418 0.5819 0.5568 -0.0190 -0.0325 0.0380  141  SER A CA  
525  C C   . SER A 110 ? 0.5815 0.5199 0.4954 -0.0174 -0.0297 0.0242  141  SER A C   
526  O O   . SER A 110 ? 0.5993 0.5370 0.5237 -0.0148 -0.0223 0.0192  141  SER A O   
527  C CB  . SER A 110 ? 0.6364 0.5790 0.5328 -0.0215 -0.0271 0.0415  141  SER A CB  
528  O OG  . SER A 110 ? 0.7802 0.7241 0.6844 -0.0220 -0.0262 0.0545  141  SER A OG  
529  N N   . LEU A 111 ? 0.5667 0.5044 0.4684 -0.0193 -0.0360 0.0180  142  LEU A N   
530  C CA  . LEU A 111 ? 0.4654 0.4009 0.3708 -0.0176 -0.0347 0.0056  142  LEU A CA  
531  C C   . LEU A 111 ? 0.5131 0.4476 0.4419 -0.0146 -0.0363 0.0064  142  LEU A C   
532  O O   . LEU A 111 ? 0.4634 0.3970 0.4015 -0.0121 -0.0306 -0.0001 142  LEU A O   
533  C CB  . LEU A 111 ? 0.5644 0.4987 0.4553 -0.0204 -0.0428 -0.0009 142  LEU A CB  
534  C CG  . LEU A 111 ? 0.5482 0.4795 0.4462 -0.0191 -0.0438 -0.0129 142  LEU A CG  
535  C CD1 . LEU A 111 ? 0.5328 0.4634 0.4297 -0.0170 -0.0324 -0.0221 142  LEU A CD1 
536  C CD2 . LEU A 111 ? 0.5393 0.4688 0.4237 -0.0224 -0.0533 -0.0191 142  LEU A CD2 
537  N N   . LEU A 112 ? 0.4734 0.4083 0.4123 -0.0148 -0.0438 0.0149  143  LEU A N   
538  C CA  . LEU A 112 ? 0.3952 0.3298 0.3558 -0.0119 -0.0443 0.0162  143  LEU A CA  
539  C C   . LEU A 112 ? 0.4276 0.3625 0.3984 -0.0091 -0.0350 0.0175  143  LEU A C   
540  O O   . LEU A 112 ? 0.4477 0.3824 0.4302 -0.0066 -0.0316 0.0134  143  LEU A O   
541  C CB  . LEU A 112 ? 0.5115 0.4470 0.4820 -0.0126 -0.0531 0.0258  143  LEU A CB  
542  C CG  . LEU A 112 ? 0.6031 0.5387 0.5653 -0.0159 -0.0645 0.0259  143  LEU A CG  
543  C CD1 . LEU A 112 ? 0.5772 0.5144 0.5522 -0.0164 -0.0728 0.0373  143  LEU A CD1 
544  C CD2 . LEU A 112 ? 0.5135 0.4474 0.4798 -0.0155 -0.0670 0.0163  143  LEU A CD2 
545  N N   . THR A 113 ? 0.4041 0.3397 0.3707 -0.0099 -0.0311 0.0234  144  THR A N   
546  C CA  . THR A 113 ? 0.4764 0.4120 0.4537 -0.0077 -0.0232 0.0243  144  THR A CA  
547  C C   . THR A 113 ? 0.4313 0.3670 0.4058 -0.0067 -0.0158 0.0153  144  THR A C   
548  O O   . THR A 113 ? 0.4132 0.3490 0.3992 -0.0045 -0.0118 0.0127  144  THR A O   
549  C CB  . THR A 113 ? 0.4634 0.3994 0.4387 -0.0091 -0.0211 0.0330  144  THR A CB  
550  O OG1 . THR A 113 ? 0.6277 0.5650 0.5845 -0.0117 -0.0194 0.0327  144  THR A OG1 
551  C CG2 . THR A 113 ? 0.4680 0.4041 0.4512 -0.0096 -0.0284 0.0431  144  THR A CG2 
552  N N   . VAL A 114 ? 0.4255 0.3616 0.3850 -0.0083 -0.0140 0.0104  145  VAL A N   
553  C CA  . VAL A 114 ? 0.4412 0.3777 0.4007 -0.0071 -0.0070 0.0021  145  VAL A CA  
554  C C   . VAL A 114 ? 0.3798 0.3156 0.3485 -0.0052 -0.0094 -0.0043 145  VAL A C   
555  O O   . VAL A 114 ? 0.3989 0.3354 0.3772 -0.0032 -0.0050 -0.0077 145  VAL A O   
556  C CB  . VAL A 114 ? 0.4975 0.4346 0.4395 -0.0090 -0.0033 -0.0020 145  VAL A CB  
557  C CG1 . VAL A 114 ? 0.4659 0.4034 0.4112 -0.0073 0.0039  -0.0108 145  VAL A CG1 
558  C CG2 . VAL A 114 ? 0.5494 0.4881 0.4836 -0.0108 0.0003  0.0058  145  VAL A CG2 
559  N N   . GLY A 115 ? 0.3763 0.3108 0.3429 -0.0059 -0.0167 -0.0054 146  GLY A N   
560  C CA  . GLY A 115 ? 0.4656 0.3996 0.4438 -0.0042 -0.0194 -0.0096 146  GLY A CA  
561  C C   . GLY A 115 ? 0.4801 0.4154 0.4739 -0.0020 -0.0187 -0.0049 146  GLY A C   
562  O O   . GLY A 115 ? 0.3647 0.3009 0.3681 -0.0001 -0.0166 -0.0079 146  GLY A O   
563  N N   . PHE A 116 ? 0.4189 0.3544 0.4156 -0.0022 -0.0203 0.0026  147  PHE A N   
564  C CA  . PHE A 116 ? 0.3523 0.2888 0.3626 0.0000  -0.0182 0.0062  147  PHE A CA  
565  C C   . PHE A 116 ? 0.3584 0.2958 0.3708 0.0012  -0.0109 0.0029  147  PHE A C   
566  O O   . PHE A 116 ? 0.3514 0.2902 0.3727 0.0030  -0.0091 0.0015  147  PHE A O   
567  C CB  . PHE A 116 ? 0.4430 0.3789 0.4562 -0.0005 -0.0202 0.0142  147  PHE A CB  
568  C CG  . PHE A 116 ? 0.4770 0.4134 0.5045 0.0018  -0.0180 0.0172  147  PHE A CG  
569  C CD1 . PHE A 116 ? 0.4732 0.4104 0.5113 0.0030  -0.0217 0.0200  147  PHE A CD1 
570  C CD2 . PHE A 116 ? 0.4481 0.3841 0.4789 0.0026  -0.0118 0.0169  147  PHE A CD2 
571  C CE1 . PHE A 116 ? 0.6646 0.6025 0.7153 0.0053  -0.0183 0.0221  147  PHE A CE1 
572  C CE2 . PHE A 116 ? 0.5265 0.4626 0.5692 0.0047  -0.0093 0.0181  147  PHE A CE2 
573  C CZ  . PHE A 116 ? 0.5129 0.4500 0.5650 0.0062  -0.0120 0.0206  147  PHE A CZ  
574  N N   . LEU A 117 ? 0.3875 0.3247 0.3920 -0.0001 -0.0068 0.0020  148  LEU A N   
575  C CA  . LEU A 117 ? 0.3572 0.2955 0.3655 0.0006  -0.0006 -0.0005 148  LEU A CA  
576  C C   . LEU A 117 ? 0.3580 0.2979 0.3682 0.0016  0.0011  -0.0069 148  LEU A C   
577  O O   . LEU A 117 ? 0.3740 0.3156 0.3916 0.0027  0.0035  -0.0085 148  LEU A O   
578  C CB  . LEU A 117 ? 0.3714 0.3096 0.3729 -0.0011 0.0035  0.0014  148  LEU A CB  
579  C CG  . LEU A 117 ? 0.4113 0.3482 0.4162 -0.0018 0.0030  0.0088  148  LEU A CG  
580  C CD1 . LEU A 117 ? 0.3441 0.2811 0.3411 -0.0040 0.0060  0.0126  148  LEU A CD1 
581  C CD2 . LEU A 117 ? 0.4360 0.3726 0.4531 -0.0004 0.0057  0.0082  148  LEU A CD2 
582  N N   . VAL A 118 ? 0.3650 0.3043 0.3691 0.0010  -0.0005 -0.0107 149  VAL A N   
583  C CA  . VAL A 118 ? 0.3755 0.3159 0.3845 0.0022  0.0007  -0.0165 149  VAL A CA  
584  C C   . VAL A 118 ? 0.3243 0.2660 0.3446 0.0039  -0.0022 -0.0151 149  VAL A C   
585  O O   . VAL A 118 ? 0.3495 0.2937 0.3772 0.0050  -0.0002 -0.0164 149  VAL A O   
586  C CB  . VAL A 118 ? 0.3917 0.3301 0.3929 0.0013  -0.0011 -0.0216 149  VAL A CB  
587  C CG1 . VAL A 118 ? 0.3903 0.3290 0.4006 0.0027  -0.0010 -0.0270 149  VAL A CG1 
588  C CG2 . VAL A 118 ? 0.3545 0.2927 0.3436 -0.0002 0.0040  -0.0237 149  VAL A CG2 
589  N N   . ALA A 119 ? 0.3721 0.3128 0.3942 0.0039  -0.0071 -0.0117 150  ALA A N   
590  C CA  . ALA A 119 ? 0.3873 0.3299 0.4202 0.0055  -0.0091 -0.0094 150  ALA A CA  
591  C C   . ALA A 119 ? 0.3991 0.3439 0.4360 0.0066  -0.0056 -0.0070 150  ALA A C   
592  O O   . ALA A 119 ? 0.3796 0.3274 0.4228 0.0077  -0.0048 -0.0069 150  ALA A O   
593  C CB  . ALA A 119 ? 0.3667 0.3082 0.4023 0.0053  -0.0146 -0.0057 150  ALA A CB  
594  N N   . SER A 120 ? 0.3872 0.3308 0.4206 0.0060  -0.0037 -0.0049 151  SER A N   
595  C CA  . SER A 120 ? 0.3850 0.3299 0.4224 0.0067  -0.0005 -0.0040 151  SER A CA  
596  C C   . SER A 120 ? 0.3950 0.3420 0.4325 0.0065  0.0026  -0.0077 151  SER A C   
597  O O   . SER A 120 ? 0.3257 0.2754 0.3669 0.0073  0.0034  -0.0082 151  SER A O   
598  C CB  . SER A 120 ? 0.4799 0.4222 0.5160 0.0060  0.0007  -0.0012 151  SER A CB  
599  O OG  . SER A 120 ? 0.4881 0.4290 0.5261 0.0062  -0.0028 0.0032  151  SER A OG  
600  N N   . PHE A 121 ? 0.3483 0.2948 0.3819 0.0053  0.0043  -0.0101 152  PHE A N   
601  C CA  . PHE A 121 ? 0.3876 0.3366 0.4240 0.0050  0.0069  -0.0130 152  PHE A CA  
602  C C   . PHE A 121 ? 0.4311 0.3831 0.4726 0.0061  0.0052  -0.0144 152  PHE A C   
603  O O   . PHE A 121 ? 0.3840 0.3393 0.4302 0.0062  0.0054  -0.0149 152  PHE A O   
604  C CB  . PHE A 121 ? 0.3453 0.2934 0.3780 0.0036  0.0103  -0.0144 152  PHE A CB  
605  C CG  . PHE A 121 ? 0.4377 0.3841 0.4693 0.0024  0.0126  -0.0122 152  PHE A CG  
606  C CD1 . PHE A 121 ? 0.5045 0.4518 0.5417 0.0021  0.0134  -0.0127 152  PHE A CD1 
607  C CD2 . PHE A 121 ? 0.4537 0.3976 0.4788 0.0013  0.0135  -0.0094 152  PHE A CD2 
608  C CE1 . PHE A 121 ? 0.4629 0.4080 0.5017 0.0009  0.0154  -0.0109 152  PHE A CE1 
609  C CE2 . PHE A 121 ? 0.4559 0.3983 0.4825 0.0001  0.0155  -0.0061 152  PHE A CE2 
610  C CZ  . PHE A 121 ? 0.6312 0.5738 0.6657 0.0000  0.0166  -0.0071 152  PHE A CZ  
611  N N   . ALA A 122 ? 0.2631 0.2138 0.3045 0.0066  0.0029  -0.0148 153  ALA A N   
612  C CA  . ALA A 122 ? 0.3765 0.3298 0.4258 0.0077  0.0009  -0.0151 153  ALA A CA  
613  C C   . ALA A 122 ? 0.3653 0.3217 0.4186 0.0086  -0.0007 -0.0112 153  ALA A C   
614  O O   . ALA A 122 ? 0.3287 0.2892 0.3875 0.0090  -0.0012 -0.0103 153  ALA A O   
615  C CB  . ALA A 122 ? 0.3446 0.2952 0.3944 0.0079  -0.0019 -0.0164 153  ALA A CB  
616  N N   . ALA A 123 ? 0.3255 0.2806 0.3763 0.0089  -0.0013 -0.0086 154  ALA A N   
617  C CA  . ALA A 123 ? 0.3470 0.3054 0.4008 0.0099  -0.0014 -0.0052 154  ALA A CA  
618  C C   . ALA A 123 ? 0.4377 0.3987 0.4889 0.0094  0.0008  -0.0066 154  ALA A C   
619  O O   . ALA A 123 ? 0.3390 0.3043 0.3915 0.0099  0.0006  -0.0048 154  ALA A O   
620  C CB  . ALA A 123 ? 0.3327 0.2890 0.3862 0.0104  -0.0016 -0.0025 154  ALA A CB  
621  N N   . SER A 124 ? 0.3536 0.3122 0.4012 0.0082  0.0028  -0.0095 155  SER A N   
622  C CA  . SER A 124 ? 0.4127 0.3732 0.4589 0.0073  0.0042  -0.0117 155  SER A CA  
623  C C   . SER A 124 ? 0.3294 0.2943 0.3791 0.0067  0.0026  -0.0123 155  SER A C   
624  O O   . SER A 124 ? 0.3181 0.2871 0.3673 0.0063  0.0013  -0.0121 155  SER A O   
625  C CB  . SER A 124 ? 0.3774 0.3340 0.4217 0.0060  0.0065  -0.0139 155  SER A CB  
626  O OG  . SER A 124 ? 0.5062 0.4641 0.5508 0.0047  0.0072  -0.0168 155  SER A OG  
627  N N   . VAL A 125 ? 0.3082 0.2725 0.3614 0.0065  0.0025  -0.0131 156  VAL A N   
628  C CA  . VAL A 125 ? 0.4643 0.4329 0.5242 0.0062  0.0012  -0.0132 156  VAL A CA  
629  C C   . VAL A 125 ? 0.3558 0.3285 0.4201 0.0073  -0.0020 -0.0093 156  VAL A C   
630  O O   . VAL A 125 ? 0.3122 0.2901 0.3801 0.0067  -0.0043 -0.0075 156  VAL A O   
631  C CB  . VAL A 125 ? 0.3710 0.3377 0.4348 0.0062  0.0032  -0.0156 156  VAL A CB  
632  C CG1 . VAL A 125 ? 0.4612 0.4324 0.5356 0.0064  0.0018  -0.0150 156  VAL A CG1 
633  C CG2 . VAL A 125 ? 0.4223 0.3866 0.4828 0.0048  0.0067  -0.0180 156  VAL A CG2 
634  N N   . SER A 126 ? 0.2931 0.2640 0.3581 0.0086  -0.0026 -0.0072 157  SER A N   
635  C CA  . SER A 126 ? 0.3355 0.3105 0.4064 0.0095  -0.0053 -0.0023 157  SER A CA  
636  C C   . SER A 126 ? 0.3674 0.3464 0.4325 0.0094  -0.0054 0.0008  157  SER A C   
637  O O   . SER A 126 ? 0.3500 0.3347 0.4182 0.0095  -0.0076 0.0054  157  SER A O   
638  C CB  . SER A 126 ? 0.3155 0.2873 0.3905 0.0106  -0.0061 -0.0011 157  SER A CB  
639  O OG  . SER A 126 ? 0.3576 0.3261 0.4263 0.0108  -0.0049 -0.0013 157  SER A OG  
640  N N   . SER A 127 ? 0.3722 0.3486 0.4292 0.0092  -0.0028 -0.0018 158  SER A N   
641  C CA  . SER A 127 ? 0.3462 0.3261 0.3967 0.0091  -0.0018 -0.0008 158  SER A CA  
642  C C   . SER A 127 ? 0.2949 0.2789 0.3421 0.0073  -0.0037 -0.0025 158  SER A C   
643  O O   . SER A 127 ? 0.3242 0.3136 0.3668 0.0069  -0.0047 -0.0001 158  SER A O   
644  C CB  . SER A 127 ? 0.3990 0.3743 0.4440 0.0094  0.0018  -0.0040 158  SER A CB  
645  O OG  . SER A 127 ? 0.3581 0.3314 0.4063 0.0110  0.0029  -0.0008 158  SER A OG  
646  N N   . LEU A 128 ? 0.3480 0.3301 0.3975 0.0059  -0.0043 -0.0063 159  LEU A N   
647  C CA  . LEU A 128 ? 0.3952 0.3816 0.4444 0.0039  -0.0072 -0.0076 159  LEU A CA  
648  C C   . LEU A 128 ? 0.3949 0.3879 0.4508 0.0040  -0.0114 -0.0017 159  LEU A C   
649  O O   . LEU A 128 ? 0.3261 0.3251 0.3787 0.0025  -0.0149 0.0002  159  LEU A O   
650  C CB  . LEU A 128 ? 0.3790 0.3624 0.4327 0.0026  -0.0065 -0.0118 159  LEU A CB  
651  C CG  . LEU A 128 ? 0.4304 0.4083 0.4790 0.0017  -0.0033 -0.0169 159  LEU A CG  
652  C CD1 . LEU A 128 ? 0.5544 0.5300 0.6095 0.0005  -0.0021 -0.0192 159  LEU A CD1 
653  C CD2 . LEU A 128 ? 0.5234 0.5031 0.5650 0.0001  -0.0045 -0.0202 159  LEU A CD2 
654  N N   . LEU A 129 ? 0.3317 0.3236 0.3972 0.0055  -0.0115 0.0011  160  LEU A N   
655  C CA  . LEU A 129 ? 0.3741 0.3717 0.4490 0.0059  -0.0152 0.0076  160  LEU A CA  
656  C C   . LEU A 129 ? 0.3275 0.3303 0.3967 0.0061  -0.0165 0.0136  160  LEU A C   
657  O O   . LEU A 129 ? 0.3180 0.3279 0.3873 0.0050  -0.0205 0.0186  160  LEU A O   
658  C CB  . LEU A 129 ? 0.3604 0.3545 0.4469 0.0077  -0.0142 0.0083  160  LEU A CB  
659  C CG  . LEU A 129 ? 0.5161 0.5148 0.6159 0.0085  -0.0177 0.0153  160  LEU A CG  
660  C CD1 . LEU A 129 ? 0.4699 0.4744 0.5774 0.0073  -0.0215 0.0177  160  LEU A CD1 
661  C CD2 . LEU A 129 ? 0.4711 0.4645 0.5818 0.0102  -0.0162 0.0134  160  LEU A CD2 
662  N N   . ALA A 130 ? 0.3759 0.3757 0.4399 0.0075  -0.0130 0.0138  161  ALA A N   
663  C CA  . ALA A 130 ? 0.3048 0.3098 0.3641 0.0079  -0.0127 0.0200  161  ALA A CA  
664  C C   . ALA A 130 ? 0.3493 0.3591 0.3949 0.0062  -0.0132 0.0185  161  ALA A C   
665  O O   . ALA A 130 ? 0.3629 0.3802 0.4048 0.0055  -0.0152 0.0249  161  ALA A O   
666  C CB  . ALA A 130 ? 0.3149 0.3156 0.3730 0.0097  -0.0083 0.0197  161  ALA A CB  
667  N N   . ILE A 131 ? 0.4029 0.4085 0.4406 0.0051  -0.0113 0.0102  162  ILE A N   
668  C CA  . ILE A 131 ? 0.3938 0.4030 0.4185 0.0030  -0.0123 0.0067  162  ILE A CA  
669  C C   . ILE A 131 ? 0.4163 0.4325 0.4431 0.0008  -0.0192 0.0104  162  ILE A C   
670  O O   . ILE A 131 ? 0.4382 0.4615 0.4553 -0.0008 -0.0218 0.0134  162  ILE A O   
671  C CB  . ILE A 131 ? 0.4743 0.4767 0.4945 0.0022  -0.0097 -0.0032 162  ILE A CB  
672  C CG1 . ILE A 131 ? 0.3585 0.3559 0.3746 0.0042  -0.0031 -0.0058 162  ILE A CG1 
673  C CG2 . ILE A 131 ? 0.5001 0.5057 0.5106 -0.0008 -0.0128 -0.0082 162  ILE A CG2 
674  C CD1 . ILE A 131 ? 0.4974 0.4871 0.5138 0.0039  -0.0004 -0.0136 162  ILE A CD1 
675  N N   . THR A 132 ? 0.3466 0.3615 0.3862 0.0004  -0.0222 0.0104  163  THR A N   
676  C CA  . THR A 132 ? 0.3565 0.3783 0.4019 -0.0017 -0.0291 0.0144  163  THR A CA  
677  C C   . THR A 132 ? 0.4053 0.4346 0.4547 -0.0011 -0.0325 0.0255  163  THR A C   
678  O O   . THR A 132 ? 0.3801 0.4175 0.4257 -0.0033 -0.0383 0.0304  163  THR A O   
679  C CB  . THR A 132 ? 0.3442 0.3627 0.4052 -0.0015 -0.0300 0.0124  163  THR A CB  
680  O OG1 . THR A 132 ? 0.4310 0.4421 0.4889 -0.0017 -0.0256 0.0036  163  THR A OG1 
681  C CG2 . THR A 132 ? 0.4272 0.4526 0.4951 -0.0041 -0.0372 0.0152  163  THR A CG2 
682  N N   . VAL A 133 ? 0.3150 0.3422 0.3731 0.0016  -0.0294 0.0301  164  VAL A N   
683  C CA  . VAL A 133 ? 0.3463 0.3804 0.4101 0.0022  -0.0320 0.0415  164  VAL A CA  
684  C C   . VAL A 133 ? 0.3602 0.4009 0.4061 0.0009  -0.0318 0.0450  164  VAL A C   
685  O O   . VAL A 133 ? 0.3402 0.3899 0.3843 -0.0007 -0.0369 0.0535  164  VAL A O   
686  C CB  . VAL A 133 ? 0.4148 0.4441 0.4904 0.0050  -0.0283 0.0443  164  VAL A CB  
687  C CG1 . VAL A 133 ? 0.3718 0.4081 0.4522 0.0056  -0.0297 0.0565  164  VAL A CG1 
688  C CG2 . VAL A 133 ? 0.3566 0.3811 0.4502 0.0060  -0.0292 0.0419  164  VAL A CG2 
689  N N   . ASP A 134 ? 0.3747 0.4113 0.4073 0.0016  -0.0255 0.0386  165  ASP A N   
690  C CA  . ASP A 134 ? 0.3838 0.4260 0.3981 0.0008  -0.0233 0.0399  165  ASP A CA  
691  C C   . ASP A 134 ? 0.4441 0.4923 0.4453 -0.0028 -0.0291 0.0377  165  ASP A C   
692  O O   . ASP A 134 ? 0.4210 0.4782 0.4116 -0.0043 -0.0316 0.0446  165  ASP A O   
693  C CB  . ASP A 134 ? 0.3712 0.4065 0.3769 0.0023  -0.0152 0.0313  165  ASP A CB  
694  C CG  . ASP A 134 ? 0.5470 0.5873 0.5346 0.0020  -0.0107 0.0313  165  ASP A CG  
695  O OD1 . ASP A 134 ? 0.3797 0.4250 0.3680 0.0034  -0.0076 0.0403  165  ASP A OD1 
696  O OD2 . ASP A 134 ? 0.4814 0.5205 0.4548 0.0004  -0.0099 0.0219  165  ASP A OD2 
697  N N   . ARG A 135 ? 0.3920 0.4356 0.3938 -0.0044 -0.0316 0.0284  166  ARG A N   
698  C CA  . ARG A 135 ? 0.4264 0.4754 0.4172 -0.0082 -0.0383 0.0256  166  ARG A CA  
699  C C   . ARG A 135 ? 0.4267 0.4852 0.4256 -0.0099 -0.0472 0.0372  166  ARG A C   
700  O O   . ARG A 135 ? 0.4294 0.4965 0.4150 -0.0128 -0.0527 0.0408  166  ARG A O   
701  C CB  . ARG A 135 ? 0.4529 0.4949 0.4474 -0.0096 -0.0393 0.0143  166  ARG A CB  
702  C CG  . ARG A 135 ? 0.7311 0.7645 0.7166 -0.0085 -0.0313 0.0034  166  ARG A CG  
703  C CD  . ARG A 135 ? 0.6367 0.6619 0.6306 -0.0091 -0.0307 -0.0056 166  ARG A CD  
704  N NE  . ARG A 135 ? 0.9260 0.9528 0.9134 -0.0130 -0.0364 -0.0125 166  ARG A NE  
705  C CZ  . ARG A 135 ? 0.8914 0.9183 0.8904 -0.0153 -0.0420 -0.0137 166  ARG A CZ  
706  N NH1 . ARG A 135 ? 1.0453 1.0705 1.0625 -0.0137 -0.0417 -0.0093 166  ARG A NH1 
707  N NH2 . ARG A 135 ? 1.0655 1.0943 1.0583 -0.0193 -0.0478 -0.0200 166  ARG A NH2 
708  N N   . TYR A 136 ? 0.3981 0.4555 0.4190 -0.0082 -0.0489 0.0432  167  TYR A N   
709  C CA  . TYR A 136 ? 0.3749 0.4411 0.4078 -0.0092 -0.0568 0.0556  167  TYR A CA  
710  C C   . TYR A 136 ? 0.3682 0.4430 0.3918 -0.0092 -0.0571 0.0672  167  TYR A C   
711  O O   . TYR A 136 ? 0.3832 0.4680 0.4003 -0.0120 -0.0645 0.0750  167  TYR A O   
712  C CB  . TYR A 136 ? 0.3628 0.4248 0.4220 -0.0065 -0.0562 0.0590  167  TYR A CB  
713  C CG  . TYR A 136 ? 0.3587 0.4287 0.4348 -0.0065 -0.0627 0.0731  167  TYR A CG  
714  C CD1 . TYR A 136 ? 0.4459 0.5221 0.5325 -0.0088 -0.0714 0.0773  167  TYR A CD1 
715  C CD2 . TYR A 136 ? 0.4707 0.5422 0.5547 -0.0042 -0.0603 0.0828  167  TYR A CD2 
716  C CE1 . TYR A 136 ? 0.5581 0.6417 0.6627 -0.0086 -0.0776 0.0911  167  TYR A CE1 
717  C CE2 . TYR A 136 ? 0.5015 0.5802 0.6034 -0.0041 -0.0662 0.0964  167  TYR A CE2 
718  C CZ  . TYR A 136 ? 0.5370 0.6217 0.6493 -0.0063 -0.0748 0.1007  167  TYR A CZ  
719  O OH  . TYR A 136 ? 0.7629 0.8547 0.8954 -0.0061 -0.0810 0.1152  167  TYR A OH  
720  N N   . LEU A 137 ? 0.3882 0.4598 0.4115 -0.0063 -0.0492 0.0692  168  LEU A N   
721  C CA  . LEU A 137 ? 0.4472 0.5273 0.4653 -0.0061 -0.0486 0.0819  168  LEU A CA  
722  C C   . LEU A 137 ? 0.4370 0.5241 0.4270 -0.0088 -0.0487 0.0805  168  LEU A C   
723  O O   . LEU A 137 ? 0.4515 0.5494 0.4347 -0.0106 -0.0529 0.0924  168  LEU A O   
724  C CB  . LEU A 137 ? 0.4034 0.4783 0.4288 -0.0025 -0.0400 0.0835  168  LEU A CB  
725  C CG  . LEU A 137 ? 0.5326 0.6025 0.5855 -0.0001 -0.0408 0.0876  168  LEU A CG  
726  C CD1 . LEU A 137 ? 0.5515 0.6148 0.6093 0.0029  -0.0328 0.0860  168  LEU A CD1 
727  C CD2 . LEU A 137 ? 0.5879 0.6663 0.6564 -0.0006 -0.0473 0.1033  168  LEU A CD2 
728  N N   . SER A 138 ? 0.4522 0.5336 0.4257 -0.0093 -0.0440 0.0663  169  SER A N   
729  C CA  . SER A 138 ? 0.4736 0.5609 0.4197 -0.0119 -0.0435 0.0627  169  SER A CA  
730  C C   . SER A 138 ? 0.4766 0.5720 0.4151 -0.0165 -0.0552 0.0649  169  SER A C   
731  O O   . SER A 138 ? 0.5565 0.6610 0.4736 -0.0192 -0.0576 0.0685  169  SER A O   
732  C CB  . SER A 138 ? 0.4780 0.5561 0.4117 -0.0112 -0.0359 0.0460  169  SER A CB  
733  O OG  . SER A 138 ? 0.5697 0.6412 0.5094 -0.0128 -0.0404 0.0355  169  SER A OG  
734  N N   . LEU A 139 ? 0.4726 0.5653 0.4280 -0.0175 -0.0626 0.0631  170  LEU A N   
735  C CA  . LEU A 139 ? 0.4327 0.5333 0.3845 -0.0221 -0.0747 0.0659  170  LEU A CA  
736  C C   . LEU A 139 ? 0.4374 0.5492 0.4003 -0.0227 -0.0825 0.0846  170  LEU A C   
737  O O   . LEU A 139 ? 0.4603 0.5825 0.4109 -0.0268 -0.0916 0.0908  170  LEU A O   
738  C CB  . LEU A 139 ? 0.4863 0.5806 0.4546 -0.0230 -0.0793 0.0573  170  LEU A CB  
739  C CG  . LEU A 139 ? 0.5153 0.6004 0.4724 -0.0239 -0.0751 0.0395  170  LEU A CG  
740  C CD1 . LEU A 139 ? 0.6019 0.6818 0.5791 -0.0246 -0.0793 0.0340  170  LEU A CD1 
741  C CD2 . LEU A 139 ? 0.6562 0.7464 0.5856 -0.0282 -0.0790 0.0330  170  LEU A CD2 
742  N N   . TYR A 140 ? 0.4598 0.5695 0.4461 -0.0191 -0.0795 0.0938  171  TYR A N   
743  C CA  . TYR A 140 ? 0.4912 0.6107 0.4927 -0.0196 -0.0868 0.1120  171  TYR A CA  
744  C C   . TYR A 140 ? 0.5868 0.7146 0.5759 -0.0192 -0.0835 0.1247  171  TYR A C   
745  O O   . TYR A 140 ? 0.5366 0.6748 0.5330 -0.0206 -0.0907 0.1413  171  TYR A O   
746  C CB  . TYR A 140 ? 0.5041 0.6175 0.5396 -0.0160 -0.0858 0.1156  171  TYR A CB  
747  C CG  . TYR A 140 ? 0.5669 0.6793 0.6197 -0.0174 -0.0936 0.1122  171  TYR A CG  
748  C CD1 . TYR A 140 ? 0.6603 0.7633 0.7127 -0.0173 -0.0905 0.0964  171  TYR A CD1 
749  C CD2 . TYR A 140 ? 0.5833 0.7048 0.6537 -0.0190 -0.1040 0.1257  171  TYR A CD2 
750  C CE1 . TYR A 140 ? 0.6175 0.7203 0.6868 -0.0187 -0.0968 0.0938  171  TYR A CE1 
751  C CE2 . TYR A 140 ? 0.6841 0.8053 0.7724 -0.0202 -0.1108 0.1230  171  TYR A CE2 
752  C CZ  . TYR A 140 ? 0.6882 0.8002 0.7758 -0.0200 -0.1068 0.1068  171  TYR A CZ  
753  O OH  . TYR A 140 ? 0.5967 0.7089 0.7033 -0.0212 -0.1127 0.1045  171  TYR A OH  
754  N N   . ASN A 141 ? 0.5881 0.7121 0.5597 -0.0176 -0.0727 0.1180  172  ASN A N   
755  C CA  . ASN A 141 ? 0.5597 0.6914 0.5197 -0.0170 -0.0674 0.1295  172  ASN A CA  
756  C C   . ASN A 141 ? 0.5523 0.6851 0.4782 -0.0184 -0.0610 0.1190  172  ASN A C   
757  O O   . ASN A 141 ? 0.6240 0.7509 0.5442 -0.0156 -0.0495 0.1120  172  ASN A O   
758  C CB  . ASN A 141 ? 0.4516 0.5771 0.4320 -0.0124 -0.0585 0.1337  172  ASN A CB  
759  C CG  . ASN A 141 ? 0.5700 0.6924 0.5845 -0.0107 -0.0638 0.1408  172  ASN A CG  
760  O OD1 . ASN A 141 ? 0.6231 0.7539 0.6511 -0.0116 -0.0705 0.1569  172  ASN A OD1 
761  N ND2 . ASN A 141 ? 0.5825 0.6928 0.6114 -0.0084 -0.0607 0.1288  172  ASN A ND2 
762  N N   . PRO A 142 ? 0.5573 0.6979 0.4606 -0.0230 -0.0686 0.1173  173  PRO A N   
763  C CA  . PRO A 142 ? 0.7830 0.9237 0.6532 -0.0246 -0.0626 0.1045  173  PRO A CA  
764  C C   . PRO A 142 ? 0.7263 0.8723 0.5814 -0.0227 -0.0512 0.1109  173  PRO A C   
765  O O   . PRO A 142 ? 0.7398 0.8834 0.5717 -0.0226 -0.0425 0.0984  173  PRO A O   
766  C CB  . PRO A 142 ? 0.7358 0.8862 0.5869 -0.0304 -0.0754 0.1055  173  PRO A CB  
767  C CG  . PRO A 142 ? 0.7951 0.9471 0.6734 -0.0315 -0.0878 0.1143  173  PRO A CG  
768  C CD  . PRO A 142 ? 0.6548 0.8045 0.5626 -0.0270 -0.0834 0.1268  173  PRO A CD  
769  N N   . LEU A 143 ? 0.4751 0.6284 0.3433 -0.0213 -0.0506 0.1299  174  LEU A N   
770  C CA  . LEU A 143 ? 0.7151 0.8737 0.5730 -0.0193 -0.0390 0.1376  174  LEU A CA  
771  C C   . LEU A 143 ? 0.5800 0.7311 0.4660 -0.0143 -0.0305 0.1416  174  LEU A C   
772  O O   . LEU A 143 ? 0.6057 0.7505 0.4876 -0.0114 -0.0185 0.1325  174  LEU A O   
773  C CB  . LEU A 143 ? 0.6654 0.8404 0.5131 -0.0222 -0.0446 0.1581  174  LEU A CB  
774  C CG  . LEU A 143 ? 0.7051 0.8884 0.5346 -0.0212 -0.0324 0.1660  174  LEU A CG  
775  C CD1 . LEU A 143 ? 0.7250 0.9249 0.5293 -0.0258 -0.0389 0.1798  174  LEU A CD1 
776  C CD2 . LEU A 143 ? 0.6297 0.8119 0.4881 -0.0171 -0.0253 0.1799  174  LEU A CD2 
777  N N   . THR A 144 ? 0.5638 0.7150 0.4796 -0.0133 -0.0367 0.1545  175  THR A N   
778  C CA  . THR A 144 ? 0.6192 0.7641 0.5615 -0.0091 -0.0298 0.1593  175  THR A CA  
779  C C   . THR A 144 ? 0.5530 0.6828 0.5053 -0.0062 -0.0247 0.1416  175  THR A C   
780  O O   . THR A 144 ? 0.5214 0.6454 0.4918 -0.0029 -0.0181 0.1431  175  THR A O   
781  C CB  . THR A 144 ? 0.7314 0.8792 0.7041 -0.0090 -0.0385 0.1756  175  THR A CB  
782  O OG1 . THR A 144 ? 0.6880 0.8301 0.6730 -0.0099 -0.0481 0.1685  175  THR A OG1 
783  C CG2 . THR A 144 ? 0.6662 0.8298 0.6308 -0.0118 -0.0437 0.1957  175  THR A CG2 
784  N N   . TYR A 145 ? 0.4840 0.6074 0.4257 -0.0076 -0.0278 0.1256  176  TYR A N   
785  C CA  . TYR A 145 ? 0.5404 0.6504 0.4876 -0.0050 -0.0217 0.1094  176  TYR A CA  
786  C C   . TYR A 145 ? 0.5479 0.6563 0.4839 -0.0027 -0.0087 0.1050  176  TYR A C   
787  O O   . TYR A 145 ? 0.4669 0.5664 0.4168 0.0005  -0.0025 0.0997  176  TYR A O   
788  C CB  . TYR A 145 ? 0.5071 0.6120 0.4425 -0.0074 -0.0266 0.0939  176  TYR A CB  
789  C CG  . TYR A 145 ? 0.4526 0.5446 0.3903 -0.0051 -0.0199 0.0776  176  TYR A CG  
790  C CD1 . TYR A 145 ? 0.5107 0.5932 0.4714 -0.0031 -0.0209 0.0745  176  TYR A CD1 
791  C CD2 . TYR A 145 ? 0.4404 0.5299 0.3575 -0.0051 -0.0122 0.0656  176  TYR A CD2 
792  C CE1 . TYR A 145 ? 0.4502 0.5217 0.4127 -0.0013 -0.0152 0.0612  176  TYR A CE1 
793  C CE2 . TYR A 145 ? 0.4521 0.5301 0.3735 -0.0030 -0.0064 0.0521  176  TYR A CE2 
794  C CZ  . TYR A 145 ? 0.5008 0.5701 0.4445 -0.0012 -0.0082 0.0507  176  TYR A CZ  
795  O OH  . TYR A 145 ? 0.4390 0.4976 0.3863 0.0006  -0.0029 0.0387  176  TYR A OH  
796  N N   . TYR A 146 ? 0.4973 0.6149 0.4086 -0.0041 -0.0044 0.1074  177  TYR A N   
797  C CA  . TYR A 146 ? 0.5857 0.7033 0.4860 -0.0018 0.0090  0.1038  177  TYR A CA  
798  C C   . TYR A 146 ? 0.5511 0.6756 0.4656 0.0001  0.0138  0.1217  177  TYR A C   
799  O O   . TYR A 146 ? 0.5161 0.6528 0.4176 -0.0013 0.0156  0.1338  177  TYR A O   
800  C CB  . TYR A 146 ? 0.5818 0.7057 0.4481 -0.0043 0.0122  0.0965  177  TYR A CB  
801  C CG  . TYR A 146 ? 0.6603 0.7767 0.5152 -0.0064 0.0071  0.0784  177  TYR A CG  
802  C CD1 . TYR A 146 ? 0.6001 0.7047 0.4573 -0.0042 0.0139  0.0619  177  TYR A CD1 
803  C CD2 . TYR A 146 ? 0.7103 0.8316 0.5549 -0.0108 -0.0052 0.0787  177  TYR A CD2 
804  C CE1 . TYR A 146 ? 0.7124 0.8100 0.5618 -0.0062 0.0092  0.0462  177  TYR A CE1 
805  C CE2 . TYR A 146 ? 0.5905 0.7050 0.4271 -0.0130 -0.0103 0.0625  177  TYR A CE2 
806  C CZ  . TYR A 146 ? 0.6599 0.7623 0.4991 -0.0107 -0.0028 0.0463  177  TYR A CZ  
807  O OH  . TYR A 146 ? 0.8135 0.9091 0.6469 -0.0130 -0.0077 0.0309  177  TYR A OH  
808  N N   . SER A 147 ? 0.4504 0.5673 0.3920 0.0031  0.0158  0.1235  178  SER A N   
809  C CA  . SER A 147 ? 0.5495 0.6714 0.5107 0.0048  0.0190  0.1401  178  SER A CA  
810  C C   . SER A 147 ? 0.5460 0.6572 0.5294 0.0082  0.0241  0.1346  178  SER A C   
811  O O   . SER A 147 ? 0.5035 0.6038 0.4886 0.0090  0.0233  0.1199  178  SER A O   
812  C CB  . SER A 147 ? 0.5533 0.6800 0.5319 0.0031  0.0078  0.1548  178  SER A CB  
813  O OG  . SER A 147 ? 0.6366 0.7526 0.6352 0.0037  0.0005  0.1478  178  SER A OG  
814  N N   . ARG A 148 ? 0.5373 0.6520 0.5383 0.0099  0.0290  0.1473  179  ARG A N   
815  C CA  A ARG A 148 ? 0.5047 0.6102 0.5284 0.0127  0.0325  0.1436  179  ARG A CA  
816  C CA  B ARG A 148 ? 0.5048 0.6103 0.5287 0.0127  0.0325  0.1437  179  ARG A CA  
817  C C   . ARG A 148 ? 0.4702 0.5660 0.5142 0.0125  0.0224  0.1396  179  ARG A C   
818  O O   . ARG A 148 ? 0.5173 0.6025 0.5698 0.0140  0.0230  0.1287  179  ARG A O   
819  C CB  A ARG A 148 ? 0.5747 0.6867 0.6153 0.0141  0.0387  0.1591  179  ARG A CB  
820  C CB  B ARG A 148 ? 0.5744 0.6866 0.6154 0.0140  0.0384  0.1596  179  ARG A CB  
821  C CG  A ARG A 148 ? 0.7184 0.8352 0.7465 0.0158  0.0525  0.1581  179  ARG A CG  
822  C CG  B ARG A 148 ? 0.7417 0.8643 0.7641 0.0145  0.0503  0.1644  179  ARG A CG  
823  C CD  A ARG A 148 ? 0.8330 0.9558 0.8826 0.0173  0.0589  0.1736  179  ARG A CD  
824  C CD  B ARG A 148 ? 0.8537 0.9843 0.8951 0.0154  0.0558  0.1826  179  ARG A CD  
825  N NE  A ARG A 148 ? 0.8597 0.9958 0.9060 0.0156  0.0590  0.1919  179  ARG A NE  
826  N NE  B ARG A 148 ? 0.8148 0.9372 0.8855 0.0176  0.0567  0.1818  179  ARG A NE  
827  C CZ  A ARG A 148 ? 0.6133 0.7610 0.6424 0.0156  0.0694  0.1995  179  ARG A CZ  
828  C CZ  B ARG A 148 ? 0.8031 0.9214 0.8770 0.0201  0.0656  0.1744  179  ARG A CZ  
829  N NH1 A ARG A 148 ? 0.6560 0.8036 0.6700 0.0175  0.0814  0.1895  179  ARG A NH1 
830  N NH1 B ARG A 148 ? 0.7539 0.8748 0.8048 0.0211  0.0757  0.1661  179  ARG A NH1 
831  N NH2 A ARG A 148 ? 0.5797 0.7397 0.6072 0.0137  0.0680  0.2177  179  ARG A NH2 
832  N NH2 B ARG A 148 ? 0.7103 0.8218 0.8122 0.0215  0.0642  0.1751  179  ARG A NH2 
833  N N   . ARG A 149 ? 0.4897 0.5892 0.5414 0.0107  0.0134  0.1484  180  ARG A N   
834  C CA  . ARG A 149 ? 0.4739 0.5648 0.5457 0.0108  0.0048  0.1448  180  ARG A CA  
835  C C   . ARG A 149 ? 0.6103 0.6916 0.6719 0.0107  0.0028  0.1269  180  ARG A C   
836  O O   . ARG A 149 ? 0.5153 0.5867 0.5914 0.0117  0.0004  0.1196  180  ARG A O   
837  C CB  . ARG A 149 ? 0.4235 0.5212 0.5034 0.0088  -0.0041 0.1569  180  ARG A CB  
838  C CG  . ARG A 149 ? 0.7670 0.8569 0.8730 0.0093  -0.0116 0.1557  180  ARG A CG  
839  C CD  . ARG A 149 ? 0.9579 1.0538 1.0691 0.0074  -0.0207 0.1641  180  ARG A CD  
840  N NE  . ARG A 149 ? 1.1704 1.2581 1.3062 0.0082  -0.0268 0.1608  180  ARG A NE  
841  C CZ  . ARG A 149 ? 1.2492 1.3392 1.3944 0.0071  -0.0347 0.1646  180  ARG A CZ  
842  N NH1 . ARG A 149 ? 1.4085 1.5088 1.5407 0.0048  -0.0391 0.1726  180  ARG A NH1 
843  N NH2 . ARG A 149 ? 1.3266 1.4085 1.4951 0.0082  -0.0384 0.1600  180  ARG A NH2 
844  N N   . THR A 150 ? 0.4564 0.5403 0.4929 0.0092  0.0037  0.1197  181  THR A N   
845  C CA  . THR A 150 ? 0.4812 0.5563 0.5098 0.0089  0.0017  0.1036  181  THR A CA  
846  C C   . THR A 150 ? 0.4344 0.5002 0.4659 0.0112  0.0085  0.0934  181  THR A C   
847  O O   . THR A 150 ? 0.3956 0.4520 0.4342 0.0117  0.0059  0.0840  181  THR A O   
848  C CB  . THR A 150 ? 0.4442 0.5240 0.4464 0.0065  0.0010  0.0976  181  THR A CB  
849  O OG1 . THR A 150 ? 0.4294 0.5175 0.4303 0.0040  -0.0074 0.1070  181  THR A OG1 
850  C CG2 . THR A 150 ? 0.4330 0.5032 0.4292 0.0062  -0.0002 0.0810  181  THR A CG2 
851  N N   . LEU A 151 ? 0.4537 0.5225 0.4805 0.0127  0.0174  0.0957  182  LEU A N   
852  C CA  . LEU A 151 ? 0.5063 0.5669 0.5385 0.0150  0.0234  0.0873  182  LEU A CA  
853  C C   . LEU A 151 ? 0.3673 0.4222 0.4248 0.0162  0.0203  0.0912  182  LEU A C   
854  O O   . LEU A 151 ? 0.3704 0.4159 0.4341 0.0170  0.0192  0.0823  182  LEU A O   
855  C CB  . LEU A 151 ? 0.5474 0.6132 0.5707 0.0165  0.0343  0.0892  182  LEU A CB  
856  C CG  . LEU A 151 ? 0.5839 0.6419 0.6141 0.0190  0.0406  0.0810  182  LEU A CG  
857  C CD1 . LEU A 151 ? 0.5886 0.6379 0.6084 0.0186  0.0393  0.0656  182  LEU A CD1 
858  C CD2 . LEU A 151 ? 0.8403 0.9044 0.8656 0.0209  0.0523  0.0842  182  LEU A CD2 
859  N N   . LEU A 152 ? 0.3532 0.4136 0.4257 0.0162  0.0186  0.1046  183  LEU A N   
860  C CA  . LEU A 152 ? 0.4119 0.4666 0.5091 0.0168  0.0141  0.1073  183  LEU A CA  
861  C C   . LEU A 152 ? 0.3826 0.4291 0.4830 0.0159  0.0064  0.0985  183  LEU A C   
862  O O   . LEU A 152 ? 0.3376 0.3755 0.4487 0.0166  0.0046  0.0921  183  LEU A O   
863  C CB  . LEU A 152 ? 0.3650 0.4271 0.4785 0.0164  0.0123  0.1233  183  LEU A CB  
864  C CG  . LEU A 152 ? 0.4491 0.5052 0.5897 0.0166  0.0065  0.1261  183  LEU A CG  
865  C CD1 . LEU A 152 ? 0.5143 0.5635 0.6649 0.0180  0.0094  0.1208  183  LEU A CD1 
866  C CD2 . LEU A 152 ? 0.3991 0.4634 0.5563 0.0161  0.0051  0.1429  183  LEU A CD2 
867  N N   . GLY A 153 ? 0.3932 0.4430 0.4844 0.0144  0.0020  0.0983  184  GLY A N   
868  C CA  . GLY A 153 ? 0.3132 0.3565 0.4099 0.0137  -0.0046 0.0912  184  GLY A CA  
869  C C   . GLY A 153 ? 0.4160 0.4503 0.5042 0.0140  -0.0031 0.0769  184  GLY A C   
870  O O   . GLY A 153 ? 0.3984 0.4252 0.4961 0.0142  -0.0063 0.0710  184  GLY A O   
871  N N   . VAL A 154 ? 0.3435 0.3784 0.4140 0.0140  0.0021  0.0711  185  VAL A N   
872  C CA  A VAL A 154 ? 0.3544 0.3809 0.4185 0.0144  0.0037  0.0587  185  VAL A CA  
873  C CA  B VAL A 154 ? 0.3550 0.3813 0.4191 0.0143  0.0037  0.0587  185  VAL A CA  
874  C C   . VAL A 154 ? 0.3740 0.3941 0.4502 0.0160  0.0057  0.0576  185  VAL A C   
875  O O   . VAL A 154 ? 0.4223 0.4345 0.5016 0.0160  0.0037  0.0503  185  VAL A O   
876  C CB  A VAL A 154 ? 0.3948 0.4233 0.4392 0.0141  0.0089  0.0528  185  VAL A CB  
877  C CB  B VAL A 154 ? 0.3946 0.4228 0.4389 0.0140  0.0087  0.0525  185  VAL A CB  
878  C CG1 A VAL A 154 ? 0.4578 0.4774 0.4989 0.0147  0.0115  0.0416  185  VAL A CG1 
879  C CG1 B VAL A 154 ? 0.4616 0.4955 0.5019 0.0153  0.0160  0.0581  185  VAL A CG1 
880  C CG2 A VAL A 154 ? 0.3652 0.3989 0.3970 0.0117  0.0049  0.0522  185  VAL A CG2 
881  C CG2 B VAL A 154 ? 0.4590 0.4781 0.4999 0.0144  0.0105  0.0409  185  VAL A CG2 
882  N N   . HIS A 155 ? 0.3692 0.3931 0.4525 0.0172  0.0095  0.0653  186  HIS A N   
883  C CA  . HIS A 155 ? 0.4149 0.4336 0.5117 0.0184  0.0104  0.0652  186  HIS A CA  
884  C C   . HIS A 155 ? 0.3554 0.3688 0.4673 0.0178  0.0034  0.0649  186  HIS A C   
885  O O   . HIS A 155 ? 0.3256 0.3315 0.4412 0.0178  0.0015  0.0586  186  HIS A O   
886  C CB  . HIS A 155 ? 0.4687 0.4939 0.5735 0.0196  0.0155  0.0752  186  HIS A CB  
887  C CG  . HIS A 155 ? 0.3973 0.4267 0.4883 0.0207  0.0240  0.0738  186  HIS A CG  
888  N ND1 . HIS A 155 ? 0.4395 0.4773 0.5321 0.0216  0.0305  0.0829  186  HIS A ND1 
889  C CD2 . HIS A 155 ? 0.3952 0.4214 0.4713 0.0210  0.0277  0.0639  186  HIS A CD2 
890  C CE1 . HIS A 155 ? 0.5180 0.5574 0.5961 0.0226  0.0383  0.0778  186  HIS A CE1 
891  N NE2 . HIS A 155 ? 0.4514 0.4836 0.5200 0.0222  0.0364  0.0660  186  HIS A NE2 
892  N N   . LEU A 156 ? 0.3147 0.3320 0.4357 0.0171  -0.0004 0.0720  187  LEU A N   
893  C CA  . LEU A 156 ? 0.3625 0.3746 0.4995 0.0167  -0.0063 0.0710  187  LEU A CA  
894  C C   . LEU A 156 ? 0.4283 0.4342 0.5582 0.0160  -0.0093 0.0605  187  LEU A C   
895  O O   . LEU A 156 ? 0.3747 0.3733 0.5108 0.0159  -0.0120 0.0544  187  LEU A O   
896  C CB  . LEU A 156 ? 0.3324 0.3503 0.4832 0.0164  -0.0092 0.0817  187  LEU A CB  
897  C CG  . LEU A 156 ? 0.3791 0.4040 0.5396 0.0169  -0.0062 0.0941  187  LEU A CG  
898  C CD1 . LEU A 156 ? 0.3358 0.3663 0.5112 0.0163  -0.0097 0.1054  187  LEU A CD1 
899  C CD2 . LEU A 156 ? 0.4564 0.4766 0.6307 0.0174  -0.0059 0.0937  187  LEU A CD2 
900  N N   . LEU A 157 ? 0.3401 0.3490 0.4566 0.0154  -0.0087 0.0582  188  LEU A N   
901  C CA  . LEU A 157 ? 0.2568 0.2607 0.3684 0.0147  -0.0109 0.0492  188  LEU A CA  
902  C C   . LEU A 157 ? 0.3848 0.3815 0.4880 0.0148  -0.0087 0.0400  188  LEU A C   
903  O O   . LEU A 157 ? 0.3396 0.3302 0.4448 0.0145  -0.0106 0.0335  188  LEU A O   
904  C CB  . LEU A 157 ? 0.3312 0.3406 0.4318 0.0136  -0.0113 0.0495  188  LEU A CB  
905  C CG  . LEU A 157 ? 0.5022 0.5077 0.5997 0.0128  -0.0133 0.0413  188  LEU A CG  
906  C CD1 . LEU A 157 ? 0.4164 0.4182 0.5300 0.0131  -0.0165 0.0405  188  LEU A CD1 
907  C CD2 . LEU A 157 ? 0.4601 0.4722 0.5492 0.0113  -0.0151 0.0429  188  LEU A CD2 
908  N N   . LEU A 158 ? 0.3110 0.3085 0.4052 0.0153  -0.0044 0.0396  189  LEU A N   
909  C CA  . LEU A 158 ? 0.3658 0.3568 0.4542 0.0155  -0.0027 0.0324  189  LEU A CA  
910  C C   . LEU A 158 ? 0.3812 0.3674 0.4804 0.0158  -0.0049 0.0327  189  LEU A C   
911  O O   . LEU A 158 ? 0.3570 0.3370 0.4539 0.0153  -0.0064 0.0267  189  LEU A O   
912  C CB  . LEU A 158 ? 0.2894 0.2824 0.3680 0.0162  0.0028  0.0318  189  LEU A CB  
913  C CG  . LEU A 158 ? 0.3911 0.3866 0.4558 0.0153  0.0046  0.0276  189  LEU A CG  
914  C CD1 . LEU A 158 ? 0.4369 0.4326 0.4937 0.0163  0.0107  0.0251  189  LEU A CD1 
915  C CD2 . LEU A 158 ? 0.3882 0.3787 0.4494 0.0140  0.0019  0.0204  189  LEU A CD2 
916  N N   . ALA A 159 ? 0.3495 0.3387 0.4604 0.0165  -0.0053 0.0400  190  ALA A N   
917  C CA  . ALA A 159 ? 0.3445 0.3291 0.4673 0.0163  -0.0089 0.0402  190  ALA A CA  
918  C C   . ALA A 159 ? 0.3202 0.2997 0.4464 0.0152  -0.0138 0.0346  190  ALA A C   
919  O O   . ALA A 159 ? 0.3397 0.3132 0.4660 0.0145  -0.0166 0.0294  190  ALA A O   
920  C CB  . ALA A 159 ? 0.3599 0.3492 0.4979 0.0168  -0.0089 0.0496  190  ALA A CB  
921  N N   . ALA A 160 ? 0.3175 0.2994 0.4461 0.0151  -0.0147 0.0356  191  ALA A N   
922  C CA  . ALA A 160 ? 0.3250 0.3023 0.4588 0.0145  -0.0181 0.0299  191  ALA A CA  
923  C C   . ALA A 160 ? 0.3763 0.3493 0.4965 0.0139  -0.0167 0.0210  191  ALA A C   
924  O O   . ALA A 160 ? 0.3865 0.3537 0.5064 0.0133  -0.0185 0.0145  191  ALA A O   
925  C CB  . ALA A 160 ? 0.3220 0.3035 0.4658 0.0147  -0.0193 0.0345  191  ALA A CB  
926  N N   . THR A 161 ? 0.3020 0.2779 0.4108 0.0139  -0.0136 0.0205  192  THR A N   
927  C CA  . THR A 161 ? 0.4445 0.4168 0.5427 0.0133  -0.0122 0.0130  192  THR A CA  
928  C C   . THR A 161 ? 0.2985 0.2656 0.3898 0.0129  -0.0118 0.0095  192  THR A C   
929  O O   . THR A 161 ? 0.2965 0.2589 0.3829 0.0121  -0.0121 0.0037  192  THR A O   
930  C CB  . THR A 161 ? 0.4102 0.3865 0.4993 0.0130  -0.0097 0.0130  192  THR A CB  
931  O OG1 . THR A 161 ? 0.3939 0.3725 0.4771 0.0134  -0.0072 0.0160  192  THR A OG1 
932  C CG2 . THR A 161 ? 0.3858 0.3676 0.4813 0.0129  -0.0113 0.0169  192  THR A CG2 
933  N N   . TRP A 162 ? 0.3209 0.2891 0.4121 0.0134  -0.0109 0.0134  193  TRP A N   
934  C CA  . TRP A 162 ? 0.2561 0.2198 0.3431 0.0130  -0.0114 0.0114  193  TRP A CA  
935  C C   . TRP A 162 ? 0.3654 0.3252 0.4588 0.0122  -0.0162 0.0102  193  TRP A C   
936  O O   . TRP A 162 ? 0.3363 0.2916 0.4234 0.0112  -0.0179 0.0063  193  TRP A O   
937  C CB  . TRP A 162 ? 0.2891 0.2553 0.3770 0.0141  -0.0087 0.0160  193  TRP A CB  
938  C CG  . TRP A 162 ? 0.3145 0.2817 0.3928 0.0144  -0.0041 0.0139  193  TRP A CG  
939  C CD1 . TRP A 162 ? 0.3496 0.3216 0.4242 0.0148  -0.0010 0.0148  193  TRP A CD1 
940  C CD2 . TRP A 162 ? 0.3353 0.2987 0.4071 0.0141  -0.0025 0.0106  193  TRP A CD2 
941  N NE1 . TRP A 162 ? 0.3166 0.2873 0.3828 0.0147  0.0024  0.0109  193  TRP A NE1 
942  C CE2 . TRP A 162 ? 0.3981 0.3634 0.4637 0.0144  0.0018  0.0087  193  TRP A CE2 
943  C CE3 . TRP A 162 ? 0.3680 0.3265 0.4387 0.0133  -0.0046 0.0095  193  TRP A CE3 
944  C CZ2 . TRP A 162 ? 0.3636 0.3256 0.4244 0.0141  0.0043  0.0054  193  TRP A CZ2 
945  C CZ3 . TRP A 162 ? 0.2926 0.2486 0.3583 0.0131  -0.0021 0.0077  193  TRP A CZ3 
946  C CH2 . TRP A 162 ? 0.3225 0.2799 0.3843 0.0136  0.0024  0.0055  193  TRP A CH2 
947  N N   . THR A 163 ? 0.2994 0.2608 0.4053 0.0125  -0.0188 0.0135  194  THR A N   
948  C CA  . THR A 163 ? 0.3973 0.3545 0.5101 0.0114  -0.0241 0.0109  194  THR A CA  
949  C C   . THR A 163 ? 0.3668 0.3194 0.4729 0.0104  -0.0247 0.0025  194  THR A C   
950  O O   . THR A 163 ? 0.3296 0.2775 0.4308 0.0090  -0.0278 -0.0025 194  THR A O   
951  C CB  . THR A 163 ? 0.3653 0.3248 0.4953 0.0118  -0.0265 0.0161  194  THR A CB  
952  O OG1 . THR A 163 ? 0.3911 0.3552 0.5274 0.0126  -0.0250 0.0243  194  THR A OG1 
953  C CG2 . THR A 163 ? 0.4394 0.3937 0.5776 0.0103  -0.0325 0.0120  194  THR A CG2 
954  N N   . VAL A 164 ? 0.3228 0.2774 0.4288 0.0111  -0.0217 0.0010  195  VAL A N   
955  C CA  . VAL A 164 ? 0.3485 0.2995 0.4502 0.0106  -0.0208 -0.0069 195  VAL A CA  
956  C C   . VAL A 164 ? 0.3743 0.3232 0.4598 0.0098  -0.0182 -0.0108 195  VAL A C   
957  O O   . VAL A 164 ? 0.3422 0.2870 0.4206 0.0087  -0.0186 -0.0171 195  VAL A O   
958  C CB  . VAL A 164 ? 0.3902 0.3447 0.4995 0.0117  -0.0185 -0.0061 195  VAL A CB  
959  C CG1 . VAL A 164 ? 0.4349 0.3867 0.5397 0.0115  -0.0158 -0.0139 195  VAL A CG1 
960  C CG2 . VAL A 164 ? 0.3608 0.3166 0.4881 0.0124  -0.0216 -0.0021 195  VAL A CG2 
961  N N   . SER A 165 ? 0.3225 0.2743 0.4020 0.0101  -0.0154 -0.0071 196  SER A N   
962  C CA  . SER A 165 ? 0.3210 0.2709 0.3877 0.0093  -0.0130 -0.0095 196  SER A CA  
963  C C   . SER A 165 ? 0.3622 0.3081 0.4231 0.0080  -0.0163 -0.0103 196  SER A C   
964  O O   . SER A 165 ? 0.3942 0.3372 0.4453 0.0068  -0.0158 -0.0145 196  SER A O   
965  C CB  . SER A 165 ? 0.3476 0.3006 0.4119 0.0099  -0.0101 -0.0056 196  SER A CB  
966  O OG  . SER A 165 ? 0.3485 0.3053 0.4154 0.0104  -0.0078 -0.0056 196  SER A OG  
967  N N   . LEU A 166 ? 0.3810 0.3274 0.4480 0.0082  -0.0198 -0.0056 197  LEU A N   
968  C CA  . LEU A 166 ? 0.4163 0.3596 0.4796 0.0067  -0.0244 -0.0053 197  LEU A CA  
969  C C   . LEU A 166 ? 0.3531 0.2926 0.4134 0.0051  -0.0282 -0.0118 197  LEU A C   
970  O O   . LEU A 166 ? 0.3341 0.2709 0.3829 0.0034  -0.0300 -0.0147 197  LEU A O   
971  C CB  . LEU A 166 ? 0.3344 0.2796 0.4091 0.0073  -0.0276 0.0011  197  LEU A CB  
972  C CG  . LEU A 166 ? 0.4202 0.3670 0.4943 0.0081  -0.0253 0.0064  197  LEU A CG  
973  C CD1 . LEU A 166 ? 0.5575 0.5072 0.6297 0.0097  -0.0186 0.0066  197  LEU A CD1 
974  C CD2 . LEU A 166 ? 0.5472 0.4959 0.6342 0.0087  -0.0283 0.0125  197  LEU A CD2 
975  N N   . GLY A 167 ? 0.4154 0.3550 0.4863 0.0057  -0.0293 -0.0141 198  GLY A N   
976  C CA  . GLY A 167 ? 0.3940 0.3293 0.4631 0.0044  -0.0321 -0.0219 198  GLY A CA  
977  C C   . GLY A 167 ? 0.4659 0.3993 0.5206 0.0038  -0.0276 -0.0287 198  GLY A C   
978  O O   . GLY A 167 ? 0.3555 0.2853 0.3998 0.0020  -0.0297 -0.0347 198  GLY A O   
979  N N   . LEU A 168 ? 0.3763 0.3125 0.4301 0.0052  -0.0213 -0.0278 199  LEU A N   
980  C CA  . LEU A 168 ? 0.4332 0.3684 0.4759 0.0048  -0.0160 -0.0334 199  LEU A CA  
981  C C   . LEU A 168 ? 0.4211 0.3550 0.4473 0.0030  -0.0162 -0.0325 199  LEU A C   
982  O O   . LEU A 168 ? 0.3728 0.3048 0.3870 0.0017  -0.0138 -0.0380 199  LEU A O   
983  C CB  . LEU A 168 ? 0.3328 0.2718 0.3803 0.0064  -0.0102 -0.0313 199  LEU A CB  
984  C CG  . LEU A 168 ? 0.4149 0.3555 0.4776 0.0080  -0.0093 -0.0326 199  LEU A CG  
985  C CD1 . LEU A 168 ? 0.3976 0.3428 0.4641 0.0090  -0.0053 -0.0290 199  LEU A CD1 
986  C CD2 . LEU A 168 ? 0.4110 0.3483 0.4746 0.0080  -0.0074 -0.0415 199  LEU A CD2 
987  N N   . GLY A 169 ? 0.4180 0.3533 0.4438 0.0028  -0.0184 -0.0252 200  GLY A N   
988  C CA  . GLY A 169 ? 0.3455 0.2798 0.3585 0.0010  -0.0196 -0.0226 200  GLY A CA  
989  C C   . GLY A 169 ? 0.4601 0.3919 0.4679 -0.0011 -0.0273 -0.0233 200  GLY A C   
990  O O   . GLY A 169 ? 0.4380 0.3689 0.4323 -0.0032 -0.0289 -0.0224 200  GLY A O   
991  N N   . LEU A 170 ? 0.3753 0.3062 0.3942 -0.0009 -0.0324 -0.0244 201  LEU A N   
992  C CA  . LEU A 170 ? 0.3779 0.3065 0.3943 -0.0033 -0.0410 -0.0254 201  LEU A CA  
993  C C   . LEU A 170 ? 0.4388 0.3639 0.4436 -0.0052 -0.0420 -0.0357 201  LEU A C   
994  O O   . LEU A 170 ? 0.4122 0.3354 0.4061 -0.0080 -0.0484 -0.0375 201  LEU A O   
995  C CB  . LEU A 170 ? 0.4564 0.3856 0.4915 -0.0025 -0.0460 -0.0225 201  LEU A CB  
996  C CG  . LEU A 170 ? 0.8683 0.7970 0.9070 -0.0046 -0.0555 -0.0184 201  LEU A CG  
997  C CD1 . LEU A 170 ? 0.8426 0.7742 0.8816 -0.0041 -0.0551 -0.0089 201  LEU A CD1 
998  C CD2 . LEU A 170 ? 0.7913 0.7202 0.8498 -0.0041 -0.0596 -0.0174 201  LEU A CD2 
999  N N   . LEU A 171 ? 0.4622 0.3864 0.4695 -0.0037 -0.0358 -0.0426 202  LEU A N   
1000 C CA  . LEU A 171 ? 0.5369 0.4573 0.5348 -0.0050 -0.0354 -0.0538 202  LEU A CA  
1001 C C   . LEU A 171 ? 0.4166 0.3366 0.3908 -0.0074 -0.0342 -0.0559 202  LEU A C   
1002 O O   . LEU A 171 ? 0.4412 0.3582 0.4036 -0.0102 -0.0396 -0.0622 202  LEU A O   
1003 C CB  . LEU A 171 ? 0.4540 0.3744 0.4611 -0.0025 -0.0274 -0.0596 202  LEU A CB  
1004 C CG  . LEU A 171 ? 0.5152 0.4352 0.5452 -0.0007 -0.0299 -0.0590 202  LEU A CG  
1005 C CD1 . LEU A 171 ? 0.4573 0.3789 0.4982 0.0020  -0.0222 -0.0612 202  LEU A CD1 
1006 C CD2 . LEU A 171 ? 0.5245 0.4396 0.5587 -0.0025 -0.0369 -0.0667 202  LEU A CD2 
1007 N N   . PRO A 172 ? 0.4425 0.3654 0.4084 -0.0069 -0.0278 -0.0508 203  PRO A N   
1008 C CA  . PRO A 172 ? 0.5105 0.4336 0.4538 -0.0095 -0.0269 -0.0510 203  PRO A CA  
1009 C C   . PRO A 172 ? 0.4372 0.3604 0.3728 -0.0124 -0.0371 -0.0449 203  PRO A C   
1010 O O   . PRO A 172 ? 0.5164 0.4388 0.4327 -0.0155 -0.0401 -0.0480 203  PRO A O   
1011 C CB  . PRO A 172 ? 0.4789 0.4055 0.4216 -0.0081 -0.0183 -0.0447 203  PRO A CB  
1012 C CG  . PRO A 172 ? 0.4576 0.3858 0.4208 -0.0053 -0.0175 -0.0397 203  PRO A CG  
1013 C CD  . PRO A 172 ? 0.4819 0.4081 0.4583 -0.0042 -0.0206 -0.0456 203  PRO A CD  
1014 N N   . VAL A 173 ? 0.4452 0.3698 0.3955 -0.0116 -0.0424 -0.0361 204  VAL A N   
1015 C CA  . VAL A 173 ? 0.4752 0.4002 0.4220 -0.0142 -0.0526 -0.0294 204  VAL A CA  
1016 C C   . VAL A 173 ? 0.4675 0.3894 0.4114 -0.0169 -0.0618 -0.0369 204  VAL A C   
1017 O O   . VAL A 173 ? 0.4198 0.3417 0.3507 -0.0204 -0.0701 -0.0355 204  VAL A O   
1018 C CB  . VAL A 173 ? 0.4578 0.3850 0.4241 -0.0123 -0.0548 -0.0191 204  VAL A CB  
1019 C CG1 . VAL A 173 ? 0.5393 0.4673 0.5063 -0.0148 -0.0656 -0.0118 204  VAL A CG1 
1020 C CG2 . VAL A 173 ? 0.4105 0.3401 0.3784 -0.0102 -0.0463 -0.0130 204  VAL A CG2 
1021 N N   . LEU A 174 ? 0.4190 0.3383 0.3754 -0.0155 -0.0611 -0.0448 205  LEU A N   
1022 C CA  . LEU A 174 ? 0.4532 0.3689 0.4099 -0.0180 -0.0700 -0.0530 205  LEU A CA  
1023 C C   . LEU A 174 ? 0.4671 0.3796 0.4017 -0.0203 -0.0681 -0.0654 205  LEU A C   
1024 O O   . LEU A 174 ? 0.6252 0.5345 0.5541 -0.0234 -0.0766 -0.0730 205  LEU A O   
1025 C CB  . LEU A 174 ? 0.4074 0.3213 0.3883 -0.0157 -0.0698 -0.0560 205  LEU A CB  
1026 C CG  . LEU A 174 ? 0.5204 0.4376 0.5233 -0.0139 -0.0726 -0.0445 205  LEU A CG  
1027 C CD1 . LEU A 174 ? 0.6942 0.6103 0.7195 -0.0116 -0.0710 -0.0468 205  LEU A CD1 
1028 C CD2 . LEU A 174 ? 0.5818 0.4997 0.5869 -0.0169 -0.0844 -0.0385 205  LEU A CD2 
1029 N N   . GLY A 175 ? 0.6047 0.5183 0.5273 -0.0189 -0.0571 -0.0681 206  GLY A N   
1030 C CA  . GLY A 175 ? 0.5301 0.4418 0.4289 -0.0210 -0.0538 -0.0788 206  GLY A CA  
1031 C C   . GLY A 175 ? 0.5509 0.4618 0.4496 -0.0182 -0.0405 -0.0872 206  GLY A C   
1032 O O   . GLY A 175 ? 0.5845 0.4942 0.4632 -0.0196 -0.0355 -0.0963 206  GLY A O   
1033 N N   . TRP A 176 ? 0.5467 0.4587 0.4669 -0.0143 -0.0343 -0.0842 207  TRP A N   
1034 C CA  . TRP A 176 ? 0.5799 0.4921 0.5032 -0.0115 -0.0220 -0.0906 207  TRP A CA  
1035 C C   . TRP A 176 ? 0.4979 0.4147 0.4100 -0.0112 -0.0140 -0.0828 207  TRP A C   
1036 O O   . TRP A 176 ? 0.4413 0.3613 0.3665 -0.0087 -0.0094 -0.0752 207  TRP A O   
1037 C CB  . TRP A 176 ? 0.5546 0.4665 0.5056 -0.0080 -0.0199 -0.0900 207  TRP A CB  
1038 C CG  . TRP A 176 ? 0.5266 0.4385 0.4838 -0.0053 -0.0086 -0.0973 207  TRP A CG  
1039 C CD1 . TRP A 176 ? 0.6906 0.6020 0.6322 -0.0056 0.0001  -0.1058 207  TRP A CD1 
1040 C CD2 . TRP A 176 ? 0.5192 0.4321 0.5007 -0.0018 -0.0046 -0.0961 207  TRP A CD2 
1041 N NE1 . TRP A 176 ? 0.5698 0.4817 0.5266 -0.0023 0.0094  -0.1101 207  TRP A NE1 
1042 C CE2 . TRP A 176 ? 0.5093 0.4222 0.4907 -0.0001 0.0060  -0.1039 207  TRP A CE2 
1043 C CE3 . TRP A 176 ? 0.5306 0.4450 0.5339 -0.0001 -0.0089 -0.0884 207  TRP A CE3 
1044 C CZ2 . TRP A 176 ? 0.5372 0.4515 0.5410 0.0032  0.0114  -0.1040 207  TRP A CZ2 
1045 C CZ3 . TRP A 176 ? 0.5480 0.4640 0.5710 0.0029  -0.0037 -0.0884 207  TRP A CZ3 
1046 C CH2 . TRP A 176 ? 0.5516 0.4675 0.5754 0.0045  0.0059  -0.0959 207  TRP A CH2 
1047 N N   . ASN A 177 ? 0.4985 0.4160 0.3858 -0.0139 -0.0126 -0.0849 208  ASN A N   
1048 C CA  . ASN A 177 ? 0.5152 0.4371 0.3903 -0.0143 -0.0058 -0.0766 208  ASN A CA  
1049 C C   . ASN A 177 ? 0.5658 0.4877 0.4162 -0.0162 0.0009  -0.0851 208  ASN A C   
1050 O O   . ASN A 177 ? 0.5567 0.4748 0.4007 -0.0168 0.0007  -0.0984 208  ASN A O   
1051 C CB  . ASN A 177 ? 0.5536 0.4778 0.4245 -0.0164 -0.0144 -0.0632 208  ASN A CB  
1052 C CG  . ASN A 177 ? 0.5634 0.4860 0.4178 -0.0204 -0.0256 -0.0649 208  ASN A CG  
1053 O OD1 . ASN A 177 ? 0.5561 0.4789 0.3866 -0.0231 -0.0242 -0.0697 208  ASN A OD1 
1054 N ND2 . ASN A 177 ? 0.5624 0.4837 0.4293 -0.0209 -0.0368 -0.0607 208  ASN A ND2 
1055 N N   . CYS A 178 ? 0.5519 0.4781 0.3883 -0.0172 0.0072  -0.0777 209  CYS A N   
1056 C CA  . CYS A 178 ? 0.6851 0.6126 0.4974 -0.0188 0.0158  -0.0843 209  CYS A CA  
1057 C C   . CYS A 178 ? 0.7318 0.6616 0.5168 -0.0233 0.0095  -0.0777 209  CYS A C   
1058 O O   . CYS A 178 ? 0.7168 0.6494 0.4795 -0.0249 0.0173  -0.0793 209  CYS A O   
1059 C CB  . CYS A 178 ? 0.5794 0.5110 0.3980 -0.0163 0.0302  -0.0812 209  CYS A CB  
1060 S SG  . CYS A 178 ? 0.6700 0.6072 0.4886 -0.0173 0.0315  -0.0620 209  CYS A SG  
1061 N N   . LEU A 179 ? 0.6793 0.6085 0.4661 -0.0253 -0.0043 -0.0699 210  LEU A N   
1062 C CA  . LEU A 179 ? 0.8194 0.7514 0.5824 -0.0298 -0.0117 -0.0618 210  LEU A CA  
1063 C C   . LEU A 179 ? 0.7491 0.6800 0.4823 -0.0331 -0.0118 -0.0740 210  LEU A C   
1064 O O   . LEU A 179 ? 0.8708 0.8058 0.5782 -0.0363 -0.0103 -0.0690 210  LEU A O   
1065 C CB  . LEU A 179 ? 0.7148 0.6460 0.4885 -0.0312 -0.0273 -0.0531 210  LEU A CB  
1066 C CG  . LEU A 179 ? 0.7281 0.6610 0.5265 -0.0285 -0.0272 -0.0395 210  LEU A CG  
1067 C CD1 . LEU A 179 ? 0.8317 0.7632 0.6444 -0.0292 -0.0412 -0.0337 210  LEU A CD1 
1068 C CD2 . LEU A 179 ? 0.7085 0.6463 0.4978 -0.0296 -0.0224 -0.0261 210  LEU A CD2 
1069 N N   . ALA A 180 ? 0.6904 0.6159 0.4266 -0.0326 -0.0135 -0.0901 211  ALA A N   
1070 C CA  . ALA A 180 ? 1.0390 0.9626 0.7470 -0.0358 -0.0137 -0.1041 211  ALA A CA  
1071 C C   . ALA A 180 ? 1.0141 0.9390 0.7105 -0.0340 0.0042  -0.1133 211  ALA A C   
1072 O O   . ALA A 180 ? 1.1851 1.1128 0.8506 -0.0370 0.0085  -0.1160 211  ALA A O   
1073 C CB  . ALA A 180 ? 1.0336 0.9502 0.7514 -0.0361 -0.0228 -0.1184 211  ALA A CB  
1074 N N   . GLU A 181 ? 0.9850 0.9086 0.7061 -0.0291 0.0149  -0.1176 212  GLU A N   
1075 C CA  . GLU A 181 ? 0.9843 0.9089 0.7010 -0.0267 0.0324  -0.1270 212  GLU A CA  
1076 C C   . GLU A 181 ? 1.0175 0.9479 0.7478 -0.0241 0.0425  -0.1129 212  GLU A C   
1077 O O   . GLU A 181 ? 0.9346 0.8644 0.6945 -0.0204 0.0443  -0.1097 212  GLU A O   
1078 C CB  . GLU A 181 ? 1.0604 0.9788 0.7975 -0.0233 0.0363  -0.1434 212  GLU A CB  
1079 C CG  . GLU A 181 ? 1.2525 1.1714 0.9866 -0.0206 0.0543  -0.1555 212  GLU A CG  
1080 C CD  . GLU A 181 ? 1.4011 1.3138 1.1607 -0.0169 0.0574  -0.1701 212  GLU A CD  
1081 O OE1 . GLU A 181 ? 1.3467 1.2543 1.1212 -0.0171 0.0450  -0.1727 212  GLU A OE1 
1082 O OE2 . GLU A 181 ? 1.4212 1.3345 1.1879 -0.0137 0.0725  -0.1784 212  GLU A OE2 
1083 N N   . ARG A 182 ? 0.9325 0.8688 0.6410 -0.0263 0.0486  -0.1043 213  ARG A N   
1084 C CA  . ARG A 182 ? 1.0557 0.9975 0.7770 -0.0245 0.0575  -0.0904 213  ARG A CA  
1085 C C   . ARG A 182 ? 1.0119 0.9546 0.7488 -0.0204 0.0740  -0.0981 213  ARG A C   
1086 O O   . ARG A 182 ? 0.7503 0.6961 0.5082 -0.0181 0.0796  -0.0888 213  ARG A O   
1087 C CB  . ARG A 182 ? 1.0258 0.9739 0.7207 -0.0282 0.0598  -0.0783 213  ARG A CB  
1088 C CG  . ARG A 182 ? 1.3188 1.2717 1.0294 -0.0274 0.0632  -0.0602 213  ARG A CG  
1089 C CD  . ARG A 182 ? 1.4158 1.3754 1.1018 -0.0307 0.0690  -0.0489 213  ARG A CD  
1090 N NE  . ARG A 182 ? 1.6206 1.5831 1.2903 -0.0303 0.0852  -0.0584 213  ARG A NE  
1091 C CZ  . ARG A 182 ? 1.4299 1.3954 1.1151 -0.0273 0.1005  -0.0585 213  ARG A CZ  
1092 N NH1 . ARG A 182 ? 1.5155 1.4816 1.2316 -0.0248 0.1013  -0.0496 213  ARG A NH1 
1093 N NH2 . ARG A 182 ? 1.1252 1.0934 0.7950 -0.0269 0.1155  -0.0681 213  ARG A NH2 
1094 N N   . ALA A 183 ? 0.7565 0.6965 0.4849 -0.0195 0.0817  -0.1153 214  ALA A N   
1095 C CA  . ALA A 183 ? 0.9405 0.8812 0.6878 -0.0152 0.0968  -0.1231 214  ALA A CA  
1096 C C   . ALA A 183 ? 0.9493 0.8866 0.7334 -0.0114 0.0925  -0.1235 214  ALA A C   
1097 O O   . ALA A 183 ? 0.8471 0.7863 0.6529 -0.0079 0.1032  -0.1248 214  ALA A O   
1098 C CB  . ALA A 183 ? 0.7695 0.7071 0.5005 -0.0149 0.1057  -0.1426 214  ALA A CB  
1099 N N   . ALA A 184 ? 0.8796 0.8125 0.6714 -0.0122 0.0772  -0.1217 215  ALA A N   
1100 C CA  . ALA A 184 ? 0.7345 0.6647 0.5588 -0.0090 0.0722  -0.1212 215  ALA A CA  
1101 C C   . ALA A 184 ? 0.6178 0.5514 0.4573 -0.0088 0.0669  -0.1044 215  ALA A C   
1102 O O   . ALA A 184 ? 0.6026 0.5346 0.4665 -0.0066 0.0616  -0.1023 215  ALA A O   
1103 C CB  . ALA A 184 ? 0.6923 0.6158 0.5185 -0.0099 0.0596  -0.1298 215  ALA A CB  
1104 N N   . CYS A 185 ? 0.5572 0.4955 0.3829 -0.0110 0.0684  -0.0926 216  CYS A N   
1105 C CA  . CYS A 185 ? 0.5391 0.4798 0.3788 -0.0109 0.0632  -0.0776 216  CYS A CA  
1106 C C   . CYS A 185 ? 0.5746 0.5181 0.4397 -0.0077 0.0716  -0.0750 216  CYS A C   
1107 O O   . CYS A 185 ? 0.6091 0.5554 0.4758 -0.0065 0.0842  -0.0791 216  CYS A O   
1108 C CB  . CYS A 185 ? 0.8151 0.7599 0.6354 -0.0142 0.0629  -0.0654 216  CYS A CB  
1109 S SG  . CYS A 185 ? 0.8945 0.8372 0.6885 -0.0186 0.0486  -0.0631 216  CYS A SG  
1110 N N   . SER A 186 ? 0.5824 0.5255 0.4676 -0.0066 0.0645  -0.0680 217  SER A N   
1111 C CA  . SER A 186 ? 0.4570 0.4033 0.3650 -0.0044 0.0699  -0.0633 217  SER A CA  
1112 C C   . SER A 186 ? 0.5931 0.5434 0.4974 -0.0062 0.0730  -0.0510 217  SER A C   
1113 O O   . SER A 186 ? 0.5073 0.4584 0.3915 -0.0090 0.0720  -0.0458 217  SER A O   
1114 C CB  . SER A 186 ? 0.5361 0.4803 0.4648 -0.0027 0.0609  -0.0616 217  SER A CB  
1115 O OG  . SER A 186 ? 0.4858 0.4295 0.4117 -0.0043 0.0518  -0.0520 217  SER A OG  
1116 N N   . VAL A 187 ? 0.4917 0.4448 0.4166 -0.0049 0.0762  -0.0459 218  VAL A N   
1117 C CA  . VAL A 187 ? 0.5144 0.4708 0.4407 -0.0067 0.0786  -0.0343 218  VAL A CA  
1118 C C   . VAL A 187 ? 0.4968 0.4510 0.4224 -0.0080 0.0677  -0.0257 218  VAL A C   
1119 O O   . VAL A 187 ? 0.5476 0.5036 0.4727 -0.0098 0.0685  -0.0157 218  VAL A O   
1120 C CB  . VAL A 187 ? 0.4971 0.4568 0.4471 -0.0051 0.0847  -0.0325 218  VAL A CB  
1121 C CG1 . VAL A 187 ? 0.4868 0.4494 0.4400 -0.0036 0.0966  -0.0401 218  VAL A CG1 
1122 C CG2 . VAL A 187 ? 0.4261 0.3840 0.3952 -0.0034 0.0763  -0.0339 218  VAL A CG2 
1123 N N   . VAL A 188 ? 0.4193 0.3697 0.3471 -0.0072 0.0580  -0.0289 219  VAL A N   
1124 C CA  . VAL A 188 ? 0.5464 0.4947 0.4742 -0.0082 0.0480  -0.0215 219  VAL A CA  
1125 C C   . VAL A 188 ? 0.5214 0.4673 0.4303 -0.0098 0.0414  -0.0237 219  VAL A C   
1126 O O   . VAL A 188 ? 0.5074 0.4506 0.4172 -0.0088 0.0367  -0.0315 219  VAL A O   
1127 C CB  . VAL A 188 ? 0.5771 0.5239 0.5241 -0.0061 0.0421  -0.0225 219  VAL A CB  
1128 C CG1 . VAL A 188 ? 0.6359 0.5804 0.5826 -0.0068 0.0326  -0.0161 219  VAL A CG1 
1129 C CG2 . VAL A 188 ? 0.5803 0.5297 0.5447 -0.0052 0.0471  -0.0201 219  VAL A CG2 
1130 N N   . ARG A 189 ? 0.5450 0.4921 0.4373 -0.0125 0.0405  -0.0165 220  ARG A N   
1131 C CA  A ARG A 189 ? 0.5706 0.5160 0.4439 -0.0146 0.0330  -0.0181 220  ARG A CA  
1132 C CA  B ARG A 189 ? 0.5706 0.5160 0.4440 -0.0146 0.0330  -0.0182 220  ARG A CA  
1133 C C   . ARG A 189 ? 0.5383 0.4810 0.4203 -0.0145 0.0209  -0.0140 220  ARG A C   
1134 O O   . ARG A 189 ? 0.5514 0.4943 0.4480 -0.0137 0.0190  -0.0061 220  ARG A O   
1135 C CB  A ARG A 189 ? 0.7122 0.6606 0.5650 -0.0178 0.0347  -0.0100 220  ARG A CB  
1136 C CB  B ARG A 189 ? 0.7122 0.6606 0.5649 -0.0178 0.0349  -0.0103 220  ARG A CB  
1137 C CG  A ARG A 189 ? 0.8236 0.7759 0.6693 -0.0182 0.0480  -0.0104 220  ARG A CG  
1138 C CG  B ARG A 189 ? 0.8236 0.7759 0.6695 -0.0180 0.0483  -0.0109 220  ARG A CG  
1139 C CD  A ARG A 189 ? 0.8696 0.8215 0.7032 -0.0175 0.0545  -0.0243 220  ARG A CD  
1140 C CD  B ARG A 189 ? 0.8631 0.8147 0.7020 -0.0168 0.0553  -0.0255 220  ARG A CD  
1141 N NE  A ARG A 189 ? 0.9482 0.9046 0.7687 -0.0186 0.0669  -0.0228 220  ARG A NE  
1142 N NE  B ARG A 189 ? 0.9511 0.9071 0.7782 -0.0175 0.0683  -0.0254 220  ARG A NE  
1143 C CZ  A ARG A 189 ? 0.8572 0.8169 0.6921 -0.0171 0.0778  -0.0203 220  ARG A CZ  
1144 C CZ  B ARG A 189 ? 0.8908 0.8492 0.6911 -0.0204 0.0705  -0.0240 220  ARG A CZ  
1145 N NH1 A ARG A 189 ? 0.6563 0.6150 0.5177 -0.0146 0.0774  -0.0200 220  ARG A NH1 
1146 N NH1 B ARG A 189 ? 0.9433 0.8999 0.7251 -0.0231 0.0597  -0.0230 220  ARG A NH1 
1147 N NH2 A ARG A 189 ? 0.7980 0.7625 0.6203 -0.0184 0.0893  -0.0178 220  ARG A NH2 
1148 N NH2 B ARG A 189 ? 0.9311 0.8942 0.7228 -0.0209 0.0839  -0.0232 220  ARG A NH2 
1149 N N   . PRO A 190 ? 0.5193 0.4594 0.3933 -0.0153 0.0128  -0.0195 221  PRO A N   
1150 C CA  . PRO A 190 ? 0.5370 0.4756 0.3946 -0.0164 0.0132  -0.0307 221  PRO A CA  
1151 C C   . PRO A 190 ? 0.5760 0.5116 0.4475 -0.0137 0.0140  -0.0424 221  PRO A C   
1152 O O   . PRO A 190 ? 0.5461 0.4787 0.4111 -0.0144 0.0092  -0.0512 221  PRO A O   
1153 C CB  . PRO A 190 ? 0.6783 0.6158 0.5231 -0.0194 0.0009  -0.0273 221  PRO A CB  
1154 C CG  . PRO A 190 ? 0.6371 0.5742 0.5011 -0.0184 -0.0066 -0.0177 221  PRO A CG  
1155 C CD  . PRO A 190 ? 0.5593 0.4977 0.4416 -0.0155 0.0014  -0.0140 221  PRO A CD  
1156 N N   . LEU A 191 ? 0.4626 0.3991 0.3539 -0.0107 0.0195  -0.0421 222  LEU A N   
1157 C CA  . LEU A 191 ? 0.5306 0.4649 0.4372 -0.0082 0.0200  -0.0511 222  LEU A CA  
1158 C C   . LEU A 191 ? 0.4764 0.4101 0.3760 -0.0076 0.0285  -0.0627 222  LEU A C   
1159 O O   . LEU A 191 ? 0.5184 0.4549 0.4103 -0.0078 0.0382  -0.0625 222  LEU A O   
1160 C CB  . LEU A 191 ? 0.4957 0.4319 0.4242 -0.0056 0.0229  -0.0467 222  LEU A CB  
1161 C CG  . LEU A 191 ? 0.5226 0.4591 0.4597 -0.0056 0.0159  -0.0369 222  LEU A CG  
1162 C CD1 . LEU A 191 ? 0.4287 0.3672 0.3849 -0.0033 0.0190  -0.0346 222  LEU A CD1 
1163 C CD2 . LEU A 191 ? 0.5052 0.4389 0.4440 -0.0060 0.0056  -0.0376 222  LEU A CD2 
1164 N N   . ALA A 192 ? 0.4931 0.4230 0.3971 -0.0068 0.0253  -0.0728 223  ALA A N   
1165 C CA  . ALA A 192 ? 0.4423 0.3707 0.3437 -0.0057 0.0335  -0.0854 223  ALA A CA  
1166 C C   . ALA A 192 ? 0.4944 0.4249 0.4181 -0.0023 0.0419  -0.0864 223  ALA A C   
1167 O O   . ALA A 192 ? 0.4565 0.3878 0.4000 -0.0006 0.0380  -0.0811 223  ALA A O   
1168 C CB  . ALA A 192 ? 0.5131 0.4361 0.4150 -0.0061 0.0264  -0.0960 223  ALA A CB  
1169 N N   . ARG A 193 ? 0.3813 0.3480 0.4501 0.0394  0.0148  -0.0010 224  ARG A N   
1170 C CA  A ARG A 193 ? 0.4836 0.4533 0.5505 0.0455  0.0118  -0.0030 224  ARG A CA  
1171 C CA  B ARG A 193 ? 0.4836 0.4534 0.5505 0.0455  0.0118  -0.0030 224  ARG A CA  
1172 C C   . ARG A 193 ? 0.4275 0.3810 0.4831 0.0491  0.0089  -0.0031 224  ARG A C   
1173 O O   . ARG A 193 ? 0.4015 0.3546 0.4551 0.0512  0.0073  -0.0030 224  ARG A O   
1174 C CB  A ARG A 193 ? 0.4918 0.4737 0.5617 0.0520  0.0103  -0.0060 224  ARG A CB  
1175 C CB  B ARG A 193 ? 0.4920 0.4740 0.5620 0.0520  0.0104  -0.0060 224  ARG A CB  
1176 C CG  A ARG A 193 ? 0.5096 0.5113 0.5917 0.0499  0.0119  -0.0055 224  ARG A CG  
1177 C CG  B ARG A 193 ? 0.5526 0.5440 0.6242 0.0570  0.0080  -0.0070 224  ARG A CG  
1178 C CD  A ARG A 193 ? 0.5832 0.5983 0.6676 0.0575  0.0097  -0.0077 224  ARG A CD  
1179 C CD  B ARG A 193 ? 0.6613 0.6698 0.7389 0.0622  0.0073  -0.0086 224  ARG A CD  
1180 N NE  A ARG A 193 ? 0.6052 0.6159 0.6839 0.0630  0.0090  -0.0101 224  ARG A NE  
1181 N NE  B ARG A 193 ? 0.6775 0.6972 0.7579 0.0654  0.0053  -0.0083 224  ARG A NE  
1182 C CZ  A ARG A 193 ? 0.6024 0.6184 0.6851 0.0611  0.0109  -0.0105 224  ARG A CZ  
1183 C CZ  B ARG A 193 ? 0.7037 0.7406 0.7898 0.0700  0.0043  -0.0087 224  ARG A CZ  
1184 N NH1 A ARG A 193 ? 0.5252 0.5515 0.6182 0.0539  0.0139  -0.0081 224  ARG A NH1 
1185 N NH1 B ARG A 193 ? 0.6388 0.6844 0.7286 0.0725  0.0052  -0.0096 224  ARG A NH1 
1186 N NH2 A ARG A 193 ? 0.5626 0.5732 0.6385 0.0666  0.0098  -0.0132 224  ARG A NH2 
1187 N NH2 B ARG A 193 ? 0.5491 0.5957 0.6374 0.0720  0.0022  -0.0077 224  ARG A NH2 
1188 N N   . SER A 194 ? 0.4385 0.3788 0.4866 0.0496  0.0080  -0.0030 225  SER A N   
1189 C CA  . SER A 194 ? 0.4443 0.3687 0.4818 0.0530  0.0048  -0.0027 225  SER A CA  
1190 C C   . SER A 194 ? 0.4537 0.3708 0.4894 0.0479  0.0056  0.0011  225  SER A C   
1191 O O   . SER A 194 ? 0.4945 0.4048 0.5246 0.0508  0.0033  0.0017  225  SER A O   
1192 C CB  . SER A 194 ? 0.4238 0.3352 0.4536 0.0542  0.0033  -0.0035 225  SER A CB  
1193 O OG  . SER A 194 ? 0.5529 0.4615 0.5844 0.0464  0.0058  -0.0007 225  SER A OG  
1194 N N   . HIS A 195 ? 0.4321 0.3509 0.4722 0.0405  0.0090  0.0040  226  HIS A N   
1195 C CA  . HIS A 195 ? 0.4284 0.3420 0.4671 0.0360  0.0103  0.0078  226  HIS A CA  
1196 C C   . HIS A 195 ? 0.4693 0.3919 0.5121 0.0369  0.0106  0.0068  226  HIS A C   
1197 O O   . HIS A 195 ? 0.3885 0.3055 0.4269 0.0375  0.0095  0.0082  226  HIS A O   
1198 C CB  . HIS A 195 ? 0.4097 0.3243 0.4525 0.0285  0.0143  0.0114  226  HIS A CB  
1199 C CG  . HIS A 195 ? 0.4144 0.3257 0.4564 0.0244  0.0164  0.0155  226  HIS A CG  
1200 N ND1 . HIS A 195 ? 0.4377 0.3579 0.4869 0.0205  0.0203  0.0165  226  HIS A ND1 
1201 C CD2 . HIS A 195 ? 0.3799 0.2802 0.4146 0.0238  0.0152  0.0189  226  HIS A CD2 
1202 C CE1 . HIS A 195 ? 0.4093 0.3237 0.4550 0.0182  0.0215  0.0200  226  HIS A CE1 
1203 N NE2 . HIS A 195 ? 0.3895 0.2926 0.4268 0.0201  0.0184  0.0217  226  HIS A NE2 
1204 N N   . VAL A 196 ? 0.4931 0.4299 0.5444 0.0369  0.0120  0.0046  227  VAL A N   
1205 C CA  . VAL A 196 ? 0.3755 0.3211 0.4306 0.0371  0.0118  0.0036  227  VAL A CA  
1206 C C   . VAL A 196 ? 0.4534 0.3982 0.5035 0.0437  0.0078  0.0017  227  VAL A C   
1207 O O   . VAL A 196 ? 0.4052 0.3509 0.4540 0.0437  0.0069  0.0019  227  VAL A O   
1208 C CB  . VAL A 196 ? 0.4734 0.4347 0.5391 0.0353  0.0135  0.0023  227  VAL A CB  
1209 C CG1 . VAL A 196 ? 0.5488 0.5196 0.6180 0.0359  0.0122  0.0009  227  VAL A CG1 
1210 C CG2 . VAL A 196 ? 0.4316 0.3938 0.5027 0.0283  0.0179  0.0048  227  VAL A CG2 
1211 N N   . ALA A 197 ? 0.4146 0.3575 0.4614 0.0495  0.0055  0.0000  228  ALA A N   
1212 C CA  . ALA A 197 ? 0.4562 0.3974 0.4976 0.0565  0.0020  -0.0012 228  ALA A CA  
1213 C C   . ALA A 197 ? 0.4096 0.3377 0.4433 0.0561  0.0007  0.0011  228  ALA A C   
1214 O O   . ALA A 197 ? 0.4351 0.3650 0.4667 0.0588  -0.0012 0.0012  228  ALA A O   
1215 C CB  . ALA A 197 ? 0.4665 0.4052 0.5043 0.0631  0.0001  -0.0034 228  ALA A CB  
1216 N N   . LEU A 198 ? 0.4941 0.4098 0.5235 0.0528  0.0014  0.0034  229  LEU A N   
1217 C CA  . LEU A 198 ? 0.5252 0.4295 0.5480 0.0518  0.0003  0.0066  229  LEU A CA  
1218 C C   . LEU A 198 ? 0.4664 0.3758 0.4917 0.0479  0.0020  0.0079  229  LEU A C   
1219 O O   . LEU A 198 ? 0.4297 0.3366 0.4510 0.0498  0.0003  0.0089  229  LEU A O   
1220 C CB  . LEU A 198 ? 0.5512 0.4434 0.5701 0.0478  0.0010  0.0096  229  LEU A CB  
1221 C CG  . LEU A 198 ? 0.5630 0.4449 0.5762 0.0453  0.0004  0.0142  229  LEU A CG  
1222 C CD1 . LEU A 198 ? 0.6028 0.4778 0.6096 0.0512  -0.0037 0.0143  229  LEU A CD1 
1223 C CD2 . LEU A 198 ? 0.5222 0.3947 0.5328 0.0404  0.0012  0.0178  229  LEU A CD2 
1224 N N   . LEU A 199 ? 0.4342 0.3507 0.4660 0.0427  0.0055  0.0079  230  LEU A N   
1225 C CA  . LEU A 199 ? 0.3593 0.2798 0.3930 0.0391  0.0072  0.0086  230  LEU A CA  
1226 C C   . LEU A 199 ? 0.4971 0.4258 0.5315 0.0424  0.0048  0.0060  230  LEU A C   
1227 O O   . LEU A 199 ? 0.3806 0.3078 0.4115 0.0421  0.0041  0.0068  230  LEU A O   
1228 C CB  . LEU A 199 ? 0.3476 0.2747 0.3887 0.0336  0.0112  0.0087  230  LEU A CB  
1229 C CG  . LEU A 199 ? 0.4013 0.3218 0.4422 0.0293  0.0143  0.0122  230  LEU A CG  
1230 C CD1 . LEU A 199 ? 0.4199 0.3483 0.4688 0.0241  0.0185  0.0125  230  LEU A CD1 
1231 C CD2 . LEU A 199 ? 0.4254 0.3353 0.4591 0.0281  0.0144  0.0162  230  LEU A CD2 
1232 N N   . SER A 200 ? 0.4133 0.3518 0.4521 0.0456  0.0035  0.0033  231  SER A N   
1233 C CA  . SER A 200 ? 0.4408 0.3888 0.4807 0.0484  0.0011  0.0016  231  SER A CA  
1234 C C   . SER A 200 ? 0.4172 0.3594 0.4498 0.0539  -0.0020 0.0024  231  SER A C   
1235 O O   . SER A 200 ? 0.4202 0.3662 0.4512 0.0545  -0.0036 0.0023  231  SER A O   
1236 C CB  . SER A 200 ? 0.4570 0.4178 0.5034 0.0509  0.0005  -0.0005 231  SER A CB  
1237 O OG  . SER A 200 ? 0.6494 0.6187 0.7038 0.0454  0.0029  -0.0009 231  SER A OG  
1238 N N   . ALA A 201 ? 0.4305 0.3635 0.4586 0.0579  -0.0032 0.0031  232  ALA A N   
1239 C CA  . ALA A 201 ? 0.5115 0.4375 0.5326 0.0630  -0.0061 0.0044  232  ALA A CA  
1240 C C   . ALA A 201 ? 0.4212 0.3408 0.4382 0.0598  -0.0059 0.0070  232  ALA A C   
1241 O O   . ALA A 201 ? 0.4752 0.3963 0.4893 0.0625  -0.0080 0.0078  232  ALA A O   
1242 C CB  . ALA A 201 ? 0.4626 0.3771 0.4789 0.0669  -0.0073 0.0048  232  ALA A CB  
1243 N N   . ALA A 202 ? 0.4783 0.3916 0.4952 0.0543  -0.0034 0.0089  233  ALA A N   
1244 C CA  . ALA A 202 ? 0.4257 0.3338 0.4386 0.0516  -0.0029 0.0118  233  ALA A CA  
1245 C C   . ALA A 202 ? 0.4641 0.3816 0.4791 0.0498  -0.0024 0.0101  233  ALA A C   
1246 O O   . ALA A 202 ? 0.4482 0.3647 0.4589 0.0507  -0.0037 0.0114  233  ALA A O   
1247 C CB  . ALA A 202 ? 0.5099 0.4111 0.5227 0.0463  0.0001  0.0146  233  ALA A CB  
1248 N N   . PHE A 203 ? 0.4117 0.3381 0.4328 0.0470  -0.0007 0.0074  234  PHE A N   
1249 C CA  . PHE A 203 ? 0.3721 0.3067 0.3948 0.0448  -0.0008 0.0056  234  PHE A CA  
1250 C C   . PHE A 203 ? 0.4788 0.4199 0.4996 0.0492  -0.0045 0.0047  234  PHE A C   
1251 O O   . PHE A 203 ? 0.3802 0.3226 0.3977 0.0486  -0.0055 0.0048  234  PHE A O   
1252 C CB  . PHE A 203 ? 0.3639 0.3071 0.3942 0.0410  0.0010  0.0032  234  PHE A CB  
1253 C CG  . PHE A 203 ? 0.4716 0.4230 0.5033 0.0386  0.0001  0.0011  234  PHE A CG  
1254 C CD1 . PHE A 203 ? 0.4656 0.4136 0.4953 0.0341  0.0021  0.0009  234  PHE A CD1 
1255 C CD2 . PHE A 203 ? 0.4575 0.4198 0.4917 0.0409  -0.0029 -0.0004 234  PHE A CD2 
1256 C CE1 . PHE A 203 ? 0.4908 0.4450 0.5207 0.0315  0.0007  -0.0014 234  PHE A CE1 
1257 C CE2 . PHE A 203 ? 0.5885 0.5583 0.6235 0.0380  -0.0044 -0.0020 234  PHE A CE2 
1258 C CZ  . PHE A 203 ? 0.4745 0.4397 0.5072 0.0331  -0.0027 -0.0028 234  PHE A CZ  
1259 N N   . PHE A 204 ? 0.3796 0.3253 0.4024 0.0540  -0.0063 0.0039  235  PHE A N   
1260 C CA  . PHE A 204 ? 0.4470 0.4005 0.4686 0.0586  -0.0095 0.0037  235  PHE A CA  
1261 C C   . PHE A 204 ? 0.4192 0.3653 0.4339 0.0616  -0.0112 0.0062  235  PHE A C   
1262 O O   . PHE A 204 ? 0.3924 0.3445 0.4053 0.0626  -0.0131 0.0065  235  PHE A O   
1263 C CB  . PHE A 204 ? 0.3815 0.3405 0.4058 0.0642  -0.0108 0.0030  235  PHE A CB  
1264 C CG  . PHE A 204 ? 0.4828 0.4538 0.5146 0.0619  -0.0100 0.0010  235  PHE A CG  
1265 C CD1 . PHE A 204 ? 0.5498 0.5328 0.5850 0.0590  -0.0111 0.0002  235  PHE A CD1 
1266 C CD2 . PHE A 204 ? 0.4260 0.3966 0.4615 0.0625  -0.0085 0.0001  235  PHE A CD2 
1267 C CE1 . PHE A 204 ? 0.4140 0.4085 0.4567 0.0565  -0.0107 -0.0010 235  PHE A CE1 
1268 C CE2 . PHE A 204 ? 0.4374 0.4202 0.4805 0.0605  -0.0078 -0.0012 235  PHE A CE2 
1269 C CZ  . PHE A 204 ? 0.4452 0.4400 0.4921 0.0574  -0.0090 -0.0015 235  PHE A CZ  
1270 N N   . MET A 205 ? 0.4584 0.3922 0.4694 0.0629  -0.0108 0.0084  236  MET A N   
1271 C CA  . MET A 205 ? 0.4852 0.4120 0.4901 0.0654  -0.0125 0.0115  236  MET A CA  
1272 C C   . MET A 205 ? 0.4733 0.4004 0.4760 0.0611  -0.0116 0.0124  236  MET A C   
1273 O O   . MET A 205 ? 0.4541 0.3844 0.4538 0.0628  -0.0134 0.0136  236  MET A O   
1274 C CB  . MET A 205 ? 0.5222 0.4354 0.5238 0.0667  -0.0126 0.0141  236  MET A CB  
1275 C CG  . MET A 205 ? 0.7585 0.6689 0.7594 0.0730  -0.0146 0.0135  236  MET A CG  
1276 S SD  . MET A 205 ? 1.0380 0.9305 1.0337 0.0738  -0.0155 0.0164  236  MET A SD  
1277 C CE  . MET A 205 ? 0.9832 0.8743 0.9829 0.0680  -0.0122 0.0146  236  MET A CE  
1278 N N   . VAL A 206 ? 0.3956 0.3199 0.3996 0.0556  -0.0086 0.0120  237  VAL A N   
1279 C CA  . VAL A 206 ? 0.4025 0.3267 0.4036 0.0521  -0.0073 0.0125  237  VAL A CA  
1280 C C   . VAL A 206 ? 0.4456 0.3806 0.4476 0.0513  -0.0087 0.0096  237  VAL A C   
1281 O O   . VAL A 206 ? 0.4000 0.3364 0.3977 0.0514  -0.0097 0.0103  237  VAL A O   
1282 C CB  . VAL A 206 ? 0.4547 0.3747 0.4575 0.0469  -0.0034 0.0125  237  VAL A CB  
1283 C CG1 . VAL A 206 ? 0.5211 0.4425 0.5212 0.0436  -0.0019 0.0118  237  VAL A CG1 
1284 C CG2 . VAL A 206 ? 0.5217 0.4312 0.5222 0.0469  -0.0024 0.0167  237  VAL A CG2 
1285 N N   . PHE A 207 ? 0.4596 0.4028 0.4669 0.0504  -0.0089 0.0066  238  PHE A N   
1286 C CA  . PHE A 207 ? 0.4355 0.3893 0.4438 0.0487  -0.0105 0.0041  238  PHE A CA  
1287 C C   . PHE A 207 ? 0.4007 0.3601 0.4062 0.0534  -0.0139 0.0055  238  PHE A C   
1288 O O   . PHE A 207 ? 0.3999 0.3643 0.4024 0.0520  -0.0154 0.0050  238  PHE A O   
1289 C CB  . PHE A 207 ? 0.4483 0.4105 0.4636 0.0468  -0.0104 0.0016  238  PHE A CB  
1290 C CG  . PHE A 207 ? 0.5614 0.5341 0.5781 0.0434  -0.0122 -0.0006 238  PHE A CG  
1291 C CD1 . PHE A 207 ? 0.6382 0.6083 0.6522 0.0382  -0.0112 -0.0024 238  PHE A CD1 
1292 C CD2 . PHE A 207 ? 0.5917 0.5767 0.6119 0.0455  -0.0149 -0.0008 238  PHE A CD2 
1293 C CE1 . PHE A 207 ? 0.6310 0.6095 0.6455 0.0344  -0.0133 -0.0046 238  PHE A CE1 
1294 C CE2 . PHE A 207 ? 0.7654 0.7604 0.7869 0.0415  -0.0170 -0.0023 238  PHE A CE2 
1295 C CZ  . PHE A 207 ? 0.5496 0.5408 0.5680 0.0357  -0.0164 -0.0044 238  PHE A CZ  
1296 N N   . GLY A 208 ? 0.4691 0.4275 0.4751 0.0591  -0.0152 0.0074  239  GLY A N   
1297 C CA  . GLY A 208 ? 0.4083 0.3714 0.4118 0.0642  -0.0181 0.0094  239  GLY A CA  
1298 C C   . GLY A 208 ? 0.4094 0.3675 0.4071 0.0643  -0.0186 0.0119  239  GLY A C   
1299 O O   . GLY A 208 ? 0.4129 0.3784 0.4085 0.0656  -0.0207 0.0127  239  GLY A O   
1300 N N   . ILE A 209 ? 0.4257 0.3724 0.4208 0.0629  -0.0168 0.0135  240  ILE A N   
1301 C CA  . ILE A 209 ? 0.4833 0.4262 0.4732 0.0630  -0.0172 0.0165  240  ILE A CA  
1302 C C   . ILE A 209 ? 0.4637 0.4124 0.4515 0.0586  -0.0167 0.0142  240  ILE A C   
1303 O O   . ILE A 209 ? 0.4189 0.3719 0.4031 0.0596  -0.0183 0.0154  240  ILE A O   
1304 C CB  . ILE A 209 ? 0.4649 0.3953 0.4527 0.0622  -0.0155 0.0195  240  ILE A CB  
1305 C CG1 . ILE A 209 ? 0.4932 0.4166 0.4816 0.0667  -0.0169 0.0219  240  ILE A CG1 
1306 C CG2 . ILE A 209 ? 0.5131 0.4413 0.4958 0.0619  -0.0157 0.0229  240  ILE A CG2 
1307 C CD1 . ILE A 209 ? 0.5534 0.4647 0.5405 0.0648  -0.0154 0.0246  240  ILE A CD1 
1308 N N   . MET A 210 ? 0.4242 0.3728 0.4140 0.0537  -0.0145 0.0108  241  MET A N   
1309 C CA  . MET A 210 ? 0.4784 0.4310 0.4655 0.0495  -0.0141 0.0079  241  MET A CA  
1310 C C   . MET A 210 ? 0.4270 0.3916 0.4142 0.0499  -0.0174 0.0065  241  MET A C   
1311 O O   . MET A 210 ? 0.4185 0.3865 0.4010 0.0486  -0.0185 0.0059  241  MET A O   
1312 C CB  . MET A 210 ? 0.4299 0.3805 0.4200 0.0445  -0.0114 0.0046  241  MET A CB  
1313 C CG  . MET A 210 ? 0.5624 0.5024 0.5523 0.0434  -0.0078 0.0063  241  MET A CG  
1314 S SD  . MET A 210 ? 0.6644 0.6029 0.6587 0.0377  -0.0044 0.0028  241  MET A SD  
1315 C CE  . MET A 210 ? 0.8399 0.7760 0.8273 0.0345  -0.0031 0.0007  241  MET A CE  
1316 N N   . LEU A 211 ? 0.4229 0.3945 0.4149 0.0519  -0.0190 0.0063  242  LEU A N   
1317 C CA  . LEU A 211 ? 0.4752 0.4597 0.4677 0.0524  -0.0221 0.0059  242  LEU A CA  
1318 C C   . LEU A 211 ? 0.4188 0.4058 0.4073 0.0568  -0.0241 0.0093  242  LEU A C   
1319 O O   . LEU A 211 ? 0.4222 0.4181 0.4083 0.0555  -0.0262 0.0091  242  LEU A O   
1320 C CB  . LEU A 211 ? 0.4311 0.4232 0.4298 0.0548  -0.0232 0.0060  242  LEU A CB  
1321 C CG  . LEU A 211 ? 0.4541 0.4482 0.4578 0.0501  -0.0220 0.0028  242  LEU A CG  
1322 C CD1 . LEU A 211 ? 0.5162 0.5159 0.5258 0.0541  -0.0225 0.0037  242  LEU A CD1 
1323 C CD2 . LEU A 211 ? 0.5077 0.5106 0.5109 0.0443  -0.0239 0.0004  242  LEU A CD2 
1324 N N   . HIS A 212 ? 0.4329 0.4124 0.4208 0.0617  -0.0236 0.0128  243  HIS A N   
1325 C CA  . HIS A 212 ? 0.4616 0.4430 0.4462 0.0658  -0.0254 0.0168  243  HIS A CA  
1326 C C   . HIS A 212 ? 0.4287 0.4089 0.4079 0.0627  -0.0250 0.0167  243  HIS A C   
1327 O O   . HIS A 212 ? 0.4324 0.4212 0.4089 0.0630  -0.0270 0.0176  243  HIS A O   
1328 C CB  . HIS A 212 ? 0.4780 0.4494 0.4628 0.0710  -0.0251 0.0205  243  HIS A CB  
1329 C CG  . HIS A 212 ? 0.5557 0.5275 0.5376 0.0750  -0.0269 0.0252  243  HIS A CG  
1330 N ND1 . HIS A 212 ? 0.7935 0.7770 0.7751 0.0774  -0.0291 0.0268  243  HIS A ND1 
1331 C CD2 . HIS A 212 ? 0.7770 0.7394 0.7563 0.0769  -0.0268 0.0293  243  HIS A CD2 
1332 C CE1 . HIS A 212 ? 0.7065 0.6879 0.6858 0.0808  -0.0302 0.0314  243  HIS A CE1 
1333 N NE2 . HIS A 212 ? 0.7721 0.7406 0.7500 0.0805  -0.0290 0.0331  243  HIS A NE2 
1334 N N   . LEU A 213 ? 0.4276 0.3979 0.4048 0.0599  -0.0224 0.0159  244  LEU A N   
1335 C CA  . LEU A 213 ? 0.4311 0.4001 0.4026 0.0575  -0.0216 0.0156  244  LEU A CA  
1336 C C   . LEU A 213 ? 0.4329 0.4099 0.4022 0.0531  -0.0226 0.0111  244  LEU A C   
1337 O O   . LEU A 213 ? 0.4378 0.4193 0.4021 0.0525  -0.0237 0.0111  244  LEU A O   
1338 C CB  . LEU A 213 ? 0.4292 0.3868 0.3995 0.0554  -0.0183 0.0157  244  LEU A CB  
1339 C CG  . LEU A 213 ? 0.4873 0.4360 0.4584 0.0587  -0.0176 0.0207  244  LEU A CG  
1340 C CD1 . LEU A 213 ? 0.5124 0.4517 0.4833 0.0558  -0.0141 0.0207  244  LEU A CD1 
1341 C CD2 . LEU A 213 ? 0.5236 0.4733 0.4910 0.0619  -0.0192 0.0257  244  LEU A CD2 
1342 N N   . TYR A 214 ? 0.4295 0.4087 0.4025 0.0497  -0.0224 0.0073  245  TYR A N   
1343 C CA  . TYR A 214 ? 0.4754 0.4613 0.4464 0.0446  -0.0238 0.0030  245  TYR A CA  
1344 C C   . TYR A 214 ? 0.4358 0.4343 0.4053 0.0458  -0.0274 0.0043  245  TYR A C   
1345 O O   . TYR A 214 ? 0.4413 0.4437 0.4053 0.0429  -0.0286 0.0024  245  TYR A O   
1346 C CB  . TYR A 214 ? 0.4698 0.4571 0.4464 0.0411  -0.0235 0.0000  245  TYR A CB  
1347 C CG  . TYR A 214 ? 0.5249 0.5209 0.5006 0.0359  -0.0261 -0.0035 245  TYR A CG  
1348 C CD1 . TYR A 214 ? 0.4296 0.4389 0.4081 0.0366  -0.0295 -0.0021 245  TYR A CD1 
1349 C CD2 . TYR A 214 ? 0.6512 0.6421 0.6229 0.0302  -0.0252 -0.0079 245  TYR A CD2 
1350 C CE1 . TYR A 214 ? 0.5421 0.5599 0.5197 0.0311  -0.0323 -0.0047 245  TYR A CE1 
1351 C CE2 . TYR A 214 ? 0.7853 0.7832 0.7558 0.0247  -0.0281 -0.0110 245  TYR A CE2 
1352 C CZ  . TYR A 214 ? 0.6964 0.7080 0.6699 0.0248  -0.0318 -0.0093 245  TYR A CZ  
1353 O OH  . TYR A 214 ? 0.7701 0.7891 0.7422 0.0187  -0.0352 -0.0118 245  TYR A OH  
1354 N N   . VAL A 215 ? 0.4335 0.4387 0.4076 0.0502  -0.0290 0.0077  246  VAL A N   
1355 C CA  . VAL A 215 ? 0.4367 0.4552 0.4102 0.0517  -0.0321 0.0097  246  VAL A CA  
1356 C C   . VAL A 215 ? 0.4670 0.4858 0.4351 0.0539  -0.0326 0.0124  246  VAL A C   
1357 O O   . VAL A 215 ? 0.5040 0.5324 0.4687 0.0522  -0.0347 0.0122  246  VAL A O   
1358 C CB  . VAL A 215 ? 0.4337 0.4584 0.4130 0.0571  -0.0332 0.0132  246  VAL A CB  
1359 C CG1 . VAL A 215 ? 0.6059 0.6449 0.5846 0.0593  -0.0361 0.0164  246  VAL A CG1 
1360 C CG2 . VAL A 215 ? 0.4905 0.5179 0.4751 0.0548  -0.0331 0.0107  246  VAL A CG2 
1361 N N   . ARG A 216 ? 0.4415 0.4504 0.4089 0.0576  -0.0307 0.0153  247  ARG A N   
1362 C CA  . ARG A 216 ? 0.4960 0.5056 0.4588 0.0597  -0.0311 0.0185  247  ARG A CA  
1363 C C   . ARG A 216 ? 0.4501 0.4590 0.4062 0.0550  -0.0305 0.0147  247  ARG A C   
1364 O O   . ARG A 216 ? 0.5080 0.5248 0.4598 0.0548  -0.0321 0.0154  247  ARG A O   
1365 C CB  . ARG A 216 ? 0.5002 0.4989 0.4639 0.0639  -0.0294 0.0227  247  ARG A CB  
1366 C CG  . ARG A 216 ? 0.5971 0.5941 0.5663 0.0688  -0.0301 0.0260  247  ARG A CG  
1367 C CD  . ARG A 216 ? 0.7732 0.7700 0.7421 0.0742  -0.0314 0.0322  247  ARG A CD  
1368 N NE  . ARG A 216 ? 0.8623 0.8724 0.8298 0.0752  -0.0336 0.0340  247  ARG A NE  
1369 C CZ  . ARG A 216 ? 1.1446 1.1574 1.1105 0.0781  -0.0346 0.0390  247  ARG A CZ  
1370 N NH1 . ARG A 216 ? 0.9113 0.9143 0.8766 0.0802  -0.0340 0.0430  247  ARG A NH1 
1371 N NH2 . ARG A 216 ? 1.0893 1.1157 1.0542 0.0786  -0.0365 0.0404  247  ARG A NH2 
1372 N N   . ILE A 217 ? 0.4630 0.4624 0.4177 0.0514  -0.0280 0.0107  248  ILE A N   
1373 C CA  . ILE A 217 ? 0.4542 0.4510 0.4018 0.0473  -0.0272 0.0065  248  ILE A CA  
1374 C C   . ILE A 217 ? 0.5180 0.5252 0.4632 0.0431  -0.0302 0.0028  248  ILE A C   
1375 O O   . ILE A 217 ? 0.4651 0.4765 0.4036 0.0419  -0.0313 0.0017  248  ILE A O   
1376 C CB  . ILE A 217 ? 0.4521 0.4371 0.3997 0.0443  -0.0239 0.0030  248  ILE A CB  
1377 C CG1 . ILE A 217 ? 0.4494 0.4247 0.3975 0.0478  -0.0208 0.0071  248  ILE A CG1 
1378 C CG2 . ILE A 217 ? 0.4872 0.4698 0.4274 0.0397  -0.0233 -0.0024 248  ILE A CG2 
1379 C CD1 . ILE A 217 ? 0.4848 0.4500 0.4355 0.0456  -0.0176 0.0052  248  ILE A CD1 
1380 N N   . YCM A 218 ? 0.5126 0.5243 0.4629 0.0406  -0.0316 0.0012  249  YCM A N   
1381 C CA  . YCM A 218 ? 0.4589 0.4813 0.4077 0.0360  -0.0350 -0.0014 249  YCM A CA  
1382 C CB  . YCM A 218 ? 0.7365 0.7640 0.6927 0.0343  -0.0362 -0.0017 249  YCM A CB  
1383 S SG  . YCM A 218 ? 1.1905 1.2350 1.1471 0.0298  -0.0410 -0.0020 249  YCM A SG  
1384 C CD  . YCM A 218 ? 1.0016 1.0416 0.9535 0.0204  -0.0422 -0.0090 249  YCM A CD  
1385 C CE  . YCM A 218 ? 1.1261 1.1582 1.0833 0.0181  -0.0404 -0.0112 249  YCM A CE  
1386 O OZ1 . YCM A 218 ? 1.0289 1.0500 0.9882 0.0214  -0.0366 -0.0110 249  YCM A OZ1 
1387 N NZ2 . YCM A 218 ? 0.9743 1.0121 0.9343 0.0120  -0.0431 -0.0132 249  YCM A NZ2 
1388 C C   . YCM A 218 ? 0.5440 0.5791 0.4906 0.0382  -0.0377 0.0020  249  YCM A C   
1389 O O   . YCM A 218 ? 0.5802 0.6218 0.5211 0.0344  -0.0400 -0.0003 249  YCM A O   
1390 N N   . GLN A 219 ? 0.5111 0.5493 0.4622 0.0445  -0.0375 0.0077  250  GLN A N   
1391 C CA  . GLN A 219 ? 0.5192 0.5692 0.4694 0.0478  -0.0397 0.0122  250  GLN A CA  
1392 C C   . GLN A 219 ? 0.6102 0.6599 0.5525 0.0472  -0.0396 0.0116  250  GLN A C   
1393 O O   . GLN A 219 ? 0.6443 0.7054 0.5830 0.0453  -0.0420 0.0116  250  GLN A O   
1394 C CB  . GLN A 219 ? 0.5657 0.6152 0.5217 0.0552  -0.0390 0.0184  250  GLN A CB  
1395 C CG  . GLN A 219 ? 0.8018 0.8638 0.7582 0.0592  -0.0410 0.0239  250  GLN A CG  
1396 C CD  . GLN A 219 ? 1.0866 1.1491 1.0495 0.0661  -0.0409 0.0295  250  GLN A CD  
1397 O OE1 . GLN A 219 ? 1.1830 1.2337 1.1476 0.0697  -0.0391 0.0313  250  GLN A OE1 
1398 N NE2 . GLN A 219 ? 0.9876 1.0637 0.9537 0.0680  -0.0429 0.0323  250  GLN A NE2 
1399 N N   . VAL A 220 ? 0.6383 0.6762 0.5781 0.0490  -0.0367 0.0116  251  VAL A N   
1400 C CA  . VAL A 220 ? 0.4985 0.5367 0.4309 0.0494  -0.0363 0.0116  251  VAL A CA  
1401 C C   . VAL A 220 ? 0.7014 0.7401 0.6258 0.0433  -0.0372 0.0049  251  VAL A C   
1402 O O   . VAL A 220 ? 0.6981 0.7447 0.6165 0.0425  -0.0389 0.0044  251  VAL A O   
1403 C CB  . VAL A 220 ? 0.7148 0.7405 0.6462 0.0527  -0.0330 0.0137  251  VAL A CB  
1404 C CG1 . VAL A 220 ? 0.7631 0.7892 0.6861 0.0530  -0.0323 0.0132  251  VAL A CG1 
1405 C CG2 . VAL A 220 ? 0.8355 0.8610 0.7733 0.0584  -0.0329 0.0208  251  VAL A CG2 
1406 N N   . VAL A 221 ? 0.5391 0.5691 0.4631 0.0389  -0.0362 -0.0005 252  VAL A N   
1407 C CA  . VAL A 221 ? 0.5515 0.5796 0.4674 0.0328  -0.0372 -0.0073 252  VAL A CA  
1408 C C   . VAL A 221 ? 0.7958 0.8380 0.7106 0.0288  -0.0417 -0.0081 252  VAL A C   
1409 O O   . VAL A 221 ? 0.7218 0.7675 0.6282 0.0255  -0.0435 -0.0115 252  VAL A O   
1410 C CB  . VAL A 221 ? 0.6085 0.6244 0.5254 0.0289  -0.0354 -0.0121 252  VAL A CB  
1411 C CG1 . VAL A 221 ? 0.7644 0.7784 0.6735 0.0220  -0.0373 -0.0191 252  VAL A CG1 
1412 C CG2 . VAL A 221 ? 0.6368 0.6394 0.5530 0.0324  -0.0308 -0.0113 252  VAL A CG2 
1413 N N   . TRP A 222 ? 0.5963 0.6475 0.5194 0.0291  -0.0435 -0.0048 253  TRP A N   
1414 C CA  . TRP A 222 ? 0.7436 0.8101 0.6664 0.0253  -0.0477 -0.0043 253  TRP A CA  
1415 C C   . TRP A 222 ? 0.7301 0.8081 0.6497 0.0283  -0.0491 -0.0005 253  TRP A C   
1416 O O   . TRP A 222 ? 0.8053 0.8921 0.7188 0.0238  -0.0521 -0.0026 253  TRP A O   
1417 C CB  . TRP A 222 ? 0.8152 0.8896 0.7478 0.0265  -0.0489 -0.0005 253  TRP A CB  
1418 C CG  . TRP A 222 ? 1.0636 1.1382 0.9976 0.0196  -0.0508 -0.0044 253  TRP A CG  
1419 C CD1 . TRP A 222 ? 1.0434 1.1071 0.9809 0.0180  -0.0489 -0.0072 253  TRP A CD1 
1420 C CD2 . TRP A 222 ? 0.9375 1.0245 0.8698 0.0131  -0.0552 -0.0053 253  TRP A CD2 
1421 N NE1 . TRP A 222 ? 1.0742 1.1427 1.0126 0.0110  -0.0520 -0.0098 253  TRP A NE1 
1422 C CE2 . TRP A 222 ? 1.1054 1.1881 1.0405 0.0077  -0.0560 -0.0086 253  TRP A CE2 
1423 C CE3 . TRP A 222 ? 0.9084 1.0106 0.8373 0.0110  -0.0587 -0.0033 253  TRP A CE3 
1424 C CZ2 . TRP A 222 ? 1.0159 1.1084 0.9503 0.0001  -0.0605 -0.0097 253  TRP A CZ2 
1425 C CZ3 . TRP A 222 ? 1.0856 1.1977 1.0136 0.0034  -0.0630 -0.0045 253  TRP A CZ3 
1426 C CH2 . TRP A 222 ? 1.0009 1.1079 0.9315 -0.0021 -0.0640 -0.0076 253  TRP A CH2 
1427 N N   . ARG A 223 ? 0.7827 0.8611 0.7062 0.0355  -0.0472 0.0053  254  ARG A N   
1428 C CA  . ARG A 223 ? 0.7071 0.7972 0.6288 0.0388  -0.0484 0.0099  254  ARG A CA  
1429 C C   . ARG A 223 ? 0.8872 0.9760 0.7982 0.0360  -0.0486 0.0056  254  ARG A C   
1430 O O   . ARG A 223 ? 0.7826 0.8837 0.6891 0.0333  -0.0514 0.0053  254  ARG A O   
1431 C CB  . ARG A 223 ? 0.8666 0.9536 0.7938 0.0467  -0.0461 0.0165  254  ARG A CB  
1432 C CG  . ARG A 223 ? 1.1482 1.2488 1.0762 0.0509  -0.0475 0.0228  254  ARG A CG  
1433 C CD  . ARG A 223 ? 1.1908 1.2850 1.1203 0.0572  -0.0452 0.0279  254  ARG A CD  
1434 N NE  . ARG A 223 ? 1.2361 1.3146 1.1692 0.0592  -0.0426 0.0277  254  ARG A NE  
1435 C CZ  . ARG A 223 ? 1.2399 1.3157 1.1806 0.0621  -0.0423 0.0306  254  ARG A CZ  
1436 N NH1 . ARG A 223 ? 1.3012 1.3885 1.2467 0.0638  -0.0443 0.0340  254  ARG A NH1 
1437 N NH2 . ARG A 223 ? 1.1061 1.1675 1.0491 0.0634  -0.0400 0.0301  254  ARG A NH2 
1438 N N   . HIS A 224 ? 0.6942 0.7685 0.6006 0.0369  -0.0456 0.0023  255  HIS A N   
1439 C CA  . HIS A 224 ? 0.7741 0.8463 0.6696 0.0356  -0.0453 -0.0016 255  HIS A CA  
1440 C C   . HIS A 224 ? 0.8019 0.8762 0.6897 0.0278  -0.0483 -0.0087 255  HIS A C   
1441 O O   . HIS A 224 ? 0.7862 0.8680 0.6661 0.0261  -0.0502 -0.0104 255  HIS A O   
1442 C CB  . HIS A 224 ? 0.7786 0.8344 0.6711 0.0381  -0.0412 -0.0036 255  HIS A CB  
1443 C CG  . HIS A 224 ? 0.9729 1.0267 0.8714 0.0451  -0.0387 0.0036  255  HIS A CG  
1444 N ND1 . HIS A 224 ? 1.0231 1.0883 0.9280 0.0493  -0.0401 0.0110  255  HIS A ND1 
1445 C CD2 . HIS A 224 ? 0.8328 0.8745 0.7319 0.0484  -0.0351 0.0050  255  HIS A CD2 
1446 C CE1 . HIS A 224 ? 0.9510 1.0103 0.8600 0.0545  -0.0378 0.0163  255  HIS A CE1 
1447 N NE2 . HIS A 224 ? 0.8051 0.8506 0.7106 0.0539  -0.0348 0.0130  255  HIS A NE2 
1448 N N   . ALA A 225 ? 0.6276 0.6954 0.5174 0.0228  -0.0489 -0.0128 256  ALA A N   
1449 C CA  . ALA A 225 ? 0.8349 0.9041 0.7177 0.0145  -0.0524 -0.0191 256  ALA A CA  
1450 C C   . ALA A 225 ? 0.9071 0.9956 0.7908 0.0119  -0.0568 -0.0159 256  ALA A C   
1451 O O   . ALA A 225 ? 0.7839 0.8772 0.6587 0.0066  -0.0599 -0.0198 256  ALA A O   
1452 C CB  . ALA A 225 ? 0.7030 0.7633 0.5898 0.0097  -0.0526 -0.0225 256  ALA A CB  
1453 N N   . ALA A 226 ? 0.7352 0.8349 0.6293 0.0157  -0.0571 -0.0087 1001 ALA A N   
1454 C CA  . ALA A 226 ? 0.7548 0.8742 0.6509 0.0139  -0.0609 -0.0045 1001 ALA A CA  
1455 C C   . ALA A 226 ? 0.7624 0.8913 0.6530 0.0166  -0.0612 -0.0023 1001 ALA A C   
1456 O O   . ALA A 226 ? 0.8567 0.9991 0.7430 0.0122  -0.0648 -0.0023 1001 ALA A O   
1457 C CB  . ALA A 226 ? 0.7260 0.8539 0.6343 0.0186  -0.0605 0.0029  1001 ALA A CB  
1458 N N   . ASP A 227 ? 0.7754 0.8984 0.6663 0.0236  -0.0578 0.0002  1002 ASP A N   
1459 C CA  . ASP A 227 ? 0.8076 0.9403 0.6940 0.0266  -0.0581 0.0029  1002 ASP A CA  
1460 C C   . ASP A 227 ? 0.8144 0.9426 0.6872 0.0220  -0.0591 -0.0048 1002 ASP A C   
1461 O O   . ASP A 227 ? 0.6947 0.8356 0.5618 0.0204  -0.0614 -0.0046 1002 ASP A O   
1462 C CB  . ASP A 227 ? 0.6675 0.7953 0.5584 0.0352  -0.0545 0.0083  1002 ASP A CB  
1463 C CG  . ASP A 227 ? 0.8026 0.9361 0.7057 0.0403  -0.0541 0.0165  1002 ASP A CG  
1464 O OD1 . ASP A 227 ? 0.8097 0.9532 0.7177 0.0380  -0.0563 0.0183  1002 ASP A OD1 
1465 O OD2 . ASP A 227 ? 0.8489 0.9770 0.7564 0.0467  -0.0516 0.0212  1002 ASP A OD2 
1466 N N   . LEU A 228 ? 0.6711 0.7814 0.5383 0.0199  -0.0572 -0.0117 1003 LEU A N   
1467 C CA  . LEU A 228 ? 0.7400 0.8436 0.5933 0.0156  -0.0581 -0.0198 1003 LEU A CA  
1468 C C   . LEU A 228 ? 0.7474 0.8600 0.5956 0.0068  -0.0632 -0.0236 1003 LEU A C   
1469 O O   . LEU A 228 ? 0.7785 0.8982 0.6171 0.0044  -0.0655 -0.0262 1003 LEU A O   
1470 C CB  . LEU A 228 ? 0.6795 0.7617 0.5290 0.0150  -0.0551 -0.0260 1003 LEU A CB  
1471 C CG  . LEU A 228 ? 0.8136 0.8852 0.6481 0.0107  -0.0557 -0.0353 1003 LEU A CG  
1472 C CD1 . LEU A 228 ? 0.7317 0.8087 0.5571 0.0151  -0.0549 -0.0352 1003 LEU A CD1 
1473 C CD2 . LEU A 228 ? 0.8478 0.8985 0.6804 0.0111  -0.0522 -0.0400 1003 LEU A CD2 
1474 N N   . GLU A 229 ? 0.7279 0.8411 0.5824 0.0018  -0.0653 -0.0235 1004 GLU A N   
1475 C CA  . GLU A 229 ? 0.8095 0.9316 0.6597 -0.0074 -0.0706 -0.0262 1004 GLU A CA  
1476 C C   . GLU A 229 ? 0.8525 0.9976 0.7048 -0.0072 -0.0734 -0.0200 1004 GLU A C   
1477 O O   . GLU A 229 ? 0.8298 0.9832 0.6739 -0.0139 -0.0775 -0.0230 1004 GLU A O   
1478 C CB  . GLU A 229 ? 0.7863 0.9060 0.6445 -0.0119 -0.0720 -0.0259 1004 GLU A CB  
1479 C CG  . GLU A 229 ? 1.0309 1.1535 0.8830 -0.0230 -0.0775 -0.0305 1004 GLU A CG  
1480 C CD  . GLU A 229 ? 1.2335 1.3512 1.0931 -0.0272 -0.0785 -0.0307 1004 GLU A CD  
1481 O OE1 . GLU A 229 ? 0.8934 1.0082 0.7636 -0.0213 -0.0751 -0.0265 1004 GLU A OE1 
1482 O OE2 . GLU A 229 ? 0.9677 1.0845 0.8225 -0.0367 -0.0830 -0.0348 1004 GLU A OE2 
1483 N N   . ASP A 230 ? 0.7926 0.9478 0.6554 0.0004  -0.0713 -0.0114 1005 ASP A N   
1484 C CA  . ASP A 230 ? 0.7207 0.8979 0.5861 0.0015  -0.0733 -0.0047 1005 ASP A CA  
1485 C C   . ASP A 230 ? 0.7504 0.9315 0.6053 0.0022  -0.0736 -0.0071 1005 ASP A C   
1486 O O   . ASP A 230 ? 0.8588 1.0517 0.7067 -0.0037 -0.0774 -0.0088 1005 ASP A O   
1487 C CB  . ASP A 230 ? 0.6328 0.8173 0.5112 0.0103  -0.0706 0.0048  1005 ASP A CB  
1488 C CG  . ASP A 230 ? 1.0849 1.2714 0.9736 0.0098  -0.0711 0.0083  1005 ASP A CG  
1489 O OD1 . ASP A 230 ? 1.2329 1.4240 1.1201 0.0021  -0.0746 0.0060  1005 ASP A OD1 
1490 O OD2 . ASP A 230 ? 1.2121 1.3958 1.1103 0.0171  -0.0682 0.0136  1005 ASP A OD2 
1491 N N   . ASN A 231 ? 0.7449 0.9168 0.5984 0.0094  -0.0696 -0.0070 1006 ASN A N   
1492 C CA  . ASN A 231 ? 0.7812 0.9585 0.6256 0.0114  -0.0695 -0.0082 1006 ASN A CA  
1493 C C   . ASN A 231 ? 0.7346 0.9047 0.5635 0.0040  -0.0720 -0.0184 1006 ASN A C   
1494 O O   . ASN A 231 ? 0.6481 0.8288 0.4686 0.0025  -0.0740 -0.0197 1006 ASN A O   
1495 C CB  . ASN A 231 ? 0.7910 0.9584 0.6366 0.0203  -0.0648 -0.0062 1006 ASN A CB  
1496 C CG  . ASN A 231 ? 0.8389 1.0142 0.6984 0.0276  -0.0629 0.0042  1006 ASN A CG  
1497 O OD1 . ASN A 231 ? 1.0494 1.2125 0.9151 0.0322  -0.0598 0.0062  1006 ASN A OD1 
1498 N ND2 . ASN A 231 ? 0.8532 1.0488 0.7174 0.0287  -0.0648 0.0111  1006 ASN A ND2 
1499 N N   . TRP A 232 ? 0.6207 0.7728 0.4455 -0.0006 -0.0720 -0.0256 1007 TRP A N   
1500 C CA  . TRP A 232 ? 0.7581 0.9016 0.5679 -0.0081 -0.0748 -0.0355 1007 TRP A CA  
1501 C C   . TRP A 232 ? 0.8162 0.9751 0.6234 -0.0172 -0.0807 -0.0356 1007 TRP A C   
1502 O O   . TRP A 232 ? 0.7770 0.9388 0.5715 -0.0219 -0.0837 -0.0410 1007 TRP A O   
1503 C CB  . TRP A 232 ? 0.7043 0.8251 0.5119 -0.0110 -0.0736 -0.0423 1007 TRP A CB  
1504 C CG  . TRP A 232 ? 0.8450 0.9533 0.6368 -0.0183 -0.0763 -0.0528 1007 TRP A CG  
1505 C CD1 . TRP A 232 ? 0.8531 0.9611 0.6406 -0.0289 -0.0815 -0.0572 1007 TRP A CD1 
1506 C CD2 . TRP A 232 ? 0.7411 0.8349 0.5189 -0.0157 -0.0740 -0.0602 1007 TRP A CD2 
1507 N NE1 . TRP A 232 ? 0.7563 0.8492 0.5277 -0.0332 -0.0828 -0.0672 1007 TRP A NE1 
1508 C CE2 . TRP A 232 ? 0.7194 0.8032 0.4843 -0.0248 -0.0781 -0.0695 1007 TRP A CE2 
1509 C CE3 . TRP A 232 ? 0.9075 0.9959 0.6821 -0.0063 -0.0690 -0.0596 1007 TRP A CE3 
1510 C CZ2 . TRP A 232 ? 0.8092 0.8769 0.5578 -0.0243 -0.0771 -0.0786 1007 TRP A CZ2 
1511 C CZ3 . TRP A 232 ? 0.7562 0.8302 0.5151 -0.0055 -0.0678 -0.0681 1007 TRP A CZ3 
1512 C CH2 . TRP A 232 ? 0.8463 0.9096 0.5920 -0.0142 -0.0717 -0.0778 1007 TRP A CH2 
1513 N N   . GLU A 233 ? 0.7488 0.9186 0.5677 -0.0196 -0.0825 -0.0295 1008 GLU A N   
1514 C CA  . GLU A 233 ? 0.8368 1.0234 0.6544 -0.0282 -0.0882 -0.0281 1008 GLU A CA  
1515 C C   . GLU A 233 ? 0.8087 1.0171 0.6256 -0.0260 -0.0892 -0.0226 1008 GLU A C   
1516 O O   . GLU A 233 ? 0.7524 0.9704 0.5600 -0.0332 -0.0936 -0.0254 1008 GLU A O   
1517 C CB  . GLU A 233 ? 0.9315 1.1255 0.7625 -0.0300 -0.0893 -0.0218 1008 GLU A CB  
1518 C CG  . GLU A 233 ? 1.1989 1.4040 1.0271 -0.0412 -0.0955 -0.0223 1008 GLU A CG  
1519 C CD  . GLU A 233 ? 1.4386 1.6252 1.2570 -0.0502 -0.0983 -0.0320 1008 GLU A CD  
1520 O OE1 . GLU A 233 ? 1.2742 1.4397 1.0913 -0.0471 -0.0949 -0.0372 1008 GLU A OE1 
1521 O OE2 . GLU A 233 ? 1.4310 1.6242 1.2429 -0.0606 -0.1041 -0.0342 1008 GLU A OE2 
1522 N N   . THR A 234 ? 0.7828 0.9996 0.6095 -0.0163 -0.0855 -0.0146 1009 THR A N   
1523 C CA  . THR A 234 ? 0.9720 1.2098 0.7989 -0.0136 -0.0861 -0.0088 1009 THR A CA  
1524 C C   . THR A 234 ? 0.7777 1.0113 0.5898 -0.0138 -0.0863 -0.0157 1009 THR A C   
1525 O O   . THR A 234 ? 0.7994 1.0494 0.6057 -0.0169 -0.0891 -0.0150 1009 THR A O   
1526 C CB  . THR A 234 ? 0.8215 1.0662 0.6617 -0.0029 -0.0820 0.0010  1009 THR A CB  
1527 O OG1 . THR A 234 ? 1.0898 1.3171 0.9283 0.0041  -0.0777 -0.0015 1009 THR A OG1 
1528 C CG2 . THR A 234 ? 0.8220 1.0692 0.6759 -0.0018 -0.0817 0.0073  1009 THR A CG2 
1529 N N   . LEU A 235 ? 0.7358 0.9482 0.5415 -0.0103 -0.0831 -0.0222 1010 LEU A N   
1530 C CA  . LEU A 235 ? 0.7056 0.9116 0.4957 -0.0103 -0.0830 -0.0298 1010 LEU A CA  
1531 C C   . LEU A 235 ? 0.7052 0.9124 0.4819 -0.0213 -0.0885 -0.0376 1010 LEU A C   
1532 O O   . LEU A 235 ? 0.6784 0.8956 0.4450 -0.0228 -0.0905 -0.0398 1010 LEU A O   
1533 C CB  . LEU A 235 ? 0.8459 1.0270 0.6315 -0.0057 -0.0788 -0.0358 1010 LEU A CB  
1534 C CG  . LEU A 235 ? 0.7628 0.9344 0.5321 -0.0037 -0.0776 -0.0437 1010 LEU A CG  
1535 C CD1 . LEU A 235 ? 0.8776 1.0646 0.6484 0.0047  -0.0754 -0.0373 1010 LEU A CD1 
1536 C CD2 . LEU A 235 ? 0.9440 1.0900 0.7094 -0.0005 -0.0737 -0.0495 1010 LEU A CD2 
1537 N N   . ASN A 236 ? 0.6544 0.8519 0.4309 -0.0294 -0.0913 -0.0416 1011 ASN A N   
1538 C CA  . ASN A 236 ? 0.7446 0.9421 0.5084 -0.0409 -0.0972 -0.0487 1011 ASN A CA  
1539 C C   . ASN A 236 ? 0.7774 1.0020 0.5447 -0.0461 -0.1015 -0.0420 1011 ASN A C   
1540 O O   . ASN A 236 ? 0.7918 1.0234 0.5468 -0.0524 -0.1056 -0.0463 1011 ASN A O   
1541 C CB  . ASN A 236 ? 0.8028 0.9837 0.5667 -0.0484 -0.0993 -0.0535 1011 ASN A CB  
1542 C CG  . ASN A 236 ? 1.1133 1.2672 0.8729 -0.0441 -0.0951 -0.0604 1011 ASN A CG  
1543 O OD1 . ASN A 236 ? 1.1481 1.2926 0.8978 -0.0387 -0.0922 -0.0653 1011 ASN A OD1 
1544 N ND2 . ASN A 236 ? 1.1261 1.2685 0.8933 -0.0462 -0.0946 -0.0605 1011 ASN A ND2 
1545 N N   . ASP A 237 ? 0.6682 0.9083 0.4518 -0.0433 -0.1007 -0.0315 1012 ASP A N   
1546 C CA  . ASP A 237 ? 0.7471 1.0142 0.5351 -0.0474 -0.1044 -0.0239 1012 ASP A CA  
1547 C C   . ASP A 237 ? 0.7622 1.0442 0.5437 -0.0445 -0.1043 -0.0229 1012 ASP A C   
1548 O O   . ASP A 237 ? 0.7119 1.0069 0.4847 -0.0524 -0.1090 -0.0245 1012 ASP A O   
1549 C CB  . ASP A 237 ? 0.6304 0.9107 0.4372 -0.0417 -0.1021 -0.0122 1012 ASP A CB  
1550 C CG  . ASP A 237 ? 0.8755 1.1464 0.6890 -0.0457 -0.1031 -0.0123 1012 ASP A CG  
1551 O OD1 . ASP A 237 ? 1.0376 1.2989 0.8423 -0.0556 -0.1071 -0.0195 1012 ASP A OD1 
1552 O OD2 . ASP A 237 ? 0.8071 1.0804 0.6346 -0.0391 -0.1000 -0.0050 1012 ASP A OD2 
1553 N N   . ASN A 238 ? 0.6474 0.9284 0.4330 -0.0335 -0.0993 -0.0197 1013 ASN A N   
1554 C CA  . ASN A 238 ? 0.7402 1.0372 0.5213 -0.0298 -0.0989 -0.0175 1013 ASN A CA  
1555 C C   . ASN A 238 ? 0.7285 1.0161 0.4897 -0.0346 -0.1012 -0.0289 1013 ASN A C   
1556 O O   . ASN A 238 ? 0.7457 1.0498 0.4998 -0.0371 -0.1037 -0.0288 1013 ASN A O   
1557 C CB  . ASN A 238 ? 0.6683 0.9650 0.4585 -0.0171 -0.0932 -0.0113 1013 ASN A CB  
1558 C CG  . ASN A 238 ? 0.6504 0.9625 0.4590 -0.0120 -0.0916 0.0012  1013 ASN A CG  
1559 O OD1 . ASN A 238 ? 0.7306 1.0658 0.5445 -0.0101 -0.0922 0.0092  1013 ASN A OD1 
1560 N ND2 . ASN A 238 ? 0.7133 1.0125 0.5314 -0.0095 -0.0894 0.0030  1013 ASN A ND2 
1561 N N   . LEU A 239 ? 0.7268 0.9880 0.4787 -0.0357 -0.1003 -0.0388 1014 LEU A N   
1562 C CA  . LEU A 239 ? 0.8142 1.0638 0.5459 -0.0403 -0.1026 -0.0504 1014 LEU A CA  
1563 C C   . LEU A 239 ? 0.9222 1.1821 0.6452 -0.0532 -0.1096 -0.0536 1014 LEU A C   
1564 O O   . LEU A 239 ? 0.7785 1.0429 0.4869 -0.0564 -0.1122 -0.0592 1014 LEU A O   
1565 C CB  . LEU A 239 ? 0.7597 0.9785 0.4842 -0.0397 -0.1005 -0.0598 1014 LEU A CB  
1566 C CG  . LEU A 239 ? 1.0523 1.2542 0.7554 -0.0420 -0.1017 -0.0724 1014 LEU A CG  
1567 C CD1 . LEU A 239 ? 1.0269 1.2376 0.7237 -0.0332 -0.0987 -0.0719 1014 LEU A CD1 
1568 C CD2 . LEU A 239 ? 0.9352 1.1074 0.6344 -0.0404 -0.0988 -0.0797 1014 LEU A CD2 
1569 N N   . LYS A 240 ? 0.8472 1.1119 0.5786 -0.0607 -0.1128 -0.0498 1015 LYS A N   
1570 C CA  . LYS A 240 ? 0.8648 1.1422 0.5894 -0.0733 -0.1198 -0.0509 1015 LYS A CA  
1571 C C   . LYS A 240 ? 0.7801 1.0889 0.5096 -0.0726 -0.1210 -0.0418 1015 LYS A C   
1572 O O   . LYS A 240 ? 0.9193 1.2393 0.6378 -0.0811 -0.1260 -0.0446 1015 LYS A O   
1573 C CB  . LYS A 240 ? 0.9641 1.2402 0.6973 -0.0811 -0.1229 -0.0479 1015 LYS A CB  
1574 C CG  . LYS A 240 ? 0.9927 1.2396 0.7191 -0.0854 -0.1236 -0.0574 1015 LYS A CG  
1575 C CD  . LYS A 240 ? 1.3335 1.5829 1.0680 -0.0944 -0.1277 -0.0538 1015 LYS A CD  
1576 C CE  . LYS A 240 ? 1.3421 1.6041 1.0975 -0.0869 -0.1238 -0.0419 1015 LYS A CE  
1577 N NZ  . LYS A 240 ? 1.3967 1.6609 1.1601 -0.0947 -0.1274 -0.0383 1015 LYS A NZ  
1578 N N   . VAL A 241 ? 0.6962 1.0196 0.4422 -0.0630 -0.1166 -0.0307 1016 VAL A N   
1579 C CA  . VAL A 241 ? 0.8019 1.1550 0.5532 -0.0611 -0.1170 -0.0217 1016 VAL A CA  
1580 C C   . VAL A 241 ? 0.7328 1.0886 0.4694 -0.0597 -0.1173 -0.0277 1016 VAL A C   
1581 O O   . VAL A 241 ? 0.7770 1.1531 0.5080 -0.0654 -0.1210 -0.0262 1016 VAL A O   
1582 C CB  . VAL A 241 ? 0.6949 1.0587 0.4655 -0.0494 -0.1116 -0.0096 1016 VAL A CB  
1583 C CG1 . VAL A 241 ? 0.6928 1.0858 0.4683 -0.0462 -0.1115 -0.0005 1016 VAL A CG1 
1584 C CG2 . VAL A 241 ? 0.6878 1.0526 0.4723 -0.0512 -0.1119 -0.0032 1016 VAL A CG2 
1585 N N   . ILE A 242 ? 0.7083 1.0442 0.4380 -0.0523 -0.1134 -0.0345 1017 ILE A N   
1586 C CA  A ILE A 242 ? 0.7627 1.1004 0.4777 -0.0498 -0.1133 -0.0406 1017 ILE A CA  
1587 C CA  B ILE A 242 ? 0.7627 1.1001 0.4776 -0.0498 -0.1132 -0.0406 1017 ILE A CA  
1588 C C   . ILE A 242 ? 0.8225 1.1561 0.5183 -0.0622 -0.1196 -0.0509 1017 ILE A C   
1589 O O   . ILE A 242 ? 0.8264 1.1781 0.5143 -0.0655 -0.1224 -0.0511 1017 ILE A O   
1590 C CB  A ILE A 242 ? 0.7444 1.0595 0.4548 -0.0397 -0.1079 -0.0461 1017 ILE A CB  
1591 C CB  B ILE A 242 ? 0.7448 1.0591 0.4548 -0.0399 -0.1079 -0.0464 1017 ILE A CB  
1592 C CG1 A ILE A 242 ? 0.7008 1.0217 0.4298 -0.0279 -0.1022 -0.0351 1017 ILE A CG1 
1593 C CG1 B ILE A 242 ? 0.7013 1.0188 0.4299 -0.0283 -0.1022 -0.0360 1017 ILE A CG1 
1594 C CG2 A ILE A 242 ? 0.7660 1.0822 0.4594 -0.0372 -0.1080 -0.0531 1017 ILE A CG2 
1595 C CG2 B ILE A 242 ? 0.7648 1.0818 0.4591 -0.0366 -0.1077 -0.0525 1017 ILE A CG2 
1596 C CD1 A ILE A 242 ? 0.7240 1.0222 0.4510 -0.0186 -0.0969 -0.0390 1017 ILE A CD1 
1597 C CD1 B ILE A 242 ? 0.8724 1.2173 0.6106 -0.0218 -0.1006 -0.0251 1017 ILE A CD1 
1598 N N   . GLU A 243 ? 0.8972 1.2071 0.5853 -0.0693 -0.1220 -0.0597 1018 GLU A N   
1599 C CA  . GLU A 243 ? 0.9836 1.2856 0.6521 -0.0813 -0.1282 -0.0704 1018 GLU A CA  
1600 C C   . GLU A 243 ? 0.9540 1.2819 0.6241 -0.0922 -0.1344 -0.0648 1018 GLU A C   
1601 O O   . GLU A 243 ? 0.9738 1.3062 0.6280 -0.1001 -0.1392 -0.0711 1018 GLU A O   
1602 C CB  . GLU A 243 ? 0.9662 1.2384 0.6289 -0.0870 -0.1297 -0.0792 1018 GLU A CB  
1603 C CG  . GLU A 243 ? 1.1556 1.4014 0.8140 -0.0769 -0.1239 -0.0858 1018 GLU A CG  
1604 C CD  . GLU A 243 ? 1.5131 1.7315 1.1702 -0.0813 -0.1244 -0.0920 1018 GLU A CD  
1605 O OE1 . GLU A 243 ? 1.4344 1.6545 1.0945 -0.0922 -0.1295 -0.0909 1018 GLU A OE1 
1606 O OE2 . GLU A 243 ? 1.2159 1.4120 0.8695 -0.0737 -0.1197 -0.0973 1018 GLU A OE2 
1607 N N   . LYS A 244 ? 0.9640 1.3094 0.6526 -0.0926 -0.1341 -0.0528 1019 LYS A N   
1608 C CA  A LYS A 244 ? 1.0413 1.4126 0.7333 -0.1027 -0.1396 -0.0459 1019 LYS A CA  
1609 C CA  B LYS A 244 ? 1.0413 1.4126 0.7332 -0.1028 -0.1396 -0.0459 1019 LYS A CA  
1610 C C   . LYS A 244 ? 0.9930 1.3963 0.6956 -0.0965 -0.1373 -0.0343 1019 LYS A C   
1611 O O   . LYS A 244 ? 0.8753 1.3033 0.5831 -0.1034 -0.1410 -0.0263 1019 LYS A O   
1612 C CB  A LYS A 244 ? 1.0290 1.4000 0.7339 -0.1079 -0.1412 -0.0398 1019 LYS A CB  
1613 C CB  B LYS A 244 ? 1.0291 1.4002 0.7338 -0.1081 -0.1413 -0.0399 1019 LYS A CB  
1614 C CG  A LYS A 244 ? 1.0387 1.3802 0.7343 -0.1152 -0.1440 -0.0502 1019 LYS A CG  
1615 C CG  B LYS A 244 ? 1.0390 1.3790 0.7361 -0.1135 -0.1430 -0.0499 1019 LYS A CG  
1616 C CD  A LYS A 244 ? 0.9522 1.2956 0.6612 -0.1202 -0.1457 -0.0435 1019 LYS A CD  
1617 C CD  B LYS A 244 ? 1.0013 1.3288 0.6761 -0.1256 -0.1496 -0.0622 1019 LYS A CD  
1618 C CE  A LYS A 244 ? 0.9221 1.2701 0.6516 -0.1077 -0.1390 -0.0336 1019 LYS A CE  
1619 C CE  B LYS A 244 ? 1.0603 1.3544 0.7273 -0.1293 -0.1505 -0.0726 1019 LYS A CE  
1620 N NZ  A LYS A 244 ? 0.7779 1.1586 0.5212 -0.1053 -0.1385 -0.0199 1019 LYS A NZ  
1621 N NZ  B LYS A 244 ? 1.0904 1.3621 0.7553 -0.1168 -0.1437 -0.0786 1019 LYS A NZ  
1622 N N   . ALA A 245 ? 0.8152 1.2189 0.5212 -0.0838 -0.1316 -0.0326 1020 ALA A N   
1623 C CA  . ALA A 245 ? 0.9213 1.3547 0.6389 -0.0772 -0.1292 -0.0209 1020 ALA A CA  
1624 C C   . ALA A 245 ? 0.9090 1.3651 0.6162 -0.0857 -0.1342 -0.0212 1020 ALA A C   
1625 O O   . ALA A 245 ? 0.7743 1.2201 0.4619 -0.0920 -0.1378 -0.0327 1020 ALA A O   
1626 C CB  . ALA A 245 ? 0.9063 1.3343 0.6264 -0.0631 -0.1229 -0.0205 1020 ALA A CB  
1627 N N   . ASP A 246 ? 0.7576 1.2448 0.4777 -0.0857 -0.1345 -0.0084 1021 ASP A N   
1628 C CA  . ASP A 246 ? 1.0491 1.5623 0.7619 -0.0926 -0.1386 -0.0065 1021 ASP A CA  
1629 C C   . ASP A 246 ? 0.8342 1.3713 0.5552 -0.0824 -0.1346 0.0021  1021 ASP A C   
1630 O O   . ASP A 246 ? 0.7530 1.3092 0.4654 -0.0865 -0.1373 0.0017  1021 ASP A O   
1631 C CB  . ASP A 246 ? 0.8644 1.3981 0.5839 -0.1035 -0.1433 0.0017  1021 ASP A CB  
1632 C CG  . ASP A 246 ? 1.1378 1.6860 0.8805 -0.0962 -0.1393 0.0164  1021 ASP A CG  
1633 O OD1 . ASP A 246 ? 1.1490 1.7195 0.9029 -0.0880 -0.1359 0.0267  1021 ASP A OD1 
1634 O OD2 . ASP A 246 ? 1.3298 1.8669 1.0792 -0.0986 -0.1397 0.0178  1021 ASP A OD2 
1635 N N   . ASN A 247 ? 0.7991 1.3355 0.5361 -0.0697 -0.1285 0.0100  1022 ASN A N   
1636 C CA  . ASN A 247 ? 0.8649 1.4219 0.6104 -0.0594 -0.1246 0.0185  1022 ASN A CA  
1637 C C   . ASN A 247 ? 0.8693 1.4061 0.6177 -0.0467 -0.1190 0.0162  1022 ASN A C   
1638 O O   . ASN A 247 ? 0.7474 1.2573 0.4958 -0.0449 -0.1173 0.0109  1022 ASN A O   
1639 C CB  . ASN A 247 ? 0.8322 1.4170 0.5981 -0.0566 -0.1232 0.0350  1022 ASN A CB  
1640 C CG  . ASN A 247 ? 0.8603 1.4325 0.6420 -0.0506 -0.1197 0.0409  1022 ASN A CG  
1641 O OD1 . ASN A 247 ? 0.9528 1.5159 0.7435 -0.0392 -0.1147 0.0440  1022 ASN A OD1 
1642 N ND2 . ASN A 247 ? 1.1818 1.7540 0.9670 -0.0584 -0.1225 0.0428  1022 ASN A ND2 
1643 N N   . ALA A 248 ? 0.7691 1.3204 0.5205 -0.0379 -0.1160 0.0211  1023 ALA A N   
1644 C CA  . ALA A 248 ? 0.7935 1.3283 0.5462 -0.0261 -0.1111 0.0192  1023 ALA A CA  
1645 C C   . ALA A 248 ? 0.7696 1.2979 0.5416 -0.0178 -0.1067 0.0286  1023 ALA A C   
1646 O O   . ALA A 248 ? 0.6580 1.1634 0.4301 -0.0110 -0.1033 0.0249  1023 ALA A O   
1647 C CB  . ALA A 248 ? 0.8248 1.3796 0.5758 -0.0194 -0.1096 0.0228  1023 ALA A CB  
1648 N N   . ALA A 249 ? 0.7626 1.3105 0.5505 -0.0182 -0.1068 0.0407  1024 ALA A N   
1649 C CA  . ALA A 249 ? 0.7321 1.2739 0.5380 -0.0100 -0.1028 0.0497  1024 ALA A CA  
1650 C C   . ALA A 249 ? 0.8059 1.3178 0.6098 -0.0123 -0.1025 0.0423  1024 ALA A C   
1651 O O   . ALA A 249 ? 0.8212 1.3164 0.6328 -0.0043 -0.0987 0.0438  1024 ALA A O   
1652 C CB  . ALA A 249 ? 1.0266 1.5947 0.8482 -0.0105 -0.1033 0.0634  1024 ALA A CB  
1653 N N   . GLN A 250 ? 0.9342 1.4395 0.7279 -0.0235 -0.1067 0.0345  1025 GLN A N   
1654 C CA  . GLN A 250 ? 0.8318 1.3101 0.6239 -0.0263 -0.1067 0.0277  1025 GLN A CA  
1655 C C   . GLN A 250 ? 0.6504 1.1008 0.4324 -0.0217 -0.1042 0.0174  1025 GLN A C   
1656 O O   . GLN A 250 ? 0.6438 1.0733 0.4312 -0.0175 -0.1014 0.0161  1025 GLN A O   
1657 C CB  . GLN A 250 ? 0.7862 1.2640 0.5681 -0.0400 -0.1124 0.0215  1025 GLN A CB  
1658 C CG  . GLN A 250 ? 0.9880 1.4925 0.7796 -0.0454 -0.1151 0.0319  1025 GLN A CG  
1659 C CD  . GLN A 250 ? 1.2072 1.7127 0.9867 -0.0599 -0.1214 0.0256  1025 GLN A CD  
1660 O OE1 . GLN A 250 ? 1.0379 1.5456 0.8018 -0.0665 -0.1249 0.0179  1025 GLN A OE1 
1661 N NE2 . GLN A 250 ? 1.3064 1.8101 1.0928 -0.0649 -0.1231 0.0287  1025 GLN A NE2 
1662 N N   . VAL A 251 ? 0.7125 1.1626 0.4796 -0.0221 -0.1050 0.0099  1026 VAL A N   
1663 C CA  . VAL A 251 ? 0.6731 1.0970 0.4288 -0.0178 -0.1027 -0.0004 1026 VAL A CA  
1664 C C   . VAL A 251 ? 0.7273 1.1457 0.4952 -0.0052 -0.0970 0.0064  1026 VAL A C   
1665 O O   . VAL A 251 ? 0.6879 1.0822 0.4565 -0.0017 -0.0943 0.0026  1026 VAL A O   
1666 C CB  . VAL A 251 ? 0.6914 1.1189 0.4285 -0.0198 -0.1046 -0.0088 1026 VAL A CB  
1667 C CG1 . VAL A 251 ? 0.6994 1.1024 0.4258 -0.0129 -0.1012 -0.0176 1026 VAL A CG1 
1668 C CG2 . VAL A 251 ? 0.7090 1.1362 0.4319 -0.0334 -0.1107 -0.0172 1026 VAL A CG2 
1669 N N   . LYS A 252 ? 0.7343 1.1753 0.5122 0.0017  -0.0953 0.0170  1027 LYS A N   
1670 C CA  A LYS A 252 ? 0.7584 1.1954 0.5482 0.0132  -0.0905 0.0244  1027 LYS A CA  
1671 C CA  B LYS A 252 ? 0.7584 1.1953 0.5482 0.0132  -0.0905 0.0244  1027 LYS A CA  
1672 C C   . LYS A 252 ? 0.7451 1.1711 0.5495 0.0150  -0.0887 0.0298  1027 LYS A C   
1673 O O   . LYS A 252 ? 0.7721 1.1790 0.5801 0.0212  -0.0853 0.0293  1027 LYS A O   
1674 C CB  A LYS A 252 ? 0.8293 1.2947 0.6282 0.0191  -0.0897 0.0359  1027 LYS A CB  
1675 C CB  B LYS A 252 ? 0.8294 1.2945 0.6283 0.0192  -0.0897 0.0358  1027 LYS A CB  
1676 C CG  A LYS A 252 ? 0.8574 1.3208 0.6687 0.0307  -0.0854 0.0446  1027 LYS A CG  
1677 C CG  B LYS A 252 ? 0.8076 1.2821 0.5931 0.0207  -0.0902 0.0313  1027 LYS A CG  
1678 C CD  A LYS A 252 ? 0.8066 1.2525 0.6071 0.0361  -0.0829 0.0375  1027 LYS A CD  
1679 C CD  B LYS A 252 ? 0.9052 1.4074 0.7015 0.0275  -0.0891 0.0436  1027 LYS A CD  
1680 C CE  A LYS A 252 ? 0.7925 1.2354 0.6058 0.0467  -0.0790 0.0468  1027 LYS A CE  
1681 C CE  B LYS A 252 ? 0.8718 1.4007 0.6772 0.0223  -0.0917 0.0521  1027 LYS A CE  
1682 N NZ  A LYS A 252 ? 0.7621 1.2326 0.5880 0.0516  -0.0789 0.0601  1027 LYS A NZ  
1683 N NZ  B LYS A 252 ? 0.7997 1.3553 0.6170 0.0294  -0.0904 0.0650  1027 LYS A NZ  
1684 N N   . ASP A 253 ? 0.7636 1.2018 0.5763 0.0096  -0.0910 0.0351  1028 ASP A N   
1685 C CA  . ASP A 253 ? 0.7120 1.1406 0.5379 0.0114  -0.0894 0.0400  1028 ASP A CA  
1686 C C   . ASP A 253 ? 0.7102 1.1090 0.5289 0.0085  -0.0889 0.0296  1028 ASP A C   
1687 O O   . ASP A 253 ? 0.7767 1.1594 0.6031 0.0143  -0.0857 0.0312  1028 ASP A O   
1688 C CB  . ASP A 253 ? 0.8293 1.2768 0.6627 0.0054  -0.0922 0.0465  1028 ASP A CB  
1689 C CG  . ASP A 253 ? 1.3015 1.7781 1.1457 0.0098  -0.0918 0.0590  1028 ASP A CG  
1690 O OD1 . ASP A 253 ? 1.2845 1.7660 1.1316 0.0176  -0.0894 0.0632  1028 ASP A OD1 
1691 O OD2 . ASP A 253 ? 1.2412 1.7364 1.0912 0.0053  -0.0939 0.0653  1028 ASP A OD2 
1692 N N   . ALA A 254 ? 0.6708 1.0621 0.4748 -0.0007 -0.0923 0.0189  1029 ALA A N   
1693 C CA  . ALA A 254 ? 0.6291 0.9928 0.4264 -0.0043 -0.0923 0.0091  1029 ALA A CA  
1694 C C   . ALA A 254 ? 0.6905 1.0336 0.4821 0.0030  -0.0883 0.0038  1029 ALA A C   
1695 O O   . ALA A 254 ? 0.6718 0.9936 0.4661 0.0050  -0.0860 0.0010  1029 ALA A O   
1696 C CB  . ALA A 254 ? 0.7820 1.1427 0.5643 -0.0162 -0.0973 -0.0007 1029 ALA A CB  
1697 N N   . LEU A 255 ? 0.6893 1.0394 0.4733 0.0073  -0.0874 0.0028  1030 LEU A N   
1698 C CA  . LEU A 255 ? 0.7158 1.0487 0.4948 0.0151  -0.0834 -0.0009 1030 LEU A CA  
1699 C C   . LEU A 255 ? 0.6219 0.9529 0.4171 0.0244  -0.0793 0.0090  1030 LEU A C   
1700 O O   . LEU A 255 ? 0.6692 0.9800 0.4640 0.0290  -0.0761 0.0063  1030 LEU A O   
1701 C CB  . LEU A 255 ? 0.6657 1.0096 0.4335 0.0183  -0.0835 -0.0030 1030 LEU A CB  
1702 C CG  . LEU A 255 ? 0.7205 1.0588 0.4681 0.0107  -0.0868 -0.0156 1030 LEU A CG  
1703 C CD1 . LEU A 255 ? 0.6791 1.0335 0.4176 0.0145  -0.0869 -0.0157 1030 LEU A CD1 
1704 C CD2 . LEU A 255 ? 0.6816 0.9889 0.4179 0.0101  -0.0853 -0.0268 1030 LEU A CD2 
1705 N N   . THR A 256 ? 0.7652 1.1168 0.5747 0.0272  -0.0795 0.0206  1031 THR A N   
1706 C CA  . THR A 256 ? 0.6859 1.0352 0.5106 0.0356  -0.0760 0.0302  1031 THR A CA  
1707 C C   . THR A 256 ? 0.6664 0.9962 0.4974 0.0342  -0.0750 0.0286  1031 THR A C   
1708 O O   . THR A 256 ? 0.7823 1.0971 0.6185 0.0401  -0.0718 0.0303  1031 THR A O   
1709 C CB  . THR A 256 ? 0.8529 1.2280 0.6910 0.0385  -0.0767 0.0429  1031 THR A CB  
1710 O OG1 . THR A 256 ? 0.8025 1.1963 0.6355 0.0405  -0.0774 0.0449  1031 THR A OG1 
1711 C CG2 . THR A 256 ? 0.7163 1.0871 0.5696 0.0468  -0.0736 0.0527  1031 THR A CG2 
1712 N N   . LYS A 257 ? 0.7049 1.0354 0.5355 0.0262  -0.0779 0.0257  1032 LYS A N   
1713 C CA  . LYS A 257 ? 0.6211 0.9342 0.4572 0.0245  -0.0771 0.0238  1032 LYS A CA  
1714 C C   . LYS A 257 ? 0.6937 0.9810 0.5188 0.0227  -0.0759 0.0128  1032 LYS A C   
1715 O O   . LYS A 257 ? 0.7002 0.9703 0.5308 0.0255  -0.0733 0.0125  1032 LYS A O   
1716 C CB  . LYS A 257 ? 0.6873 1.0104 0.5259 0.0163  -0.0808 0.0244  1032 LYS A CB  
1717 C CG  . LYS A 257 ? 0.7789 1.1271 0.6296 0.0187  -0.0815 0.0362  1032 LYS A CG  
1718 C CD  . LYS A 257 ? 0.9482 1.3110 0.7982 0.0098  -0.0856 0.0366  1032 LYS A CD  
1719 C CE  . LYS A 257 ? 0.9973 1.3872 0.8582 0.0125  -0.0861 0.0487  1032 LYS A CE  
1720 N NZ  . LYS A 257 ? 1.1276 1.5355 0.9859 0.0034  -0.0903 0.0494  1032 LYS A NZ  
1721 N N   . MET A 258 ? 0.6343 0.9182 0.4437 0.0184  -0.0775 0.0037  1033 MET A N   
1722 C CA  . MET A 258 ? 0.6769 0.9357 0.4752 0.0174  -0.0760 -0.0067 1033 MET A CA  
1723 C C   . MET A 258 ? 0.7131 0.9609 0.5141 0.0271  -0.0711 -0.0042 1033 MET A C   
1724 O O   . MET A 258 ? 0.8495 1.0764 0.6500 0.0283  -0.0687 -0.0083 1033 MET A O   
1725 C CB  . MET A 258 ? 0.7521 1.0096 0.5320 0.0119  -0.0787 -0.0168 1033 MET A CB  
1726 C CG  . MET A 258 ? 0.8135 1.0740 0.5878 0.0004  -0.0838 -0.0219 1033 MET A CG  
1727 S SD  . MET A 258 ? 0.8719 1.1266 0.6227 -0.0061 -0.0871 -0.0348 1033 MET A SD  
1728 C CE  . MET A 258 ? 0.8015 1.0230 0.5429 -0.0026 -0.0833 -0.0447 1033 MET A CE  
1729 N N   . ARG A 259 ? 0.7710 1.0336 0.5753 0.0340  -0.0698 0.0029  1034 ARG A N   
1730 C CA  . ARG A 259 ? 0.7864 1.0407 0.5937 0.0430  -0.0655 0.0066  1034 ARG A CA  
1731 C C   . ARG A 259 ? 0.7483 0.9930 0.5699 0.0461  -0.0634 0.0127  1034 ARG A C   
1732 O O   . ARG A 259 ? 0.8614 1.0878 0.6826 0.0494  -0.0602 0.0107  1034 ARG A O   
1733 C CB  . ARG A 259 ? 0.6936 0.9683 0.5035 0.0493  -0.0652 0.0147  1034 ARG A CB  
1734 C CG  . ARG A 259 ? 0.9886 1.2559 0.7993 0.0582  -0.0612 0.0183  1034 ARG A CG  
1735 C CD  . ARG A 259 ? 0.8835 1.1725 0.6981 0.0644  -0.0611 0.0274  1034 ARG A CD  
1736 N NE  . ARG A 259 ? 1.1390 1.4215 0.9528 0.0724  -0.0577 0.0306  1034 ARG A NE  
1737 C CZ  . ARG A 259 ? 1.1090 1.3857 0.9347 0.0774  -0.0555 0.0388  1034 ARG A CZ  
1738 N NH1 . ARG A 259 ? 1.2348 1.5100 1.0737 0.0760  -0.0562 0.0442  1034 ARG A NH1 
1739 N NH2 . ARG A 259 ? 1.2234 1.4955 1.0470 0.0841  -0.0527 0.0418  1034 ARG A NH2 
1740 N N   . ALA A 260 ? 0.7377 0.9948 0.5719 0.0452  -0.0649 0.0203  1035 ALA A N   
1741 C CA  . ALA A 260 ? 0.7628 1.0113 0.6103 0.0484  -0.0630 0.0260  1035 ALA A CA  
1742 C C   . ALA A 260 ? 0.8204 1.0485 0.6653 0.0435  -0.0627 0.0181  1035 ALA A C   
1743 O O   . ALA A 260 ? 0.9038 1.1157 0.7529 0.0468  -0.0598 0.0184  1035 ALA A O   
1744 C CB  . ALA A 260 ? 0.7133 0.9798 0.5734 0.0487  -0.0648 0.0353  1035 ALA A CB  
1745 N N   . ALA A 261 ? 0.7602 0.9894 0.5985 0.0352  -0.0658 0.0113  1036 ALA A N   
1746 C CA  . ALA A 261 ? 0.7699 0.9810 0.6059 0.0299  -0.0659 0.0041  1036 ALA A CA  
1747 C C   . ALA A 261 ? 0.9462 1.1361 0.7725 0.0315  -0.0631 -0.0035 1036 ALA A C   
1748 O O   . ALA A 261 ? 0.9109 1.0837 0.7404 0.0318  -0.0610 -0.0056 1036 ALA A O   
1749 C CB  . ALA A 261 ? 0.7568 0.9742 0.5862 0.0202  -0.0704 -0.0015 1036 ALA A CB  
1750 N N   . ALA A 262 ? 0.8020 0.9932 0.6165 0.0330  -0.0628 -0.0075 1037 ALA A N   
1751 C CA  . ALA A 262 ? 0.9385 1.1103 0.7430 0.0354  -0.0597 -0.0143 1037 ALA A CA  
1752 C C   . ALA A 262 ? 1.0388 1.2022 0.8523 0.0432  -0.0553 -0.0080 1037 ALA A C   
1753 O O   . ALA A 262 ? 0.9896 1.1341 0.8018 0.0436  -0.0527 -0.0120 1037 ALA A O   
1754 C CB  . ALA A 262 ? 0.9774 1.1548 0.7679 0.0371  -0.0599 -0.0184 1037 ALA A CB  
1755 N N   . LEU A 263 ? 1.0090 1.1863 0.8319 0.0493  -0.0546 0.0021  1038 LEU A N   
1756 C CA  . LEU A 263 ? 1.0954 1.2654 0.9270 0.0562  -0.0511 0.0089  1038 LEU A CA  
1757 C C   . LEU A 263 ? 1.0579 1.2175 0.9002 0.0545  -0.0505 0.0105  1038 LEU A C   
1758 O O   . LEU A 263 ? 1.0714 1.2150 0.9154 0.0567  -0.0475 0.0099  1038 LEU A O   
1759 C CB  . LEU A 263 ? 0.9897 1.1776 0.8290 0.0623  -0.0512 0.0197  1038 LEU A CB  
1760 C CG  . LEU A 263 ? 0.9481 1.1459 0.7776 0.0658  -0.0509 0.0194  1038 LEU A CG  
1761 C CD1 . LEU A 263 ? 1.2208 1.4395 1.0590 0.0706  -0.0519 0.0306  1038 LEU A CD1 
1762 C CD2 . LEU A 263 ? 1.0223 1.2053 0.8449 0.0706  -0.0471 0.0171  1038 LEU A CD2 
1763 N N   . ASP A 264 ? 1.0137 1.1829 0.8634 0.0507  -0.0534 0.0127  1039 ASP A N   
1764 C CA  . ASP A 264 ? 1.0194 1.1799 0.8789 0.0494  -0.0530 0.0141  1039 ASP A CA  
1765 C C   . ASP A 264 ? 1.0875 1.2295 0.9408 0.0444  -0.0522 0.0047  1039 ASP A C   
1766 O O   . ASP A 264 ? 1.2121 1.3405 1.0709 0.0457  -0.0499 0.0050  1039 ASP A O   
1767 C CB  . ASP A 264 ? 0.8070 0.9828 0.6741 0.0465  -0.0562 0.0181  1039 ASP A CB  
1768 C CG  . ASP A 264 ? 1.1708 1.3633 1.0465 0.0522  -0.0565 0.0287  1039 ASP A CG  
1769 O OD1 . ASP A 264 ? 1.1143 1.3030 0.9939 0.0586  -0.0542 0.0341  1039 ASP A OD1 
1770 O OD2 . ASP A 264 ? 1.1934 1.4031 1.0721 0.0502  -0.0592 0.0319  1039 ASP A OD2 
1771 N N   . ALA A 265 ? 0.9470 1.0881 0.7888 0.0384  -0.0542 -0.0037 1040 ALA A N   
1772 C CA  . ALA A 265 ? 1.0718 1.1945 0.9070 0.0336  -0.0536 -0.0127 1040 ALA A CA  
1773 C C   . ALA A 265 ? 1.0975 1.2038 0.9287 0.0387  -0.0491 -0.0144 1040 ALA A C   
1774 O O   . ALA A 265 ? 1.1231 1.2134 0.9552 0.0372  -0.0472 -0.0180 1040 ALA A O   
1775 C CB  . ALA A 265 ? 0.8666 0.9907 0.6887 0.0265  -0.0570 -0.0212 1040 ALA A CB  
1776 N N   . GLN A 266 ? 0.9860 1.0971 0.8131 0.0447  -0.0473 -0.0113 1041 GLN A N   
1777 C CA  . GLN A 266 ? 1.0139 1.1116 0.8376 0.0502  -0.0429 -0.0115 1041 GLN A CA  
1778 C C   . GLN A 266 ? 1.1555 1.2471 0.9921 0.0537  -0.0404 -0.0046 1041 GLN A C   
1779 O O   . GLN A 266 ? 1.2003 1.2759 1.0364 0.0542  -0.0374 -0.0071 1041 GLN A O   
1780 C CB  . GLN A 266 ? 0.9995 1.1069 0.8169 0.0561  -0.0419 -0.0084 1041 GLN A CB  
1781 C CG  . GLN A 266 ? 1.0584 1.1538 0.8704 0.0620  -0.0373 -0.0084 1041 GLN A CG  
1782 C CD  . GLN A 266 ? 1.0506 1.1573 0.8558 0.0680  -0.0366 -0.0053 1041 GLN A CD  
1783 O OE1 . GLN A 266 ? 1.1841 1.3083 0.9952 0.0703  -0.0384 0.0020  1041 GLN A OE1 
1784 N NE2 . GLN A 266 ? 1.1276 1.2248 0.9202 0.0708  -0.0337 -0.0106 1041 GLN A NE2 
1785 N N   . LYS A 267 ? 1.1276 1.2315 0.9755 0.0562  -0.0417 0.0042  1042 LYS A N   
1786 C CA  . LYS A 267 ? 1.0582 1.1561 0.9176 0.0596  -0.0398 0.0108  1042 LYS A CA  
1787 C C   . LYS A 267 ? 1.1974 1.2829 1.0611 0.0551  -0.0395 0.0065  1042 LYS A C   
1788 O O   . LYS A 267 ? 1.1686 1.2414 1.0362 0.0569  -0.0367 0.0076  1042 LYS A O   
1789 C CB  . LYS A 267 ? 0.9747 1.0877 0.8446 0.0627  -0.0418 0.0203  1042 LYS A CB  
1790 N N   . ALA A 268 ? 1.2907 1.3805 1.1537 0.0491  -0.0426 0.0020  1043 ALA A N   
1791 C CA  . ALA A 268 ? 1.2633 1.3434 1.1308 0.0447  -0.0427 -0.0017 1043 ALA A CA  
1792 C C   . ALA A 268 ? 1.2169 1.2793 1.0771 0.0424  -0.0402 -0.0092 1043 ALA A C   
1793 O O   . ALA A 268 ? 1.2179 1.2704 1.0829 0.0400  -0.0393 -0.0111 1043 ALA A O   
1794 C CB  . ALA A 268 ? 1.2203 1.3108 1.0881 0.0384  -0.0469 -0.0042 1043 ALA A CB  
1795 N N   . THR A 269 ? 1.1380 1.1965 0.9866 0.0433  -0.0389 -0.0134 1044 THR A N   
1796 C CA  . THR A 269 ? 1.2884 1.3294 1.1296 0.0421  -0.0360 -0.0201 1044 THR A CA  
1797 C C   . THR A 269 ? 1.4342 1.4663 1.2801 0.0481  -0.0314 -0.0151 1044 THR A C   
1798 O O   . THR A 269 ? 1.4441 1.4825 1.2907 0.0539  -0.0302 -0.0087 1044 THR A O   
1799 C CB  . THR A 269 ? 1.4149 1.4543 1.2409 0.0418  -0.0361 -0.0265 1044 THR A CB  
1800 O OG1 . THR A 269 ? 1.4034 1.4501 1.2244 0.0352  -0.0407 -0.0316 1044 THR A OG1 
1801 C CG2 . THR A 269 ? 1.4020 1.4225 1.2198 0.0417  -0.0326 -0.0330 1044 THR A CG2 
1802 N N   . PRO A 270 ? 1.5661 1.5846 1.4155 0.0465  -0.0291 -0.0172 1045 PRO A N   
1803 C CA  . PRO A 270 ? 1.4316 1.4422 1.2852 0.0516  -0.0248 -0.0120 1045 PRO A CA  
1804 C C   . PRO A 270 ? 1.5986 1.6063 1.4421 0.0564  -0.0218 -0.0120 1045 PRO A C   
1805 O O   . PRO A 270 ? 1.6883 1.6935 1.5199 0.0551  -0.0220 -0.0188 1045 PRO A O   
1806 C CB  . PRO A 270 ? 1.4268 1.4234 1.2835 0.0477  -0.0230 -0.0163 1045 PRO A CB  
1807 C CG  . PRO A 270 ? 1.3462 1.3406 1.1960 0.0413  -0.0257 -0.0250 1045 PRO A CG  
1808 C CD  . PRO A 270 ? 1.4244 1.4346 1.2740 0.0398  -0.0302 -0.0239 1045 PRO A CD  
1809 N N   . PRO A 271 ? 1.8131 1.8212 1.6604 0.0621  -0.0191 -0.0044 1046 PRO A N   
1810 C CA  . PRO A 271 ? 1.8479 1.8566 1.6863 0.0677  -0.0163 -0.0027 1046 PRO A CA  
1811 C C   . PRO A 271 ? 1.9558 1.9491 1.7858 0.0681  -0.0121 -0.0082 1046 PRO A C   
1812 O O   . PRO A 271 ? 1.9564 1.9383 1.7888 0.0641  -0.0110 -0.0125 1046 PRO A O   
1813 C CB  . PRO A 271 ? 1.8315 1.8456 1.6786 0.0727  -0.0153 0.0084  1046 PRO A CB  
1814 C CG  . PRO A 271 ? 1.7835 1.7910 1.6419 0.0698  -0.0154 0.0103  1046 PRO A CG  
1815 C CD  . PRO A 271 ? 1.6476 1.6563 1.5076 0.0639  -0.0187 0.0037  1046 PRO A CD  
1816 N N   . LYS A 272 ? 1.9168 1.9108 1.7370 0.0734  -0.0095 -0.0076 1047 LYS A N   
1817 C CA  . LYS A 272 ? 1.9456 1.9257 1.7563 0.0750  -0.0051 -0.0126 1047 LYS A CA  
1818 C C   . LYS A 272 ? 1.9332 1.9043 1.7513 0.0765  -0.0010 -0.0073 1047 LYS A C   
1819 O O   . LYS A 272 ? 1.8800 1.8384 1.6987 0.0732  0.0010  -0.0121 1047 LYS A O   
1820 C CB  . LYS A 272 ? 1.8095 1.7940 1.6077 0.0815  -0.0031 -0.0122 1047 LYS A CB  
1821 N N   . LEU A 273 ? 1.9262 1.9044 1.7504 0.0812  0.0002  0.0030  1048 LEU A N   
1822 C CA  . LEU A 273 ? 1.7838 1.7546 1.6139 0.0829  0.0041  0.0088  1048 LEU A CA  
1823 C C   . LEU A 273 ? 1.5504 1.5313 1.3860 0.0877  0.0043  0.0207  1048 LEU A C   
1824 O O   . LEU A 273 ? 1.5034 1.4971 1.3398 0.0895  0.0010  0.0245  1048 LEU A O   
1825 C CB  . LEU A 273 ? 1.5457 1.5048 1.3657 0.0854  0.0094  0.0047  1048 LEU A CB  
1826 N N   . GLU A 274 ? 1.4189 1.3945 1.2586 0.0895  0.0078  0.0271  1049 GLU A N   
1827 C CA  . GLU A 274 ? 1.1529 1.1370 0.9983 0.0933  0.0076  0.0392  1049 GLU A CA  
1828 C C   . GLU A 274 ? 1.2310 1.2105 1.0728 0.0974  0.0129  0.0446  1049 GLU A C   
1829 O O   . GLU A 274 ? 1.0520 1.0257 0.9008 0.0958  0.0147  0.0495  1049 GLU A O   
1830 C CB  . GLU A 274 ? 0.9896 0.9735 0.8483 0.0895  0.0047  0.0440  1049 GLU A CB  
1831 N N   . MET A 283 ? 1.6142 1.5621 1.4121 0.0625  -0.0048 -0.0356 1058 MET A N   
1832 C CA  . MET A 283 ? 1.8489 1.7973 1.6315 0.0649  -0.0052 -0.0411 1058 MET A CA  
1833 C C   . MET A 283 ? 1.8577 1.8237 1.6405 0.0649  -0.0097 -0.0387 1058 MET A C   
1834 O O   . MET A 283 ? 1.7918 1.7670 1.5852 0.0610  -0.0134 -0.0356 1058 MET A O   
1835 C CB  . MET A 283 ? 1.6930 1.6277 1.4656 0.0592  -0.0064 -0.0524 1058 MET A CB  
1836 C CG  . MET A 283 ? 1.7486 1.6808 1.5034 0.0616  -0.0067 -0.0594 1058 MET A CG  
1837 S SD  . MET A 283 ? 1.9855 1.9116 1.7300 0.0726  0.0004  -0.0568 1058 MET A SD  
1838 C CE  . MET A 283 ? 1.6674 1.6091 1.4009 0.0776  -0.0019 -0.0565 1058 MET A CE  
1839 N N   . LYS A 284 ? 1.8597 1.8308 1.6307 0.0698  -0.0093 -0.0398 1059 LYS A N   
1840 C CA  . LYS A 284 ? 1.8002 1.7886 1.5699 0.0702  -0.0132 -0.0378 1059 LYS A CA  
1841 C C   . LYS A 284 ? 1.6691 1.6555 1.4216 0.0697  -0.0147 -0.0471 1059 LYS A C   
1842 O O   . LYS A 284 ? 1.6570 1.6532 1.4018 0.0750  -0.0145 -0.0455 1059 LYS A O   
1843 C CB  . LYS A 284 ? 1.8256 1.8271 1.6005 0.0778  -0.0114 -0.0269 1059 LYS A CB  
1844 C CG  . LYS A 284 ? 1.8122 1.8236 1.6040 0.0766  -0.0134 -0.0178 1059 LYS A CG  
1845 C CD  . LYS A 284 ? 1.7229 1.7449 1.5197 0.0838  -0.0116 -0.0066 1059 LYS A CD  
1846 C CE  . LYS A 284 ? 1.6579 1.6972 1.4501 0.0869  -0.0142 -0.0042 1059 LYS A CE  
1847 N NZ  . LYS A 284 ? 1.4749 1.5255 1.2724 0.0937  -0.0128 0.0074  1059 LYS A NZ  
1848 N N   . ASP A 285 ? 1.6685 1.6418 1.4144 0.0631  -0.0163 -0.0569 1060 ASP A N   
1849 C CA  . ASP A 285 ? 1.4687 1.4389 1.1983 0.0606  -0.0190 -0.0666 1060 ASP A CA  
1850 C C   . ASP A 285 ? 1.5448 1.5251 1.2770 0.0521  -0.0255 -0.0692 1060 ASP A C   
1851 O O   . ASP A 285 ? 1.4613 1.4526 1.1857 0.0518  -0.0286 -0.0712 1060 ASP A O   
1852 C CB  . ASP A 285 ? 1.5412 1.4887 1.2597 0.0588  -0.0168 -0.0761 1060 ASP A CB  
1853 C CG  . ASP A 285 ? 1.4366 1.3785 1.1375 0.0552  -0.0201 -0.0870 1060 ASP A CG  
1854 O OD1 . ASP A 285 ? 1.5890 1.5339 1.2771 0.0614  -0.0188 -0.0888 1060 ASP A OD1 
1855 O OD2 . ASP A 285 ? 1.2984 1.2331 0.9980 0.0460  -0.0243 -0.0936 1060 ASP A OD2 
1856 N N   . PHE A 286 ? 1.3591 1.3366 1.1023 0.0450  -0.0278 -0.0690 1061 PHE A N   
1857 C CA  . PHE A 286 ? 1.2785 1.2694 1.0278 0.0378  -0.0337 -0.0684 1061 PHE A CA  
1858 C C   . PHE A 286 ? 1.3273 1.3395 1.0842 0.0422  -0.0346 -0.0593 1061 PHE A C   
1859 O O   . PHE A 286 ? 1.2161 1.2423 0.9710 0.0390  -0.0389 -0.0596 1061 PHE A O   
1860 C CB  . PHE A 286 ? 1.3594 1.3457 1.1216 0.0316  -0.0349 -0.0673 1061 PHE A CB  
1861 C CG  . PHE A 286 ? 1.2678 1.2674 1.0361 0.0241  -0.0408 -0.0665 1061 PHE A CG  
1862 C CD1 . PHE A 286 ? 1.2761 1.2753 1.0337 0.0167  -0.0456 -0.0742 1061 PHE A CD1 
1863 C CD2 . PHE A 286 ? 1.2619 1.2740 1.0461 0.0245  -0.0416 -0.0580 1061 PHE A CD2 
1864 C CE1 . PHE A 286 ? 1.1822 1.1949 0.9455 0.0096  -0.0510 -0.0726 1061 PHE A CE1 
1865 C CE2 . PHE A 286 ? 1.1899 1.2150 0.9796 0.0182  -0.0467 -0.0567 1061 PHE A CE2 
1866 C CZ  . PHE A 286 ? 1.1407 1.1669 0.9203 0.0107  -0.0514 -0.0637 1061 PHE A CZ  
1867 N N   . ARG A 287 ? 1.3657 1.3808 1.1315 0.0494  -0.0306 -0.0507 1062 ARG A N   
1868 C CA  . ARG A 287 ? 1.3272 1.3616 1.1006 0.0540  -0.0314 -0.0413 1062 ARG A CA  
1869 C C   . ARG A 287 ? 1.1985 1.2422 0.9595 0.0582  -0.0317 -0.0427 1062 ARG A C   
1870 O O   . ARG A 287 ? 1.3853 1.4463 1.1478 0.0572  -0.0351 -0.0399 1062 ARG A O   
1871 C CB  . ARG A 287 ? 1.4934 1.5267 1.2778 0.0604  -0.0273 -0.0320 1062 ARG A CB  
1872 C CG  . ARG A 287 ? 1.4143 1.4512 1.2152 0.0578  -0.0286 -0.0258 1062 ARG A CG  
1873 C CD  . ARG A 287 ? 1.4267 1.4693 1.2375 0.0645  -0.0262 -0.0149 1062 ARG A CD  
1874 N NE  . ARG A 287 ? 1.4357 1.4851 1.2612 0.0628  -0.0283 -0.0085 1062 ARG A NE  
1875 C CZ  . ARG A 287 ? 1.5613 1.6190 1.3963 0.0674  -0.0279 0.0014  1062 ARG A CZ  
1876 N NH1 . ARG A 287 ? 1.5219 1.5839 1.3543 0.0737  -0.0258 0.0069  1062 ARG A NH1 
1877 N NH2 . ARG A 287 ? 1.5064 1.5682 1.3536 0.0658  -0.0299 0.0061  1062 ARG A NH2 
1878 N N   . HIS A 288 ? 1.2575 1.2907 1.0064 0.0633  -0.0279 -0.0466 1063 HIS A N   
1879 C CA  . HIS A 288 ? 1.2815 1.3232 1.0176 0.0681  -0.0279 -0.0482 1063 HIS A CA  
1880 C C   . HIS A 288 ? 1.2808 1.3262 1.0062 0.0615  -0.0329 -0.0568 1063 HIS A C   
1881 O O   . HIS A 288 ? 1.1443 1.2022 0.8615 0.0642  -0.0342 -0.0571 1063 HIS A O   
1882 C CB  . HIS A 288 ? 1.1726 1.2002 0.8966 0.0750  -0.0227 -0.0515 1063 HIS A CB  
1883 C CG  . HIS A 288 ? 1.1064 1.1431 0.8172 0.0815  -0.0220 -0.0524 1063 HIS A CG  
1884 N ND1 . HIS A 288 ? 1.1597 1.1892 0.8523 0.0802  -0.0231 -0.0634 1063 HIS A ND1 
1885 C CD2 . HIS A 288 ? 1.1172 1.1697 0.8302 0.0895  -0.0203 -0.0437 1063 HIS A CD2 
1886 C CE1 . HIS A 288 ? 1.1947 1.2355 0.8786 0.0875  -0.0220 -0.0616 1063 HIS A CE1 
1887 N NE2 . HIS A 288 ? 1.1389 1.1944 0.8353 0.0932  -0.0203 -0.0494 1063 HIS A NE2 
1888 N N   . GLY A 289 ? 1.1734 1.2090 0.8986 0.0525  -0.0358 -0.0635 1064 GLY A N   
1889 C CA  . GLY A 289 ? 1.1392 1.1809 0.8567 0.0449  -0.0414 -0.0699 1064 GLY A CA  
1890 C C   . GLY A 289 ? 1.1151 1.1811 0.8423 0.0437  -0.0449 -0.0623 1064 GLY A C   
1891 O O   . GLY A 289 ? 0.9676 1.0449 0.6866 0.0411  -0.0485 -0.0652 1064 GLY A O   
1892 N N   . PHE A 290 ? 1.0344 1.1086 0.7789 0.0457  -0.0440 -0.0523 1065 PHE A N   
1893 C CA  . PHE A 290 ? 1.0940 1.1912 0.8485 0.0461  -0.0467 -0.0439 1065 PHE A CA  
1894 C C   . PHE A 290 ? 1.0490 1.1594 0.8009 0.0546  -0.0447 -0.0382 1065 PHE A C   
1895 O O   . PHE A 290 ? 1.0478 1.1780 0.8017 0.0546  -0.0475 -0.0340 1065 PHE A O   
1896 C CB  . PHE A 290 ? 0.9265 1.0267 0.6996 0.0460  -0.0463 -0.0353 1065 PHE A CB  
1897 C CG  . PHE A 290 ? 0.9474 1.0402 0.7250 0.0376  -0.0489 -0.0393 1065 PHE A CG  
1898 C CD1 . PHE A 290 ? 0.8362 0.9416 0.6151 0.0306  -0.0539 -0.0399 1065 PHE A CD1 
1899 C CD2 . PHE A 290 ? 1.1603 1.2350 0.9413 0.0367  -0.0464 -0.0416 1065 PHE A CD2 
1900 C CE1 . PHE A 290 ? 0.8301 0.9303 0.6135 0.0230  -0.0565 -0.0427 1065 PHE A CE1 
1901 C CE2 . PHE A 290 ? 1.1871 1.2565 0.9729 0.0291  -0.0489 -0.0446 1065 PHE A CE2 
1902 C CZ  . PHE A 290 ? 1.0733 1.1556 0.8602 0.0223  -0.0540 -0.0451 1065 PHE A CZ  
1903 N N   . ASP A 291 ? 1.2011 1.3020 0.9488 0.0620  -0.0400 -0.0374 1066 ASP A N   
1904 C CA  . ASP A 291 ? 1.0636 1.1776 0.8088 0.0705  -0.0381 -0.0313 1066 ASP A CA  
1905 C C   . ASP A 291 ? 1.1412 1.2642 0.8713 0.0699  -0.0405 -0.0376 1066 ASP A C   
1906 O O   . ASP A 291 ? 1.0117 1.1549 0.7437 0.0731  -0.0418 -0.0317 1066 ASP A O   
1907 C CB  . ASP A 291 ? 1.0639 1.1651 0.8058 0.0781  -0.0326 -0.0299 1066 ASP A CB  
1908 C CG  . ASP A 291 ? 1.2065 1.3052 0.9646 0.0805  -0.0303 -0.0203 1066 ASP A CG  
1909 O OD1 . ASP A 291 ? 1.0925 1.2058 0.8638 0.0807  -0.0323 -0.0113 1066 ASP A OD1 
1910 O OD2 . ASP A 291 ? 1.2081 1.2900 0.9656 0.0822  -0.0266 -0.0218 1066 ASP A OD2 
1911 N N   . ILE A 292 ? 0.9933 1.1013 0.7080 0.0657  -0.0413 -0.0497 1067 ILE A N   
1912 C CA  . ILE A 292 ? 1.1547 1.2695 0.8535 0.0646  -0.0438 -0.0567 1067 ILE A CA  
1913 C C   . ILE A 292 ? 1.0608 1.1891 0.7623 0.0554  -0.0498 -0.0578 1067 ILE A C   
1914 O O   . ILE A 292 ? 0.9926 1.1340 0.6848 0.0546  -0.0524 -0.0603 1067 ILE A O   
1915 C CB  . ILE A 292 ? 1.3328 1.4251 1.0126 0.0641  -0.0424 -0.0693 1067 ILE A CB  
1916 C CG1 . ILE A 292 ? 1.2048 1.2795 0.8847 0.0542  -0.0448 -0.0767 1067 ILE A CG1 
1917 C CG2 . ILE A 292 ? 1.2604 1.3411 0.9375 0.0739  -0.0361 -0.0672 1067 ILE A CG2 
1918 C CD1 . ILE A 292 ? 1.1963 1.2715 0.8640 0.0452  -0.0504 -0.0861 1067 ILE A CD1 
1919 N N   . LEU A 293 ? 0.9363 1.0627 0.6501 0.0486  -0.0519 -0.0557 1068 LEU A N   
1920 C CA  . LEU A 293 ? 0.9125 1.0555 0.6314 0.0409  -0.0572 -0.0541 1068 LEU A CA  
1921 C C   . LEU A 293 ? 0.9345 1.1029 0.6648 0.0457  -0.0574 -0.0425 1068 LEU A C   
1922 O O   . LEU A 293 ? 0.7894 0.9756 0.5159 0.0434  -0.0607 -0.0421 1068 LEU A O   
1923 C CB  . LEU A 293 ? 0.8795 1.0152 0.6095 0.0336  -0.0590 -0.0536 1068 LEU A CB  
1924 C CG  . LEU A 293 ? 1.0610 1.1795 0.7805 0.0243  -0.0618 -0.0649 1068 LEU A CG  
1925 C CD1 . LEU A 293 ? 1.1796 1.2936 0.9127 0.0186  -0.0631 -0.0622 1068 LEU A CD1 
1926 C CD2 . LEU A 293 ? 1.0502 1.1787 0.7576 0.0171  -0.0672 -0.0707 1068 LEU A CD2 
1927 N N   . VAL A 294 ? 0.7919 0.9622 0.5362 0.0523  -0.0541 -0.0327 1069 VAL A N   
1928 C CA  . VAL A 294 ? 0.9974 1.1903 0.7523 0.0576  -0.0542 -0.0212 1069 VAL A CA  
1929 C C   . VAL A 294 ? 0.8473 1.0517 0.5905 0.0628  -0.0538 -0.0222 1069 VAL A C   
1930 O O   . VAL A 294 ? 0.8756 1.1023 0.6216 0.0631  -0.0561 -0.0170 1069 VAL A O   
1931 C CB  . VAL A 294 ? 0.8689 1.0582 0.6383 0.0641  -0.0506 -0.0115 1069 VAL A CB  
1932 C CG1 . VAL A 294 ? 0.8959 1.1074 0.6753 0.0701  -0.0507 0.0005  1069 VAL A CG1 
1933 C CG2 . VAL A 294 ? 0.8139 0.9946 0.5954 0.0592  -0.0513 -0.0101 1069 VAL A CG2 
1934 N N   . GLY A 295 ? 0.8992 1.0894 0.6291 0.0672  -0.0507 -0.0286 1070 GLY A N   
1935 C CA  . GLY A 295 ? 0.9505 1.1510 0.6678 0.0727  -0.0501 -0.0302 1070 GLY A CA  
1936 C C   . GLY A 295 ? 0.9653 1.1753 0.6711 0.0660  -0.0547 -0.0376 1070 GLY A C   
1937 O O   . GLY A 295 ? 0.9773 1.2091 0.6824 0.0681  -0.0563 -0.0335 1070 GLY A O   
1938 N N   . GLN A 296 ? 0.8852 1.0794 0.5820 0.0574  -0.0571 -0.0484 1071 GLN A N   
1939 C CA  . GLN A 296 ? 0.8743 1.0764 0.5598 0.0496  -0.0621 -0.0556 1071 GLN A CA  
1940 C C   . GLN A 296 ? 0.8195 1.0461 0.5187 0.0450  -0.0658 -0.0470 1071 GLN A C   
1941 O O   . GLN A 296 ? 0.8973 1.1423 0.5909 0.0429  -0.0688 -0.0472 1071 GLN A O   
1942 C CB  . GLN A 296 ? 0.9024 1.0817 0.5774 0.0406  -0.0644 -0.0676 1071 GLN A CB  
1943 C CG  . GLN A 296 ? 1.0236 1.1788 0.6818 0.0447  -0.0611 -0.0776 1071 GLN A CG  
1944 C CD  . GLN A 296 ? 1.0083 1.1404 0.6571 0.0355  -0.0636 -0.0889 1071 GLN A CD  
1945 O OE1 . GLN A 296 ? 1.1734 1.3068 0.8298 0.0262  -0.0675 -0.0885 1071 GLN A OE1 
1946 N NE2 . GLN A 296 ? 1.1510 1.2618 0.7829 0.0383  -0.0614 -0.0987 1071 GLN A NE2 
1947 N N   . ILE A 297 ? 0.8187 1.0462 0.5357 0.0436  -0.0655 -0.0392 1072 ILE A N   
1948 C CA  . ILE A 297 ? 0.8104 1.0610 0.5410 0.0403  -0.0685 -0.0302 1072 ILE A CA  
1949 C C   . ILE A 297 ? 0.7688 1.0424 0.5052 0.0483  -0.0673 -0.0203 1072 ILE A C   
1950 O O   . ILE A 297 ? 0.8293 1.1256 0.5683 0.0458  -0.0702 -0.0161 1072 ILE A O   
1951 C CB  . ILE A 297 ? 0.7771 1.0224 0.5249 0.0386  -0.0680 -0.0239 1072 ILE A CB  
1952 C CG1 . ILE A 297 ? 0.7732 1.0002 0.5158 0.0294  -0.0702 -0.0331 1072 ILE A CG1 
1953 C CG2 . ILE A 297 ? 0.7887 1.0585 0.5513 0.0376  -0.0702 -0.0130 1072 ILE A CG2 
1954 C CD1 . ILE A 297 ? 0.8174 1.0347 0.5748 0.0287  -0.0689 -0.0287 1072 ILE A CD1 
1955 N N   . ASP A 298 ? 0.8019 1.0708 0.5407 0.0578  -0.0629 -0.0159 1073 ASP A N   
1956 C CA  . ASP A 298 ? 0.9344 1.2250 0.6784 0.0656  -0.0619 -0.0062 1073 ASP A CA  
1957 C C   . ASP A 298 ? 0.6742 0.9764 0.4021 0.0660  -0.0634 -0.0120 1073 ASP A C   
1958 O O   . ASP A 298 ? 0.8449 1.1720 0.5770 0.0678  -0.0649 -0.0050 1073 ASP A O   
1959 C CB  . ASP A 298 ? 0.9262 1.2082 0.6751 0.0751  -0.0572 -0.0004 1073 ASP A CB  
1960 C CG  . ASP A 298 ? 1.0922 1.3670 0.8587 0.0755  -0.0559 0.0075  1073 ASP A CG  
1961 O OD1 . ASP A 298 ? 1.1470 1.4335 0.9260 0.0719  -0.0583 0.0137  1073 ASP A OD1 
1962 O OD2 . ASP A 298 ? 1.2958 1.5534 1.0633 0.0796  -0.0524 0.0077  1073 ASP A OD2 
1963 N N   . ASP A 299 ? 0.7038 0.9883 0.4130 0.0645  -0.0630 -0.0247 1074 ASP A N   
1964 C CA  . ASP A 299 ? 0.7109 1.0045 0.4028 0.0640  -0.0649 -0.0318 1074 ASP A CA  
1965 C C   . ASP A 299 ? 0.7368 1.0479 0.4293 0.0547  -0.0702 -0.0324 1074 ASP A C   
1966 O O   . ASP A 299 ? 0.7324 1.0664 0.4223 0.0559  -0.0719 -0.0294 1074 ASP A O   
1967 C CB  . ASP A 299 ? 0.9166 1.1845 0.5878 0.0630  -0.0640 -0.0463 1074 ASP A CB  
1968 C CG  . ASP A 299 ? 1.1710 1.4231 0.8401 0.0728  -0.0585 -0.0457 1074 ASP A CG  
1969 O OD1 . ASP A 299 ? 1.1460 1.4099 0.8272 0.0809  -0.0556 -0.0342 1074 ASP A OD1 
1970 O OD2 . ASP A 299 ? 1.0571 1.2849 0.7123 0.0723  -0.0570 -0.0563 1074 ASP A OD2 
1971 N N   . ALA A 300 ? 0.7120 1.0137 0.4080 0.0452  -0.0730 -0.0357 1075 ALA A N   
1972 C CA  . ALA A 300 ? 0.7299 1.0483 0.4265 0.0357  -0.0781 -0.0357 1075 ALA A CA  
1973 C C   . ALA A 300 ? 0.6954 1.0418 0.4105 0.0382  -0.0784 -0.0212 1075 ALA A C   
1974 O O   . ALA A 300 ? 0.7350 1.1039 0.4491 0.0344  -0.0817 -0.0191 1075 ALA A O   
1975 C CB  . ALA A 300 ? 0.7163 1.0188 0.4136 0.0254  -0.0809 -0.0413 1075 ALA A CB  
1976 N N   . LEU A 301 ? 0.6944 1.0400 0.4265 0.0446  -0.0752 -0.0112 1076 LEU A N   
1977 C CA  . LEU A 301 ? 0.7436 1.1142 0.4933 0.0478  -0.0753 0.0028  1076 LEU A CA  
1978 C C   . LEU A 301 ? 0.8070 1.1985 0.5543 0.0549  -0.0745 0.0079  1076 LEU A C   
1979 O O   . LEU A 301 ? 0.8311 1.2487 0.5860 0.0543  -0.0763 0.0159  1076 LEU A O   
1980 C CB  . LEU A 301 ? 0.7120 1.0738 0.4789 0.0528  -0.0723 0.0116  1076 LEU A CB  
1981 C CG  . LEU A 301 ? 0.7523 1.1029 0.5272 0.0460  -0.0736 0.0108  1076 LEU A CG  
1982 C CD1 . LEU A 301 ? 0.9632 1.2991 0.7509 0.0515  -0.0701 0.0165  1076 LEU A CD1 
1983 C CD2 . LEU A 301 ? 0.8155 1.1891 0.6004 0.0411  -0.0768 0.0180  1076 LEU A CD2 
1984 N N   . LYS A 302 ? 0.7350 1.1165 0.4721 0.0620  -0.0715 0.0039  1077 LYS A N   
1985 C CA  . LYS A 302 ? 0.9084 1.3103 0.6420 0.0690  -0.0708 0.0084  1077 LYS A CA  
1986 C C   . LYS A 302 ? 0.7879 1.2067 0.5095 0.0630  -0.0747 0.0027  1077 LYS A C   
1987 O O   . LYS A 302 ? 0.7846 1.2311 0.5125 0.0647  -0.0759 0.0110  1077 LYS A O   
1988 C CB  . LYS A 302 ? 0.8184 1.2053 0.5405 0.0773  -0.0670 0.0036  1077 LYS A CB  
1989 C CG  . LYS A 302 ? 1.0749 1.4835 0.7983 0.0867  -0.0654 0.0119  1077 LYS A CG  
1990 C CD  . LYS A 302 ? 1.2806 1.6748 0.9927 0.0954  -0.0614 0.0080  1077 LYS A CD  
1991 C CE  . LYS A 302 ? 1.4470 1.8309 1.1346 0.0938  -0.0620 -0.0071 1077 LYS A CE  
1992 N NZ  . LYS A 302 ? 1.2067 1.6161 0.8865 0.0941  -0.0645 -0.0073 1077 LYS A NZ  
1993 N N   . LEU A 303 ? 0.7247 1.1274 0.4291 0.0557  -0.0768 -0.0111 1078 LEU A N   
1994 C CA  . LEU A 303 ? 0.8204 1.2374 0.5124 0.0486  -0.0811 -0.0172 1078 LEU A CA  
1995 C C   . LEU A 303 ? 0.7448 1.1849 0.4510 0.0419  -0.0844 -0.0084 1078 LEU A C   
1996 O O   . LEU A 303 ? 0.8103 1.2765 0.5159 0.0409  -0.0865 -0.0046 1078 LEU A O   
1997 C CB  . LEU A 303 ? 0.7916 1.1840 0.4640 0.0406  -0.0834 -0.0332 1078 LEU A CB  
1998 C CG  . LEU A 303 ? 0.8500 1.2198 0.5046 0.0467  -0.0804 -0.0436 1078 LEU A CG  
1999 C CD1 . LEU A 303 ? 0.7839 1.1257 0.4234 0.0380  -0.0826 -0.0579 1078 LEU A CD1 
2000 C CD2 . LEU A 303 ? 0.7827 1.1684 0.4236 0.0520  -0.0805 -0.0461 1078 LEU A CD2 
2001 N N   . ALA A 304 ? 0.7637 1.1955 0.4829 0.0376  -0.0847 -0.0047 1079 ALA A N   
2002 C CA  . ALA A 304 ? 0.8279 1.2807 0.5599 0.0314  -0.0876 0.0035  1079 ALA A CA  
2003 C C   . ALA A 304 ? 0.7050 1.1854 0.4533 0.0387  -0.0861 0.0184  1079 ALA A C   
2004 O O   . ALA A 304 ? 0.7616 1.2676 0.5152 0.0349  -0.0887 0.0246  1079 ALA A O   
2005 C CB  . ALA A 304 ? 0.6831 1.1205 0.4257 0.0268  -0.0878 0.0048  1079 ALA A CB  
2006 N N   . ASN A 305 ? 0.9103 1.3864 0.6669 0.0489  -0.0821 0.0249  1080 ASN A N   
2007 C CA  . ASN A 305 ? 0.8766 1.3774 0.6493 0.0559  -0.0809 0.0397  1080 ASN A CA  
2008 C C   . ASN A 305 ? 0.8685 1.3924 0.6333 0.0593  -0.0815 0.0407  1080 ASN A C   
2009 O O   . ASN A 305 ? 0.9888 1.5400 0.7655 0.0617  -0.0821 0.0522  1080 ASN A O   
2010 C CB  . ASN A 305 ? 0.8289 1.3171 0.6130 0.0650  -0.0769 0.0467  1080 ASN A CB  
2011 C CG  . ASN A 305 ? 1.1480 1.6186 0.9434 0.0625  -0.0763 0.0487  1080 ASN A CG  
2012 O OD1 . ASN A 305 ? 1.0548 1.5337 0.8584 0.0568  -0.0784 0.0521  1080 ASN A OD1 
2013 N ND2 . ASN A 305 ? 1.1316 1.5786 0.9274 0.0669  -0.0733 0.0467  1080 ASN A ND2 
2014 N N   . GLU A 306 ? 0.7401 1.2540 0.4851 0.0598  -0.0815 0.0290  1081 GLU A N   
2015 C CA  . GLU A 306 ? 0.7529 1.2884 0.4880 0.0625  -0.0824 0.0282  1081 GLU A CA  
2016 C C   . GLU A 306 ? 0.7186 1.2714 0.4463 0.0526  -0.0869 0.0242  1081 GLU A C   
2017 O O   . GLU A 306 ? 0.8111 1.3836 0.5302 0.0539  -0.0881 0.0233  1081 GLU A O   
2018 C CB  . GLU A 306 ? 0.7206 1.2381 0.4359 0.0673  -0.0805 0.0168  1081 GLU A CB  
2019 C CG  . GLU A 306 ? 0.9196 1.4223 0.6408 0.0774  -0.0759 0.0212  1081 GLU A CG  
2020 C CD  . GLU A 306 ? 0.9202 1.4014 0.6213 0.0817  -0.0737 0.0091  1081 GLU A CD  
2021 O OE1 . GLU A 306 ? 0.9670 1.4453 0.6487 0.0775  -0.0758 -0.0029 1081 GLU A OE1 
2022 O OE2 . GLU A 306 ? 1.0478 1.5147 0.7521 0.0893  -0.0699 0.0117  1081 GLU A OE2 
2023 N N   . GLY A 307 ? 0.8197 1.3665 0.5503 0.0429  -0.0895 0.0220  1082 GLY A N   
2024 C CA  . GLY A 307 ? 0.6949 1.2564 0.4177 0.0324  -0.0941 0.0179  1082 GLY A CA  
2025 C C   . GLY A 307 ? 0.7177 1.2574 0.4180 0.0242  -0.0970 0.0011  1082 GLY A C   
2026 O O   . GLY A 307 ? 0.7289 1.2798 0.4201 0.0147  -0.1013 -0.0033 1082 GLY A O   
2027 N N   . LYS A 308 ? 0.7255 1.2344 0.4163 0.0272  -0.0947 -0.0081 1083 LYS A N   
2028 C CA  . LYS A 308 ? 0.7660 1.2513 0.4348 0.0200  -0.0973 -0.0245 1083 LYS A CA  
2029 C C   . LYS A 308 ? 0.7460 1.2095 0.4191 0.0121  -0.0986 -0.0276 1083 LYS A C   
2030 O O   . LYS A 308 ? 0.7503 1.1850 0.4184 0.0138  -0.0966 -0.0347 1083 LYS A O   
2031 C CB  . LYS A 308 ? 0.7866 1.2527 0.4406 0.0289  -0.0938 -0.0329 1083 LYS A CB  
2032 C CG  . LYS A 308 ? 0.8163 1.3045 0.4660 0.0378  -0.0923 -0.0293 1083 LYS A CG  
2033 C CD  . LYS A 308 ? 0.8579 1.3274 0.4958 0.0483  -0.0881 -0.0354 1083 LYS A CD  
2034 C CE  . LYS A 308 ? 0.9118 1.4050 0.5469 0.0581  -0.0863 -0.0304 1083 LYS A CE  
2035 N NZ  . LYS A 308 ? 1.1411 1.6595 0.8001 0.0644  -0.0843 -0.0127 1083 LYS A NZ  
2036 N N   . VAL A 309 ? 0.7385 1.2176 0.4215 0.0036  -0.1019 -0.0217 1084 VAL A N   
2037 C CA  . VAL A 309 ? 0.7336 1.1969 0.4233 -0.0036 -0.1033 -0.0225 1084 VAL A CA  
2038 C C   . VAL A 309 ? 0.7562 1.1980 0.4259 -0.0141 -0.1074 -0.0374 1084 VAL A C   
2039 O O   . VAL A 309 ? 0.7575 1.1743 0.4267 -0.0171 -0.1072 -0.0426 1084 VAL A O   
2040 C CB  . VAL A 309 ? 0.7459 1.2345 0.4532 -0.0083 -0.1052 -0.0101 1084 VAL A CB  
2041 C CG1 . VAL A 309 ? 0.7122 1.1854 0.4270 -0.0148 -0.1064 -0.0101 1084 VAL A CG1 
2042 C CG2 . VAL A 309 ? 0.6974 1.2060 0.4236 0.0024  -0.1013 0.0046  1084 VAL A CG2 
2043 N N   . LYS A 310 ? 0.7748 1.2258 0.4278 -0.0201 -0.1114 -0.0445 1085 LYS A N   
2044 C CA  . LYS A 310 ? 0.7995 1.2274 0.4310 -0.0294 -0.1154 -0.0598 1085 LYS A CA  
2045 C C   . LYS A 310 ? 0.8081 1.2034 0.4297 -0.0225 -0.1116 -0.0693 1085 LYS A C   
2046 O O   . LYS A 310 ? 0.8159 1.1850 0.4320 -0.0280 -0.1128 -0.0771 1085 LYS A O   
2047 C CB  . LYS A 310 ? 0.8194 1.2618 0.4329 -0.0345 -0.1195 -0.0662 1085 LYS A CB  
2048 C CG  . LYS A 310 ? 0.8478 1.2674 0.4373 -0.0450 -0.1246 -0.0821 1085 LYS A CG  
2049 C CD  . LYS A 310 ? 0.9028 1.3335 0.4726 -0.0460 -0.1272 -0.0895 1085 LYS A CD  
2050 C CE  . LYS A 310 ? 1.0482 1.4557 0.5929 -0.0568 -0.1327 -0.1057 1085 LYS A CE  
2051 N NZ  . LYS A 310 ? 1.2871 1.7086 0.8303 -0.0726 -0.1400 -0.1048 1085 LYS A NZ  
2052 N N   . GLU A 311 ? 0.8063 1.2038 0.4262 -0.0101 -0.1069 -0.0679 1086 GLU A N   
2053 C CA  . GLU A 311 ? 0.8127 1.1817 0.4246 -0.0021 -0.1026 -0.0752 1086 GLU A CA  
2054 C C   . GLU A 311 ? 0.7945 1.1485 0.4235 0.0005  -0.0993 -0.0694 1086 GLU A C   
2055 O O   . GLU A 311 ? 0.8348 1.1599 0.4568 0.0011  -0.0977 -0.0774 1086 GLU A O   
2056 C CB  . GLU A 311 ? 0.8119 1.1912 0.4209 0.0111  -0.0982 -0.0723 1086 GLU A CB  
2057 C CG  . GLU A 311 ? 0.8349 1.2217 0.4222 0.0106  -0.1007 -0.0813 1086 GLU A CG  
2058 C CD  . GLU A 311 ? 0.8332 1.2525 0.4235 0.0040  -0.1050 -0.0758 1086 GLU A CD  
2059 O OE1 . GLU A 311 ? 0.8133 1.2511 0.4233 0.0007  -0.1059 -0.0640 1086 GLU A OE1 
2060 O OE2 . GLU A 311 ? 0.8523 1.2790 0.4248 0.0024  -0.1075 -0.0832 1086 GLU A OE2 
2061 N N   . ALA A 312 ? 0.8165 1.1896 0.4677 0.0022  -0.0982 -0.0556 1087 ALA A N   
2062 C CA  . ALA A 312 ? 0.7532 1.1130 0.4205 0.0046  -0.0953 -0.0500 1087 ALA A CA  
2063 C C   . ALA A 312 ? 0.7587 1.1017 0.4240 -0.0068 -0.0989 -0.0561 1087 ALA A C   
2064 O O   . ALA A 312 ? 0.7565 1.0755 0.4238 -0.0059 -0.0968 -0.0594 1087 ALA A O   
2065 C CB  . ALA A 312 ? 0.7287 1.1130 0.4191 0.0090  -0.0937 -0.0340 1087 ALA A CB  
2066 N N   . GLN A 313 ? 0.7657 1.1220 0.4273 -0.0179 -0.1045 -0.0572 1088 GLN A N   
2067 C CA  . GLN A 313 ? 0.7726 1.1145 0.4312 -0.0296 -0.1087 -0.0629 1088 GLN A CA  
2068 C C   . GLN A 313 ? 0.7951 1.1059 0.4335 -0.0324 -0.1095 -0.0780 1088 GLN A C   
2069 O O   . GLN A 313 ? 0.8253 1.1133 0.4652 -0.0350 -0.1091 -0.0818 1088 GLN A O   
2070 C CB  . GLN A 313 ? 0.7776 1.1420 0.4345 -0.0410 -0.1149 -0.0608 1088 GLN A CB  
2071 C CG  . GLN A 313 ? 0.7867 1.1384 0.4391 -0.0543 -0.1201 -0.0664 1088 GLN A CG  
2072 C CD  . GLN A 313 ? 0.7935 1.1680 0.4426 -0.0660 -0.1264 -0.0643 1088 GLN A CD  
2073 O OE1 . GLN A 313 ? 0.8626 1.2534 0.5022 -0.0666 -0.1282 -0.0656 1088 GLN A OE1 
2074 N NE2 . GLN A 313 ? 0.8963 1.2730 0.5532 -0.0754 -0.1300 -0.0607 1088 GLN A NE2 
2075 N N   . ALA A 314 ? 0.8154 1.1247 0.4343 -0.0318 -0.1106 -0.0868 1089 ALA A N   
2076 C CA  . ALA A 314 ? 0.9497 1.2290 0.5476 -0.0342 -0.1116 -0.1017 1089 ALA A CA  
2077 C C   . ALA A 314 ? 0.8864 1.1409 0.4873 -0.0248 -0.1056 -0.1034 1089 ALA A C   
2078 O O   . ALA A 314 ? 1.0426 1.2691 0.6314 -0.0281 -0.1061 -0.1140 1089 ALA A O   
2079 C CB  . ALA A 314 ? 0.8612 1.1448 0.4383 -0.0323 -0.1128 -0.1099 1089 ALA A CB  
2080 N N   . ALA A 315 ? 0.9137 1.1778 0.5303 -0.0134 -0.1000 -0.0930 1090 ALA A N   
2081 C CA  . ALA A 315 ? 0.9675 1.2101 0.5884 -0.0046 -0.0942 -0.0932 1090 ALA A CA  
2082 C C   . ALA A 315 ? 1.0414 1.2680 0.6731 -0.0103 -0.0946 -0.0925 1090 ALA A C   
2083 O O   . ALA A 315 ? 1.0408 1.2472 0.6749 -0.0046 -0.0902 -0.0938 1090 ALA A O   
2084 C CB  . ALA A 315 ? 0.8624 1.1214 0.4984 0.0078  -0.0889 -0.0811 1090 ALA A CB  
2085 N N   . ALA A 316 ? 1.0168 1.2528 0.6553 -0.0211 -0.0995 -0.0898 1091 ALA A N   
2086 C CA  . ALA A 316 ? 1.1499 1.3718 0.7985 -0.0265 -0.1001 -0.0890 1091 ALA A CA  
2087 C C   . ALA A 316 ? 1.1219 1.3133 0.7546 -0.0319 -0.1015 -0.1021 1091 ALA A C   
2088 O O   . ALA A 316 ? 1.1845 1.3576 0.8238 -0.0315 -0.0994 -0.1026 1091 ALA A O   
2089 C CB  . ALA A 316 ? 1.0362 1.2775 0.6952 -0.0366 -0.1052 -0.0825 1091 ALA A CB  
2090 N N   . GLU A 317 ? 0.9187 1.1038 0.5304 -0.0370 -0.1052 -0.1128 1092 GLU A N   
2091 C CA  . GLU A 317 ? 1.1576 1.3117 0.7527 -0.0412 -0.1064 -0.1258 1092 GLU A CA  
2092 C C   . GLU A 317 ? 1.0442 1.1776 0.6401 -0.0298 -0.0993 -0.1273 1092 GLU A C   
2093 O O   . GLU A 317 ? 1.0786 1.1885 0.6740 -0.0322 -0.0986 -0.1320 1092 GLU A O   
2094 C CB  . GLU A 317 ? 1.2671 1.4175 0.8379 -0.0455 -0.1105 -0.1370 1092 GLU A CB  
2095 C CG  . GLU A 317 ? 1.2205 1.3655 0.7818 -0.0615 -0.1186 -0.1437 1092 GLU A CG  
2096 C CD  . GLU A 317 ? 1.8159 1.9579 1.3526 -0.0661 -0.1230 -0.1547 1092 GLU A CD  
2097 O OE1 . GLU A 317 ? 1.9094 2.0542 1.4365 -0.0561 -0.1194 -0.1573 1092 GLU A OE1 
2098 O OE2 . GLU A 317 ? 1.8441 1.9812 1.3708 -0.0797 -0.1302 -0.1607 1092 GLU A OE2 
2099 N N   . GLN A 318 ? 0.9690 1.1120 0.5669 -0.0174 -0.0940 -0.1227 1093 GLN A N   
2100 C CA  . GLN A 318 ? 0.9537 1.0796 0.5530 -0.0062 -0.0872 -0.1227 1093 GLN A CA  
2101 C C   . GLN A 318 ? 1.0641 1.1902 0.6858 -0.0041 -0.0841 -0.1129 1093 GLN A C   
2102 O O   . GLN A 318 ? 1.0873 1.1926 0.7103 -0.0001 -0.0800 -0.1149 1093 GLN A O   
2103 C CB  . GLN A 318 ? 0.9827 1.1212 0.5780 0.0060  -0.0829 -0.1195 1093 GLN A CB  
2104 C CG  . GLN A 318 ? 1.3166 1.4401 0.9128 0.0182  -0.0757 -0.1184 1093 GLN A CG  
2105 C CD  . GLN A 318 ? 1.4730 1.6088 1.0626 0.0298  -0.0720 -0.1160 1093 GLN A CD  
2106 O OE1 . GLN A 318 ? 1.5342 1.6895 1.1180 0.0290  -0.0749 -0.1157 1093 GLN A OE1 
2107 N NE2 . GLN A 318 ? 1.3548 1.4804 0.9454 0.0408  -0.0658 -0.1138 1093 GLN A NE2 
2108 N N   . LEU A 319 ? 0.9672 1.1163 0.6062 -0.0066 -0.0858 -0.1022 1094 LEU A N   
2109 C CA  . LEU A 319 ? 1.0075 1.1564 0.6669 -0.0053 -0.0834 -0.0934 1094 LEU A CA  
2110 C C   . LEU A 319 ? 1.0066 1.1382 0.6665 -0.0152 -0.0864 -0.0986 1094 LEU A C   
2111 O O   . LEU A 319 ? 0.9712 1.0895 0.6408 -0.0130 -0.0833 -0.0966 1094 LEU A O   
2112 C CB  . LEU A 319 ? 0.9821 1.1597 0.6585 -0.0051 -0.0847 -0.0811 1094 LEU A CB  
2113 C CG  . LEU A 319 ? 1.0237 1.2202 0.7043 0.0053  -0.0814 -0.0732 1094 LEU A CG  
2114 C CD1 . LEU A 319 ? 1.1414 1.3669 0.8351 0.0031  -0.0840 -0.0629 1094 LEU A CD1 
2115 C CD2 . LEU A 319 ? 1.0152 1.2031 0.7061 0.0159  -0.0751 -0.0674 1094 LEU A CD2 
2116 N N   . LYS A 320 ? 0.9393 1.0714 0.5891 -0.0266 -0.0928 -0.1050 1095 LYS A N   
2117 C CA  . LYS A 320 ? 1.0060 1.1215 0.6551 -0.0367 -0.0962 -0.1100 1095 LYS A CA  
2118 C C   . LYS A 320 ? 1.1084 1.1931 0.7446 -0.0347 -0.0937 -0.1204 1095 LYS A C   
2119 O O   . LYS A 320 ? 1.0466 1.1153 0.6888 -0.0374 -0.0930 -0.1214 1095 LYS A O   
2120 C CB  . LYS A 320 ? 1.0114 1.1357 0.6518 -0.0498 -0.1041 -0.1139 1095 LYS A CB  
2121 C CG  . LYS A 320 ? 1.2420 1.3524 0.8831 -0.0612 -0.1085 -0.1176 1095 LYS A CG  
2122 C CD  . LYS A 320 ? 1.0409 1.1657 0.6777 -0.0745 -0.1166 -0.1179 1095 LYS A CD  
2123 C CE  . LYS A 320 ? 1.2478 1.3662 0.8611 -0.0793 -0.1206 -0.1288 1095 LYS A CE  
2124 N NZ  . LYS A 320 ? 1.5080 1.6383 1.1166 -0.0938 -0.1290 -0.1294 1095 LYS A NZ  
2125 N N   . THR A 321 ? 1.0895 1.1660 0.7082 -0.0294 -0.0920 -0.1279 1096 THR A N   
2126 C CA  . THR A 321 ? 1.1509 1.1983 0.7571 -0.0256 -0.0886 -0.1371 1096 THR A CA  
2127 C C   . THR A 321 ? 1.0784 1.1189 0.6987 -0.0158 -0.0816 -0.1306 1096 THR A C   
2128 O O   . THR A 321 ? 1.0667 1.0864 0.6883 -0.0172 -0.0799 -0.1340 1096 THR A O   
2129 C CB  . THR A 321 ? 1.1527 1.1957 0.7380 -0.0197 -0.0875 -0.1450 1096 THR A CB  
2130 O OG1 . THR A 321 ? 1.0564 1.0992 0.6257 -0.0302 -0.0945 -0.1534 1096 THR A OG1 
2131 C CG2 . THR A 321 ? 0.9793 0.9945 0.5537 -0.0123 -0.0822 -0.1523 1096 THR A CG2 
2132 N N   . THR A 322 ? 1.0259 1.0841 0.6570 -0.0062 -0.0774 -0.1211 1097 THR A N   
2133 C CA  . THR A 322 ? 0.9781 1.0318 0.6232 0.0026  -0.0711 -0.1139 1097 THR A CA  
2134 C C   . THR A 322 ? 1.0321 1.0829 0.6938 -0.0035 -0.0722 -0.1094 1097 THR A C   
2135 O O   . THR A 322 ? 1.0027 1.0355 0.6680 -0.0017 -0.0689 -0.1106 1097 THR A O   
2136 C CB  . THR A 322 ? 0.9996 1.0758 0.6547 0.0121  -0.0680 -0.1032 1097 THR A CB  
2137 O OG1 . THR A 322 ? 1.1747 1.2504 0.8150 0.0201  -0.0654 -0.1069 1097 THR A OG1 
2138 C CG2 . THR A 322 ? 0.9865 1.0612 0.6594 0.0187  -0.0629 -0.0940 1097 THR A CG2 
2139 N N   . ARG A 323 ? 0.9626 1.0322 0.6346 -0.0104 -0.0768 -0.1038 1098 ARG A N   
2140 C CA  . ARG A 323 ? 0.8899 0.9596 0.5782 -0.0154 -0.0778 -0.0987 1098 ARG A CA  
2141 C C   . ARG A 323 ? 1.1413 1.1880 0.8231 -0.0233 -0.0799 -0.1073 1098 ARG A C   
2142 O O   . ARG A 323 ? 1.0158 1.0524 0.7082 -0.0229 -0.0775 -0.1051 1098 ARG A O   
2143 C CB  . ARG A 323 ? 0.9542 1.0485 0.6517 -0.0217 -0.0828 -0.0920 1098 ARG A CB  
2144 C CG  . ARG A 323 ? 0.9858 1.0849 0.7017 -0.0251 -0.0835 -0.0847 1098 ARG A CG  
2145 C CD  . ARG A 323 ? 1.0458 1.1324 0.7586 -0.0363 -0.0880 -0.0907 1098 ARG A CD  
2146 N NE  . ARG A 323 ? 1.0778 1.1673 0.7761 -0.0461 -0.0943 -0.0974 1098 ARG A NE  
2147 C CZ  . ARG A 323 ? 0.9626 1.0736 0.6639 -0.0527 -0.0993 -0.0930 1098 ARG A CZ  
2148 N NH1 . ARG A 323 ? 1.1092 1.2410 0.8273 -0.0499 -0.0986 -0.0819 1098 ARG A NH1 
2149 N NH2 . ARG A 323 ? 0.9321 1.0435 0.6189 -0.0622 -0.1053 -0.0998 1098 ARG A NH2 
2150 N N   . ASN A 324 ? 0.9502 0.9883 0.6145 -0.0307 -0.0844 -0.1171 1099 ASN A N   
2151 C CA  . ASN A 324 ? 1.1386 1.1544 0.7963 -0.0390 -0.0870 -0.1253 1099 ASN A CA  
2152 C C   . ASN A 324 ? 1.1765 1.1678 0.8294 -0.0317 -0.0810 -0.1299 1099 ASN A C   
2153 O O   . ASN A 324 ? 1.1671 1.1413 0.8222 -0.0362 -0.0812 -0.1330 1099 ASN A O   
2154 C CB  . ASN A 324 ? 1.0449 1.0561 0.6836 -0.0486 -0.0936 -0.1349 1099 ASN A CB  
2155 C CG  . ASN A 324 ? 1.0767 1.1117 0.7202 -0.0577 -0.1001 -0.1302 1099 ASN A CG  
2156 O OD1 . ASN A 324 ? 1.2119 1.2619 0.8730 -0.0597 -0.1008 -0.1210 1099 ASN A OD1 
2157 N ND2 . ASN A 324 ? 1.2143 1.2530 0.8416 -0.0632 -0.1049 -0.1364 1099 ASN A ND2 
2158 N N   . ALA A 325 ? 0.9977 0.9877 0.6444 -0.0206 -0.0756 -0.1300 1100 ALA A N   
2159 C CA  . ALA A 325 ? 0.9033 0.8713 0.5451 -0.0130 -0.0695 -0.1337 1100 ALA A CA  
2160 C C   . ALA A 325 ? 1.1200 1.0863 0.7809 -0.0095 -0.0652 -0.1257 1100 ALA A C   
2161 O O   . ALA A 325 ? 1.1746 1.1208 0.8341 -0.0076 -0.0616 -0.1291 1100 ALA A O   
2162 C CB  . ALA A 325 ? 0.9506 0.9211 0.5823 -0.0013 -0.0648 -0.1341 1100 ALA A CB  
2163 N N   . TYR A 326 ? 1.0760 1.0629 0.7544 -0.0084 -0.0653 -0.1153 1101 TYR A N   
2164 C CA  . TYR A 326 ? 0.9647 0.9516 0.6611 -0.0046 -0.0612 -0.1074 1101 TYR A CA  
2165 C C   . TYR A 326 ? 1.0096 1.0013 0.7191 -0.0137 -0.0654 -0.1044 1101 TYR A C   
2166 O O   . TYR A 326 ? 0.9313 0.9280 0.6572 -0.0111 -0.0630 -0.0967 1101 TYR A O   
2167 C CB  . TYR A 326 ? 1.0191 1.0241 0.7258 0.0049  -0.0577 -0.0972 1101 TYR A CB  
2168 C CG  . TYR A 326 ? 0.9802 0.9799 0.6779 0.0155  -0.0523 -0.0979 1101 TYR A CG  
2169 C CD1 . TYR A 326 ? 1.0777 1.0813 0.7595 0.0178  -0.0533 -0.1026 1101 TYR A CD1 
2170 C CD2 . TYR A 326 ? 1.0639 1.0553 0.7685 0.0233  -0.0461 -0.0934 1101 TYR A CD2 
2171 C CE1 . TYR A 326 ? 1.0726 1.0726 0.7461 0.0281  -0.0482 -0.1027 1101 TYR A CE1 
2172 C CE2 . TYR A 326 ? 1.0774 1.0652 0.7739 0.0331  -0.0412 -0.0930 1101 TYR A CE2 
2173 C CZ  . TYR A 326 ? 1.0694 1.0618 0.7504 0.0358  -0.0422 -0.0976 1101 TYR A CZ  
2174 O OH  . TYR A 326 ? 1.1990 1.1890 0.8721 0.0462  -0.0371 -0.0967 1101 TYR A OH  
2175 N N   . ILE A 327 ? 1.0726 1.0628 0.7747 -0.0245 -0.0717 -0.1103 1102 ILE A N   
2176 C CA  . ILE A 327 ? 0.9996 0.9970 0.7140 -0.0333 -0.0761 -0.1067 1102 ILE A CA  
2177 C C   . ILE A 327 ? 1.2495 1.2293 0.9705 -0.0349 -0.0739 -0.1080 1102 ILE A C   
2178 O O   . ILE A 327 ? 1.1546 1.1415 0.8909 -0.0374 -0.0746 -0.1019 1102 ILE A O   
2179 C CB  . ILE A 327 ? 1.0916 1.0932 0.7956 -0.0449 -0.0838 -0.1120 1102 ILE A CB  
2180 C CG1 . ILE A 327 ? 1.2296 1.2469 0.9478 -0.0528 -0.0885 -0.1054 1102 ILE A CG1 
2181 C CG2 . ILE A 327 ? 1.1932 1.1699 0.8818 -0.0509 -0.0858 -0.1232 1102 ILE A CG2 
2182 C CD1 . ILE A 327 ? 1.3438 1.3748 1.0547 -0.0627 -0.0959 -0.1069 1102 ILE A CD1 
2183 N N   . GLN A 328 ? 1.1487 1.1058 0.8584 -0.0330 -0.0711 -0.1156 1103 GLN A N   
2184 C CA  . GLN A 328 ? 1.1260 1.0664 0.8421 -0.0342 -0.0687 -0.1166 1103 GLN A CA  
2185 C C   . GLN A 328 ? 1.0240 0.9669 0.7542 -0.0244 -0.0619 -0.1088 1103 GLN A C   
2186 O O   . GLN A 328 ? 1.0489 0.9925 0.7934 -0.0261 -0.0612 -0.1042 1103 GLN A O   
2187 C CB  . GLN A 328 ? 1.1423 1.0575 0.8415 -0.0350 -0.0677 -0.1270 1103 GLN A CB  
2188 C CG  . GLN A 328 ? 1.3001 1.2096 0.9847 -0.0457 -0.0750 -0.1354 1103 GLN A CG  
2189 C CD  . GLN A 328 ? 1.2884 1.2041 0.9826 -0.0576 -0.0814 -0.1333 1103 GLN A CD  
2190 O OE1 . GLN A 328 ? 1.2985 1.2263 0.9892 -0.0657 -0.0880 -0.1337 1103 GLN A OE1 
2191 N NE2 . GLN A 328 ? 1.3879 1.2965 1.0944 -0.0587 -0.0795 -0.1305 1103 GLN A NE2 
2192 N N   . LYS A 329 ? 0.9283 0.8728 0.6544 -0.0144 -0.0570 -0.1069 1104 LYS A N   
2193 C CA  . LYS A 329 ? 1.0012 0.9492 0.7404 -0.0055 -0.0510 -0.0987 1104 LYS A CA  
2194 C C   . LYS A 329 ? 0.9675 0.9347 0.7241 -0.0068 -0.0529 -0.0896 1104 LYS A C   
2195 O O   . LYS A 329 ? 0.9887 0.9558 0.7586 -0.0033 -0.0496 -0.0837 1104 LYS A O   
2196 C CB  . LYS A 329 ? 0.8179 0.7685 0.5497 0.0047  -0.0466 -0.0972 1104 LYS A CB  
2197 C CG  . LYS A 329 ? 1.1055 1.0354 0.8235 0.0092  -0.0423 -0.1040 1104 LYS A CG  
2198 C CD  . LYS A 329 ? 1.2994 1.2337 1.0060 0.0179  -0.0395 -0.1041 1104 LYS A CD  
2199 C CE  . LYS A 329 ? 1.3660 1.2795 1.0578 0.0229  -0.0351 -0.1111 1104 LYS A CE  
2200 N NZ  . LYS A 329 ? 1.2990 1.2163 0.9761 0.0302  -0.0336 -0.1132 1104 LYS A NZ  
2201 N N   . TYR A 330 ? 0.9677 0.9514 0.7240 -0.0116 -0.0582 -0.0884 1105 TYR A N   
2202 C CA  . TYR A 330 ? 0.9195 0.9217 0.6915 -0.0127 -0.0602 -0.0798 1105 TYR A CA  
2203 C C   . TYR A 330 ? 0.9022 0.9009 0.6834 -0.0201 -0.0627 -0.0798 1105 TYR A C   
2204 O O   . TYR A 330 ? 0.8484 0.8529 0.6444 -0.0178 -0.0611 -0.0730 1105 TYR A O   
2205 C CB  . TYR A 330 ? 0.8332 0.8545 0.6017 -0.0157 -0.0650 -0.0783 1105 TYR A CB  
2206 C CG  . TYR A 330 ? 0.8084 0.8484 0.5909 -0.0191 -0.0682 -0.0707 1105 TYR A CG  
2207 C CD1 . TYR A 330 ? 0.7403 0.7936 0.5356 -0.0119 -0.0657 -0.0614 1105 TYR A CD1 
2208 C CD2 . TYR A 330 ? 0.8028 0.8472 0.5853 -0.0293 -0.0740 -0.0727 1105 TYR A CD2 
2209 C CE1 . TYR A 330 ? 0.7722 0.8421 0.5796 -0.0141 -0.0683 -0.0545 1105 TYR A CE1 
2210 C CE2 . TYR A 330 ? 0.8368 0.8993 0.6318 -0.0317 -0.0767 -0.0652 1105 TYR A CE2 
2211 C CZ  . TYR A 330 ? 0.7596 0.8346 0.5668 -0.0237 -0.0737 -0.0563 1105 TYR A CZ  
2212 O OH  . TYR A 330 ? 0.8702 0.9627 0.6893 -0.0253 -0.0761 -0.0489 1105 TYR A OH  
2213 N N   . LEU A 331 ? 0.8496 0.8388 0.6221 -0.0291 -0.0668 -0.0871 1106 LEU A N   
2214 C CA  . LEU A 331 ? 0.9192 0.9050 0.7001 -0.0364 -0.0694 -0.0870 1106 LEU A CA  
2215 C C   . LEU A 331 ? 0.9396 0.9096 0.7268 -0.0324 -0.0640 -0.0870 1106 LEU A C   
2216 O O   . LEU A 331 ? 0.8113 0.7844 0.6120 -0.0338 -0.0639 -0.0825 1106 LEU A O   
2217 C CB  . LEU A 331 ? 0.9376 0.9157 0.7067 -0.0474 -0.0754 -0.0949 1106 LEU A CB  
2218 C CG  . LEU A 331 ? 1.0730 1.0673 0.8359 -0.0534 -0.0816 -0.0949 1106 LEU A CG  
2219 C CD1 . LEU A 331 ? 1.0923 1.0737 0.8391 -0.0631 -0.0869 -0.1044 1106 LEU A CD1 
2220 C CD2 . LEU A 331 ? 1.0165 1.0313 0.7939 -0.0575 -0.0852 -0.0867 1106 LEU A CD2 
2221 N N   . ALA A 332 ? 0.8396 0.7933 0.6171 -0.0272 -0.0595 -0.0917 900  ALA A N   
2222 C CA  . ALA A 332 ? 0.7471 0.6864 0.5302 -0.0229 -0.0539 -0.0912 900  ALA A CA  
2223 C C   . ALA A 332 ? 0.9586 0.9081 0.7564 -0.0153 -0.0498 -0.0820 900  ALA A C   
2224 O O   . ALA A 332 ? 0.9722 0.9177 0.7811 -0.0148 -0.0474 -0.0791 900  ALA A O   
2225 C CB  . ALA A 332 ? 0.8136 0.7351 0.5824 -0.0179 -0.0497 -0.0974 900  ALA A CB  
2226 N N   . HIS A 333 ? 0.8419 0.8045 0.6398 -0.0093 -0.0490 -0.0774 270  HIS A N   
2227 C CA  . HIS A 333 ? 0.7869 0.7585 0.5982 -0.0024 -0.0456 -0.0685 270  HIS A CA  
2228 C C   . HIS A 333 ? 0.7674 0.7508 0.5927 -0.0063 -0.0486 -0.0635 270  HIS A C   
2229 O O   . HIS A 333 ? 0.8352 0.8176 0.6722 -0.0034 -0.0459 -0.0588 270  HIS A O   
2230 C CB  . HIS A 333 ? 0.8519 0.8356 0.6602 0.0042  -0.0448 -0.0644 270  HIS A CB  
2231 C CG  . HIS A 333 ? 0.9402 0.9327 0.7615 0.0110  -0.0419 -0.0552 270  HIS A CG  
2232 N ND1 . HIS A 333 ? 1.1052 1.0900 0.9283 0.0183  -0.0365 -0.0520 270  HIS A ND1 
2233 C CD2 . HIS A 333 ? 0.8140 0.8218 0.6467 0.0116  -0.0439 -0.0482 270  HIS A CD2 
2234 C CE1 . HIS A 333 ? 1.0761 1.0704 0.9109 0.0225  -0.0356 -0.0438 270  HIS A CE1 
2235 N NE2 . HIS A 333 ? 0.8956 0.9034 0.7363 0.0189  -0.0399 -0.0415 270  HIS A NE2 
2236 N N   . LEU A 334 ? 0.8636 0.8588 0.6877 -0.0128 -0.0544 -0.0642 271  LEU A N   
2237 C CA  . LEU A 334 ? 0.8927 0.8998 0.7295 -0.0166 -0.0574 -0.0593 271  LEU A CA  
2238 C C   . LEU A 334 ? 0.8933 0.8892 0.7350 -0.0215 -0.0574 -0.0619 271  LEU A C   
2239 O O   . LEU A 334 ? 0.7497 0.7511 0.6043 -0.0209 -0.0569 -0.0569 271  LEU A O   
2240 C CB  . LEU A 334 ? 0.8614 0.8837 0.6947 -0.0231 -0.0636 -0.0593 271  LEU A CB  
2241 C CG  . LEU A 334 ? 0.9729 1.0107 0.8040 -0.0186 -0.0642 -0.0552 271  LEU A CG  
2242 C CD1 . LEU A 334 ? 0.9918 1.0456 0.8209 -0.0261 -0.0705 -0.0546 271  LEU A CD1 
2243 C CD2 . LEU A 334 ? 0.8898 0.9366 0.7335 -0.0101 -0.0607 -0.0464 271  LEU A CD2 
2244 N N   . ALA A 335 ? 1.0116 0.9919 0.8431 -0.0262 -0.0579 -0.0696 272  ALA A N   
2245 C CA  . ALA A 335 ? 0.7726 0.7416 0.6087 -0.0309 -0.0577 -0.0719 272  ALA A CA  
2246 C C   . ALA A 335 ? 1.0024 0.9625 0.8464 -0.0239 -0.0512 -0.0691 272  ALA A C   
2247 O O   . ALA A 335 ? 0.8883 0.8469 0.7426 -0.0258 -0.0506 -0.0672 272  ALA A O   
2248 C CB  . ALA A 335 ? 0.8786 0.8316 0.7009 -0.0373 -0.0597 -0.0809 272  ALA A CB  
2249 N N   . ALA A 336 ? 0.8985 0.8536 0.7378 -0.0159 -0.0463 -0.0684 273  ALA A N   
2250 C CA  . ALA A 336 ? 0.8506 0.7976 0.6968 -0.0096 -0.0402 -0.0653 273  ALA A CA  
2251 C C   . ALA A 336 ? 0.8879 0.8476 0.7485 -0.0056 -0.0394 -0.0571 273  ALA A C   
2252 O O   . ALA A 336 ? 0.7533 0.7093 0.6236 -0.0048 -0.0369 -0.0546 273  ALA A O   
2253 C CB  . ALA A 336 ? 0.6783 0.6173 0.5149 -0.0023 -0.0356 -0.0663 273  ALA A CB  
2254 N N   . THR A 337 ? 0.7335 0.7079 0.5954 -0.0030 -0.0415 -0.0529 274  THR A N   
2255 C CA  . THR A 337 ? 0.9353 0.9209 0.8100 0.0009  -0.0410 -0.0453 274  THR A CA  
2256 C C   . THR A 337 ? 0.8526 0.8438 0.7369 -0.0044 -0.0440 -0.0444 274  THR A C   
2257 O O   . THR A 337 ? 0.7054 0.6969 0.6003 -0.0018 -0.0419 -0.0404 274  THR A O   
2258 C CB  . THR A 337 ? 0.8730 0.8736 0.7469 0.0043  -0.0430 -0.0409 274  THR A CB  
2259 O OG1 . THR A 337 ? 0.9866 0.9962 0.8551 -0.0020 -0.0483 -0.0438 274  THR A OG1 
2260 C CG2 . THR A 337 ? 0.8045 0.8011 0.6705 0.0105  -0.0398 -0.0406 274  THR A CG2 
2261 N N   . ARG A 338 ? 0.7245 0.7204 0.6049 -0.0121 -0.0490 -0.0478 275  ARG A N   
2262 C CA  . ARG A 338 ? 0.7625 0.7643 0.6515 -0.0178 -0.0522 -0.0468 275  ARG A CA  
2263 C C   . ARG A 338 ? 0.8072 0.7961 0.7016 -0.0185 -0.0490 -0.0483 275  ARG A C   
2264 O O   . ARG A 338 ? 0.7255 0.7192 0.6313 -0.0173 -0.0483 -0.0443 275  ARG A O   
2265 C CB  . ARG A 338 ? 0.8322 0.8378 0.7138 -0.0270 -0.0582 -0.0510 275  ARG A CB  
2266 C CG  . ARG A 338 ? 1.0804 1.0982 0.9709 -0.0330 -0.0627 -0.0480 275  ARG A CG  
2267 C CD  . ARG A 338 ? 1.1227 1.1435 1.0052 -0.0431 -0.0691 -0.0520 275  ARG A CD  
2268 N NE  . ARG A 338 ? 1.3015 1.3285 1.1738 -0.0432 -0.0713 -0.0531 275  ARG A NE  
2269 C CZ  . ARG A 338 ? 1.2069 1.2235 1.0652 -0.0467 -0.0725 -0.0600 275  ARG A CZ  
2270 N NH1 . ARG A 338 ? 1.2078 1.2059 1.0599 -0.0505 -0.0718 -0.0666 275  ARG A NH1 
2271 N NH2 . ARG A 338 ? 0.9181 0.9430 0.7683 -0.0463 -0.0744 -0.0602 275  ARG A NH2 
2272 N N   . LYS A 339 ? 0.8169 0.7895 0.7028 -0.0201 -0.0469 -0.0542 276  LYS A N   
2273 C CA  . LYS A 339 ? 0.7504 0.7106 0.6411 -0.0208 -0.0436 -0.0555 276  LYS A CA  
2274 C C   . LYS A 339 ? 0.8206 0.7797 0.7196 -0.0129 -0.0381 -0.0504 276  LYS A C   
2275 O O   . LYS A 339 ? 0.7240 0.6819 0.6329 -0.0131 -0.0365 -0.0484 276  LYS A O   
2276 C CB  . LYS A 339 ? 0.9469 0.8897 0.8256 -0.0229 -0.0420 -0.0625 276  LYS A CB  
2277 C CG  . LYS A 339 ? 1.0016 0.9308 0.8841 -0.0245 -0.0387 -0.0644 276  LYS A CG  
2278 C CD  . LYS A 339 ? 1.0725 0.9851 0.9420 -0.0280 -0.0386 -0.0719 276  LYS A CD  
2279 C CE  . LYS A 339 ? 1.2293 1.1271 1.1015 -0.0270 -0.0336 -0.0731 276  LYS A CE  
2280 N NZ  . LYS A 339 ? 1.2450 1.1387 1.1179 -0.0179 -0.0268 -0.0698 276  LYS A NZ  
2281 N N   . GLY A 340 ? 0.6786 0.6387 0.5739 -0.0061 -0.0356 -0.0480 277  GLY A N   
2282 C CA  . GLY A 340 ? 0.6762 0.6351 0.5787 0.0009  -0.0310 -0.0428 277  GLY A CA  
2283 C C   . GLY A 340 ? 0.7499 0.7205 0.6647 0.0022  -0.0324 -0.0373 277  GLY A C   
2284 O O   . GLY A 340 ? 0.6594 0.6270 0.5825 0.0047  -0.0294 -0.0346 277  GLY A O   
2285 N N   . VAL A 341 ? 0.6829 0.6675 0.5988 0.0008  -0.0369 -0.0355 278  VAL A N   
2286 C CA  . VAL A 341 ? 0.7723 0.7687 0.6991 0.0026  -0.0383 -0.0304 278  VAL A CA  
2287 C C   . VAL A 341 ? 0.6471 0.6423 0.5816 -0.0019 -0.0388 -0.0314 278  VAL A C   
2288 O O   . VAL A 341 ? 0.6898 0.6864 0.6336 0.0013  -0.0369 -0.0280 278  VAL A O   
2289 C CB  . VAL A 341 ? 0.7085 0.7208 0.6343 0.0014  -0.0431 -0.0283 278  VAL A CB  
2290 C CG1 . VAL A 341 ? 0.8431 0.8679 0.7798 0.0025  -0.0449 -0.0234 278  VAL A CG1 
2291 C CG2 . VAL A 341 ? 0.7721 0.7876 0.6930 0.0070  -0.0423 -0.0257 278  VAL A CG2 
2292 N N   . ARG A 342 ? 0.7129 0.7054 0.6435 -0.0094 -0.0415 -0.0361 279  ARG A N   
2293 C CA  . ARG A 342 ? 0.7028 0.6940 0.6407 -0.0142 -0.0421 -0.0370 279  ARG A CA  
2294 C C   . ARG A 342 ? 0.6261 0.6053 0.5684 -0.0110 -0.0366 -0.0369 279  ARG A C   
2295 O O   . ARG A 342 ? 0.5843 0.5670 0.5368 -0.0100 -0.0356 -0.0340 279  ARG A O   
2296 C CB  . ARG A 342 ? 0.7651 0.7521 0.6964 -0.0230 -0.0458 -0.0423 279  ARG A CB  
2297 C CG  . ARG A 342 ? 1.0444 1.0302 0.9831 -0.0289 -0.0470 -0.0431 279  ARG A CG  
2298 C CD  . ARG A 342 ? 0.8759 0.8572 0.8073 -0.0381 -0.0516 -0.0481 279  ARG A CD  
2299 N N   . THR A 343 ? 0.6028 0.5684 0.5373 -0.0090 -0.0329 -0.0397 280  THR A N   
2300 C CA  . THR A 343 ? 0.6974 0.6521 0.6354 -0.0061 -0.0274 -0.0391 280  THR A CA  
2301 C C   . THR A 343 ? 0.5810 0.5408 0.5274 0.0003  -0.0250 -0.0333 280  THR A C   
2302 O O   . THR A 343 ? 0.5158 0.4739 0.4706 0.0007  -0.0227 -0.0316 280  THR A O   
2303 C CB  . THR A 343 ? 0.5660 0.5075 0.4933 -0.0038 -0.0238 -0.0420 280  THR A CB  
2304 O OG1 . THR A 343 ? 0.6818 0.6166 0.6004 -0.0097 -0.0260 -0.0480 280  THR A OG1 
2305 C CG2 . THR A 343 ? 0.6260 0.5569 0.5568 -0.0007 -0.0179 -0.0406 280  THR A CG2 
2306 N N   . LEU A 344 ? 0.5540 0.5197 0.4981 0.0052  -0.0257 -0.0302 281  LEU A N   
2307 C CA  . LEU A 344 ? 0.6267 0.5968 0.5779 0.0112  -0.0242 -0.0248 281  LEU A CA  
2308 C C   . LEU A 344 ? 0.5172 0.4951 0.4791 0.0100  -0.0256 -0.0230 281  LEU A C   
2309 O O   . LEU A 344 ? 0.4630 0.4373 0.4315 0.0122  -0.0227 -0.0211 281  LEU A O   
2310 C CB  . LEU A 344 ? 0.7216 0.7002 0.6697 0.0153  -0.0264 -0.0217 281  LEU A CB  
2311 C CG  . LEU A 344 ? 0.7811 0.7540 0.7219 0.0197  -0.0240 -0.0204 281  LEU A CG  
2312 C CD1 . LEU A 344 ? 0.8640 0.8476 0.8022 0.0225  -0.0271 -0.0177 281  LEU A CD1 
2313 C CD2 . LEU A 344 ? 0.8428 0.8086 0.7880 0.0244  -0.0200 -0.0166 281  LEU A CD2 
2314 N N   . ALA A 345 ? 0.4573 0.4466 0.4207 0.0066  -0.0302 -0.0234 282  ALA A N   
2315 C CA  . ALA A 345 ? 0.5412 0.5405 0.5145 0.0063  -0.0319 -0.0209 282  ALA A CA  
2316 C C   . ALA A 345 ? 0.4478 0.4421 0.4265 0.0019  -0.0305 -0.0230 282  ALA A C   
2317 O O   . ALA A 345 ? 0.4805 0.4779 0.4678 0.0039  -0.0292 -0.0206 282  ALA A O   
2318 C CB  . ALA A 345 ? 0.5167 0.5306 0.4898 0.0032  -0.0372 -0.0202 282  ALA A CB  
2319 N N   . VAL A 346 ? 0.4476 0.4343 0.4212 -0.0040 -0.0307 -0.0274 283  VAL A N   
2320 C CA  . VAL A 346 ? 0.4429 0.4250 0.4219 -0.0087 -0.0296 -0.0291 283  VAL A CA  
2321 C C   . VAL A 346 ? 0.4588 0.4313 0.4414 -0.0047 -0.0239 -0.0280 283  VAL A C   
2322 O O   . VAL A 346 ? 0.4699 0.4444 0.4614 -0.0053 -0.0226 -0.0266 283  VAL A O   
2323 C CB  . VAL A 346 ? 0.4818 0.4559 0.4533 -0.0156 -0.0312 -0.0343 283  VAL A CB  
2324 C CG1 . VAL A 346 ? 0.6256 0.5923 0.6023 -0.0196 -0.0291 -0.0358 283  VAL A CG1 
2325 C CG2 . VAL A 346 ? 0.6768 0.6620 0.6465 -0.0211 -0.0375 -0.0349 283  VAL A CG2 
2326 N N   . VAL A 347 ? 0.4391 0.4020 0.4148 -0.0007 -0.0205 -0.0281 284  VAL A N   
2327 C CA  . VAL A 347 ? 0.4331 0.3871 0.4115 0.0026  -0.0152 -0.0264 284  VAL A CA  
2328 C C   . VAL A 347 ? 0.4223 0.3827 0.4088 0.0073  -0.0146 -0.0219 284  VAL A C   
2329 O O   . VAL A 347 ? 0.4145 0.3728 0.4079 0.0076  -0.0118 -0.0206 284  VAL A O   
2330 C CB  . VAL A 347 ? 0.4881 0.4319 0.4568 0.0058  -0.0122 -0.0268 284  VAL A CB  
2331 C CG1 . VAL A 347 ? 0.5503 0.4876 0.5221 0.0099  -0.0072 -0.0234 284  VAL A CG1 
2332 C CG2 . VAL A 347 ? 0.4822 0.4169 0.4430 0.0016  -0.0117 -0.0317 284  VAL A CG2 
2333 N N   . LEU A 348 ? 0.4718 0.4400 0.4575 0.0112  -0.0171 -0.0196 285  LEU A N   
2334 C CA  . LEU A 348 ? 0.4138 0.3869 0.4061 0.0162  -0.0167 -0.0157 285  LEU A CA  
2335 C C   . LEU A 348 ? 0.4437 0.4265 0.4450 0.0141  -0.0186 -0.0154 285  LEU A C   
2336 O O   . LEU A 348 ? 0.4286 0.4116 0.4365 0.0164  -0.0167 -0.0136 285  LEU A O   
2337 C CB  . LEU A 348 ? 0.4329 0.4115 0.4218 0.0211  -0.0191 -0.0130 285  LEU A CB  
2338 C CG  . LEU A 348 ? 0.5632 0.5444 0.5572 0.0272  -0.0186 -0.0091 285  LEU A CG  
2339 C CD1 . LEU A 348 ? 0.5735 0.5440 0.5695 0.0288  -0.0144 -0.0078 285  LEU A CD1 
2340 C CD2 . LEU A 348 ? 0.5744 0.5586 0.5639 0.0320  -0.0205 -0.0063 285  LEU A CD2 
2341 N N   . GLY A 349 ? 0.4106 0.4022 0.4122 0.0097  -0.0226 -0.0170 286  GLY A N   
2342 C CA  . GLY A 349 ? 0.4547 0.4568 0.4650 0.0073  -0.0245 -0.0162 286  GLY A CA  
2343 C C   . GLY A 349 ? 0.4586 0.4549 0.4746 0.0038  -0.0216 -0.0175 286  GLY A C   
2344 O O   . GLY A 349 ? 0.4369 0.4394 0.4614 0.0047  -0.0211 -0.0157 286  GLY A O   
2345 N N   . THR A 350 ? 0.4169 0.4015 0.4280 0.0000  -0.0194 -0.0205 287  THR A N   
2346 C CA  . THR A 350 ? 0.4006 0.3791 0.4168 -0.0031 -0.0162 -0.0213 287  THR A CA  
2347 C C   . THR A 350 ? 0.3924 0.3665 0.4125 0.0018  -0.0116 -0.0187 287  THR A C   
2348 O O   . THR A 350 ? 0.3843 0.3614 0.4129 0.0009  -0.0100 -0.0176 287  THR A O   
2349 C CB  . THR A 350 ? 0.4665 0.4326 0.4752 -0.0072 -0.0146 -0.0250 287  THR A CB  
2350 O OG1 . THR A 350 ? 0.4878 0.4577 0.4927 -0.0126 -0.0194 -0.0276 287  THR A OG1 
2351 C CG2 . THR A 350 ? 0.5237 0.4830 0.5377 -0.0101 -0.0108 -0.0254 287  THR A CG2 
2352 N N   . PHE A 351 ? 0.4030 0.3706 0.4170 0.0066  -0.0097 -0.0175 288  PHE A N   
2353 C CA  . PHE A 351 ? 0.4810 0.4449 0.4980 0.0112  -0.0063 -0.0146 288  PHE A CA  
2354 C C   . PHE A 351 ? 0.3816 0.3560 0.4067 0.0138  -0.0080 -0.0126 288  PHE A C   
2355 O O   . PHE A 351 ? 0.3729 0.3470 0.4043 0.0143  -0.0055 -0.0113 288  PHE A O   
2356 C CB  . PHE A 351 ? 0.5157 0.4733 0.5248 0.0159  -0.0056 -0.0129 288  PHE A CB  
2357 C CG  . PHE A 351 ? 0.4196 0.3724 0.4307 0.0200  -0.0027 -0.0096 288  PHE A CG  
2358 C CD1 . PHE A 351 ? 0.5087 0.4531 0.5206 0.0187  0.0018  -0.0087 288  PHE A CD1 
2359 C CD2 . PHE A 351 ? 0.6451 0.6013 0.6566 0.0251  -0.0045 -0.0071 288  PHE A CD2 
2360 C CE1 . PHE A 351 ? 0.5035 0.4436 0.5168 0.0218  0.0041  -0.0053 288  PHE A CE1 
2361 C CE2 . PHE A 351 ? 0.5671 0.5176 0.5796 0.0283  -0.0024 -0.0042 288  PHE A CE2 
2362 C CZ  . PHE A 351 ? 0.6096 0.5522 0.6229 0.0263  0.0018  -0.0032 288  PHE A CZ  
2363 N N   . GLY A 352 ? 0.3821 0.3665 0.4069 0.0157  -0.0121 -0.0121 289  GLY A N   
2364 C CA  . GLY A 352 ? 0.4301 0.4251 0.4619 0.0191  -0.0137 -0.0100 289  GLY A CA  
2365 C C   . GLY A 352 ? 0.3695 0.3729 0.4102 0.0150  -0.0141 -0.0104 289  GLY A C   
2366 O O   . GLY A 352 ? 0.3623 0.3694 0.4096 0.0172  -0.0127 -0.0090 289  GLY A O   
2367 N N   . ALA A 353 ? 0.4246 0.4310 0.4654 0.0088  -0.0162 -0.0123 290  ALA A N   
2368 C CA  . ALA A 353 ? 0.4025 0.4172 0.4522 0.0042  -0.0170 -0.0121 290  ALA A CA  
2369 C C   . ALA A 353 ? 0.4060 0.4133 0.4605 0.0028  -0.0123 -0.0122 290  ALA A C   
2370 O O   . ALA A 353 ? 0.3622 0.3777 0.4258 0.0020  -0.0120 -0.0108 290  ALA A O   
2371 C CB  . ALA A 353 ? 0.4006 0.4175 0.4484 -0.0029 -0.0204 -0.0141 290  ALA A CB  
2372 N N   . CYS A 354 ? 0.3984 0.3915 0.4471 0.0028  -0.0086 -0.0133 291  CYS A N   
2373 C CA  . CYS A 354 ? 0.4194 0.4057 0.4723 0.0014  -0.0038 -0.0128 291  CYS A CA  
2374 C C   . CYS A 354 ? 0.4453 0.4320 0.5017 0.0065  -0.0013 -0.0104 291  CYS A C   
2375 O O   . CYS A 354 ? 0.3989 0.3877 0.4627 0.0053  0.0012  -0.0093 291  CYS A O   
2376 C CB  . CYS A 354 ? 0.4094 0.3809 0.4544 0.0000  -0.0005 -0.0143 291  CYS A CB  
2377 S SG  . CYS A 354 ? 0.5085 0.4757 0.5502 -0.0070 -0.0019 -0.0178 291  CYS A SG  
2378 N N   . TRP A 355 ? 0.3770 0.3615 0.4279 0.0120  -0.0021 -0.0094 292  TRP A N   
2379 C CA  . TRP A 355 ? 0.3732 0.3549 0.4254 0.0166  0.0001  -0.0073 292  TRP A CA  
2380 C C   . TRP A 355 ? 0.3611 0.3532 0.4173 0.0213  -0.0025 -0.0064 292  TRP A C   
2381 O O   . TRP A 355 ? 0.3417 0.3337 0.4015 0.0237  -0.0007 -0.0052 292  TRP A O   
2382 C CB  . TRP A 355 ? 0.3560 0.3261 0.3992 0.0199  0.0013  -0.0064 292  TRP A CB  
2383 C CG  . TRP A 355 ? 0.5359 0.4950 0.5765 0.0173  0.0056  -0.0058 292  TRP A CG  
2384 C CD1 . TRP A 355 ? 0.4743 0.4265 0.5086 0.0149  0.0066  -0.0069 292  TRP A CD1 
2385 C CD2 . TRP A 355 ? 0.4610 0.4151 0.5045 0.0170  0.0096  -0.0035 292  TRP A CD2 
2386 N NE1 . TRP A 355 ? 0.5381 0.4817 0.5715 0.0137  0.0112  -0.0052 292  TRP A NE1 
2387 C CE2 . TRP A 355 ? 0.4670 0.4119 0.5062 0.0147  0.0131  -0.0029 292  TRP A CE2 
2388 C CE3 . TRP A 355 ? 0.4397 0.3965 0.4886 0.0187  0.0106  -0.0020 292  TRP A CE3 
2389 C CZ2 . TRP A 355 ? 0.4707 0.4099 0.5114 0.0137  0.0175  -0.0001 292  TRP A CZ2 
2390 C CZ3 . TRP A 355 ? 0.5275 0.4782 0.5778 0.0172  0.0147  0.0004  292  TRP A CZ3 
2391 C CH2 . TRP A 355 ? 0.3990 0.3415 0.4455 0.0146  0.0182  0.0016  292  TRP A CH2 
2392 N N   . LEU A 356 ? 0.4026 0.4037 0.4580 0.0228  -0.0065 -0.0066 293  LEU A N   
2393 C CA  . LEU A 356 ? 0.4184 0.4287 0.4761 0.0287  -0.0087 -0.0053 293  LEU A CA  
2394 C C   . LEU A 356 ? 0.3399 0.3614 0.4073 0.0281  -0.0084 -0.0047 293  LEU A C   
2395 O O   . LEU A 356 ? 0.3543 0.3776 0.4237 0.0331  -0.0077 -0.0039 293  LEU A O   
2396 C CB  . LEU A 356 ? 0.4265 0.4452 0.4811 0.0305  -0.0129 -0.0050 293  LEU A CB  
2397 C CG  . LEU A 356 ? 0.6558 0.6658 0.7013 0.0342  -0.0134 -0.0046 293  LEU A CG  
2398 C CD1 . LEU A 356 ? 0.5866 0.6052 0.6290 0.0343  -0.0173 -0.0043 293  LEU A CD1 
2399 C CD2 . LEU A 356 ? 0.5271 0.5328 0.5709 0.0415  -0.0127 -0.0031 293  LEU A CD2 
2400 N N   . PRO A 357 ? 0.3533 0.3826 0.4269 0.0222  -0.0092 -0.0051 294  PRO A N   
2401 C CA  . PRO A 357 ? 0.3671 0.4080 0.4507 0.0216  -0.0088 -0.0039 294  PRO A CA  
2402 C C   . PRO A 357 ? 0.3536 0.3877 0.4398 0.0225  -0.0045 -0.0038 294  PRO A C   
2403 O O   . PRO A 357 ? 0.3174 0.3587 0.4082 0.0264  -0.0042 -0.0029 294  PRO A O   
2404 C CB  . PRO A 357 ? 0.3914 0.4378 0.4802 0.0137  -0.0100 -0.0042 294  PRO A CB  
2405 C CG  . PRO A 357 ? 0.4104 0.4529 0.4915 0.0117  -0.0128 -0.0055 294  PRO A CG  
2406 C CD  . PRO A 357 ? 0.3743 0.4026 0.4460 0.0158  -0.0107 -0.0064 294  PRO A CD  
2407 N N   . PHE A 358 ? 0.3606 0.3812 0.4434 0.0192  -0.0012 -0.0044 295  PHE A N   
2408 C CA  . PHE A 358 ? 0.3704 0.3841 0.4549 0.0196  0.0029  -0.0037 295  PHE A CA  
2409 C C   . PHE A 358 ? 0.3527 0.3612 0.4319 0.0263  0.0028  -0.0032 295  PHE A C   
2410 O O   . PHE A 358 ? 0.3178 0.3292 0.4006 0.0288  0.0040  -0.0027 295  PHE A O   
2411 C CB  . PHE A 358 ? 0.3211 0.3219 0.4019 0.0151  0.0064  -0.0038 295  PHE A CB  
2412 C CG  . PHE A 358 ? 0.4163 0.4112 0.4995 0.0142  0.0109  -0.0022 295  PHE A CG  
2413 C CD1 . PHE A 358 ? 0.3673 0.3708 0.4600 0.0124  0.0126  -0.0013 295  PHE A CD1 
2414 C CD2 . PHE A 358 ? 0.4175 0.3990 0.4934 0.0150  0.0134  -0.0012 295  PHE A CD2 
2415 C CE1 . PHE A 358 ? 0.4037 0.4026 0.4985 0.0113  0.0167  0.0005  295  PHE A CE1 
2416 C CE2 . PHE A 358 ? 0.6061 0.5829 0.6840 0.0137  0.0174  0.0009  295  PHE A CE2 
2417 C CZ  . PHE A 358 ? 0.4658 0.4512 0.5531 0.0117  0.0191  0.0017  295  PHE A CZ  
2418 N N   . ALA A 359 ? 0.3483 0.3488 0.4187 0.0293  0.0013  -0.0035 296  ALA A N   
2419 C CA  . ALA A 359 ? 0.3347 0.3285 0.3995 0.0354  0.0009  -0.0029 296  ALA A CA  
2420 C C   . ALA A 359 ? 0.4025 0.4069 0.4704 0.0411  -0.0013 -0.0030 296  ALA A C   
2421 O O   . ALA A 359 ? 0.3620 0.3623 0.4284 0.0453  -0.0007 -0.0029 296  ALA A O   
2422 C CB  . ALA A 359 ? 0.3435 0.3294 0.3993 0.0376  -0.0009 -0.0027 296  ALA A CB  
2423 N N   . ILE A 360 ? 0.3320 0.3502 0.4040 0.0414  -0.0040 -0.0031 297  ILE A N   
2424 C CA  . ILE A 360 ? 0.3310 0.3611 0.4060 0.0474  -0.0060 -0.0027 297  ILE A CA  
2425 C C   . ILE A 360 ? 0.3234 0.3612 0.4067 0.0464  -0.0041 -0.0026 297  ILE A C   
2426 O O   . ILE A 360 ? 0.3749 0.4139 0.4581 0.0520  -0.0038 -0.0028 297  ILE A O   
2427 C CB  . ILE A 360 ? 0.3320 0.3760 0.4089 0.0478  -0.0096 -0.0019 297  ILE A CB  
2428 C CG1 . ILE A 360 ? 0.3539 0.3915 0.4221 0.0505  -0.0116 -0.0017 297  ILE A CG1 
2429 C CG2 . ILE A 360 ? 0.3294 0.3888 0.4111 0.0535  -0.0112 -0.0007 297  ILE A CG2 
2430 C CD1 . ILE A 360 ? 0.3426 0.3925 0.4117 0.0488  -0.0151 -0.0007 297  ILE A CD1 
2431 N N   . TYR A 361 ? 0.3663 0.4092 0.4567 0.0394  -0.0028 -0.0023 298  TYR A N   
2432 C CA  . TYR A 361 ? 0.3066 0.3588 0.4061 0.0381  -0.0010 -0.0017 298  TYR A CA  
2433 C C   . TYR A 361 ? 0.3468 0.3882 0.4442 0.0391  0.0023  -0.0022 298  TYR A C   
2434 O O   . TYR A 361 ? 0.3337 0.3821 0.4359 0.0413  0.0032  -0.0020 298  TYR A O   
2435 C CB  . TYR A 361 ? 0.3696 0.4277 0.4770 0.0299  -0.0002 -0.0010 298  TYR A CB  
2436 C CG  . TYR A 361 ? 0.2939 0.3620 0.4115 0.0280  0.0019  0.0002  298  TYR A CG  
2437 C CD1 . TYR A 361 ? 0.3462 0.4316 0.4705 0.0317  -0.0001 0.0014  298  TYR A CD1 
2438 C CD2 . TYR A 361 ? 0.3353 0.3965 0.4559 0.0230  0.0059  0.0005  298  TYR A CD2 
2439 C CE1 . TYR A 361 ? 0.3548 0.4505 0.4887 0.0301  0.0018  0.0026  298  TYR A CE1 
2440 C CE2 . TYR A 361 ? 0.3726 0.4438 0.5030 0.0212  0.0079  0.0019  298  TYR A CE2 
2441 C CZ  . TYR A 361 ? 0.3538 0.4423 0.4908 0.0247  0.0057  0.0029  298  TYR A CZ  
2442 O OH  . TYR A 361 ? 0.3859 0.4855 0.5329 0.0230  0.0077  0.0045  298  TYR A OH  
2443 N N   . CYS A 362 ? 0.3110 0.3359 0.4010 0.0376  0.0039  -0.0025 299  CYS A N   
2444 C CA  . CYS A 362 ? 0.3110 0.3253 0.3986 0.0377  0.0068  -0.0022 299  CYS A CA  
2445 C C   . CYS A 362 ? 0.3311 0.3425 0.4135 0.0451  0.0053  -0.0031 299  CYS A C   
2446 O O   . CYS A 362 ? 0.4596 0.4666 0.5418 0.0454  0.0071  -0.0031 299  CYS A O   
2447 C CB  . CYS A 362 ? 0.3157 0.3142 0.3964 0.0343  0.0085  -0.0015 299  CYS A CB  
2448 S SG  . CYS A 362 ? 0.4445 0.4423 0.5310 0.0256  0.0126  -0.0001 299  CYS A SG  
2449 N N   . VAL A 363 ? 0.3646 0.3781 0.4426 0.0512  0.0020  -0.0038 300  VAL A N   
2450 C CA  . VAL A 363 ? 0.4017 0.4124 0.4746 0.0591  0.0006  -0.0048 300  VAL A CA  
2451 C C   . VAL A 363 ? 0.4847 0.5126 0.5634 0.0641  -0.0007 -0.0052 300  VAL A C   
2452 O O   . VAL A 363 ? 0.4992 0.5260 0.5748 0.0706  -0.0012 -0.0064 300  VAL A O   
2453 C CB  . VAL A 363 ? 0.4646 0.4654 0.5280 0.0640  -0.0019 -0.0047 300  VAL A CB  
2454 C CG1 . VAL A 363 ? 0.5196 0.5031 0.5765 0.0604  -0.0007 -0.0039 300  VAL A CG1 
2455 C CG2 . VAL A 363 ? 0.3998 0.4106 0.4646 0.0643  -0.0042 -0.0041 300  VAL A CG2 
2456 N N   . VAL A 364 ? 0.3450 0.3885 0.4315 0.0613  -0.0015 -0.0041 301  VAL A N   
2457 C CA  . VAL A 364 ? 0.3496 0.4117 0.4423 0.0658  -0.0030 -0.0035 301  VAL A CA  
2458 C C   . VAL A 364 ? 0.4314 0.5035 0.5337 0.0621  -0.0007 -0.0031 301  VAL A C   
2459 O O   . VAL A 364 ? 0.4055 0.4873 0.5105 0.0674  -0.0008 -0.0034 301  VAL A O   
2460 C CB  . VAL A 364 ? 0.3236 0.3988 0.4196 0.0648  -0.0058 -0.0017 301  VAL A CB  
2461 C CG1 . VAL A 364 ? 0.5107 0.6076 0.6149 0.0679  -0.0072 0.0000  301  VAL A CG1 
2462 C CG2 . VAL A 364 ? 0.4560 0.5245 0.5428 0.0702  -0.0081 -0.0017 301  VAL A CG2 
2463 N N   . GLY A 365 ? 0.3537 0.4242 0.4614 0.0534  0.0013  -0.0023 302  GLY A N   
2464 C CA  . GLY A 365 ? 0.3961 0.4769 0.5139 0.0494  0.0036  -0.0013 302  GLY A CA  
2465 C C   . GLY A 365 ? 0.3895 0.4624 0.5051 0.0507  0.0063  -0.0025 302  GLY A C   
2466 O O   . GLY A 365 ? 0.4436 0.5012 0.5495 0.0539  0.0064  -0.0040 302  GLY A O   
2467 N N   . SER A 366 ? 0.3924 0.4765 0.5174 0.0478  0.0083  -0.0014 303  SER A N   
2468 C CA  . SER A 366 ? 0.4451 0.5240 0.5693 0.0479  0.0110  -0.0022 303  SER A CA  
2469 C C   . SER A 366 ? 0.4328 0.5184 0.5675 0.0398  0.0144  0.0001  303  SER A C   
2470 O O   . SER A 366 ? 0.4351 0.5308 0.5784 0.0352  0.0143  0.0021  303  SER A O   
2471 C CB  . SER A 366 ? 0.6136 0.7021 0.7374 0.0559  0.0098  -0.0036 303  SER A CB  
2472 O OG  . SER A 366 ? 0.8260 0.9356 0.9619 0.0548  0.0103  -0.0018 303  SER A OG  
2473 N N   . HIS A 367 ? 0.4508 0.5306 0.5848 0.0382  0.0172  0.0000  304  HIS A N   
2474 C CA  . HIS A 367 ? 0.4924 0.5763 0.6353 0.0305  0.0211  0.0027  304  HIS A CA  
2475 C C   . HIS A 367 ? 0.3862 0.4924 0.5428 0.0292  0.0212  0.0046  304  HIS A C   
2476 O O   . HIS A 367 ? 0.4131 0.5246 0.5789 0.0224  0.0239  0.0074  304  HIS A O   
2477 C CB  . HIS A 367 ? 0.5458 0.6205 0.6847 0.0293  0.0238  0.0025  304  HIS A CB  
2478 C CG  . HIS A 367 ? 0.5781 0.6594 0.7157 0.0354  0.0227  0.0004  304  HIS A CG  
2479 N ND1 . HIS A 367 ? 0.6560 0.7543 0.8037 0.0345  0.0243  0.0016  304  HIS A ND1 
2480 C CD2 . HIS A 367 ? 0.5603 0.6331 0.6872 0.0426  0.0202  -0.0028 304  HIS A CD2 
2481 C CE1 . HIS A 367 ? 0.6102 0.7104 0.7531 0.0412  0.0229  -0.0011 304  HIS A CE1 
2482 N NE2 . HIS A 367 ? 0.7474 0.8317 0.8775 0.0463  0.0204  -0.0039 304  HIS A NE2 
2483 N N   . GLU A 368 ? 0.4137 0.5333 0.5720 0.0358  0.0185  0.0036  305  GLU A N   
2484 C CA  . GLU A 368 ? 0.4570 0.5995 0.6287 0.0348  0.0182  0.0062  305  GLU A CA  
2485 C C   . GLU A 368 ? 0.5567 0.7065 0.7353 0.0302  0.0165  0.0086  305  GLU A C   
2486 O O   . GLU A 368 ? 0.3841 0.5504 0.5752 0.0263  0.0168  0.0117  305  GLU A O   
2487 C CB  . GLU A 368 ? 0.4146 0.5703 0.5855 0.0439  0.0156  0.0049  305  GLU A CB  
2488 C CG  . GLU A 368 ? 0.6847 0.8352 0.8493 0.0488  0.0169  0.0022  305  GLU A CG  
2489 C CD  . GLU A 368 ? 0.8710 1.0362 1.0354 0.0583  0.0147  0.0011  305  GLU A CD  
2490 O OE1 . GLU A 368 ? 0.8537 1.0404 1.0286 0.0589  0.0134  0.0040  305  GLU A OE1 
2491 O OE2 . GLU A 368 ? 1.0971 1.2524 1.2506 0.0653  0.0140  -0.0024 305  GLU A OE2 
2492 N N   . ASP A 369 ? 0.3601 0.4983 0.5308 0.0303  0.0144  0.0073  306  ASP A N   
2493 C CA  . ASP A 369 ? 0.4217 0.5657 0.5977 0.0256  0.0123  0.0092  306  ASP A CA  
2494 C C   . ASP A 369 ? 0.2650 0.4075 0.4490 0.0166  0.0155  0.0115  306  ASP A C   
2495 O O   . ASP A 369 ? 0.3214 0.4512 0.5025 0.0138  0.0194  0.0111  306  ASP A O   
2496 C CB  . ASP A 369 ? 0.3485 0.4782 0.5135 0.0267  0.0100  0.0073  306  ASP A CB  
2497 C CG  . ASP A 369 ? 0.4559 0.5868 0.6129 0.0357  0.0069  0.0055  306  ASP A CG  
2498 O OD1 . ASP A 369 ? 0.3104 0.4558 0.4711 0.0413  0.0059  0.0061  306  ASP A OD1 
2499 O OD2 . ASP A 369 ? 0.3867 0.5043 0.5337 0.0375  0.0056  0.0038  306  ASP A OD2 
2500 N N   . PRO A 370 ? 0.3079 0.4630 0.5020 0.0118  0.0140  0.0142  307  PRO A N   
2501 C CA  . PRO A 370 ? 0.3720 0.5230 0.5725 0.0034  0.0168  0.0162  307  PRO A CA  
2502 C C   . PRO A 370 ? 0.3525 0.4817 0.5425 0.0008  0.0181  0.0140  307  PRO A C   
2503 O O   . PRO A 370 ? 0.3729 0.4943 0.5535 0.0035  0.0151  0.0118  307  PRO A O   
2504 C CB  . PRO A 370 ? 0.3534 0.5206 0.5643 -0.0005 0.0133  0.0191  307  PRO A CB  
2505 C CG  . PRO A 370 ? 0.4808 0.6657 0.6940 0.0060  0.0097  0.0198  307  PRO A CG  
2506 C CD  . PRO A 370 ? 0.2623 0.4358 0.4621 0.0137  0.0094  0.0160  307  PRO A CD  
2507 N N   . ALA A 371 ? 0.3355 0.4556 0.5272 -0.0043 0.0226  0.0151  308  ALA A N   
2508 C CA  . ALA A 371 ? 0.3881 0.4876 0.5694 -0.0060 0.0245  0.0135  308  ALA A CA  
2509 C C   . ALA A 371 ? 0.3347 0.4289 0.5127 -0.0089 0.0216  0.0124  308  ALA A C   
2510 O O   . ALA A 371 ? 0.3583 0.4366 0.5257 -0.0085 0.0219  0.0104  308  ALA A O   
2511 C CB  . ALA A 371 ? 0.4110 0.5043 0.5959 -0.0106 0.0302  0.0158  308  ALA A CB  
2512 N N   . VAL A 372 ? 0.2497 0.3572 0.4364 -0.0119 0.0184  0.0138  309  VAL A N   
2513 C CA  . VAL A 372 ? 0.3083 0.4105 0.4920 -0.0159 0.0154  0.0128  309  VAL A CA  
2514 C C   . VAL A 372 ? 0.3926 0.4882 0.5644 -0.0115 0.0118  0.0098  309  VAL A C   
2515 O O   . VAL A 372 ? 0.3542 0.4384 0.5187 -0.0138 0.0106  0.0080  309  VAL A O   
2516 C CB  . VAL A 372 ? 0.3399 0.4592 0.5355 -0.0201 0.0119  0.0156  309  VAL A CB  
2517 C CG1 . VAL A 372 ? 0.3817 0.5198 0.5815 -0.0151 0.0080  0.0168  309  VAL A CG1 
2518 C CG2 . VAL A 372 ? 0.4200 0.5325 0.6117 -0.0251 0.0085  0.0144  309  VAL A CG2 
2519 N N   . TYR A 373 ? 0.3267 0.4294 0.4964 -0.0048 0.0100  0.0094  310  TYR A N   
2520 C CA  . TYR A 373 ? 0.3351 0.4331 0.4944 -0.0004 0.0065  0.0072  310  TYR A CA  
2521 C C   . TYR A 373 ? 0.3300 0.4081 0.4774 0.0015  0.0090  0.0048  310  TYR A C   
2522 O O   . TYR A 373 ? 0.3405 0.4105 0.4790 0.0024  0.0068  0.0030  310  TYR A O   
2523 C CB  . TYR A 373 ? 0.3158 0.4278 0.4767 0.0067  0.0040  0.0078  310  TYR A CB  
2524 C CG  . TYR A 373 ? 0.3503 0.4836 0.5228 0.0049  0.0009  0.0108  310  TYR A CG  
2525 C CD1 . TYR A 373 ? 0.3835 0.5235 0.5569 0.0017  -0.0037 0.0118  310  TYR A CD1 
2526 C CD2 . TYR A 373 ? 0.4357 0.5831 0.6185 0.0058  0.0025  0.0131  310  TYR A CD2 
2527 C CE1 . TYR A 373 ? 0.4473 0.6075 0.6316 -0.0004 -0.0069 0.0155  310  TYR A CE1 
2528 C CE2 . TYR A 373 ? 0.3753 0.5436 0.5692 0.0042  -0.0005 0.0167  310  TYR A CE2 
2529 C CZ  . TYR A 373 ? 0.4556 0.6302 0.6504 0.0009  -0.0053 0.0180  310  TYR A CZ  
2530 O OH  . TYR A 373 ? 0.5320 0.7281 0.7381 -0.0012 -0.0087 0.0223  310  TYR A OH  
2531 N N   . THR A 374 ? 0.3157 0.3865 0.4629 0.0018  0.0136  0.0052  311  THR A N   
2532 C CA  . THR A 374 ? 0.3294 0.3818 0.4663 0.0024  0.0162  0.0040  311  THR A CA  
2533 C C   . THR A 374 ? 0.4167 0.4591 0.5514 -0.0032 0.0177  0.0038  311  THR A C   
2534 O O   . THR A 374 ? 0.3195 0.3500 0.4444 -0.0024 0.0171  0.0021  311  THR A O   
2535 C CB  . THR A 374 ? 0.3624 0.4114 0.5005 0.0033  0.0205  0.0054  311  THR A CB  
2536 O OG1 . THR A 374 ? 0.4000 0.4558 0.5378 0.0092  0.0188  0.0048  311  THR A OG1 
2537 C CG2 . THR A 374 ? 0.4274 0.4585 0.5557 0.0032  0.0233  0.0053  311  THR A CG2 
2538 N N   . TYR A 375 ? 0.3327 0.3801 0.4766 -0.0086 0.0197  0.0055  312  TYR A N   
2539 C CA  . TYR A 375 ? 0.3515 0.3891 0.4932 -0.0137 0.0211  0.0050  312  TYR A CA  
2540 C C   . TYR A 375 ? 0.3358 0.3723 0.4723 -0.0147 0.0162  0.0026  312  TYR A C   
2541 O O   . TYR A 375 ? 0.3325 0.3558 0.4600 -0.0157 0.0166  0.0007  312  TYR A O   
2542 C CB  . TYR A 375 ? 0.3816 0.4262 0.5351 -0.0191 0.0234  0.0075  312  TYR A CB  
2543 C CG  . TYR A 375 ? 0.3472 0.3900 0.5050 -0.0197 0.0293  0.0102  312  TYR A CG  
2544 C CD1 . TYR A 375 ? 0.3711 0.3989 0.5214 -0.0196 0.0337  0.0106  312  TYR A CD1 
2545 C CD2 . TYR A 375 ? 0.4244 0.4817 0.5940 -0.0204 0.0304  0.0129  312  TYR A CD2 
2546 C CE1 . TYR A 375 ? 0.4463 0.4735 0.6006 -0.0204 0.0391  0.0138  312  TYR A CE1 
2547 C CE2 . TYR A 375 ? 0.3855 0.4422 0.5592 -0.0213 0.0358  0.0157  312  TYR A CE2 
2548 C CZ  . TYR A 375 ? 0.3903 0.4319 0.5564 -0.0215 0.0401  0.0163  312  TYR A CZ  
2549 O OH  . TYR A 375 ? 0.4352 0.4771 0.6053 -0.0227 0.0454  0.0197  312  TYR A OH  
2550 N N   . ALA A 376 ? 0.3142 0.3653 0.4560 -0.0144 0.0115  0.0029  313  ALA A N   
2551 C CA  . ALA A 376 ? 0.3015 0.3535 0.4395 -0.0166 0.0065  0.0013  313  ALA A CA  
2552 C C   . ALA A 376 ? 0.3676 0.4109 0.4931 -0.0121 0.0048  -0.0011 313  ALA A C   
2553 O O   . ALA A 376 ? 0.3815 0.4193 0.5006 -0.0144 0.0021  -0.0030 313  ALA A O   
2554 C CB  . ALA A 376 ? 0.4158 0.4874 0.5629 -0.0172 0.0018  0.0033  313  ALA A CB  
2555 N N   . THR A 377 ? 0.3487 0.3906 0.4707 -0.0059 0.0060  -0.0009 314  THR A N   
2556 C CA  . THR A 377 ? 0.3610 0.3942 0.4716 -0.0015 0.0046  -0.0027 314  THR A CA  
2557 C C   . THR A 377 ? 0.3994 0.4153 0.5020 -0.0014 0.0087  -0.0034 314  THR A C   
2558 O O   . THR A 377 ? 0.4068 0.4140 0.4998 0.0002  0.0076  -0.0049 314  THR A O   
2559 C CB  . THR A 377 ? 0.3017 0.3416 0.4118 0.0056  0.0033  -0.0020 314  THR A CB  
2560 O OG1 . THR A 377 ? 0.3309 0.3696 0.4446 0.0074  0.0071  -0.0009 314  THR A OG1 
2561 C CG2 . THR A 377 ? 0.3183 0.3763 0.4351 0.0065  -0.0010 -0.0009 314  THR A CG2 
2562 N N   . LEU A 378 ? 0.4021 0.4141 0.5088 -0.0032 0.0135  -0.0019 315  LEU A N   
2563 C CA  . LEU A 378 ? 0.3079 0.3050 0.4075 -0.0032 0.0176  -0.0016 315  LEU A CA  
2564 C C   . LEU A 378 ? 0.4254 0.4139 0.5209 -0.0074 0.0184  -0.0030 315  LEU A C   
2565 O O   . LEU A 378 ? 0.3618 0.3386 0.4477 -0.0061 0.0195  -0.0038 315  LEU A O   
2566 C CB  . LEU A 378 ? 0.4370 0.4339 0.5424 -0.0040 0.0224  0.0011  315  LEU A CB  
2567 C CG  . LEU A 378 ? 0.5280 0.5113 0.6277 -0.0048 0.0273  0.0027  315  LEU A CG  
2568 C CD1 . LEU A 378 ? 0.5217 0.4953 0.6104 -0.0005 0.0266  0.0025  315  LEU A CD1 
2569 C CD2 . LEU A 378 ? 0.5263 0.5125 0.6333 -0.0063 0.0319  0.0059  315  LEU A CD2 
2570 N N   . LEU A 379 ? 0.3373 0.3312 0.4398 -0.0124 0.0177  -0.0033 316  LEU A N   
2571 C CA  . LEU A 379 ? 0.4091 0.3930 0.5072 -0.0164 0.0187  -0.0049 316  LEU A CA  
2572 C C   . LEU A 379 ? 0.4322 0.4095 0.5191 -0.0154 0.0153  -0.0080 316  LEU A C   
2573 O O   . LEU A 379 ? 0.4097 0.3742 0.4880 -0.0153 0.0177  -0.0091 316  LEU A O   
2574 C CB  . LEU A 379 ? 0.4433 0.4346 0.5511 -0.0222 0.0175  -0.0046 316  LEU A CB  
2575 C CG  . LEU A 379 ? 0.7550 0.7348 0.8588 -0.0266 0.0189  -0.0063 316  LEU A CG  
2576 C CD1 . LEU A 379 ? 0.5303 0.4996 0.6329 -0.0260 0.0258  -0.0045 316  LEU A CD1 
2577 C CD2 . LEU A 379 ? 0.7672 0.7550 0.8802 -0.0326 0.0160  -0.0060 316  LEU A CD2 
2578 N N   . PRO A 380 ? 0.4434 0.4293 0.5297 -0.0143 0.0099  -0.0091 317  PRO A N   
2579 C CA  . PRO A 380 ? 0.4768 0.4569 0.5522 -0.0133 0.0068  -0.0117 317  PRO A CA  
2580 C C   . PRO A 380 ? 0.4372 0.4075 0.5034 -0.0082 0.0092  -0.0114 317  PRO A C   
2581 O O   . PRO A 380 ? 0.4312 0.3921 0.4879 -0.0081 0.0092  -0.0133 317  PRO A O   
2582 C CB  . PRO A 380 ? 0.5277 0.5218 0.6061 -0.0124 0.0011  -0.0116 317  PRO A CB  
2583 C CG  . PRO A 380 ? 0.5171 0.5236 0.6080 -0.0152 0.0006  -0.0095 317  PRO A CG  
2584 C CD  . PRO A 380 ? 0.4856 0.4878 0.5810 -0.0142 0.0063  -0.0077 317  PRO A CD  
2585 N N   . ALA A 381 ? 0.3791 0.3515 0.4479 -0.0040 0.0110  -0.0090 318  ALA A N   
2586 C CA  . ALA A 381 ? 0.4098 0.3728 0.4703 0.0003  0.0130  -0.0080 318  ALA A CA  
2587 C C   . ALA A 381 ? 0.4710 0.4218 0.5268 -0.0012 0.0177  -0.0075 318  ALA A C   
2588 O O   . ALA A 381 ? 0.4680 0.4104 0.5144 0.0010  0.0183  -0.0076 318  ALA A O   
2589 C CB  . ALA A 381 ? 0.4115 0.3778 0.4760 0.0041  0.0142  -0.0054 318  ALA A CB  
2590 N N   . THR A 382 ? 0.4277 0.3781 0.4898 -0.0048 0.0212  -0.0066 319  THR A N   
2591 C CA  . THR A 382 ? 0.4600 0.3991 0.5174 -0.0058 0.0261  -0.0059 319  THR A CA  
2592 C C   . THR A 382 ? 0.4377 0.3700 0.4874 -0.0077 0.0245  -0.0095 319  THR A C   
2593 O O   . THR A 382 ? 0.5121 0.4341 0.5533 -0.0063 0.0274  -0.0095 319  THR A O   
2594 C CB  . THR A 382 ? 0.3914 0.3325 0.4581 -0.0090 0.0304  -0.0036 319  THR A CB  
2595 O OG1 . THR A 382 ? 0.3845 0.3297 0.4568 -0.0136 0.0284  -0.0059 319  THR A OG1 
2596 C CG2 . THR A 382 ? 0.3557 0.3054 0.4306 -0.0077 0.0310  -0.0007 319  THR A CG2 
2597 N N   . LEU A 383 ? 0.4332 0.3715 0.4855 -0.0110 0.0200  -0.0125 320  LEU A N   
2598 C CA  . LEU A 383 ? 0.5087 0.4402 0.5531 -0.0135 0.0179  -0.0163 320  LEU A CA  
2599 C C   . LEU A 383 ? 0.3940 0.3204 0.4267 -0.0096 0.0164  -0.0176 320  LEU A C   
2600 O O   . LEU A 383 ? 0.4330 0.3503 0.4566 -0.0102 0.0167  -0.0203 320  LEU A O   
2601 C CB  . LEU A 383 ? 0.5063 0.4469 0.5557 -0.0181 0.0123  -0.0185 320  LEU A CB  
2602 C CG  . LEU A 383 ? 0.7649 0.7115 0.8262 -0.0227 0.0130  -0.0171 320  LEU A CG  
2603 C CD1 . LEU A 383 ? 0.5856 0.5416 0.6507 -0.0274 0.0067  -0.0187 320  LEU A CD1 
2604 C CD2 . LEU A 383 ? 0.6031 0.5381 0.6634 -0.0251 0.0178  -0.0174 320  LEU A CD2 
2605 N N   . ASN A 384 ? 0.4446 0.3767 0.4774 -0.0055 0.0147  -0.0157 321  ASN A N   
2606 C CA  . ASN A 384 ? 0.4339 0.3621 0.4566 -0.0017 0.0133  -0.0162 321  ASN A CA  
2607 C C   . ASN A 384 ? 0.5008 0.4176 0.5162 0.0007  0.0183  -0.0146 321  ASN A C   
2608 O O   . ASN A 384 ? 0.4627 0.3740 0.4684 0.0025  0.0178  -0.0160 321  ASN A O   
2609 C CB  . ASN A 384 ? 0.4422 0.3779 0.4671 0.0024  0.0109  -0.0139 321  ASN A CB  
2610 C CG  . ASN A 384 ? 0.5027 0.4368 0.5183 0.0058  0.0084  -0.0143 321  ASN A CG  
2611 O OD1 . ASN A 384 ? 0.6709 0.6011 0.6829 0.0099  0.0100  -0.0116 321  ASN A OD1 
2612 N ND2 . ASN A 384 ? 0.4496 0.3871 0.4616 0.0039  0.0043  -0.0174 321  ASN A ND2 
2613 N N   . SER A 385 ? 0.3819 0.2964 0.4022 0.0010  0.0232  -0.0113 322  SER A N   
2614 C CA  . SER A 385 ? 0.4143 0.3192 0.4283 0.0031  0.0282  -0.0090 322  SER A CA  
2615 C C   . SER A 385 ? 0.4325 0.3289 0.4409 0.0011  0.0302  -0.0120 322  SER A C   
2616 O O   . SER A 385 ? 0.4548 0.3432 0.4554 0.0037  0.0339  -0.0108 322  SER A O   
2617 C CB  . SER A 385 ? 0.4883 0.3939 0.5094 0.0034  0.0328  -0.0041 322  SER A CB  
2618 O OG  . SER A 385 ? 0.5097 0.4201 0.5330 0.0060  0.0312  -0.0012 322  SER A OG  
2619 N N   . MET A 386 ? 0.4615 0.3595 0.4734 -0.0035 0.0279  -0.0158 323  MET A N   
2620 C CA  . MET A 386 ? 0.5360 0.4246 0.5410 -0.0055 0.0286  -0.0197 323  MET A CA  
2621 C C   . MET A 386 ? 0.4819 0.3682 0.4761 -0.0049 0.0243  -0.0238 323  MET A C   
2622 O O   . MET A 386 ? 0.5429 0.4193 0.5275 -0.0046 0.0256  -0.0268 323  MET A O   
2623 C CB  . MET A 386 ? 0.5989 0.4893 0.6114 -0.0114 0.0271  -0.0220 323  MET A CB  
2624 C CG  . MET A 386 ? 0.5365 0.4292 0.5598 -0.0129 0.0314  -0.0184 323  MET A CG  
2625 S SD  . MET A 386 ? 0.6441 0.5400 0.6759 -0.0202 0.0282  -0.0211 323  MET A SD  
2626 C CE  . MET A 386 ? 0.6539 0.5574 0.7003 -0.0208 0.0329  -0.0156 323  MET A CE  
2627 N N   . ILE A 387 ? 0.5156 0.4111 0.5113 -0.0046 0.0192  -0.0242 324  ILE A N   
2628 C CA  . ILE A 387 ? 0.4642 0.3597 0.4507 -0.0044 0.0147  -0.0277 324  ILE A CA  
2629 C C   . ILE A 387 ? 0.4354 0.3279 0.4134 0.0014  0.0163  -0.0257 324  ILE A C   
2630 O O   . ILE A 387 ? 0.4736 0.3609 0.4409 0.0024  0.0155  -0.0285 324  ILE A O   
2631 C CB  . ILE A 387 ? 0.5205 0.4287 0.5130 -0.0064 0.0087  -0.0281 324  ILE A CB  
2632 C CG1 . ILE A 387 ? 0.6634 0.5759 0.6646 -0.0124 0.0067  -0.0294 324  ILE A CG1 
2633 C CG2 . ILE A 387 ? 0.5029 0.4128 0.4865 -0.0064 0.0040  -0.0310 324  ILE A CG2 
2634 C CD1 . ILE A 387 ? 0.8130 0.7399 0.8217 -0.0137 0.0015  -0.0285 324  ILE A CD1 
2635 N N   . ASN A 388 ? 0.4340 0.3299 0.4163 0.0050  0.0184  -0.0207 325  ASN A N   
2636 C CA  . ASN A 388 ? 0.5093 0.4032 0.4847 0.0102  0.0196  -0.0176 325  ASN A CA  
2637 C C   . ASN A 388 ? 0.5275 0.4117 0.4923 0.0123  0.0231  -0.0185 325  ASN A C   
2638 O O   . ASN A 388 ? 0.5093 0.3931 0.4652 0.0148  0.0212  -0.0196 325  ASN A O   
2639 C CB  . ASN A 388 ? 0.4703 0.3662 0.4522 0.0127  0.0224  -0.0117 325  ASN A CB  
2640 C CG  . ASN A 388 ? 0.4774 0.3825 0.4665 0.0130  0.0186  -0.0105 325  ASN A CG  
2641 O OD1 . ASN A 388 ? 0.4832 0.3941 0.4714 0.0127  0.0139  -0.0130 325  ASN A OD1 
2642 N ND2 . ASN A 388 ? 0.4805 0.3873 0.4766 0.0138  0.0206  -0.0066 325  ASN A ND2 
2643 N N   . PRO A 389 ? 0.4428 0.3196 0.4076 0.0119  0.0282  -0.0179 326  PRO A N   
2644 C CA  . PRO A 389 ? 0.5192 0.3869 0.4728 0.0150  0.0318  -0.0184 326  PRO A CA  
2645 C C   . PRO A 389 ? 0.4616 0.3248 0.4055 0.0136  0.0286  -0.0251 326  PRO A C   
2646 O O   . PRO A 389 ? 0.5229 0.3816 0.4559 0.0173  0.0297  -0.0258 326  PRO A O   
2647 C CB  . PRO A 389 ? 0.4736 0.3351 0.4309 0.0142  0.0377  -0.0166 326  PRO A CB  
2648 C CG  . PRO A 389 ? 0.5328 0.3993 0.5021 0.0091  0.0360  -0.0174 326  PRO A CG  
2649 C CD  . PRO A 389 ? 0.4276 0.3046 0.4024 0.0090  0.0312  -0.0163 326  PRO A CD  
2650 N N   . ILE A 390 ? 0.4750 0.3401 0.4225 0.0082  0.0245  -0.0297 327  ILE A N   
2651 C CA  . ILE A 390 ? 0.4771 0.3379 0.4150 0.0059  0.0208  -0.0361 327  ILE A CA  
2652 C C   . ILE A 390 ? 0.4795 0.3476 0.4122 0.0079  0.0163  -0.0365 327  ILE A C   
2653 O O   . ILE A 390 ? 0.5082 0.3722 0.4294 0.0098  0.0156  -0.0394 327  ILE A O   
2654 C CB  . ILE A 390 ? 0.5162 0.3777 0.4599 -0.0012 0.0172  -0.0401 327  ILE A CB  
2655 C CG1 . ILE A 390 ? 0.6099 0.4633 0.5581 -0.0029 0.0219  -0.0397 327  ILE A CG1 
2656 C CG2 . ILE A 390 ? 0.6182 0.4759 0.5519 -0.0045 0.0123  -0.0466 327  ILE A CG2 
2657 C CD1 . ILE A 390 ? 0.6476 0.5044 0.6053 -0.0097 0.0188  -0.0414 327  ILE A CD1 
2658 N N   . ILE A 391 ? 0.4966 0.3758 0.4377 0.0079  0.0134  -0.0332 328  ILE A N   
2659 C CA  A ILE A 391 ? 0.5485 0.4356 0.4860 0.0097  0.0090  -0.0331 328  ILE A CA  
2660 C CA  B ILE A 391 ? 0.5485 0.4356 0.4860 0.0097  0.0090  -0.0330 328  ILE A CA  
2661 C C   . ILE A 391 ? 0.4716 0.3573 0.4025 0.0160  0.0117  -0.0293 328  ILE A C   
2662 O O   . ILE A 391 ? 0.4805 0.3670 0.4023 0.0179  0.0098  -0.0310 328  ILE A O   
2663 C CB  A ILE A 391 ? 0.5865 0.4854 0.5349 0.0086  0.0055  -0.0304 328  ILE A CB  
2664 C CB  B ILE A 391 ? 0.5865 0.4853 0.5348 0.0087  0.0056  -0.0303 328  ILE A CB  
2665 C CG1 A ILE A 391 ? 0.4882 0.3905 0.4425 0.0022  0.0021  -0.0337 328  ILE A CG1 
2666 C CG1 B ILE A 391 ? 0.4875 0.3902 0.4415 0.0024  0.0019  -0.0338 328  ILE A CG1 
2667 C CG2 A ILE A 391 ? 0.6008 0.5079 0.5459 0.0114  0.0018  -0.0290 328  ILE A CG2 
2668 C CG2 B ILE A 391 ? 0.6000 0.5069 0.5452 0.0118  0.0020  -0.0286 328  ILE A CG2 
2669 C CD1 A ILE A 391 ? 0.5554 0.4571 0.5017 -0.0018 -0.0023 -0.0392 328  ILE A CD1 
2670 C CD1 B ILE A 391 ? 0.6172 0.5301 0.5831 0.0019  0.0002  -0.0306 328  ILE A CD1 
2671 N N   . TYR A 392 ? 0.5374 0.4219 0.4730 0.0192  0.0160  -0.0238 329  TYR A N   
2672 C CA  . TYR A 392 ? 0.5010 0.3863 0.4321 0.0248  0.0178  -0.0187 329  TYR A CA  
2673 C C   . TYR A 392 ? 0.4921 0.3690 0.4146 0.0282  0.0229  -0.0178 329  TYR A C   
2674 O O   . TYR A 392 ? 0.5595 0.4378 0.4762 0.0328  0.0238  -0.0142 329  TYR A O   
2675 C CB  . TYR A 392 ? 0.4558 0.3457 0.3964 0.0262  0.0186  -0.0124 329  TYR A CB  
2676 C CG  . TYR A 392 ? 0.4441 0.3430 0.3913 0.0249  0.0135  -0.0126 329  TYR A CG  
2677 C CD1 . TYR A 392 ? 0.5611 0.4661 0.5048 0.0274  0.0097  -0.0117 329  TYR A CD1 
2678 C CD2 . TYR A 392 ? 0.4361 0.3382 0.3929 0.0214  0.0125  -0.0136 329  TYR A CD2 
2679 C CE1 . TYR A 392 ? 0.5092 0.4225 0.4586 0.0268  0.0054  -0.0116 329  TYR A CE1 
2680 C CE2 . TYR A 392 ? 0.4939 0.4047 0.4562 0.0210  0.0080  -0.0136 329  TYR A CE2 
2681 C CZ  . TYR A 392 ? 0.5223 0.4384 0.4808 0.0238  0.0046  -0.0125 329  TYR A CZ  
2682 O OH  . TYR A 392 ? 0.5364 0.4613 0.5000 0.0240  0.0005  -0.0121 329  TYR A OH  
2683 N N   . ALA A 393 ? 0.4971 0.3656 0.4186 0.0263  0.0264  -0.0206 330  ALA A N   
2684 C CA  . ALA A 393 ? 0.5044 0.3648 0.4174 0.0303  0.0319  -0.0194 330  ALA A CA  
2685 C C   . ALA A 393 ? 0.5733 0.4248 0.4759 0.0292  0.0318  -0.0268 330  ALA A C   
2686 O O   . ALA A 393 ? 0.5755 0.4246 0.4666 0.0331  0.0321  -0.0282 330  ALA A O   
2687 C CB  . ALA A 393 ? 0.5591 0.4163 0.4792 0.0304  0.0374  -0.0146 330  ALA A CB  
2688 N N   . PHE A 394 ? 0.5457 0.3920 0.4516 0.0241  0.0312  -0.0315 331  PHE A N   
2689 C CA  . PHE A 394 ? 0.5358 0.3708 0.4312 0.0231  0.0318  -0.0382 331  PHE A CA  
2690 C C   . PHE A 394 ? 0.6435 0.4796 0.5298 0.0214  0.0260  -0.0443 331  PHE A C   
2691 O O   . PHE A 394 ? 0.6008 0.4272 0.4750 0.0223  0.0266  -0.0496 331  PHE A O   
2692 C CB  . PHE A 394 ? 0.5687 0.3980 0.4711 0.0174  0.0323  -0.0409 331  PHE A CB  
2693 C CG  . PHE A 394 ? 0.5831 0.4096 0.4925 0.0192  0.0388  -0.0356 331  PHE A CG  
2694 C CD1 . PHE A 394 ? 0.6909 0.5105 0.5928 0.0252  0.0451  -0.0327 331  PHE A CD1 
2695 C CD2 . PHE A 394 ? 0.6351 0.4668 0.5584 0.0150  0.0387  -0.0330 331  PHE A CD2 
2696 C CE1 . PHE A 394 ? 0.6836 0.5018 0.5921 0.0267  0.0512  -0.0272 331  PHE A CE1 
2697 C CE2 . PHE A 394 ? 0.7007 0.5308 0.6306 0.0163  0.0447  -0.0279 331  PHE A CE2 
2698 C CZ  . PHE A 394 ? 0.5863 0.4097 0.5089 0.0220  0.0509  -0.0248 331  PHE A CZ  
2699 N N   . ARG A 395 ? 0.5578 0.4052 0.4490 0.0193  0.0207  -0.0436 332  ARG A N   
2700 C CA  . ARG A 395 ? 0.6849 0.5353 0.5676 0.0179  0.0153  -0.0484 332  ARG A CA  
2701 C C   . ARG A 395 ? 0.6545 0.5079 0.5281 0.0244  0.0163  -0.0461 332  ARG A C   
2702 O O   . ARG A 395 ? 0.7058 0.5615 0.5709 0.0240  0.0125  -0.0500 332  ARG A O   
2703 C CB  . ARG A 395 ? 0.6874 0.5497 0.5791 0.0131  0.0092  -0.0481 332  ARG A CB  
2704 C CG  . ARG A 395 ? 0.8422 0.7023 0.7393 0.0056  0.0063  -0.0522 332  ARG A CG  
2705 C CD  . ARG A 395 ? 0.7003 0.5738 0.6072 0.0016  0.0008  -0.0508 332  ARG A CD  
2706 N NE  . ARG A 395 ? 0.9174 0.7994 0.8187 0.0024  -0.0037 -0.0514 332  ARG A NE  
2707 C CZ  . ARG A 395 ? 1.0710 0.9630 0.9758 0.0067  -0.0041 -0.0464 332  ARG A CZ  
2708 N NH1 . ARG A 395 ? 0.7915 0.6859 0.7048 0.0104  -0.0008 -0.0406 332  ARG A NH1 
2709 N NH2 . ARG A 395 ? 0.9970 0.8966 0.8963 0.0072  -0.0081 -0.0471 332  ARG A NH2 
2710 N N   . ASN A 396 ? 0.7070 0.5612 0.5823 0.0302  0.0212  -0.0395 333  ASN A N   
2711 C CA  . ASN A 396 ? 0.6211 0.4791 0.4886 0.0366  0.0223  -0.0362 333  ASN A CA  
2712 C C   . ASN A 396 ? 0.6949 0.5421 0.5483 0.0405  0.0262  -0.0398 333  ASN A C   
2713 O O   . ASN A 396 ? 0.5989 0.4366 0.4517 0.0415  0.0311  -0.0398 333  ASN A O   
2714 C CB  . ASN A 396 ? 0.6576 0.5213 0.5329 0.0406  0.0255  -0.0270 333  ASN A CB  
2715 C CG  . ASN A 396 ? 0.6757 0.5448 0.5442 0.0470  0.0263  -0.0222 333  ASN A CG  
2716 O OD1 . ASN A 396 ? 0.7529 0.6173 0.6135 0.0520  0.0308  -0.0205 333  ASN A OD1 
2717 N ND2 . ASN A 396 ? 0.8496 0.7293 0.7214 0.0472  0.0219  -0.0196 333  ASN A ND2 
2718 N N   . GLN A 397 ? 0.6863 0.5355 0.5284 0.0431  0.0240  -0.0428 334  GLN A N   
2719 C CA  . GLN A 397 ? 0.7569 0.5955 0.5841 0.0470  0.0270  -0.0475 334  GLN A CA  
2720 C C   . GLN A 397 ? 0.6231 0.4589 0.4480 0.0545  0.0341  -0.0411 334  GLN A C   
2721 O O   . GLN A 397 ? 0.6625 0.4865 0.4788 0.0573  0.0386  -0.0440 334  GLN A O   
2722 C CB  . GLN A 397 ? 0.8410 0.6843 0.6567 0.0486  0.0232  -0.0513 334  GLN A CB  
2723 C CG  . GLN A 397 ? 1.2146 1.0710 1.0312 0.0544  0.0233  -0.0438 334  GLN A CG  
2724 C CD  . GLN A 397 ? 1.3989 1.2591 1.2024 0.0575  0.0209  -0.0474 334  GLN A CD  
2725 O OE1 . GLN A 397 ? 1.2336 1.0880 1.0281 0.0540  0.0178  -0.0559 334  GLN A OE1 
2726 N NE2 . GLN A 397 ? 1.3036 1.1737 1.1057 0.0638  0.0221  -0.0406 334  GLN A NE2 
2727 N N   . GLU A 398 ? 0.6430 0.4893 0.4750 0.0579  0.0353  -0.0321 335  GLU A N   
2728 C CA  . GLU A 398 ? 0.7351 0.5805 0.5652 0.0647  0.0417  -0.0248 335  GLU A CA  
2729 C C   . GLU A 398 ? 0.6222 0.4601 0.4598 0.0629  0.0464  -0.0227 335  GLU A C   
2730 O O   . GLU A 398 ? 0.6670 0.4986 0.4992 0.0678  0.0525  -0.0203 335  GLU A O   
2731 C CB  . GLU A 398 ? 0.7003 0.5590 0.5364 0.0677  0.0408  -0.0153 335  GLU A CB  
2732 C CG  . GLU A 398 ? 1.0439 0.9091 0.8693 0.0739  0.0402  -0.0137 335  GLU A CG  
2733 C CD  . GLU A 398 ? 1.1672 1.0461 0.9997 0.0755  0.0377  -0.0048 335  GLU A CD  
2734 O OE1 . GLU A 398 ? 1.1122 0.9973 0.9524 0.0710  0.0325  -0.0055 335  GLU A OE1 
2735 O OE2 . GLU A 398 ? 1.1208 1.0044 0.9512 0.0814  0.0410  0.0032  335  GLU A OE2 
2736 N N   . ILE A 399 ? 0.5887 0.4279 0.4385 0.0562  0.0439  -0.0233 336  ILE A N   
2737 C CA  . ILE A 399 ? 0.5925 0.4251 0.4498 0.0539  0.0480  -0.0220 336  ILE A CA  
2738 C C   . ILE A 399 ? 0.5747 0.3934 0.4235 0.0531  0.0501  -0.0298 336  ILE A C   
2739 O O   . ILE A 399 ? 0.5850 0.3961 0.4327 0.0557  0.0561  -0.0278 336  ILE A O   
2740 C CB  . ILE A 399 ? 0.6005 0.4386 0.4724 0.0470  0.0442  -0.0216 336  ILE A CB  
2741 C CG1 . ILE A 399 ? 0.6706 0.5201 0.5508 0.0483  0.0431  -0.0133 336  ILE A CG1 
2742 C CG2 . ILE A 399 ? 0.5741 0.4053 0.4533 0.0437  0.0479  -0.0217 336  ILE A CG2 
2743 C CD1 . ILE A 399 ? 0.7770 0.6269 0.6621 0.0512  0.0488  -0.0047 336  ILE A CD1 
2744 N N   . GLN A 400 ? 0.5945 0.4094 0.4369 0.0494  0.0451  -0.0384 337  GLN A N   
2745 C CA  . GLN A 400 ? 0.7454 0.5456 0.5783 0.0484  0.0462  -0.0463 337  GLN A CA  
2746 C C   . GLN A 400 ? 0.6482 0.4406 0.4671 0.0569  0.0521  -0.0458 337  GLN A C   
2747 O O   . GLN A 400 ? 0.6159 0.3960 0.4306 0.0584  0.0567  -0.0478 337  GLN A O   
2748 C CB  . GLN A 400 ? 0.6502 0.4490 0.4771 0.0430  0.0391  -0.0551 337  GLN A CB  
2749 C CG  . GLN A 400 ? 0.6831 0.4898 0.5233 0.0347  0.0334  -0.0555 337  GLN A CG  
2750 C CD  . GLN A 400 ? 0.6587 0.4676 0.4934 0.0297  0.0260  -0.0624 337  GLN A CD  
2751 O OE1 . GLN A 400 ? 0.7400 0.5451 0.5609 0.0322  0.0249  -0.0670 337  GLN A OE1 
2752 N NE2 . GLN A 400 ? 0.6656 0.4815 0.5111 0.0226  0.0210  -0.0629 337  GLN A NE2 
2753 N N   . ARG A 401 ? 0.7066 0.5067 0.5184 0.0628  0.0520  -0.0428 338  ARG A N   
2754 C CA  A ARG A 401 ? 0.6981 0.4928 0.4965 0.0718  0.0577  -0.0415 338  ARG A CA  
2755 C CA  B ARG A 401 ? 0.6981 0.4927 0.4965 0.0718  0.0577  -0.0416 338  ARG A CA  
2756 C C   . ARG A 401 ? 0.6853 0.4787 0.4891 0.0760  0.0652  -0.0333 338  ARG A C   
2757 O O   . ARG A 401 ? 0.6790 0.4613 0.4745 0.0806  0.0708  -0.0346 338  ARG A O   
2758 C CB  A ARG A 401 ? 0.7425 0.5490 0.5349 0.0771  0.0558  -0.0382 338  ARG A CB  
2759 C CB  B ARG A 401 ? 0.7428 0.5488 0.5348 0.0773  0.0560  -0.0383 338  ARG A CB  
2760 C CG  A ARG A 401 ? 0.7990 0.6029 0.5777 0.0872  0.0614  -0.0359 338  ARG A CG  
2761 C CG  B ARG A 401 ? 0.8435 0.6513 0.6288 0.0738  0.0491  -0.0462 338  ARG A CG  
2762 C CD  A ARG A 401 ? 0.8788 0.6980 0.6561 0.0921  0.0600  -0.0292 338  ARG A CD  
2763 C CD  B ARG A 401 ? 0.9358 0.7483 0.7076 0.0812  0.0494  -0.0461 338  ARG A CD  
2764 N NE  A ARG A 401 ? 0.9223 0.7428 0.6912 0.1020  0.0664  -0.0229 338  ARG A NE  
2765 N NE  B ARG A 401 ? 0.9408 0.7569 0.7078 0.0769  0.0424  -0.0531 338  ARG A NE  
2766 C CZ  A ARG A 401 ? 0.9123 0.7360 0.6880 0.1052  0.0719  -0.0131 338  ARG A CZ  
2767 C CZ  B ARG A 401 ? 0.9926 0.8221 0.7690 0.0727  0.0370  -0.0504 338  ARG A CZ  
2768 N NH1 A ARG A 401 ? 0.8911 0.7161 0.6816 0.0993  0.0719  -0.0090 338  ARG A NH1 
2769 N NH1 B ARG A 401 ? 0.9042 0.7441 0.6944 0.0726  0.0376  -0.0412 338  ARG A NH1 
2770 N NH2 A ARG A 401 ? 0.9414 0.7676 0.7085 0.1145  0.0774  -0.0071 338  ARG A NH2 
2771 N NH2 B ARG A 401 ? 1.1955 1.0278 0.9671 0.0685  0.0309  -0.0570 338  ARG A NH2 
2772 N N   . ALA A 402 ? 0.5922 0.3970 0.4097 0.0745  0.0655  -0.0245 339  ALA A N   
2773 C CA  . ALA A 402 ? 0.6103 0.4151 0.4340 0.0773  0.0722  -0.0161 339  ALA A CA  
2774 C C   . ALA A 402 ? 0.5810 0.3735 0.4078 0.0737  0.0752  -0.0203 339  ALA A C   
2775 O O   . ALA A 402 ? 0.6231 0.4094 0.4469 0.0784  0.0820  -0.0170 339  ALA A O   
2776 C CB  . ALA A 402 ? 0.6243 0.4423 0.4627 0.0744  0.0707  -0.0073 339  ALA A CB  
2777 N N   . LEU A 403 ? 0.6876 0.4769 0.5206 0.0656  0.0700  -0.0270 340  LEU A N   
2778 C CA  . LEU A 403 ? 0.6522 0.4300 0.4883 0.0617  0.0722  -0.0311 340  LEU A CA  
2779 C C   . LEU A 403 ? 0.6196 0.3816 0.4398 0.0662  0.0753  -0.0376 340  LEU A C   
2780 O O   . LEU A 403 ? 0.6703 0.4228 0.4902 0.0680  0.0810  -0.0368 340  LEU A O   
2781 C CB  . LEU A 403 ? 0.6007 0.3795 0.4457 0.0521  0.0652  -0.0369 340  LEU A CB  
2782 C CG  . LEU A 403 ? 0.7038 0.4725 0.5544 0.0467  0.0663  -0.0405 340  LEU A CG  
2783 C CD1 . LEU A 403 ? 0.6018 0.3725 0.4627 0.0481  0.0730  -0.0324 340  LEU A CD1 
2784 C CD2 . LEU A 403 ? 0.7282 0.5014 0.5883 0.0374  0.0589  -0.0449 340  LEU A CD2 
2785 N N   . TRP A 404 ? 0.7229 0.4819 0.5297 0.0682  0.0717  -0.0441 341  TRP A N   
2786 C CA  A TRP A 404 ? 0.7855 0.5287 0.5755 0.0731  0.0746  -0.0508 341  TRP A CA  
2787 C CA  B TRP A 404 ? 0.7855 0.5289 0.5752 0.0732  0.0745  -0.0508 341  TRP A CA  
2788 C C   . TRP A 404 ? 0.8769 0.6187 0.6602 0.0835  0.0832  -0.0439 341  TRP A C   
2789 O O   . TRP A 404 ? 0.8660 0.5938 0.6422 0.0871  0.0884  -0.0462 341  TRP A O   
2790 C CB  A TRP A 404 ? 0.7927 0.5347 0.5694 0.0732  0.0688  -0.0587 341  TRP A CB  
2791 C CB  B TRP A 404 ? 0.7925 0.5360 0.5691 0.0738  0.0688  -0.0580 341  TRP A CB  
2792 C CG  A TRP A 404 ? 0.8195 0.5635 0.6017 0.0630  0.0602  -0.0651 341  TRP A CG  
2793 C CG  B TRP A 404 ? 0.8812 0.6108 0.6378 0.0811  0.0719  -0.0641 341  TRP A CG  
2794 C CD1 A TRP A 404 ? 0.8839 0.6345 0.6610 0.0608  0.0537  -0.0693 341  TRP A CD1 
2795 C CD1 B TRP A 404 ? 0.9710 0.6816 0.7177 0.0797  0.0721  -0.0730 341  TRP A CD1 
2796 C CD2 A TRP A 404 ? 0.8245 0.5653 0.6185 0.0538  0.0572  -0.0674 341  TRP A CD2 
2797 C CD2 B TRP A 404 ? 0.9032 0.6369 0.6470 0.0910  0.0748  -0.0618 341  TRP A CD2 
2798 N NE1 A TRP A 404 ? 0.8059 0.5576 0.5906 0.0509  0.0470  -0.0738 341  TRP A NE1 
2799 N NE1 B TRP A 404 ? 0.8930 0.5947 0.6209 0.0884  0.0752  -0.0768 341  TRP A NE1 
2800 C CE2 A TRP A 404 ? 0.8300 0.5760 0.6252 0.0465  0.0489  -0.0727 341  TRP A CE2 
2801 C CE2 B TRP A 404 ? 0.7786 0.4949 0.5045 0.0957  0.0770  -0.0699 341  TRP A CE2 
2802 C CE3 A TRP A 404 ? 0.7282 0.4635 0.5323 0.0510  0.0609  -0.0650 341  TRP A CE3 
2803 C CE3 B TRP A 404 ? 0.9019 0.6522 0.6476 0.0964  0.0757  -0.0534 341  TRP A CE3 
2804 C CZ2 A TRP A 404 ? 0.8311 0.5770 0.6368 0.0368  0.0440  -0.0754 341  TRP A CZ2 
2805 C CZ2 B TRP A 404 ? 1.0218 0.7376 0.7314 0.1060  0.0803  -0.0701 341  TRP A CZ2 
2806 C CZ3 A TRP A 404 ? 0.7588 0.4940 0.5736 0.0414  0.0560  -0.0680 341  TRP A CZ3 
2807 C CZ3 B TRP A 404 ? 1.0141 0.7648 0.7445 0.1062  0.0787  -0.0530 341  TRP A CZ3 
2808 C CH2 A TRP A 404 ? 0.7046 0.4452 0.5201 0.0345  0.0476  -0.0730 341  TRP A CH2 
2809 C CH2 B TRP A 404 ? 0.8668 0.6008 0.5793 0.1112  0.0811  -0.0613 341  TRP A CH2 
2810 N N   . LEU A 405 ? 0.7370 0.4932 0.5227 0.0885  0.0849  -0.0351 342  LEU A N   
2811 C CA  . LEU A 405 ? 0.8127 0.5699 0.5932 0.0983  0.0930  -0.0270 342  LEU A CA  
2812 C C   . LEU A 405 ? 0.8577 0.6130 0.6493 0.0972  0.0989  -0.0205 342  LEU A C   
2813 O O   . LEU A 405 ? 0.9403 0.6901 0.7258 0.1045  0.1064  -0.0167 342  LEU A O   
2814 C CB  . LEU A 405 ? 0.7604 0.5348 0.5425 0.1026  0.0926  -0.0179 342  LEU A CB  
2815 C CG  . LEU A 405 ? 0.9580 0.7358 0.7273 0.1065  0.0886  -0.0222 342  LEU A CG  
2816 C CD1 . LEU A 405 ? 0.9077 0.7039 0.6823 0.1092  0.0875  -0.0121 342  LEU A CD1 
2817 C CD2 . LEU A 405 ? 0.9051 0.6716 0.6556 0.1158  0.0934  -0.0264 342  LEU A CD2 
2818 N N   . LEU A 406 ? 0.7969 0.5575 0.6048 0.0884  0.0958  -0.0190 343  LEU A N   
2819 C CA  . LEU A 406 ? 0.7832 0.5434 0.6025 0.0867  0.1012  -0.0128 343  LEU A CA  
2820 C C   . LEU A 406 ? 0.8835 0.6265 0.6988 0.0858  0.1039  -0.0196 343  LEU A C   
2821 O O   . LEU A 406 ? 0.9061 0.6443 0.7212 0.0903  0.1114  -0.0149 343  LEU A O   
2822 C CB  . LEU A 406 ? 0.8054 0.5764 0.6426 0.0779  0.0967  -0.0098 343  LEU A CB  
2823 C CG  . LEU A 406 ? 0.8636 0.6342 0.7140 0.0742  0.1010  -0.0051 343  LEU A CG  
2824 C CD1 . LEU A 406 ? 0.9570 0.7313 0.8068 0.0814  0.1094  0.0055  343  LEU A CD1 
2825 C CD2 . LEU A 406 ? 0.7459 0.5277 0.6125 0.0661  0.0960  -0.0028 343  LEU A CD2 
2826 N N   . LEU A 407 ? 0.8390 0.5727 0.6512 0.0797  0.0979  -0.0303 344  LEU A N   
2827 C CA  . LEU A 407 ? 1.0331 0.7495 0.8415 0.0779  0.0996  -0.0370 344  LEU A CA  
2828 C C   . LEU A 407 ? 1.0486 0.7513 0.8388 0.0879  0.1054  -0.0394 344  LEU A C   
2829 O O   . LEU A 407 ? 1.2021 0.8931 0.9905 0.0904  0.1112  -0.0392 344  LEU A O   
2830 C CB  . LEU A 407 ? 0.8959 0.6062 0.7041 0.0689  0.0909  -0.0475 344  LEU A CB  
2831 C CG  . LEU A 407 ? 0.8337 0.5566 0.6600 0.0592  0.0852  -0.0455 344  LEU A CG  
2832 C CD1 . LEU A 407 ? 0.7979 0.5175 0.6224 0.0511  0.0763  -0.0550 344  LEU A CD1 
2833 C CD2 . LEU A 407 ? 0.9631 0.6856 0.8038 0.0555  0.0891  -0.0409 344  LEU A CD2 
2834 N N   . ASP A 408 ? 1.0271 0.7316 0.8035 0.0940  0.1042  -0.0415 345  ASP A N   
2835 C CA  . ASP A 408 ? 1.1544 0.8463 0.9118 0.1041  0.1093  -0.0446 345  ASP A CA  
2836 C C   . ASP A 408 ? 1.3177 1.0165 1.0737 0.1145  0.1184  -0.0333 345  ASP A C   
2837 O O   . ASP A 408 ? 1.6230 1.3180 1.3632 0.1245  0.1221  -0.0336 345  ASP A O   
2838 C CB  . ASP A 408 ? 1.1982 0.8899 0.9409 0.1063  0.1039  -0.0518 345  ASP A CB  
2839 C CG  . ASP A 408 ? 1.2941 0.9792 1.0367 0.0960  0.0948  -0.0627 345  ASP A CG  
2840 O OD1 . ASP A 408 ? 1.0740 0.7547 0.8279 0.0874  0.0926  -0.0646 345  ASP A OD1 
2841 O OD2 . ASP A 408 ? 1.3244 1.0098 1.0559 0.0964  0.0898  -0.0690 345  ASP A OD2 
2842 N N   . GLY A 409 ? 1.2186 0.9280 0.9905 0.1124  0.1219  -0.0231 346  GLY A N   
2843 C CA  . GLY A 409 ? 1.1461 0.8635 0.9176 0.1215  0.1304  -0.0113 346  GLY A CA  
2844 C C   . GLY A 409 ? 1.4613 1.1907 1.2243 0.1289  0.1303  -0.0064 346  GLY A C   
2845 O O   . GLY A 409 ? 1.6596 1.3900 1.4132 0.1394  0.1372  -0.0004 346  GLY A O   
2846 N N   . CYS A 410 ? 1.3381 1.0775 1.1043 0.1239  0.1226  -0.0085 347  CYS A N   
2847 C CA  . CYS A 410 ? 1.5386 1.2906 1.2979 0.1301  0.1216  -0.0038 347  CYS A CA  
2848 C C   . CYS A 410 ? 1.5595 1.3012 1.2977 0.1394  0.1235  -0.0106 347  CYS A C   
2849 O O   . CYS A 410 ? 1.4176 1.1463 1.1469 0.1367  0.1191  -0.0228 347  CYS A O   
2850 C CB  . CYS A 410 ? 1.5839 1.3509 1.3501 0.1350  0.1273  0.0113  347  CYS A CB  
2851 S SG  . CYS A 410 ? 1.5764 1.3535 1.3660 0.1249  0.1266  0.0197  347  CYS A SG  
# 
