data_9G9N
# 
_entry.id   9G9N 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.401 
_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   9G9N         pdb_00009g9n 10.2210/pdb9g9n/pdb 
WWPDB D_1292140349 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-01-22 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9G9N 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-25 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB . 9G95 unspecified 
PDB . 9G97 unspecified 
PDB . 9G9M unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              james.naismith@mpls.ox.ac.uk 
_pdbx_contact_author.name_first         James 
_pdbx_contact_author.name_last          Naismith 
_pdbx_contact_author.name_mi            H. 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-6744-5061 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Le Bas, A.'     1 0000-0002-1100-6833 
'Naismith, J.H.' 2 0000-0001-6744-5061 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Open Biology' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2046-2441 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            15 
_citation.language                  ? 
_citation.page_first                240310 
_citation.page_last                 240310 
_citation.title                     'Structure of WzxE the lipid III flippase for Enterobacterial Common Antigen polysaccharide.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1098/rsob.240310 
_citation.pdbx_database_id_PubMed   39772807 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Le Bas, A.'       1  0000-0002-1100-6833 
primary 'Clarke, B.R.'     2  ?                   
primary 'Teelucksingh, T.' 3  ?                   
primary 'Lee, M.'          4  ?                   
primary 'El Omari, K.'     5  ?                   
primary 'Giltrap, A.M.'    6  ?                   
primary 'McMahon, S.A.'    7  ?                   
primary 'Liu, H.'          8  ?                   
primary 'Beale, J.H.'      9  0000-0003-1171-2428 
primary 'Mykhaylyk, V.'    10 ?                   
primary 'Duman, R.'        11 ?                   
primary 'Paterson, N.G.'   12 ?                   
primary 'Ward, P.N.'       13 0000-0003-2546-3426 
primary 'Harrison, P.J.'   14 0000-0001-5167-0547 
primary 'Weckener, M.'     15 ?                   
primary 'Pardon, E.'       16 ?                   
primary 'Steyaert, J.'     17 ?                   
primary 'Liu, H.'          18 ?                   
primary 'Quigley, A.'      19 0000-0002-5022-9845 
primary 'Davis, B.G.'      20 ?                   
primary 'Wagner, A.'       21 ?                   
primary 'Whitfield, C.'    22 ?                   
primary 'Naismith, J.H.'   23 0000-0001-6744-5061 
# 
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 'Lipid III flippase' 46130.621 1 ? ? ? ? 
2 polymer man 'NB10 Nanobody'      15132.753 1 ? ? ? ? 
3 polymer man 'NB7 Nanobody'       15223.880 1 ? ? ? ? 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;MVSLAKASLWTAASTLVKIGAGLLVGKLLAVSFGPAGLGLAANFRQLITVLGVLAGAGIFNGVTKYVAQYHDNPQQLRRV
VGTSSAMVLGFSTLMALVFVLAAAPISQGLFGNTDYQGLVRLVALVQMGIAWGNLLLALMKGFRDAAGNALSLIVGSLIG
VLAYYVSYRLGGYEGALLGLALIPALVVIPAAIMLIKRGVIPLSYLKPSWDNGLAGQLSKFTLMALITSVTLPVAYIMMR
KLLAAQYSWDEVGIWQGVSSISDAYLQFITASFSVYLLPTLSRLTEKRDITREVVKSLKFVLPAVAAASFTVWLLRDFAI
WLLLSNKFTAMRDLFAWQLVGDVLKVGAYVFGYLVIAKASLRFYILAEVSQFTLLMVFAHWLIPAHGALGAAQAYMATYI
VYFSLCCGVFLLWRRRALEENLYFQ
;
;MVSLAKASLWTAASTLVKIGAGLLVGKLLAVSFGPAGLGLAANFRQLITVLGVLAGAGIFNGVTKYVAQYHDNPQQLRRV
VGTSSAMVLGFSTLMALVFVLAAAPISQGLFGNTDYQGLVRLVALVQMGIAWGNLLLALMKGFRDAAGNALSLIVGSLIG
VLAYYVSYRLGGYEGALLGLALIPALVVIPAAIMLIKRGVIPLSYLKPSWDNGLAGQLSKFTLMALITSVTLPVAYIMMR
KLLAAQYSWDEVGIWQGVSSISDAYLQFITASFSVYLLPTLSRLTEKRDITREVVKSLKFVLPAVAAASFTVWLLRDFAI
WLLLSNKFTAMRDLFAWQLVGDVLKVGAYVFGYLVIAKASLRFYILAEVSQFTLLMVFAHWLIPAHGALGAAQAYMATYI
VYFSLCCGVFLLWRRRALEENLYFQ
;
A ? 
2 'polypeptide(L)' no no 
;MAQVQLVESGGGLVQAGGSLGLSCAASGRTFSNYVMAWFRQAPGKEREFVARISESRGTTDYADSVKGRFTISRDNAKNT
IYLQMNSLNPGDTAVYSCAATLPAWTGIIGGRRPGNYPYWGQGTQVTVSSHHHHHHEPEA
;
;MAQVQLVESGGGLVQAGGSLGLSCAASGRTFSNYVMAWFRQAPGKEREFVARISESRGTTDYADSVKGRFTISRDNAKNT
IYLQMNSLNPGDTAVYSCAATLPAWTGIIGGRRPGNYPYWGQGTQVTVSSHHHHHHEPEA
;
B ? 
3 'polypeptide(L)' no no 
;MAQVQLVESGGGLVQAGDSLTLSCAASGRTAYRYGMGWFRQHPGKEREFVASIWWTGTTTYYADSVKGRFTISRDDVKNM
VYLQMNSLKPEDTAVYYCAAKFYGGNSKRPGDYAYWGQGTQVTVSSHHHHHHEPEA
;
;MAQVQLVESGGGLVQAGDSLTLSCAASGRTAYRYGMGWFRQHPGKEREFVASIWWTGTTTYYADSVKGRFTISRDDVKNM
VYLQMNSLKPEDTAVYYCAAKFYGGNSKRPGDYAYWGQGTQVTVSSHHHHHHEPEA
;
C ? 
# 
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   VAL n 
1 3   SER n 
1 4   LEU n 
1 5   ALA n 
1 6   LYS n 
1 7   ALA n 
1 8   SER n 
1 9   LEU n 
1 10  TRP n 
1 11  THR n 
1 12  ALA n 
1 13  ALA n 
1 14  SER n 
1 15  THR n 
1 16  LEU n 
1 17  VAL n 
1 18  LYS n 
1 19  ILE n 
1 20  GLY n 
1 21  ALA n 
1 22  GLY n 
1 23  LEU n 
1 24  LEU n 
1 25  VAL n 
1 26  GLY n 
1 27  LYS n 
1 28  LEU n 
1 29  LEU n 
1 30  ALA n 
1 31  VAL n 
1 32  SER n 
1 33  PHE n 
1 34  GLY n 
1 35  PRO n 
1 36  ALA n 
1 37  GLY n 
1 38  LEU n 
1 39  GLY n 
1 40  LEU n 
1 41  ALA n 
1 42  ALA n 
1 43  ASN n 
1 44  PHE n 
1 45  ARG n 
1 46  GLN n 
1 47  LEU n 
1 48  ILE n 
1 49  THR n 
1 50  VAL n 
1 51  LEU n 
1 52  GLY n 
1 53  VAL n 
1 54  LEU n 
1 55  ALA n 
1 56  GLY n 
1 57  ALA n 
1 58  GLY n 
1 59  ILE n 
1 60  PHE n 
1 61  ASN n 
1 62  GLY n 
1 63  VAL n 
1 64  THR n 
1 65  LYS n 
1 66  TYR n 
1 67  VAL n 
1 68  ALA n 
1 69  GLN n 
1 70  TYR n 
1 71  HIS n 
1 72  ASP n 
1 73  ASN n 
1 74  PRO n 
1 75  GLN n 
1 76  GLN n 
1 77  LEU n 
1 78  ARG n 
1 79  ARG n 
1 80  VAL n 
1 81  VAL n 
1 82  GLY n 
1 83  THR n 
1 84  SER n 
1 85  SER n 
1 86  ALA n 
1 87  MET n 
1 88  VAL n 
1 89  LEU n 
1 90  GLY n 
1 91  PHE n 
1 92  SER n 
1 93  THR n 
1 94  LEU n 
1 95  MET n 
1 96  ALA n 
1 97  LEU n 
1 98  VAL n 
1 99  PHE n 
1 100 VAL n 
1 101 LEU n 
1 102 ALA n 
1 103 ALA n 
1 104 ALA n 
1 105 PRO n 
1 106 ILE n 
1 107 SER n 
1 108 GLN n 
1 109 GLY n 
1 110 LEU n 
1 111 PHE n 
1 112 GLY n 
1 113 ASN n 
1 114 THR n 
1 115 ASP n 
1 116 TYR n 
1 117 GLN n 
1 118 GLY n 
1 119 LEU n 
1 120 VAL n 
1 121 ARG n 
1 122 LEU n 
1 123 VAL n 
1 124 ALA n 
1 125 LEU n 
1 126 VAL n 
1 127 GLN n 
1 128 MET n 
1 129 GLY n 
1 130 ILE n 
1 131 ALA n 
1 132 TRP n 
1 133 GLY n 
1 134 ASN n 
1 135 LEU n 
1 136 LEU n 
1 137 LEU n 
1 138 ALA n 
1 139 LEU n 
1 140 MET n 
1 141 LYS n 
1 142 GLY n 
1 143 PHE n 
1 144 ARG n 
1 145 ASP n 
1 146 ALA n 
1 147 ALA n 
1 148 GLY n 
1 149 ASN n 
1 150 ALA n 
1 151 LEU n 
1 152 SER n 
1 153 LEU n 
1 154 ILE n 
1 155 VAL n 
1 156 GLY n 
1 157 SER n 
1 158 LEU n 
1 159 ILE n 
1 160 GLY n 
1 161 VAL n 
1 162 LEU n 
1 163 ALA n 
1 164 TYR n 
1 165 TYR n 
1 166 VAL n 
1 167 SER n 
1 168 TYR n 
1 169 ARG n 
1 170 LEU n 
1 171 GLY n 
1 172 GLY n 
1 173 TYR n 
1 174 GLU n 
1 175 GLY n 
1 176 ALA n 
1 177 LEU n 
1 178 LEU n 
1 179 GLY n 
1 180 LEU n 
1 181 ALA n 
1 182 LEU n 
1 183 ILE n 
1 184 PRO n 
1 185 ALA n 
1 186 LEU n 
1 187 VAL n 
1 188 VAL n 
1 189 ILE n 
1 190 PRO n 
1 191 ALA n 
1 192 ALA n 
1 193 ILE n 
1 194 MET n 
1 195 LEU n 
1 196 ILE n 
1 197 LYS n 
1 198 ARG n 
1 199 GLY n 
1 200 VAL n 
1 201 ILE n 
1 202 PRO n 
1 203 LEU n 
1 204 SER n 
1 205 TYR n 
1 206 LEU n 
1 207 LYS n 
1 208 PRO n 
1 209 SER n 
1 210 TRP n 
1 211 ASP n 
1 212 ASN n 
1 213 GLY n 
1 214 LEU n 
1 215 ALA n 
1 216 GLY n 
1 217 GLN n 
1 218 LEU n 
1 219 SER n 
1 220 LYS n 
1 221 PHE n 
1 222 THR n 
1 223 LEU n 
1 224 MET n 
1 225 ALA n 
1 226 LEU n 
1 227 ILE n 
1 228 THR n 
1 229 SER n 
1 230 VAL n 
1 231 THR n 
1 232 LEU n 
1 233 PRO n 
1 234 VAL n 
1 235 ALA n 
1 236 TYR n 
1 237 ILE n 
1 238 MET n 
1 239 MET n 
1 240 ARG n 
1 241 LYS n 
1 242 LEU n 
1 243 LEU n 
1 244 ALA n 
1 245 ALA n 
1 246 GLN n 
1 247 TYR n 
1 248 SER n 
1 249 TRP n 
1 250 ASP n 
1 251 GLU n 
1 252 VAL n 
1 253 GLY n 
1 254 ILE n 
1 255 TRP n 
1 256 GLN n 
1 257 GLY n 
1 258 VAL n 
1 259 SER n 
1 260 SER n 
1 261 ILE n 
1 262 SER n 
1 263 ASP n 
1 264 ALA n 
1 265 TYR n 
1 266 LEU n 
1 267 GLN n 
1 268 PHE n 
1 269 ILE n 
1 270 THR n 
1 271 ALA n 
1 272 SER n 
1 273 PHE n 
1 274 SER n 
1 275 VAL n 
1 276 TYR n 
1 277 LEU n 
1 278 LEU n 
1 279 PRO n 
1 280 THR n 
1 281 LEU n 
1 282 SER n 
1 283 ARG n 
1 284 LEU n 
1 285 THR n 
1 286 GLU n 
1 287 LYS n 
1 288 ARG n 
1 289 ASP n 
1 290 ILE n 
1 291 THR n 
1 292 ARG n 
1 293 GLU n 
1 294 VAL n 
1 295 VAL n 
1 296 LYS n 
1 297 SER n 
1 298 LEU n 
1 299 LYS n 
1 300 PHE n 
1 301 VAL n 
1 302 LEU n 
1 303 PRO n 
1 304 ALA n 
1 305 VAL n 
1 306 ALA n 
1 307 ALA n 
1 308 ALA n 
1 309 SER n 
1 310 PHE n 
1 311 THR n 
1 312 VAL n 
1 313 TRP n 
1 314 LEU n 
1 315 LEU n 
1 316 ARG n 
1 317 ASP n 
1 318 PHE n 
1 319 ALA n 
1 320 ILE n 
1 321 TRP n 
1 322 LEU n 
1 323 LEU n 
1 324 LEU n 
1 325 SER n 
1 326 ASN n 
1 327 LYS n 
1 328 PHE n 
1 329 THR n 
1 330 ALA n 
1 331 MET n 
1 332 ARG n 
1 333 ASP n 
1 334 LEU n 
1 335 PHE n 
1 336 ALA n 
1 337 TRP n 
1 338 GLN n 
1 339 LEU n 
1 340 VAL n 
1 341 GLY n 
1 342 ASP n 
1 343 VAL n 
1 344 LEU n 
1 345 LYS n 
1 346 VAL n 
1 347 GLY n 
1 348 ALA n 
1 349 TYR n 
1 350 VAL n 
1 351 PHE n 
1 352 GLY n 
1 353 TYR n 
1 354 LEU n 
1 355 VAL n 
1 356 ILE n 
1 357 ALA n 
1 358 LYS n 
1 359 ALA n 
1 360 SER n 
1 361 LEU n 
1 362 ARG n 
1 363 PHE n 
1 364 TYR n 
1 365 ILE n 
1 366 LEU n 
1 367 ALA n 
1 368 GLU n 
1 369 VAL n 
1 370 SER n 
1 371 GLN n 
1 372 PHE n 
1 373 THR n 
1 374 LEU n 
1 375 LEU n 
1 376 MET n 
1 377 VAL n 
1 378 PHE n 
1 379 ALA n 
1 380 HIS n 
1 381 TRP n 
1 382 LEU n 
1 383 ILE n 
1 384 PRO n 
1 385 ALA n 
1 386 HIS n 
1 387 GLY n 
1 388 ALA n 
1 389 LEU n 
1 390 GLY n 
1 391 ALA n 
1 392 ALA n 
1 393 GLN n 
1 394 ALA n 
1 395 TYR n 
1 396 MET n 
1 397 ALA n 
1 398 THR n 
1 399 TYR n 
1 400 ILE n 
1 401 VAL n 
1 402 TYR n 
1 403 PHE n 
1 404 SER n 
1 405 LEU n 
1 406 CYS n 
1 407 CYS n 
1 408 GLY n 
1 409 VAL n 
1 410 PHE n 
1 411 LEU n 
1 412 LEU n 
1 413 TRP n 
1 414 ARG n 
1 415 ARG n 
1 416 ARG n 
1 417 ALA n 
1 418 LEU n 
1 419 GLU n 
1 420 GLU n 
1 421 ASN n 
1 422 LEU n 
1 423 TYR n 
1 424 PHE n 
1 425 GLN n 
2 1   MET n 
2 2   ALA n 
2 3   GLN n 
2 4   VAL n 
2 5   GLN n 
2 6   LEU n 
2 7   VAL n 
2 8   GLU n 
2 9   SER n 
2 10  GLY n 
2 11  GLY n 
2 12  GLY n 
2 13  LEU n 
2 14  VAL n 
2 15  GLN n 
2 16  ALA n 
2 17  GLY n 
2 18  GLY n 
2 19  SER n 
2 20  LEU n 
2 21  GLY n 
2 22  LEU n 
2 23  SER n 
2 24  CYS n 
2 25  ALA n 
2 26  ALA n 
2 27  SER n 
2 28  GLY n 
2 29  ARG n 
2 30  THR n 
2 31  PHE n 
2 32  SER n 
2 33  ASN n 
2 34  TYR n 
2 35  VAL n 
2 36  MET n 
2 37  ALA n 
2 38  TRP n 
2 39  PHE n 
2 40  ARG n 
2 41  GLN n 
2 42  ALA n 
2 43  PRO n 
2 44  GLY n 
2 45  LYS n 
2 46  GLU n 
2 47  ARG n 
2 48  GLU n 
2 49  PHE n 
2 50  VAL n 
2 51  ALA n 
2 52  ARG n 
2 53  ILE n 
2 54  SER n 
2 55  GLU n 
2 56  SER n 
2 57  ARG n 
2 58  GLY n 
2 59  THR n 
2 60  THR n 
2 61  ASP n 
2 62  TYR n 
2 63  ALA n 
2 64  ASP n 
2 65  SER n 
2 66  VAL n 
2 67  LYS n 
2 68  GLY n 
2 69  ARG n 
2 70  PHE n 
2 71  THR n 
2 72  ILE n 
2 73  SER n 
2 74  ARG n 
2 75  ASP n 
2 76  ASN n 
2 77  ALA n 
2 78  LYS n 
2 79  ASN n 
2 80  THR n 
2 81  ILE n 
2 82  TYR n 
2 83  LEU n 
2 84  GLN n 
2 85  MET n 
2 86  ASN n 
2 87  SER n 
2 88  LEU n 
2 89  ASN n 
2 90  PRO n 
2 91  GLY n 
2 92  ASP n 
2 93  THR n 
2 94  ALA n 
2 95  VAL n 
2 96  TYR n 
2 97  SER n 
2 98  CYS n 
2 99  ALA n 
2 100 ALA n 
2 101 THR n 
2 102 LEU n 
2 103 PRO n 
2 104 ALA n 
2 105 TRP n 
2 106 THR n 
2 107 GLY n 
2 108 ILE n 
2 109 ILE n 
2 110 GLY n 
2 111 GLY n 
2 112 ARG n 
2 113 ARG n 
2 114 PRO n 
2 115 GLY n 
2 116 ASN n 
2 117 TYR n 
2 118 PRO n 
2 119 TYR n 
2 120 TRP n 
2 121 GLY n 
2 122 GLN n 
2 123 GLY n 
2 124 THR n 
2 125 GLN n 
2 126 VAL n 
2 127 THR n 
2 128 VAL n 
2 129 SER n 
2 130 SER n 
2 131 HIS n 
2 132 HIS n 
2 133 HIS n 
2 134 HIS n 
2 135 HIS n 
2 136 HIS n 
2 137 GLU n 
2 138 PRO n 
2 139 GLU n 
2 140 ALA n 
3 1   MET n 
3 2   ALA n 
3 3   GLN n 
3 4   VAL n 
3 5   GLN n 
3 6   LEU n 
3 7   VAL n 
3 8   GLU n 
3 9   SER n 
3 10  GLY n 
3 11  GLY n 
3 12  GLY n 
3 13  LEU n 
3 14  VAL n 
3 15  GLN n 
3 16  ALA n 
3 17  GLY n 
3 18  ASP n 
3 19  SER n 
3 20  LEU n 
3 21  THR n 
3 22  LEU n 
3 23  SER n 
3 24  CYS n 
3 25  ALA n 
3 26  ALA n 
3 27  SER n 
3 28  GLY n 
3 29  ARG n 
3 30  THR n 
3 31  ALA n 
3 32  TYR n 
3 33  ARG n 
3 34  TYR n 
3 35  GLY n 
3 36  MET n 
3 37  GLY n 
3 38  TRP n 
3 39  PHE n 
3 40  ARG n 
3 41  GLN n 
3 42  HIS n 
3 43  PRO n 
3 44  GLY n 
3 45  LYS n 
3 46  GLU n 
3 47  ARG n 
3 48  GLU n 
3 49  PHE n 
3 50  VAL n 
3 51  ALA n 
3 52  SER n 
3 53  ILE n 
3 54  TRP n 
3 55  TRP n 
3 56  THR n 
3 57  GLY n 
3 58  THR n 
3 59  THR n 
3 60  THR n 
3 61  TYR n 
3 62  TYR n 
3 63  ALA n 
3 64  ASP n 
3 65  SER n 
3 66  VAL n 
3 67  LYS n 
3 68  GLY n 
3 69  ARG n 
3 70  PHE n 
3 71  THR n 
3 72  ILE n 
3 73  SER n 
3 74  ARG n 
3 75  ASP n 
3 76  ASP n 
3 77  VAL n 
3 78  LYS n 
3 79  ASN n 
3 80  MET n 
3 81  VAL n 
3 82  TYR n 
3 83  LEU n 
3 84  GLN n 
3 85  MET n 
3 86  ASN n 
3 87  SER n 
3 88  LEU n 
3 89  LYS n 
3 90  PRO n 
3 91  GLU n 
3 92  ASP n 
3 93  THR n 
3 94  ALA n 
3 95  VAL n 
3 96  TYR n 
3 97  TYR n 
3 98  CYS n 
3 99  ALA n 
3 100 ALA n 
3 101 LYS n 
3 102 PHE n 
3 103 TYR n 
3 104 GLY n 
3 105 GLY n 
3 106 ASN n 
3 107 SER n 
3 108 LYS n 
3 109 ARG n 
3 110 PRO n 
3 111 GLY n 
3 112 ASP n 
3 113 TYR n 
3 114 ALA n 
3 115 TYR n 
3 116 TRP n 
3 117 GLY n 
3 118 GLN n 
3 119 GLY n 
3 120 THR n 
3 121 GLN n 
3 122 VAL n 
3 123 THR n 
3 124 VAL n 
3 125 SER n 
3 126 SER n 
3 127 HIS n 
3 128 HIS n 
3 129 HIS n 
3 130 HIS n 
3 131 HIS n 
3 132 HIS n 
3 133 GLU n 
3 134 PRO n 
3 135 GLU n 
3 136 ALA 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' 1 425 ? ? 'wzxE, wzx, yifJ, b3792, JW3766' ? ? ? ? ? ? 'Escherichia coli' 562  ? ? ? ? ? ? ? ? 
'Escherichia coli BL21(DE3)' 469008 ? ? ? ? ? ? ?         C43 ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 140 ? ? ?                                ? ? ? ? ? ? 'Lama glama'       9844 ? ? ? ? ? ? ? ? 
'Escherichia coli'           562    ? ? ? ? ? ? 'wk6 su-' ?   ? ? ? ? ? ? ? ? ? ? ? ? ? 
3 1 sample 'Biological sequence' 1 136 ? ? ?                                ? ? ? ? ? ? 'Lama glama'       9844 ? ? ? ? ? ? ? ? 
'Escherichia coli'           562    ? ? ? ? ? ? 'wk6 su-' ?   ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
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 
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   0   ?   ?   ?   A . n 
A 1 2   VAL 2   1   ?   ?   ?   A . n 
A 1 3   SER 3   2   ?   ?   ?   A . n 
A 1 4   LEU 4   3   ?   ?   ?   A . n 
A 1 5   ALA 5   4   ?   ?   ?   A . n 
A 1 6   LYS 6   5   ?   ?   ?   A . n 
A 1 7   ALA 7   6   6   ALA ALA A . n 
A 1 8   SER 8   7   7   SER SER A . n 
A 1 9   LEU 9   8   8   LEU LEU A . n 
A 1 10  TRP 10  9   9   TRP TRP A . n 
A 1 11  THR 11  10  10  THR THR A . n 
A 1 12  ALA 12  11  11  ALA ALA A . n 
A 1 13  ALA 13  12  12  ALA ALA A . n 
A 1 14  SER 14  13  13  SER SER A . n 
A 1 15  THR 15  14  14  THR THR A . n 
A 1 16  LEU 16  15  15  LEU LEU A . n 
A 1 17  VAL 17  16  16  VAL VAL A . n 
A 1 18  LYS 18  17  17  LYS LYS A . n 
A 1 19  ILE 19  18  18  ILE ILE A . n 
A 1 20  GLY 20  19  19  GLY GLY A . n 
A 1 21  ALA 21  20  20  ALA ALA A . n 
A 1 22  GLY 22  21  21  GLY GLY A . n 
A 1 23  LEU 23  22  22  LEU LEU A . n 
A 1 24  LEU 24  23  23  LEU LEU A . n 
A 1 25  VAL 25  24  24  VAL VAL A . n 
A 1 26  GLY 26  25  25  GLY GLY A . n 
A 1 27  LYS 27  26  26  LYS LYS A . n 
A 1 28  LEU 28  27  27  LEU LEU A . n 
A 1 29  LEU 29  28  28  LEU LEU A . n 
A 1 30  ALA 30  29  29  ALA ALA A . n 
A 1 31  VAL 31  30  30  VAL VAL A . n 
A 1 32  SER 32  31  31  SER SER A . n 
A 1 33  PHE 33  32  32  PHE PHE A . n 
A 1 34  GLY 34  33  33  GLY GLY A . n 
A 1 35  PRO 35  34  34  PRO PRO A . n 
A 1 36  ALA 36  35  35  ALA ALA A . n 
A 1 37  GLY 37  36  36  GLY GLY A . n 
A 1 38  LEU 38  37  37  LEU LEU A . n 
A 1 39  GLY 39  38  38  GLY GLY A . n 
A 1 40  LEU 40  39  39  LEU LEU A . n 
A 1 41  ALA 41  40  40  ALA ALA A . n 
A 1 42  ALA 42  41  41  ALA ALA A . n 
A 1 43  ASN 43  42  42  ASN ASN A . n 
A 1 44  PHE 44  43  43  PHE PHE A . n 
A 1 45  ARG 45  44  44  ARG ARG A . n 
A 1 46  GLN 46  45  45  GLN GLN A . n 
A 1 47  LEU 47  46  46  LEU LEU A . n 
A 1 48  ILE 48  47  47  ILE ILE A . n 
A 1 49  THR 49  48  48  THR THR A . n 
A 1 50  VAL 50  49  49  VAL VAL A . n 
A 1 51  LEU 51  50  50  LEU LEU A . n 
A 1 52  GLY 52  51  51  GLY GLY A . n 
A 1 53  VAL 53  52  52  VAL VAL A . n 
A 1 54  LEU 54  53  53  LEU LEU A . n 
A 1 55  ALA 55  54  54  ALA ALA A . n 
A 1 56  GLY 56  55  55  GLY GLY A . n 
A 1 57  ALA 57  56  56  ALA ALA A . n 
A 1 58  GLY 58  57  57  GLY GLY A . n 
A 1 59  ILE 59  58  58  ILE ILE A . n 
A 1 60  PHE 60  59  59  PHE PHE A . n 
A 1 61  ASN 61  60  60  ASN ASN A . n 
A 1 62  GLY 62  61  61  GLY GLY A . n 
A 1 63  VAL 63  62  62  VAL VAL A . n 
A 1 64  THR 64  63  63  THR THR A . n 
A 1 65  LYS 65  64  64  LYS LYS A . n 
A 1 66  TYR 66  65  65  TYR TYR A . n 
A 1 67  VAL 67  66  66  VAL VAL A . n 
A 1 68  ALA 68  67  67  ALA ALA A . n 
A 1 69  GLN 69  68  68  GLN GLN A . n 
A 1 70  TYR 70  69  69  TYR TYR A . n 
A 1 71  HIS 71  70  70  HIS HIS A . n 
A 1 72  ASP 72  71  71  ASP ASP A . n 
A 1 73  ASN 73  72  72  ASN ASN A . n 
A 1 74  PRO 74  73  73  PRO PRO A . n 
A 1 75  GLN 75  74  74  GLN GLN A . n 
A 1 76  GLN 76  75  75  GLN GLN A . n 
A 1 77  LEU 77  76  76  LEU LEU A . n 
A 1 78  ARG 78  77  77  ARG ARG A . n 
A 1 79  ARG 79  78  78  ARG ARG A . n 
A 1 80  VAL 80  79  79  VAL VAL A . n 
A 1 81  VAL 81  80  80  VAL VAL A . n 
A 1 82  GLY 82  81  81  GLY GLY A . n 
A 1 83  THR 83  82  82  THR THR A . n 
A 1 84  SER 84  83  83  SER SER A . n 
A 1 85  SER 85  84  84  SER SER A . n 
A 1 86  ALA 86  85  85  ALA ALA A . n 
A 1 87  MET 87  86  86  MET MET A . n 
A 1 88  VAL 88  87  87  VAL VAL A . n 
A 1 89  LEU 89  88  88  LEU LEU A . n 
A 1 90  GLY 90  89  89  GLY GLY A . n 
A 1 91  PHE 91  90  90  PHE PHE A . n 
A 1 92  SER 92  91  91  SER SER A . n 
A 1 93  THR 93  92  92  THR THR A . n 
A 1 94  LEU 94  93  93  LEU LEU A . n 
A 1 95  MET 95  94  94  MET MET A . n 
A 1 96  ALA 96  95  95  ALA ALA A . n 
A 1 97  LEU 97  96  96  LEU LEU A . n 
A 1 98  VAL 98  97  97  VAL VAL A . n 
A 1 99  PHE 99  98  98  PHE PHE A . n 
A 1 100 VAL 100 99  99  VAL VAL A . n 
A 1 101 LEU 101 100 100 LEU LEU A . n 
A 1 102 ALA 102 101 101 ALA ALA A . n 
A 1 103 ALA 103 102 102 ALA ALA A . n 
A 1 104 ALA 104 103 103 ALA ALA A . n 
A 1 105 PRO 105 104 104 PRO PRO A . n 
A 1 106 ILE 106 105 105 ILE ILE A . n 
A 1 107 SER 107 106 106 SER SER A . n 
A 1 108 GLN 108 107 107 GLN GLN A . n 
A 1 109 GLY 109 108 108 GLY GLY A . n 
A 1 110 LEU 110 109 109 LEU LEU A . n 
A 1 111 PHE 111 110 110 PHE PHE A . n 
A 1 112 GLY 112 111 111 GLY GLY A . n 
A 1 113 ASN 113 112 112 ASN ASN A . n 
A 1 114 THR 114 113 113 THR THR A . n 
A 1 115 ASP 115 114 114 ASP ASP A . n 
A 1 116 TYR 116 115 115 TYR TYR A . n 
A 1 117 GLN 117 116 116 GLN GLN A . n 
A 1 118 GLY 118 117 117 GLY GLY A . n 
A 1 119 LEU 119 118 118 LEU LEU A . n 
A 1 120 VAL 120 119 119 VAL VAL A . n 
A 1 121 ARG 121 120 120 ARG ARG A . n 
A 1 122 LEU 122 121 121 LEU LEU A . n 
A 1 123 VAL 123 122 122 VAL VAL A . n 
A 1 124 ALA 124 123 123 ALA ALA A . n 
A 1 125 LEU 125 124 124 LEU LEU A . n 
A 1 126 VAL 126 125 125 VAL VAL A . n 
A 1 127 GLN 127 126 126 GLN GLN A . n 
A 1 128 MET 128 127 127 MET MET A . n 
A 1 129 GLY 129 128 128 GLY GLY A . n 
A 1 130 ILE 130 129 129 ILE ILE A . n 
A 1 131 ALA 131 130 130 ALA ALA A . n 
A 1 132 TRP 132 131 131 TRP TRP A . n 
A 1 133 GLY 133 132 132 GLY GLY A . n 
A 1 134 ASN 134 133 133 ASN ASN A . n 
A 1 135 LEU 135 134 134 LEU LEU A . n 
A 1 136 LEU 136 135 135 LEU LEU A . n 
A 1 137 LEU 137 136 136 LEU LEU A . n 
A 1 138 ALA 138 137 137 ALA ALA A . n 
A 1 139 LEU 139 138 138 LEU LEU A . n 
A 1 140 MET 140 139 139 MET MET A . n 
A 1 141 LYS 141 140 140 LYS LYS A . n 
A 1 142 GLY 142 141 141 GLY GLY A . n 
A 1 143 PHE 143 142 142 PHE PHE A . n 
A 1 144 ARG 144 143 143 ARG ARG A . n 
A 1 145 ASP 145 144 144 ASP ASP A . n 
A 1 146 ALA 146 145 145 ALA ALA A . n 
A 1 147 ALA 147 146 146 ALA ALA A . n 
A 1 148 GLY 148 147 147 GLY GLY A . n 
A 1 149 ASN 149 148 148 ASN ASN A . n 
A 1 150 ALA 150 149 149 ALA ALA A . n 
A 1 151 LEU 151 150 150 LEU LEU A . n 
A 1 152 SER 152 151 151 SER SER A . n 
A 1 153 LEU 153 152 152 LEU LEU A . n 
A 1 154 ILE 154 153 153 ILE ILE A . n 
A 1 155 VAL 155 154 154 VAL VAL A . n 
A 1 156 GLY 156 155 155 GLY GLY A . n 
A 1 157 SER 157 156 156 SER SER A . n 
A 1 158 LEU 158 157 157 LEU LEU A . n 
A 1 159 ILE 159 158 158 ILE ILE A . n 
A 1 160 GLY 160 159 159 GLY GLY A . n 
A 1 161 VAL 161 160 160 VAL VAL A . n 
A 1 162 LEU 162 161 161 LEU LEU A . n 
A 1 163 ALA 163 162 162 ALA ALA A . n 
A 1 164 TYR 164 163 163 TYR TYR A . n 
A 1 165 TYR 165 164 164 TYR TYR A . n 
A 1 166 VAL 166 165 165 VAL VAL A . n 
A 1 167 SER 167 166 166 SER SER A . n 
A 1 168 TYR 168 167 167 TYR TYR A . n 
A 1 169 ARG 169 168 168 ARG ARG A . n 
A 1 170 LEU 170 169 169 LEU LEU A . n 
A 1 171 GLY 171 170 170 GLY GLY A . n 
A 1 172 GLY 172 171 171 GLY GLY A . n 
A 1 173 TYR 173 172 172 TYR TYR A . n 
A 1 174 GLU 174 173 173 GLU GLU A . n 
A 1 175 GLY 175 174 174 GLY GLY A . n 
A 1 176 ALA 176 175 175 ALA ALA A . n 
A 1 177 LEU 177 176 176 LEU LEU A . n 
A 1 178 LEU 178 177 177 LEU LEU A . n 
A 1 179 GLY 179 178 178 GLY GLY A . n 
A 1 180 LEU 180 179 179 LEU LEU A . n 
A 1 181 ALA 181 180 180 ALA ALA A . n 
A 1 182 LEU 182 181 181 LEU LEU A . n 
A 1 183 ILE 183 182 182 ILE ILE A . n 
A 1 184 PRO 184 183 183 PRO PRO A . n 
A 1 185 ALA 185 184 184 ALA ALA A . n 
A 1 186 LEU 186 185 185 LEU LEU A . n 
A 1 187 VAL 187 186 186 VAL VAL A . n 
A 1 188 VAL 188 187 187 VAL VAL A . n 
A 1 189 ILE 189 188 188 ILE ILE A . n 
A 1 190 PRO 190 189 189 PRO PRO A . n 
A 1 191 ALA 191 190 190 ALA ALA A . n 
A 1 192 ALA 192 191 191 ALA ALA A . n 
A 1 193 ILE 193 192 192 ILE ILE A . n 
A 1 194 MET 194 193 193 MET MET A . n 
A 1 195 LEU 195 194 194 LEU LEU A . n 
A 1 196 ILE 196 195 195 ILE ILE A . n 
A 1 197 LYS 197 196 196 LYS LYS A . n 
A 1 198 ARG 198 197 197 ARG ARG A . n 
A 1 199 GLY 199 198 198 GLY GLY A . n 
A 1 200 VAL 200 199 199 VAL VAL A . n 
A 1 201 ILE 201 200 200 ILE ILE A . n 
A 1 202 PRO 202 201 201 PRO PRO A . n 
A 1 203 LEU 203 202 202 LEU LEU A . n 
A 1 204 SER 204 203 203 SER SER A . n 
A 1 205 TYR 205 204 204 TYR TYR A . n 
A 1 206 LEU 206 205 205 LEU LEU A . n 
A 1 207 LYS 207 206 206 LYS LYS A . n 
A 1 208 PRO 208 207 207 PRO PRO A . n 
A 1 209 SER 209 208 208 SER SER A . n 
A 1 210 TRP 210 209 209 TRP TRP A . n 
A 1 211 ASP 211 210 210 ASP ASP A . n 
A 1 212 ASN 212 211 211 ASN ASN A . n 
A 1 213 GLY 213 212 212 GLY GLY A . n 
A 1 214 LEU 214 213 213 LEU LEU A . n 
A 1 215 ALA 215 214 214 ALA ALA A . n 
A 1 216 GLY 216 215 215 GLY GLY A . n 
A 1 217 GLN 217 216 216 GLN GLN A . n 
A 1 218 LEU 218 217 217 LEU LEU A . n 
A 1 219 SER 219 218 218 SER SER A . n 
A 1 220 LYS 220 219 219 LYS LYS A . n 
A 1 221 PHE 221 220 220 PHE PHE A . n 
A 1 222 THR 222 221 221 THR THR A . n 
A 1 223 LEU 223 222 222 LEU LEU A . n 
A 1 224 MET 224 223 223 MET MET A . n 
A 1 225 ALA 225 224 224 ALA ALA A . n 
A 1 226 LEU 226 225 225 LEU LEU A . n 
A 1 227 ILE 227 226 226 ILE ILE A . n 
A 1 228 THR 228 227 227 THR THR A . n 
A 1 229 SER 229 228 228 SER SER A . n 
A 1 230 VAL 230 229 229 VAL VAL A . n 
A 1 231 THR 231 230 230 THR THR A . n 
A 1 232 LEU 232 231 231 LEU LEU A . n 
A 1 233 PRO 233 232 232 PRO PRO A . n 
A 1 234 VAL 234 233 233 VAL VAL A . n 
A 1 235 ALA 235 234 234 ALA ALA A . n 
A 1 236 TYR 236 235 235 TYR TYR A . n 
A 1 237 ILE 237 236 236 ILE ILE A . n 
A 1 238 MET 238 237 237 MET MET A . n 
A 1 239 MET 239 238 238 MET MET A . n 
A 1 240 ARG 240 239 239 ARG ARG A . n 
A 1 241 LYS 241 240 240 LYS LYS A . n 
A 1 242 LEU 242 241 241 LEU LEU A . n 
A 1 243 LEU 243 242 242 LEU LEU A . n 
A 1 244 ALA 244 243 243 ALA ALA A . n 
A 1 245 ALA 245 244 244 ALA ALA A . n 
A 1 246 GLN 246 245 245 GLN GLN A . n 
A 1 247 TYR 247 246 246 TYR TYR A . n 
A 1 248 SER 248 247 247 SER SER A . n 
A 1 249 TRP 249 248 248 TRP TRP A . n 
A 1 250 ASP 250 249 249 ASP ASP A . n 
A 1 251 GLU 251 250 250 GLU GLU A . n 
A 1 252 VAL 252 251 251 VAL VAL A . n 
A 1 253 GLY 253 252 252 GLY GLY A . n 
A 1 254 ILE 254 253 253 ILE ILE A . n 
A 1 255 TRP 255 254 254 TRP TRP A . n 
A 1 256 GLN 256 255 255 GLN GLN A . n 
A 1 257 GLY 257 256 256 GLY GLY A . n 
A 1 258 VAL 258 257 257 VAL VAL A . n 
A 1 259 SER 259 258 258 SER SER A . n 
A 1 260 SER 260 259 259 SER SER A . n 
A 1 261 ILE 261 260 260 ILE ILE A . n 
A 1 262 SER 262 261 261 SER SER A . n 
A 1 263 ASP 263 262 262 ASP ASP A . n 
A 1 264 ALA 264 263 263 ALA ALA A . n 
A 1 265 TYR 265 264 264 TYR TYR A . n 
A 1 266 LEU 266 265 265 LEU LEU A . n 
A 1 267 GLN 267 266 266 GLN GLN A . n 
A 1 268 PHE 268 267 267 PHE PHE A . n 
A 1 269 ILE 269 268 268 ILE ILE A . n 
A 1 270 THR 270 269 269 THR THR A . n 
A 1 271 ALA 271 270 270 ALA ALA A . n 
A 1 272 SER 272 271 271 SER SER A . n 
A 1 273 PHE 273 272 272 PHE PHE A . n 
A 1 274 SER 274 273 273 SER SER A . n 
A 1 275 VAL 275 274 274 VAL VAL A . n 
A 1 276 TYR 276 275 275 TYR TYR A . n 
A 1 277 LEU 277 276 276 LEU LEU A . n 
A 1 278 LEU 278 277 277 LEU LEU A . n 
A 1 279 PRO 279 278 278 PRO PRO A . n 
A 1 280 THR 280 279 279 THR THR A . n 
A 1 281 LEU 281 280 280 LEU LEU A . n 
A 1 282 SER 282 281 281 SER SER A . n 
A 1 283 ARG 283 282 282 ARG ARG A . n 
A 1 284 LEU 284 283 283 LEU LEU A . n 
A 1 285 THR 285 284 284 THR THR A . n 
A 1 286 GLU 286 285 285 GLU GLU A . n 
A 1 287 LYS 287 286 286 LYS LYS A . n 
A 1 288 ARG 288 287 287 ARG ARG A . n 
A 1 289 ASP 289 288 288 ASP ASP A . n 
A 1 290 ILE 290 289 289 ILE ILE A . n 
A 1 291 THR 291 290 290 THR THR A . n 
A 1 292 ARG 292 291 291 ARG ARG A . n 
A 1 293 GLU 293 292 292 GLU GLU A . n 
A 1 294 VAL 294 293 293 VAL VAL A . n 
A 1 295 VAL 295 294 294 VAL VAL A . n 
A 1 296 LYS 296 295 295 LYS LYS A . n 
A 1 297 SER 297 296 296 SER SER A . n 
A 1 298 LEU 298 297 297 LEU LEU A . n 
A 1 299 LYS 299 298 298 LYS LYS A . n 
A 1 300 PHE 300 299 299 PHE PHE A . n 
A 1 301 VAL 301 300 300 VAL VAL A . n 
A 1 302 LEU 302 301 301 LEU LEU A . n 
A 1 303 PRO 303 302 302 PRO PRO A . n 
A 1 304 ALA 304 303 303 ALA ALA A . n 
A 1 305 VAL 305 304 304 VAL VAL A . n 
A 1 306 ALA 306 305 305 ALA ALA A . n 
A 1 307 ALA 307 306 306 ALA ALA A . n 
A 1 308 ALA 308 307 307 ALA ALA A . n 
A 1 309 SER 309 308 308 SER SER A . n 
A 1 310 PHE 310 309 309 PHE PHE A . n 
A 1 311 THR 311 310 310 THR THR A . n 
A 1 312 VAL 312 311 311 VAL VAL A . n 
A 1 313 TRP 313 312 312 TRP TRP A . n 
A 1 314 LEU 314 313 313 LEU LEU A . n 
A 1 315 LEU 315 314 314 LEU LEU A . n 
A 1 316 ARG 316 315 315 ARG ARG A . n 
A 1 317 ASP 317 316 316 ASP ASP A . n 
A 1 318 PHE 318 317 317 PHE PHE A . n 
A 1 319 ALA 319 318 318 ALA ALA A . n 
A 1 320 ILE 320 319 319 ILE ILE A . n 
A 1 321 TRP 321 320 320 TRP TRP A . n 
A 1 322 LEU 322 321 321 LEU LEU A . n 
A 1 323 LEU 323 322 322 LEU LEU A . n 
A 1 324 LEU 324 323 323 LEU LEU A . n 
A 1 325 SER 325 324 324 SER SER A . n 
A 1 326 ASN 326 325 325 ASN ASN A . n 
A 1 327 LYS 327 326 326 LYS LYS A . n 
A 1 328 PHE 328 327 327 PHE PHE A . n 
A 1 329 THR 329 328 328 THR THR A . n 
A 1 330 ALA 330 329 329 ALA ALA A . n 
A 1 331 MET 331 330 330 MET MET A . n 
A 1 332 ARG 332 331 331 ARG ARG A . n 
A 1 333 ASP 333 332 332 ASP ASP A . n 
A 1 334 LEU 334 333 333 LEU LEU A . n 
A 1 335 PHE 335 334 334 PHE PHE A . n 
A 1 336 ALA 336 335 335 ALA ALA A . n 
A 1 337 TRP 337 336 336 TRP TRP A . n 
A 1 338 GLN 338 337 337 GLN GLN A . n 
A 1 339 LEU 339 338 338 LEU LEU A . n 
A 1 340 VAL 340 339 339 VAL VAL A . n 
A 1 341 GLY 341 340 340 GLY GLY A . n 
A 1 342 ASP 342 341 341 ASP ASP A . n 
A 1 343 VAL 343 342 342 VAL VAL A . n 
A 1 344 LEU 344 343 343 LEU LEU A . n 
A 1 345 LYS 345 344 344 LYS LYS A . n 
A 1 346 VAL 346 345 345 VAL VAL A . n 
A 1 347 GLY 347 346 346 GLY GLY A . n 
A 1 348 ALA 348 347 347 ALA ALA A . n 
A 1 349 TYR 349 348 348 TYR TYR A . n 
A 1 350 VAL 350 349 349 VAL VAL A . n 
A 1 351 PHE 351 350 350 PHE PHE A . n 
A 1 352 GLY 352 351 351 GLY GLY A . n 
A 1 353 TYR 353 352 352 TYR TYR A . n 
A 1 354 LEU 354 353 353 LEU LEU A . n 
A 1 355 VAL 355 354 354 VAL VAL A . n 
A 1 356 ILE 356 355 355 ILE ILE A . n 
A 1 357 ALA 357 356 356 ALA ALA A . n 
A 1 358 LYS 358 357 357 LYS LYS A . n 
A 1 359 ALA 359 358 358 ALA ALA A . n 
A 1 360 SER 360 359 359 SER SER A . n 
A 1 361 LEU 361 360 360 LEU LEU A . n 
A 1 362 ARG 362 361 361 ARG ARG A . n 
A 1 363 PHE 363 362 362 PHE PHE A . n 
A 1 364 TYR 364 363 363 TYR TYR A . n 
A 1 365 ILE 365 364 364 ILE ILE A . n 
A 1 366 LEU 366 365 365 LEU LEU A . n 
A 1 367 ALA 367 366 366 ALA ALA A . n 
A 1 368 GLU 368 367 367 GLU GLU A . n 
A 1 369 VAL 369 368 368 VAL VAL A . n 
A 1 370 SER 370 369 369 SER SER A . n 
A 1 371 GLN 371 370 370 GLN GLN A . n 
A 1 372 PHE 372 371 371 PHE PHE A . n 
A 1 373 THR 373 372 372 THR THR A . n 
A 1 374 LEU 374 373 373 LEU LEU A . n 
A 1 375 LEU 375 374 374 LEU LEU A . n 
A 1 376 MET 376 375 375 MET MET A . n 
A 1 377 VAL 377 376 376 VAL VAL A . n 
A 1 378 PHE 378 377 377 PHE PHE A . n 
A 1 379 ALA 379 378 378 ALA ALA A . n 
A 1 380 HIS 380 379 379 HIS HIS A . n 
A 1 381 TRP 381 380 380 TRP TRP A . n 
A 1 382 LEU 382 381 381 LEU LEU A . n 
A 1 383 ILE 383 382 382 ILE ILE A . n 
A 1 384 PRO 384 383 383 PRO PRO A . n 
A 1 385 ALA 385 384 384 ALA ALA A . n 
A 1 386 HIS 386 385 385 HIS HIS A . n 
A 1 387 GLY 387 386 386 GLY GLY A . n 
A 1 388 ALA 388 387 387 ALA ALA A . n 
A 1 389 LEU 389 388 388 LEU LEU A . n 
A 1 390 GLY 390 389 389 GLY GLY A . n 
A 1 391 ALA 391 390 390 ALA ALA A . n 
A 1 392 ALA 392 391 391 ALA ALA A . n 
A 1 393 GLN 393 392 392 GLN GLN A . n 
A 1 394 ALA 394 393 393 ALA ALA A . n 
A 1 395 TYR 395 394 394 TYR TYR A . n 
A 1 396 MET 396 395 395 MET MET A . n 
A 1 397 ALA 397 396 396 ALA ALA A . n 
A 1 398 THR 398 397 397 THR THR A . n 
A 1 399 TYR 399 398 398 TYR TYR A . n 
A 1 400 ILE 400 399 399 ILE ILE A . n 
A 1 401 VAL 401 400 400 VAL VAL A . n 
A 1 402 TYR 402 401 401 TYR TYR A . n 
A 1 403 PHE 403 402 402 PHE PHE A . n 
A 1 404 SER 404 403 403 SER SER A . n 
A 1 405 LEU 405 404 404 LEU LEU A . n 
A 1 406 CYS 406 405 405 CYS CYS A . n 
A 1 407 CYS 407 406 406 CYS CYS A . n 
A 1 408 GLY 408 407 407 GLY GLY A . n 
A 1 409 VAL 409 408 408 VAL VAL A . n 
A 1 410 PHE 410 409 409 PHE PHE A . n 
A 1 411 LEU 411 410 410 LEU LEU A . n 
A 1 412 LEU 412 411 411 LEU LEU A . n 
A 1 413 TRP 413 412 412 TRP TRP A . n 
A 1 414 ARG 414 413 413 ARG ARG A . n 
A 1 415 ARG 415 414 414 ARG ARG A . n 
A 1 416 ARG 416 415 415 ARG ARG A . n 
A 1 417 ALA 417 416 416 ALA ALA A . n 
A 1 418 LEU 418 417 ?   ?   ?   A . n 
A 1 419 GLU 419 418 ?   ?   ?   A . n 
A 1 420 GLU 420 419 ?   ?   ?   A . n 
A 1 421 ASN 421 420 ?   ?   ?   A . n 
A 1 422 LEU 422 421 ?   ?   ?   A . n 
A 1 423 TYR 423 422 ?   ?   ?   A . n 
A 1 424 PHE 424 423 ?   ?   ?   A . n 
A 1 425 GLN 425 424 ?   ?   ?   A . n 
B 2 1   MET 1   -1  ?   ?   ?   B . n 
B 2 2   ALA 2   0   0   ALA ALA B . n 
B 2 3   GLN 3   1   1   GLN GLN B . n 
B 2 4   VAL 4   2   2   VAL VAL B . n 
B 2 5   GLN 5   3   3   GLN GLN B . n 
B 2 6   LEU 6   4   4   LEU LEU B . n 
B 2 7   VAL 7   5   5   VAL VAL B . n 
B 2 8   GLU 8   6   6   GLU GLU B . n 
B 2 9   SER 9   7   7   SER SER B . n 
B 2 10  GLY 10  8   8   GLY GLY B . n 
B 2 11  GLY 11  9   9   GLY GLY B . n 
B 2 12  GLY 12  10  10  GLY GLY B . n 
B 2 13  LEU 13  11  11  LEU LEU B . n 
B 2 14  VAL 14  12  12  VAL VAL B . n 
B 2 15  GLN 15  13  13  GLN GLN B . n 
B 2 16  ALA 16  14  14  ALA ALA B . n 
B 2 17  GLY 17  15  15  GLY GLY B . n 
B 2 18  GLY 18  16  16  GLY GLY B . n 
B 2 19  SER 19  17  17  SER SER B . n 
B 2 20  LEU 20  18  18  LEU LEU B . n 
B 2 21  GLY 21  19  19  GLY GLY B . n 
B 2 22  LEU 22  20  20  LEU LEU B . n 
B 2 23  SER 23  21  21  SER SER B . n 
B 2 24  CYS 24  22  22  CYS CYS B . n 
B 2 25  ALA 25  23  23  ALA ALA B . n 
B 2 26  ALA 26  24  24  ALA ALA B . n 
B 2 27  SER 27  25  25  SER SER B . n 
B 2 28  GLY 28  26  26  GLY GLY B . n 
B 2 29  ARG 29  27  27  ARG ARG B . n 
B 2 30  THR 30  28  28  THR THR B . n 
B 2 31  PHE 31  29  29  PHE PHE B . n 
B 2 32  SER 32  30  30  SER SER B . n 
B 2 33  ASN 33  31  31  ASN ASN B . n 
B 2 34  TYR 34  32  32  TYR TYR B . n 
B 2 35  VAL 35  33  33  VAL VAL B . n 
B 2 36  MET 36  34  34  MET MET B . n 
B 2 37  ALA 37  35  35  ALA ALA B . n 
B 2 38  TRP 38  36  36  TRP TRP B . n 
B 2 39  PHE 39  37  37  PHE PHE B . n 
B 2 40  ARG 40  38  38  ARG ARG B . n 
B 2 41  GLN 41  39  39  GLN GLN B . n 
B 2 42  ALA 42  40  40  ALA ALA B . n 
B 2 43  PRO 43  41  41  PRO PRO B . n 
B 2 44  GLY 44  42  42  GLY GLY B . n 
B 2 45  LYS 45  43  43  LYS LYS B . n 
B 2 46  GLU 46  44  44  GLU GLU B . n 
B 2 47  ARG 47  45  45  ARG ARG B . n 
B 2 48  GLU 48  46  46  GLU GLU B . n 
B 2 49  PHE 49  47  47  PHE PHE B . n 
B 2 50  VAL 50  48  48  VAL VAL B . n 
B 2 51  ALA 51  49  49  ALA ALA B . n 
B 2 52  ARG 52  50  50  ARG ARG B . n 
B 2 53  ILE 53  51  51  ILE ILE B . n 
B 2 54  SER 54  52  52  SER SER B . n 
B 2 55  GLU 55  53  53  GLU GLU B . n 
B 2 56  SER 56  54  54  SER SER B . n 
B 2 57  ARG 57  55  55  ARG ARG B . n 
B 2 58  GLY 58  56  56  GLY GLY B . n 
B 2 59  THR 59  57  57  THR THR B . n 
B 2 60  THR 60  58  58  THR THR B . n 
B 2 61  ASP 61  59  59  ASP ASP B . n 
B 2 62  TYR 62  60  60  TYR TYR B . n 
B 2 63  ALA 63  61  61  ALA ALA B . n 
B 2 64  ASP 64  62  62  ASP ASP B . n 
B 2 65  SER 65  63  63  SER SER B . n 
B 2 66  VAL 66  64  64  VAL VAL B . n 
B 2 67  LYS 67  65  65  LYS LYS B . n 
B 2 68  GLY 68  66  66  GLY GLY B . n 
B 2 69  ARG 69  67  67  ARG ARG B . n 
B 2 70  PHE 70  68  68  PHE PHE B . n 
B 2 71  THR 71  69  69  THR THR B . n 
B 2 72  ILE 72  70  70  ILE ILE B . n 
B 2 73  SER 73  71  71  SER SER B . n 
B 2 74  ARG 74  72  72  ARG ARG B . n 
B 2 75  ASP 75  73  73  ASP ASP B . n 
B 2 76  ASN 76  74  74  ASN ASN B . n 
B 2 77  ALA 77  75  75  ALA ALA B . n 
B 2 78  LYS 78  76  76  LYS LYS B . n 
B 2 79  ASN 79  77  77  ASN ASN B . n 
B 2 80  THR 80  78  78  THR THR B . n 
B 2 81  ILE 81  79  79  ILE ILE B . n 
B 2 82  TYR 82  80  80  TYR TYR B . n 
B 2 83  LEU 83  81  81  LEU LEU B . n 
B 2 84  GLN 84  82  82  GLN GLN B . n 
B 2 85  MET 85  83  83  MET MET B . n 
B 2 86  ASN 86  84  84  ASN ASN B . n 
B 2 87  SER 87  85  85  SER SER B . n 
B 2 88  LEU 88  86  86  LEU LEU B . n 
B 2 89  ASN 89  87  87  ASN ASN B . n 
B 2 90  PRO 90  88  88  PRO PRO B . n 
B 2 91  GLY 91  89  89  GLY GLY B . n 
B 2 92  ASP 92  90  90  ASP ASP B . n 
B 2 93  THR 93  91  91  THR THR B . n 
B 2 94  ALA 94  92  92  ALA ALA B . n 
B 2 95  VAL 95  93  93  VAL VAL B . n 
B 2 96  TYR 96  94  94  TYR TYR B . n 
B 2 97  SER 97  95  95  SER SER B . n 
B 2 98  CYS 98  96  96  CYS CYS B . n 
B 2 99  ALA 99  97  97  ALA ALA B . n 
B 2 100 ALA 100 98  98  ALA ALA B . n 
B 2 101 THR 101 99  99  THR THR B . n 
B 2 102 LEU 102 100 100 LEU LEU B . n 
B 2 103 PRO 103 101 101 PRO PRO B . n 
B 2 104 ALA 104 102 102 ALA ALA B . n 
B 2 105 TRP 105 103 103 TRP TRP B . n 
B 2 106 THR 106 104 104 THR THR B . n 
B 2 107 GLY 107 105 105 GLY GLY B . n 
B 2 108 ILE 108 106 106 ILE ILE B . n 
B 2 109 ILE 109 107 107 ILE ILE B . n 
B 2 110 GLY 110 108 108 GLY GLY B . n 
B 2 111 GLY 111 109 109 GLY GLY B . n 
B 2 112 ARG 112 110 110 ARG ARG B . n 
B 2 113 ARG 113 111 111 ARG ARG B . n 
B 2 114 PRO 114 112 112 PRO PRO B . n 
B 2 115 GLY 115 113 113 GLY GLY B . n 
B 2 116 ASN 116 114 114 ASN ASN B . n 
B 2 117 TYR 117 115 115 TYR TYR B . n 
B 2 118 PRO 118 116 116 PRO PRO B . n 
B 2 119 TYR 119 117 117 TYR TYR B . n 
B 2 120 TRP 120 118 118 TRP TRP B . n 
B 2 121 GLY 121 119 119 GLY GLY B . n 
B 2 122 GLN 122 120 120 GLN GLN B . n 
B 2 123 GLY 123 121 121 GLY GLY B . n 
B 2 124 THR 124 122 122 THR THR B . n 
B 2 125 GLN 125 123 123 GLN GLN B . n 
B 2 126 VAL 126 124 124 VAL VAL B . n 
B 2 127 THR 127 125 125 THR THR B . n 
B 2 128 VAL 128 126 126 VAL VAL B . n 
B 2 129 SER 129 127 127 SER SER B . n 
B 2 130 SER 130 128 ?   ?   ?   B . n 
B 2 131 HIS 131 129 ?   ?   ?   B . n 
B 2 132 HIS 132 130 ?   ?   ?   B . n 
B 2 133 HIS 133 131 ?   ?   ?   B . n 
B 2 134 HIS 134 132 ?   ?   ?   B . n 
B 2 135 HIS 135 133 ?   ?   ?   B . n 
B 2 136 HIS 136 134 ?   ?   ?   B . n 
B 2 137 GLU 137 135 ?   ?   ?   B . n 
B 2 138 PRO 138 136 ?   ?   ?   B . n 
B 2 139 GLU 139 137 ?   ?   ?   B . n 
B 2 140 ALA 140 138 ?   ?   ?   B . n 
C 3 1   MET 1   -1  ?   ?   ?   C . n 
C 3 2   ALA 2   0   ?   ?   ?   C . n 
C 3 3   GLN 3   1   ?   ?   ?   C . n 
C 3 4   VAL 4   2   2   VAL VAL C . n 
C 3 5   GLN 5   3   3   GLN GLN C . n 
C 3 6   LEU 6   4   4   LEU LEU C . n 
C 3 7   VAL 7   5   5   VAL VAL C . n 
C 3 8   GLU 8   6   6   GLU GLU C . n 
C 3 9   SER 9   7   7   SER SER C . n 
C 3 10  GLY 10  8   8   GLY GLY C . n 
C 3 11  GLY 11  9   9   GLY GLY C . n 
C 3 12  GLY 12  10  10  GLY GLY C . n 
C 3 13  LEU 13  11  11  LEU LEU C . n 
C 3 14  VAL 14  12  12  VAL VAL C . n 
C 3 15  GLN 15  13  13  GLN GLN C . n 
C 3 16  ALA 16  14  14  ALA ALA C . n 
C 3 17  GLY 17  15  15  GLY GLY C . n 
C 3 18  ASP 18  16  16  ASP ASP C . n 
C 3 19  SER 19  17  17  SER SER C . n 
C 3 20  LEU 20  18  18  LEU LEU C . n 
C 3 21  THR 21  19  19  THR THR C . n 
C 3 22  LEU 22  20  20  LEU LEU C . n 
C 3 23  SER 23  21  21  SER SER C . n 
C 3 24  CYS 24  22  22  CYS CYS C . n 
C 3 25  ALA 25  23  23  ALA ALA C . n 
C 3 26  ALA 26  24  24  ALA ALA C . n 
C 3 27  SER 27  25  25  SER SER C . n 
C 3 28  GLY 28  26  26  GLY GLY C . n 
C 3 29  ARG 29  27  27  ARG ARG C . n 
C 3 30  THR 30  28  28  THR THR C . n 
C 3 31  ALA 31  29  29  ALA ALA C . n 
C 3 32  TYR 32  30  30  TYR TYR C . n 
C 3 33  ARG 33  31  31  ARG ARG C . n 
C 3 34  TYR 34  32  32  TYR TYR C . n 
C 3 35  GLY 35  33  33  GLY GLY C . n 
C 3 36  MET 36  34  34  MET MET C . n 
C 3 37  GLY 37  35  35  GLY GLY C . n 
C 3 38  TRP 38  36  36  TRP TRP C . n 
C 3 39  PHE 39  37  37  PHE PHE C . n 
C 3 40  ARG 40  38  38  ARG ARG C . n 
C 3 41  GLN 41  39  39  GLN GLN C . n 
C 3 42  HIS 42  40  40  HIS HIS C . n 
C 3 43  PRO 43  41  41  PRO PRO C . n 
C 3 44  GLY 44  42  42  GLY GLY C . n 
C 3 45  LYS 45  43  43  LYS LYS C . n 
C 3 46  GLU 46  44  44  GLU GLU C . n 
C 3 47  ARG 47  45  45  ARG ARG C . n 
C 3 48  GLU 48  46  46  GLU GLU C . n 
C 3 49  PHE 49  47  47  PHE PHE C . n 
C 3 50  VAL 50  48  48  VAL VAL C . n 
C 3 51  ALA 51  49  49  ALA ALA C . n 
C 3 52  SER 52  50  50  SER SER C . n 
C 3 53  ILE 53  51  51  ILE ILE C . n 
C 3 54  TRP 54  52  52  TRP TRP C . n 
C 3 55  TRP 55  53  53  TRP TRP C . n 
C 3 56  THR 56  54  54  THR THR C . n 
C 3 57  GLY 57  55  55  GLY GLY C . n 
C 3 58  THR 58  56  56  THR THR C . n 
C 3 59  THR 59  57  57  THR THR C . n 
C 3 60  THR 60  58  58  THR THR C . n 
C 3 61  TYR 61  59  59  TYR TYR C . n 
C 3 62  TYR 62  60  60  TYR TYR C . n 
C 3 63  ALA 63  61  61  ALA ALA C . n 
C 3 64  ASP 64  62  62  ASP ASP C . n 
C 3 65  SER 65  63  63  SER SER C . n 
C 3 66  VAL 66  64  64  VAL VAL C . n 
C 3 67  LYS 67  65  65  LYS LYS C . n 
C 3 68  GLY 68  66  66  GLY GLY C . n 
C 3 69  ARG 69  67  67  ARG ARG C . n 
C 3 70  PHE 70  68  68  PHE PHE C . n 
C 3 71  THR 71  69  69  THR THR C . n 
C 3 72  ILE 72  70  70  ILE ILE C . n 
C 3 73  SER 73  71  71  SER SER C . n 
C 3 74  ARG 74  72  72  ARG ARG C . n 
C 3 75  ASP 75  73  73  ASP ASP C . n 
C 3 76  ASP 76  74  74  ASP ASP C . n 
C 3 77  VAL 77  75  75  VAL VAL C . n 
C 3 78  LYS 78  76  76  LYS LYS C . n 
C 3 79  ASN 79  77  77  ASN ASN C . n 
C 3 80  MET 80  78  78  MET MET C . n 
C 3 81  VAL 81  79  79  VAL VAL C . n 
C 3 82  TYR 82  80  80  TYR TYR C . n 
C 3 83  LEU 83  81  81  LEU LEU C . n 
C 3 84  GLN 84  82  82  GLN GLN C . n 
C 3 85  MET 85  83  83  MET MET C . n 
C 3 86  ASN 86  84  84  ASN ASN C . n 
C 3 87  SER 87  85  85  SER SER C . n 
C 3 88  LEU 88  86  86  LEU LEU C . n 
C 3 89  LYS 89  87  87  LYS LYS C . n 
C 3 90  PRO 90  88  88  PRO PRO C . n 
C 3 91  GLU 91  89  89  GLU GLU C . n 
C 3 92  ASP 92  90  90  ASP ASP C . n 
C 3 93  THR 93  91  91  THR THR C . n 
C 3 94  ALA 94  92  92  ALA ALA C . n 
C 3 95  VAL 95  93  93  VAL VAL C . n 
C 3 96  TYR 96  94  94  TYR TYR C . n 
C 3 97  TYR 97  95  95  TYR TYR C . n 
C 3 98  CYS 98  96  96  CYS CYS C . n 
C 3 99  ALA 99  97  97  ALA ALA C . n 
C 3 100 ALA 100 98  98  ALA ALA C . n 
C 3 101 LYS 101 99  99  LYS LYS C . n 
C 3 102 PHE 102 100 100 PHE PHE C . n 
C 3 103 TYR 103 101 101 TYR TYR C . n 
C 3 104 GLY 104 102 102 GLY GLY C . n 
C 3 105 GLY 105 103 103 GLY GLY C . n 
C 3 106 ASN 106 104 104 ASN ASN C . n 
C 3 107 SER 107 105 105 SER SER C . n 
C 3 108 LYS 108 106 106 LYS LYS C . n 
C 3 109 ARG 109 107 107 ARG ARG C . n 
C 3 110 PRO 110 108 108 PRO PRO C . n 
C 3 111 GLY 111 109 109 GLY GLY C . n 
C 3 112 ASP 112 110 110 ASP ASP C . n 
C 3 113 TYR 113 111 111 TYR TYR C . n 
C 3 114 ALA 114 112 112 ALA ALA C . n 
C 3 115 TYR 115 113 113 TYR TYR C . n 
C 3 116 TRP 116 114 114 TRP TRP C . n 
C 3 117 GLY 117 115 115 GLY GLY C . n 
C 3 118 GLN 118 116 116 GLN GLN C . n 
C 3 119 GLY 119 117 117 GLY GLY C . n 
C 3 120 THR 120 118 118 THR THR C . n 
C 3 121 GLN 121 119 119 GLN GLN C . n 
C 3 122 VAL 122 120 120 VAL VAL C . n 
C 3 123 THR 123 121 121 THR THR C . n 
C 3 124 VAL 124 122 122 VAL VAL C . n 
C 3 125 SER 125 123 123 SER SER C . n 
C 3 126 SER 126 124 124 SER SER C . n 
C 3 127 HIS 127 125 ?   ?   ?   C . n 
C 3 128 HIS 128 126 ?   ?   ?   C . n 
C 3 129 HIS 129 127 ?   ?   ?   C . n 
C 3 130 HIS 130 128 ?   ?   ?   C . n 
C 3 131 HIS 131 129 ?   ?   ?   C . n 
C 3 132 HIS 132 130 ?   ?   ?   C . n 
C 3 133 GLU 133 131 ?   ?   ?   C . n 
C 3 134 PRO 134 132 ?   ?   ?   C . n 
C 3 135 GLU 135 133 ?   ?   ?   C . n 
C 3 136 ALA 136 134 ?   ?   ?   C . n 
# 
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 scaling'   ? ? ? ? ? ? ? ? ? ? ? xia2   ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? xia2   ? ? ? .                    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                     9G9N 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     84.240 
_cell.length_a_esd                 ? 
_cell.length_b                     191.910 
_cell.length_b_esd                 ? 
_cell.length_c                     101.410 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         9G9N 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                20 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 2 2 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9G9N 
_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             2.68 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          54.09 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'LIPIDIC CUBIC PHASE' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    'tri-sodium citrate, lithium sulphate, sodium chloride, PEG400, E coli polar lipids, monoolein' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 X CdTe 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-07-07 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.6199 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'DIAMOND BEAMLINE I24' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.6199 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I24 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9G9N 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.80 
_reflns.d_resolution_low                               33.80 
_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                                     20612 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          6.5 
_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                                   1.0 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.80 
_reflns_shell.d_res_low                                     2.85 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.3 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1002 
_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                               6.9 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_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                                  0.7 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          100.0 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9G9N 
_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                            2.80 
_refine.ls_d_res_low                             32.40 
_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                     20563 
_refine.ls_number_reflns_R_free                  1027 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.67 
_refine.ls_percent_reflns_R_free                 4.99 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2587 
_refine.ls_R_factor_R_free                       0.3133 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2558 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 36.78 
_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                            0.44 
_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.pdbx_number_atoms_protein        5060 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               5060 
_refine_hist.d_res_high                       2.80 
_refine_hist.d_res_low                        32.40 
# 
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' ? 0.002 ? 5177 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.495 ? 7037 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 3.942 ? 726  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.037 ? 803  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.004 ? 872  ? 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' 2.80 2.95  . . 135 2736 100.00 . . . . 0.3629 . . . . . . . . . . . 0.4398 
'X-RAY DIFFRACTION' 2.95 3.13  . . 164 2751 100.00 . . . . 0.3377 . . . . . . . . . . . 0.4284 
'X-RAY DIFFRACTION' 3.13 3.37  . . 139 2783 100.00 . . . . 0.3033 . . . . . . . . . . . 0.3782 
'X-RAY DIFFRACTION' 3.37 3.71  . . 146 2758 100.00 . . . . 0.2615 . . . . . . . . . . . 0.3247 
'X-RAY DIFFRACTION' 3.71 4.25  . . 140 2803 100.00 . . . . 0.2304 . . . . . . . . . . . 0.2698 
'X-RAY DIFFRACTION' 4.25 5.35  . . 139 2791 99.00  . . . . 0.2377 . . . . . . . . . . . 0.3214 
'X-RAY DIFFRACTION' 5.35 32.40 . . 164 2914 100.00 . . . . 0.2194 . . . . . . . . . . . 0.2467 
# 
_struct.entry_id                     9G9N 
_struct.title                        
'Lipid III flippase WzxE with NB10 and NB7 nanobodies in inward-facing conformation - crystal 1' 
_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        9G9N 
_struct_keywords.text            
'membrane protein, flippase, cell wall, enterobacterial common antigen, lipid III, TRANSPORT PROTEIN' 
_struct_keywords.pdbx_keywords   'TRANSPORT 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 3 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP WZXE_ECOLI P0AAA7 ? 1 
;SLAKASLWTAASTLVKIGAGLLVGKLLAVSFGPAGLGLAANFRQLITVLGVLAGAGIFNGVTKYVAQYHDNPQQLRRVVG
TSSAMVLGFSTLMALVFVLAAAPISQGLFGNTDYQGLVRLVALVQMGIAWGNLLLALMKGFRDAAGNALSLIVGSLIGVL
AYYVSYRLGGYEGALLGLALIPALVVIPAAIMLIKRGVIPLSYLKPSWDNGLAGQLSKFTLMALITSVTLPVAYIMMRKL
LAAQYSWDEVGIWQGVSSISDAYLQFITASFSVYLLPTLSRLTEKRDITREVVKSLKFVLPAVAAASFTVWLLRDFAIWL
LLSNKFTAMRDLFAWQLVGDVLKVGAYVFGYLVIAKASLRFYILAEVSQFTLLMVFAHWLIPAHGALGAAQAYMATYIVY
FSLCCGVFLLWRRRA
;
2 
2 PDB 9G9N       9G9N   ? 2 ? 1 
3 PDB 9G9N       9G9N   ? 3 ? 1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9G9N A 3 ? 417 ? P0AAA7 2  ? 416 ? 2  416 
2 2 9G9N B 1 ? 140 ? 9G9N   -1 ? 138 ? -1 138 
3 3 9G9N C 1 ? 136 ? 9G9N   -1 ? 134 ? -1 134 
# 
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 9G9N MET A 1   ? UNP P0AAA7 ? ? 'initiating methionine' 0   1  
1 9G9N VAL A 2   ? UNP P0AAA7 ? ? 'cloning artifact'      1   2  
1 9G9N LEU A 418 ? UNP P0AAA7 ? ? 'expression tag'        417 3  
1 9G9N GLU A 419 ? UNP P0AAA7 ? ? 'expression tag'        418 4  
1 9G9N GLU A 420 ? UNP P0AAA7 ? ? 'expression tag'        419 5  
1 9G9N ASN A 421 ? UNP P0AAA7 ? ? 'expression tag'        420 6  
1 9G9N LEU A 422 ? UNP P0AAA7 ? ? 'expression tag'        421 7  
1 9G9N TYR A 423 ? UNP P0AAA7 ? ? 'expression tag'        422 8  
1 9G9N PHE A 424 ? UNP P0AAA7 ? ? 'expression tag'        423 9  
1 9G9N GLN A 425 ? UNP P0AAA7 ? ? 'expression tag'        424 10 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   trimeric 
_pdbx_struct_assembly.oligomeric_count     3 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 8   ? ALA A 55  ? SER A 7   ALA A 54  1 ? 48 
HELX_P HELX_P2  AA2 ILE A 59  ? HIS A 71  ? ILE A 58  HIS A 70  1 ? 13 
HELX_P HELX_P3  AA3 ASN A 73  ? ALA A 102 ? ASN A 72  ALA A 101 1 ? 30 
HELX_P HELX_P4  AA4 ALA A 102 ? GLY A 112 ? ALA A 101 GLY A 111 1 ? 11 
HELX_P HELX_P5  AA5 TYR A 116 ? PHE A 143 ? TYR A 115 PHE A 142 1 ? 28 
HELX_P HELX_P6  AA6 ASP A 145 ? LEU A 186 ? ASP A 144 LEU A 185 1 ? 42 
HELX_P HELX_P7  AA7 VAL A 187 ? ARG A 198 ? VAL A 186 ARG A 197 1 ? 12 
HELX_P HELX_P8  AA8 PRO A 202 ? LYS A 207 ? PRO A 201 LYS A 206 5 ? 6  
HELX_P HELX_P9  AA9 ASP A 211 ? VAL A 230 ? ASP A 210 VAL A 229 1 ? 20 
HELX_P HELX_P10 AB1 THR A 231 ? TYR A 247 ? THR A 230 TYR A 246 1 ? 17 
HELX_P HELX_P11 AB2 SER A 248 ? VAL A 275 ? SER A 247 VAL A 274 1 ? 28 
HELX_P HELX_P12 AB3 TYR A 276 ? LEU A 284 ? TYR A 275 LEU A 283 1 ? 9  
HELX_P HELX_P13 AB4 GLU A 286 ? LEU A 315 ? GLU A 285 LEU A 314 1 ? 30 
HELX_P HELX_P14 AB5 LEU A 315 ? LEU A 324 ? LEU A 314 LEU A 323 1 ? 10 
HELX_P HELX_P15 AB6 SER A 325 ? ARG A 332 ? SER A 324 ARG A 331 5 ? 8  
HELX_P HELX_P16 AB7 ASP A 333 ? ALA A 359 ? ASP A 332 ALA A 358 1 ? 27 
HELX_P HELX_P17 AB8 SER A 360 ? GLY A 387 ? SER A 359 GLY A 386 1 ? 28 
HELX_P HELX_P18 AB9 GLY A 387 ? ARG A 415 ? GLY A 386 ARG A 414 1 ? 29 
HELX_P HELX_P19 AC1 THR B 30  ? TYR B 34  ? THR B 28  TYR B 32  5 ? 5  
HELX_P HELX_P20 AC2 ASN B 89  ? THR B 93  ? ASN B 87  THR B 91  5 ? 5  
HELX_P HELX_P21 AC3 LEU B 102 ? GLY B 107 ? LEU B 100 GLY B 105 1 ? 6  
HELX_P HELX_P22 AC4 ILE B 109 ? TYR B 117 ? ILE B 107 TYR B 115 5 ? 9  
HELX_P HELX_P23 AC5 THR C 30  ? TYR C 32  ? THR C 28  TYR C 30  5 ? 3  
HELX_P HELX_P24 AC6 LYS C 89  ? THR C 93  ? LYS C 87  THR C 91  5 ? 5  
HELX_P HELX_P25 AC7 ARG C 109 ? TYR C 113 ? ARG C 107 TYR C 111 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ? ? B CYS 24 SG ? ? ? 1_555 B CYS 98 SG ? ? B CYS 22 B CYS 96 1_555 ? ? ? ? ? ? ? 2.033 ? ? 
disulf2 disulf ? ? C CYS 24 SG ? ? ? 1_555 C CYS 98 SG ? ? C CYS 22 C CYS 96 1_555 ? ? ? ? ? ? ? 2.036 ? ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
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 CYS B 24 ? CYS B 98 ? CYS B 22 ? 1_555 CYS B 96 ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS C 24 ? CYS C 98 ? CYS C 22 ? 1_555 CYS C 96 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 6 ? 
AA3 ? 4 ? 
AA4 ? 6 ? 
AA5 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLN B 5   ? GLY B 10  ? GLN B 3   GLY B 8   
AA1 2 LEU B 20  ? SER B 27  ? LEU B 18  SER B 25  
AA1 3 THR B 80  ? MET B 85  ? THR B 78  MET B 83  
AA1 4 PHE B 70  ? ASP B 75  ? PHE B 68  ASP B 73  
AA2 1 LEU B 13  ? VAL B 14  ? LEU B 11  VAL B 12  
AA2 2 THR B 124 ? VAL B 128 ? THR B 122 VAL B 126 
AA2 3 ALA B 94  ? THR B 101 ? ALA B 92  THR B 99  
AA2 4 VAL B 35  ? GLN B 41  ? VAL B 33  GLN B 39  
AA2 5 GLU B 48  ? ILE B 53  ? GLU B 46  ILE B 51  
AA2 6 THR B 60  ? TYR B 62  ? THR B 58  TYR B 60  
AA3 1 LEU C 6   ? SER C 9   ? LEU C 4   SER C 7   
AA3 2 LEU C 20  ? ALA C 26  ? LEU C 18  ALA C 24  
AA3 3 MET C 80  ? MET C 85  ? MET C 78  MET C 83  
AA3 4 THR C 71  ? ASP C 75  ? THR C 69  ASP C 73  
AA4 1 GLY C 12  ? GLN C 15  ? GLY C 10  GLN C 13  
AA4 2 THR C 120 ? SER C 125 ? THR C 118 SER C 123 
AA4 3 ALA C 94  ? PHE C 102 ? ALA C 92  PHE C 100 
AA4 4 TYR C 34  ? GLN C 41  ? TYR C 32  GLN C 39  
AA4 5 ARG C 47  ? ILE C 53  ? ARG C 45  ILE C 51  
AA4 6 THR C 60  ? TYR C 62  ? THR C 58  TYR C 60  
AA5 1 GLY C 12  ? GLN C 15  ? GLY C 10  GLN C 13  
AA5 2 THR C 120 ? SER C 125 ? THR C 118 SER C 123 
AA5 3 ALA C 94  ? PHE C 102 ? ALA C 92  PHE C 100 
AA5 4 TYR C 115 ? TRP C 116 ? TYR C 113 TRP C 114 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N VAL B 7   ? N VAL B 5   O ALA B 25  ? O ALA B 23  
AA1 2 3 N LEU B 22  ? N LEU B 20  O LEU B 83  ? O LEU B 81  
AA1 3 4 O GLN B 84  ? O GLN B 82  N THR B 71  ? N THR B 69  
AA2 1 2 N VAL B 14  ? N VAL B 12  O THR B 127 ? O THR B 125 
AA2 2 3 O THR B 124 ? O THR B 122 N TYR B 96  ? N TYR B 94  
AA2 3 4 O THR B 101 ? O THR B 99  N VAL B 35  ? N VAL B 33  
AA2 4 5 N TRP B 38  ? N TRP B 36  O ALA B 51  ? O ALA B 49  
AA2 5 6 N ARG B 52  ? N ARG B 50  O ASP B 61  ? O ASP B 59  
AA3 1 2 N SER C 9   ? N SER C 7   O SER C 23  ? O SER C 21  
AA3 2 3 N LEU C 20  ? N LEU C 18  O MET C 85  ? O MET C 83  
AA3 3 4 O GLN C 84  ? O GLN C 82  N THR C 71  ? N THR C 69  
AA4 1 2 N VAL C 14  ? N VAL C 12  O THR C 123 ? O THR C 121 
AA4 2 3 O THR C 120 ? O THR C 118 N TYR C 96  ? N TYR C 94  
AA4 3 4 O LYS C 101 ? O LYS C 99  N GLY C 35  ? N GLY C 33  
AA4 4 5 N TRP C 38  ? N TRP C 36  O ALA C 51  ? O ALA C 49  
AA4 5 6 N SER C 52  ? N SER C 50  O TYR C 61  ? O TYR C 59  
AA5 1 2 N VAL C 14  ? N VAL C 12  O THR C 123 ? O THR C 121 
AA5 2 3 O THR C 120 ? O THR C 118 N TYR C 96  ? N TYR C 94  
AA5 3 4 N ALA C 100 ? N ALA C 98  O TYR C 115 ? O TYR C 113 
# 
_pdbx_entry_details.entry_id                   9G9N 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_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 LEU A 185 ? ? -69.05  1.33    
2  1 THR A 230 ? ? -113.50 -91.64  
3  1 TYR A 246 ? ? -106.89 -154.66 
4  1 PHE A 272 ? ? -112.06 -70.92  
5  1 THR A 284 ? ? -131.36 -42.40  
6  1 LEU A 323 ? ? -118.92 -146.87 
7  1 ARG A 415 ? ? 57.11   72.22   
8  1 SER B 54  ? ? -111.93 -87.86  
9  1 ASN B 84  ? ? -97.30  -82.13  
10 1 THR C 28  ? ? 48.95   28.28   
11 1 PRO C 41  ? ? -55.93  107.68  
12 1 ASN C 84  ? ? -122.09 -51.41  
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 20.4469 2.0387   24.9379 0.8002 ? -0.0380 ? 0.0632  ? 0.2863 ? -0.0248 ? 0.3977 ? 0.7111 ? 0.2060  
? -0.0938 ? 0.4547 ? -0.5909 ? 0.7868 ? 0.0480  ? -0.0247 ? 0.1435  ? 0.2366  ? -0.0338 ? -0.0154 ? -0.1153 ? 0.0766  ? 0.0088  ? 
2 'X-RAY DIFFRACTION' ? refined 18.0834 -34.3734 10.8502 0.9860 ? 0.0247  ? 0.0677  ? 0.3387 ? 0.0274  ? 0.3801 ? 3.8782 ? -2.7161 
? -0.7866 ? 5.3823 ? 2.6476  ? 1.6242 ? -0.1223 ? 0.0982  ? -0.2656 ? -0.3270 ? 0.0063  ? 0.0129  ? 0.4123  ? -0.1177 ? 0.0898  ? 
3 'X-RAY DIFFRACTION' ? refined 24.4295 -39.5051 39.1763 1.2450 ? 0.1704  ? -0.0156 ? 0.4445 ? 0.0398  ? 0.3604 ? 3.1075 ? 1.5696  
? 1.4445  ? 6.0771 ? -0.5602 ? 0.9873 ? 0.0245  ? 0.0638  ? -0.2306 ? 0.3094  ? -0.0300 ? -0.0815 ? 0.5201  ? 0.2615  ? -0.0145 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? 
;(chain 'A' and resid 7 through 416)
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;(chain 'B' and resid 2 through 127)
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;(chain 'C' and resid 4 through 124)
;
# 
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 0   ? A MET 1   
2  1 Y 1 A VAL 1   ? A VAL 2   
3  1 Y 1 A SER 2   ? A SER 3   
4  1 Y 1 A LEU 3   ? A LEU 4   
5  1 Y 1 A ALA 4   ? A ALA 5   
6  1 Y 1 A LYS 5   ? A LYS 6   
7  1 Y 1 A LEU 417 ? A LEU 418 
8  1 Y 1 A GLU 418 ? A GLU 419 
9  1 Y 1 A GLU 419 ? A GLU 420 
10 1 Y 1 A ASN 420 ? A ASN 421 
11 1 Y 1 A LEU 421 ? A LEU 422 
12 1 Y 1 A TYR 422 ? A TYR 423 
13 1 Y 1 A PHE 423 ? A PHE 424 
14 1 Y 1 A GLN 424 ? A GLN 425 
15 1 Y 1 B MET -1  ? B MET 1   
16 1 Y 1 B SER 128 ? B SER 130 
17 1 Y 1 B HIS 129 ? B HIS 131 
18 1 Y 1 B HIS 130 ? B HIS 132 
19 1 Y 1 B HIS 131 ? B HIS 133 
20 1 Y 1 B HIS 132 ? B HIS 134 
21 1 Y 1 B HIS 133 ? B HIS 135 
22 1 Y 1 B HIS 134 ? B HIS 136 
23 1 Y 1 B GLU 135 ? B GLU 137 
24 1 Y 1 B PRO 136 ? B PRO 138 
25 1 Y 1 B GLU 137 ? B GLU 139 
26 1 Y 1 B ALA 138 ? B ALA 140 
27 1 Y 1 C MET -1  ? C MET 1   
28 1 Y 1 C ALA 0   ? C ALA 2   
29 1 Y 1 C GLN 1   ? C GLN 3   
30 1 Y 1 C HIS 125 ? C HIS 127 
31 1 Y 1 C HIS 126 ? C HIS 128 
32 1 Y 1 C HIS 127 ? C HIS 129 
33 1 Y 1 C HIS 128 ? C HIS 130 
34 1 Y 1 C HIS 129 ? C HIS 131 
35 1 Y 1 C HIS 130 ? C HIS 132 
36 1 Y 1 C GLU 131 ? C GLU 133 
37 1 Y 1 C PRO 132 ? C PRO 134 
38 1 Y 1 C GLU 133 ? C GLU 135 
39 1 Y 1 C ALA 134 ? C ALA 136 
# 
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  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
ILE N    N N N 158 
ILE CA   C N S 159 
ILE C    C N N 160 
ILE O    O N N 161 
ILE CB   C N S 162 
ILE CG1  C N N 163 
ILE CG2  C N N 164 
ILE CD1  C N N 165 
ILE OXT  O N N 166 
ILE H    H N N 167 
ILE H2   H N N 168 
ILE HA   H N N 169 
ILE HB   H N N 170 
ILE HG12 H N N 171 
ILE HG13 H N N 172 
ILE HG21 H N N 173 
ILE HG22 H N N 174 
ILE HG23 H N N 175 
ILE HD11 H N N 176 
ILE HD12 H N N 177 
ILE HD13 H N N 178 
ILE HXT  H N N 179 
LEU N    N N N 180 
LEU CA   C N S 181 
LEU C    C N N 182 
LEU O    O N N 183 
LEU CB   C N N 184 
LEU CG   C N N 185 
LEU CD1  C N N 186 
LEU CD2  C N N 187 
LEU OXT  O N N 188 
LEU H    H N N 189 
LEU H2   H N N 190 
LEU HA   H N N 191 
LEU HB2  H N N 192 
LEU HB3  H N N 193 
LEU HG   H N N 194 
LEU HD11 H N N 195 
LEU HD12 H N N 196 
LEU HD13 H N N 197 
LEU HD21 H N N 198 
LEU HD22 H N N 199 
LEU HD23 H N N 200 
LEU HXT  H N N 201 
LYS N    N N N 202 
LYS CA   C N S 203 
LYS C    C N N 204 
LYS O    O N N 205 
LYS CB   C N N 206 
LYS CG   C N N 207 
LYS CD   C N N 208 
LYS CE   C N N 209 
LYS NZ   N N N 210 
LYS OXT  O N N 211 
LYS H    H N N 212 
LYS H2   H N N 213 
LYS HA   H N N 214 
LYS HB2  H N N 215 
LYS HB3  H N N 216 
LYS HG2  H N N 217 
LYS HG3  H N N 218 
LYS HD2  H N N 219 
LYS HD3  H N N 220 
LYS HE2  H N N 221 
LYS HE3  H N N 222 
LYS HZ1  H N N 223 
LYS HZ2  H N N 224 
LYS HZ3  H N N 225 
LYS HXT  H N N 226 
MET N    N N N 227 
MET CA   C N S 228 
MET C    C N N 229 
MET O    O N N 230 
MET CB   C N N 231 
MET CG   C N N 232 
MET SD   S N N 233 
MET CE   C N N 234 
MET OXT  O N N 235 
MET H    H N N 236 
MET H2   H N N 237 
MET HA   H N N 238 
MET HB2  H N N 239 
MET HB3  H N N 240 
MET HG2  H N N 241 
MET HG3  H N N 242 
MET HE1  H N N 243 
MET HE2  H N N 244 
MET HE3  H N N 245 
MET HXT  H N N 246 
PHE N    N N N 247 
PHE CA   C N S 248 
PHE C    C N N 249 
PHE O    O N N 250 
PHE CB   C N N 251 
PHE CG   C Y N 252 
PHE CD1  C Y N 253 
PHE CD2  C Y N 254 
PHE CE1  C Y N 255 
PHE CE2  C Y N 256 
PHE CZ   C Y N 257 
PHE OXT  O N N 258 
PHE H    H N N 259 
PHE H2   H N N 260 
PHE HA   H N N 261 
PHE HB2  H N N 262 
PHE HB3  H N N 263 
PHE HD1  H N N 264 
PHE HD2  H N N 265 
PHE HE1  H N N 266 
PHE HE2  H N N 267 
PHE HZ   H N N 268 
PHE HXT  H N N 269 
PRO N    N N N 270 
PRO CA   C N S 271 
PRO C    C N N 272 
PRO O    O N N 273 
PRO CB   C N N 274 
PRO CG   C N N 275 
PRO CD   C N N 276 
PRO OXT  O N N 277 
PRO H    H N N 278 
PRO HA   H N N 279 
PRO HB2  H N N 280 
PRO HB3  H N N 281 
PRO HG2  H N N 282 
PRO HG3  H N N 283 
PRO HD2  H N N 284 
PRO HD3  H N N 285 
PRO HXT  H N N 286 
SER N    N N N 287 
SER CA   C N S 288 
SER C    C N N 289 
SER O    O N N 290 
SER CB   C N N 291 
SER OG   O N N 292 
SER OXT  O N N 293 
SER H    H N N 294 
SER H2   H N N 295 
SER HA   H N N 296 
SER HB2  H N N 297 
SER HB3  H N N 298 
SER HG   H N N 299 
SER HXT  H N N 300 
THR N    N N N 301 
THR CA   C N S 302 
THR C    C N N 303 
THR O    O N N 304 
THR CB   C N R 305 
THR OG1  O N N 306 
THR CG2  C N N 307 
THR OXT  O N N 308 
THR H    H N N 309 
THR H2   H N N 310 
THR HA   H N N 311 
THR HB   H N N 312 
THR HG1  H N N 313 
THR HG21 H N N 314 
THR HG22 H N N 315 
THR HG23 H N N 316 
THR HXT  H N N 317 
TRP N    N N N 318 
TRP CA   C N S 319 
TRP C    C N N 320 
TRP O    O N N 321 
TRP CB   C N N 322 
TRP CG   C Y N 323 
TRP CD1  C Y N 324 
TRP CD2  C Y N 325 
TRP NE1  N Y N 326 
TRP CE2  C Y N 327 
TRP CE3  C Y N 328 
TRP CZ2  C Y N 329 
TRP CZ3  C Y N 330 
TRP CH2  C Y N 331 
TRP OXT  O N N 332 
TRP H    H N N 333 
TRP H2   H N N 334 
TRP HA   H N N 335 
TRP HB2  H N N 336 
TRP HB3  H N N 337 
TRP HD1  H N N 338 
TRP HE1  H N N 339 
TRP HE3  H N N 340 
TRP HZ2  H N N 341 
TRP HZ3  H N N 342 
TRP HH2  H N N 343 
TRP HXT  H N N 344 
TYR N    N N N 345 
TYR CA   C N S 346 
TYR C    C N N 347 
TYR O    O N N 348 
TYR CB   C N N 349 
TYR CG   C Y N 350 
TYR CD1  C Y N 351 
TYR CD2  C Y N 352 
TYR CE1  C Y N 353 
TYR CE2  C Y N 354 
TYR CZ   C Y N 355 
TYR OH   O N N 356 
TYR OXT  O N N 357 
TYR H    H N N 358 
TYR H2   H N N 359 
TYR HA   H N N 360 
TYR HB2  H N N 361 
TYR HB3  H N N 362 
TYR HD1  H N N 363 
TYR HD2  H N N 364 
TYR HE1  H N N 365 
TYR HE2  H N N 366 
TYR HH   H N N 367 
TYR HXT  H N N 368 
VAL N    N N N 369 
VAL CA   C N S 370 
VAL C    C N N 371 
VAL O    O N N 372 
VAL CB   C N N 373 
VAL CG1  C N N 374 
VAL CG2  C N N 375 
VAL OXT  O N N 376 
VAL H    H N N 377 
VAL H2   H N N 378 
VAL HA   H N N 379 
VAL HB   H N N 380 
VAL HG11 H N N 381 
VAL HG12 H N N 382 
VAL HG13 H N N 383 
VAL HG21 H N N 384 
VAL HG22 H N N 385 
VAL HG23 H N N 386 
VAL HXT  H N N 387 
# 
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  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
ILE N   CA   sing N N 150 
ILE N   H    sing N N 151 
ILE N   H2   sing N N 152 
ILE CA  C    sing N N 153 
ILE CA  CB   sing N N 154 
ILE CA  HA   sing N N 155 
ILE C   O    doub N N 156 
ILE C   OXT  sing N N 157 
ILE CB  CG1  sing N N 158 
ILE CB  CG2  sing N N 159 
ILE CB  HB   sing N N 160 
ILE CG1 CD1  sing N N 161 
ILE CG1 HG12 sing N N 162 
ILE CG1 HG13 sing N N 163 
ILE CG2 HG21 sing N N 164 
ILE CG2 HG22 sing N N 165 
ILE CG2 HG23 sing N N 166 
ILE CD1 HD11 sing N N 167 
ILE CD1 HD12 sing N N 168 
ILE CD1 HD13 sing N N 169 
ILE OXT HXT  sing N N 170 
LEU N   CA   sing N N 171 
LEU N   H    sing N N 172 
LEU N   H2   sing N N 173 
LEU CA  C    sing N N 174 
LEU CA  CB   sing N N 175 
LEU CA  HA   sing N N 176 
LEU C   O    doub N N 177 
LEU C   OXT  sing N N 178 
LEU CB  CG   sing N N 179 
LEU CB  HB2  sing N N 180 
LEU CB  HB3  sing N N 181 
LEU CG  CD1  sing N N 182 
LEU CG  CD2  sing N N 183 
LEU CG  HG   sing N N 184 
LEU CD1 HD11 sing N N 185 
LEU CD1 HD12 sing N N 186 
LEU CD1 HD13 sing N N 187 
LEU CD2 HD21 sing N N 188 
LEU CD2 HD22 sing N N 189 
LEU CD2 HD23 sing N N 190 
LEU OXT HXT  sing N N 191 
LYS N   CA   sing N N 192 
LYS N   H    sing N N 193 
LYS N   H2   sing N N 194 
LYS CA  C    sing N N 195 
LYS CA  CB   sing N N 196 
LYS CA  HA   sing N N 197 
LYS C   O    doub N N 198 
LYS C   OXT  sing N N 199 
LYS CB  CG   sing N N 200 
LYS CB  HB2  sing N N 201 
LYS CB  HB3  sing N N 202 
LYS CG  CD   sing N N 203 
LYS CG  HG2  sing N N 204 
LYS CG  HG3  sing N N 205 
LYS CD  CE   sing N N 206 
LYS CD  HD2  sing N N 207 
LYS CD  HD3  sing N N 208 
LYS CE  NZ   sing N N 209 
LYS CE  HE2  sing N N 210 
LYS CE  HE3  sing N N 211 
LYS NZ  HZ1  sing N N 212 
LYS NZ  HZ2  sing N N 213 
LYS NZ  HZ3  sing N N 214 
LYS OXT HXT  sing N N 215 
MET N   CA   sing N N 216 
MET N   H    sing N N 217 
MET N   H2   sing N N 218 
MET CA  C    sing N N 219 
MET CA  CB   sing N N 220 
MET CA  HA   sing N N 221 
MET C   O    doub N N 222 
MET C   OXT  sing N N 223 
MET CB  CG   sing N N 224 
MET CB  HB2  sing N N 225 
MET CB  HB3  sing N N 226 
MET CG  SD   sing N N 227 
MET CG  HG2  sing N N 228 
MET CG  HG3  sing N N 229 
MET SD  CE   sing N N 230 
MET CE  HE1  sing N N 231 
MET CE  HE2  sing N N 232 
MET CE  HE3  sing N N 233 
MET OXT HXT  sing N N 234 
PHE N   CA   sing N N 235 
PHE N   H    sing N N 236 
PHE N   H2   sing N N 237 
PHE CA  C    sing N N 238 
PHE CA  CB   sing N N 239 
PHE CA  HA   sing N N 240 
PHE C   O    doub N N 241 
PHE C   OXT  sing N N 242 
PHE CB  CG   sing N N 243 
PHE CB  HB2  sing N N 244 
PHE CB  HB3  sing N N 245 
PHE CG  CD1  doub Y N 246 
PHE CG  CD2  sing Y N 247 
PHE CD1 CE1  sing Y N 248 
PHE CD1 HD1  sing N N 249 
PHE CD2 CE2  doub Y N 250 
PHE CD2 HD2  sing N N 251 
PHE CE1 CZ   doub Y N 252 
PHE CE1 HE1  sing N N 253 
PHE CE2 CZ   sing Y N 254 
PHE CE2 HE2  sing N N 255 
PHE CZ  HZ   sing N N 256 
PHE OXT HXT  sing N N 257 
PRO N   CA   sing N N 258 
PRO N   CD   sing N N 259 
PRO N   H    sing N N 260 
PRO CA  C    sing N N 261 
PRO CA  CB   sing N N 262 
PRO CA  HA   sing N N 263 
PRO C   O    doub N N 264 
PRO C   OXT  sing N N 265 
PRO CB  CG   sing N N 266 
PRO CB  HB2  sing N N 267 
PRO CB  HB3  sing N N 268 
PRO CG  CD   sing N N 269 
PRO CG  HG2  sing N N 270 
PRO CG  HG3  sing N N 271 
PRO CD  HD2  sing N N 272 
PRO CD  HD3  sing N N 273 
PRO OXT HXT  sing N N 274 
SER N   CA   sing N N 275 
SER N   H    sing N N 276 
SER N   H2   sing N N 277 
SER CA  C    sing N N 278 
SER CA  CB   sing N N 279 
SER CA  HA   sing N N 280 
SER C   O    doub N N 281 
SER C   OXT  sing N N 282 
SER CB  OG   sing N N 283 
SER CB  HB2  sing N N 284 
SER CB  HB3  sing N N 285 
SER OG  HG   sing N N 286 
SER OXT HXT  sing N N 287 
THR N   CA   sing N N 288 
THR N   H    sing N N 289 
THR N   H2   sing N N 290 
THR CA  C    sing N N 291 
THR CA  CB   sing N N 292 
THR CA  HA   sing N N 293 
THR C   O    doub N N 294 
THR C   OXT  sing N N 295 
THR CB  OG1  sing N N 296 
THR CB  CG2  sing N N 297 
THR CB  HB   sing N N 298 
THR OG1 HG1  sing N N 299 
THR CG2 HG21 sing N N 300 
THR CG2 HG22 sing N N 301 
THR CG2 HG23 sing N N 302 
THR OXT HXT  sing N N 303 
TRP N   CA   sing N N 304 
TRP N   H    sing N N 305 
TRP N   H2   sing N N 306 
TRP CA  C    sing N N 307 
TRP CA  CB   sing N N 308 
TRP CA  HA   sing N N 309 
TRP C   O    doub N N 310 
TRP C   OXT  sing N N 311 
TRP CB  CG   sing N N 312 
TRP CB  HB2  sing N N 313 
TRP CB  HB3  sing N N 314 
TRP CG  CD1  doub Y N 315 
TRP CG  CD2  sing Y N 316 
TRP CD1 NE1  sing Y N 317 
TRP CD1 HD1  sing N N 318 
TRP CD2 CE2  doub Y N 319 
TRP CD2 CE3  sing Y N 320 
TRP NE1 CE2  sing Y N 321 
TRP NE1 HE1  sing N N 322 
TRP CE2 CZ2  sing Y N 323 
TRP CE3 CZ3  doub Y N 324 
TRP CE3 HE3  sing N N 325 
TRP CZ2 CH2  doub Y N 326 
TRP CZ2 HZ2  sing N N 327 
TRP CZ3 CH2  sing Y N 328 
TRP CZ3 HZ3  sing N N 329 
TRP CH2 HH2  sing N N 330 
TRP OXT HXT  sing N N 331 
TYR N   CA   sing N N 332 
TYR N   H    sing N N 333 
TYR N   H2   sing N N 334 
TYR CA  C    sing N N 335 
TYR CA  CB   sing N N 336 
TYR CA  HA   sing N N 337 
TYR C   O    doub N N 338 
TYR C   OXT  sing N N 339 
TYR CB  CG   sing N N 340 
TYR CB  HB2  sing N N 341 
TYR CB  HB3  sing N N 342 
TYR CG  CD1  doub Y N 343 
TYR CG  CD2  sing Y N 344 
TYR CD1 CE1  sing Y N 345 
TYR CD1 HD1  sing N N 346 
TYR CD2 CE2  doub Y N 347 
TYR CD2 HD2  sing N N 348 
TYR CE1 CZ   doub Y N 349 
TYR CE1 HE1  sing N N 350 
TYR CE2 CZ   sing Y N 351 
TYR CE2 HE2  sing N N 352 
TYR CZ  OH   sing N N 353 
TYR OH  HH   sing N N 354 
TYR OXT HXT  sing N N 355 
VAL N   CA   sing N N 356 
VAL N   H    sing N N 357 
VAL N   H2   sing N N 358 
VAL CA  C    sing N N 359 
VAL CA  CB   sing N N 360 
VAL CA  HA   sing N N 361 
VAL C   O    doub N N 362 
VAL C   OXT  sing N N 363 
VAL CB  CG1  sing N N 364 
VAL CB  CG2  sing N N 365 
VAL CB  HB   sing N N 366 
VAL CG1 HG11 sing N N 367 
VAL CG1 HG12 sing N N 368 
VAL CG1 HG13 sing N N 369 
VAL CG2 HG21 sing N N 370 
VAL CG2 HG22 sing N N 371 
VAL CG2 HG23 sing N N 372 
VAL OXT HXT  sing N N 373 
# 
_pdbx_audit_support.funding_organization   'Wellcome Trust' 
_pdbx_audit_support.country                'United Kingdom' 
_pdbx_audit_support.grant_number           ? 
_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   9G97 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9G9N 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.011871 
_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]   0.005211 
_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]   0.009861 
_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   . ALA A 1 7   ? 5.987  20.852  32.592 1.00 70.70  ? 6   ALA A N   1 
ATOM 2    C CA  . ALA A 1 7   ? 5.301  19.569  32.701 1.00 88.23  ? 6   ALA A CA  1 
ATOM 3    C C   . ALA A 1 7   ? 5.357  18.804  31.382 1.00 87.83  ? 6   ALA A C   1 
ATOM 4    O O   . ALA A 1 7   ? 4.508  18.990  30.509 1.00 81.18  ? 6   ALA A O   1 
ATOM 5    C CB  . ALA A 1 7   ? 3.857  19.774  33.136 1.00 75.89  ? 6   ALA A CB  1 
ATOM 6    N N   . SER A 1 8   ? 6.365  17.943  31.241 1.00 87.65  ? 7   SER A N   1 
ATOM 7    C CA  . SER A 1 8   ? 6.525  17.127  30.036 1.00 82.47  ? 7   SER A CA  1 
ATOM 8    C C   . SER A 1 8   ? 5.785  15.802  30.221 1.00 78.44  ? 7   SER A C   1 
ATOM 9    O O   . SER A 1 8   ? 6.370  14.738  30.436 1.00 78.24  ? 7   SER A O   1 
ATOM 10   C CB  . SER A 1 8   ? 8.001  16.909  29.730 1.00 79.96  ? 7   SER A CB  1 
ATOM 11   O OG  . SER A 1 8   ? 8.512  15.808  30.460 1.00 81.63  ? 7   SER A OG  1 
ATOM 12   N N   . LEU A 1 9   ? 4.457  15.892  30.133 1.00 74.20  ? 8   LEU A N   1 
ATOM 13   C CA  . LEU A 1 9   ? 3.620  14.705  30.257 1.00 74.28  ? 8   LEU A CA  1 
ATOM 14   C C   . LEU A 1 9   ? 3.664  13.841  29.004 1.00 74.68  ? 8   LEU A C   1 
ATOM 15   O O   . LEU A 1 9   ? 3.491  12.620  29.096 1.00 76.94  ? 8   LEU A O   1 
ATOM 16   C CB  . LEU A 1 9   ? 2.178  15.108  30.565 1.00 72.19  ? 8   LEU A CB  1 
ATOM 17   C CG  . LEU A 1 9   ? 1.939  15.843  31.882 1.00 70.92  ? 8   LEU A CG  1 
ATOM 18   C CD1 . LEU A 1 9   ? 0.466  15.787  32.245 1.00 66.03  ? 8   LEU A CD1 1 
ATOM 19   C CD2 . LEU A 1 9   ? 2.796  15.262  33.001 1.00 71.53  ? 8   LEU A CD2 1 
ATOM 20   N N   . TRP A 1 10  ? 3.885  14.448  27.836 1.00 67.60  ? 9   TRP A N   1 
ATOM 21   C CA  . TRP A 1 10  ? 4.030  13.671  26.608 1.00 67.79  ? 9   TRP A CA  1 
ATOM 22   C C   . TRP A 1 10  ? 5.210  12.713  26.709 1.00 72.63  ? 9   TRP A C   1 
ATOM 23   O O   . TRP A 1 10  ? 5.107  11.538  26.336 1.00 69.84  ? 9   TRP A O   1 
ATOM 24   C CB  . TRP A 1 10  ? 4.204  14.607  25.410 1.00 73.57  ? 9   TRP A CB  1 
ATOM 25   C CG  . TRP A 1 10  ? 2.926  15.206  24.900 1.00 71.66  ? 9   TRP A CG  1 
ATOM 26   C CD1 . TRP A 1 10  ? 2.558  16.519  24.955 1.00 64.39  ? 9   TRP A CD1 1 
ATOM 27   C CD2 . TRP A 1 10  ? 1.853  14.517  24.244 1.00 73.11  ? 9   TRP A CD2 1 
ATOM 28   N NE1 . TRP A 1 10  ? 1.322  16.690  24.380 1.00 64.17  ? 9   TRP A NE1 1 
ATOM 29   C CE2 . TRP A 1 10  ? 0.867  15.476  23.936 1.00 70.87  ? 9   TRP A CE2 1 
ATOM 30   C CE3 . TRP A 1 10  ? 1.629  13.183  23.891 1.00 65.20  ? 9   TRP A CE3 1 
ATOM 31   C CZ2 . TRP A 1 10  ? -0.323 15.143  23.293 1.00 71.97  ? 9   TRP A CZ2 1 
ATOM 32   C CZ3 . TRP A 1 10  ? 0.448  12.855  23.252 1.00 68.71  ? 9   TRP A CZ3 1 
ATOM 33   C CH2 . TRP A 1 10  ? -0.513 13.830  22.960 1.00 74.09  ? 9   TRP A CH2 1 
ATOM 34   N N   . THR A 1 11  ? 6.344  13.202  27.219 1.00 67.34  ? 10  THR A N   1 
ATOM 35   C CA  . THR A 1 11  ? 7.537  12.368  27.323 1.00 70.26  ? 10  THR A CA  1 
ATOM 36   C C   . THR A 1 11  ? 7.308  11.190  28.262 1.00 70.05  ? 10  THR A C   1 
ATOM 37   O O   . THR A 1 11  ? 7.682  10.053  27.947 1.00 66.95  ? 10  THR A O   1 
ATOM 38   C CB  . THR A 1 11  ? 8.722  13.211  27.798 1.00 70.69  ? 10  THR A CB  1 
ATOM 39   O OG1 . THR A 1 11  ? 9.250  13.959  26.696 1.00 83.28  ? 10  THR A OG1 1 
ATOM 40   C CG2 . THR A 1 11  ? 9.822  12.327  28.372 1.00 74.96  ? 10  THR A CG2 1 
ATOM 41   N N   . ALA A 1 12  ? 6.687  11.439  29.416 1.00 77.48  ? 11  ALA A N   1 
ATOM 42   C CA  . ALA A 1 12  ? 6.436  10.361  30.366 1.00 77.58  ? 11  ALA A CA  1 
ATOM 43   C C   . ALA A 1 12  ? 5.439  9.352   29.809 1.00 79.45  ? 11  ALA A C   1 
ATOM 44   O O   . ALA A 1 12  ? 5.579  8.144   30.037 1.00 76.76  ? 11  ALA A O   1 
ATOM 45   C CB  . ALA A 1 12  ? 5.938  10.936  31.692 1.00 70.66  ? 11  ALA A CB  1 
ATOM 46   N N   . ALA A 1 13  ? 4.433  9.825   29.070 1.00 71.01  ? 12  ALA A N   1 
ATOM 47   C CA  . ALA A 1 13  ? 3.432  8.922   28.510 1.00 66.26  ? 12  ALA A CA  1 
ATOM 48   C C   . ALA A 1 13  ? 4.051  7.981   27.483 1.00 64.77  ? 12  ALA A C   1 
ATOM 49   O O   . ALA A 1 13  ? 3.810  6.769   27.513 1.00 67.78  ? 12  ALA A O   1 
ATOM 50   C CB  . ALA A 1 13  ? 2.290  9.726   27.888 1.00 59.42  ? 12  ALA A CB  1 
ATOM 51   N N   . SER A 1 14  ? 4.853  8.522   26.563 1.00 70.24  ? 13  SER A N   1 
ATOM 52   C CA  . SER A 1 14  ? 5.509  7.676   25.571 1.00 62.62  ? 13  SER A CA  1 
ATOM 53   C C   . SER A 1 14  ? 6.507  6.733   26.227 1.00 58.91  ? 13  SER A C   1 
ATOM 54   O O   . SER A 1 14  ? 6.675  5.591   25.783 1.00 63.40  ? 13  SER A O   1 
ATOM 55   C CB  . SER A 1 14  ? 6.198  8.538   24.513 1.00 61.31  ? 13  SER A CB  1 
ATOM 56   O OG  . SER A 1 14  ? 7.473  8.970   24.955 1.00 55.94  ? 13  SER A OG  1 
ATOM 57   N N   . THR A 1 15  ? 7.181  7.191   27.285 1.00 55.83  ? 14  THR A N   1 
ATOM 58   C CA  . THR A 1 15  ? 8.077  6.310   28.027 1.00 65.91  ? 14  THR A CA  1 
ATOM 59   C C   . THR A 1 15  ? 7.308  5.160   28.663 1.00 62.48  ? 14  THR A C   1 
ATOM 60   O O   . THR A 1 15  ? 7.776  4.015   28.666 1.00 54.19  ? 14  THR A O   1 
ATOM 61   C CB  . THR A 1 15  ? 8.833  7.104   29.094 1.00 60.34  ? 14  THR A CB  1 
ATOM 62   O OG1 . THR A 1 15  ? 9.502  8.213   28.482 1.00 71.23  ? 14  THR A OG1 1 
ATOM 63   C CG2 . THR A 1 15  ? 9.858  6.222   29.793 1.00 67.58  ? 14  THR A CG2 1 
ATOM 64   N N   . LEU A 1 16  ? 6.120  5.445   29.198 1.00 57.60  ? 15  LEU A N   1 
ATOM 65   C CA  . LEU A 1 16  ? 5.309  4.399   29.813 1.00 62.08  ? 15  LEU A CA  1 
ATOM 66   C C   . LEU A 1 16  ? 4.845  3.383   28.777 1.00 63.29  ? 15  LEU A C   1 
ATOM 67   O O   . LEU A 1 16  ? 4.934  2.169   28.999 1.00 58.09  ? 15  LEU A O   1 
ATOM 68   C CB  . LEU A 1 16  ? 4.113  5.023   30.531 1.00 56.46  ? 15  LEU A CB  1 
ATOM 69   C CG  . LEU A 1 16  ? 4.407  5.697   31.871 1.00 64.96  ? 15  LEU A CG  1 
ATOM 70   C CD1 . LEU A 1 16  ? 3.117  6.159   32.527 1.00 67.72  ? 15  LEU A CD1 1 
ATOM 71   C CD2 . LEU A 1 16  ? 5.175  4.758   32.788 1.00 67.34  ? 15  LEU A CD2 1 
ATOM 72   N N   . VAL A 1 17  ? 4.347  3.862   27.634 1.00 58.15  ? 16  VAL A N   1 
ATOM 73   C CA  . VAL A 1 17  ? 3.872  2.956   26.592 1.00 60.77  ? 16  VAL A CA  1 
ATOM 74   C C   . VAL A 1 17  ? 5.020  2.107   26.060 1.00 59.06  ? 16  VAL A C   1 
ATOM 75   O O   . VAL A 1 17  ? 4.856  0.909   25.799 1.00 59.84  ? 16  VAL A O   1 
ATOM 76   C CB  . VAL A 1 17  ? 3.183  3.749   25.467 1.00 58.61  ? 16  VAL A CB  1 
ATOM 77   C CG1 . VAL A 1 17  ? 2.781  2.823   24.329 1.00 50.68  ? 16  VAL A CG1 1 
ATOM 78   C CG2 . VAL A 1 17  ? 1.971  4.490   26.010 1.00 58.04  ? 16  VAL A CG2 1 
ATOM 79   N N   . LYS A 1 18  ? 6.200  2.710   25.898 1.00 56.74  ? 17  LYS A N   1 
ATOM 80   C CA  . LYS A 1 18  ? 7.357  1.954   25.430 1.00 56.50  ? 17  LYS A CA  1 
ATOM 81   C C   . LYS A 1 18  ? 7.741  0.861   26.420 1.00 56.34  ? 17  LYS A C   1 
ATOM 82   O O   . LYS A 1 18  ? 8.079  -0.259  26.020 1.00 64.70  ? 17  LYS A O   1 
ATOM 83   C CB  . LYS A 1 18  ? 8.538  2.894   25.187 1.00 53.74  ? 17  LYS A CB  1 
ATOM 84   C CG  . LYS A 1 18  ? 9.857  2.179   24.935 1.00 62.35  ? 17  LYS A CG  1 
ATOM 85   C CD  . LYS A 1 18  ? 10.946 3.152   24.514 1.00 65.93  ? 17  LYS A CD  1 
ATOM 86   C CE  . LYS A 1 18  ? 12.318 2.496   24.549 1.00 64.27  ? 17  LYS A CE  1 
ATOM 87   N NZ  . LYS A 1 18  ? 12.411 1.337   23.617 1.00 54.32  ? 17  LYS A NZ  1 
ATOM 88   N N   . ILE A 1 19  ? 7.690  1.167   27.719 1.00 56.21  ? 18  ILE A N   1 
ATOM 89   C CA  . ILE A 1 19  ? 8.067  0.183   28.729 1.00 57.99  ? 18  ILE A CA  1 
ATOM 90   C C   . ILE A 1 19  ? 7.049  -0.950  28.782 1.00 63.38  ? 18  ILE A C   1 
ATOM 91   O O   . ILE A 1 19  ? 7.417  -2.128  28.879 1.00 61.55  ? 18  ILE A O   1 
ATOM 92   C CB  . ILE A 1 19  ? 8.235  0.866   30.099 1.00 55.64  ? 18  ILE A CB  1 
ATOM 93   C CG1 . ILE A 1 19  ? 9.572  1.609   30.165 1.00 57.40  ? 18  ILE A CG1 1 
ATOM 94   C CG2 . ILE A 1 19  ? 8.135  -0.152  31.227 1.00 59.32  ? 18  ILE A CG2 1 
ATOM 95   C CD1 . ILE A 1 19  ? 9.755  2.437   31.423 1.00 63.79  ? 18  ILE A CD1 1 
ATOM 96   N N   . GLY A 1 20  ? 5.758  -0.617  28.710 1.00 60.07  ? 19  GLY A N   1 
ATOM 97   C CA  . GLY A 1 20  ? 4.736  -1.653  28.725 1.00 55.95  ? 19  GLY A CA  1 
ATOM 98   C C   . GLY A 1 20  ? 4.865  -2.622  27.566 1.00 56.52  ? 19  GLY A C   1 
ATOM 99   O O   . GLY A 1 20  ? 4.666  -3.829  27.728 1.00 57.78  ? 19  GLY A O   1 
ATOM 100  N N   . ALA A 1 21  ? 5.205  -2.110  26.381 1.00 61.02  ? 20  ALA A N   1 
ATOM 101  C CA  . ALA A 1 21  ? 5.409  -2.986  25.232 1.00 53.08  ? 20  ALA A CA  1 
ATOM 102  C C   . ALA A 1 21  ? 6.640  -3.862  25.420 1.00 49.98  ? 20  ALA A C   1 
ATOM 103  O O   . ALA A 1 21  ? 6.619  -5.051  25.081 1.00 53.55  ? 20  ALA A O   1 
ATOM 104  C CB  . ALA A 1 21  ? 5.530  -2.159  23.953 1.00 58.55  ? 20  ALA A CB  1 
ATOM 105  N N   . GLY A 1 22  ? 7.722  -3.293  25.957 1.00 43.39  ? 21  GLY A N   1 
ATOM 106  C CA  . GLY A 1 22  ? 8.916  -4.085  26.201 1.00 54.76  ? 21  GLY A CA  1 
ATOM 107  C C   . GLY A 1 22  ? 8.677  -5.201  27.198 1.00 61.33  ? 21  GLY A C   1 
ATOM 108  O O   . GLY A 1 22  ? 9.184  -6.315  27.035 1.00 55.44  ? 21  GLY A O   1 
ATOM 109  N N   . LEU A 1 23  ? 7.898  -4.919  28.245 1.00 54.29  ? 22  LEU A N   1 
ATOM 110  C CA  . LEU A 1 23  ? 7.521  -5.965  29.189 1.00 51.53  ? 22  LEU A CA  1 
ATOM 111  C C   . LEU A 1 23  ? 6.669  -7.028  28.510 1.00 48.85  ? 22  LEU A C   1 
ATOM 112  O O   . LEU A 1 23  ? 6.806  -8.223  28.798 1.00 47.35  ? 22  LEU A O   1 
ATOM 113  C CB  . LEU A 1 23  ? 6.776  -5.356  30.376 1.00 52.57  ? 22  LEU A CB  1 
ATOM 114  C CG  . LEU A 1 23  ? 7.579  -4.416  31.278 1.00 55.92  ? 22  LEU A CG  1 
ATOM 115  C CD1 . LEU A 1 23  ? 6.703  -3.870  32.397 1.00 46.46  ? 22  LEU A CD1 1 
ATOM 116  C CD2 . LEU A 1 23  ? 8.803  -5.124  31.845 1.00 52.16  ? 22  LEU A CD2 1 
ATOM 117  N N   . LEU A 1 24  ? 5.787  -6.611  27.602 1.00 46.54  ? 23  LEU A N   1 
ATOM 118  C CA  . LEU A 1 24  ? 4.954  -7.541  26.853 1.00 50.48  ? 23  LEU A CA  1 
ATOM 119  C C   . LEU A 1 24  ? 5.818  -8.469  26.010 1.00 45.73  ? 23  LEU A C   1 
ATOM 120  O O   . LEU A 1 24  ? 5.923  -9.662  26.308 1.00 51.18  ? 23  LEU A O   1 
ATOM 121  C CB  . LEU A 1 24  ? 3.965  -6.783  25.964 1.00 49.01  ? 23  LEU A CB  1 
ATOM 122  C CG  . LEU A 1 24  ? 2.883  -7.602  25.256 1.00 49.36  ? 23  LEU A CG  1 
ATOM 123  C CD1 . LEU A 1 24  ? 2.042  -8.368  26.260 1.00 53.49  ? 23  LEU A CD1 1 
ATOM 124  C CD2 . LEU A 1 24  ? 2.008  -6.696  24.408 1.00 48.90  ? 23  LEU A CD2 1 
ATOM 125  N N   . VAL A 1 25  ? 6.459  -7.922  24.973 1.00 40.25  ? 24  VAL A N   1 
ATOM 126  C CA  . VAL A 1 25  ? 7.224  -8.752  24.043 1.00 56.46  ? 24  VAL A CA  1 
ATOM 127  C C   . VAL A 1 25  ? 8.310  -9.536  24.767 1.00 48.54  ? 24  VAL A C   1 
ATOM 128  O O   . VAL A 1 25  ? 8.651  -10.653 24.360 1.00 48.72  ? 24  VAL A O   1 
ATOM 129  C CB  . VAL A 1 25  ? 7.810  -7.890  22.906 1.00 43.01  ? 24  VAL A CB  1 
ATOM 130  C CG1 . VAL A 1 25  ? 6.693  -7.203  22.136 1.00 37.90  ? 24  VAL A CG1 1 
ATOM 131  C CG2 . VAL A 1 25  ? 8.794  -6.867  23.456 1.00 57.04  ? 24  VAL A CG2 1 
ATOM 132  N N   . GLY A 1 26  ? 8.867  -8.979  25.845 1.00 41.60  ? 25  GLY A N   1 
ATOM 133  C CA  . GLY A 1 26  ? 9.825  -9.735  26.634 1.00 52.63  ? 25  GLY A CA  1 
ATOM 134  C C   . GLY A 1 26  ? 9.193  -10.944 27.295 1.00 43.19  ? 25  GLY A C   1 
ATOM 135  O O   . GLY A 1 26  ? 9.795  -12.019 27.355 1.00 38.10  ? 25  GLY A O   1 
ATOM 136  N N   . LYS A 1 27  ? 7.966  -10.783 27.795 1.00 38.78  ? 26  LYS A N   1 
ATOM 137  C CA  . LYS A 1 27  ? 7.239  -11.906 28.376 1.00 46.40  ? 26  LYS A CA  1 
ATOM 138  C C   . LYS A 1 27  ? 6.934  -12.962 27.322 1.00 44.53  ? 26  LYS A C   1 
ATOM 139  O O   . LYS A 1 27  ? 7.148  -14.160 27.545 1.00 47.09  ? 26  LYS A O   1 
ATOM 140  C CB  . LYS A 1 27  ? 5.950  -11.406 29.029 1.00 41.36  ? 26  LYS A CB  1 
ATOM 141  C CG  . LYS A 1 27  ? 4.981  -12.500 29.426 1.00 42.21  ? 26  LYS A CG  1 
ATOM 142  C CD  . LYS A 1 27  ? 5.524  -13.326 30.574 1.00 42.94  ? 26  LYS A CD  1 
ATOM 143  C CE  . LYS A 1 27  ? 4.410  -14.070 31.281 1.00 47.91  ? 26  LYS A CE  1 
ATOM 144  N NZ  . LYS A 1 27  ? 3.592  -13.136 32.088 1.00 56.92  ? 26  LYS A NZ  1 
ATOM 145  N N   . LEU A 1 28  ? 6.428  -12.533 26.162 1.00 41.70  ? 27  LEU A N   1 
ATOM 146  C CA  . LEU A 1 28  ? 6.125  -13.479 25.092 1.00 47.83  ? 27  LEU A CA  1 
ATOM 147  C C   . LEU A 1 28  ? 7.375  -14.226 24.646 1.00 43.78  ? 27  LEU A C   1 
ATOM 148  O O   . LEU A 1 28  ? 7.334  -15.443 24.425 1.00 42.55  ? 27  LEU A O   1 
ATOM 149  C CB  . LEU A 1 28  ? 5.483  -12.756 23.905 1.00 49.20  ? 27  LEU A CB  1 
ATOM 150  C CG  . LEU A 1 28  ? 3.994  -12.380 23.957 1.00 45.39  ? 27  LEU A CG  1 
ATOM 151  C CD1 . LEU A 1 28  ? 3.132  -13.608 24.213 1.00 46.50  ? 27  LEU A CD1 1 
ATOM 152  C CD2 . LEU A 1 28  ? 3.691  -11.290 24.974 1.00 56.74  ? 27  LEU A CD2 1 
ATOM 153  N N   . LEU A 1 29  ? 8.499  -13.516 24.516 1.00 44.71  ? 28  LEU A N   1 
ATOM 154  C CA  . LEU A 1 29  ? 9.749  -14.165 24.130 1.00 48.80  ? 28  LEU A CA  1 
ATOM 155  C C   . LEU A 1 29  ? 10.213 -15.163 25.182 1.00 55.41  ? 28  LEU A C   1 
ATOM 156  O O   . LEU A 1 29  ? 10.831 -16.179 24.844 1.00 52.44  ? 28  LEU A O   1 
ATOM 157  C CB  . LEU A 1 29  ? 10.827 -13.109 23.883 1.00 48.03  ? 28  LEU A CB  1 
ATOM 158  C CG  . LEU A 1 29  ? 12.167 -13.583 23.315 1.00 51.14  ? 28  LEU A CG  1 
ATOM 159  C CD1 . LEU A 1 29  ? 12.056 -13.840 21.821 1.00 59.28  ? 28  LEU A CD1 1 
ATOM 160  C CD2 . LEU A 1 29  ? 13.255 -12.561 23.602 1.00 54.78  ? 28  LEU A CD2 1 
ATOM 161  N N   . ALA A 1 30  ? 9.924  -14.896 26.458 1.00 50.86  ? 29  ALA A N   1 
ATOM 162  C CA  . ALA A 1 30  ? 10.349 -15.799 27.521 1.00 44.47  ? 29  ALA A CA  1 
ATOM 163  C C   . ALA A 1 30  ? 9.399  -16.977 27.690 1.00 52.45  ? 29  ALA A C   1 
ATOM 164  O O   . ALA A 1 30  ? 9.838  -18.071 28.060 1.00 54.11  ? 29  ALA A O   1 
ATOM 165  C CB  . ALA A 1 30  ? 10.475 -15.035 28.839 1.00 42.44  ? 29  ALA A CB  1 
ATOM 166  N N   . VAL A 1 31  ? 8.106  -16.781 27.432 1.00 45.86  ? 30  VAL A N   1 
ATOM 167  C CA  . VAL A 1 31  ? 7.156  -17.879 27.570 1.00 43.46  ? 30  VAL A CA  1 
ATOM 168  C C   . VAL A 1 31  ? 7.219  -18.802 26.359 1.00 58.70  ? 30  VAL A C   1 
ATOM 169  O O   . VAL A 1 31  ? 7.091  -20.025 26.488 1.00 58.48  ? 30  VAL A O   1 
ATOM 170  C CB  . VAL A 1 31  ? 5.738  -17.324 27.796 1.00 40.24  ? 30  VAL A CB  1 
ATOM 171  C CG1 . VAL A 1 31  ? 4.697  -18.432 27.709 1.00 39.44  ? 30  VAL A CG1 1 
ATOM 172  C CG2 . VAL A 1 31  ? 5.660  -16.638 29.144 1.00 45.74  ? 30  VAL A CG2 1 
ATOM 173  N N   . SER A 1 32  ? 7.440  -18.241 25.171 1.00 58.32  ? 31  SER A N   1 
ATOM 174  C CA  . SER A 1 32  ? 7.427  -19.053 23.959 1.00 61.21  ? 31  SER A CA  1 
ATOM 175  C C   . SER A 1 32  ? 8.735  -19.815 23.768 1.00 59.57  ? 31  SER A C   1 
ATOM 176  O O   . SER A 1 32  ? 8.721  -20.965 23.316 1.00 63.88  ? 31  SER A O   1 
ATOM 177  C CB  . SER A 1 32  ? 7.141  -18.171 22.743 1.00 60.03  ? 31  SER A CB  1 
ATOM 178  O OG  . SER A 1 32  ? 5.999  -17.359 22.959 1.00 61.13  ? 31  SER A OG  1 
ATOM 179  N N   . PHE A 1 33  ? 9.869  -19.203 24.111 1.00 52.30  ? 32  PHE A N   1 
ATOM 180  C CA  . PHE A 1 33  ? 11.172 -19.775 23.802 1.00 48.20  ? 32  PHE A CA  1 
ATOM 181  C C   . PHE A 1 33  ? 12.040 -20.035 25.026 1.00 48.08  ? 32  PHE A C   1 
ATOM 182  O O   . PHE A 1 33  ? 13.171 -20.511 24.870 1.00 47.11  ? 32  PHE A O   1 
ATOM 183  C CB  . PHE A 1 33  ? 11.925 -18.868 22.819 1.00 54.15  ? 32  PHE A CB  1 
ATOM 184  C CG  . PHE A 1 33  ? 11.065 -18.350 21.701 1.00 55.86  ? 32  PHE A CG  1 
ATOM 185  C CD1 . PHE A 1 33  ? 10.854 -19.114 20.567 1.00 51.52  ? 32  PHE A CD1 1 
ATOM 186  C CD2 . PHE A 1 33  ? 10.470 -17.100 21.783 1.00 51.82  ? 32  PHE A CD2 1 
ATOM 187  C CE1 . PHE A 1 33  ? 10.062 -18.648 19.537 1.00 51.93  ? 32  PHE A CE1 1 
ATOM 188  C CE2 . PHE A 1 33  ? 9.678  -16.626 20.754 1.00 50.46  ? 32  PHE A CE2 1 
ATOM 189  C CZ  . PHE A 1 33  ? 9.475  -17.401 19.628 1.00 55.56  ? 32  PHE A CZ  1 
ATOM 190  N N   . GLY A 1 34  ? 11.554 -19.735 26.229 1.00 41.51  ? 33  GLY A N   1 
ATOM 191  C CA  . GLY A 1 34  ? 12.230 -20.112 27.449 1.00 44.76  ? 33  GLY A CA  1 
ATOM 192  C C   . GLY A 1 34  ? 13.601 -19.490 27.614 1.00 41.54  ? 33  GLY A C   1 
ATOM 193  O O   . GLY A 1 34  ? 13.992 -18.578 26.879 1.00 54.41  ? 33  GLY A O   1 
ATOM 194  N N   . PRO A 1 35  ? 14.357 -19.976 28.603 1.00 45.49  ? 34  PRO A N   1 
ATOM 195  C CA  . PRO A 1 35  ? 15.702 -19.422 28.838 1.00 49.16  ? 34  PRO A CA  1 
ATOM 196  C C   . PRO A 1 35  ? 16.633 -19.550 27.647 1.00 50.22  ? 34  PRO A C   1 
ATOM 197  O O   . PRO A 1 35  ? 17.503 -18.691 27.462 1.00 53.12  ? 34  PRO A O   1 
ATOM 198  C CB  . PRO A 1 35  ? 16.205 -20.231 30.042 1.00 43.01  ? 34  PRO A CB  1 
ATOM 199  C CG  . PRO A 1 35  ? 14.962 -20.680 30.738 1.00 39.70  ? 34  PRO A CG  1 
ATOM 200  C CD  . PRO A 1 35  ? 13.960 -20.933 29.650 1.00 39.59  ? 34  PRO A CD  1 
ATOM 201  N N   . ALA A 1 36  ? 16.482 -20.596 26.832 1.00 49.52  ? 35  ALA A N   1 
ATOM 202  C CA  . ALA A 1 36  ? 17.325 -20.724 25.648 1.00 51.57  ? 35  ALA A CA  1 
ATOM 203  C C   . ALA A 1 36  ? 17.062 -19.593 24.663 1.00 49.44  ? 35  ALA A C   1 
ATOM 204  O O   . ALA A 1 36  ? 17.993 -19.077 24.034 1.00 48.83  ? 35  ALA A O   1 
ATOM 205  C CB  . ALA A 1 36  ? 17.099 -22.080 24.983 1.00 62.41  ? 35  ALA A CB  1 
ATOM 206  N N   . GLY A 1 37  ? 15.799 -19.186 24.523 1.00 56.55  ? 36  GLY A N   1 
ATOM 207  C CA  . GLY A 1 37  ? 15.481 -18.101 23.611 1.00 55.23  ? 36  GLY A CA  1 
ATOM 208  C C   . GLY A 1 37  ? 15.913 -16.746 24.138 1.00 57.62  ? 36  GLY A C   1 
ATOM 209  O O   . GLY A 1 37  ? 16.464 -15.928 23.395 1.00 53.59  ? 36  GLY A O   1 
ATOM 210  N N   . LEU A 1 38  ? 15.672 -16.488 25.426 1.00 50.33  ? 37  LEU A N   1 
ATOM 211  C CA  . LEU A 1 38  ? 16.069 -15.209 26.004 1.00 50.54  ? 37  LEU A CA  1 
ATOM 212  C C   . LEU A 1 38  ? 17.583 -15.052 26.039 1.00 48.39  ? 37  LEU A C   1 
ATOM 213  O O   . LEU A 1 38  ? 18.090 -13.928 25.960 1.00 56.03  ? 37  LEU A O   1 
ATOM 214  C CB  . LEU A 1 38  ? 15.489 -15.061 27.409 1.00 55.84  ? 37  LEU A CB  1 
ATOM 215  C CG  . LEU A 1 38  ? 15.057 -13.643 27.788 1.00 53.99  ? 37  LEU A CG  1 
ATOM 216  C CD1 . LEU A 1 38  ? 13.690 -13.316 27.200 1.00 55.30  ? 37  LEU A CD1 1 
ATOM 217  C CD2 . LEU A 1 38  ? 15.053 -13.471 29.297 1.00 49.49  ? 37  LEU A CD2 1 
ATOM 218  N N   . GLY A 1 39  ? 18.317 -16.155 26.157 1.00 48.49  ? 38  GLY A N   1 
ATOM 219  C CA  . GLY A 1 39  ? 19.764 -16.094 26.159 1.00 48.08  ? 38  GLY A CA  1 
ATOM 220  C C   . GLY A 1 39  ? 20.340 -15.919 24.771 1.00 53.12  ? 38  GLY A C   1 
ATOM 221  O O   . GLY A 1 39  ? 21.312 -15.182 24.582 1.00 61.03  ? 38  GLY A O   1 
ATOM 222  N N   . LEU A 1 40  ? 19.740 -16.592 23.785 1.00 57.28  ? 39  LEU A N   1 
ATOM 223  C CA  . LEU A 1 40  ? 20.244 -16.506 22.418 1.00 52.58  ? 39  LEU A CA  1 
ATOM 224  C C   . LEU A 1 40  ? 19.896 -15.167 21.780 1.00 48.83  ? 39  LEU A C   1 
ATOM 225  O O   . LEU A 1 40  ? 20.713 -14.589 21.054 1.00 51.09  ? 39  LEU A O   1 
ATOM 226  C CB  . LEU A 1 40  ? 19.690 -17.658 21.582 1.00 50.62  ? 39  LEU A CB  1 
ATOM 227  C CG  . LEU A 1 40  ? 20.692 -18.692 21.066 1.00 48.40  ? 39  LEU A CG  1 
ATOM 228  C CD1 . LEU A 1 40  ? 19.981 -19.731 20.215 1.00 48.41  ? 39  LEU A CD1 1 
ATOM 229  C CD2 . LEU A 1 40  ? 21.814 -18.027 20.283 1.00 42.88  ? 39  LEU A CD2 1 
ATOM 230  N N   . ALA A 1 41  ? 18.689 -14.658 22.038 1.00 55.81  ? 40  ALA A N   1 
ATOM 231  C CA  . ALA A 1 41  ? 18.273 -13.372 21.491 1.00 48.01  ? 40  ALA A CA  1 
ATOM 232  C C   . ALA A 1 41  ? 18.979 -12.193 22.142 1.00 48.56  ? 40  ALA A C   1 
ATOM 233  O O   . ALA A 1 41  ? 18.883 -11.076 21.623 1.00 56.30  ? 40  ALA A O   1 
ATOM 234  C CB  . ALA A 1 41  ? 16.761 -13.198 21.643 1.00 41.02  ? 40  ALA A CB  1 
ATOM 235  N N   . ALA A 1 42  ? 19.677 -12.412 23.259 1.00 54.51  ? 41  ALA A N   1 
ATOM 236  C CA  . ALA A 1 42  ? 20.285 -11.301 23.984 1.00 60.21  ? 41  ALA A CA  1 
ATOM 237  C C   . ALA A 1 42  ? 21.347 -10.602 23.146 1.00 56.57  ? 41  ALA A C   1 
ATOM 238  O O   . ALA A 1 42  ? 21.432 -9.369  23.141 1.00 60.51  ? 41  ALA A O   1 
ATOM 239  C CB  . ALA A 1 42  ? 20.884 -11.802 25.295 1.00 54.28  ? 41  ALA A CB  1 
ATOM 240  N N   . ASN A 1 43  ? 22.170 -11.373 22.432 1.00 50.19  ? 42  ASN A N   1 
ATOM 241  C CA  . ASN A 1 43  ? 23.190 -10.765 21.586 1.00 53.68  ? 42  ASN A CA  1 
ATOM 242  C C   . ASN A 1 43  ? 22.563 -10.028 20.410 1.00 59.59  ? 42  ASN A C   1 
ATOM 243  O O   . ASN A 1 43  ? 23.073 -8.988  19.978 1.00 50.25  ? 42  ASN A O   1 
ATOM 244  C CB  . ASN A 1 43  ? 24.168 -11.830 21.094 1.00 53.99  ? 42  ASN A CB  1 
ATOM 245  C CG  . ASN A 1 43  ? 25.246 -12.141 22.110 1.00 57.04  ? 42  ASN A CG  1 
ATOM 246  O OD1 . ASN A 1 43  ? 25.561 -11.317 22.968 1.00 58.36  ? 42  ASN A OD1 1 
ATOM 247  N ND2 . ASN A 1 43  ? 25.821 -13.335 22.018 1.00 56.87  ? 42  ASN A ND2 1 
ATOM 248  N N   . PHE A 1 44  ? 21.456 -10.551 19.879 1.00 65.07  ? 43  PHE A N   1 
ATOM 249  C CA  . PHE A 1 44  ? 20.787 -9.886  18.765 1.00 54.29  ? 43  PHE A CA  1 
ATOM 250  C C   . PHE A 1 44  ? 20.110 -8.600  19.218 1.00 52.65  ? 43  PHE A C   1 
ATOM 251  O O   . PHE A 1 44  ? 20.146 -7.589  18.506 1.00 49.87  ? 43  PHE A O   1 
ATOM 252  C CB  . PHE A 1 44  ? 19.771 -10.830 18.126 1.00 50.32  ? 43  PHE A CB  1 
ATOM 253  C CG  . PHE A 1 44  ? 19.209 -10.323 16.833 1.00 39.98  ? 43  PHE A CG  1 
ATOM 254  C CD1 . PHE A 1 44  ? 20.025 -10.159 15.726 1.00 37.58  ? 43  PHE A CD1 1 
ATOM 255  C CD2 . PHE A 1 44  ? 17.866 -10.009 16.723 1.00 40.62  ? 43  PHE A CD2 1 
ATOM 256  C CE1 . PHE A 1 44  ? 19.509 -9.693  14.531 1.00 37.51  ? 43  PHE A CE1 1 
ATOM 257  C CE2 . PHE A 1 44  ? 17.345 -9.543  15.531 1.00 39.56  ? 43  PHE A CE2 1 
ATOM 258  C CZ  . PHE A 1 44  ? 18.168 -9.385  14.434 1.00 37.37  ? 43  PHE A CZ  1 
ATOM 259  N N   . ARG A 1 45  ? 19.483 -8.622  20.397 1.00 56.02  ? 44  ARG A N   1 
ATOM 260  C CA  . ARG A 1 45  ? 18.891 -7.407  20.946 1.00 55.22  ? 44  ARG A CA  1 
ATOM 261  C C   . ARG A 1 45  ? 19.950 -6.342  21.196 1.00 54.17  ? 44  ARG A C   1 
ATOM 262  O O   . ARG A 1 45  ? 19.647 -5.144  21.170 1.00 57.50  ? 44  ARG A O   1 
ATOM 263  C CB  . ARG A 1 45  ? 18.142 -7.731  22.238 1.00 59.09  ? 44  ARG A CB  1 
ATOM 264  C CG  . ARG A 1 45  ? 16.665 -7.368  22.230 1.00 66.21  ? 44  ARG A CG  1 
ATOM 265  C CD  . ARG A 1 45  ? 15.933 -8.083  23.360 1.00 77.52  ? 44  ARG A CD  1 
ATOM 266  N NE  . ARG A 1 45  ? 14.718 -7.388  23.768 1.00 88.55  ? 44  ARG A NE  1 
ATOM 267  C CZ  . ARG A 1 45  ? 13.879 -7.830  24.696 1.00 81.94  ? 44  ARG A CZ  1 
ATOM 268  N NH1 . ARG A 1 45  ? 14.089 -8.971  25.331 1.00 77.03  ? 44  ARG A NH1 1 
ATOM 269  N NH2 . ARG A 1 45  ? 12.803 -7.107  24.996 1.00 65.28  ? 44  ARG A NH2 1 
ATOM 270  N N   . GLN A 1 46  ? 21.195 -6.759  21.428 1.00 44.82  ? 45  GLN A N   1 
ATOM 271  C CA  . GLN A 1 46  ? 22.277 -5.803  21.630 1.00 50.56  ? 45  GLN A CA  1 
ATOM 272  C C   . GLN A 1 46  ? 22.600 -5.057  20.342 1.00 57.67  ? 45  GLN A C   1 
ATOM 273  O O   . GLN A 1 46  ? 22.782 -3.833  20.350 1.00 47.60  ? 45  GLN A O   1 
ATOM 274  C CB  . GLN A 1 46  ? 23.509 -6.532  22.157 1.00 43.17  ? 45  GLN A CB  1 
ATOM 275  C CG  . GLN A 1 46  ? 24.617 -5.631  22.640 1.00 64.12  ? 45  GLN A CG  1 
ATOM 276  C CD  . GLN A 1 46  ? 24.510 -5.386  24.129 1.00 62.23  ? 45  GLN A CD  1 
ATOM 277  O OE1 . GLN A 1 46  ? 23.420 -5.158  24.649 1.00 62.13  ? 45  GLN A OE1 1 
ATOM 278  N NE2 . GLN A 1 46  ? 25.621 -5.498  24.827 1.00 61.50  ? 45  GLN A NE2 1 
ATOM 279  N N   . LEU A 1 47  ? 22.677 -5.783  19.221 1.00 53.39  ? 46  LEU A N   1 
ATOM 280  C CA  . LEU A 1 47  ? 22.960 -5.147  17.939 1.00 43.44  ? 46  LEU A CA  1 
ATOM 281  C C   . LEU A 1 47  ? 21.883 -4.139  17.567 1.00 47.72  ? 46  LEU A C   1 
ATOM 282  O O   . LEU A 1 47  ? 22.178 -3.120  16.934 1.00 50.90  ? 46  LEU A O   1 
ATOM 283  C CB  . LEU A 1 47  ? 23.096 -6.208  16.846 1.00 47.35  ? 46  LEU A CB  1 
ATOM 284  C CG  . LEU A 1 47  ? 23.303 -5.710  15.411 1.00 54.25  ? 46  LEU A CG  1 
ATOM 285  C CD1 . LEU A 1 47  ? 24.684 -5.094  15.242 1.00 48.36  ? 46  LEU A CD1 1 
ATOM 286  C CD2 . LEU A 1 47  ? 23.090 -6.835  14.408 1.00 39.29  ? 46  LEU A CD2 1 
ATOM 287  N N   . ILE A 1 48  ? 20.638 -4.400  17.963 1.00 40.92  ? 47  ILE A N   1 
ATOM 288  C CA  . ILE A 1 48  ? 19.544 -3.480  17.670 1.00 40.11  ? 47  ILE A CA  1 
ATOM 289  C C   . ILE A 1 48  ? 19.768 -2.147  18.371 1.00 56.31  ? 47  ILE A C   1 
ATOM 290  O O   . ILE A 1 48  ? 19.705 -1.079  17.751 1.00 55.01  ? 47  ILE A O   1 
ATOM 291  C CB  . ILE A 1 48  ? 18.208 -4.109  18.093 1.00 42.25  ? 47  ILE A CB  1 
ATOM 292  C CG1 . ILE A 1 48  ? 17.792 -5.173  17.090 1.00 51.80  ? 47  ILE A CG1 1 
ATOM 293  C CG2 . ILE A 1 48  ? 17.133 -3.038  18.216 1.00 49.83  ? 47  ILE A CG2 1 
ATOM 294  C CD1 . ILE A 1 48  ? 16.364 -5.553  17.228 1.00 52.77  ? 47  ILE A CD1 1 
ATOM 295  N N   . THR A 1 49  ? 20.018 -2.194  19.682 1.00 57.19  ? 48  THR A N   1 
ATOM 296  C CA  . THR A 1 49  ? 20.199 -0.965  20.445 1.00 54.68  ? 48  THR A CA  1 
ATOM 297  C C   . THR A 1 49  ? 21.384 -0.164  19.924 1.00 54.97  ? 48  THR A C   1 
ATOM 298  O O   . THR A 1 49  ? 21.354 1.072   19.919 1.00 50.12  ? 48  THR A O   1 
ATOM 299  C CB  . THR A 1 49  ? 20.379 -1.292  21.925 1.00 53.27  ? 48  THR A CB  1 
ATOM 300  O OG1 . THR A 1 49  ? 21.508 -2.161  22.085 1.00 59.91  ? 48  THR A OG1 1 
ATOM 301  C CG2 . THR A 1 49  ? 19.137 -1.981  22.464 1.00 47.23  ? 48  THR A CG2 1 
ATOM 302  N N   . VAL A 1 50  ? 22.435 -0.852  19.474 1.00 54.84  ? 49  VAL A N   1 
ATOM 303  C CA  . VAL A 1 50  ? 23.571 -0.161  18.872 1.00 58.81  ? 49  VAL A CA  1 
ATOM 304  C C   . VAL A 1 50  ? 23.145 0.535   17.587 1.00 63.60  ? 49  VAL A C   1 
ATOM 305  O O   . VAL A 1 50  ? 23.548 1.674   17.316 1.00 64.85  ? 49  VAL A O   1 
ATOM 306  C CB  . VAL A 1 50  ? 24.727 -1.150  18.631 1.00 57.17  ? 49  VAL A CB  1 
ATOM 307  C CG1 . VAL A 1 50  ? 25.623 -0.672  17.499 1.00 55.64  ? 49  VAL A CG1 1 
ATOM 308  C CG2 . VAL A 1 50  ? 25.528 -1.336  19.903 1.00 60.81  ? 49  VAL A CG2 1 
ATOM 309  N N   . LEU A 1 51  ? 22.316 -0.132  16.778 1.00 58.05  ? 50  LEU A N   1 
ATOM 310  C CA  . LEU A 1 51  ? 21.827 0.483   15.548 1.00 61.63  ? 50  LEU A CA  1 
ATOM 311  C C   . LEU A 1 51  ? 21.007 1.732   15.850 1.00 68.35  ? 50  LEU A C   1 
ATOM 312  O O   . LEU A 1 51  ? 21.200 2.781   15.226 1.00 69.56  ? 50  LEU A O   1 
ATOM 313  C CB  . LEU A 1 51  ? 21.005 -0.528  14.745 1.00 53.83  ? 50  LEU A CB  1 
ATOM 314  C CG  . LEU A 1 51  ? 21.802 -1.681  14.128 1.00 53.42  ? 50  LEU A CG  1 
ATOM 315  C CD1 . LEU A 1 51  ? 20.872 -2.699  13.483 1.00 44.87  ? 50  LEU A CD1 1 
ATOM 316  C CD2 . LEU A 1 51  ? 22.817 -1.156  13.126 1.00 58.33  ? 50  LEU A CD2 1 
ATOM 317  N N   . GLY A 1 52  ? 20.092 1.641   16.819 1.00 59.20  ? 51  GLY A N   1 
ATOM 318  C CA  . GLY A 1 52  ? 19.400 2.828   17.291 1.00 63.43  ? 51  GLY A CA  1 
ATOM 319  C C   . GLY A 1 52  ? 20.335 3.920   17.766 1.00 67.60  ? 51  GLY A C   1 
ATOM 320  O O   . GLY A 1 52  ? 19.970 5.098   17.737 1.00 67.99  ? 51  GLY A O   1 
ATOM 321  N N   . VAL A 1 53  ? 21.545 3.555   18.182 1.00 65.10  ? 52  VAL A N   1 
ATOM 322  C CA  . VAL A 1 53  ? 22.540 4.531   18.604 1.00 60.51  ? 52  VAL A CA  1 
ATOM 323  C C   . VAL A 1 53  ? 23.378 5.037   17.428 1.00 70.66  ? 52  VAL A C   1 
ATOM 324  O O   . VAL A 1 53  ? 23.851 6.177   17.455 1.00 68.79  ? 52  VAL A O   1 
ATOM 325  C CB  . VAL A 1 53  ? 23.418 3.903   19.707 1.00 60.64  ? 52  VAL A CB  1 
ATOM 326  C CG1 . VAL A 1 53  ? 24.783 4.579   19.811 1.00 64.49  ? 52  VAL A CG1 1 
ATOM 327  C CG2 . VAL A 1 53  ? 22.695 3.940   21.050 1.00 51.43  ? 52  VAL A CG2 1 
ATOM 328  N N   . LEU A 1 54  ? 23.536 4.234   16.369 1.00 72.54  ? 53  LEU A N   1 
ATOM 329  C CA  . LEU A 1 54  ? 24.550 4.506   15.354 1.00 67.49  ? 53  LEU A CA  1 
ATOM 330  C C   . LEU A 1 54  ? 24.090 4.363   13.905 1.00 75.74  ? 53  LEU A C   1 
ATOM 331  O O   . LEU A 1 54  ? 24.797 4.851   13.018 1.00 79.06  ? 53  LEU A O   1 
ATOM 332  C CB  . LEU A 1 54  ? 25.764 3.585   15.577 1.00 62.14  ? 53  LEU A CB  1 
ATOM 333  C CG  . LEU A 1 54  ? 27.086 3.894   14.870 1.00 65.75  ? 53  LEU A CG  1 
ATOM 334  C CD1 . LEU A 1 54  ? 27.805 5.052   15.536 1.00 65.28  ? 53  LEU A CD1 1 
ATOM 335  C CD2 . LEU A 1 54  ? 27.974 2.660   14.840 1.00 69.00  ? 53  LEU A CD2 1 
ATOM 336  N N   . ALA A 1 55  ? 22.944 3.728   13.632 1.00 86.50  ? 54  ALA A N   1 
ATOM 337  C CA  . ALA A 1 55  ? 22.578 3.431   12.245 1.00 85.77  ? 54  ALA A CA  1 
ATOM 338  C C   . ALA A 1 55  ? 22.480 4.697   11.401 1.00 87.44  ? 54  ALA A C   1 
ATOM 339  O O   . ALA A 1 55  ? 22.852 4.693   10.221 1.00 87.67  ? 54  ALA A O   1 
ATOM 340  C CB  . ALA A 1 55  ? 21.260 2.655   12.194 1.00 83.00  ? 54  ALA A CB  1 
ATOM 341  N N   . GLY A 1 56  ? 21.983 5.785   11.981 1.00 88.69  ? 55  GLY A N   1 
ATOM 342  C CA  . GLY A 1 56  ? 21.942 7.050   11.275 1.00 77.57  ? 55  GLY A CA  1 
ATOM 343  C C   . GLY A 1 56  ? 23.126 7.926   11.617 1.00 73.86  ? 55  GLY A C   1 
ATOM 344  O O   . GLY A 1 56  ? 22.983 9.140   11.790 1.00 65.51  ? 55  GLY A O   1 
ATOM 345  N N   . ALA A 1 57  ? 24.300 7.304   11.727 1.00 77.50  ? 56  ALA A N   1 
ATOM 346  C CA  . ALA A 1 57  ? 25.554 7.932   12.134 1.00 75.30  ? 56  ALA A CA  1 
ATOM 347  C C   . ALA A 1 57  ? 25.509 8.479   13.557 1.00 77.93  ? 56  ALA A C   1 
ATOM 348  O O   . ALA A 1 57  ? 26.470 9.115   13.998 1.00 65.48  ? 56  ALA A O   1 
ATOM 349  C CB  . ALA A 1 57  ? 25.977 9.041   11.160 1.00 60.32  ? 56  ALA A CB  1 
ATOM 350  N N   . GLY A 1 58  ? 24.424 8.242   14.289 1.00 85.37  ? 57  GLY A N   1 
ATOM 351  C CA  . GLY A 1 58  ? 24.335 8.699   15.668 1.00 85.72  ? 57  GLY A CA  1 
ATOM 352  C C   . GLY A 1 58  ? 24.462 10.197  15.839 1.00 87.50  ? 57  GLY A C   1 
ATOM 353  O O   . GLY A 1 58  ? 25.102 10.659  16.792 1.00 89.34  ? 57  GLY A O   1 
ATOM 354  N N   . ILE A 1 59  ? 23.866 10.972  14.930 1.00 86.42  ? 58  ILE A N   1 
ATOM 355  C CA  . ILE A 1 59  ? 23.921 12.427  14.996 1.00 80.32  ? 58  ILE A CA  1 
ATOM 356  C C   . ILE A 1 59  ? 22.644 13.030  15.561 1.00 83.14  ? 58  ILE A C   1 
ATOM 357  O O   . ILE A 1 59  ? 22.545 14.260  15.664 1.00 82.47  ? 58  ILE A O   1 
ATOM 358  C CB  . ILE A 1 59  ? 24.214 13.027  13.606 1.00 70.59  ? 58  ILE A CB  1 
ATOM 359  C CG1 . ILE A 1 59  ? 23.077 12.694  12.638 1.00 64.00  ? 58  ILE A CG1 1 
ATOM 360  C CG2 . ILE A 1 59  ? 25.540 12.512  13.067 1.00 61.44  ? 58  ILE A CG2 1 
ATOM 361  C CD1 . ILE A 1 59  ? 23.328 13.155  11.225 1.00 58.03  ? 58  ILE A CD1 1 
ATOM 362  N N   . PHE A 1 60  ? 21.677 12.198  15.958 1.00 105.36 ? 59  PHE A N   1 
ATOM 363  C CA  . PHE A 1 60  ? 20.328 12.682  16.241 1.00 104.39 ? 59  PHE A CA  1 
ATOM 364  C C   . PHE A 1 60  ? 20.305 13.661  17.409 1.00 103.45 ? 59  PHE A C   1 
ATOM 365  O O   . PHE A 1 60  ? 19.546 14.637  17.392 1.00 102.84 ? 59  PHE A O   1 
ATOM 366  C CB  . PHE A 1 60  ? 19.405 11.495  16.507 1.00 104.32 ? 59  PHE A CB  1 
ATOM 367  C CG  . PHE A 1 60  ? 19.547 10.388  15.503 1.00 108.03 ? 59  PHE A CG  1 
ATOM 368  C CD1 . PHE A 1 60  ? 19.148 10.574  14.190 1.00 102.39 ? 59  PHE A CD1 1 
ATOM 369  C CD2 . PHE A 1 60  ? 20.089 9.166   15.867 1.00 111.89 ? 59  PHE A CD2 1 
ATOM 370  C CE1 . PHE A 1 60  ? 19.281 9.562   13.260 1.00 102.52 ? 59  PHE A CE1 1 
ATOM 371  C CE2 . PHE A 1 60  ? 20.225 8.149   14.941 1.00 103.67 ? 59  PHE A CE2 1 
ATOM 372  C CZ  . PHE A 1 60  ? 19.819 8.348   13.637 1.00 103.79 ? 59  PHE A CZ  1 
ATOM 373  N N   . ASN A 1 61  ? 21.118 13.417  18.438 1.00 90.43  ? 60  ASN A N   1 
ATOM 374  C CA  . ASN A 1 61  ? 21.198 14.385  19.527 1.00 84.20  ? 60  ASN A CA  1 
ATOM 375  C C   . ASN A 1 61  ? 21.881 15.668  19.075 1.00 80.63  ? 60  ASN A C   1 
ATOM 376  O O   . ASN A 1 61  ? 21.519 16.757  19.533 1.00 71.70  ? 60  ASN A O   1 
ATOM 377  C CB  . ASN A 1 61  ? 21.919 13.775  20.727 1.00 74.37  ? 60  ASN A CB  1 
ATOM 378  C CG  . ASN A 1 61  ? 20.972 13.044  21.657 1.00 81.27  ? 60  ASN A CG  1 
ATOM 379  O OD1 . ASN A 1 61  ? 20.895 11.816  21.645 1.00 80.55  ? 60  ASN A OD1 1 
ATOM 380  N ND2 . ASN A 1 61  ? 20.233 13.801  22.460 1.00 84.89  ? 60  ASN A ND2 1 
ATOM 381  N N   . GLY A 1 62  ? 22.861 15.564  18.176 1.00 76.96  ? 61  GLY A N   1 
ATOM 382  C CA  . GLY A 1 62  ? 23.389 16.756  17.540 1.00 69.57  ? 61  GLY A CA  1 
ATOM 383  C C   . GLY A 1 62  ? 22.394 17.396  16.594 1.00 72.83  ? 61  GLY A C   1 
ATOM 384  O O   . GLY A 1 62  ? 22.453 18.606  16.353 1.00 70.93  ? 61  GLY A O   1 
ATOM 385  N N   . VAL A 1 63  ? 21.474 16.601  16.043 1.00 79.15  ? 62  VAL A N   1 
ATOM 386  C CA  . VAL A 1 63  ? 20.426 17.152  15.189 1.00 69.75  ? 62  VAL A CA  1 
ATOM 387  C C   . VAL A 1 63  ? 19.477 18.021  16.004 1.00 63.85  ? 62  VAL A C   1 
ATOM 388  O O   . VAL A 1 63  ? 19.262 19.195  15.688 1.00 65.81  ? 62  VAL A O   1 
ATOM 389  C CB  . VAL A 1 63  ? 19.667 16.028  14.461 1.00 71.57  ? 62  VAL A CB  1 
ATOM 390  C CG1 . VAL A 1 63  ? 18.465 16.600  13.738 1.00 59.19  ? 62  VAL A CG1 1 
ATOM 391  C CG2 . VAL A 1 63  ? 20.577 15.316  13.476 1.00 69.03  ? 62  VAL A CG2 1 
ATOM 392  N N   . THR A 1 64  ? 18.900 17.458  17.070 1.00 73.20  ? 63  THR A N   1 
ATOM 393  C CA  . THR A 1 64  ? 17.941 18.203  17.881 1.00 72.78  ? 63  THR A CA  1 
ATOM 394  C C   . THR A 1 64  ? 18.563 19.418  18.559 1.00 64.81  ? 63  THR A C   1 
ATOM 395  O O   . THR A 1 64  ? 17.843 20.373  18.867 1.00 60.20  ? 63  THR A O   1 
ATOM 396  C CB  . THR A 1 64  ? 17.307 17.285  18.930 1.00 65.55  ? 63  THR A CB  1 
ATOM 397  O OG1 . THR A 1 64  ? 16.305 18.004  19.659 1.00 71.10  ? 63  THR A OG1 1 
ATOM 398  C CG2 . THR A 1 64  ? 18.351 16.767  19.904 1.00 65.46  ? 63  THR A CG2 1 
ATOM 399  N N   . LYS A 1 65  ? 19.879 19.415  18.784 1.00 64.61  ? 64  LYS A N   1 
ATOM 400  C CA  . LYS A 1 65  ? 20.530 20.573  19.389 1.00 60.56  ? 64  LYS A CA  1 
ATOM 401  C C   . LYS A 1 65  ? 20.651 21.718  18.391 1.00 62.45  ? 64  LYS A C   1 
ATOM 402  O O   . LYS A 1 65  ? 20.158 22.826  18.635 1.00 70.06  ? 64  LYS A O   1 
ATOM 403  C CB  . LYS A 1 65  ? 21.909 20.186  19.930 1.00 61.20  ? 64  LYS A CB  1 
ATOM 404  C CG  . LYS A 1 65  ? 22.804 21.382  20.240 1.00 80.68  ? 64  LYS A CG  1 
ATOM 405  C CD  . LYS A 1 65  ? 24.225 20.957  20.578 1.00 84.47  ? 64  LYS A CD  1 
ATOM 406  C CE  . LYS A 1 65  ? 25.104 22.169  20.843 1.00 89.12  ? 64  LYS A CE  1 
ATOM 407  N NZ  . LYS A 1 65  ? 26.492 21.785  21.212 1.00 98.18  ? 64  LYS A NZ  1 
ATOM 408  N N   . TYR A 1 66  ? 21.313 21.469  17.257 1.00 67.03  ? 65  TYR A N   1 
ATOM 409  C CA  . TYR A 1 66  ? 21.522 22.515  16.261 1.00 65.57  ? 65  TYR A CA  1 
ATOM 410  C C   . TYR A 1 66  ? 20.231 22.933  15.576 1.00 58.34  ? 65  TYR A C   1 
ATOM 411  O O   . TYR A 1 66  ? 20.164 24.040  15.032 1.00 54.50  ? 65  TYR A O   1 
ATOM 412  C CB  . TYR A 1 66  ? 22.536 22.051  15.217 1.00 57.81  ? 65  TYR A CB  1 
ATOM 413  C CG  . TYR A 1 66  ? 23.947 22.030  15.738 1.00 67.10  ? 65  TYR A CG  1 
ATOM 414  C CD1 . TYR A 1 66  ? 24.474 23.129  16.402 1.00 74.94  ? 65  TYR A CD1 1 
ATOM 415  C CD2 . TYR A 1 66  ? 24.751 20.910  15.579 1.00 68.25  ? 65  TYR A CD2 1 
ATOM 416  C CE1 . TYR A 1 66  ? 25.765 23.117  16.889 1.00 83.90  ? 65  TYR A CE1 1 
ATOM 417  C CE2 . TYR A 1 66  ? 26.045 20.889  16.062 1.00 79.03  ? 65  TYR A CE2 1 
ATOM 418  C CZ  . TYR A 1 66  ? 26.547 21.995  16.716 1.00 93.98  ? 65  TYR A CZ  1 
ATOM 419  O OH  . TYR A 1 66  ? 27.835 21.978  17.199 1.00 104.66 ? 65  TYR A OH  1 
ATOM 420  N N   . VAL A 1 67  ? 19.215 22.072  15.580 1.00 55.06  ? 66  VAL A N   1 
ATOM 421  C CA  . VAL A 1 67  ? 17.916 22.453  15.036 1.00 50.60  ? 66  VAL A CA  1 
ATOM 422  C C   . VAL A 1 67  ? 17.281 23.541  15.891 1.00 54.25  ? 66  VAL A C   1 
ATOM 423  O O   . VAL A 1 67  ? 16.763 24.536  15.372 1.00 59.53  ? 66  VAL A O   1 
ATOM 424  C CB  . VAL A 1 67  ? 17.003 21.221  14.920 1.00 54.36  ? 66  VAL A CB  1 
ATOM 425  C CG1 . VAL A 1 67  ? 15.564 21.632  15.047 1.00 46.23  ? 66  VAL A CG1 1 
ATOM 426  C CG2 . VAL A 1 67  ? 17.229 20.526  13.588 1.00 45.80  ? 66  VAL A CG2 1 
ATOM 427  N N   . ALA A 1 68  ? 17.313 23.368  17.214 1.00 62.84  ? 67  ALA A N   1 
ATOM 428  C CA  . ALA A 1 68  ? 16.782 24.390  18.109 1.00 59.19  ? 67  ALA A CA  1 
ATOM 429  C C   . ALA A 1 68  ? 17.586 25.681  18.005 1.00 57.87  ? 67  ALA A C   1 
ATOM 430  O O   . ALA A 1 68  ? 17.028 26.780  18.111 1.00 52.20  ? 67  ALA A O   1 
ATOM 431  C CB  . ALA A 1 68  ? 16.773 23.866  19.544 1.00 62.05  ? 67  ALA A CB  1 
ATOM 432  N N   . GLN A 1 69  ? 18.899 25.565  17.785 1.00 53.55  ? 68  GLN A N   1 
ATOM 433  C CA  . GLN A 1 69  ? 19.737 26.751  17.641 1.00 58.60  ? 68  GLN A CA  1 
ATOM 434  C C   . GLN A 1 69  ? 19.313 27.587  16.442 1.00 50.52  ? 68  GLN A C   1 
ATOM 435  O O   . GLN A 1 69  ? 19.297 28.821  16.512 1.00 55.17  ? 68  GLN A O   1 
ATOM 436  C CB  . GLN A 1 69  ? 21.205 26.345  17.503 1.00 57.41  ? 68  GLN A CB  1 
ATOM 437  C CG  . GLN A 1 69  ? 21.888 25.968  18.804 1.00 68.32  ? 68  GLN A CG  1 
ATOM 438  C CD  . GLN A 1 69  ? 23.396 26.116  18.730 1.00 78.32  ? 68  GLN A CD  1 
ATOM 439  O OE1 . GLN A 1 69  ? 23.936 26.614  17.740 1.00 63.06  ? 68  GLN A OE1 1 
ATOM 440  N NE2 . GLN A 1 69  ? 24.085 25.676  19.776 1.00 91.11  ? 68  GLN A NE2 1 
ATOM 441  N N   . TYR A 1 70  ? 18.961 26.932  15.332 1.00 58.67  ? 69  TYR A N   1 
ATOM 442  C CA  . TYR A 1 70  ? 18.689 27.613  14.071 1.00 56.81  ? 69  TYR A CA  1 
ATOM 443  C C   . TYR A 1 70  ? 17.252 27.422  13.596 1.00 53.84  ? 69  TYR A C   1 
ATOM 444  O O   . TYR A 1 70  ? 16.967 27.631  12.414 1.00 60.96  ? 69  TYR A O   1 
ATOM 445  C CB  . TYR A 1 70  ? 19.661 27.135  12.992 1.00 58.45  ? 69  TYR A CB  1 
ATOM 446  C CG  . TYR A 1 70  ? 21.118 27.300  13.354 1.00 56.76  ? 69  TYR A CG  1 
ATOM 447  C CD1 . TYR A 1 70  ? 21.621 28.529  13.758 1.00 61.98  ? 69  TYR A CD1 1 
ATOM 448  C CD2 . TYR A 1 70  ? 21.993 26.224  13.286 1.00 63.60  ? 69  TYR A CD2 1 
ATOM 449  C CE1 . TYR A 1 70  ? 22.955 28.681  14.087 1.00 69.18  ? 69  TYR A CE1 1 
ATOM 450  C CE2 . TYR A 1 70  ? 23.327 26.366  13.613 1.00 63.79  ? 69  TYR A CE2 1 
ATOM 451  C CZ  . TYR A 1 70  ? 23.803 27.594  14.012 1.00 60.88  ? 69  TYR A CZ  1 
ATOM 452  O OH  . TYR A 1 70  ? 25.132 27.732  14.337 1.00 71.33  ? 69  TYR A OH  1 
ATOM 453  N N   . HIS A 1 71  ? 16.337 27.038  14.489 1.00 55.77  ? 70  HIS A N   1 
ATOM 454  C CA  . HIS A 1 71  ? 14.935 26.912  14.104 1.00 61.01  ? 70  HIS A CA  1 
ATOM 455  C C   . HIS A 1 71  ? 14.324 28.237  13.667 1.00 64.92  ? 70  HIS A C   1 
ATOM 456  O O   . HIS A 1 71  ? 13.239 28.233  13.076 1.00 68.18  ? 70  HIS A O   1 
ATOM 457  C CB  . HIS A 1 71  ? 14.115 26.329  15.259 1.00 59.58  ? 70  HIS A CB  1 
ATOM 458  C CG  . HIS A 1 71  ? 13.472 27.369  16.123 1.00 72.10  ? 70  HIS A CG  1 
ATOM 459  N ND1 . HIS A 1 71  ? 14.176 28.101  17.055 1.00 68.80  ? 70  HIS A ND1 1 
ATOM 460  C CD2 . HIS A 1 71  ? 12.191 27.803  16.193 1.00 70.85  ? 70  HIS A CD2 1 
ATOM 461  C CE1 . HIS A 1 71  ? 13.357 28.940  17.662 1.00 73.35  ? 70  HIS A CE1 1 
ATOM 462  N NE2 . HIS A 1 71  ? 12.146 28.780  17.158 1.00 69.94  ? 70  HIS A NE2 1 
ATOM 463  N N   . ASP A 1 72  ? 14.986 29.360  13.941 1.00 70.53  ? 71  ASP A N   1 
ATOM 464  C CA  . ASP A 1 72  ? 14.485 30.677  13.575 1.00 70.23  ? 71  ASP A CA  1 
ATOM 465  C C   . ASP A 1 72  ? 15.166 31.259  12.346 1.00 66.25  ? 71  ASP A C   1 
ATOM 466  O O   . ASP A 1 72  ? 14.735 32.311  11.862 1.00 77.23  ? 71  ASP A O   1 
ATOM 467  C CB  . ASP A 1 72  ? 14.651 31.648  14.751 1.00 74.31  ? 71  ASP A CB  1 
ATOM 468  C CG  . ASP A 1 72  ? 13.377 31.820  15.544 1.00 88.66  ? 71  ASP A CG  1 
ATOM 469  O OD1 . ASP A 1 72  ? 12.336 31.283  15.109 1.00 85.79  ? 71  ASP A OD1 1 
ATOM 470  O OD2 . ASP A 1 72  ? 13.417 32.485  16.602 1.00 93.10  ? 71  ASP A OD2 1 
ATOM 471  N N   . ASN A 1 73  ? 16.225 30.619  11.845 1.00 68.41  ? 72  ASN A N   1 
ATOM 472  C CA  . ASN A 1 73  ? 16.943 31.064  10.652 1.00 77.25  ? 72  ASN A CA  1 
ATOM 473  C C   . ASN A 1 73  ? 16.664 30.078  9.525  1.00 76.60  ? 72  ASN A C   1 
ATOM 474  O O   . ASN A 1 73  ? 17.342 29.044  9.420  1.00 64.31  ? 72  ASN A O   1 
ATOM 475  C CB  . ASN A 1 73  ? 18.449 31.171  10.914 1.00 68.87  ? 72  ASN A CB  1 
ATOM 476  C CG  . ASN A 1 73  ? 18.777 31.872  12.221 1.00 80.29  ? 72  ASN A CG  1 
ATOM 477  O OD1 . ASN A 1 73  ? 17.888 32.299  12.957 1.00 88.55  ? 72  ASN A OD1 1 
ATOM 478  N ND2 . ASN A 1 73  ? 20.067 31.986  12.518 1.00 75.99  ? 72  ASN A ND2 1 
ATOM 479  N N   . PRO A 1 74  ? 15.674 30.344  8.668  1.00 89.80  ? 73  PRO A N   1 
ATOM 480  C CA  . PRO A 1 74  ? 15.338 29.395  7.591  1.00 90.05  ? 73  PRO A CA  1 
ATOM 481  C C   . PRO A 1 74  ? 16.522 28.935  6.755  1.00 85.14  ? 73  PRO A C   1 
ATOM 482  O O   . PRO A 1 74  ? 16.503 27.807  6.246  1.00 83.42  ? 73  PRO A O   1 
ATOM 483  C CB  . PRO A 1 74  ? 14.334 30.180  6.734  1.00 89.95  ? 73  PRO A CB  1 
ATOM 484  C CG  . PRO A 1 74  ? 13.857 31.328  7.587  1.00 87.02  ? 73  PRO A CG  1 
ATOM 485  C CD  . PRO A 1 74  ? 14.619 31.349  8.875  1.00 87.40  ? 73  PRO A CD  1 
ATOM 486  N N   . GLN A 1 75  ? 17.551 29.768  6.588  1.00 75.92  ? 74  GLN A N   1 
ATOM 487  C CA  . GLN A 1 75  ? 18.724 29.337  5.834  1.00 72.04  ? 74  GLN A CA  1 
ATOM 488  C C   . GLN A 1 75  ? 19.507 28.280  6.603  1.00 62.74  ? 74  GLN A C   1 
ATOM 489  O O   . GLN A 1 75  ? 19.739 27.174  6.103  1.00 68.64  ? 74  GLN A O   1 
ATOM 490  C CB  . GLN A 1 75  ? 19.620 30.532  5.501  1.00 65.63  ? 74  GLN A CB  1 
ATOM 491  C CG  . GLN A 1 75  ? 20.748 30.180  4.540  1.00 61.54  ? 74  GLN A CG  1 
ATOM 492  C CD  . GLN A 1 75  ? 21.841 31.229  4.498  1.00 71.20  ? 74  GLN A CD  1 
ATOM 493  O OE1 . GLN A 1 75  ? 21.760 32.256  5.172  1.00 87.52  ? 74  GLN A OE1 1 
ATOM 494  N NE2 . GLN A 1 75  ? 22.877 30.969  3.710  1.00 66.18  ? 74  GLN A NE2 1 
ATOM 495  N N   . GLN A 1 76  ? 19.925 28.604  7.830  1.00 60.67  ? 75  GLN A N   1 
ATOM 496  C CA  . GLN A 1 76  ? 20.700 27.659  8.623  1.00 61.82  ? 75  GLN A CA  1 
ATOM 497  C C   . GLN A 1 76  ? 19.879 26.451  9.054  1.00 66.28  ? 75  GLN A C   1 
ATOM 498  O O   . GLN A 1 76  ? 20.455 25.392  9.324  1.00 56.02  ? 75  GLN A O   1 
ATOM 499  C CB  . GLN A 1 76  ? 21.288 28.356  9.849  1.00 54.97  ? 75  GLN A CB  1 
ATOM 500  C CG  . GLN A 1 76  ? 22.508 29.206  9.541  1.00 64.71  ? 75  GLN A CG  1 
ATOM 501  C CD  . GLN A 1 76  ? 23.770 28.381  9.383  1.00 64.34  ? 75  GLN A CD  1 
ATOM 502  O OE1 . GLN A 1 76  ? 23.789 27.188  9.688  1.00 63.26  ? 75  GLN A OE1 1 
ATOM 503  N NE2 . GLN A 1 76  ? 24.833 29.013  8.902  1.00 73.45  ? 75  GLN A NE2 1 
ATOM 504  N N   . LEU A 1 77  ? 18.552 26.583  9.127  1.00 62.92  ? 76  LEU A N   1 
ATOM 505  C CA  . LEU A 1 77  ? 17.718 25.433  9.462  1.00 56.14  ? 76  LEU A CA  1 
ATOM 506  C C   . LEU A 1 77  ? 17.695 24.421  8.323  1.00 67.94  ? 76  LEU A C   1 
ATOM 507  O O   . LEU A 1 77  ? 17.631 23.209  8.563  1.00 71.96  ? 76  LEU A O   1 
ATOM 508  C CB  . LEU A 1 77  ? 16.301 25.892  9.806  1.00 52.99  ? 76  LEU A CB  1 
ATOM 509  C CG  . LEU A 1 77  ? 15.341 24.810  10.308 1.00 58.83  ? 76  LEU A CG  1 
ATOM 510  C CD1 . LEU A 1 77  ? 15.874 24.156  11.574 1.00 46.11  ? 76  LEU A CD1 1 
ATOM 511  C CD2 . LEU A 1 77  ? 13.954 25.390  10.541 1.00 56.62  ? 76  LEU A CD2 1 
ATOM 512  N N   . ARG A 1 78  ? 17.744 24.895  7.076  1.00 63.50  ? 77  ARG A N   1 
ATOM 513  C CA  . ARG A 1 78  ? 17.800 23.972  5.947  1.00 64.39  ? 77  ARG A CA  1 
ATOM 514  C C   . ARG A 1 78  ? 19.163 23.302  5.842  1.00 62.15  ? 77  ARG A C   1 
ATOM 515  O O   . ARG A 1 78  ? 19.249 22.132  5.452  1.00 67.58  ? 77  ARG A O   1 
ATOM 516  C CB  . ARG A 1 78  ? 17.462 24.705  4.647  1.00 67.22  ? 77  ARG A CB  1 
ATOM 517  C CG  . ARG A 1 78  ? 17.517 23.827  3.403  1.00 69.99  ? 77  ARG A CG  1 
ATOM 518  C CD  . ARG A 1 78  ? 16.245 23.939  2.572  1.00 77.83  ? 77  ARG A CD  1 
ATOM 519  N NE  . ARG A 1 78  ? 16.057 25.278  2.026  1.00 86.20  ? 77  ARG A NE  1 
ATOM 520  C CZ  . ARG A 1 78  ? 14.947 25.697  1.434  1.00 88.30  ? 77  ARG A CZ  1 
ATOM 521  N NH1 . ARG A 1 78  ? 13.901 24.900  1.284  1.00 82.57  ? 77  ARG A NH1 1 
ATOM 522  N NH2 . ARG A 1 78  ? 14.884 26.946  0.981  1.00 81.66  ? 77  ARG A NH2 1 
ATOM 523  N N   . ARG A 1 79  ? 20.231 24.016  6.198  1.00 64.63  ? 78  ARG A N   1 
ATOM 524  C CA  . ARG A 1 79  ? 21.569 23.450  6.075  1.00 63.53  ? 78  ARG A CA  1 
ATOM 525  C C   . ARG A 1 79  ? 21.803 22.345  7.099  1.00 64.38  ? 78  ARG A C   1 
ATOM 526  O O   . ARG A 1 79  ? 22.475 21.352  6.801  1.00 70.39  ? 78  ARG A O   1 
ATOM 527  C CB  . ARG A 1 79  ? 22.619 24.551  6.219  1.00 70.08  ? 78  ARG A CB  1 
ATOM 528  C CG  . ARG A 1 79  ? 22.825 25.378  4.957  1.00 77.99  ? 78  ARG A CG  1 
ATOM 529  C CD  . ARG A 1 79  ? 22.873 26.866  5.271  1.00 75.97  ? 78  ARG A CD  1 
ATOM 530  N NE  . ARG A 1 79  ? 24.120 27.249  5.921  1.00 81.62  ? 78  ARG A NE  1 
ATOM 531  C CZ  . ARG A 1 79  ? 25.137 27.836  5.306  1.00 83.66  ? 78  ARG A CZ  1 
ATOM 532  N NH1 . ARG A 1 79  ? 25.089 28.131  4.017  1.00 85.75  ? 78  ARG A NH1 1 
ATOM 533  N NH2 . ARG A 1 79  ? 26.231 28.136  6.002  1.00 78.99  ? 78  ARG A NH2 1 
ATOM 534  N N   . VAL A 1 80  ? 21.253 22.493  8.308  1.00 61.34  ? 79  VAL A N   1 
ATOM 535  C CA  . VAL A 1 80  ? 21.482 21.486  9.340  1.00 64.91  ? 79  VAL A CA  1 
ATOM 536  C C   . VAL A 1 80  ? 20.701 20.211  9.032  1.00 59.77  ? 79  VAL A C   1 
ATOM 537  O O   . VAL A 1 80  ? 21.208 19.099  9.222  1.00 50.31  ? 79  VAL A O   1 
ATOM 538  C CB  . VAL A 1 80  ? 21.142 22.046  10.738 1.00 57.24  ? 79  VAL A CB  1 
ATOM 539  C CG1 . VAL A 1 80  ? 22.052 23.213  11.085 1.00 53.32  ? 79  VAL A CG1 1 
ATOM 540  C CG2 . VAL A 1 80  ? 19.686 22.471  10.831 1.00 55.52  ? 79  VAL A CG2 1 
ATOM 541  N N   . VAL A 1 81  ? 19.468 20.345  8.538  1.00 55.94  ? 80  VAL A N   1 
ATOM 542  C CA  . VAL A 1 81  ? 18.659 19.166  8.242  1.00 50.61  ? 80  VAL A CA  1 
ATOM 543  C C   . VAL A 1 81  ? 19.156 18.480  6.976  1.00 58.36  ? 80  VAL A C   1 
ATOM 544  O O   . VAL A 1 81  ? 19.220 17.246  6.904  1.00 57.51  ? 80  VAL A O   1 
ATOM 545  C CB  . VAL A 1 81  ? 17.173 19.552  8.136  1.00 53.93  ? 80  VAL A CB  1 
ATOM 546  C CG1 . VAL A 1 81  ? 16.320 18.325  7.845  1.00 52.16  ? 80  VAL A CG1 1 
ATOM 547  C CG2 . VAL A 1 81  ? 16.712 20.232  9.415  1.00 46.53  ? 80  VAL A CG2 1 
ATOM 548  N N   . GLY A 1 82  ? 19.522 19.268  5.960  1.00 53.06  ? 81  GLY A N   1 
ATOM 549  C CA  . GLY A 1 82  ? 20.051 18.691  4.736  1.00 55.73  ? 81  GLY A CA  1 
ATOM 550  C C   . GLY A 1 82  ? 21.366 17.963  4.934  1.00 59.23  ? 81  GLY A C   1 
ATOM 551  O O   . GLY A 1 82  ? 21.618 16.946  4.282  1.00 58.65  ? 81  GLY A O   1 
ATOM 552  N N   . THR A 1 83  ? 22.221 18.468  5.827  1.00 55.61  ? 82  THR A N   1 
ATOM 553  C CA  . THR A 1 83  ? 23.467 17.770  6.131  1.00 59.87  ? 82  THR A CA  1 
ATOM 554  C C   . THR A 1 83  ? 23.209 16.541  6.995  1.00 58.77  ? 82  THR A C   1 
ATOM 555  O O   . THR A 1 83  ? 23.874 15.510  6.837  1.00 56.68  ? 82  THR A O   1 
ATOM 556  C CB  . THR A 1 83  ? 24.451 18.719  6.819  1.00 55.76  ? 82  THR A CB  1 
ATOM 557  O OG1 . THR A 1 83  ? 24.656 19.873  5.993  1.00 66.05  ? 82  THR A OG1 1 
ATOM 558  C CG2 . THR A 1 83  ? 25.792 18.036  7.057  1.00 58.17  ? 82  THR A CG2 1 
ATOM 559  N N   . SER A 1 84  ? 22.241 16.629  7.911  1.00 58.17  ? 83  SER A N   1 
ATOM 560  C CA  . SER A 1 84  ? 21.901 15.475  8.736  1.00 57.11  ? 83  SER A CA  1 
ATOM 561  C C   . SER A 1 84  ? 21.279 14.365  7.900  1.00 60.43  ? 83  SER A C   1 
ATOM 562  O O   . SER A 1 84  ? 21.566 13.181  8.115  1.00 61.36  ? 83  SER A O   1 
ATOM 563  C CB  . SER A 1 84  ? 20.957 15.893  9.863  1.00 48.04  ? 83  SER A CB  1 
ATOM 564  O OG  . SER A 1 84  ? 21.574 16.839  10.717 1.00 45.10  ? 83  SER A OG  1 
ATOM 565  N N   . SER A 1 85  ? 20.423 14.727  6.941  1.00 55.39  ? 84  SER A N   1 
ATOM 566  C CA  . SER A 1 85  ? 19.857 13.726  6.045  1.00 57.90  ? 84  SER A CA  1 
ATOM 567  C C   . SER A 1 85  ? 20.928 13.101  5.160  1.00 53.46  ? 84  SER A C   1 
ATOM 568  O O   . SER A 1 85  ? 20.818 11.926  4.793  1.00 55.51  ? 84  SER A O   1 
ATOM 569  C CB  . SER A 1 85  ? 18.755 14.348  5.189  1.00 55.69  ? 84  SER A CB  1 
ATOM 570  O OG  . SER A 1 85  ? 18.378 13.475  4.140  1.00 56.21  ? 84  SER A OG  1 
ATOM 571  N N   . ALA A 1 86  ? 21.965 13.866  4.812  1.00 51.00  ? 85  ALA A N   1 
ATOM 572  C CA  . ALA A 1 86  ? 23.058 13.317  4.017  1.00 54.89  ? 85  ALA A CA  1 
ATOM 573  C C   . ALA A 1 86  ? 23.849 12.282  4.806  1.00 60.57  ? 85  ALA A C   1 
ATOM 574  O O   . ALA A 1 86  ? 24.213 11.229  4.270  1.00 53.59  ? 85  ALA A O   1 
ATOM 575  C CB  . ALA A 1 86  ? 23.976 14.443  3.540  1.00 45.92  ? 85  ALA A CB  1 
ATOM 576  N N   . MET A 1 87  ? 24.122 12.564  6.081  1.00 62.14  ? 86  MET A N   1 
ATOM 577  C CA  . MET A 1 87  ? 24.872 11.619  6.901  1.00 54.43  ? 86  MET A CA  1 
ATOM 578  C C   . MET A 1 87  ? 24.071 10.350  7.156  1.00 55.59  ? 86  MET A C   1 
ATOM 579  O O   . MET A 1 87  ? 24.627 9.245   7.141  1.00 62.92  ? 86  MET A O   1 
ATOM 580  C CB  . MET A 1 87  ? 25.268 12.270  8.223  1.00 55.21  ? 86  MET A CB  1 
ATOM 581  C CG  . MET A 1 87  ? 26.360 13.310  8.104  1.00 61.55  ? 86  MET A CG  1 
ATOM 582  S SD  . MET A 1 87  ? 26.325 14.463  9.484  1.00 72.47  ? 86  MET A SD  1 
ATOM 583  C CE  . MET A 1 87  ? 27.981 14.236  10.119 1.00 65.77  ? 86  MET A CE  1 
ATOM 584  N N   . VAL A 1 88  ? 22.766 10.489  7.401  1.00 54.48  ? 87  VAL A N   1 
ATOM 585  C CA  . VAL A 1 88  ? 21.920 9.322   7.640  1.00 55.47  ? 87  VAL A CA  1 
ATOM 586  C C   . VAL A 1 88  ? 21.891 8.431   6.405  1.00 60.38  ? 87  VAL A C   1 
ATOM 587  O O   . VAL A 1 88  ? 22.038 7.206   6.495  1.00 60.77  ? 87  VAL A O   1 
ATOM 588  C CB  . VAL A 1 88  ? 20.504 9.765   8.054  1.00 55.86  ? 87  VAL A CB  1 
ATOM 589  C CG1 . VAL A 1 88  ? 19.468 8.714   7.662  1.00 53.68  ? 87  VAL A CG1 1 
ATOM 590  C CG2 . VAL A 1 88  ? 20.451 10.050  9.546  1.00 66.54  ? 87  VAL A CG2 1 
ATOM 591  N N   . LEU A 1 89  ? 21.722 9.039   5.229  1.00 56.22  ? 88  LEU A N   1 
ATOM 592  C CA  . LEU A 1 89  ? 21.595 8.268   3.996  1.00 52.56  ? 88  LEU A CA  1 
ATOM 593  C C   . LEU A 1 89  ? 22.885 7.522   3.674  1.00 52.93  ? 88  LEU A C   1 
ATOM 594  O O   . LEU A 1 89  ? 22.860 6.329   3.346  1.00 57.93  ? 88  LEU A O   1 
ATOM 595  C CB  . LEU A 1 89  ? 21.197 9.197   2.849  1.00 59.42  ? 88  LEU A CB  1 
ATOM 596  C CG  . LEU A 1 89  ? 20.877 8.576   1.489  1.00 71.91  ? 88  LEU A CG  1 
ATOM 597  C CD1 . LEU A 1 89  ? 19.712 9.300   0.835  1.00 73.48  ? 88  LEU A CD1 1 
ATOM 598  C CD2 . LEU A 1 89  ? 22.094 8.636   0.593  1.00 65.14  ? 88  LEU A CD2 1 
ATOM 599  N N   . GLY A 1 90  ? 24.024 8.209   3.762  1.00 50.40  ? 89  GLY A N   1 
ATOM 600  C CA  . GLY A 1 90  ? 25.289 7.565   3.443  1.00 48.53  ? 89  GLY A CA  1 
ATOM 601  C C   . GLY A 1 90  ? 25.631 6.445   4.405  1.00 61.81  ? 89  GLY A C   1 
ATOM 602  O O   . GLY A 1 90  ? 26.029 5.353   3.992  1.00 65.92  ? 89  GLY A O   1 
ATOM 603  N N   . PHE A 1 91  ? 25.475 6.701   5.707  1.00 61.02  ? 90  PHE A N   1 
ATOM 604  C CA  . PHE A 1 91  ? 25.768 5.673   6.702  1.00 58.53  ? 90  PHE A CA  1 
ATOM 605  C C   . PHE A 1 91  ? 24.810 4.494   6.575  1.00 60.08  ? 90  PHE A C   1 
ATOM 606  O O   . PHE A 1 91  ? 25.215 3.337   6.739  1.00 61.82  ? 90  PHE A O   1 
ATOM 607  C CB  . PHE A 1 91  ? 25.709 6.268   8.110  1.00 58.69  ? 90  PHE A CB  1 
ATOM 608  C CG  . PHE A 1 91  ? 26.589 5.561   9.105  1.00 72.62  ? 90  PHE A CG  1 
ATOM 609  C CD1 . PHE A 1 91  ? 27.940 5.856   9.191  1.00 70.21  ? 90  PHE A CD1 1 
ATOM 610  C CD2 . PHE A 1 91  ? 26.065 4.594   9.950  1.00 73.85  ? 90  PHE A CD2 1 
ATOM 611  C CE1 . PHE A 1 91  ? 28.752 5.203   10.105 1.00 68.77  ? 90  PHE A CE1 1 
ATOM 612  C CE2 . PHE A 1 91  ? 26.871 3.937   10.863 1.00 64.87  ? 90  PHE A CE2 1 
ATOM 613  C CZ  . PHE A 1 91  ? 28.216 4.243   10.941 1.00 63.10  ? 90  PHE A CZ  1 
ATOM 614  N N   . SER A 1 92  ? 23.535 4.766   6.274  1.00 55.00  ? 91  SER A N   1 
ATOM 615  C CA  . SER A 1 92  ? 22.566 3.685   6.111  1.00 56.90  ? 91  SER A CA  1 
ATOM 616  C C   . SER A 1 92  ? 22.920 2.803   4.923  1.00 59.75  ? 91  SER A C   1 
ATOM 617  O O   . SER A 1 92  ? 22.809 1.573   4.998  1.00 58.72  ? 91  SER A O   1 
ATOM 618  C CB  . SER A 1 92  ? 21.159 4.255   5.942  1.00 54.95  ? 91  SER A CB  1 
ATOM 619  O OG  . SER A 1 92  ? 20.610 4.622   7.191  1.00 66.64  ? 91  SER A OG  1 
ATOM 620  N N   . THR A 1 93  ? 23.337 3.413   3.813  1.00 57.73  ? 92  THR A N   1 
ATOM 621  C CA  . THR A 1 93  ? 23.738 2.627   2.654  1.00 58.01  ? 92  THR A CA  1 
ATOM 622  C C   . THR A 1 93  ? 25.005 1.834   2.943  1.00 56.98  ? 92  THR A C   1 
ATOM 623  O O   . THR A 1 93  ? 25.114 0.665   2.556  1.00 64.71  ? 92  THR A O   1 
ATOM 624  C CB  . THR A 1 93  ? 23.933 3.537   1.442  1.00 66.02  ? 92  THR A CB  1 
ATOM 625  O OG1 . THR A 1 93  ? 22.768 4.352   1.265  1.00 62.72  ? 92  THR A OG1 1 
ATOM 626  C CG2 . THR A 1 93  ? 24.145 2.703   0.191  1.00 58.66  ? 92  THR A CG2 1 
ATOM 627  N N   . LEU A 1 94  ? 25.973 2.448   3.627  1.00 52.05  ? 93  LEU A N   1 
ATOM 628  C CA  . LEU A 1 94  ? 27.158 1.706   4.041  1.00 58.18  ? 93  LEU A CA  1 
ATOM 629  C C   . LEU A 1 94  ? 26.807 0.623   5.049  1.00 59.84  ? 93  LEU A C   1 
ATOM 630  O O   . LEU A 1 94  ? 27.440 -0.440  5.065  1.00 53.85  ? 93  LEU A O   1 
ATOM 631  C CB  . LEU A 1 94  ? 28.201 2.657   4.626  1.00 52.08  ? 93  LEU A CB  1 
ATOM 632  C CG  . LEU A 1 94  ? 29.539 2.032   5.025  1.00 54.47  ? 93  LEU A CG  1 
ATOM 633  C CD1 . LEU A 1 94  ? 30.089 1.160   3.905  1.00 52.28  ? 93  LEU A CD1 1 
ATOM 634  C CD2 . LEU A 1 94  ? 30.543 3.108   5.412  1.00 48.68  ? 93  LEU A CD2 1 
ATOM 635  N N   . MET A 1 95  ? 25.807 0.872   5.895  1.00 64.07  ? 94  MET A N   1 
ATOM 636  C CA  . MET A 1 95  ? 25.384 -0.149  6.844  1.00 55.17  ? 94  MET A CA  1 
ATOM 637  C C   . MET A 1 95  ? 24.708 -1.313  6.134  1.00 59.25  ? 94  MET A C   1 
ATOM 638  O O   . MET A 1 95  ? 24.856 -2.468  6.549  1.00 65.76  ? 94  MET A O   1 
ATOM 639  C CB  . MET A 1 95  ? 24.446 0.450   7.886  1.00 50.25  ? 94  MET A CB  1 
ATOM 640  C CG  . MET A 1 95  ? 25.094 0.987   9.170  1.00 65.80  ? 94  MET A CG  1 
ATOM 641  S SD  . MET A 1 95  ? 26.323 -0.047  10.019 1.00 77.34  ? 94  MET A SD  1 
ATOM 642  C CE  . MET A 1 95  ? 27.879 0.326   9.197  1.00 62.89  ? 94  MET A CE  1 
ATOM 643  N N   . ALA A 1 96  ? 23.945 -1.029  5.077  1.00 59.83  ? 95  ALA A N   1 
ATOM 644  C CA  . ALA A 1 96  ? 23.346 -2.106  4.299  1.00 56.69  ? 95  ALA A CA  1 
ATOM 645  C C   . ALA A 1 96  ? 24.418 -2.970  3.646  1.00 58.84  ? 95  ALA A C   1 
ATOM 646  O O   . ALA A 1 96  ? 24.296 -4.200  3.607  1.00 53.51  ? 95  ALA A O   1 
ATOM 647  C CB  . ALA A 1 96  ? 22.397 -1.530  3.247  1.00 51.52  ? 95  ALA A CB  1 
ATOM 648  N N   . LEU A 1 97  ? 25.489 -2.347  3.151  1.00 56.54  ? 96  LEU A N   1 
ATOM 649  C CA  . LEU A 1 97  ? 26.517 -3.097  2.437  1.00 54.91  ? 96  LEU A CA  1 
ATOM 650  C C   . LEU A 1 97  ? 27.269 -4.040  3.369  1.00 55.18  ? 96  LEU A C   1 
ATOM 651  O O   . LEU A 1 97  ? 27.474 -5.215  3.044  1.00 54.10  ? 96  LEU A O   1 
ATOM 652  C CB  . LEU A 1 97  ? 27.485 -2.139  1.744  1.00 48.61  ? 96  LEU A CB  1 
ATOM 653  C CG  . LEU A 1 97  ? 28.517 -2.812  0.838  1.00 51.52  ? 96  LEU A CG  1 
ATOM 654  C CD1 . LEU A 1 97  ? 27.833 -3.477  -0.348 1.00 48.96  ? 96  LEU A CD1 1 
ATOM 655  C CD2 . LEU A 1 97  ? 29.561 -1.811  0.370  1.00 46.10  ? 96  LEU A CD2 1 
ATOM 656  N N   . VAL A 1 98  ? 27.690 -3.548  4.535  1.00 54.86  ? 97  VAL A N   1 
ATOM 657  C CA  . VAL A 1 98  ? 28.444 -4.404  5.445  1.00 65.55  ? 97  VAL A CA  1 
ATOM 658  C C   . VAL A 1 98  ? 27.564 -5.520  5.993  1.00 53.56  ? 97  VAL A C   1 
ATOM 659  O O   . VAL A 1 98  ? 28.058 -6.602  6.328  1.00 54.14  ? 97  VAL A O   1 
ATOM 660  C CB  . VAL A 1 98  ? 29.058 -3.572  6.584  1.00 53.33  ? 97  VAL A CB  1 
ATOM 661  C CG1 . VAL A 1 98  ? 30.122 -2.632  6.041  1.00 55.50  ? 97  VAL A CG1 1 
ATOM 662  C CG2 . VAL A 1 98  ? 27.978 -2.802  7.313  1.00 55.31  ? 97  VAL A CG2 1 
ATOM 663  N N   . PHE A 1 99  ? 26.256 -5.280  6.102  1.00 56.05  ? 98  PHE A N   1 
ATOM 664  C CA  . PHE A 1 99  ? 25.358 -6.315  6.600  1.00 57.19  ? 98  PHE A CA  1 
ATOM 665  C C   . PHE A 1 99  ? 25.176 -7.422  5.570  1.00 60.98  ? 98  PHE A C   1 
ATOM 666  O O   . PHE A 1 99  ? 25.225 -8.611  5.907  1.00 67.41  ? 98  PHE A O   1 
ATOM 667  C CB  . PHE A 1 99  ? 24.009 -5.706  6.980  1.00 58.58  ? 98  PHE A CB  1 
ATOM 668  C CG  . PHE A 1 99  ? 23.947 -5.196  8.390  1.00 65.91  ? 98  PHE A CG  1 
ATOM 669  C CD1 . PHE A 1 99  ? 24.803 -5.691  9.360  1.00 66.12  ? 98  PHE A CD1 1 
ATOM 670  C CD2 . PHE A 1 99  ? 23.031 -4.221  8.748  1.00 63.26  ? 98  PHE A CD2 1 
ATOM 671  C CE1 . PHE A 1 99  ? 24.748 -5.223  10.659 1.00 59.09  ? 98  PHE A CE1 1 
ATOM 672  C CE2 . PHE A 1 99  ? 22.973 -3.747  10.044 1.00 67.02  ? 98  PHE A CE2 1 
ATOM 673  C CZ  . PHE A 1 99  ? 23.831 -4.250  11.001 1.00 63.22  ? 98  PHE A CZ  1 
ATOM 674  N N   . VAL A 1 100 ? 24.966 -7.051  4.305  1.00 55.22  ? 99  VAL A N   1 
ATOM 675  C CA  . VAL A 1 100 ? 24.771 -8.057  3.269  1.00 55.78  ? 99  VAL A CA  1 
ATOM 676  C C   . VAL A 1 100 ? 26.073 -8.755  2.901  1.00 58.03  ? 99  VAL A C   1 
ATOM 677  O O   . VAL A 1 100 ? 26.043 -9.880  2.390  1.00 64.29  ? 99  VAL A O   1 
ATOM 678  C CB  . VAL A 1 100 ? 24.121 -7.438  2.017  1.00 51.44  ? 99  VAL A CB  1 
ATOM 679  C CG1 . VAL A 1 100 ? 22.848 -6.690  2.388  1.00 52.00  ? 99  VAL A CG1 1 
ATOM 680  C CG2 . VAL A 1 100 ? 25.098 -6.521  1.296  1.00 57.85  ? 99  VAL A CG2 1 
ATOM 681  N N   . LEU A 1 101 ? 27.221 -8.126  3.155  1.00 53.11  ? 100 LEU A N   1 
ATOM 682  C CA  . LEU A 1 101 ? 28.502 -8.718  2.797  1.00 51.30  ? 100 LEU A CA  1 
ATOM 683  C C   . LEU A 1 101 ? 29.136 -9.509  3.932  1.00 56.04  ? 100 LEU A C   1 
ATOM 684  O O   . LEU A 1 101 ? 30.032 -10.321 3.676  1.00 74.80  ? 100 LEU A O   1 
ATOM 685  C CB  . LEU A 1 101 ? 29.480 -7.632  2.339  1.00 48.82  ? 100 LEU A CB  1 
ATOM 686  C CG  . LEU A 1 101 ? 29.862 -7.648  0.859  1.00 55.32  ? 100 LEU A CG  1 
ATOM 687  C CD1 . LEU A 1 101 ? 28.666 -7.272  -0.002 1.00 55.77  ? 100 LEU A CD1 1 
ATOM 688  C CD2 . LEU A 1 101 ? 31.031 -6.712  0.600  1.00 67.57  ? 100 LEU A CD2 1 
ATOM 689  N N   . ALA A 1 102 ? 28.699 -9.298  5.169  1.00 51.23  ? 101 ALA A N   1 
ATOM 690  C CA  . ALA A 1 102 ? 29.281 -9.968  6.325  1.00 50.67  ? 101 ALA A CA  1 
ATOM 691  C C   . ALA A 1 102 ? 28.194 -10.563 7.207  1.00 56.56  ? 101 ALA A C   1 
ATOM 692  O O   . ALA A 1 102 ? 28.276 -10.523 8.438  1.00 67.71  ? 101 ALA A O   1 
ATOM 693  C CB  . ALA A 1 102 ? 30.164 -9.011  7.122  1.00 44.47  ? 101 ALA A CB  1 
ATOM 694  N N   . ALA A 1 103 ? 27.161 -11.138 6.587  1.00 53.56  ? 102 ALA A N   1 
ATOM 695  C CA  . ALA A 1 103 ? 26.072 -11.727 7.360  1.00 57.19  ? 102 ALA A CA  1 
ATOM 696  C C   . ALA A 1 103 ? 26.554 -12.911 8.193  1.00 60.61  ? 102 ALA A C   1 
ATOM 697  O O   . ALA A 1 103 ? 26.190 -13.040 9.368  1.00 61.88  ? 102 ALA A O   1 
ATOM 698  C CB  . ALA A 1 103 ? 24.937 -12.148 6.428  1.00 58.19  ? 102 ALA A CB  1 
ATOM 699  N N   . ALA A 1 104 ? 27.384 -13.784 7.606  1.00 58.09  ? 103 ALA A N   1 
ATOM 700  C CA  . ALA A 1 104 ? 27.863 -14.950 8.348  1.00 48.19  ? 103 ALA A CA  1 
ATOM 701  C C   . ALA A 1 104 ? 28.837 -14.581 9.462  1.00 50.74  ? 103 ALA A C   1 
ATOM 702  O O   . ALA A 1 104 ? 28.696 -15.118 10.575 1.00 56.85  ? 103 ALA A O   1 
ATOM 703  C CB  . ALA A 1 104 ? 28.470 -15.974 7.383  1.00 53.43  ? 103 ALA A CB  1 
ATOM 704  N N   . PRO A 1 105 ? 29.841 -13.718 9.251  1.00 55.60  ? 104 PRO A N   1 
ATOM 705  C CA  . PRO A 1 105 ? 30.709 -13.345 10.383 1.00 57.75  ? 104 PRO A CA  1 
ATOM 706  C C   . PRO A 1 105 ? 29.969 -12.664 11.521 1.00 50.41  ? 104 PRO A C   1 
ATOM 707  O O   . PRO A 1 105 ? 30.348 -12.842 12.685 1.00 53.80  ? 104 PRO A O   1 
ATOM 708  C CB  . PRO A 1 105 ? 31.741 -12.405 9.744  1.00 46.15  ? 104 PRO A CB  1 
ATOM 709  C CG  . PRO A 1 105 ? 31.760 -12.777 8.318  1.00 56.32  ? 104 PRO A CG  1 
ATOM 710  C CD  . PRO A 1 105 ? 30.363 -13.193 7.975  1.00 53.87  ? 104 PRO A CD  1 
ATOM 711  N N   . ILE A 1 106 ? 28.924 -11.887 11.227 1.00 44.01  ? 105 ILE A N   1 
ATOM 712  C CA  . ILE A 1 106 ? 28.164 -11.256 12.300 1.00 55.58  ? 105 ILE A CA  1 
ATOM 713  C C   . ILE A 1 106 ? 27.378 -12.302 13.080 1.00 52.93  ? 105 ILE A C   1 
ATOM 714  O O   . ILE A 1 106 ? 27.346 -12.281 14.317 1.00 55.09  ? 105 ILE A O   1 
ATOM 715  C CB  . ILE A 1 106 ? 27.247 -10.152 11.742 1.00 57.01  ? 105 ILE A CB  1 
ATOM 716  C CG1 . ILE A 1 106 ? 28.057 -8.894  11.422 1.00 48.60  ? 105 ILE A CG1 1 
ATOM 717  C CG2 . ILE A 1 106 ? 26.154 -9.809  12.742 1.00 54.92  ? 105 ILE A CG2 1 
ATOM 718  C CD1 . ILE A 1 106 ? 27.482 -8.052  10.298 1.00 47.13  ? 105 ILE A CD1 1 
ATOM 719  N N   . SER A 1 107 ? 26.735 -13.236 12.372 1.00 52.18  ? 106 SER A N   1 
ATOM 720  C CA  . SER A 1 107 ? 26.044 -14.333 13.042 1.00 55.01  ? 106 SER A CA  1 
ATOM 721  C C   . SER A 1 107 ? 27.003 -15.136 13.912 1.00 60.42  ? 106 SER A C   1 
ATOM 722  O O   . SER A 1 107 ? 26.633 -15.591 15.002 1.00 56.22  ? 106 SER A O   1 
ATOM 723  C CB  . SER A 1 107 ? 25.372 -15.239 12.009 1.00 51.72  ? 106 SER A CB  1 
ATOM 724  O OG  . SER A 1 107 ? 24.560 -16.219 12.630 1.00 43.26  ? 106 SER A OG  1 
ATOM 725  N N   . GLN A 1 108 ? 28.243 -15.316 13.449 1.00 59.48  ? 107 GLN A N   1 
ATOM 726  C CA  . GLN A 1 108 ? 29.242 -16.031 14.238 1.00 63.75  ? 107 GLN A CA  1 
ATOM 727  C C   . GLN A 1 108 ? 29.534 -15.308 15.548 1.00 63.68  ? 107 GLN A C   1 
ATOM 728  O O   . GLN A 1 108 ? 29.448 -15.900 16.630 1.00 62.35  ? 107 GLN A O   1 
ATOM 729  C CB  . GLN A 1 108 ? 30.526 -16.206 13.424 1.00 59.35  ? 107 GLN A CB  1 
ATOM 730  C CG  . GLN A 1 108 ? 31.352 -17.478 13.699 1.00 68.66  ? 107 GLN A CG  1 
ATOM 731  C CD  . GLN A 1 108 ? 30.550 -18.779 13.776 1.00 77.85  ? 107 GLN A CD  1 
ATOM 732  O OE1 . GLN A 1 108 ? 29.390 -18.853 13.374 1.00 80.16  ? 107 GLN A OE1 1 
ATOM 733  N NE2 . GLN A 1 108 ? 31.183 -19.817 14.310 1.00 77.92  ? 107 GLN A NE2 1 
ATOM 734  N N   . GLY A 1 109 ? 29.896 -14.026 15.471 1.00 55.86  ? 108 GLY A N   1 
ATOM 735  C CA  . GLY A 1 109 ? 30.204 -13.274 16.673 1.00 59.82  ? 108 GLY A CA  1 
ATOM 736  C C   . GLY A 1 109 ? 29.022 -13.077 17.599 1.00 49.58  ? 108 GLY A C   1 
ATOM 737  O O   . GLY A 1 109 ? 29.215 -12.849 18.797 1.00 60.28  ? 108 GLY A O   1 
ATOM 738  N N   . LEU A 1 110 ? 27.801 -13.165 17.074 1.00 49.96  ? 109 LEU A N   1 
ATOM 739  C CA  . LEU A 1 110 ? 26.594 -12.940 17.861 1.00 48.61  ? 109 LEU A CA  1 
ATOM 740  C C   . LEU A 1 110 ? 25.944 -14.228 18.346 1.00 54.37  ? 109 LEU A C   1 
ATOM 741  O O   . LEU A 1 110 ? 25.477 -14.287 19.488 1.00 59.71  ? 109 LEU A O   1 
ATOM 742  C CB  . LEU A 1 110 ? 25.575 -12.138 17.045 1.00 51.64  ? 109 LEU A CB  1 
ATOM 743  C CG  . LEU A 1 110 ? 25.437 -10.653 17.380 1.00 55.04  ? 109 LEU A CG  1 
ATOM 744  C CD1 . LEU A 1 110 ? 26.702 -9.894  17.004 1.00 48.86  ? 109 LEU A CD1 1 
ATOM 745  C CD2 . LEU A 1 110 ? 24.221 -10.062 16.683 1.00 47.22  ? 109 LEU A CD2 1 
ATOM 746  N N   . PHE A 1 111 ? 25.900 -15.266 17.510 1.00 53.49  ? 110 PHE A N   1 
ATOM 747  C CA  . PHE A 1 111 ? 25.212 -16.499 17.858 1.00 53.61  ? 110 PHE A CA  1 
ATOM 748  C C   . PHE A 1 111 ? 26.116 -17.716 17.974 1.00 55.31  ? 110 PHE A C   1 
ATOM 749  O O   . PHE A 1 111 ? 25.680 -18.729 18.531 1.00 56.04  ? 110 PHE A O   1 
ATOM 750  C CB  . PHE A 1 111 ? 24.117 -16.814 16.826 1.00 55.41  ? 110 PHE A CB  1 
ATOM 751  C CG  . PHE A 1 111 ? 23.072 -15.745 16.700 1.00 42.67  ? 110 PHE A CG  1 
ATOM 752  C CD1 . PHE A 1 111 ? 21.978 -15.722 17.548 1.00 38.94  ? 110 PHE A CD1 1 
ATOM 753  C CD2 . PHE A 1 111 ? 23.178 -14.769 15.724 1.00 39.70  ? 110 PHE A CD2 1 
ATOM 754  C CE1 . PHE A 1 111 ? 21.010 -14.743 17.429 1.00 49.54  ? 110 PHE A CE1 1 
ATOM 755  C CE2 . PHE A 1 111 ? 22.215 -13.787 15.600 1.00 43.66  ? 110 PHE A CE2 1 
ATOM 756  C CZ  . PHE A 1 111 ? 21.129 -13.773 16.453 1.00 43.27  ? 110 PHE A CZ  1 
ATOM 757  N N   . GLY A 1 112 ? 27.346 -17.659 17.467 1.00 53.08  ? 111 GLY A N   1 
ATOM 758  C CA  . GLY A 1 112 ? 28.223 -18.805 17.453 1.00 53.09  ? 111 GLY A CA  1 
ATOM 759  C C   . GLY A 1 112 ? 28.091 -19.693 16.233 1.00 61.58  ? 111 GLY A C   1 
ATOM 760  O O   . GLY A 1 112 ? 29.002 -20.480 15.956 1.00 70.34  ? 111 GLY A O   1 
ATOM 761  N N   . ASN A 1 113 ? 26.984 -19.592 15.500 1.00 54.08  ? 112 ASN A N   1 
ATOM 762  C CA  . ASN A 1 113 ? 26.792 -20.324 14.257 1.00 50.47  ? 112 ASN A CA  1 
ATOM 763  C C   . ASN A 1 113 ? 26.387 -19.347 13.160 1.00 63.48  ? 112 ASN A C   1 
ATOM 764  O O   . ASN A 1 113 ? 25.870 -18.260 13.430 1.00 61.27  ? 112 ASN A O   1 
ATOM 765  C CB  . ASN A 1 113 ? 25.735 -21.425 14.407 1.00 47.48  ? 112 ASN A CB  1 
ATOM 766  C CG  . ASN A 1 113 ? 24.457 -20.922 15.045 1.00 49.65  ? 112 ASN A CG  1 
ATOM 767  O OD1 . ASN A 1 113 ? 23.752 -20.090 14.474 1.00 55.77  ? 112 ASN A OD1 1 
ATOM 768  N ND2 . ASN A 1 113 ? 24.155 -21.418 16.239 1.00 57.44  ? 112 ASN A ND2 1 
ATOM 769  N N   . THR A 1 114 ? 26.637 -19.744 11.911 1.00 57.58  ? 113 THR A N   1 
ATOM 770  C CA  . THR A 1 114 ? 26.258 -18.947 10.752 1.00 43.29  ? 113 THR A CA  1 
ATOM 771  C C   . THR A 1 114 ? 24.840 -19.244 10.280 1.00 43.01  ? 113 THR A C   1 
ATOM 772  O O   . THR A 1 114 ? 24.496 -18.926 9.136  1.00 46.94  ? 113 THR A O   1 
ATOM 773  C CB  . THR A 1 114 ? 27.246 -19.169 9.603  1.00 47.74  ? 113 THR A CB  1 
ATOM 774  O OG1 . THR A 1 114 ? 27.247 -20.553 9.225  1.00 61.64  ? 113 THR A OG1 1 
ATOM 775  C CG2 . THR A 1 114 ? 28.651 -18.755 10.016 1.00 42.49  ? 113 THR A CG2 1 
ATOM 776  N N   . ASP A 1 115 ? 24.014 -19.843 11.135 1.00 42.67  ? 114 ASP A N   1 
ATOM 777  C CA  . ASP A 1 115 ? 22.653 -20.217 10.776 1.00 50.79  ? 114 ASP A CA  1 
ATOM 778  C C   . ASP A 1 115 ? 21.694 -19.034 10.756 1.00 43.40  ? 114 ASP A C   1 
ATOM 779  O O   . ASP A 1 115 ? 20.514 -19.221 10.438 1.00 44.62  ? 114 ASP A O   1 
ATOM 780  C CB  . ASP A 1 115 ? 22.134 -21.289 11.741 1.00 56.37  ? 114 ASP A CB  1 
ATOM 781  C CG  . ASP A 1 115 ? 22.997 -22.543 11.747 1.00 55.39  ? 114 ASP A CG  1 
ATOM 782  O OD1 . ASP A 1 115 ? 23.659 -22.825 10.726 1.00 51.96  ? 114 ASP A OD1 1 
ATOM 783  O OD2 . ASP A 1 115 ? 23.008 -23.253 12.775 1.00 66.36  ? 114 ASP A OD2 1 
ATOM 784  N N   . TYR A 1 116 ? 22.164 -17.829 11.083 1.00 55.56  ? 115 TYR A N   1 
ATOM 785  C CA  . TYR A 1 116 ? 21.334 -16.632 11.069 1.00 55.35  ? 115 TYR A CA  1 
ATOM 786  C C   . TYR A 1 116 ? 21.769 -15.642 9.992  1.00 56.87  ? 115 TYR A C   1 
ATOM 787  O O   . TYR A 1 116 ? 21.525 -14.439 10.129 1.00 48.24  ? 115 TYR A O   1 
ATOM 788  C CB  . TYR A 1 116 ? 21.342 -15.968 12.448 1.00 50.91  ? 115 TYR A CB  1 
ATOM 789  C CG  . TYR A 1 116 ? 20.788 -16.855 13.544 1.00 43.89  ? 115 TYR A CG  1 
ATOM 790  C CD1 . TYR A 1 116 ? 19.429 -16.872 13.832 1.00 39.22  ? 115 TYR A CD1 1 
ATOM 791  C CD2 . TYR A 1 116 ? 21.624 -17.685 14.281 1.00 43.04  ? 115 TYR A CD2 1 
ATOM 792  C CE1 . TYR A 1 116 ? 18.918 -17.688 14.828 1.00 44.27  ? 115 TYR A CE1 1 
ATOM 793  C CE2 . TYR A 1 116 ? 21.122 -18.505 15.279 1.00 39.78  ? 115 TYR A CE2 1 
ATOM 794  C CZ  . TYR A 1 116 ? 19.770 -18.503 15.548 1.00 45.50  ? 115 TYR A CZ  1 
ATOM 795  O OH  . TYR A 1 116 ? 19.270 -19.318 16.539 1.00 39.65  ? 115 TYR A OH  1 
ATOM 796  N N   . GLN A 1 117 ? 22.409 -16.131 8.924  1.00 60.16  ? 116 GLN A N   1 
ATOM 797  C CA  . GLN A 1 117 ? 22.831 -15.263 7.828  1.00 45.91  ? 116 GLN A CA  1 
ATOM 798  C C   . GLN A 1 117 ? 21.666 -14.441 7.295  1.00 44.52  ? 116 GLN A C   1 
ATOM 799  O O   . GLN A 1 117 ? 21.767 -13.218 7.147  1.00 52.07  ? 116 GLN A O   1 
ATOM 800  C CB  . GLN A 1 117 ? 23.436 -16.095 6.697  1.00 62.01  ? 116 GLN A CB  1 
ATOM 801  C CG  . GLN A 1 117 ? 24.831 -16.627 6.947  1.00 62.78  ? 116 GLN A CG  1 
ATOM 802  C CD  . GLN A 1 117 ? 25.342 -17.435 5.771  1.00 60.86  ? 116 GLN A CD  1 
ATOM 803  O OE1 . GLN A 1 117 ? 26.512 -17.811 5.716  1.00 62.47  ? 116 GLN A OE1 1 
ATOM 804  N NE2 . GLN A 1 117 ? 24.458 -17.704 4.817  1.00 67.46  ? 116 GLN A NE2 1 
ATOM 805  N N   . GLY A 1 118 ? 20.547 -15.104 6.997  1.00 50.39  ? 117 GLY A N   1 
ATOM 806  C CA  . GLY A 1 118 ? 19.406 -14.403 6.438  1.00 51.10  ? 117 GLY A CA  1 
ATOM 807  C C   . GLY A 1 118 ? 18.828 -13.362 7.374  1.00 49.40  ? 117 GLY A C   1 
ATOM 808  O O   . GLY A 1 118 ? 18.267 -12.360 6.923  1.00 60.28  ? 117 GLY A O   1 
ATOM 809  N N   . LEU A 1 119 ? 18.956 -13.579 8.684  1.00 52.39  ? 118 LEU A N   1 
ATOM 810  C CA  . LEU A 1 119 ? 18.462 -12.597 9.642  1.00 54.77  ? 118 LEU A CA  1 
ATOM 811  C C   . LEU A 1 119 ? 19.301 -11.325 9.615  1.00 50.54  ? 118 LEU A C   1 
ATOM 812  O O   . LEU A 1 119 ? 18.756 -10.216 9.652  1.00 48.69  ? 118 LEU A O   1 
ATOM 813  C CB  . LEU A 1 119 ? 18.443 -13.198 11.047 1.00 54.25  ? 118 LEU A CB  1 
ATOM 814  C CG  . LEU A 1 119 ? 17.818 -12.313 12.126 1.00 53.86  ? 118 LEU A CG  1 
ATOM 815  C CD1 . LEU A 1 119 ? 16.333 -12.101 11.859 1.00 49.81  ? 118 LEU A CD1 1 
ATOM 816  C CD2 . LEU A 1 119 ? 18.045 -12.907 13.508 1.00 47.30  ? 118 LEU A CD2 1 
ATOM 817  N N   . VAL A 1 120 ? 20.627 -11.464 9.545  1.00 46.42  ? 119 VAL A N   1 
ATOM 818  C CA  . VAL A 1 120 ? 21.497 -10.291 9.528  1.00 46.34  ? 119 VAL A CA  1 
ATOM 819  C C   . VAL A 1 120 ? 21.350 -9.527  8.219  1.00 53.65  ? 119 VAL A C   1 
ATOM 820  O O   . VAL A 1 120 ? 21.407 -8.291  8.197  1.00 56.26  ? 119 VAL A O   1 
ATOM 821  C CB  . VAL A 1 120 ? 22.959 -10.705 9.776  1.00 46.56  ? 119 VAL A CB  1 
ATOM 822  C CG1 . VAL A 1 120 ? 23.794 -9.486  10.119 1.00 57.92  ? 119 VAL A CG1 1 
ATOM 823  C CG2 . VAL A 1 120 ? 23.037 -11.734 10.889 1.00 53.26  ? 119 VAL A CG2 1 
ATOM 824  N N   . ARG A 1 121 ? 21.166 -10.243 7.107  1.00 53.14  ? 120 ARG A N   1 
ATOM 825  C CA  . ARG A 1 121 ? 21.022 -9.579  5.816  1.00 53.52  ? 120 ARG A CA  1 
ATOM 826  C C   . ARG A 1 121 ? 19.730 -8.775  5.749  1.00 53.78  ? 120 ARG A C   1 
ATOM 827  O O   . ARG A 1 121 ? 19.716 -7.653  5.231  1.00 59.36  ? 120 ARG A O   1 
ATOM 828  C CB  . ARG A 1 121 ? 21.073 -10.608 4.688  1.00 49.35  ? 120 ARG A CB  1 
ATOM 829  C CG  . ARG A 1 121 ? 22.460 -10.832 4.114  1.00 52.72  ? 120 ARG A CG  1 
ATOM 830  C CD  . ARG A 1 121 ? 22.399 -11.639 2.830  1.00 54.99  ? 120 ARG A CD  1 
ATOM 831  N NE  . ARG A 1 121 ? 21.628 -12.864 2.996  1.00 52.97  ? 120 ARG A NE  1 
ATOM 832  C CZ  . ARG A 1 121 ? 22.150 -14.034 3.335  1.00 52.66  ? 120 ARG A CZ  1 
ATOM 833  N NH1 . ARG A 1 121 ? 23.447 -14.174 3.558  1.00 46.09  ? 120 ARG A NH1 1 
ATOM 834  N NH2 . ARG A 1 121 ? 21.351 -15.091 3.455  1.00 55.33  ? 120 ARG A NH2 1 
ATOM 835  N N   . LEU A 1 122 ? 18.634 -9.334  6.267  1.00 46.89  ? 121 LEU A N   1 
ATOM 836  C CA  . LEU A 1 122 ? 17.371 -8.606  6.284  1.00 54.21  ? 121 LEU A CA  1 
ATOM 837  C C   . LEU A 1 122 ? 17.454 -7.365  7.165  1.00 59.14  ? 121 LEU A C   1 
ATOM 838  O O   . LEU A 1 122 ? 16.764 -6.372  6.907  1.00 59.61  ? 121 LEU A O   1 
ATOM 839  C CB  . LEU A 1 122 ? 16.248 -9.530  6.757  1.00 52.66  ? 121 LEU A CB  1 
ATOM 840  C CG  . LEU A 1 122 ? 14.806 -9.030  6.636  1.00 70.27  ? 121 LEU A CG  1 
ATOM 841  C CD1 . LEU A 1 122 ? 14.593 -8.283  5.326  1.00 59.29  ? 121 LEU A CD1 1 
ATOM 842  C CD2 . LEU A 1 122 ? 13.831 -10.192 6.764  1.00 46.24  ? 121 LEU A CD2 1 
ATOM 843  N N   . VAL A 1 123 ? 18.299 -7.399  8.199  1.00 56.54  ? 122 VAL A N   1 
ATOM 844  C CA  . VAL A 1 123 ? 18.463 -6.249  9.084  1.00 53.30  ? 122 VAL A CA  1 
ATOM 845  C C   . VAL A 1 123 ? 18.996 -5.046  8.314  1.00 58.78  ? 122 VAL A C   1 
ATOM 846  O O   . VAL A 1 123 ? 18.692 -3.895  8.656  1.00 57.02  ? 122 VAL A O   1 
ATOM 847  C CB  . VAL A 1 123 ? 19.375 -6.636  10.268 1.00 45.76  ? 122 VAL A CB  1 
ATOM 848  C CG1 . VAL A 1 123 ? 20.042 -5.417  10.884 1.00 51.72  ? 122 VAL A CG1 1 
ATOM 849  C CG2 . VAL A 1 123 ? 18.576 -7.395  11.315 1.00 44.76  ? 122 VAL A CG2 1 
ATOM 850  N N   . ALA A 1 124 ? 19.771 -5.290  7.251  1.00 54.62  ? 123 ALA A N   1 
ATOM 851  C CA  . ALA A 1 124 ? 20.277 -4.203  6.417  1.00 59.69  ? 123 ALA A CA  1 
ATOM 852  C C   . ALA A 1 124 ? 19.149 -3.318  5.904  1.00 57.70  ? 123 ALA A C   1 
ATOM 853  O O   . ALA A 1 124 ? 19.307 -2.098  5.789  1.00 57.82  ? 123 ALA A O   1 
ATOM 854  C CB  . ALA A 1 124 ? 21.078 -4.770  5.246  1.00 53.93  ? 123 ALA A CB  1 
ATOM 855  N N   . LEU A 1 125 ? 18.004 -3.917  5.580  1.00 51.54  ? 124 LEU A N   1 
ATOM 856  C CA  . LEU A 1 125 ? 16.834 -3.123  5.229  1.00 58.75  ? 124 LEU A CA  1 
ATOM 857  C C   . LEU A 1 125 ? 16.171 -2.546  6.473  1.00 63.04  ? 124 LEU A C   1 
ATOM 858  O O   . LEU A 1 125 ? 15.683 -1.411  6.455  1.00 64.42  ? 124 LEU A O   1 
ATOM 859  C CB  . LEU A 1 125 ? 15.841 -3.975  4.437  1.00 58.38  ? 124 LEU A CB  1 
ATOM 860  C CG  . LEU A 1 125 ? 14.535 -3.307  4.000  1.00 59.76  ? 124 LEU A CG  1 
ATOM 861  C CD1 . LEU A 1 125 ? 14.212 -3.667  2.560  1.00 54.04  ? 124 LEU A CD1 1 
ATOM 862  C CD2 . LEU A 1 125 ? 13.390 -3.703  4.924  1.00 61.59  ? 124 LEU A CD2 1 
ATOM 863  N N   . VAL A 1 126 ? 16.160 -3.315  7.563  1.00 57.75  ? 125 VAL A N   1 
ATOM 864  C CA  . VAL A 1 126 ? 15.498 -2.877  8.786  1.00 57.32  ? 125 VAL A CA  1 
ATOM 865  C C   . VAL A 1 126 ? 16.238 -1.700  9.411  1.00 52.52  ? 125 VAL A C   1 
ATOM 866  O O   . VAL A 1 126 ? 15.615 -0.762  9.925  1.00 55.38  ? 125 VAL A O   1 
ATOM 867  C CB  . VAL A 1 126 ? 15.371 -4.063  9.758  1.00 48.05  ? 125 VAL A CB  1 
ATOM 868  C CG1 . VAL A 1 126 ? 14.868 -3.605  11.110 1.00 52.80  ? 125 VAL A CG1 1 
ATOM 869  C CG2 . VAL A 1 126 ? 14.440 -5.112  9.176  1.00 53.34  ? 125 VAL A CG2 1 
ATOM 870  N N   . GLN A 1 127 ? 17.573 -1.718  9.368  1.00 51.53  ? 126 GLN A N   1 
ATOM 871  C CA  . GLN A 1 127 ? 18.348 -0.642  9.974  1.00 53.45  ? 126 GLN A CA  1 
ATOM 872  C C   . GLN A 1 127 ? 18.149 0.689   9.263  1.00 59.77  ? 126 GLN A C   1 
ATOM 873  O O   . GLN A 1 127 ? 18.392 1.740   9.865  1.00 58.42  ? 126 GLN A O   1 
ATOM 874  C CB  . GLN A 1 127 ? 19.833 -1.007  10.002 1.00 51.78  ? 126 GLN A CB  1 
ATOM 875  C CG  . GLN A 1 127 ? 20.460 -1.232  8.634  1.00 55.51  ? 126 GLN A CG  1 
ATOM 876  C CD  . GLN A 1 127 ? 20.992 0.045   8.012  1.00 57.81  ? 126 GLN A CD  1 
ATOM 877  O OE1 . GLN A 1 127 ? 21.368 0.983   8.715  1.00 63.40  ? 126 GLN A OE1 1 
ATOM 878  N NE2 . GLN A 1 127 ? 21.031 0.084   6.686  1.00 57.03  ? 126 GLN A NE2 1 
ATOM 879  N N   . MET A 1 128 ? 17.724 0.672   7.997  1.00 57.21  ? 127 MET A N   1 
ATOM 880  C CA  . MET A 1 128 ? 17.369 1.921   7.333  1.00 62.99  ? 127 MET A CA  1 
ATOM 881  C C   . MET A 1 128 ? 16.150 2.558   7.990  1.00 55.90  ? 127 MET A C   1 
ATOM 882  O O   . MET A 1 128 ? 16.091 3.784   8.143  1.00 51.73  ? 127 MET A O   1 
ATOM 883  C CB  . MET A 1 128 ? 17.120 1.680   5.845  1.00 59.12  ? 127 MET A CB  1 
ATOM 884  C CG  . MET A 1 128 ? 18.380 1.723   4.994  1.00 60.67  ? 127 MET A CG  1 
ATOM 885  S SD  . MET A 1 128 ? 18.204 0.895   3.400  1.00 84.54  ? 127 MET A SD  1 
ATOM 886  C CE  . MET A 1 128 ? 16.431 0.640   3.326  1.00 76.85  ? 127 MET A CE  1 
ATOM 887  N N   . GLY A 1 129 ? 15.172 1.743   8.389  1.00 46.78  ? 128 GLY A N   1 
ATOM 888  C CA  . GLY A 1 129 ? 14.055 2.267   9.155  1.00 47.22  ? 128 GLY A CA  1 
ATOM 889  C C   . GLY A 1 129 ? 14.473 2.773   10.519 1.00 55.53  ? 128 GLY A C   1 
ATOM 890  O O   . GLY A 1 129 ? 13.836 3.670   11.077 1.00 60.03  ? 128 GLY A O   1 
ATOM 891  N N   . ILE A 1 130 ? 15.543 2.205   11.078 1.00 56.71  ? 129 ILE A N   1 
ATOM 892  C CA  . ILE A 1 130 ? 16.097 2.727   12.324 1.00 59.88  ? 129 ILE A CA  1 
ATOM 893  C C   . ILE A 1 130 ? 16.609 4.145   12.115 1.00 56.72  ? 129 ILE A C   1 
ATOM 894  O O   . ILE A 1 130 ? 16.223 5.078   12.829 1.00 59.03  ? 129 ILE A O   1 
ATOM 895  C CB  . ILE A 1 130 ? 17.216 1.805   12.843 1.00 55.70  ? 129 ILE A CB  1 
ATOM 896  C CG1 . ILE A 1 130 ? 16.652 0.454   13.273 1.00 60.98  ? 129 ILE A CG1 1 
ATOM 897  C CG2 . ILE A 1 130 ? 17.947 2.462   13.999 1.00 51.12  ? 129 ILE A CG2 1 
ATOM 898  C CD1 . ILE A 1 130 ? 15.411 0.563   14.098 1.00 55.15  ? 129 ILE A CD1 1 
ATOM 899  N N   . ALA A 1 131 ? 17.478 4.325   11.119 1.00 55.44  ? 130 ALA A N   1 
ATOM 900  C CA  . ALA A 1 131 ? 18.145 5.607   10.922 1.00 63.89  ? 130 ALA A CA  1 
ATOM 901  C C   . ALA A 1 131 ? 17.150 6.703   10.566 1.00 61.38  ? 130 ALA A C   1 
ATOM 902  O O   . ALA A 1 131 ? 17.158 7.784   11.166 1.00 64.12  ? 130 ALA A O   1 
ATOM 903  C CB  . ALA A 1 131 ? 19.207 5.476   9.834  1.00 57.74  ? 130 ALA A CB  1 
ATOM 904  N N   . TRP A 1 132 ? 16.284 6.444   9.585  1.00 53.38  ? 131 TRP A N   1 
ATOM 905  C CA  . TRP A 1 132 ? 15.351 7.472   9.140  1.00 54.35  ? 131 TRP A CA  1 
ATOM 906  C C   . TRP A 1 132 ? 14.300 7.766   10.203 1.00 60.46  ? 131 TRP A C   1 
ATOM 907  O O   . TRP A 1 132 ? 13.956 8.931   10.433 1.00 66.92  ? 131 TRP A O   1 
ATOM 908  C CB  . TRP A 1 132 ? 14.699 7.052   7.824  1.00 52.66  ? 131 TRP A CB  1 
ATOM 909  C CG  . TRP A 1 132 ? 15.666 7.073   6.679  1.00 52.62  ? 131 TRP A CG  1 
ATOM 910  C CD1 . TRP A 1 132 ? 16.201 5.995   6.035  1.00 61.02  ? 131 TRP A CD1 1 
ATOM 911  C CD2 . TRP A 1 132 ? 16.234 8.232   6.058  1.00 55.62  ? 131 TRP A CD2 1 
ATOM 912  N NE1 . TRP A 1 132 ? 17.058 6.410   5.047  1.00 54.36  ? 131 TRP A NE1 1 
ATOM 913  C CE2 . TRP A 1 132 ? 17.096 7.779   5.040  1.00 59.59  ? 131 TRP A CE2 1 
ATOM 914  C CE3 . TRP A 1 132 ? 16.094 9.609   6.261  1.00 63.13  ? 131 TRP A CE3 1 
ATOM 915  C CZ2 . TRP A 1 132 ? 17.814 8.653   4.227  1.00 56.03  ? 131 TRP A CZ2 1 
ATOM 916  C CZ3 . TRP A 1 132 ? 16.807 10.474  5.453  1.00 44.18  ? 131 TRP A CZ3 1 
ATOM 917  C CH2 . TRP A 1 132 ? 17.656 9.993   4.449  1.00 50.86  ? 131 TRP A CH2 1 
ATOM 918  N N   . GLY A 1 133 ? 13.780 6.728   10.861 1.00 55.81  ? 132 GLY A N   1 
ATOM 919  C CA  . GLY A 1 133 ? 12.835 6.952   11.944 1.00 59.27  ? 132 GLY A CA  1 
ATOM 920  C C   . GLY A 1 133 ? 13.422 7.800   13.054 1.00 60.01  ? 132 GLY A C   1 
ATOM 921  O O   . GLY A 1 133 ? 12.776 8.722   13.557 1.00 62.83  ? 132 GLY A O   1 
ATOM 922  N N   . ASN A 1 134 ? 14.667 7.509   13.439 1.00 59.22  ? 133 ASN A N   1 
ATOM 923  C CA  . ASN A 1 134 ? 15.318 8.286   14.489 1.00 69.24  ? 133 ASN A CA  1 
ATOM 924  C C   . ASN A 1 134 ? 15.556 9.724   14.046 1.00 67.92  ? 133 ASN A C   1 
ATOM 925  O O   . ASN A 1 134 ? 15.373 10.659  14.834 1.00 63.28  ? 133 ASN A O   1 
ATOM 926  C CB  . ASN A 1 134 ? 16.636 7.625   14.887 1.00 69.78  ? 133 ASN A CB  1 
ATOM 927  C CG  . ASN A 1 134 ? 16.432 6.347   15.672 1.00 60.64  ? 133 ASN A CG  1 
ATOM 928  O OD1 . ASN A 1 134 ? 15.302 5.967   15.979 1.00 54.52  ? 133 ASN A OD1 1 
ATOM 929  N ND2 . ASN A 1 134 ? 17.528 5.668   15.993 1.00 59.09  ? 133 ASN A ND2 1 
ATOM 930  N N   . LEU A 1 135 ? 15.967 9.917   12.790 1.00 69.45  ? 134 LEU A N   1 
ATOM 931  C CA  . LEU A 1 135 ? 16.192 11.267  12.282 1.00 67.84  ? 134 LEU A CA  1 
ATOM 932  C C   . LEU A 1 135 ? 14.898 12.070  12.273 1.00 57.38  ? 134 LEU A C   1 
ATOM 933  O O   . LEU A 1 135 ? 14.897 13.265  12.594 1.00 44.57  ? 134 LEU A O   1 
ATOM 934  C CB  . LEU A 1 135 ? 16.806 11.200  10.880 1.00 69.98  ? 134 LEU A CB  1 
ATOM 935  C CG  . LEU A 1 135 ? 17.224 12.485  10.151 1.00 72.88  ? 134 LEU A CG  1 
ATOM 936  C CD1 . LEU A 1 135 ? 16.063 13.135  9.390  1.00 59.91  ? 134 LEU A CD1 1 
ATOM 937  C CD2 . LEU A 1 135 ? 17.857 13.470  11.119 1.00 60.62  ? 134 LEU A CD2 1 
ATOM 938  N N   . LEU A 1 136 ? 13.785 11.429  11.909 1.00 54.96  ? 135 LEU A N   1 
ATOM 939  C CA  . LEU A 1 136 ? 12.494 12.110  11.911 1.00 53.00  ? 135 LEU A CA  1 
ATOM 940  C C   . LEU A 1 136 ? 12.038 12.447  13.321 1.00 60.08  ? 135 LEU A C   1 
ATOM 941  O O   . LEU A 1 136 ? 11.390 13.478  13.530 1.00 62.65  ? 135 LEU A O   1 
ATOM 942  C CB  . LEU A 1 136 ? 11.446 11.249  11.212 1.00 57.66  ? 135 LEU A CB  1 
ATOM 943  C CG  . LEU A 1 136 ? 11.256 11.466  9.714  1.00 60.84  ? 135 LEU A CG  1 
ATOM 944  C CD1 . LEU A 1 136 ? 12.498 11.078  8.950  1.00 56.26  ? 135 LEU A CD1 1 
ATOM 945  C CD2 . LEU A 1 136 ? 10.100 10.626  9.250  1.00 55.43  ? 135 LEU A CD2 1 
ATOM 946  N N   . LEU A 1 137 ? 12.358 11.593  14.295 1.00 61.33  ? 136 LEU A N   1 
ATOM 947  C CA  . LEU A 1 137 ? 12.009 11.893  15.680 1.00 57.05  ? 136 LEU A CA  1 
ATOM 948  C C   . LEU A 1 137 ? 12.888 13.003  16.240 1.00 58.05  ? 136 LEU A C   1 
ATOM 949  O O   . LEU A 1 137 ? 12.390 13.918  16.907 1.00 56.93  ? 136 LEU A O   1 
ATOM 950  C CB  . LEU A 1 137 ? 12.119 10.633  16.534 1.00 53.33  ? 136 LEU A CB  1 
ATOM 951  C CG  . LEU A 1 137 ? 11.079 9.553   16.240 1.00 51.86  ? 136 LEU A CG  1 
ATOM 952  C CD1 . LEU A 1 137 ? 11.438 8.260   16.954 1.00 56.95  ? 136 LEU A CD1 1 
ATOM 953  C CD2 . LEU A 1 137 ? 9.686  10.026  16.636 1.00 55.96  ? 136 LEU A CD2 1 
ATOM 954  N N   . ALA A 1 138 ? 14.197 12.941  15.981 1.00 54.14  ? 137 ALA A N   1 
ATOM 955  C CA  . ALA A 1 138 ? 15.088 14.013  16.412 1.00 59.93  ? 137 ALA A CA  1 
ATOM 956  C C   . ALA A 1 138 ? 14.681 15.349  15.811 1.00 67.85  ? 137 ALA A C   1 
ATOM 957  O O   . ALA A 1 138 ? 14.861 16.395  16.445 1.00 62.99  ? 137 ALA A O   1 
ATOM 958  C CB  . ALA A 1 138 ? 16.531 13.683  16.038 1.00 60.77  ? 137 ALA A CB  1 
ATOM 959  N N   . LEU A 1 139 ? 14.137 15.335  14.591 1.00 63.64  ? 138 LEU A N   1 
ATOM 960  C CA  . LEU A 1 139 ? 13.615 16.559  13.993 1.00 59.48  ? 138 LEU A CA  1 
ATOM 961  C C   . LEU A 1 139 ? 12.469 17.125  14.822 1.00 66.31  ? 138 LEU A C   1 
ATOM 962  O O   . LEU A 1 139 ? 12.463 18.313  15.166 1.00 73.89  ? 138 LEU A O   1 
ATOM 963  C CB  . LEU A 1 139 ? 13.155 16.289  12.559 1.00 57.07  ? 138 LEU A CB  1 
ATOM 964  C CG  . LEU A 1 139 ? 14.079 16.697  11.408 1.00 51.50  ? 138 LEU A CG  1 
ATOM 965  C CD1 . LEU A 1 139 ? 15.524 16.334  11.696 1.00 48.19  ? 138 LEU A CD1 1 
ATOM 966  C CD2 . LEU A 1 139 ? 13.615 16.055  10.108 1.00 56.12  ? 138 LEU A CD2 1 
ATOM 967  N N   . MET A 1 140 ? 11.488 16.284  15.157 1.00 57.30  ? 139 MET A N   1 
ATOM 968  C CA  . MET A 1 140 ? 10.347 16.744  15.941 1.00 64.47  ? 139 MET A CA  1 
ATOM 969  C C   . MET A 1 140 ? 10.745 17.164  17.349 1.00 66.23  ? 139 MET A C   1 
ATOM 970  O O   . MET A 1 140 ? 10.038 17.967  17.965 1.00 63.15  ? 139 MET A O   1 
ATOM 971  C CB  . MET A 1 140 ? 9.278  15.655  16.007 1.00 60.02  ? 139 MET A CB  1 
ATOM 972  C CG  . MET A 1 140 ? 8.580  15.394  14.688 1.00 57.87  ? 139 MET A CG  1 
ATOM 973  S SD  . MET A 1 140 ? 6.947  14.670  14.905 1.00 71.47  ? 139 MET A SD  1 
ATOM 974  C CE  . MET A 1 140 ? 7.065  13.300  13.763 1.00 57.83  ? 139 MET A CE  1 
ATOM 975  N N   . LYS A 1 141 ? 11.854 16.637  17.873 1.00 69.76  ? 140 LYS A N   1 
ATOM 976  C CA  . LYS A 1 141 ? 12.340 17.091  19.172 1.00 73.24  ? 140 LYS A CA  1 
ATOM 977  C C   . LYS A 1 141 ? 12.878 18.514  19.084 1.00 82.05  ? 140 LYS A C   1 
ATOM 978  O O   . LYS A 1 141 ? 12.551 19.365  19.919 1.00 86.17  ? 140 LYS A O   1 
ATOM 979  C CB  . LYS A 1 141 ? 13.419 16.143  19.696 1.00 66.30  ? 140 LYS A CB  1 
ATOM 980  C CG  . LYS A 1 141 ? 12.942 14.727  19.966 1.00 66.72  ? 140 LYS A CG  1 
ATOM 981  C CD  . LYS A 1 141 ? 14.080 13.852  20.471 1.00 73.30  ? 140 LYS A CD  1 
ATOM 982  C CE  . LYS A 1 141 ? 14.099 12.502  19.768 1.00 71.68  ? 140 LYS A CE  1 
ATOM 983  N NZ  . LYS A 1 141 ? 15.476 11.937  19.689 1.00 69.86  ? 140 LYS A NZ  1 
ATOM 984  N N   . GLY A 1 142 ? 13.703 18.792  18.073 1.00 71.77  ? 141 GLY A N   1 
ATOM 985  C CA  . GLY A 1 142 ? 14.301 20.108  17.946 1.00 62.29  ? 141 GLY A CA  1 
ATOM 986  C C   . GLY A 1 142 ? 13.309 21.215  17.666 1.00 70.72  ? 141 GLY A C   1 
ATOM 987  O O   . GLY A 1 142 ? 13.644 22.393  17.829 1.00 73.54  ? 141 GLY A O   1 
ATOM 988  N N   . PHE A 1 143 ? 12.099 20.867  17.239 1.00 70.57  ? 142 PHE A N   1 
ATOM 989  C CA  . PHE A 1 143 ? 11.032 21.836  17.043 1.00 66.41  ? 142 PHE A CA  1 
ATOM 990  C C   . PHE A 1 143 ? 10.124 21.934  18.262 1.00 77.06  ? 142 PHE A C   1 
ATOM 991  O O   . PHE A 1 143 ? 9.040  22.519  18.171 1.00 76.93  ? 142 PHE A O   1 
ATOM 992  C CB  . PHE A 1 143 ? 10.209 21.491  15.800 1.00 66.24  ? 142 PHE A CB  1 
ATOM 993  C CG  . PHE A 1 143 ? 10.933 21.673  14.483 1.00 79.12  ? 142 PHE A CG  1 
ATOM 994  C CD1 . PHE A 1 143 ? 10.265 22.219  13.399 1.00 83.50  ? 142 PHE A CD1 1 
ATOM 995  C CD2 . PHE A 1 143 ? 12.253 21.275  14.312 1.00 79.24  ? 142 PHE A CD2 1 
ATOM 996  C CE1 . PHE A 1 143 ? 10.899 22.394  12.179 1.00 81.79  ? 142 PHE A CE1 1 
ATOM 997  C CE2 . PHE A 1 143 ? 12.894 21.441  13.091 1.00 76.24  ? 142 PHE A CE2 1 
ATOM 998  C CZ  . PHE A 1 143 ? 12.216 22.004  12.024 1.00 78.15  ? 142 PHE A CZ  1 
ATOM 999  N N   . ARG A 1 144 ? 10.548 21.363  19.394 1.00 82.68  ? 143 ARG A N   1 
ATOM 1000 C CA  . ARG A 1 144 ? 9.768  21.340  20.634 1.00 83.39  ? 143 ARG A CA  1 
ATOM 1001 C C   . ARG A 1 144 ? 8.390  20.717  20.427 1.00 85.20  ? 143 ARG A C   1 
ATOM 1002 O O   . ARG A 1 144 ? 7.412  21.114  21.066 1.00 90.64  ? 143 ARG A O   1 
ATOM 1003 C CB  . ARG A 1 144 ? 9.641  22.741  21.241 1.00 90.49  ? 143 ARG A CB  1 
ATOM 1004 C CG  . ARG A 1 144 ? 10.938 23.539  21.243 1.00 90.34  ? 143 ARG A CG  1 
ATOM 1005 C CD  . ARG A 1 144 ? 11.951 22.961  22.222 1.00 99.09  ? 143 ARG A CD  1 
ATOM 1006 N NE  . ARG A 1 144 ? 13.119 23.823  22.363 1.00 104.06 ? 143 ARG A NE  1 
ATOM 1007 C CZ  . ARG A 1 144 ? 14.269 23.449  22.908 1.00 104.77 ? 143 ARG A CZ  1 
ATOM 1008 N NH1 . ARG A 1 144 ? 14.446 22.225  23.378 1.00 105.38 ? 143 ARG A NH1 1 
ATOM 1009 N NH2 . ARG A 1 144 ? 15.266 24.326  22.984 1.00 100.34 ? 143 ARG A NH2 1 
ATOM 1010 N N   . ASP A 1 145 ? 8.305  19.734  19.532 1.00 76.06  ? 144 ASP A N   1 
ATOM 1011 C CA  . ASP A 1 145 ? 7.047  19.048  19.246 1.00 70.64  ? 144 ASP A CA  1 
ATOM 1012 C C   . ASP A 1 145 ? 6.985  17.743  20.041 1.00 75.42  ? 144 ASP A C   1 
ATOM 1013 O O   . ASP A 1 145 ? 7.095  16.638  19.508 1.00 73.75  ? 144 ASP A O   1 
ATOM 1014 C CB  . ASP A 1 145 ? 6.906  18.803  17.746 1.00 54.87  ? 144 ASP A CB  1 
ATOM 1015 C CG  . ASP A 1 145 ? 5.523  18.314  17.363 1.00 62.01  ? 144 ASP A CG  1 
ATOM 1016 O OD1 . ASP A 1 145 ? 4.609  18.384  18.212 1.00 55.25  ? 144 ASP A OD1 1 
ATOM 1017 O OD2 . ASP A 1 145 ? 5.346  17.858  16.213 1.00 70.58  ? 144 ASP A OD2 1 
ATOM 1018 N N   . ALA A 1 146 ? 6.803  17.901  21.354 1.00 72.45  ? 145 ALA A N   1 
ATOM 1019 C CA  . ALA A 1 146 ? 6.723  16.741  22.235 1.00 70.52  ? 145 ALA A CA  1 
ATOM 1020 C C   . ALA A 1 146 ? 5.484  15.902  21.950 1.00 72.30  ? 145 ALA A C   1 
ATOM 1021 O O   . ALA A 1 146 ? 5.500  14.684  22.163 1.00 69.71  ? 145 ALA A O   1 
ATOM 1022 C CB  . ALA A 1 146 ? 6.736  17.188  23.697 1.00 82.49  ? 145 ALA A CB  1 
ATOM 1023 N N   . ALA A 1 147 ? 4.410  16.531  21.468 1.00 62.91  ? 146 ALA A N   1 
ATOM 1024 C CA  . ALA A 1 147 ? 3.186  15.794  21.174 1.00 72.49  ? 146 ALA A CA  1 
ATOM 1025 C C   . ALA A 1 147 ? 3.371  14.877  19.971 1.00 74.59  ? 146 ALA A C   1 
ATOM 1026 O O   . ALA A 1 147 ? 3.067  13.680  20.038 1.00 69.82  ? 146 ALA A O   1 
ATOM 1027 C CB  . ALA A 1 147 ? 2.033  16.770  20.938 1.00 61.44  ? 146 ALA A CB  1 
ATOM 1028 N N   . GLY A 1 148 ? 3.867  15.423  18.858 1.00 68.12  ? 147 GLY A N   1 
ATOM 1029 C CA  . GLY A 1 148 ? 4.098  14.604  17.681 1.00 62.90  ? 147 GLY A CA  1 
ATOM 1030 C C   . GLY A 1 148 ? 5.146  13.532  17.897 1.00 62.89  ? 147 GLY A C   1 
ATOM 1031 O O   . GLY A 1 148 ? 5.073  12.457  17.295 1.00 62.53  ? 147 GLY A O   1 
ATOM 1032 N N   . ASN A 1 149 ? 6.131  13.803  18.755 1.00 63.41  ? 148 ASN A N   1 
ATOM 1033 C CA  . ASN A 1 149 ? 7.141  12.797  19.064 1.00 61.45  ? 148 ASN A CA  1 
ATOM 1034 C C   . ASN A 1 149 ? 6.552  11.668  19.898 1.00 69.67  ? 148 ASN A C   1 
ATOM 1035 O O   . ASN A 1 149 ? 6.723  10.487  19.574 1.00 63.01  ? 148 ASN A O   1 
ATOM 1036 C CB  . ASN A 1 149 ? 8.320  13.442  19.792 1.00 53.70  ? 148 ASN A CB  1 
ATOM 1037 C CG  . ASN A 1 149 ? 9.610  12.669  19.610 1.00 60.61  ? 148 ASN A CG  1 
ATOM 1038 O OD1 . ASN A 1 149 ? 10.485 13.075  18.848 1.00 63.62  ? 148 ASN A OD1 1 
ATOM 1039 N ND2 . ASN A 1 149 ? 9.735  11.548  20.311 1.00 62.13  ? 148 ASN A ND2 1 
ATOM 1040 N N   . ALA A 1 150 ? 5.855  12.015  20.983 1.00 90.44  ? 149 ALA A N   1 
ATOM 1041 C CA  . ALA A 1 150 ? 5.289  10.993  21.857 1.00 91.21  ? 149 ALA A CA  1 
ATOM 1042 C C   . ALA A 1 150 ? 4.212  10.187  21.144 1.00 90.07  ? 149 ALA A C   1 
ATOM 1043 O O   . ALA A 1 150 ? 4.101  8.973   21.350 1.00 89.77  ? 149 ALA A O   1 
ATOM 1044 C CB  . ALA A 1 150 ? 4.728  11.638  23.123 1.00 91.45  ? 149 ALA A CB  1 
ATOM 1045 N N   . LEU A 1 151 ? 3.408  10.842  20.304 1.00 66.96  ? 150 LEU A N   1 
ATOM 1046 C CA  . LEU A 1 151 ? 2.387  10.118  19.557 1.00 66.17  ? 150 LEU A CA  1 
ATOM 1047 C C   . LEU A 1 151 ? 3.021  9.139   18.577 1.00 64.73  ? 150 LEU A C   1 
ATOM 1048 O O   . LEU A 1 151 ? 2.657  7.958   18.544 1.00 68.16  ? 150 LEU A O   1 
ATOM 1049 C CB  . LEU A 1 151 ? 1.465  11.098  18.831 1.00 66.83  ? 150 LEU A CB  1 
ATOM 1050 C CG  . LEU A 1 151 ? 0.064  10.575  18.500 1.00 62.61  ? 150 LEU A CG  1 
ATOM 1051 C CD1 . LEU A 1 151 ? -0.457 9.654   19.598 1.00 66.30  ? 150 LEU A CD1 1 
ATOM 1052 C CD2 . LEU A 1 151 ? -0.900 11.726  18.263 1.00 66.15  ? 150 LEU A CD2 1 
ATOM 1053 N N   . SER A 1 152 ? 3.988  9.609   17.782 1.00 60.07  ? 151 SER A N   1 
ATOM 1054 C CA  . SER A 1 152 ? 4.696  8.719   16.864 1.00 63.03  ? 151 SER A CA  1 
ATOM 1055 C C   . SER A 1 152 ? 5.343  7.551   17.596 1.00 66.13  ? 151 SER A C   1 
ATOM 1056 O O   . SER A 1 152 ? 5.407  6.440   17.057 1.00 64.13  ? 151 SER A O   1 
ATOM 1057 C CB  . SER A 1 152 ? 5.751  9.500   16.083 1.00 54.58  ? 151 SER A CB  1 
ATOM 1058 O OG  . SER A 1 152 ? 5.160  10.510  15.288 1.00 54.70  ? 151 SER A OG  1 
ATOM 1059 N N   . LEU A 1 153 ? 5.825  7.779   18.820 1.00 67.15  ? 152 LEU A N   1 
ATOM 1060 C CA  . LEU A 1 153 ? 6.408  6.696   19.603 1.00 56.94  ? 152 LEU A CA  1 
ATOM 1061 C C   . LEU A 1 153 ? 5.341  5.739   20.116 1.00 65.18  ? 152 LEU A C   1 
ATOM 1062 O O   . LEU A 1 153 ? 5.602  4.538   20.251 1.00 55.97  ? 152 LEU A O   1 
ATOM 1063 C CB  . LEU A 1 153 ? 7.208  7.268   20.772 1.00 45.83  ? 152 LEU A CB  1 
ATOM 1064 C CG  . LEU A 1 153 ? 8.599  7.815   20.446 1.00 47.38  ? 152 LEU A CG  1 
ATOM 1065 C CD1 . LEU A 1 153 ? 9.303  8.294   21.707 1.00 49.36  ? 152 LEU A CD1 1 
ATOM 1066 C CD2 . LEU A 1 153 ? 9.436  6.773   19.723 1.00 39.76  ? 152 LEU A CD2 1 
ATOM 1067 N N   . ILE A 1 154 ? 4.143  6.246   20.411 1.00 60.87  ? 153 ILE A N   1 
ATOM 1068 C CA  . ILE A 1 154 ? 3.073  5.382   20.898 1.00 59.41  ? 153 ILE A CA  1 
ATOM 1069 C C   . ILE A 1 154 ? 2.563  4.482   19.778 1.00 59.07  ? 153 ILE A C   1 
ATOM 1070 O O   . ILE A 1 154 ? 2.473  3.260   19.940 1.00 64.34  ? 153 ILE A O   1 
ATOM 1071 C CB  . ILE A 1 154 ? 1.939  6.221   21.514 1.00 58.36  ? 153 ILE A CB  1 
ATOM 1072 C CG1 . ILE A 1 154 ? 2.366  6.765   22.878 1.00 66.48  ? 153 ILE A CG1 1 
ATOM 1073 C CG2 . ILE A 1 154 ? 0.673  5.390   21.650 1.00 49.34  ? 153 ILE A CG2 1 
ATOM 1074 C CD1 . ILE A 1 154 ? 1.418  7.794   23.447 1.00 68.73  ? 153 ILE A CD1 1 
ATOM 1075 N N   . VAL A 1 155 ? 2.225  5.068   18.625 1.00 59.18  ? 154 VAL A N   1 
ATOM 1076 C CA  . VAL A 1 155 ? 1.752  4.264   17.499 1.00 61.76  ? 154 VAL A CA  1 
ATOM 1077 C C   . VAL A 1 155 ? 2.829  3.286   17.049 1.00 56.11  ? 154 VAL A C   1 
ATOM 1078 O O   . VAL A 1 155 ? 2.541  2.124   16.738 1.00 57.34  ? 154 VAL A O   1 
ATOM 1079 C CB  . VAL A 1 155 ? 1.290  5.166   16.338 1.00 61.38  ? 154 VAL A CB  1 
ATOM 1080 C CG1 . VAL A 1 155 ? 0.371  4.391   15.408 1.00 49.54  ? 154 VAL A CG1 1 
ATOM 1081 C CG2 . VAL A 1 155 ? 0.570  6.389   16.868 1.00 56.05  ? 154 VAL A CG2 1 
ATOM 1082 N N   . GLY A 1 156 ? 4.086  3.735   17.017 1.00 61.36  ? 155 GLY A N   1 
ATOM 1083 C CA  . GLY A 1 156 ? 5.163  2.859   16.583 1.00 62.60  ? 155 GLY A CA  1 
ATOM 1084 C C   . GLY A 1 156 ? 5.342  1.655   17.487 1.00 63.02  ? 155 GLY A C   1 
ATOM 1085 O O   . GLY A 1 156 ? 5.582  0.541   17.013 1.00 62.85  ? 155 GLY A O   1 
ATOM 1086 N N   . SER A 1 157 ? 5.229  1.859   18.801 1.00 59.66  ? 156 SER A N   1 
ATOM 1087 C CA  . SER A 1 157 ? 5.336  0.737   19.726 1.00 57.47  ? 156 SER A CA  1 
ATOM 1088 C C   . SER A 1 157 ? 4.127  -0.183  19.630 1.00 58.35  ? 156 SER A C   1 
ATOM 1089 O O   . SER A 1 157 ? 4.255  -1.394  19.843 1.00 59.27  ? 156 SER A O   1 
ATOM 1090 C CB  . SER A 1 157 ? 5.502  1.246   21.157 1.00 61.36  ? 156 SER A CB  1 
ATOM 1091 O OG  . SER A 1 157 ? 4.368  1.989   21.568 1.00 66.65  ? 156 SER A OG  1 
ATOM 1092 N N   . LEU A 1 158 ? 2.952  0.365   19.312 1.00 54.48  ? 157 LEU A N   1 
ATOM 1093 C CA  . LEU A 1 158 ? 1.762  -0.468  19.164 1.00 55.78  ? 157 LEU A CA  1 
ATOM 1094 C C   . LEU A 1 158 ? 1.850  -1.329  17.909 1.00 61.98  ? 157 LEU A C   1 
ATOM 1095 O O   . LEU A 1 158 ? 1.637  -2.546  17.963 1.00 57.98  ? 157 LEU A O   1 
ATOM 1096 C CB  . LEU A 1 158 ? 0.504  0.401   19.130 1.00 50.73  ? 157 LEU A CB  1 
ATOM 1097 C CG  . LEU A 1 158 ? 0.131  1.215   20.372 1.00 56.81  ? 157 LEU A CG  1 
ATOM 1098 C CD1 . LEU A 1 158 ? -1.380 1.336   20.488 1.00 54.39  ? 157 LEU A CD1 1 
ATOM 1099 C CD2 . LEU A 1 158 ? 0.723  0.614   21.642 1.00 58.96  ? 157 LEU A CD2 1 
ATOM 1100 N N   . ILE A 1 159 ? 2.164  -0.713  16.766 1.00 57.58  ? 158 ILE A N   1 
ATOM 1101 C CA  . ILE A 1 159 ? 2.315  -1.485  15.537 1.00 62.16  ? 158 ILE A CA  1 
ATOM 1102 C C   . ILE A 1 159 ? 3.497  -2.436  15.642 1.00 59.47  ? 158 ILE A C   1 
ATOM 1103 O O   . ILE A 1 159 ? 3.546  -3.459  14.947 1.00 60.86  ? 158 ILE A O   1 
ATOM 1104 C CB  . ILE A 1 159 ? 2.448  -0.548  14.320 1.00 56.10  ? 158 ILE A CB  1 
ATOM 1105 C CG1 . ILE A 1 159 ? 3.763  0.232   14.378 1.00 53.07  ? 158 ILE A CG1 1 
ATOM 1106 C CG2 . ILE A 1 159 ? 1.259  0.397   14.247 1.00 41.96  ? 158 ILE A CG2 1 
ATOM 1107 C CD1 . ILE A 1 159 ? 3.955  1.186   13.223 1.00 53.33  ? 158 ILE A CD1 1 
ATOM 1108 N N   . GLY A 1 160 ? 4.464  -2.125  16.507 1.00 54.91  ? 159 GLY A N   1 
ATOM 1109 C CA  . GLY A 1 160 ? 5.551  -3.060  16.743 1.00 52.52  ? 159 GLY A CA  1 
ATOM 1110 C C   . GLY A 1 160 ? 5.063  -4.350  17.372 1.00 57.82  ? 159 GLY A C   1 
ATOM 1111 O O   . GLY A 1 160 ? 5.350  -5.444  16.879 1.00 56.50  ? 159 GLY A O   1 
ATOM 1112 N N   . VAL A 1 161 ? 4.308  -4.235  18.469 1.00 58.11  ? 160 VAL A N   1 
ATOM 1113 C CA  . VAL A 1 161 ? 3.727  -5.413  19.110 1.00 55.19  ? 160 VAL A CA  1 
ATOM 1114 C C   . VAL A 1 161 ? 2.906  -6.208  18.105 1.00 53.90  ? 160 VAL A C   1 
ATOM 1115 O O   . VAL A 1 161 ? 2.974  -7.443  18.059 1.00 56.22  ? 160 VAL A O   1 
ATOM 1116 C CB  . VAL A 1 161 ? 2.885  -4.994  20.331 1.00 58.94  ? 160 VAL A CB  1 
ATOM 1117 C CG1 . VAL A 1 161 ? 1.923  -6.104  20.731 1.00 46.38  ? 160 VAL A CG1 1 
ATOM 1118 C CG2 . VAL A 1 161 ? 3.791  -4.622  21.495 1.00 51.67  ? 160 VAL A CG2 1 
ATOM 1119 N N   . LEU A 1 162 ? 2.130  -5.510  17.271 1.00 59.13  ? 161 LEU A N   1 
ATOM 1120 C CA  . LEU A 1 162 ? 1.420  -6.178  16.186 1.00 58.29  ? 161 LEU A CA  1 
ATOM 1121 C C   . LEU A 1 162 ? 2.391  -6.884  15.249 1.00 58.37  ? 161 LEU A C   1 
ATOM 1122 O O   . LEU A 1 162 ? 2.157  -8.029  14.845 1.00 63.31  ? 161 LEU A O   1 
ATOM 1123 C CB  . LEU A 1 162 ? 0.573  -5.168  15.412 1.00 54.56  ? 161 LEU A CB  1 
ATOM 1124 C CG  . LEU A 1 162 ? -0.931 -5.182  15.683 1.00 61.59  ? 161 LEU A CG  1 
ATOM 1125 C CD1 . LEU A 1 162 ? -1.516 -6.546  15.365 1.00 67.97  ? 161 LEU A CD1 1 
ATOM 1126 C CD2 . LEU A 1 162 ? -1.222 -4.794  17.123 1.00 75.24  ? 161 LEU A CD2 1 
ATOM 1127 N N   . ALA A 1 163 ? 3.495  -6.218  14.901 1.00 52.18  ? 162 ALA A N   1 
ATOM 1128 C CA  . ALA A 1 163 ? 4.469  -6.820  13.998 1.00 55.82  ? 162 ALA A CA  1 
ATOM 1129 C C   . ALA A 1 163 ? 5.175  -8.002  14.649 1.00 50.15  ? 162 ALA A C   1 
ATOM 1130 O O   . ALA A 1 163 ? 5.457  -9.003  13.983 1.00 44.67  ? 162 ALA A O   1 
ATOM 1131 C CB  . ALA A 1 163 ? 5.484  -5.772  13.544 1.00 49.01  ? 162 ALA A CB  1 
ATOM 1132 N N   . TYR A 1 164 ? 5.468  -7.906  15.949 1.00 51.21  ? 163 TYR A N   1 
ATOM 1133 C CA  . TYR A 1 164 ? 6.178  -8.988  16.625 1.00 49.71  ? 163 TYR A CA  1 
ATOM 1134 C C   . TYR A 1 164 ? 5.324  -10.246 16.709 1.00 48.53  ? 163 TYR A C   1 
ATOM 1135 O O   . TYR A 1 164 ? 5.839  -11.361 16.558 1.00 45.42  ? 163 TYR A O   1 
ATOM 1136 C CB  . TYR A 1 164 ? 6.616  -8.543  18.022 1.00 50.92  ? 163 TYR A CB  1 
ATOM 1137 C CG  . TYR A 1 164 ? 7.294  -9.629  18.835 1.00 47.36  ? 163 TYR A CG  1 
ATOM 1138 C CD1 . TYR A 1 164 ? 8.657  -9.868  18.709 1.00 47.36  ? 163 TYR A CD1 1 
ATOM 1139 C CD2 . TYR A 1 164 ? 6.574  -10.405 19.736 1.00 39.88  ? 163 TYR A CD2 1 
ATOM 1140 C CE1 . TYR A 1 164 ? 9.281  -10.855 19.452 1.00 43.31  ? 163 TYR A CE1 1 
ATOM 1141 C CE2 . TYR A 1 164 ? 7.190  -11.394 20.481 1.00 43.20  ? 163 TYR A CE2 1 
ATOM 1142 C CZ  . TYR A 1 164 ? 8.543  -11.615 20.336 1.00 47.51  ? 163 TYR A CZ  1 
ATOM 1143 O OH  . TYR A 1 164 ? 9.157  -12.599 21.077 1.00 50.56  ? 163 TYR A OH  1 
ATOM 1144 N N   . TYR A 1 165 ? 4.020  -10.091 16.951 1.00 46.58  ? 164 TYR A N   1 
ATOM 1145 C CA  . TYR A 1 165 ? 3.149  -11.255 17.080 1.00 44.98  ? 164 TYR A CA  1 
ATOM 1146 C C   . TYR A 1 165 ? 3.106  -12.053 15.783 1.00 45.82  ? 164 TYR A C   1 
ATOM 1147 O O   . TYR A 1 165 ? 3.393  -13.255 15.768 1.00 53.09  ? 164 TYR A O   1 
ATOM 1148 C CB  . TYR A 1 165 ? 1.740  -10.827 17.492 1.00 41.57  ? 164 TYR A CB  1 
ATOM 1149 C CG  . TYR A 1 165 ? 0.762  -11.981 17.508 1.00 41.61  ? 164 TYR A CG  1 
ATOM 1150 C CD1 . TYR A 1 165 ? 0.826  -12.957 18.495 1.00 48.97  ? 164 TYR A CD1 1 
ATOM 1151 C CD2 . TYR A 1 165 ? -0.209 -12.108 16.524 1.00 43.37  ? 164 TYR A CD2 1 
ATOM 1152 C CE1 . TYR A 1 165 ? -0.060 -14.019 18.510 1.00 52.45  ? 164 TYR A CE1 1 
ATOM 1153 C CE2 . TYR A 1 165 ? -1.099 -13.167 16.529 1.00 48.96  ? 164 TYR A CE2 1 
ATOM 1154 C CZ  . TYR A 1 165 ? -1.017 -14.121 17.522 1.00 59.22  ? 164 TYR A CZ  1 
ATOM 1155 O OH  . TYR A 1 165 ? -1.904 -15.175 17.533 1.00 63.41  ? 164 TYR A OH  1 
ATOM 1156 N N   . VAL A 1 166 ? 2.749  -11.394 14.677 1.00 47.68  ? 165 VAL A N   1 
ATOM 1157 C CA  . VAL A 1 166 ? 2.656  -12.090 13.397 1.00 53.11  ? 165 VAL A CA  1 
ATOM 1158 C C   . VAL A 1 166 ? 4.021  -12.602 12.958 1.00 48.76  ? 165 VAL A C   1 
ATOM 1159 O O   . VAL A 1 166 ? 4.116  -13.627 12.271 1.00 39.37  ? 165 VAL A O   1 
ATOM 1160 C CB  . VAL A 1 166 ? 2.025  -11.173 12.328 1.00 42.60  ? 165 VAL A CB  1 
ATOM 1161 C CG1 . VAL A 1 166 ? 0.648  -10.707 12.774 1.00 39.67  ? 165 VAL A CG1 1 
ATOM 1162 C CG2 . VAL A 1 166 ? 2.924  -9.982  12.045 1.00 46.67  ? 165 VAL A CG2 1 
ATOM 1163 N N   . SER A 1 167 ? 5.095  -11.919 13.356 1.00 47.11  ? 166 SER A N   1 
ATOM 1164 C CA  . SER A 1 167 ? 6.431  -12.343 12.952 1.00 46.54  ? 166 SER A CA  1 
ATOM 1165 C C   . SER A 1 167 ? 6.829  -13.638 13.651 1.00 49.01  ? 166 SER A C   1 
ATOM 1166 O O   . SER A 1 167 ? 7.315  -14.576 13.008 1.00 45.82  ? 166 SER A O   1 
ATOM 1167 C CB  . SER A 1 167 ? 7.442  -11.233 13.241 1.00 49.33  ? 166 SER A CB  1 
ATOM 1168 O OG  . SER A 1 167 ? 8.729  -11.566 12.750 1.00 53.81  ? 166 SER A OG  1 
ATOM 1169 N N   . TYR A 1 168 ? 6.621  -13.717 14.969 1.00 53.29  ? 167 TYR A N   1 
ATOM 1170 C CA  . TYR A 1 168 ? 6.993  -14.932 15.686 1.00 47.56  ? 167 TYR A CA  1 
ATOM 1171 C C   . TYR A 1 168 ? 6.003  -16.061 15.430 1.00 50.92  ? 167 TYR A C   1 
ATOM 1172 O O   . TYR A 1 168 ? 6.384  -17.236 15.476 1.00 53.36  ? 167 TYR A O   1 
ATOM 1173 C CB  . TYR A 1 168 ? 7.140  -14.641 17.187 1.00 45.52  ? 167 TYR A CB  1 
ATOM 1174 C CG  . TYR A 1 168 ? 5.910  -14.863 18.054 1.00 52.73  ? 167 TYR A CG  1 
ATOM 1175 C CD1 . TYR A 1 168 ? 5.556  -16.135 18.498 1.00 52.95  ? 167 TYR A CD1 1 
ATOM 1176 C CD2 . TYR A 1 168 ? 5.130  -13.790 18.465 1.00 52.93  ? 167 TYR A CD2 1 
ATOM 1177 C CE1 . TYR A 1 168 ? 4.442  -16.332 19.295 1.00 54.03  ? 167 TYR A CE1 1 
ATOM 1178 C CE2 . TYR A 1 168 ? 4.017  -13.978 19.267 1.00 52.66  ? 167 TYR A CE2 1 
ATOM 1179 C CZ  . TYR A 1 168 ? 3.678  -15.250 19.678 1.00 61.69  ? 167 TYR A CZ  1 
ATOM 1180 O OH  . TYR A 1 168 ? 2.571  -15.440 20.474 1.00 64.66  ? 167 TYR A OH  1 
ATOM 1181 N N   . ARG A 1 169 ? 4.738  -15.734 15.158 1.00 44.26  ? 168 ARG A N   1 
ATOM 1182 C CA  . ARG A 1 169 ? 3.766  -16.776 14.844 1.00 45.85  ? 168 ARG A CA  1 
ATOM 1183 C C   . ARG A 1 169 ? 4.073  -17.429 13.502 1.00 49.05  ? 168 ARG A C   1 
ATOM 1184 O O   . ARG A 1 169 ? 3.942  -18.649 13.355 1.00 57.73  ? 168 ARG A O   1 
ATOM 1185 C CB  . ARG A 1 169 ? 2.350  -16.200 14.849 1.00 44.06  ? 168 ARG A CB  1 
ATOM 1186 C CG  . ARG A 1 169 ? 1.753  -16.026 16.237 1.00 46.11  ? 168 ARG A CG  1 
ATOM 1187 C CD  . ARG A 1 169 ? 1.502  -17.368 16.913 1.00 57.03  ? 168 ARG A CD  1 
ATOM 1188 N NE  . ARG A 1 169 ? 0.674  -18.253 16.102 1.00 51.28  ? 168 ARG A NE  1 
ATOM 1189 C CZ  . ARG A 1 169 ? -0.645 -18.348 16.204 1.00 56.76  ? 168 ARG A CZ  1 
ATOM 1190 N NH1 . ARG A 1 169 ? -1.326 -17.622 17.076 1.00 63.82  ? 168 ARG A NH1 1 
ATOM 1191 N NH2 . ARG A 1 169 ? -1.299 -19.192 15.410 1.00 62.43  ? 168 ARG A NH2 1 
ATOM 1192 N N   . LEU A 1 170 ? 4.491  -16.635 12.515 1.00 44.02  ? 169 LEU A N   1 
ATOM 1193 C CA  . LEU A 1 170 ? 4.815  -17.190 11.205 1.00 40.34  ? 169 LEU A CA  1 
ATOM 1194 C C   . LEU A 1 170 ? 6.229  -17.760 11.174 1.00 52.28  ? 169 LEU A C   1 
ATOM 1195 O O   . LEU A 1 170 ? 6.445  -18.874 10.685 1.00 60.00  ? 169 LEU A O   1 
ATOM 1196 C CB  . LEU A 1 170 ? 4.646  -16.123 10.121 1.00 40.31  ? 169 LEU A CB  1 
ATOM 1197 C CG  . LEU A 1 170 ? 3.230  -15.611 9.844  1.00 40.52  ? 169 LEU A CG  1 
ATOM 1198 C CD1 . LEU A 1 170 ? 3.266  -14.480 8.833  1.00 40.46  ? 169 LEU A CD1 1 
ATOM 1199 C CD2 . LEU A 1 170 ? 2.326  -16.734 9.361  1.00 52.48  ? 169 LEU A CD2 1 
ATOM 1200 N N   . GLY A 1 171 ? 7.201  -17.018 11.699 1.00 44.37  ? 170 GLY A N   1 
ATOM 1201 C CA  . GLY A 1 171 ? 8.595  -17.387 11.542 1.00 42.93  ? 170 GLY A CA  1 
ATOM 1202 C C   . GLY A 1 171 ? 9.210  -18.162 12.690 1.00 48.02  ? 170 GLY A C   1 
ATOM 1203 O O   . GLY A 1 171 ? 10.334 -18.658 12.570 1.00 47.11  ? 170 GLY A O   1 
ATOM 1204 N N   . GLY A 1 172 ? 8.499  -18.273 13.804 1.00 45.25  ? 171 GLY A N   1 
ATOM 1205 C CA  . GLY A 1 172 ? 9.039  -18.993 14.948 1.00 40.90  ? 171 GLY A CA  1 
ATOM 1206 C C   . GLY A 1 172 ? 10.018 -18.132 15.713 1.00 45.64  ? 171 GLY A C   1 
ATOM 1207 O O   . GLY A 1 172 ? 9.745  -16.961 15.992 1.00 48.44  ? 171 GLY A O   1 
ATOM 1208 N N   . TYR A 1 173 ? 11.174 -18.708 16.055 1.00 47.67  ? 172 TYR A N   1 
ATOM 1209 C CA  . TYR A 1 173 ? 12.154 -17.976 16.853 1.00 50.77  ? 172 TYR A CA  1 
ATOM 1210 C C   . TYR A 1 173 ? 12.815 -16.873 16.037 1.00 48.50  ? 172 TYR A C   1 
ATOM 1211 O O   . TYR A 1 173 ? 12.914 -15.727 16.492 1.00 47.57  ? 172 TYR A O   1 
ATOM 1212 C CB  . TYR A 1 173 ? 13.207 -18.930 17.415 1.00 44.72  ? 172 TYR A CB  1 
ATOM 1213 C CG  . TYR A 1 173 ? 14.192 -18.253 18.342 1.00 38.78  ? 172 TYR A CG  1 
ATOM 1214 C CD1 . TYR A 1 173 ? 13.753 -17.569 19.469 1.00 42.78  ? 172 TYR A CD1 1 
ATOM 1215 C CD2 . TYR A 1 173 ? 15.557 -18.291 18.088 1.00 38.85  ? 172 TYR A CD2 1 
ATOM 1216 C CE1 . TYR A 1 173 ? 14.646 -16.946 20.320 1.00 46.69  ? 172 TYR A CE1 1 
ATOM 1217 C CE2 . TYR A 1 173 ? 16.459 -17.669 18.934 1.00 38.66  ? 172 TYR A CE2 1 
ATOM 1218 C CZ  . TYR A 1 173 ? 15.997 -16.999 20.048 1.00 46.87  ? 172 TYR A CZ  1 
ATOM 1219 O OH  . TYR A 1 173 ? 16.886 -16.379 20.894 1.00 47.12  ? 172 TYR A OH  1 
ATOM 1220 N N   . GLU A 1 174 ? 13.291 -17.205 14.834 1.00 46.45  ? 173 GLU A N   1 
ATOM 1221 C CA  . GLU A 1 174 ? 13.849 -16.180 13.959 1.00 45.70  ? 173 GLU A CA  1 
ATOM 1222 C C   . GLU A 1 174 ? 12.813 -15.116 13.630 1.00 45.26  ? 173 GLU A C   1 
ATOM 1223 O O   . GLU A 1 174 ? 13.161 -13.941 13.463 1.00 42.62  ? 173 GLU A O   1 
ATOM 1224 C CB  . GLU A 1 174 ? 14.390 -16.816 12.679 1.00 48.74  ? 173 GLU A CB  1 
ATOM 1225 C CG  . GLU A 1 174 ? 15.838 -17.271 12.774 1.00 48.98  ? 173 GLU A CG  1 
ATOM 1226 C CD  . GLU A 1 174 ? 16.527 -17.320 11.422 1.00 67.76  ? 173 GLU A CD  1 
ATOM 1227 O OE1 . GLU A 1 174 ? 16.043 -16.657 10.478 1.00 65.11  ? 173 GLU A OE1 1 
ATOM 1228 O OE2 . GLU A 1 174 ? 17.552 -18.023 11.302 1.00 65.05  ? 173 GLU A OE2 1 
ATOM 1229 N N   . GLY A 1 175 ? 11.539 -15.504 13.541 1.00 44.79  ? 174 GLY A N   1 
ATOM 1230 C CA  . GLY A 1 175 ? 10.488 -14.517 13.372 1.00 41.70  ? 174 GLY A CA  1 
ATOM 1231 C C   . GLY A 1 175 ? 10.371 -13.590 14.566 1.00 48.95  ? 174 GLY A C   1 
ATOM 1232 O O   . GLY A 1 175 ? 10.147 -12.388 14.412 1.00 58.06  ? 174 GLY A O   1 
ATOM 1233 N N   . ALA A 1 176 ? 10.525 -14.137 15.775 1.00 54.84  ? 175 ALA A N   1 
ATOM 1234 C CA  . ALA A 1 176 ? 10.567 -13.291 16.963 1.00 48.64  ? 175 ALA A CA  1 
ATOM 1235 C C   . ALA A 1 176 ? 11.787 -12.381 16.954 1.00 50.08  ? 175 ALA A C   1 
ATOM 1236 O O   . ALA A 1 176 ? 11.717 -11.247 17.442 1.00 46.15  ? 175 ALA A O   1 
ATOM 1237 C CB  . ALA A 1 176 ? 10.555 -14.153 18.225 1.00 44.74  ? 175 ALA A CB  1 
ATOM 1238 N N   . LEU A 1 177 ? 12.907 -12.853 16.403 1.00 54.10  ? 176 LEU A N   1 
ATOM 1239 C CA  . LEU A 1 177 ? 14.091 -12.008 16.297 1.00 55.52  ? 176 LEU A CA  1 
ATOM 1240 C C   . LEU A 1 177 ? 13.882 -10.900 15.272 1.00 57.58  ? 176 LEU A C   1 
ATOM 1241 O O   . LEU A 1 177 ? 14.272 -9.750  15.503 1.00 55.66  ? 176 LEU A O   1 
ATOM 1242 C CB  . LEU A 1 177 ? 15.312 -12.855 15.935 1.00 54.06  ? 176 LEU A CB  1 
ATOM 1243 C CG  . LEU A 1 177 ? 15.740 -13.935 16.933 1.00 50.16  ? 176 LEU A CG  1 
ATOM 1244 C CD1 . LEU A 1 177 ? 17.224 -14.245 16.798 1.00 50.19  ? 176 LEU A CD1 1 
ATOM 1245 C CD2 . LEU A 1 177 ? 15.409 -13.525 18.358 1.00 50.54  ? 176 LEU A CD2 1 
ATOM 1246 N N   . LEU A 1 178 ? 13.270 -11.229 14.132 1.00 54.51  ? 177 LEU A N   1 
ATOM 1247 C CA  . LEU A 1 178 ? 12.942 -10.200 13.152 1.00 54.54  ? 177 LEU A CA  1 
ATOM 1248 C C   . LEU A 1 178 ? 11.907 -9.229  13.704 1.00 52.62  ? 177 LEU A C   1 
ATOM 1249 O O   . LEU A 1 178 ? 11.974 -8.023  13.439 1.00 55.39  ? 177 LEU A O   1 
ATOM 1250 C CB  . LEU A 1 178 ? 12.441 -10.845 11.860 1.00 47.03  ? 177 LEU A CB  1 
ATOM 1251 C CG  . LEU A 1 178 ? 11.753 -9.916  10.857 1.00 50.14  ? 177 LEU A CG  1 
ATOM 1252 C CD1 . LEU A 1 178 ? 12.744 -8.912  10.278 1.00 51.89  ? 177 LEU A CD1 1 
ATOM 1253 C CD2 . LEU A 1 178 ? 11.079 -10.715 9.751  1.00 44.79  ? 177 LEU A CD2 1 
ATOM 1254 N N   . GLY A 1 179 ? 10.943 -9.739  14.473 1.00 57.80  ? 178 GLY A N   1 
ATOM 1255 C CA  . GLY A 1 179 ? 9.973  -8.860  15.105 1.00 61.86  ? 178 GLY A CA  1 
ATOM 1256 C C   . GLY A 1 179 ? 10.632 -7.818  15.987 1.00 65.80  ? 178 GLY A C   1 
ATOM 1257 O O   . GLY A 1 179 ? 10.340 -6.625  15.882 1.00 72.96  ? 178 GLY A O   1 
ATOM 1258 N N   . LEU A 1 180 ? 11.550 -8.257  16.854 1.00 54.02  ? 179 LEU A N   1 
ATOM 1259 C CA  . LEU A 1 180 ? 12.292 -7.324  17.697 1.00 51.50  ? 179 LEU A CA  1 
ATOM 1260 C C   . LEU A 1 180 ? 12.970 -6.238  16.872 1.00 56.54  ? 179 LEU A C   1 
ATOM 1261 O O   . LEU A 1 180 ? 13.120 -5.104  17.337 1.00 57.26  ? 179 LEU A O   1 
ATOM 1262 C CB  . LEU A 1 180 ? 13.331 -8.082  18.526 1.00 53.60  ? 179 LEU A CB  1 
ATOM 1263 C CG  . LEU A 1 180 ? 12.808 -9.003  19.635 1.00 54.58  ? 179 LEU A CG  1 
ATOM 1264 C CD1 . LEU A 1 180 ? 13.948 -9.498  20.514 1.00 52.81  ? 179 LEU A CD1 1 
ATOM 1265 C CD2 . LEU A 1 180 ? 11.749 -8.308  20.475 1.00 52.22  ? 179 LEU A CD2 1 
ATOM 1266 N N   . ALA A 1 181 ? 13.378 -6.561  15.643 1.00 59.51  ? 180 ALA A N   1 
ATOM 1267 C CA  . ALA A 1 181 ? 13.965 -5.548  14.777 1.00 52.88  ? 180 ALA A CA  1 
ATOM 1268 C C   . ALA A 1 181 ? 12.906 -4.612  14.217 1.00 51.78  ? 180 ALA A C   1 
ATOM 1269 O O   . ALA A 1 181 ? 13.195 -3.440  13.947 1.00 59.12  ? 180 ALA A O   1 
ATOM 1270 C CB  . ALA A 1 181 ? 14.747 -6.212  13.644 1.00 41.03  ? 180 ALA A CB  1 
ATOM 1271 N N   . LEU A 1 182 ? 11.679 -5.101  14.045 1.00 49.58  ? 181 LEU A N   1 
ATOM 1272 C CA  . LEU A 1 182 ? 10.623 -4.286  13.464 1.00 57.83  ? 181 LEU A CA  1 
ATOM 1273 C C   . LEU A 1 182 ? 10.006 -3.313  14.461 1.00 60.47  ? 181 LEU A C   1 
ATOM 1274 O O   . LEU A 1 182 ? 9.359  -2.349  14.038 1.00 64.15  ? 181 LEU A O   1 
ATOM 1275 C CB  . LEU A 1 182 ? 9.535  -5.185  12.872 1.00 57.14  ? 181 LEU A CB  1 
ATOM 1276 C CG  . LEU A 1 182 ? 9.939  -5.982  11.626 1.00 57.29  ? 181 LEU A CG  1 
ATOM 1277 C CD1 . LEU A 1 182 ? 8.718  -6.603  10.966 1.00 42.65  ? 181 LEU A CD1 1 
ATOM 1278 C CD2 . LEU A 1 182 ? 10.707 -5.110  10.637 1.00 45.43  ? 181 LEU A CD2 1 
ATOM 1279 N N   . ILE A 1 183 ? 10.195 -3.530  15.766 1.00 59.35  ? 182 ILE A N   1 
ATOM 1280 C CA  . ILE A 1 183 ? 9.622  -2.612  16.754 1.00 64.51  ? 182 ILE A CA  1 
ATOM 1281 C C   . ILE A 1 183 ? 10.188 -1.202  16.616 1.00 55.09  ? 182 ILE A C   1 
ATOM 1282 O O   . ILE A 1 183 ? 9.395  -0.249  16.549 1.00 55.27  ? 182 ILE A O   1 
ATOM 1283 C CB  . ILE A 1 183 ? 9.787  -3.188  18.176 1.00 61.17  ? 182 ILE A CB  1 
ATOM 1284 C CG1 . ILE A 1 183 ? 8.585  -4.048  18.578 1.00 59.15  ? 182 ILE A CG1 1 
ATOM 1285 C CG2 . ILE A 1 183 ? 9.959  -2.073  19.195 1.00 49.48  ? 182 ILE A CG2 1 
ATOM 1286 C CD1 . ILE A 1 183 ? 8.341  -5.241  17.710 1.00 54.71  ? 182 ILE A CD1 1 
ATOM 1287 N N   . PRO A 1 184 ? 11.523 -0.985  16.557 1.00 51.43  ? 183 PRO A N   1 
ATOM 1288 C CA  . PRO A 1 184 ? 12.015 0.392   16.415 1.00 57.30  ? 183 PRO A CA  1 
ATOM 1289 C C   . PRO A 1 184 ? 12.113 0.837   14.964 1.00 61.99  ? 183 PRO A C   1 
ATOM 1290 O O   . PRO A 1 184 ? 12.237 2.035   14.679 1.00 62.99  ? 183 PRO A O   1 
ATOM 1291 C CB  . PRO A 1 184 ? 13.389 0.337   17.087 1.00 53.09  ? 183 PRO A CB  1 
ATOM 1292 C CG  . PRO A 1 184 ? 13.859 -1.049  16.814 1.00 44.28  ? 183 PRO A CG  1 
ATOM 1293 C CD  . PRO A 1 184 ? 12.634 -1.928  16.799 1.00 54.11  ? 183 PRO A CD  1 
ATOM 1294 N N   . ALA A 1 185 ? 12.053 -0.114  14.034 1.00 54.63  ? 184 ALA A N   1 
ATOM 1295 C CA  . ALA A 1 185 ? 12.184 0.233   12.624 1.00 58.04  ? 184 ALA A CA  1 
ATOM 1296 C C   . ALA A 1 185 ? 10.878 0.768   12.050 1.00 61.35  ? 184 ALA A C   1 
ATOM 1297 O O   . ALA A 1 185 ? 10.885 1.748   11.296 1.00 62.62  ? 184 ALA A O   1 
ATOM 1298 C CB  . ALA A 1 185 ? 12.658 -0.980  11.828 1.00 51.62  ? 184 ALA A CB  1 
ATOM 1299 N N   . LEU A 1 186 ? 9.751  0.148   12.402 1.00 57.58  ? 185 LEU A N   1 
ATOM 1300 C CA  . LEU A 1 186 ? 8.455  0.562   11.876 1.00 57.60  ? 185 LEU A CA  1 
ATOM 1301 C C   . LEU A 1 186 ? 8.005  1.919   12.396 1.00 64.77  ? 185 LEU A C   1 
ATOM 1302 O O   . LEU A 1 186 ? 6.909  2.363   12.037 1.00 70.46  ? 185 LEU A O   1 
ATOM 1303 C CB  . LEU A 1 186 ? 7.397  -0.495  12.199 1.00 58.20  ? 185 LEU A CB  1 
ATOM 1304 C CG  . LEU A 1 186 ? 7.047  -1.460  11.064 1.00 65.13  ? 185 LEU A CG  1 
ATOM 1305 C CD1 . LEU A 1 186 ? 8.157  -2.476  10.866 1.00 55.14  ? 185 LEU A CD1 1 
ATOM 1306 C CD2 . LEU A 1 186 ? 5.724  -2.160  11.336 1.00 51.77  ? 185 LEU A CD2 1 
ATOM 1307 N N   . VAL A 1 187 ? 8.813  2.587   13.225 1.00 63.76  ? 186 VAL A N   1 
ATOM 1308 C CA  . VAL A 1 187 ? 8.488  3.934   13.678 1.00 67.10  ? 186 VAL A CA  1 
ATOM 1309 C C   . VAL A 1 187 ? 8.573  4.962   12.561 1.00 65.00  ? 186 VAL A C   1 
ATOM 1310 O O   . VAL A 1 187 ? 8.111  6.094   12.741 1.00 62.83  ? 186 VAL A O   1 
ATOM 1311 C CB  . VAL A 1 187 ? 9.411  4.346   14.844 1.00 59.05  ? 186 VAL A CB  1 
ATOM 1312 C CG1 . VAL A 1 187 ? 10.722 4.921   14.319 1.00 51.47  ? 186 VAL A CG1 1 
ATOM 1313 C CG2 . VAL A 1 187 ? 8.706  5.335   15.760 1.00 55.77  ? 186 VAL A CG2 1 
ATOM 1314 N N   . VAL A 1 188 ? 9.150  4.595   11.411 1.00 63.89  ? 187 VAL A N   1 
ATOM 1315 C CA  . VAL A 1 188 ? 9.217  5.515   10.278 1.00 54.20  ? 187 VAL A CA  1 
ATOM 1316 C C   . VAL A 1 188 ? 7.820  5.921   9.832  1.00 58.31  ? 187 VAL A C   1 
ATOM 1317 O O   . VAL A 1 188 ? 7.569  7.090   9.516  1.00 60.29  ? 187 VAL A O   1 
ATOM 1318 C CB  . VAL A 1 188 ? 10.011 4.888   9.116  1.00 59.17  ? 187 VAL A CB  1 
ATOM 1319 C CG1 . VAL A 1 188 ? 11.487 4.875   9.422  1.00 60.70  ? 187 VAL A CG1 1 
ATOM 1320 C CG2 . VAL A 1 188 ? 9.520  3.475   8.826  1.00 57.68  ? 187 VAL A CG2 1 
ATOM 1321 N N   . ILE A 1 189 ? 6.889  4.966   9.801  1.00 60.53  ? 188 ILE A N   1 
ATOM 1322 C CA  . ILE A 1 189 ? 5.553  5.256   9.284  1.00 66.28  ? 188 ILE A CA  1 
ATOM 1323 C C   . ILE A 1 189 ? 4.817  6.274   10.148 1.00 69.72  ? 188 ILE A C   1 
ATOM 1324 O O   . ILE A 1 189 ? 4.352  7.288   9.602  1.00 58.13  ? 188 ILE A O   1 
ATOM 1325 C CB  . ILE A 1 189 ? 4.765  3.945   9.094  1.00 66.80  ? 188 ILE A CB  1 
ATOM 1326 C CG1 . ILE A 1 189 ? 5.646  2.901   8.404  1.00 61.27  ? 188 ILE A CG1 1 
ATOM 1327 C CG2 . ILE A 1 189 ? 3.496  4.200   8.294  1.00 59.59  ? 188 ILE A CG2 1 
ATOM 1328 C CD1 . ILE A 1 189 ? 4.955  1.580   8.163  1.00 69.26  ? 188 ILE A CD1 1 
ATOM 1329 N N   . PRO A 1 190 ? 4.684  6.095   11.469 1.00 67.08  ? 189 PRO A N   1 
ATOM 1330 C CA  . PRO A 1 190 ? 4.005  7.141   12.250 1.00 62.53  ? 189 PRO A CA  1 
ATOM 1331 C C   . PRO A 1 190 ? 4.774  8.448   12.281 1.00 65.48  ? 189 PRO A C   1 
ATOM 1332 O O   . PRO A 1 190 ? 4.158  9.521   12.252 1.00 70.78  ? 189 PRO A O   1 
ATOM 1333 C CB  . PRO A 1 190 ? 3.884  6.514   13.649 1.00 64.73  ? 189 PRO A CB  1 
ATOM 1334 C CG  . PRO A 1 190 ? 4.048  5.047   13.430 1.00 69.20  ? 189 PRO A CG  1 
ATOM 1335 C CD  . PRO A 1 190 ? 5.049  4.954   12.326 1.00 64.32  ? 189 PRO A CD  1 
ATOM 1336 N N   . ALA A 1 191 ? 6.107  8.393   12.331 1.00 55.46  ? 190 ALA A N   1 
ATOM 1337 C CA  . ALA A 1 191 ? 6.895  9.620   12.396 1.00 59.90  ? 190 ALA A CA  1 
ATOM 1338 C C   . ALA A 1 191 ? 6.754  10.430  11.114 1.00 67.37  ? 190 ALA A C   1 
ATOM 1339 O O   . ALA A 1 191 ? 6.552  11.649  11.155 1.00 58.43  ? 190 ALA A O   1 
ATOM 1340 C CB  . ALA A 1 191 ? 8.363  9.290   12.668 1.00 52.64  ? 190 ALA A CB  1 
ATOM 1341 N N   . ALA A 1 192 ? 6.857  9.765   9.960  1.00 68.13  ? 191 ALA A N   1 
ATOM 1342 C CA  . ALA A 1 192 ? 6.720  10.470  8.690  1.00 53.99  ? 191 ALA A CA  1 
ATOM 1343 C C   . ALA A 1 192 ? 5.331  11.070  8.538  1.00 58.43  ? 191 ALA A C   1 
ATOM 1344 O O   . ALA A 1 192 ? 5.184  12.201  8.061  1.00 68.80  ? 191 ALA A O   1 
ATOM 1345 C CB  . ALA A 1 192 ? 7.029  9.526   7.528  1.00 60.55  ? 191 ALA A CB  1 
ATOM 1346 N N   . ILE A 1 193 ? 4.299  10.327  8.940  1.00 58.56  ? 192 ILE A N   1 
ATOM 1347 C CA  . ILE A 1 193 ? 2.940  10.847  8.859  1.00 60.59  ? 192 ILE A CA  1 
ATOM 1348 C C   . ILE A 1 193 ? 2.787  12.070  9.752  1.00 63.96  ? 192 ILE A C   1 
ATOM 1349 O O   . ILE A 1 193 ? 2.182  13.075  9.357  1.00 72.08  ? 192 ILE A O   1 
ATOM 1350 C CB  . ILE A 1 193 ? 1.924  9.749   9.221  1.00 61.52  ? 192 ILE A CB  1 
ATOM 1351 C CG1 . ILE A 1 193 ? 1.942  8.638   8.167  1.00 58.95  ? 192 ILE A CG1 1 
ATOM 1352 C CG2 . ILE A 1 193 ? 0.528  10.336  9.369  1.00 58.88  ? 192 ILE A CG2 1 
ATOM 1353 C CD1 . ILE A 1 193 ? 1.983  9.142   6.740  1.00 52.95  ? 192 ILE A CD1 1 
ATOM 1354 N N   . MET A 1 194 ? 3.351  12.018  10.959 1.00 60.42  ? 193 MET A N   1 
ATOM 1355 C CA  . MET A 1 194 ? 3.209  13.141  11.878 1.00 66.15  ? 193 MET A CA  1 
ATOM 1356 C C   . MET A 1 194 ? 4.040  14.339  11.434 1.00 61.38  ? 193 MET A C   1 
ATOM 1357 O O   . MET A 1 194 ? 3.600  15.485  11.569 1.00 66.13  ? 193 MET A O   1 
ATOM 1358 C CB  . MET A 1 194 ? 3.588  12.717  13.295 1.00 56.57  ? 193 MET A CB  1 
ATOM 1359 C CG  . MET A 1 194 ? 2.588  11.784  13.951 1.00 61.97  ? 193 MET A CG  1 
ATOM 1360 S SD  . MET A 1 194 ? 1.298  12.683  14.831 1.00 74.63  ? 193 MET A SD  1 
ATOM 1361 C CE  . MET A 1 194 ? -0.002 12.703  13.599 1.00 65.39  ? 193 MET A CE  1 
ATOM 1362 N N   . LEU A 1 195 ? 5.240  14.102  10.901 1.00 63.74  ? 194 LEU A N   1 
ATOM 1363 C CA  . LEU A 1 195 ? 6.080  15.220  10.473 1.00 62.61  ? 194 LEU A CA  1 
ATOM 1364 C C   . LEU A 1 195 ? 5.468  15.954  9.286  1.00 68.19  ? 194 LEU A C   1 
ATOM 1365 O O   . LEU A 1 195 ? 5.528  17.186  9.213  1.00 70.01  ? 194 LEU A O   1 
ATOM 1366 C CB  . LEU A 1 195 ? 7.485  14.726  10.133 1.00 59.16  ? 194 LEU A CB  1 
ATOM 1367 C CG  . LEU A 1 195 ? 8.465  15.796  9.641  1.00 68.41  ? 194 LEU A CG  1 
ATOM 1368 C CD1 . LEU A 1 195 ? 9.780  15.719  10.399 1.00 62.27  ? 194 LEU A CD1 1 
ATOM 1369 C CD2 . LEU A 1 195 ? 8.699  15.675  8.139  1.00 62.27  ? 194 LEU A CD2 1 
ATOM 1370 N N   . ILE A 1 196 ? 4.868  15.215  8.359  1.00 65.90  ? 195 ILE A N   1 
ATOM 1371 C CA  . ILE A 1 196 ? 4.344  15.799  7.128  1.00 70.67  ? 195 ILE A CA  1 
ATOM 1372 C C   . ILE A 1 196 ? 2.942  16.360  7.328  1.00 73.15  ? 195 ILE A C   1 
ATOM 1373 O O   . ILE A 1 196 ? 2.669  17.513  6.980  1.00 89.31  ? 195 ILE A O   1 
ATOM 1374 C CB  . ILE A 1 196 ? 4.379  14.755  5.992  1.00 76.78  ? 195 ILE A CB  1 
ATOM 1375 C CG1 . ILE A 1 196 ? 5.815  14.527  5.522  1.00 80.77  ? 195 ILE A CG1 1 
ATOM 1376 C CG2 . ILE A 1 196 ? 3.500  15.196  4.831  1.00 75.82  ? 195 ILE A CG2 1 
ATOM 1377 C CD1 . ILE A 1 196 ? 6.524  15.793  5.096  1.00 80.12  ? 195 ILE A CD1 1 
ATOM 1378 N N   . LYS A 1 197 ? 2.027  15.564  7.888  1.00 59.36  ? 196 LYS A N   1 
ATOM 1379 C CA  . LYS A 1 197 ? 0.641  16.010  7.994  1.00 69.02  ? 196 LYS A CA  1 
ATOM 1380 C C   . LYS A 1 197 ? 0.484  17.153  8.990  1.00 73.21  ? 196 LYS A C   1 
ATOM 1381 O O   . LYS A 1 197 ? -0.409 17.993  8.827  1.00 79.19  ? 196 LYS A O   1 
ATOM 1382 C CB  . LYS A 1 197 ? -0.268 14.841  8.380  1.00 64.18  ? 196 LYS A CB  1 
ATOM 1383 C CG  . LYS A 1 197 ? -1.753 15.138  8.233  1.00 64.22  ? 196 LYS A CG  1 
ATOM 1384 C CD  . LYS A 1 197 ? -2.567 13.862  8.082  1.00 73.22  ? 196 LYS A CD  1 
ATOM 1385 C CE  . LYS A 1 197 ? -2.874 13.232  9.433  1.00 75.48  ? 196 LYS A CE  1 
ATOM 1386 N NZ  . LYS A 1 197 ? -3.984 12.240  9.345  1.00 65.70  ? 196 LYS A NZ  1 
ATOM 1387 N N   . ARG A 1 198 ? 1.333  17.210  10.017 1.00 66.46  ? 197 ARG A N   1 
ATOM 1388 C CA  . ARG A 1 198 ? 1.258  18.307  10.974 1.00 72.06  ? 197 ARG A CA  1 
ATOM 1389 C C   . ARG A 1 198 ? 1.835  19.603  10.423 1.00 76.32  ? 197 ARG A C   1 
ATOM 1390 O O   . ARG A 1 198 ? 1.534  20.676  10.959 1.00 71.25  ? 197 ARG A O   1 
ATOM 1391 C CB  . ARG A 1 198 ? 1.983  17.942  12.270 1.00 68.02  ? 197 ARG A CB  1 
ATOM 1392 C CG  . ARG A 1 198 ? 1.168  17.084  13.222 1.00 70.41  ? 197 ARG A CG  1 
ATOM 1393 C CD  . ARG A 1 198 ? 2.053  16.413  14.267 1.00 65.00  ? 197 ARG A CD  1 
ATOM 1394 N NE  . ARG A 1 198 ? 2.605  17.359  15.231 1.00 57.76  ? 197 ARG A NE  1 
ATOM 1395 C CZ  . ARG A 1 198 ? 1.891  18.020  16.133 1.00 63.49  ? 197 ARG A CZ  1 
ATOM 1396 N NH1 . ARG A 1 198 ? 0.579  17.876  16.221 1.00 65.67  ? 197 ARG A NH1 1 
ATOM 1397 N NH2 . ARG A 1 198 ? 2.509  18.850  16.968 1.00 55.94  ? 197 ARG A NH2 1 
ATOM 1398 N N   . GLY A 1 199 ? 2.650  19.532  9.375  1.00 73.37  ? 198 GLY A N   1 
ATOM 1399 C CA  . GLY A 1 199 ? 3.225  20.732  8.800  1.00 72.11  ? 198 GLY A CA  1 
ATOM 1400 C C   . GLY A 1 199 ? 4.261  21.404  9.670  1.00 72.78  ? 198 GLY A C   1 
ATOM 1401 O O   . GLY A 1 199 ? 4.419  22.627  9.603  1.00 74.09  ? 198 GLY A O   1 
ATOM 1402 N N   . VAL A 1 200 ? 4.977  20.635  10.495 1.00 70.29  ? 199 VAL A N   1 
ATOM 1403 C CA  . VAL A 1 200 ? 6.008  21.219  11.342 1.00 78.06  ? 199 VAL A CA  1 
ATOM 1404 C C   . VAL A 1 200 ? 7.220  21.653  10.528 1.00 73.62  ? 199 VAL A C   1 
ATOM 1405 O O   . VAL A 1 200 ? 8.003  22.492  10.988 1.00 71.96  ? 199 VAL A O   1 
ATOM 1406 C CB  . VAL A 1 200 ? 6.411  20.228  12.452 1.00 76.20  ? 199 VAL A CB  1 
ATOM 1407 C CG1 . VAL A 1 200 ? 7.417  19.207  11.930 1.00 74.69  ? 199 VAL A CG1 1 
ATOM 1408 C CG2 . VAL A 1 200 ? 6.964  20.973  13.658 1.00 66.44  ? 199 VAL A CG2 1 
ATOM 1409 N N   . ILE A 1 201 ? 7.385  21.117  9.322  1.00 76.14  ? 200 ILE A N   1 
ATOM 1410 C CA  . ILE A 1 201 ? 8.510  21.448  8.451  1.00 81.64  ? 200 ILE A CA  1 
ATOM 1411 C C   . ILE A 1 201 ? 8.179  20.961  7.044  1.00 82.10  ? 200 ILE A C   1 
ATOM 1412 O O   . ILE A 1 201 ? 7.604  19.873  6.887  1.00 71.56  ? 200 ILE A O   1 
ATOM 1413 C CB  . ILE A 1 201 ? 9.821  20.839  8.981  1.00 78.34  ? 200 ILE A CB  1 
ATOM 1414 C CG1 . ILE A 1 201 ? 11.021 21.312  8.156  1.00 81.39  ? 200 ILE A CG1 1 
ATOM 1415 C CG2 . ILE A 1 201 ? 9.746  19.315  9.019  1.00 74.52  ? 200 ILE A CG2 1 
ATOM 1416 C CD1 . ILE A 1 201 ? 12.329 20.664  8.556  1.00 77.11  ? 200 ILE A CD1 1 
ATOM 1417 N N   . PRO A 1 202 ? 8.477  21.732  6.002  1.00 85.13  ? 201 PRO A N   1 
ATOM 1418 C CA  . PRO A 1 202 ? 8.245  21.241  4.639  1.00 89.58  ? 201 PRO A CA  1 
ATOM 1419 C C   . PRO A 1 202 ? 9.321  20.260  4.200  1.00 79.91  ? 201 PRO A C   1 
ATOM 1420 O O   . PRO A 1 202 ? 10.485 20.345  4.599  1.00 76.19  ? 201 PRO A O   1 
ATOM 1421 C CB  . PRO A 1 202 ? 8.268  22.513  3.780  1.00 83.42  ? 201 PRO A CB  1 
ATOM 1422 C CG  . PRO A 1 202 ? 8.861  23.577  4.616  1.00 87.18  ? 201 PRO A CG  1 
ATOM 1423 C CD  . PRO A 1 202 ? 8.925  23.134  6.042  1.00 81.44  ? 201 PRO A CD  1 
ATOM 1424 N N   . LEU A 1 203 ? 8.903  19.315  3.352  1.00 63.76  ? 202 LEU A N   1 
ATOM 1425 C CA  . LEU A 1 203 ? 9.781  18.228  2.932  1.00 61.38  ? 202 LEU A CA  1 
ATOM 1426 C C   . LEU A 1 203 ? 10.994 18.717  2.150  1.00 70.42  ? 202 LEU A C   1 
ATOM 1427 O O   . LEU A 1 203 ? 11.993 17.994  2.066  1.00 76.47  ? 202 LEU A O   1 
ATOM 1428 C CB  . LEU A 1 203 ? 8.988  17.219  2.096  1.00 72.45  ? 202 LEU A CB  1 
ATOM 1429 C CG  . LEU A 1 203 ? 9.668  15.899  1.722  1.00 78.22  ? 202 LEU A CG  1 
ATOM 1430 C CD1 . LEU A 1 203 ? 8.750  14.722  2.011  1.00 66.76  ? 202 LEU A CD1 1 
ATOM 1431 C CD2 . LEU A 1 203 ? 10.096 15.906  0.258  1.00 76.91  ? 202 LEU A CD2 1 
ATOM 1432 N N   . SER A 1 204 ? 10.937 19.927  1.584  1.00 64.81  ? 203 SER A N   1 
ATOM 1433 C CA  . SER A 1 204 ? 12.072 20.446  0.823  1.00 63.39  ? 203 SER A CA  1 
ATOM 1434 C C   . SER A 1 204 ? 13.333 20.531  1.674  1.00 69.44  ? 203 SER A C   1 
ATOM 1435 O O   . SER A 1 204 ? 14.447 20.485  1.140  1.00 64.34  ? 203 SER A O   1 
ATOM 1436 C CB  . SER A 1 204 ? 11.729 21.820  0.245  1.00 80.48  ? 203 SER A CB  1 
ATOM 1437 O OG  . SER A 1 204 ? 12.806 22.347  -0.511 1.00 93.52  ? 203 SER A OG  1 
ATOM 1438 N N   . TYR A 1 205 ? 13.180 20.646  2.995  1.00 77.67  ? 204 TYR A N   1 
ATOM 1439 C CA  . TYR A 1 205 ? 14.330 20.781  3.881  1.00 75.21  ? 204 TYR A CA  1 
ATOM 1440 C C   . TYR A 1 205 ? 15.113 19.483  4.028  1.00 65.23  ? 204 TYR A C   1 
ATOM 1441 O O   . TYR A 1 205 ? 16.255 19.514  4.499  1.00 58.08  ? 204 TYR A O   1 
ATOM 1442 C CB  . TYR A 1 205 ? 13.869 21.270  5.256  1.00 73.13  ? 204 TYR A CB  1 
ATOM 1443 C CG  . TYR A 1 205 ? 13.558 22.751  5.308  1.00 85.69  ? 204 TYR A CG  1 
ATOM 1444 C CD1 . TYR A 1 205 ? 12.428 23.268  4.688  1.00 83.57  ? 204 TYR A CD1 1 
ATOM 1445 C CD2 . TYR A 1 205 ? 14.389 23.630  5.988  1.00 77.66  ? 204 TYR A CD2 1 
ATOM 1446 C CE1 . TYR A 1 205 ? 12.142 24.620  4.736  1.00 83.35  ? 204 TYR A CE1 1 
ATOM 1447 C CE2 . TYR A 1 205 ? 14.112 24.983  6.042  1.00 76.16  ? 204 TYR A CE2 1 
ATOM 1448 C CZ  . TYR A 1 205 ? 12.986 25.473  5.415  1.00 82.21  ? 204 TYR A CZ  1 
ATOM 1449 O OH  . TYR A 1 205 ? 12.702 26.818  5.466  1.00 84.09  ? 204 TYR A OH  1 
ATOM 1450 N N   . LEU A 1 206 ? 14.532 18.351  3.634  1.00 77.16  ? 205 LEU A N   1 
ATOM 1451 C CA  . LEU A 1 206 ? 15.167 17.049  3.795  1.00 61.28  ? 205 LEU A CA  1 
ATOM 1452 C C   . LEU A 1 206 ? 16.031 16.647  2.607  1.00 57.50  ? 205 LEU A C   1 
ATOM 1453 O O   . LEU A 1 206 ? 16.664 15.587  2.657  1.00 61.05  ? 205 LEU A O   1 
ATOM 1454 C CB  . LEU A 1 206 ? 14.105 15.972  4.042  1.00 52.39  ? 205 LEU A CB  1 
ATOM 1455 C CG  . LEU A 1 206 ? 13.545 15.887  5.464  1.00 57.84  ? 205 LEU A CG  1 
ATOM 1456 C CD1 . LEU A 1 206 ? 12.055 15.580  5.441  1.00 52.43  ? 205 LEU A CD1 1 
ATOM 1457 C CD2 . LEU A 1 206 ? 14.300 14.844  6.277  1.00 45.31  ? 205 LEU A CD2 1 
ATOM 1458 N N   . LYS A 1 207 ? 16.075 17.451  1.550  1.00 57.52  ? 206 LYS A N   1 
ATOM 1459 C CA  . LYS A 1 207 ? 16.935 17.140  0.418  1.00 59.12  ? 206 LYS A CA  1 
ATOM 1460 C C   . LYS A 1 207 ? 18.392 17.119  0.873  1.00 55.41  ? 206 LYS A C   1 
ATOM 1461 O O   . LYS A 1 207 ? 18.855 18.081  1.500  1.00 64.59  ? 206 LYS A O   1 
ATOM 1462 C CB  . LYS A 1 207 ? 16.744 18.160  -0.703 1.00 62.12  ? 206 LYS A CB  1 
ATOM 1463 C CG  . LYS A 1 207 ? 15.513 17.914  -1.562 1.00 53.27  ? 206 LYS A CG  1 
ATOM 1464 C CD  . LYS A 1 207 ? 15.534 18.770  -2.818 1.00 45.44  ? 206 LYS A CD  1 
ATOM 1465 C CE  . LYS A 1 207 ? 15.444 20.251  -2.482 1.00 62.68  ? 206 LYS A CE  1 
ATOM 1466 N NZ  . LYS A 1 207 ? 15.258 21.095  -3.698 1.00 61.53  ? 206 LYS A NZ  1 
ATOM 1467 N N   . PRO A 1 208 ? 19.139 16.051  0.590  1.00 62.72  ? 207 PRO A N   1 
ATOM 1468 C CA  . PRO A 1 208 ? 20.510 15.934  1.116  1.00 54.94  ? 207 PRO A CA  1 
ATOM 1469 C C   . PRO A 1 208 ? 21.432 16.988  0.518  1.00 60.43  ? 207 PRO A C   1 
ATOM 1470 O O   . PRO A 1 208 ? 21.610 17.061  -0.700 1.00 68.78  ? 207 PRO A O   1 
ATOM 1471 C CB  . PRO A 1 208 ? 20.929 14.516  0.704  1.00 48.50  ? 207 PRO A CB  1 
ATOM 1472 C CG  . PRO A 1 208 ? 19.646 13.796  0.416  1.00 46.37  ? 207 PRO A CG  1 
ATOM 1473 C CD  . PRO A 1 208 ? 18.715 14.836  -0.123 1.00 62.59  ? 207 PRO A CD  1 
ATOM 1474 N N   . SER A 1 209 ? 22.010 17.810  1.389  1.00 60.39  ? 208 SER A N   1 
ATOM 1475 C CA  . SER A 1 209 ? 23.079 18.732  1.039  1.00 62.17  ? 208 SER A CA  1 
ATOM 1476 C C   . SER A 1 209 ? 24.245 18.485  1.986  1.00 58.68  ? 208 SER A C   1 
ATOM 1477 O O   . SER A 1 209 ? 24.144 17.705  2.936  1.00 57.67  ? 208 SER A O   1 
ATOM 1478 C CB  . SER A 1 209 ? 22.618 20.194  1.112  1.00 62.75  ? 208 SER A CB  1 
ATOM 1479 O OG  . SER A 1 209 ? 22.566 20.648  2.453  1.00 64.03  ? 208 SER A OG  1 
ATOM 1480 N N   . TRP A 1 210 ? 25.365 19.154  1.727  1.00 57.78  ? 209 TRP A N   1 
ATOM 1481 C CA  . TRP A 1 210 ? 26.563 18.980  2.540  1.00 68.38  ? 209 TRP A CA  1 
ATOM 1482 C C   . TRP A 1 210 ? 27.085 20.337  2.983  1.00 72.90  ? 209 TRP A C   1 
ATOM 1483 O O   . TRP A 1 210 ? 27.427 21.179  2.146  1.00 80.91  ? 209 TRP A O   1 
ATOM 1484 C CB  . TRP A 1 210 ? 27.650 18.216  1.779  1.00 64.74  ? 209 TRP A CB  1 
ATOM 1485 C CG  . TRP A 1 210 ? 28.679 17.616  2.688  1.00 68.07  ? 209 TRP A CG  1 
ATOM 1486 C CD1 . TRP A 1 210 ? 29.956 18.055  2.887  1.00 70.69  ? 209 TRP A CD1 1 
ATOM 1487 C CD2 . TRP A 1 210 ? 28.513 16.470  3.533  1.00 62.03  ? 209 TRP A CD2 1 
ATOM 1488 N NE1 . TRP A 1 210 ? 30.597 17.251  3.799  1.00 67.72  ? 209 TRP A NE1 1 
ATOM 1489 C CE2 . TRP A 1 210 ? 29.733 16.271  4.210  1.00 61.20  ? 209 TRP A CE2 1 
ATOM 1490 C CE3 . TRP A 1 210 ? 27.453 15.593  3.779  1.00 62.29  ? 209 TRP A CE3 1 
ATOM 1491 C CZ2 . TRP A 1 210 ? 29.922 15.229  5.117  1.00 61.02  ? 209 TRP A CZ2 1 
ATOM 1492 C CZ3 . TRP A 1 210 ? 27.642 14.560  4.681  1.00 64.16  ? 209 TRP A CZ3 1 
ATOM 1493 C CH2 . TRP A 1 210 ? 28.867 14.387  5.339  1.00 61.28  ? 209 TRP A CH2 1 
ATOM 1494 N N   . ASP A 1 211 ? 27.146 20.541  4.296  1.00 62.09  ? 210 ASP A N   1 
ATOM 1495 C CA  . ASP A 1 211 ? 27.816 21.688  4.896  1.00 69.60  ? 210 ASP A CA  1 
ATOM 1496 C C   . ASP A 1 211 ? 29.024 21.159  5.660  1.00 68.81  ? 210 ASP A C   1 
ATOM 1497 O O   . ASP A 1 211 ? 28.869 20.418  6.637  1.00 75.90  ? 210 ASP A O   1 
ATOM 1498 C CB  . ASP A 1 211 ? 26.873 22.464  5.812  1.00 74.00  ? 210 ASP A CB  1 
ATOM 1499 C CG  . ASP A 1 211 ? 27.359 23.875  6.085  1.00 74.98  ? 210 ASP A CG  1 
ATOM 1500 O OD1 . ASP A 1 211 ? 28.401 24.028  6.755  1.00 74.77  ? 210 ASP A OD1 1 
ATOM 1501 O OD2 . ASP A 1 211 ? 26.700 24.832  5.625  1.00 79.58  ? 210 ASP A OD2 1 
ATOM 1502 N N   . ASN A 1 212 ? 30.221 21.536  5.201  1.00 69.02  ? 211 ASN A N   1 
ATOM 1503 C CA  . ASN A 1 212 ? 31.462 21.071  5.818  1.00 69.65  ? 211 ASN A CA  1 
ATOM 1504 C C   . ASN A 1 212 ? 31.449 21.310  7.324  1.00 72.05  ? 211 ASN A C   1 
ATOM 1505 O O   . ASN A 1 212 ? 31.783 20.416  8.110  1.00 77.35  ? 211 ASN A O   1 
ATOM 1506 C CB  . ASN A 1 212 ? 32.654 21.773  5.150  1.00 84.11  ? 211 ASN A CB  1 
ATOM 1507 C CG  . ASN A 1 212 ? 34.010 21.377  5.739  1.00 91.48  ? 211 ASN A CG  1 
ATOM 1508 O OD1 . ASN A 1 212 ? 34.182 21.246  6.950  1.00 94.35  ? 211 ASN A OD1 1 
ATOM 1509 N ND2 . ASN A 1 212 ? 34.985 21.184  4.858  1.00 85.74  ? 211 ASN A ND2 1 
ATOM 1510 N N   . GLY A 1 213 ? 31.052 22.512  7.745  1.00 75.86  ? 212 GLY A N   1 
ATOM 1511 C CA  . GLY A 1 213 ? 31.126 22.850  9.158  1.00 80.12  ? 212 GLY A CA  1 
ATOM 1512 C C   . GLY A 1 213 ? 30.186 22.023  10.013 1.00 73.88  ? 212 GLY A C   1 
ATOM 1513 O O   . GLY A 1 213 ? 30.601 21.412  11.002 1.00 80.44  ? 212 GLY A O   1 
ATOM 1514 N N   . LEU A 1 214 ? 28.903 21.991  9.644  1.00 75.24  ? 213 LEU A N   1 
ATOM 1515 C CA  . LEU A 1 214 ? 27.922 21.264  10.443 1.00 77.47  ? 213 LEU A CA  1 
ATOM 1516 C C   . LEU A 1 214 ? 28.194 19.767  10.443 1.00 81.71  ? 213 LEU A C   1 
ATOM 1517 O O   . LEU A 1 214 ? 27.853 19.075  11.409 1.00 89.69  ? 213 LEU A O   1 
ATOM 1518 C CB  . LEU A 1 214 ? 26.514 21.550  9.925  1.00 72.29  ? 213 LEU A CB  1 
ATOM 1519 C CG  . LEU A 1 214 ? 26.066 23.006  10.046 1.00 76.08  ? 213 LEU A CG  1 
ATOM 1520 C CD1 . LEU A 1 214 ? 24.977 23.320  9.032  1.00 75.22  ? 213 LEU A CD1 1 
ATOM 1521 C CD2 . LEU A 1 214 ? 25.604 23.308  11.462 1.00 71.10  ? 213 LEU A CD2 1 
ATOM 1522 N N   . ALA A 1 215 ? 28.803 19.247  9.374  1.00 77.05  ? 214 ALA A N   1 
ATOM 1523 C CA  . ALA A 1 215 ? 29.137 17.828  9.339  1.00 75.78  ? 214 ALA A CA  1 
ATOM 1524 C C   . ALA A 1 215 ? 30.191 17.483  10.383 1.00 77.96  ? 214 ALA A C   1 
ATOM 1525 O O   . ALA A 1 215 ? 30.113 16.430  11.025 1.00 79.46  ? 214 ALA A O   1 
ATOM 1526 C CB  . ALA A 1 215 ? 29.613 17.434  7.941  1.00 67.65  ? 214 ALA A CB  1 
ATOM 1527 N N   . GLY A 1 216 ? 31.178 18.361  10.574 1.00 73.50  ? 215 GLY A N   1 
ATOM 1528 C CA  . GLY A 1 216 ? 32.217 18.089  11.555 1.00 84.96  ? 215 GLY A CA  1 
ATOM 1529 C C   . GLY A 1 216 ? 31.695 18.079  12.979 1.00 88.96  ? 215 GLY A C   1 
ATOM 1530 O O   . GLY A 1 216 ? 32.125 17.263  13.801 1.00 79.49  ? 215 GLY A O   1 
ATOM 1531 N N   . GLN A 1 217 ? 30.768 18.986  13.296 1.00 107.11 ? 216 GLN A N   1 
ATOM 1532 C CA  . GLN A 1 217 ? 30.159 18.991  14.622 1.00 109.44 ? 216 GLN A CA  1 
ATOM 1533 C C   . GLN A 1 217 ? 29.357 17.718  14.854 1.00 105.01 ? 216 GLN A C   1 
ATOM 1534 O O   . GLN A 1 217 ? 29.521 17.041  15.876 1.00 107.33 ? 216 GLN A O   1 
ATOM 1535 C CB  . GLN A 1 217 ? 29.271 20.224  14.788 1.00 111.54 ? 216 GLN A CB  1 
ATOM 1536 C CG  . GLN A 1 217 ? 29.919 21.523  14.344 1.00 113.78 ? 216 GLN A CG  1 
ATOM 1537 C CD  . GLN A 1 217 ? 31.051 21.948  15.257 1.00 128.36 ? 216 GLN A CD  1 
ATOM 1538 O OE1 . GLN A 1 217 ? 30.882 22.041  16.472 1.00 134.76 ? 216 GLN A OE1 1 
ATOM 1539 N NE2 . GLN A 1 217 ? 32.215 22.210  14.673 1.00 134.81 ? 216 GLN A NE2 1 
ATOM 1540 N N   . LEU A 1 218 ? 28.482 17.373  13.907 1.00 74.20  ? 217 LEU A N   1 
ATOM 1541 C CA  . LEU A 1 218 ? 27.750 16.118  13.998 1.00 79.24  ? 217 LEU A CA  1 
ATOM 1542 C C   . LEU A 1 218 ? 28.676 14.912  13.915 1.00 74.38  ? 217 LEU A C   1 
ATOM 1543 O O   . LEU A 1 218 ? 28.315 13.833  14.396 1.00 71.82  ? 217 LEU A O   1 
ATOM 1544 C CB  . LEU A 1 218 ? 26.693 16.053  12.896 1.00 69.90  ? 217 LEU A CB  1 
ATOM 1545 C CG  . LEU A 1 218 ? 25.651 17.173  12.887 1.00 59.80  ? 217 LEU A CG  1 
ATOM 1546 C CD1 . LEU A 1 218 ? 24.761 17.065  11.660 1.00 57.09  ? 217 LEU A CD1 1 
ATOM 1547 C CD2 . LEU A 1 218 ? 24.820 17.143  14.156 1.00 64.29  ? 217 LEU A CD2 1 
ATOM 1548 N N   . SER A 1 219 ? 29.862 15.071  13.319 1.00 67.90  ? 218 SER A N   1 
ATOM 1549 C CA  . SER A 1 219 ? 30.827 13.976  13.290 1.00 67.74  ? 218 SER A CA  1 
ATOM 1550 C C   . SER A 1 219 ? 31.322 13.643  14.690 1.00 76.64  ? 218 SER A C   1 
ATOM 1551 O O   . SER A 1 219 ? 31.562 12.472  15.007 1.00 82.14  ? 218 SER A O   1 
ATOM 1552 C CB  . SER A 1 219 ? 32.003 14.327  12.380 1.00 66.74  ? 218 SER A CB  1 
ATOM 1553 O OG  . SER A 1 219 ? 31.663 14.147  11.017 1.00 73.30  ? 218 SER A OG  1 
ATOM 1554 N N   . LYS A 1 220 ? 31.490 14.660  15.539 1.00 78.52  ? 219 LYS A N   1 
ATOM 1555 C CA  . LYS A 1 220 ? 31.872 14.403  16.922 1.00 75.75  ? 219 LYS A CA  1 
ATOM 1556 C C   . LYS A 1 220 ? 30.788 13.631  17.660 1.00 72.34  ? 219 LYS A C   1 
ATOM 1557 O O   . LYS A 1 220 ? 31.093 12.828  18.549 1.00 76.46  ? 219 LYS A O   1 
ATOM 1558 C CB  . LYS A 1 220 ? 32.179 15.718  17.637 1.00 71.17  ? 219 LYS A CB  1 
ATOM 1559 C CG  . LYS A 1 220 ? 33.459 16.397  17.169 1.00 83.37  ? 219 LYS A CG  1 
ATOM 1560 C CD  . LYS A 1 220 ? 34.585 15.392  16.965 1.00 82.27  ? 219 LYS A CD  1 
ATOM 1561 C CE  . LYS A 1 220 ? 35.692 15.970  16.096 1.00 87.18  ? 219 LYS A CE  1 
ATOM 1562 N NZ  . LYS A 1 220 ? 35.161 16.626  14.868 1.00 79.44  ? 219 LYS A NZ  1 
ATOM 1563 N N   . PHE A 1 221 ? 29.521 13.858  17.307 1.00 68.78  ? 220 PHE A N   1 
ATOM 1564 C CA  . PHE A 1 221 ? 28.447 13.029  17.843 1.00 74.69  ? 220 PHE A CA  1 
ATOM 1565 C C   . PHE A 1 221 ? 28.548 11.603  17.318 1.00 71.01  ? 220 PHE A C   1 
ATOM 1566 O O   . PHE A 1 221 ? 28.255 10.644  18.042 1.00 65.72  ? 220 PHE A O   1 
ATOM 1567 C CB  . PHE A 1 221 ? 27.089 13.634  17.490 1.00 74.70  ? 220 PHE A CB  1 
ATOM 1568 C CG  . PHE A 1 221 ? 26.636 14.706  18.438 1.00 77.41  ? 220 PHE A CG  1 
ATOM 1569 C CD1 . PHE A 1 221 ? 27.102 16.004  18.312 1.00 73.84  ? 220 PHE A CD1 1 
ATOM 1570 C CD2 . PHE A 1 221 ? 25.741 14.416  19.455 1.00 75.96  ? 220 PHE A CD2 1 
ATOM 1571 C CE1 . PHE A 1 221 ? 26.685 16.992  19.182 1.00 66.84  ? 220 PHE A CE1 1 
ATOM 1572 C CE2 . PHE A 1 221 ? 25.320 15.401  20.329 1.00 65.33  ? 220 PHE A CE2 1 
ATOM 1573 C CZ  . PHE A 1 221 ? 25.793 16.690  20.192 1.00 62.69  ? 220 PHE A CZ  1 
ATOM 1574 N N   . THR A 1 222 ? 28.959 11.446  16.057 1.00 69.94  ? 221 THR A N   1 
ATOM 1575 C CA  . THR A 1 222 ? 29.153 10.115  15.494 1.00 71.08  ? 221 THR A CA  1 
ATOM 1576 C C   . THR A 1 222 ? 30.305 9.392   16.179 1.00 73.81  ? 221 THR A C   1 
ATOM 1577 O O   . THR A 1 222 ? 30.193 8.205   16.510 1.00 74.12  ? 221 THR A O   1 
ATOM 1578 C CB  . THR A 1 222 ? 29.398 10.219  13.987 1.00 66.59  ? 221 THR A CB  1 
ATOM 1579 O OG1 . THR A 1 222 ? 28.145 10.363  13.308 1.00 69.85  ? 221 THR A OG1 1 
ATOM 1580 C CG2 . THR A 1 222 ? 30.101 8.974   13.464 1.00 70.71  ? 221 THR A CG2 1 
ATOM 1581 N N   . LEU A 1 223 ? 31.417 10.096  16.408 1.00 80.00  ? 222 LEU A N   1 
ATOM 1582 C CA  . LEU A 1 223 ? 32.557 9.492   17.091 1.00 79.70  ? 222 LEU A CA  1 
ATOM 1583 C C   . LEU A 1 223 ? 32.180 9.040   18.495 1.00 79.26  ? 222 LEU A C   1 
ATOM 1584 O O   . LEU A 1 223 ? 32.656 8.004   18.974 1.00 79.65  ? 222 LEU A O   1 
ATOM 1585 C CB  . LEU A 1 223 ? 33.717 10.486  17.146 1.00 78.48  ? 222 LEU A CB  1 
ATOM 1586 C CG  . LEU A 1 223 ? 34.542 10.683  15.873 1.00 91.28  ? 222 LEU A CG  1 
ATOM 1587 C CD1 . LEU A 1 223 ? 35.961 11.105  16.224 1.00 98.58  ? 222 LEU A CD1 1 
ATOM 1588 C CD2 . LEU A 1 223 ? 34.549 9.426   15.013 1.00 88.23  ? 222 LEU A CD2 1 
ATOM 1589 N N   . MET A 1 224 ? 31.322 9.806   19.170 1.00 72.78  ? 223 MET A N   1 
ATOM 1590 C CA  . MET A 1 224 ? 30.892 9.433   20.512 1.00 70.87  ? 223 MET A CA  1 
ATOM 1591 C C   . MET A 1 224 ? 30.047 8.165   20.490 1.00 69.01  ? 223 MET A C   1 
ATOM 1592 O O   . MET A 1 224 ? 30.247 7.266   21.315 1.00 68.97  ? 223 MET A O   1 
ATOM 1593 C CB  . MET A 1 224 ? 30.126 10.592  21.146 1.00 68.65  ? 223 MET A CB  1 
ATOM 1594 C CG  . MET A 1 224 ? 29.150 10.192  22.228 1.00 68.84  ? 223 MET A CG  1 
ATOM 1595 S SD  . MET A 1 224 ? 28.304 11.632  22.903 1.00 86.13  ? 223 MET A SD  1 
ATOM 1596 C CE  . MET A 1 224 ? 29.660 12.795  23.024 1.00 64.29  ? 223 MET A CE  1 
ATOM 1597 N N   . ALA A 1 225 ? 29.104 8.068   19.549 1.00 70.72  ? 224 ALA A N   1 
ATOM 1598 C CA  . ALA A 1 225 ? 28.305 6.853   19.431 1.00 69.46  ? 224 ALA A CA  1 
ATOM 1599 C C   . ALA A 1 225 ? 29.152 5.667   18.988 1.00 63.23  ? 224 ALA A C   1 
ATOM 1600 O O   . ALA A 1 225 ? 28.862 4.526   19.365 1.00 62.16  ? 224 ALA A O   1 
ATOM 1601 C CB  . ALA A 1 225 ? 27.148 7.073   18.458 1.00 63.75  ? 224 ALA A CB  1 
ATOM 1602 N N   . LEU A 1 226 ? 30.192 5.914   18.187 1.00 58.10  ? 225 LEU A N   1 
ATOM 1603 C CA  . LEU A 1 226 ? 31.107 4.842   17.809 1.00 70.01  ? 225 LEU A CA  1 
ATOM 1604 C C   . LEU A 1 226 ? 31.824 4.285   19.031 1.00 70.39  ? 225 LEU A C   1 
ATOM 1605 O O   . LEU A 1 226 ? 31.924 3.064   19.207 1.00 58.90  ? 225 LEU A O   1 
ATOM 1606 C CB  . LEU A 1 226 ? 32.118 5.351   16.781 1.00 61.03  ? 225 LEU A CB  1 
ATOM 1607 C CG  . LEU A 1 226 ? 31.657 5.399   15.324 1.00 61.25  ? 225 LEU A CG  1 
ATOM 1608 C CD1 . LEU A 1 226 ? 32.654 6.177   14.480 1.00 64.45  ? 225 LEU A CD1 1 
ATOM 1609 C CD2 . LEU A 1 226 ? 31.470 3.995   14.780 1.00 45.97  ? 225 LEU A CD2 1 
ATOM 1610 N N   . ILE A 1 227 ? 32.332 5.173   19.889 1.00 67.22  ? 226 ILE A N   1 
ATOM 1611 C CA  . ILE A 1 227 ? 32.980 4.734   21.121 1.00 67.92  ? 226 ILE A CA  1 
ATOM 1612 C C   . ILE A 1 227 ? 31.984 4.006   22.013 1.00 66.13  ? 226 ILE A C   1 
ATOM 1613 O O   . ILE A 1 227 ? 32.329 3.028   22.688 1.00 61.32  ? 226 ILE A O   1 
ATOM 1614 C CB  . ILE A 1 227 ? 33.623 5.935   21.839 1.00 63.65  ? 226 ILE A CB  1 
ATOM 1615 C CG1 . ILE A 1 227 ? 34.718 6.543   20.960 1.00 64.69  ? 226 ILE A CG1 1 
ATOM 1616 C CG2 . ILE A 1 227 ? 34.178 5.525   23.196 1.00 69.06  ? 226 ILE A CG2 1 
ATOM 1617 C CD1 . ILE A 1 227 ? 35.996 5.732   20.922 1.00 66.74  ? 226 ILE A CD1 1 
ATOM 1618 N N   . THR A 1 228 ? 30.728 4.457   22.016 1.00 65.85  ? 227 THR A N   1 
ATOM 1619 C CA  . THR A 1 228 ? 29.699 3.763   22.783 1.00 61.26  ? 227 THR A CA  1 
ATOM 1620 C C   . THR A 1 228 ? 29.418 2.376   22.221 1.00 64.07  ? 227 THR A C   1 
ATOM 1621 O O   . THR A 1 228 ? 29.135 1.449   22.984 1.00 71.96  ? 227 THR A O   1 
ATOM 1622 C CB  . THR A 1 228 ? 28.411 4.590   22.808 1.00 61.85  ? 227 THR A CB  1 
ATOM 1623 O OG1 . THR A 1 228 ? 28.712 5.940   23.181 1.00 70.43  ? 227 THR A OG1 1 
ATOM 1624 C CG2 . THR A 1 228 ? 27.415 4.010   23.802 1.00 53.68  ? 227 THR A CG2 1 
ATOM 1625 N N   . SER A 1 229 ? 29.513 2.209   20.900 1.00 63.37  ? 228 SER A N   1 
ATOM 1626 C CA  . SER A 1 229 ? 29.082 0.966   20.269 1.00 66.69  ? 228 SER A CA  1 
ATOM 1627 C C   . SER A 1 229 ? 30.108 -0.152  20.432 1.00 59.20  ? 228 SER A C   1 
ATOM 1628 O O   . SER A 1 229 ? 29.739 -1.303  20.685 1.00 55.35  ? 228 SER A O   1 
ATOM 1629 C CB  . SER A 1 229 ? 28.789 1.213   18.787 1.00 62.47  ? 228 SER A CB  1 
ATOM 1630 O OG  . SER A 1 229 ? 27.796 2.209   18.622 1.00 67.70  ? 228 SER A OG  1 
ATOM 1631 N N   . VAL A 1 230 ? 31.392 0.165   20.304 1.00 59.57  ? 229 VAL A N   1 
ATOM 1632 C CA  . VAL A 1 230 ? 32.438 -0.846  20.269 1.00 57.26  ? 229 VAL A CA  1 
ATOM 1633 C C   . VAL A 1 230 ? 33.025 -1.083  21.668 1.00 61.79  ? 229 VAL A C   1 
ATOM 1634 O O   . VAL A 1 230 ? 34.084 -1.692  21.806 1.00 60.74  ? 229 VAL A O   1 
ATOM 1635 C CB  . VAL A 1 230 ? 33.522 -0.472  19.239 1.00 61.18  ? 229 VAL A CB  1 
ATOM 1636 C CG1 . VAL A 1 230 ? 34.528 -1.607  18.985 1.00 60.39  ? 229 VAL A CG1 1 
ATOM 1637 C CG2 . VAL A 1 230 ? 32.865 -0.041  17.937 1.00 54.84  ? 229 VAL A CG2 1 
ATOM 1638 N N   . THR A 1 231 ? 32.346 -0.618  22.717 1.00 60.06  ? 230 THR A N   1 
ATOM 1639 C CA  . THR A 1 231 ? 32.846 -0.863  24.066 1.00 59.49  ? 230 THR A CA  1 
ATOM 1640 C C   . THR A 1 231 ? 31.937 -1.779  24.869 1.00 63.29  ? 230 THR A C   1 
ATOM 1641 O O   . THR A 1 231 ? 32.089 -3.003  24.827 1.00 57.57  ? 230 THR A O   1 
ATOM 1642 C CB  . THR A 1 231 ? 33.043 0.452   24.819 1.00 60.71  ? 230 THR A CB  1 
ATOM 1643 O OG1 . THR A 1 231 ? 31.926 1.317   24.582 1.00 66.15  ? 230 THR A OG1 1 
ATOM 1644 C CG2 . THR A 1 231 ? 34.326 1.132   24.368 1.00 58.62  ? 230 THR A CG2 1 
ATOM 1645 N N   . LEU A 1 232 ? 30.995 -1.198  25.609 1.00 66.74  ? 231 LEU A N   1 
ATOM 1646 C CA  . LEU A 1 232 ? 30.103 -2.013  26.430 1.00 52.58  ? 231 LEU A CA  1 
ATOM 1647 C C   . LEU A 1 232 ? 29.268 -3.006  25.633 1.00 61.55  ? 231 LEU A C   1 
ATOM 1648 O O   . LEU A 1 232 ? 29.068 -4.128  26.129 1.00 67.88  ? 231 LEU A O   1 
ATOM 1649 C CB  . LEU A 1 232 ? 29.205 -1.105  27.281 1.00 50.25  ? 231 LEU A CB  1 
ATOM 1650 C CG  . LEU A 1 232 ? 29.869 -0.467  28.504 1.00 57.22  ? 231 LEU A CG  1 
ATOM 1651 C CD1 . LEU A 1 232 ? 28.846 -0.246  29.609 1.00 59.52  ? 231 LEU A CD1 1 
ATOM 1652 C CD2 . LEU A 1 232 ? 31.030 -1.317  29.002 1.00 57.07  ? 231 LEU A CD2 1 
ATOM 1653 N N   . PRO A 1 233 ? 28.739 -2.684  24.447 1.00 58.87  ? 232 PRO A N   1 
ATOM 1654 C CA  . PRO A 1 233 ? 28.007 -3.718  23.691 1.00 63.97  ? 232 PRO A CA  1 
ATOM 1655 C C   . PRO A 1 233 ? 28.845 -4.937  23.345 1.00 58.94  ? 232 PRO A C   1 
ATOM 1656 O O   . PRO A 1 233 ? 28.414 -6.067  23.602 1.00 57.03  ? 232 PRO A O   1 
ATOM 1657 C CB  . PRO A 1 233 ? 27.533 -2.957  22.449 1.00 65.10  ? 232 PRO A CB  1 
ATOM 1658 C CG  . PRO A 1 233 ? 27.353 -1.574  22.942 1.00 65.38  ? 232 PRO A CG  1 
ATOM 1659 C CD  . PRO A 1 233 ? 28.504 -1.348  23.876 1.00 56.91  ? 232 PRO A CD  1 
ATOM 1660 N N   . VAL A 1 234 ? 30.035 -4.749  22.773 1.00 53.61  ? 233 VAL A N   1 
ATOM 1661 C CA  . VAL A 1 234 ? 30.876 -5.897  22.464 1.00 63.43  ? 233 VAL A CA  1 
ATOM 1662 C C   . VAL A 1 234 ? 31.372 -6.577  23.733 1.00 60.95  ? 233 VAL A C   1 
ATOM 1663 O O   . VAL A 1 234 ? 31.754 -7.752  23.694 1.00 67.18  ? 233 VAL A O   1 
ATOM 1664 C CB  . VAL A 1 234 ? 32.052 -5.473  21.563 1.00 54.75  ? 233 VAL A CB  1 
ATOM 1665 C CG1 . VAL A 1 234 ? 31.542 -4.635  20.399 1.00 59.59  ? 233 VAL A CG1 1 
ATOM 1666 C CG2 . VAL A 1 234 ? 33.091 -4.714  22.363 1.00 63.74  ? 233 VAL A CG2 1 
ATOM 1667 N N   . ALA A 1 235 ? 31.369 -5.870  24.865 1.00 62.12  ? 234 ALA A N   1 
ATOM 1668 C CA  . ALA A 1 235 ? 31.714 -6.504  26.132 1.00 61.42  ? 234 ALA A CA  1 
ATOM 1669 C C   . ALA A 1 235 ? 30.662 -7.529  26.530 1.00 69.08  ? 234 ALA A C   1 
ATOM 1670 O O   . ALA A 1 235 ? 30.984 -8.687  26.820 1.00 68.54  ? 234 ALA A O   1 
ATOM 1671 C CB  . ALA A 1 235 ? 31.873 -5.450  27.227 1.00 60.65  ? 234 ALA A CB  1 
ATOM 1672 N N   . TYR A 1 236 ? 29.392 -7.118  26.547 1.00 67.30  ? 235 TYR A N   1 
ATOM 1673 C CA  . TYR A 1 236 ? 28.324 -8.035  26.924 1.00 70.96  ? 235 TYR A CA  1 
ATOM 1674 C C   . TYR A 1 236 ? 28.251 -9.228  25.981 1.00 67.40  ? 235 TYR A C   1 
ATOM 1675 O O   . TYR A 1 236 ? 27.922 -10.338 26.412 1.00 70.37  ? 235 TYR A O   1 
ATOM 1676 C CB  . TYR A 1 236 ? 26.986 -7.299  26.950 1.00 72.15  ? 235 TYR A CB  1 
ATOM 1677 C CG  . TYR A 1 236 ? 26.715 -6.522  28.219 1.00 79.64  ? 235 TYR A CG  1 
ATOM 1678 C CD1 . TYR A 1 236 ? 27.718 -6.306  29.156 1.00 80.24  ? 235 TYR A CD1 1 
ATOM 1679 C CD2 . TYR A 1 236 ? 25.457 -5.990  28.473 1.00 84.34  ? 235 TYR A CD2 1 
ATOM 1680 C CE1 . TYR A 1 236 ? 27.472 -5.593  30.315 1.00 78.66  ? 235 TYR A CE1 1 
ATOM 1681 C CE2 . TYR A 1 236 ? 25.203 -5.274  29.629 1.00 91.16  ? 235 TYR A CE2 1 
ATOM 1682 C CZ  . TYR A 1 236 ? 26.215 -5.079  30.546 1.00 87.71  ? 235 TYR A CZ  1 
ATOM 1683 O OH  . TYR A 1 236 ? 25.968 -4.367  31.698 1.00 88.92  ? 235 TYR A OH  1 
ATOM 1684 N N   . ILE A 1 237 ? 28.564 -9.027  24.700 1.00 63.43  ? 236 ILE A N   1 
ATOM 1685 C CA  . ILE A 1 237 ? 28.483 -10.123 23.738 1.00 61.76  ? 236 ILE A CA  1 
ATOM 1686 C C   . ILE A 1 237 ? 29.520 -11.192 24.059 1.00 60.46  ? 236 ILE A C   1 
ATOM 1687 O O   . ILE A 1 237 ? 29.212 -12.390 24.080 1.00 64.52  ? 236 ILE A O   1 
ATOM 1688 C CB  . ILE A 1 237 ? 28.643 -9.593  22.303 1.00 61.93  ? 236 ILE A CB  1 
ATOM 1689 C CG1 . ILE A 1 237 ? 27.487 -8.655  21.956 1.00 60.96  ? 236 ILE A CG1 1 
ATOM 1690 C CG2 . ILE A 1 237 ? 28.709 -10.747 21.316 1.00 49.30  ? 236 ILE A CG2 1 
ATOM 1691 C CD1 . ILE A 1 237 ? 27.617 -8.011  20.599 1.00 61.43  ? 236 ILE A CD1 1 
ATOM 1692 N N   . MET A 1 238 ? 30.764 -10.777 24.315 1.00 57.71  ? 237 MET A N   1 
ATOM 1693 C CA  . MET A 1 238 ? 31.807 -11.741 24.646 1.00 68.64  ? 237 MET A CA  1 
ATOM 1694 C C   . MET A 1 238 ? 31.496 -12.482 25.938 1.00 65.21  ? 237 MET A C   1 
ATOM 1695 O O   . MET A 1 238 ? 31.818 -13.669 26.067 1.00 61.25  ? 237 MET A O   1 
ATOM 1696 C CB  . MET A 1 238 ? 33.161 -11.042 24.764 1.00 60.10  ? 237 MET A CB  1 
ATOM 1697 C CG  . MET A 1 238 ? 33.797 -10.678 23.440 1.00 56.60  ? 237 MET A CG  1 
ATOM 1698 S SD  . MET A 1 238 ? 35.038 -9.389  23.638 1.00 77.05  ? 237 MET A SD  1 
ATOM 1699 C CE  . MET A 1 238 ? 36.539 -10.363 23.673 1.00 68.22  ? 237 MET A CE  1 
ATOM 1700 N N   . MET A 1 239 ? 30.870 -11.804 26.900 1.00 65.31  ? 238 MET A N   1 
ATOM 1701 C CA  . MET A 1 239 ? 30.576 -12.442 28.176 1.00 67.15  ? 238 MET A CA  1 
ATOM 1702 C C   . MET A 1 239 ? 29.430 -13.440 28.044 1.00 66.92  ? 238 MET A C   1 
ATOM 1703 O O   . MET A 1 239 ? 29.436 -14.485 28.703 1.00 68.89  ? 238 MET A O   1 
ATOM 1704 C CB  . MET A 1 239 ? 30.271 -11.374 29.224 1.00 68.14  ? 238 MET A CB  1 
ATOM 1705 C CG  . MET A 1 239 ? 31.531 -10.680 29.730 1.00 74.15  ? 238 MET A CG  1 
ATOM 1706 S SD  . MET A 1 239 ? 31.276 -9.326  30.896 1.00 94.42  ? 238 MET A SD  1 
ATOM 1707 C CE  . MET A 1 239 ? 29.497 -9.304  31.046 1.00 69.19  ? 238 MET A CE  1 
ATOM 1708 N N   . ARG A 1 240 ? 28.444 -13.150 27.191 1.00 63.30  ? 239 ARG A N   1 
ATOM 1709 C CA  . ARG A 1 240 ? 27.391 -14.130 26.953 1.00 62.52  ? 239 ARG A CA  1 
ATOM 1710 C C   . ARG A 1 240 ? 27.884 -15.274 26.075 1.00 59.99  ? 239 ARG A C   1 
ATOM 1711 O O   . ARG A 1 240 ? 27.350 -16.387 26.152 1.00 63.09  ? 239 ARG A O   1 
ATOM 1712 C CB  . ARG A 1 240 ? 26.173 -13.468 26.310 1.00 58.14  ? 239 ARG A CB  1 
ATOM 1713 C CG  . ARG A 1 240 ? 25.600 -12.298 27.071 1.00 52.89  ? 239 ARG A CG  1 
ATOM 1714 C CD  . ARG A 1 240 ? 24.166 -12.048 26.635 1.00 56.73  ? 239 ARG A CD  1 
ATOM 1715 N NE  . ARG A 1 240 ? 23.687 -10.704 26.943 1.00 65.85  ? 239 ARG A NE  1 
ATOM 1716 C CZ  . ARG A 1 240 ? 24.187 -9.579  26.445 1.00 72.04  ? 239 ARG A CZ  1 
ATOM 1717 N NH1 . ARG A 1 240 ? 25.165 -9.588  25.553 1.00 63.43  ? 239 ARG A NH1 1 
ATOM 1718 N NH2 . ARG A 1 240 ? 23.679 -8.414  26.839 1.00 75.58  ? 239 ARG A NH2 1 
ATOM 1719 N N   . LYS A 1 241 ? 28.880 -15.020 25.222 1.00 61.37  ? 240 LYS A N   1 
ATOM 1720 C CA  . LYS A 1 241 ? 29.440 -16.098 24.415 1.00 57.30  ? 240 LYS A CA  1 
ATOM 1721 C C   . LYS A 1 241 ? 30.322 -17.013 25.255 1.00 58.10  ? 240 LYS A C   1 
ATOM 1722 O O   . LYS A 1 241 ? 30.248 -18.241 25.126 1.00 53.03  ? 240 LYS A O   1 
ATOM 1723 C CB  . LYS A 1 241 ? 30.227 -15.525 23.237 1.00 52.50  ? 240 LYS A CB  1 
ATOM 1724 C CG  . LYS A 1 241 ? 29.413 -15.391 21.962 1.00 62.85  ? 240 LYS A CG  1 
ATOM 1725 C CD  . LYS A 1 241 ? 30.280 -15.584 20.727 1.00 64.84  ? 240 LYS A CD  1 
ATOM 1726 C CE  . LYS A 1 241 ? 31.522 -14.702 20.771 1.00 66.34  ? 240 LYS A CE  1 
ATOM 1727 N NZ  . LYS A 1 241 ? 32.382 -14.883 19.566 1.00 68.59  ? 240 LYS A NZ  1 
ATOM 1728 N N   . LEU A 1 242 ? 31.155 -16.434 26.122 1.00 56.49  ? 241 LEU A N   1 
ATOM 1729 C CA  . LEU A 1 242 ? 31.943 -17.242 27.044 1.00 58.74  ? 241 LEU A CA  1 
ATOM 1730 C C   . LEU A 1 242 ? 31.051 -17.984 28.029 1.00 61.41  ? 241 LEU A C   1 
ATOM 1731 O O   . LEU A 1 242 ? 31.370 -19.108 28.434 1.00 60.59  ? 241 LEU A O   1 
ATOM 1732 C CB  . LEU A 1 242 ? 32.943 -16.357 27.789 1.00 57.75  ? 241 LEU A CB  1 
ATOM 1733 C CG  . LEU A 1 242 ? 33.751 -17.011 28.913 1.00 56.34  ? 241 LEU A CG  1 
ATOM 1734 C CD1 . LEU A 1 242 ? 34.681 -18.077 28.359 1.00 58.84  ? 241 LEU A CD1 1 
ATOM 1735 C CD2 . LEU A 1 242 ? 34.530 -15.968 29.700 1.00 62.49  ? 241 LEU A CD2 1 
ATOM 1736 N N   . LEU A 1 243 ? 29.927 -17.378 28.414 1.00 62.83  ? 242 LEU A N   1 
ATOM 1737 C CA  . LEU A 1 243 ? 29.026 -18.023 29.362 1.00 57.80  ? 242 LEU A CA  1 
ATOM 1738 C C   . LEU A 1 243 ? 28.245 -19.151 28.701 1.00 61.45  ? 242 LEU A C   1 
ATOM 1739 O O   . LEU A 1 243 ? 27.987 -20.185 29.328 1.00 63.45  ? 242 LEU A O   1 
ATOM 1740 C CB  . LEU A 1 243 ? 28.083 -16.986 29.968 1.00 51.17  ? 242 LEU A CB  1 
ATOM 1741 C CG  . LEU A 1 243 ? 26.959 -17.491 30.863 1.00 54.48  ? 242 LEU A CG  1 
ATOM 1742 C CD1 . LEU A 1 243 ? 27.405 -17.405 32.287 1.00 61.13  ? 242 LEU A CD1 1 
ATOM 1743 C CD2 . LEU A 1 243 ? 25.733 -16.638 30.662 1.00 56.40  ? 242 LEU A CD2 1 
ATOM 1744 N N   . ALA A 1 244 ? 27.868 -18.976 27.435 1.00 59.19  ? 243 ALA A N   1 
ATOM 1745 C CA  . ALA A 1 244 ? 27.187 -20.028 26.693 1.00 60.95  ? 243 ALA A CA  1 
ATOM 1746 C C   . ALA A 1 244 ? 28.131 -21.119 26.209 1.00 58.98  ? 243 ALA A C   1 
ATOM 1747 O O   . ALA A 1 244 ? 27.659 -22.171 25.767 1.00 56.31  ? 243 ALA A O   1 
ATOM 1748 C CB  . ALA A 1 244 ? 26.443 -19.432 25.497 1.00 56.74  ? 243 ALA A CB  1 
ATOM 1749 N N   . ALA A 1 245 ? 29.443 -20.891 26.267 1.00 60.44  ? 244 ALA A N   1 
ATOM 1750 C CA  . ALA A 1 245 ? 30.412 -21.899 25.856 1.00 54.61  ? 244 ALA A CA  1 
ATOM 1751 C C   . ALA A 1 245 ? 30.751 -22.859 26.986 1.00 65.72  ? 244 ALA A C   1 
ATOM 1752 O O   . ALA A 1 245 ? 30.869 -24.068 26.756 1.00 67.99  ? 244 ALA A O   1 
ATOM 1753 C CB  . ALA A 1 245 ? 31.687 -21.226 25.339 1.00 45.40  ? 244 ALA A CB  1 
ATOM 1754 N N   . GLN A 1 246 ? 30.912 -22.343 28.206 1.00 73.05  ? 245 GLN A N   1 
ATOM 1755 C CA  . GLN A 1 246 ? 31.134 -23.208 29.361 1.00 80.89  ? 245 GLN A CA  1 
ATOM 1756 C C   . GLN A 1 246 ? 29.839 -23.883 29.794 1.00 75.57  ? 245 GLN A C   1 
ATOM 1757 O O   . GLN A 1 246 ? 29.809 -25.095 30.034 1.00 73.66  ? 245 GLN A O   1 
ATOM 1758 C CB  . GLN A 1 246 ? 31.728 -22.401 30.516 1.00 76.39  ? 245 GLN A CB  1 
ATOM 1759 C CG  . GLN A 1 246 ? 32.933 -21.564 30.135 1.00 78.44  ? 245 GLN A CG  1 
ATOM 1760 C CD  . GLN A 1 246 ? 34.239 -22.284 30.386 1.00 89.40  ? 245 GLN A CD  1 
ATOM 1761 O OE1 . GLN A 1 246 ? 34.320 -23.171 31.235 1.00 89.17  ? 245 GLN A OE1 1 
ATOM 1762 N NE2 . GLN A 1 246 ? 35.273 -21.904 29.646 1.00 99.06  ? 245 GLN A NE2 1 
ATOM 1763 N N   . TYR A 1 247 ? 28.758 -23.112 29.893 1.00 70.18  ? 246 TYR A N   1 
ATOM 1764 C CA  . TYR A 1 247 ? 27.449 -23.604 30.276 1.00 68.95  ? 246 TYR A CA  1 
ATOM 1765 C C   . TYR A 1 247 ? 26.549 -23.628 29.036 1.00 68.50  ? 246 TYR A C   1 
ATOM 1766 O O   . TYR A 1 247 ? 27.040 -23.726 27.904 1.00 78.52  ? 246 TYR A O   1 
ATOM 1767 C CB  . TYR A 1 247 ? 26.903 -22.740 31.418 1.00 66.61  ? 246 TYR A CB  1 
ATOM 1768 C CG  . TYR A 1 247 ? 27.766 -22.785 32.663 1.00 69.13  ? 246 TYR A CG  1 
ATOM 1769 C CD1 . TYR A 1 247 ? 28.922 -22.019 32.761 1.00 68.54  ? 246 TYR A CD1 1 
ATOM 1770 C CD2 . TYR A 1 247 ? 27.434 -23.604 33.735 1.00 73.72  ? 246 TYR A CD2 1 
ATOM 1771 C CE1 . TYR A 1 247 ? 29.719 -22.065 33.890 1.00 71.27  ? 246 TYR A CE1 1 
ATOM 1772 C CE2 . TYR A 1 247 ? 28.225 -23.654 34.870 1.00 72.01  ? 246 TYR A CE2 1 
ATOM 1773 C CZ  . TYR A 1 247 ? 29.365 -22.882 34.943 1.00 68.38  ? 246 TYR A CZ  1 
ATOM 1774 O OH  . TYR A 1 247 ? 30.154 -22.928 36.069 1.00 67.65  ? 246 TYR A OH  1 
ATOM 1775 N N   . SER A 1 248 ? 25.241 -23.541 29.246 1.00 66.51  ? 247 SER A N   1 
ATOM 1776 C CA  . SER A 1 248 ? 24.275 -23.603 28.159 1.00 63.85  ? 247 SER A CA  1 
ATOM 1777 C C   . SER A 1 248 ? 23.813 -22.204 27.760 1.00 58.64  ? 247 SER A C   1 
ATOM 1778 O O   . SER A 1 248 ? 24.090 -21.209 28.433 1.00 63.43  ? 247 SER A O   1 
ATOM 1779 C CB  . SER A 1 248 ? 23.072 -24.460 28.563 1.00 58.05  ? 247 SER A CB  1 
ATOM 1780 O OG  . SER A 1 248 ? 22.472 -23.975 29.752 1.00 60.89  ? 247 SER A OG  1 
ATOM 1781 N N   . TRP A 1 249 ? 23.104 -22.139 26.628 1.00 58.18  ? 248 TRP A N   1 
ATOM 1782 C CA  . TRP A 1 249 ? 22.369 -20.927 26.284 1.00 47.65  ? 248 TRP A CA  1 
ATOM 1783 C C   . TRP A 1 249 ? 21.179 -20.716 27.208 1.00 50.67  ? 248 TRP A C   1 
ATOM 1784 O O   . TRP A 1 249 ? 20.697 -19.585 27.332 1.00 52.76  ? 248 TRP A O   1 
ATOM 1785 C CB  . TRP A 1 249 ? 21.894 -20.976 24.827 1.00 54.00  ? 248 TRP A CB  1 
ATOM 1786 C CG  . TRP A 1 249 ? 22.932 -20.549 23.818 1.00 49.06  ? 248 TRP A CG  1 
ATOM 1787 C CD1 . TRP A 1 249 ? 23.541 -21.339 22.886 1.00 50.25  ? 248 TRP A CD1 1 
ATOM 1788 C CD2 . TRP A 1 249 ? 23.471 -19.231 23.637 1.00 56.05  ? 248 TRP A CD2 1 
ATOM 1789 N NE1 . TRP A 1 249 ? 24.429 -20.600 22.143 1.00 48.40  ? 248 TRP A NE1 1 
ATOM 1790 C CE2 . TRP A 1 249 ? 24.405 -19.303 22.583 1.00 51.02  ? 248 TRP A CE2 1 
ATOM 1791 C CE3 . TRP A 1 249 ? 23.258 -18.001 24.267 1.00 53.65  ? 248 TRP A CE3 1 
ATOM 1792 C CZ2 . TRP A 1 249 ? 25.124 -18.192 22.145 1.00 44.03  ? 248 TRP A CZ2 1 
ATOM 1793 C CZ3 . TRP A 1 249 ? 23.974 -16.900 23.831 1.00 54.72  ? 248 TRP A CZ3 1 
ATOM 1794 C CH2 . TRP A 1 249 ? 24.894 -17.003 22.779 1.00 54.35  ? 248 TRP A CH2 1 
ATOM 1795 N N   . ASP A 1 250 ? 20.691 -21.782 27.851 1.00 58.65  ? 249 ASP A N   1 
ATOM 1796 C CA  . ASP A 1 250 ? 19.671 -21.622 28.882 1.00 58.74  ? 249 ASP A CA  1 
ATOM 1797 C C   . ASP A 1 250 ? 20.222 -20.867 30.084 1.00 56.73  ? 249 ASP A C   1 
ATOM 1798 O O   . ASP A 1 250 ? 19.493 -20.105 30.730 1.00 46.85  ? 249 ASP A O   1 
ATOM 1799 C CB  . ASP A 1 250 ? 19.140 -22.988 29.320 1.00 54.64  ? 249 ASP A CB  1 
ATOM 1800 C CG  . ASP A 1 250 ? 18.826 -23.899 28.150 1.00 54.98  ? 249 ASP A CG  1 
ATOM 1801 O OD1 . ASP A 1 250 ? 19.747 -24.193 27.360 1.00 54.13  ? 249 ASP A OD1 1 
ATOM 1802 O OD2 . ASP A 1 250 ? 17.660 -24.331 28.029 1.00 59.65  ? 249 ASP A OD2 1 
ATOM 1803 N N   . GLU A 1 251 ? 21.503 -21.073 30.402 1.00 56.13  ? 250 GLU A N   1 
ATOM 1804 C CA  . GLU A 1 251 ? 22.128 -20.327 31.486 1.00 51.70  ? 250 GLU A CA  1 
ATOM 1805 C C   . GLU A 1 251 ? 22.275 -18.853 31.135 1.00 53.32  ? 250 GLU A C   1 
ATOM 1806 O O   . GLU A 1 251 ? 22.230 -17.997 32.026 1.00 60.71  ? 250 GLU A O   1 
ATOM 1807 C CB  . GLU A 1 251 ? 23.487 -20.943 31.824 1.00 54.55  ? 250 GLU A CB  1 
ATOM 1808 C CG  . GLU A 1 251 ? 24.114 -20.436 33.114 1.00 56.26  ? 250 GLU A CG  1 
ATOM 1809 C CD  . GLU A 1 251 ? 23.436 -20.972 34.367 1.00 59.42  ? 250 GLU A CD  1 
ATOM 1810 O OE1 . GLU A 1 251 ? 22.429 -21.703 34.251 1.00 65.70  ? 250 GLU A OE1 1 
ATOM 1811 O OE2 . GLU A 1 251 ? 23.917 -20.658 35.476 1.00 58.46  ? 250 GLU A OE2 1 
ATOM 1812 N N   . VAL A 1 252 ? 22.446 -18.537 29.849 1.00 54.01  ? 251 VAL A N   1 
ATOM 1813 C CA  . VAL A 1 252 ? 22.477 -17.139 29.429 1.00 51.19  ? 251 VAL A CA  1 
ATOM 1814 C C   . VAL A 1 252 ? 21.118 -16.491 29.651 1.00 54.76  ? 251 VAL A C   1 
ATOM 1815 O O   . VAL A 1 252 ? 21.026 -15.333 30.076 1.00 57.62  ? 251 VAL A O   1 
ATOM 1816 C CB  . VAL A 1 252 ? 22.925 -17.031 27.960 1.00 59.55  ? 251 VAL A CB  1 
ATOM 1817 C CG1 . VAL A 1 252 ? 23.244 -15.586 27.603 1.00 48.00  ? 251 VAL A CG1 1 
ATOM 1818 C CG2 . VAL A 1 252 ? 24.124 -17.925 27.712 1.00 54.79  ? 251 VAL A CG2 1 
ATOM 1819 N N   . GLY A 1 253 ? 20.041 -17.230 29.376 1.00 50.78  ? 252 GLY A N   1 
ATOM 1820 C CA  . GLY A 1 253 ? 18.705 -16.712 29.603 1.00 53.85  ? 252 GLY A CA  1 
ATOM 1821 C C   . GLY A 1 253 ? 18.365 -16.504 31.062 1.00 51.70  ? 252 GLY A C   1 
ATOM 1822 O O   . GLY A 1 253 ? 17.454 -15.728 31.370 1.00 55.05  ? 252 GLY A O   1 
ATOM 1823 N N   . ILE A 1 254 ? 19.072 -17.182 31.967 1.00 58.58  ? 253 ILE A N   1 
ATOM 1824 C CA  . ILE A 1 254 ? 18.849 -16.971 33.394 1.00 57.05  ? 253 ILE A CA  1 
ATOM 1825 C C   . ILE A 1 254 ? 19.414 -15.623 33.821 1.00 57.76  ? 253 ILE A C   1 
ATOM 1826 O O   . ILE A 1 254 ? 18.761 -14.851 34.533 1.00 65.39  ? 253 ILE A O   1 
ATOM 1827 C CB  . ILE A 1 254 ? 19.460 -18.127 34.207 1.00 57.58  ? 253 ILE A CB  1 
ATOM 1828 C CG1 . ILE A 1 254 ? 18.617 -19.392 34.044 1.00 51.80  ? 253 ILE A CG1 1 
ATOM 1829 C CG2 . ILE A 1 254 ? 19.577 -17.750 35.676 1.00 62.95  ? 253 ILE A CG2 1 
ATOM 1830 C CD1 . ILE A 1 254 ? 17.184 -19.227 34.500 1.00 52.87  ? 253 ILE A CD1 1 
ATOM 1831 N N   . TRP A 1 255 ? 20.635 -15.313 33.381 1.00 55.92  ? 254 TRP A N   1 
ATOM 1832 C CA  . TRP A 1 255 ? 21.243 -14.035 33.732 1.00 60.97  ? 254 TRP A CA  1 
ATOM 1833 C C   . TRP A 1 255 ? 20.629 -12.890 32.936 1.00 62.97  ? 254 TRP A C   1 
ATOM 1834 O O   . TRP A 1 255 ? 20.450 -11.788 33.464 1.00 71.55  ? 254 TRP A O   1 
ATOM 1835 C CB  . TRP A 1 255 ? 22.750 -14.096 33.502 1.00 58.33  ? 254 TRP A CB  1 
ATOM 1836 C CG  . TRP A 1 255 ? 23.444 -12.789 33.688 1.00 59.25  ? 254 TRP A CG  1 
ATOM 1837 C CD1 . TRP A 1 255 ? 23.186 -11.845 34.641 1.00 66.29  ? 254 TRP A CD1 1 
ATOM 1838 C CD2 . TRP A 1 255 ? 24.507 -12.271 32.887 1.00 66.62  ? 254 TRP A CD2 1 
ATOM 1839 N NE1 . TRP A 1 255 ? 24.032 -10.773 34.484 1.00 61.30  ? 254 TRP A NE1 1 
ATOM 1840 C CE2 . TRP A 1 255 ? 24.854 -11.012 33.414 1.00 61.96  ? 254 TRP A CE2 1 
ATOM 1841 C CE3 . TRP A 1 255 ? 25.204 -12.754 31.775 1.00 65.15  ? 254 TRP A CE3 1 
ATOM 1842 C CZ2 . TRP A 1 255 ? 25.867 -10.230 32.868 1.00 64.71  ? 254 TRP A CZ2 1 
ATOM 1843 C CZ3 . TRP A 1 255 ? 26.209 -11.978 31.236 1.00 64.02  ? 254 TRP A CZ3 1 
ATOM 1844 C CH2 . TRP A 1 255 ? 26.529 -10.730 31.781 1.00 67.06  ? 254 TRP A CH2 1 
ATOM 1845 N N   . GLN A 1 256 ? 20.304 -13.126 31.663 1.00 61.69  ? 255 GLN A N   1 
ATOM 1846 C CA  . GLN A 1 256 ? 19.696 -12.064 30.869 1.00 61.41  ? 255 GLN A CA  1 
ATOM 1847 C C   . GLN A 1 256 ? 18.309 -11.707 31.383 1.00 63.21  ? 255 GLN A C   1 
ATOM 1848 O O   . GLN A 1 256 ? 17.850 -10.575 31.190 1.00 67.99  ? 255 GLN A O   1 
ATOM 1849 C CB  . GLN A 1 256 ? 19.629 -12.470 29.398 1.00 58.42  ? 255 GLN A CB  1 
ATOM 1850 C CG  . GLN A 1 256 ? 19.397 -11.300 28.458 1.00 66.03  ? 255 GLN A CG  1 
ATOM 1851 C CD  . GLN A 1 256 ? 20.570 -10.338 28.423 1.00 72.44  ? 255 GLN A CD  1 
ATOM 1852 O OE1 . GLN A 1 256 ? 21.715 -10.726 28.660 1.00 75.53  ? 255 GLN A OE1 1 
ATOM 1853 N NE2 . GLN A 1 256 ? 20.290 -9.076  28.121 1.00 75.53  ? 255 GLN A NE2 1 
ATOM 1854 N N   . GLY A 1 257 ? 17.637 -12.648 32.047 1.00 50.45  ? 256 GLY A N   1 
ATOM 1855 C CA  . GLY A 1 257 ? 16.320 -12.358 32.586 1.00 57.96  ? 256 GLY A CA  1 
ATOM 1856 C C   . GLY A 1 257 ? 16.351 -11.333 33.704 1.00 68.21  ? 256 GLY A C   1 
ATOM 1857 O O   . GLY A 1 257 ? 15.464 -10.479 33.796 1.00 66.47  ? 256 GLY A O   1 
ATOM 1858 N N   . VAL A 1 258 ? 17.366 -11.399 34.570 1.00 65.18  ? 257 VAL A N   1 
ATOM 1859 C CA  . VAL A 1 258 ? 17.444 -10.429 35.657 1.00 69.59  ? 257 VAL A CA  1 
ATOM 1860 C C   . VAL A 1 258 ? 17.795 -9.052  35.116 1.00 65.62  ? 257 VAL A C   1 
ATOM 1861 O O   . VAL A 1 258 ? 17.405 -8.031  35.696 1.00 61.17  ? 257 VAL A O   1 
ATOM 1862 C CB  . VAL A 1 258 ? 18.447 -10.883 36.737 1.00 71.37  ? 257 VAL A CB  1 
ATOM 1863 C CG1 . VAL A 1 258 ? 18.211 -12.329 37.096 1.00 64.34  ? 257 VAL A CG1 1 
ATOM 1864 C CG2 . VAL A 1 258 ? 19.883 -10.663 36.294 1.00 70.73  ? 257 VAL A CG2 1 
ATOM 1865 N N   . SER A 1 259 ? 18.526 -8.992  34.000 1.00 65.93  ? 258 SER A N   1 
ATOM 1866 C CA  . SER A 1 259 ? 18.785 -7.705  33.370 1.00 71.07  ? 258 SER A CA  1 
ATOM 1867 C C   . SER A 1 259 ? 17.525 -7.162  32.711 1.00 67.83  ? 258 SER A C   1 
ATOM 1868 O O   . SER A 1 259 ? 17.280 -5.951  32.731 1.00 72.65  ? 258 SER A O   1 
ATOM 1869 C CB  . SER A 1 259 ? 19.917 -7.832  32.351 1.00 68.16  ? 258 SER A CB  1 
ATOM 1870 O OG  . SER A 1 259 ? 21.031 -8.504  32.912 1.00 71.31  ? 258 SER A OG  1 
ATOM 1871 N N   . SER A 1 260 ? 16.704 -8.046  32.139 1.00 68.05  ? 259 SER A N   1 
ATOM 1872 C CA  . SER A 1 260 ? 15.465 -7.607  31.505 1.00 67.84  ? 259 SER A CA  1 
ATOM 1873 C C   . SER A 1 260 ? 14.481 -7.039  32.520 1.00 60.27  ? 259 SER A C   1 
ATOM 1874 O O   . SER A 1 260 ? 13.732 -6.109  32.200 1.00 68.08  ? 259 SER A O   1 
ATOM 1875 C CB  . SER A 1 260 ? 14.826 -8.768  30.745 1.00 67.68  ? 259 SER A CB  1 
ATOM 1876 O OG  . SER A 1 260 ? 13.927 -9.483  31.575 1.00 67.12  ? 259 SER A OG  1 
ATOM 1877 N N   . ILE A 1 261 ? 14.464 -7.583  33.738 1.00 69.42  ? 260 ILE A N   1 
ATOM 1878 C CA  . ILE A 1 261 ? 13.547 -7.086  34.758 1.00 69.32  ? 260 ILE A CA  1 
ATOM 1879 C C   . ILE A 1 261 ? 14.015 -5.736  35.283 1.00 70.39  ? 260 ILE A C   1 
ATOM 1880 O O   . ILE A 1 261 ? 13.214 -4.809  35.458 1.00 65.56  ? 260 ILE A O   1 
ATOM 1881 C CB  . ILE A 1 261 ? 13.404 -8.119  35.892 1.00 56.70  ? 260 ILE A CB  1 
ATOM 1882 C CG1 . ILE A 1 261 ? 12.254 -9.080  35.590 1.00 62.35  ? 260 ILE A CG1 1 
ATOM 1883 C CG2 . ILE A 1 261 ? 13.188 -7.431  37.231 1.00 57.54  ? 260 ILE A CG2 1 
ATOM 1884 C CD1 . ILE A 1 261 ? 12.121 -10.205 36.589 1.00 56.33  ? 260 ILE A CD1 1 
ATOM 1885 N N   . SER A 1 262 ? 15.317 -5.604  35.537 1.00 76.41  ? 261 SER A N   1 
ATOM 1886 C CA  . SER A 1 262 ? 15.852 -4.348  36.046 1.00 78.47  ? 261 SER A CA  1 
ATOM 1887 C C   . SER A 1 262 ? 15.698 -3.224  35.035 1.00 78.82  ? 261 SER A C   1 
ATOM 1888 O O   . SER A 1 262 ? 15.508 -2.065  35.421 1.00 82.07  ? 261 SER A O   1 
ATOM 1889 C CB  . SER A 1 262 ? 17.319 -4.526  36.418 1.00 77.50  ? 261 SER A CB  1 
ATOM 1890 O OG  . SER A 1 262 ? 18.148 -4.473  35.270 1.00 82.76  ? 261 SER A OG  1 
ATOM 1891 N N   . ASP A 1 263 ? 15.759 -3.546  33.741 1.00 75.76  ? 262 ASP A N   1 
ATOM 1892 C CA  . ASP A 1 263 ? 15.591 -2.540  32.700 1.00 77.33  ? 262 ASP A CA  1 
ATOM 1893 C C   . ASP A 1 263 ? 14.192 -1.941  32.674 1.00 76.80  ? 262 ASP A C   1 
ATOM 1894 O O   . ASP A 1 263 ? 13.974 -0.961  31.955 1.00 83.54  ? 262 ASP A O   1 
ATOM 1895 C CB  . ASP A 1 263 ? 15.917 -3.140  31.329 1.00 79.61  ? 262 ASP A CB  1 
ATOM 1896 C CG  . ASP A 1 263 ? 17.385 -3.487  31.176 1.00 87.88  ? 262 ASP A CG  1 
ATOM 1897 O OD1 . ASP A 1 263 ? 17.775 -3.962  30.088 1.00 85.51  ? 262 ASP A OD1 1 
ATOM 1898 O OD2 . ASP A 1 263 ? 18.148 -3.290  32.146 1.00 86.96  ? 262 ASP A OD2 1 
ATOM 1899 N N   . ALA A 1 264 ? 13.244 -2.496  33.430 1.00 76.06  ? 263 ALA A N   1 
ATOM 1900 C CA  . ALA A 1 264 ? 11.888 -1.958  33.430 1.00 72.91  ? 263 ALA A CA  1 
ATOM 1901 C C   . ALA A 1 264 ? 11.828 -0.614  34.146 1.00 72.37  ? 263 ALA A C   1 
ATOM 1902 O O   . ALA A 1 264 ? 11.387 0.390   33.574 1.00 77.42  ? 263 ALA A O   1 
ATOM 1903 C CB  . ALA A 1 264 ? 10.927 -2.960  34.073 1.00 71.28  ? 263 ALA A CB  1 
ATOM 1904 N N   . TYR A 1 265 ? 12.274 -0.574  35.403 1.00 79.83  ? 264 TYR A N   1 
ATOM 1905 C CA  . TYR A 1 265 ? 12.198 0.655   36.185 1.00 75.84  ? 264 TYR A CA  1 
ATOM 1906 C C   . TYR A 1 265 ? 13.345 1.611   35.898 1.00 75.29  ? 264 TYR A C   1 
ATOM 1907 O O   . TYR A 1 265 ? 13.208 2.813   36.151 1.00 81.60  ? 264 TYR A O   1 
ATOM 1908 C CB  . TYR A 1 265 ? 12.152 0.324   37.684 1.00 72.03  ? 264 TYR A CB  1 
ATOM 1909 C CG  . TYR A 1 265 ? 13.397 -0.344  38.251 1.00 65.57  ? 264 TYR A CG  1 
ATOM 1910 C CD1 . TYR A 1 265 ? 14.566 0.376   38.482 1.00 69.02  ? 264 TYR A CD1 1 
ATOM 1911 C CD2 . TYR A 1 265 ? 13.394 -1.697  38.569 1.00 63.15  ? 264 TYR A CD2 1 
ATOM 1912 C CE1 . TYR A 1 265 ? 15.695 -0.233  39.000 1.00 69.88  ? 264 TYR A CE1 1 
ATOM 1913 C CE2 . TYR A 1 265 ? 14.519 -2.313  39.089 1.00 63.91  ? 264 TYR A CE2 1 
ATOM 1914 C CZ  . TYR A 1 265 ? 15.667 -1.576  39.302 1.00 69.16  ? 264 TYR A CZ  1 
ATOM 1915 O OH  . TYR A 1 265 ? 16.789 -2.184  39.818 1.00 57.71  ? 264 TYR A OH  1 
ATOM 1916 N N   . LEU A 1 266 ? 14.465 1.109   35.374 1.00 73.91  ? 265 LEU A N   1 
ATOM 1917 C CA  . LEU A 1 266 ? 15.648 1.948   35.217 1.00 84.22  ? 265 LEU A CA  1 
ATOM 1918 C C   . LEU A 1 266 ? 15.432 3.061   34.200 1.00 96.05  ? 265 LEU A C   1 
ATOM 1919 O O   . LEU A 1 266 ? 15.984 4.154   34.359 1.00 101.63 ? 265 LEU A O   1 
ATOM 1920 C CB  . LEU A 1 266 ? 16.851 1.094   34.816 1.00 83.59  ? 265 LEU A CB  1 
ATOM 1921 C CG  . LEU A 1 266 ? 17.564 0.353   35.947 1.00 69.70  ? 265 LEU A CG  1 
ATOM 1922 C CD1 . LEU A 1 266 ? 18.685 -0.517  35.398 1.00 77.47  ? 265 LEU A CD1 1 
ATOM 1923 C CD2 . LEU A 1 266 ? 18.095 1.330   36.978 1.00 74.22  ? 265 LEU A CD2 1 
ATOM 1924 N N   . GLN A 1 267 ? 14.635 2.813   33.159 1.00 100.37 ? 266 GLN A N   1 
ATOM 1925 C CA  . GLN A 1 267 ? 14.466 3.823   32.119 1.00 99.01  ? 266 GLN A CA  1 
ATOM 1926 C C   . GLN A 1 267 ? 13.503 4.924   32.539 1.00 105.28 ? 266 GLN A C   1 
ATOM 1927 O O   . GLN A 1 267 ? 13.686 6.081   32.146 1.00 102.39 ? 266 GLN A O   1 
ATOM 1928 C CB  . GLN A 1 267 ? 13.995 3.181   30.811 1.00 95.36  ? 266 GLN A CB  1 
ATOM 1929 C CG  . GLN A 1 267 ? 14.447 1.736   30.551 1.00 98.10  ? 266 GLN A CG  1 
ATOM 1930 C CD  . GLN A 1 267 ? 15.913 1.438   30.871 1.00 105.69 ? 266 GLN A CD  1 
ATOM 1931 O OE1 . GLN A 1 267 ? 16.751 2.334   30.985 1.00 115.37 ? 266 GLN A OE1 1 
ATOM 1932 N NE2 . GLN A 1 267 ? 16.219 0.158   31.024 1.00 102.52 ? 266 GLN A NE2 1 
ATOM 1933 N N   . PHE A 1 268 ? 12.473 4.588   33.321 1.00 114.21 ? 267 PHE A N   1 
ATOM 1934 C CA  . PHE A 1 268 ? 11.649 5.627   33.928 1.00 111.28 ? 267 PHE A CA  1 
ATOM 1935 C C   . PHE A 1 268 ? 12.459 6.459   34.911 1.00 112.62 ? 267 PHE A C   1 
ATOM 1936 O O   . PHE A 1 268 ? 12.150 7.635   35.134 1.00 121.18 ? 267 PHE A O   1 
ATOM 1937 C CB  . PHE A 1 268 ? 10.439 5.008   34.630 1.00 108.57 ? 267 PHE A CB  1 
ATOM 1938 C CG  . PHE A 1 268 ? 9.277  5.952   34.786 1.00 116.39 ? 267 PHE A CG  1 
ATOM 1939 C CD1 . PHE A 1 268 ? 9.093  6.997   33.896 1.00 114.82 ? 267 PHE A CD1 1 
ATOM 1940 C CD2 . PHE A 1 268 ? 8.372  5.795   35.824 1.00 120.92 ? 267 PHE A CD2 1 
ATOM 1941 C CE1 . PHE A 1 268 ? 8.027  7.868   34.036 1.00 113.69 ? 267 PHE A CE1 1 
ATOM 1942 C CE2 . PHE A 1 268 ? 7.302  6.664   35.969 1.00 115.92 ? 267 PHE A CE2 1 
ATOM 1943 C CZ  . PHE A 1 268 ? 7.131  7.700   35.074 1.00 115.43 ? 267 PHE A CZ  1 
ATOM 1944 N N   . ILE A 1 269 ? 13.497 5.866   35.504 1.00 105.88 ? 268 ILE A N   1 
ATOM 1945 C CA  . ILE A 1 269 ? 14.387 6.615   36.382 1.00 103.62 ? 268 ILE A CA  1 
ATOM 1946 C C   . ILE A 1 269 ? 15.322 7.500   35.564 1.00 107.83 ? 268 ILE A C   1 
ATOM 1947 O O   . ILE A 1 269 ? 15.586 8.651   35.933 1.00 106.71 ? 268 ILE A O   1 
ATOM 1948 C CB  . ILE A 1 269 ? 15.161 5.649   37.304 1.00 97.15  ? 268 ILE A CB  1 
ATOM 1949 C CG1 . ILE A 1 269 ? 14.441 5.457   38.645 1.00 91.13  ? 268 ILE A CG1 1 
ATOM 1950 C CG2 . ILE A 1 269 ? 16.585 6.137   37.545 1.00 95.52  ? 268 ILE A CG2 1 
ATOM 1951 C CD1 . ILE A 1 269 ? 12.969 5.120   38.540 1.00 93.96  ? 268 ILE A CD1 1 
ATOM 1952 N N   . THR A 1 270 ? 15.821 6.992   34.431 1.00 106.49 ? 269 THR A N   1 
ATOM 1953 C CA  . THR A 1 270 ? 16.679 7.796   33.565 1.00 109.49 ? 269 THR A CA  1 
ATOM 1954 C C   . THR A 1 270 ? 15.915 8.886   32.826 1.00 115.61 ? 269 THR A C   1 
ATOM 1955 O O   . THR A 1 270 ? 16.547 9.779   32.253 1.00 112.86 ? 269 THR A O   1 
ATOM 1956 C CB  . THR A 1 270 ? 17.413 6.916   32.548 1.00 96.47  ? 269 THR A CB  1 
ATOM 1957 O OG1 . THR A 1 270 ? 16.464 6.190   31.759 1.00 95.13  ? 269 THR A OG1 1 
ATOM 1958 C CG2 . THR A 1 270 ? 18.345 5.941   33.254 1.00 95.44  ? 269 THR A CG2 1 
ATOM 1959 N N   . ALA A 1 271 ? 14.581 8.834   32.816 1.00 125.21 ? 270 ALA A N   1 
ATOM 1960 C CA  . ALA A 1 271 ? 13.809 9.949   32.284 1.00 115.83 ? 270 ALA A CA  1 
ATOM 1961 C C   . ALA A 1 271 ? 13.970 11.203  33.131 1.00 111.08 ? 270 ALA A C   1 
ATOM 1962 O O   . ALA A 1 271 ? 13.717 12.307  32.638 1.00 115.57 ? 270 ALA A O   1 
ATOM 1963 C CB  . ALA A 1 271 ? 12.331 9.572   32.178 1.00 116.91 ? 270 ALA A CB  1 
ATOM 1964 N N   . SER A 1 272 ? 14.382 11.057  34.389 1.00 105.42 ? 271 SER A N   1 
ATOM 1965 C CA  . SER A 1 272 ? 14.735 12.182  35.244 1.00 110.26 ? 271 SER A CA  1 
ATOM 1966 C C   . SER A 1 272 ? 16.160 12.668  35.012 1.00 109.10 ? 271 SER A C   1 
ATOM 1967 O O   . SER A 1 272 ? 16.672 13.455  35.816 1.00 98.22  ? 271 SER A O   1 
ATOM 1968 C CB  . SER A 1 272 ? 14.549 11.800  36.716 1.00 97.11  ? 271 SER A CB  1 
ATOM 1969 O OG  . SER A 1 272 ? 14.920 12.866  37.573 1.00 103.21 ? 271 SER A OG  1 
ATOM 1970 N N   . PHE A 1 273 ? 16.804 12.217  33.936 1.00 114.57 ? 272 PHE A N   1 
ATOM 1971 C CA  . PHE A 1 273 ? 18.189 12.570  33.637 1.00 109.43 ? 272 PHE A CA  1 
ATOM 1972 C C   . PHE A 1 273 ? 18.272 13.450  32.395 1.00 104.78 ? 272 PHE A C   1 
ATOM 1973 O O   . PHE A 1 273 ? 18.562 14.643  32.503 1.00 103.29 ? 272 PHE A O   1 
ATOM 1974 C CB  . PHE A 1 273 ? 19.031 11.305  33.460 1.00 101.89 ? 272 PHE A CB  1 
ATOM 1975 C CG  . PHE A 1 273 ? 19.562 10.738  34.743 1.00 104.31 ? 272 PHE A CG  1 
ATOM 1976 C CD1 . PHE A 1 273 ? 20.630 11.334  35.388 1.00 102.99 ? 272 PHE A CD1 1 
ATOM 1977 C CD2 . PHE A 1 273 ? 19.003 9.599   35.297 1.00 98.18  ? 272 PHE A CD2 1 
ATOM 1978 C CE1 . PHE A 1 273 ? 21.123 10.811  36.563 1.00 92.07  ? 272 PHE A CE1 1 
ATOM 1979 C CE2 . PHE A 1 273 ? 19.494 9.071   36.472 1.00 92.38  ? 272 PHE A CE2 1 
ATOM 1980 C CZ  . PHE A 1 273 ? 20.558 9.677   37.105 1.00 86.64  ? 272 PHE A CZ  1 
ATOM 1981 N N   . SER A 1 274 ? 18.017 12.890  31.210 1.00 102.29 ? 273 SER A N   1 
ATOM 1982 C CA  . SER A 1 274 ? 18.274 13.616  29.970 1.00 107.01 ? 273 SER A CA  1 
ATOM 1983 C C   . SER A 1 274 ? 17.409 14.864  29.841 1.00 105.36 ? 273 SER A C   1 
ATOM 1984 O O   . SER A 1 274 ? 17.835 15.849  29.226 1.00 102.45 ? 273 SER A O   1 
ATOM 1985 C CB  . SER A 1 274 ? 18.051 12.693  28.772 1.00 109.80 ? 273 SER A CB  1 
ATOM 1986 O OG  . SER A 1 274 ? 16.864 11.935  28.929 1.00 122.15 ? 273 SER A OG  1 
ATOM 1987 N N   . VAL A 1 275 ? 16.204 14.853  30.412 1.00 106.80 ? 274 VAL A N   1 
ATOM 1988 C CA  . VAL A 1 275 ? 15.314 15.994  30.224 1.00 108.45 ? 274 VAL A CA  1 
ATOM 1989 C C   . VAL A 1 275 ? 15.600 17.104  31.234 1.00 108.35 ? 274 VAL A C   1 
ATOM 1990 O O   . VAL A 1 275 ? 15.427 18.287  30.920 1.00 110.14 ? 274 VAL A O   1 
ATOM 1991 C CB  . VAL A 1 275 ? 13.841 15.544  30.276 1.00 105.24 ? 274 VAL A CB  1 
ATOM 1992 C CG1 . VAL A 1 275 ? 13.632 14.305  29.415 1.00 99.75  ? 274 VAL A CG1 1 
ATOM 1993 C CG2 . VAL A 1 275 ? 13.386 15.295  31.708 1.00 109.96 ? 274 VAL A CG2 1 
ATOM 1994 N N   . TYR A 1 276 ? 16.052 16.764  32.440 1.00 101.28 ? 275 TYR A N   1 
ATOM 1995 C CA  . TYR A 1 276 ? 16.276 17.752  33.489 1.00 100.65 ? 275 TYR A CA  1 
ATOM 1996 C C   . TYR A 1 276 ? 17.742 17.962  33.826 1.00 94.94  ? 275 TYR A C   1 
ATOM 1997 O O   . TYR A 1 276 ? 18.167 19.104  34.018 1.00 91.74  ? 275 TYR A O   1 
ATOM 1998 C CB  . TYR A 1 276 ? 15.521 17.356  34.765 1.00 104.97 ? 275 TYR A CB  1 
ATOM 1999 C CG  . TYR A 1 276 ? 14.815 18.514  35.439 1.00 109.72 ? 275 TYR A CG  1 
ATOM 2000 C CD1 . TYR A 1 276 ? 13.641 18.317  36.156 1.00 113.45 ? 275 TYR A CD1 1 
ATOM 2001 C CD2 . TYR A 1 276 ? 15.321 19.805  35.356 1.00 109.66 ? 275 TYR A CD2 1 
ATOM 2002 C CE1 . TYR A 1 276 ? 12.992 19.374  36.773 1.00 117.93 ? 275 TYR A CE1 1 
ATOM 2003 C CE2 . TYR A 1 276 ? 14.680 20.868  35.969 1.00 111.81 ? 275 TYR A CE2 1 
ATOM 2004 C CZ  . TYR A 1 276 ? 13.516 20.647  36.676 1.00 114.42 ? 275 TYR A CZ  1 
ATOM 2005 O OH  . TYR A 1 276 ? 12.874 21.700  37.287 1.00 108.64 ? 275 TYR A OH  1 
ATOM 2006 N N   . LEU A 1 277 ? 18.529 16.890  33.905 1.00 92.95  ? 276 LEU A N   1 
ATOM 2007 C CA  . LEU A 1 277 ? 19.934 17.016  34.272 1.00 87.93  ? 276 LEU A CA  1 
ATOM 2008 C C   . LEU A 1 277 ? 20.745 17.621  33.132 1.00 93.23  ? 276 LEU A C   1 
ATOM 2009 O O   . LEU A 1 277 ? 21.232 18.749  33.254 1.00 87.85  ? 276 LEU A O   1 
ATOM 2010 C CB  . LEU A 1 277 ? 20.509 15.657  34.678 1.00 88.00  ? 276 LEU A CB  1 
ATOM 2011 C CG  . LEU A 1 277 ? 21.791 15.679  35.514 1.00 76.85  ? 276 LEU A CG  1 
ATOM 2012 C CD1 . LEU A 1 277 ? 21.494 15.973  36.976 1.00 69.39  ? 276 LEU A CD1 1 
ATOM 2013 C CD2 . LEU A 1 277 ? 22.569 14.379  35.361 1.00 83.98  ? 276 LEU A CD2 1 
ATOM 2014 N N   . LEU A 1 278 ? 20.878 16.886  32.021 1.00 97.44  ? 277 LEU A N   1 
ATOM 2015 C CA  . LEU A 1 278 ? 21.767 17.263  30.914 1.00 94.38  ? 277 LEU A CA  1 
ATOM 2016 C C   . LEU A 1 278 ? 21.691 18.731  30.505 1.00 92.50  ? 277 LEU A C   1 
ATOM 2017 O O   . LEU A 1 278 ? 22.753 19.350  30.354 1.00 89.70  ? 277 LEU A O   1 
ATOM 2018 C CB  . LEU A 1 278 ? 21.486 16.344  29.713 1.00 87.45  ? 277 LEU A CB  1 
ATOM 2019 C CG  . LEU A 1 278 ? 22.509 16.302  28.570 1.00 90.39  ? 277 LEU A CG  1 
ATOM 2020 C CD1 . LEU A 1 278 ? 22.246 17.382  27.519 1.00 88.85  ? 277 LEU A CD1 1 
ATOM 2021 C CD2 . LEU A 1 278 ? 23.930 16.407  29.105 1.00 86.54  ? 277 LEU A CD2 1 
ATOM 2022 N N   . PRO A 1 279 ? 20.518 19.346  30.310 1.00 93.45  ? 278 PRO A N   1 
ATOM 2023 C CA  . PRO A 1 279 ? 20.517 20.782  29.980 1.00 97.69  ? 278 PRO A CA  1 
ATOM 2024 C C   . PRO A 1 279 ? 21.070 21.656  31.092 1.00 96.86  ? 278 PRO A C   1 
ATOM 2025 O O   . PRO A 1 279 ? 21.564 22.756  30.813 1.00 92.40  ? 278 PRO A O   1 
ATOM 2026 C CB  . PRO A 1 279 ? 19.035 21.083  29.708 1.00 95.88  ? 278 PRO A CB  1 
ATOM 2027 C CG  . PRO A 1 279 ? 18.289 19.993  30.387 1.00 95.30  ? 278 PRO A CG  1 
ATOM 2028 C CD  . PRO A 1 279 ? 19.156 18.783  30.280 1.00 90.30  ? 278 PRO A CD  1 
ATOM 2029 N N   . THR A 1 280 ? 21.015 21.197  32.345 1.00 96.54  ? 279 THR A N   1 
ATOM 2030 C CA  . THR A 1 280 ? 21.481 22.021  33.456 1.00 94.73  ? 279 THR A CA  1 
ATOM 2031 C C   . THR A 1 280 ? 23.005 22.073  33.505 1.00 96.35  ? 279 THR A C   1 
ATOM 2032 O O   . THR A 1 280 ? 23.593 23.160  33.525 1.00 101.65 ? 279 THR A O   1 
ATOM 2033 C CB  . THR A 1 280 ? 20.914 21.499  34.779 1.00 87.04  ? 279 THR A CB  1 
ATOM 2034 O OG1 . THR A 1 280 ? 19.566 21.958  34.940 1.00 81.84  ? 279 THR A OG1 1 
ATOM 2035 C CG2 . THR A 1 280 ? 21.748 21.994  35.952 1.00 93.02  ? 279 THR A CG2 1 
ATOM 2036 N N   . LEU A 1 281 ? 23.667 20.907  33.516 1.00 96.06  ? 280 LEU A N   1 
ATOM 2037 C CA  . LEU A 1 281 ? 25.124 20.893  33.637 1.00 96.83  ? 280 LEU A CA  1 
ATOM 2038 C C   . LEU A 1 281 ? 25.793 21.633  32.488 1.00 99.58  ? 280 LEU A C   1 
ATOM 2039 O O   . LEU A 1 281 ? 26.885 22.185  32.662 1.00 99.26  ? 280 LEU A O   1 
ATOM 2040 C CB  . LEU A 1 281 ? 25.669 19.464  33.690 1.00 93.60  ? 280 LEU A CB  1 
ATOM 2041 C CG  . LEU A 1 281 ? 25.012 18.381  34.539 1.00 84.32  ? 280 LEU A CG  1 
ATOM 2042 C CD1 . LEU A 1 281 ? 24.103 17.566  33.657 1.00 83.22  ? 280 LEU A CD1 1 
ATOM 2043 C CD2 . LEU A 1 281 ? 26.064 17.493  35.184 1.00 86.19  ? 280 LEU A CD2 1 
ATOM 2044 N N   . SER A 1 282 ? 25.167 21.648  31.310 1.00 98.66  ? 281 SER A N   1 
ATOM 2045 C CA  . SER A 1 282 ? 25.769 22.333  30.171 1.00 102.76 ? 281 SER A CA  1 
ATOM 2046 C C   . SER A 1 282 ? 25.788 23.843  30.379 1.00 99.67  ? 281 SER A C   1 
ATOM 2047 O O   . SER A 1 282 ? 26.758 24.513  30.006 1.00 105.04 ? 281 SER A O   1 
ATOM 2048 C CB  . SER A 1 282 ? 25.021 21.977  28.888 1.00 105.33 ? 281 SER A CB  1 
ATOM 2049 O OG  . SER A 1 282 ? 23.700 22.490  28.910 1.00 108.04 ? 281 SER A OG  1 
ATOM 2050 N N   . ARG A 1 283 ? 24.731 24.395  30.978 1.00 101.40 ? 282 ARG A N   1 
ATOM 2051 C CA  . ARG A 1 283 ? 24.648 25.842  31.155 1.00 102.18 ? 282 ARG A CA  1 
ATOM 2052 C C   . ARG A 1 283 ? 25.652 26.331  32.195 1.00 107.59 ? 282 ARG A C   1 
ATOM 2053 O O   . ARG A 1 283 ? 26.498 27.186  31.905 1.00 115.70 ? 282 ARG A O   1 
ATOM 2054 C CB  . ARG A 1 283 ? 23.225 26.245  31.549 1.00 103.07 ? 282 ARG A CB  1 
ATOM 2055 C CG  . ARG A 1 283 ? 22.169 25.927  30.501 1.00 105.18 ? 282 ARG A CG  1 
ATOM 2056 C CD  . ARG A 1 283 ? 21.461 27.188  30.023 1.00 116.19 ? 282 ARG A CD  1 
ATOM 2057 N NE  . ARG A 1 283 ? 20.412 26.895  29.053 1.00 114.12 ? 282 ARG A NE  1 
ATOM 2058 C CZ  . ARG A 1 283 ? 20.040 27.713  28.077 1.00 110.04 ? 282 ARG A CZ  1 
ATOM 2059 N NH1 . ARG A 1 283 ? 20.618 28.892  27.904 1.00 101.12 ? 282 ARG A NH1 1 
ATOM 2060 N NH2 . ARG A 1 283 ? 19.063 27.341  27.255 1.00 100.03 ? 282 ARG A NH2 1 
ATOM 2061 N N   . LEU A 1 284 ? 25.571 25.803  33.416 1.00 104.86 ? 283 LEU A N   1 
ATOM 2062 C CA  . LEU A 1 284 ? 26.449 26.247  34.490 1.00 107.11 ? 283 LEU A CA  1 
ATOM 2063 C C   . LEU A 1 284 ? 27.909 25.918  34.176 1.00 105.39 ? 283 LEU A C   1 
ATOM 2064 O O   . LEU A 1 284 ? 28.223 24.994  33.419 1.00 99.85  ? 283 LEU A O   1 
ATOM 2065 C CB  . LEU A 1 284 ? 26.048 25.618  35.828 1.00 101.60 ? 283 LEU A CB  1 
ATOM 2066 C CG  . LEU A 1 284 ? 24.684 25.958  36.455 1.00 95.49  ? 283 LEU A CG  1 
ATOM 2067 C CD1 . LEU A 1 284 ? 24.457 27.468  36.508 1.00 97.30  ? 283 LEU A CD1 1 
ATOM 2068 C CD2 . LEU A 1 284 ? 23.515 25.249  35.775 1.00 84.36  ? 283 LEU A CD2 1 
ATOM 2069 N N   . THR A 1 285 ? 28.805 26.692  34.777 1.00 115.68 ? 284 THR A N   1 
ATOM 2070 C CA  . THR A 1 285 ? 30.235 26.615  34.493 1.00 110.94 ? 284 THR A CA  1 
ATOM 2071 C C   . THR A 1 285 ? 31.096 26.538  35.747 1.00 116.84 ? 284 THR A C   1 
ATOM 2072 O O   . THR A 1 285 ? 32.044 25.749  35.780 1.00 117.04 ? 284 THR A O   1 
ATOM 2073 C CB  . THR A 1 285 ? 30.656 27.830  33.638 1.00 115.79 ? 284 THR A CB  1 
ATOM 2074 O OG1 . THR A 1 285 ? 30.287 27.605  32.272 1.00 123.90 ? 284 THR A OG1 1 
ATOM 2075 C CG2 . THR A 1 285 ? 32.160 28.066  33.719 1.00 107.21 ? 284 THR A CG2 1 
ATOM 2076 N N   . GLU A 1 286 ? 30.787 27.326  36.776 1.00 121.34 ? 285 GLU A N   1 
ATOM 2077 C CA  . GLU A 1 286 ? 31.620 27.372  37.971 1.00 126.27 ? 285 GLU A CA  1 
ATOM 2078 C C   . GLU A 1 286 ? 31.682 26.006  38.650 1.00 123.78 ? 285 GLU A C   1 
ATOM 2079 O O   . GLU A 1 286 ? 30.726 25.226  38.620 1.00 118.54 ? 285 GLU A O   1 
ATOM 2080 C CB  . GLU A 1 286 ? 31.087 28.424  38.948 1.00 129.82 ? 285 GLU A CB  1 
ATOM 2081 C CG  . GLU A 1 286 ? 32.004 28.708  40.128 1.00 125.13 ? 285 GLU A CG  1 
ATOM 2082 C CD  . GLU A 1 286 ? 31.438 29.751  41.072 1.00 128.85 ? 285 GLU A CD  1 
ATOM 2083 O OE1 . GLU A 1 286 ? 30.345 30.283  40.787 1.00 136.20 ? 285 GLU A OE1 1 
ATOM 2084 O OE2 . GLU A 1 286 ? 32.085 30.035  42.101 1.00 127.55 ? 285 GLU A OE2 1 
ATOM 2085 N N   . LYS A 1 287 ? 32.835 25.723  39.263 1.00 118.01 ? 286 LYS A N   1 
ATOM 2086 C CA  . LYS A 1 287 ? 33.052 24.440  39.926 1.00 108.54 ? 286 LYS A CA  1 
ATOM 2087 C C   . LYS A 1 287 ? 32.039 24.214  41.042 1.00 113.93 ? 286 LYS A C   1 
ATOM 2088 O O   . LYS A 1 287 ? 31.355 23.184  41.081 1.00 106.89 ? 286 LYS A O   1 
ATOM 2089 C CB  . LYS A 1 287 ? 34.478 24.377  40.476 1.00 103.19 ? 286 LYS A CB  1 
ATOM 2090 C CG  . LYS A 1 287 ? 34.999 22.968  40.689 1.00 93.05  ? 286 LYS A CG  1 
ATOM 2091 C CD  . LYS A 1 287 ? 35.074 22.216  39.376 1.00 96.40  ? 286 LYS A CD  1 
ATOM 2092 C CE  . LYS A 1 287 ? 36.180 22.758  38.490 1.00 91.79  ? 286 LYS A CE  1 
ATOM 2093 N NZ  . LYS A 1 287 ? 37.439 21.978  38.638 1.00 92.14  ? 286 LYS A NZ  1 
ATOM 2094 N N   . ARG A 1 288 ? 31.938 25.173  41.969 1.00 122.92 ? 287 ARG A N   1 
ATOM 2095 C CA  . ARG A 1 288 ? 31.008 25.039  43.086 1.00 121.83 ? 287 ARG A CA  1 
ATOM 2096 C C   . ARG A 1 288 ? 29.579 24.827  42.606 1.00 121.75 ? 287 ARG A C   1 
ATOM 2097 O O   . ARG A 1 288 ? 28.804 24.116  43.256 1.00 112.86 ? 287 ARG A O   1 
ATOM 2098 C CB  . ARG A 1 288 ? 31.088 26.274  43.986 1.00 124.27 ? 287 ARG A CB  1 
ATOM 2099 C CG  . ARG A 1 288 ? 32.181 26.221  45.047 1.00 124.67 ? 287 ARG A CG  1 
ATOM 2100 C CD  . ARG A 1 288 ? 33.543 26.567  44.463 1.00 124.52 ? 287 ARG A CD  1 
ATOM 2101 N NE  . ARG A 1 288 ? 34.551 26.771  45.498 1.00 112.62 ? 287 ARG A NE  1 
ATOM 2102 C CZ  . ARG A 1 288 ? 34.881 27.953  46.000 1.00 118.43 ? 287 ARG A CZ  1 
ATOM 2103 N NH1 . ARG A 1 288 ? 34.302 29.067  45.584 1.00 120.47 ? 287 ARG A NH1 1 
ATOM 2104 N NH2 . ARG A 1 288 ? 35.816 28.018  46.944 1.00 123.24 ? 287 ARG A NH2 1 
ATOM 2105 N N   . ASP A 1 289 ? 29.213 25.428  41.471 1.00 135.46 ? 288 ASP A N   1 
ATOM 2106 C CA  . ASP A 1 289 ? 27.881 25.213  40.915 1.00 127.65 ? 288 ASP A CA  1 
ATOM 2107 C C   . ASP A 1 289 ? 27.740 23.805  40.350 1.00 120.63 ? 288 ASP A C   1 
ATOM 2108 O O   . ASP A 1 289 ? 26.670 23.195  40.450 1.00 121.94 ? 288 ASP A O   1 
ATOM 2109 C CB  . ASP A 1 289 ? 27.592 26.254  39.832 1.00 131.41 ? 288 ASP A CB  1 
ATOM 2110 C CG  . ASP A 1 289 ? 27.583 27.673  40.370 1.00 138.56 ? 288 ASP A CG  1 
ATOM 2111 O OD1 . ASP A 1 289 ? 27.787 27.852  41.590 1.00 131.75 ? 288 ASP A OD1 1 
ATOM 2112 O OD2 . ASP A 1 289 ? 27.377 28.610  39.570 1.00 140.83 ? 288 ASP A OD2 1 
ATOM 2113 N N   . ILE A 1 290 ? 28.809 23.274  39.752 1.00 112.79 ? 289 ILE A N   1 
ATOM 2114 C CA  . ILE A 1 290 ? 28.744 21.948  39.145 1.00 103.69 ? 289 ILE A CA  1 
ATOM 2115 C C   . ILE A 1 290 ? 28.653 20.868  40.217 1.00 94.93  ? 289 ILE A C   1 
ATOM 2116 O O   . ILE A 1 290 ? 27.856 19.929  40.106 1.00 87.46  ? 289 ILE A O   1 
ATOM 2117 C CB  . ILE A 1 290 ? 29.953 21.728  38.218 1.00 98.42  ? 289 ILE A CB  1 
ATOM 2118 C CG1 . ILE A 1 290 ? 29.845 22.618  36.976 1.00 98.30  ? 289 ILE A CG1 1 
ATOM 2119 C CG2 . ILE A 1 290 ? 30.069 20.265  37.823 1.00 86.80  ? 289 ILE A CG2 1 
ATOM 2120 C CD1 . ILE A 1 290 ? 28.494 22.565  36.296 1.00 95.47  ? 289 ILE A CD1 1 
ATOM 2121 N N   . THR A 1 291 ? 29.466 20.983  41.271 1.00 98.46  ? 290 THR A N   1 
ATOM 2122 C CA  . THR A 1 291 ? 29.445 19.988  42.340 1.00 88.08  ? 290 THR A CA  1 
ATOM 2123 C C   . THR A 1 291 ? 28.086 19.945  43.029 1.00 90.07  ? 290 THR A C   1 
ATOM 2124 O O   . THR A 1 291 ? 27.607 18.869  43.406 1.00 89.51  ? 290 THR A O   1 
ATOM 2125 C CB  . THR A 1 291 ? 30.556 20.283  43.352 1.00 89.74  ? 290 THR A CB  1 
ATOM 2126 O OG1 . THR A 1 291 ? 31.826 20.270  42.688 1.00 92.88  ? 290 THR A OG1 1 
ATOM 2127 C CG2 . THR A 1 291 ? 30.566 19.245  44.469 1.00 71.17  ? 290 THR A CG2 1 
ATOM 2128 N N   . ARG A 1 292 ? 27.441 21.104  43.188 1.00 94.58  ? 291 ARG A N   1 
ATOM 2129 C CA  . ARG A 1 292 ? 26.136 21.140  43.841 1.00 90.86  ? 291 ARG A CA  1 
ATOM 2130 C C   . ARG A 1 292 ? 25.088 20.378  43.036 1.00 88.46  ? 291 ARG A C   1 
ATOM 2131 O O   . ARG A 1 292 ? 24.200 19.738  43.612 1.00 79.93  ? 291 ARG A O   1 
ATOM 2132 C CB  . ARG A 1 292 ? 25.695 22.589  44.057 1.00 82.05  ? 291 ARG A CB  1 
ATOM 2133 C CG  . ARG A 1 292 ? 26.419 23.307  45.186 1.00 79.47  ? 291 ARG A CG  1 
ATOM 2134 C CD  . ARG A 1 292 ? 25.576 24.443  45.749 1.00 94.29  ? 291 ARG A CD  1 
ATOM 2135 N NE  . ARG A 1 292 ? 26.323 25.278  46.683 1.00 103.26 ? 291 ARG A NE  1 
ATOM 2136 C CZ  . ARG A 1 292 ? 26.429 25.044  47.984 1.00 89.74  ? 291 ARG A CZ  1 
ATOM 2137 N NH1 . ARG A 1 292 ? 25.854 23.994  48.548 1.00 69.16  ? 291 ARG A NH1 1 
ATOM 2138 N NH2 . ARG A 1 292 ? 27.130 25.886  48.740 1.00 72.79  ? 291 ARG A NH2 1 
ATOM 2139 N N   . GLU A 1 293 ? 25.175 20.432  41.705 1.00 87.35  ? 292 GLU A N   1 
ATOM 2140 C CA  . GLU A 1 293 ? 24.186 19.754  40.872 1.00 86.70  ? 292 GLU A CA  1 
ATOM 2141 C C   . GLU A 1 293 ? 24.445 18.256  40.779 1.00 85.35  ? 292 GLU A C   1 
ATOM 2142 O O   . GLU A 1 293 ? 23.502 17.479  40.594 1.00 78.49  ? 292 GLU A O   1 
ATOM 2143 C CB  . GLU A 1 293 ? 24.157 20.373  39.474 1.00 90.52  ? 292 GLU A CB  1 
ATOM 2144 C CG  . GLU A 1 293 ? 23.132 21.488  39.318 1.00 98.40  ? 292 GLU A CG  1 
ATOM 2145 C CD  . GLU A 1 293 ? 21.701 20.978  39.340 1.00 102.72 ? 292 GLU A CD  1 
ATOM 2146 O OE1 . GLU A 1 293 ? 21.486 19.782  39.046 1.00 107.11 ? 292 GLU A OE1 1 
ATOM 2147 O OE2 . GLU A 1 293 ? 20.790 21.773  39.654 1.00 104.16 ? 292 GLU A OE2 1 
ATOM 2148 N N   . VAL A 1 294 ? 25.703 17.833  40.900 1.00 86.98  ? 293 VAL A N   1 
ATOM 2149 C CA  . VAL A 1 294 ? 25.995 16.404  40.915 1.00 78.67  ? 293 VAL A CA  1 
ATOM 2150 C C   . VAL A 1 294 ? 25.540 15.785  42.225 1.00 80.34  ? 293 VAL A C   1 
ATOM 2151 O O   . VAL A 1 294 ? 24.988 14.677  42.250 1.00 75.90  ? 293 VAL A O   1 
ATOM 2152 C CB  . VAL A 1 294 ? 27.494 16.166  40.665 1.00 74.84  ? 293 VAL A CB  1 
ATOM 2153 C CG1 . VAL A 1 294 ? 27.969 14.902  41.371 1.00 71.55  ? 293 VAL A CG1 1 
ATOM 2154 C CG2 . VAL A 1 294 ? 27.740 16.051  39.191 1.00 81.64  ? 293 VAL A CG2 1 
ATOM 2155 N N   . VAL A 1 295 ? 25.743 16.498  43.331 1.00 78.31  ? 294 VAL A N   1 
ATOM 2156 C CA  . VAL A 1 295 ? 25.391 15.958  44.636 1.00 71.25  ? 294 VAL A CA  1 
ATOM 2157 C C   . VAL A 1 295 ? 23.878 15.853  44.784 1.00 75.65  ? 294 VAL A C   1 
ATOM 2158 O O   . VAL A 1 295 ? 23.363 14.864  45.318 1.00 78.50  ? 294 VAL A O   1 
ATOM 2159 C CB  . VAL A 1 295 ? 26.024 16.821  45.742 1.00 74.16  ? 294 VAL A CB  1 
ATOM 2160 C CG1 . VAL A 1 295 ? 25.456 16.453  47.096 1.00 78.43  ? 294 VAL A CG1 1 
ATOM 2161 C CG2 . VAL A 1 295 ? 27.539 16.658  45.727 1.00 72.95  ? 294 VAL A CG2 1 
ATOM 2162 N N   . LYS A 1 296 ? 23.138 16.850  44.292 1.00 74.77  ? 295 LYS A N   1 
ATOM 2163 C CA  . LYS A 1 296 ? 21.688 16.828  44.460 1.00 73.92  ? 295 LYS A CA  1 
ATOM 2164 C C   . LYS A 1 296 ? 21.036 15.740  43.616 1.00 76.79  ? 295 LYS A C   1 
ATOM 2165 O O   . LYS A 1 296 ? 20.027 15.161  44.034 1.00 79.58  ? 295 LYS A O   1 
ATOM 2166 C CB  . LYS A 1 296 ? 21.086 18.193  44.124 1.00 81.18  ? 295 LYS A CB  1 
ATOM 2167 C CG  . LYS A 1 296 ? 21.286 18.637  42.685 1.00 87.92  ? 295 LYS A CG  1 
ATOM 2168 C CD  . LYS A 1 296 ? 20.248 19.670  42.267 1.00 93.29  ? 295 LYS A CD  1 
ATOM 2169 C CE  . LYS A 1 296 ? 18.847 19.273  42.711 1.00 94.51  ? 295 LYS A CE  1 
ATOM 2170 N NZ  . LYS A 1 296 ? 17.796 19.936  41.887 1.00 95.75  ? 295 LYS A NZ  1 
ATOM 2171 N N   . SER A 1 297 ? 21.587 15.449  42.434 1.00 77.58  ? 296 SER A N   1 
ATOM 2172 C CA  . SER A 1 297 ? 21.050 14.359  41.625 1.00 80.51  ? 296 SER A CA  1 
ATOM 2173 C C   . SER A 1 297 ? 21.312 13.011  42.284 1.00 71.13  ? 296 SER A C   1 
ATOM 2174 O O   . SER A 1 297 ? 20.452 12.123  42.260 1.00 67.12  ? 296 SER A O   1 
ATOM 2175 C CB  . SER A 1 297 ? 21.647 14.396  40.218 1.00 76.67  ? 296 SER A CB  1 
ATOM 2176 O OG  . SER A 1 297 ? 23.051 14.204  40.245 1.00 78.12  ? 296 SER A OG  1 
ATOM 2177 N N   . LEU A 1 298 ? 22.496 12.843  42.876 1.00 70.27  ? 297 LEU A N   1 
ATOM 2178 C CA  . LEU A 1 298 ? 22.800 11.616  43.606 1.00 72.27  ? 297 LEU A CA  1 
ATOM 2179 C C   . LEU A 1 298 ? 21.872 11.433  44.800 1.00 72.59  ? 297 LEU A C   1 
ATOM 2180 O O   . LEU A 1 298 ? 21.418 10.316  45.077 1.00 70.44  ? 297 LEU A O   1 
ATOM 2181 C CB  . LEU A 1 298 ? 24.263 11.630  44.045 1.00 68.31  ? 297 LEU A CB  1 
ATOM 2182 C CG  . LEU A 1 298 ? 25.225 11.412  42.878 1.00 73.70  ? 297 LEU A CG  1 
ATOM 2183 C CD1 . LEU A 1 298 ? 26.655 11.286  43.362 1.00 78.95  ? 297 LEU A CD1 1 
ATOM 2184 C CD2 . LEU A 1 298 ? 24.800 10.154  42.136 1.00 65.66  ? 297 LEU A CD2 1 
ATOM 2185 N N   . LYS A 1 299 ? 21.565 12.519  45.511 1.00 73.09  ? 298 LYS A N   1 
ATOM 2186 C CA  . LYS A 1 299 ? 20.638 12.452  46.635 1.00 77.83  ? 298 LYS A CA  1 
ATOM 2187 C C   . LYS A 1 299 ? 19.219 12.103  46.205 1.00 69.55  ? 298 LYS A C   1 
ATOM 2188 O O   . LYS A 1 299 ? 18.380 11.821  47.068 1.00 58.48  ? 298 LYS A O   1 
ATOM 2189 C CB  . LYS A 1 299 ? 20.645 13.783  47.390 1.00 81.66  ? 298 LYS A CB  1 
ATOM 2190 C CG  . LYS A 1 299 ? 21.968 14.086  48.085 1.00 73.00  ? 298 LYS A CG  1 
ATOM 2191 C CD  . LYS A 1 299 ? 22.092 15.554  48.482 1.00 72.45  ? 298 LYS A CD  1 
ATOM 2192 C CE  . LYS A 1 299 ? 20.737 16.190  48.758 1.00 74.46  ? 298 LYS A CE  1 
ATOM 2193 N NZ  . LYS A 1 299 ? 20.837 17.670  48.894 1.00 73.05  ? 298 LYS A NZ  1 
ATOM 2194 N N   . PHE A 1 300 ? 18.930 12.119  44.904 1.00 79.57  ? 299 PHE A N   1 
ATOM 2195 C CA  . PHE A 1 300 ? 17.638 11.706  44.372 1.00 86.34  ? 299 PHE A CA  1 
ATOM 2196 C C   . PHE A 1 300 ? 17.691 10.318  43.744 1.00 87.36  ? 299 PHE A C   1 
ATOM 2197 O O   . PHE A 1 300 ? 16.903 9.443   44.112 1.00 90.95  ? 299 PHE A O   1 
ATOM 2198 C CB  . PHE A 1 300 ? 17.138 12.730  43.340 1.00 87.24  ? 299 PHE A CB  1 
ATOM 2199 C CG  . PHE A 1 300 ? 15.746 12.451  42.819 1.00 94.00  ? 299 PHE A CG  1 
ATOM 2200 C CD1 . PHE A 1 300 ? 15.524 11.491  41.839 1.00 90.64  ? 299 PHE A CD1 1 
ATOM 2201 C CD2 . PHE A 1 300 ? 14.660 13.156  43.312 1.00 96.46  ? 299 PHE A CD2 1 
ATOM 2202 C CE1 . PHE A 1 300 ? 14.247 11.236  41.370 1.00 86.47  ? 299 PHE A CE1 1 
ATOM 2203 C CE2 . PHE A 1 300 ? 13.382 12.907  42.845 1.00 104.52 ? 299 PHE A CE2 1 
ATOM 2204 C CZ  . PHE A 1 300 ? 13.176 11.946  41.873 1.00 107.17 ? 299 PHE A CZ  1 
ATOM 2205 N N   . VAL A 1 301 ? 18.611 10.097  42.804 1.00 73.38  ? 300 VAL A N   1 
ATOM 2206 C CA  . VAL A 1 301 ? 18.558 8.873   42.013 1.00 81.18  ? 300 VAL A CA  1 
ATOM 2207 C C   . VAL A 1 301 ? 19.078 7.670   42.796 1.00 73.94  ? 300 VAL A C   1 
ATOM 2208 O O   . VAL A 1 301 ? 18.594 6.551   42.599 1.00 73.79  ? 300 VAL A O   1 
ATOM 2209 C CB  . VAL A 1 301 ? 19.313 9.059   40.685 1.00 69.53  ? 300 VAL A CB  1 
ATOM 2210 C CG1 . VAL A 1 301 ? 18.729 10.236  39.920 1.00 82.72  ? 300 VAL A CG1 1 
ATOM 2211 C CG2 . VAL A 1 301 ? 20.806 9.250   40.921 1.00 66.94  ? 300 VAL A CG2 1 
ATOM 2212 N N   . LEU A 1 302 ? 20.048 7.864   43.693 1.00 69.04  ? 301 LEU A N   1 
ATOM 2213 C CA  . LEU A 1 302 ? 20.560 6.732   44.464 1.00 61.75  ? 301 LEU A CA  1 
ATOM 2214 C C   . LEU A 1 302 ? 19.509 6.136   45.393 1.00 63.68  ? 301 LEU A C   1 
ATOM 2215 O O   . LEU A 1 302 ? 19.351 4.902   45.395 1.00 69.05  ? 301 LEU A O   1 
ATOM 2216 C CB  . LEU A 1 302 ? 21.825 7.143   45.228 1.00 60.88  ? 301 LEU A CB  1 
ATOM 2217 C CG  . LEU A 1 302 ? 23.147 7.001   44.470 1.00 65.69  ? 301 LEU A CG  1 
ATOM 2218 C CD1 . LEU A 1 302 ? 24.326 7.335   45.372 1.00 51.02  ? 301 LEU A CD1 1 
ATOM 2219 C CD2 . LEU A 1 302 ? 23.286 5.601   43.896 1.00 57.18  ? 301 LEU A CD2 1 
ATOM 2220 N N   . PRO A 1 303 ? 18.763 6.913   46.190 1.00 63.98  ? 302 PRO A N   1 
ATOM 2221 C CA  . PRO A 1 303 ? 17.655 6.307   46.949 1.00 64.29  ? 302 PRO A CA  1 
ATOM 2222 C C   . PRO A 1 303 ? 16.496 5.863   46.076 1.00 65.76  ? 302 PRO A C   1 
ATOM 2223 O O   . PRO A 1 303 ? 15.746 4.968   46.482 1.00 60.83  ? 302 PRO A O   1 
ATOM 2224 C CB  . PRO A 1 303 ? 17.226 7.425   47.907 1.00 61.72  ? 302 PRO A CB  1 
ATOM 2225 C CG  . PRO A 1 303 ? 17.667 8.676   47.252 1.00 59.69  ? 302 PRO A CG  1 
ATOM 2226 C CD  . PRO A 1 303 ? 18.920 8.345   46.509 1.00 65.63  ? 302 PRO A CD  1 
ATOM 2227 N N   . ALA A 1 304 ? 16.321 6.461   44.895 1.00 65.28  ? 303 ALA A N   1 
ATOM 2228 C CA  . ALA A 1 304 ? 15.220 6.067   44.023 1.00 70.22  ? 303 ALA A CA  1 
ATOM 2229 C C   . ALA A 1 304 ? 15.462 4.693   43.411 1.00 73.48  ? 303 ALA A C   1 
ATOM 2230 O O   . ALA A 1 304 ? 14.553 3.855   43.378 1.00 70.85  ? 303 ALA A O   1 
ATOM 2231 C CB  . ALA A 1 304 ? 15.013 7.111   42.928 1.00 58.18  ? 303 ALA A CB  1 
ATOM 2232 N N   . VAL A 1 305 ? 16.678 4.440   42.921 1.00 76.34  ? 304 VAL A N   1 
ATOM 2233 C CA  . VAL A 1 305 ? 16.975 3.133   42.344 1.00 70.79  ? 304 VAL A CA  1 
ATOM 2234 C C   . VAL A 1 305 ? 17.100 2.081   43.440 1.00 70.24  ? 304 VAL A C   1 
ATOM 2235 O O   . VAL A 1 305 ? 16.802 0.902   43.215 1.00 70.14  ? 304 VAL A O   1 
ATOM 2236 C CB  . VAL A 1 305 ? 18.242 3.207   41.468 1.00 69.10  ? 304 VAL A CB  1 
ATOM 2237 C CG1 . VAL A 1 305 ? 19.460 3.567   42.303 1.00 74.02  ? 304 VAL A CG1 1 
ATOM 2238 C CG2 . VAL A 1 305 ? 18.466 1.897   40.720 1.00 72.32  ? 304 VAL A CG2 1 
ATOM 2239 N N   . ALA A 1 306 ? 17.521 2.482   44.644 1.00 70.04  ? 305 ALA A N   1 
ATOM 2240 C CA  . ALA A 1 306 ? 17.646 1.522   45.737 1.00 56.29  ? 305 ALA A CA  1 
ATOM 2241 C C   . ALA A 1 306 ? 16.280 1.052   46.219 1.00 48.87  ? 305 ALA A C   1 
ATOM 2242 O O   . ALA A 1 306 ? 16.101 -0.129  46.539 1.00 53.71  ? 305 ALA A O   1 
ATOM 2243 C CB  . ALA A 1 306 ? 18.441 2.135   46.889 1.00 48.69  ? 305 ALA A CB  1 
ATOM 2244 N N   . ALA A 1 307 ? 15.304 1.961   46.279 1.00 49.12  ? 306 ALA A N   1 
ATOM 2245 C CA  . ALA A 1 307 ? 13.959 1.570   46.688 1.00 55.22  ? 306 ALA A CA  1 
ATOM 2246 C C   . ALA A 1 307 ? 13.311 0.659   45.653 1.00 62.57  ? 306 ALA A C   1 
ATOM 2247 O O   . ALA A 1 307 ? 12.682 -0.345  46.008 1.00 58.38  ? 306 ALA A O   1 
ATOM 2248 C CB  . ALA A 1 307 ? 13.099 2.810   46.930 1.00 57.31  ? 306 ALA A CB  1 
ATOM 2249 N N   . ALA A 1 308 ? 13.458 0.988   44.368 1.00 59.97  ? 307 ALA A N   1 
ATOM 2250 C CA  . ALA A 1 308 ? 12.909 0.133   43.320 1.00 60.74  ? 307 ALA A CA  1 
ATOM 2251 C C   . ALA A 1 308 ? 13.598 -1.225  43.299 1.00 65.60  ? 307 ALA A C   1 
ATOM 2252 O O   . ALA A 1 308 ? 12.933 -2.262  43.194 1.00 63.73  ? 307 ALA A O   1 
ATOM 2253 C CB  . ALA A 1 308 ? 13.029 0.819   41.962 1.00 48.96  ? 307 ALA A CB  1 
ATOM 2254 N N   . SER A 1 309 ? 14.930 -1.241  43.404 1.00 67.10  ? 308 SER A N   1 
ATOM 2255 C CA  . SER A 1 309 ? 15.656 -2.508  43.412 1.00 56.17  ? 308 SER A CA  1 
ATOM 2256 C C   . SER A 1 309 ? 15.216 -3.381  44.579 1.00 53.29  ? 308 SER A C   1 
ATOM 2257 O O   . SER A 1 309 ? 14.818 -4.535  44.391 1.00 64.01  ? 308 SER A O   1 
ATOM 2258 C CB  . SER A 1 309 ? 17.163 -2.254  43.472 1.00 51.33  ? 308 SER A CB  1 
ATOM 2259 O OG  . SER A 1 309 ? 17.616 -1.577  42.313 1.00 59.98  ? 308 SER A OG  1 
ATOM 2260 N N   . PHE A 1 310 ? 15.262 -2.834  45.797 1.00 51.96  ? 309 PHE A N   1 
ATOM 2261 C CA  . PHE A 1 310 ? 14.866 -3.605  46.970 1.00 57.60  ? 309 PHE A CA  1 
ATOM 2262 C C   . PHE A 1 310 ? 13.441 -4.130  46.849 1.00 56.16  ? 309 PHE A C   1 
ATOM 2263 O O   . PHE A 1 310 ? 13.125 -5.194  47.393 1.00 63.27  ? 309 PHE A O   1 
ATOM 2264 C CB  . PHE A 1 310 ? 15.010 -2.752  48.232 1.00 56.71  ? 309 PHE A CB  1 
ATOM 2265 C CG  . PHE A 1 310 ? 15.042 -3.552  49.501 1.00 52.66  ? 309 PHE A CG  1 
ATOM 2266 C CD1 . PHE A 1 310 ? 16.235 -4.069  49.980 1.00 48.06  ? 309 PHE A CD1 1 
ATOM 2267 C CD2 . PHE A 1 310 ? 13.879 -3.794  50.212 1.00 48.23  ? 309 PHE A CD2 1 
ATOM 2268 C CE1 . PHE A 1 310 ? 16.267 -4.807  51.147 1.00 49.03  ? 309 PHE A CE1 1 
ATOM 2269 C CE2 . PHE A 1 310 ? 13.904 -4.531  51.377 1.00 48.75  ? 309 PHE A CE2 1 
ATOM 2270 C CZ  . PHE A 1 310 ? 15.099 -5.038  51.846 1.00 54.04  ? 309 PHE A CZ  1 
ATOM 2271 N N   . THR A 1 311 ? 12.572 -3.410  46.136 1.00 54.90  ? 310 THR A N   1 
ATOM 2272 C CA  . THR A 1 311 ? 11.187 -3.850  46.012 1.00 54.84  ? 310 THR A CA  1 
ATOM 2273 C C   . THR A 1 311 ? 11.057 -5.018  45.040 1.00 62.15  ? 310 THR A C   1 
ATOM 2274 O O   . THR A 1 311 ? 10.263 -5.937  45.274 1.00 62.40  ? 310 THR A O   1 
ATOM 2275 C CB  . THR A 1 311 ? 10.301 -2.685  45.575 1.00 55.65  ? 310 THR A CB  1 
ATOM 2276 O OG1 . THR A 1 311 ? 10.607 -1.535  46.373 1.00 66.29  ? 310 THR A OG1 1 
ATOM 2277 C CG2 . THR A 1 311 ? 8.830  -3.040  45.755 1.00 46.02  ? 310 THR A CG2 1 
ATOM 2278 N N   . VAL A 1 312 ? 11.820 -5.006  43.943 1.00 56.35  ? 311 VAL A N   1 
ATOM 2279 C CA  . VAL A 1 312 ? 11.767 -6.148  43.037 1.00 65.42  ? 311 VAL A CA  1 
ATOM 2280 C C   . VAL A 1 312 ? 12.498 -7.340  43.642 1.00 67.28  ? 311 VAL A C   1 
ATOM 2281 O O   . VAL A 1 312 ? 12.188 -8.493  43.318 1.00 68.70  ? 311 VAL A O   1 
ATOM 2282 C CB  . VAL A 1 312 ? 12.317 -5.782  41.642 1.00 62.14  ? 311 VAL A CB  1 
ATOM 2283 C CG1 . VAL A 1 312 ? 11.797 -4.422  41.195 1.00 61.90  ? 311 VAL A CG1 1 
ATOM 2284 C CG2 . VAL A 1 312 ? 13.833 -5.819  41.620 1.00 57.40  ? 311 VAL A CG2 1 
ATOM 2285 N N   . TRP A 1 313 ? 13.462 -7.096  44.534 1.00 61.37  ? 312 TRP A N   1 
ATOM 2286 C CA  . TRP A 1 313 ? 14.056 -8.198  45.284 1.00 62.16  ? 312 TRP A CA  1 
ATOM 2287 C C   . TRP A 1 313 ? 13.051 -8.788  46.263 1.00 59.81  ? 312 TRP A C   1 
ATOM 2288 O O   . TRP A 1 313 ? 13.040 -10.001 46.498 1.00 60.24  ? 312 TRP A O   1 
ATOM 2289 C CB  . TRP A 1 313 ? 15.309 -7.729  46.024 1.00 61.03  ? 312 TRP A CB  1 
ATOM 2290 C CG  . TRP A 1 313 ? 15.940 -8.801  46.876 1.00 60.38  ? 312 TRP A CG  1 
ATOM 2291 C CD1 . TRP A 1 313 ? 16.956 -9.639  46.518 1.00 59.55  ? 312 TRP A CD1 1 
ATOM 2292 C CD2 . TRP A 1 313 ? 15.592 -9.149  48.224 1.00 70.38  ? 312 TRP A CD2 1 
ATOM 2293 N NE1 . TRP A 1 313 ? 17.262 -10.485 47.557 1.00 61.30  ? 312 TRP A NE1 1 
ATOM 2294 C CE2 . TRP A 1 313 ? 16.439 -10.205 48.615 1.00 67.55  ? 312 TRP A CE2 1 
ATOM 2295 C CE3 . TRP A 1 313 ? 14.646 -8.670  49.138 1.00 64.89  ? 312 TRP A CE3 1 
ATOM 2296 C CZ2 . TRP A 1 313 ? 16.370 -10.790 49.879 1.00 66.52  ? 312 TRP A CZ2 1 
ATOM 2297 C CZ3 . TRP A 1 313 ? 14.579 -9.253  50.390 1.00 64.00  ? 312 TRP A CZ3 1 
ATOM 2298 C CH2 . TRP A 1 313 ? 15.435 -10.301 50.750 1.00 61.38  ? 312 TRP A CH2 1 
ATOM 2299 N N   . LEU A 1 314 ? 12.201 -7.942  46.847 1.00 62.25  ? 313 LEU A N   1 
ATOM 2300 C CA  . LEU A 1 314 ? 11.206 -8.433  47.793 1.00 72.52  ? 313 LEU A CA  1 
ATOM 2301 C C   . LEU A 1 314 ? 10.172 -9.321  47.112 1.00 71.55  ? 313 LEU A C   1 
ATOM 2302 O O   . LEU A 1 314 ? 9.622  -10.229 47.748 1.00 79.80  ? 313 LEU A O   1 
ATOM 2303 C CB  . LEU A 1 314 ? 10.527 -7.253  48.489 1.00 56.44  ? 313 LEU A CB  1 
ATOM 2304 C CG  . LEU A 1 314 ? 10.781 -7.140  49.991 1.00 59.90  ? 313 LEU A CG  1 
ATOM 2305 C CD1 . LEU A 1 314 ? 10.158 -5.868  50.549 1.00 61.47  ? 313 LEU A CD1 1 
ATOM 2306 C CD2 . LEU A 1 314 ? 10.247 -8.369  50.711 1.00 51.25  ? 313 LEU A CD2 1 
ATOM 2307 N N   . LEU A 1 315 ? 9.903  -9.085  45.830 1.00 59.57  ? 314 LEU A N   1 
ATOM 2308 C CA  . LEU A 1 315 ? 8.929  -9.851  45.063 1.00 68.65  ? 314 LEU A CA  1 
ATOM 2309 C C   . LEU A 1 315 ? 9.600  -10.559 43.891 1.00 69.48  ? 314 LEU A C   1 
ATOM 2310 O O   . LEU A 1 315 ? 9.021  -10.695 42.809 1.00 63.41  ? 314 LEU A O   1 
ATOM 2311 C CB  . LEU A 1 315 ? 7.796  -8.951  44.571 1.00 62.56  ? 314 LEU A CB  1 
ATOM 2312 C CG  . LEU A 1 315 ? 7.042  -8.152  45.637 1.00 56.78  ? 314 LEU A CG  1 
ATOM 2313 C CD1 . LEU A 1 315 ? 5.894  -7.364  45.021 1.00 62.54  ? 314 LEU A CD1 1 
ATOM 2314 C CD2 . LEU A 1 315 ? 6.534  -9.070  46.735 1.00 67.51  ? 314 LEU A CD2 1 
ATOM 2315 N N   . ARG A 1 316 ? 10.838 -11.019 44.101 1.00 73.83  ? 315 ARG A N   1 
ATOM 2316 C CA  . ARG A 1 316 ? 11.577 -11.681 43.030 1.00 64.08  ? 315 ARG A CA  1 
ATOM 2317 C C   . ARG A 1 316 ? 10.847 -12.925 42.541 1.00 61.46  ? 315 ARG A C   1 
ATOM 2318 O O   . ARG A 1 316 ? 10.854 -13.225 41.341 1.00 59.10  ? 315 ARG A O   1 
ATOM 2319 C CB  . ARG A 1 316 ? 12.990 -12.032 43.499 1.00 63.07  ? 315 ARG A CB  1 
ATOM 2320 C CG  . ARG A 1 316 ? 13.060 -12.810 44.806 1.00 65.59  ? 315 ARG A CG  1 
ATOM 2321 C CD  . ARG A 1 316 ? 14.421 -12.645 45.465 1.00 62.65  ? 315 ARG A CD  1 
ATOM 2322 N NE  . ARG A 1 316 ? 14.878 -13.873 46.104 1.00 71.81  ? 315 ARG A NE  1 
ATOM 2323 C CZ  . ARG A 1 316 ? 14.919 -14.062 47.416 1.00 72.84  ? 315 ARG A CZ  1 
ATOM 2324 N NH1 . ARG A 1 316 ? 14.524 -13.124 48.262 1.00 74.07  ? 315 ARG A NH1 1 
ATOM 2325 N NH2 . ARG A 1 316 ? 15.366 -15.221 47.890 1.00 75.25  ? 315 ARG A NH2 1 
ATOM 2326 N N   . ASP A 1 317 ? 10.205 -13.659 43.452 1.00 65.25  ? 316 ASP A N   1 
ATOM 2327 C CA  . ASP A 1 317 ? 9.376  -14.782 43.030 1.00 59.30  ? 316 ASP A CA  1 
ATOM 2328 C C   . ASP A 1 317 ? 8.213  -14.304 42.173 1.00 57.71  ? 316 ASP A C   1 
ATOM 2329 O O   . ASP A 1 317 ? 7.906  -14.903 41.136 1.00 72.73  ? 316 ASP A O   1 
ATOM 2330 C CB  . ASP A 1 317 ? 8.863  -15.548 44.249 1.00 53.97  ? 316 ASP A CB  1 
ATOM 2331 C CG  . ASP A 1 317 ? 9.956  -16.329 44.947 1.00 61.34  ? 316 ASP A CG  1 
ATOM 2332 O OD1 . ASP A 1 317 ? 11.074 -16.411 44.396 1.00 52.93  ? 316 ASP A OD1 1 
ATOM 2333 O OD2 . ASP A 1 317 ? 9.699  -16.860 46.049 1.00 65.59  ? 316 ASP A OD2 1 
ATOM 2334 N N   . PHE A 1 318 ? 7.559  -13.216 42.585 1.00 56.23  ? 317 PHE A N   1 
ATOM 2335 C CA  . PHE A 1 318 ? 6.463  -12.677 41.792 1.00 56.10  ? 317 PHE A CA  1 
ATOM 2336 C C   . PHE A 1 318 ? 6.962  -12.036 40.505 1.00 59.57  ? 317 PHE A C   1 
ATOM 2337 O O   . PHE A 1 318 ? 6.274  -12.097 39.480 1.00 52.75  ? 317 PHE A O   1 
ATOM 2338 C CB  . PHE A 1 318 ? 5.666  -11.664 42.611 1.00 45.48  ? 317 PHE A CB  1 
ATOM 2339 C CG  . PHE A 1 318 ? 4.315  -11.356 42.038 1.00 45.90  ? 317 PHE A CG  1 
ATOM 2340 C CD1 . PHE A 1 318 ? 3.310  -12.309 42.051 1.00 57.16  ? 317 PHE A CD1 1 
ATOM 2341 C CD2 . PHE A 1 318 ? 4.052  -10.118 41.479 1.00 59.15  ? 317 PHE A CD2 1 
ATOM 2342 C CE1 . PHE A 1 318 ? 2.065  -12.029 41.522 1.00 61.01  ? 317 PHE A CE1 1 
ATOM 2343 C CE2 . PHE A 1 318 ? 2.810  -9.831  40.949 1.00 58.12  ? 317 PHE A CE2 1 
ATOM 2344 C CZ  . PHE A 1 318 ? 1.815  -10.788 40.970 1.00 60.20  ? 317 PHE A CZ  1 
ATOM 2345 N N   . ALA A 1 319 ? 8.147  -11.423 40.535 1.00 57.92  ? 318 ALA A N   1 
ATOM 2346 C CA  . ALA A 1 319 ? 8.672  -10.760 39.345 1.00 55.28  ? 318 ALA A CA  1 
ATOM 2347 C C   . ALA A 1 319 ? 8.955  -11.764 38.235 1.00 57.49  ? 318 ALA A C   1 
ATOM 2348 O O   . ALA A 1 319 ? 8.586  -11.544 37.075 1.00 51.10  ? 318 ALA A O   1 
ATOM 2349 C CB  . ALA A 1 319 ? 9.936  -9.974  39.697 1.00 53.50  ? 318 ALA A CB  1 
ATOM 2350 N N   . ILE A 1 320 ? 9.614  -12.875 38.575 1.00 58.91  ? 319 ILE A N   1 
ATOM 2351 C CA  . ILE A 1 320 ? 9.885  -13.911 37.584 1.00 48.89  ? 319 ILE A CA  1 
ATOM 2352 C C   . ILE A 1 320 ? 8.582  -14.483 37.044 1.00 41.49  ? 319 ILE A C   1 
ATOM 2353 O O   . ILE A 1 320 ? 8.421  -14.667 35.832 1.00 43.24  ? 319 ILE A O   1 
ATOM 2354 C CB  . ILE A 1 320 ? 10.775 -15.011 38.191 1.00 49.30  ? 319 ILE A CB  1 
ATOM 2355 C CG1 . ILE A 1 320 ? 12.119 -14.432 38.637 1.00 57.54  ? 319 ILE A CG1 1 
ATOM 2356 C CG2 . ILE A 1 320 ? 10.977 -16.135 37.198 1.00 44.93  ? 319 ILE A CG2 1 
ATOM 2357 C CD1 . ILE A 1 320 ? 12.871 -15.310 39.618 1.00 58.42  ? 319 ILE A CD1 1 
ATOM 2358 N N   . TRP A 1 321 ? 7.628  -14.761 37.932 1.00 47.46  ? 320 TRP A N   1 
ATOM 2359 C CA  . TRP A 1 321 ? 6.361  -15.341 37.503 1.00 47.22  ? 320 TRP A CA  1 
ATOM 2360 C C   . TRP A 1 321 ? 5.529  -14.355 36.692 1.00 40.56  ? 320 TRP A C   1 
ATOM 2361 O O   . TRP A 1 321 ? 4.718  -14.772 35.857 1.00 50.58  ? 320 TRP A O   1 
ATOM 2362 C CB  . TRP A 1 321 ? 5.574  -15.826 38.721 1.00 42.25  ? 320 TRP A CB  1 
ATOM 2363 C CG  . TRP A 1 321 ? 4.214  -16.348 38.390 1.00 41.27  ? 320 TRP A CG  1 
ATOM 2364 C CD1 . TRP A 1 321 ? 3.891  -17.625 38.041 1.00 41.27  ? 320 TRP A CD1 1 
ATOM 2365 C CD2 . TRP A 1 321 ? 2.991  -15.603 38.370 1.00 51.34  ? 320 TRP A CD2 1 
ATOM 2366 N NE1 . TRP A 1 321 ? 2.540  -17.724 37.808 1.00 44.41  ? 320 TRP A NE1 1 
ATOM 2367 C CE2 . TRP A 1 321 ? 1.965  -16.496 38.002 1.00 48.54  ? 320 TRP A CE2 1 
ATOM 2368 C CE3 . TRP A 1 321 ? 2.663  -14.268 38.627 1.00 46.69  ? 320 TRP A CE3 1 
ATOM 2369 C CZ2 . TRP A 1 321 ? 0.634  -16.098 37.886 1.00 52.18  ? 320 TRP A CZ2 1 
ATOM 2370 C CZ3 . TRP A 1 321 ? 1.342  -13.875 38.512 1.00 41.88  ? 320 TRP A CZ3 1 
ATOM 2371 C CH2 . TRP A 1 321 ? 0.344  -14.787 38.144 1.00 50.05  ? 320 TRP A CH2 1 
ATOM 2372 N N   . LEU A 1 322 ? 5.712  -13.054 36.912 1.00 47.62  ? 321 LEU A N   1 
ATOM 2373 C CA  . LEU A 1 322 ? 4.906  -12.050 36.225 1.00 46.88  ? 321 LEU A CA  1 
ATOM 2374 C C   . LEU A 1 322 ? 5.500  -11.673 34.872 1.00 46.20  ? 321 LEU A C   1 
ATOM 2375 O O   . LEU A 1 322 ? 4.886  -11.912 33.828 1.00 50.66  ? 321 LEU A O   1 
ATOM 2376 C CB  . LEU A 1 322 ? 4.751  -10.803 37.102 1.00 47.88  ? 321 LEU A CB  1 
ATOM 2377 C CG  . LEU A 1 322 ? 4.039  -9.624  36.438 1.00 53.80  ? 321 LEU A CG  1 
ATOM 2378 C CD1 . LEU A 1 322 ? 2.540  -9.865  36.400 1.00 47.44  ? 321 LEU A CD1 1 
ATOM 2379 C CD2 . LEU A 1 322 ? 4.363  -8.324  37.157 1.00 51.03  ? 321 LEU A CD2 1 
ATOM 2380 N N   . LEU A 1 323 ? 6.696  -11.082 34.878 1.00 42.67  ? 322 LEU A N   1 
ATOM 2381 C CA  . LEU A 1 323 ? 7.281  -10.563 33.646 1.00 44.28  ? 322 LEU A CA  1 
ATOM 2382 C C   . LEU A 1 323 ? 7.867  -11.663 32.771 1.00 49.45  ? 322 LEU A C   1 
ATOM 2383 O O   . LEU A 1 323 ? 7.905  -11.514 31.546 1.00 49.10  ? 322 LEU A O   1 
ATOM 2384 C CB  . LEU A 1 323 ? 8.352  -9.526  33.979 1.00 42.30  ? 322 LEU A CB  1 
ATOM 2385 C CG  . LEU A 1 323 ? 7.843  -8.389  34.868 1.00 52.45  ? 322 LEU A CG  1 
ATOM 2386 C CD1 . LEU A 1 323 ? 8.970  -7.435  35.237 1.00 43.38  ? 322 LEU A CD1 1 
ATOM 2387 C CD2 . LEU A 1 323 ? 6.695  -7.649  34.191 1.00 45.34  ? 322 LEU A CD2 1 
ATOM 2388 N N   . LEU A 1 324 ? 8.331  -12.759 33.369 1.00 39.37  ? 323 LEU A N   1 
ATOM 2389 C CA  . LEU A 1 324 ? 8.865  -13.871 32.594 1.00 47.46  ? 323 LEU A CA  1 
ATOM 2390 C C   . LEU A 1 324 ? 8.040  -15.129 32.851 1.00 42.79  ? 323 LEU A C   1 
ATOM 2391 O O   . LEU A 1 324 ? 6.829  -15.041 33.076 1.00 46.64  ? 323 LEU A O   1 
ATOM 2392 C CB  . LEU A 1 324 ? 10.342 -14.092 32.930 1.00 43.57  ? 323 LEU A CB  1 
ATOM 2393 C CG  . LEU A 1 324 ? 11.284 -12.945 32.538 1.00 39.68  ? 323 LEU A CG  1 
ATOM 2394 C CD1 . LEU A 1 324 ? 12.719 -13.434 32.465 1.00 49.39  ? 323 LEU A CD1 1 
ATOM 2395 C CD2 . LEU A 1 324 ? 10.884 -12.302 31.214 1.00 41.26  ? 323 LEU A CD2 1 
ATOM 2396 N N   . SER A 1 325 ? 8.672  -16.297 32.826 1.00 40.36  ? 324 SER A N   1 
ATOM 2397 C CA  . SER A 1 325 ? 7.984  -17.558 33.060 1.00 52.03  ? 324 SER A CA  1 
ATOM 2398 C C   . SER A 1 325 ? 8.536  -18.237 34.305 1.00 44.67  ? 324 SER A C   1 
ATOM 2399 O O   . SER A 1 325 ? 9.610  -17.897 34.808 1.00 42.43  ? 324 SER A O   1 
ATOM 2400 C CB  . SER A 1 325 ? 8.117  -18.500 31.856 1.00 57.67  ? 324 SER A CB  1 
ATOM 2401 O OG  . SER A 1 325 ? 9.195  -19.403 32.032 1.00 39.61  ? 324 SER A OG  1 
ATOM 2402 N N   . ASN A 1 326 ? 7.781  -19.224 34.794 1.00 49.37  ? 325 ASN A N   1 
ATOM 2403 C CA  . ASN A 1 326 ? 8.243  -20.031 35.916 1.00 48.14  ? 325 ASN A CA  1 
ATOM 2404 C C   . ASN A 1 326 ? 9.462  -20.873 35.562 1.00 52.49  ? 325 ASN A C   1 
ATOM 2405 O O   . ASN A 1 326 ? 10.213 -21.261 36.464 1.00 51.47  ? 325 ASN A O   1 
ATOM 2406 C CB  . ASN A 1 326 ? 7.115  -20.934 36.418 1.00 55.60  ? 325 ASN A CB  1 
ATOM 2407 C CG  . ASN A 1 326 ? 6.568  -20.487 37.758 1.00 63.58  ? 325 ASN A CG  1 
ATOM 2408 O OD1 . ASN A 1 326 ? 7.299  -19.949 38.589 1.00 50.46  ? 325 ASN A OD1 1 
ATOM 2409 N ND2 . ASN A 1 326 ? 5.276  -20.711 37.977 1.00 56.75  ? 325 ASN A ND2 1 
ATOM 2410 N N   . LYS A 1 327 ? 9.677  -21.162 34.276 1.00 52.03  ? 326 LYS A N   1 
ATOM 2411 C CA  . LYS A 1 327 ? 10.897 -21.839 33.850 1.00 45.62  ? 326 LYS A CA  1 
ATOM 2412 C C   . LYS A 1 327 ? 12.141 -20.999 34.100 1.00 51.14  ? 326 LYS A C   1 
ATOM 2413 O O   . LYS A 1 327 ? 13.256 -21.503 33.924 1.00 47.45  ? 326 LYS A O   1 
ATOM 2414 C CB  . LYS A 1 327 ? 10.807 -22.203 32.367 1.00 43.76  ? 326 LYS A CB  1 
ATOM 2415 C CG  . LYS A 1 327 ? 9.721  -23.215 32.036 1.00 44.91  ? 326 LYS A CG  1 
ATOM 2416 C CD  . LYS A 1 327 ? 10.234 -24.643 32.163 1.00 68.17  ? 326 LYS A CD  1 
ATOM 2417 C CE  . LYS A 1 327 ? 9.831  -25.270 33.493 1.00 46.28  ? 326 LYS A CE  1 
ATOM 2418 N NZ  . LYS A 1 327 ? 10.742 -26.382 33.877 1.00 53.08  ? 326 LYS A NZ  1 
ATOM 2419 N N   . PHE A 1 328 ? 11.974 -19.735 34.493 1.00 56.91  ? 327 PHE A N   1 
ATOM 2420 C CA  . PHE A 1 328 ? 13.071 -18.862 34.886 1.00 54.37  ? 327 PHE A CA  1 
ATOM 2421 C C   . PHE A 1 328 ? 13.211 -18.769 36.401 1.00 54.94  ? 327 PHE A C   1 
ATOM 2422 O O   . PHE A 1 328 ? 13.655 -17.739 36.917 1.00 55.47  ? 327 PHE A O   1 
ATOM 2423 C CB  . PHE A 1 328 ? 12.870 -17.461 34.306 1.00 50.63  ? 327 PHE A CB  1 
ATOM 2424 C CG  . PHE A 1 328 ? 13.077 -17.370 32.823 1.00 50.90  ? 327 PHE A CG  1 
ATOM 2425 C CD1 . PHE A 1 328 ? 12.109 -17.831 31.946 1.00 51.11  ? 327 PHE A CD1 1 
ATOM 2426 C CD2 . PHE A 1 328 ? 14.224 -16.794 32.304 1.00 49.23  ? 327 PHE A CD2 1 
ATOM 2427 C CE1 . PHE A 1 328 ? 12.288 -17.735 30.580 1.00 50.63  ? 327 PHE A CE1 1 
ATOM 2428 C CE2 . PHE A 1 328 ? 14.409 -16.695 30.937 1.00 48.76  ? 327 PHE A CE2 1 
ATOM 2429 C CZ  . PHE A 1 328 ? 13.437 -17.164 30.075 1.00 50.80  ? 327 PHE A CZ  1 
ATOM 2430 N N   . THR A 1 329 ? 12.826 -19.814 37.135 1.00 63.52  ? 328 THR A N   1 
ATOM 2431 C CA  . THR A 1 329 ? 12.849 -19.711 38.591 1.00 56.40  ? 328 THR A CA  1 
ATOM 2432 C C   . THR A 1 329 ? 14.261 -19.598 39.148 1.00 50.78  ? 328 THR A C   1 
ATOM 2433 O O   . THR A 1 329 ? 14.435 -19.074 40.254 1.00 55.17  ? 328 THR A O   1 
ATOM 2434 C CB  . THR A 1 329 ? 12.143 -20.906 39.225 1.00 54.10  ? 328 THR A CB  1 
ATOM 2435 O OG1 . THR A 1 329 ? 12.399 -20.918 40.636 1.00 68.00  ? 328 THR A OG1 1 
ATOM 2436 C CG2 . THR A 1 329 ? 12.641 -22.202 38.609 1.00 49.60  ? 328 THR A CG2 1 
ATOM 2437 N N   . ALA A 1 330 ? 15.268 -20.051 38.405 1.00 56.33  ? 329 ALA A N   1 
ATOM 2438 C CA  . ALA A 1 330 ? 16.653 -20.040 38.869 1.00 52.23  ? 329 ALA A CA  1 
ATOM 2439 C C   . ALA A 1 330 ? 17.287 -18.646 38.883 1.00 56.87  ? 329 ALA A C   1 
ATOM 2440 O O   . ALA A 1 330 ? 18.490 -18.575 39.159 1.00 57.55  ? 329 ALA A O   1 
ATOM 2441 C CB  . ALA A 1 330 ? 17.497 -20.983 38.010 1.00 52.54  ? 329 ALA A CB  1 
ATOM 2442 N N   . MET A 1 331 ? 16.589 -17.545 38.607 1.00 64.43  ? 330 MET A N   1 
ATOM 2443 C CA  . MET A 1 331 ? 17.204 -16.228 38.720 1.00 66.59  ? 330 MET A CA  1 
ATOM 2444 C C   . MET A 1 331 ? 17.142 -15.657 40.131 1.00 59.77  ? 330 MET A C   1 
ATOM 2445 O O   . MET A 1 331 ? 17.779 -14.630 40.386 1.00 60.43  ? 330 MET A O   1 
ATOM 2446 C CB  . MET A 1 331 ? 16.534 -15.228 37.774 1.00 66.21  ? 330 MET A CB  1 
ATOM 2447 C CG  . MET A 1 331 ? 15.873 -15.803 36.546 1.00 60.26  ? 330 MET A CG  1 
ATOM 2448 S SD  . MET A 1 331 ? 15.657 -14.565 35.263 1.00 69.40  ? 330 MET A SD  1 
ATOM 2449 C CE  . MET A 1 331 ? 14.009 -14.017 35.676 1.00 54.35  ? 330 MET A CE  1 
ATOM 2450 N N   . ARG A 1 332 ? 16.397 -16.292 41.042 1.00 61.06  ? 331 ARG A N   1 
ATOM 2451 C CA  . ARG A 1 332 ? 16.093 -15.670 42.329 1.00 62.91  ? 331 ARG A CA  1 
ATOM 2452 C C   . ARG A 1 332 ? 17.357 -15.258 43.079 1.00 61.12  ? 331 ARG A C   1 
ATOM 2453 O O   . ARG A 1 332 ? 17.377 -14.218 43.748 1.00 64.46  ? 331 ARG A O   1 
ATOM 2454 C CB  . ARG A 1 332 ? 15.238 -16.619 43.176 1.00 72.75  ? 331 ARG A CB  1 
ATOM 2455 C CG  . ARG A 1 332 ? 16.026 -17.613 44.015 1.00 69.03  ? 331 ARG A CG  1 
ATOM 2456 C CD  . ARG A 1 332 ? 15.127 -18.649 44.654 1.00 78.31  ? 331 ARG A CD  1 
ATOM 2457 N NE  . ARG A 1 332 ? 14.680 -18.229 45.976 1.00 78.50  ? 331 ARG A NE  1 
ATOM 2458 C CZ  . ARG A 1 332 ? 13.419 -17.966 46.288 1.00 70.67  ? 331 ARG A CZ  1 
ATOM 2459 N NH1 . ARG A 1 332 ? 12.450 -18.079 45.396 1.00 72.19  ? 331 ARG A NH1 1 
ATOM 2460 N NH2 . ARG A 1 332 ? 13.124 -17.582 47.527 1.00 73.78  ? 331 ARG A NH2 1 
ATOM 2461 N N   . ASP A 1 333 ? 18.428 -16.041 42.961 1.00 65.87  ? 332 ASP A N   1 
ATOM 2462 C CA  . ASP A 1 333 ? 19.646 -15.763 43.710 1.00 61.86  ? 332 ASP A CA  1 
ATOM 2463 C C   . ASP A 1 333 ? 20.569 -14.787 42.997 1.00 59.40  ? 332 ASP A C   1 
ATOM 2464 O O   . ASP A 1 333 ? 21.455 -14.211 43.639 1.00 63.43  ? 332 ASP A O   1 
ATOM 2465 C CB  . ASP A 1 333 ? 20.392 -17.069 44.003 1.00 61.85  ? 332 ASP A CB  1 
ATOM 2466 C CG  . ASP A 1 333 ? 19.835 -17.798 45.214 1.00 58.54  ? 332 ASP A CG  1 
ATOM 2467 O OD1 . ASP A 1 333 ? 18.783 -17.371 45.738 1.00 61.82  ? 332 ASP A OD1 1 
ATOM 2468 O OD2 . ASP A 1 333 ? 20.447 -18.800 45.639 1.00 54.19  ? 332 ASP A OD2 1 
ATOM 2469 N N   . LEU A 1 334 ? 20.383 -14.588 41.692 1.00 69.63  ? 333 LEU A N   1 
ATOM 2470 C CA  . LEU A 1 334 ? 21.125 -13.570 40.961 1.00 61.36  ? 333 LEU A CA  1 
ATOM 2471 C C   . LEU A 1 334 ? 20.556 -12.173 41.163 1.00 59.37  ? 333 LEU A C   1 
ATOM 2472 O O   . LEU A 1 334 ? 21.213 -11.196 40.787 1.00 57.04  ? 333 LEU A O   1 
ATOM 2473 C CB  . LEU A 1 334 ? 21.145 -13.894 39.462 1.00 58.37  ? 333 LEU A CB  1 
ATOM 2474 C CG  . LEU A 1 334 ? 21.810 -15.190 38.989 1.00 63.76  ? 333 LEU A CG  1 
ATOM 2475 C CD1 . LEU A 1 334 ? 20.846 -16.365 39.052 1.00 65.40  ? 333 LEU A CD1 1 
ATOM 2476 C CD2 . LEU A 1 334 ? 22.346 -15.019 37.576 1.00 64.35  ? 333 LEU A CD2 1 
ATOM 2477 N N   . PHE A 1 335 ? 19.360 -12.061 41.747 1.00 59.62  ? 334 PHE A N   1 
ATOM 2478 C CA  . PHE A 1 335 ? 18.716 -10.760 41.900 1.00 59.14  ? 334 PHE A CA  1 
ATOM 2479 C C   . PHE A 1 335 ? 19.564 -9.817  42.745 1.00 65.44  ? 334 PHE A C   1 
ATOM 2480 O O   . PHE A 1 335 ? 19.832 -8.679  42.345 1.00 67.35  ? 334 PHE A O   1 
ATOM 2481 C CB  . PHE A 1 335 ? 17.329 -10.935 42.522 1.00 59.48  ? 334 PHE A CB  1 
ATOM 2482 C CG  . PHE A 1 335 ? 16.219 -11.048 41.515 1.00 67.26  ? 334 PHE A CG  1 
ATOM 2483 C CD1 . PHE A 1 335 ? 16.210 -12.073 40.586 1.00 63.63  ? 334 PHE A CD1 1 
ATOM 2484 C CD2 . PHE A 1 335 ? 15.185 -10.127 41.498 1.00 73.44  ? 334 PHE A CD2 1 
ATOM 2485 C CE1 . PHE A 1 335 ? 15.191 -12.181 39.658 1.00 65.36  ? 334 PHE A CE1 1 
ATOM 2486 C CE2 . PHE A 1 335 ? 14.162 -10.229 40.573 1.00 71.69  ? 334 PHE A CE2 1 
ATOM 2487 C CZ  . PHE A 1 335 ? 14.166 -11.257 39.652 1.00 70.38  ? 334 PHE A CZ  1 
ATOM 2488 N N   . ALA A 1 336 ? 20.002 -10.280 43.918 1.00 67.60  ? 335 ALA A N   1 
ATOM 2489 C CA  . ALA A 1 336 ? 20.715 -9.410  44.849 1.00 48.49  ? 335 ALA A CA  1 
ATOM 2490 C C   . ALA A 1 336 ? 21.984 -8.841  44.225 1.00 51.29  ? 335 ALA A C   1 
ATOM 2491 O O   . ALA A 1 336 ? 22.262 -7.642  44.341 1.00 56.49  ? 335 ALA A O   1 
ATOM 2492 C CB  . ALA A 1 336 ? 21.043 -10.179 46.129 1.00 44.88  ? 335 ALA A CB  1 
ATOM 2493 N N   . TRP A 1 337 ? 22.763 -9.686  43.547 1.00 55.03  ? 336 TRP A N   1 
ATOM 2494 C CA  . TRP A 1 337 ? 24.047 -9.234  43.021 1.00 59.83  ? 336 TRP A CA  1 
ATOM 2495 C C   . TRP A 1 337 ? 23.870 -8.232  41.884 1.00 66.57  ? 336 TRP A C   1 
ATOM 2496 O O   . TRP A 1 337 ? 24.663 -7.292  41.750 1.00 60.76  ? 336 TRP A O   1 
ATOM 2497 C CB  . TRP A 1 337 ? 24.879 -10.430 42.558 1.00 54.70  ? 336 TRP A CB  1 
ATOM 2498 C CG  . TRP A 1 337 ? 25.115 -11.456 43.628 1.00 58.99  ? 336 TRP A CG  1 
ATOM 2499 C CD1 . TRP A 1 337 ? 24.227 -12.389 44.080 1.00 56.09  ? 336 TRP A CD1 1 
ATOM 2500 C CD2 . TRP A 1 337 ? 26.320 -11.655 44.379 1.00 58.10  ? 336 TRP A CD2 1 
ATOM 2501 N NE1 . TRP A 1 337 ? 24.803 -13.155 45.064 1.00 62.07  ? 336 TRP A NE1 1 
ATOM 2502 C CE2 . TRP A 1 337 ? 26.088 -12.725 45.266 1.00 56.34  ? 336 TRP A CE2 1 
ATOM 2503 C CE3 . TRP A 1 337 ? 27.572 -11.031 44.388 1.00 63.77  ? 336 TRP A CE3 1 
ATOM 2504 C CZ2 . TRP A 1 337 ? 27.061 -13.185 46.153 1.00 55.96  ? 336 TRP A CZ2 1 
ATOM 2505 C CZ3 . TRP A 1 337 ? 28.537 -11.490 45.268 1.00 54.96  ? 336 TRP A CZ3 1 
ATOM 2506 C CH2 . TRP A 1 337 ? 28.275 -12.557 46.138 1.00 63.48  ? 336 TRP A CH2 1 
ATOM 2507 N N   . GLN A 1 338 ? 22.838 -8.410  41.057 1.00 62.24  ? 337 GLN A N   1 
ATOM 2508 C CA  . GLN A 1 338 ? 22.642 -7.511  39.924 1.00 59.66  ? 337 GLN A CA  1 
ATOM 2509 C C   . GLN A 1 338 ? 22.127 -6.150  40.374 1.00 64.62  ? 337 GLN A C   1 
ATOM 2510 O O   . GLN A 1 338 ? 22.553 -5.113  39.850 1.00 62.07  ? 337 GLN A O   1 
ATOM 2511 C CB  . GLN A 1 338 ? 21.680 -8.138  38.915 1.00 65.70  ? 337 GLN A CB  1 
ATOM 2512 C CG  . GLN A 1 338 ? 21.607 -7.409  37.579 1.00 68.51  ? 337 GLN A CG  1 
ATOM 2513 C CD  . GLN A 1 338 ? 22.610 -7.934  36.570 1.00 61.92  ? 337 GLN A CD  1 
ATOM 2514 O OE1 . GLN A 1 338 ? 23.525 -8.679  36.917 1.00 67.16  ? 337 GLN A OE1 1 
ATOM 2515 N NE2 . GLN A 1 338 ? 22.441 -7.545  35.312 1.00 69.12  ? 337 GLN A NE2 1 
ATOM 2516 N N   . LEU A 1 339 ? 21.213 -6.132  41.345 1.00 61.01  ? 338 LEU A N   1 
ATOM 2517 C CA  . LEU A 1 339 ? 20.588 -4.878  41.750 1.00 62.02  ? 338 LEU A CA  1 
ATOM 2518 C C   . LEU A 1 339 ? 21.582 -3.934  42.411 1.00 59.26  ? 338 LEU A C   1 
ATOM 2519 O O   . LEU A 1 339 ? 21.441 -2.710  42.299 1.00 63.60  ? 338 LEU A O   1 
ATOM 2520 C CB  . LEU A 1 339 ? 19.421 -5.170  42.685 1.00 54.99  ? 338 LEU A CB  1 
ATOM 2521 C CG  . LEU A 1 339 ? 18.310 -6.006  42.054 1.00 51.42  ? 338 LEU A CG  1 
ATOM 2522 C CD1 . LEU A 1 339 ? 17.123 -6.042  42.974 1.00 49.16  ? 338 LEU A CD1 1 
ATOM 2523 C CD2 . LEU A 1 339 ? 17.917 -5.461  40.688 1.00 60.75  ? 338 LEU A CD2 1 
ATOM 2524 N N   . VAL A 1 340 ? 22.585 -4.474  43.104 1.00 49.54  ? 339 VAL A N   1 
ATOM 2525 C CA  . VAL A 1 340 ? 23.616 -3.621  43.682 1.00 57.06  ? 339 VAL A CA  1 
ATOM 2526 C C   . VAL A 1 340 ? 24.416 -2.940  42.580 1.00 66.00  ? 339 VAL A C   1 
ATOM 2527 O O   . VAL A 1 340 ? 24.736 -1.748  42.671 1.00 69.65  ? 339 VAL A O   1 
ATOM 2528 C CB  . VAL A 1 340 ? 24.516 -4.437  44.627 1.00 57.12  ? 339 VAL A CB  1 
ATOM 2529 C CG1 . VAL A 1 340 ? 25.867 -3.758  44.811 1.00 56.80  ? 339 VAL A CG1 1 
ATOM 2530 C CG2 . VAL A 1 340 ? 23.825 -4.640  45.964 1.00 49.29  ? 339 VAL A CG2 1 
ATOM 2531 N N   . GLY A 1 341 ? 24.738 -3.678  41.514 1.00 58.63  ? 340 GLY A N   1 
ATOM 2532 C CA  . GLY A 1 341 ? 25.413 -3.068  40.383 1.00 62.69  ? 340 GLY A CA  1 
ATOM 2533 C C   . GLY A 1 341 ? 24.558 -2.039  39.673 1.00 59.77  ? 340 GLY A C   1 
ATOM 2534 O O   . GLY A 1 341 ? 25.079 -1.064  39.125 1.00 61.15  ? 340 GLY A O   1 
ATOM 2535 N N   . ASP A 1 342 ? 23.238 -2.237  39.675 1.00 53.55  ? 341 ASP A N   1 
ATOM 2536 C CA  . ASP A 1 342 ? 22.334 -1.265  39.069 1.00 56.09  ? 341 ASP A CA  1 
ATOM 2537 C C   . ASP A 1 342 ? 22.389 0.066   39.804 1.00 65.95  ? 341 ASP A C   1 
ATOM 2538 O O   . ASP A 1 342 ? 22.451 1.133   39.182 1.00 60.50  ? 341 ASP A O   1 
ATOM 2539 C CB  . ASP A 1 342 ? 20.910 -1.808  39.078 1.00 56.95  ? 341 ASP A CB  1 
ATOM 2540 C CG  . ASP A 1 342 ? 20.694 -2.881  38.052 1.00 73.07  ? 341 ASP A CG  1 
ATOM 2541 O OD1 . ASP A 1 342 ? 21.666 -3.296  37.388 1.00 74.15  ? 341 ASP A OD1 1 
ATOM 2542 O OD2 . ASP A 1 342 ? 19.540 -3.323  37.929 1.00 75.80  ? 341 ASP A OD2 1 
ATOM 2543 N N   . VAL A 1 343 ? 22.338 0.016   41.137 1.00 68.75  ? 342 VAL A N   1 
ATOM 2544 C CA  . VAL A 1 343 ? 22.427 1.230   41.942 1.00 63.55  ? 342 VAL A CA  1 
ATOM 2545 C C   . VAL A 1 343 ? 23.712 1.981   41.623 1.00 59.22  ? 342 VAL A C   1 
ATOM 2546 O O   . VAL A 1 343 ? 23.710 3.206   41.452 1.00 64.19  ? 342 VAL A O   1 
ATOM 2547 C CB  . VAL A 1 343 ? 22.329 0.875   43.438 1.00 54.99  ? 342 VAL A CB  1 
ATOM 2548 C CG1 . VAL A 1 343 ? 22.974 1.952   44.298 1.00 49.88  ? 342 VAL A CG1 1 
ATOM 2549 C CG2 . VAL A 1 343 ? 20.880 0.648   43.841 1.00 57.20  ? 342 VAL A CG2 1 
ATOM 2550 N N   . LEU A 1 344 ? 24.823 1.253   41.508 1.00 57.14  ? 343 LEU A N   1 
ATOM 2551 C CA  . LEU A 1 344 ? 26.114 1.892   41.282 1.00 59.68  ? 343 LEU A CA  1 
ATOM 2552 C C   . LEU A 1 344 ? 26.256 2.370   39.844 1.00 67.89  ? 343 LEU A C   1 
ATOM 2553 O O   . LEU A 1 344 ? 26.935 3.372   39.589 1.00 68.50  ? 343 LEU A O   1 
ATOM 2554 C CB  . LEU A 1 344 ? 27.239 0.923   41.642 1.00 64.57  ? 343 LEU A CB  1 
ATOM 2555 C CG  . LEU A 1 344 ? 27.625 0.696   43.109 1.00 71.62  ? 343 LEU A CG  1 
ATOM 2556 C CD1 . LEU A 1 344 ? 26.451 0.766   44.074 1.00 63.07  ? 343 LEU A CD1 1 
ATOM 2557 C CD2 . LEU A 1 344 ? 28.275 -0.656  43.221 1.00 68.66  ? 343 LEU A CD2 1 
ATOM 2558 N N   . LYS A 1 345 ? 25.629 1.671   38.896 1.00 64.46  ? 344 LYS A N   1 
ATOM 2559 C CA  . LYS A 1 345 ? 25.637 2.126   37.509 1.00 70.18  ? 344 LYS A CA  1 
ATOM 2560 C C   . LYS A 1 345 ? 24.852 3.424   37.358 1.00 64.45  ? 344 LYS A C   1 
ATOM 2561 O O   . LYS A 1 345 ? 25.317 4.372   36.714 1.00 65.66  ? 344 LYS A O   1 
ATOM 2562 C CB  . LYS A 1 345 ? 25.068 1.037   36.599 1.00 63.92  ? 344 LYS A CB  1 
ATOM 2563 C CG  . LYS A 1 345 ? 25.153 1.361   35.117 1.00 69.32  ? 344 LYS A CG  1 
ATOM 2564 C CD  . LYS A 1 345 ? 24.617 0.220   34.268 1.00 61.70  ? 344 LYS A CD  1 
ATOM 2565 C CE  . LYS A 1 345 ? 23.098 0.162   34.305 1.00 69.10  ? 344 LYS A CE  1 
ATOM 2566 N NZ  . LYS A 1 345 ? 22.559 -0.849  33.352 1.00 60.43  ? 344 LYS A NZ  1 
ATOM 2567 N N   . VAL A 1 346 ? 23.657 3.485   37.952 1.00 61.31  ? 345 VAL A N   1 
ATOM 2568 C CA  . VAL A 1 346 ? 22.856 4.705   37.906 1.00 67.10  ? 345 VAL A CA  1 
ATOM 2569 C C   . VAL A 1 346 ? 23.535 5.827   38.682 1.00 66.74  ? 345 VAL A C   1 
ATOM 2570 O O   . VAL A 1 346 ? 23.430 7.003   38.311 1.00 62.48  ? 345 VAL A O   1 
ATOM 2571 C CB  . VAL A 1 346 ? 21.434 4.414   38.427 1.00 68.81  ? 345 VAL A CB  1 
ATOM 2572 C CG1 . VAL A 1 346 ? 20.799 5.657   39.043 1.00 67.81  ? 345 VAL A CG1 1 
ATOM 2573 C CG2 . VAL A 1 346 ? 20.569 3.878   37.301 1.00 54.18  ? 345 VAL A CG2 1 
ATOM 2574 N N   . GLY A 1 347 ? 24.248 5.495   39.757 1.00 66.13  ? 346 GLY A N   1 
ATOM 2575 C CA  . GLY A 1 347 ? 25.020 6.510   40.452 1.00 67.14  ? 346 GLY A CA  1 
ATOM 2576 C C   . GLY A 1 347 ? 26.145 7.062   39.597 1.00 65.69  ? 346 GLY A C   1 
ATOM 2577 O O   . GLY A 1 347 ? 26.363 8.275   39.549 1.00 68.54  ? 346 GLY A O   1 
ATOM 2578 N N   . ALA A 1 348 ? 26.871 6.181   38.906 1.00 67.00  ? 347 ALA A N   1 
ATOM 2579 C CA  . ALA A 1 348 ? 27.888 6.628   37.964 1.00 66.85  ? 347 ALA A CA  1 
ATOM 2580 C C   . ALA A 1 348 ? 27.289 7.242   36.707 1.00 69.58  ? 347 ALA A C   1 
ATOM 2581 O O   . ALA A 1 348 ? 28.038 7.788   35.890 1.00 70.01  ? 347 ALA A O   1 
ATOM 2582 C CB  . ALA A 1 348 ? 28.808 5.465   37.588 1.00 62.89  ? 347 ALA A CB  1 
ATOM 2583 N N   . TYR A 1 349 ? 25.966 7.161   36.531 1.00 67.01  ? 348 TYR A N   1 
ATOM 2584 C CA  . TYR A 1 349 ? 25.329 7.815   35.392 1.00 66.57  ? 348 TYR A CA  1 
ATOM 2585 C C   . TYR A 1 349 ? 25.469 9.330   35.482 1.00 74.84  ? 348 TYR A C   1 
ATOM 2586 O O   . TYR A 1 349 ? 25.667 10.003  34.464 1.00 78.28  ? 348 TYR A O   1 
ATOM 2587 C CB  . TYR A 1 349 ? 23.852 7.424   35.313 1.00 60.78  ? 348 TYR A CB  1 
ATOM 2588 C CG  . TYR A 1 349 ? 23.550 6.172   34.517 1.00 58.07  ? 348 TYR A CG  1 
ATOM 2589 C CD1 . TYR A 1 349 ? 24.551 5.489   33.837 1.00 70.50  ? 348 TYR A CD1 1 
ATOM 2590 C CD2 . TYR A 1 349 ? 22.255 5.674   34.445 1.00 59.72  ? 348 TYR A CD2 1 
ATOM 2591 C CE1 . TYR A 1 349 ? 24.267 4.341   33.106 1.00 66.52  ? 348 TYR A CE1 1 
ATOM 2592 C CE2 . TYR A 1 349 ? 21.962 4.533   33.721 1.00 66.06  ? 348 TYR A CE2 1 
ATOM 2593 C CZ  . TYR A 1 349 ? 22.970 3.870   33.054 1.00 63.05  ? 348 TYR A CZ  1 
ATOM 2594 O OH  . TYR A 1 349 ? 22.676 2.735   32.333 1.00 59.77  ? 348 TYR A OH  1 
ATOM 2595 N N   . VAL A 1 350 ? 25.378 9.886   36.695 1.00 70.44  ? 349 VAL A N   1 
ATOM 2596 C CA  . VAL A 1 350 ? 25.455 11.337  36.841 1.00 74.87  ? 349 VAL A CA  1 
ATOM 2597 C C   . VAL A 1 350 ? 26.854 11.835  36.505 1.00 72.24  ? 349 VAL A C   1 
ATOM 2598 O O   . VAL A 1 350 ? 27.018 12.959  36.018 1.00 70.60  ? 349 VAL A O   1 
ATOM 2599 C CB  . VAL A 1 350 ? 25.034 11.770  38.261 1.00 78.70  ? 349 VAL A CB  1 
ATOM 2600 C CG1 . VAL A 1 350 ? 23.737 11.087  38.674 1.00 73.92  ? 349 VAL A CG1 1 
ATOM 2601 C CG2 . VAL A 1 350 ? 26.144 11.516  39.273 1.00 75.22  ? 349 VAL A CG2 1 
ATOM 2602 N N   . PHE A 1 351 ? 27.880 11.020  36.760 1.00 68.19  ? 350 PHE A N   1 
ATOM 2603 C CA  . PHE A 1 351 ? 29.229 11.413  36.382 1.00 73.04  ? 350 PHE A CA  1 
ATOM 2604 C C   . PHE A 1 351 ? 29.428 11.314  34.877 1.00 83.00  ? 350 PHE A C   1 
ATOM 2605 O O   . PHE A 1 351 ? 30.187 12.101  34.299 1.00 87.19  ? 350 PHE A O   1 
ATOM 2606 C CB  . PHE A 1 351 ? 30.263 10.555  37.115 1.00 64.63  ? 350 PHE A CB  1 
ATOM 2607 C CG  . PHE A 1 351 ? 30.250 10.733  38.608 1.00 77.42  ? 350 PHE A CG  1 
ATOM 2608 C CD1 . PHE A 1 351 ? 30.705 11.907  39.184 1.00 76.28  ? 350 PHE A CD1 1 
ATOM 2609 C CD2 . PHE A 1 351 ? 29.794 9.719   39.436 1.00 84.91  ? 350 PHE A CD2 1 
ATOM 2610 C CE1 . PHE A 1 351 ? 30.697 12.071  40.556 1.00 84.90  ? 350 PHE A CE1 1 
ATOM 2611 C CE2 . PHE A 1 351 ? 29.784 9.877   40.810 1.00 78.86  ? 350 PHE A CE2 1 
ATOM 2612 C CZ  . PHE A 1 351 ? 30.237 11.054  41.371 1.00 77.32  ? 350 PHE A CZ  1 
ATOM 2613 N N   . GLY A 1 352 ? 28.753 10.366  34.226 1.00 74.86  ? 351 GLY A N   1 
ATOM 2614 C CA  . GLY A 1 352 ? 28.843 10.272  32.779 1.00 74.66  ? 351 GLY A CA  1 
ATOM 2615 C C   . GLY A 1 352 ? 28.092 11.387  32.076 1.00 77.59  ? 351 GLY A C   1 
ATOM 2616 O O   . GLY A 1 352 ? 28.557 11.919  31.064 1.00 80.64  ? 351 GLY A O   1 
ATOM 2617 N N   . TYR A 1 353 ? 26.920 11.757  32.600 1.00 71.17  ? 352 TYR A N   1 
ATOM 2618 C CA  . TYR A 1 353 ? 26.165 12.862  32.021 1.00 78.31  ? 352 TYR A CA  1 
ATOM 2619 C C   . TYR A 1 353 ? 26.879 14.197  32.193 1.00 85.20  ? 352 TYR A C   1 
ATOM 2620 O O   . TYR A 1 353 ? 26.617 15.128  31.424 1.00 92.05  ? 352 TYR A O   1 
ATOM 2621 C CB  . TYR A 1 353 ? 24.763 12.921  32.632 1.00 72.29  ? 352 TYR A CB  1 
ATOM 2622 C CG  . TYR A 1 353 ? 23.776 11.987  31.966 1.00 74.68  ? 352 TYR A CG  1 
ATOM 2623 C CD1 . TYR A 1 353 ? 23.374 12.190  30.652 1.00 82.68  ? 352 TYR A CD1 1 
ATOM 2624 C CD2 . TYR A 1 353 ? 23.248 10.899  32.650 1.00 74.38  ? 352 TYR A CD2 1 
ATOM 2625 C CE1 . TYR A 1 353 ? 22.474 11.337  30.038 1.00 89.37  ? 352 TYR A CE1 1 
ATOM 2626 C CE2 . TYR A 1 353 ? 22.348 10.041  32.045 1.00 85.04  ? 352 TYR A CE2 1 
ATOM 2627 C CZ  . TYR A 1 353 ? 21.964 10.264  30.738 1.00 88.53  ? 352 TYR A CZ  1 
ATOM 2628 O OH  . TYR A 1 353 ? 21.068 9.413   30.132 1.00 75.00  ? 352 TYR A OH  1 
ATOM 2629 N N   . LEU A 1 354 ? 27.770 14.313  33.182 1.00 81.63  ? 353 LEU A N   1 
ATOM 2630 C CA  . LEU A 1 354 ? 28.645 15.479  33.258 1.00 78.52  ? 353 LEU A CA  1 
ATOM 2631 C C   . LEU A 1 354 ? 29.650 15.488  32.117 1.00 85.39  ? 353 LEU A C   1 
ATOM 2632 O O   . LEU A 1 354 ? 29.899 16.535  31.509 1.00 94.16  ? 353 LEU A O   1 
ATOM 2633 C CB  . LEU A 1 354 ? 29.388 15.502  34.591 1.00 82.86  ? 353 LEU A CB  1 
ATOM 2634 C CG  . LEU A 1 354 ? 29.818 16.867  35.122 1.00 84.11  ? 353 LEU A CG  1 
ATOM 2635 C CD1 . LEU A 1 354 ? 29.836 16.834  36.625 1.00 83.99  ? 353 LEU A CD1 1 
ATOM 2636 C CD2 . LEU A 1 354 ? 31.187 17.257  34.575 1.00 82.28  ? 353 LEU A CD2 1 
ATOM 2637 N N   . VAL A 1 355 ? 30.261 14.334  31.838 1.00 83.65  ? 354 VAL A N   1 
ATOM 2638 C CA  . VAL A 1 355 ? 31.239 14.239  30.759 1.00 97.67  ? 354 VAL A CA  1 
ATOM 2639 C C   . VAL A 1 355 ? 30.569 14.473  29.410 1.00 91.24  ? 354 VAL A C   1 
ATOM 2640 O O   . VAL A 1 355 ? 31.151 15.093  28.511 1.00 87.83  ? 354 VAL A O   1 
ATOM 2641 C CB  . VAL A 1 355 ? 31.951 12.874  30.819 1.00 96.17  ? 354 VAL A CB  1 
ATOM 2642 C CG1 . VAL A 1 355 ? 32.655 12.566  29.503 1.00 92.89  ? 354 VAL A CG1 1 
ATOM 2643 C CG2 . VAL A 1 355 ? 32.933 12.837  31.985 1.00 83.25  ? 354 VAL A CG2 1 
ATOM 2644 N N   . ILE A 1 356 ? 29.334 13.989  29.250 1.00 90.78  ? 355 ILE A N   1 
ATOM 2645 C CA  . ILE A 1 356 ? 28.595 14.224  28.012 1.00 91.05  ? 355 ILE A CA  1 
ATOM 2646 C C   . ILE A 1 356 ? 28.361 15.716  27.809 1.00 94.25  ? 355 ILE A C   1 
ATOM 2647 O O   . ILE A 1 356 ? 28.499 16.236  26.695 1.00 102.78 ? 355 ILE A O   1 
ATOM 2648 C CB  . ILE A 1 356 ? 27.270 13.437  28.024 1.00 86.68  ? 355 ILE A CB  1 
ATOM 2649 C CG1 . ILE A 1 356 ? 27.542 11.931  27.970 1.00 75.50  ? 355 ILE A CG1 1 
ATOM 2650 C CG2 . ILE A 1 356 ? 26.379 13.860  26.864 1.00 86.75  ? 355 ILE A CG2 1 
ATOM 2651 C CD1 . ILE A 1 356 ? 26.288 11.085  27.916 1.00 70.46  ? 355 ILE A CD1 1 
ATOM 2652 N N   . ALA A 1 357 ? 28.014 16.429  28.884 1.00 92.84  ? 356 ALA A N   1 
ATOM 2653 C CA  . ALA A 1 357 ? 27.824 17.872  28.783 1.00 100.46 ? 356 ALA A CA  1 
ATOM 2654 C C   . ALA A 1 357 ? 29.129 18.577  28.434 1.00 104.18 ? 356 ALA A C   1 
ATOM 2655 O O   . ALA A 1 357 ? 29.132 19.554  27.676 1.00 107.72 ? 356 ALA A O   1 
ATOM 2656 C CB  . ALA A 1 357 ? 27.246 18.418  30.088 1.00 92.05  ? 356 ALA A CB  1 
ATOM 2657 N N   . LYS A 1 358 ? 30.249 18.095  28.975 1.00 114.41 ? 357 LYS A N   1 
ATOM 2658 C CA  . LYS A 1 358 ? 31.556 18.644  28.639 1.00 113.61 ? 357 LYS A CA  1 
ATOM 2659 C C   . LYS A 1 358 ? 32.043 18.204  27.264 1.00 114.44 ? 357 LYS A C   1 
ATOM 2660 O O   . LYS A 1 358 ? 32.995 18.798  26.745 1.00 122.01 ? 357 LYS A O   1 
ATOM 2661 C CB  . LYS A 1 358 ? 32.583 18.243  29.704 1.00 114.11 ? 357 LYS A CB  1 
ATOM 2662 C CG  . LYS A 1 358 ? 33.800 19.157  29.787 1.00 110.98 ? 357 LYS A CG  1 
ATOM 2663 C CD  . LYS A 1 358 ? 34.702 18.791  30.959 1.00 116.26 ? 357 LYS A CD  1 
ATOM 2664 C CE  . LYS A 1 358 ? 34.896 17.286  31.072 1.00 106.88 ? 357 LYS A CE  1 
ATOM 2665 N NZ  . LYS A 1 358 ? 35.642 16.918  32.308 1.00 98.86  ? 357 LYS A NZ  1 
ATOM 2666 N N   . ALA A 1 359 ? 31.416 17.186  26.669 1.00 108.89 ? 358 ALA A N   1 
ATOM 2667 C CA  . ALA A 1 359 ? 31.775 16.671  25.346 1.00 106.70 ? 358 ALA A CA  1 
ATOM 2668 C C   . ALA A 1 359 ? 33.242 16.263  25.269 1.00 100.05 ? 358 ALA A C   1 
ATOM 2669 O O   . ALA A 1 359 ? 33.835 16.243  24.184 1.00 86.45  ? 358 ALA A O   1 
ATOM 2670 C CB  . ALA A 1 359 ? 31.445 17.682  24.241 1.00 104.72 ? 358 ALA A CB  1 
ATOM 2671 N N   . SER A 1 360 ? 33.840 15.941  26.412 1.00 100.78 ? 359 SER A N   1 
ATOM 2672 C CA  . SER A 1 360 ? 35.240 15.534  26.464 1.00 90.87  ? 359 SER A CA  1 
ATOM 2673 C C   . SER A 1 360 ? 35.338 14.100  25.965 1.00 88.62  ? 359 SER A C   1 
ATOM 2674 O O   . SER A 1 360 ? 35.102 13.151  26.715 1.00 87.67  ? 359 SER A O   1 
ATOM 2675 C CB  . SER A 1 360 ? 35.792 15.668  27.877 1.00 88.37  ? 359 SER A CB  1 
ATOM 2676 O OG  . SER A 1 360 ? 37.173 15.354  27.907 1.00 85.59  ? 359 SER A OG  1 
ATOM 2677 N N   . LEU A 1 361 ? 35.682 13.940  24.685 1.00 86.61  ? 360 LEU A N   1 
ATOM 2678 C CA  . LEU A 1 361 ? 35.870 12.607  24.127 1.00 74.37  ? 360 LEU A CA  1 
ATOM 2679 C C   . LEU A 1 361 ? 36.967 11.839  24.848 1.00 76.60  ? 360 LEU A C   1 
ATOM 2680 O O   . LEU A 1 361 ? 36.962 10.604  24.829 1.00 82.76  ? 360 LEU A O   1 
ATOM 2681 C CB  . LEU A 1 361 ? 36.186 12.702  22.634 1.00 73.82  ? 360 LEU A CB  1 
ATOM 2682 C CG  . LEU A 1 361 ? 35.107 12.184  21.681 1.00 68.49  ? 360 LEU A CG  1 
ATOM 2683 C CD1 . LEU A 1 361 ? 33.789 12.904  21.917 1.00 76.89  ? 360 LEU A CD1 1 
ATOM 2684 C CD2 . LEU A 1 361 ? 35.552 12.334  20.236 1.00 78.12  ? 360 LEU A CD2 1 
ATOM 2685 N N   . ARG A 1 362 ? 37.903 12.543  25.485 1.00 79.26  ? 361 ARG A N   1 
ATOM 2686 C CA  . ARG A 1 362 ? 38.924 11.875  26.284 1.00 83.06  ? 361 ARG A CA  1 
ATOM 2687 C C   . ARG A 1 362 ? 38.309 11.207  27.508 1.00 83.26  ? 361 ARG A C   1 
ATOM 2688 O O   . ARG A 1 362 ? 38.615 10.049  27.817 1.00 81.06  ? 361 ARG A O   1 
ATOM 2689 C CB  . ARG A 1 362 ? 39.995 12.882  26.700 1.00 81.52  ? 361 ARG A CB  1 
ATOM 2690 C CG  . ARG A 1 362 ? 40.406 13.830  25.588 1.00 81.80  ? 361 ARG A CG  1 
ATOM 2691 C CD  . ARG A 1 362 ? 40.373 15.279  26.043 1.00 84.31  ? 361 ARG A CD  1 
ATOM 2692 N NE  . ARG A 1 362 ? 40.287 16.192  24.910 1.00 78.30  ? 361 ARG A NE  1 
ATOM 2693 C CZ  . ARG A 1 362 ? 39.152 16.631  24.385 1.00 81.77  ? 361 ARG A CZ  1 
ATOM 2694 N NH1 . ARG A 1 362 ? 37.978 16.271  24.878 1.00 73.91  ? 361 ARG A NH1 1 
ATOM 2695 N NH2 . ARG A 1 362 ? 39.194 17.449  23.338 1.00 81.12  ? 361 ARG A NH2 1 
ATOM 2696 N N   . PHE A 1 363 ? 37.435 11.925  28.215 1.00 92.99  ? 362 PHE A N   1 
ATOM 2697 C CA  . PHE A 1 363 ? 36.812 11.367  29.411 1.00 90.94  ? 362 PHE A CA  1 
ATOM 2698 C C   . PHE A 1 363 ? 35.800 10.284  29.056 1.00 88.82  ? 362 PHE A C   1 
ATOM 2699 O O   . PHE A 1 363 ? 35.692 9.275   29.762 1.00 88.68  ? 362 PHE A O   1 
ATOM 2700 C CB  . PHE A 1 363 ? 36.148 12.480  30.221 1.00 94.06  ? 362 PHE A CB  1 
ATOM 2701 C CG  . PHE A 1 363 ? 37.060 13.131  31.221 1.00 101.35 ? 362 PHE A CG  1 
ATOM 2702 C CD1 . PHE A 1 363 ? 38.060 13.994  30.807 1.00 101.52 ? 362 PHE A CD1 1 
ATOM 2703 C CD2 . PHE A 1 363 ? 36.915 12.880  32.576 1.00 94.95  ? 362 PHE A CD2 1 
ATOM 2704 C CE1 . PHE A 1 363 ? 38.901 14.595  31.724 1.00 99.19  ? 362 PHE A CE1 1 
ATOM 2705 C CE2 . PHE A 1 363 ? 37.752 13.477  33.498 1.00 95.87  ? 362 PHE A CE2 1 
ATOM 2706 C CZ  . PHE A 1 363 ? 38.746 14.336  33.072 1.00 105.72 ? 362 PHE A CZ  1 
ATOM 2707 N N   . TYR A 1 364 ? 35.047 10.478  27.970 1.00 77.93  ? 363 TYR A N   1 
ATOM 2708 C CA  . TYR A 1 364 ? 34.085 9.465   27.547 1.00 82.50  ? 363 TYR A CA  1 
ATOM 2709 C C   . TYR A 1 364 ? 34.788 8.173   27.150 1.00 75.33  ? 363 TYR A C   1 
ATOM 2710 O O   . TYR A 1 364 ? 34.336 7.077   27.503 1.00 67.44  ? 363 TYR A O   1 
ATOM 2711 C CB  . TYR A 1 364 ? 33.237 9.994   26.390 1.00 79.76  ? 363 TYR A CB  1 
ATOM 2712 C CG  . TYR A 1 364 ? 31.978 9.194   26.141 1.00 81.09  ? 363 TYR A CG  1 
ATOM 2713 C CD1 . TYR A 1 364 ? 31.074 8.947   27.168 1.00 81.04  ? 363 TYR A CD1 1 
ATOM 2714 C CD2 . TYR A 1 364 ? 31.694 8.682   24.882 1.00 67.38  ? 363 TYR A CD2 1 
ATOM 2715 C CE1 . TYR A 1 364 ? 29.922 8.214   26.946 1.00 73.18  ? 363 TYR A CE1 1 
ATOM 2716 C CE2 . TYR A 1 364 ? 30.545 7.948   24.651 1.00 66.86  ? 363 TYR A CE2 1 
ATOM 2717 C CZ  . TYR A 1 364 ? 29.663 7.717   25.686 1.00 73.55  ? 363 TYR A CZ  1 
ATOM 2718 O OH  . TYR A 1 364 ? 28.518 6.986   25.461 1.00 67.59  ? 363 TYR A OH  1 
ATOM 2719 N N   . ILE A 1 365 ? 35.896 8.284   26.412 1.00 71.08  ? 364 ILE A N   1 
ATOM 2720 C CA  . ILE A 1 365 ? 36.688 7.105   26.067 1.00 76.44  ? 364 ILE A CA  1 
ATOM 2721 C C   . ILE A 1 365 ? 37.162 6.402   27.333 1.00 73.83  ? 364 ILE A C   1 
ATOM 2722 O O   . ILE A 1 365 ? 37.061 5.176   27.461 1.00 70.28  ? 364 ILE A O   1 
ATOM 2723 C CB  . ILE A 1 365 ? 37.871 7.499   25.162 1.00 71.62  ? 364 ILE A CB  1 
ATOM 2724 C CG1 . ILE A 1 365 ? 37.446 7.495   23.694 1.00 72.51  ? 364 ILE A CG1 1 
ATOM 2725 C CG2 . ILE A 1 365 ? 39.057 6.562   25.364 1.00 73.08  ? 364 ILE A CG2 1 
ATOM 2726 C CD1 . ILE A 1 365 ? 38.556 7.880   22.739 1.00 74.79  ? 364 ILE A CD1 1 
ATOM 2727 N N   . LEU A 1 366 ? 37.667 7.176   28.296 1.00 71.52  ? 365 LEU A N   1 
ATOM 2728 C CA  . LEU A 1 366 ? 38.169 6.590   29.534 1.00 67.36  ? 365 LEU A CA  1 
ATOM 2729 C C   . LEU A 1 366 ? 37.050 5.925   30.326 1.00 64.52  ? 365 LEU A C   1 
ATOM 2730 O O   . LEU A 1 366 ? 37.257 4.873   30.941 1.00 61.80  ? 365 LEU A O   1 
ATOM 2731 C CB  . LEU A 1 366 ? 38.858 7.663   30.376 1.00 68.58  ? 365 LEU A CB  1 
ATOM 2732 C CG  . LEU A 1 366 ? 40.163 7.255   31.058 1.00 71.74  ? 365 LEU A CG  1 
ATOM 2733 C CD1 . LEU A 1 366 ? 41.131 6.656   30.049 1.00 61.09  ? 365 LEU A CD1 1 
ATOM 2734 C CD2 . LEU A 1 366 ? 40.787 8.448   31.763 1.00 64.60  ? 365 LEU A CD2 1 
ATOM 2735 N N   . ALA A 1 367 ? 35.857 6.521   30.317 1.00 61.38  ? 366 ALA A N   1 
ATOM 2736 C CA  . ALA A 1 367 ? 34.733 5.946   31.050 1.00 60.97  ? 366 ALA A CA  1 
ATOM 2737 C C   . ALA A 1 367 ? 34.315 4.606   30.457 1.00 66.17  ? 366 ALA A C   1 
ATOM 2738 O O   . ALA A 1 367 ? 34.142 3.620   31.184 1.00 56.42  ? 366 ALA A O   1 
ATOM 2739 C CB  . ALA A 1 367 ? 33.558 6.923   31.054 1.00 52.08  ? 366 ALA A CB  1 
ATOM 2740 N N   . GLU A 1 368 ? 34.152 4.550   29.134 1.00 65.85  ? 367 GLU A N   1 
ATOM 2741 C CA  . GLU A 1 368 ? 33.692 3.320   28.498 1.00 59.57  ? 367 GLU A CA  1 
ATOM 2742 C C   . GLU A 1 368 ? 34.771 2.245   28.519 1.00 62.99  ? 367 GLU A C   1 
ATOM 2743 O O   . GLU A 1 368 ? 34.471 1.061   28.713 1.00 61.23  ? 367 GLU A O   1 
ATOM 2744 C CB  . GLU A 1 368 ? 33.245 3.607   27.066 1.00 62.18  ? 367 GLU A CB  1 
ATOM 2745 C CG  . GLU A 1 368 ? 32.104 4.604   26.971 1.00 56.09  ? 367 GLU A CG  1 
ATOM 2746 C CD  . GLU A 1 368 ? 30.744 3.951   27.120 1.00 65.62  ? 367 GLU A CD  1 
ATOM 2747 O OE1 . GLU A 1 368 ? 30.683 2.709   27.254 1.00 65.53  ? 367 GLU A OE1 1 
ATOM 2748 O OE2 . GLU A 1 368 ? 29.733 4.684   27.106 1.00 62.16  ? 367 GLU A OE2 1 
ATOM 2749 N N   . VAL A 1 369 ? 36.031 2.635   28.321 1.00 60.05  ? 368 VAL A N   1 
ATOM 2750 C CA  . VAL A 1 369 ? 37.119 1.663   28.365 1.00 57.90  ? 368 VAL A CA  1 
ATOM 2751 C C   . VAL A 1 369 ? 37.261 1.085   29.768 1.00 58.71  ? 368 VAL A C   1 
ATOM 2752 O O   . VAL A 1 369 ? 37.502 -0.116  29.938 1.00 63.42  ? 368 VAL A O   1 
ATOM 2753 C CB  . VAL A 1 369 ? 38.429 2.306   27.872 1.00 62.17  ? 368 VAL A CB  1 
ATOM 2754 C CG1 . VAL A 1 369 ? 39.639 1.630   28.501 1.00 56.09  ? 368 VAL A CG1 1 
ATOM 2755 C CG2 . VAL A 1 369 ? 38.507 2.251   26.353 1.00 65.32  ? 368 VAL A CG2 1 
ATOM 2756 N N   . SER A 1 370 ? 37.099 1.924   30.795 1.00 60.79  ? 369 SER A N   1 
ATOM 2757 C CA  . SER A 1 370 ? 37.211 1.439   32.168 1.00 60.33  ? 369 SER A CA  1 
ATOM 2758 C C   . SER A 1 370 ? 36.135 0.408   32.480 1.00 57.42  ? 369 SER A C   1 
ATOM 2759 O O   . SER A 1 370 ? 36.416 -0.623  33.103 1.00 58.13  ? 369 SER A O   1 
ATOM 2760 C CB  . SER A 1 370 ? 37.130 2.608   33.150 1.00 59.69  ? 369 SER A CB  1 
ATOM 2761 O OG  . SER A 1 370 ? 38.201 3.514   32.956 1.00 59.64  ? 369 SER A OG  1 
ATOM 2762 N N   . GLN A 1 371 ? 34.897 0.667   32.055 1.00 56.88  ? 370 GLN A N   1 
ATOM 2763 C CA  . GLN A 1 371 ? 33.818 -0.287  32.292 1.00 56.84  ? 370 GLN A CA  1 
ATOM 2764 C C   . GLN A 1 371 ? 34.053 -1.582  31.525 1.00 65.16  ? 370 GLN A C   1 
ATOM 2765 O O   . GLN A 1 371 ? 33.873 -2.678  32.068 1.00 68.64  ? 370 GLN A O   1 
ATOM 2766 C CB  . GLN A 1 371 ? 32.477 0.331   31.898 1.00 55.94  ? 370 GLN A CB  1 
ATOM 2767 C CG  . GLN A 1 371 ? 32.028 1.481   32.777 1.00 55.67  ? 370 GLN A CG  1 
ATOM 2768 C CD  . GLN A 1 371 ? 30.701 2.059   32.330 1.00 55.62  ? 370 GLN A CD  1 
ATOM 2769 O OE1 . GLN A 1 371 ? 29.665 1.398   32.409 1.00 55.34  ? 370 GLN A OE1 1 
ATOM 2770 N NE2 . GLN A 1 371 ? 30.726 3.295   31.847 1.00 51.39  ? 370 GLN A NE2 1 
ATOM 2771 N N   . PHE A 1 372 ? 34.453 -1.472  30.255 1.00 60.76  ? 371 PHE A N   1 
ATOM 2772 C CA  . PHE A 1 372 ? 34.711 -2.660  29.447 1.00 62.61  ? 371 PHE A CA  1 
ATOM 2773 C C   . PHE A 1 372 ? 35.822 -3.507  30.054 1.00 62.60  ? 371 PHE A C   1 
ATOM 2774 O O   . PHE A 1 372 ? 35.710 -4.736  30.124 1.00 64.50  ? 371 PHE A O   1 
ATOM 2775 C CB  . PHE A 1 372 ? 35.058 -2.246  28.013 1.00 65.93  ? 371 PHE A CB  1 
ATOM 2776 C CG  . PHE A 1 372 ? 35.711 -3.333  27.195 1.00 68.06  ? 371 PHE A CG  1 
ATOM 2777 C CD1 . PHE A 1 372 ? 37.092 -3.469  27.160 1.00 68.64  ? 371 PHE A CD1 1 
ATOM 2778 C CD2 . PHE A 1 372 ? 34.942 -4.204  26.443 1.00 70.83  ? 371 PHE A CD2 1 
ATOM 2779 C CE1 . PHE A 1 372 ? 37.686 -4.466  26.406 1.00 74.28  ? 371 PHE A CE1 1 
ATOM 2780 C CE2 . PHE A 1 372 ? 35.530 -5.201  25.685 1.00 72.54  ? 371 PHE A CE2 1 
ATOM 2781 C CZ  . PHE A 1 372 ? 36.903 -5.332  25.666 1.00 71.83  ? 371 PHE A CZ  1 
ATOM 2782 N N   . THR A 1 373 ? 36.902 -2.864  30.503 1.00 59.22  ? 372 THR A N   1 
ATOM 2783 C CA  . THR A 1 373 ? 38.027 -3.604  31.064 1.00 57.32  ? 372 THR A CA  1 
ATOM 2784 C C   . THR A 1 373 ? 37.644 -4.278  32.375 1.00 65.12  ? 372 THR A C   1 
ATOM 2785 O O   . THR A 1 373 ? 37.964 -5.452  32.597 1.00 77.20  ? 372 THR A O   1 
ATOM 2786 C CB  . THR A 1 373 ? 39.218 -2.668  31.270 1.00 59.20  ? 372 THR A CB  1 
ATOM 2787 O OG1 . THR A 1 373 ? 39.568 -2.060  30.021 1.00 69.35  ? 372 THR A OG1 1 
ATOM 2788 C CG2 . THR A 1 373 ? 40.415 -3.439  31.805 1.00 51.84  ? 372 THR A CG2 1 
ATOM 2789 N N   . LEU A 1 374 ? 36.957 -3.549  33.258 1.00 69.95  ? 373 LEU A N   1 
ATOM 2790 C CA  . LEU A 1 374 ? 36.525 -4.135  34.522 1.00 70.33  ? 373 LEU A CA  1 
ATOM 2791 C C   . LEU A 1 374 ? 35.564 -5.295  34.292 1.00 72.79  ? 373 LEU A C   1 
ATOM 2792 O O   . LEU A 1 374 ? 35.606 -6.299  35.013 1.00 78.32  ? 373 LEU A O   1 
ATOM 2793 C CB  . LEU A 1 374 ? 35.876 -3.065  35.400 1.00 61.74  ? 373 LEU A CB  1 
ATOM 2794 C CG  . LEU A 1 374 ? 36.789 -1.992  35.994 1.00 66.43  ? 373 LEU A CG  1 
ATOM 2795 C CD1 . LEU A 1 374 ? 35.988 -1.040  36.871 1.00 72.03  ? 373 LEU A CD1 1 
ATOM 2796 C CD2 . LEU A 1 374 ? 37.925 -2.628  36.780 1.00 72.70  ? 373 LEU A CD2 1 
ATOM 2797 N N   . LEU A 1 375 ? 34.695 -5.176  33.287 1.00 67.20  ? 374 LEU A N   1 
ATOM 2798 C CA  . LEU A 1 375 ? 33.762 -6.254  32.975 1.00 63.60  ? 374 LEU A CA  1 
ATOM 2799 C C   . LEU A 1 375 ? 34.493 -7.491  32.470 1.00 73.24  ? 374 LEU A C   1 
ATOM 2800 O O   . LEU A 1 375 ? 34.151 -8.619  32.845 1.00 79.99  ? 374 LEU A O   1 
ATOM 2801 C CB  . LEU A 1 375 ? 32.744 -5.772  31.942 1.00 63.38  ? 374 LEU A CB  1 
ATOM 2802 C CG  . LEU A 1 375 ? 31.485 -5.080  32.466 1.00 64.99  ? 374 LEU A CG  1 
ATOM 2803 C CD1 . LEU A 1 375 ? 30.633 -4.609  31.304 1.00 71.78  ? 374 LEU A CD1 1 
ATOM 2804 C CD2 . LEU A 1 375 ? 30.689 -6.011  33.366 1.00 67.26  ? 374 LEU A CD2 1 
ATOM 2805 N N   . MET A 1 376 ? 35.507 -7.297  31.625 1.00 69.75  ? 375 MET A N   1 
ATOM 2806 C CA  . MET A 1 376 ? 36.208 -8.428  31.023 1.00 71.28  ? 375 MET A CA  1 
ATOM 2807 C C   . MET A 1 376 ? 36.983 -9.221  32.068 1.00 76.57  ? 375 MET A C   1 
ATOM 2808 O O   . MET A 1 376 ? 36.883 -10.452 32.126 1.00 79.30  ? 375 MET A O   1 
ATOM 2809 C CB  . MET A 1 376 ? 37.146 -7.932  29.922 1.00 70.51  ? 375 MET A CB  1 
ATOM 2810 C CG  . MET A 1 376 ? 36.547 -7.975  28.527 1.00 72.83  ? 375 MET A CG  1 
ATOM 2811 S SD  . MET A 1 376 ? 35.545 -9.447  28.253 1.00 89.07  ? 375 MET A SD  1 
ATOM 2812 C CE  . MET A 1 376 ? 34.004 -8.710  27.735 1.00 67.98  ? 375 MET A CE  1 
ATOM 2813 N N   . VAL A 1 377 ? 37.765 -8.533  32.902 1.00 75.72  ? 376 VAL A N   1 
ATOM 2814 C CA  . VAL A 1 377 ? 38.618 -9.230  33.859 1.00 81.64  ? 376 VAL A CA  1 
ATOM 2815 C C   . VAL A 1 377 ? 37.778 -9.942  34.913 1.00 80.28  ? 376 VAL A C   1 
ATOM 2816 O O   . VAL A 1 377 ? 38.104 -11.059 35.335 1.00 80.73  ? 376 VAL A O   1 
ATOM 2817 C CB  . VAL A 1 377 ? 39.626 -8.249  34.489 1.00 72.11  ? 376 VAL A CB  1 
ATOM 2818 C CG1 . VAL A 1 377 ? 38.907 -7.108  35.192 1.00 65.96  ? 376 VAL A CG1 1 
ATOM 2819 C CG2 . VAL A 1 377 ? 40.551 -8.978  35.453 1.00 68.75  ? 376 VAL A CG2 1 
ATOM 2820 N N   . PHE A 1 378 ? 36.676 -9.324  35.339 1.00 82.11  ? 377 PHE A N   1 
ATOM 2821 C CA  . PHE A 1 378 ? 35.848 -9.917  36.383 1.00 82.12  ? 377 PHE A CA  1 
ATOM 2822 C C   . PHE A 1 378 ? 35.022 -11.082 35.858 1.00 75.84  ? 377 PHE A C   1 
ATOM 2823 O O   . PHE A 1 378 ? 34.718 -12.010 36.615 1.00 78.07  ? 377 PHE A O   1 
ATOM 2824 C CB  . PHE A 1 378 ? 34.948 -8.845  36.997 1.00 77.48  ? 377 PHE A CB  1 
ATOM 2825 C CG  . PHE A 1 378 ? 35.666 -7.935  37.954 1.00 84.99  ? 377 PHE A CG  1 
ATOM 2826 C CD1 . PHE A 1 378 ? 35.044 -6.811  38.467 1.00 84.71  ? 377 PHE A CD1 1 
ATOM 2827 C CD2 . PHE A 1 378 ? 36.968 -8.209  38.342 1.00 95.06  ? 377 PHE A CD2 1 
ATOM 2828 C CE1 . PHE A 1 378 ? 35.707 -5.975  39.347 1.00 88.34  ? 377 PHE A CE1 1 
ATOM 2829 C CE2 . PHE A 1 378 ? 37.635 -7.378  39.222 1.00 100.33 ? 377 PHE A CE2 1 
ATOM 2830 C CZ  . PHE A 1 378 ? 37.003 -6.260  39.726 1.00 88.34  ? 377 PHE A CZ  1 
ATOM 2831 N N   . ALA A 1 379 ? 34.659 -11.058 34.576 1.00 72.00  ? 378 ALA A N   1 
ATOM 2832 C CA  . ALA A 1 379 ? 34.000 -12.214 33.980 1.00 77.45  ? 378 ALA A CA  1 
ATOM 2833 C C   . ALA A 1 379 ? 34.973 -13.376 33.833 1.00 77.03  ? 378 ALA A C   1 
ATOM 2834 O O   . ALA A 1 379 ? 34.664 -14.510 34.213 1.00 72.19  ? 378 ALA A O   1 
ATOM 2835 C CB  . ALA A 1 379 ? 33.399 -11.836 32.626 1.00 72.01  ? 378 ALA A CB  1 
ATOM 2836 N N   . HIS A 1 380 ? 36.167 -13.106 33.298 1.00 75.45  ? 379 HIS A N   1 
ATOM 2837 C CA  . HIS A 1 380 ? 37.166 -14.155 33.119 1.00 78.58  ? 379 HIS A CA  1 
ATOM 2838 C C   . HIS A 1 380 ? 37.481 -14.868 34.430 1.00 80.41  ? 379 HIS A C   1 
ATOM 2839 O O   . HIS A 1 380 ? 37.791 -16.064 34.426 1.00 83.49  ? 379 HIS A O   1 
ATOM 2840 C CB  . HIS A 1 380 ? 38.438 -13.557 32.517 1.00 80.79  ? 379 HIS A CB  1 
ATOM 2841 C CG  . HIS A 1 380 ? 39.527 -14.556 32.279 1.00 101.15 ? 379 HIS A CG  1 
ATOM 2842 N ND1 . HIS A 1 380 ? 40.848 -14.300 32.579 1.00 105.47 ? 379 HIS A ND1 1 
ATOM 2843 C CD2 . HIS A 1 380 ? 39.494 -15.808 31.764 1.00 98.60  ? 379 HIS A CD2 1 
ATOM 2844 C CE1 . HIS A 1 380 ? 41.581 -15.352 32.263 1.00 96.24  ? 379 HIS A CE1 1 
ATOM 2845 N NE2 . HIS A 1 380 ? 40.784 -16.281 31.766 1.00 94.53  ? 379 HIS A NE2 1 
ATOM 2846 N N   . TRP A 1 381 ? 37.395 -14.158 35.556 1.00 91.49  ? 380 TRP A N   1 
ATOM 2847 C CA  . TRP A 1 381 ? 37.646 -14.775 36.852 1.00 97.51  ? 380 TRP A CA  1 
ATOM 2848 C C   . TRP A 1 381 ? 36.411 -15.483 37.401 1.00 96.31  ? 380 TRP A C   1 
ATOM 2849 O O   . TRP A 1 381 ? 36.545 -16.482 38.115 1.00 99.79  ? 380 TRP A O   1 
ATOM 2850 C CB  . TRP A 1 381 ? 38.131 -13.719 37.849 1.00 100.76 ? 380 TRP A CB  1 
ATOM 2851 C CG  . TRP A 1 381 ? 38.794 -14.279 39.077 1.00 115.23 ? 380 TRP A CG  1 
ATOM 2852 C CD1 . TRP A 1 381 ? 38.223 -14.458 40.304 1.00 114.72 ? 380 TRP A CD1 1 
ATOM 2853 C CD2 . TRP A 1 381 ? 40.155 -14.711 39.202 1.00 122.75 ? 380 TRP A CD2 1 
ATOM 2854 N NE1 . TRP A 1 381 ? 39.140 -14.984 41.181 1.00 117.91 ? 380 TRP A NE1 1 
ATOM 2855 C CE2 . TRP A 1 381 ? 40.334 -15.148 40.530 1.00 121.79 ? 380 TRP A CE2 1 
ATOM 2856 C CE3 . TRP A 1 381 ? 41.238 -14.776 38.319 1.00 123.95 ? 380 TRP A CE3 1 
ATOM 2857 C CZ2 . TRP A 1 381 ? 41.551 -15.643 40.996 1.00 124.01 ? 380 TRP A CZ2 1 
ATOM 2858 C CZ3 . TRP A 1 381 ? 42.446 -15.268 38.785 1.00 123.52 ? 380 TRP A CZ3 1 
ATOM 2859 C CH2 . TRP A 1 381 ? 42.592 -15.694 40.111 1.00 123.78 ? 380 TRP A CH2 1 
ATOM 2860 N N   . LEU A 1 382 ? 35.213 -14.999 37.074 1.00 76.26  ? 381 LEU A N   1 
ATOM 2861 C CA  . LEU A 1 382 ? 33.986 -15.483 37.689 1.00 71.01  ? 381 LEU A CA  1 
ATOM 2862 C C   . LEU A 1 382 ? 33.089 -16.281 36.755 1.00 72.30  ? 381 LEU A C   1 
ATOM 2863 O O   . LEU A 1 382 ? 32.342 -17.140 37.232 1.00 76.30  ? 381 LEU A O   1 
ATOM 2864 C CB  . LEU A 1 382 ? 33.185 -14.308 38.268 1.00 71.55  ? 381 LEU A CB  1 
ATOM 2865 C CG  . LEU A 1 382 ? 33.846 -13.542 39.416 1.00 70.03  ? 381 LEU A CG  1 
ATOM 2866 C CD1 . LEU A 1 382 ? 33.030 -12.309 39.760 1.00 64.38  ? 381 LEU A CD1 1 
ATOM 2867 C CD2 . LEU A 1 382 ? 34.022 -14.432 40.641 1.00 67.48  ? 381 LEU A CD2 1 
ATOM 2868 N N   . ILE A 1 383 ? 33.135 -16.025 35.445 1.00 77.48  ? 382 ILE A N   1 
ATOM 2869 C CA  . ILE A 1 383 ? 32.267 -16.757 34.517 1.00 70.75  ? 382 ILE A CA  1 
ATOM 2870 C C   . ILE A 1 383 ? 32.576 -18.250 34.510 1.00 65.83  ? 382 ILE A C   1 
ATOM 2871 O O   . ILE A 1 383 ? 31.652 -19.051 34.739 1.00 59.94  ? 382 ILE A O   1 
ATOM 2872 C CB  . ILE A 1 383 ? 32.336 -16.125 33.114 1.00 70.12  ? 382 ILE A CB  1 
ATOM 2873 C CG1 . ILE A 1 383 ? 31.506 -14.835 33.068 1.00 66.20  ? 382 ILE A CG1 1 
ATOM 2874 C CG2 . ILE A 1 383 ? 31.848 -17.106 32.054 1.00 65.39  ? 382 ILE A CG2 1 
ATOM 2875 C CD1 . ILE A 1 383 ? 30.038 -15.060 32.863 1.00 59.08  ? 382 ILE A CD1 1 
ATOM 2876 N N   . PRO A 1 384 ? 33.820 -18.701 34.284 1.00 70.12  ? 383 PRO A N   1 
ATOM 2877 C CA  . PRO A 1 384 ? 34.064 -20.153 34.246 1.00 72.31  ? 383 PRO A CA  1 
ATOM 2878 C C   . PRO A 1 384 ? 33.784 -20.850 35.564 1.00 67.81  ? 383 PRO A C   1 
ATOM 2879 O O   . PRO A 1 384 ? 33.528 -22.060 35.568 1.00 73.12  ? 383 PRO A O   1 
ATOM 2880 C CB  . PRO A 1 384 ? 35.548 -20.253 33.865 1.00 70.62  ? 383 PRO A CB  1 
ATOM 2881 C CG  . PRO A 1 384 ? 35.899 -18.926 33.280 1.00 74.96  ? 383 PRO A CG  1 
ATOM 2882 C CD  . PRO A 1 384 ? 35.066 -17.949 34.045 1.00 73.31  ? 383 PRO A CD  1 
ATOM 2883 N N   . ALA A 1 385 ? 33.820 -20.126 36.682 1.00 66.97  ? 384 ALA A N   1 
ATOM 2884 C CA  . ALA A 1 385 ? 33.599 -20.723 37.994 1.00 64.22  ? 384 ALA A CA  1 
ATOM 2885 C C   . ALA A 1 385 ? 32.114 -20.778 38.348 1.00 68.89  ? 384 ALA A C   1 
ATOM 2886 O O   . ALA A 1 385 ? 31.548 -21.863 38.512 1.00 69.93  ? 384 ALA A O   1 
ATOM 2887 C CB  . ALA A 1 385 ? 34.381 -19.940 39.055 1.00 69.53  ? 384 ALA A CB  1 
ATOM 2888 N N   . HIS A 1 386 ? 31.470 -19.616 38.456 1.00 68.81  ? 385 HIS A N   1 
ATOM 2889 C CA  . HIS A 1 386 ? 30.107 -19.536 38.965 1.00 71.41  ? 385 HIS A CA  1 
ATOM 2890 C C   . HIS A 1 386 ? 29.048 -19.431 37.873 1.00 65.85  ? 385 HIS A C   1 
ATOM 2891 O O   . HIS A 1 386 ? 27.854 -19.466 38.190 1.00 59.91  ? 385 HIS A O   1 
ATOM 2892 C CB  . HIS A 1 386 ? 29.973 -18.346 39.924 1.00 67.38  ? 385 HIS A CB  1 
ATOM 2893 C CG  . HIS A 1 386 ? 30.877 -18.422 41.117 1.00 71.54  ? 385 HIS A CG  1 
ATOM 2894 N ND1 . HIS A 1 386 ? 32.240 -18.235 41.031 1.00 75.08  ? 385 HIS A ND1 1 
ATOM 2895 C CD2 . HIS A 1 386 ? 30.612 -18.658 42.423 1.00 74.53  ? 385 HIS A CD2 1 
ATOM 2896 C CE1 . HIS A 1 386 ? 32.776 -18.356 42.233 1.00 67.79  ? 385 HIS A CE1 1 
ATOM 2897 N NE2 . HIS A 1 386 ? 31.809 -18.613 43.095 1.00 77.74  ? 385 HIS A NE2 1 
ATOM 2898 N N   . GLY A 1 387 ? 29.443 -19.301 36.610 1.00 61.70  ? 386 GLY A N   1 
ATOM 2899 C CA  . GLY A 1 387 ? 28.456 -19.305 35.539 1.00 59.20  ? 386 GLY A CA  1 
ATOM 2900 C C   . GLY A 1 387 ? 27.641 -18.027 35.517 1.00 59.05  ? 386 GLY A C   1 
ATOM 2901 O O   . GLY A 1 387 ? 28.182 -16.919 35.603 1.00 66.63  ? 386 GLY A O   1 
ATOM 2902 N N   . ALA A 1 388 ? 26.318 -18.176 35.384 1.00 53.96  ? 387 ALA A N   1 
ATOM 2903 C CA  . ALA A 1 388 ? 25.444 -17.010 35.278 1.00 57.27  ? 387 ALA A CA  1 
ATOM 2904 C C   . ALA A 1 388 ? 25.511 -16.151 36.531 1.00 68.89  ? 387 ALA A C   1 
ATOM 2905 O O   . ALA A 1 388 ? 25.488 -14.917 36.450 1.00 61.01  ? 387 ALA A O   1 
ATOM 2906 C CB  . ALA A 1 388 ? 24.005 -17.445 35.008 1.00 55.91  ? 387 ALA A CB  1 
ATOM 2907 N N   . LEU A 1 389 ? 25.584 -16.785 37.703 1.00 73.36  ? 388 LEU A N   1 
ATOM 2908 C CA  . LEU A 1 389 ? 25.763 -16.023 38.933 1.00 74.55  ? 388 LEU A CA  1 
ATOM 2909 C C   . LEU A 1 389 ? 27.096 -15.288 38.927 1.00 76.39  ? 388 LEU A C   1 
ATOM 2910 O O   . LEU A 1 389 ? 27.185 -14.145 39.389 1.00 79.66  ? 388 LEU A O   1 
ATOM 2911 C CB  . LEU A 1 389 ? 25.661 -16.945 40.145 1.00 76.85  ? 388 LEU A CB  1 
ATOM 2912 C CG  . LEU A 1 389 ? 25.687 -16.244 41.503 1.00 75.30  ? 388 LEU A CG  1 
ATOM 2913 C CD1 . LEU A 1 389 ? 24.571 -15.215 41.596 1.00 74.85  ? 388 LEU A CD1 1 
ATOM 2914 C CD2 . LEU A 1 389 ? 25.580 -17.260 42.624 1.00 75.57  ? 388 LEU A CD2 1 
ATOM 2915 N N   . GLY A 1 390 ? 28.143 -15.925 38.396 1.00 73.90  ? 389 GLY A N   1 
ATOM 2916 C CA  . GLY A 1 390 ? 29.425 -15.253 38.275 1.00 74.16  ? 389 GLY A CA  1 
ATOM 2917 C C   . GLY A 1 390 ? 29.371 -14.041 37.367 1.00 75.76  ? 389 GLY A C   1 
ATOM 2918 O O   . GLY A 1 390 ? 30.157 -13.104 37.528 1.00 81.14  ? 389 GLY A O   1 
ATOM 2919 N N   . ALA A 1 391 ? 28.446 -14.040 36.405 1.00 63.18  ? 390 ALA A N   1 
ATOM 2920 C CA  . ALA A 1 391 ? 28.264 -12.866 35.560 1.00 64.40  ? 390 ALA A CA  1 
ATOM 2921 C C   . ALA A 1 391 ? 27.608 -11.731 36.333 1.00 67.29  ? 390 ALA A C   1 
ATOM 2922 O O   . ALA A 1 391 ? 27.994 -10.566 36.185 1.00 65.05  ? 390 ALA A O   1 
ATOM 2923 C CB  . ALA A 1 391 ? 27.432 -13.227 34.333 1.00 64.26  ? 390 ALA A CB  1 
ATOM 2924 N N   . ALA A 1 392 ? 26.609 -12.052 37.159 1.00 67.24  ? 391 ALA A N   1 
ATOM 2925 C CA  . ALA A 1 392 ? 26.013 -11.040 38.023 1.00 61.35  ? 391 ALA A CA  1 
ATOM 2926 C C   . ALA A 1 392 ? 27.012 -10.557 39.066 1.00 66.80  ? 391 ALA A C   1 
ATOM 2927 O O   . ALA A 1 392 ? 27.029 -9.370  39.416 1.00 66.46  ? 391 ALA A O   1 
ATOM 2928 C CB  . ALA A 1 392 ? 24.757 -11.595 38.693 1.00 58.43  ? 391 ALA A CB  1 
ATOM 2929 N N   . GLN A 1 393 ? 27.853 -11.463 39.575 1.00 66.67  ? 392 GLN A N   1 
ATOM 2930 C CA  . GLN A 1 393 ? 28.912 -11.054 40.491 1.00 68.76  ? 392 GLN A CA  1 
ATOM 2931 C C   . GLN A 1 393 ? 29.912 -10.142 39.794 1.00 61.16  ? 392 GLN A C   1 
ATOM 2932 O O   . GLN A 1 393 ? 30.431 -9.197  40.401 1.00 72.39  ? 392 GLN A O   1 
ATOM 2933 C CB  . GLN A 1 393 ? 29.618 -12.282 41.067 1.00 64.86  ? 392 GLN A CB  1 
ATOM 2934 C CG  . GLN A 1 393 ? 28.730 -13.183 41.909 1.00 61.75  ? 392 GLN A CG  1 
ATOM 2935 C CD  . GLN A 1 393 ? 29.327 -14.564 42.111 1.00 66.62  ? 392 GLN A CD  1 
ATOM 2936 O OE1 . GLN A 1 393 ? 30.351 -14.903 41.517 1.00 66.75  ? 392 GLN A OE1 1 
ATOM 2937 N NE2 . GLN A 1 393 ? 28.685 -15.370 42.948 1.00 65.00  ? 392 GLN A NE2 1 
ATOM 2938 N N   . ALA A 1 394 ? 30.199 -10.412 38.520 1.00 61.09  ? 393 ALA A N   1 
ATOM 2939 C CA  . ALA A 1 394 ? 31.044 -9.512  37.744 1.00 69.29  ? 393 ALA A CA  1 
ATOM 2940 C C   . ALA A 1 394 ? 30.392 -8.142  37.612 1.00 73.98  ? 393 ALA A C   1 
ATOM 2941 O O   . ALA A 1 394 ? 30.981 -7.121  37.981 1.00 78.24  ? 393 ALA A O   1 
ATOM 2942 C CB  . ALA A 1 394 ? 31.327 -10.115 36.366 1.00 62.35  ? 393 ALA A CB  1 
ATOM 2943 N N   . TYR A 1 395 ? 29.154 -8.112  37.108 1.00 67.57  ? 394 TYR A N   1 
ATOM 2944 C CA  . TYR A 1 395 ? 28.433 -6.858  36.899 1.00 57.37  ? 394 TYR A CA  1 
ATOM 2945 C C   . TYR A 1 395 ? 28.479 -5.957  38.128 1.00 70.02  ? 394 TYR A C   1 
ATOM 2946 O O   . TYR A 1 395 ? 28.695 -4.745  38.009 1.00 79.94  ? 394 TYR A O   1 
ATOM 2947 C CB  . TYR A 1 395 ? 26.986 -7.167  36.514 1.00 59.01  ? 394 TYR A CB  1 
ATOM 2948 C CG  . TYR A 1 395 ? 26.113 -5.955  36.297 1.00 66.50  ? 394 TYR A CG  1 
ATOM 2949 C CD1 . TYR A 1 395 ? 26.131 -5.263  35.094 1.00 77.88  ? 394 TYR A CD1 1 
ATOM 2950 C CD2 . TYR A 1 395 ? 25.261 -5.510  37.297 1.00 64.36  ? 394 TYR A CD2 1 
ATOM 2951 C CE1 . TYR A 1 395 ? 25.323 -4.159  34.895 1.00 74.43  ? 394 TYR A CE1 1 
ATOM 2952 C CE2 . TYR A 1 395 ? 24.457 -4.410  37.111 1.00 67.99  ? 394 TYR A CE2 1 
ATOM 2953 C CZ  . TYR A 1 395 ? 24.490 -3.737  35.909 1.00 69.71  ? 394 TYR A CZ  1 
ATOM 2954 O OH  . TYR A 1 395 ? 23.684 -2.639  35.723 1.00 64.95  ? 394 TYR A OH  1 
ATOM 2955 N N   . MET A 1 396 ? 28.285 -6.528  39.320 1.00 72.62  ? 395 MET A N   1 
ATOM 2956 C CA  . MET A 1 396 ? 28.373 -5.729  40.539 1.00 63.92  ? 395 MET A CA  1 
ATOM 2957 C C   . MET A 1 396 ? 29.792 -5.223  40.766 1.00 64.73  ? 395 MET A C   1 
ATOM 2958 O O   . MET A 1 396 ? 30.005 -4.031  41.019 1.00 72.03  ? 395 MET A O   1 
ATOM 2959 C CB  . MET A 1 396 ? 27.915 -6.545  41.749 1.00 57.37  ? 395 MET A CB  1 
ATOM 2960 C CG  . MET A 1 396 ? 28.636 -6.127  43.028 1.00 68.91  ? 395 MET A CG  1 
ATOM 2961 S SD  . MET A 1 396 ? 28.330 -7.113  44.502 1.00 64.71  ? 395 MET A SD  1 
ATOM 2962 C CE  . MET A 1 396 ? 26.570 -7.368  44.397 1.00 50.51  ? 395 MET A CE  1 
ATOM 2963 N N   . ALA A 1 397 ? 30.779 -6.119  40.674 1.00 61.03  ? 396 ALA A N   1 
ATOM 2964 C CA  . ALA A 1 397 ? 32.126 -5.789  41.123 1.00 71.60  ? 396 ALA A CA  1 
ATOM 2965 C C   . ALA A 1 397 ? 32.785 -4.733  40.245 1.00 75.75  ? 396 ALA A C   1 
ATOM 2966 O O   . ALA A 1 397 ? 33.600 -3.947  40.740 1.00 77.59  ? 396 ALA A O   1 
ATOM 2967 C CB  . ALA A 1 397 ? 32.981 -7.054  41.180 1.00 64.54  ? 396 ALA A CB  1 
ATOM 2968 N N   . THR A 1 398 ? 32.462 -4.696  38.950 1.00 91.86  ? 397 THR A N   1 
ATOM 2969 C CA  . THR A 1 398 ? 32.979 -3.623  38.104 1.00 92.75  ? 397 THR A CA  1 
ATOM 2970 C C   . THR A 1 398 ? 32.435 -2.273  38.546 1.00 91.77  ? 397 THR A C   1 
ATOM 2971 O O   . THR A 1 398 ? 33.194 -1.314  38.729 1.00 93.37  ? 397 THR A O   1 
ATOM 2972 C CB  . THR A 1 398 ? 32.637 -3.875  36.634 1.00 91.95  ? 397 THR A CB  1 
ATOM 2973 O OG1 . THR A 1 398 ? 31.324 -3.374  36.348 1.00 91.13  ? 397 THR A OG1 1 
ATOM 2974 C CG2 . THR A 1 398 ? 32.720 -5.348  36.300 1.00 90.32  ? 397 THR A CG2 1 
ATOM 2975 N N   . TYR A 1 399 ? 31.119 -2.180  38.724 1.00 77.84  ? 398 TYR A N   1 
ATOM 2976 C CA  . TYR A 1 399 ? 30.500 -0.920  39.107 1.00 81.19  ? 398 TYR A CA  1 
ATOM 2977 C C   . TYR A 1 399 ? 30.716 -0.579  40.576 1.00 77.30  ? 398 TYR A C   1 
ATOM 2978 O O   . TYR A 1 399 ? 30.459 0.562   40.972 1.00 78.73  ? 398 TYR A O   1 
ATOM 2979 C CB  . TYR A 1 399 ? 29.009 -0.956  38.766 1.00 79.82  ? 398 TYR A CB  1 
ATOM 2980 C CG  . TYR A 1 399 ? 28.765 -0.957  37.271 1.00 85.78  ? 398 TYR A CG  1 
ATOM 2981 C CD1 . TYR A 1 399 ? 29.693 -0.397  36.401 1.00 78.80  ? 398 TYR A CD1 1 
ATOM 2982 C CD2 . TYR A 1 399 ? 27.624 -1.532  36.727 1.00 82.26  ? 398 TYR A CD2 1 
ATOM 2983 C CE1 . TYR A 1 399 ? 29.488 -0.398  35.035 1.00 81.49  ? 398 TYR A CE1 1 
ATOM 2984 C CE2 . TYR A 1 399 ? 27.411 -1.537  35.358 1.00 82.63  ? 398 TYR A CE2 1 
ATOM 2985 C CZ  . TYR A 1 399 ? 28.346 -0.967  34.517 1.00 84.38  ? 398 TYR A CZ  1 
ATOM 2986 O OH  . TYR A 1 399 ? 28.144 -0.966  33.154 1.00 72.88  ? 398 TYR A OH  1 
ATOM 2987 N N   . ILE A 1 400 ? 31.181 -1.532  41.387 1.00 69.73  ? 399 ILE A N   1 
ATOM 2988 C CA  . ILE A 1 400 ? 31.740 -1.180  42.689 1.00 68.89  ? 399 ILE A CA  1 
ATOM 2989 C C   . ILE A 1 400 ? 33.025 -0.388  42.501 1.00 70.76  ? 399 ILE A C   1 
ATOM 2990 O O   . ILE A 1 400 ? 33.193 0.706   43.055 1.00 69.76  ? 399 ILE A O   1 
ATOM 2991 C CB  . ILE A 1 400 ? 31.982 -2.440  43.541 1.00 66.44  ? 399 ILE A CB  1 
ATOM 2992 C CG1 . ILE A 1 400 ? 30.670 -2.993  44.098 1.00 65.34  ? 399 ILE A CG1 1 
ATOM 2993 C CG2 . ILE A 1 400 ? 32.939 -2.130  44.683 1.00 56.97  ? 399 ILE A CG2 1 
ATOM 2994 C CD1 . ILE A 1 400 ? 30.854 -4.140  45.068 1.00 61.11  ? 399 ILE A CD1 1 
ATOM 2995 N N   . VAL A 1 401 ? 33.948 -0.929  41.705 1.00 63.14  ? 400 VAL A N   1 
ATOM 2996 C CA  . VAL A 1 401 ? 35.195 -0.231  41.418 1.00 72.28  ? 400 VAL A CA  1 
ATOM 2997 C C   . VAL A 1 401 ? 34.930 1.008   40.571 1.00 73.25  ? 400 VAL A C   1 
ATOM 2998 O O   . VAL A 1 401 ? 35.573 2.049   40.754 1.00 69.85  ? 400 VAL A O   1 
ATOM 2999 C CB  . VAL A 1 401 ? 36.187 -1.188  40.733 1.00 67.20  ? 400 VAL A CB  1 
ATOM 3000 C CG1 . VAL A 1 401 ? 37.524 -0.503  40.500 1.00 69.40  ? 400 VAL A CG1 1 
ATOM 3001 C CG2 . VAL A 1 401 ? 36.365 -2.446  41.566 1.00 58.31  ? 400 VAL A CG2 1 
ATOM 3002 N N   . TYR A 1 402 ? 33.975 0.924   39.642 1.00 68.69  ? 401 TYR A N   1 
ATOM 3003 C CA  . TYR A 1 402 ? 33.711 2.049   38.750 1.00 73.73  ? 401 TYR A CA  1 
ATOM 3004 C C   . TYR A 1 402 ? 33.154 3.244   39.515 1.00 72.82  ? 401 TYR A C   1 
ATOM 3005 O O   . TYR A 1 402 ? 33.620 4.376   39.340 1.00 68.07  ? 401 TYR A O   1 
ATOM 3006 C CB  . TYR A 1 402 ? 32.752 1.628   37.636 1.00 71.01  ? 401 TYR A CB  1 
ATOM 3007 C CG  . TYR A 1 402 ? 32.585 2.679   36.564 1.00 68.99  ? 401 TYR A CG  1 
ATOM 3008 C CD1 . TYR A 1 402 ? 33.690 3.213   35.913 1.00 63.70  ? 401 TYR A CD1 1 
ATOM 3009 C CD2 . TYR A 1 402 ? 31.326 3.145   36.210 1.00 62.50  ? 401 TYR A CD2 1 
ATOM 3010 C CE1 . TYR A 1 402 ? 33.545 4.176   34.936 1.00 54.79  ? 401 TYR A CE1 1 
ATOM 3011 C CE2 . TYR A 1 402 ? 31.172 4.110   35.235 1.00 57.49  ? 401 TYR A CE2 1 
ATOM 3012 C CZ  . TYR A 1 402 ? 32.285 4.622   34.601 1.00 58.47  ? 401 TYR A CZ  1 
ATOM 3013 O OH  . TYR A 1 402 ? 32.138 5.583   33.630 1.00 64.01  ? 401 TYR A OH  1 
ATOM 3014 N N   . PHE A 1 403 ? 32.149 3.013   40.363 1.00 68.87  ? 402 PHE A N   1 
ATOM 3015 C CA  . PHE A 1 403 ? 31.601 4.097   41.173 1.00 73.68  ? 402 PHE A CA  1 
ATOM 3016 C C   . PHE A 1 403 ? 32.672 4.699   42.073 1.00 70.92  ? 402 PHE A C   1 
ATOM 3017 O O   . PHE A 1 403 ? 32.791 5.925   42.183 1.00 68.41  ? 402 PHE A O   1 
ATOM 3018 C CB  . PHE A 1 403 ? 30.422 3.592   42.004 1.00 66.85  ? 402 PHE A CB  1 
ATOM 3019 C CG  . PHE A 1 403 ? 29.579 4.689   42.584 1.00 73.20  ? 402 PHE A CG  1 
ATOM 3020 C CD1 . PHE A 1 403 ? 28.429 5.112   41.939 1.00 71.51  ? 402 PHE A CD1 1 
ATOM 3021 C CD2 . PHE A 1 403 ? 29.932 5.296   43.777 1.00 80.26  ? 402 PHE A CD2 1 
ATOM 3022 C CE1 . PHE A 1 403 ? 27.653 6.121   42.474 1.00 73.32  ? 402 PHE A CE1 1 
ATOM 3023 C CE2 . PHE A 1 403 ? 29.158 6.305   44.314 1.00 83.51  ? 402 PHE A CE2 1 
ATOM 3024 C CZ  . PHE A 1 403 ? 28.015 6.717   43.661 1.00 78.24  ? 402 PHE A CZ  1 
ATOM 3025 N N   . SER A 1 404 ? 33.459 3.845   42.731 1.00 65.94  ? 403 SER A N   1 
ATOM 3026 C CA  . SER A 1 404 ? 34.536 4.333   43.586 1.00 64.74  ? 403 SER A CA  1 
ATOM 3027 C C   . SER A 1 404 ? 35.554 5.129   42.780 1.00 72.69  ? 403 SER A C   1 
ATOM 3028 O O   . SER A 1 404 ? 35.978 6.215   43.191 1.00 85.86  ? 403 SER A O   1 
ATOM 3029 C CB  . SER A 1 404 ? 35.212 3.158   44.293 1.00 64.37  ? 403 SER A CB  1 
ATOM 3030 O OG  . SER A 1 404 ? 34.251 2.294   44.873 1.00 66.64  ? 403 SER A OG  1 
ATOM 3031 N N   . LEU A 1 405 ? 35.954 4.603   41.621 1.00 71.96  ? 404 LEU A N   1 
ATOM 3032 C CA  . LEU A 1 405 ? 36.939 5.297   40.798 1.00 74.64  ? 404 LEU A CA  1 
ATOM 3033 C C   . LEU A 1 405 ? 36.374 6.595   40.235 1.00 78.92  ? 404 LEU A C   1 
ATOM 3034 O O   . LEU A 1 405 ? 37.095 7.593   40.121 1.00 82.66  ? 404 LEU A O   1 
ATOM 3035 C CB  . LEU A 1 405 ? 37.420 4.385   39.669 1.00 73.26  ? 404 LEU A CB  1 
ATOM 3036 C CG  . LEU A 1 405 ? 38.681 3.550   39.915 1.00 75.12  ? 404 LEU A CG  1 
ATOM 3037 C CD1 . LEU A 1 405 ? 39.925 4.393   39.683 1.00 73.26  ? 404 LEU A CD1 1 
ATOM 3038 C CD2 . LEU A 1 405 ? 38.699 2.933   41.311 1.00 63.85  ? 404 LEU A CD2 1 
ATOM 3039 N N   . CYS A 1 406 ? 35.087 6.602   39.879 1.00 80.87  ? 405 CYS A N   1 
ATOM 3040 C CA  . CYS A 1 406 ? 34.477 7.815   39.343 1.00 84.73  ? 405 CYS A CA  1 
ATOM 3041 C C   . CYS A 1 406 ? 34.462 8.929   40.380 1.00 86.95  ? 405 CYS A C   1 
ATOM 3042 O O   . CYS A 1 406 ? 34.725 10.093  40.056 1.00 94.03  ? 405 CYS A O   1 
ATOM 3043 C CB  . CYS A 1 406 ? 33.059 7.522   38.853 1.00 84.56  ? 405 CYS A CB  1 
ATOM 3044 S SG  . CYS A 1 406 ? 32.973 6.748   37.224 1.00 90.39  ? 405 CYS A SG  1 
ATOM 3045 N N   . CYS A 1 407 ? 34.152 8.594   41.633 1.00 82.32  ? 406 CYS A N   1 
ATOM 3046 C CA  . CYS A 1 407 ? 34.171 9.602   42.687 1.00 84.20  ? 406 CYS A CA  1 
ATOM 3047 C C   . CYS A 1 407 ? 35.589 10.088  42.958 1.00 86.18  ? 406 CYS A C   1 
ATOM 3048 O O   . CYS A 1 407 ? 35.799 11.269  43.260 1.00 85.59  ? 406 CYS A O   1 
ATOM 3049 C CB  . CYS A 1 407 ? 33.545 9.038   43.961 1.00 79.65  ? 406 CYS A CB  1 
ATOM 3050 S SG  . CYS A 1 407 ? 31.800 8.611   43.801 1.00 76.18  ? 406 CYS A SG  1 
ATOM 3051 N N   . GLY A 1 408 ? 36.572 9.193   42.852 1.00 91.25  ? 407 GLY A N   1 
ATOM 3052 C CA  . GLY A 1 408 ? 37.948 9.589   43.104 1.00 90.63  ? 407 GLY A CA  1 
ATOM 3053 C C   . GLY A 1 408 ? 38.469 10.565  42.067 1.00 86.56  ? 407 GLY A C   1 
ATOM 3054 O O   . GLY A 1 408 ? 39.057 11.596  42.407 1.00 91.14  ? 407 GLY A O   1 
ATOM 3055 N N   . VAL A 1 409 ? 38.260 10.256  40.785 1.00 92.19  ? 408 VAL A N   1 
ATOM 3056 C CA  . VAL A 1 409 ? 38.671 11.178  39.735 1.00 94.40  ? 408 VAL A CA  1 
ATOM 3057 C C   . VAL A 1 409 ? 37.852 12.460  39.774 1.00 89.77  ? 408 VAL A C   1 
ATOM 3058 O O   . VAL A 1 409 ? 38.310 13.494  39.278 1.00 90.58  ? 408 VAL A O   1 
ATOM 3059 C CB  . VAL A 1 409 ? 38.580 10.517  38.345 1.00 91.07  ? 408 VAL A CB  1 
ATOM 3060 C CG1 . VAL A 1 409 ? 39.290 9.171   38.346 1.00 85.72  ? 408 VAL A CG1 1 
ATOM 3061 C CG2 . VAL A 1 409 ? 37.130 10.364  37.907 1.00 81.84  ? 408 VAL A CG2 1 
ATOM 3062 N N   . PHE A 1 410 ? 36.653 12.424  40.359 1.00 90.75  ? 409 PHE A N   1 
ATOM 3063 C CA  . PHE A 1 410 ? 35.866 13.645  40.496 1.00 92.98  ? 409 PHE A CA  1 
ATOM 3064 C C   . PHE A 1 410 ? 36.504 14.591  41.505 1.00 93.40  ? 409 PHE A C   1 
ATOM 3065 O O   . PHE A 1 410 ? 36.702 15.777  41.218 1.00 100.31 ? 409 PHE A O   1 
ATOM 3066 C CB  . PHE A 1 410 ? 34.432 13.309  40.902 1.00 93.99  ? 409 PHE A CB  1 
ATOM 3067 C CG  . PHE A 1 410 ? 33.487 14.472  40.800 1.00 100.39 ? 409 PHE A CG  1 
ATOM 3068 C CD1 . PHE A 1 410 ? 33.026 14.903  39.567 1.00 100.32 ? 409 PHE A CD1 1 
ATOM 3069 C CD2 . PHE A 1 410 ? 33.066 15.141  41.938 1.00 100.28 ? 409 PHE A CD2 1 
ATOM 3070 C CE1 . PHE A 1 410 ? 32.158 15.976  39.470 1.00 100.92 ? 409 PHE A CE1 1 
ATOM 3071 C CE2 . PHE A 1 410 ? 32.199 16.214  41.848 1.00 102.43 ? 409 PHE A CE2 1 
ATOM 3072 C CZ  . PHE A 1 410 ? 31.745 16.632  40.612 1.00 100.91 ? 409 PHE A CZ  1 
ATOM 3073 N N   . LEU A 1 411 ? 36.837 14.081  42.694 1.00 86.73  ? 410 LEU A N   1 
ATOM 3074 C CA  . LEU A 1 411 ? 37.495 14.911  43.696 1.00 84.38  ? 410 LEU A CA  1 
ATOM 3075 C C   . LEU A 1 411 ? 38.898 15.312  43.260 1.00 93.57  ? 410 LEU A C   1 
ATOM 3076 O O   . LEU A 1 411 ? 39.393 16.370  43.666 1.00 96.05  ? 410 LEU A O   1 
ATOM 3077 C CB  . LEU A 1 411 ? 37.541 14.180  45.036 1.00 77.19  ? 410 LEU A CB  1 
ATOM 3078 C CG  . LEU A 1 411 ? 36.183 13.814  45.636 1.00 81.48  ? 410 LEU A CG  1 
ATOM 3079 C CD1 . LEU A 1 411 ? 36.345 13.341  47.070 1.00 77.80  ? 410 LEU A CD1 1 
ATOM 3080 C CD2 . LEU A 1 411 ? 35.223 14.992  45.560 1.00 90.24  ? 410 LEU A CD2 1 
ATOM 3081 N N   . LEU A 1 412 ? 39.554 14.483  42.445 1.00 91.27  ? 411 LEU A N   1 
ATOM 3082 C CA  . LEU A 1 412 ? 40.827 14.881  41.853 1.00 95.36  ? 411 LEU A CA  1 
ATOM 3083 C C   . LEU A 1 412 ? 40.624 15.999  40.838 1.00 95.43  ? 411 LEU A C   1 
ATOM 3084 O O   . LEU A 1 412 ? 41.322 17.019  40.871 1.00 100.02 ? 411 LEU A O   1 
ATOM 3085 C CB  . LEU A 1 412 ? 41.502 13.675  41.198 1.00 91.03  ? 411 LEU A CB  1 
ATOM 3086 C CG  . LEU A 1 412 ? 42.611 12.975  41.984 1.00 80.12  ? 411 LEU A CG  1 
ATOM 3087 C CD1 . LEU A 1 412 ? 43.349 11.987  41.094 1.00 75.81  ? 411 LEU A CD1 1 
ATOM 3088 C CD2 . LEU A 1 412 ? 43.576 13.989  42.579 1.00 91.81  ? 411 LEU A CD2 1 
ATOM 3089 N N   . TRP A 1 413 ? 39.663 15.820  39.929 1.00 93.75  ? 412 TRP A N   1 
ATOM 3090 C CA  . TRP A 1 413 ? 39.350 16.851  38.947 1.00 91.75  ? 412 TRP A CA  1 
ATOM 3091 C C   . TRP A 1 413 ? 38.725 18.074  39.606 1.00 91.48  ? 412 TRP A C   1 
ATOM 3092 O O   . TRP A 1 413 ? 38.842 19.188  39.081 1.00 87.58  ? 412 TRP A O   1 
ATOM 3093 C CB  . TRP A 1 413 ? 38.438 16.255  37.868 1.00 87.39  ? 412 TRP A CB  1 
ATOM 3094 C CG  . TRP A 1 413 ? 37.663 17.222  37.022 1.00 98.62  ? 412 TRP A CG  1 
ATOM 3095 C CD1 . TRP A 1 413 ? 37.925 17.561  35.725 1.00 98.56  ? 412 TRP A CD1 1 
ATOM 3096 C CD2 . TRP A 1 413 ? 36.463 17.921  37.382 1.00 100.10 ? 412 TRP A CD2 1 
ATOM 3097 N NE1 . TRP A 1 413 ? 36.984 18.450  35.267 1.00 96.15  ? 412 TRP A NE1 1 
ATOM 3098 C CE2 . TRP A 1 413 ? 36.075 18.687  36.264 1.00 92.32  ? 412 TRP A CE2 1 
ATOM 3099 C CE3 . TRP A 1 413 ? 35.688 17.986  38.546 1.00 95.78  ? 412 TRP A CE3 1 
ATOM 3100 C CZ2 . TRP A 1 413 ? 34.949 19.506  36.276 1.00 87.31  ? 412 TRP A CZ2 1 
ATOM 3101 C CZ3 . TRP A 1 413 ? 34.572 18.801  38.555 1.00 95.43  ? 412 TRP A CZ3 1 
ATOM 3102 C CH2 . TRP A 1 413 ? 34.212 19.548  37.427 1.00 94.21  ? 412 TRP A CH2 1 
ATOM 3103 N N   . ARG A 1 414 ? 38.065 17.891  40.755 1.00 91.57  ? 413 ARG A N   1 
ATOM 3104 C CA  . ARG A 1 414 ? 37.532 19.031  41.494 1.00 100.54 ? 413 ARG A CA  1 
ATOM 3105 C C   . ARG A 1 414 ? 38.646 19.880  42.092 1.00 104.25 ? 413 ARG A C   1 
ATOM 3106 O O   . ARG A 1 414 ? 38.491 21.099  42.228 1.00 97.68  ? 413 ARG A O   1 
ATOM 3107 C CB  . ARG A 1 414 ? 36.584 18.550  42.594 1.00 95.63  ? 413 ARG A CB  1 
ATOM 3108 C CG  . ARG A 1 414 ? 35.738 19.646  43.222 1.00 93.77  ? 413 ARG A CG  1 
ATOM 3109 C CD  . ARG A 1 414 ? 34.913 19.109  44.384 1.00 100.83 ? 413 ARG A CD  1 
ATOM 3110 N NE  . ARG A 1 414 ? 35.750 18.647  45.486 1.00 115.43 ? 413 ARG A NE  1 
ATOM 3111 C CZ  . ARG A 1 414 ? 35.576 18.991  46.755 1.00 114.69 ? 413 ARG A CZ  1 
ATOM 3112 N NH1 . ARG A 1 414 ? 34.600 19.804  47.125 1.00 101.38 ? 413 ARG A NH1 1 
ATOM 3113 N NH2 . ARG A 1 414 ? 36.402 18.505  47.678 1.00 109.06 ? 413 ARG A NH2 1 
ATOM 3114 N N   . ARG A 1 415 ? 39.769 19.259  42.454 1.00 109.06 ? 414 ARG A N   1 
ATOM 3115 C CA  . ARG A 1 415 ? 40.929 19.964  42.980 1.00 111.44 ? 414 ARG A CA  1 
ATOM 3116 C C   . ARG A 1 415 ? 41.989 20.212  41.912 1.00 121.75 ? 414 ARG A C   1 
ATOM 3117 O O   . ARG A 1 415 ? 43.162 20.409  42.247 1.00 126.95 ? 414 ARG A O   1 
ATOM 3118 C CB  . ARG A 1 415 ? 41.531 19.189  44.152 1.00 110.58 ? 414 ARG A CB  1 
ATOM 3119 C CG  . ARG A 1 415 ? 40.572 18.965  45.309 1.00 110.78 ? 414 ARG A CG  1 
ATOM 3120 C CD  . ARG A 1 415 ? 41.308 18.517  46.562 1.00 115.84 ? 414 ARG A CD  1 
ATOM 3121 N NE  . ARG A 1 415 ? 42.127 17.335  46.321 1.00 120.82 ? 414 ARG A NE  1 
ATOM 3122 C CZ  . ARG A 1 415 ? 43.453 17.335  46.291 1.00 121.70 ? 414 ARG A CZ  1 
ATOM 3123 N NH1 . ARG A 1 415 ? 44.148 18.445  46.481 1.00 119.37 ? 414 ARG A NH1 1 
ATOM 3124 N NH2 . ARG A 1 415 ? 44.097 16.195  46.060 1.00 125.92 ? 414 ARG A NH2 1 
ATOM 3125 N N   . ARG A 1 416 ? 41.596 20.202  40.635 1.00 129.53 ? 415 ARG A N   1 
ATOM 3126 C CA  . ARG A 1 416 ? 42.482 20.470  39.500 1.00 121.84 ? 415 ARG A CA  1 
ATOM 3127 C C   . ARG A 1 416 ? 43.672 19.503  39.492 1.00 128.49 ? 415 ARG A C   1 
ATOM 3128 O O   . ARG A 1 416 ? 44.816 19.864  39.778 1.00 136.40 ? 415 ARG A O   1 
ATOM 3129 C CB  . ARG A 1 416 ? 42.953 21.930  39.509 1.00 123.26 ? 415 ARG A CB  1 
ATOM 3130 C CG  . ARG A 1 416 ? 41.865 22.939  39.852 1.00 121.74 ? 415 ARG A CG  1 
ATOM 3131 C CD  . ARG A 1 416 ? 42.415 24.078  40.698 1.00 118.55 ? 415 ARG A CD  1 
ATOM 3132 N NE  . ARG A 1 416 ? 43.199 23.589  41.826 1.00 122.73 ? 415 ARG A NE  1 
ATOM 3133 C CZ  . ARG A 1 416 ? 43.983 24.347  42.579 1.00 127.74 ? 415 ARG A CZ  1 
ATOM 3134 N NH1 . ARG A 1 416 ? 44.116 25.644  42.352 1.00 123.64 ? 415 ARG A NH1 1 
ATOM 3135 N NH2 . ARG A 1 416 ? 44.653 23.791  43.585 1.00 120.85 ? 415 ARG A NH2 1 
ATOM 3136 N N   . ALA A 1 417 ? 43.365 18.256  39.149 1.00 113.28 ? 416 ALA A N   1 
ATOM 3137 C CA  . ALA A 1 417 ? 44.388 17.219  39.050 1.00 111.11 ? 416 ALA A CA  1 
ATOM 3138 C C   . ALA A 1 417 ? 45.227 17.399  37.788 1.00 106.28 ? 416 ALA A C   1 
ATOM 3139 O O   . ALA A 1 417 ? 46.447 17.226  37.809 1.00 97.97  ? 416 ALA A O   1 
ATOM 3140 C CB  . ALA A 1 417 ? 43.752 15.835  39.070 1.00 105.31 ? 416 ALA A CB  1 
ATOM 3141 N N   . ALA B 2 2   ? 22.981 -26.931 26.462 1.00 73.25  ? 0   ALA B N   1 
ATOM 3142 C CA  . ALA B 2 2   ? 23.456 -28.109 27.175 1.00 67.41  ? 0   ALA B CA  1 
ATOM 3143 C C   . ALA B 2 2   ? 22.358 -28.678 28.067 1.00 73.81  ? 0   ALA B C   1 
ATOM 3144 O O   . ALA B 2 2   ? 22.631 -29.285 29.102 1.00 74.22  ? 0   ALA B O   1 
ATOM 3145 C CB  . ALA B 2 2   ? 24.690 -27.778 27.992 1.00 65.76  ? 0   ALA B CB  1 
ATOM 3146 N N   . GLN B 2 3   ? 21.108 -28.460 27.660 1.00 91.02  ? 1   GLN B N   1 
ATOM 3147 C CA  . GLN B 2 3   ? 19.976 -29.148 28.266 1.00 92.59  ? 1   GLN B CA  1 
ATOM 3148 C C   . GLN B 2 3   ? 19.704 -30.471 27.558 1.00 91.28  ? 1   GLN B C   1 
ATOM 3149 O O   . GLN B 2 3   ? 19.560 -31.511 28.208 1.00 92.04  ? 1   GLN B O   1 
ATOM 3150 C CB  . GLN B 2 3   ? 18.732 -28.254 28.234 1.00 93.49  ? 1   GLN B CB  1 
ATOM 3151 C CG  . GLN B 2 3   ? 17.412 -29.001 28.394 1.00 100.79 ? 1   GLN B CG  1 
ATOM 3152 C CD  . GLN B 2 3   ? 17.358 -29.842 29.658 1.00 101.40 ? 1   GLN B CD  1 
ATOM 3153 O OE1 . GLN B 2 3   ? 17.138 -31.053 29.603 1.00 88.77  ? 1   GLN B OE1 1 
ATOM 3154 N NE2 . GLN B 2 3   ? 17.560 -29.202 30.804 1.00 103.12 ? 1   GLN B NE2 1 
ATOM 3155 N N   . VAL B 2 4   ? 19.640 -30.443 26.230 1.00 74.65  ? 2   VAL B N   1 
ATOM 3156 C CA  . VAL B 2 4   ? 19.465 -31.634 25.408 1.00 73.99  ? 2   VAL B CA  1 
ATOM 3157 C C   . VAL B 2 4   ? 20.673 -31.725 24.488 1.00 70.73  ? 2   VAL B C   1 
ATOM 3158 O O   . VAL B 2 4   ? 20.791 -30.954 23.526 1.00 66.33  ? 2   VAL B O   1 
ATOM 3159 C CB  . VAL B 2 4   ? 18.156 -31.596 24.607 1.00 67.90  ? 2   VAL B CB  1 
ATOM 3160 C CG1 . VAL B 2 4   ? 18.111 -32.738 23.600 1.00 55.92  ? 2   VAL B CG1 1 
ATOM 3161 C CG2 . VAL B 2 4   ? 16.967 -31.667 25.548 1.00 77.55  ? 2   VAL B CG2 1 
ATOM 3162 N N   . GLN B 2 5   ? 21.576 -32.653 24.786 1.00 62.41  ? 3   GLN B N   1 
ATOM 3163 C CA  . GLN B 2 5   ? 22.776 -32.867 23.991 1.00 61.66  ? 3   GLN B CA  1 
ATOM 3164 C C   . GLN B 2 5   ? 22.547 -34.014 23.016 1.00 69.72  ? 3   GLN B C   1 
ATOM 3165 O O   . GLN B 2 5   ? 21.914 -35.017 23.360 1.00 69.46  ? 3   GLN B O   1 
ATOM 3166 C CB  . GLN B 2 5   ? 23.976 -33.163 24.894 1.00 55.87  ? 3   GLN B CB  1 
ATOM 3167 C CG  . GLN B 2 5   ? 24.552 -31.931 25.579 1.00 61.69  ? 3   GLN B CG  1 
ATOM 3168 C CD  . GLN B 2 5   ? 24.100 -31.791 27.021 1.00 67.35  ? 3   GLN B CD  1 
ATOM 3169 O OE1 . GLN B 2 5   ? 22.903 -31.732 27.306 1.00 64.05  ? 3   GLN B OE1 1 
ATOM 3170 N NE2 . GLN B 2 5   ? 25.058 -31.734 27.939 1.00 66.62  ? 3   GLN B NE2 1 
ATOM 3171 N N   . LEU B 2 6   ? 23.062 -33.862 21.798 1.00 59.07  ? 4   LEU B N   1 
ATOM 3172 C CA  . LEU B 2 6   ? 22.824 -34.811 20.720 1.00 49.91  ? 4   LEU B CA  1 
ATOM 3173 C C   . LEU B 2 6   ? 24.141 -35.392 20.225 1.00 50.60  ? 4   LEU B C   1 
ATOM 3174 O O   . LEU B 2 6   ? 25.147 -34.682 20.130 1.00 50.64  ? 4   LEU B O   1 
ATOM 3175 C CB  . LEU B 2 6   ? 22.079 -34.143 19.563 1.00 47.77  ? 4   LEU B CB  1 
ATOM 3176 C CG  . LEU B 2 6   ? 20.830 -33.366 19.981 1.00 54.87  ? 4   LEU B CG  1 
ATOM 3177 C CD1 . LEU B 2 6   ? 20.188 -32.678 18.791 1.00 52.91  ? 4   LEU B CD1 1 
ATOM 3178 C CD2 . LEU B 2 6   ? 19.836 -34.287 20.663 1.00 48.28  ? 4   LEU B CD2 1 
ATOM 3179 N N   . VAL B 2 7   ? 24.125 -36.683 19.902 1.00 62.80  ? 5   VAL B N   1 
ATOM 3180 C CA  . VAL B 2 7   ? 25.304 -37.397 19.422 1.00 68.80  ? 5   VAL B CA  1 
ATOM 3181 C C   . VAL B 2 7   ? 24.939 -38.111 18.127 1.00 66.96  ? 5   VAL B C   1 
ATOM 3182 O O   . VAL B 2 7   ? 24.023 -38.943 18.111 1.00 62.79  ? 5   VAL B O   1 
ATOM 3183 C CB  . VAL B 2 7   ? 25.832 -38.401 20.459 1.00 59.90  ? 5   VAL B CB  1 
ATOM 3184 C CG1 . VAL B 2 7   ? 26.843 -39.340 19.818 1.00 55.77  ? 5   VAL B CG1 1 
ATOM 3185 C CG2 . VAL B 2 7   ? 26.450 -37.668 21.638 1.00 56.20  ? 5   VAL B CG2 1 
ATOM 3186 N N   . GLU B 2 8   ? 25.654 -37.791 17.050 1.00 72.91  ? 6   GLU B N   1 
ATOM 3187 C CA  . GLU B 2 8   ? 25.465 -38.463 15.775 1.00 73.01  ? 6   GLU B CA  1 
ATOM 3188 C C   . GLU B 2 8   ? 26.218 -39.793 15.751 1.00 72.65  ? 6   GLU B C   1 
ATOM 3189 O O   . GLU B 2 8   ? 27.042 -40.093 16.620 1.00 79.26  ? 6   GLU B O   1 
ATOM 3190 C CB  . GLU B 2 8   ? 25.936 -37.581 14.618 1.00 75.59  ? 6   GLU B CB  1 
ATOM 3191 C CG  . GLU B 2 8   ? 24.899 -36.599 14.093 1.00 80.77  ? 6   GLU B CG  1 
ATOM 3192 C CD  . GLU B 2 8   ? 24.638 -35.452 15.049 1.00 80.18  ? 6   GLU B CD  1 
ATOM 3193 O OE1 . GLU B 2 8   ? 25.593 -34.706 15.341 1.00 79.87  ? 6   GLU B OE1 1 
ATOM 3194 O OE2 . GLU B 2 8   ? 23.482 -35.280 15.488 1.00 78.59  ? 6   GLU B OE2 1 
ATOM 3195 N N   . SER B 2 9   ? 25.923 -40.595 14.730 1.00 63.55  ? 7   SER B N   1 
ATOM 3196 C CA  . SER B 2 9   ? 26.593 -41.872 14.537 1.00 71.29  ? 7   SER B CA  1 
ATOM 3197 C C   . SER B 2 9   ? 26.328 -42.358 13.122 1.00 62.88  ? 7   SER B C   1 
ATOM 3198 O O   . SER B 2 9   ? 25.236 -42.159 12.582 1.00 53.45  ? 7   SER B O   1 
ATOM 3199 C CB  . SER B 2 9   ? 26.128 -42.923 15.553 1.00 68.68  ? 7   SER B CB  1 
ATOM 3200 O OG  . SER B 2 9   ? 24.716 -42.979 15.627 1.00 75.27  ? 7   SER B OG  1 
ATOM 3201 N N   . GLY B 2 10  ? 27.330 -42.993 12.535 1.00 59.14  ? 8   GLY B N   1 
ATOM 3202 C CA  . GLY B 2 10  ? 27.213 -43.530 11.194 1.00 60.01  ? 8   GLY B CA  1 
ATOM 3203 C C   . GLY B 2 10  ? 27.820 -42.620 10.148 1.00 66.89  ? 8   GLY B C   1 
ATOM 3204 O O   . GLY B 2 10  ? 28.568 -41.681 10.433 1.00 75.91  ? 8   GLY B O   1 
ATOM 3205 N N   . GLY B 2 11  ? 27.483 -42.921 8.900  1.00 60.56  ? 9   GLY B N   1 
ATOM 3206 C CA  . GLY B 2 11  ? 27.969 -42.155 7.771  1.00 65.39  ? 9   GLY B CA  1 
ATOM 3207 C C   . GLY B 2 11  ? 29.419 -42.432 7.453  1.00 65.17  ? 9   GLY B C   1 
ATOM 3208 O O   . GLY B 2 11  ? 30.148 -43.079 8.209  1.00 63.33  ? 9   GLY B O   1 
ATOM 3209 N N   . GLY B 2 12  ? 29.843 -41.929 6.296  1.00 59.77  ? 10  GLY B N   1 
ATOM 3210 C CA  . GLY B 2 12  ? 31.209 -42.103 5.840  1.00 58.89  ? 10  GLY B CA  1 
ATOM 3211 C C   . GLY B 2 12  ? 31.313 -42.161 4.330  1.00 66.92  ? 10  GLY B C   1 
ATOM 3212 O O   . GLY B 2 12  ? 30.838 -41.263 3.631  1.00 75.05  ? 10  GLY B O   1 
ATOM 3213 N N   . LEU B 2 13  ? 31.926 -43.220 3.817  1.00 60.15  ? 11  LEU B N   1 
ATOM 3214 C CA  . LEU B 2 13  ? 32.080 -43.395 2.384  1.00 72.00  ? 11  LEU B CA  1 
ATOM 3215 C C   . LEU B 2 13  ? 30.951 -44.256 1.832  1.00 71.76  ? 11  LEU B C   1 
ATOM 3216 O O   . LEU B 2 13  ? 30.472 -45.183 2.490  1.00 73.65  ? 11  LEU B O   1 
ATOM 3217 C CB  . LEU B 2 13  ? 33.433 -44.032 2.052  1.00 76.63  ? 11  LEU B CB  1 
ATOM 3218 C CG  . LEU B 2 13  ? 34.431 -43.157 1.287  1.00 77.14  ? 11  LEU B CG  1 
ATOM 3219 C CD1 . LEU B 2 13  ? 35.631 -43.971 0.814  1.00 67.86  ? 11  LEU B CD1 1 
ATOM 3220 C CD2 . LEU B 2 13  ? 33.758 -42.463 0.113  1.00 66.49  ? 11  LEU B CD2 1 
ATOM 3221 N N   . VAL B 2 14  ? 30.528 -43.934 0.613  1.00 71.28  ? 12  VAL B N   1 
ATOM 3222 C CA  . VAL B 2 14  ? 29.438 -44.648 -0.042 1.00 63.48  ? 12  VAL B CA  1 
ATOM 3223 C C   . VAL B 2 14  ? 29.521 -44.363 -1.535 1.00 73.09  ? 12  VAL B C   1 
ATOM 3224 O O   . VAL B 2 14  ? 29.855 -43.250 -1.951 1.00 73.17  ? 12  VAL B O   1 
ATOM 3225 C CB  . VAL B 2 14  ? 28.068 -44.243 0.556  1.00 61.70  ? 12  VAL B CB  1 
ATOM 3226 C CG1 . VAL B 2 14  ? 27.918 -42.731 0.585  1.00 60.75  ? 12  VAL B CG1 1 
ATOM 3227 C CG2 . VAL B 2 14  ? 26.925 -44.887 -0.213 1.00 62.81  ? 12  VAL B CG2 1 
ATOM 3228 N N   . GLN B 2 15  ? 29.236 -45.383 -2.340 1.00 77.01  ? 13  GLN B N   1 
ATOM 3229 C CA  . GLN B 2 15  ? 29.229 -45.218 -3.784 1.00 70.01  ? 13  GLN B CA  1 
ATOM 3230 C C   . GLN B 2 15  ? 27.909 -44.607 -4.244 1.00 70.11  ? 13  GLN B C   1 
ATOM 3231 O O   . GLN B 2 15  ? 26.877 -44.714 -3.575 1.00 68.51  ? 13  GLN B O   1 
ATOM 3232 C CB  . GLN B 2 15  ? 29.459 -46.559 -4.482 1.00 73.08  ? 13  GLN B CB  1 
ATOM 3233 C CG  . GLN B 2 15  ? 30.299 -47.537 -3.682 1.00 71.62  ? 13  GLN B CG  1 
ATOM 3234 C CD  . GLN B 2 15  ? 30.839 -48.670 -4.532 1.00 85.53  ? 13  GLN B CD  1 
ATOM 3235 O OE1 . GLN B 2 15  ? 31.637 -48.451 -5.444 1.00 92.28  ? 13  GLN B OE1 1 
ATOM 3236 N NE2 . GLN B 2 15  ? 30.403 -49.890 -4.239 1.00 74.39  ? 13  GLN B NE2 1 
ATOM 3237 N N   . ALA B 2 16  ? 27.956 -43.958 -5.408 1.00 72.40  ? 14  ALA B N   1 
ATOM 3238 C CA  . ALA B 2 16  ? 26.764 -43.335 -5.969 1.00 73.13  ? 14  ALA B CA  1 
ATOM 3239 C C   . ALA B 2 16  ? 25.678 -44.376 -6.208 1.00 73.92  ? 14  ALA B C   1 
ATOM 3240 O O   . ALA B 2 16  ? 25.939 -45.453 -6.753 1.00 75.78  ? 14  ALA B O   1 
ATOM 3241 C CB  . ALA B 2 16  ? 27.108 -42.617 -7.274 1.00 76.32  ? 14  ALA B CB  1 
ATOM 3242 N N   . GLY B 2 17  ? 24.454 -44.051 -5.794 1.00 72.75  ? 15  GLY B N   1 
ATOM 3243 C CA  . GLY B 2 17  ? 23.338 -44.963 -5.874 1.00 73.58  ? 15  GLY B CA  1 
ATOM 3244 C C   . GLY B 2 17  ? 23.148 -45.841 -4.656 1.00 71.49  ? 15  GLY B C   1 
ATOM 3245 O O   . GLY B 2 17  ? 22.042 -46.354 -4.445 1.00 71.80  ? 15  GLY B O   1 
ATOM 3246 N N   . GLY B 2 18  ? 24.193 -46.021 -3.845 1.00 70.55  ? 16  GLY B N   1 
ATOM 3247 C CA  . GLY B 2 18  ? 24.114 -46.854 -2.666 1.00 70.55  ? 16  GLY B CA  1 
ATOM 3248 C C   . GLY B 2 18  ? 23.453 -46.156 -1.492 1.00 72.66  ? 16  GLY B C   1 
ATOM 3249 O O   . GLY B 2 18  ? 23.159 -44.961 -1.518 1.00 78.45  ? 16  GLY B O   1 
ATOM 3250 N N   . SER B 2 19  ? 23.232 -46.930 -0.432 1.00 76.73  ? 17  SER B N   1 
ATOM 3251 C CA  . SER B 2 19  ? 22.480 -46.491 0.735  1.00 69.03  ? 17  SER B CA  1 
ATOM 3252 C C   . SER B 2 19  ? 23.397 -46.255 1.929  1.00 60.99  ? 17  SER B C   1 
ATOM 3253 O O   . SER B 2 19  ? 24.556 -46.677 1.956  1.00 61.30  ? 17  SER B O   1 
ATOM 3254 C CB  . SER B 2 19  ? 21.403 -47.518 1.101  1.00 75.20  ? 17  SER B CB  1 
ATOM 3255 O OG  . SER B 2 19  ? 20.175 -47.207 0.473  1.00 83.15  ? 17  SER B OG  1 
ATOM 3256 N N   . LEU B 2 20  ? 22.842 -45.572 2.930  1.00 61.56  ? 18  LEU B N   1 
ATOM 3257 C CA  . LEU B 2 20  ? 23.550 -45.255 4.161  1.00 57.69  ? 18  LEU B CA  1 
ATOM 3258 C C   . LEU B 2 20  ? 22.533 -44.822 5.209  1.00 57.06  ? 18  LEU B C   1 
ATOM 3259 O O   . LEU B 2 20  ? 21.610 -44.062 4.907  1.00 57.31  ? 18  LEU B O   1 
ATOM 3260 C CB  . LEU B 2 20  ? 24.592 -44.151 3.942  1.00 58.75  ? 18  LEU B CB  1 
ATOM 3261 C CG  . LEU B 2 20  ? 25.648 -43.949 5.032  1.00 63.20  ? 18  LEU B CG  1 
ATOM 3262 C CD1 . LEU B 2 20  ? 25.996 -45.266 5.714  1.00 75.49  ? 18  LEU B CD1 1 
ATOM 3263 C CD2 . LEU B 2 20  ? 26.894 -43.299 4.452  1.00 65.69  ? 18  LEU B CD2 1 
ATOM 3264 N N   . GLY B 2 21  ? 22.709 -45.311 6.434  1.00 64.22  ? 19  GLY B N   1 
ATOM 3265 C CA  . GLY B 2 21  ? 21.833 -44.978 7.541  1.00 59.89  ? 19  GLY B CA  1 
ATOM 3266 C C   . GLY B 2 21  ? 22.525 -44.049 8.520  1.00 61.38  ? 19  GLY B C   1 
ATOM 3267 O O   . GLY B 2 21  ? 23.739 -44.128 8.718  1.00 66.07  ? 19  GLY B O   1 
ATOM 3268 N N   . LEU B 2 22  ? 21.743 -43.161 9.132  1.00 58.00  ? 20  LEU B N   1 
ATOM 3269 C CA  . LEU B 2 22  ? 22.245 -42.215 10.118 1.00 54.59  ? 20  LEU B CA  1 
ATOM 3270 C C   . LEU B 2 22  ? 21.370 -42.267 11.361 1.00 58.04  ? 20  LEU B C   1 
ATOM 3271 O O   . LEU B 2 22  ? 20.154 -42.455 11.265 1.00 55.65  ? 20  LEU B O   1 
ATOM 3272 C CB  . LEU B 2 22  ? 22.276 -40.789 9.556  1.00 54.28  ? 20  LEU B CB  1 
ATOM 3273 C CG  . LEU B 2 22  ? 23.454 -40.449 8.643  1.00 55.34  ? 20  LEU B CG  1 
ATOM 3274 C CD1 . LEU B 2 22  ? 23.592 -38.945 8.493  1.00 53.11  ? 20  LEU B CD1 1 
ATOM 3275 C CD2 . LEU B 2 22  ? 24.739 -41.054 9.181  1.00 51.00  ? 20  LEU B CD2 1 
ATOM 3276 N N   . SER B 2 23  ? 21.993 -42.095 12.527 1.00 57.71  ? 21  SER B N   1 
ATOM 3277 C CA  . SER B 2 23  ? 21.286 -42.150 13.799 1.00 65.24  ? 21  SER B CA  1 
ATOM 3278 C C   . SER B 2 23  ? 21.784 -41.045 14.722 1.00 53.94  ? 21  SER B C   1 
ATOM 3279 O O   . SER B 2 23  ? 22.972 -40.713 14.724 1.00 50.88  ? 21  SER B O   1 
ATOM 3280 C CB  . SER B 2 23  ? 21.460 -43.516 14.475 1.00 61.31  ? 21  SER B CB  1 
ATOM 3281 O OG  . SER B 2 23  ? 22.814 -43.932 14.441 1.00 66.07  ? 21  SER B OG  1 
ATOM 3282 N N   . CYS B 2 24  ? 20.866 -40.488 15.510 1.00 59.61  ? 22  CYS B N   1 
ATOM 3283 C CA  . CYS B 2 24  ? 21.167 -39.414 16.447 1.00 63.60  ? 22  CYS B CA  1 
ATOM 3284 C C   . CYS B 2 24  ? 20.526 -39.736 17.789 1.00 67.44  ? 22  CYS B C   1 
ATOM 3285 O O   . CYS B 2 24  ? 19.312 -39.954 17.859 1.00 68.76  ? 22  CYS B O   1 
ATOM 3286 C CB  . CYS B 2 24  ? 20.661 -38.067 15.921 1.00 60.70  ? 22  CYS B CB  1 
ATOM 3287 S SG  . CYS B 2 24  ? 21.120 -36.654 16.941 1.00 80.28  ? 22  CYS B SG  1 
ATOM 3288 N N   . ALA B 2 25  ? 21.333 -39.754 18.849 1.00 54.09  ? 23  ALA B N   1 
ATOM 3289 C CA  . ALA B 2 25  ? 20.873 -40.092 20.190 1.00 61.35  ? 23  ALA B CA  1 
ATOM 3290 C C   . ALA B 2 25  ? 20.830 -38.845 21.061 1.00 61.93  ? 23  ALA B C   1 
ATOM 3291 O O   . ALA B 2 25  ? 21.713 -37.985 20.980 1.00 59.89  ? 23  ALA B O   1 
ATOM 3292 C CB  . ALA B 2 25  ? 21.777 -41.148 20.832 1.00 62.69  ? 23  ALA B CB  1 
ATOM 3293 N N   . ALA B 2 26  ? 19.805 -38.757 21.904 1.00 55.52  ? 24  ALA B N   1 
ATOM 3294 C CA  . ALA B 2 26  ? 19.545 -37.570 22.709 1.00 65.03  ? 24  ALA B CA  1 
ATOM 3295 C C   . ALA B 2 26  ? 19.609 -37.916 24.190 1.00 69.31  ? 24  ALA B C   1 
ATOM 3296 O O   . ALA B 2 26  ? 18.936 -38.848 24.645 1.00 59.82  ? 24  ALA B O   1 
ATOM 3297 C CB  . ALA B 2 26  ? 18.182 -36.968 22.363 1.00 55.17  ? 24  ALA B CB  1 
ATOM 3298 N N   . SER B 2 27  ? 20.412 -37.162 24.933 1.00 74.69  ? 25  SER B N   1 
ATOM 3299 C CA  . SER B 2 27  ? 20.515 -37.277 26.387 1.00 69.56  ? 25  SER B CA  1 
ATOM 3300 C C   . SER B 2 27  ? 19.844 -36.039 26.979 1.00 74.55  ? 25  SER B C   1 
ATOM 3301 O O   . SER B 2 27  ? 20.493 -35.024 27.236 1.00 79.83  ? 25  SER B O   1 
ATOM 3302 C CB  . SER B 2 27  ? 21.974 -37.408 26.835 1.00 68.35  ? 25  SER B CB  1 
ATOM 3303 O OG  . SER B 2 27  ? 22.587 -36.141 27.005 1.00 79.71  ? 25  SER B OG  1 
ATOM 3304 N N   . GLY B 2 28  ? 18.535 -36.127 27.179 1.00 60.75  ? 26  GLY B N   1 
ATOM 3305 C CA  . GLY B 2 28  ? 17.788 -35.018 27.737 1.00 60.31  ? 26  GLY B CA  1 
ATOM 3306 C C   . GLY B 2 28  ? 16.404 -35.462 28.147 1.00 61.93  ? 26  GLY B C   1 
ATOM 3307 O O   . GLY B 2 28  ? 15.871 -36.455 27.640 1.00 66.93  ? 26  GLY B O   1 
ATOM 3308 N N   . ARG B 2 29  ? 15.824 -34.702 29.073 1.00 71.74  ? 27  ARG B N   1 
ATOM 3309 C CA  . ARG B 2 29  ? 14.521 -35.038 29.626 1.00 71.72  ? 27  ARG B CA  1 
ATOM 3310 C C   . ARG B 2 29  ? 13.406 -34.666 28.658 1.00 74.01  ? 27  ARG B C   1 
ATOM 3311 O O   . ARG B 2 29  ? 13.454 -33.620 28.001 1.00 80.02  ? 27  ARG B O   1 
ATOM 3312 C CB  . ARG B 2 29  ? 14.309 -34.327 30.964 1.00 73.78  ? 27  ARG B CB  1 
ATOM 3313 C CG  . ARG B 2 29  ? 14.752 -32.873 30.985 1.00 85.22  ? 27  ARG B CG  1 
ATOM 3314 C CD  . ARG B 2 29  ? 13.731 -32.001 31.703 1.00 97.91  ? 27  ARG B CD  1 
ATOM 3315 N NE  . ARG B 2 29  ? 13.873 -30.591 31.358 1.00 109.22 ? 27  ARG B NE  1 
ATOM 3316 C CZ  . ARG B 2 29  ? 13.395 -30.039 30.251 1.00 105.74 ? 27  ARG B CZ  1 
ATOM 3317 N NH1 . ARG B 2 29  ? 12.736 -30.752 29.352 1.00 92.87  ? 27  ARG B NH1 1 
ATOM 3318 N NH2 . ARG B 2 29  ? 13.588 -28.741 30.038 1.00 98.78  ? 27  ARG B NH2 1 
ATOM 3319 N N   . THR B 2 30  ? 12.397 -35.538 28.578 1.00 64.45  ? 28  THR B N   1 
ATOM 3320 C CA  . THR B 2 30  ? 11.211 -35.349 27.740 1.00 71.39  ? 28  THR B CA  1 
ATOM 3321 C C   . THR B 2 30  ? 11.603 -35.179 26.268 1.00 71.43  ? 28  THR B C   1 
ATOM 3322 O O   . THR B 2 30  ? 11.444 -34.119 25.659 1.00 75.20  ? 28  THR B O   1 
ATOM 3323 C CB  . THR B 2 30  ? 10.374 -34.161 28.229 1.00 85.80  ? 28  THR B CB  1 
ATOM 3324 O OG1 . THR B 2 30  ? 10.453 -34.073 29.658 1.00 75.38  ? 28  THR B OG1 1 
ATOM 3325 C CG2 . THR B 2 30  ? 8.922  -34.334 27.816 1.00 88.68  ? 28  THR B CG2 1 
ATOM 3326 N N   . PHE B 2 31  ? 12.120 -36.276 25.711 1.00 70.52  ? 29  PHE B N   1 
ATOM 3327 C CA  . PHE B 2 31  ? 12.542 -36.273 24.314 1.00 57.41  ? 29  PHE B CA  1 
ATOM 3328 C C   . PHE B 2 31  ? 11.351 -36.247 23.365 1.00 62.63  ? 29  PHE B C   1 
ATOM 3329 O O   . PHE B 2 31  ? 11.462 -35.731 22.246 1.00 61.59  ? 29  PHE B O   1 
ATOM 3330 C CB  . PHE B 2 31  ? 13.425 -37.493 24.042 1.00 58.39  ? 29  PHE B CB  1 
ATOM 3331 C CG  . PHE B 2 31  ? 13.682 -37.752 22.582 1.00 65.18  ? 29  PHE B CG  1 
ATOM 3332 C CD1 . PHE B 2 31  ? 14.654 -37.041 21.900 1.00 63.05  ? 29  PHE B CD1 1 
ATOM 3333 C CD2 . PHE B 2 31  ? 12.964 -38.721 21.898 1.00 65.22  ? 29  PHE B CD2 1 
ATOM 3334 C CE1 . PHE B 2 31  ? 14.899 -37.281 20.559 1.00 59.64  ? 29  PHE B CE1 1 
ATOM 3335 C CE2 . PHE B 2 31  ? 13.204 -38.965 20.557 1.00 56.18  ? 29  PHE B CE2 1 
ATOM 3336 C CZ  . PHE B 2 31  ? 14.173 -38.244 19.889 1.00 53.50  ? 29  PHE B CZ  1 
ATOM 3337 N N   . SER B 2 32  ? 10.207 -36.783 23.791 1.00 59.65  ? 30  SER B N   1 
ATOM 3338 C CA  . SER B 2 32  ? 9.027  -36.880 22.940 1.00 61.45  ? 30  SER B CA  1 
ATOM 3339 C C   . SER B 2 32  ? 8.309  -35.550 22.749 1.00 65.97  ? 30  SER B C   1 
ATOM 3340 O O   . SER B 2 32  ? 7.265  -35.521 22.089 1.00 68.47  ? 30  SER B O   1 
ATOM 3341 C CB  . SER B 2 32  ? 8.051  -37.909 23.516 1.00 63.29  ? 30  SER B CB  1 
ATOM 3342 O OG  . SER B 2 32  ? 7.826  -37.686 24.898 1.00 77.79  ? 30  SER B OG  1 
ATOM 3343 N N   . ASN B 2 33  ? 8.829  -34.459 23.305 1.00 74.20  ? 31  ASN B N   1 
ATOM 3344 C CA  . ASN B 2 33  ? 8.222  -33.145 23.156 1.00 78.36  ? 31  ASN B CA  1 
ATOM 3345 C C   . ASN B 2 33  ? 8.984  -32.248 22.190 1.00 72.90  ? 31  ASN B C   1 
ATOM 3346 O O   . ASN B 2 33  ? 8.562  -31.110 21.958 1.00 73.17  ? 31  ASN B O   1 
ATOM 3347 C CB  . ASN B 2 33  ? 8.115  -32.453 24.521 1.00 77.35  ? 31  ASN B CB  1 
ATOM 3348 C CG  . ASN B 2 33  ? 6.842  -32.816 25.263 1.00 76.14  ? 31  ASN B CG  1 
ATOM 3349 O OD1 . ASN B 2 33  ? 6.010  -33.572 24.763 1.00 80.78  ? 31  ASN B OD1 1 
ATOM 3350 N ND2 . ASN B 2 33  ? 6.680  -32.266 26.461 1.00 77.59  ? 31  ASN B ND2 1 
ATOM 3351 N N   . TYR B 2 34  ? 10.080 -32.731 21.615 1.00 67.57  ? 32  TYR B N   1 
ATOM 3352 C CA  . TYR B 2 34  ? 10.961 -31.916 20.793 1.00 58.87  ? 32  TYR B CA  1 
ATOM 3353 C C   . TYR B 2 34  ? 10.713 -32.171 19.312 1.00 60.36  ? 32  TYR B C   1 
ATOM 3354 O O   . TYR B 2 34  ? 10.265 -33.248 18.910 1.00 52.62  ? 32  TYR B O   1 
ATOM 3355 C CB  . TYR B 2 34  ? 12.430 -32.196 21.124 1.00 57.98  ? 32  TYR B CB  1 
ATOM 3356 C CG  . TYR B 2 34  ? 12.908 -31.582 22.425 1.00 73.42  ? 32  TYR B CG  1 
ATOM 3357 C CD1 . TYR B 2 34  ? 12.280 -31.878 23.628 1.00 73.78  ? 32  TYR B CD1 1 
ATOM 3358 C CD2 . TYR B 2 34  ? 13.987 -30.706 22.448 1.00 69.40  ? 32  TYR B CD2 1 
ATOM 3359 C CE1 . TYR B 2 34  ? 12.711 -31.320 24.818 1.00 78.99  ? 32  TYR B CE1 1 
ATOM 3360 C CE2 . TYR B 2 34  ? 14.425 -30.142 23.635 1.00 75.44  ? 32  TYR B CE2 1 
ATOM 3361 C CZ  . TYR B 2 34  ? 13.783 -30.453 24.817 1.00 80.50  ? 32  TYR B CZ  1 
ATOM 3362 O OH  . TYR B 2 34  ? 14.211 -29.899 26.004 1.00 81.83  ? 32  TYR B OH  1 
ATOM 3363 N N   . VAL B 2 35  ? 11.009 -31.160 18.502 1.00 65.97  ? 33  VAL B N   1 
ATOM 3364 C CA  . VAL B 2 35  ? 10.970 -31.282 17.049 1.00 66.39  ? 33  VAL B CA  1 
ATOM 3365 C C   . VAL B 2 35  ? 12.372 -31.666 16.592 1.00 64.22  ? 33  VAL B C   1 
ATOM 3366 O O   . VAL B 2 35  ? 13.315 -30.881 16.725 1.00 64.37  ? 33  VAL B O   1 
ATOM 3367 C CB  . VAL B 2 35  ? 10.499 -29.984 16.382 1.00 60.10  ? 33  VAL B CB  1 
ATOM 3368 C CG1 . VAL B 2 35  ? 10.843 -29.991 14.900 1.00 64.26  ? 33  VAL B CG1 1 
ATOM 3369 C CG2 . VAL B 2 35  ? 9.005  -29.792 16.586 1.00 60.01  ? 33  VAL B CG2 1 
ATOM 3370 N N   . MET B 2 36  ? 12.512 -32.879 16.071 1.00 55.01  ? 34  MET B N   1 
ATOM 3371 C CA  . MET B 2 36  ? 13.795 -33.388 15.611 1.00 53.46  ? 34  MET B CA  1 
ATOM 3372 C C   . MET B 2 36  ? 13.931 -33.163 14.112 1.00 56.41  ? 34  MET B C   1 
ATOM 3373 O O   . MET B 2 36  ? 12.957 -33.285 13.363 1.00 57.91  ? 34  MET B O   1 
ATOM 3374 C CB  . MET B 2 36  ? 13.940 -34.876 15.934 1.00 61.34  ? 34  MET B CB  1 
ATOM 3375 C CG  . MET B 2 36  ? 13.881 -35.203 17.419 1.00 56.22  ? 34  MET B CG  1 
ATOM 3376 S SD  . MET B 2 36  ? 14.820 -34.056 18.442 1.00 61.18  ? 34  MET B SD  1 
ATOM 3377 C CE  . MET B 2 36  ? 16.475 -34.722 18.277 1.00 46.61  ? 34  MET B CE  1 
ATOM 3378 N N   . ALA B 2 37  ? 15.146 -32.833 13.678 1.00 43.86  ? 35  ALA B N   1 
ATOM 3379 C CA  . ALA B 2 37  ? 15.398 -32.569 12.271 1.00 45.30  ? 35  ALA B CA  1 
ATOM 3380 C C   . ALA B 2 37  ? 16.822 -32.978 11.926 1.00 50.38  ? 35  ALA B C   1 
ATOM 3381 O O   . ALA B 2 37  ? 17.663 -33.178 12.807 1.00 46.18  ? 35  ALA B O   1 
ATOM 3382 C CB  . ALA B 2 37  ? 15.163 -31.094 11.924 1.00 52.75  ? 35  ALA B CB  1 
ATOM 3383 N N   . TRP B 2 38  ? 17.078 -33.109 10.627 1.00 45.84  ? 36  TRP B N   1 
ATOM 3384 C CA  . TRP B 2 38  ? 18.400 -33.422 10.100 1.00 47.89  ? 36  TRP B CA  1 
ATOM 3385 C C   . TRP B 2 38  ? 18.845 -32.292 9.184  1.00 52.96  ? 36  TRP B C   1 
ATOM 3386 O O   . TRP B 2 38  ? 18.081 -31.851 8.319  1.00 50.03  ? 36  TRP B O   1 
ATOM 3387 C CB  . TRP B 2 38  ? 18.397 -34.751 9.336  1.00 46.34  ? 36  TRP B CB  1 
ATOM 3388 C CG  . TRP B 2 38  ? 18.513 -35.961 10.213 1.00 46.72  ? 36  TRP B CG  1 
ATOM 3389 C CD1 . TRP B 2 38  ? 17.500 -36.781 10.613 1.00 48.61  ? 36  TRP B CD1 1 
ATOM 3390 C CD2 . TRP B 2 38  ? 19.711 -36.493 10.794 1.00 46.21  ? 36  TRP B CD2 1 
ATOM 3391 N NE1 . TRP B 2 38  ? 17.988 -37.787 11.410 1.00 47.42  ? 36  TRP B NE1 1 
ATOM 3392 C CE2 . TRP B 2 38  ? 19.344 -37.634 11.537 1.00 47.00  ? 36  TRP B CE2 1 
ATOM 3393 C CE3 . TRP B 2 38  ? 21.057 -36.115 10.761 1.00 46.03  ? 36  TRP B CE3 1 
ATOM 3394 C CZ2 . TRP B 2 38  ? 20.272 -38.399 12.239 1.00 47.59  ? 36  TRP B CZ2 1 
ATOM 3395 C CZ3 . TRP B 2 38  ? 21.978 -36.877 11.460 1.00 47.91  ? 36  TRP B CZ3 1 
ATOM 3396 C CH2 . TRP B 2 38  ? 21.581 -38.005 12.188 1.00 50.04  ? 36  TRP B CH2 1 
ATOM 3397 N N   . PHE B 2 39  ? 20.075 -31.824 9.378  1.00 47.58  ? 37  PHE B N   1 
ATOM 3398 C CA  . PHE B 2 39  ? 20.652 -30.763 8.567  1.00 46.12  ? 37  PHE B CA  1 
ATOM 3399 C C   . PHE B 2 39  ? 22.018 -31.202 8.066  1.00 53.84  ? 37  PHE B C   1 
ATOM 3400 O O   . PHE B 2 39  ? 22.790 -31.814 8.807  1.00 57.64  ? 37  PHE B O   1 
ATOM 3401 C CB  . PHE B 2 39  ? 20.793 -29.455 9.359  1.00 55.08  ? 37  PHE B CB  1 
ATOM 3402 C CG  . PHE B 2 39  ? 19.485 -28.858 9.795  1.00 52.31  ? 37  PHE B CG  1 
ATOM 3403 C CD1 . PHE B 2 39  ? 18.909 -29.222 11.001 1.00 47.81  ? 37  PHE B CD1 1 
ATOM 3404 C CD2 . PHE B 2 39  ? 18.839 -27.922 9.005  1.00 44.30  ? 37  PHE B CD2 1 
ATOM 3405 C CE1 . PHE B 2 39  ? 17.709 -28.669 11.407 1.00 50.73  ? 37  PHE B CE1 1 
ATOM 3406 C CE2 . PHE B 2 39  ? 17.638 -27.366 9.405  1.00 43.76  ? 37  PHE B CE2 1 
ATOM 3407 C CZ  . PHE B 2 39  ? 17.072 -27.740 10.608 1.00 50.68  ? 37  PHE B CZ  1 
ATOM 3408 N N   . ARG B 2 40  ? 22.312 -30.888 6.808  1.00 53.05  ? 38  ARG B N   1 
ATOM 3409 C CA  . ARG B 2 40  ? 23.613 -31.166 6.222  1.00 54.63  ? 38  ARG B CA  1 
ATOM 3410 C C   . ARG B 2 40  ? 24.292 -29.855 5.856  1.00 49.97  ? 38  ARG B C   1 
ATOM 3411 O O   . ARG B 2 40  ? 23.651 -28.805 5.764  1.00 49.95  ? 38  ARG B O   1 
ATOM 3412 C CB  . ARG B 2 40  ? 23.496 -32.061 4.981  1.00 61.34  ? 38  ARG B CB  1 
ATOM 3413 C CG  . ARG B 2 40  ? 22.576 -31.519 3.908  1.00 56.72  ? 38  ARG B CG  1 
ATOM 3414 C CD  . ARG B 2 40  ? 23.003 -31.978 2.527  1.00 62.94  ? 38  ARG B CD  1 
ATOM 3415 N NE  . ARG B 2 40  ? 22.097 -31.490 1.495  1.00 76.28  ? 38  ARG B NE  1 
ATOM 3416 C CZ  . ARG B 2 40  ? 21.389 -32.268 0.688  1.00 70.97  ? 38  ARG B CZ  1 
ATOM 3417 N NH1 . ARG B 2 40  ? 21.474 -33.588 0.748  1.00 61.33  ? 38  ARG B NH1 1 
ATOM 3418 N NH2 . ARG B 2 40  ? 20.571 -31.709 -0.199 1.00 65.08  ? 38  ARG B NH2 1 
ATOM 3419 N N   . GLN B 2 41  ? 25.604 -29.926 5.643  1.00 51.24  ? 39  GLN B N   1 
ATOM 3420 C CA  . GLN B 2 41  ? 26.382 -28.734 5.335  1.00 54.92  ? 39  GLN B CA  1 
ATOM 3421 C C   . GLN B 2 41  ? 27.647 -29.140 4.595  1.00 54.97  ? 39  GLN B C   1 
ATOM 3422 O O   . GLN B 2 41  ? 28.373 -30.029 5.049  1.00 54.74  ? 39  GLN B O   1 
ATOM 3423 C CB  . GLN B 2 41  ? 26.727 -27.961 6.614  1.00 61.48  ? 39  GLN B CB  1 
ATOM 3424 C CG  . GLN B 2 41  ? 28.061 -27.227 6.571  1.00 70.37  ? 39  GLN B CG  1 
ATOM 3425 C CD  . GLN B 2 41  ? 28.195 -26.196 7.677  1.00 82.14  ? 39  GLN B CD  1 
ATOM 3426 O OE1 . GLN B 2 41  ? 27.205 -25.613 8.121  1.00 78.41  ? 39  GLN B OE1 1 
ATOM 3427 N NE2 . GLN B 2 41  ? 29.423 -25.969 8.129  1.00 86.09  ? 39  GLN B NE2 1 
ATOM 3428 N N   . ALA B 2 42  ? 27.902 -28.485 3.452  1.00 59.80  ? 40  ALA B N   1 
ATOM 3429 C CA  . ALA B 2 42  ? 29.076 -28.634 2.610  1.00 60.81  ? 40  ALA B CA  1 
ATOM 3430 C C   . ALA B 2 42  ? 30.112 -27.567 2.949  1.00 83.82  ? 40  ALA B C   1 
ATOM 3431 O O   . ALA B 2 42  ? 29.761 -26.492 3.444  1.00 83.36  ? 40  ALA B O   1 
ATOM 3432 C CB  . ALA B 2 42  ? 28.693 -28.527 1.130  1.00 62.41  ? 40  ALA B CB  1 
ATOM 3433 N N   . PRO B 2 43  ? 31.397 -27.836 2.707  1.00 92.17  ? 41  PRO B N   1 
ATOM 3434 C CA  . PRO B 2 43  ? 32.439 -26.856 3.057  1.00 93.85  ? 41  PRO B CA  1 
ATOM 3435 C C   . PRO B 2 43  ? 32.237 -25.533 2.335  1.00 101.60 ? 41  PRO B C   1 
ATOM 3436 O O   . PRO B 2 43  ? 32.241 -25.468 1.103  1.00 108.15 ? 41  PRO B O   1 
ATOM 3437 C CB  . PRO B 2 43  ? 33.735 -27.549 2.619  1.00 93.86  ? 41  PRO B CB  1 
ATOM 3438 C CG  . PRO B 2 43  ? 33.410 -29.001 2.627  1.00 102.55 ? 41  PRO B CG  1 
ATOM 3439 C CD  . PRO B 2 43  ? 31.973 -29.098 2.211  1.00 96.02  ? 41  PRO B CD  1 
ATOM 3440 N N   . GLY B 2 44  ? 32.060 -24.470 3.119  1.00 106.52 ? 42  GLY B N   1 
ATOM 3441 C CA  . GLY B 2 44  ? 31.855 -23.141 2.588  1.00 106.45 ? 42  GLY B CA  1 
ATOM 3442 C C   . GLY B 2 44  ? 30.410 -22.750 2.374  1.00 103.24 ? 42  GLY B C   1 
ATOM 3443 O O   . GLY B 2 44  ? 30.144 -21.587 2.042  1.00 109.75 ? 42  GLY B O   1 
ATOM 3444 N N   . LYS B 2 45  ? 29.472 -23.672 2.553  1.00 81.57  ? 43  LYS B N   1 
ATOM 3445 C CA  . LYS B 2 45  ? 28.058 -23.413 2.336  1.00 81.46  ? 43  LYS B CA  1 
ATOM 3446 C C   . LYS B 2 45  ? 27.332 -23.295 3.670  1.00 76.07  ? 43  LYS B C   1 
ATOM 3447 O O   . LYS B 2 45  ? 27.869 -23.615 4.734  1.00 76.34  ? 43  LYS B O   1 
ATOM 3448 C CB  . LYS B 2 45  ? 27.428 -24.518 1.480  1.00 77.91  ? 43  LYS B CB  1 
ATOM 3449 C CG  . LYS B 2 45  ? 27.446 -24.235 -0.015 1.00 81.32  ? 43  LYS B CG  1 
ATOM 3450 C CD  . LYS B 2 45  ? 26.178 -24.734 -0.690 1.00 78.65  ? 43  LYS B CD  1 
ATOM 3451 C CE  . LYS B 2 45  ? 25.206 -23.593 -0.956 1.00 82.17  ? 43  LYS B CE  1 
ATOM 3452 N NZ  . LYS B 2 45  ? 24.174 -23.961 -1.965 1.00 71.94  ? 43  LYS B NZ  1 
ATOM 3453 N N   . GLU B 2 46  ? 26.090 -22.827 3.597  1.00 77.63  ? 44  GLU B N   1 
ATOM 3454 C CA  . GLU B 2 46  ? 25.261 -22.691 4.782  1.00 74.93  ? 44  GLU B CA  1 
ATOM 3455 C C   . GLU B 2 46  ? 24.562 -24.010 5.102  1.00 72.29  ? 44  GLU B C   1 
ATOM 3456 O O   . GLU B 2 46  ? 24.377 -24.874 4.241  1.00 82.07  ? 44  GLU B O   1 
ATOM 3457 C CB  . GLU B 2 46  ? 24.227 -21.581 4.592  1.00 88.11  ? 44  GLU B CB  1 
ATOM 3458 C CG  . GLU B 2 46  ? 23.197 -21.870 3.510  1.00 96.49  ? 44  GLU B CG  1 
ATOM 3459 C CD  . GLU B 2 46  ? 22.181 -20.753 3.356  1.00 114.08 ? 44  GLU B CD  1 
ATOM 3460 O OE1 . GLU B 2 46  ? 22.221 -19.793 4.154  1.00 112.92 ? 44  GLU B OE1 1 
ATOM 3461 O OE2 . GLU B 2 46  ? 21.343 -20.834 2.432  1.00 116.05 ? 44  GLU B OE2 1 
ATOM 3462 N N   . ARG B 2 47  ? 24.179 -24.156 6.368  1.00 68.76  ? 45  ARG B N   1 
ATOM 3463 C CA  . ARG B 2 47  ? 23.459 -25.343 6.808  1.00 51.09  ? 45  ARG B CA  1 
ATOM 3464 C C   . ARG B 2 47  ? 22.102 -25.421 6.117  1.00 55.63  ? 45  ARG B C   1 
ATOM 3465 O O   . ARG B 2 47  ? 21.317 -24.469 6.159  1.00 55.23  ? 45  ARG B O   1 
ATOM 3466 C CB  . ARG B 2 47  ? 23.283 -25.309 8.326  1.00 49.92  ? 45  ARG B CB  1 
ATOM 3467 C CG  . ARG B 2 47  ? 23.005 -26.659 8.959  1.00 68.30  ? 45  ARG B CG  1 
ATOM 3468 C CD  . ARG B 2 47  ? 23.619 -26.759 10.349 1.00 63.37  ? 45  ARG B CD  1 
ATOM 3469 N NE  . ARG B 2 47  ? 24.982 -26.244 10.390 1.00 65.40  ? 45  ARG B NE  1 
ATOM 3470 C CZ  . ARG B 2 47  ? 25.601 -25.850 11.495 1.00 74.55  ? 45  ARG B CZ  1 
ATOM 3471 N NH1 . ARG B 2 47  ? 25.002 -25.888 12.675 1.00 65.76  ? 45  ARG B NH1 1 
ATOM 3472 N NH2 . ARG B 2 47  ? 26.852 -25.406 11.415 1.00 83.29  ? 45  ARG B NH2 1 
ATOM 3473 N N   . GLU B 2 48  ? 21.828 -26.553 5.474  1.00 61.34  ? 46  GLU B N   1 
ATOM 3474 C CA  . GLU B 2 48  ? 20.586 -26.732 4.738  1.00 58.52  ? 46  GLU B CA  1 
ATOM 3475 C C   . GLU B 2 48  ? 19.727 -27.815 5.377  1.00 48.88  ? 46  GLU B C   1 
ATOM 3476 O O   . GLU B 2 48  ? 20.229 -28.732 6.033  1.00 47.92  ? 46  GLU B O   1 
ATOM 3477 C CB  . GLU B 2 48  ? 20.843 -27.078 3.266  1.00 65.10  ? 46  GLU B CB  1 
ATOM 3478 C CG  . GLU B 2 48  ? 22.078 -27.923 2.996  1.00 67.07  ? 46  GLU B CG  1 
ATOM 3479 C CD  . GLU B 2 48  ? 22.239 -28.248 1.521  1.00 74.32  ? 46  GLU B CD  1 
ATOM 3480 O OE1 . GLU B 2 48  ? 21.456 -27.715 0.706  1.00 80.21  ? 46  GLU B OE1 1 
ATOM 3481 O OE2 . GLU B 2 48  ? 23.145 -29.036 1.174  1.00 66.63  ? 46  GLU B OE2 1 
ATOM 3482 N N   . PHE B 2 49  ? 18.420 -27.690 5.164  1.00 48.95  ? 47  PHE B N   1 
ATOM 3483 C CA  . PHE B 2 49  ? 17.442 -28.602 5.737  1.00 47.92  ? 47  PHE B CA  1 
ATOM 3484 C C   . PHE B 2 49  ? 17.367 -29.892 4.929  1.00 56.42  ? 47  PHE B C   1 
ATOM 3485 O O   . PHE B 2 49  ? 17.382 -29.873 3.694  1.00 54.02  ? 47  PHE B O   1 
ATOM 3486 C CB  . PHE B 2 49  ? 16.073 -27.920 5.784  1.00 47.99  ? 47  PHE B CB  1 
ATOM 3487 C CG  . PHE B 2 49  ? 14.953 -28.815 6.225  1.00 47.61  ? 47  PHE B CG  1 
ATOM 3488 C CD1 . PHE B 2 49  ? 14.774 -29.118 7.564  1.00 50.37  ? 47  PHE B CD1 1 
ATOM 3489 C CD2 . PHE B 2 49  ? 14.063 -29.338 5.300  1.00 54.98  ? 47  PHE B CD2 1 
ATOM 3490 C CE1 . PHE B 2 49  ? 13.736 -29.937 7.971  1.00 56.04  ? 47  PHE B CE1 1 
ATOM 3491 C CE2 . PHE B 2 49  ? 13.025 -30.157 5.700  1.00 56.99  ? 47  PHE B CE2 1 
ATOM 3492 C CZ  . PHE B 2 49  ? 12.860 -30.456 7.037  1.00 57.52  ? 47  PHE B CZ  1 
ATOM 3493 N N   . VAL B 2 50  ? 17.293 -31.018 5.636  1.00 50.78  ? 48  VAL B N   1 
ATOM 3494 C CA  . VAL B 2 50  ? 17.151 -32.336 5.021  1.00 58.27  ? 48  VAL B CA  1 
ATOM 3495 C C   . VAL B 2 50  ? 15.786 -32.938 5.330  1.00 58.25  ? 48  VAL B C   1 
ATOM 3496 O O   . VAL B 2 50  ? 15.000 -33.219 4.423  1.00 56.77  ? 48  VAL B O   1 
ATOM 3497 C CB  . VAL B 2 50  ? 18.289 -33.284 5.460  1.00 49.56  ? 48  VAL B CB  1 
ATOM 3498 C CG1 . VAL B 2 50  ? 17.890 -34.737 5.233  1.00 56.32  ? 48  VAL B CG1 1 
ATOM 3499 C CG2 . VAL B 2 50  ? 19.557 -32.968 4.711  1.00 50.18  ? 48  VAL B CG2 1 
ATOM 3500 N N   . ALA B 2 51  ? 15.487 -33.147 6.608  1.00 48.08  ? 49  ALA B N   1 
ATOM 3501 C CA  . ALA B 2 51  ? 14.230 -33.752 7.006  1.00 56.61  ? 49  ALA B CA  1 
ATOM 3502 C C   . ALA B 2 51  ? 13.937 -33.353 8.441  1.00 52.66  ? 49  ALA B C   1 
ATOM 3503 O O   . ALA B 2 51  ? 14.836 -32.970 9.193  1.00 45.88  ? 49  ALA B O   1 
ATOM 3504 C CB  . ALA B 2 51  ? 14.267 -35.278 6.864  1.00 49.67  ? 49  ALA B CB  1 
ATOM 3505 N N   . ARG B 2 52  ? 12.661 -33.444 8.810  1.00 48.40  ? 50  ARG B N   1 
ATOM 3506 C CA  . ARG B 2 52  ? 12.243 -33.190 10.180 1.00 56.96  ? 50  ARG B CA  1 
ATOM 3507 C C   . ARG B 2 52  ? 11.044 -34.069 10.497 1.00 58.05  ? 50  ARG B C   1 
ATOM 3508 O O   . ARG B 2 52  ? 10.293 -34.468 9.602  1.00 56.80  ? 50  ARG B O   1 
ATOM 3509 C CB  . ARG B 2 52  ? 11.901 -31.711 10.412 1.00 60.18  ? 50  ARG B CB  1 
ATOM 3510 C CG  . ARG B 2 52  ? 10.454 -31.347 10.122 1.00 59.96  ? 50  ARG B CG  1 
ATOM 3511 C CD  . ARG B 2 52  ? 10.087 -30.001 10.726 1.00 60.73  ? 50  ARG B CD  1 
ATOM 3512 N NE  . ARG B 2 52  ? 8.704  -29.640 10.436 1.00 73.75  ? 50  ARG B NE  1 
ATOM 3513 C CZ  . ARG B 2 52  ? 8.294  -29.100 9.297  1.00 66.53  ? 50  ARG B CZ  1 
ATOM 3514 N NH1 . ARG B 2 52  ? 9.140  -28.831 8.315  1.00 56.57  ? 50  ARG B NH1 1 
ATOM 3515 N NH2 . ARG B 2 52  ? 7.003  -28.825 9.137  1.00 67.36  ? 50  ARG B NH2 1 
ATOM 3516 N N   . ILE B 2 53  ? 10.878 -34.374 11.780 1.00 54.46  ? 51  ILE B N   1 
ATOM 3517 C CA  . ILE B 2 53  ? 9.760  -35.172 12.261 1.00 56.25  ? 51  ILE B CA  1 
ATOM 3518 C C   . ILE B 2 53  ? 9.051  -34.391 13.360 1.00 59.80  ? 51  ILE B C   1 
ATOM 3519 O O   . ILE B 2 53  ? 9.693  -33.715 14.172 1.00 58.66  ? 51  ILE B O   1 
ATOM 3520 C CB  . ILE B 2 53  ? 10.223 -36.561 12.759 1.00 62.53  ? 51  ILE B CB  1 
ATOM 3521 C CG1 . ILE B 2 53  ? 9.020  -37.462 13.044 1.00 60.38  ? 51  ILE B CG1 1 
ATOM 3522 C CG2 . ILE B 2 53  ? 11.129 -36.444 13.980 1.00 64.20  ? 51  ILE B CG2 1 
ATOM 3523 C CD1 . ILE B 2 53  ? 9.226  -38.895 12.617 1.00 71.92  ? 51  ILE B CD1 1 
ATOM 3524 N N   . SER B 2 54  ? 7.724  -34.460 13.364 1.00 58.12  ? 52  SER B N   1 
ATOM 3525 C CA  . SER B 2 54  ? 6.945  -33.709 14.332 1.00 58.63  ? 52  SER B CA  1 
ATOM 3526 C C   . SER B 2 54  ? 6.958  -34.408 15.687 1.00 70.00  ? 52  SER B C   1 
ATOM 3527 O O   . SER B 2 54  ? 7.253  -35.601 15.804 1.00 70.54  ? 52  SER B O   1 
ATOM 3528 C CB  . SER B 2 54  ? 5.506  -33.527 13.848 1.00 63.98  ? 52  SER B CB  1 
ATOM 3529 O OG  . SER B 2 54  ? 4.740  -32.797 14.793 1.00 65.09  ? 52  SER B OG  1 
ATOM 3530 N N   . GLU B 2 55  ? 6.632  -33.641 16.720 1.00 63.64  ? 53  GLU B N   1 
ATOM 3531 C CA  . GLU B 2 55  ? 6.589  -34.142 18.085 1.00 62.20  ? 53  GLU B CA  1 
ATOM 3532 C C   . GLU B 2 55  ? 5.238  -34.740 18.454 1.00 66.91  ? 53  GLU B C   1 
ATOM 3533 O O   . GLU B 2 55  ? 5.061  -35.171 19.599 1.00 81.64  ? 53  GLU B O   1 
ATOM 3534 C CB  . GLU B 2 55  ? 6.937  -33.013 19.061 1.00 62.76  ? 53  GLU B CB  1 
ATOM 3535 C CG  . GLU B 2 55  ? 5.759  -32.119 19.434 1.00 68.95  ? 53  GLU B CG  1 
ATOM 3536 C CD  . GLU B 2 55  ? 5.236  -31.311 18.257 1.00 72.54  ? 53  GLU B CD  1 
ATOM 3537 O OE1 . GLU B 2 55  ? 4.006  -31.298 18.042 1.00 73.17  ? 53  GLU B OE1 1 
ATOM 3538 O OE2 . GLU B 2 55  ? 6.054  -30.694 17.544 1.00 62.76  ? 53  GLU B OE2 1 
ATOM 3539 N N   . SER B 2 56  ? 4.287  -34.794 17.517 1.00 68.10  ? 54  SER B N   1 
ATOM 3540 C CA  . SER B 2 56  ? 2.923  -35.156 17.858 1.00 77.98  ? 54  SER B CA  1 
ATOM 3541 C C   . SER B 2 56  ? 2.609  -36.505 17.242 1.00 88.26  ? 54  SER B C   1 
ATOM 3542 O O   . SER B 2 56  ? 2.803  -37.545 17.901 1.00 92.86  ? 54  SER B O   1 
ATOM 3543 C CB  . SER B 2 56  ? 1.964  -34.033 17.428 1.00 77.18  ? 54  SER B CB  1 
ATOM 3544 O OG  . SER B 2 56  ? 0.624  -34.345 17.768 1.00 84.21  ? 54  SER B OG  1 
ATOM 3545 N N   . ARG B 2 57  ? 2.132  -36.567 15.996 1.00 82.54  ? 55  ARG B N   1 
ATOM 3546 C CA  . ARG B 2 57  ? 1.735  -37.822 15.369 1.00 88.73  ? 55  ARG B CA  1 
ATOM 3547 C C   . ARG B 2 57  ? 2.826  -38.419 14.488 1.00 84.37  ? 55  ARG B C   1 
ATOM 3548 O O   . ARG B 2 57  ? 2.557  -39.368 13.746 1.00 80.67  ? 55  ARG B O   1 
ATOM 3549 C CB  . ARG B 2 57  ? 0.459  -37.630 14.538 1.00 85.70  ? 55  ARG B CB  1 
ATOM 3550 C CG  . ARG B 2 57  ? -0.768 -37.193 15.330 1.00 94.06  ? 55  ARG B CG  1 
ATOM 3551 C CD  . ARG B 2 57  ? -0.874 -35.677 15.395 1.00 99.38  ? 55  ARG B CD  1 
ATOM 3552 N NE  . ARG B 2 57  ? -2.233 -35.180 15.211 1.00 107.69 ? 55  ARG B NE  1 
ATOM 3553 C CZ  . ARG B 2 57  ? -2.951 -34.616 16.173 1.00 106.59 ? 55  ARG B CZ  1 
ATOM 3554 N NH1 . ARG B 2 57  ? -2.480 -34.494 17.404 1.00 106.69 ? 55  ARG B NH1 1 
ATOM 3555 N NH2 . ARG B 2 57  ? -4.167 -34.156 15.892 1.00 101.34 ? 55  ARG B NH2 1 
ATOM 3556 N N   . GLY B 2 58  ? 4.045  -37.890 14.551 1.00 88.86  ? 56  GLY B N   1 
ATOM 3557 C CA  . GLY B 2 58  ? 5.109  -38.379 13.698 1.00 85.68  ? 56  GLY B CA  1 
ATOM 3558 C C   . GLY B 2 58  ? 5.083  -37.829 12.291 1.00 88.09  ? 56  GLY B C   1 
ATOM 3559 O O   . GLY B 2 58  ? 5.549  -38.498 11.363 1.00 88.69  ? 56  GLY B O   1 
ATOM 3560 N N   . THR B 2 59  ? 4.543  -36.627 12.103 1.00 84.56  ? 57  THR B N   1 
ATOM 3561 C CA  . THR B 2 59  ? 4.485  -36.031 10.776 1.00 72.65  ? 57  THR B CA  1 
ATOM 3562 C C   . THR B 2 59  ? 5.882  -35.658 10.300 1.00 68.17  ? 57  THR B C   1 
ATOM 3563 O O   . THR B 2 59  ? 6.690  -35.109 11.054 1.00 61.97  ? 57  THR B O   1 
ATOM 3564 C CB  . THR B 2 59  ? 3.584  -34.797 10.780 1.00 70.87  ? 57  THR B CB  1 
ATOM 3565 O OG1 . THR B 2 59  ? 2.382  -35.086 11.505 1.00 84.27  ? 57  THR B OG1 1 
ATOM 3566 C CG2 . THR B 2 59  ? 3.225  -34.394 9.356  1.00 72.22  ? 57  THR B CG2 1 
ATOM 3567 N N   . THR B 2 60  ? 6.163  -35.959 9.037  1.00 64.24  ? 58  THR B N   1 
ATOM 3568 C CA  . THR B 2 60  ? 7.492  -35.799 8.473  1.00 61.70  ? 58  THR B CA  1 
ATOM 3569 C C   . THR B 2 60  ? 7.474  -34.753 7.368  1.00 63.85  ? 58  THR B C   1 
ATOM 3570 O O   . THR B 2 60  ? 6.445  -34.519 6.726  1.00 64.73  ? 58  THR B O   1 
ATOM 3571 C CB  . THR B 2 60  ? 8.013  -37.124 7.914  1.00 56.85  ? 58  THR B CB  1 
ATOM 3572 O OG1 . THR B 2 60  ? 6.949  -37.800 7.235  1.00 60.53  ? 58  THR B OG1 1 
ATOM 3573 C CG2 . THR B 2 60  ? 8.514  -38.008 9.042  1.00 61.91  ? 58  THR B CG2 1 
ATOM 3574 N N   . ASP B 2 61  ? 8.628  -34.127 7.155  1.00 59.08  ? 59  ASP B N   1 
ATOM 3575 C CA  . ASP B 2 61  ? 8.817  -33.164 6.082  1.00 62.54  ? 59  ASP B CA  1 
ATOM 3576 C C   . ASP B 2 61  ? 10.228 -33.314 5.537  1.00 61.61  ? 59  ASP B C   1 
ATOM 3577 O O   . ASP B 2 61  ? 11.181 -33.472 6.304  1.00 59.17  ? 59  ASP B O   1 
ATOM 3578 C CB  . ASP B 2 61  ? 8.585  -31.726 6.566  1.00 69.96  ? 59  ASP B CB  1 
ATOM 3579 C CG  . ASP B 2 61  ? 8.801  -30.701 5.471  1.00 73.80  ? 59  ASP B CG  1 
ATOM 3580 O OD1 . ASP B 2 61  ? 8.359  -30.947 4.328  1.00 80.13  ? 59  ASP B OD1 1 
ATOM 3581 O OD2 . ASP B 2 61  ? 9.415  -29.650 5.752  1.00 72.10  ? 59  ASP B OD2 1 
ATOM 3582 N N   . TYR B 2 62  ? 10.355 -33.267 4.213  1.00 62.72  ? 60  TYR B N   1 
ATOM 3583 C CA  . TYR B 2 62  ? 11.634 -33.458 3.546  1.00 67.63  ? 60  TYR B CA  1 
ATOM 3584 C C   . TYR B 2 62  ? 11.906 -32.288 2.612  1.00 70.99  ? 60  TYR B C   1 
ATOM 3585 O O   . TYR B 2 62  ? 11.006 -31.522 2.257  1.00 70.50  ? 60  TYR B O   1 
ATOM 3586 C CB  . TYR B 2 62  ? 11.670 -34.778 2.760  1.00 56.86  ? 60  TYR B CB  1 
ATOM 3587 C CG  . TYR B 2 62  ? 11.342 -35.995 3.596  1.00 56.69  ? 60  TYR B CG  1 
ATOM 3588 C CD1 . TYR B 2 62  ? 10.033 -36.442 3.721  1.00 58.34  ? 60  TYR B CD1 1 
ATOM 3589 C CD2 . TYR B 2 62  ? 12.338 -36.694 4.265  1.00 55.30  ? 60  TYR B CD2 1 
ATOM 3590 C CE1 . TYR B 2 62  ? 9.725  -37.551 4.488  1.00 61.36  ? 60  TYR B CE1 1 
ATOM 3591 C CE2 . TYR B 2 62  ? 12.040 -37.805 5.036  1.00 55.58  ? 60  TYR B CE2 1 
ATOM 3592 C CZ  . TYR B 2 62  ? 10.731 -38.230 5.142  1.00 59.54  ? 60  TYR B CZ  1 
ATOM 3593 O OH  . TYR B 2 62  ? 10.424 -39.335 5.905  1.00 58.10  ? 60  TYR B OH  1 
ATOM 3594 N N   . ALA B 2 63  ? 13.169 -32.160 2.221  1.00 71.25  ? 61  ALA B N   1 
ATOM 3595 C CA  . ALA B 2 63  ? 13.562 -31.136 1.272  1.00 64.04  ? 61  ALA B CA  1 
ATOM 3596 C C   . ALA B 2 63  ? 13.171 -31.548 -0.143 1.00 70.40  ? 61  ALA B C   1 
ATOM 3597 O O   . ALA B 2 63  ? 12.915 -32.719 -0.431 1.00 72.73  ? 61  ALA B O   1 
ATOM 3598 C CB  . ALA B 2 63  ? 15.069 -30.883 1.345  1.00 58.54  ? 61  ALA B CB  1 
ATOM 3599 N N   . ASP B 2 64  ? 13.122 -30.557 -1.035 1.00 77.34  ? 62  ASP B N   1 
ATOM 3600 C CA  . ASP B 2 64  ? 12.946 -30.852 -2.449 1.00 77.75  ? 62  ASP B CA  1 
ATOM 3601 C C   . ASP B 2 64  ? 14.131 -31.613 -3.028 1.00 78.61  ? 62  ASP B C   1 
ATOM 3602 O O   . ASP B 2 64  ? 14.024 -32.152 -4.133 1.00 83.98  ? 62  ASP B O   1 
ATOM 3603 C CB  . ASP B 2 64  ? 12.725 -29.558 -3.233 1.00 73.31  ? 62  ASP B CB  1 
ATOM 3604 C CG  . ASP B 2 64  ? 11.596 -28.716 -2.662 1.00 86.11  ? 62  ASP B CG  1 
ATOM 3605 O OD1 . ASP B 2 64  ? 10.996 -29.130 -1.649 1.00 97.66  ? 62  ASP B OD1 1 
ATOM 3606 O OD2 . ASP B 2 64  ? 11.307 -27.640 -3.228 1.00 83.36  ? 62  ASP B OD2 1 
ATOM 3607 N N   . SER B 2 65  ? 15.250 -31.675 -2.308 1.00 75.98  ? 63  SER B N   1 
ATOM 3608 C CA  . SER B 2 65  ? 16.437 -32.353 -2.808 1.00 69.45  ? 63  SER B CA  1 
ATOM 3609 C C   . SER B 2 65  ? 16.414 -33.843 -2.489 1.00 77.41  ? 63  SER B C   1 
ATOM 3610 O O   . SER B 2 65  ? 16.871 -34.661 -3.296 1.00 78.58  ? 63  SER B O   1 
ATOM 3611 C CB  . SER B 2 65  ? 17.688 -31.698 -2.217 1.00 73.40  ? 63  SER B CB  1 
ATOM 3612 O OG  . SER B 2 65  ? 18.750 -32.629 -2.121 1.00 84.60  ? 63  SER B OG  1 
ATOM 3613 N N   . VAL B 2 66  ? 15.885 -34.215 -1.324 1.00 71.09  ? 64  VAL B N   1 
ATOM 3614 C CA  . VAL B 2 66  ? 16.001 -35.580 -0.826 1.00 70.80  ? 64  VAL B CA  1 
ATOM 3615 C C   . VAL B 2 66  ? 14.676 -36.328 -0.806 1.00 68.56  ? 64  VAL B C   1 
ATOM 3616 O O   . VAL B 2 66  ? 14.679 -37.539 -0.531 1.00 61.83  ? 64  VAL B O   1 
ATOM 3617 C CB  . VAL B 2 66  ? 16.641 -35.606 0.579  1.00 66.52  ? 64  VAL B CB  1 
ATOM 3618 C CG1 . VAL B 2 66  ? 18.118 -35.247 0.493  1.00 58.03  ? 64  VAL B CG1 1 
ATOM 3619 C CG2 . VAL B 2 66  ? 15.904 -34.666 1.524  1.00 62.24  ? 64  VAL B CG2 1 
ATOM 3620 N N   . LYS B 2 67  ? 13.555 -35.665 -1.093 1.00 62.98  ? 65  LYS B N   1 
ATOM 3621 C CA  . LYS B 2 67  ? 12.252 -36.306 -0.967 1.00 64.22  ? 65  LYS B CA  1 
ATOM 3622 C C   . LYS B 2 67  ? 12.166 -37.538 -1.859 1.00 68.49  ? 65  LYS B C   1 
ATOM 3623 O O   . LYS B 2 67  ? 12.406 -37.467 -3.068 1.00 78.38  ? 65  LYS B O   1 
ATOM 3624 C CB  . LYS B 2 67  ? 11.139 -35.322 -1.319 1.00 65.65  ? 65  LYS B CB  1 
ATOM 3625 C CG  . LYS B 2 67  ? 9.772  -35.722 -0.783 1.00 66.30  ? 65  LYS B CG  1 
ATOM 3626 C CD  . LYS B 2 67  ? 8.728  -34.671 -1.118 1.00 71.07  ? 65  LYS B CD  1 
ATOM 3627 C CE  . LYS B 2 67  ? 7.355  -35.068 -0.602 1.00 68.82  ? 65  LYS B CE  1 
ATOM 3628 N NZ  . LYS B 2 67  ? 6.281  -34.180 -1.129 1.00 71.11  ? 65  LYS B NZ  1 
ATOM 3629 N N   . GLY B 2 68  ? 11.825 -38.672 -1.252 1.00 66.83  ? 66  GLY B N   1 
ATOM 3630 C CA  . GLY B 2 68  ? 11.765 -39.930 -1.968 1.00 69.43  ? 66  GLY B CA  1 
ATOM 3631 C C   . GLY B 2 68  ? 12.951 -40.823 -1.670 1.00 68.17  ? 66  GLY B C   1 
ATOM 3632 O O   . GLY B 2 68  ? 12.801 -42.039 -1.520 1.00 69.19  ? 66  GLY B O   1 
ATOM 3633 N N   . ARG B 2 69  ? 14.139 -40.226 -1.577 1.00 66.23  ? 67  ARG B N   1 
ATOM 3634 C CA  . ARG B 2 69  ? 15.355 -40.981 -1.302 1.00 65.16  ? 67  ARG B CA  1 
ATOM 3635 C C   . ARG B 2 69  ? 15.709 -41.019 0.177  1.00 65.81  ? 67  ARG B C   1 
ATOM 3636 O O   . ARG B 2 69  ? 16.308 -41.998 0.636  1.00 70.57  ? 67  ARG B O   1 
ATOM 3637 C CB  . ARG B 2 69  ? 16.529 -40.394 -2.088 1.00 65.38  ? 67  ARG B CB  1 
ATOM 3638 C CG  . ARG B 2 69  ? 16.162 -39.915 -3.477 1.00 68.39  ? 67  ARG B CG  1 
ATOM 3639 C CD  . ARG B 2 69  ? 17.322 -39.186 -4.128 1.00 70.35  ? 67  ARG B CD  1 
ATOM 3640 N NE  . ARG B 2 69  ? 17.661 -37.953 -3.429 1.00 67.59  ? 67  ARG B NE  1 
ATOM 3641 C CZ  . ARG B 2 69  ? 18.873 -37.655 -2.981 1.00 64.76  ? 67  ARG B CZ  1 
ATOM 3642 N NH1 . ARG B 2 69  ? 19.888 -38.492 -3.122 1.00 65.02  ? 67  ARG B NH1 1 
ATOM 3643 N NH2 . ARG B 2 69  ? 19.074 -36.486 -2.381 1.00 63.04  ? 67  ARG B NH2 1 
ATOM 3644 N N   . PHE B 2 70  ? 15.364 -39.981 0.933  1.00 65.21  ? 68  PHE B N   1 
ATOM 3645 C CA  . PHE B 2 70  ? 15.636 -39.933 2.361  1.00 57.84  ? 68  PHE B CA  1 
ATOM 3646 C C   . PHE B 2 70  ? 14.356 -40.198 3.142  1.00 58.05  ? 68  PHE B C   1 
ATOM 3647 O O   . PHE B 2 70  ? 13.256 -39.849 2.705  1.00 59.35  ? 68  PHE B O   1 
ATOM 3648 C CB  . PHE B 2 70  ? 16.219 -38.577 2.772  1.00 62.40  ? 68  PHE B CB  1 
ATOM 3649 C CG  . PHE B 2 70  ? 17.670 -38.391 2.410  1.00 63.44  ? 68  PHE B CG  1 
ATOM 3650 C CD1 . PHE B 2 70  ? 18.223 -39.034 1.313  1.00 57.26  ? 68  PHE B CD1 1 
ATOM 3651 C CD2 . PHE B 2 70  ? 18.479 -37.560 3.168  1.00 66.00  ? 68  PHE B CD2 1 
ATOM 3652 C CE1 . PHE B 2 70  ? 19.552 -38.853 0.981  1.00 58.22  ? 68  PHE B CE1 1 
ATOM 3653 C CE2 . PHE B 2 70  ? 19.811 -37.375 2.842  1.00 67.78  ? 68  PHE B CE2 1 
ATOM 3654 C CZ  . PHE B 2 70  ? 20.348 -38.024 1.746  1.00 67.56  ? 68  PHE B CZ  1 
ATOM 3655 N N   . THR B 2 71  ? 14.509 -40.824 4.308  1.00 63.06  ? 69  THR B N   1 
ATOM 3656 C CA  . THR B 2 71  ? 13.383 -41.130 5.184  1.00 65.02  ? 69  THR B CA  1 
ATOM 3657 C C   . THR B 2 71  ? 13.826 -40.937 6.624  1.00 69.91  ? 69  THR B C   1 
ATOM 3658 O O   . THR B 2 71  ? 14.795 -41.563 7.064  1.00 74.31  ? 69  THR B O   1 
ATOM 3659 C CB  . THR B 2 71  ? 12.875 -42.560 4.968  1.00 65.72  ? 69  THR B CB  1 
ATOM 3660 O OG1 . THR B 2 71  ? 12.551 -42.755 3.586  1.00 70.08  ? 69  THR B OG1 1 
ATOM 3661 C CG2 . THR B 2 71  ? 11.635 -42.819 5.814  1.00 65.85  ? 69  THR B CG2 1 
ATOM 3662 N N   . ILE B 2 72  ? 13.122 -40.075 7.354  1.00 58.09  ? 70  ILE B N   1 
ATOM 3663 C CA  . ILE B 2 72  ? 13.426 -39.810 8.755  1.00 56.18  ? 70  ILE B CA  1 
ATOM 3664 C C   . ILE B 2 72  ? 12.407 -40.526 9.630  1.00 59.29  ? 70  ILE B C   1 
ATOM 3665 O O   . ILE B 2 72  ? 11.242 -40.712 9.254  1.00 56.45  ? 70  ILE B O   1 
ATOM 3666 C CB  . ILE B 2 72  ? 13.462 -38.293 9.053  1.00 63.56  ? 70  ILE B CB  1 
ATOM 3667 C CG1 . ILE B 2 72  ? 14.301 -38.008 10.300 1.00 61.34  ? 70  ILE B CG1 1 
ATOM 3668 C CG2 . ILE B 2 72  ? 12.063 -37.731 9.217  1.00 58.36  ? 70  ILE B CG2 1 
ATOM 3669 C CD1 . ILE B 2 72  ? 14.133 -36.604 10.836 1.00 48.87  ? 70  ILE B CD1 1 
ATOM 3670 N N   . SER B 2 73  ? 12.861 -40.954 10.806 1.00 56.85  ? 71  SER B N   1 
ATOM 3671 C CA  . SER B 2 73  ? 12.009 -41.646 11.761 1.00 59.48  ? 71  SER B CA  1 
ATOM 3672 C C   . SER B 2 73  ? 12.523 -41.367 13.164 1.00 55.50  ? 71  SER B C   1 
ATOM 3673 O O   . SER B 2 73  ? 13.667 -40.947 13.357 1.00 53.81  ? 71  SER B O   1 
ATOM 3674 C CB  . SER B 2 73  ? 11.963 -43.158 11.492 1.00 73.26  ? 71  SER B CB  1 
ATOM 3675 O OG  . SER B 2 73  ? 13.261 -43.728 11.512 1.00 60.54  ? 71  SER B OG  1 
ATOM 3676 N N   . ARG B 2 74  ? 11.659 -41.608 14.147 1.00 57.06  ? 72  ARG B N   1 
ATOM 3677 C CA  . ARG B 2 74  ? 11.974 -41.342 15.542 1.00 63.35  ? 72  ARG B CA  1 
ATOM 3678 C C   . ARG B 2 74  ? 11.563 -42.526 16.404 1.00 62.49  ? 72  ARG B C   1 
ATOM 3679 O O   . ARG B 2 74  ? 10.669 -43.298 16.048 1.00 62.26  ? 72  ARG B O   1 
ATOM 3680 C CB  . ARG B 2 74  ? 11.277 -40.069 16.046 1.00 55.74  ? 72  ARG B CB  1 
ATOM 3681 C CG  . ARG B 2 74  ? 9.766  -40.197 16.149 1.00 57.76  ? 72  ARG B CG  1 
ATOM 3682 C CD  . ARG B 2 74  ? 9.139  -38.980 16.807 1.00 59.95  ? 72  ARG B CD  1 
ATOM 3683 N NE  . ARG B 2 74  ? 10.080 -38.255 17.652 1.00 76.39  ? 72  ARG B NE  1 
ATOM 3684 C CZ  . ARG B 2 74  ? 10.137 -36.933 17.748 1.00 66.37  ? 72  ARG B CZ  1 
ATOM 3685 N NH1 . ARG B 2 74  ? 9.328  -36.154 17.048 1.00 64.00  ? 72  ARG B NH1 1 
ATOM 3686 N NH2 . ARG B 2 74  ? 11.026 -36.379 18.567 1.00 61.51  ? 72  ARG B NH2 1 
ATOM 3687 N N   . ASP B 2 75  ? 12.235 -42.657 17.545 1.00 69.93  ? 73  ASP B N   1 
ATOM 3688 C CA  . ASP B 2 75  ? 11.915 -43.678 18.541 1.00 63.99  ? 73  ASP B CA  1 
ATOM 3689 C C   . ASP B 2 75  ? 12.058 -43.022 19.910 1.00 64.08  ? 73  ASP B C   1 
ATOM 3690 O O   . ASP B 2 75  ? 13.168 -42.919 20.442 1.00 68.12  ? 73  ASP B O   1 
ATOM 3691 C CB  . ASP B 2 75  ? 12.823 -44.895 18.405 1.00 65.36  ? 73  ASP B CB  1 
ATOM 3692 C CG  . ASP B 2 75  ? 12.277 -46.113 19.123 1.00 72.71  ? 73  ASP B CG  1 
ATOM 3693 O OD1 . ASP B 2 75  ? 11.105 -46.082 19.555 1.00 72.77  ? 73  ASP B OD1 1 
ATOM 3694 O OD2 . ASP B 2 75  ? 13.025 -47.104 19.256 1.00 79.72  ? 73  ASP B OD2 1 
ATOM 3695 N N   . ASN B 2 76  ? 10.933 -42.570 20.469 1.00 66.61  ? 74  ASN B N   1 
ATOM 3696 C CA  . ASN B 2 76  ? 10.958 -41.894 21.761 1.00 68.22  ? 74  ASN B CA  1 
ATOM 3697 C C   . ASN B 2 76  ? 11.418 -42.804 22.890 1.00 68.36  ? 74  ASN B C   1 
ATOM 3698 O O   . ASN B 2 76  ? 11.928 -42.305 23.898 1.00 75.20  ? 74  ASN B O   1 
ATOM 3699 C CB  . ASN B 2 76  ? 9.574  -41.333 22.084 1.00 66.66  ? 74  ASN B CB  1 
ATOM 3700 C CG  . ASN B 2 76  ? 9.069  -40.380 21.018 1.00 68.09  ? 74  ASN B CG  1 
ATOM 3701 O OD1 . ASN B 2 76  ? 9.828  -39.574 20.480 1.00 63.12  ? 74  ASN B OD1 1 
ATOM 3702 N ND2 . ASN B 2 76  ? 7.780  -40.465 20.710 1.00 73.79  ? 74  ASN B ND2 1 
ATOM 3703 N N   . ALA B 2 77  ? 11.254 -44.120 22.744 1.00 71.41  ? 75  ALA B N   1 
ATOM 3704 C CA  . ALA B 2 77  ? 11.658 -45.038 23.805 1.00 74.82  ? 75  ALA B CA  1 
ATOM 3705 C C   . ALA B 2 77  ? 13.166 -45.021 24.014 1.00 73.59  ? 75  ALA B C   1 
ATOM 3706 O O   . ALA B 2 77  ? 13.641 -45.125 25.151 1.00 76.40  ? 75  ALA B O   1 
ATOM 3707 C CB  . ALA B 2 77  ? 11.180 -46.454 23.487 1.00 78.27  ? 75  ALA B CB  1 
ATOM 3708 N N   . LYS B 2 78  ? 13.935 -44.895 22.935 1.00 70.56  ? 76  LYS B N   1 
ATOM 3709 C CA  . LYS B 2 78  ? 15.389 -44.884 23.015 1.00 69.50  ? 76  LYS B CA  1 
ATOM 3710 C C   . LYS B 2 78  ? 15.980 -43.489 22.874 1.00 65.92  ? 76  LYS B C   1 
ATOM 3711 O O   . LYS B 2 78  ? 17.208 -43.353 22.853 1.00 64.96  ? 76  LYS B O   1 
ATOM 3712 C CB  . LYS B 2 78  ? 15.984 -45.807 21.945 1.00 69.20  ? 76  LYS B CB  1 
ATOM 3713 C CG  . LYS B 2 78  ? 15.515 -47.251 22.038 1.00 73.00  ? 76  LYS B CG  1 
ATOM 3714 C CD  . LYS B 2 78  ? 16.476 -48.193 21.326 1.00 80.71  ? 76  LYS B CD  1 
ATOM 3715 C CE  . LYS B 2 78  ? 15.919 -48.644 19.982 1.00 88.04  ? 76  LYS B CE  1 
ATOM 3716 N NZ  . LYS B 2 78  ? 15.799 -47.514 19.018 1.00 71.33  ? 76  LYS B NZ  1 
ATOM 3717 N N   . ASN B 2 79  ? 15.140 -42.455 22.778 1.00 64.21  ? 77  ASN B N   1 
ATOM 3718 C CA  . ASN B 2 79  ? 15.597 -41.072 22.628 1.00 63.43  ? 77  ASN B CA  1 
ATOM 3719 C C   . ASN B 2 79  ? 16.505 -40.915 21.410 1.00 60.60  ? 77  ASN B C   1 
ATOM 3720 O O   . ASN B 2 79  ? 17.499 -40.187 21.442 1.00 58.32  ? 77  ASN B O   1 
ATOM 3721 C CB  . ASN B 2 79  ? 16.301 -40.579 23.895 1.00 61.99  ? 77  ASN B CB  1 
ATOM 3722 C CG  . ASN B 2 79  ? 15.328 -40.163 24.979 1.00 63.69  ? 77  ASN B CG  1 
ATOM 3723 O OD1 . ASN B 2 79  ? 14.238 -40.721 25.101 1.00 73.59  ? 77  ASN B OD1 1 
ATOM 3724 N ND2 . ASN B 2 79  ? 15.719 -39.173 25.774 1.00 63.27  ? 77  ASN B ND2 1 
ATOM 3725 N N   . THR B 2 80  ? 16.162 -41.605 20.324 1.00 60.27  ? 78  THR B N   1 
ATOM 3726 C CA  . THR B 2 80  ? 16.964 -41.595 19.110 1.00 62.00  ? 78  THR B CA  1 
ATOM 3727 C C   . THR B 2 80  ? 16.089 -41.300 17.901 1.00 60.21  ? 78  THR B C   1 
ATOM 3728 O O   . THR B 2 80  ? 14.892 -41.600 17.888 1.00 57.19  ? 78  THR B O   1 
ATOM 3729 C CB  . THR B 2 80  ? 17.691 -42.934 18.897 1.00 59.08  ? 78  THR B CB  1 
ATOM 3730 O OG1 . THR B 2 80  ? 16.745 -44.008 18.956 1.00 60.68  ? 78  THR B OG1 1 
ATOM 3731 C CG2 . THR B 2 80  ? 18.759 -43.143 19.958 1.00 59.48  ? 78  THR B CG2 1 
ATOM 3732 N N   . ILE B 2 81  ? 16.705 -40.705 16.881 1.00 60.62  ? 79  ILE B N   1 
ATOM 3733 C CA  . ILE B 2 81  ? 16.069 -40.488 15.589 1.00 66.75  ? 79  ILE B CA  1 
ATOM 3734 C C   . ILE B 2 81  ? 16.964 -41.078 14.509 1.00 60.17  ? 79  ILE B C   1 
ATOM 3735 O O   . ILE B 2 81  ? 18.188 -41.144 14.657 1.00 54.55  ? 79  ILE B O   1 
ATOM 3736 C CB  . ILE B 2 81  ? 15.792 -38.995 15.314 1.00 56.35  ? 79  ILE B CB  1 
ATOM 3737 C CG1 . ILE B 2 81  ? 17.068 -38.169 15.486 1.00 50.48  ? 79  ILE B CG1 1 
ATOM 3738 C CG2 . ILE B 2 81  ? 14.693 -38.488 16.229 1.00 56.71  ? 79  ILE B CG2 1 
ATOM 3739 C CD1 . ILE B 2 81  ? 17.001 -36.799 14.844 1.00 56.38  ? 79  ILE B CD1 1 
ATOM 3740 N N   . TYR B 2 82  ? 16.343 -41.514 13.418 1.00 60.83  ? 80  TYR B N   1 
ATOM 3741 C CA  . TYR B 2 82  ? 17.045 -42.180 12.335 1.00 67.22  ? 80  TYR B CA  1 
ATOM 3742 C C   . TYR B 2 82  ? 16.790 -41.460 11.019 1.00 63.08  ? 80  TYR B C   1 
ATOM 3743 O O   . TYR B 2 82  ? 15.751 -40.822 10.830 1.00 65.96  ? 80  TYR B O   1 
ATOM 3744 C CB  . TYR B 2 82  ? 16.614 -43.647 12.214 1.00 70.30  ? 80  TYR B CB  1 
ATOM 3745 C CG  . TYR B 2 82  ? 16.822 -44.448 13.478 1.00 71.07  ? 80  TYR B CG  1 
ATOM 3746 C CD1 . TYR B 2 82  ? 18.100 -44.701 13.960 1.00 72.96  ? 80  TYR B CD1 1 
ATOM 3747 C CD2 . TYR B 2 82  ? 15.741 -44.950 14.192 1.00 68.47  ? 80  TYR B CD2 1 
ATOM 3748 C CE1 . TYR B 2 82  ? 18.296 -45.433 15.116 1.00 75.70  ? 80  TYR B CE1 1 
ATOM 3749 C CE2 . TYR B 2 82  ? 15.928 -45.683 15.349 1.00 75.10  ? 80  TYR B CE2 1 
ATOM 3750 C CZ  . TYR B 2 82  ? 17.208 -45.921 15.806 1.00 75.64  ? 80  TYR B CZ  1 
ATOM 3751 O OH  . TYR B 2 82  ? 17.400 -46.650 16.957 1.00 73.99  ? 80  TYR B OH  1 
ATOM 3752 N N   . LEU B 2 83  ? 17.756 -41.570 10.109 1.00 58.96  ? 81  LEU B N   1 
ATOM 3753 C CA  . LEU B 2 83  ? 17.631 -41.012 8.764  1.00 62.90  ? 81  LEU B CA  1 
ATOM 3754 C C   . LEU B 2 83  ? 18.166 -42.042 7.780  1.00 60.63  ? 81  LEU B C   1 
ATOM 3755 O O   . LEU B 2 83  ? 19.382 -42.232 7.677  1.00 54.02  ? 81  LEU B O   1 
ATOM 3756 C CB  . LEU B 2 83  ? 18.384 -39.688 8.631  1.00 50.05  ? 81  LEU B CB  1 
ATOM 3757 C CG  . LEU B 2 83  ? 18.274 -39.013 7.262  1.00 53.97  ? 81  LEU B CG  1 
ATOM 3758 C CD1 . LEU B 2 83  ? 16.851 -38.538 7.010  1.00 52.72  ? 81  LEU B CD1 1 
ATOM 3759 C CD2 . LEU B 2 83  ? 19.259 -37.861 7.142  1.00 50.53  ? 81  LEU B CD2 1 
ATOM 3760 N N   . GLN B 2 84  ? 17.262 -42.711 7.070  1.00 65.07  ? 82  GLN B N   1 
ATOM 3761 C CA  . GLN B 2 84  ? 17.638 -43.696 6.064  1.00 62.65  ? 82  GLN B CA  1 
ATOM 3762 C C   . GLN B 2 84  ? 17.786 -42.991 4.721  1.00 62.09  ? 82  GLN B C   1 
ATOM 3763 O O   . GLN B 2 84  ? 16.807 -42.478 4.167  1.00 63.84  ? 82  GLN B O   1 
ATOM 3764 C CB  . GLN B 2 84  ? 16.606 -44.819 5.987  1.00 62.67  ? 82  GLN B CB  1 
ATOM 3765 C CG  . GLN B 2 84  ? 16.988 -45.946 5.039  1.00 70.39  ? 82  GLN B CG  1 
ATOM 3766 C CD  . GLN B 2 84  ? 18.284 -46.630 5.434  1.00 72.01  ? 82  GLN B CD  1 
ATOM 3767 O OE1 . GLN B 2 84  ? 19.261 -46.614 4.685  1.00 68.30  ? 82  GLN B OE1 1 
ATOM 3768 N NE2 . GLN B 2 84  ? 18.298 -47.236 6.616  1.00 84.84  ? 82  GLN B NE2 1 
ATOM 3769 N N   . MET B 2 85  ? 19.010 -42.961 4.202  1.00 59.85  ? 83  MET B N   1 
ATOM 3770 C CA  . MET B 2 85  ? 19.312 -42.360 2.908  1.00 61.08  ? 83  MET B CA  1 
ATOM 3771 C C   . MET B 2 85  ? 19.466 -43.469 1.873  1.00 72.70  ? 83  MET B C   1 
ATOM 3772 O O   . MET B 2 85  ? 20.354 -44.319 1.998  1.00 87.46  ? 83  MET B O   1 
ATOM 3773 C CB  . MET B 2 85  ? 20.575 -41.508 2.996  1.00 60.68  ? 83  MET B CB  1 
ATOM 3774 C CG  . MET B 2 85  ? 20.552 -40.528 4.158  1.00 61.38  ? 83  MET B CG  1 
ATOM 3775 S SD  . MET B 2 85  ? 22.172 -39.977 4.727  1.00 55.49  ? 83  MET B SD  1 
ATOM 3776 C CE  . MET B 2 85  ? 23.111 -40.010 3.206  1.00 59.77  ? 83  MET B CE  1 
ATOM 3777 N N   . ASN B 2 86  ? 18.604 -43.458 0.855  1.00 74.26  ? 84  ASN B N   1 
ATOM 3778 C CA  . ASN B 2 86  ? 18.530 -44.578 -0.076 1.00 78.31  ? 84  ASN B CA  1 
ATOM 3779 C C   . ASN B 2 86  ? 19.335 -44.329 -1.346 1.00 85.40  ? 84  ASN B C   1 
ATOM 3780 O O   . ASN B 2 86  ? 20.462 -44.816 -1.473 1.00 91.08  ? 84  ASN B O   1 
ATOM 3781 C CB  . ASN B 2 86  ? 17.074 -44.882 -0.428 1.00 80.04  ? 84  ASN B CB  1 
ATOM 3782 C CG  . ASN B 2 86  ? 16.434 -45.861 0.538  1.00 79.76  ? 84  ASN B CG  1 
ATOM 3783 O OD1 . ASN B 2 86  ? 15.209 -45.960 0.614  1.00 82.34  ? 84  ASN B OD1 1 
ATOM 3784 N ND2 . ASN B 2 86  ? 17.260 -46.586 1.284  1.00 81.13  ? 84  ASN B ND2 1 
ATOM 3785 N N   . SER B 2 87  ? 18.763 -43.604 -2.304 1.00 79.78  ? 85  SER B N   1 
ATOM 3786 C CA  . SER B 2 87  ? 19.488 -43.263 -3.521 1.00 77.18  ? 85  SER B CA  1 
ATOM 3787 C C   . SER B 2 87  ? 20.367 -42.049 -3.255 1.00 70.67  ? 85  SER B C   1 
ATOM 3788 O O   . SER B 2 87  ? 19.878 -41.006 -2.811 1.00 78.74  ? 85  SER B O   1 
ATOM 3789 C CB  . SER B 2 87  ? 18.520 -42.991 -4.671 1.00 71.49  ? 85  SER B CB  1 
ATOM 3790 O OG  . SER B 2 87  ? 17.609 -44.063 -4.831 1.00 73.34  ? 85  SER B OG  1 
ATOM 3791 N N   . LEU B 2 88  ? 21.665 -42.188 -3.514 1.00 67.02  ? 86  LEU B N   1 
ATOM 3792 C CA  . LEU B 2 88  ? 22.655 -41.198 -3.099 1.00 65.49  ? 86  LEU B CA  1 
ATOM 3793 C C   . LEU B 2 88  ? 23.422 -40.699 -4.314 1.00 71.42  ? 86  LEU B C   1 
ATOM 3794 O O   . LEU B 2 88  ? 24.217 -41.442 -4.901 1.00 69.59  ? 86  LEU B O   1 
ATOM 3795 C CB  . LEU B 2 88  ? 23.608 -41.789 -2.062 1.00 65.29  ? 86  LEU B CB  1 
ATOM 3796 C CG  . LEU B 2 88  ? 23.355 -41.376 -0.615 1.00 65.82  ? 86  LEU B CG  1 
ATOM 3797 C CD1 . LEU B 2 88  ? 21.947 -41.761 -0.218 1.00 72.24  ? 86  LEU B CD1 1 
ATOM 3798 C CD2 . LEU B 2 88  ? 24.367 -42.034 0.301  1.00 67.47  ? 86  LEU B CD2 1 
ATOM 3799 N N   . ASN B 2 89  ? 23.190 -39.441 -4.684 1.00 78.96  ? 87  ASN B N   1 
ATOM 3800 C CA  . ASN B 2 89  ? 24.001 -38.776 -5.689 1.00 71.03  ? 87  ASN B CA  1 
ATOM 3801 C C   . ASN B 2 89  ? 25.213 -38.129 -5.031 1.00 69.63  ? 87  ASN B C   1 
ATOM 3802 O O   . ASN B 2 89  ? 25.214 -37.877 -3.822 1.00 67.50  ? 87  ASN B O   1 
ATOM 3803 C CB  . ASN B 2 89  ? 23.168 -37.729 -6.431 1.00 72.91  ? 87  ASN B CB  1 
ATOM 3804 C CG  . ASN B 2 89  ? 22.477 -36.755 -5.496 1.00 70.37  ? 87  ASN B CG  1 
ATOM 3805 O OD1 . ASN B 2 89  ? 23.109 -35.862 -4.929 1.00 69.54  ? 87  ASN B OD1 1 
ATOM 3806 N ND2 . ASN B 2 89  ? 21.168 -36.914 -5.341 1.00 69.97  ? 87  ASN B ND2 1 
ATOM 3807 N N   . PRO B 2 90  ? 26.278 -37.867 -5.795 1.00 72.01  ? 88  PRO B N   1 
ATOM 3808 C CA  . PRO B 2 90  ? 27.473 -37.249 -5.193 1.00 76.17  ? 88  PRO B CA  1 
ATOM 3809 C C   . PRO B 2 90  ? 27.222 -35.877 -4.587 1.00 69.86  ? 88  PRO B C   1 
ATOM 3810 O O   . PRO B 2 90  ? 28.010 -35.439 -3.739 1.00 68.48  ? 88  PRO B O   1 
ATOM 3811 C CB  . PRO B 2 90  ? 28.457 -37.170 -6.370 1.00 74.94  ? 88  PRO B CB  1 
ATOM 3812 C CG  . PRO B 2 90  ? 28.005 -38.236 -7.309 1.00 76.93  ? 88  PRO B CG  1 
ATOM 3813 C CD  . PRO B 2 90  ? 26.510 -38.261 -7.195 1.00 75.84  ? 88  PRO B CD  1 
ATOM 3814 N N   . GLY B 2 91  ? 26.155 -35.186 -4.988 1.00 70.46  ? 89  GLY B N   1 
ATOM 3815 C CA  . GLY B 2 91  ? 25.836 -33.896 -4.402 1.00 69.24  ? 89  GLY B CA  1 
ATOM 3816 C C   . GLY B 2 91  ? 25.371 -33.959 -2.963 1.00 66.44  ? 89  GLY B C   1 
ATOM 3817 O O   . GLY B 2 91  ? 25.220 -32.907 -2.333 1.00 77.55  ? 89  GLY B O   1 
ATOM 3818 N N   . ASP B 2 92  ? 25.142 -35.159 -2.434 1.00 66.97  ? 90  ASP B N   1 
ATOM 3819 C CA  . ASP B 2 92  ? 24.727 -35.331 -1.049 1.00 64.92  ? 90  ASP B CA  1 
ATOM 3820 C C   . ASP B 2 92  ? 25.900 -35.358 -0.079 1.00 62.38  ? 90  ASP B C   1 
ATOM 3821 O O   . ASP B 2 92  ? 25.678 -35.495 1.130  1.00 59.04  ? 90  ASP B O   1 
ATOM 3822 C CB  . ASP B 2 92  ? 23.907 -36.615 -0.908 1.00 60.00  ? 90  ASP B CB  1 
ATOM 3823 C CG  . ASP B 2 92  ? 22.615 -36.570 -1.701 1.00 63.18  ? 90  ASP B CG  1 
ATOM 3824 O OD1 . ASP B 2 92  ? 22.000 -35.485 -1.777 1.00 68.21  ? 90  ASP B OD1 1 
ATOM 3825 O OD2 . ASP B 2 92  ? 22.219 -37.618 -2.255 1.00 62.62  ? 90  ASP B OD2 1 
ATOM 3826 N N   . THR B 2 93  ? 27.133 -35.231 -0.571 1.00 61.04  ? 91  THR B N   1 
ATOM 3827 C CA  . THR B 2 93  ? 28.304 -35.195 0.296  1.00 60.35  ? 91  THR B CA  1 
ATOM 3828 C C   . THR B 2 93  ? 28.279 -33.956 1.182  1.00 67.39  ? 91  THR B C   1 
ATOM 3829 O O   . THR B 2 93  ? 28.406 -32.830 0.689  1.00 60.43  ? 91  THR B O   1 
ATOM 3830 C CB  . THR B 2 93  ? 29.592 -35.225 -0.530 1.00 63.06  ? 91  THR B CB  1 
ATOM 3831 O OG1 . THR B 2 93  ? 29.676 -36.464 -1.242 1.00 66.73  ? 91  THR B OG1 1 
ATOM 3832 C CG2 . THR B 2 93  ? 30.806 -35.085 0.376  1.00 62.75  ? 91  THR B CG2 1 
ATOM 3833 N N   . ALA B 2 94  ? 28.117 -34.155 2.487  1.00 57.65  ? 92  ALA B N   1 
ATOM 3834 C CA  . ALA B 2 94  ? 28.040 -33.056 3.441  1.00 55.53  ? 92  ALA B CA  1 
ATOM 3835 C C   . ALA B 2 94  ? 28.188 -33.626 4.845  1.00 57.00  ? 92  ALA B C   1 
ATOM 3836 O O   . ALA B 2 94  ? 28.167 -34.843 5.049  1.00 63.63  ? 92  ALA B O   1 
ATOM 3837 C CB  . ALA B 2 94  ? 26.725 -32.284 3.308  1.00 56.77  ? 92  ALA B CB  1 
ATOM 3838 N N   . VAL B 2 95  ? 28.340 -32.726 5.811  1.00 61.08  ? 93  VAL B N   1 
ATOM 3839 C CA  . VAL B 2 95  ? 28.341 -33.093 7.222  1.00 52.98  ? 93  VAL B CA  1 
ATOM 3840 C C   . VAL B 2 95  ? 26.909 -32.980 7.726  1.00 53.05  ? 93  VAL B C   1 
ATOM 3841 O O   . VAL B 2 95  ? 26.332 -31.887 7.746  1.00 49.79  ? 93  VAL B O   1 
ATOM 3842 C CB  . VAL B 2 95  ? 29.292 -32.200 8.033  1.00 52.05  ? 93  VAL B CB  1 
ATOM 3843 C CG1 . VAL B 2 95  ? 28.928 -32.234 9.511  1.00 59.00  ? 93  VAL B CG1 1 
ATOM 3844 C CG2 . VAL B 2 95  ? 30.733 -32.634 7.824  1.00 53.95  ? 93  VAL B CG2 1 
ATOM 3845 N N   . TYR B 2 96  ? 26.331 -34.111 8.118  1.00 55.77  ? 94  TYR B N   1 
ATOM 3846 C CA  . TYR B 2 96  ? 24.930 -34.184 8.505  1.00 53.33  ? 94  TYR B CA  1 
ATOM 3847 C C   . TYR B 2 96  ? 24.812 -34.063 10.017 1.00 46.83  ? 94  TYR B C   1 
ATOM 3848 O O   . TYR B 2 96  ? 25.492 -34.781 10.758 1.00 51.54  ? 94  TYR B O   1 
ATOM 3849 C CB  . TYR B 2 96  ? 24.297 -35.492 8.023  1.00 58.80  ? 94  TYR B CB  1 
ATOM 3850 C CG  . TYR B 2 96  ? 24.066 -35.551 6.527  1.00 52.63  ? 94  TYR B CG  1 
ATOM 3851 C CD1 . TYR B 2 96  ? 25.129 -35.466 5.636  1.00 56.71  ? 94  TYR B CD1 1 
ATOM 3852 C CD2 . TYR B 2 96  ? 22.786 -35.688 6.005  1.00 54.57  ? 94  TYR B CD2 1 
ATOM 3853 C CE1 . TYR B 2 96  ? 24.926 -35.517 4.270  1.00 60.44  ? 94  TYR B CE1 1 
ATOM 3854 C CE2 . TYR B 2 96  ? 22.572 -35.741 4.638  1.00 56.45  ? 94  TYR B CE2 1 
ATOM 3855 C CZ  . TYR B 2 96  ? 23.647 -35.654 3.776  1.00 61.31  ? 94  TYR B CZ  1 
ATOM 3856 O OH  . TYR B 2 96  ? 23.447 -35.704 2.415  1.00 61.30  ? 94  TYR B OH  1 
ATOM 3857 N N   . SER B 2 97  ? 23.951 -33.156 10.469 1.00 50.65  ? 95  SER B N   1 
ATOM 3858 C CA  . SER B 2 97  ? 23.758 -32.896 11.887 1.00 45.22  ? 95  SER B CA  1 
ATOM 3859 C C   . SER B 2 97  ? 22.280 -32.991 12.226 1.00 47.49  ? 95  SER B C   1 
ATOM 3860 O O   . SER B 2 97  ? 21.427 -32.517 11.469 1.00 44.13  ? 95  SER B O   1 
ATOM 3861 C CB  . SER B 2 97  ? 24.289 -31.512 12.280 1.00 50.63  ? 95  SER B CB  1 
ATOM 3862 O OG  . SER B 2 97  ? 25.679 -31.404 12.033 1.00 53.51  ? 95  SER B OG  1 
ATOM 3863 N N   . CYS B 2 98  ? 21.983 -33.606 13.364 1.00 60.36  ? 96  CYS B N   1 
ATOM 3864 C CA  . CYS B 2 98  ? 20.625 -33.675 13.879 1.00 59.79  ? 96  CYS B CA  1 
ATOM 3865 C C   . CYS B 2 98  ? 20.442 -32.594 14.937 1.00 59.54  ? 96  CYS B C   1 
ATOM 3866 O O   . CYS B 2 98  ? 21.356 -32.315 15.717 1.00 58.52  ? 96  CYS B O   1 
ATOM 3867 C CB  . CYS B 2 98  ? 20.327 -35.063 14.457 1.00 61.00  ? 96  CYS B CB  1 
ATOM 3868 S SG  . CYS B 2 98  ? 19.996 -35.114 16.234 1.00 89.01  ? 96  CYS B SG  1 
ATOM 3869 N N   . ALA B 2 99  ? 19.267 -31.969 14.940 1.00 45.62  ? 97  ALA B N   1 
ATOM 3870 C CA  . ALA B 2 99  ? 18.985 -30.854 15.830 1.00 52.53  ? 97  ALA B CA  1 
ATOM 3871 C C   . ALA B 2 99  ? 17.652 -31.068 16.533 1.00 56.10  ? 97  ALA B C   1 
ATOM 3872 O O   . ALA B 2 99  ? 16.783 -31.804 16.059 1.00 55.44  ? 97  ALA B O   1 
ATOM 3873 C CB  . ALA B 2 99  ? 18.965 -29.520 15.073 1.00 49.39  ? 97  ALA B CB  1 
ATOM 3874 N N   . ALA B 2 100 ? 17.502 -30.404 17.676 1.00 48.00  ? 98  ALA B N   1 
ATOM 3875 C CA  . ALA B 2 100 ? 16.293 -30.488 18.478 1.00 49.42  ? 98  ALA B CA  1 
ATOM 3876 C C   . ALA B 2 100 ? 15.769 -29.089 18.760 1.00 47.93  ? 98  ALA B C   1 
ATOM 3877 O O   . ALA B 2 100 ? 16.540 -28.137 18.908 1.00 45.18  ? 98  ALA B O   1 
ATOM 3878 C CB  . ALA B 2 100 ? 16.543 -31.227 19.800 1.00 47.02  ? 98  ALA B CB  1 
ATOM 3879 N N   . THR B 2 101 ? 14.445 -28.976 18.836 1.00 42.54  ? 99  THR B N   1 
ATOM 3880 C CA  . THR B 2 101 ? 13.806 -27.707 19.148 1.00 42.05  ? 99  THR B CA  1 
ATOM 3881 C C   . THR B 2 101 ? 12.374 -27.972 19.585 1.00 45.01  ? 99  THR B C   1 
ATOM 3882 O O   . THR B 2 101 ? 11.787 -29.009 19.263 1.00 51.08  ? 99  THR B O   1 
ATOM 3883 C CB  . THR B 2 101 ? 13.835 -26.748 17.953 1.00 50.31  ? 99  THR B CB  1 
ATOM 3884 O OG1 . THR B 2 101 ? 13.763 -25.397 18.424 1.00 40.71  ? 99  THR B OG1 1 
ATOM 3885 C CG2 . THR B 2 101 ? 12.667 -27.017 17.016 1.00 50.70  ? 99  THR B CG2 1 
ATOM 3886 N N   . LEU B 2 102 ? 11.825 -27.023 20.333 1.00 48.21  ? 100 LEU B N   1 
ATOM 3887 C CA  . LEU B 2 102 ? 10.440 -27.103 20.761 1.00 48.11  ? 100 LEU B CA  1 
ATOM 3888 C C   . LEU B 2 102 ? 9.523  -26.593 19.651 1.00 51.85  ? 100 LEU B C   1 
ATOM 3889 O O   . LEU B 2 102 ? 9.947  -25.814 18.794 1.00 44.08  ? 100 LEU B O   1 
ATOM 3890 C CB  . LEU B 2 102 ? 10.241 -26.296 22.042 1.00 61.43  ? 100 LEU B CB  1 
ATOM 3891 C CG  . LEU B 2 102 ? 10.483 -27.015 23.377 1.00 57.64  ? 100 LEU B CG  1 
ATOM 3892 C CD1 . LEU B 2 102 ? 9.742  -28.345 23.439 1.00 50.84  ? 100 LEU B CD1 1 
ATOM 3893 C CD2 . LEU B 2 102 ? 11.971 -27.218 23.634 1.00 60.08  ? 100 LEU B CD2 1 
ATOM 3894 N N   . PRO B 2 103 ? 8.260  -27.033 19.635 1.00 51.19  ? 101 PRO B N   1 
ATOM 3895 C CA  . PRO B 2 103 ? 7.364  -26.627 18.536 1.00 46.38  ? 101 PRO B CA  1 
ATOM 3896 C C   . PRO B 2 103 ? 7.166  -25.127 18.430 1.00 50.50  ? 101 PRO B C   1 
ATOM 3897 O O   . PRO B 2 103 ? 6.917  -24.624 17.327 1.00 52.45  ? 101 PRO B O   1 
ATOM 3898 C CB  . PRO B 2 103 ? 6.048  -27.344 18.870 1.00 50.12  ? 101 PRO B CB  1 
ATOM 3899 C CG  . PRO B 2 103 ? 6.432  -28.459 19.776 1.00 52.21  ? 101 PRO B CG  1 
ATOM 3900 C CD  . PRO B 2 103 ? 7.610  -27.979 20.557 1.00 55.04  ? 101 PRO B CD  1 
ATOM 3901 N N   . ALA B 2 104 ? 7.266  -24.393 19.541 1.00 58.11  ? 102 ALA B N   1 
ATOM 3902 C CA  . ALA B 2 104 ? 7.104  -22.945 19.489 1.00 50.40  ? 102 ALA B CA  1 
ATOM 3903 C C   . ALA B 2 104 ? 8.225  -22.264 18.717 1.00 49.61  ? 102 ALA B C   1 
ATOM 3904 O O   . ALA B 2 104 ? 8.024  -21.159 18.200 1.00 53.70  ? 102 ALA B O   1 
ATOM 3905 C CB  . ALA B 2 104 ? 7.021  -22.372 20.903 1.00 57.96  ? 102 ALA B CB  1 
ATOM 3906 N N   . TRP B 2 105 ? 9.397  -22.893 18.625 1.00 50.21  ? 103 TRP B N   1 
ATOM 3907 C CA  . TRP B 2 105 ? 10.489 -22.319 17.850 1.00 46.64  ? 103 TRP B CA  1 
ATOM 3908 C C   . TRP B 2 105 ? 10.263 -22.464 16.350 1.00 48.89  ? 103 TRP B C   1 
ATOM 3909 O O   . TRP B 2 105 ? 10.802 -21.673 15.568 1.00 49.83  ? 103 TRP B O   1 
ATOM 3910 C CB  . TRP B 2 105 ? 11.814 -22.977 18.233 1.00 45.86  ? 103 TRP B CB  1 
ATOM 3911 C CG  . TRP B 2 105 ? 12.260 -22.712 19.634 1.00 40.80  ? 103 TRP B CG  1 
ATOM 3912 C CD1 . TRP B 2 105 ? 11.557 -22.947 20.780 1.00 42.93  ? 103 TRP B CD1 1 
ATOM 3913 C CD2 . TRP B 2 105 ? 13.525 -22.177 20.041 1.00 42.29  ? 103 TRP B CD2 1 
ATOM 3914 N NE1 . TRP B 2 105 ? 12.303 -22.582 21.876 1.00 48.90  ? 103 TRP B NE1 1 
ATOM 3915 C CE2 . TRP B 2 105 ? 13.515 -22.107 21.449 1.00 46.08  ? 103 TRP B CE2 1 
ATOM 3916 C CE3 . TRP B 2 105 ? 14.663 -21.747 19.352 1.00 40.35  ? 103 TRP B CE3 1 
ATOM 3917 C CZ2 . TRP B 2 105 ? 14.599 -21.623 22.180 1.00 44.17  ? 103 TRP B CZ2 1 
ATOM 3918 C CZ3 . TRP B 2 105 ? 15.737 -21.267 20.079 1.00 40.85  ? 103 TRP B CZ3 1 
ATOM 3919 C CH2 . TRP B 2 105 ? 15.698 -21.210 21.478 1.00 41.53  ? 103 TRP B CH2 1 
ATOM 3920 N N   . THR B 2 106 ? 9.483  -23.463 15.930 1.00 49.00  ? 104 THR B N   1 
ATOM 3921 C CA  . THR B 2 106 ? 9.257  -23.677 14.505 1.00 52.47  ? 104 THR B CA  1 
ATOM 3922 C C   . THR B 2 106 ? 8.251  -22.691 13.929 1.00 48.41  ? 104 THR B C   1 
ATOM 3923 O O   . THR B 2 106 ? 8.376  -22.297 12.764 1.00 51.90  ? 104 THR B O   1 
ATOM 3924 C CB  . THR B 2 106 ? 8.778  -25.108 14.249 1.00 47.37  ? 104 THR B CB  1 
ATOM 3925 O OG1 . THR B 2 106 ? 7.508  -25.311 14.881 1.00 45.29  ? 104 THR B OG1 1 
ATOM 3926 C CG2 . THR B 2 106 ? 9.780  -26.112 14.795 1.00 48.48  ? 104 THR B CG2 1 
ATOM 3927 N N   . GLY B 2 107 ? 7.259  -22.285 14.712 1.00 47.49  ? 105 GLY B N   1 
ATOM 3928 C CA  . GLY B 2 107 ? 6.259  -21.365 14.194 1.00 50.35  ? 105 GLY B CA  1 
ATOM 3929 C C   . GLY B 2 107 ? 5.346  -22.074 13.216 1.00 55.20  ? 105 GLY B C   1 
ATOM 3930 O O   . GLY B 2 107 ? 4.841  -23.170 13.486 1.00 55.94  ? 105 GLY B O   1 
ATOM 3931 N N   . ILE B 2 108 ? 5.128  -21.450 12.058 1.00 52.71  ? 106 ILE B N   1 
ATOM 3932 C CA  . ILE B 2 108 ? 4.274  -21.995 11.010 1.00 53.36  ? 106 ILE B CA  1 
ATOM 3933 C C   . ILE B 2 108 ? 5.070  -22.304 9.747  1.00 54.53  ? 106 ILE B C   1 
ATOM 3934 O O   . ILE B 2 108 ? 4.948  -23.391 9.173  1.00 63.21  ? 106 ILE B O   1 
ATOM 3935 C CB  . ILE B 2 108 ? 3.093  -21.046 10.697 1.00 53.66  ? 106 ILE B CB  1 
ATOM 3936 C CG1 . ILE B 2 108 ? 1.937  -21.304 11.665 1.00 54.69  ? 106 ILE B CG1 1 
ATOM 3937 C CG2 . ILE B 2 108 ? 2.617  -21.224 9.261  1.00 52.75  ? 106 ILE B CG2 1 
ATOM 3938 C CD1 . ILE B 2 108 ? 0.656  -20.585 11.295 1.00 62.53  ? 106 ILE B CD1 1 
ATOM 3939 N N   . ILE B 2 109 ? 5.903  -21.362 9.305  1.00 53.17  ? 107 ILE B N   1 
ATOM 3940 C CA  . ILE B 2 109 ? 6.712  -21.543 8.103  1.00 49.94  ? 107 ILE B CA  1 
ATOM 3941 C C   . ILE B 2 109 ? 8.182  -21.770 8.408  1.00 48.30  ? 107 ILE B C   1 
ATOM 3942 O O   . ILE B 2 109 ? 8.950  -22.068 7.477  1.00 49.09  ? 107 ILE B O   1 
ATOM 3943 C CB  . ILE B 2 109 ? 6.560  -20.352 7.131  1.00 51.85  ? 107 ILE B CB  1 
ATOM 3944 C CG1 . ILE B 2 109 ? 7.322  -19.122 7.641  1.00 50.81  ? 107 ILE B CG1 1 
ATOM 3945 C CG2 . ILE B 2 109 ? 5.092  -20.028 6.908  1.00 53.68  ? 107 ILE B CG2 1 
ATOM 3946 C CD1 . ILE B 2 109 ? 8.567  -18.773 6.838  1.00 51.56  ? 107 ILE B CD1 1 
ATOM 3947 N N   . GLY B 2 110 ? 8.603  -21.647 9.663  1.00 52.09  ? 108 GLY B N   1 
ATOM 3948 C CA  . GLY B 2 110 ? 10.011 -21.730 9.994  1.00 46.60  ? 108 GLY B CA  1 
ATOM 3949 C C   . GLY B 2 110 ? 10.473 -23.094 10.462 1.00 44.27  ? 108 GLY B C   1 
ATOM 3950 O O   . GLY B 2 110 ? 11.380 -23.192 11.292 1.00 50.04  ? 108 GLY B O   1 
ATOM 3951 N N   . GLY B 2 111 ? 9.861  -24.157 9.934  1.00 45.15  ? 109 GLY B N   1 
ATOM 3952 C CA  . GLY B 2 111 ? 10.271 -25.501 10.298 1.00 44.67  ? 109 GLY B CA  1 
ATOM 3953 C C   . GLY B 2 111 ? 11.568 -25.959 9.665  1.00 48.42  ? 109 GLY B C   1 
ATOM 3954 O O   . GLY B 2 111 ? 12.202 -26.883 10.185 1.00 52.69  ? 109 GLY B O   1 
ATOM 3955 N N   . ARG B 2 112 ? 11.981 -25.335 8.563  1.00 53.05  ? 110 ARG B N   1 
ATOM 3956 C CA  . ARG B 2 112 ? 13.173 -25.738 7.829  1.00 52.36  ? 110 ARG B CA  1 
ATOM 3957 C C   . ARG B 2 112 ? 14.377 -24.847 8.104  1.00 51.47  ? 110 ARG B C   1 
ATOM 3958 O O   . ARG B 2 112 ? 15.429 -25.047 7.488  1.00 47.47  ? 110 ARG B O   1 
ATOM 3959 C CB  . ARG B 2 112 ? 12.886 -25.748 6.324  1.00 48.21  ? 110 ARG B CB  1 
ATOM 3960 C CG  . ARG B 2 112 ? 11.724 -26.637 5.910  1.00 49.34  ? 110 ARG B CG  1 
ATOM 3961 C CD  . ARG B 2 112 ? 11.465 -26.530 4.416  1.00 55.64  ? 110 ARG B CD  1 
ATOM 3962 N NE  . ARG B 2 112 ? 10.415 -27.436 3.970  1.00 61.32  ? 110 ARG B NE  1 
ATOM 3963 C CZ  . ARG B 2 112 ? 10.303 -27.898 2.732  1.00 62.27  ? 110 ARG B CZ  1 
ATOM 3964 N NH1 . ARG B 2 112 ? 11.164 -27.555 1.787  1.00 68.41  ? 110 ARG B NH1 1 
ATOM 3965 N NH2 . ARG B 2 112 ? 9.306  -28.726 2.435  1.00 57.48  ? 110 ARG B NH2 1 
ATOM 3966 N N   . ARG B 2 113 ? 14.255 -23.871 9.009  1.00 48.94  ? 111 ARG B N   1 
ATOM 3967 C CA  . ARG B 2 113 ? 15.342 -22.926 9.249  1.00 44.56  ? 111 ARG B CA  1 
ATOM 3968 C C   . ARG B 2 113 ? 16.251 -23.443 10.357 1.00 43.32  ? 111 ARG B C   1 
ATOM 3969 O O   . ARG B 2 113 ? 15.762 -23.778 11.443 1.00 42.24  ? 111 ARG B O   1 
ATOM 3970 C CB  . ARG B 2 113 ? 14.796 -21.556 9.627  1.00 51.09  ? 111 ARG B CB  1 
ATOM 3971 C CG  . ARG B 2 113 ? 15.828 -20.437 9.586  1.00 53.11  ? 111 ARG B CG  1 
ATOM 3972 C CD  . ARG B 2 113 ? 16.044 -19.938 8.164  1.00 68.92  ? 111 ARG B CD  1 
ATOM 3973 N NE  . ARG B 2 113 ? 17.387 -19.404 7.967  1.00 78.09  ? 111 ARG B NE  1 
ATOM 3974 C CZ  . ARG B 2 113 ? 18.191 -19.741 6.967  1.00 79.13  ? 111 ARG B CZ  1 
ATOM 3975 N NH1 . ARG B 2 113 ? 17.825 -20.628 6.056  1.00 56.77  ? 111 ARG B NH1 1 
ATOM 3976 N NH2 . ARG B 2 113 ? 19.392 -19.176 6.881  1.00 83.14  ? 111 ARG B NH2 1 
ATOM 3977 N N   . PRO B 2 114 ? 17.565 -23.515 10.126 1.00 43.80  ? 112 PRO B N   1 
ATOM 3978 C CA  . PRO B 2 114 ? 18.456 -24.052 11.166 1.00 49.43  ? 112 PRO B CA  1 
ATOM 3979 C C   . PRO B 2 114 ? 18.526 -23.181 12.406 1.00 49.66  ? 112 PRO B C   1 
ATOM 3980 O O   . PRO B 2 114 ? 18.689 -23.712 13.511 1.00 53.00  ? 112 PRO B O   1 
ATOM 3981 C CB  . PRO B 2 114 ? 19.814 -24.135 10.456 1.00 46.66  ? 112 PRO B CB  1 
ATOM 3982 C CG  . PRO B 2 114 ? 19.736 -23.119 9.371  1.00 45.63  ? 112 PRO B CG  1 
ATOM 3983 C CD  . PRO B 2 114 ? 18.301 -23.095 8.921  1.00 45.49  ? 112 PRO B CD  1 
ATOM 3984 N N   . GLY B 2 115 ? 18.404 -21.861 12.261 1.00 48.84  ? 113 GLY B N   1 
ATOM 3985 C CA  . GLY B 2 115 ? 18.435 -20.975 13.411 1.00 46.30  ? 113 GLY B CA  1 
ATOM 3986 C C   . GLY B 2 115 ? 17.281 -21.162 14.372 1.00 46.85  ? 113 GLY B C   1 
ATOM 3987 O O   . GLY B 2 115 ? 17.312 -20.593 15.470 1.00 41.91  ? 113 GLY B O   1 
ATOM 3988 N N   . ASN B 2 116 ? 16.266 -21.932 13.987 1.00 42.62  ? 114 ASN B N   1 
ATOM 3989 C CA  . ASN B 2 116 ? 15.151 -22.255 14.864 1.00 50.91  ? 114 ASN B CA  1 
ATOM 3990 C C   . ASN B 2 116 ? 15.429 -23.464 15.747 1.00 41.64  ? 114 ASN B C   1 
ATOM 3991 O O   . ASN B 2 116 ? 14.543 -23.879 16.501 1.00 46.84  ? 114 ASN B O   1 
ATOM 3992 C CB  . ASN B 2 116 ? 13.886 -22.503 14.036 1.00 51.18  ? 114 ASN B CB  1 
ATOM 3993 C CG  . ASN B 2 116 ? 13.163 -21.220 13.677 1.00 44.18  ? 114 ASN B CG  1 
ATOM 3994 O OD1 . ASN B 2 116 ? 13.642 -20.122 13.967 1.00 52.02  ? 114 ASN B OD1 1 
ATOM 3995 N ND2 . ASN B 2 116 ? 12.003 -21.351 13.045 1.00 42.10  ? 114 ASN B ND2 1 
ATOM 3996 N N   . TYR B 2 117 ? 16.629 -24.033 15.675 1.00 44.20  ? 115 TYR B N   1 
ATOM 3997 C CA  . TYR B 2 117 ? 16.992 -25.219 16.452 1.00 56.26  ? 115 TYR B CA  1 
ATOM 3998 C C   . TYR B 2 117 ? 18.176 -24.889 17.349 1.00 55.12  ? 115 TYR B C   1 
ATOM 3999 O O   . TYR B 2 117 ? 19.320 -24.806 16.868 1.00 58.24  ? 115 TYR B O   1 
ATOM 4000 C CB  . TYR B 2 117 ? 17.325 -26.392 15.529 1.00 53.48  ? 115 TYR B CB  1 
ATOM 4001 C CG  . TYR B 2 117 ? 16.152 -26.898 14.715 1.00 52.81  ? 115 TYR B CG  1 
ATOM 4002 C CD1 . TYR B 2 117 ? 15.693 -26.193 13.606 1.00 47.64  ? 115 TYR B CD1 1 
ATOM 4003 C CD2 . TYR B 2 117 ? 15.506 -28.082 15.050 1.00 46.45  ? 115 TYR B CD2 1 
ATOM 4004 C CE1 . TYR B 2 117 ? 14.622 -26.649 12.859 1.00 44.14  ? 115 TYR B CE1 1 
ATOM 4005 C CE2 . TYR B 2 117 ? 14.434 -28.546 14.307 1.00 51.93  ? 115 TYR B CE2 1 
ATOM 4006 C CZ  . TYR B 2 117 ? 13.997 -27.826 13.213 1.00 52.03  ? 115 TYR B CZ  1 
ATOM 4007 O OH  . TYR B 2 117 ? 12.932 -28.280 12.470 1.00 45.81  ? 115 TYR B OH  1 
ATOM 4008 N N   . PRO B 2 118 ? 17.961 -24.694 18.654 1.00 43.80  ? 116 PRO B N   1 
ATOM 4009 C CA  . PRO B 2 118 ? 19.086 -24.289 19.513 1.00 49.83  ? 116 PRO B CA  1 
ATOM 4010 C C   . PRO B 2 118 ? 20.061 -25.414 19.808 1.00 59.10  ? 116 PRO B C   1 
ATOM 4011 O O   . PRO B 2 118 ? 21.276 -25.179 19.838 1.00 64.92  ? 116 PRO B O   1 
ATOM 4012 C CB  . PRO B 2 118 ? 18.387 -23.790 20.784 1.00 54.63  ? 116 PRO B CB  1 
ATOM 4013 C CG  . PRO B 2 118 ? 17.103 -24.551 20.826 1.00 52.73  ? 116 PRO B CG  1 
ATOM 4014 C CD  . PRO B 2 118 ? 16.689 -24.768 19.393 1.00 47.79  ? 116 PRO B CD  1 
ATOM 4015 N N   . TYR B 2 119 ? 19.568 -26.631 20.028 1.00 62.86  ? 117 TYR B N   1 
ATOM 4016 C CA  . TYR B 2 119 ? 20.412 -27.753 20.419 1.00 60.55  ? 117 TYR B CA  1 
ATOM 4017 C C   . TYR B 2 119 ? 20.837 -28.544 19.188 1.00 54.09  ? 117 TYR B C   1 
ATOM 4018 O O   . TYR B 2 119 ? 20.002 -28.899 18.350 1.00 44.99  ? 117 TYR B O   1 
ATOM 4019 C CB  . TYR B 2 119 ? 19.674 -28.652 21.412 1.00 62.45  ? 117 TYR B CB  1 
ATOM 4020 C CG  . TYR B 2 119 ? 19.047 -27.881 22.553 1.00 57.01  ? 117 TYR B CG  1 
ATOM 4021 C CD1 . TYR B 2 119 ? 19.822 -27.405 23.603 1.00 58.24  ? 117 TYR B CD1 1 
ATOM 4022 C CD2 . TYR B 2 119 ? 17.682 -27.619 22.574 1.00 45.39  ? 117 TYR B CD2 1 
ATOM 4023 C CE1 . TYR B 2 119 ? 19.255 -26.694 24.645 1.00 67.84  ? 117 TYR B CE1 1 
ATOM 4024 C CE2 . TYR B 2 119 ? 17.107 -26.910 23.611 1.00 51.68  ? 117 TYR B CE2 1 
ATOM 4025 C CZ  . TYR B 2 119 ? 17.898 -26.449 24.644 1.00 68.22  ? 117 TYR B CZ  1 
ATOM 4026 O OH  . TYR B 2 119 ? 17.330 -25.742 25.680 1.00 52.93  ? 117 TYR B OH  1 
ATOM 4027 N N   . TRP B 2 120 ? 22.135 -28.822 19.089 1.00 55.01  ? 118 TRP B N   1 
ATOM 4028 C CA  . TRP B 2 120 ? 22.724 -29.436 17.910 1.00 53.84  ? 118 TRP B CA  1 
ATOM 4029 C C   . TRP B 2 120 ? 23.574 -30.634 18.309 1.00 57.05  ? 118 TRP B C   1 
ATOM 4030 O O   . TRP B 2 120 ? 23.792 -30.911 19.492 1.00 63.44  ? 118 TRP B O   1 
ATOM 4031 C CB  . TRP B 2 120 ? 23.585 -28.431 17.134 1.00 55.93  ? 118 TRP B CB  1 
ATOM 4032 C CG  . TRP B 2 120 ? 22.796 -27.361 16.465 1.00 65.34  ? 118 TRP B CG  1 
ATOM 4033 C CD1 . TRP B 2 120 ? 22.467 -26.141 16.978 1.00 55.95  ? 118 TRP B CD1 1 
ATOM 4034 C CD2 . TRP B 2 120 ? 22.231 -27.412 15.151 1.00 62.29  ? 118 TRP B CD2 1 
ATOM 4035 N NE1 . TRP B 2 120 ? 21.730 -25.428 16.063 1.00 60.03  ? 118 TRP B NE1 1 
ATOM 4036 C CE2 . TRP B 2 120 ? 21.573 -26.186 14.933 1.00 64.58  ? 118 TRP B CE2 1 
ATOM 4037 C CE3 . TRP B 2 120 ? 22.219 -28.375 14.138 1.00 58.14  ? 118 TRP B CE3 1 
ATOM 4038 C CZ2 . TRP B 2 120 ? 20.908 -25.898 13.743 1.00 60.73  ? 118 TRP B CZ2 1 
ATOM 4039 C CZ3 . TRP B 2 120 ? 21.560 -28.088 12.958 1.00 62.52  ? 118 TRP B CZ3 1 
ATOM 4040 C CH2 . TRP B 2 120 ? 20.913 -26.859 12.770 1.00 62.60  ? 118 TRP B CH2 1 
ATOM 4041 N N   . GLY B 2 121 ? 24.057 -31.348 17.289 1.00 62.53  ? 119 GLY B N   1 
ATOM 4042 C CA  . GLY B 2 121 ? 25.018 -32.410 17.468 1.00 59.49  ? 119 GLY B CA  1 
ATOM 4043 C C   . GLY B 2 121 ? 26.312 -32.080 16.738 1.00 62.03  ? 119 GLY B C   1 
ATOM 4044 O O   . GLY B 2 121 ? 26.390 -31.125 15.956 1.00 65.98  ? 119 GLY B O   1 
ATOM 4045 N N   . GLN B 2 122 ? 27.336 -32.891 17.006 1.00 64.66  ? 120 GLN B N   1 
ATOM 4046 C CA  . GLN B 2 122 ? 28.651 -32.647 16.424 1.00 68.20  ? 120 GLN B CA  1 
ATOM 4047 C C   . GLN B 2 122 ? 28.715 -32.974 14.939 1.00 70.33  ? 120 GLN B C   1 
ATOM 4048 O O   . GLN B 2 122 ? 29.743 -32.702 14.307 1.00 65.45  ? 120 GLN B O   1 
ATOM 4049 C CB  . GLN B 2 122 ? 29.715 -33.447 17.181 1.00 67.99  ? 120 GLN B CB  1 
ATOM 4050 C CG  . GLN B 2 122 ? 29.860 -34.889 16.720 1.00 83.38  ? 120 GLN B CG  1 
ATOM 4051 C CD  . GLN B 2 122 ? 28.823 -35.809 17.337 1.00 81.24  ? 120 GLN B CD  1 
ATOM 4052 O OE1 . GLN B 2 122 ? 27.656 -35.803 16.943 1.00 77.34  ? 120 GLN B OE1 1 
ATOM 4053 N NE2 . GLN B 2 122 ? 29.243 -36.603 18.315 1.00 86.14  ? 120 GLN B NE2 1 
ATOM 4054 N N   . GLY B 2 123 ? 27.659 -33.542 14.373 1.00 67.08  ? 121 GLY B N   1 
ATOM 4055 C CA  . GLY B 2 123 ? 27.624 -33.846 12.960 1.00 64.62  ? 121 GLY B CA  1 
ATOM 4056 C C   . GLY B 2 123 ? 28.495 -35.039 12.600 1.00 73.03  ? 121 GLY B C   1 
ATOM 4057 O O   . GLY B 2 123 ? 29.445 -35.404 13.298 1.00 72.49  ? 121 GLY B O   1 
ATOM 4058 N N   . THR B 2 124 ? 28.150 -35.661 11.479 1.00 70.42  ? 122 THR B N   1 
ATOM 4059 C CA  . THR B 2 124 ? 28.887 -36.800 10.956 1.00 67.61  ? 122 THR B CA  1 
ATOM 4060 C C   . THR B 2 124 ? 29.124 -36.614 9.464  1.00 59.44  ? 122 THR B C   1 
ATOM 4061 O O   . THR B 2 124 ? 28.313 -36.011 8.755  1.00 60.66  ? 122 THR B O   1 
ATOM 4062 C CB  . THR B 2 124 ? 28.155 -38.123 11.231 1.00 64.62  ? 122 THR B CB  1 
ATOM 4063 O OG1 . THR B 2 124 ? 29.107 -39.194 11.275 1.00 73.22  ? 122 THR B OG1 1 
ATOM 4064 C CG2 . THR B 2 124 ? 27.115 -38.407 10.153 1.00 61.53  ? 122 THR B CG2 1 
ATOM 4065 N N   . GLN B 2 125 ? 30.258 -37.127 8.999  1.00 53.63  ? 123 GLN B N   1 
ATOM 4066 C CA  . GLN B 2 125 ? 30.698 -36.924 7.627  1.00 57.45  ? 123 GLN B CA  1 
ATOM 4067 C C   . GLN B 2 125 ? 30.147 -38.020 6.723  1.00 64.38  ? 123 GLN B C   1 
ATOM 4068 O O   . GLN B 2 125 ? 30.334 -39.210 6.994  1.00 62.24  ? 123 GLN B O   1 
ATOM 4069 C CB  . GLN B 2 125 ? 32.225 -36.898 7.553  1.00 55.86  ? 123 GLN B CB  1 
ATOM 4070 C CG  . GLN B 2 125 ? 32.779 -36.682 6.161  1.00 57.57  ? 123 GLN B CG  1 
ATOM 4071 C CD  . GLN B 2 125 ? 32.316 -35.374 5.547  1.00 70.30  ? 123 GLN B CD  1 
ATOM 4072 O OE1 . GLN B 2 125 ? 31.278 -35.317 4.885  1.00 71.07  ? 123 GLN B OE1 1 
ATOM 4073 N NE2 . GLN B 2 125 ? 33.087 -34.314 5.762  1.00 75.14  ? 123 GLN B NE2 1 
ATOM 4074 N N   . VAL B 2 126 ? 29.466 -37.613 5.655  1.00 64.26  ? 124 VAL B N   1 
ATOM 4075 C CA  . VAL B 2 126 ? 28.934 -38.523 4.647  1.00 61.84  ? 124 VAL B CA  1 
ATOM 4076 C C   . VAL B 2 126 ? 29.523 -38.114 3.304  1.00 63.34  ? 124 VAL B C   1 
ATOM 4077 O O   . VAL B 2 126 ? 29.337 -36.974 2.860  1.00 65.43  ? 124 VAL B O   1 
ATOM 4078 C CB  . VAL B 2 126 ? 27.398 -38.498 4.606  1.00 61.19  ? 124 VAL B CB  1 
ATOM 4079 C CG1 . VAL B 2 126 ? 26.880 -39.389 3.485  1.00 55.18  ? 124 VAL B CG1 1 
ATOM 4080 C CG2 . VAL B 2 126 ? 26.824 -38.927 5.949  1.00 52.34  ? 124 VAL B CG2 1 
ATOM 4081 N N   . THR B 2 127 ? 30.233 -39.038 2.662  1.00 60.35  ? 125 THR B N   1 
ATOM 4082 C CA  . THR B 2 127 ? 30.915 -38.779 1.399  1.00 68.42  ? 125 THR B CA  1 
ATOM 4083 C C   . THR B 2 127 ? 30.440 -39.787 0.363  1.00 69.38  ? 125 THR B C   1 
ATOM 4084 O O   . THR B 2 127 ? 30.565 -40.999 0.569  1.00 64.63  ? 125 THR B O   1 
ATOM 4085 C CB  . THR B 2 127 ? 32.434 -38.858 1.569  1.00 70.83  ? 125 THR B CB  1 
ATOM 4086 O OG1 . THR B 2 127 ? 32.819 -38.159 2.760  1.00 67.55  ? 125 THR B OG1 1 
ATOM 4087 C CG2 . THR B 2 127 ? 33.138 -38.238 0.369  1.00 64.87  ? 125 THR B CG2 1 
ATOM 4088 N N   . VAL B 2 128 ? 29.908 -39.285 -0.748 1.00 63.27  ? 126 VAL B N   1 
ATOM 4089 C CA  . VAL B 2 128 ? 29.331 -40.113 -1.802 1.00 64.79  ? 126 VAL B CA  1 
ATOM 4090 C C   . VAL B 2 128 ? 30.271 -40.071 -2.999 1.00 67.88  ? 126 VAL B C   1 
ATOM 4091 O O   . VAL B 2 128 ? 30.392 -39.038 -3.669 1.00 86.30  ? 126 VAL B O   1 
ATOM 4092 C CB  . VAL B 2 128 ? 27.923 -39.641 -2.188 1.00 66.67  ? 126 VAL B CB  1 
ATOM 4093 C CG1 . VAL B 2 128 ? 27.245 -40.669 -3.082 1.00 66.16  ? 126 VAL B CG1 1 
ATOM 4094 C CG2 . VAL B 2 128 ? 27.093 -39.375 -0.941 1.00 62.60  ? 126 VAL B CG2 1 
ATOM 4095 N N   . SER B 2 129 ? 30.930 -41.191 -3.276 1.00 69.04  ? 127 SER B N   1 
ATOM 4096 C CA  . SER B 2 129 ? 31.814 -41.287 -4.433 1.00 72.27  ? 127 SER B CA  1 
ATOM 4097 C C   . SER B 2 129 ? 31.016 -41.293 -5.732 1.00 80.29  ? 127 SER B C   1 
ATOM 4098 O O   . SER B 2 129 ? 31.443 -40.725 -6.737 1.00 92.40  ? 127 SER B O   1 
ATOM 4099 C CB  . SER B 2 129 ? 32.682 -42.543 -4.345 1.00 72.94  ? 127 SER B CB  1 
ATOM 4100 O OG  . SER B 2 129 ? 33.053 -42.810 -3.006 1.00 82.40  ? 127 SER B OG  1 
ATOM 4101 N N   . VAL C 3 4   ? 22.407 -31.769 53.482 1.00 86.58  ? 2   VAL C N   1 
ATOM 4102 C CA  . VAL C 3 4   ? 21.491 -32.618 52.731 1.00 93.63  ? 2   VAL C CA  1 
ATOM 4103 C C   . VAL C 3 4   ? 22.029 -34.050 52.683 1.00 85.85  ? 2   VAL C C   1 
ATOM 4104 O O   . VAL C 3 4   ? 23.230 -34.268 52.536 1.00 80.08  ? 2   VAL C O   1 
ATOM 4105 C CB  . VAL C 3 4   ? 21.246 -32.048 51.309 1.00 84.90  ? 2   VAL C CB  1 
ATOM 4106 C CG1 . VAL C 3 4   ? 22.536 -31.984 50.511 1.00 72.34  ? 2   VAL C CG1 1 
ATOM 4107 C CG2 . VAL C 3 4   ? 20.208 -32.866 50.574 1.00 88.47  ? 2   VAL C CG2 1 
ATOM 4108 N N   . GLN C 3 5   ? 21.134 -35.023 52.833 1.00 86.99  ? 3   GLN C N   1 
ATOM 4109 C CA  . GLN C 3 5   ? 21.492 -36.434 52.847 1.00 90.08  ? 3   GLN C CA  1 
ATOM 4110 C C   . GLN C 3 5   ? 21.031 -37.097 51.556 1.00 83.73  ? 3   GLN C C   1 
ATOM 4111 O O   . GLN C 3 5   ? 19.927 -36.830 51.072 1.00 77.95  ? 3   GLN C O   1 
ATOM 4112 C CB  . GLN C 3 5   ? 20.873 -37.146 54.053 1.00 92.20  ? 3   GLN C CB  1 
ATOM 4113 C CG  . GLN C 3 5   ? 21.781 -38.176 54.707 1.00 110.33 ? 3   GLN C CG  1 
ATOM 4114 C CD  . GLN C 3 5   ? 21.328 -39.603 54.453 1.00 114.65 ? 3   GLN C CD  1 
ATOM 4115 O OE1 . GLN C 3 5   ? 20.180 -39.846 54.080 1.00 114.85 ? 3   GLN C OE1 1 
ATOM 4116 N NE2 . GLN C 3 5   ? 22.231 -40.555 54.656 1.00 107.64 ? 3   GLN C NE2 1 
ATOM 4117 N N   . LEU C 3 6   ? 21.876 -37.965 51.006 1.00 80.67  ? 4   LEU C N   1 
ATOM 4118 C CA  . LEU C 3 6   ? 21.617 -38.615 49.728 1.00 79.28  ? 4   LEU C CA  1 
ATOM 4119 C C   . LEU C 3 6   ? 21.518 -40.121 49.923 1.00 70.07  ? 4   LEU C C   1 
ATOM 4120 O O   . LEU C 3 6   ? 22.389 -40.727 50.556 1.00 75.21  ? 4   LEU C O   1 
ATOM 4121 C CB  . LEU C 3 6   ? 22.716 -38.283 48.714 1.00 75.13  ? 4   LEU C CB  1 
ATOM 4122 C CG  . LEU C 3 6   ? 23.129 -36.811 48.637 1.00 73.54  ? 4   LEU C CG  1 
ATOM 4123 C CD1 . LEU C 3 6   ? 24.409 -36.653 47.830 1.00 60.29  ? 4   LEU C CD1 1 
ATOM 4124 C CD2 . LEU C 3 6   ? 22.008 -35.966 48.047 1.00 65.27  ? 4   LEU C CD2 1 
ATOM 4125 N N   . VAL C 3 7   ? 20.460 -40.717 49.377 1.00 65.15  ? 5   VAL C N   1 
ATOM 4126 C CA  . VAL C 3 7   ? 20.262 -42.160 49.411 1.00 72.80  ? 5   VAL C CA  1 
ATOM 4127 C C   . VAL C 3 7   ? 19.900 -42.631 48.008 1.00 64.22  ? 5   VAL C C   1 
ATOM 4128 O O   . VAL C 3 7   ? 19.252 -41.915 47.239 1.00 68.98  ? 5   VAL C O   1 
ATOM 4129 C CB  . VAL C 3 7   ? 19.186 -42.575 50.444 1.00 68.83  ? 5   VAL C CB  1 
ATOM 4130 C CG1 . VAL C 3 7   ? 17.785 -42.509 49.849 1.00 72.27  ? 5   VAL C CG1 1 
ATOM 4131 C CG2 . VAL C 3 7   ? 19.479 -43.964 50.984 1.00 76.75  ? 5   VAL C CG2 1 
ATOM 4132 N N   . GLU C 3 8   ? 20.340 -43.840 47.670 1.00 72.16  ? 6   GLU C N   1 
ATOM 4133 C CA  . GLU C 3 8   ? 20.221 -44.368 46.318 1.00 73.11  ? 6   GLU C CA  1 
ATOM 4134 C C   . GLU C 3 8   ? 19.111 -45.410 46.224 1.00 66.87  ? 6   GLU C C   1 
ATOM 4135 O O   . GLU C 3 8   ? 18.671 -45.981 47.225 1.00 73.08  ? 6   GLU C O   1 
ATOM 4136 C CB  . GLU C 3 8   ? 21.545 -44.984 45.861 1.00 65.80  ? 6   GLU C CB  1 
ATOM 4137 C CG  . GLU C 3 8   ? 22.435 -44.049 45.058 1.00 64.79  ? 6   GLU C CG  1 
ATOM 4138 C CD  . GLU C 3 8   ? 23.420 -43.290 45.925 1.00 65.55  ? 6   GLU C CD  1 
ATOM 4139 O OE1 . GLU C 3 8   ? 23.244 -43.277 47.161 1.00 80.23  ? 6   GLU C OE1 1 
ATOM 4140 O OE2 . GLU C 3 8   ? 24.384 -42.723 45.369 1.00 69.86  ? 6   GLU C OE2 1 
ATOM 4141 N N   . SER C 3 9   ? 18.675 -45.662 44.991 1.00 66.82  ? 7   SER C N   1 
ATOM 4142 C CA  . SER C 3 9   ? 17.620 -46.629 44.713 1.00 73.96  ? 7   SER C CA  1 
ATOM 4143 C C   . SER C 3 9   ? 17.562 -46.870 43.210 1.00 73.52  ? 7   SER C C   1 
ATOM 4144 O O   . SER C 3 9   ? 18.098 -46.089 42.419 1.00 68.15  ? 7   SER C O   1 
ATOM 4145 C CB  . SER C 3 9   ? 16.262 -46.142 45.232 1.00 64.67  ? 7   SER C CB  1 
ATOM 4146 O OG  . SER C 3 9   ? 15.419 -47.231 45.566 1.00 68.39  ? 7   SER C OG  1 
ATOM 4147 N N   . GLY C 3 10  ? 16.911 -47.971 42.828 1.00 64.40  ? 8   GLY C N   1 
ATOM 4148 C CA  . GLY C 3 10  ? 16.610 -48.251 41.438 1.00 73.71  ? 8   GLY C CA  1 
ATOM 4149 C C   . GLY C 3 10  ? 17.570 -49.173 40.717 1.00 67.95  ? 8   GLY C C   1 
ATOM 4150 O O   . GLY C 3 10  ? 17.339 -49.476 39.540 1.00 63.04  ? 8   GLY C O   1 
ATOM 4151 N N   . GLY C 3 11  ? 18.630 -49.633 41.375 1.00 63.85  ? 9   GLY C N   1 
ATOM 4152 C CA  . GLY C 3 11  ? 19.599 -50.493 40.724 1.00 74.26  ? 9   GLY C CA  1 
ATOM 4153 C C   . GLY C 3 11  ? 19.120 -51.914 40.514 1.00 74.89  ? 9   GLY C C   1 
ATOM 4154 O O   . GLY C 3 11  ? 17.913 -52.173 40.467 1.00 74.77  ? 9   GLY C O   1 
ATOM 4155 N N   . GLY C 3 12  ? 20.057 -52.846 40.377 1.00 83.40  ? 10  GLY C N   1 
ATOM 4156 C CA  . GLY C 3 12  ? 19.746 -54.250 40.224 1.00 92.88  ? 10  GLY C CA  1 
ATOM 4157 C C   . GLY C 3 12  ? 20.410 -54.843 39.002 1.00 85.20  ? 10  GLY C C   1 
ATOM 4158 O O   . GLY C 3 12  ? 21.155 -54.186 38.277 1.00 84.22  ? 10  GLY C O   1 
ATOM 4159 N N   . LEU C 3 13  ? 20.123 -56.123 38.780 1.00 89.64  ? 11  LEU C N   1 
ATOM 4160 C CA  . LEU C 3 13  ? 20.661 -56.856 37.643 1.00 81.64  ? 11  LEU C CA  1 
ATOM 4161 C C   . LEU C 3 13  ? 19.748 -56.676 36.437 1.00 75.30  ? 11  LEU C C   1 
ATOM 4162 O O   . LEU C 3 13  ? 18.525 -56.807 36.551 1.00 78.32  ? 11  LEU C O   1 
ATOM 4163 C CB  . LEU C 3 13  ? 20.813 -58.340 37.978 1.00 76.41  ? 11  LEU C CB  1 
ATOM 4164 C CG  . LEU C 3 13  ? 21.032 -59.280 36.791 1.00 81.00  ? 11  LEU C CG  1 
ATOM 4165 C CD1 . LEU C 3 13  ? 22.516 -59.458 36.509 1.00 81.36  ? 11  LEU C CD1 1 
ATOM 4166 C CD2 . LEU C 3 13  ? 20.362 -60.627 37.032 1.00 86.31  ? 11  LEU C CD2 1 
ATOM 4167 N N   . VAL C 3 14  ? 20.348 -56.372 35.285 1.00 76.45  ? 12  VAL C N   1 
ATOM 4168 C CA  . VAL C 3 14  ? 19.616 -56.153 34.045 1.00 79.42  ? 12  VAL C CA  1 
ATOM 4169 C C   . VAL C 3 14  ? 20.394 -56.800 32.907 1.00 79.31  ? 12  VAL C C   1 
ATOM 4170 O O   . VAL C 3 14  ? 21.590 -57.074 33.019 1.00 85.35  ? 12  VAL C O   1 
ATOM 4171 C CB  . VAL C 3 14  ? 19.383 -54.647 33.766 1.00 74.48  ? 12  VAL C CB  1 
ATOM 4172 C CG1 . VAL C 3 14  ? 20.603 -54.022 33.101 1.00 70.71  ? 12  VAL C CG1 1 
ATOM 4173 C CG2 . VAL C 3 14  ? 18.132 -54.441 32.923 1.00 77.47  ? 12  VAL C CG2 1 
ATOM 4174 N N   . GLN C 3 15  ? 19.695 -57.067 31.808 1.00 76.56  ? 13  GLN C N   1 
ATOM 4175 C CA  . GLN C 3 15  ? 20.362 -57.614 30.639 1.00 85.30  ? 13  GLN C CA  1 
ATOM 4176 C C   . GLN C 3 15  ? 20.955 -56.487 29.796 1.00 85.17  ? 13  GLN C C   1 
ATOM 4177 O O   . GLN C 3 15  ? 20.766 -55.299 30.072 1.00 85.54  ? 13  GLN C O   1 
ATOM 4178 C CB  . GLN C 3 15  ? 19.394 -58.461 29.811 1.00 94.65  ? 13  GLN C CB  1 
ATOM 4179 C CG  . GLN C 3 15  ? 19.087 -59.828 30.412 1.00 90.14  ? 13  GLN C CG  1 
ATOM 4180 C CD  . GLN C 3 15  ? 18.058 -60.602 29.608 1.00 94.70  ? 13  GLN C CD  1 
ATOM 4181 O OE1 . GLN C 3 15  ? 17.254 -60.018 28.881 1.00 99.62  ? 13  GLN C OE1 1 
ATOM 4182 N NE2 . GLN C 3 15  ? 18.078 -61.924 29.737 1.00 105.98 ? 13  GLN C NE2 1 
ATOM 4183 N N   . ALA C 3 16  ? 21.685 -56.871 28.754 1.00 91.53  ? 14  ALA C N   1 
ATOM 4184 C CA  . ALA C 3 16  ? 22.312 -55.895 27.874 1.00 83.00  ? 14  ALA C CA  1 
ATOM 4185 C C   . ALA C 3 16  ? 21.285 -55.322 26.907 1.00 87.21  ? 14  ALA C C   1 
ATOM 4186 O O   . ALA C 3 16  ? 20.546 -56.068 26.256 1.00 82.53  ? 14  ALA C O   1 
ATOM 4187 C CB  . ALA C 3 16  ? 23.468 -56.532 27.105 1.00 92.08  ? 14  ALA C CB  1 
ATOM 4188 N N   . GLY C 3 17  ? 21.238 -53.993 26.819 1.00 86.65  ? 15  GLY C N   1 
ATOM 4189 C CA  . GLY C 3 17  ? 20.347 -53.304 25.911 1.00 81.09  ? 15  GLY C CA  1 
ATOM 4190 C C   . GLY C 3 17  ? 19.071 -52.783 26.535 1.00 86.53  ? 15  GLY C C   1 
ATOM 4191 O O   . GLY C 3 17  ? 18.391 -51.958 25.912 1.00 89.42  ? 15  GLY C O   1 
ATOM 4192 N N   . ASP C 3 18  ? 18.723 -53.234 27.737 1.00 86.40  ? 16  ASP C N   1 
ATOM 4193 C CA  . ASP C 3 18  ? 17.505 -52.784 28.389 1.00 84.13  ? 16  ASP C CA  1 
ATOM 4194 C C   . ASP C 3 18  ? 17.726 -51.440 29.077 1.00 75.12  ? 16  ASP C C   1 
ATOM 4195 O O   . ASP C 3 18  ? 18.835 -50.901 29.115 1.00 69.39  ? 16  ASP C O   1 
ATOM 4196 C CB  . ASP C 3 18  ? 17.020 -53.826 29.395 1.00 75.44  ? 16  ASP C CB  1 
ATOM 4197 C CG  . ASP C 3 18  ? 17.199 -55.241 28.895 1.00 95.60  ? 16  ASP C CG  1 
ATOM 4198 O OD1 . ASP C 3 18  ? 16.182 -55.931 28.674 1.00 113.50 ? 16  ASP C OD1 1 
ATOM 4199 O OD2 . ASP C 3 18  ? 18.358 -55.657 28.699 1.00 99.75  ? 16  ASP C OD2 1 
ATOM 4200 N N   . SER C 3 19  ? 16.645 -50.900 29.628 1.00 82.21  ? 17  SER C N   1 
ATOM 4201 C CA  . SER C 3 19  ? 16.663 -49.612 30.302 1.00 83.88  ? 17  SER C CA  1 
ATOM 4202 C C   . SER C 3 19  ? 16.595 -49.793 31.815 1.00 80.34  ? 17  SER C C   1 
ATOM 4203 O O   . SER C 3 19  ? 16.187 -50.840 32.326 1.00 88.48  ? 17  SER C O   1 
ATOM 4204 C CB  . SER C 3 19  ? 15.503 -48.732 29.822 1.00 81.16  ? 17  SER C CB  1 
ATOM 4205 O OG  . SER C 3 19  ? 14.261 -49.193 30.324 1.00 90.93  ? 17  SER C OG  1 
ATOM 4206 N N   . LEU C 3 20  ? 17.004 -48.747 32.528 1.00 68.07  ? 18  LEU C N   1 
ATOM 4207 C CA  . LEU C 3 20  ? 17.021 -48.752 33.983 1.00 65.13  ? 18  LEU C CA  1 
ATOM 4208 C C   . LEU C 3 20  ? 17.007 -47.310 34.463 1.00 65.16  ? 18  LEU C C   1 
ATOM 4209 O O   . LEU C 3 20  ? 17.573 -46.426 33.818 1.00 68.71  ? 18  LEU C O   1 
ATOM 4210 C CB  . LEU C 3 20  ? 18.250 -49.491 34.526 1.00 64.54  ? 18  LEU C CB  1 
ATOM 4211 C CG  . LEU C 3 20  ? 18.265 -49.851 36.012 1.00 63.17  ? 18  LEU C CG  1 
ATOM 4212 C CD1 . LEU C 3 20  ? 17.016 -50.629 36.387 1.00 64.13  ? 18  LEU C CD1 1 
ATOM 4213 C CD2 . LEU C 3 20  ? 19.514 -50.646 36.348 1.00 64.06  ? 18  LEU C CD2 1 
ATOM 4214 N N   . THR C 3 21  ? 16.349 -47.074 35.595 1.00 65.31  ? 19  THR C N   1 
ATOM 4215 C CA  . THR C 3 21  ? 16.226 -45.732 36.150 1.00 59.99  ? 19  THR C CA  1 
ATOM 4216 C C   . THR C 3 21  ? 16.810 -45.718 37.554 1.00 65.19  ? 19  THR C C   1 
ATOM 4217 O O   . THR C 3 21  ? 16.390 -46.500 38.414 1.00 63.68  ? 19  THR C O   1 
ATOM 4218 C CB  . THR C 3 21  ? 14.767 -45.267 36.160 1.00 59.33  ? 19  THR C CB  1 
ATOM 4219 O OG1 . THR C 3 21  ? 14.414 -44.783 34.858 1.00 78.47  ? 19  THR C OG1 1 
ATOM 4220 C CG2 . THR C 3 21  ? 14.568 -44.149 37.172 1.00 58.58  ? 19  THR C CG2 1 
ATOM 4221 N N   . LEU C 3 22  ? 17.780 -44.838 37.778 1.00 67.02  ? 20  LEU C N   1 
ATOM 4222 C CA  . LEU C 3 22  ? 18.407 -44.667 39.079 1.00 66.82  ? 20  LEU C CA  1 
ATOM 4223 C C   . LEU C 3 22  ? 17.809 -43.452 39.775 1.00 66.59  ? 20  LEU C C   1 
ATOM 4224 O O   . LEU C 3 22  ? 17.571 -42.419 39.143 1.00 65.65  ? 20  LEU C O   1 
ATOM 4225 C CB  . LEU C 3 22  ? 19.920 -44.496 38.939 1.00 57.31  ? 20  LEU C CB  1 
ATOM 4226 C CG  . LEU C 3 22  ? 20.802 -45.745 38.969 1.00 60.65  ? 20  LEU C CG  1 
ATOM 4227 C CD1 . LEU C 3 22  ? 20.251 -46.848 38.076 1.00 59.49  ? 20  LEU C CD1 1 
ATOM 4228 C CD2 . LEU C 3 22  ? 22.213 -45.376 38.553 1.00 58.27  ? 20  LEU C CD2 1 
ATOM 4229 N N   . SER C 3 23  ? 17.566 -43.581 41.076 1.00 58.04  ? 21  SER C N   1 
ATOM 4230 C CA  . SER C 3 23  ? 16.977 -42.514 41.871 1.00 70.34  ? 21  SER C CA  1 
ATOM 4231 C C   . SER C 3 23  ? 17.881 -42.186 43.051 1.00 74.91  ? 21  SER C C   1 
ATOM 4232 O O   . SER C 3 23  ? 18.482 -43.080 43.656 1.00 74.78  ? 21  SER C O   1 
ATOM 4233 C CB  . SER C 3 23  ? 15.580 -42.901 42.371 1.00 70.46  ? 21  SER C CB  1 
ATOM 4234 O OG  . SER C 3 23  ? 14.624 -42.829 41.327 1.00 59.39  ? 21  SER C OG  1 
ATOM 4235 N N   . CYS C 3 24  ? 17.972 -40.896 43.372 1.00 66.56  ? 22  CYS C N   1 
ATOM 4236 C CA  . CYS C 3 24  ? 18.794 -40.413 44.478 1.00 65.70  ? 22  CYS C CA  1 
ATOM 4237 C C   . CYS C 3 24  ? 17.979 -39.388 45.254 1.00 68.38  ? 22  CYS C C   1 
ATOM 4238 O O   . CYS C 3 24  ? 17.782 -38.264 44.782 1.00 70.67  ? 22  CYS C O   1 
ATOM 4239 C CB  . CYS C 3 24  ? 20.106 -39.809 43.970 1.00 75.41  ? 22  CYS C CB  1 
ATOM 4240 S SG  . CYS C 3 24  ? 21.117 -38.983 45.229 1.00 84.32  ? 22  CYS C SG  1 
ATOM 4241 N N   . ALA C 3 25  ? 17.501 -39.775 46.435 1.00 79.59  ? 23  ALA C N   1 
ATOM 4242 C CA  . ALA C 3 25  ? 16.668 -38.910 47.258 1.00 68.57  ? 23  ALA C CA  1 
ATOM 4243 C C   . ALA C 3 25  ? 17.530 -37.997 48.118 1.00 73.99  ? 23  ALA C C   1 
ATOM 4244 O O   . ALA C 3 25  ? 18.548 -38.421 48.670 1.00 79.72  ? 23  ALA C O   1 
ATOM 4245 C CB  . ALA C 3 25  ? 15.739 -39.739 48.147 1.00 65.34  ? 23  ALA C CB  1 
ATOM 4246 N N   . ALA C 3 26  ? 17.109 -36.740 48.233 1.00 79.70  ? 24  ALA C N   1 
ATOM 4247 C CA  . ALA C 3 26  ? 17.852 -35.728 48.965 1.00 84.62  ? 24  ALA C CA  1 
ATOM 4248 C C   . ALA C 3 26  ? 17.024 -35.201 50.129 1.00 92.72  ? 24  ALA C C   1 
ATOM 4249 O O   . ALA C 3 26  ? 15.791 -35.155 50.067 1.00 85.91  ? 24  ALA C O   1 
ATOM 4250 C CB  . ALA C 3 26  ? 18.259 -34.569 48.047 1.00 85.79  ? 24  ALA C CB  1 
ATOM 4251 N N   . SER C 3 27  ? 17.716 -34.809 51.196 1.00 116.35 ? 25  SER C N   1 
ATOM 4252 C CA  . SER C 3 27  ? 17.058 -34.199 52.342 1.00 118.48 ? 25  SER C CA  1 
ATOM 4253 C C   . SER C 3 27  ? 16.445 -32.857 51.955 1.00 124.18 ? 25  SER C C   1 
ATOM 4254 O O   . SER C 3 27  ? 16.913 -32.173 51.040 1.00 121.97 ? 25  SER C O   1 
ATOM 4255 C CB  . SER C 3 27  ? 18.048 -34.012 53.490 1.00 116.35 ? 25  SER C CB  1 
ATOM 4256 O OG  . SER C 3 27  ? 17.562 -33.077 54.437 1.00 122.02 ? 25  SER C OG  1 
ATOM 4257 N N   . GLY C 3 28  ? 15.388 -32.480 52.670 1.00 111.27 ? 26  GLY C N   1 
ATOM 4258 C CA  . GLY C 3 28  ? 14.647 -31.279 52.343 1.00 115.65 ? 26  GLY C CA  1 
ATOM 4259 C C   . GLY C 3 28  ? 15.126 -30.025 53.045 1.00 111.51 ? 26  GLY C C   1 
ATOM 4260 O O   . GLY C 3 28  ? 14.479 -29.546 53.980 1.00 115.26 ? 26  GLY C O   1 
ATOM 4261 N N   . ARG C 3 29  ? 16.259 -29.482 52.602 1.00 111.79 ? 27  ARG C N   1 
ATOM 4262 C CA  . ARG C 3 29  ? 16.754 -28.210 53.125 1.00 113.51 ? 27  ARG C CA  1 
ATOM 4263 C C   . ARG C 3 29  ? 17.630 -27.574 52.056 1.00 102.94 ? 27  ARG C C   1 
ATOM 4264 O O   . ARG C 3 29  ? 18.742 -28.052 51.809 1.00 100.12 ? 27  ARG C O   1 
ATOM 4265 C CB  . ARG C 3 29  ? 17.528 -28.404 54.426 1.00 118.65 ? 27  ARG C CB  1 
ATOM 4266 C CG  . ARG C 3 29  ? 17.860 -27.100 55.135 1.00 117.89 ? 27  ARG C CG  1 
ATOM 4267 C CD  . ARG C 3 29  ? 16.597 -26.310 55.447 1.00 127.35 ? 27  ARG C CD  1 
ATOM 4268 N NE  . ARG C 3 29  ? 16.870 -24.896 55.677 1.00 130.50 ? 27  ARG C NE  1 
ATOM 4269 C CZ  . ARG C 3 29  ? 16.258 -23.903 55.044 1.00 127.97 ? 27  ARG C CZ  1 
ATOM 4270 N NH1 . ARG C 3 29  ? 15.334 -24.134 54.126 1.00 131.29 ? 27  ARG C NH1 1 
ATOM 4271 N NH2 . ARG C 3 29  ? 16.584 -22.648 55.339 1.00 130.29 ? 27  ARG C NH2 1 
ATOM 4272 N N   . THR C 3 30  ? 17.114 -26.515 51.422 1.00 103.69 ? 28  THR C N   1 
ATOM 4273 C CA  . THR C 3 30  ? 17.821 -25.738 50.392 1.00 96.02  ? 28  THR C CA  1 
ATOM 4274 C C   . THR C 3 30  ? 18.448 -26.631 49.317 1.00 89.61  ? 28  THR C C   1 
ATOM 4275 O O   . THR C 3 30  ? 19.422 -26.258 48.656 1.00 87.24  ? 28  THR C O   1 
ATOM 4276 C CB  . THR C 3 30  ? 18.852 -24.785 51.026 1.00 88.16  ? 28  THR C CB  1 
ATOM 4277 O OG1 . THR C 3 30  ? 19.088 -23.681 50.144 1.00 90.24  ? 28  THR C OG1 1 
ATOM 4278 C CG2 . THR C 3 30  ? 20.187 -25.464 51.374 1.00 93.07  ? 28  THR C CG2 1 
ATOM 4279 N N   . ALA C 3 31  ? 17.845 -27.801 49.088 1.00 88.41  ? 29  ALA C N   1 
ATOM 4280 C CA  . ALA C 3 31  ? 18.380 -28.745 48.113 1.00 84.22  ? 29  ALA C CA  1 
ATOM 4281 C C   . ALA C 3 31  ? 18.327 -28.212 46.688 1.00 75.10  ? 29  ALA C C   1 
ATOM 4282 O O   . ALA C 3 31  ? 19.053 -28.718 45.825 1.00 75.68  ? 29  ALA C O   1 
ATOM 4283 C CB  . ALA C 3 31  ? 17.624 -30.071 48.197 1.00 88.01  ? 29  ALA C CB  1 
ATOM 4284 N N   . TYR C 3 32  ? 17.490 -27.208 46.416 1.00 76.67  ? 30  TYR C N   1 
ATOM 4285 C CA  . TYR C 3 32  ? 17.402 -26.661 45.068 1.00 78.77  ? 30  TYR C CA  1 
ATOM 4286 C C   . TYR C 3 32  ? 18.593 -25.784 44.703 1.00 68.75  ? 30  TYR C C   1 
ATOM 4287 O O   . TYR C 3 32  ? 18.753 -25.447 43.525 1.00 80.76  ? 30  TYR C O   1 
ATOM 4288 C CB  . TYR C 3 32  ? 16.100 -25.870 44.898 1.00 76.07  ? 30  TYR C CB  1 
ATOM 4289 C CG  . TYR C 3 32  ? 15.865 -24.811 45.951 1.00 81.86  ? 30  TYR C CG  1 
ATOM 4290 C CD1 . TYR C 3 32  ? 15.211 -25.117 47.139 1.00 84.57  ? 30  TYR C CD1 1 
ATOM 4291 C CD2 . TYR C 3 32  ? 16.288 -23.504 45.755 1.00 74.88  ? 30  TYR C CD2 1 
ATOM 4292 C CE1 . TYR C 3 32  ? 14.992 -24.151 48.103 1.00 84.41  ? 30  TYR C CE1 1 
ATOM 4293 C CE2 . TYR C 3 32  ? 16.074 -22.531 46.713 1.00 86.83  ? 30  TYR C CE2 1 
ATOM 4294 C CZ  . TYR C 3 32  ? 15.426 -22.860 47.885 1.00 94.71  ? 30  TYR C CZ  1 
ATOM 4295 O OH  . TYR C 3 32  ? 15.210 -21.893 48.842 1.00 86.95  ? 30  TYR C OH  1 
ATOM 4296 N N   . ARG C 3 33  ? 19.428 -25.408 45.670 1.00 70.85  ? 31  ARG C N   1 
ATOM 4297 C CA  . ARG C 3 33  ? 20.651 -24.666 45.401 1.00 62.58  ? 31  ARG C CA  1 
ATOM 4298 C C   . ARG C 3 33  ? 21.874 -25.574 45.316 1.00 62.80  ? 31  ARG C C   1 
ATOM 4299 O O   . ARG C 3 33  ? 23.000 -25.076 45.217 1.00 56.05  ? 31  ARG C O   1 
ATOM 4300 C CB  . ARG C 3 33  ? 20.865 -23.590 46.471 1.00 59.52  ? 31  ARG C CB  1 
ATOM 4301 C CG  . ARG C 3 33  ? 19.693 -22.633 46.636 1.00 72.88  ? 31  ARG C CG  1 
ATOM 4302 C CD  . ARG C 3 33  ? 19.879 -21.730 47.847 1.00 75.13  ? 31  ARG C CD  1 
ATOM 4303 N NE  . ARG C 3 33  ? 18.604 -21.378 48.464 1.00 70.48  ? 31  ARG C NE  1 
ATOM 4304 C CZ  . ARG C 3 33  ? 18.253 -20.153 48.830 1.00 78.25  ? 31  ARG C CZ  1 
ATOM 4305 N NH1 . ARG C 3 33  ? 19.066 -19.122 48.668 1.00 88.40  ? 31  ARG C NH1 1 
ATOM 4306 N NH2 . ARG C 3 33  ? 17.056 -19.958 49.376 1.00 88.10  ? 31  ARG C NH2 1 
ATOM 4307 N N   . TYR C 3 34  ? 21.674 -26.891 45.337 1.00 71.68  ? 32  TYR C N   1 
ATOM 4308 C CA  . TYR C 3 34  ? 22.759 -27.864 45.316 1.00 65.73  ? 32  TYR C CA  1 
ATOM 4309 C C   . TYR C 3 34  ? 22.903 -28.467 43.923 1.00 67.40  ? 32  TYR C C   1 
ATOM 4310 O O   . TYR C 3 34  ? 21.910 -28.829 43.284 1.00 57.98  ? 32  TYR C O   1 
ATOM 4311 C CB  . TYR C 3 34  ? 22.513 -28.976 46.343 1.00 58.01  ? 32  TYR C CB  1 
ATOM 4312 C CG  . TYR C 3 34  ? 23.144 -28.732 47.703 1.00 70.07  ? 32  TYR C CG  1 
ATOM 4313 C CD1 . TYR C 3 34  ? 22.448 -28.066 48.704 1.00 68.70  ? 32  TYR C CD1 1 
ATOM 4314 C CD2 . TYR C 3 34  ? 24.431 -29.177 47.988 1.00 64.48  ? 32  TYR C CD2 1 
ATOM 4315 C CE1 . TYR C 3 34  ? 23.018 -27.839 49.947 1.00 62.99  ? 32  TYR C CE1 1 
ATOM 4316 C CE2 . TYR C 3 34  ? 25.010 -28.954 49.230 1.00 63.39  ? 32  TYR C CE2 1 
ATOM 4317 C CZ  . TYR C 3 34  ? 24.298 -28.285 50.205 1.00 64.21  ? 32  TYR C CZ  1 
ATOM 4318 O OH  . TYR C 3 34  ? 24.863 -28.060 51.442 1.00 65.37  ? 32  TYR C OH  1 
ATOM 4319 N N   . GLY C 3 35  ? 24.146 -28.567 43.456 1.00 63.60  ? 33  GLY C N   1 
ATOM 4320 C CA  . GLY C 3 35  ? 24.435 -29.216 42.187 1.00 57.71  ? 33  GLY C CA  1 
ATOM 4321 C C   . GLY C 3 35  ? 24.765 -30.686 42.395 1.00 62.75  ? 33  GLY C C   1 
ATOM 4322 O O   . GLY C 3 35  ? 25.412 -31.060 43.371 1.00 61.91  ? 33  GLY C O   1 
ATOM 4323 N N   . MET C 3 36  ? 24.310 -31.515 41.462 1.00 61.52  ? 34  MET C N   1 
ATOM 4324 C CA  . MET C 3 36  ? 24.368 -32.960 41.618 1.00 55.82  ? 34  MET C CA  1 
ATOM 4325 C C   . MET C 3 36  ? 25.167 -33.601 40.491 1.00 59.86  ? 34  MET C C   1 
ATOM 4326 O O   . MET C 3 36  ? 25.367 -33.014 39.424 1.00 59.13  ? 34  MET C O   1 
ATOM 4327 C CB  . MET C 3 36  ? 22.958 -33.559 41.666 1.00 55.68  ? 34  MET C CB  1 
ATOM 4328 C CG  . MET C 3 36  ? 21.961 -32.677 42.397 1.00 63.34  ? 34  MET C CG  1 
ATOM 4329 S SD  . MET C 3 36  ? 22.165 -32.655 44.191 1.00 73.20  ? 34  MET C SD  1 
ATOM 4330 C CE  . MET C 3 36  ? 22.755 -34.318 44.501 1.00 65.18  ? 34  MET C CE  1 
ATOM 4331 N N   . GLY C 3 37  ? 25.620 -34.826 40.749 1.00 61.63  ? 35  GLY C N   1 
ATOM 4332 C CA  . GLY C 3 37  ? 26.389 -35.576 39.776 1.00 69.02  ? 35  GLY C CA  1 
ATOM 4333 C C   . GLY C 3 37  ? 26.399 -37.050 40.109 1.00 71.19  ? 35  GLY C C   1 
ATOM 4334 O O   . GLY C 3 37  ? 26.218 -37.449 41.264 1.00 73.13  ? 35  GLY C O   1 
ATOM 4335 N N   . TRP C 3 38  ? 26.617 -37.859 39.076 1.00 71.99  ? 36  TRP C N   1 
ATOM 4336 C CA  . TRP C 3 38  ? 26.643 -39.309 39.196 1.00 55.00  ? 36  TRP C CA  1 
ATOM 4337 C C   . TRP C 3 38  ? 28.042 -39.832 38.899 1.00 64.00  ? 36  TRP C C   1 
ATOM 4338 O O   . TRP C 3 38  ? 28.692 -39.392 37.945 1.00 70.16  ? 36  TRP C O   1 
ATOM 4339 C CB  . TRP C 3 38  ? 25.636 -39.959 38.242 1.00 56.98  ? 36  TRP C CB  1 
ATOM 4340 C CG  . TRP C 3 38  ? 24.214 -39.890 38.712 1.00 59.83  ? 36  TRP C CG  1 
ATOM 4341 C CD1 . TRP C 3 38  ? 23.271 -38.976 38.339 1.00 62.31  ? 36  TRP C CD1 1 
ATOM 4342 C CD2 . TRP C 3 38  ? 23.567 -40.780 39.631 1.00 65.35  ? 36  TRP C CD2 1 
ATOM 4343 N NE1 . TRP C 3 38  ? 22.081 -39.237 38.974 1.00 61.56  ? 36  TRP C NE1 1 
ATOM 4344 C CE2 . TRP C 3 38  ? 22.236 -40.340 39.772 1.00 66.60  ? 36  TRP C CE2 1 
ATOM 4345 C CE3 . TRP C 3 38  ? 23.985 -41.904 40.350 1.00 59.79  ? 36  TRP C CE3 1 
ATOM 4346 C CZ2 . TRP C 3 38  ? 21.320 -40.984 40.602 1.00 64.04  ? 36  TRP C CZ2 1 
ATOM 4347 C CZ3 . TRP C 3 38  ? 23.074 -42.541 41.174 1.00 58.24  ? 36  TRP C CZ3 1 
ATOM 4348 C CH2 . TRP C 3 38  ? 21.758 -42.080 41.293 1.00 58.59  ? 36  TRP C CH2 1 
ATOM 4349 N N   . PHE C 3 39  ? 28.498 -40.775 39.720 1.00 70.84  ? 37  PHE C N   1 
ATOM 4350 C CA  . PHE C 3 39  ? 29.793 -41.415 39.551 1.00 75.16  ? 37  PHE C CA  1 
ATOM 4351 C C   . PHE C 3 39  ? 29.624 -42.924 39.640 1.00 77.29  ? 37  PHE C C   1 
ATOM 4352 O O   . PHE C 3 39  ? 28.715 -43.422 40.309 1.00 79.33  ? 37  PHE C O   1 
ATOM 4353 C CB  . PHE C 3 39  ? 30.803 -40.949 40.613 1.00 75.30  ? 37  PHE C CB  1 
ATOM 4354 C CG  . PHE C 3 39  ? 31.317 -39.554 40.397 1.00 70.14  ? 37  PHE C CG  1 
ATOM 4355 C CD1 . PHE C 3 39  ? 30.542 -38.454 40.728 1.00 69.21  ? 37  PHE C CD1 1 
ATOM 4356 C CD2 . PHE C 3 39  ? 32.582 -39.342 39.873 1.00 68.87  ? 37  PHE C CD2 1 
ATOM 4357 C CE1 . PHE C 3 39  ? 31.015 -37.170 40.534 1.00 63.03  ? 37  PHE C CE1 1 
ATOM 4358 C CE2 . PHE C 3 39  ? 33.061 -38.061 39.678 1.00 72.89  ? 37  PHE C CE2 1 
ATOM 4359 C CZ  . PHE C 3 39  ? 32.277 -36.973 40.009 1.00 66.29  ? 37  PHE C CZ  1 
ATOM 4360 N N   . ARG C 3 40  ? 30.508 -43.652 38.961 1.00 81.71  ? 38  ARG C N   1 
ATOM 4361 C CA  . ARG C 3 40  ? 30.531 -45.104 39.046 1.00 74.42  ? 38  ARG C CA  1 
ATOM 4362 C C   . ARG C 3 40  ? 31.949 -45.574 39.334 1.00 78.46  ? 38  ARG C C   1 
ATOM 4363 O O   . ARG C 3 40  ? 32.924 -44.850 39.117 1.00 81.72  ? 38  ARG C O   1 
ATOM 4364 C CB  . ARG C 3 40  ? 29.992 -45.765 37.770 1.00 85.14  ? 38  ARG C CB  1 
ATOM 4365 C CG  . ARG C 3 40  ? 30.860 -45.623 36.539 1.00 81.01  ? 38  ARG C CG  1 
ATOM 4366 C CD  . ARG C 3 40  ? 30.193 -46.303 35.352 1.00 77.10  ? 38  ARG C CD  1 
ATOM 4367 N NE  . ARG C 3 40  ? 30.800 -45.933 34.080 1.00 76.94  ? 38  ARG C NE  1 
ATOM 4368 C CZ  . ARG C 3 40  ? 30.206 -46.068 32.902 1.00 79.74  ? 38  ARG C CZ  1 
ATOM 4369 N NH1 . ARG C 3 40  ? 28.981 -46.557 32.799 1.00 77.54  ? 38  ARG C NH1 1 
ATOM 4370 N NH2 . ARG C 3 40  ? 30.856 -45.702 31.801 1.00 87.08  ? 38  ARG C NH2 1 
ATOM 4371 N N   . GLN C 3 41  ? 32.052 -46.805 39.831 1.00 79.80  ? 39  GLN C N   1 
ATOM 4372 C CA  . GLN C 3 41  ? 33.320 -47.317 40.330 1.00 84.20  ? 39  GLN C CA  1 
ATOM 4373 C C   . GLN C 3 41  ? 33.417 -48.813 40.078 1.00 84.85  ? 39  GLN C C   1 
ATOM 4374 O O   . GLN C 3 41  ? 32.518 -49.569 40.458 1.00 79.31  ? 39  GLN C O   1 
ATOM 4375 C CB  . GLN C 3 41  ? 33.465 -47.024 41.827 1.00 86.53  ? 39  GLN C CB  1 
ATOM 4376 C CG  . GLN C 3 41  ? 34.649 -47.700 42.485 1.00 89.77  ? 39  GLN C CG  1 
ATOM 4377 C CD  . GLN C 3 41  ? 35.015 -47.057 43.804 1.00 90.54  ? 39  GLN C CD  1 
ATOM 4378 O OE1 . GLN C 3 41  ? 34.159 -46.846 44.663 1.00 96.71  ? 39  GLN C OE1 1 
ATOM 4379 N NE2 . GLN C 3 41  ? 36.293 -46.737 43.973 1.00 94.54  ? 39  GLN C NE2 1 
ATOM 4380 N N   . HIS C 3 42  ? 34.509 -49.231 39.445 1.00 89.82  ? 40  HIS C N   1 
ATOM 4381 C CA  . HIS C 3 42  ? 34.795 -50.641 39.256 1.00 77.95  ? 40  HIS C CA  1 
ATOM 4382 C C   . HIS C 3 42  ? 35.393 -51.228 40.530 1.00 84.08  ? 40  HIS C C   1 
ATOM 4383 O O   . HIS C 3 42  ? 35.954 -50.501 41.353 1.00 89.22  ? 40  HIS C O   1 
ATOM 4384 C CB  . HIS C 3 42  ? 35.754 -50.827 38.083 1.00 85.81  ? 40  HIS C CB  1 
ATOM 4385 C CG  . HIS C 3 42  ? 35.164 -50.460 36.757 1.00 87.13  ? 40  HIS C CG  1 
ATOM 4386 N ND1 . HIS C 3 42  ? 33.826 -50.172 36.593 1.00 82.36  ? 40  HIS C ND1 1 
ATOM 4387 C CD2 . HIS C 3 42  ? 35.730 -50.331 35.534 1.00 85.38  ? 40  HIS C CD2 1 
ATOM 4388 C CE1 . HIS C 3 42  ? 33.593 -49.883 35.325 1.00 85.82  ? 40  HIS C CE1 1 
ATOM 4389 N NE2 . HIS C 3 42  ? 34.732 -49.972 34.661 1.00 93.40  ? 40  HIS C NE2 1 
ATOM 4390 N N   . PRO C 3 43  ? 35.271 -52.551 40.727 1.00 90.97  ? 41  PRO C N   1 
ATOM 4391 C CA  . PRO C 3 43  ? 35.833 -53.172 41.937 1.00 84.51  ? 41  PRO C CA  1 
ATOM 4392 C C   . PRO C 3 43  ? 37.319 -52.895 42.108 1.00 88.79  ? 41  PRO C C   1 
ATOM 4393 O O   . PRO C 3 43  ? 38.152 -53.442 41.380 1.00 89.62  ? 41  PRO C O   1 
ATOM 4394 C CB  . PRO C 3 43  ? 35.569 -54.672 41.733 1.00 86.81  ? 41  PRO C CB  1 
ATOM 4395 C CG  . PRO C 3 43  ? 35.024 -54.827 40.351 1.00 85.92  ? 41  PRO C CG  1 
ATOM 4396 C CD  . PRO C 3 43  ? 34.504 -53.505 39.909 1.00 85.37  ? 41  PRO C CD  1 
ATOM 4397 N N   . GLY C 3 44  ? 37.656 -52.043 43.075 1.00 91.92  ? 42  GLY C N   1 
ATOM 4398 C CA  . GLY C 3 44  ? 39.031 -51.672 43.328 1.00 97.79  ? 42  GLY C CA  1 
ATOM 4399 C C   . GLY C 3 44  ? 39.549 -50.514 42.503 1.00 98.36  ? 42  GLY C C   1 
ATOM 4400 O O   . GLY C 3 44  ? 40.687 -50.080 42.724 1.00 95.93  ? 42  GLY C O   1 
ATOM 4401 N N   . LYS C 3 45  ? 38.759 -49.999 41.566 1.00 92.56  ? 43  LYS C N   1 
ATOM 4402 C CA  . LYS C 3 45  ? 39.178 -48.900 40.714 1.00 98.58  ? 43  LYS C CA  1 
ATOM 4403 C C   . LYS C 3 45  ? 38.596 -47.584 41.228 1.00 101.64 ? 43  LYS C C   1 
ATOM 4404 O O   . LYS C 3 45  ? 37.854 -47.540 42.212 1.00 102.35 ? 43  LYS C O   1 
ATOM 4405 C CB  . LYS C 3 45  ? 38.770 -49.165 39.263 1.00 97.56  ? 43  LYS C CB  1 
ATOM 4406 C CG  . LYS C 3 45  ? 39.419 -50.400 38.660 1.00 90.87  ? 43  LYS C CG  1 
ATOM 4407 C CD  . LYS C 3 45  ? 40.936 -50.273 38.654 1.00 95.61  ? 43  LYS C CD  1 
ATOM 4408 C CE  . LYS C 3 45  ? 41.591 -51.318 39.548 1.00 108.74 ? 43  LYS C CE  1 
ATOM 4409 N NZ  . LYS C 3 45  ? 43.077 -51.293 39.442 1.00 106.73 ? 43  LYS C NZ  1 
ATOM 4410 N N   . GLU C 3 46  ? 38.942 -46.496 40.546 1.00 103.95 ? 44  GLU C N   1 
ATOM 4411 C CA  . GLU C 3 46  ? 38.562 -45.167 40.995 1.00 106.03 ? 44  GLU C CA  1 
ATOM 4412 C C   . GLU C 3 46  ? 37.114 -44.857 40.619 1.00 98.34  ? 44  GLU C C   1 
ATOM 4413 O O   . GLU C 3 46  ? 36.475 -45.566 39.837 1.00 95.66  ? 44  GLU C O   1 
ATOM 4414 C CB  . GLU C 3 46  ? 39.501 -44.116 40.403 1.00 100.48 ? 44  GLU C CB  1 
ATOM 4415 C CG  . GLU C 3 46  ? 40.974 -44.385 40.668 1.00 111.52 ? 44  GLU C CG  1 
ATOM 4416 C CD  . GLU C 3 46  ? 41.380 -44.063 42.093 1.00 118.57 ? 44  GLU C CD  1 
ATOM 4417 O OE1 . GLU C 3 46  ? 40.636 -43.325 42.774 1.00 121.88 ? 44  GLU C OE1 1 
ATOM 4418 O OE2 . GLU C 3 46  ? 42.442 -44.550 42.535 1.00 120.76 ? 44  GLU C OE2 1 
ATOM 4419 N N   . ARG C 3 47  ? 36.596 -43.776 41.199 1.00 94.62  ? 45  ARG C N   1 
ATOM 4420 C CA  . ARG C 3 47  ? 35.248 -43.296 40.913 1.00 91.57  ? 45  ARG C CA  1 
ATOM 4421 C C   . ARG C 3 47  ? 35.325 -42.338 39.732 1.00 87.68  ? 45  ARG C C   1 
ATOM 4422 O O   . ARG C 3 47  ? 35.805 -41.208 39.871 1.00 85.61  ? 45  ARG C O   1 
ATOM 4423 C CB  . ARG C 3 47  ? 34.644 -42.611 42.137 1.00 81.65  ? 45  ARG C CB  1 
ATOM 4424 C CG  . ARG C 3 47  ? 35.420 -42.854 43.421 1.00 94.96  ? 45  ARG C CG  1 
ATOM 4425 C CD  . ARG C 3 47  ? 34.828 -42.094 44.605 1.00 92.09  ? 45  ARG C CD  1 
ATOM 4426 N NE  . ARG C 3 47  ? 33.699 -42.775 45.229 1.00 92.41  ? 45  ARG C NE  1 
ATOM 4427 C CZ  . ARG C 3 47  ? 33.811 -43.634 46.234 1.00 93.11  ? 45  ARG C CZ  1 
ATOM 4428 N NH1 . ARG C 3 47  ? 34.993 -43.986 46.714 1.00 95.03  ? 45  ARG C NH1 1 
ATOM 4429 N NH2 . ARG C 3 47  ? 32.711 -44.149 46.775 1.00 89.43  ? 45  ARG C NH2 1 
ATOM 4430 N N   . GLU C 3 48  ? 34.858 -42.786 38.572 1.00 86.92  ? 46  GLU C N   1 
ATOM 4431 C CA  . GLU C 3 48  ? 34.896 -41.983 37.361 1.00 86.75  ? 46  GLU C CA  1 
ATOM 4432 C C   . GLU C 3 48  ? 33.546 -41.321 37.114 1.00 83.53  ? 46  GLU C C   1 
ATOM 4433 O O   . GLU C 3 48  ? 32.506 -41.758 37.616 1.00 82.38  ? 46  GLU C O   1 
ATOM 4434 C CB  . GLU C 3 48  ? 35.302 -42.835 36.156 1.00 89.53  ? 46  GLU C CB  1 
ATOM 4435 C CG  . GLU C 3 48  ? 34.401 -44.026 35.874 1.00 90.99  ? 46  GLU C CG  1 
ATOM 4436 C CD  . GLU C 3 48  ? 33.686 -43.908 34.541 1.00 101.89 ? 46  GLU C CD  1 
ATOM 4437 O OE1 . GLU C 3 48  ? 34.080 -43.046 33.728 1.00 102.80 ? 46  GLU C OE1 1 
ATOM 4438 O OE2 . GLU C 3 48  ? 32.747 -44.693 34.294 1.00 100.59 ? 46  GLU C OE2 1 
ATOM 4439 N N   . PHE C 3 49  ? 33.581 -40.252 36.326 1.00 76.46  ? 47  PHE C N   1 
ATOM 4440 C CA  . PHE C 3 49  ? 32.415 -39.411 36.105 1.00 73.20  ? 47  PHE C CA  1 
ATOM 4441 C C   . PHE C 3 49  ? 31.417 -40.077 35.166 1.00 74.55  ? 47  PHE C C   1 
ATOM 4442 O O   . PHE C 3 49  ? 31.791 -40.785 34.227 1.00 83.50  ? 47  PHE C O   1 
ATOM 4443 C CB  . PHE C 3 49  ? 32.841 -38.067 35.519 1.00 77.75  ? 47  PHE C CB  1 
ATOM 4444 C CG  . PHE C 3 49  ? 31.729 -37.071 35.416 1.00 75.24  ? 47  PHE C CG  1 
ATOM 4445 C CD1 . PHE C 3 49  ? 30.868 -36.856 36.478 1.00 71.74  ? 47  PHE C CD1 1 
ATOM 4446 C CD2 . PHE C 3 49  ? 31.535 -36.358 34.246 1.00 66.75  ? 47  PHE C CD2 1 
ATOM 4447 C CE1 . PHE C 3 49  ? 29.841 -35.937 36.376 1.00 60.61  ? 47  PHE C CE1 1 
ATOM 4448 C CE2 . PHE C 3 49  ? 30.515 -35.440 34.140 1.00 66.01  ? 47  PHE C CE2 1 
ATOM 4449 C CZ  . PHE C 3 49  ? 29.668 -35.229 35.203 1.00 62.23  ? 47  PHE C CZ  1 
ATOM 4450 N N   . VAL C 3 50  ? 30.133 -39.830 35.424 1.00 66.21  ? 48  VAL C N   1 
ATOM 4451 C CA  . VAL C 3 50  ? 29.068 -40.298 34.544 1.00 74.42  ? 48  VAL C CA  1 
ATOM 4452 C C   . VAL C 3 50  ? 28.318 -39.090 33.995 1.00 73.92  ? 48  VAL C C   1 
ATOM 4453 O O   . VAL C 3 50  ? 28.355 -38.820 32.789 1.00 75.22  ? 48  VAL C O   1 
ATOM 4454 C CB  . VAL C 3 50  ? 28.118 -41.268 35.272 1.00 73.26  ? 48  VAL C CB  1 
ATOM 4455 C CG1 . VAL C 3 50  ? 26.771 -41.345 34.561 1.00 69.39  ? 48  VAL C CG1 1 
ATOM 4456 C CG2 . VAL C 3 50  ? 28.745 -42.649 35.375 1.00 78.16  ? 48  VAL C CG2 1 
ATOM 4457 N N   . ALA C 3 51  ? 27.651 -38.341 34.873 1.00 65.09  ? 49  ALA C N   1 
ATOM 4458 C CA  . ALA C 3 51  ? 26.830 -37.221 34.437 1.00 70.10  ? 49  ALA C CA  1 
ATOM 4459 C C   . ALA C 3 51  ? 26.542 -36.308 35.620 1.00 64.35  ? 49  ALA C C   1 
ATOM 4460 O O   . ALA C 3 51  ? 26.369 -36.779 36.746 1.00 59.83  ? 49  ALA C O   1 
ATOM 4461 C CB  . ALA C 3 51  ? 25.516 -37.704 33.810 1.00 60.29  ? 49  ALA C CB  1 
ATOM 4462 N N   . SER C 3 52  ? 26.492 -35.004 35.354 1.00 58.78  ? 50  SER C N   1 
ATOM 4463 C CA  . SER C 3 52  ? 26.195 -34.016 36.380 1.00 67.86  ? 50  SER C CA  1 
ATOM 4464 C C   . SER C 3 52  ? 25.223 -32.987 35.825 1.00 58.89  ? 50  SER C C   1 
ATOM 4465 O O   . SER C 3 52  ? 25.144 -32.762 34.615 1.00 58.89  ? 50  SER C O   1 
ATOM 4466 C CB  . SER C 3 52  ? 27.461 -33.310 36.885 1.00 63.49  ? 50  SER C CB  1 
ATOM 4467 O OG  . SER C 3 52  ? 28.017 -32.482 35.877 1.00 58.59  ? 50  SER C OG  1 
ATOM 4468 N N   . ILE C 3 53  ? 24.484 -32.360 36.733 1.00 52.57  ? 51  ILE C N   1 
ATOM 4469 C CA  . ILE C 3 53  ? 23.549 -31.297 36.398 1.00 53.29  ? 51  ILE C CA  1 
ATOM 4470 C C   . ILE C 3 53  ? 23.977 -30.035 37.132 1.00 59.78  ? 51  ILE C C   1 
ATOM 4471 O O   . ILE C 3 53  ? 24.341 -30.083 38.313 1.00 58.11  ? 51  ILE C O   1 
ATOM 4472 C CB  . ILE C 3 53  ? 22.096 -31.688 36.750 1.00 50.18  ? 51  ILE C CB  1 
ATOM 4473 C CG1 . ILE C 3 53  ? 21.127 -30.556 36.411 1.00 50.24  ? 51  ILE C CG1 1 
ATOM 4474 C CG2 . ILE C 3 53  ? 21.973 -32.082 38.214 1.00 52.67  ? 51  ILE C CG2 1 
ATOM 4475 C CD1 . ILE C 3 53  ? 19.713 -30.825 36.867 1.00 53.34  ? 51  ILE C CD1 1 
ATOM 4476 N N   . TRP C 3 54  ? 23.968 -28.912 36.420 1.00 67.24  ? 52  TRP C N   1 
ATOM 4477 C CA  . TRP C 3 54  ? 24.264 -27.629 37.041 1.00 69.78  ? 52  TRP C CA  1 
ATOM 4478 C C   . TRP C 3 54  ? 23.188 -27.291 38.068 1.00 66.49  ? 52  TRP C C   1 
ATOM 4479 O O   . TRP C 3 54  ? 22.030 -27.698 37.943 1.00 67.94  ? 52  TRP C O   1 
ATOM 4480 C CB  . TRP C 3 54  ? 24.365 -26.535 35.974 1.00 70.87  ? 52  TRP C CB  1 
ATOM 4481 C CG  . TRP C 3 54  ? 24.892 -25.205 36.456 1.00 70.46  ? 52  TRP C CG  1 
ATOM 4482 C CD1 . TRP C 3 54  ? 24.352 -23.977 36.204 1.00 67.65  ? 52  TRP C CD1 1 
ATOM 4483 C CD2 . TRP C 3 54  ? 26.066 -24.968 37.249 1.00 68.63  ? 52  TRP C CD2 1 
ATOM 4484 N NE1 . TRP C 3 54  ? 25.106 -22.994 36.796 1.00 64.40  ? 52  TRP C NE1 1 
ATOM 4485 C CE2 . TRP C 3 54  ? 26.163 -23.575 37.444 1.00 69.21  ? 52  TRP C CE2 1 
ATOM 4486 C CE3 . TRP C 3 54  ? 27.041 -25.797 37.815 1.00 68.36  ? 52  TRP C CE3 1 
ATOM 4487 C CZ2 . TRP C 3 54  ? 27.195 -22.994 38.179 1.00 70.62  ? 52  TRP C CZ2 1 
ATOM 4488 C CZ3 . TRP C 3 54  ? 28.062 -25.217 38.548 1.00 67.82  ? 52  TRP C CZ3 1 
ATOM 4489 C CH2 . TRP C 3 54  ? 28.131 -23.829 38.722 1.00 69.86  ? 52  TRP C CH2 1 
ATOM 4490 N N   . TRP C 3 55  ? 23.583 -26.543 39.103 1.00 58.88  ? 53  TRP C N   1 
ATOM 4491 C CA  . TRP C 3 55  ? 22.685 -26.317 40.230 1.00 56.05  ? 53  TRP C CA  1 
ATOM 4492 C C   . TRP C 3 55  ? 21.461 -25.489 39.855 1.00 61.50  ? 53  TRP C C   1 
ATOM 4493 O O   . TRP C 3 55  ? 20.489 -25.471 40.618 1.00 55.72  ? 53  TRP C O   1 
ATOM 4494 C CB  . TRP C 3 55  ? 23.441 -25.658 41.388 1.00 57.19  ? 53  TRP C CB  1 
ATOM 4495 C CG  . TRP C 3 55  ? 23.749 -24.201 41.203 1.00 64.54  ? 53  TRP C CG  1 
ATOM 4496 C CD1 . TRP C 3 55  ? 24.893 -23.666 40.688 1.00 63.80  ? 53  TRP C CD1 1 
ATOM 4497 C CD2 . TRP C 3 55  ? 22.912 -23.092 41.557 1.00 61.36  ? 53  TRP C CD2 1 
ATOM 4498 N NE1 . TRP C 3 55  ? 24.818 -22.294 40.690 1.00 66.38  ? 53  TRP C NE1 1 
ATOM 4499 C CE2 . TRP C 3 55  ? 23.611 -21.916 41.218 1.00 58.36  ? 53  TRP C CE2 1 
ATOM 4500 C CE3 . TRP C 3 55  ? 21.637 -22.978 42.122 1.00 59.87  ? 53  TRP C CE3 1 
ATOM 4501 C CZ2 . TRP C 3 55  ? 23.079 -20.645 41.425 1.00 57.68  ? 53  TRP C CZ2 1 
ATOM 4502 C CZ3 . TRP C 3 55  ? 21.111 -21.715 42.326 1.00 57.81  ? 53  TRP C CZ3 1 
ATOM 4503 C CH2 . TRP C 3 55  ? 21.831 -20.566 41.978 1.00 58.06  ? 53  TRP C CH2 1 
ATOM 4504 N N   . THR C 3 56  ? 21.478 -24.813 38.706 1.00 58.87  ? 54  THR C N   1 
ATOM 4505 C CA  . THR C 3 56  ? 20.294 -24.115 38.224 1.00 55.42  ? 54  THR C CA  1 
ATOM 4506 C C   . THR C 3 56  ? 19.367 -25.009 37.412 1.00 59.55  ? 54  THR C C   1 
ATOM 4507 O O   . THR C 3 56  ? 18.194 -24.659 37.233 1.00 60.35  ? 54  THR C O   1 
ATOM 4508 C CB  . THR C 3 56  ? 20.691 -22.900 37.376 1.00 57.80  ? 54  THR C CB  1 
ATOM 4509 O OG1 . THR C 3 56  ? 20.872 -23.300 36.012 1.00 67.00  ? 54  THR C OG1 1 
ATOM 4510 C CG2 . THR C 3 56  ? 21.974 -22.272 37.899 1.00 64.44  ? 54  THR C CG2 1 
ATOM 4511 N N   . GLY C 3 57  ? 19.855 -26.148 36.927 1.00 61.68  ? 55  GLY C N   1 
ATOM 4512 C CA  . GLY C 3 57  ? 19.054 -27.044 36.121 1.00 67.58  ? 55  GLY C CA  1 
ATOM 4513 C C   . GLY C 3 57  ? 19.057 -26.757 34.637 1.00 66.68  ? 55  GLY C C   1 
ATOM 4514 O O   . GLY C 3 57  ? 18.300 -27.399 33.898 1.00 70.17  ? 55  GLY C O   1 
ATOM 4515 N N   . THR C 3 58  ? 19.882 -25.818 34.175 1.00 54.13  ? 56  THR C N   1 
ATOM 4516 C CA  . THR C 3 58  ? 19.934 -25.476 32.759 1.00 71.59  ? 56  THR C CA  1 
ATOM 4517 C C   . THR C 3 58  ? 21.020 -26.231 32.007 1.00 67.85  ? 56  THR C C   1 
ATOM 4518 O O   . THR C 3 58  ? 20.827 -26.571 30.834 1.00 70.72  ? 56  THR C O   1 
ATOM 4519 C CB  . THR C 3 58  ? 20.154 -23.968 32.584 1.00 69.07  ? 56  THR C CB  1 
ATOM 4520 O OG1 . THR C 3 58  ? 21.437 -23.601 33.106 1.00 61.45  ? 56  THR C OG1 1 
ATOM 4521 C CG2 . THR C 3 58  ? 19.068 -23.177 33.302 1.00 60.59  ? 56  THR C CG2 1 
ATOM 4522 N N   . THR C 3 59  ? 22.150 -26.503 32.651 1.00 63.56  ? 57  THR C N   1 
ATOM 4523 C CA  . THR C 3 59  ? 23.294 -27.135 32.011 1.00 67.03  ? 57  THR C CA  1 
ATOM 4524 C C   . THR C 3 59  ? 23.489 -28.533 32.580 1.00 66.80  ? 57  THR C C   1 
ATOM 4525 O O   . THR C 3 59  ? 23.425 -28.728 33.798 1.00 60.07  ? 57  THR C O   1 
ATOM 4526 C CB  . THR C 3 59  ? 24.560 -26.299 32.213 1.00 66.58  ? 57  THR C CB  1 
ATOM 4527 O OG1 . THR C 3 59  ? 24.258 -24.916 31.990 1.00 67.61  ? 57  THR C OG1 1 
ATOM 4528 C CG2 . THR C 3 59  ? 25.649 -26.731 31.248 1.00 62.04  ? 57  THR C CG2 1 
ATOM 4529 N N   . THR C 3 60  ? 23.715 -29.501 31.697 1.00 77.61  ? 58  THR C N   1 
ATOM 4530 C CA  . THR C 3 60  ? 24.011 -30.871 32.087 1.00 61.29  ? 58  THR C CA  1 
ATOM 4531 C C   . THR C 3 60  ? 25.291 -31.316 31.399 1.00 53.64  ? 58  THR C C   1 
ATOM 4532 O O   . THR C 3 60  ? 25.530 -30.979 30.236 1.00 58.46  ? 58  THR C O   1 
ATOM 4533 C CB  . THR C 3 60  ? 22.868 -31.827 31.724 1.00 60.98  ? 58  THR C CB  1 
ATOM 4534 O OG1 . THR C 3 60  ? 22.691 -31.842 30.302 1.00 65.40  ? 58  THR C OG1 1 
ATOM 4535 C CG2 . THR C 3 60  ? 21.572 -31.395 32.395 1.00 62.97  ? 58  THR C CG2 1 
ATOM 4536 N N   . TYR C 3 61  ? 26.111 -32.072 32.122 1.00 57.13  ? 59  TYR C N   1 
ATOM 4537 C CA  . TYR C 3 61  ? 27.383 -32.560 31.612 1.00 63.34  ? 59  TYR C CA  1 
ATOM 4538 C C   . TYR C 3 61  ? 27.372 -34.082 31.587 1.00 66.66  ? 59  TYR C C   1 
ATOM 4539 O O   . TYR C 3 61  ? 26.860 -34.721 32.511 1.00 69.41  ? 59  TYR C O   1 
ATOM 4540 C CB  . TYR C 3 61  ? 28.552 -32.058 32.467 1.00 68.41  ? 59  TYR C CB  1 
ATOM 4541 C CG  . TYR C 3 61  ? 28.725 -30.555 32.461 1.00 75.09  ? 59  TYR C CG  1 
ATOM 4542 C CD1 . TYR C 3 61  ? 27.853 -29.730 33.162 1.00 65.27  ? 59  TYR C CD1 1 
ATOM 4543 C CD2 . TYR C 3 61  ? 29.761 -29.960 31.753 1.00 72.17  ? 59  TYR C CD2 1 
ATOM 4544 C CE1 . TYR C 3 61  ? 28.010 -28.361 33.161 1.00 67.46  ? 59  TYR C CE1 1 
ATOM 4545 C CE2 . TYR C 3 61  ? 29.924 -28.591 31.745 1.00 66.56  ? 59  TYR C CE2 1 
ATOM 4546 C CZ  . TYR C 3 61  ? 29.045 -27.796 32.449 1.00 73.14  ? 59  TYR C CZ  1 
ATOM 4547 O OH  . TYR C 3 61  ? 29.202 -26.430 32.445 1.00 73.61  ? 59  TYR C OH  1 
ATOM 4548 N N   . TYR C 3 62  ? 27.934 -34.657 30.523 1.00 72.01  ? 60  TYR C N   1 
ATOM 4549 C CA  . TYR C 3 62  ? 27.995 -36.103 30.353 1.00 70.22  ? 60  TYR C CA  1 
ATOM 4550 C C   . TYR C 3 62  ? 29.388 -36.503 29.886 1.00 67.44  ? 60  TYR C C   1 
ATOM 4551 O O   . TYR C 3 62  ? 30.087 -35.726 29.232 1.00 71.84  ? 60  TYR C O   1 
ATOM 4552 C CB  . TYR C 3 62  ? 26.957 -36.609 29.337 1.00 68.67  ? 60  TYR C CB  1 
ATOM 4553 C CG  . TYR C 3 62  ? 25.515 -36.379 29.734 1.00 75.41  ? 60  TYR C CG  1 
ATOM 4554 C CD1 . TYR C 3 62  ? 24.889 -35.163 29.483 1.00 68.99  ? 60  TYR C CD1 1 
ATOM 4555 C CD2 . TYR C 3 62  ? 24.775 -37.380 30.351 1.00 66.06  ? 60  TYR C CD2 1 
ATOM 4556 C CE1 . TYR C 3 62  ? 23.570 -34.949 29.842 1.00 66.16  ? 60  TYR C CE1 1 
ATOM 4557 C CE2 . TYR C 3 62  ? 23.456 -37.174 30.716 1.00 67.03  ? 60  TYR C CE2 1 
ATOM 4558 C CZ  . TYR C 3 62  ? 22.859 -35.957 30.457 1.00 67.94  ? 60  TYR C CZ  1 
ATOM 4559 O OH  . TYR C 3 62  ? 21.546 -35.747 30.814 1.00 62.01  ? 60  TYR C OH  1 
ATOM 4560 N N   . ALA C 3 63  ? 29.781 -37.728 30.225 1.00 74.39  ? 61  ALA C N   1 
ATOM 4561 C CA  . ALA C 3 63  ? 31.035 -38.275 29.734 1.00 63.28  ? 61  ALA C CA  1 
ATOM 4562 C C   . ALA C 3 63  ? 30.846 -38.849 28.334 1.00 74.30  ? 61  ALA C C   1 
ATOM 4563 O O   . ALA C 3 63  ? 29.728 -39.128 27.894 1.00 81.15  ? 61  ALA C O   1 
ATOM 4564 C CB  . ALA C 3 63  ? 31.568 -39.353 30.678 1.00 70.07  ? 61  ALA C CB  1 
ATOM 4565 N N   . ASP C 3 64  ? 31.966 -39.023 27.628 1.00 80.75  ? 62  ASP C N   1 
ATOM 4566 C CA  . ASP C 3 64  ? 31.897 -39.500 26.250 1.00 80.95  ? 62  ASP C CA  1 
ATOM 4567 C C   . ASP C 3 64  ? 31.319 -40.907 26.178 1.00 81.37  ? 62  ASP C C   1 
ATOM 4568 O O   . ASP C 3 64  ? 30.569 -41.231 25.250 1.00 84.52  ? 62  ASP C O   1 
ATOM 4569 C CB  . ASP C 3 64  ? 33.282 -39.451 25.607 1.00 83.26  ? 62  ASP C CB  1 
ATOM 4570 C CG  . ASP C 3 64  ? 33.601 -38.092 25.020 1.00 103.44 ? 62  ASP C CG  1 
ATOM 4571 O OD1 . ASP C 3 64  ? 32.706 -37.219 25.020 1.00 103.68 ? 62  ASP C OD1 1 
ATOM 4572 O OD2 . ASP C 3 64  ? 34.744 -37.897 24.557 1.00 118.69 ? 62  ASP C OD2 1 
ATOM 4573 N N   . SER C 3 65  ? 31.644 -41.750 27.151 1.00 75.57  ? 63  SER C N   1 
ATOM 4574 C CA  . SER C 3 65  ? 31.086 -43.097 27.234 1.00 77.09  ? 63  SER C CA  1 
ATOM 4575 C C   . SER C 3 65  ? 29.653 -43.109 27.730 1.00 78.50  ? 63  SER C C   1 
ATOM 4576 O O   . SER C 3 65  ? 29.088 -44.185 27.970 1.00 90.06  ? 63  SER C O   1 
ATOM 4577 C CB  . SER C 3 65  ? 31.958 -43.962 28.146 1.00 83.32  ? 63  SER C CB  1 
ATOM 4578 O OG  . SER C 3 65  ? 32.491 -43.195 29.213 1.00 84.18  ? 63  SER C OG  1 
ATOM 4579 N N   . VAL C 3 66  ? 29.054 -41.928 27.881 1.00 79.68  ? 64  VAL C N   1 
ATOM 4580 C CA  . VAL C 3 66  ? 27.757 -41.772 28.519 1.00 78.96  ? 64  VAL C CA  1 
ATOM 4581 C C   . VAL C 3 66  ? 26.766 -41.039 27.624 1.00 74.37  ? 64  VAL C C   1 
ATOM 4582 O O   . VAL C 3 66  ? 25.581 -41.392 27.584 1.00 63.65  ? 64  VAL C O   1 
ATOM 4583 C CB  . VAL C 3 66  ? 27.905 -41.044 29.874 1.00 78.69  ? 64  VAL C CB  1 
ATOM 4584 C CG1 . VAL C 3 66  ? 26.550 -40.765 30.497 1.00 80.37  ? 64  VAL C CG1 1 
ATOM 4585 C CG2 . VAL C 3 66  ? 28.777 -41.859 30.820 1.00 77.91  ? 64  VAL C CG2 1 
ATOM 4586 N N   . LYS C 3 67  ? 27.231 -40.031 26.888 1.00 78.15  ? 65  LYS C N   1 
ATOM 4587 C CA  . LYS C 3 67  ? 26.338 -39.163 26.131 1.00 75.77  ? 65  LYS C CA  1 
ATOM 4588 C C   . LYS C 3 67  ? 25.551 -39.949 25.089 1.00 72.97  ? 65  LYS C C   1 
ATOM 4589 O O   . LYS C 3 67  ? 26.091 -40.817 24.398 1.00 77.48  ? 65  LYS C O   1 
ATOM 4590 C CB  . LYS C 3 67  ? 27.138 -38.050 25.452 1.00 71.61  ? 65  LYS C CB  1 
ATOM 4591 C CG  . LYS C 3 67  ? 26.533 -36.665 25.609 1.00 74.52  ? 65  LYS C CG  1 
ATOM 4592 C CD  . LYS C 3 67  ? 27.255 -35.642 24.742 1.00 81.46  ? 65  LYS C CD  1 
ATOM 4593 C CE  . LYS C 3 67  ? 28.733 -35.563 25.088 1.00 85.51  ? 65  LYS C CE  1 
ATOM 4594 N NZ  . LYS C 3 67  ? 29.364 -34.336 24.527 1.00 97.07  ? 65  LYS C NZ  1 
ATOM 4595 N N   . GLY C 3 68  ? 24.259 -39.632 24.980 1.00 65.59  ? 66  GLY C N   1 
ATOM 4596 C CA  . GLY C 3 68  ? 23.362 -40.260 24.043 1.00 68.47  ? 66  GLY C CA  1 
ATOM 4597 C C   . GLY C 3 68  ? 22.495 -41.351 24.643 1.00 66.71  ? 66  GLY C C   1 
ATOM 4598 O O   . GLY C 3 68  ? 21.390 -41.594 24.146 1.00 67.41  ? 66  GLY C O   1 
ATOM 4599 N N   . ARG C 3 69  ? 22.966 -42.010 25.698 1.00 65.64  ? 67  ARG C N   1 
ATOM 4600 C CA  . ARG C 3 69  ? 22.236 -43.112 26.311 1.00 65.30  ? 67  ARG C CA  1 
ATOM 4601 C C   . ARG C 3 69  ? 21.652 -42.771 27.670 1.00 67.03  ? 67  ARG C C   1 
ATOM 4602 O O   . ARG C 3 69  ? 20.523 -43.166 27.966 1.00 72.86  ? 67  ARG C O   1 
ATOM 4603 C CB  . ARG C 3 69  ? 23.147 -44.336 26.449 1.00 77.60  ? 67  ARG C CB  1 
ATOM 4604 C CG  . ARG C 3 69  ? 24.118 -44.515 25.297 1.00 74.49  ? 67  ARG C CG  1 
ATOM 4605 C CD  . ARG C 3 69  ? 24.788 -45.875 25.351 1.00 71.72  ? 67  ARG C CD  1 
ATOM 4606 N NE  . ARG C 3 69  ? 25.937 -45.883 26.248 1.00 71.11  ? 67  ARG C NE  1 
ATOM 4607 C CZ  . ARG C 3 69  ? 25.950 -46.455 27.444 1.00 69.84  ? 67  ARG C CZ  1 
ATOM 4608 N NH1 . ARG C 3 69  ? 24.886 -47.076 27.924 1.00 68.97  ? 67  ARG C NH1 1 
ATOM 4609 N NH2 . ARG C 3 69  ? 27.060 -46.403 28.175 1.00 69.73  ? 67  ARG C NH2 1 
ATOM 4610 N N   . PHE C 3 70  ? 22.383 -42.042 28.505 1.00 70.12  ? 68  PHE C N   1 
ATOM 4611 C CA  . PHE C 3 70  ? 21.931 -41.741 29.853 1.00 64.98  ? 68  PHE C CA  1 
ATOM 4612 C C   . PHE C 3 70  ? 21.444 -40.300 29.941 1.00 62.75  ? 68  PHE C C   1 
ATOM 4613 O O   . PHE C 3 70  ? 21.958 -39.408 29.263 1.00 59.42  ? 68  PHE C O   1 
ATOM 4614 C CB  . PHE C 3 70  ? 23.053 -41.988 30.866 1.00 69.56  ? 68  PHE C CB  1 
ATOM 4615 C CG  . PHE C 3 70  ? 23.563 -43.402 30.862 1.00 79.15  ? 68  PHE C CG  1 
ATOM 4616 C CD1 . PHE C 3 70  ? 22.697 -44.458 30.647 1.00 82.16  ? 68  PHE C CD1 1 
ATOM 4617 C CD2 . PHE C 3 70  ? 24.903 -43.676 31.086 1.00 76.16  ? 68  PHE C CD2 1 
ATOM 4618 C CE1 . PHE C 3 70  ? 23.150 -45.757 30.642 1.00 85.41  ? 68  PHE C CE1 1 
ATOM 4619 C CE2 . PHE C 3 70  ? 25.365 -44.976 31.087 1.00 84.46  ? 68  PHE C CE2 1 
ATOM 4620 C CZ  . PHE C 3 70  ? 24.484 -46.019 30.866 1.00 88.29  ? 68  PHE C CZ  1 
ATOM 4621 N N   . THR C 3 71  ? 20.437 -40.086 30.785 1.00 74.94  ? 69  THR C N   1 
ATOM 4622 C CA  . THR C 3 71  ? 19.824 -38.777 30.977 1.00 59.97  ? 69  THR C CA  1 
ATOM 4623 C C   . THR C 3 71  ? 19.756 -38.487 32.468 1.00 61.00  ? 69  THR C C   1 
ATOM 4624 O O   . THR C 3 71  ? 19.171 -39.267 33.227 1.00 55.13  ? 69  THR C O   1 
ATOM 4625 C CB  . THR C 3 71  ? 18.422 -38.728 30.361 1.00 56.15  ? 69  THR C CB  1 
ATOM 4626 O OG1 . THR C 3 71  ? 18.528 -38.498 28.953 1.00 63.13  ? 69  THR C OG1 1 
ATOM 4627 C CG2 . THR C 3 71  ? 17.597 -37.615 30.988 1.00 55.24  ? 69  THR C CG2 1 
ATOM 4628 N N   . ILE C 3 72  ? 20.360 -37.379 32.887 1.00 64.61  ? 70  ILE C N   1 
ATOM 4629 C CA  . ILE C 3 72  ? 20.281 -36.918 34.268 1.00 60.72  ? 70  ILE C CA  1 
ATOM 4630 C C   . ILE C 3 72  ? 19.306 -35.752 34.330 1.00 58.55  ? 70  ILE C C   1 
ATOM 4631 O O   . ILE C 3 72  ? 19.350 -34.844 33.490 1.00 52.10  ? 70  ILE C O   1 
ATOM 4632 C CB  . ILE C 3 72  ? 21.666 -36.524 34.813 1.00 55.96  ? 70  ILE C CB  1 
ATOM 4633 C CG1 . ILE C 3 72  ? 21.541 -35.980 36.238 1.00 55.91  ? 70  ILE C CG1 1 
ATOM 4634 C CG2 . ILE C 3 72  ? 22.351 -35.513 33.903 1.00 56.17  ? 70  ILE C CG2 1 
ATOM 4635 C CD1 . ILE C 3 72  ? 22.823 -35.399 36.783 1.00 57.57  ? 70  ILE C CD1 1 
ATOM 4636 N N   . SER C 3 73  ? 18.408 -35.789 35.311 1.00 52.12  ? 71  SER C N   1 
ATOM 4637 C CA  . SER C 3 73  ? 17.425 -34.737 35.509 1.00 52.23  ? 71  SER C CA  1 
ATOM 4638 C C   . SER C 3 73  ? 17.235 -34.536 37.006 1.00 57.85  ? 71  SER C C   1 
ATOM 4639 O O   . SER C 3 73  ? 17.920 -35.153 37.828 1.00 63.47  ? 71  SER C O   1 
ATOM 4640 C CB  . SER C 3 73  ? 16.102 -35.074 34.808 1.00 53.18  ? 71  SER C CB  1 
ATOM 4641 O OG  . SER C 3 73  ? 15.457 -36.174 35.423 1.00 53.80  ? 71  SER C OG  1 
ATOM 4642 N N   . ARG C 3 74  ? 16.299 -33.662 37.362 1.00 63.61  ? 72  ARG C N   1 
ATOM 4643 C CA  . ARG C 3 74  ? 16.055 -33.342 38.760 1.00 64.14  ? 72  ARG C CA  1 
ATOM 4644 C C   . ARG C 3 74  ? 14.591 -32.975 38.942 1.00 67.31  ? 72  ARG C C   1 
ATOM 4645 O O   . ARG C 3 74  ? 14.015 -32.262 38.115 1.00 77.58  ? 72  ARG C O   1 
ATOM 4646 C CB  . ARG C 3 74  ? 16.960 -32.196 39.233 1.00 65.31  ? 72  ARG C CB  1 
ATOM 4647 C CG  . ARG C 3 74  ? 16.418 -31.419 40.423 1.00 68.49  ? 72  ARG C CG  1 
ATOM 4648 C CD  . ARG C 3 74  ? 17.478 -30.512 41.022 1.00 72.50  ? 72  ARG C CD  1 
ATOM 4649 N NE  . ARG C 3 74  ? 16.965 -29.169 41.264 1.00 86.42  ? 72  ARG C NE  1 
ATOM 4650 C CZ  . ARG C 3 74  ? 17.703 -28.069 41.228 1.00 86.54  ? 72  ARG C CZ  1 
ATOM 4651 N NH1 . ARG C 3 74  ? 18.999 -28.115 40.966 1.00 81.81  ? 72  ARG C NH1 1 
ATOM 4652 N NH2 . ARG C 3 74  ? 17.127 -26.893 41.458 1.00 92.43  ? 72  ARG C NH2 1 
ATOM 4653 N N   . ASP C 3 75  ? 13.996 -33.475 40.023 1.00 72.02  ? 73  ASP C N   1 
ATOM 4654 C CA  . ASP C 3 75  ? 12.625 -33.153 40.405 1.00 76.08  ? 73  ASP C CA  1 
ATOM 4655 C C   . ASP C 3 75  ? 12.675 -32.415 41.737 1.00 82.52  ? 73  ASP C C   1 
ATOM 4656 O O   . ASP C 3 75  ? 12.980 -33.016 42.774 1.00 88.54  ? 73  ASP C O   1 
ATOM 4657 C CB  . ASP C 3 75  ? 11.769 -34.416 40.500 1.00 82.55  ? 73  ASP C CB  1 
ATOM 4658 C CG  . ASP C 3 75  ? 10.292 -34.109 40.638 1.00 81.41  ? 73  ASP C CG  1 
ATOM 4659 O OD1 . ASP C 3 75  ? 9.868  -33.715 41.742 1.00 73.08  ? 73  ASP C OD1 1 
ATOM 4660 O OD2 . ASP C 3 75  ? 9.554  -34.263 39.641 1.00 91.89  ? 73  ASP C OD2 1 
ATOM 4661 N N   . ASP C 3 76  ? 12.373 -31.116 41.709 1.00 79.09  ? 74  ASP C N   1 
ATOM 4662 C CA  . ASP C 3 76  ? 12.542 -30.283 42.895 1.00 88.39  ? 74  ASP C CA  1 
ATOM 4663 C C   . ASP C 3 76  ? 11.422 -30.473 43.910 1.00 84.30  ? 74  ASP C C   1 
ATOM 4664 O O   . ASP C 3 76  ? 11.661 -30.338 45.116 1.00 87.80  ? 74  ASP C O   1 
ATOM 4665 C CB  . ASP C 3 76  ? 12.636 -28.812 42.491 1.00 84.81  ? 74  ASP C CB  1 
ATOM 4666 C CG  . ASP C 3 76  ? 13.826 -28.530 41.598 1.00 83.66  ? 74  ASP C CG  1 
ATOM 4667 O OD1 . ASP C 3 76  ? 13.853 -29.043 40.459 1.00 82.60  ? 74  ASP C OD1 1 
ATOM 4668 O OD2 . ASP C 3 76  ? 14.738 -27.798 42.037 1.00 90.31  ? 74  ASP C OD2 1 
ATOM 4669 N N   . VAL C 3 77  ? 10.203 -30.776 43.456 1.00 80.12  ? 75  VAL C N   1 
ATOM 4670 C CA  . VAL C 3 77  ? 9.099  -30.954 44.391 1.00 81.81  ? 75  VAL C CA  1 
ATOM 4671 C C   . VAL C 3 77  ? 9.211  -32.272 45.147 1.00 91.53  ? 75  VAL C C   1 
ATOM 4672 O O   . VAL C 3 77  ? 8.607  -32.422 46.216 1.00 98.82  ? 75  VAL C O   1 
ATOM 4673 C CB  . VAL C 3 77  ? 7.746  -30.849 43.660 1.00 74.78  ? 75  VAL C CB  1 
ATOM 4674 C CG1 . VAL C 3 77  ? 7.398  -32.158 42.971 1.00 92.07  ? 75  VAL C CG1 1 
ATOM 4675 C CG2 . VAL C 3 77  ? 6.646  -30.442 44.629 1.00 90.04  ? 75  VAL C CG2 1 
ATOM 4676 N N   . LYS C 3 78  ? 9.977  -33.232 44.629 1.00 89.88  ? 76  LYS C N   1 
ATOM 4677 C CA  . LYS C 3 78  ? 10.208 -34.500 45.307 1.00 89.06  ? 76  LYS C CA  1 
ATOM 4678 C C   . LYS C 3 78  ? 11.615 -34.616 45.876 1.00 88.11  ? 76  LYS C C   1 
ATOM 4679 O O   . LYS C 3 78  ? 11.921 -35.621 46.528 1.00 85.71  ? 76  LYS C O   1 
ATOM 4680 C CB  . LYS C 3 78  ? 9.939  -35.674 44.355 1.00 92.77  ? 76  LYS C CB  1 
ATOM 4681 C CG  . LYS C 3 78  ? 8.516  -35.736 43.813 1.00 94.23  ? 76  LYS C CG  1 
ATOM 4682 C CD  . LYS C 3 78  ? 7.485  -35.460 44.896 1.00 95.38  ? 76  LYS C CD  1 
ATOM 4683 C CE  . LYS C 3 78  ? 6.071  -35.519 44.339 1.00 99.61  ? 76  LYS C CE  1 
ATOM 4684 N NZ  . LYS C 3 78  ? 5.469  -36.873 44.487 1.00 108.65 ? 76  LYS C NZ  1 
ATOM 4685 N N   . ASN C 3 79  ? 12.474 -33.620 45.644 1.00 92.97  ? 77  ASN C N   1 
ATOM 4686 C CA  . ASN C 3 79  ? 13.835 -33.597 46.185 1.00 90.82  ? 77  ASN C CA  1 
ATOM 4687 C C   . ASN C 3 79  ? 14.629 -34.828 45.753 1.00 92.76  ? 77  ASN C C   1 
ATOM 4688 O O   . ASN C 3 79  ? 15.346 -35.437 46.549 1.00 91.94  ? 77  ASN C O   1 
ATOM 4689 C CB  . ASN C 3 79  ? 13.820 -33.471 47.710 1.00 93.85  ? 77  ASN C CB  1 
ATOM 4690 C CG  . ASN C 3 79  ? 13.807 -32.032 48.176 1.00 101.73 ? 77  ASN C CG  1 
ATOM 4691 O OD1 . ASN C 3 79  ? 14.796 -31.531 48.708 1.00 107.64 ? 77  ASN C OD1 1 
ATOM 4692 N ND2 . ASN C 3 79  ? 12.682 -31.356 47.976 1.00 106.98 ? 77  ASN C ND2 1 
ATOM 4693 N N   . MET C 3 80  ? 14.504 -35.198 44.482 1.00 83.35  ? 78  MET C N   1 
ATOM 4694 C CA  . MET C 3 80  ? 15.138 -36.399 43.962 1.00 68.40  ? 78  MET C CA  1 
ATOM 4695 C C   . MET C 3 80  ? 15.852 -36.094 42.654 1.00 69.83  ? 78  MET C C   1 
ATOM 4696 O O   . MET C 3 80  ? 15.422 -35.239 41.875 1.00 71.73  ? 78  MET C O   1 
ATOM 4697 C CB  . MET C 3 80  ? 14.113 -37.521 43.752 1.00 68.44  ? 78  MET C CB  1 
ATOM 4698 C CG  . MET C 3 80  ? 13.929 -38.417 44.965 1.00 71.91  ? 78  MET C CG  1 
ATOM 4699 S SD  . MET C 3 80  ? 12.989 -39.911 44.608 1.00 79.51  ? 78  MET C SD  1 
ATOM 4700 C CE  . MET C 3 80  ? 11.315 -39.279 44.684 1.00 69.29  ? 78  MET C CE  1 
ATOM 4701 N N   . VAL C 3 81  ? 16.952 -36.807 42.425 1.00 72.94  ? 79  VAL C N   1 
ATOM 4702 C CA  . VAL C 3 81  ? 17.745 -36.698 41.206 1.00 68.10  ? 79  VAL C CA  1 
ATOM 4703 C C   . VAL C 3 81  ? 17.719 -38.050 40.508 1.00 68.03  ? 79  VAL C C   1 
ATOM 4704 O O   . VAL C 3 81  ? 17.900 -39.089 41.154 1.00 70.57  ? 79  VAL C O   1 
ATOM 4705 C CB  . VAL C 3 81  ? 19.190 -36.260 41.507 1.00 64.49  ? 79  VAL C CB  1 
ATOM 4706 C CG1 . VAL C 3 81  ? 20.013 -36.204 40.228 1.00 60.76  ? 79  VAL C CG1 1 
ATOM 4707 C CG2 . VAL C 3 81  ? 19.194 -34.916 42.217 1.00 53.85  ? 79  VAL C CG2 1 
ATOM 4708 N N   . TYR C 3 82  ? 17.496 -38.038 39.197 1.00 68.06  ? 80  TYR C N   1 
ATOM 4709 C CA  . TYR C 3 82  ? 17.325 -39.258 38.425 1.00 60.16  ? 80  TYR C CA  1 
ATOM 4710 C C   . TYR C 3 82  ? 18.471 -39.452 37.441 1.00 59.59  ? 80  TYR C C   1 
ATOM 4711 O O   . TYR C 3 82  ? 19.100 -38.491 36.988 1.00 62.28  ? 80  TYR C O   1 
ATOM 4712 C CB  . TYR C 3 82  ? 15.997 -39.242 37.660 1.00 55.31  ? 80  TYR C CB  1 
ATOM 4713 C CG  . TYR C 3 82  ? 14.786 -39.003 38.531 1.00 62.28  ? 80  TYR C CG  1 
ATOM 4714 C CD1 . TYR C 3 82  ? 14.449 -39.888 39.546 1.00 64.85  ? 80  TYR C CD1 1 
ATOM 4715 C CD2 . TYR C 3 82  ? 13.978 -37.891 38.336 1.00 60.96  ? 80  TYR C CD2 1 
ATOM 4716 C CE1 . TYR C 3 82  ? 13.340 -39.672 40.344 1.00 62.57  ? 80  TYR C CE1 1 
ATOM 4717 C CE2 . TYR C 3 82  ? 12.869 -37.666 39.128 1.00 64.26  ? 80  TYR C CE2 1 
ATOM 4718 C CZ  . TYR C 3 82  ? 12.553 -38.558 40.129 1.00 66.18  ? 80  TYR C CZ  1 
ATOM 4719 O OH  . TYR C 3 82  ? 11.448 -38.333 40.917 1.00 76.04  ? 80  TYR C OH  1 
ATOM 4720 N N   . LEU C 3 83  ? 18.733 -40.717 37.119 1.00 67.23  ? 81  LEU C N   1 
ATOM 4721 C CA  . LEU C 3 83  ? 19.638 -41.104 36.038 1.00 66.20  ? 81  LEU C CA  1 
ATOM 4722 C C   . LEU C 3 83  ? 18.916 -42.179 35.232 1.00 61.38  ? 81  LEU C C   1 
ATOM 4723 O O   . LEU C 3 83  ? 18.923 -43.355 35.608 1.00 57.17  ? 81  LEU C O   1 
ATOM 4724 C CB  . LEU C 3 83  ? 20.975 -41.613 36.568 1.00 62.16  ? 81  LEU C CB  1 
ATOM 4725 C CG  . LEU C 3 83  ? 22.017 -42.054 35.530 1.00 57.59  ? 81  LEU C CG  1 
ATOM 4726 C CD1 . LEU C 3 83  ? 21.943 -41.219 34.254 1.00 59.95  ? 81  LEU C CD1 1 
ATOM 4727 C CD2 . LEU C 3 83  ? 23.418 -42.015 36.114 1.00 55.56  ? 81  LEU C CD2 1 
ATOM 4728 N N   . GLN C 3 84  ? 18.291 -41.774 34.131 1.00 64.74  ? 82  GLN C N   1 
ATOM 4729 C CA  . GLN C 3 84  ? 17.580 -42.708 33.269 1.00 59.35  ? 82  GLN C CA  1 
ATOM 4730 C C   . GLN C 3 84  ? 18.569 -43.369 32.317 1.00 60.64  ? 82  GLN C C   1 
ATOM 4731 O O   . GLN C 3 84  ? 19.178 -42.695 31.480 1.00 64.12  ? 82  GLN C O   1 
ATOM 4732 C CB  . GLN C 3 84  ? 16.478 -41.987 32.496 1.00 60.35  ? 82  GLN C CB  1 
ATOM 4733 C CG  . GLN C 3 84  ? 15.453 -42.917 31.868 1.00 74.94  ? 82  GLN C CG  1 
ATOM 4734 C CD  . GLN C 3 84  ? 15.220 -42.625 30.397 1.00 84.21  ? 82  GLN C CD  1 
ATOM 4735 O OE1 . GLN C 3 84  ? 16.022 -41.948 29.752 1.00 79.32  ? 82  GLN C OE1 1 
ATOM 4736 N NE2 . GLN C 3 84  ? 14.124 -43.145 29.856 1.00 79.83  ? 82  GLN C NE2 1 
ATOM 4737 N N   . MET C 3 85  ? 18.731 -44.681 32.447 1.00 69.08  ? 83  MET C N   1 
ATOM 4738 C CA  . MET C 3 85  ? 19.627 -45.453 31.598 1.00 74.61  ? 83  MET C CA  1 
ATOM 4739 C C   . MET C 3 85  ? 18.804 -46.132 30.509 1.00 69.33  ? 83  MET C C   1 
ATOM 4740 O O   . MET C 3 85  ? 17.681 -46.573 30.762 1.00 70.85  ? 83  MET C O   1 
ATOM 4741 C CB  . MET C 3 85  ? 20.381 -46.494 32.429 1.00 68.09  ? 83  MET C CB  1 
ATOM 4742 C CG  . MET C 3 85  ? 20.706 -46.044 33.857 1.00 66.97  ? 83  MET C CG  1 
ATOM 4743 S SD  . MET C 3 85  ? 22.259 -46.676 34.538 1.00 67.82  ? 83  MET C SD  1 
ATOM 4744 C CE  . MET C 3 85  ? 23.410 -45.365 34.113 1.00 78.34  ? 83  MET C CE  1 
ATOM 4745 N N   . ASN C 3 86  ? 19.364 -46.219 29.302 1.00 66.85  ? 84  ASN C N   1 
ATOM 4746 C CA  . ASN C 3 86  ? 18.603 -46.659 28.136 1.00 67.89  ? 84  ASN C CA  1 
ATOM 4747 C C   . ASN C 3 86  ? 19.193 -47.881 27.448 1.00 78.56  ? 84  ASN C C   1 
ATOM 4748 O O   . ASN C 3 86  ? 18.466 -48.849 27.190 1.00 88.05  ? 84  ASN C O   1 
ATOM 4749 C CB  . ASN C 3 86  ? 18.479 -45.508 27.124 1.00 66.79  ? 84  ASN C CB  1 
ATOM 4750 C CG  . ASN C 3 86  ? 17.121 -44.835 27.171 1.00 73.09  ? 84  ASN C CG  1 
ATOM 4751 O OD1 . ASN C 3 86  ? 16.183 -45.346 27.785 1.00 68.45  ? 84  ASN C OD1 1 
ATOM 4752 N ND2 . ASN C 3 86  ? 17.009 -43.681 26.522 1.00 69.14  ? 84  ASN C ND2 1 
ATOM 4753 N N   . SER C 3 87  ? 20.487 -47.865 27.116 1.00 76.86  ? 85  SER C N   1 
ATOM 4754 C CA  . SER C 3 87  ? 21.147 -48.997 26.454 1.00 72.77  ? 85  SER C CA  1 
ATOM 4755 C C   . SER C 3 87  ? 22.352 -49.404 27.297 1.00 75.88  ? 85  SER C C   1 
ATOM 4756 O O   . SER C 3 87  ? 23.485 -49.004 27.022 1.00 75.74  ? 85  SER C O   1 
ATOM 4757 C CB  . SER C 3 87  ? 21.546 -48.648 25.021 1.00 73.68  ? 85  SER C CB  1 
ATOM 4758 O OG  . SER C 3 87  ? 20.492 -47.983 24.348 1.00 87.57  ? 85  SER C OG  1 
ATOM 4759 N N   . LEU C 3 88  ? 22.103 -50.213 28.322 1.00 71.67  ? 86  LEU C N   1 
ATOM 4760 C CA  . LEU C 3 88  ? 23.173 -50.620 29.219 1.00 71.46  ? 86  LEU C CA  1 
ATOM 4761 C C   . LEU C 3 88  ? 24.061 -51.665 28.556 1.00 73.95  ? 86  LEU C C   1 
ATOM 4762 O O   . LEU C 3 88  ? 23.582 -52.562 27.858 1.00 76.03  ? 86  LEU C O   1 
ATOM 4763 C CB  . LEU C 3 88  ? 22.599 -51.170 30.523 1.00 78.89  ? 86  LEU C CB  1 
ATOM 4764 C CG  . LEU C 3 88  ? 22.169 -50.135 31.563 1.00 69.07  ? 86  LEU C CG  1 
ATOM 4765 C CD1 . LEU C 3 88  ? 20.698 -49.810 31.396 1.00 70.74  ? 86  LEU C CD1 1 
ATOM 4766 C CD2 . LEU C 3 88  ? 22.447 -50.641 32.965 1.00 94.75  ? 86  LEU C CD2 1 
ATOM 4767 N N   . LYS C 3 89  ? 25.367 -51.537 28.778 1.00 74.96  ? 87  LYS C N   1 
ATOM 4768 C CA  . LYS C 3 89  ? 26.380 -52.423 28.233 1.00 77.92  ? 87  LYS C CA  1 
ATOM 4769 C C   . LYS C 3 89  ? 27.312 -52.885 29.344 1.00 83.77  ? 87  LYS C C   1 
ATOM 4770 O O   . LYS C 3 89  ? 27.550 -52.146 30.304 1.00 88.56  ? 87  LYS C O   1 
ATOM 4771 C CB  . LYS C 3 89  ? 27.182 -51.720 27.126 1.00 79.48  ? 87  LYS C CB  1 
ATOM 4772 C CG  . LYS C 3 89  ? 26.494 -50.480 26.573 1.00 79.54  ? 87  LYS C CG  1 
ATOM 4773 C CD  . LYS C 3 89  ? 27.126 -49.991 25.280 1.00 82.65  ? 87  LYS C CD  1 
ATOM 4774 C CE  . LYS C 3 89  ? 28.527 -49.455 25.504 1.00 83.35  ? 87  LYS C CE  1 
ATOM 4775 N NZ  . LYS C 3 89  ? 29.116 -48.927 24.242 1.00 83.13  ? 87  LYS C NZ  1 
ATOM 4776 N N   . PRO C 3 90  ? 27.851 -54.123 29.241 1.00 86.80  ? 88  PRO C N   1 
ATOM 4777 C CA  . PRO C 3 90  ? 28.664 -54.696 30.329 1.00 81.82  ? 88  PRO C CA  1 
ATOM 4778 C C   . PRO C 3 90  ? 29.721 -53.771 30.922 1.00 80.85  ? 88  PRO C C   1 
ATOM 4779 O O   . PRO C 3 90  ? 30.134 -53.957 32.071 1.00 87.71  ? 88  PRO C O   1 
ATOM 4780 C CB  . PRO C 3 90  ? 29.321 -55.908 29.658 1.00 86.02  ? 88  PRO C CB  1 
ATOM 4781 C CG  . PRO C 3 90  ? 28.343 -56.332 28.602 1.00 87.01  ? 88  PRO C CG  1 
ATOM 4782 C CD  . PRO C 3 90  ? 27.493 -55.134 28.230 1.00 84.12  ? 88  PRO C CD  1 
ATOM 4783 N N   . GLU C 3 91  ? 30.166 -52.778 30.154 1.00 80.71  ? 89  GLU C N   1 
ATOM 4784 C CA  . GLU C 3 91  ? 31.132 -51.814 30.661 1.00 79.83  ? 89  GLU C CA  1 
ATOM 4785 C C   . GLU C 3 91  ? 30.506 -50.843 31.652 1.00 79.80  ? 89  GLU C C   1 
ATOM 4786 O O   . GLU C 3 91  ? 31.233 -50.196 32.416 1.00 75.23  ? 89  GLU C O   1 
ATOM 4787 C CB  . GLU C 3 91  ? 31.772 -51.030 29.506 1.00 81.11  ? 89  GLU C CB  1 
ATOM 4788 C CG  . GLU C 3 91  ? 32.307 -51.840 28.298 1.00 99.11  ? 89  GLU C CG  1 
ATOM 4789 C CD  . GLU C 3 91  ? 31.274 -52.705 27.571 1.00 101.63 ? 89  GLU C CD  1 
ATOM 4790 O OE1 . GLU C 3 91  ? 31.695 -53.578 26.784 1.00 92.06  ? 89  GLU C OE1 1 
ATOM 4791 O OE2 . GLU C 3 91  ? 30.055 -52.509 27.770 1.00 97.91  ? 89  GLU C OE2 1 
ATOM 4792 N N   . ASP C 3 92  ? 29.180 -50.714 31.643 1.00 79.43  ? 90  ASP C N   1 
ATOM 4793 C CA  . ASP C 3 92  ? 28.481 -49.887 32.616 1.00 77.50  ? 90  ASP C CA  1 
ATOM 4794 C C   . ASP C 3 92  ? 28.363 -50.555 33.980 1.00 81.94  ? 90  ASP C C   1 
ATOM 4795 O O   . ASP C 3 92  ? 27.958 -49.893 34.943 1.00 76.11  ? 90  ASP C O   1 
ATOM 4796 C CB  . ASP C 3 92  ? 27.085 -49.535 32.096 1.00 79.18  ? 90  ASP C CB  1 
ATOM 4797 C CG  . ASP C 3 92  ? 27.122 -48.793 30.773 1.00 82.72  ? 90  ASP C CG  1 
ATOM 4798 O OD1 . ASP C 3 92  ? 27.931 -47.851 30.635 1.00 84.13  ? 90  ASP C OD1 1 
ATOM 4799 O OD2 . ASP C 3 92  ? 26.340 -49.154 29.868 1.00 74.97  ? 90  ASP C OD2 1 
ATOM 4800 N N   . THR C 3 93  ? 28.698 -51.841 34.085 1.00 86.87  ? 91  THR C N   1 
ATOM 4801 C CA  . THR C 3 93  ? 28.648 -52.540 35.363 1.00 79.35  ? 91  THR C CA  1 
ATOM 4802 C C   . THR C 3 93  ? 29.616 -51.908 36.352 1.00 74.29  ? 91  THR C C   1 
ATOM 4803 O O   . THR C 3 93  ? 30.836 -51.975 36.171 1.00 75.01  ? 91  THR C O   1 
ATOM 4804 C CB  . THR C 3 93  ? 28.970 -54.026 35.188 1.00 82.15  ? 91  THR C CB  1 
ATOM 4805 O OG1 . THR C 3 93  ? 27.962 -54.646 34.381 1.00 78.96  ? 91  THR C OG1 1 
ATOM 4806 C CG2 . THR C 3 93  ? 29.021 -54.721 36.540 1.00 77.00  ? 91  THR C CG2 1 
ATOM 4807 N N   . ALA C 3 94  ? 29.076 -51.292 37.393 1.00 79.24  ? 92  ALA C N   1 
ATOM 4808 C CA  . ALA C 3 94  ? 29.859 -50.640 38.437 1.00 74.05  ? 92  ALA C CA  1 
ATOM 4809 C C   . ALA C 3 94  ? 28.911 -50.329 39.589 1.00 69.05  ? 92  ALA C C   1 
ATOM 4810 O O   . ALA C 3 94  ? 27.762 -50.786 39.608 1.00 68.57  ? 92  ALA C O   1 
ATOM 4811 C CB  . ALA C 3 94  ? 30.556 -49.384 37.909 1.00 82.24  ? 92  ALA C CB  1 
ATOM 4812 N N   . VAL C 3 95  ? 29.394 -49.551 40.552 1.00 78.30  ? 93  VAL C N   1 
ATOM 4813 C CA  . VAL C 3 95  ? 28.588 -49.070 41.668 1.00 72.72  ? 93  VAL C CA  1 
ATOM 4814 C C   . VAL C 3 95  ? 28.338 -47.586 41.442 1.00 65.08  ? 93  VAL C C   1 
ATOM 4815 O O   . VAL C 3 95  ? 29.287 -46.801 41.333 1.00 64.93  ? 93  VAL C O   1 
ATOM 4816 C CB  . VAL C 3 95  ? 29.276 -49.316 43.018 1.00 69.12  ? 93  VAL C CB  1 
ATOM 4817 C CG1 . VAL C 3 95  ? 28.249 -49.320 44.138 1.00 68.91  ? 93  VAL C CG1 1 
ATOM 4818 C CG2 . VAL C 3 95  ? 30.052 -50.624 42.987 1.00 71.87  ? 93  VAL C CG2 1 
ATOM 4819 N N   . TYR C 3 96  ? 27.067 -47.202 41.380 1.00 63.51  ? 94  TYR C N   1 
ATOM 4820 C CA  . TYR C 3 96  ? 26.670 -45.850 41.009 1.00 63.52  ? 94  TYR C CA  1 
ATOM 4821 C C   . TYR C 3 96  ? 26.438 -45.006 42.257 1.00 62.80  ? 94  TYR C C   1 
ATOM 4822 O O   . TYR C 3 96  ? 25.602 -45.352 43.099 1.00 61.43  ? 94  TYR C O   1 
ATOM 4823 C CB  . TYR C 3 96  ? 25.413 -45.884 40.142 1.00 61.98  ? 94  TYR C CB  1 
ATOM 4824 C CG  . TYR C 3 96  ? 25.633 -46.525 38.793 1.00 83.30  ? 94  TYR C CG  1 
ATOM 4825 C CD1 . TYR C 3 96  ? 26.584 -46.026 37.915 1.00 88.62  ? 94  TYR C CD1 1 
ATOM 4826 C CD2 . TYR C 3 96  ? 24.902 -47.636 38.401 1.00 79.40  ? 94  TYR C CD2 1 
ATOM 4827 C CE1 . TYR C 3 96  ? 26.795 -46.609 36.681 1.00 85.82  ? 94  TYR C CE1 1 
ATOM 4828 C CE2 . TYR C 3 96  ? 25.105 -48.221 37.167 1.00 81.62  ? 94  TYR C CE2 1 
ATOM 4829 C CZ  . TYR C 3 96  ? 26.053 -47.707 36.313 1.00 84.29  ? 94  TYR C CZ  1 
ATOM 4830 O OH  . TYR C 3 96  ? 26.260 -48.289 35.085 1.00 90.78  ? 94  TYR C OH  1 
ATOM 4831 N N   . TYR C 3 97  ? 27.166 -43.898 42.363 1.00 70.20  ? 95  TYR C N   1 
ATOM 4832 C CA  . TYR C 3 97  ? 27.030 -42.942 43.452 1.00 71.67  ? 95  TYR C CA  1 
ATOM 4833 C C   . TYR C 3 97  ? 26.435 -41.639 42.934 1.00 66.85  ? 95  TYR C C   1 
ATOM 4834 O O   . TYR C 3 97  ? 26.686 -41.234 41.797 1.00 69.49  ? 95  TYR C O   1 
ATOM 4835 C CB  . TYR C 3 97  ? 28.389 -42.648 44.097 1.00 74.67  ? 95  TYR C CB  1 
ATOM 4836 C CG  . TYR C 3 97  ? 29.133 -43.866 44.586 1.00 77.74  ? 95  TYR C CG  1 
ATOM 4837 C CD1 . TYR C 3 97  ? 28.572 -44.718 45.525 1.00 79.81  ? 95  TYR C CD1 1 
ATOM 4838 C CD2 . TYR C 3 97  ? 30.397 -44.170 44.098 1.00 82.95  ? 95  TYR C CD2 1 
ATOM 4839 C CE1 . TYR C 3 97  ? 29.250 -45.836 45.972 1.00 73.26  ? 95  TYR C CE1 1 
ATOM 4840 C CE2 . TYR C 3 97  ? 31.082 -45.287 44.535 1.00 87.85  ? 95  TYR C CE2 1 
ATOM 4841 C CZ  . TYR C 3 97  ? 30.505 -46.115 45.474 1.00 83.17  ? 95  TYR C CZ  1 
ATOM 4842 O OH  . TYR C 3 97  ? 31.185 -47.227 45.915 1.00 94.61  ? 95  TYR C OH  1 
ATOM 4843 N N   . CYS C 3 98  ? 25.645 -40.981 43.780 1.00 69.50  ? 96  CYS C N   1 
ATOM 4844 C CA  . CYS C 3 98  ? 25.178 -39.625 43.524 1.00 72.94  ? 96  CYS C CA  1 
ATOM 4845 C C   . CYS C 3 98  ? 25.827 -38.680 44.527 1.00 71.27  ? 96  CYS C C   1 
ATOM 4846 O O   . CYS C 3 98  ? 25.929 -38.998 45.716 1.00 74.41  ? 96  CYS C O   1 
ATOM 4847 C CB  . CYS C 3 98  ? 23.648 -39.523 43.604 1.00 74.10  ? 96  CYS C CB  1 
ATOM 4848 S SG  . CYS C 3 98  ? 22.898 -39.968 45.194 1.00 88.71  ? 96  CYS C SG  1 
ATOM 4849 N N   . ALA C 3 99  ? 26.278 -37.523 44.042 1.00 62.37  ? 97  ALA C N   1 
ATOM 4850 C CA  . ALA C 3 99  ? 27.035 -36.583 44.855 1.00 70.97  ? 97  ALA C CA  1 
ATOM 4851 C C   . ALA C 3 99  ? 26.439 -35.187 44.743 1.00 66.83  ? 97  ALA C C   1 
ATOM 4852 O O   . ALA C 3 99  ? 25.880 -34.814 43.708 1.00 69.16  ? 97  ALA C O   1 
ATOM 4853 C CB  . ALA C 3 99  ? 28.512 -36.558 44.445 1.00 70.59  ? 97  ALA C CB  1 
ATOM 4854 N N   . ALA C 3 100 ? 26.575 -34.413 45.820 1.00 72.18  ? 98  ALA C N   1 
ATOM 4855 C CA  . ALA C 3 100 ? 25.985 -33.086 45.923 1.00 64.62  ? 98  ALA C CA  1 
ATOM 4856 C C   . ALA C 3 100 ? 27.062 -32.031 46.135 1.00 69.81  ? 98  ALA C C   1 
ATOM 4857 O O   . ALA C 3 100 ? 28.122 -32.304 46.708 1.00 61.43  ? 98  ALA C O   1 
ATOM 4858 C CB  . ALA C 3 100 ? 24.972 -33.014 47.073 1.00 57.99  ? 98  ALA C CB  1 
ATOM 4859 N N   . LYS C 3 101 ? 26.772 -30.815 45.674 1.00 67.85  ? 99  LYS C N   1 
ATOM 4860 C CA  . LYS C 3 101 ? 27.668 -29.680 45.859 1.00 65.34  ? 99  LYS C CA  1 
ATOM 4861 C C   . LYS C 3 101 ? 26.860 -28.393 45.818 1.00 73.27  ? 99  LYS C C   1 
ATOM 4862 O O   . LYS C 3 101 ? 26.112 -28.157 44.864 1.00 67.83  ? 99  LYS C O   1 
ATOM 4863 C CB  . LYS C 3 101 ? 28.761 -29.653 44.786 1.00 66.47  ? 99  LYS C CB  1 
ATOM 4864 C CG  . LYS C 3 101 ? 30.123 -29.225 45.307 1.00 69.48  ? 99  LYS C CG  1 
ATOM 4865 C CD  . LYS C 3 101 ? 30.196 -27.734 45.586 1.00 72.73  ? 99  LYS C CD  1 
ATOM 4866 C CE  . LYS C 3 101 ? 31.642 -27.270 45.637 1.00 78.57  ? 99  LYS C CE  1 
ATOM 4867 N NZ  . LYS C 3 101 ? 32.436 -28.018 46.654 1.00 77.54  ? 99  LYS C NZ  1 
ATOM 4868 N N   . PHE C 3 102 ? 27.020 -27.566 46.848 1.00 69.92  ? 100 PHE C N   1 
ATOM 4869 C CA  . PHE C 3 102 ? 26.306 -26.298 46.912 1.00 67.08  ? 100 PHE C CA  1 
ATOM 4870 C C   . PHE C 3 102 ? 26.865 -25.332 45.874 1.00 66.71  ? 100 PHE C C   1 
ATOM 4871 O O   . PHE C 3 102 ? 28.077 -25.101 45.817 1.00 72.69  ? 100 PHE C O   1 
ATOM 4872 C CB  . PHE C 3 102 ? 26.417 -25.703 48.317 1.00 69.70  ? 100 PHE C CB  1 
ATOM 4873 C CG  . PHE C 3 102 ? 25.778 -24.351 48.459 1.00 62.66  ? 100 PHE C CG  1 
ATOM 4874 C CD1 . PHE C 3 102 ? 24.419 -24.233 48.698 1.00 61.98  ? 100 PHE C CD1 1 
ATOM 4875 C CD2 . PHE C 3 102 ? 26.538 -23.197 48.358 1.00 63.44  ? 100 PHE C CD2 1 
ATOM 4876 C CE1 . PHE C 3 102 ? 23.829 -22.989 48.829 1.00 69.74  ? 100 PHE C CE1 1 
ATOM 4877 C CE2 . PHE C 3 102 ? 25.956 -21.952 48.487 1.00 63.42  ? 100 PHE C CE2 1 
ATOM 4878 C CZ  . PHE C 3 102 ? 24.599 -21.847 48.723 1.00 65.84  ? 100 PHE C CZ  1 
ATOM 4879 N N   . TYR C 3 103 ? 25.976 -24.774 45.048 1.00 55.64  ? 101 TYR C N   1 
ATOM 4880 C CA  . TYR C 3 103 ? 26.358 -23.851 43.977 1.00 61.51  ? 101 TYR C CA  1 
ATOM 4881 C C   . TYR C 3 103 ? 27.374 -24.479 43.026 1.00 69.93  ? 101 TYR C C   1 
ATOM 4882 O O   . TYR C 3 103 ? 28.209 -23.782 42.445 1.00 68.40  ? 101 TYR C O   1 
ATOM 4883 C CB  . TYR C 3 103 ? 26.905 -22.535 44.541 1.00 69.07  ? 101 TYR C CB  1 
ATOM 4884 C CG  . TYR C 3 103 ? 25.855 -21.485 44.833 1.00 57.24  ? 101 TYR C CG  1 
ATOM 4885 C CD1 . TYR C 3 103 ? 24.500 -21.780 44.745 1.00 58.99  ? 101 TYR C CD1 1 
ATOM 4886 C CD2 . TYR C 3 103 ? 26.222 -20.198 45.204 1.00 57.58  ? 101 TYR C CD2 1 
ATOM 4887 C CE1 . TYR C 3 103 ? 23.541 -20.820 45.015 1.00 61.27  ? 101 TYR C CE1 1 
ATOM 4888 C CE2 . TYR C 3 103 ? 25.270 -19.233 45.477 1.00 58.71  ? 101 TYR C CE2 1 
ATOM 4889 C CZ  . TYR C 3 103 ? 23.932 -19.549 45.380 1.00 58.90  ? 101 TYR C CZ  1 
ATOM 4890 O OH  . TYR C 3 103 ? 22.981 -18.590 45.649 1.00 60.29  ? 101 TYR C OH  1 
ATOM 4891 N N   . GLY C 3 104 ? 27.316 -25.799 42.865 1.00 77.02  ? 102 GLY C N   1 
ATOM 4892 C CA  . GLY C 3 104 ? 28.256 -26.534 42.049 1.00 69.27  ? 102 GLY C CA  1 
ATOM 4893 C C   . GLY C 3 104 ? 27.543 -27.418 41.044 1.00 64.60  ? 102 GLY C C   1 
ATOM 4894 O O   . GLY C 3 104 ? 26.419 -27.140 40.618 1.00 61.73  ? 102 GLY C O   1 
ATOM 4895 N N   . GLY C 3 105 ? 28.220 -28.494 40.666 1.00 68.16  ? 103 GLY C N   1 
ATOM 4896 C CA  . GLY C 3 105 ? 27.703 -29.432 39.699 1.00 63.49  ? 103 GLY C CA  1 
ATOM 4897 C C   . GLY C 3 105 ? 28.248 -29.294 38.295 1.00 54.89  ? 103 GLY C C   1 
ATOM 4898 O O   . GLY C 3 105 ? 27.558 -29.677 37.344 1.00 50.92  ? 103 GLY C O   1 
ATOM 4899 N N   . ASN C 3 106 ? 29.461 -28.756 38.131 1.00 57.20  ? 104 ASN C N   1 
ATOM 4900 C CA  . ASN C 3 106 ? 30.068 -28.591 36.815 1.00 64.30  ? 104 ASN C CA  1 
ATOM 4901 C C   . ASN C 3 106 ? 31.502 -29.104 36.789 1.00 67.04  ? 104 ASN C C   1 
ATOM 4902 O O   . ASN C 3 106 ? 32.272 -28.737 35.894 1.00 68.49  ? 104 ASN C O   1 
ATOM 4903 C CB  . ASN C 3 106 ? 30.029 -27.126 36.373 1.00 72.73  ? 104 ASN C CB  1 
ATOM 4904 C CG  . ASN C 3 106 ? 30.990 -26.253 37.157 1.00 74.01  ? 104 ASN C CG  1 
ATOM 4905 O OD1 . ASN C 3 106 ? 31.166 -26.429 38.364 1.00 66.52  ? 104 ASN C OD1 1 
ATOM 4906 N ND2 . ASN C 3 106 ? 31.620 -25.304 36.473 1.00 70.94  ? 104 ASN C ND2 1 
ATOM 4907 N N   . SER C 3 107 ? 31.876 -29.941 37.749 1.00 55.48  ? 105 SER C N   1 
ATOM 4908 C CA  . SER C 3 107 ? 33.212 -30.504 37.828 1.00 60.37  ? 105 SER C CA  1 
ATOM 4909 C C   . SER C 3 107 ? 33.173 -31.996 37.527 1.00 70.41  ? 105 SER C C   1 
ATOM 4910 O O   . SER C 3 107 ? 32.192 -32.684 37.829 1.00 68.84  ? 105 SER C O   1 
ATOM 4911 C CB  . SER C 3 107 ? 33.819 -30.266 39.215 1.00 64.16  ? 105 SER C CB  1 
ATOM 4912 O OG  . SER C 3 107 ? 35.172 -30.683 39.266 1.00 78.58  ? 105 SER C OG  1 
ATOM 4913 N N   . LYS C 3 108 ? 34.253 -32.486 36.914 1.00 72.38  ? 106 LYS C N   1 
ATOM 4914 C CA  . LYS C 3 108 ? 34.429 -33.915 36.680 1.00 64.59  ? 106 LYS C CA  1 
ATOM 4915 C C   . LYS C 3 108 ? 35.027 -34.632 37.881 1.00 72.60  ? 106 LYS C C   1 
ATOM 4916 O O   . LYS C 3 108 ? 34.711 -35.803 38.114 1.00 70.20  ? 106 LYS C O   1 
ATOM 4917 C CB  . LYS C 3 108 ? 35.324 -34.144 35.459 1.00 60.82  ? 106 LYS C CB  1 
ATOM 4918 C CG  . LYS C 3 108 ? 34.941 -33.319 34.237 1.00 69.37  ? 106 LYS C CG  1 
ATOM 4919 C CD  . LYS C 3 108 ? 33.798 -33.963 33.469 1.00 59.82  ? 106 LYS C CD  1 
ATOM 4920 C CE  . LYS C 3 108 ? 33.560 -33.268 32.136 1.00 70.32  ? 106 LYS C CE  1 
ATOM 4921 N NZ  . LYS C 3 108 ? 32.125 -33.281 31.723 1.00 67.57  ? 106 LYS C NZ  1 
ATOM 4922 N N   . ARG C 3 109 ? 35.872 -33.951 38.652 1.00 77.77  ? 107 ARG C N   1 
ATOM 4923 C CA  . ARG C 3 109 ? 36.550 -34.591 39.769 1.00 76.05  ? 107 ARG C CA  1 
ATOM 4924 C C   . ARG C 3 109 ? 35.560 -34.914 40.886 1.00 71.21  ? 107 ARG C C   1 
ATOM 4925 O O   . ARG C 3 109 ? 34.622 -34.147 41.128 1.00 72.70  ? 107 ARG C O   1 
ATOM 4926 C CB  . ARG C 3 109 ? 37.657 -33.688 40.316 1.00 79.29  ? 107 ARG C CB  1 
ATOM 4927 C CG  . ARG C 3 109 ? 38.651 -33.205 39.275 1.00 86.22  ? 107 ARG C CG  1 
ATOM 4928 C CD  . ARG C 3 109 ? 39.246 -31.860 39.665 1.00 86.44  ? 107 ARG C CD  1 
ATOM 4929 N NE  . ARG C 3 109 ? 40.041 -31.950 40.884 1.00 88.80  ? 107 ARG C NE  1 
ATOM 4930 C CZ  . ARG C 3 109 ? 41.332 -31.658 40.960 1.00 94.44  ? 107 ARG C CZ  1 
ATOM 4931 N NH1 . ARG C 3 109 ? 42.012 -31.245 39.903 1.00 99.35  ? 107 ARG C NH1 1 
ATOM 4932 N NH2 . ARG C 3 109 ? 41.957 -31.785 42.127 1.00 96.09  ? 107 ARG C NH2 1 
ATOM 4933 N N   . PRO C 3 110 ? 35.742 -36.038 41.584 1.00 75.96  ? 108 PRO C N   1 
ATOM 4934 C CA  . PRO C 3 110 ? 34.884 -36.316 42.745 1.00 77.30  ? 108 PRO C CA  1 
ATOM 4935 C C   . PRO C 3 110 ? 35.202 -35.435 43.939 1.00 74.62  ? 108 PRO C C   1 
ATOM 4936 O O   . PRO C 3 110 ? 34.312 -35.181 44.761 1.00 66.97  ? 108 PRO C O   1 
ATOM 4937 C CB  . PRO C 3 110 ? 35.160 -37.798 43.046 1.00 65.35  ? 108 PRO C CB  1 
ATOM 4938 C CG  . PRO C 3 110 ? 35.935 -38.322 41.860 1.00 66.51  ? 108 PRO C CG  1 
ATOM 4939 C CD  . PRO C 3 110 ? 36.664 -37.148 41.300 1.00 71.39  ? 108 PRO C CD  1 
ATOM 4940 N N   . GLY C 3 111 ? 36.444 -34.960 44.058 1.00 80.40  ? 109 GLY C N   1 
ATOM 4941 C CA  . GLY C 3 111 ? 36.821 -34.100 45.165 1.00 68.82  ? 109 GLY C CA  1 
ATOM 4942 C C   . GLY C 3 111 ? 36.072 -32.787 45.207 1.00 67.11  ? 109 GLY C C   1 
ATOM 4943 O O   . GLY C 3 111 ? 35.969 -32.175 46.275 1.00 72.66  ? 109 GLY C O   1 
ATOM 4944 N N   . ASP C 3 112 ? 35.547 -32.334 44.068 1.00 65.66  ? 110 ASP C N   1 
ATOM 4945 C CA  . ASP C 3 112 ? 34.725 -31.135 44.004 1.00 72.05  ? 110 ASP C CA  1 
ATOM 4946 C C   . ASP C 3 112 ? 33.259 -31.417 44.306 1.00 67.18  ? 110 ASP C C   1 
ATOM 4947 O O   . ASP C 3 112 ? 32.389 -30.660 43.862 1.00 62.87  ? 110 ASP C O   1 
ATOM 4948 C CB  . ASP C 3 112 ? 34.856 -30.476 42.630 1.00 76.38  ? 110 ASP C CB  1 
ATOM 4949 C CG  . ASP C 3 112 ? 36.220 -29.861 42.406 1.00 80.97  ? 110 ASP C CG  1 
ATOM 4950 O OD1 . ASP C 3 112 ? 36.748 -29.227 43.345 1.00 74.32  ? 110 ASP C OD1 1 
ATOM 4951 O OD2 . ASP C 3 112 ? 36.763 -30.009 41.291 1.00 83.82  ? 110 ASP C OD2 1 
ATOM 4952 N N   . TYR C 3 113 ? 32.970 -32.503 45.022 1.00 62.29  ? 111 TYR C N   1 
ATOM 4953 C CA  . TYR C 3 113 ? 31.621 -32.845 45.459 1.00 61.61  ? 111 TYR C CA  1 
ATOM 4954 C C   . TYR C 3 113 ? 31.701 -33.247 46.923 1.00 65.08  ? 111 TYR C C   1 
ATOM 4955 O O   . TYR C 3 113 ? 32.335 -34.254 47.257 1.00 73.43  ? 111 TYR C O   1 
ATOM 4956 C CB  . TYR C 3 113 ? 31.024 -33.978 44.615 1.00 66.07  ? 111 TYR C CB  1 
ATOM 4957 C CG  . TYR C 3 113 ? 30.658 -33.592 43.192 1.00 66.69  ? 111 TYR C CG  1 
ATOM 4958 C CD1 . TYR C 3 113 ? 31.638 -33.296 42.253 1.00 69.57  ? 111 TYR C CD1 1 
ATOM 4959 C CD2 . TYR C 3 113 ? 29.329 -33.524 42.791 1.00 62.05  ? 111 TYR C CD2 1 
ATOM 4960 C CE1 . TYR C 3 113 ? 31.308 -32.940 40.957 1.00 62.97  ? 111 TYR C CE1 1 
ATOM 4961 C CE2 . TYR C 3 113 ? 28.988 -33.171 41.495 1.00 67.42  ? 111 TYR C CE2 1 
ATOM 4962 C CZ  . TYR C 3 113 ? 29.983 -32.880 40.583 1.00 64.04  ? 111 TYR C CZ  1 
ATOM 4963 O OH  . TYR C 3 113 ? 29.656 -32.527 39.293 1.00 59.72  ? 111 TYR C OH  1 
ATOM 4964 N N   . ALA C 3 114 ? 31.062 -32.465 47.796 1.00 64.60  ? 112 ALA C N   1 
ATOM 4965 C CA  . ALA C 3 114 ? 31.257 -32.641 49.232 1.00 74.87  ? 112 ALA C CA  1 
ATOM 4966 C C   . ALA C 3 114 ? 30.419 -33.783 49.796 1.00 73.02  ? 112 ALA C C   1 
ATOM 4967 O O   . ALA C 3 114 ? 30.920 -34.587 50.590 1.00 68.27  ? 112 ALA C O   1 
ATOM 4968 C CB  . ALA C 3 114 ? 30.938 -31.340 49.969 1.00 68.12  ? 112 ALA C CB  1 
ATOM 4969 N N   . TYR C 3 115 ? 29.149 -33.868 49.414 1.00 74.25  ? 113 TYR C N   1 
ATOM 4970 C CA  . TYR C 3 115 ? 28.228 -34.845 49.977 1.00 73.25  ? 113 TYR C CA  1 
ATOM 4971 C C   . TYR C 3 115 ? 28.085 -36.027 49.026 1.00 72.28  ? 113 TYR C C   1 
ATOM 4972 O O   . TYR C 3 115 ? 28.083 -35.854 47.804 1.00 70.32  ? 113 TYR C O   1 
ATOM 4973 C CB  . TYR C 3 115 ? 26.857 -34.216 50.246 1.00 71.79  ? 113 TYR C CB  1 
ATOM 4974 C CG  . TYR C 3 115 ? 26.837 -33.124 51.304 1.00 82.17  ? 113 TYR C CG  1 
ATOM 4975 C CD1 . TYR C 3 115 ? 28.010 -32.610 51.843 1.00 95.82  ? 113 TYR C CD1 1 
ATOM 4976 C CD2 . TYR C 3 115 ? 25.635 -32.601 51.753 1.00 88.93  ? 113 TYR C CD2 1 
ATOM 4977 C CE1 . TYR C 3 115 ? 27.982 -31.610 52.801 1.00 98.13  ? 113 TYR C CE1 1 
ATOM 4978 C CE2 . TYR C 3 115 ? 25.595 -31.604 52.708 1.00 94.52  ? 113 TYR C CE2 1 
ATOM 4979 C CZ  . TYR C 3 115 ? 26.771 -31.111 53.229 1.00 93.62  ? 113 TYR C CZ  1 
ATOM 4980 O OH  . TYR C 3 115 ? 26.731 -30.118 54.181 1.00 79.60  ? 113 TYR C OH  1 
ATOM 4981 N N   . TRP C 3 116 ? 27.964 -37.227 49.593 1.00 70.63  ? 114 TRP C N   1 
ATOM 4982 C CA  . TRP C 3 116 ? 27.893 -38.455 48.813 1.00 66.14  ? 114 TRP C CA  1 
ATOM 4983 C C   . TRP C 3 116 ? 26.747 -39.328 49.305 1.00 72.11  ? 114 TRP C C   1 
ATOM 4984 O O   . TRP C 3 116 ? 26.224 -39.147 50.408 1.00 80.97  ? 114 TRP C O   1 
ATOM 4985 C CB  . TRP C 3 116 ? 29.206 -39.248 48.885 1.00 64.62  ? 114 TRP C CB  1 
ATOM 4986 C CG  . TRP C 3 116 ? 30.351 -38.582 48.198 1.00 66.99  ? 114 TRP C CG  1 
ATOM 4987 C CD1 . TRP C 3 116 ? 31.258 -37.730 48.756 1.00 64.88  ? 114 TRP C CD1 1 
ATOM 4988 C CD2 . TRP C 3 116 ? 30.715 -38.708 46.818 1.00 68.67  ? 114 TRP C CD2 1 
ATOM 4989 N NE1 . TRP C 3 116 ? 32.166 -37.319 47.811 1.00 69.57  ? 114 TRP C NE1 1 
ATOM 4990 C CE2 . TRP C 3 116 ? 31.854 -37.905 46.612 1.00 71.44  ? 114 TRP C CE2 1 
ATOM 4991 C CE3 . TRP C 3 116 ? 30.189 -39.423 45.738 1.00 71.91  ? 114 TRP C CE3 1 
ATOM 4992 C CZ2 . TRP C 3 116 ? 32.475 -37.796 45.370 1.00 65.15  ? 114 TRP C CZ2 1 
ATOM 4993 C CZ3 . TRP C 3 116 ? 30.807 -39.313 44.505 1.00 71.73  ? 114 TRP C CZ3 1 
ATOM 4994 C CH2 . TRP C 3 116 ? 31.938 -38.506 44.332 1.00 60.94  ? 114 TRP C CH2 1 
ATOM 4995 N N   . GLY C 3 117 ? 26.365 -40.287 48.461 1.00 67.15  ? 115 GLY C N   1 
ATOM 4996 C CA  . GLY C 3 117 ? 25.377 -41.283 48.801 1.00 64.30  ? 115 GLY C CA  1 
ATOM 4997 C C   . GLY C 3 117 ? 26.031 -42.638 49.021 1.00 65.93  ? 115 GLY C C   1 
ATOM 4998 O O   . GLY C 3 117 ? 27.228 -42.824 48.814 1.00 73.00  ? 115 GLY C O   1 
ATOM 4999 N N   . GLN C 3 118 ? 25.209 -43.596 49.453 1.00 67.93  ? 116 GLN C N   1 
ATOM 5000 C CA  . GLN C 3 118 ? 25.715 -44.927 49.769 1.00 69.15  ? 116 GLN C CA  1 
ATOM 5001 C C   . GLN C 3 118 ? 26.002 -45.762 48.529 1.00 74.05  ? 116 GLN C C   1 
ATOM 5002 O O   . GLN C 3 118 ? 26.823 -46.683 48.597 1.00 77.22  ? 116 GLN C O   1 
ATOM 5003 C CB  . GLN C 3 118 ? 24.724 -45.667 50.671 1.00 71.20  ? 116 GLN C CB  1 
ATOM 5004 C CG  . GLN C 3 118 ? 23.707 -46.513 49.924 1.00 70.51  ? 116 GLN C CG  1 
ATOM 5005 C CD  . GLN C 3 118 ? 22.485 -45.721 49.498 1.00 68.87  ? 116 GLN C CD  1 
ATOM 5006 O OE1 . GLN C 3 118 ? 22.478 -44.492 49.556 1.00 72.66  ? 116 GLN C OE1 1 
ATOM 5007 N NE2 . GLN C 3 118 ? 21.444 -46.423 49.066 1.00 68.84  ? 116 GLN C NE2 1 
ATOM 5008 N N   . GLY C 3 119 ? 25.347 -45.468 47.408 1.00 71.65  ? 117 GLY C N   1 
ATOM 5009 C CA  . GLY C 3 119 ? 25.601 -46.181 46.173 1.00 68.50  ? 117 GLY C CA  1 
ATOM 5010 C C   . GLY C 3 119 ? 24.693 -47.367 45.928 1.00 72.19  ? 117 GLY C C   1 
ATOM 5011 O O   . GLY C 3 119 ? 24.347 -48.103 46.858 1.00 74.37  ? 117 GLY C O   1 
ATOM 5012 N N   . THR C 3 120 ? 24.305 -47.561 44.671 1.00 64.65  ? 118 THR C N   1 
ATOM 5013 C CA  . THR C 3 120 ? 23.495 -48.696 44.253 1.00 65.34  ? 118 THR C CA  1 
ATOM 5014 C C   . THR C 3 120 ? 24.226 -49.437 43.142 1.00 70.14  ? 118 THR C C   1 
ATOM 5015 O O   . THR C 3 120 ? 24.673 -48.822 42.167 1.00 78.42  ? 118 THR C O   1 
ATOM 5016 C CB  . THR C 3 120 ? 22.104 -48.244 43.786 1.00 65.26  ? 118 THR C CB  1 
ATOM 5017 O OG1 . THR C 3 120 ? 21.440 -49.328 43.125 1.00 66.73  ? 118 THR C OG1 1 
ATOM 5018 C CG2 . THR C 3 120 ? 22.203 -47.049 42.840 1.00 72.67  ? 118 THR C CG2 1 
ATOM 5019 N N   . GLN C 3 121 ? 24.361 -50.752 43.297 1.00 77.31  ? 119 GLN C N   1 
ATOM 5020 C CA  . GLN C 3 121 ? 25.098 -51.572 42.344 1.00 73.49  ? 119 GLN C CA  1 
ATOM 5021 C C   . GLN C 3 121 ? 24.190 -51.988 41.194 1.00 68.07  ? 119 GLN C C   1 
ATOM 5022 O O   . GLN C 3 121 ? 23.061 -52.439 41.416 1.00 68.28  ? 119 GLN C O   1 
ATOM 5023 C CB  . GLN C 3 121 ? 25.681 -52.808 43.033 1.00 71.23  ? 119 GLN C CB  1 
ATOM 5024 C CG  . GLN C 3 121 ? 26.080 -53.929 42.085 1.00 72.79  ? 119 GLN C CG  1 
ATOM 5025 C CD  . GLN C 3 121 ? 27.559 -53.914 41.753 1.00 73.93  ? 119 GLN C CD  1 
ATOM 5026 O OE1 . GLN C 3 121 ? 28.406 -53.838 42.642 1.00 75.06  ? 119 GLN C OE1 1 
ATOM 5027 N NE2 . GLN C 3 121 ? 27.877 -53.985 40.466 1.00 73.98  ? 119 GLN C NE2 1 
ATOM 5028 N N   . VAL C 3 122 ? 24.684 -51.831 39.969 1.00 67.74  ? 120 VAL C N   1 
ATOM 5029 C CA  . VAL C 3 122 ? 23.983 -52.264 38.766 1.00 67.79  ? 120 VAL C CA  1 
ATOM 5030 C C   . VAL C 3 122 ? 24.911 -53.188 37.993 1.00 75.24  ? 120 VAL C C   1 
ATOM 5031 O O   . VAL C 3 122 ? 26.009 -52.781 37.591 1.00 78.33  ? 120 VAL C O   1 
ATOM 5032 C CB  . VAL C 3 122 ? 23.547 -51.078 37.893 1.00 84.43  ? 120 VAL C CB  1 
ATOM 5033 C CG1 . VAL C 3 122 ? 23.123 -51.556 36.509 1.00 77.38  ? 120 VAL C CG1 1 
ATOM 5034 C CG2 . VAL C 3 122 ? 22.432 -50.296 38.566 1.00 80.52  ? 120 VAL C CG2 1 
ATOM 5035 N N   . THR C 3 123 ? 24.476 -54.427 37.792 1.00 77.10  ? 121 THR C N   1 
ATOM 5036 C CA  . THR C 3 123 ? 25.190 -55.396 36.975 1.00 81.63  ? 121 THR C CA  1 
ATOM 5037 C C   . THR C 3 123 ? 24.383 -55.654 35.710 1.00 74.22  ? 121 THR C C   1 
ATOM 5038 O O   . THR C 3 123 ? 23.163 -55.837 35.775 1.00 73.63  ? 121 THR C O   1 
ATOM 5039 C CB  . THR C 3 123 ? 25.414 -56.706 37.735 1.00 76.40  ? 121 THR C CB  1 
ATOM 5040 O OG1 . THR C 3 123 ? 24.280 -56.976 38.567 1.00 85.98  ? 121 THR C OG1 1 
ATOM 5041 C CG2 . THR C 3 123 ? 26.662 -56.617 38.603 1.00 77.67  ? 121 THR C CG2 1 
ATOM 5042 N N   . VAL C 3 124 ? 25.060 -55.652 34.565 1.00 75.39  ? 122 VAL C N   1 
ATOM 5043 C CA  . VAL C 3 124 ? 24.434 -55.931 33.279 1.00 77.48  ? 122 VAL C CA  1 
ATOM 5044 C C   . VAL C 3 124 ? 25.186 -57.079 32.616 1.00 79.65  ? 122 VAL C C   1 
ATOM 5045 O O   . VAL C 3 124 ? 26.421 -57.074 32.566 1.00 81.01  ? 122 VAL C O   1 
ATOM 5046 C CB  . VAL C 3 124 ? 24.386 -54.679 32.379 1.00 90.12  ? 122 VAL C CB  1 
ATOM 5047 C CG1 . VAL C 3 124 ? 25.751 -54.048 32.243 1.00 88.34  ? 122 VAL C CG1 1 
ATOM 5048 C CG2 . VAL C 3 124 ? 23.822 -55.024 31.017 1.00 81.66  ? 122 VAL C CG2 1 
ATOM 5049 N N   . SER C 3 125 ? 24.441 -58.070 32.130 1.00 83.14  ? 123 SER C N   1 
ATOM 5050 C CA  . SER C 3 125 ? 24.989 -59.345 31.690 1.00 95.24  ? 123 SER C CA  1 
ATOM 5051 C C   . SER C 3 125 ? 24.853 -59.502 30.177 1.00 95.17  ? 123 SER C C   1 
ATOM 5052 O O   . SER C 3 125 ? 24.298 -58.646 29.482 1.00 96.98  ? 123 SER C O   1 
ATOM 5053 C CB  . SER C 3 125 ? 24.298 -60.500 32.418 1.00 102.55 ? 123 SER C CB  1 
ATOM 5054 O OG  . SER C 3 125 ? 22.962 -60.656 31.968 1.00 98.67  ? 123 SER C OG  1 
ATOM 5055 N N   . SER C 3 126 ? 25.370 -60.625 29.680 1.00 104.66 ? 124 SER C N   1 
ATOM 5056 C CA  . SER C 3 126 ? 25.345 -60.969 28.259 1.00 113.32 ? 124 SER C CA  1 
ATOM 5057 C C   . SER C 3 126 ? 25.959 -59.868 27.399 1.00 112.65 ? 124 SER C C   1 
ATOM 5058 O O   . SER C 3 126 ? 27.172 -59.836 27.191 1.00 117.37 ? 124 SER C O   1 
ATOM 5059 C CB  . SER C 3 126 ? 23.914 -61.261 27.798 1.00 117.56 ? 124 SER C CB  1 
ATOM 5060 O OG  . SER C 3 126 ? 23.909 -61.969 26.570 1.00 124.90 ? 124 SER C OG  1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . ALA A 7   ? 1.3065 0.5333 0.8466 0.0324  0.2247  -0.0497 6   ALA A N   
2    C CA  . ALA A 7   ? 1.5203 0.7683 1.0635 0.0351  0.2241  -0.0450 6   ALA A CA  
3    C C   . ALA A 7   ? 1.4986 0.7752 1.0634 0.0332  0.2158  -0.0346 6   ALA A C   
4    O O   . ALA A 7   ? 1.4038 0.6932 0.9876 0.0396  0.2210  -0.0241 6   ALA A O   
5    C CB  . ALA A 7   ? 1.3645 0.6100 0.9090 0.0466  0.2387  -0.0407 6   ALA A CB  
6    N N   . SER A 8   ? 1.4940 0.7807 1.0557 0.0244  0.2030  -0.0374 7   SER A N   
7    C CA  . SER A 8   ? 1.4138 0.7264 0.9932 0.0219  0.1947  -0.0291 7   SER A CA  
8    C C   . SER A 8   ? 1.3566 0.6867 0.9369 0.0241  0.1943  -0.0251 7   SER A C   
9    O O   . SER A 8   ? 1.3536 0.6919 0.9275 0.0184  0.1855  -0.0281 7   SER A O   
10   C CB  . SER A 8   ? 1.3823 0.6967 0.9590 0.0120  0.1818  -0.0335 7   SER A CB  
11   O OG  . SER A 8   ? 1.4068 0.7246 0.9702 0.0069  0.1748  -0.0389 7   SER A OG  
12   N N   . LEU A 9   ? 1.2982 0.6341 0.8870 0.0326  0.2043  -0.0177 8   LEU A N   
13   C CA  . LEU A 9   ? 1.2928 0.6458 0.8839 0.0349  0.2046  -0.0125 8   LEU A CA  
14   C C   . LEU A 9   ? 1.2839 0.6618 0.8916 0.0316  0.1963  -0.0041 8   LEU A C   
15   O O   . LEU A 9   ? 1.3088 0.6998 0.9148 0.0294  0.1916  -0.0026 8   LEU A O   
16   C CB  . LEU A 9   ? 1.2651 0.6173 0.8606 0.0449  0.2180  -0.0062 8   LEU A CB  
17   C CG  . LEU A 9   ? 1.2630 0.5910 0.8407 0.0495  0.2280  -0.0143 8   LEU A CG  
18   C CD1 . LEU A 9   ? 1.1979 0.5312 0.7797 0.0593  0.2400  -0.0071 8   LEU A CD1 
19   C CD2 . LEU A 9   ? 1.2817 0.5990 0.8372 0.0428  0.2217  -0.0260 8   LEU A CD2 
20   N N   . TRP A 10  ? 1.1871 0.5713 0.8101 0.0310  0.1946  0.0014  9   TRP A N   
21   C CA  . TRP A 10  ? 1.1772 0.5840 0.8143 0.0271  0.1864  0.0084  9   TRP A CA  
22   C C   . TRP A 10  ? 1.2407 0.6502 0.8686 0.0190  0.1747  0.0016  9   TRP A C   
23   O O   . TRP A 10  ? 1.1991 0.6246 0.8300 0.0165  0.1691  0.0047  9   TRP A O   
24   C CB  . TRP A 10  ? 1.2435 0.6549 0.8971 0.0274  0.1865  0.0146  9   TRP A CB  
25   C CG  . TRP A 10  ? 1.2116 0.6304 0.8807 0.0349  0.1962  0.0256  9   TRP A CG  
26   C CD1 . TRP A 10  ? 1.1222 0.5284 0.7961 0.0408  0.2055  0.0277  9   TRP A CD1 
27   C CD2 . TRP A 10  ? 1.2184 0.6591 0.9004 0.0373  0.1976  0.0368  9   TRP A CD2 
28   N NE1 . TRP A 10  ? 1.1094 0.5293 0.7995 0.0472  0.2128  0.0400  9   TRP A NE1 
29   C CE2 . TRP A 10  ? 1.1853 0.6271 0.8805 0.0448  0.2079  0.0459  9   TRP A CE2 
30   C CE3 . TRP A 10  ? 1.1115 0.5707 0.7951 0.0335  0.1911  0.0401  9   TRP A CE3 
31   C CZ2 . TRP A 10  ? 1.1874 0.6495 0.8976 0.0482  0.2115  0.0588  9   TRP A CZ2 
32   C CZ3 . TRP A 10  ? 1.1450 0.6231 0.8424 0.0364  0.1944  0.0522  9   TRP A CZ3 
33   C CH2 . TRP A 10  ? 1.2080 0.6883 0.9187 0.0435  0.2043  0.0617  9   TRP A CH2 
34   N N   . THR A 11  ? 1.1827 0.5765 0.7994 0.0147  0.1709  -0.0074 10  THR A N   
35   C CA  . THR A 11  ? 1.2214 0.6180 0.8302 0.0072  0.1599  -0.0131 10  THR A CA  
36   C C   . THR A 11  ? 1.2223 0.6205 0.8189 0.0066  0.1585  -0.0164 10  THR A C   
37   O O   . THR A 11  ? 1.1784 0.5893 0.7760 0.0029  0.1509  -0.0155 10  THR A O   
38   C CB  . THR A 11  ? 1.2361 0.6150 0.8347 0.0026  0.1568  -0.0213 10  THR A CB  
39   O OG1 . THR A 11  ? 1.3900 0.7727 1.0016 0.0009  0.1540  -0.0176 10  THR A OG1 
40   C CG2 . THR A 11  ? 1.2945 0.6731 0.8806 -0.0042 0.1473  -0.0280 10  THR A CG2 
41   N N   . ALA A 12  ? 1.3246 0.7100 0.9095 0.0104  0.1660  -0.0200 11  ALA A N   
42   C CA  . ALA A 12  ? 1.3291 0.7162 0.9023 0.0099  0.1650  -0.0227 11  ALA A CA  
43   C C   . ALA A 12  ? 1.3427 0.7492 0.9268 0.0125  0.1655  -0.0139 11  ALA A C   
44   O O   . ALA A 12  ? 1.3074 0.7220 0.8872 0.0094  0.1597  -0.0144 11  ALA A O   
45   C CB  . ALA A 12  ? 1.2524 0.6217 0.8107 0.0137  0.1738  -0.0281 11  ALA A CB  
46   N N   . ALA A 13  ? 1.2285 0.6428 0.8268 0.0178  0.1720  -0.0054 12  ALA A N   
47   C CA  . ALA A 13  ? 1.1586 0.5918 0.7673 0.0195  0.1724  0.0038  12  ALA A CA  
48   C C   . ALA A 13  ? 1.1323 0.5804 0.7481 0.0135  0.1620  0.0059  12  ALA A C   
49   O O   . ALA A 13  ? 1.1676 0.6257 0.7819 0.0113  0.1579  0.0078  12  ALA A O   
50   C CB  . ALA A 13  ? 1.0650 0.5041 0.6884 0.0260  0.1814  0.0134  12  ALA A CB  
51   N N   . SER A 14  ? 1.1986 0.6481 0.8220 0.0108  0.1578  0.0058  13  SER A N   
52   C CA  . SER A 14  ? 1.0957 0.5586 0.7249 0.0054  0.1484  0.0073  13  SER A CA  
53   C C   . SER A 14  ? 1.0545 0.5131 0.6707 0.0006  0.1408  -0.0004 13  SER A C   
54   O O   . SER A 14  ? 1.1073 0.5767 0.7249 -0.0025 0.1347  0.0010  13  SER A O   
55   C CB  . SER A 14  ? 1.0750 0.5399 0.7145 0.0038  0.1461  0.0088  13  SER A CB  
56   O OG  . SER A 14  ? 1.0143 0.4664 0.6450 0.0004  0.1419  0.0006  13  SER A OG  
57   N N   . THR A 15  ? 1.0252 0.4678 0.6285 -0.0002 0.1411  -0.0084 14  THR A N   
58   C CA  . THR A 15  ? 1.1580 0.5971 0.7490 -0.0046 0.1342  -0.0148 14  THR A CA  
59   C C   . THR A 15  ? 1.1148 0.5588 0.7003 -0.0036 0.1350  -0.0133 14  THR A C   
60   O O   . THR A 15  ? 1.0088 0.4588 0.5914 -0.0070 0.1283  -0.0143 14  THR A O   
61   C CB  . THR A 15  ? 1.0981 0.5192 0.6755 -0.0062 0.1349  -0.0230 14  THR A CB  
62   O OG1 . THR A 15  ? 1.2358 0.6520 0.8188 -0.0075 0.1341  -0.0238 14  THR A OG1 
63   C CG2 . THR A 15  ? 1.1941 0.6134 0.7601 -0.0114 0.1270  -0.0285 14  THR A CG2 
64   N N   . LEU A 16  ? 1.0541 0.4958 0.6387 0.0014  0.1434  -0.0105 15  LEU A N   
65   C CA  . LEU A 16  ? 1.1106 0.5577 0.6907 0.0024  0.1445  -0.0080 15  LEU A CA  
66   C C   . LEU A 16  ? 1.1164 0.5807 0.7076 0.0009  0.1405  -0.0008 15  LEU A C   
67   O O   . LEU A 16  ? 1.0504 0.5196 0.6373 -0.0019 0.1354  -0.0010 15  LEU A O   
68   C CB  . LEU A 16  ? 1.0417 0.4837 0.6197 0.0086  0.1551  -0.0056 15  LEU A CB  
69   C CG  . LEU A 16  ? 1.1607 0.5846 0.7229 0.0099  0.1595  -0.0137 15  LEU A CG  
70   C CD1 . LEU A 16  ? 1.1973 0.6180 0.7578 0.0169  0.1707  -0.0104 15  LEU A CD1 
71   C CD2 . LEU A 16  ? 1.1966 0.6173 0.7449 0.0050  0.1527  -0.0198 15  LEU A CD2 
72   N N   . VAL A 17  ? 1.0436 0.5170 0.6488 0.0024  0.1426  0.0059  16  VAL A N   
73   C CA  . VAL A 17  ? 1.0681 0.5577 0.6830 0.0002  0.1389  0.0128  16  VAL A CA  
74   C C   . VAL A 17  ? 1.0463 0.5386 0.6592 -0.0053 0.1293  0.0089  16  VAL A C   
75   O O   . VAL A 17  ? 1.0536 0.5538 0.6662 -0.0081 0.1248  0.0108  16  VAL A O   
76   C CB  . VAL A 17  ? 1.0326 0.5316 0.6627 0.0024  0.1429  0.0210  16  VAL A CB  
77   C CG1 . VAL A 17  ? 0.9237 0.4394 0.5626 -0.0012 0.1382  0.0277  16  VAL A CG1 
78   C CG2 . VAL A 17  ? 1.0250 0.5223 0.6579 0.0087  0.1531  0.0261  16  VAL A CG2 
79   N N   . LYS A 18  ? 1.0195 0.5053 0.6310 -0.0069 0.1262  0.0035  17  LYS A N   
80   C CA  . LYS A 18  ? 1.0162 0.5047 0.6261 -0.0113 0.1177  0.0000  17  LYS A CA  
81   C C   . LYS A 18  ? 1.0195 0.5035 0.6176 -0.0132 0.1138  -0.0045 17  LYS A C   
82   O O   . LYS A 18  ? 1.1235 0.6134 0.7214 -0.0160 0.1082  -0.0043 17  LYS A O   
83   C CB  . LYS A 18  ? 0.9829 0.4654 0.5936 -0.0125 0.1155  -0.0043 17  LYS A CB  
84   C CG  . LYS A 18  ? 1.0924 0.5765 0.7001 -0.0165 0.1074  -0.0082 17  LYS A CG  
85   C CD  . LYS A 18  ? 1.1377 0.6188 0.7486 -0.0179 0.1051  -0.0105 17  LYS A CD  
86   C CE  . LYS A 18  ? 1.1180 0.5995 0.7245 -0.0213 0.0976  -0.0146 17  LYS A CE  
87   N NZ  . LYS A 18  ? 0.9866 0.4795 0.5977 -0.0224 0.0936  -0.0120 17  LYS A NZ  
88   N N   . ILE A 19  ? 1.0249 0.4981 0.6126 -0.0118 0.1170  -0.0085 18  ILE A N   
89   C CA  . ILE A 19  ? 1.0525 0.5218 0.6290 -0.0137 0.1133  -0.0122 18  ILE A CA  
90   C C   . ILE A 19  ? 1.1179 0.5950 0.6953 -0.0134 0.1137  -0.0073 18  ILE A C   
91   O O   . ILE A 19  ? 1.0950 0.5746 0.6689 -0.0161 0.1082  -0.0080 18  ILE A O   
92   C CB  . ILE A 19  ? 1.0311 0.4872 0.5956 -0.0128 0.1168  -0.0176 18  ILE A CB  
93   C CG1 . ILE A 19  ? 1.0573 0.5054 0.6182 -0.0155 0.1131  -0.0233 18  ILE A CG1 
94   C CG2 . ILE A 19  ? 1.0820 0.5363 0.6358 -0.0138 0.1151  -0.0192 18  ILE A CG2 
95   C CD1 . ILE A 19  ? 1.1473 0.5810 0.6955 -0.0154 0.1166  -0.0291 18  ILE A CD1 
96   N N   . GLY A 20  ? 1.0729 0.5541 0.6553 -0.0102 0.1202  -0.0017 19  GLY A N   
97   C CA  . GLY A 20  ? 1.0175 0.5070 0.6013 -0.0105 0.1204  0.0040  19  GLY A CA  
98   C C   . GLY A 20  ? 1.0193 0.5187 0.6097 -0.0142 0.1142  0.0070  19  GLY A C   
99   O O   . GLY A 20  ? 1.0353 0.5376 0.6225 -0.0166 0.1106  0.0083  19  GLY A O   
100  N N   . ALA A 21  ? 1.0718 0.5758 0.6708 -0.0150 0.1130  0.0081  20  ALA A N   
101  C CA  . ALA A 21  ? 0.9668 0.4792 0.5707 -0.0187 0.1074  0.0101  20  ALA A CA  
102  C C   . ALA A 21  ? 0.9317 0.4390 0.5284 -0.0212 0.1008  0.0040  20  ALA A C   
103  O O   . ALA A 21  ? 0.9763 0.4869 0.5716 -0.0240 0.0966  0.0049  20  ALA A O   
104  C CB  . ALA A 21  ? 1.0304 0.5493 0.6448 -0.0188 0.1080  0.0127  20  ALA A CB  
105  N N   . GLY A 22  ? 0.8524 0.3517 0.4445 -0.0205 0.0997  -0.0018 21  GLY A N   
106  C CA  . GLY A 22  ? 0.9997 0.4952 0.5858 -0.0226 0.0937  -0.0066 21  GLY A CA  
107  C C   . GLY A 22  ? 1.0867 0.5791 0.6645 -0.0233 0.0922  -0.0070 21  GLY A C   
108  O O   . GLY A 22  ? 1.0126 0.5057 0.5884 -0.0252 0.0873  -0.0078 21  GLY A O   
109  N N   . LEU A 23  ? 1.0002 0.4892 0.5734 -0.0216 0.0966  -0.0061 22  LEU A N   
110  C CA  . LEU A 23  ? 0.9682 0.4557 0.5342 -0.0224 0.0954  -0.0054 22  LEU A CA  
111  C C   . LEU A 23  ? 0.9303 0.4252 0.5006 -0.0242 0.0939  0.0000  22  LEU A C   
112  O O   . LEU A 23  ? 0.9129 0.4070 0.4791 -0.0262 0.0900  0.0001  22  LEU A O   
113  C CB  . LEU A 23  ? 0.9846 0.4679 0.5449 -0.0199 0.1013  -0.0051 22  LEU A CB  
114  C CG  . LEU A 23  ? 1.0329 0.5065 0.5855 -0.0191 0.1026  -0.0111 22  LEU A CG  
115  C CD1 . LEU A 23  ? 0.9166 0.3858 0.4627 -0.0163 0.1094  -0.0108 22  LEU A CD1 
116  C CD2 . LEU A 23  ? 0.9888 0.4586 0.5343 -0.0219 0.0961  -0.0153 22  LEU A CD2 
117  N N   . LEU A 24  ? 0.8959 0.3981 0.4745 -0.0238 0.0969  0.0049  23  LEU A N   
118  C CA  . LEU A 24  ? 0.9419 0.4517 0.5245 -0.0266 0.0951  0.0103  23  LEU A CA  
119  C C   . LEU A 24  ? 0.8820 0.3914 0.4642 -0.0298 0.0889  0.0076  23  LEU A C   
120  O O   . LEU A 24  ? 0.9536 0.4604 0.5308 -0.0319 0.0852  0.0072  23  LEU A O   
121  C CB  . LEU A 24  ? 0.9170 0.4358 0.5093 -0.0261 0.0992  0.0165  23  LEU A CB  
122  C CG  . LEU A 24  ? 0.9170 0.4450 0.5134 -0.0297 0.0979  0.0236  23  LEU A CG  
123  C CD1 . LEU A 24  ? 0.9709 0.4988 0.5625 -0.0301 0.0987  0.0271  23  LEU A CD1 
124  C CD2 . LEU A 24  ? 0.9044 0.4424 0.5112 -0.0289 0.1021  0.0302  23  LEU A CD2 
125  N N   . VAL A 25  ? 0.8101 0.3218 0.3975 -0.0298 0.0879  0.0059  24  VAL A N   
126  C CA  . VAL A 25  ? 1.0153 0.5273 0.6025 -0.0323 0.0829  0.0036  24  VAL A CA  
127  C C   . VAL A 25  ? 0.9200 0.4241 0.5000 -0.0319 0.0792  -0.0013 24  VAL A C   
128  O O   . VAL A 25  ? 0.9238 0.4262 0.5013 -0.0338 0.0755  -0.0023 24  VAL A O   
129  C CB  . VAL A 25  ? 0.8412 0.3577 0.4352 -0.0319 0.0831  0.0027  24  VAL A CB  
130  C CG1 . VAL A 25  ? 0.7708 0.2964 0.3728 -0.0326 0.0866  0.0087  24  VAL A CG1 
131  C CG2 . VAL A 25  ? 1.0206 0.5323 0.6143 -0.0290 0.0841  -0.0015 24  VAL A CG2 
132  N N   . GLY A 26  ? 0.8352 0.3341 0.4114 -0.0297 0.0802  -0.0043 25  GLY A N   
133  C CA  . GLY A 26  ? 0.9791 0.4718 0.5489 -0.0296 0.0765  -0.0077 25  GLY A CA  
134  C C   . GLY A 26  ? 0.8618 0.3525 0.4266 -0.0310 0.0752  -0.0054 25  GLY A C   
135  O O   . GLY A 26  ? 0.7995 0.2869 0.3613 -0.0318 0.0714  -0.0065 25  GLY A O   
136  N N   . LYS A 27  ? 0.8053 0.2982 0.3697 -0.0312 0.0786  -0.0015 26  LYS A N   
137  C CA  . LYS A 27  ? 0.9034 0.3956 0.4639 -0.0330 0.0774  0.0018  26  LYS A CA  
138  C C   . LYS A 27  ? 0.8785 0.3725 0.4410 -0.0362 0.0742  0.0039  26  LYS A C   
139  O O   . LYS A 27  ? 0.9136 0.4033 0.4722 -0.0379 0.0707  0.0038  26  LYS A O   
140  C CB  . LYS A 27  ? 0.8382 0.3342 0.3989 -0.0322 0.0822  0.0063  26  LYS A CB  
141  C CG  . LYS A 27  ? 0.8491 0.3469 0.4077 -0.0346 0.0812  0.0114  26  LYS A CG  
142  C CD  . LYS A 27  ? 0.8628 0.3547 0.4140 -0.0348 0.0783  0.0096  26  LYS A CD  
143  C CE  . LYS A 27  ? 0.9255 0.4202 0.4747 -0.0364 0.0788  0.0155  26  LYS A CE  
144  N NZ  . LYS A 27  ? 1.0387 0.5370 0.5871 -0.0337 0.0848  0.0179  26  LYS A NZ  
145  N N   . LEU A 28  ? 0.8387 0.3386 0.4071 -0.0375 0.0755  0.0060  27  LEU A N   
146  C CA  . LEU A 28  ? 0.9157 0.4170 0.4848 -0.0414 0.0725  0.0076  27  LEU A CA  
147  C C   . LEU A 28  ? 0.8675 0.3624 0.4336 -0.0413 0.0687  0.0024  27  LEU A C   
148  O O   . LEU A 28  ? 0.8547 0.3450 0.4170 -0.0439 0.0656  0.0024  27  LEU A O   
149  C CB  . LEU A 28  ? 0.9278 0.4377 0.5038 -0.0429 0.0744  0.0107  27  LEU A CB  
150  C CG  . LEU A 28  ? 0.8754 0.3937 0.4557 -0.0444 0.0776  0.0182  27  LEU A CG  
151  C CD1 . LEU A 28  ? 0.8907 0.4087 0.4673 -0.0487 0.0751  0.0224  27  LEU A CD1 
152  C CD2 . LEU A 28  ? 1.0180 0.5376 0.6001 -0.0399 0.0829  0.0194  27  LEU A CD2 
153  N N   . LEU A 29  ? 0.8789 0.3730 0.4467 -0.0382 0.0689  -0.0018 28  LEU A N   
154  C CA  . LEU A 29  ? 0.9332 0.4222 0.4989 -0.0371 0.0659  -0.0061 28  LEU A CA  
155  C C   . LEU A 29  ? 1.0211 0.5028 0.5813 -0.0363 0.0636  -0.0069 28  LEU A C   
156  O O   . LEU A 29  ? 0.9862 0.4626 0.5439 -0.0363 0.0611  -0.0087 28  LEU A O   
157  C CB  . LEU A 29  ? 0.9214 0.4127 0.4909 -0.0341 0.0667  -0.0092 28  LEU A CB  
158  C CG  . LEU A 29  ? 0.9618 0.4504 0.5310 -0.0324 0.0643  -0.0128 28  LEU A CG  
159  C CD1 . LEU A 29  ? 1.0632 0.5547 0.6344 -0.0341 0.0642  -0.0132 28  LEU A CD1 
160  C CD2 . LEU A 29  ? 1.0063 0.4968 0.5785 -0.0296 0.0645  -0.0149 28  LEU A CD2 
161  N N   . ALA A 30  ? 0.9644 0.4456 0.5224 -0.0356 0.0646  -0.0055 29  ALA A N   
162  C CA  . ALA A 30  ? 0.8871 0.3626 0.4401 -0.0351 0.0622  -0.0055 29  ALA A CA  
163  C C   . ALA A 30  ? 0.9899 0.4629 0.5400 -0.0381 0.0609  -0.0019 29  ALA A C   
164  O O   . ALA A 30  ? 1.0140 0.4810 0.5610 -0.0382 0.0581  -0.0019 29  ALA A O   
165  C CB  . ALA A 30  ? 0.8618 0.3380 0.4125 -0.0335 0.0637  -0.0056 29  ALA A CB  
166  N N   . VAL A 31  ? 0.9045 0.3821 0.4561 -0.0407 0.0627  0.0019  30  VAL A N   
167  C CA  . VAL A 31  ? 0.8755 0.3514 0.4245 -0.0444 0.0610  0.0061  30  VAL A CA  
168  C C   . VAL A 31  ? 1.0702 0.5419 0.6184 -0.0475 0.0584  0.0050  30  VAL A C   
169  O O   . VAL A 31  ? 1.0708 0.5359 0.6152 -0.0499 0.0556  0.0061  30  VAL A O   
170  C CB  . VAL A 31  ? 0.8313 0.3150 0.3826 -0.0462 0.0640  0.0115  30  VAL A CB  
171  C CG1 . VAL A 31  ? 0.8218 0.3052 0.3714 -0.0511 0.0617  0.0167  30  VAL A CG1 
172  C CG2 . VAL A 31  ? 0.9008 0.3863 0.4507 -0.0431 0.0668  0.0123  30  VAL A CG2 
173  N N   . SER A 32  ? 1.0633 0.5380 0.6145 -0.0476 0.0592  0.0027  31  SER A N   
174  C CA  . SER A 32  ? 1.1019 0.5727 0.6510 -0.0509 0.0572  0.0013  31  SER A CA  
175  C C   . SER A 32  ? 1.0853 0.5468 0.6312 -0.0481 0.0554  -0.0037 31  SER A C   
176  O O   . SER A 32  ? 1.1442 0.5975 0.6854 -0.0506 0.0534  -0.0047 31  SER A O   
177  C CB  . SER A 32  ? 1.0829 0.5616 0.6363 -0.0523 0.0588  0.0013  31  SER A CB  
178  O OG  . SER A 32  ? 1.0923 0.5804 0.6501 -0.0538 0.0611  0.0066  31  SER A OG  
179  N N   . PHE A 33  ? 0.9922 0.4545 0.5405 -0.0431 0.0564  -0.0067 32  PHE A N   
180  C CA  . PHE A 33  ? 0.9428 0.3987 0.4898 -0.0397 0.0554  -0.0107 32  PHE A CA  
181  C C   . PHE A 33  ? 0.9425 0.3951 0.4891 -0.0360 0.0544  -0.0106 32  PHE A C   
182  O O   . PHE A 33  ? 0.9318 0.3800 0.4783 -0.0325 0.0538  -0.0128 32  PHE A O   
183  C CB  . PHE A 33  ? 1.0151 0.4763 0.5661 -0.0373 0.0570  -0.0139 32  PHE A CB  
184  C CG  . PHE A 33  ? 1.0342 0.5015 0.5868 -0.0411 0.0581  -0.0131 32  PHE A CG  
185  C CD1 . PHE A 33  ? 0.9818 0.4451 0.5305 -0.0442 0.0573  -0.0146 32  PHE A CD1 
186  C CD2 . PHE A 33  ? 0.9782 0.4549 0.5359 -0.0416 0.0600  -0.0107 32  PHE A CD2 
187  C CE1 . PHE A 33  ? 0.9844 0.4544 0.5344 -0.0483 0.0579  -0.0133 32  PHE A CE1 
188  C CE2 . PHE A 33  ? 0.9579 0.4413 0.5181 -0.0450 0.0610  -0.0089 32  PHE A CE2 
189  C CZ  . PHE A 33  ? 1.0245 0.5054 0.5810 -0.0486 0.0596  -0.0100 32  PHE A CZ  
190  N N   . GLY A 34  ? 0.8585 0.3138 0.4048 -0.0364 0.0545  -0.0076 33  GLY A N   
191  C CA  . GLY A 34  ? 0.9010 0.3537 0.4460 -0.0341 0.0530  -0.0066 33  GLY A CA  
192  C C   . GLY A 34  ? 0.8585 0.3136 0.4062 -0.0301 0.0530  -0.0090 33  GLY A C   
193  O O   . GLY A 34  ? 1.0190 0.4785 0.5699 -0.0289 0.0544  -0.0114 33  GLY A O   
194  N N   . PRO A 35  ? 0.9096 0.3624 0.4562 -0.0282 0.0512  -0.0076 34  PRO A N   
195  C CA  . PRO A 35  ? 0.9540 0.4102 0.5034 -0.0249 0.0506  -0.0088 34  PRO A CA  
196  C C   . PRO A 35  ? 0.9666 0.4222 0.5194 -0.0220 0.0511  -0.0113 34  PRO A C   
197  O O   . PRO A 35  ? 1.0004 0.4614 0.5567 -0.0201 0.0512  -0.0125 34  PRO A O   
198  C CB  . PRO A 35  ? 0.8776 0.3314 0.4253 -0.0241 0.0482  -0.0056 34  PRO A CB  
199  C CG  . PRO A 35  ? 0.8376 0.2893 0.3813 -0.0273 0.0481  -0.0030 34  PRO A CG  
200  C CD  . PRO A 35  ? 0.8373 0.2862 0.3806 -0.0294 0.0495  -0.0040 34  PRO A CD  
201  N N   . ALA A 36  ? 0.9604 0.4092 0.5119 -0.0216 0.0513  -0.0120 35  ALA A N   
202  C CA  . ALA A 36  ? 0.9858 0.4338 0.5396 -0.0185 0.0525  -0.0147 35  ALA A CA  
203  C C   . ALA A 36  ? 0.9559 0.4105 0.5121 -0.0197 0.0542  -0.0172 35  ALA A C   
204  O O   . ALA A 36  ? 0.9454 0.4045 0.5053 -0.0169 0.0550  -0.0186 35  ALA A O   
205  C CB  . ALA A 36  ? 1.1280 0.5655 0.6780 -0.0183 0.0529  -0.0157 35  ALA A CB  
206  N N   . GLY A 37  ? 1.0460 0.5023 0.6006 -0.0239 0.0549  -0.0169 36  GLY A N   
207  C CA  . GLY A 37  ? 1.0258 0.4891 0.5835 -0.0252 0.0566  -0.0183 36  GLY A CA  
208  C C   . GLY A 37  ? 1.0523 0.5230 0.6140 -0.0241 0.0569  -0.0180 36  GLY A C   
209  O O   . GLY A 37  ? 0.9980 0.4742 0.5639 -0.0229 0.0578  -0.0193 36  GLY A O   
210  N N   . LEU A 38  ? 0.9606 0.4312 0.5206 -0.0248 0.0563  -0.0163 37  LEU A N   
211  C CA  . LEU A 38  ? 0.9608 0.4365 0.5230 -0.0244 0.0567  -0.0165 37  LEU A CA  
212  C C   . LEU A 38  ? 0.9320 0.4097 0.4969 -0.0216 0.0550  -0.0172 37  LEU A C   
213  O O   . LEU A 38  ? 1.0261 0.5086 0.5941 -0.0215 0.0552  -0.0180 37  LEU A O   
214  C CB  . LEU A 38  ? 1.0298 0.5039 0.5878 -0.0259 0.0566  -0.0149 37  LEU A CB  
215  C CG  . LEU A 38  ? 1.0052 0.4827 0.5635 -0.0269 0.0588  -0.0155 37  LEU A CG  
216  C CD1 . LEU A 38  ? 1.0206 0.5002 0.5804 -0.0285 0.0618  -0.0143 37  LEU A CD1 
217  C CD2 . LEU A 38  ? 0.9506 0.4262 0.5036 -0.0277 0.0583  -0.0148 37  LEU A CD2 
218  N N   . GLY A 39  ? 0.9346 0.4089 0.4989 -0.0194 0.0534  -0.0164 38  GLY A N   
219  C CA  . GLY A 39  ? 0.9271 0.4046 0.4950 -0.0164 0.0519  -0.0158 38  GLY A CA  
220  C C   . GLY A 39  ? 0.9883 0.4693 0.5608 -0.0141 0.0533  -0.0174 38  GLY A C   
221  O O   . GLY A 39  ? 1.0849 0.5721 0.6618 -0.0127 0.0526  -0.0170 38  GLY A O   
222  N N   . LEU A 40  ? 1.0429 0.5199 0.6137 -0.0140 0.0550  -0.0190 39  LEU A N   
223  C CA  . LEU A 40  ? 0.9813 0.4614 0.5552 -0.0119 0.0566  -0.0207 39  LEU A CA  
224  C C   . LEU A 40  ? 0.9301 0.4177 0.5075 -0.0141 0.0576  -0.0215 39  LEU A C   
225  O O   . LEU A 40  ? 0.9550 0.4491 0.5372 -0.0123 0.0580  -0.0217 39  LEU A O   
226  C CB  . LEU A 40  ? 0.9605 0.4330 0.5298 -0.0119 0.0581  -0.0226 39  LEU A CB  
227  C CG  . LEU A 40  ? 0.9340 0.4021 0.5030 -0.0071 0.0591  -0.0233 39  LEU A CG  
228  C CD1 . LEU A 40  ? 0.9394 0.3981 0.5020 -0.0083 0.0606  -0.0261 39  LEU A CD1 
229  C CD2 . LEU A 40  ? 0.8593 0.3359 0.4341 -0.0036 0.0602  -0.0235 39  LEU A CD2 
230  N N   . ALA A 41  ? 1.0191 0.5065 0.5949 -0.0178 0.0581  -0.0214 40  ALA A N   
231  C CA  . ALA A 41  ? 0.9167 0.4109 0.4965 -0.0197 0.0594  -0.0214 40  ALA A CA  
232  C C   . ALA A 41  ? 0.9210 0.4196 0.5045 -0.0194 0.0585  -0.0207 40  ALA A C   
233  O O   . ALA A 41  ? 1.0158 0.5199 0.6036 -0.0203 0.0596  -0.0206 40  ALA A O   
234  C CB  . ALA A 41  ? 0.8293 0.3223 0.4069 -0.0232 0.0608  -0.0205 40  ALA A CB  
235  N N   . ALA A 42  ? 0.9978 0.4940 0.5793 -0.0185 0.0565  -0.0200 41  ALA A N   
236  C CA  . ALA A 42  ? 1.0685 0.5677 0.6516 -0.0194 0.0551  -0.0195 41  ALA A CA  
237  C C   . ALA A 42  ? 1.0177 0.5242 0.6073 -0.0181 0.0545  -0.0191 41  ALA A C   
238  O O   . ALA A 42  ? 1.0657 0.5754 0.6581 -0.0199 0.0545  -0.0191 41  ALA A O   
239  C CB  . ALA A 42  ? 0.9956 0.4918 0.5749 -0.0193 0.0525  -0.0183 41  ALA A CB  
240  N N   . ASN A 43  ? 0.9353 0.4443 0.5275 -0.0150 0.0542  -0.0185 42  ASN A N   
241  C CA  . ASN A 43  ? 0.9746 0.4918 0.5734 -0.0134 0.0539  -0.0174 42  ASN A CA  
242  C C   . ASN A 43  ? 1.0469 0.5683 0.6491 -0.0146 0.0561  -0.0184 42  ASN A C   
243  O O   . ASN A 43  ? 0.9245 0.4526 0.5322 -0.0152 0.0556  -0.0173 42  ASN A O   
244  C CB  . ASN A 43  ? 0.9775 0.4962 0.5779 -0.0089 0.0539  -0.0164 42  ASN A CB  
245  C CG  . ASN A 43  ? 1.0155 0.5352 0.6166 -0.0075 0.0511  -0.0134 42  ASN A CG  
246  O OD1 . ASN A 43  ? 1.0314 0.5532 0.6329 -0.0104 0.0486  -0.0120 42  ASN A OD1 
247  N ND2 . ASN A 43  ? 1.0141 0.5319 0.6150 -0.0033 0.0517  -0.0121 42  ASN A ND2 
248  N N   . PHE A 44  ? 1.1185 0.6364 0.7176 -0.0154 0.0583  -0.0199 43  PHE A N   
249  C CA  . PHE A 44  ? 0.9792 0.5021 0.5816 -0.0170 0.0602  -0.0200 43  PHE A CA  
250  C C   . PHE A 44  ? 0.9573 0.4812 0.5619 -0.0199 0.0607  -0.0191 43  PHE A C   
251  O O   . PHE A 44  ? 0.9179 0.4484 0.5284 -0.0207 0.0615  -0.0180 43  PHE A O   
252  C CB  . PHE A 44  ? 0.9316 0.4508 0.5295 -0.0180 0.0619  -0.0213 43  PHE A CB  
253  C CG  . PHE A 44  ? 0.7973 0.3231 0.3985 -0.0198 0.0636  -0.0208 43  PHE A CG  
254  C CD1 . PHE A 44  ? 0.7633 0.2963 0.3684 -0.0181 0.0640  -0.0208 43  PHE A CD1 
255  C CD2 . PHE A 44  ? 0.8054 0.3315 0.4063 -0.0233 0.0648  -0.0197 43  PHE A CD2 
256  C CE1 . PHE A 44  ? 0.7590 0.2990 0.3670 -0.0202 0.0654  -0.0200 43  PHE A CE1 
257  C CE2 . PHE A 44  ? 0.7885 0.3219 0.3929 -0.0253 0.0661  -0.0184 43  PHE A CE2 
258  C CZ  . PHE A 44  ? 0.7573 0.2977 0.3650 -0.0240 0.0663  -0.0186 43  PHE A CZ  
259  N N   . ARG A 45  ? 1.0037 0.5211 0.6037 -0.0212 0.0607  -0.0195 44  ARG A N   
260  C CA  . ARG A 45  ? 0.9934 0.5101 0.5945 -0.0232 0.0619  -0.0190 44  ARG A CA  
261  C C   . ARG A 45  ? 0.9781 0.4974 0.5827 -0.0235 0.0601  -0.0187 44  ARG A C   
262  O O   . ARG A 45  ? 1.0191 0.5391 0.6267 -0.0250 0.0614  -0.0182 44  ARG A O   
263  C CB  . ARG A 45  ? 1.0474 0.5564 0.6415 -0.0241 0.0623  -0.0196 44  ARG A CB  
264  C CG  . ARG A 45  ? 1.1379 0.6459 0.7317 -0.0255 0.0656  -0.0186 44  ARG A CG  
265  C CD  . ARG A 45  ? 1.2857 0.7873 0.8725 -0.0259 0.0660  -0.0187 44  ARG A CD  
266  N NE  . ARG A 45  ? 1.4259 0.9263 1.0123 -0.0267 0.0695  -0.0173 44  ARG A NE  
267  C CZ  . ARG A 45  ? 1.3453 0.8416 0.9263 -0.0271 0.0707  -0.0167 44  ARG A CZ  
268  N NH1 . ARG A 45  ? 1.2862 0.7788 0.8618 -0.0272 0.0683  -0.0171 44  ARG A NH1 
269  N NH2 . ARG A 45  ? 1.1343 0.6304 0.7158 -0.0271 0.0747  -0.0150 44  ARG A NH2 
270  N N   . GLN A 46  ? 0.8593 0.3800 0.4638 -0.0223 0.0572  -0.0185 45  GLN A N   
271  C CA  . GLN A 46  ? 0.9296 0.4538 0.5377 -0.0233 0.0548  -0.0175 45  GLN A CA  
272  C C   . GLN A 46  ? 1.0140 0.5467 0.6304 -0.0231 0.0555  -0.0159 45  GLN A C   
273  O O   . GLN A 46  ? 0.8848 0.4190 0.5047 -0.0251 0.0550  -0.0151 45  GLN A O   
274  C CB  . GLN A 46  ? 0.8360 0.3615 0.4429 -0.0220 0.0515  -0.0163 45  GLN A CB  
275  C CG  . GLN A 46  ? 1.0995 0.6282 0.7087 -0.0243 0.0481  -0.0147 45  GLN A CG  
276  C CD  . GLN A 46  ? 1.0805 0.6017 0.6821 -0.0274 0.0464  -0.0158 45  GLN A CD  
277  O OE1 . GLN A 46  ? 1.0834 0.5975 0.6798 -0.0287 0.0488  -0.0182 45  GLN A OE1 
278  N NE2 . GLN A 46  ? 1.0709 0.5944 0.6716 -0.0287 0.0425  -0.0138 45  GLN A NE2 
279  N N   . LEU A 47  ? 0.9571 0.4952 0.5762 -0.0207 0.0565  -0.0154 46  LEU A N   
280  C CA  . LEU A 47  ? 0.8256 0.3729 0.4522 -0.0204 0.0572  -0.0136 46  LEU A CA  
281  C C   . LEU A 47  ? 0.8785 0.4264 0.5082 -0.0227 0.0596  -0.0131 46  LEU A C   
282  O O   . LEU A 47  ? 0.9143 0.4686 0.5510 -0.0237 0.0595  -0.0109 46  LEU A O   
283  C CB  . LEU A 47  ? 0.8736 0.4251 0.5003 -0.0176 0.0585  -0.0140 46  LEU A CB  
284  C CG  . LEU A 47  ? 0.9553 0.5172 0.5888 -0.0174 0.0597  -0.0122 46  LEU A CG  
285  C CD1 . LEU A 47  ? 0.8758 0.4459 0.5159 -0.0163 0.0575  -0.0094 46  LEU A CD1 
286  C CD2 . LEU A 47  ? 0.7666 0.3295 0.3968 -0.0154 0.0617  -0.0137 46  LEU A CD2 
287  N N   . ILE A 48  ? 0.7960 0.3377 0.4212 -0.0236 0.0617  -0.0142 47  ILE A N   
288  C CA  . ILE A 48  ? 0.7842 0.3268 0.4129 -0.0252 0.0645  -0.0128 47  ILE A CA  
289  C C   . ILE A 48  ? 0.9898 0.5291 0.6205 -0.0266 0.0643  -0.0124 47  ILE A C   
290  O O   . ILE A 48  ? 0.9695 0.5133 0.6072 -0.0274 0.0653  -0.0102 47  ILE A O   
291  C CB  . ILE A 48  ? 0.8150 0.3520 0.4382 -0.0257 0.0667  -0.0134 47  ILE A CB  
292  C CG1 . ILE A 48  ? 0.9350 0.4759 0.5573 -0.0256 0.0672  -0.0132 47  ILE A CG1 
293  C CG2 . ILE A 48  ? 0.9102 0.4465 0.5367 -0.0268 0.0699  -0.0114 47  ILE A CG2 
294  C CD1 . ILE A 48  ? 0.9492 0.4875 0.5685 -0.0271 0.0693  -0.0122 47  ILE A CD1 
295  N N   . THR A 49  ? 1.0060 0.5369 0.6301 -0.0271 0.0631  -0.0146 48  THR A N   
296  C CA  . THR A 49  ? 0.9762 0.5015 0.5998 -0.0291 0.0630  -0.0152 48  THR A CA  
297  C C   . THR A 49  ? 0.9757 0.5070 0.6058 -0.0303 0.0601  -0.0134 48  THR A C   
298  O O   . THR A 49  ? 0.9138 0.4433 0.5473 -0.0320 0.0609  -0.0126 48  THR A O   
299  C CB  . THR A 49  ? 0.9647 0.4807 0.5786 -0.0300 0.0616  -0.0180 48  THR A CB  
300  O OG1 . THR A 49  ? 1.0482 0.5673 0.6606 -0.0296 0.0575  -0.0179 48  THR A OG1 
301  C CG2 . THR A 49  ? 0.8919 0.4026 0.5000 -0.0289 0.0646  -0.0191 48  THR A CG2 
302  N N   . VAL A 50  ? 0.9710 0.5094 0.6032 -0.0293 0.0571  -0.0124 49  VAL A N   
303  C CA  . VAL A 50  ? 1.0162 0.5625 0.6556 -0.0303 0.0544  -0.0097 49  VAL A CA  
304  C C   . VAL A 50  ? 1.0714 0.6254 0.7196 -0.0300 0.0566  -0.0070 49  VAL A C   
305  O O   . VAL A 50  ? 1.0844 0.6411 0.7386 -0.0320 0.0557  -0.0048 49  VAL A O   
306  C CB  . VAL A 50  ? 0.9930 0.5463 0.6331 -0.0282 0.0515  -0.0085 49  VAL A CB  
307  C CG1 . VAL A 50  ? 0.9664 0.5318 0.6159 -0.0279 0.0502  -0.0048 49  VAL A CG1 
308  C CG2 . VAL A 50  ? 1.0426 0.5909 0.6769 -0.0298 0.0479  -0.0091 49  VAL A CG2 
309  N N   . LEU A 51  ? 0.9995 0.5573 0.6486 -0.0281 0.0594  -0.0068 50  LEU A N   
310  C CA  . LEU A 51  ? 1.0394 0.6056 0.6967 -0.0284 0.0615  -0.0037 50  LEU A CA  
311  C C   . LEU A 51  ? 1.1252 0.6865 0.7854 -0.0300 0.0639  -0.0026 50  LEU A C   
312  O O   . LEU A 51  ? 1.1360 0.7025 0.8044 -0.0311 0.0640  0.0007  50  LEU A O   
313  C CB  . LEU A 51  ? 0.9398 0.5099 0.5955 -0.0270 0.0637  -0.0039 50  LEU A CB  
314  C CG  . LEU A 51  ? 0.9334 0.5090 0.5872 -0.0249 0.0623  -0.0048 50  LEU A CG  
315  C CD1 . LEU A 51  ? 0.8264 0.4025 0.4761 -0.0246 0.0645  -0.0059 50  LEU A CD1 
316  C CD2 . LEU A 51  ? 0.9891 0.5763 0.6509 -0.0246 0.0610  -0.0017 50  LEU A CD2 
317  N N   . GLY A 52  ? 1.0149 0.5658 0.6686 -0.0299 0.0662  -0.0049 51  GLY A N   
318  C CA  . GLY A 52  ? 1.0703 0.6142 0.7255 -0.0307 0.0691  -0.0043 51  GLY A CA  
319  C C   . GLY A 52  ? 1.1243 0.6636 0.7805 -0.0329 0.0668  -0.0047 51  GLY A C   
320  O O   . GLY A 52  ? 1.1290 0.6647 0.7895 -0.0337 0.0691  -0.0032 51  GLY A O   
321  N N   . VAL A 53  ? 1.0938 0.6332 0.7464 -0.0342 0.0623  -0.0062 52  VAL A N   
322  C CA  . VAL A 53  ? 1.0365 0.5726 0.6899 -0.0374 0.0591  -0.0061 52  VAL A CA  
323  C C   . VAL A 53  ? 1.1573 0.7058 0.8215 -0.0382 0.0567  -0.0015 52  VAL A C   
324  O O   . VAL A 53  ? 1.1330 0.6796 0.8011 -0.0411 0.0552  0.0001  52  VAL A O   
325  C CB  . VAL A 53  ? 1.0428 0.5740 0.6871 -0.0389 0.0550  -0.0089 52  VAL A CB  
326  C CG1 . VAL A 53  ? 1.0900 0.6238 0.7368 -0.0427 0.0499  -0.0071 52  VAL A CG1 
327  C CG2 . VAL A 53  ? 0.9346 0.4515 0.5680 -0.0397 0.0571  -0.0133 52  VAL A CG2 
328  N N   . LEU A 54  ? 1.1754 0.7364 0.8445 -0.0358 0.0565  0.0007  53  LEU A N   
329  C CA  . LEU A 54  ? 1.1041 0.6781 0.7821 -0.0363 0.0538  0.0050  53  LEU A CA  
330  C C   . LEU A 54  ? 1.2018 0.7882 0.8877 -0.0343 0.0562  0.0083  53  LEU A C   
331  O O   . LEU A 54  ? 1.2374 0.8348 0.9318 -0.0350 0.0546  0.0124  53  LEU A O   
332  C CB  . LEU A 54  ? 1.0357 0.6144 0.7108 -0.0355 0.0500  0.0047  53  LEU A CB  
333  C CG  . LEU A 54  ? 1.0745 0.6658 0.7577 -0.0362 0.0465  0.0093  53  LEU A CG  
334  C CD1 . LEU A 54  ? 1.0695 0.6566 0.7541 -0.0410 0.0427  0.0109  53  LEU A CD1 
335  C CD2 . LEU A 54  ? 1.1143 0.7120 0.7952 -0.0332 0.0448  0.0095  53  LEU A CD2 
336  N N   . ALA A 55  ? 1.3392 0.9248 1.0225 -0.0325 0.0598  0.0070  54  ALA A N   
337  C CA  . ALA A 55  ? 1.3239 0.9219 1.0130 -0.0314 0.0615  0.0100  54  ALA A CA  
338  C C   . ALA A 55  ? 1.3387 0.9446 1.0390 -0.0331 0.0621  0.0153  54  ALA A C   
339  O O   . ALA A 55  ? 1.3350 0.9543 1.0419 -0.0330 0.0616  0.0189  54  ALA A O   
340  C CB  . ALA A 55  ? 1.2915 0.8865 0.9757 -0.0304 0.0648  0.0083  54  ALA A CB  
341  N N   . GLY A 56  ? 1.3566 0.9542 1.0592 -0.0345 0.0635  0.0161  55  GLY A N   
342  C CA  . GLY A 56  ? 1.2100 0.8136 0.9237 -0.0360 0.0640  0.0215  55  GLY A CA  
343  C C   . GLY A 56  ? 1.1627 0.7642 0.8793 -0.0384 0.0603  0.0225  55  GLY A C   
344  O O   . GLY A 56  ? 1.0572 0.6533 0.7788 -0.0403 0.0609  0.0247  55  GLY A O   
345  N N   . ALA A 57  ? 1.2085 0.8140 0.9221 -0.0386 0.0564  0.0213  56  ALA A N   
346  C CA  . ALA A 57  ? 1.1803 0.7852 0.8956 -0.0414 0.0518  0.0226  56  ALA A CA  
347  C C   . ALA A 57  ? 1.2221 0.8094 0.9296 -0.0440 0.0510  0.0186  56  ALA A C   
348  O O   . ALA A 57  ? 1.0651 0.6499 0.7730 -0.0476 0.0470  0.0196  56  ALA A O   
349  C CB  . ALA A 57  ? 0.9829 0.5982 0.7107 -0.0435 0.0506  0.0291  56  ALA A CB  
350  N N   . GLY A 58  ? 1.3228 0.8981 1.0228 -0.0426 0.0548  0.0144  57  GLY A N   
351  C CA  . GLY A 58  ? 1.3360 0.8941 1.0269 -0.0448 0.0546  0.0100  57  GLY A CA  
352  C C   . GLY A 58  ? 1.3599 0.9102 1.0546 -0.0483 0.0543  0.0116  57  GLY A C   
353  O O   . GLY A 58  ? 1.3889 0.9286 1.0770 -0.0522 0.0513  0.0091  57  GLY A O   
354  N N   . ILE A 59  ? 1.3412 0.8962 1.0462 -0.0474 0.0574  0.0161  58  ILE A N   
355  C CA  . ILE A 59  ? 1.2650 0.8120 0.9749 -0.0503 0.0577  0.0182  58  ILE A CA  
356  C C   . ILE A 59  ? 1.3067 0.8388 1.0135 -0.0483 0.0641  0.0159  58  ILE A C   
357  O O   . ILE A 59  ? 1.3001 0.8229 1.0103 -0.0501 0.0655  0.0173  58  ILE A O   
358  C CB  . ILE A 59  ? 1.1315 0.6941 0.8565 -0.0508 0.0567  0.0258  58  ILE A CB  
359  C CG1 . ILE A 59  ? 1.0422 0.6150 0.7743 -0.0466 0.0617  0.0291  58  ILE A CG1 
360  C CG2 . ILE A 59  ? 1.0095 0.5871 0.7377 -0.0524 0.0508  0.0285  58  ILE A CG2 
361  C CD1 . ILE A 59  ? 0.9561 0.5462 0.7025 -0.0470 0.0607  0.0369  58  ILE A CD1 
362  N N   . PHE A 60  ? 1.5912 1.1203 1.2915 -0.0447 0.0681  0.0127  59  PHE A N   
363  C CA  . PHE A 60  ? 1.5823 1.1017 1.2825 -0.0415 0.0751  0.0125  59  PHE A CA  
364  C C   . PHE A 60  ? 1.5802 1.0784 1.2720 -0.0433 0.0769  0.0081  59  PHE A C   
365  O O   . PHE A 60  ? 1.5739 1.0638 1.2698 -0.0416 0.0823  0.0099  59  PHE A O   
366  C CB  . PHE A 60  ? 1.5828 1.1039 1.2769 -0.0379 0.0781  0.0102  59  PHE A CB  
367  C CG  . PHE A 60  ? 1.6223 1.1614 1.3209 -0.0369 0.0757  0.0129  59  PHE A CG  
368  C CD1 . PHE A 60  ? 1.5419 1.0954 1.2529 -0.0359 0.0771  0.0194  59  PHE A CD1 
369  C CD2 . PHE A 60  ? 1.6733 1.2146 1.3636 -0.0371 0.0723  0.0090  59  PHE A CD2 
370  C CE1 . PHE A 60  ? 1.5377 1.1066 1.2512 -0.0354 0.0751  0.0212  59  PHE A CE1 
371  C CE2 . PHE A 60  ? 1.5632 1.1190 1.2567 -0.0360 0.0706  0.0110  59  PHE A CE2 
372  C CZ  . PHE A 60  ? 1.5566 1.1258 1.2610 -0.0353 0.0721  0.0167  59  PHE A CZ  
373  N N   . ASN A 61  ? 1.4225 0.9114 1.1021 -0.0468 0.0728  0.0024  60  ASN A N   
374  C CA  . ASN A 61  ? 1.3536 0.8217 1.0238 -0.0497 0.0740  -0.0022 60  ASN A CA  
375  C C   . ASN A 61  ? 1.3068 0.7722 0.9845 -0.0537 0.0716  0.0011  60  ASN A C   
376  O O   . ASN A 61  ? 1.2002 0.6488 0.8752 -0.0544 0.0754  -0.0006 60  ASN A O   
377  C CB  . ASN A 61  ? 1.2368 0.6970 0.8917 -0.0533 0.0696  -0.0086 60  ASN A CB  
378  C CG  . ASN A 61  ? 1.3307 0.7829 0.9744 -0.0498 0.0743  -0.0135 60  ASN A CG  
379  O OD1 . ASN A 61  ? 1.3190 0.7808 0.9609 -0.0478 0.0730  -0.0138 60  ASN A OD1 
380  N ND2 . ASN A 61  ? 1.3850 0.8193 1.0212 -0.0488 0.0800  -0.0173 60  ASN A ND2 
381  N N   . GLY A 62  ? 1.2519 0.7331 0.9390 -0.0564 0.0656  0.0060  61  GLY A N   
382  C CA  . GLY A 62  ? 1.1548 0.6366 0.8519 -0.0598 0.0636  0.0109  61  GLY A CA  
383  C C   . GLY A 62  ? 1.1902 0.6764 0.9007 -0.0554 0.0696  0.0167  61  GLY A C   
384  O O   . GLY A 62  ? 1.1662 0.6457 0.8831 -0.0573 0.0705  0.0198  61  GLY A O   
385  N N   . VAL A 63  ? 1.2649 0.7627 0.9799 -0.0500 0.0737  0.0188  62  VAL A N   
386  C CA  . VAL A 63  ? 1.1399 0.6429 0.8675 -0.0459 0.0796  0.0250  62  VAL A CA  
387  C C   . VAL A 63  ? 1.0735 0.5559 0.7966 -0.0434 0.0869  0.0224  62  VAL A C   
388  O O   . VAL A 63  ? 1.0975 0.5740 0.8289 -0.0432 0.0898  0.0265  62  VAL A O   
389  C CB  . VAL A 63  ? 1.1557 0.6759 0.8876 -0.0417 0.0816  0.0278  62  VAL A CB  
390  C CG1 . VAL A 63  ? 0.9934 0.5183 0.7373 -0.0377 0.0881  0.0346  62  VAL A CG1 
391  C CG2 . VAL A 63  ? 1.1149 0.6554 0.8525 -0.0436 0.0755  0.0311  62  VAL A CG2 
392  N N   . THR A 64  ? 1.2002 0.6711 0.9100 -0.0411 0.0902  0.0159  63  THR A N   
393  C CA  . THR A 64  ? 1.2031 0.6545 0.9076 -0.0378 0.0981  0.0132  63  THR A CA  
394  C C   . THR A 64  ? 1.1113 0.5418 0.8095 -0.0420 0.0975  0.0094  63  THR A C   
395  O O   . THR A 64  ? 1.0579 0.4731 0.7564 -0.0391 0.1045  0.0093  63  THR A O   
396  C CB  . THR A 64  ? 1.1186 0.5629 0.8091 -0.0350 0.1012  0.0068  63  THR A CB  
397  O OG1 . THR A 64  ? 1.1964 0.6230 0.8823 -0.0309 0.1099  0.0047  63  THR A OG1 
398  C CG2 . THR A 64  ? 1.1251 0.5618 0.8002 -0.0402 0.0948  -0.0009 63  THR A CG2 
399  N N   . LYS A 65  ? 1.1109 0.5404 0.8036 -0.0488 0.0893  0.0067  64  LYS A N   
400  C CA  . LYS A 65  ? 1.0683 0.4781 0.7546 -0.0543 0.0876  0.0033  64  LYS A CA  
401  C C   . LYS A 65  ? 1.0861 0.4988 0.7882 -0.0551 0.0879  0.0109  64  LYS A C   
402  O O   . LYS A 65  ? 1.1881 0.5832 0.8905 -0.0538 0.0936  0.0106  64  LYS A O   
403  C CB  . LYS A 65  ? 1.0797 0.4896 0.7559 -0.0620 0.0781  -0.0007 64  LYS A CB  
404  C CG  . LYS A 65  ? 1.3327 0.7275 1.0054 -0.0696 0.0740  -0.0019 64  LYS A CG  
405  C CD  . LYS A 65  ? 1.3811 0.7812 1.0471 -0.0776 0.0638  -0.0034 64  LYS A CD  
406  C CE  . LYS A 65  ? 1.4458 0.8316 1.1087 -0.0861 0.0591  -0.0037 64  LYS A CE  
407  N NZ  . LYS A 65  ? 1.5606 0.9525 1.2173 -0.0945 0.0488  -0.0042 64  LYS A NZ  
408  N N   . TYR A 66  ? 1.1323 0.5669 0.8477 -0.0570 0.0821  0.0179  65  TYR A N   
409  C CA  . TYR A 66  ? 1.1068 0.5466 0.8380 -0.0583 0.0815  0.0260  65  TYR A CA  
410  C C   . TYR A 66  ? 1.0097 0.4531 0.7538 -0.0513 0.0900  0.0322  65  TYR A C   
411  O O   . TYR A 66  ? 0.9584 0.3987 0.7138 -0.0516 0.0918  0.0380  65  TYR A O   
412  C CB  . TYR A 66  ? 0.9968 0.4611 0.7385 -0.0618 0.0734  0.0321  65  TYR A CB  
413  C CG  . TYR A 66  ? 1.1184 0.5796 0.8517 -0.0696 0.0647  0.0289  65  TYR A CG  
414  C CD1 . TYR A 66  ? 1.2265 0.6674 0.9535 -0.0757 0.0626  0.0262  65  TYR A CD1 
415  C CD2 . TYR A 66  ? 1.1280 0.6060 0.8593 -0.0711 0.0585  0.0287  65  TYR A CD2 
416  C CE1 . TYR A 66  ? 1.3431 0.7821 1.0624 -0.0837 0.0541  0.0241  65  TYR A CE1 
417  C CE2 . TYR A 66  ? 1.2672 0.7439 0.9918 -0.0783 0.0505  0.0270  65  TYR A CE2 
418  C CZ  . TYR A 66  ? 1.4647 0.9226 1.1835 -0.0849 0.0480  0.0249  65  TYR A CZ  
419  O OH  . TYR A 66  ? 1.6022 1.0598 1.3144 -0.0928 0.0395  0.0240  65  TYR A OH  
420  N N   . VAL A 67  ? 0.9660 0.4165 0.7093 -0.0452 0.0951  0.0319  66  VAL A N   
421  C CA  . VAL A 67  ? 0.9046 0.3585 0.6596 -0.0385 0.1035  0.0383  66  VAL A CA  
422  C C   . VAL A 67  ? 0.9614 0.3890 0.7110 -0.0358 0.1113  0.0352  66  VAL A C   
423  O O   . VAL A 67  ? 1.0249 0.4499 0.7870 -0.0330 0.1164  0.0418  66  VAL A O   
424  C CB  . VAL A 67  ? 0.9480 0.4154 0.7020 -0.0335 0.1065  0.0387  66  VAL A CB  
425  C CG1 . VAL A 67  ? 0.8456 0.3068 0.6041 -0.0266 0.1166  0.0419  66  VAL A CG1 
426  C CG2 . VAL A 67  ? 0.8262 0.3214 0.5926 -0.0344 0.1019  0.0459  66  VAL A CG2 
427  N N   . ALA A 68  ? 1.0830 0.4907 0.8139 -0.0365 0.1127  0.0252  67  ALA A N   
428  C CA  . ALA A 68  ? 1.0485 0.4288 0.7715 -0.0341 0.1204  0.0208  67  ALA A CA  
429  C C   . ALA A 68  ? 1.0355 0.4020 0.7611 -0.0396 0.1177  0.0216  67  ALA A C   
430  O O   . ALA A 68  ? 0.9682 0.3179 0.6971 -0.0364 0.1249  0.0230  67  ALA A O   
431  C CB  . ALA A 68  ? 1.0978 0.4610 0.7987 -0.0348 0.1214  0.0095  67  ALA A CB  
432  N N   . GLN A 69  ? 0.9790 0.3522 0.7035 -0.0477 0.1073  0.0211  68  GLN A N   
433  C CA  . GLN A 69  ? 1.0457 0.4076 0.7732 -0.0541 0.1035  0.0226  68  GLN A CA  
434  C C   . GLN A 69  ? 0.9330 0.3043 0.6822 -0.0508 0.1068  0.0338  68  GLN A C   
435  O O   . GLN A 69  ? 0.9970 0.3503 0.7488 -0.0518 0.1098  0.0350  68  GLN A O   
436  C CB  . GLN A 69  ? 1.0279 0.4008 0.7527 -0.0631 0.0915  0.0220  68  GLN A CB  
437  C CG  . GLN A 69  ? 1.1785 0.5361 0.8814 -0.0689 0.0870  0.0114  68  GLN A CG  
438  C CD  . GLN A 69  ? 1.3041 0.6660 1.0056 -0.0791 0.0758  0.0122  68  GLN A CD  
439  O OE1 . GLN A 69  ? 1.1018 0.4760 0.8183 -0.0818 0.0716  0.0203  68  GLN A OE1 
440  N NE2 . GLN A 69  ? 1.4750 0.8280 1.1588 -0.0849 0.0706  0.0044  68  GLN A NE2 
441  N N   . TYR A 70  ? 1.0218 0.4209 0.7863 -0.0472 0.1063  0.0422  69  TYR A N   
442  C CA  . TYR A 70  ? 0.9863 0.3995 0.7725 -0.0452 0.1078  0.0540  69  TYR A CA  
443  C C   . TYR A 70  ? 0.9419 0.3649 0.7389 -0.0362 0.1169  0.0604  69  TYR A C   
444  O O   . TYR A 70  ? 1.0193 0.4618 0.8350 -0.0345 0.1173  0.0712  69  TYR A O   
445  C CB  . TYR A 70  ? 0.9947 0.4349 0.7914 -0.0502 0.0983  0.0602  69  TYR A CB  
446  C CG  . TYR A 70  ? 0.9779 0.4124 0.7664 -0.0593 0.0889  0.0561  69  TYR A CG  
447  C CD1 . TYR A 70  ? 1.0519 0.4650 0.8379 -0.0642 0.0878  0.0549  69  TYR A CD1 
448  C CD2 . TYR A 70  ? 1.0610 0.5114 0.8442 -0.0629 0.0810  0.0538  69  TYR A CD2 
449  C CE1 . TYR A 70  ? 1.1470 0.5560 0.9257 -0.0734 0.0786  0.0519  69  TYR A CE1 
450  C CE2 . TYR A 70  ? 1.0667 0.5138 0.8434 -0.0712 0.0723  0.0512  69  TYR A CE2 
451  C CZ  . TYR A 70  ? 1.0372 0.4642 0.8117 -0.0767 0.0708  0.0505  69  TYR A CZ  
452  O OH  . TYR A 70  ? 1.1725 0.5971 0.9406 -0.0858 0.0616  0.0487  69  TYR A OH  
453  N N   . HIS A 71  ? 0.9740 0.3850 0.7599 -0.0307 0.1241  0.0544  70  HIS A N   
454  C CA  . HIS A 71  ? 1.0339 0.4538 0.8303 -0.0222 0.1330  0.0612  70  HIS A CA  
455  C C   . HIS A 71  ? 1.0811 0.4934 0.8924 -0.0181 0.1403  0.0697  70  HIS A C   
456  O O   . HIS A 71  ? 1.1136 0.5385 0.9385 -0.0116 0.1468  0.0786  70  HIS A O   
457  C CB  . HIS A 71  ? 1.0255 0.4321 0.8064 -0.0172 0.1396  0.0532  70  HIS A CB  
458  C CG  . HIS A 71  ? 1.1952 0.5737 0.9705 -0.0124 0.1495  0.0500  70  HIS A CG  
459  N ND1 . HIS A 71  ? 1.1675 0.5185 0.9281 -0.0167 0.1486  0.0409  70  HIS A ND1 
460  C CD2 . HIS A 71  ? 1.1788 0.5523 0.9608 -0.0037 0.1607  0.0549  70  HIS A CD2 
461  C CE1 . HIS A 71  ? 1.2335 0.5623 0.9911 -0.0106 0.1592  0.0395  70  HIS A CE1 
462  N NE2 . HIS A 71  ? 1.1813 0.5236 0.9524 -0.0022 0.1670  0.0482  70  HIS A NE2 
463  N N   . ASP A 72  ? 1.1595 0.5516 0.9688 -0.0218 0.1394  0.0676  71  ASP A N   
464  C CA  . ASP A 72  ? 1.1545 0.5365 0.9776 -0.0181 0.1463  0.0753  71  ASP A CA  
465  C C   . ASP A 72  ? 1.0925 0.4907 0.9340 -0.0228 0.1400  0.0856  71  ASP A C   
466  O O   . ASP A 72  ? 1.2280 0.6220 1.0842 -0.0197 0.1453  0.0942  71  ASP A O   
467  C CB  . ASP A 72  ? 1.2236 0.5684 1.0315 -0.0187 0.1509  0.0660  71  ASP A CB  
468  C CG  . ASP A 72  ? 1.4130 0.7406 1.2150 -0.0092 0.1637  0.0633  71  ASP A CG  
469  O OD1 . ASP A 72  ? 1.3671 0.7129 1.1795 -0.0020 0.1691  0.0703  71  ASP A OD1 
470  O OD2 . ASP A 72  ? 1.4848 0.7810 1.2714 -0.0090 0.1685  0.0542  71  ASP A OD2 
471  N N   . ASN A 73  ? 1.1139 0.5303 0.9552 -0.0301 0.1291  0.0854  72  ASN A N   
472  C CA  . ASN A 73  ? 1.2141 0.6487 1.0723 -0.0349 0.1224  0.0953  72  ASN A CA  
473  C C   . ASN A 73  ? 1.1902 0.6598 1.0605 -0.0334 0.1198  0.1033  72  ASN A C   
474  O O   . ASN A 73  ? 1.0322 0.5160 0.8954 -0.0374 0.1125  0.0993  72  ASN A O   
475  C CB  . ASN A 73  ? 1.1129 0.5417 0.9620 -0.0446 0.1120  0.0897  72  ASN A CB  
476  C CG  . ASN A 73  ? 1.2753 0.6687 1.1066 -0.0475 0.1136  0.0791  72  ASN A CG  
477  O OD1 . ASN A 73  ? 1.3893 0.7610 1.2144 -0.0418 0.1229  0.0751  72  ASN A OD1 
478  N ND2 . ASN A 73  ? 1.2256 0.6133 1.0483 -0.0567 0.1043  0.0745  72  ASN A ND2 
479  N N   . PRO A 74  ? 1.3467 0.8308 1.2347 -0.0280 0.1256  0.1147  73  PRO A N   
480  C CA  . PRO A 74  ? 1.3355 0.8524 1.2335 -0.0273 0.1231  0.1222  73  PRO A CA  
481  C C   . PRO A 74  ? 1.2652 0.8034 1.1663 -0.0344 0.1126  0.1240  73  PRO A C   
482  O O   . PRO A 74  ? 1.2367 0.7963 1.1365 -0.0348 0.1093  0.1242  73  PRO A O   
483  C CB  . PRO A 74  ? 1.3238 0.8508 1.2432 -0.0222 0.1299  0.1362  73  PRO A CB  
484  C CG  . PRO A 74  ? 1.2973 0.7940 1.2152 -0.0178 0.1384  0.1344  73  PRO A CG  
485  C CD  . PRO A 74  ? 1.3187 0.7873 1.2147 -0.0211 0.1362  0.1197  73  PRO A CD  
486  N N   . GLN A 75  ? 1.1490 0.6817 1.0539 -0.0399 0.1073  0.1256  74  GLN A N   
487  C CA  . GLN A 75  ? 1.0922 0.6454 0.9998 -0.0464 0.0976  0.1276  74  GLN A CA  
488  C C   . GLN A 75  ? 0.9821 0.5313 0.8704 -0.0495 0.0920  0.1157  74  GLN A C   
489  O O   . GLN A 75  ? 1.0505 0.6204 0.9370 -0.0501 0.0882  0.1153  74  GLN A O   
490  C CB  . GLN A 75  ? 1.0094 0.5577 0.9265 -0.0517 0.0932  0.1331  74  GLN A CB  
491  C CG  . GLN A 75  ? 0.9470 0.5205 0.8706 -0.0577 0.0839  0.1380  74  GLN A CG  
492  C CD  . GLN A 75  ? 1.0704 0.6360 0.9987 -0.0644 0.0782  0.1409  74  GLN A CD  
493  O OE1 . GLN A 75  ? 1.2864 0.8262 1.2128 -0.0651 0.0810  0.1391  74  GLN A OE1 
494  N NE2 . GLN A 75  ? 0.9978 0.5851 0.9318 -0.0695 0.0701  0.1456  74  GLN A NE2 
495  N N   . GLN A 76  ? 0.9699 0.4921 0.8432 -0.0516 0.0917  0.1059  75  GLN A N   
496  C CA  . GLN A 76  ? 0.9919 0.5099 0.8472 -0.0550 0.0863  0.0952  75  GLN A CA  
497  C C   . GLN A 76  ? 1.0507 0.5716 0.8959 -0.0498 0.0903  0.0893  75  GLN A C   
498  O O   . GLN A 76  ? 0.9223 0.4495 0.7567 -0.0518 0.0854  0.0832  75  GLN A O   
499  C CB  . GLN A 76  ? 0.9197 0.4079 0.7610 -0.0592 0.0850  0.0867  75  GLN A CB  
500  C CG  . GLN A 76  ? 1.0415 0.5290 0.8883 -0.0671 0.0775  0.0905  75  GLN A CG  
501  C CD  . GLN A 76  ? 1.0329 0.5367 0.8752 -0.0728 0.0678  0.0889  75  GLN A CD  
502  O OE1 . GLN A 76  ? 1.0201 0.5311 0.8524 -0.0711 0.0667  0.0832  75  GLN A OE1 
503  N NE2 . GLN A 76  ? 1.1436 0.6535 0.9936 -0.0794 0.0608  0.0946  75  GLN A NE2 
504  N N   . LEU A 77  ? 1.0085 0.5251 0.8573 -0.0432 0.0990  0.0915  76  LEU A N   
505  C CA  . LEU A 77  ? 0.9238 0.4450 0.7643 -0.0386 0.1026  0.0872  76  LEU A CA  
506  C C   . LEU A 77  ? 1.0606 0.6119 0.9088 -0.0388 0.0991  0.0928  76  LEU A C   
507  O O   . LEU A 77  ? 1.1129 0.6702 0.9509 -0.0381 0.0976  0.0872  76  LEU A O   
508  C CB  . LEU A 77  ? 0.8865 0.3966 0.7301 -0.0315 0.1130  0.0894  76  LEU A CB  
509  C CG  . LEU A 77  ? 0.9629 0.4748 0.7975 -0.0267 0.1174  0.0852  76  LEU A CG  
510  C CD1 . LEU A 77  ? 0.8144 0.3097 0.6276 -0.0288 0.1149  0.0721  76  LEU A CD1 
511  C CD2 . LEU A 77  ? 0.9358 0.4390 0.7764 -0.0194 0.1281  0.0896  76  LEU A CD2 
512  N N   . ARG A 78  ? 0.9924 0.5625 0.8580 -0.0398 0.0977  0.1037  77  ARG A N   
513  C CA  . ARG A 78  ? 0.9921 0.5906 0.8638 -0.0407 0.0941  0.1087  77  ARG A CA  
514  C C   . ARG A 78  ? 0.9636 0.5700 0.8280 -0.0457 0.0857  0.1040  77  ARG A C   
515  O O   . ARG A 78  ? 1.0287 0.6504 0.8886 -0.0457 0.0833  0.1022  77  ARG A O   
516  C CB  . ARG A 78  ? 1.0149 0.6320 0.9071 -0.0407 0.0952  0.1222  77  ARG A CB  
517  C CG  . ARG A 78  ? 1.0381 0.6849 0.9363 -0.0422 0.0916  0.1277  77  ARG A CG  
518  C CD  . ARG A 78  ? 1.1278 0.7900 1.0394 -0.0391 0.0969  0.1381  77  ARG A CD  
519  N NE  . ARG A 78  ? 1.2273 0.8913 1.1566 -0.0389 0.0992  0.1491  77  ARG A NE  
520  C CZ  . ARG A 78  ? 1.2459 0.9198 1.1892 -0.0358 0.1045  0.1597  77  ARG A CZ  
521  N NH1 . ARG A 78  ? 1.1707 0.8544 1.1124 -0.0332 0.1079  0.1612  77  ARG A NH1 
522  N NH2 . ARG A 78  ? 1.1563 0.8304 1.1159 -0.0356 0.1064  0.1697  77  ARG A NH2 
523  N N   . ARG A 79  ? 0.9989 0.5948 0.8619 -0.0500 0.0812  0.1022  78  ARG A N   
524  C CA  . ARG A 79  ? 0.9837 0.5885 0.8414 -0.0546 0.0732  0.0993  78  ARG A CA  
525  C C   . ARG A 79  ? 1.0038 0.5992 0.8430 -0.0542 0.0719  0.0881  78  ARG A C   
526  O O   . ARG A 79  ? 1.0768 0.6860 0.9118 -0.0554 0.0674  0.0862  78  ARG A O   
527  C CB  . ARG A 79  ? 1.0684 0.6645 0.9298 -0.0600 0.0686  0.1013  78  ARG A CB  
528  C CG  . ARG A 79  ? 1.1563 0.7698 1.0370 -0.0619 0.0670  0.1135  78  ARG A CG  
529  C CD  . ARG A 79  ? 1.1349 0.7299 1.0218 -0.0641 0.0682  0.1167  78  ARG A CD  
530  N NE  . ARG A 79  ? 1.2130 0.7958 1.0925 -0.0705 0.0616  0.1125  78  ARG A NE  
531  C CZ  . ARG A 79  ? 1.2322 0.8252 1.1213 -0.0760 0.0553  0.1193  78  ARG A CZ  
532  N NH1 . ARG A 79  ? 1.2454 0.8608 1.1519 -0.0757 0.0548  0.1305  78  ARG A NH1 
533  N NH2 . ARG A 79  ? 1.1798 0.7608 1.0608 -0.0823 0.0492  0.1152  78  ARG A NH2 
534  N N   . VAL A 80  ? 0.9768 0.5489 0.8048 -0.0523 0.0760  0.0808  79  VAL A N   
535  C CA  . VAL A 80  ? 1.0309 0.5938 0.8414 -0.0523 0.0746  0.0706  79  VAL A CA  
536  C C   . VAL A 80  ? 0.9625 0.5383 0.7703 -0.0480 0.0772  0.0695  79  VAL A C   
537  O O   . VAL A 80  ? 0.8439 0.4251 0.6425 -0.0486 0.0736  0.0645  79  VAL A O   
538  C CB  . VAL A 80  ? 0.9475 0.4816 0.7458 -0.0519 0.0783  0.0630  79  VAL A CB  
539  C CG1 . VAL A 80  ? 0.9024 0.4225 0.7008 -0.0575 0.0746  0.0630  79  VAL A CG1 
540  C CG2 . VAL A 80  ? 0.9270 0.4532 0.7294 -0.0461 0.0875  0.0651  79  VAL A CG2 
541  N N   . VAL A 81  ? 0.9096 0.4906 0.7255 -0.0439 0.0833  0.0748  80  VAL A N   
542  C CA  . VAL A 81  ? 0.8390 0.4317 0.6522 -0.0408 0.0855  0.0743  80  VAL A CA  
543  C C   . VAL A 81  ? 0.9266 0.5444 0.7463 -0.0426 0.0810  0.0790  80  VAL A C   
544  O O   . VAL A 81  ? 0.9160 0.5413 0.7277 -0.0421 0.0793  0.0750  80  VAL A O   
545  C CB  . VAL A 81  ? 0.8792 0.4705 0.6994 -0.0363 0.0933  0.0794  80  VAL A CB  
546  C CG1 . VAL A 81  ? 0.8537 0.4572 0.6707 -0.0340 0.0950  0.0793  80  VAL A CG1 
547  C CG2 . VAL A 81  ? 0.7966 0.3621 0.6094 -0.0338 0.0985  0.0742  80  VAL A CG2 
548  N N   . GLY A 82  ? 0.8505 0.4810 0.6843 -0.0446 0.0792  0.0875  81  GLY A N   
549  C CA  . GLY A 82  ? 0.8745 0.5289 0.7141 -0.0464 0.0752  0.0921  81  GLY A CA  
550  C C   . GLY A 82  ? 0.9211 0.5778 0.7517 -0.0487 0.0692  0.0863  81  GLY A C   
551  O O   . GLY A 82  ? 0.9095 0.5814 0.7376 -0.0486 0.0673  0.0858  81  GLY A O   
552  N N   . THR A 83  ? 0.8819 0.5236 0.7074 -0.0510 0.0663  0.0822  82  THR A N   
553  C CA  . THR A 83  ? 0.9380 0.5817 0.7551 -0.0531 0.0607  0.0774  82  THR A CA  
554  C C   . THR A 83  ? 0.9321 0.5673 0.7338 -0.0507 0.0617  0.0683  82  THR A C   
555  O O   . THR A 83  ? 0.9044 0.5485 0.7006 -0.0505 0.0587  0.0656  82  THR A O   
556  C CB  . THR A 83  ? 0.8903 0.5214 0.7068 -0.0574 0.0567  0.0767  82  THR A CB  
557  O OG1 . THR A 83  ? 1.0132 0.6520 0.8446 -0.0597 0.0557  0.0856  82  THR A OG1 
558  C CG2 . THR A 83  ? 0.9214 0.5576 0.7312 -0.0597 0.0505  0.0736  82  THR A CG2 
559  N N   . SER A 84  ? 0.9323 0.5505 0.7273 -0.0486 0.0662  0.0639  83  SER A N   
560  C CA  . SER A 84  ? 0.9261 0.5366 0.7072 -0.0464 0.0674  0.0560  83  SER A CA  
561  C C   . SER A 84  ? 0.9628 0.5888 0.7444 -0.0439 0.0690  0.0573  83  SER A C   
562  O O   . SER A 84  ? 0.9772 0.6049 0.7493 -0.0431 0.0673  0.0522  83  SER A O   
563  C CB  . SER A 84  ? 0.8204 0.4101 0.5947 -0.0446 0.0724  0.0518  83  SER A CB  
564  O OG  . SER A 84  ? 0.7898 0.3630 0.5607 -0.0475 0.0707  0.0492  83  SER A OG  
565  N N   . SER A 85  ? 0.8917 0.5287 0.6840 -0.0430 0.0722  0.0643  84  SER A N   
566  C CA  . SER A 85  ? 0.9183 0.5708 0.7109 -0.0419 0.0731  0.0661  84  SER A CA  
567  C C   . SER A 85  ? 0.8565 0.5251 0.6497 -0.0433 0.0687  0.0668  84  SER A C   
568  O O   . SER A 85  ? 0.8822 0.5581 0.6688 -0.0425 0.0685  0.0641  84  SER A O   
569  C CB  . SER A 85  ? 0.8830 0.5453 0.6878 -0.0414 0.0771  0.0747  84  SER A CB  
570  O OG  . SER A 85  ? 0.8834 0.5633 0.6891 -0.0418 0.0769  0.0773  84  SER A OG  
571  N N   . ALA A 86  ? 0.8210 0.4950 0.6216 -0.0455 0.0652  0.0706  85  ALA A N   
572  C CA  . ALA A 86  ? 0.8648 0.5544 0.6663 -0.0464 0.0614  0.0717  85  ALA A CA  
573  C C   . ALA A 86  ? 0.9434 0.6259 0.7321 -0.0453 0.0590  0.0638  85  ALA A C   
574  O O   . ALA A 86  ? 0.8532 0.5456 0.6373 -0.0440 0.0582  0.0621  85  ALA A O   
575  C CB  . ALA A 86  ? 0.7448 0.4418 0.5580 -0.0491 0.0582  0.0784  85  ALA A CB  
576  N N   . MET A 87  ? 0.9713 0.6363 0.7536 -0.0459 0.0579  0.0591  86  MET A N   
577  C CA  . MET A 87  ? 0.8796 0.5381 0.6503 -0.0452 0.0554  0.0525  86  MET A CA  
578  C C   . MET A 87  ? 0.8990 0.5536 0.6594 -0.0422 0.0582  0.0469  86  MET A C   
579  O O   . MET A 87  ? 0.9930 0.6512 0.7465 -0.0406 0.0569  0.0435  86  MET A O   
580  C CB  . MET A 87  ? 0.8971 0.5377 0.6628 -0.0474 0.0534  0.0491  86  MET A CB  
581  C CG  . MET A 87  ? 0.9738 0.6175 0.7472 -0.0513 0.0491  0.0538  86  MET A CG  
582  S SD  . MET A 87  ? 1.1216 0.7416 0.8903 -0.0550 0.0484  0.0506  86  MET A SD  
583  C CE  . MET A 87  ? 1.0383 0.6589 0.8019 -0.0588 0.0411  0.0494  86  MET A CE  
584  N N   . VAL A 88  ? 0.8878 0.5350 0.6471 -0.0413 0.0624  0.0462  87  VAL A N   
585  C CA  . VAL A 88  ? 0.9046 0.5483 0.6546 -0.0391 0.0649  0.0417  87  VAL A CA  
586  C C   . VAL A 88  ? 0.9611 0.6211 0.7121 -0.0385 0.0649  0.0435  87  VAL A C   
587  O O   . VAL A 88  ? 0.9693 0.6286 0.7110 -0.0370 0.0646  0.0387  87  VAL A O   
588  C CB  . VAL A 88  ? 0.9123 0.5472 0.6629 -0.0384 0.0695  0.0424  87  VAL A CB  
589  C CG1 . VAL A 88  ? 0.8845 0.5242 0.6308 -0.0372 0.0720  0.0417  87  VAL A CG1 
590  C CG2 . VAL A 88  ? 1.0567 0.6719 0.7994 -0.0380 0.0701  0.0370  87  VAL A CG2 
591  N N   . LEU A 89  ? 0.9000 0.5743 0.6617 -0.0398 0.0654  0.0503  88  LEU A N   
592  C CA  . LEU A 89  ? 0.8485 0.5383 0.6104 -0.0399 0.0658  0.0522  88  LEU A CA  
593  C C   . LEU A 89  ? 0.8523 0.5487 0.6100 -0.0387 0.0631  0.0496  88  LEU A C   
594  O O   . LEU A 89  ? 0.9177 0.6165 0.6670 -0.0374 0.0638  0.0458  88  LEU A O   
595  C CB  . LEU A 89  ? 0.9261 0.6307 0.7011 -0.0419 0.0667  0.0609  88  LEU A CB  
596  C CG  . LEU A 89  ? 1.0783 0.8000 0.8539 -0.0431 0.0673  0.0638  88  LEU A CG  
597  C CD1 . LEU A 89  ? 1.0921 0.8222 0.8776 -0.0451 0.0696  0.0715  88  LEU A CD1 
598  C CD2 . LEU A 89  ? 0.9864 0.7224 0.7661 -0.0433 0.0649  0.0664  88  LEU A CD2 
599  N N   . GLY A 90  ? 0.8175 0.5166 0.5810 -0.0392 0.0602  0.0520  89  GLY A N   
600  C CA  . GLY A 90  ? 0.7920 0.4989 0.5530 -0.0377 0.0580  0.0510  89  GLY A CA  
601  C C   . GLY A 90  ? 0.9681 0.6634 0.7169 -0.0351 0.0576  0.0436  89  GLY A C   
602  O O   . GLY A 90  ? 1.0206 0.7206 0.7634 -0.0326 0.0582  0.0409  89  GLY A O   
603  N N   . PHE A 91  ? 0.9647 0.6442 0.7094 -0.0357 0.0568  0.0403  90  PHE A N   
604  C CA  . PHE A 91  ? 0.9407 0.6091 0.6742 -0.0336 0.0563  0.0340  90  PHE A CA  
605  C C   . PHE A 91  ? 0.9644 0.6292 0.6890 -0.0318 0.0593  0.0295  90  PHE A C   
606  O O   . PHE A 91  ? 0.9898 0.6525 0.7065 -0.0293 0.0593  0.0255  90  PHE A O   
607  C CB  . PHE A 91  ? 0.9489 0.6015 0.6794 -0.0353 0.0549  0.0315  90  PHE A CB  
608  C CG  . PHE A 91  ? 1.1304 0.7760 0.8530 -0.0342 0.0523  0.0276  90  PHE A CG  
609  C CD1 . PHE A 91  ? 1.0965 0.7480 0.8231 -0.0351 0.0485  0.0305  90  PHE A CD1 
610  C CD2 . PHE A 91  ? 1.1533 0.7875 0.8652 -0.0326 0.0537  0.0219  90  PHE A CD2 
611  C CE1 . PHE A 91  ? 1.0821 0.7285 0.8022 -0.0343 0.0460  0.0279  90  PHE A CE1 
612  C CE2 . PHE A 91  ? 1.0436 0.6722 0.7489 -0.0316 0.0513  0.0190  90  PHE A CE2 
613  C CZ  . PHE A 91  ? 1.0176 0.6526 0.7272 -0.0325 0.0475  0.0222  90  PHE A CZ  
614  N N   . SER A 92  ? 0.8998 0.5639 0.6260 -0.0332 0.0619  0.0307  91  SER A N   
615  C CA  . SER A 92  ? 0.9275 0.5888 0.6455 -0.0326 0.0643  0.0273  91  SER A CA  
616  C C   . SER A 92  ? 0.9605 0.6335 0.6761 -0.0316 0.0648  0.0271  91  SER A C   
617  O O   . SER A 92  ? 0.9526 0.6206 0.6581 -0.0301 0.0656  0.0222  91  SER A O   
618  C CB  . SER A 92  ? 0.9016 0.5627 0.6235 -0.0346 0.0669  0.0304  91  SER A CB  
619  O OG  . SER A 92  ? 1.0554 0.7021 0.7748 -0.0344 0.0677  0.0283  91  SER A OG  
620  N N   . THR A 93  ? 0.9271 0.6150 0.6512 -0.0326 0.0644  0.0324  92  THR A N   
621  C CA  . THR A 93  ? 0.9279 0.6271 0.6490 -0.0316 0.0652  0.0320  92  THR A CA  
622  C C   . THR A 93  ? 0.9174 0.6146 0.6332 -0.0277 0.0644  0.0285  92  THR A C   
623  O O   . THR A 93  ? 1.0185 0.7149 0.7253 -0.0255 0.0661  0.0244  92  THR A O   
624  C CB  . THR A 93  ? 1.0199 0.7365 0.7520 -0.0336 0.0650  0.0391  92  THR A CB  
625  O OG1 . THR A 93  ? 0.9754 0.6938 0.7140 -0.0369 0.0658  0.0435  92  THR A OG1 
626  C CG2 . THR A 93  ? 0.9245 0.6525 0.6517 -0.0330 0.0665  0.0384  92  THR A CG2 
627  N N   . LEU A 94  ? 0.8536 0.5495 0.5746 -0.0268 0.0619  0.0302  93  LEU A N   
628  C CA  . LEU A 94  ? 0.9332 0.6274 0.6501 -0.0230 0.0610  0.0279  93  LEU A CA  
629  C C   . LEU A 94  ? 0.9631 0.6417 0.6687 -0.0212 0.0617  0.0213  93  LEU A C   
630  O O   . LEU A 94  ? 0.8898 0.5670 0.5892 -0.0174 0.0626  0.0184  93  LEU A O   
631  C CB  . LEU A 94  ? 0.8524 0.5490 0.5775 -0.0237 0.0575  0.0320  93  LEU A CB  
632  C CG  . LEU A 94  ? 0.8827 0.5808 0.6061 -0.0201 0.0561  0.0317  93  LEU A CG  
633  C CD1 . LEU A 94  ? 0.8519 0.5612 0.5734 -0.0159 0.0589  0.0318  93  LEU A CD1 
634  C CD2 . LEU A 94  ? 0.8046 0.5079 0.5373 -0.0223 0.0520  0.0373  93  LEU A CD2 
635  N N   . MET A 95  ? 1.0214 0.6884 0.7244 -0.0235 0.0616  0.0194  94  MET A N   
636  C CA  . MET A 95  ? 0.9170 0.5698 0.6095 -0.0221 0.0622  0.0137  94  MET A CA  
637  C C   . MET A 95  ? 0.9716 0.6236 0.6558 -0.0213 0.0650  0.0102  94  MET A C   
638  O O   . MET A 95  ? 1.0598 0.7036 0.7352 -0.0188 0.0656  0.0058  94  MET A O   
639  C CB  . MET A 95  ? 0.8586 0.5001 0.5504 -0.0248 0.0619  0.0129  94  MET A CB  
640  C CG  . MET A 95  ? 1.0581 0.6916 0.7505 -0.0251 0.0592  0.0126  94  MET A CG  
641  S SD  . MET A 95  ? 1.2078 0.8368 0.8939 -0.0218 0.0571  0.0098  94  MET A SD  
642  C CE  . MET A 95  ? 1.0166 0.6614 0.7116 -0.0204 0.0552  0.0151  94  MET A CE  
643  N N   . ALA A 96  ? 0.9755 0.6357 0.6622 -0.0240 0.0664  0.0124  95  ALA A N   
644  C CA  . ALA A 96  ? 0.9387 0.5988 0.6166 -0.0243 0.0686  0.0093  95  ALA A CA  
645  C C   . ALA A 96  ? 0.9659 0.6302 0.6394 -0.0204 0.0698  0.0071  95  ALA A C   
646  O O   . ALA A 96  ? 0.9046 0.5610 0.5674 -0.0187 0.0714  0.0020  95  ALA A O   
647  C CB  . ALA A 96  ? 0.8683 0.5387 0.5506 -0.0286 0.0694  0.0132  95  ALA A CB  
648  N N   . LEU A 97  ? 0.9302 0.6064 0.6118 -0.0186 0.0692  0.0110  96  LEU A N   
649  C CA  . LEU A 97  ? 0.9087 0.5907 0.5869 -0.0142 0.0711  0.0098  96  LEU A CA  
650  C C   . LEU A 97  ? 0.9176 0.5889 0.5901 -0.0093 0.0714  0.0061  96  LEU A C   
651  O O   . LEU A 97  ? 0.9085 0.5752 0.5719 -0.0058 0.0741  0.0019  96  LEU A O   
652  C CB  . LEU A 97  ? 0.8196 0.5183 0.5091 -0.0135 0.0703  0.0160  96  LEU A CB  
653  C CG  . LEU A 97  ? 0.8543 0.5618 0.5413 -0.0087 0.0731  0.0157  96  LEU A CG  
654  C CD1 . LEU A 97  ? 0.8241 0.5339 0.5022 -0.0101 0.0763  0.0125  96  LEU A CD1 
655  C CD2 . LEU A 97  ? 0.7759 0.5002 0.4753 -0.0079 0.0717  0.0229  96  LEU A CD2 
656  N N   . VAL A 98  ? 0.9134 0.5803 0.5907 -0.0090 0.0685  0.0078  97  VAL A N   
657  C CA  . VAL A 98  ? 1.0530 0.7115 0.7260 -0.0046 0.0684  0.0056  97  VAL A CA  
658  C C   . VAL A 98  ? 0.9102 0.5531 0.5718 -0.0046 0.0697  -0.0005 97  VAL A C   
659  O O   . VAL A 98  ? 0.9219 0.5577 0.5773 -0.0002 0.0711  -0.0033 97  VAL A O   
660  C CB  . VAL A 98  ? 0.8961 0.5540 0.5762 -0.0056 0.0644  0.0091  97  VAL A CB  
661  C CG1 . VAL A 98  ? 0.9147 0.5881 0.6058 -0.0054 0.0629  0.0154  97  VAL A CG1 
662  C CG2 . VAL A 98  ? 0.9237 0.5736 0.6042 -0.0108 0.0626  0.0085  97  VAL A CG2 
663  N N   . PHE A 99  ? 0.9444 0.5818 0.6034 -0.0093 0.0693  -0.0019 98  PHE A N   
664  C CA  . PHE A 99  ? 0.9670 0.5904 0.6155 -0.0099 0.0702  -0.0069 98  PHE A CA  
665  C C   . PHE A 99  ? 1.0185 0.6405 0.6579 -0.0087 0.0734  -0.0107 98  PHE A C   
666  O O   . PHE A 99  ? 1.1066 0.7175 0.7372 -0.0061 0.0747  -0.0149 98  PHE A O   
667  C CB  . PHE A 99  ? 0.9856 0.6053 0.6348 -0.0152 0.0692  -0.0063 98  PHE A CB  
668  C CG  . PHE A 99  ? 1.0802 0.6925 0.7318 -0.0158 0.0669  -0.0057 98  PHE A CG  
669  C CD1 . PHE A 99  ? 1.0856 0.6916 0.7350 -0.0125 0.0657  -0.0069 98  PHE A CD1 
670  C CD2 . PHE A 99  ? 1.0454 0.6571 0.7012 -0.0196 0.0663  -0.0036 98  PHE A CD2 
671  C CE1 . PHE A 99  ? 0.9985 0.5978 0.6489 -0.0137 0.0635  -0.0065 98  PHE A CE1 
672  C CE2 . PHE A 99  ? 1.0954 0.6993 0.7518 -0.0202 0.0647  -0.0036 98  PHE A CE2 
673  C CZ  . PHE A 99  ? 1.0504 0.6481 0.7036 -0.0176 0.0631  -0.0053 98  PHE A CZ  
674  N N   . VAL A 100 ? 0.9414 0.5742 0.5824 -0.0109 0.0747  -0.0093 99  VAL A N   
675  C CA  . VAL A 100 ? 0.9525 0.5837 0.5833 -0.0106 0.0777  -0.0133 99  VAL A CA  
676  C C   . VAL A 100 ? 0.9814 0.6138 0.6097 -0.0038 0.0805  -0.0149 99  VAL A C   
677  O O   . VAL A 100 ? 1.0668 0.6918 0.6841 -0.0020 0.0836  -0.0198 99  VAL A O   
678  C CB  . VAL A 100 ? 0.8929 0.5362 0.5255 -0.0156 0.0780  -0.0109 99  VAL A CB  
679  C CG1 . VAL A 100 ? 0.8986 0.5419 0.5354 -0.0217 0.0757  -0.0081 99  VAL A CG1 
680  C CG2 . VAL A 100 ? 0.9651 0.6250 0.6080 -0.0136 0.0782  -0.0060 99  VAL A CG2 
681  N N   . LEU A 101 ? 0.9128 0.5541 0.5510 0.0001  0.0797  -0.0105 100 LEU A N   
682  C CA  . LEU A 101 ? 0.8888 0.5337 0.5265 0.0071  0.0828  -0.0106 100 LEU A CA  
683  C C   . LEU A 101 ? 0.9531 0.5871 0.5889 0.0123  0.0828  -0.0118 100 LEU A C   
684  O O   . LEU A 101 ? 1.1920 0.8252 0.8250 0.0188  0.0863  -0.0127 100 LEU A O   
685  C CB  . LEU A 101 ? 0.8472 0.5102 0.4974 0.0085  0.0819  -0.0039 100 LEU A CB  
686  C CG  . LEU A 101 ? 0.9258 0.6012 0.5750 0.0100  0.0854  -0.0033 100 LEU A CG  
687  C CD1 . LEU A 101 ? 0.9315 0.6101 0.5775 0.0031  0.0851  -0.0043 100 LEU A CD1 
688  C CD2 . LEU A 101 ? 1.0708 0.7637 0.7330 0.0125  0.0844  0.0041  100 LEU A CD2 
689  N N   . ALA A 102 ? 0.8943 0.5203 0.5318 0.0097  0.0793  -0.0114 101 ALA A N   
690  C CA  . ALA A 102 ? 0.8906 0.5076 0.5271 0.0138  0.0787  -0.0116 101 ALA A CA  
691  C C   . ALA A 102 ? 0.9731 0.5743 0.6017 0.0106  0.0775  -0.0157 101 ALA A C   
692  O O   . ALA A 102 ? 1.1155 0.7112 0.7460 0.0105  0.0748  -0.0145 101 ALA A O   
693  C CB  . ALA A 102 ? 0.8054 0.4311 0.4533 0.0140  0.0750  -0.0055 101 ALA A CB  
694  N N   . ALA A 103 ? 0.9405 0.5346 0.5598 0.0077  0.0792  -0.0203 102 ALA A N   
695  C CA  . ALA A 103 ? 0.9936 0.5737 0.6056 0.0043  0.0780  -0.0236 102 ALA A CA  
696  C C   . ALA A 103 ? 1.0428 0.6105 0.6497 0.0092  0.0789  -0.0256 102 ALA A C   
697  O O   . ALA A 103 ? 1.0616 0.6216 0.6681 0.0078  0.0765  -0.0254 102 ALA A O   
698  C CB  . ALA A 103 ? 1.0106 0.5867 0.6136 -0.0004 0.0794  -0.0274 102 ALA A CB  
699  N N   . ALA A 104 ? 1.0126 0.5785 0.6158 0.0152  0.0828  -0.0273 103 ALA A N   
700  C CA  . ALA A 104 ? 0.8927 0.4467 0.4917 0.0205  0.0842  -0.0286 103 ALA A CA  
701  C C   . ALA A 104 ? 0.9200 0.4792 0.5286 0.0239  0.0818  -0.0232 103 ALA A C   
702  O O   . ALA A 104 ? 1.0012 0.5510 0.6080 0.0241  0.0801  -0.0231 103 ALA A O   
703  C CB  . ALA A 104 ? 0.9627 0.5124 0.5549 0.0266  0.0899  -0.0319 103 ALA A CB  
704  N N   . PRO A 105 ? 0.9732 0.5473 0.5919 0.0261  0.0812  -0.0182 104 PRO A N   
705  C CA  . PRO A 105 ? 0.9961 0.5751 0.6232 0.0278  0.0780  -0.0126 104 PRO A CA  
706  C C   . PRO A 105 ? 0.9038 0.4794 0.5320 0.0213  0.0730  -0.0120 104 PRO A C   
707  O O   . PRO A 105 ? 0.9472 0.5198 0.5771 0.0220  0.0706  -0.0095 104 PRO A O   
708  C CB  . PRO A 105 ? 0.8399 0.4364 0.4771 0.0295  0.0778  -0.0073 104 PRO A CB  
709  C CG  . PRO A 105 ? 0.9693 0.5684 0.6024 0.0325  0.0828  -0.0102 104 PRO A CG  
710  C CD  . PRO A 105 ? 0.9458 0.5330 0.5681 0.0277  0.0836  -0.0168 104 PRO A CD  
711  N N   . ILE A 106 ? 0.8230 0.3992 0.4501 0.0151  0.0716  -0.0139 105 ILE A N   
712  C CA  . ILE A 106 ? 0.9708 0.5428 0.5982 0.0096  0.0679  -0.0136 105 ILE A CA  
713  C C   . ILE A 106 ? 0.9450 0.5023 0.5638 0.0091  0.0680  -0.0170 105 ILE A C   
714  O O   . ILE A 106 ? 0.9739 0.5267 0.5926 0.0079  0.0654  -0.0158 105 ILE A O   
715  C CB  . ILE A 106 ? 0.9866 0.5635 0.6161 0.0040  0.0671  -0.0139 105 ILE A CB  
716  C CG1 . ILE A 106 ? 0.8721 0.4629 0.5117 0.0034  0.0655  -0.0093 105 ILE A CG1 
717  C CG2 . ILE A 106 ? 0.9637 0.5327 0.5904 -0.0009 0.0649  -0.0150 105 ILE A CG2 
718  C CD1 . ILE A 106 ? 0.8496 0.4485 0.4924 0.0002  0.0664  -0.0089 105 ILE A CD1 
719  N N   . SER A 107 ? 0.9407 0.4903 0.5515 0.0096  0.0710  -0.0212 106 SER A N   
720  C CA  . SER A 107 ? 0.9841 0.5194 0.5867 0.0091  0.0711  -0.0241 106 SER A CA  
721  C C   . SER A 107 ? 1.0537 0.5848 0.6572 0.0145  0.0710  -0.0221 106 SER A C   
722  O O   . SER A 107 ? 1.0042 0.5271 0.6049 0.0133  0.0692  -0.0220 106 SER A O   
723  C CB  . SER A 107 ? 0.9480 0.4756 0.5415 0.0087  0.0743  -0.0288 106 SER A CB  
724  O OG  . SER A 107 ? 0.8481 0.3619 0.4338 0.0069  0.0739  -0.0313 106 SER A OG  
725  N N   . GLN A 108 ? 1.0382 0.5758 0.6461 0.0205  0.0731  -0.0199 107 GLN A N   
726  C CA  . GLN A 108 ? 1.0920 0.6277 0.7025 0.0261  0.0732  -0.0165 107 GLN A CA  
727  C C   . GLN A 108 ? 1.0875 0.6282 0.7038 0.0233  0.0684  -0.0119 107 GLN A C   
728  O O   . GLN A 108 ? 1.0738 0.6073 0.6879 0.0233  0.0668  -0.0109 107 GLN A O   
729  C CB  . GLN A 108 ? 1.0318 0.5760 0.6473 0.0332  0.0767  -0.0139 107 GLN A CB  
730  C CG  . GLN A 108 ? 1.1519 0.6899 0.7669 0.0411  0.0799  -0.0122 107 GLN A CG  
731  C CD  . GLN A 108 ? 1.2780 0.7976 0.8822 0.0417  0.0823  -0.0174 107 GLN A CD  
732  O OE1 . GLN A 108 ? 1.3125 0.8243 0.9088 0.0366  0.0823  -0.0228 107 GLN A OE1 
733  N NE2 . GLN A 108 ? 1.2809 0.7941 0.8856 0.0479  0.0843  -0.0151 107 GLN A NE2 
734  N N   . GLY A 109 ? 0.9821 0.5348 0.6054 0.0205  0.0659  -0.0091 108 GLY A N   
735  C CA  . GLY A 109 ? 1.0296 0.5863 0.6570 0.0171  0.0612  -0.0052 108 GLY A CA  
736  C C   . GLY A 109 ? 0.9049 0.4525 0.5265 0.0113  0.0589  -0.0080 108 GLY A C   
737  O O   . GLY A 109 ? 1.0405 0.5876 0.6625 0.0091  0.0555  -0.0056 108 GLY A O   
738  N N   . LEU A 110 ? 0.9137 0.4549 0.5298 0.0087  0.0607  -0.0126 109 LEU A N   
739  C CA  . LEU A 110 ? 0.9008 0.4344 0.5118 0.0035  0.0591  -0.0147 109 LEU A CA  
740  C C   . LEU A 110 ? 0.9802 0.5017 0.5838 0.0043  0.0600  -0.0169 109 LEU A C   
741  O O   . LEU A 110 ? 1.0505 0.5670 0.6512 0.0017  0.0580  -0.0165 109 LEU A O   
742  C CB  . LEU A 110 ? 0.9386 0.4742 0.5493 -0.0005 0.0602  -0.0171 109 LEU A CB  
743  C CG  . LEU A 110 ? 0.9781 0.5196 0.5935 -0.0046 0.0581  -0.0155 109 LEU A CG  
744  C CD1 . LEU A 110 ? 0.8935 0.4463 0.5169 -0.0031 0.0569  -0.0121 109 LEU A CD1 
745  C CD2 . LEU A 110 ? 0.8792 0.4210 0.4939 -0.0082 0.0597  -0.0173 109 LEU A CD2 
746  N N   . PHE A 111 ? 0.9721 0.4884 0.5720 0.0076  0.0631  -0.0192 110 PHE A N   
747  C CA  . PHE A 111 ? 0.9804 0.4840 0.5728 0.0077  0.0639  -0.0214 110 PHE A CA  
748  C C   . PHE A 111 ? 1.0038 0.5022 0.5957 0.0140  0.0656  -0.0202 110 PHE A C   
749  O O   . PHE A 111 ? 1.0183 0.5059 0.6050 0.0141  0.0657  -0.0209 110 PHE A O   
750  C CB  . PHE A 111 ? 1.0070 0.5052 0.5932 0.0049  0.0661  -0.0257 110 PHE A CB  
751  C CG  . PHE A 111 ? 0.8438 0.3466 0.4307 -0.0011 0.0649  -0.0261 110 PHE A CG  
752  C CD1 . PHE A 111 ? 0.7995 0.2971 0.3831 -0.0054 0.0633  -0.0260 110 PHE A CD1 
753  C CD2 . PHE A 111 ? 0.8015 0.3142 0.3928 -0.0021 0.0657  -0.0260 110 PHE A CD2 
754  C CE1 . PHE A 111 ? 0.9317 0.4338 0.5166 -0.0101 0.0629  -0.0258 110 PHE A CE1 
755  C CE2 . PHE A 111 ? 0.8496 0.3666 0.4425 -0.0071 0.0650  -0.0256 110 PHE A CE2 
756  C CZ  . PHE A 111 ? 0.8477 0.3591 0.4374 -0.0108 0.0638  -0.0255 110 PHE A CZ  
757  N N   . GLY A 112 ? 0.9711 0.4770 0.5687 0.0193  0.0673  -0.0179 111 GLY A N   
758  C CA  . GLY A 112 ? 0.9726 0.4740 0.5704 0.0263  0.0699  -0.0163 111 GLY A CA  
759  C C   . GLY A 112 ? 1.0850 0.5782 0.6766 0.0298  0.0749  -0.0209 111 GLY A C   
760  O O   . GLY A 112 ? 1.1962 0.6873 0.7890 0.0369  0.0784  -0.0196 111 GLY A O   
761  N N   . ASN A 113 ? 0.9939 0.4824 0.5787 0.0248  0.0754  -0.0259 112 ASN A N   
762  C CA  . ASN A 113 ? 0.9532 0.4341 0.5304 0.0266  0.0798  -0.0309 112 ASN A CA  
763  C C   . ASN A 113 ? 1.1148 0.6050 0.6922 0.0226  0.0801  -0.0330 112 ASN A C   
764  O O   . ASN A 113 ? 1.0828 0.5811 0.6642 0.0173  0.0768  -0.0314 112 ASN A O   
765  C CB  . ASN A 113 ? 0.9245 0.3883 0.4912 0.0235  0.0800  -0.0349 112 ASN A CB  
766  C CG  . ASN A 113 ? 0.9527 0.4161 0.5177 0.0154  0.0758  -0.0349 112 ASN A CG  
767  O OD1 . ASN A 113 ? 1.0282 0.4980 0.5930 0.0102  0.0748  -0.0362 112 ASN A OD1 
768  N ND2 . ASN A 113 ? 1.0537 0.5105 0.6182 0.0144  0.0734  -0.0329 112 ASN A ND2 
769  N N   . THR A 114 ? 1.0421 0.5307 0.6148 0.0254  0.0843  -0.0364 113 THR A N   
770  C CA  . THR A 114 ? 0.8585 0.3559 0.4305 0.0216  0.0849  -0.0383 113 THR A CA  
771  C C   . THR A 114 ? 0.8612 0.3499 0.4230 0.0142  0.0842  -0.0429 113 THR A C   
772  O O   . THR A 114 ? 0.9106 0.4039 0.4691 0.0112  0.0855  -0.0452 113 THR A O   
773  C CB  . THR A 114 ? 0.9137 0.4153 0.4851 0.0279  0.0899  -0.0394 113 THR A CB  
774  O OG1 . THR A 114 ? 1.0986 0.5841 0.6593 0.0314  0.0941  -0.0442 113 THR A OG1 
775  C CG2 . THR A 114 ? 0.8395 0.3527 0.4224 0.0347  0.0903  -0.0335 113 THR A CG2 
776  N N   . ASP A 115 ? 0.8622 0.3396 0.4195 0.0108  0.0819  -0.0435 114 ASP A N   
777  C CA  . ASP A 115 ? 0.9709 0.4400 0.5188 0.0034  0.0808  -0.0469 114 ASP A CA  
778  C C   . ASP A 115 ? 0.8722 0.3524 0.4246 -0.0037 0.0776  -0.0446 114 ASP A C   
779  O O   . ASP A 115 ? 0.8911 0.3672 0.4371 -0.0105 0.0764  -0.0461 114 ASP A O   
780  C CB  . ASP A 115 ? 1.0486 0.5024 0.5909 0.0024  0.0795  -0.0475 114 ASP A CB  
781  C CG  . ASP A 115 ? 1.0420 0.4831 0.5797 0.0095  0.0831  -0.0497 114 ASP A CG  
782  O OD1 . ASP A 115 ? 1.0000 0.4401 0.5342 0.0137  0.0873  -0.0526 114 ASP A OD1 
783  O OD2 . ASP A 115 ? 1.1840 0.6160 0.7215 0.0111  0.0820  -0.0481 114 ASP A OD2 
784  N N   . TYR A 116 ? 1.0180 0.5118 0.5812 -0.0025 0.0763  -0.0405 115 TYR A N   
785  C CA  . TYR A 116 ? 1.0102 0.5141 0.5786 -0.0083 0.0739  -0.0379 115 TYR A CA  
786  C C   . TYR A 116 ? 1.0229 0.5409 0.5971 -0.0081 0.0750  -0.0368 115 TYR A C   
787  O O   . TYR A 116 ? 0.9074 0.4358 0.4895 -0.0106 0.0733  -0.0334 115 TYR A O   
788  C CB  . TYR A 116 ? 0.9509 0.4572 0.5264 -0.0082 0.0711  -0.0342 115 TYR A CB  
789  C CG  . TYR A 116 ? 0.8678 0.3619 0.4381 -0.0092 0.0698  -0.0346 115 TYR A CG  
790  C CD1 . TYR A 116 ? 0.8108 0.3016 0.3777 -0.0152 0.0682  -0.0343 115 TYR A CD1 
791  C CD2 . TYR A 116 ? 0.8596 0.3466 0.4291 -0.0041 0.0700  -0.0346 115 TYR A CD2 
792  C CE1 . TYR A 116 ? 0.8797 0.3602 0.4421 -0.0162 0.0669  -0.0341 115 TYR A CE1 
793  C CE2 . TYR A 116 ? 0.8233 0.2997 0.3884 -0.0051 0.0686  -0.0344 115 TYR A CE2 
794  C CZ  . TYR A 116 ? 0.8981 0.3713 0.4595 -0.0113 0.0670  -0.0343 115 TYR A CZ  
795  O OH  . TYR A 116 ? 0.8286 0.2921 0.3860 -0.0124 0.0655  -0.0336 115 TYR A OH  
796  N N   . GLN A 117 ? 1.0658 0.5840 0.6359 -0.0050 0.0781  -0.0395 116 GLN A N   
797  C CA  . GLN A 117 ? 0.8790 0.4112 0.4540 -0.0048 0.0794  -0.0381 116 GLN A CA  
798  C C   . GLN A 117 ? 0.8585 0.3983 0.4349 -0.0123 0.0776  -0.0366 116 GLN A C   
799  O O   . GLN A 117 ? 0.9465 0.4994 0.5325 -0.0134 0.0765  -0.0326 116 GLN A O   
800  C CB  . GLN A 117 ? 1.0866 0.6157 0.6539 -0.0012 0.0835  -0.0422 116 GLN A CB  
801  C CG  . GLN A 117 ? 1.0964 0.6233 0.6656 0.0078  0.0864  -0.0421 116 GLN A CG  
802  C CD  . GLN A 117 ? 1.0762 0.5993 0.6368 0.0116  0.0914  -0.0464 116 GLN A CD  
803  O OE1 . GLN A 117 ? 1.0959 0.6194 0.6584 0.0196  0.0948  -0.0459 116 GLN A OE1 
804  N NE2 . GLN A 117 ? 1.1643 0.6838 0.7149 0.0058  0.0921  -0.0505 116 GLN A NE2 
805  N N   . GLY A 118 ? 0.9386 0.4705 0.5056 -0.0179 0.0773  -0.0391 117 GLY A N   
806  C CA  . GLY A 118 ? 0.9444 0.4845 0.5128 -0.0252 0.0757  -0.0367 117 GLY A CA  
807  C C   . GLY A 118 ? 0.9176 0.4634 0.4958 -0.0272 0.0732  -0.0318 117 GLY A C   
808  O O   . GLY A 118 ? 1.0495 0.6066 0.6341 -0.0310 0.0725  -0.0280 117 GLY A O   
809  N N   . LEU A 119 ? 0.9578 0.4957 0.5372 -0.0247 0.0721  -0.0316 118 LEU A N   
810  C CA  . LEU A 119 ? 0.9840 0.5258 0.5713 -0.0261 0.0704  -0.0275 118 LEU A CA  
811  C C   . LEU A 119 ? 0.9229 0.4762 0.5211 -0.0233 0.0703  -0.0245 118 LEU A C   
812  O O   . LEU A 119 ? 0.8946 0.4555 0.4999 -0.0260 0.0697  -0.0208 118 LEU A O   
813  C CB  . LEU A 119 ? 0.9820 0.5126 0.5667 -0.0242 0.0692  -0.0284 118 LEU A CB  
814  C CG  . LEU A 119 ? 0.9745 0.5069 0.5649 -0.0259 0.0679  -0.0250 118 LEU A CG  
815  C CD1 . LEU A 119 ? 0.9227 0.4574 0.5123 -0.0318 0.0677  -0.0226 118 LEU A CD1 
816  C CD2 . LEU A 119 ? 0.8958 0.4182 0.4832 -0.0235 0.0668  -0.0258 118 LEU A CD2 
817  N N   . VAL A 120 ? 0.8697 0.4243 0.4697 -0.0180 0.0710  -0.0255 119 VAL A N   
818  C CA  . VAL A 120 ? 0.8617 0.4272 0.4719 -0.0159 0.0705  -0.0221 119 VAL A CA  
819  C C   . VAL A 120 ? 0.9486 0.5267 0.5633 -0.0183 0.0713  -0.0200 119 VAL A C   
820  O O   . VAL A 120 ? 0.9754 0.5628 0.5994 -0.0194 0.0704  -0.0161 119 VAL A O   
821  C CB  . VAL A 120 ? 0.8642 0.4292 0.4755 -0.0098 0.0709  -0.0226 119 VAL A CB  
822  C CG1 . VAL A 120 ? 1.0015 0.5762 0.6233 -0.0086 0.0692  -0.0185 119 VAL A CG1 
823  C CG2 . VAL A 120 ? 0.9554 0.5076 0.5608 -0.0075 0.0704  -0.0247 119 VAL A CG2 
824  N N   . ARG A 121 ? 0.9442 0.5227 0.5521 -0.0193 0.0731  -0.0225 120 ARG A N   
825  C CA  . ARG A 121 ? 0.9435 0.5349 0.5549 -0.0220 0.0739  -0.0202 120 ARG A CA  
826  C C   . ARG A 121 ? 0.9437 0.5402 0.5594 -0.0280 0.0726  -0.0165 120 ARG A C   
827  O O   . ARG A 121 ? 1.0073 0.6162 0.6321 -0.0295 0.0724  -0.0121 120 ARG A O   
828  C CB  . ARG A 121 ? 0.8950 0.4842 0.4960 -0.0223 0.0762  -0.0244 120 ARG A CB  
829  C CG  . ARG A 121 ? 0.9361 0.5296 0.5374 -0.0162 0.0785  -0.0256 120 ARG A CG  
830  C CD  . ARG A 121 ? 0.9687 0.5614 0.5594 -0.0172 0.0813  -0.0296 120 ARG A CD  
831  N NE  . ARG A 121 ? 0.9527 0.5297 0.5303 -0.0198 0.0817  -0.0347 120 ARG A NE  
832  C CZ  . ARG A 121 ? 0.9562 0.5194 0.5254 -0.0151 0.0837  -0.0394 120 ARG A CZ  
833  N NH1 . ARG A 121 ? 0.8714 0.4353 0.4444 -0.0072 0.0859  -0.0393 120 ARG A NH1 
834  N NH2 . ARG A 121 ? 0.9987 0.5473 0.5562 -0.0185 0.0836  -0.0436 120 ARG A NH2 
835  N N   . LEU A 122 ? 0.8615 0.4490 0.4712 -0.0314 0.0720  -0.0176 121 LEU A N   
836  C CA  . LEU A 122 ? 0.9508 0.5436 0.5652 -0.0366 0.0712  -0.0132 121 LEU A CA  
837  C C   . LEU A 122 ? 1.0087 0.6045 0.6339 -0.0349 0.0707  -0.0093 121 LEU A C   
838  O O   . LEU A 122 ? 1.0092 0.6135 0.6421 -0.0377 0.0709  -0.0044 121 LEU A O   
839  C CB  . LEU A 122 ? 0.9375 0.5200 0.5433 -0.0402 0.0706  -0.0147 121 LEU A CB  
840  C CG  . LEU A 122 ? 1.1574 0.7457 0.7666 -0.0460 0.0701  -0.0096 121 LEU A CG  
841  C CD1 . LEU A 122 ? 1.0115 0.6149 0.6262 -0.0494 0.0704  -0.0054 121 LEU A CD1 
842  C CD2 . LEU A 122 ? 0.8596 0.4389 0.4583 -0.0505 0.0691  -0.0113 121 LEU A CD2 
843  N N   . VAL A 123 ? 0.9779 0.5669 0.6036 -0.0305 0.0702  -0.0112 122 VAL A N   
844  C CA  . VAL A 123 ? 0.9337 0.5236 0.5677 -0.0294 0.0695  -0.0084 122 VAL A CA  
845  C C   . VAL A 123 ? 0.9954 0.5981 0.6397 -0.0293 0.0696  -0.0045 122 VAL A C   
846  O O   . VAL A 123 ? 0.9697 0.5752 0.6217 -0.0303 0.0696  -0.0009 122 VAL A O   
847  C CB  . VAL A 123 ? 0.8422 0.4230 0.4734 -0.0255 0.0684  -0.0113 122 VAL A CB  
848  C CG1 . VAL A 123 ? 0.9141 0.4977 0.5534 -0.0242 0.0674  -0.0089 122 VAL A CG1 
849  C CG2 . VAL A 123 ? 0.8359 0.4049 0.4599 -0.0263 0.0682  -0.0133 122 VAL A CG2 
850  N N   . ALA A 124 ? 0.9403 0.5506 0.5845 -0.0282 0.0699  -0.0049 123 ALA A N   
851  C CA  . ALA A 124 ? 0.9967 0.6204 0.6508 -0.0285 0.0698  -0.0006 123 ALA A CA  
852  C C   . ALA A 124 ? 0.9668 0.5982 0.6273 -0.0328 0.0704  0.0043  123 ALA A C   
853  O O   . ALA A 124 ? 0.9624 0.6013 0.6333 -0.0331 0.0702  0.0089  123 ALA A O   
854  C CB  . ALA A 124 ? 0.9222 0.5533 0.5735 -0.0269 0.0707  -0.0019 123 ALA A CB  
855  N N   . LEU A 125 ? 0.8911 0.5211 0.5461 -0.0363 0.0711  0.0041  124 LEU A N   
856  C CA  . LEU A 125 ? 0.9777 0.6152 0.6394 -0.0402 0.0717  0.0098  124 LEU A CA  
857  C C   . LEU A 125 ? 1.0335 0.6631 0.6986 -0.0396 0.0723  0.0113  124 LEU A C   
858  O O   . LEU A 125 ? 1.0459 0.6811 0.7206 -0.0404 0.0733  0.0167  124 LEU A O   
859  C CB  . LEU A 125 ? 0.9746 0.6145 0.6291 -0.0449 0.0719  0.0098  124 LEU A CB  
860  C CG  . LEU A 125 ? 0.9867 0.6359 0.6479 -0.0496 0.0724  0.0168  124 LEU A CG  
861  C CD1 . LEU A 125 ? 0.9115 0.5720 0.5697 -0.0545 0.0720  0.0187  124 LEU A CD1 
862  C CD2 . LEU A 125 ? 1.0141 0.6545 0.6717 -0.0511 0.0728  0.0172  124 LEU A CD2 
863  N N   . VAL A 126 ? 0.9735 0.5901 0.6307 -0.0379 0.0720  0.0068  125 VAL A N   
864  C CA  . VAL A 126 ? 0.9703 0.5789 0.6288 -0.0372 0.0729  0.0076  125 VAL A CA  
865  C C   . VAL A 126 ? 0.9075 0.5147 0.5732 -0.0346 0.0729  0.0085  125 VAL A C   
866  O O   . VAL A 126 ? 0.9424 0.5482 0.6136 -0.0347 0.0745  0.0116  125 VAL A O   
867  C CB  . VAL A 126 ? 0.8608 0.4565 0.5086 -0.0363 0.0722  0.0027  125 VAL A CB  
868  C CG1 . VAL A 126 ? 0.9236 0.5108 0.5718 -0.0351 0.0733  0.0030  125 VAL A CG1 
869  C CG2 . VAL A 126 ? 0.9300 0.5260 0.5708 -0.0400 0.0722  0.0025  125 VAL A CG2 
870  N N   . GLN A 127 ? 0.8948 0.5025 0.5605 -0.0325 0.0711  0.0062  126 GLN A N   
871  C CA  . GLN A 127 ? 0.9177 0.5238 0.5894 -0.0310 0.0703  0.0070  126 GLN A CA  
872  C C   . GLN A 127 ? 0.9907 0.6065 0.6738 -0.0324 0.0713  0.0128  126 GLN A C   
873  O O   . GLN A 127 ? 0.9731 0.5853 0.6612 -0.0320 0.0713  0.0141  126 GLN A O   
874  C CB  . GLN A 127 ? 0.8969 0.5035 0.5668 -0.0287 0.0680  0.0045  126 GLN A CB  
875  C CG  . GLN A 127 ? 0.9392 0.5581 0.6120 -0.0285 0.0677  0.0059  126 GLN A CG  
876  C CD  . GLN A 127 ? 0.9611 0.5906 0.6450 -0.0292 0.0670  0.0109  126 GLN A CD  
877  O OE1 . GLN A 127 ? 1.0314 0.6576 0.7199 -0.0293 0.0660  0.0122  126 GLN A OE1 
878  N NE2 . GLN A 127 ? 0.9456 0.5879 0.6334 -0.0302 0.0676  0.0137  126 GLN A NE2 
879  N N   . MET A 128 ? 0.9530 0.5806 0.6401 -0.0343 0.0720  0.0164  127 MET A N   
880  C CA  . MET A 128 ? 1.0191 0.6565 0.7179 -0.0358 0.0731  0.0230  127 MET A CA  
881  C C   . MET A 128 ? 0.9300 0.5620 0.6319 -0.0362 0.0758  0.0258  127 MET A C   
882  O O   . MET A 128 ? 0.8743 0.5065 0.5849 -0.0358 0.0771  0.0296  127 MET A O   
883  C CB  . MET A 128 ? 0.9643 0.6164 0.6658 -0.0383 0.0731  0.0265  127 MET A CB  
884  C CG  . MET A 128 ? 0.9799 0.6414 0.6839 -0.0376 0.0713  0.0266  127 MET A CG  
885  S SD  . MET A 128 ? 1.2789 0.9539 0.9792 -0.0403 0.0714  0.0274  127 MET A SD  
886  C CE  . MET A 128 ? 1.1823 0.8570 0.8807 -0.0443 0.0730  0.0302  127 MET A CE  
887  N N   . GLY A 129 ? 0.8185 0.4453 0.5135 -0.0367 0.0770  0.0244  128 GLY A N   
888  C CA  . GLY A 129 ? 0.8253 0.4464 0.5226 -0.0362 0.0801  0.0270  128 GLY A CA  
889  C C   . GLY A 129 ? 0.9361 0.5433 0.6307 -0.0335 0.0808  0.0232  128 GLY A C   
890  O O   . GLY A 129 ? 0.9931 0.5956 0.6920 -0.0324 0.0839  0.0258  128 GLY A O   
891  N N   . ILE A 130 ? 0.9558 0.5560 0.6429 -0.0326 0.0779  0.0173  129 ILE A N   
892  C CA  . ILE A 130 ? 1.0010 0.5891 0.6851 -0.0310 0.0777  0.0138  129 ILE A CA  
893  C C   . ILE A 130 ? 0.9573 0.5473 0.6506 -0.0312 0.0779  0.0169  129 ILE A C   
894  O O   . ILE A 130 ? 0.9887 0.5705 0.6838 -0.0305 0.0804  0.0175  129 ILE A O   
895  C CB  . ILE A 130 ? 0.9527 0.5356 0.6282 -0.0304 0.0742  0.0082  129 ILE A CB  
896  C CG1 . ILE A 130 ? 1.0243 0.6023 0.6903 -0.0300 0.0743  0.0050  129 ILE A CG1 
897  C CG2 . ILE A 130 ? 0.8989 0.4715 0.5719 -0.0299 0.0730  0.0054  129 ILE A CG2 
898  C CD1 . ILE A 130 ? 0.9537 0.5246 0.6171 -0.0298 0.0775  0.0056  129 ILE A CD1 
899  N N   . ALA A 131 ? 0.9356 0.5362 0.6347 -0.0321 0.0754  0.0190  130 ALA A N   
900  C CA  . ALA A 131 ? 1.0391 0.6417 0.7469 -0.0328 0.0746  0.0220  130 ALA A CA  
901  C C   . ALA A 131 ? 1.0031 0.6083 0.7206 -0.0329 0.0784  0.0280  130 ALA A C   
902  O O   . ALA A 131 ? 1.0397 0.6363 0.7602 -0.0326 0.0798  0.0286  130 ALA A O   
903  C CB  . ALA A 131 ? 0.9552 0.5710 0.6678 -0.0337 0.0714  0.0240  130 ALA A CB  
904  N N   . TRP A 132 ? 0.8963 0.5130 0.6187 -0.0335 0.0801  0.0326  131 TRP A N   
905  C CA  . TRP A 132 ? 0.9034 0.5250 0.6368 -0.0335 0.0837  0.0398  131 TRP A CA  
906  C C   . TRP A 132 ? 0.9857 0.5950 0.7165 -0.0313 0.0882  0.0393  131 TRP A C   
907  O O   . TRP A 132 ? 1.0667 0.6715 0.8045 -0.0300 0.0915  0.0428  131 TRP A O   
908  C CB  . TRP A 132 ? 0.8746 0.5129 0.6132 -0.0354 0.0839  0.0455  131 TRP A CB  
909  C CG  . TRP A 132 ? 0.8682 0.5198 0.6114 -0.0372 0.0805  0.0473  131 TRP A CG  
910  C CD1 . TRP A 132 ? 0.9743 0.6329 0.7112 -0.0384 0.0778  0.0444  131 TRP A CD1 
911  C CD2 . TRP A 132 ? 0.8998 0.5588 0.6546 -0.0379 0.0798  0.0526  131 TRP A CD2 
912  N NE1 . TRP A 132 ? 0.8836 0.5544 0.6274 -0.0395 0.0757  0.0475  131 TRP A NE1 
913  C CE2 . TRP A 132 ? 0.9457 0.6176 0.7010 -0.0394 0.0766  0.0529  131 TRP A CE2 
914  C CE3 . TRP A 132 ? 0.9927 0.6484 0.7576 -0.0372 0.0818  0.0573  131 TRP A CE3 
915  C CZ2 . TRP A 132 ? 0.8935 0.5762 0.6592 -0.0406 0.0751  0.0582  131 TRP A CZ2 
916  C CZ3 . TRP A 132 ? 0.7459 0.4114 0.5213 -0.0386 0.0800  0.0624  131 TRP A CZ3 
917  C CH2 . TRP A 132 ? 0.8257 0.5053 0.6017 -0.0404 0.0765  0.0631  131 TRP A CH2 
918  N N   . GLY A 133 ? 0.9321 0.5356 0.6528 -0.0307 0.0887  0.0352  132 GLY A N   
919  C CA  . GLY A 133 ? 0.9808 0.5728 0.6982 -0.0283 0.0932  0.0346  132 GLY A CA  
920  C C   . GLY A 133 ? 0.9966 0.5730 0.7104 -0.0268 0.0940  0.0302  132 GLY A C   
921  O O   . GLY A 133 ? 1.0339 0.6026 0.7509 -0.0246 0.0988  0.0322  132 GLY A O   
922  N N   . ASN A 134 ? 0.9906 0.5618 0.6976 -0.0281 0.0895  0.0244  133 ASN A N   
923  C CA  . ASN A 134 ? 1.1240 0.6805 0.8264 -0.0280 0.0893  0.0201  133 ASN A CA  
924  C C   . ASN A 134 ? 1.1037 0.6604 0.8165 -0.0285 0.0905  0.0244  133 ASN A C   
925  O O   . ASN A 134 ? 1.0500 0.5932 0.7613 -0.0275 0.0937  0.0230  133 ASN A O   
926  C CB  . ASN A 134 ? 1.1344 0.6884 0.8285 -0.0299 0.0836  0.0145  133 ASN A CB  
927  C CG  . ASN A 134 ? 1.0241 0.5733 0.7067 -0.0292 0.0829  0.0096  133 ASN A CG  
928  O OD1 . ASN A 134 ? 0.9481 0.4951 0.6282 -0.0276 0.0866  0.0101  133 ASN A OD1 
929  N ND2 . ASN A 134 ? 1.0070 0.5551 0.6832 -0.0304 0.0782  0.0056  133 ASN A ND2 
930  N N   . LEU A 135 ? 1.1149 0.6861 0.8379 -0.0300 0.0881  0.0295  134 LEU A N   
931  C CA  . LEU A 135 ? 1.0903 0.6630 0.8244 -0.0307 0.0889  0.0345  134 LEU A CA  
932  C C   . LEU A 135 ? 0.9562 0.5263 0.6977 -0.0279 0.0956  0.0398  134 LEU A C   
933  O O   . LEU A 135 ? 0.7959 0.3562 0.5414 -0.0272 0.0983  0.0410  134 LEU A O   
934  C CB  . LEU A 135 ? 1.1080 0.6992 0.8517 -0.0327 0.0852  0.0397  134 LEU A CB  
935  C CG  . LEU A 135 ? 1.1386 0.7351 0.8953 -0.0341 0.0847  0.0459  134 LEU A CG  
936  C CD1 . LEU A 135 ? 0.9675 0.5721 0.7365 -0.0326 0.0895  0.0544  134 LEU A CD1 
937  C CD2 . LEU A 135 ? 0.9901 0.5695 0.7437 -0.0351 0.0842  0.0425  134 LEU A CD2 
938  N N   . LEU A 136 ? 0.9221 0.5007 0.6654 -0.0263 0.0985  0.0432  135 LEU A N   
939  C CA  . LEU A 136 ? 0.8950 0.4729 0.6459 -0.0232 0.1052  0.0494  135 LEU A CA  
940  C C   . LEU A 136 ? 0.9941 0.5523 0.7364 -0.0200 0.1101  0.0445  135 LEU A C   
941  O O   . LEU A 136 ? 1.0268 0.5783 0.7752 -0.0169 0.1160  0.0482  135 LEU A O   
942  C CB  . LEU A 136 ? 0.9480 0.5408 0.7022 -0.0231 0.1064  0.0546  135 LEU A CB  
943  C CG  . LEU A 136 ? 0.9770 0.5899 0.7447 -0.0252 0.1052  0.0637  135 LEU A CG  
944  C CD1 . LEU A 136 ? 0.9165 0.5380 0.6832 -0.0288 0.0987  0.0613  135 LEU A CD1 
945  C CD2 . LEU A 136 ? 0.9041 0.5290 0.6728 -0.0257 0.1066  0.0684  135 LEU A CD2 
946  N N   . LEU A 137 ? 1.0178 0.5667 0.7458 -0.0204 0.1081  0.0364  136 LEU A N   
947  C CA  . LEU A 137 ? 0.9731 0.5033 0.6913 -0.0178 0.1124  0.0311  136 LEU A CA  
948  C C   . LEU A 137 ? 0.9917 0.5067 0.7072 -0.0190 0.1119  0.0271  136 LEU A C   
949  O O   . LEU A 137 ? 0.9826 0.4836 0.6970 -0.0162 0.1178  0.0266  136 LEU A O   
950  C CB  . LEU A 137 ? 0.9322 0.4580 0.6362 -0.0185 0.1099  0.0243  136 LEU A CB  
951  C CG  . LEU A 137 ? 0.9098 0.4465 0.6142 -0.0174 0.1113  0.0276  136 LEU A CG  
952  C CD1 . LEU A 137 ? 0.9798 0.5129 0.6710 -0.0188 0.1074  0.0209  136 LEU A CD1 
953  C CD2 . LEU A 137 ? 0.9616 0.4950 0.6695 -0.0130 0.1193  0.0322  136 LEU A CD2 
954  N N   . ALA A 138 ? 0.9419 0.4591 0.6560 -0.0232 0.1050  0.0245  137 ALA A N   
955  C CA  . ALA A 138 ? 1.0202 0.5244 0.7325 -0.0255 0.1035  0.0216  137 ALA A CA  
956  C C   . ALA A 138 ? 1.1164 0.6198 0.8417 -0.0239 0.1079  0.0282  137 ALA A C   
957  O O   . ALA A 138 ? 1.0615 0.5480 0.7838 -0.0241 0.1102  0.0257  137 ALA A O   
958  C CB  . ALA A 138 ? 1.0288 0.5400 0.7402 -0.0303 0.0952  0.0198  137 ALA A CB  
959  N N   . LEU A 139 ? 1.0526 0.5736 0.7919 -0.0227 0.1089  0.0367  138 LEU A N   
960  C CA  . LEU A 139 ? 0.9950 0.5169 0.7483 -0.0207 0.1137  0.0444  138 LEU A CA  
961  C C   . LEU A 139 ? 1.0871 0.5942 0.8382 -0.0154 0.1227  0.0443  138 LEU A C   
962  O O   . LEU A 139 ? 1.1874 0.6798 0.9404 -0.0140 0.1266  0.0445  138 LEU A O   
963  C CB  . LEU A 139 ? 0.9517 0.4972 0.7196 -0.0206 0.1130  0.0540  138 LEU A CB  
964  C CG  . LEU A 139 ? 0.8731 0.4320 0.6518 -0.0244 0.1076  0.0589  138 LEU A CG  
965  C CD1 . LEU A 139 ? 0.8352 0.3909 0.6048 -0.0287 0.1002  0.0520  138 LEU A CD1 
966  C CD2 . LEU A 139 ? 0.9203 0.5033 0.7087 -0.0249 0.1064  0.0665  138 LEU A CD2 
967  N N   . MET A 140 ? 0.9733 0.4837 0.7202 -0.0122 0.1262  0.0443  139 MET A N   
968  C CA  . MET A 140 ? 1.0688 0.5670 0.8139 -0.0065 0.1353  0.0449  139 MET A CA  
969  C C   . MET A 140 ? 1.1046 0.5778 0.8340 -0.0062 0.1373  0.0350  139 MET A C   
970  O O   . MET A 140 ? 1.0708 0.5296 0.7992 -0.0016 0.1454  0.0351  139 MET A O   
971  C CB  . MET A 140 ? 1.0094 0.5181 0.7530 -0.0040 0.1377  0.0473  139 MET A CB  
972  C CG  . MET A 140 ? 0.9693 0.5012 0.7283 -0.0039 0.1376  0.0582  139 MET A CG  
973  S SD  . MET A 140 ? 1.1385 0.6785 0.8987 0.0004  0.1439  0.0639  139 MET A SD  
974  C CE  . MET A 140 ? 0.9571 0.5208 0.7196 -0.0052 0.1358  0.0669  139 MET A CE  
975  N N   . LYS A 141 ? 1.1553 0.6230 0.8722 -0.0111 0.1302  0.0267  140 LYS A N   
976  C CA  . LYS A 141 ? 1.2123 0.6568 0.9138 -0.0123 0.1311  0.0174  140 LYS A CA  
977  C C   . LYS A 141 ? 1.3270 0.7584 1.0323 -0.0139 0.1319  0.0177  140 LYS A C   
978  O O   . LYS A 141 ? 1.3882 0.7991 1.0867 -0.0115 0.1382  0.0141  140 LYS A O   
979  C CB  . LYS A 141 ? 1.1288 0.5731 0.8172 -0.0177 0.1227  0.0099  140 LYS A CB  
980  C CG  . LYS A 141 ? 1.1331 0.5865 0.8154 -0.0164 0.1219  0.0085  140 LYS A CG  
981  C CD  . LYS A 141 ? 1.2205 0.6735 0.8912 -0.0214 0.1138  0.0018  140 LYS A CD  
982  C CE  . LYS A 141 ? 1.1923 0.6644 0.8666 -0.0219 0.1093  0.0044  140 LYS A CE  
983  N NZ  . LYS A 141 ? 1.1692 0.6458 0.8394 -0.0268 0.1007  0.0011  140 LYS A NZ  
984  N N   . GLY A 142 ? 1.1894 0.6322 0.9054 -0.0179 0.1258  0.0221  141 GLY A N   
985  C CA  . GLY A 142 ? 1.0718 0.5030 0.7919 -0.0203 0.1255  0.0229  141 GLY A CA  
986  C C   . GLY A 142 ? 1.1770 0.6020 0.9083 -0.0147 0.1347  0.0293  141 GLY A C   
987  O O   . GLY A 142 ? 1.2176 0.6268 0.9496 -0.0159 0.1363  0.0286  141 GLY A O   
988  N N   . PHE A 143 ? 1.1679 0.6051 0.9083 -0.0088 0.1406  0.0360  142 PHE A N   
989  C CA  . PHE A 143 ? 1.1132 0.5455 0.8646 -0.0024 0.1503  0.0430  142 PHE A CA  
990  C C   . PHE A 143 ? 1.2582 0.6719 0.9980 0.0036  0.1596  0.0380  142 PHE A C   
991  O O   . PHE A 143 ? 1.2541 0.6659 1.0028 0.0105  0.1690  0.0444  142 PHE A O   
992  C CB  . PHE A 143 ? 1.0962 0.5545 0.8661 0.0004  0.1516  0.0551  142 PHE A CB  
993  C CG  . PHE A 143 ? 1.2486 0.7250 1.0326 -0.0043 0.1446  0.0620  142 PHE A CG  
994  C CD1 . PHE A 143 ? 1.2927 0.7838 1.0960 -0.0016 0.1480  0.0743  142 PHE A CD1 
995  C CD2 . PHE A 143 ? 1.2507 0.7309 1.0291 -0.0112 0.1348  0.0571  142 PHE A CD2 
996  C CE1 . PHE A 143 ? 1.2609 0.7697 1.0772 -0.0059 0.1418  0.0810  142 PHE A CE1 
997  C CE2 . PHE A 143 ? 1.2026 0.7003 0.9940 -0.0150 0.1290  0.0638  142 PHE A CE2 
998  C CZ  . PHE A 143 ? 1.2159 0.7277 1.0258 -0.0125 0.1324  0.0755  142 PHE A CZ  
999  N N   . ARG A 144 ? 1.3401 0.7410 1.0604 0.0011  0.1573  0.0271  143 ARG A N   
1000 C CA  . ARG A 144 ? 1.3594 0.7431 1.0661 0.0062  0.1656  0.0213  143 ARG A CA  
1001 C C   . ARG A 144 ? 1.3748 0.7731 1.0894 0.0131  0.1722  0.0286  143 ARG A C   
1002 O O   . ARG A 144 ? 1.4481 0.8354 1.1603 0.0200  0.1823  0.0291  143 ARG A O   
1003 C CB  . ARG A 144 ? 1.4594 0.8168 1.1621 0.0091  0.1735  0.0183  143 ARG A CB  
1004 C CG  . ARG A 144 ? 1.4633 0.8073 1.1617 0.0018  0.1670  0.0135  143 ARG A CG  
1005 C CD  . ARG A 144 ? 1.5844 0.9184 1.2620 -0.0053 0.1595  0.0019  143 ARG A CD  
1006 N NE  . ARG A 144 ? 1.6543 0.9730 1.3264 -0.0126 0.1540  -0.0027 143 ARG A NE  
1007 C CZ  . ARG A 144 ? 1.6693 0.9836 1.3277 -0.0208 0.1449  -0.0102 143 ARG A CZ  
1008 N NH1 . ARG A 144 ? 1.6772 1.0006 1.3260 -0.0225 0.1405  -0.0143 143 ARG A NH1 
1009 N NH2 . ARG A 144 ? 1.6189 0.9198 1.2736 -0.0277 0.1402  -0.0131 143 ARG A NH2 
1010 N N   . ASP A 145 ? 1.2478 0.6709 0.9714 0.0111  0.1665  0.0345  144 ASP A N   
1011 C CA  . ASP A 145 ? 1.1711 0.6104 0.9023 0.0160  0.1712  0.0421  144 ASP A CA  
1012 C C   . ASP A 145 ? 1.2361 0.6769 0.9526 0.0146  0.1683  0.0356  144 ASP A C   
1013 O O   . ASP A 145 ? 1.2085 0.6669 0.9268 0.0112  0.1618  0.0373  144 ASP A O   
1014 C CB  . ASP A 145 ? 0.9567 0.4219 0.7065 0.0142  0.1671  0.0531  144 ASP A CB  
1015 C CG  . ASP A 145 ? 1.0381 0.5201 0.7979 0.0189  0.1724  0.0629  144 ASP A CG  
1016 O OD1 . ASP A 145 ? 0.9570 0.4300 0.7121 0.0248  0.1807  0.0626  144 ASP A OD1 
1017 O OD2 . ASP A 145 ? 1.1351 0.6395 0.9071 0.0164  0.1683  0.0711  144 ASP A OD2 
1018 N N   . ALA A 146 ? 1.2102 0.6311 0.9115 0.0173  0.1735  0.0278  145 ALA A N   
1019 C CA  . ALA A 146 ? 1.1907 0.6112 0.8774 0.0162  0.1714  0.0215  145 ALA A CA  
1020 C C   . ALA A 146 ? 1.2049 0.6431 0.8990 0.0202  0.1749  0.0296  145 ALA A C   
1021 O O   . ALA A 146 ? 1.1716 0.6182 0.8590 0.0175  0.1700  0.0274  145 ALA A O   
1022 C CB  . ALA A 146 ? 1.3566 0.7522 1.0253 0.0183  0.1770  0.0120  145 ALA A CB  
1023 N N   . ALA A 147 ? 1.0793 0.5234 0.7875 0.0263  0.1831  0.0395  146 ALA A N   
1024 C CA  . ALA A 147 ? 1.1920 0.6539 0.9082 0.0296  0.1863  0.0485  146 ALA A CA  
1025 C C   . ALA A 147 ? 1.2076 0.6932 0.9332 0.0239  0.1774  0.0542  146 ALA A C   
1026 O O   . ALA A 147 ? 1.1451 0.6413 0.8666 0.0217  0.1738  0.0544  146 ALA A O   
1027 C CB  . ALA A 147 ? 1.0471 0.5101 0.7772 0.0375  0.1974  0.0587  146 ALA A CB  
1028 N N   . GLY A 148 ? 1.1188 0.6126 0.8568 0.0212  0.1738  0.0588  147 GLY A N   
1029 C CA  . GLY A 148 ? 1.0430 0.5584 0.7887 0.0157  0.1656  0.0636  147 GLY A CA  
1030 C C   . GLY A 148 ? 1.0475 0.5621 0.7800 0.0095  0.1562  0.0541  147 GLY A C   
1031 O O   . GLY A 148 ? 1.0373 0.5675 0.7709 0.0058  0.1507  0.0563  147 GLY A O   
1032 N N   . ASN A 149 ? 1.0644 0.5608 0.7841 0.0081  0.1542  0.0437  148 ASN A N   
1033 C CA  . ASN A 149 ? 1.0440 0.5393 0.7513 0.0027  0.1457  0.0353  148 ASN A CA  
1034 C C   . ASN A 149 ? 1.1519 0.6468 0.8484 0.0036  0.1464  0.0324  148 ASN A C   
1035 O O   . ASN A 149 ? 1.0647 0.5706 0.7588 0.0000  0.1404  0.0320  148 ASN A O   
1036 C CB  . ASN A 149 ? 0.9556 0.4323 0.6525 0.0005  0.1433  0.0261  148 ASN A CB  
1037 C CG  . ASN A 149 ? 1.0438 0.5245 0.7346 -0.0057 0.1333  0.0206  148 ASN A CG  
1038 O OD1 . ASN A 149 ? 1.0783 0.5635 0.7754 -0.0089 0.1286  0.0217  148 ASN A OD1 
1039 N ND2 . ASN A 149 ? 1.0675 0.5470 0.7463 -0.0071 0.1303  0.0152  148 ASN A ND2 
1040 N N   . ALA A 150 ? 1.4215 0.9035 1.1111 0.0084  0.1539  0.0305  149 ALA A N   
1041 C CA  . ALA A 150 ? 1.4349 0.9164 1.1142 0.0093  0.1549  0.0280  149 ALA A CA  
1042 C C   . ALA A 150 ? 1.4108 0.9118 1.0997 0.0098  0.1554  0.0374  149 ALA A C   
1043 O O   . ALA A 150 ? 1.4072 0.9140 1.0897 0.0073  0.1513  0.0360  149 ALA A O   
1044 C CB  . ALA A 150 ? 1.4467 0.9108 1.1171 0.0148  0.1638  0.0246  149 ALA A CB  
1045 N N   . LEU A 151 ? 1.1095 0.6208 0.8138 0.0127  0.1601  0.0475  150 LEU A N   
1046 C CA  . LEU A 151 ? 1.0897 0.6208 0.8035 0.0122  0.1599  0.0574  150 LEU A CA  
1047 C C   . LEU A 151 ? 1.0668 0.6112 0.7816 0.0051  0.1501  0.0571  150 LEU A C   
1048 O O   . LEU A 151 ? 1.1088 0.6615 0.8196 0.0023  0.1466  0.0579  150 LEU A O   
1049 C CB  . LEU A 151 ? 1.0893 0.6295 0.8204 0.0164  0.1668  0.0691  150 LEU A CB  
1050 C CG  . LEU A 151 ? 1.0271 0.5846 0.7670 0.0179  0.1701  0.0806  150 LEU A CG  
1051 C CD1 . LEU A 151 ? 1.0794 0.6325 0.8071 0.0190  0.1715  0.0772  150 LEU A CD1 
1052 C CD2 . LEU A 151 ? 1.0658 0.6269 0.8206 0.0245  0.1798  0.0913  150 LEU A CD2 
1053 N N   . SER A 152 ? 1.0057 0.5516 0.7252 0.0023  0.1457  0.0557  151 SER A N   
1054 C CA  . SER A 152 ? 1.0394 0.5967 0.7586 -0.0039 0.1369  0.0545  151 SER A CA  
1055 C C   . SER A 152 ? 1.0861 0.6364 0.7900 -0.0067 0.1315  0.0452  151 SER A C   
1056 O O   . SER A 152 ? 1.0582 0.6183 0.7602 -0.0107 0.1261  0.0455  151 SER A O   
1057 C CB  . SER A 152 ? 0.9301 0.4881 0.6556 -0.0059 0.1335  0.0536  151 SER A CB  
1058 O OG  . SER A 152 ? 0.9236 0.4901 0.6645 -0.0038 0.1379  0.0632  151 SER A OG  
1059 N N   . LEU A 153 ? 1.1085 0.6416 0.8012 -0.0048 0.1329  0.0372  152 LEU A N   
1060 C CA  . LEU A 153 ? 0.9860 0.5127 0.6646 -0.0072 0.1281  0.0292  152 LEU A CA  
1061 C C   . LEU A 153 ? 1.0907 0.6209 0.7650 -0.0063 0.1301  0.0316  152 LEU A C   
1062 O O   . LEU A 153 ? 0.9758 0.5080 0.6427 -0.0094 0.1250  0.0284  152 LEU A O   
1063 C CB  . LEU A 153 ? 0.8551 0.3634 0.5229 -0.0062 0.1289  0.0206  152 LEU A CB  
1064 C CG  . LEU A 153 ? 0.8761 0.3801 0.5439 -0.0091 0.1239  0.0161  152 LEU A CG  
1065 C CD1 . LEU A 153 ? 0.9115 0.3971 0.5668 -0.0091 0.1243  0.0078  152 LEU A CD1 
1066 C CD2 . LEU A 153 ? 0.7765 0.2906 0.4437 -0.0135 0.1157  0.0147  152 LEU A CD2 
1067 N N   . ILE A 154 ? 1.0341 0.5652 0.7134 -0.0019 0.1377  0.0377  153 ILE A N   
1068 C CA  . ILE A 154 ? 1.0150 0.5509 0.6913 -0.0010 0.1399  0.0413  153 ILE A CA  
1069 C C   . ILE A 154 ? 1.0024 0.5561 0.6858 -0.0053 0.1356  0.0483  153 ILE A C   
1070 O O   . ILE A 154 ? 1.0705 0.6269 0.7471 -0.0086 0.1313  0.0468  153 ILE A O   
1071 C CB  . ILE A 154 ? 1.0015 0.5342 0.6818 0.0054  0.1498  0.0466  153 ILE A CB  
1072 C CG1 . ILE A 154 ? 1.1151 0.6280 0.7829 0.0088  0.1538  0.0379  153 ILE A CG1 
1073 C CG2 . ILE A 154 ? 0.8830 0.4266 0.5650 0.0059  0.1519  0.0540  153 ILE A CG2 
1074 C CD1 . ILE A 154 ? 1.1444 0.6512 0.8156 0.0160  0.1646  0.0419  153 ILE A CD1 
1075 N N   . VAL A 155 ? 0.9953 0.5611 0.6922 -0.0058 0.1365  0.0562  154 VAL A N   
1076 C CA  . VAL A 155 ? 1.0203 0.6032 0.7232 -0.0108 0.1321  0.0629  154 VAL A CA  
1077 C C   . VAL A 155 ? 0.9514 0.5340 0.6464 -0.0163 0.1236  0.0558  154 VAL A C   
1078 O O   . VAL A 155 ? 0.9660 0.5553 0.6573 -0.0206 0.1193  0.0567  154 VAL A O   
1079 C CB  . VAL A 155 ? 1.0056 0.6020 0.7245 -0.0105 0.1346  0.0728  154 VAL A CB  
1080 C CG1 . VAL A 155 ? 0.8476 0.4624 0.5725 -0.0153 0.1320  0.0820  154 VAL A CG1 
1081 C CG2 . VAL A 155 ? 0.9370 0.5291 0.6635 -0.0035 0.1439  0.0780  154 VAL A CG2 
1082 N N   . GLY A 156 ? 1.0214 0.5961 0.7139 -0.0162 0.1210  0.0487  155 GLY A N   
1083 C CA  . GLY A 156 ? 1.0393 0.6140 0.7251 -0.0205 0.1136  0.0425  155 GLY A CA  
1084 C C   . GLY A 156 ? 1.0517 0.6185 0.7244 -0.0216 0.1107  0.0362  155 GLY A C   
1085 O O   . GLY A 156 ? 1.0497 0.6204 0.7180 -0.0256 0.1056  0.0346  155 GLY A O   
1086 N N   . SER A 157 ? 1.0154 0.5702 0.6813 -0.0182 0.1141  0.0327  156 SER A N   
1087 C CA  . SER A 157 ? 0.9939 0.5418 0.6480 -0.0192 0.1116  0.0277  156 SER A CA  
1088 C C   . SER A 157 ? 1.0021 0.5583 0.6566 -0.0210 0.1120  0.0337  156 SER A C   
1089 O O   . SER A 157 ? 1.0169 0.5716 0.6636 -0.0238 0.1077  0.0309  156 SER A O   
1090 C CB  . SER A 157 ? 1.0504 0.5843 0.6967 -0.0154 0.1153  0.0227  156 SER A CB  
1091 O OG  . SER A 157 ? 1.1158 0.6499 0.7665 -0.0114 0.1228  0.0281  156 SER A OG  
1092 N N   . LEU A 158 ? 0.9470 0.5120 0.6108 -0.0195 0.1169  0.0424  157 LEU A N   
1093 C CA  . LEU A 158 ? 0.9598 0.5345 0.6250 -0.0219 0.1169  0.0495  157 LEU A CA  
1094 C C   . LEU A 158 ? 1.0345 0.6194 0.7012 -0.0283 0.1107  0.0514  157 LEU A C   
1095 O O   . LEU A 158 ? 0.9859 0.5713 0.6459 -0.0323 0.1067  0.0508  157 LEU A O   
1096 C CB  . LEU A 158 ? 0.8896 0.4724 0.5656 -0.0184 0.1241  0.0595  157 LEU A CB  
1097 C CG  . LEU A 158 ? 0.9703 0.5435 0.6447 -0.0116 0.1318  0.0589  157 LEU A CG  
1098 C CD1 . LEU A 158 ? 0.9337 0.5172 0.6157 -0.0092 0.1378  0.0699  157 LEU A CD1 
1099 C CD2 . LEU A 158 ? 1.0070 0.5661 0.6669 -0.0109 0.1303  0.0496  157 LEU A CD2 
1100 N N   . ILE A 159 ? 0.9734 0.5660 0.6483 -0.0296 0.1098  0.0538  158 ILE A N   
1101 C CA  . ILE A 159 ? 1.0283 0.6302 0.7033 -0.0358 0.1041  0.0550  158 ILE A CA  
1102 C C   . ILE A 159 ? 1.0012 0.5936 0.6649 -0.0378 0.0985  0.0450  158 ILE A C   
1103 O O   . ILE A 159 ? 1.0191 0.6149 0.6783 -0.0428 0.0939  0.0443  158 ILE A O   
1104 C CB  . ILE A 159 ? 0.9442 0.5569 0.6305 -0.0365 0.1046  0.0598  158 ILE A CB  
1105 C CG1 . ILE A 159 ? 0.9084 0.5131 0.5948 -0.0334 0.1044  0.0529  158 ILE A CG1 
1106 C CG2 . ILE A 159 ? 0.7577 0.3801 0.4564 -0.0340 0.1106  0.0706  158 ILE A CG2 
1107 C CD1 . ILE A 159 ? 0.9043 0.5196 0.6022 -0.0339 0.1049  0.0578  158 ILE A CD1 
1108 N N   . GLY A 160 ? 0.9492 0.5294 0.6079 -0.0339 0.0990  0.0376  159 GLY A N   
1109 C CA  . GLY A 160 ? 0.9252 0.4967 0.5736 -0.0351 0.0942  0.0292  159 GLY A CA  
1110 C C   . GLY A 160 ? 0.9966 0.5639 0.6363 -0.0371 0.0922  0.0283  159 GLY A C   
1111 O O   . GLY A 160 ? 0.9819 0.5489 0.6159 -0.0408 0.0878  0.0258  159 GLY A O   
1112 N N   . VAL A 161 ? 1.0020 0.5657 0.6402 -0.0347 0.0958  0.0304  160 VAL A N   
1113 C CA  . VAL A 161 ? 0.9684 0.5292 0.5992 -0.0368 0.0941  0.0308  160 VAL A CA  
1114 C C   . VAL A 161 ? 0.9482 0.5188 0.5808 -0.0427 0.0914  0.0365  160 VAL A C   
1115 O O   . VAL A 161 ? 0.9813 0.5485 0.6064 -0.0465 0.0871  0.0342  160 VAL A O   
1116 C CB  . VAL A 161 ? 1.0168 0.5750 0.6475 -0.0331 0.0993  0.0338  160 VAL A CB  
1117 C CG1 . VAL A 161 ? 0.8584 0.4187 0.4850 -0.0361 0.0981  0.0378  160 VAL A CG1 
1118 C CG2 . VAL A 161 ? 0.9312 0.4768 0.5552 -0.0289 0.1005  0.0264  160 VAL A CG2 
1119 N N   . LEU A 162 ? 1.0072 0.5899 0.6496 -0.0438 0.0936  0.0441  161 LEU A N   
1120 C CA  . LEU A 162 ? 0.9925 0.5857 0.6365 -0.0505 0.0904  0.0497  161 LEU A CA  
1121 C C   . LEU A 162 ? 0.9964 0.5870 0.6344 -0.0543 0.0852  0.0435  161 LEU A C   
1122 O O   . LEU A 162 ? 1.0613 0.6515 0.6927 -0.0599 0.0811  0.0431  161 LEU A O   
1123 C CB  . LEU A 162 ? 0.9362 0.5440 0.5929 -0.0508 0.0938  0.0594  161 LEU A CB  
1124 C CG  . LEU A 162 ? 1.0201 0.6375 0.6823 -0.0520 0.0966  0.0700  161 LEU A CG  
1125 C CD1 . LEU A 162 ? 1.1023 0.7226 0.7578 -0.0598 0.0914  0.0722  161 LEU A CD1 
1126 C CD2 . LEU A 162 ? 1.1958 0.8058 0.8572 -0.0454 0.1019  0.0697  161 LEU A CD2 
1127 N N   . ALA A 163 ? 0.9180 0.5065 0.5581 -0.0513 0.0853  0.0386  162 ALA A N   
1128 C CA  . ALA A 163 ? 0.9664 0.5532 0.6013 -0.0540 0.0811  0.0329  162 ALA A CA  
1129 C C   . ALA A 163 ? 0.9029 0.4764 0.5262 -0.0537 0.0781  0.0252  162 ALA A C   
1130 O O   . ALA A 163 ? 0.8364 0.4077 0.4529 -0.0576 0.0746  0.0221  162 ALA A O   
1131 C CB  . ALA A 163 ? 0.8775 0.4662 0.5183 -0.0505 0.0822  0.0304  162 ALA A CB  
1132 N N   . TYR A 164 ? 0.9203 0.4847 0.5409 -0.0493 0.0796  0.0221  163 TYR A N   
1133 C CA  . TYR A 164 ? 0.9085 0.4611 0.5193 -0.0487 0.0769  0.0156  163 TYR A CA  
1134 C C   . TYR A 164 ? 0.8963 0.4469 0.5007 -0.0534 0.0745  0.0177  163 TYR A C   
1135 O O   . TYR A 164 ? 0.8621 0.4052 0.4585 -0.0553 0.0712  0.0132  163 TYR A O   
1136 C CB  . TYR A 164 ? 0.9269 0.4716 0.5363 -0.0435 0.0789  0.0128  163 TYR A CB  
1137 C CG  . TYR A 164 ? 0.8885 0.4222 0.4886 -0.0428 0.0761  0.0074  163 TYR A CG  
1138 C CD1 . TYR A 164 ? 0.8913 0.4197 0.4885 -0.0408 0.0739  0.0015  163 TYR A CD1 
1139 C CD2 . TYR A 164 ? 0.7969 0.3264 0.3920 -0.0439 0.0758  0.0091  163 TYR A CD2 
1140 C CE1 . TYR A 164 ? 0.8455 0.3646 0.4354 -0.0399 0.0716  -0.0025 163 TYR A CE1 
1141 C CE2 . TYR A 164 ? 0.8447 0.3646 0.4322 -0.0432 0.0732  0.0049  163 TYR A CE2 
1142 C CZ  . TYR A 164 ? 0.9018 0.4165 0.4869 -0.0411 0.0712  -0.0008 163 TYR A CZ  
1143 O OH  . TYR A 164 ? 0.9456 0.4515 0.5241 -0.0402 0.0689  -0.0039 163 TYR A OH  
1144 N N   . TYR A 165 ? 0.8682 0.4253 0.4762 -0.0554 0.0763  0.0250  164 TYR A N   
1145 C CA  . TYR A 165 ? 0.8503 0.4061 0.4527 -0.0606 0.0737  0.0279  164 TYR A CA  
1146 C C   . TYR A 165 ? 0.8617 0.4195 0.4600 -0.0672 0.0698  0.0275  164 TYR A C   
1147 O O   . TYR A 165 ? 0.9599 0.5084 0.5489 -0.0701 0.0664  0.0233  164 TYR A O   
1148 C CB  . TYR A 165 ? 0.8020 0.3669 0.4106 -0.0615 0.0766  0.0371  164 TYR A CB  
1149 C CG  . TYR A 165 ? 0.8037 0.3695 0.4076 -0.0679 0.0735  0.0416  164 TYR A CG  
1150 C CD1 . TYR A 165 ? 0.9030 0.4587 0.4991 -0.0679 0.0717  0.0390  164 TYR A CD1 
1151 C CD2 . TYR A 165 ? 0.8213 0.3982 0.4284 -0.0746 0.0719  0.0489  164 TYR A CD2 
1152 C CE1 . TYR A 165 ? 0.9483 0.5043 0.5402 -0.0742 0.0685  0.0434  164 TYR A CE1 
1153 C CE2 . TYR A 165 ? 0.8935 0.4710 0.4959 -0.0815 0.0685  0.0533  164 TYR A CE2 
1154 C CZ  . TYR A 165 ? 1.0295 0.5962 0.6244 -0.0812 0.0668  0.0505  164 TYR A CZ  
1155 O OH  . TYR A 165 ? 1.0841 0.6510 0.6744 -0.0885 0.0631  0.0552  164 TYR A OH  
1156 N N   . VAL A 166 ? 0.8792 0.4487 0.4839 -0.0700 0.0703  0.0318  165 VAL A N   
1157 C CA  . VAL A 166 ? 0.9486 0.5208 0.5486 -0.0770 0.0667  0.0315  165 VAL A CA  
1158 C C   . VAL A 166 ? 0.8993 0.4616 0.4917 -0.0753 0.0649  0.0220  165 VAL A C   
1159 O O   . VAL A 166 ? 0.7850 0.3422 0.3685 -0.0804 0.0618  0.0188  165 VAL A O   
1160 C CB  . VAL A 166 ? 0.8070 0.3954 0.4162 -0.0801 0.0678  0.0388  165 VAL A CB  
1161 C CG1 . VAL A 166 ? 0.7637 0.3626 0.3811 -0.0813 0.0700  0.0493  165 VAL A CG1 
1162 C CG2 . VAL A 166 ? 0.8548 0.4468 0.4715 -0.0742 0.0706  0.0365  165 VAL A CG2 
1163 N N   . SER A 167 ? 0.8784 0.4375 0.4741 -0.0683 0.0671  0.0174  166 SER A N   
1164 C CA  . SER A 167 ? 0.8757 0.4271 0.4657 -0.0659 0.0659  0.0094  166 SER A CA  
1165 C C   . SER A 167 ? 0.9152 0.4520 0.4950 -0.0654 0.0639  0.0042  166 SER A C   
1166 O O   . SER A 167 ? 0.8797 0.4097 0.4514 -0.0674 0.0620  -0.0005 166 SER A O   
1167 C CB  . SER A 167 ? 0.9082 0.4612 0.5051 -0.0591 0.0683  0.0072  166 SER A CB  
1168 O OG  . SER A 167 ? 0.9678 0.5161 0.5608 -0.0568 0.0673  0.0008  166 SER A OG  
1169 N N   . TYR A 168 ? 0.9710 0.5026 0.5510 -0.0626 0.0645  0.0051  167 TYR A N   
1170 C CA  . TYR A 168 ? 0.9058 0.4243 0.4772 -0.0620 0.0626  0.0010  167 TYR A CA  
1171 C C   . TYR A 168 ? 0.9517 0.4667 0.5162 -0.0691 0.0598  0.0033  167 TYR A C   
1172 O O   . TYR A 168 ? 0.9894 0.4927 0.5453 -0.0701 0.0577  -0.0009 167 TYR A O   
1173 C CB  . TYR A 168 ? 0.8805 0.3953 0.4539 -0.0570 0.0640  0.0013  167 TYR A CB  
1174 C CG  . TYR A 168 ? 0.9715 0.4873 0.5448 -0.0595 0.0641  0.0069  167 TYR A CG  
1175 C CD1 . TYR A 168 ? 0.9794 0.4871 0.5455 -0.0626 0.0615  0.0069  167 TYR A CD1 
1176 C CD2 . TYR A 168 ? 0.9685 0.4934 0.5493 -0.0582 0.0672  0.0123  167 TYR A CD2 
1177 C CE1 . TYR A 168 ? 0.9921 0.5019 0.5587 -0.0648 0.0616  0.0127  167 TYR A CE1 
1178 C CE2 . TYR A 168 ? 0.9643 0.4912 0.5454 -0.0598 0.0679  0.0180  167 TYR A CE2 
1179 C CZ  . TYR A 168 ? 1.0833 0.6033 0.6574 -0.0633 0.0649  0.0183  167 TYR A CZ  
1180 O OH  . TYR A 168 ? 1.1196 0.6427 0.6944 -0.0650 0.0656  0.0245  167 TYR A OH  
1181 N N   . ARG A 169 ? 0.8627 0.3878 0.4311 -0.0742 0.0598  0.0104  168 ARG A N   
1182 C CA  . ARG A 169 ? 0.8857 0.4086 0.4477 -0.0822 0.0566  0.0135  168 ARG A CA  
1183 C C   . ARG A 169 ? 0.9300 0.4494 0.4842 -0.0873 0.0542  0.0093  168 ARG A C   
1184 O O   . ARG A 169 ? 1.0469 0.5556 0.5910 -0.0921 0.0513  0.0069  168 ARG A O   
1185 C CB  . ARG A 169 ? 0.8561 0.3927 0.4252 -0.0864 0.0572  0.0233  168 ARG A CB  
1186 C CG  . ARG A 169 ? 0.8806 0.4179 0.4536 -0.0832 0.0590  0.0278  168 ARG A CG  
1187 C CD  . ARG A 169 ? 1.0254 0.5517 0.5898 -0.0864 0.0558  0.0271  168 ARG A CD  
1188 N NE  . ARG A 169 ? 0.9543 0.4811 0.5131 -0.0961 0.0518  0.0304  168 ARG A NE  
1189 C CZ  . ARG A 169 ? 1.0197 0.5555 0.5814 -0.1019 0.0506  0.0395  168 ARG A CZ  
1190 N NH1 . ARG A 169 ? 1.1031 0.6482 0.6734 -0.0983 0.0539  0.0463  168 ARG A NH1 
1191 N NH2 . ARG A 169 ? 1.0937 0.6290 0.6491 -0.1116 0.0463  0.0419  168 ARG A NH2 
1192 N N   . LEU A 170 ? 0.8622 0.3900 0.4204 -0.0866 0.0556  0.0084  169 LEU A N   
1193 C CA  . LEU A 170 ? 0.8192 0.3443 0.3693 -0.0913 0.0539  0.0042  169 LEU A CA  
1194 C C   . LEU A 170 ? 0.9770 0.4889 0.5204 -0.0856 0.0546  -0.0050 169 LEU A C   
1195 O O   . LEU A 170 ? 1.0824 0.5828 0.6144 -0.0888 0.0530  -0.0100 169 LEU A O   
1196 C CB  . LEU A 170 ? 0.8111 0.3520 0.3683 -0.0931 0.0549  0.0079  169 LEU A CB  
1197 C CG  . LEU A 170 ? 0.8067 0.3625 0.3705 -0.0997 0.0541  0.0180  169 LEU A CG  
1198 C CD1 . LEU A 170 ? 0.7978 0.3692 0.3702 -0.1000 0.0556  0.0216  169 LEU A CD1 
1199 C CD2 . LEU A 170 ? 0.9626 0.5151 0.5164 -0.1101 0.0499  0.0199  169 LEU A CD2 
1200 N N   . GLY A 171 ? 0.8741 0.3873 0.4243 -0.0772 0.0573  -0.0072 170 GLY A N   
1201 C CA  . GLY A 171 ? 0.8603 0.3645 0.4063 -0.0715 0.0583  -0.0146 170 GLY A CA  
1202 C C   . GLY A 171 ? 0.9304 0.4213 0.4729 -0.0665 0.0582  -0.0180 170 GLY A C   
1203 O O   . GLY A 171 ? 0.9229 0.4055 0.4615 -0.0619 0.0591  -0.0235 170 GLY A O   
1204 N N   . GLY A 172 ? 0.8952 0.3846 0.4395 -0.0672 0.0574  -0.0141 171 GLY A N   
1205 C CA  . GLY A 172 ? 0.8449 0.3228 0.3863 -0.0629 0.0570  -0.0164 171 GLY A CA  
1206 C C   . GLY A 172 ? 0.9014 0.3827 0.4501 -0.0552 0.0590  -0.0173 171 GLY A C   
1207 O O   . GLY A 172 ? 0.9307 0.4223 0.4874 -0.0541 0.0603  -0.0139 171 GLY A O   
1208 N N   . TYR A 173 ? 0.9309 0.4034 0.4770 -0.0500 0.0592  -0.0215 172 TYR A N   
1209 C CA  . TYR A 173 ? 0.9671 0.4426 0.5194 -0.0436 0.0603  -0.0219 172 TYR A CA  
1210 C C   . TYR A 173 ? 0.9330 0.4183 0.4914 -0.0412 0.0620  -0.0228 172 TYR A C   
1211 O O   . TYR A 173 ? 0.9163 0.4093 0.4819 -0.0393 0.0628  -0.0207 172 TYR A O   
1212 C CB  . TYR A 173 ? 0.8953 0.3600 0.4439 -0.0389 0.0600  -0.0250 172 TYR A CB  
1213 C CG  . TYR A 173 ? 0.8170 0.2850 0.3714 -0.0332 0.0604  -0.0246 172 TYR A CG  
1214 C CD1 . TYR A 173 ? 0.8651 0.3371 0.4231 -0.0335 0.0600  -0.0215 172 TYR A CD1 
1215 C CD2 . TYR A 173 ? 0.8175 0.2851 0.3737 -0.0279 0.0612  -0.0271 172 TYR A CD2 
1216 C CE1 . TYR A 173 ? 0.9125 0.3869 0.4744 -0.0294 0.0601  -0.0214 172 TYR A CE1 
1217 C CE2 . TYR A 173 ? 0.8120 0.2834 0.3734 -0.0238 0.0610  -0.0261 172 TYR A CE2 
1218 C CZ  . TYR A 173 ? 0.9143 0.3887 0.4780 -0.0250 0.0602  -0.0235 172 TYR A CZ  
1219 O OH  . TYR A 173 ? 0.9150 0.3926 0.4825 -0.0219 0.0596  -0.0227 172 TYR A OH  
1220 N N   . GLU A 174 ? 0.9083 0.3930 0.4636 -0.0414 0.0626  -0.0259 173 GLU A N   
1221 C CA  . GLU A 174 ? 0.8933 0.3886 0.4546 -0.0398 0.0640  -0.0261 173 GLU A CA  
1222 C C   . GLU A 174 ? 0.8819 0.3888 0.4492 -0.0440 0.0642  -0.0215 173 GLU A C   
1223 O O   . GLU A 174 ? 0.8426 0.3590 0.4179 -0.0420 0.0653  -0.0199 173 GLU A O   
1224 C CB  . GLU A 174 ? 0.9345 0.4273 0.4900 -0.0398 0.0649  -0.0301 173 GLU A CB  
1225 C CG  . GLU A 174 ? 0.9397 0.4271 0.4944 -0.0329 0.0662  -0.0336 173 GLU A CG  
1226 C CD  . GLU A 174 ? 1.1772 0.6677 0.7297 -0.0316 0.0681  -0.0367 173 GLU A CD  
1227 O OE1 . GLU A 174 ? 1.1399 0.6399 0.6941 -0.0355 0.0683  -0.0354 173 GLU A OE1 
1228 O OE2 . GLU A 174 ? 1.1463 0.6300 0.6955 -0.0264 0.0698  -0.0399 173 GLU A OE2 
1229 N N   . GLY A 175 ? 0.8772 0.3835 0.4411 -0.0499 0.0632  -0.0188 174 GLY A N   
1230 C CA  . GLY A 175 ? 0.8320 0.3498 0.4027 -0.0534 0.0637  -0.0132 174 GLY A CA  
1231 C C   . GLY A 175 ? 0.9206 0.4411 0.4984 -0.0499 0.0650  -0.0103 174 GLY A C   
1232 O O   . GLY A 175 ? 1.0300 0.5601 0.6159 -0.0493 0.0666  -0.0070 174 GLY A O   
1233 N N   . ALA A 176 ? 0.9992 0.5109 0.5736 -0.0476 0.0644  -0.0115 175 ALA A N   
1234 C CA  . ALA A 176 ? 0.9186 0.4315 0.4979 -0.0442 0.0657  -0.0099 175 ALA A CA  
1235 C C   . ALA A 176 ? 0.9343 0.4500 0.5186 -0.0395 0.0666  -0.0122 175 ALA A C   
1236 O O   . ALA A 176 ? 0.8812 0.4011 0.4712 -0.0379 0.0682  -0.0103 175 ALA A O   
1237 C CB  . ALA A 176 ? 0.8744 0.3776 0.4481 -0.0431 0.0646  -0.0107 175 ALA A CB  
1238 N N   . LEU A 177 ? 0.9867 0.4998 0.5689 -0.0374 0.0657  -0.0160 176 LEU A N   
1239 C CA  . LEU A 177 ? 1.0017 0.5189 0.5891 -0.0335 0.0661  -0.0174 176 LEU A CA  
1240 C C   . LEU A 177 ? 1.0216 0.5498 0.6162 -0.0349 0.0674  -0.0150 176 LEU A C   
1241 O O   . LEU A 177 ? 0.9936 0.5265 0.5947 -0.0330 0.0682  -0.0138 176 LEU A O   
1242 C CB  . LEU A 177 ? 0.9858 0.4985 0.5697 -0.0304 0.0652  -0.0212 176 LEU A CB  
1243 C CG  . LEU A 177 ? 0.9418 0.4440 0.5200 -0.0282 0.0640  -0.0229 176 LEU A CG  
1244 C CD1 . LEU A 177 ? 0.9423 0.4434 0.5211 -0.0233 0.0638  -0.0252 176 LEU A CD1 
1245 C CD2 . LEU A 177 ? 0.9469 0.4473 0.5260 -0.0280 0.0635  -0.0211 176 LEU A CD2 
1246 N N   . LEU A 178 ? 0.9818 0.5141 0.5750 -0.0386 0.0675  -0.0141 177 LEU A N   
1247 C CA  . LEU A 178 ? 0.9760 0.5200 0.5764 -0.0404 0.0686  -0.0107 177 LEU A CA  
1248 C C   . LEU A 178 ? 0.9481 0.4966 0.5547 -0.0415 0.0702  -0.0057 177 LEU A C   
1249 O O   . LEU A 178 ? 0.9778 0.5339 0.5927 -0.0406 0.0717  -0.0030 177 LEU A O   
1250 C CB  . LEU A 178 ? 0.8811 0.4286 0.4774 -0.0451 0.0680  -0.0106 177 LEU A CB  
1251 C CG  . LEU A 178 ? 0.9136 0.4745 0.5171 -0.0486 0.0689  -0.0055 177 LEU A CG  
1252 C CD1 . LEU A 178 ? 0.9305 0.4994 0.5415 -0.0455 0.0697  -0.0054 177 LEU A CD1 
1253 C CD2 . LEU A 178 ? 0.8472 0.4103 0.4443 -0.0546 0.0677  -0.0051 177 LEU A CD2 
1254 N N   . GLY A 179 ? 1.0165 0.5602 0.6194 -0.0433 0.0702  -0.0041 178 GLY A N   
1255 C CA  . GLY A 179 ? 1.0648 0.6121 0.6733 -0.0433 0.0726  0.0007  178 GLY A CA  
1256 C C   . GLY A 179 ? 1.1142 0.6592 0.7267 -0.0388 0.0742  -0.0005 178 GLY A C   
1257 O O   . GLY A 179 ? 1.2004 0.7512 0.8206 -0.0380 0.0766  0.0028  178 GLY A O   
1258 N N   . LEU A 180 ? 0.9697 0.5060 0.5770 -0.0361 0.0727  -0.0050 179 LEU A N   
1259 C CA  . LEU A 180 ? 0.9379 0.4714 0.5476 -0.0329 0.0735  -0.0066 179 LEU A CA  
1260 C C   . LEU A 180 ? 0.9968 0.5373 0.6141 -0.0320 0.0739  -0.0060 179 LEU A C   
1261 O O   . LEU A 180 ? 1.0047 0.5449 0.6262 -0.0306 0.0755  -0.0053 179 LEU A O   
1262 C CB  . LEU A 180 ? 0.9694 0.4946 0.5726 -0.0309 0.0710  -0.0109 179 LEU A CB  
1263 C CG  . LEU A 180 ? 0.9867 0.5042 0.5828 -0.0312 0.0706  -0.0114 179 LEU A CG  
1264 C CD1 . LEU A 180 ? 0.9681 0.4789 0.5596 -0.0290 0.0682  -0.0147 179 LEU A CD1 
1265 C CD2 . LEU A 180 ? 0.9568 0.4739 0.5536 -0.0314 0.0735  -0.0086 179 LEU A CD2 
1266 N N   . ALA A 181 ? 1.0319 0.5784 0.6508 -0.0331 0.0726  -0.0062 180 ALA A N   
1267 C CA  . ALA A 181 ? 0.9426 0.4974 0.5694 -0.0326 0.0730  -0.0047 180 ALA A CA  
1268 C C   . ALA A 181 ? 0.9233 0.4862 0.5577 -0.0344 0.0755  0.0008  180 ALA A C   
1269 O O   . ALA A 181 ? 1.0121 0.5799 0.6543 -0.0335 0.0766  0.0029  180 ALA A O   
1270 C CB  . ALA A 181 ? 0.7914 0.3506 0.4168 -0.0329 0.0712  -0.0065 180 ALA A CB  
1271 N N   . LEU A 182 ? 0.8953 0.4602 0.5283 -0.0371 0.0764  0.0038  181 LEU A N   
1272 C CA  . LEU A 182 ? 0.9940 0.5683 0.6351 -0.0389 0.0789  0.0103  181 LEU A CA  
1273 C C   . LEU A 182 ? 1.0270 0.5981 0.6723 -0.0364 0.0825  0.0129  181 LEU A C   
1274 O O   . LEU A 182 ? 1.0683 0.6468 0.7223 -0.0365 0.0852  0.0186  181 LEU A O   
1275 C CB  . LEU A 182 ? 0.9848 0.5635 0.6228 -0.0433 0.0782  0.0134  181 LEU A CB  
1276 C CG  . LEU A 182 ? 0.9865 0.5696 0.6206 -0.0466 0.0755  0.0115  181 LEU A CG  
1277 C CD1 . LEU A 182 ? 0.7998 0.3889 0.4320 -0.0524 0.0748  0.0159  181 LEU A CD1 
1278 C CD2 . LEU A 182 ? 0.8309 0.4231 0.4723 -0.0459 0.0756  0.0125  181 LEU A CD2 
1279 N N   . ILE A 183 ? 1.0186 0.5788 0.6575 -0.0341 0.0827  0.0092  182 ILE A N   
1280 C CA  . ILE A 183 ? 1.0847 0.6406 0.7258 -0.0316 0.0867  0.0110  182 ILE A CA  
1281 C C   . ILE A 183 ? 0.9628 0.5193 0.6112 -0.0296 0.0885  0.0115  182 ILE A C   
1282 O O   . ILE A 183 ? 0.9615 0.5212 0.6171 -0.0284 0.0926  0.0164  182 ILE A O   
1283 C CB  . ILE A 183 ? 1.0495 0.5937 0.6810 -0.0301 0.0864  0.0065  182 ILE A CB  
1284 C CG1 . ILE A 183 ? 1.0252 0.5694 0.6529 -0.0314 0.0873  0.0093  182 ILE A CG1 
1285 C CG2 . ILE A 183 ? 0.9039 0.4408 0.5355 -0.0271 0.0895  0.0050  182 ILE A CG2 
1286 C CD1 . ILE A 183 ? 0.9682 0.5172 0.5936 -0.0352 0.0841  0.0103  182 ILE A CD1 
1287 N N   . PRO A 184 ? 0.9175 0.4714 0.5651 -0.0291 0.0857  0.0072  183 PRO A N   
1288 C CA  . PRO A 184 ? 0.9893 0.5436 0.6440 -0.0278 0.0870  0.0083  183 PRO A CA  
1289 C C   . PRO A 184 ? 1.0414 0.6083 0.7058 -0.0293 0.0865  0.0127  183 PRO A C   
1290 O O   . PRO A 184 ? 1.0505 0.6197 0.7231 -0.0286 0.0882  0.0155  183 PRO A O   
1291 C CB  . PRO A 184 ? 0.9406 0.4871 0.5895 -0.0274 0.0837  0.0024  183 PRO A CB  
1292 C CG  . PRO A 184 ? 0.8303 0.3786 0.4734 -0.0283 0.0800  -0.0002 183 PRO A CG  
1293 C CD  . PRO A 184 ? 0.9555 0.5048 0.5955 -0.0293 0.0814  0.0017  183 PRO A CD  
1294 N N   . ALA A 185 ? 0.9458 0.5206 0.6092 -0.0316 0.0841  0.0134  184 ALA A N   
1295 C CA  . ALA A 185 ? 0.9821 0.5697 0.6536 -0.0334 0.0834  0.0174  184 ALA A CA  
1296 C C   . ALA A 185 ? 1.0182 0.6148 0.6980 -0.0346 0.0866  0.0251  184 ALA A C   
1297 O O   . ALA A 185 ? 1.0281 0.6332 0.7180 -0.0348 0.0877  0.0299  184 ALA A O   
1298 C CB  . ALA A 185 ? 0.9013 0.4930 0.5671 -0.0355 0.0800  0.0148  184 ALA A CB  
1299 N N   . LEU A 186 ? 0.9719 0.5677 0.6483 -0.0355 0.0881  0.0271  185 LEU A N   
1300 C CA  . LEU A 186 ? 0.9660 0.5719 0.6506 -0.0369 0.0910  0.0355  185 LEU A CA  
1301 C C   . LEU A 186 ? 1.0547 0.6585 0.7479 -0.0332 0.0960  0.0397  185 LEU A C   
1302 O O   . LEU A 186 ? 1.1211 0.7335 0.8226 -0.0334 0.0993  0.0477  185 LEU A O   
1303 C CB  . LEU A 186 ? 0.9758 0.5813 0.6543 -0.0391 0.0910  0.0369  185 LEU A CB  
1304 C CG  . LEU A 186 ? 1.0612 0.6764 0.7372 -0.0447 0.0877  0.0390  185 LEU A CG  
1305 C CD1 . LEU A 186 ? 0.9400 0.5493 0.6059 -0.0458 0.0835  0.0309  185 LEU A CD1 
1306 C CD2 . LEU A 186 ? 0.8921 0.5093 0.5656 -0.0474 0.0883  0.0435  185 LEU A CD2 
1307 N N   . VAL A 187 ? 1.0462 0.6388 0.7376 -0.0300 0.0969  0.0348  186 VAL A N   
1308 C CA  . VAL A 187 ? 1.0875 0.6760 0.7862 -0.0265 0.1019  0.0380  186 VAL A CA  
1309 C C   . VAL A 187 ? 1.0530 0.6522 0.7647 -0.0270 0.1026  0.0443  186 VAL A C   
1310 O O   . VAL A 187 ? 1.0233 0.6209 0.7431 -0.0242 0.1074  0.0488  186 VAL A O   
1311 C CB  . VAL A 187 ? 0.9932 0.5658 0.6847 -0.0241 0.1018  0.0304  186 VAL A CB  
1312 C CG1 . VAL A 187 ? 0.8958 0.4692 0.5905 -0.0252 0.0984  0.0282  186 VAL A CG1 
1313 C CG2 . VAL A 187 ? 0.9542 0.5175 0.6474 -0.0202 0.1082  0.0320  186 VAL A CG2 
1314 N N   . VAL A 188 ? 1.0345 0.6446 0.7484 -0.0304 0.0983  0.0450  187 VAL A N   
1315 C CA  . VAL A 188 ? 0.9034 0.5258 0.6301 -0.0314 0.0987  0.0518  187 VAL A CA  
1316 C C   . VAL A 188 ? 0.9486 0.5815 0.6853 -0.0314 0.1028  0.0618  187 VAL A C   
1317 O O   . VAL A 188 ? 0.9684 0.6054 0.7170 -0.0296 0.1060  0.0683  187 VAL A O   
1318 C CB  . VAL A 188 ? 0.9632 0.5963 0.6888 -0.0352 0.0935  0.0506  187 VAL A CB  
1319 C CG1 . VAL A 188 ? 0.9869 0.6122 0.7071 -0.0343 0.0902  0.0432  187 VAL A CG1 
1320 C CG2 . VAL A 188 ? 0.9458 0.5829 0.6628 -0.0384 0.0913  0.0492  187 VAL A CG2 
1321 N N   . ILE A 189 ? 0.9765 0.6141 0.7091 -0.0335 0.1026  0.0639  188 ILE A N   
1322 C CA  . ILE A 189 ? 1.0418 0.6921 0.7844 -0.0344 0.1059  0.0748  188 ILE A CA  
1323 C C   . ILE A 189 ? 1.0853 0.7290 0.8347 -0.0287 0.1128  0.0790  188 ILE A C   
1324 O O   . ILE A 189 ? 0.9312 0.5835 0.6942 -0.0273 0.1162  0.0878  188 ILE A O   
1325 C CB  . ILE A 189 ? 1.0487 0.7051 0.7843 -0.0388 0.1035  0.0760  188 ILE A CB  
1326 C CG1 . ILE A 189 ? 0.9812 0.6393 0.7074 -0.0435 0.0972  0.0694  188 ILE A CG1 
1327 C CG2 . ILE A 189 ? 0.9478 0.6214 0.6947 -0.0413 0.1054  0.0884  188 ILE A CG2 
1328 C CD1 . ILE A 189 ? 1.0839 0.7460 0.8018 -0.0486 0.0944  0.0698  188 ILE A CD1 
1329 N N   . PRO A 190 ? 1.0596 0.6884 0.8005 -0.0251 0.1155  0.0735  189 PRO A N   
1330 C CA  . PRO A 190 ? 1.0024 0.6242 0.7493 -0.0193 0.1229  0.0773  189 PRO A CA  
1331 C C   . PRO A 190 ? 1.0404 0.6544 0.7930 -0.0163 0.1250  0.0759  189 PRO A C   
1332 O O   . PRO A 190 ? 1.1035 0.7185 0.8671 -0.0124 0.1310  0.0829  189 PRO A O   
1333 C CB  . PRO A 190 ? 1.0395 0.6466 0.7732 -0.0169 0.1243  0.0701  189 PRO A CB  
1334 C CG  . PRO A 190 ? 1.0980 0.7091 0.8221 -0.0220 0.1181  0.0663  189 PRO A CG  
1335 C CD  . PRO A 190 ? 1.0334 0.6514 0.7592 -0.0260 0.1125  0.0644  189 PRO A CD  
1336 N N   . ALA A 191 ? 0.9182 0.5248 0.6642 -0.0180 0.1202  0.0675  190 ALA A N   
1337 C CA  . ALA A 191 ? 0.9756 0.5742 0.7263 -0.0160 0.1214  0.0660  190 ALA A CA  
1338 C C   . ALA A 191 ? 1.0599 0.6734 0.8265 -0.0171 0.1218  0.0756  190 ALA A C   
1339 O O   . ALA A 191 ? 0.9447 0.5545 0.7208 -0.0138 0.1266  0.0801  190 ALA A O   
1340 C CB  . ALA A 191 ? 0.8897 0.4797 0.6304 -0.0184 0.1154  0.0560  190 ALA A CB  
1341 N N   . ALA A 192 ? 1.0630 0.6932 0.8325 -0.0218 0.1169  0.0788  191 ALA A N   
1342 C CA  . ALA A 192 ? 0.8735 0.5199 0.6579 -0.0235 0.1168  0.0885  191 ALA A CA  
1343 C C   . ALA A 192 ? 0.9230 0.5773 0.7197 -0.0207 0.1231  0.0999  191 ALA A C   
1344 O O   . ALA A 192 ? 1.0482 0.7072 0.8586 -0.0189 0.1262  0.1076  191 ALA A O   
1345 C CB  . ALA A 192 ? 0.9518 0.6143 0.7345 -0.0294 0.1106  0.0892  191 ALA A CB  
1346 N N   . ILE A 193 ? 0.9253 0.5817 0.7180 -0.0204 0.1251  0.1019  192 ILE A N   
1347 C CA  . ILE A 193 ? 0.9441 0.6090 0.7489 -0.0174 0.1315  0.1136  192 ILE A CA  
1348 C C   . ILE A 193 ? 0.9905 0.6401 0.7998 -0.0101 0.1392  0.1139  192 ILE A C   
1349 O O   . ILE A 193 ? 1.0862 0.7422 0.9104 -0.0069 0.1443  0.1241  192 ILE A O   
1350 C CB  . ILE A 193 ? 0.9566 0.6259 0.7551 -0.0188 0.1318  0.1153  192 ILE A CB  
1351 C CG1 . ILE A 193 ? 0.9198 0.6051 0.7151 -0.0267 0.1246  0.1166  192 ILE A CG1 
1352 C CG2 . ILE A 193 ? 0.9168 0.5931 0.7274 -0.0145 0.1393  0.1274  192 ILE A CG2 
1353 C CD1 . ILE A 193 ? 0.8333 0.5373 0.6414 -0.0305 0.1224  0.1256  192 ILE A CD1 
1354 N N   . MET A 194 ? 0.9568 0.5857 0.7531 -0.0073 0.1401  0.1028  193 MET A N   
1355 C CA  . MET A 194 ? 1.0345 0.6465 0.8325 -0.0007 0.1476  0.1017  193 MET A CA  
1356 C C   . MET A 194 ? 0.9728 0.5804 0.7788 -0.0003 0.1475  0.1022  193 MET A C   
1357 O O   . MET A 194 ? 1.0317 0.6338 0.8474 0.0047  0.1544  0.1078  193 MET A O   
1358 C CB  . MET A 194 ? 0.9258 0.5173 0.7063 0.0012  0.1482  0.0895  193 MET A CB  
1359 C CG  . MET A 194 ? 0.9958 0.5891 0.7698 0.0025  0.1506  0.0903  193 MET A CG  
1360 S SD  . MET A 194 ? 1.1569 0.7422 0.9364 0.0115  0.1629  0.0967  193 MET A SD  
1361 C CE  . MET A 194 ? 1.0244 0.6365 0.8235 0.0110  0.1651  0.1143  193 MET A CE  
1362 N N   . LEU A 195 ? 1.0031 0.6129 0.8057 -0.0054 0.1399  0.0969  194 LEU A N   
1363 C CA  . LEU A 195 ? 0.9874 0.5937 0.7977 -0.0057 0.1390  0.0977  194 LEU A CA  
1364 C C   . LEU A 195 ? 1.0457 0.6698 0.8754 -0.0055 0.1413  0.1115  194 LEU A C   
1365 O O   . LEU A 195 ? 1.0673 0.6857 0.9070 -0.0025 0.1453  0.1158  194 LEU A O   
1366 C CB  . LEU A 195 ? 0.9460 0.5532 0.7488 -0.0112 0.1303  0.0901  194 LEU A CB  
1367 C CG  . LEU A 195 ? 1.0611 0.6664 0.8716 -0.0126 0.1282  0.0911  194 LEU A CG  
1368 C CD1 . LEU A 195 ? 0.9931 0.5825 0.7905 -0.0145 0.1237  0.0795  194 LEU A CD1 
1369 C CD2 . LEU A 195 ? 0.9720 0.6003 0.7937 -0.0169 0.1235  0.0988  194 LEU A CD2 
1370 N N   . ILE A 196 ? 1.0079 0.6533 0.8429 -0.0089 0.1387  0.1188  195 ILE A N   
1371 C CA  . ILE A 196 ? 1.0555 0.7210 0.9086 -0.0099 0.1396  0.1325  195 ILE A CA  
1372 C C   . ILE A 196 ? 1.0820 0.7508 0.9467 -0.0044 0.1482  0.1434  195 ILE A C   
1373 O O   . ILE A 196 ? 1.2809 0.9519 1.1606 -0.0011 0.1529  0.1524  195 ILE A O   
1374 C CB  . ILE A 196 ? 1.1258 0.8132 0.9784 -0.0170 0.1326  0.1353  195 ILE A CB  
1375 C CG1 . ILE A 196 ? 1.1784 0.8656 1.0248 -0.0216 0.1252  0.1276  195 ILE A CG1 
1376 C CG2 . ILE A 196 ? 1.1000 0.8102 0.9705 -0.0184 0.1342  0.1509  195 ILE A CG2 
1377 C CD1 . ILE A 196 ? 1.1667 0.8529 1.0244 -0.0207 0.1254  0.1310  195 ILE A CD1 
1378 N N   . LYS A 197 ? 0.9090 0.5787 0.7676 -0.0031 0.1506  0.1436  196 LYS A N   
1379 C CA  . LYS A 197 ? 1.0252 0.7015 0.8958 0.0021  0.1588  0.1557  196 LYS A CA  
1380 C C   . LYS A 197 ? 1.0845 0.7400 0.9573 0.0107  0.1679  0.1543  196 LYS A C   
1381 O O   . LYS A 197 ? 1.1535 0.8140 1.0413 0.0160  0.1755  0.1661  196 LYS A O   
1382 C CB  . LYS A 197 ? 0.9644 0.6469 0.8274 0.0009  0.1587  0.1563  196 LYS A CB  
1383 C CG  . LYS A 197 ? 0.9554 0.6517 0.8328 0.0047  0.1657  0.1715  196 LYS A CG  
1384 C CD  . LYS A 197 ? 1.0661 0.7773 0.9388 -0.0001 0.1623  0.1751  196 LYS A CD  
1385 C CE  . LYS A 197 ? 1.1046 0.8003 0.9631 0.0035  0.1654  0.1669  196 LYS A CE  
1386 N NZ  . LYS A 197 ? 0.9756 0.6868 0.8340 0.0003  0.1644  0.1744  196 LYS A NZ  
1387 N N   . ARG A 198 ? 1.0118 0.6437 0.8696 0.0122  0.1677  0.1405  197 ARG A N   
1388 C CA  . ARG A 198 ? 1.0902 0.7000 0.9476 0.0197  0.1762  0.1378  197 ARG A CA  
1389 C C   . ARG A 198 ? 1.1416 0.7474 1.0108 0.0205  0.1773  0.1415  197 ARG A C   
1390 O O   . ARG A 198 ? 1.0810 0.6716 0.9547 0.0272  0.1857  0.1432  197 ARG A O   
1391 C CB  . ARG A 198 ? 1.0541 0.6400 0.8905 0.0200  0.1752  0.1218  197 ARG A CB  
1392 C CG  . ARG A 198 ? 1.0889 0.6715 0.9148 0.0227  0.1786  0.1190  197 ARG A CG  
1393 C CD  . ARG A 198 ? 1.0334 0.5983 0.8381 0.0203  0.1743  0.1034  197 ARG A CD  
1394 N NE  . ARG A 198 ? 0.9529 0.4923 0.7496 0.0240  0.1787  0.0950  197 ARG A NE  
1395 C CZ  . ARG A 198 ? 1.0309 0.5555 0.8258 0.0314  0.1888  0.0952  197 ARG A CZ  
1396 N NH1 . ARG A 198 ? 1.0531 0.5868 0.8551 0.0367  0.1959  0.1042  197 ARG A NH1 
1397 N NH2 . ARG A 198 ? 0.9466 0.4467 0.7322 0.0334  0.1918  0.0863  197 ARG A NH2 
1398 N N   . GLY A 199 ? 1.0984 0.7169 0.9725 0.0140  0.1692  0.1428  198 GLY A N   
1399 C CA  . GLY A 199 ? 1.0792 0.6956 0.9652 0.0142  0.1695  0.1470  198 GLY A CA  
1400 C C   . GLY A 199 ? 1.1003 0.6897 0.9754 0.0150  0.1695  0.1352  198 GLY A C   
1401 O O   . GLY A 199 ? 1.1170 0.6969 1.0012 0.0178  0.1735  0.1387  198 GLY A O   
1402 N N   . VAL A 200 ? 1.0793 0.6563 0.9352 0.0122  0.1650  0.1216  199 VAL A N   
1403 C CA  . VAL A 200 ? 1.1898 0.7420 1.0342 0.0118  0.1641  0.1103  199 VAL A CA  
1404 C C   . VAL A 200 ? 1.1302 0.6872 0.9799 0.0059  0.1565  0.1104  199 VAL A C   
1405 O O   . VAL A 200 ? 1.1168 0.6551 0.9625 0.0054  0.1564  0.1049  199 VAL A O   
1406 C CB  . VAL A 200 ? 1.1776 0.7172 1.0005 0.0101  0.1611  0.0968  199 VAL A CB  
1407 C CG1 . VAL A 200 ? 1.1565 0.7082 0.9731 0.0028  0.1503  0.0919  199 VAL A CG1 
1408 C CG2 . VAL A 200 ? 1.0679 0.5783 0.8782 0.0119  0.1642  0.0865  199 VAL A CG2 
1409 N N   . ILE A 201 ? 1.1510 0.7325 1.0093 0.0013  0.1504  0.1168  200 ILE A N   
1410 C CA  . ILE A 201 ? 1.2161 0.8057 1.0802 -0.0041 0.1431  0.1180  200 ILE A CA  
1411 C C   . ILE A 201 ? 1.2079 0.8271 1.0845 -0.0073 0.1396  0.1285  200 ILE A C   
1412 O O   . ILE A 201 ? 1.0718 0.7032 0.9441 -0.0083 0.1385  0.1289  200 ILE A O   
1413 C CB  . ILE A 201 ? 1.1831 0.7630 1.0305 -0.0090 0.1355  0.1051  200 ILE A CB  
1414 C CG1 . ILE A 201 ? 1.2171 0.8043 1.0711 -0.0142 0.1287  0.1069  200 ILE A CG1 
1415 C CG2 . ILE A 201 ? 1.1350 0.7251 0.9714 -0.0112 0.1314  0.1001  200 ILE A CG2 
1416 C CD1 . ILE A 201 ? 1.1696 0.7512 1.0091 -0.0189 0.1209  0.0961  200 ILE A CD1 
1417 N N   . PRO A 202 ? 1.2370 0.8685 1.1289 -0.0093 0.1378  0.1376  201 PRO A N   
1418 C CA  . PRO A 202 ? 1.2804 0.9406 1.1827 -0.0132 0.1338  0.1471  201 PRO A CA  
1419 C C   . PRO A 202 ? 1.1582 0.8275 1.0504 -0.0194 0.1248  0.1399  201 PRO A C   
1420 O O   . PRO A 202 ? 1.1178 0.7754 1.0016 -0.0214 0.1207  0.1313  201 PRO A O   
1421 C CB  . PRO A 202 ? 1.1931 0.8614 1.1151 -0.0129 0.1354  0.1590  201 PRO A CB  
1422 C CG  . PRO A 202 ? 1.2498 0.8928 1.1697 -0.0104 0.1380  0.1537  201 PRO A CG  
1423 C CD  . PRO A 202 ? 1.1914 0.8106 1.0923 -0.0079 0.1401  0.1403  201 PRO A CD  
1424 N N   . LEU A 203 ? 0.9464 0.6370 0.8393 -0.0226 0.1219  0.1440  202 LEU A N   
1425 C CA  . LEU A 203 ? 0.9171 0.6162 0.7991 -0.0278 0.1144  0.1370  202 LEU A CA  
1426 C C   . LEU A 203 ? 1.0270 0.7337 0.9148 -0.0314 0.1091  0.1383  202 LEU A C   
1427 O O   . LEU A 203 ? 1.1068 0.8146 0.9842 -0.0345 0.1035  0.1306  202 LEU A O   
1428 C CB  . LEU A 203 ? 1.0502 0.7702 0.9324 -0.0308 0.1130  0.1421  202 LEU A CB  
1429 C CG  . LEU A 203 ? 1.1253 0.8526 0.9941 -0.0355 0.1065  0.1343  202 LEU A CG  
1430 C CD1 . LEU A 203 ? 0.9830 0.7117 0.8419 -0.0360 0.1073  0.1318  202 LEU A CD1 
1431 C CD2 . LEU A 203 ? 1.0984 0.8485 0.9751 -0.0404 0.1021  0.1411  202 LEU A CD2 
1432 N N   . SER A 204 ? 0.9487 0.6607 0.8529 -0.0309 0.1110  0.1483  203 SER A N   
1433 C CA  . SER A 204 ? 0.9258 0.6461 0.8366 -0.0345 0.1059  0.1507  203 SER A CA  
1434 C C   . SER A 204 ? 1.0125 0.7140 0.9121 -0.0351 0.1024  0.1395  203 SER A C   
1435 O O   . SER A 204 ? 0.9452 0.6545 0.8448 -0.0387 0.0967  0.1385  203 SER A O   
1436 C CB  . SER A 204 ? 1.1338 0.8598 1.0646 -0.0333 0.1091  0.1635  203 SER A CB  
1437 O OG  . SER A 204 ? 1.2935 1.0285 1.2315 -0.0371 0.1040  0.1667  203 SER A OG  
1438 N N   . TYR A 205 ? 1.1280 0.8054 1.0177 -0.0317 0.1058  0.1315  204 TYR A N   
1439 C CA  . TYR A 205 ? 1.1067 0.7656 0.9855 -0.0329 0.1025  0.1214  204 TYR A CA  
1440 C C   . TYR A 205 ? 0.9841 0.6461 0.8480 -0.0355 0.0969  0.1120  204 TYR A C   
1441 O O   . TYR A 205 ? 0.8991 0.5520 0.7557 -0.0376 0.0926  0.1054  204 TYR A O   
1442 C CB  . TYR A 205 ? 1.0916 0.7240 0.9631 -0.0288 0.1082  0.1155  204 TYR A CB  
1443 C CG  . TYR A 205 ? 1.2499 0.8722 1.1339 -0.0265 0.1131  0.1223  204 TYR A CG  
1444 C CD1 . TYR A 205 ? 1.2146 0.8470 1.1138 -0.0232 0.1189  0.1338  204 TYR A CD1 
1445 C CD2 . TYR A 205 ? 1.1560 0.7582 1.0364 -0.0277 0.1120  0.1175  204 TYR A CD2 
1446 C CE1 . TYR A 205 ? 1.2110 0.8335 1.1222 -0.0204 0.1239  0.1403  204 TYR A CE1 
1447 C CE2 . TYR A 205 ? 1.1373 0.7281 1.0284 -0.0256 0.1168  0.1233  204 TYR A CE2 
1448 C CZ  . TYR A 205 ? 1.2053 0.8061 1.1121 -0.0216 0.1230  0.1347  204 TYR A CZ  
1449 O OH  . TYR A 205 ? 1.2294 0.8182 1.1474 -0.0188 0.1282  0.1409  204 TYR A OH  
1450 N N   . LEU A 206 ? 1.1325 0.8071 0.9919 -0.0355 0.0968  0.1117  205 LEU A N   
1451 C CA  . LEU A 206 ? 0.9357 0.6118 0.7807 -0.0373 0.0923  0.1029  205 LEU A CA  
1452 C C   . LEU A 206 ? 0.8801 0.5763 0.7283 -0.0410 0.0869  0.1055  205 LEU A C   
1453 O O   . LEU A 206 ? 0.9282 0.6261 0.7652 -0.0421 0.0834  0.0986  205 LEU A O   
1454 C CB  . LEU A 206 ? 0.8255 0.5027 0.6624 -0.0357 0.0950  0.1005  205 LEU A CB  
1455 C CG  . LEU A 206 ? 0.9050 0.5607 0.7320 -0.0322 0.0991  0.0938  205 LEU A CG  
1456 C CD1 . LEU A 206 ? 0.8340 0.4944 0.6636 -0.0299 0.1043  0.0987  205 LEU A CD1 
1457 C CD2 . LEU A 206 ? 0.7553 0.4010 0.5654 -0.0329 0.0955  0.0823  205 LEU A CD2 
1458 N N   . LYS A 207 ? 0.8703 0.5817 0.7335 -0.0426 0.0864  0.1155  206 LYS A N   
1459 C CA  . LYS A 207 ? 0.8831 0.6138 0.7492 -0.0460 0.0816  0.1183  206 LYS A CA  
1460 C C   . LYS A 207 ? 0.8408 0.5639 0.7005 -0.0471 0.0770  0.1116  206 LYS A C   
1461 O O   . LYS A 207 ? 0.9604 0.6703 0.8233 -0.0471 0.0767  0.1114  206 LYS A O   
1462 C CB  . LYS A 207 ? 0.9095 0.6571 0.7939 -0.0477 0.0820  0.1309  206 LYS A CB  
1463 C CG  . LYS A 207 ? 0.7896 0.5538 0.6805 -0.0482 0.0847  0.1390  206 LYS A CG  
1464 C CD  . LYS A 207 ? 0.6778 0.4626 0.5861 -0.0507 0.0839  0.1517  206 LYS A CD  
1465 C CE  . LYS A 207 ? 0.8948 0.6698 0.8169 -0.0488 0.0865  0.1582  206 LYS A CE  
1466 N NZ  . LYS A 207 ? 0.8671 0.6628 0.8078 -0.0510 0.0864  0.1721  206 LYS A NZ  
1467 N N   . PRO A 208 ? 0.9340 0.6645 0.7844 -0.0481 0.0734  0.1064  207 PRO A N   
1468 C CA  . PRO A 208 ? 0.8400 0.5636 0.6840 -0.0487 0.0692  0.1005  207 PRO A CA  
1469 C C   . PRO A 208 ? 0.9024 0.6348 0.7588 -0.0512 0.0661  0.1076  207 PRO A C   
1470 O O   . PRO A 208 ? 0.9984 0.7513 0.8635 -0.0528 0.0649  0.1146  207 PRO A O   
1471 C CB  . PRO A 208 ? 0.7587 0.4919 0.5921 -0.0486 0.0673  0.0953  207 PRO A CB  
1472 C CG  . PRO A 208 ? 0.7318 0.4687 0.5616 -0.0478 0.0707  0.0954  207 PRO A CG  
1473 C CD  . PRO A 208 ? 0.9301 0.6739 0.7742 -0.0485 0.0735  0.1052  207 PRO A CD  
1474 N N   . SER A 209 ? 0.9069 0.6237 0.7637 -0.0520 0.0647  0.1058  208 SER A N   
1475 C CA  . SER A 209 ? 0.9246 0.6468 0.7909 -0.0551 0.0606  0.1112  208 SER A CA  
1476 C C   . SER A 209 ? 0.8876 0.5981 0.7438 -0.0564 0.0564  0.1040  208 SER A C   
1477 O O   . SER A 209 ? 0.8838 0.5811 0.7264 -0.0547 0.0571  0.0952  208 SER A O   
1478 C CB  . SER A 209 ? 0.9304 0.6447 0.8090 -0.0560 0.0627  0.1180  208 SER A CB  
1479 O OG  . SER A 209 ? 0.9578 0.6464 0.8287 -0.0556 0.0638  0.1116  208 SER A OG  
1480 N N   . TRP A 210 ? 0.8720 0.5882 0.7352 -0.0597 0.0518  0.1085  209 TRP A N   
1481 C CA  . TRP A 210 ? 1.0117 0.7197 0.8669 -0.0617 0.0471  0.1035  209 TRP A CA  
1482 C C   . TRP A 210 ? 1.0705 0.7673 0.9320 -0.0661 0.0442  0.1069  209 TRP A C   
1483 O O   . TRP A 210 ? 1.1635 0.8721 1.0385 -0.0686 0.0424  0.1159  209 TRP A O   
1484 C CB  . TRP A 210 ? 0.9585 0.6870 0.8142 -0.0619 0.0433  0.1054  209 TRP A CB  
1485 C CG  . TRP A 210 ? 1.0068 0.7278 0.8518 -0.0625 0.0396  0.0992  209 TRP A CG  
1486 C CD1 . TRP A 210 ? 1.0382 0.7616 0.8860 -0.0662 0.0340  0.1021  209 TRP A CD1 
1487 C CD2 . TRP A 210 ? 0.9386 0.6493 0.7688 -0.0597 0.0408  0.0898  209 TRP A CD2 
1488 N NE1 . TRP A 210 ? 1.0070 0.7230 0.8430 -0.0658 0.0318  0.0954  209 TRP A NE1 
1489 C CE2 . TRP A 210 ? 0.9308 0.6386 0.7559 -0.0616 0.0360  0.0877  209 TRP A CE2 
1490 C CE3 . TRP A 210 ? 0.9470 0.6513 0.7683 -0.0559 0.0454  0.0837  209 TRP A CE3 
1491 C CZ2 . TRP A 210 ? 0.9360 0.6348 0.7478 -0.0597 0.0358  0.0799  209 TRP A CZ2 
1492 C CZ3 . TRP A 210 ? 0.9784 0.6730 0.7862 -0.0541 0.0451  0.0756  209 TRP A CZ3 
1493 C CH2 . TRP A 210 ? 0.9443 0.6363 0.7476 -0.0558 0.0404  0.0737  209 TRP A CH2 
1494 N N   . ASP A 211 ? 0.9447 0.6185 0.7958 -0.0673 0.0438  0.0998  210 ASP A N   
1495 C CA  . ASP A 211 ? 1.0438 0.7040 0.8968 -0.0725 0.0402  0.1011  210 ASP A CA  
1496 C C   . ASP A 211 ? 1.0383 0.6953 0.8809 -0.0756 0.0344  0.0962  210 ASP A C   
1497 O O   . ASP A 211 ? 1.1370 0.7815 0.9656 -0.0741 0.0353  0.0875  210 ASP A O   
1498 C CB  . ASP A 211 ? 1.1095 0.7441 0.9582 -0.0720 0.0448  0.0971  210 ASP A CB  
1499 C CG  . ASP A 211 ? 1.1244 0.7462 0.9785 -0.0774 0.0421  0.1007  210 ASP A CG  
1500 O OD1 . ASP A 211 ? 1.1264 0.7405 0.9739 -0.0826 0.0364  0.0979  210 ASP A OD1 
1501 O OD2 . ASP A 211 ? 1.1796 0.7991 1.0448 -0.0767 0.0456  0.1066  210 ASP A OD2 
1502 N N   . ASN A 212 ? 1.0343 0.7038 0.8844 -0.0799 0.0284  0.1026  211 ASN A N   
1503 C CA  . ASN A 212 ? 1.0445 0.7147 0.8872 -0.0831 0.0225  0.1001  211 ASN A CA  
1504 C C   . ASN A 212 ? 1.0885 0.7321 0.9172 -0.0864 0.0214  0.0919  211 ASN A C   
1505 O O   . ASN A 212 ? 1.1610 0.8003 0.9777 -0.0858 0.0200  0.0855  211 ASN A O   
1506 C CB  . ASN A 212 ? 1.2186 0.9040 1.0733 -0.0883 0.0163  0.1098  211 ASN A CB  
1507 C CG  . ASN A 212 ? 1.3128 1.0013 1.1617 -0.0922 0.0096  0.1093  211 ASN A CG  
1508 O OD1 . ASN A 212 ? 1.3592 1.0301 1.1957 -0.0948 0.0078  0.1024  211 ASN A OD1 
1509 N ND2 . ASN A 212 ? 1.2290 0.9414 1.0874 -0.0926 0.0060  0.1173  211 ASN A ND2 
1510 N N   . GLY A 213 ? 1.1425 0.7676 0.9723 -0.0898 0.0223  0.0919  212 GLY A N   
1511 C CA  . GLY A 213 ? 1.2098 0.8090 1.0256 -0.0939 0.0210  0.0842  212 GLY A CA  
1512 C C   . GLY A 213 ? 1.1399 0.7255 0.9417 -0.0889 0.0265  0.0743  212 GLY A C   
1513 O O   . GLY A 213 ? 1.2302 0.8075 1.0186 -0.0905 0.0240  0.0678  212 GLY A O   
1514 N N   . LEU A 214 ? 1.1566 0.7406 0.9617 -0.0829 0.0338  0.0738  213 LEU A N   
1515 C CA  . LEU A 214 ? 1.1932 0.7644 0.9858 -0.0782 0.0393  0.0653  213 LEU A CA  
1516 C C   . LEU A 214 ? 1.2448 0.8290 1.0309 -0.0751 0.0380  0.0620  213 LEU A C   
1517 O O   . LEU A 214 ? 1.3543 0.9268 1.1270 -0.0734 0.0397  0.0542  213 LEU A O   
1518 C CB  . LEU A 214 ? 1.1256 0.6958 0.9253 -0.0726 0.0472  0.0675  213 LEU A CB  
1519 C CG  . LEU A 214 ? 1.1771 0.7312 0.9825 -0.0742 0.0501  0.0701  213 LEU A CG  
1520 C CD1 . LEU A 214 ? 1.1581 0.7222 0.9775 -0.0691 0.0562  0.0772  213 LEU A CD1 
1521 C CD2 . LEU A 214 ? 1.1287 0.6540 0.9188 -0.0745 0.0534  0.0609  213 LEU A CD2 
1522 N N   . ALA A 215 ? 1.1748 0.7827 0.9699 -0.0742 0.0353  0.0679  214 ALA A N   
1523 C CA  . ALA A 215 ? 1.1570 0.7764 0.9460 -0.0710 0.0344  0.0650  214 ALA A CA  
1524 C C   . ALA A 215 ? 1.1903 0.8029 0.9688 -0.0748 0.0289  0.0609  214 ALA A C   
1525 O O   . ALA A 215 ? 1.2141 0.8232 0.9818 -0.0723 0.0296  0.0549  214 ALA A O   
1526 C CB  . ALA A 215 ? 1.0415 0.6870 0.8421 -0.0691 0.0332  0.0723  214 ALA A CB  
1527 N N   . GLY A 216 ? 1.1334 0.7441 0.9150 -0.0813 0.0232  0.0647  215 GLY A N   
1528 C CA  . GLY A 216 ? 1.2834 0.8891 1.0556 -0.0860 0.0173  0.0620  215 GLY A CA  
1529 C C   . GLY A 216 ? 1.3475 0.9287 1.1038 -0.0875 0.0188  0.0528  215 GLY A C   
1530 O O   . GLY A 216 ? 1.2319 0.8107 0.9777 -0.0880 0.0165  0.0486  215 GLY A O   
1531 N N   . GLN A 217 ? 1.5841 1.1472 1.3385 -0.0879 0.0231  0.0500  216 GLN A N   
1532 C CA  . GLN A 217 ? 1.6267 1.1661 1.3653 -0.0885 0.0257  0.0409  216 GLN A CA  
1533 C C   . GLN A 217 ? 1.5723 1.1135 1.3040 -0.0816 0.0305  0.0357  216 GLN A C   
1534 O O   . GLN A 217 ? 1.6087 1.1421 1.3274 -0.0824 0.0292  0.0298  216 GLN A O   
1535 C CB  . GLN A 217 ? 1.6594 1.1798 1.3986 -0.0891 0.0306  0.0396  216 GLN A CB  
1536 C CG  . GLN A 217 ? 1.6851 1.2043 1.4336 -0.0952 0.0267  0.0459  216 GLN A CG  
1537 C CD  . GLN A 217 ? 1.8764 1.3851 1.6156 -0.1046 0.0191  0.0440  216 GLN A CD  
1538 O OE1 . GLN A 217 ? 1.9697 1.4575 1.6932 -0.1074 0.0196  0.0361  216 GLN A OE1 
1539 N NE2 . GLN A 217 ? 1.9500 1.4738 1.6985 -0.1098 0.0119  0.0517  216 GLN A NE2 
1540 N N   . LEU A 218 ? 1.1758 0.7276 0.9159 -0.0753 0.0358  0.0382  217 LEU A N   
1541 C CA  . LEU A 218 ? 1.2404 0.7957 0.9748 -0.0692 0.0398  0.0341  217 LEU A CA  
1542 C C   . LEU A 218 ? 1.1747 0.7444 0.9069 -0.0686 0.0355  0.0343  217 LEU A C   
1543 O O   . LEU A 218 ? 1.1459 0.7137 0.8694 -0.0652 0.0373  0.0294  217 LEU A O   
1544 C CB  . LEU A 218 ? 1.1153 0.6808 0.8600 -0.0638 0.0455  0.0378  217 LEU A CB  
1545 C CG  . LEU A 218 ? 0.9900 0.5432 0.7389 -0.0629 0.0510  0.0388  217 LEU A CG  
1546 C CD1 . LEU A 218 ? 0.9468 0.5148 0.7077 -0.0584 0.0555  0.0446  217 LEU A CD1 
1547 C CD2 . LEU A 218 ? 1.0585 0.5902 0.7940 -0.0615 0.0554  0.0311  217 LEU A CD2 
1548 N N   . SER A 219 ? 1.0852 0.6693 0.8254 -0.0716 0.0300  0.0403  218 SER A N   
1549 C CA  . SER A 219 ? 1.0794 0.6767 0.8178 -0.0706 0.0262  0.0412  218 SER A CA  
1550 C C   . SER A 219 ? 1.2007 0.7856 0.9258 -0.0741 0.0227  0.0361  218 SER A C   
1551 O O   . SER A 219 ? 1.2707 0.8602 0.9902 -0.0712 0.0223  0.0338  218 SER A O   
1552 C CB  . SER A 219 ? 1.0565 0.6723 0.8070 -0.0731 0.0214  0.0496  218 SER A CB  
1553 O OG  . SER A 219 ? 1.1305 0.7627 0.8918 -0.0686 0.0246  0.0542  218 SER A OG  
1554 N N   . LYS A 220 ? 1.2315 0.8005 0.9512 -0.0805 0.0202  0.0342  219 LYS A N   
1555 C CA  . LYS A 220 ? 1.2055 0.7617 0.9111 -0.0846 0.0170  0.0291  219 LYS A CA  
1556 C C   . LYS A 220 ? 1.1699 0.7144 0.8642 -0.0800 0.0224  0.0214  219 LYS A C   
1557 O O   . LYS A 220 ? 1.2263 0.7681 0.9107 -0.0806 0.0204  0.0180  219 LYS A O   
1558 C CB  . LYS A 220 ? 1.1546 0.6943 0.8554 -0.0930 0.0136  0.0281  219 LYS A CB  
1559 C CG  . LYS A 220 ? 1.3024 0.8532 1.0123 -0.0994 0.0064  0.0359  219 LYS A CG  
1560 C CD  . LYS A 220 ? 1.2804 0.8515 0.9939 -0.0988 0.0015  0.0408  219 LYS A CD  
1561 C CE  . LYS A 220 ? 1.3325 0.9206 1.0595 -0.1027 -0.0040 0.0506  219 LYS A CE  
1562 N NZ  . LYS A 220 ? 1.2279 0.8223 0.9679 -0.0996 -0.0003 0.0545  219 LYS A NZ  
1563 N N   . PHE A 221 ? 1.1262 0.6647 0.8224 -0.0754 0.0292  0.0193  220 PHE A N   
1564 C CA  . PHE A 221 ? 1.2066 0.7374 0.8939 -0.0704 0.0346  0.0133  220 PHE A CA  
1565 C C   . PHE A 221 ? 1.1539 0.7005 0.8436 -0.0652 0.0348  0.0145  220 PHE A C   
1566 O O   . PHE A 221 ? 1.0916 0.6337 0.7718 -0.0630 0.0359  0.0100  220 PHE A O   
1567 C CB  . PHE A 221 ? 1.2080 0.7312 0.8988 -0.0668 0.0418  0.0125  220 PHE A CB  
1568 C CG  . PHE A 221 ? 1.2525 0.7536 0.9350 -0.0699 0.0440  0.0081  220 PHE A CG  
1569 C CD1 . PHE A 221 ? 1.2080 0.7027 0.8948 -0.0750 0.0418  0.0107  220 PHE A CD1 
1570 C CD2 . PHE A 221 ? 1.2433 0.7293 0.9135 -0.0678 0.0486  0.0015  220 PHE A CD2 
1571 C CE1 . PHE A 221 ? 1.1298 0.6021 0.8078 -0.0778 0.0444  0.0060  220 PHE A CE1 
1572 C CE2 . PHE A 221 ? 1.1185 0.5834 0.7801 -0.0702 0.0514  -0.0030 220 PHE A CE2 
1573 C CZ  . PHE A 221 ? 1.0865 0.5437 0.7516 -0.0752 0.0495  -0.0010 220 PHE A CZ  
1574 N N   . THR A 222 ? 1.1302 0.6950 0.8320 -0.0631 0.0340  0.0204  221 THR A N   
1575 C CA  . THR A 222 ? 1.1395 0.7184 0.8429 -0.0583 0.0344  0.0214  221 THR A CA  
1576 C C   . THR A 222 ? 1.1748 0.7570 0.8728 -0.0599 0.0292  0.0213  221 THR A C   
1577 O O   . THR A 222 ? 1.1805 0.7633 0.8725 -0.0564 0.0303  0.0185  221 THR A O   
1578 C CB  . THR A 222 ? 1.0720 0.6692 0.7888 -0.0561 0.0347  0.0278  221 THR A CB  
1579 O OG1 . THR A 222 ? 1.1121 0.7092 0.8327 -0.0529 0.0403  0.0276  221 THR A OG1 
1580 C CG2 . THR A 222 ? 1.1187 0.7310 0.8369 -0.0524 0.0336  0.0294  221 THR A CG2 
1581 N N   . LEU A 223 ? 1.2516 0.8360 0.9521 -0.0656 0.0235  0.0250  222 LEU A N   
1582 C CA  . LEU A 223 ? 1.2477 0.8364 0.9441 -0.0678 0.0182  0.0263  222 LEU A CA  
1583 C C   . LEU A 223 ? 1.2520 0.8254 0.9341 -0.0691 0.0183  0.0198  222 LEU A C   
1584 O O   . LEU A 223 ? 1.2570 0.8344 0.9348 -0.0675 0.0166  0.0197  222 LEU A O   
1585 C CB  . LEU A 223 ? 1.2293 0.8221 0.9306 -0.0750 0.0117  0.0319  222 LEU A CB  
1586 C CG  . LEU A 223 ? 1.3797 0.9928 1.0956 -0.0741 0.0098  0.0403  222 LEU A CG  
1587 C CD1 . LEU A 223 ? 1.4690 1.0891 1.1874 -0.0807 0.0021  0.0464  222 LEU A CD1 
1588 C CD2 . LEU A 223 ? 1.3347 0.9628 1.0550 -0.0659 0.0132  0.0416  222 LEU A CD2 
1589 N N   . MET A 224 ? 1.1784 0.7339 0.8529 -0.0717 0.0207  0.0147  223 MET A N   
1590 C CA  . MET A 224 ? 1.1640 0.7047 0.8242 -0.0730 0.0213  0.0083  223 MET A CA  
1591 C C   . MET A 224 ? 1.1410 0.6830 0.7980 -0.0660 0.0261  0.0051  223 MET A C   
1592 O O   . MET A 224 ? 1.1437 0.6840 0.7928 -0.0657 0.0247  0.0031  223 MET A O   
1593 C CB  . MET A 224 ? 1.1448 0.6660 0.7978 -0.0767 0.0238  0.0036  223 MET A CB  
1594 C CG  . MET A 224 ? 1.1566 0.6626 0.7962 -0.0751 0.0278  -0.0036 223 MET A CG  
1595 S SD  . MET A 224 ? 1.3861 0.8688 1.0176 -0.0786 0.0318  -0.0089 223 MET A SD  
1596 C CE  . MET A 224 ? 1.1099 0.5907 0.7423 -0.0884 0.0240  -0.0057 223 MET A CE  
1597 N N   . ALA A 225 ? 1.1595 0.7048 0.8228 -0.0608 0.0315  0.0052  224 ALA A N   
1598 C CA  . ALA A 225 ? 1.1438 0.6910 0.8044 -0.0548 0.0356  0.0027  224 ALA A CA  
1599 C C   . ALA A 225 ? 1.0591 0.6204 0.7231 -0.0517 0.0333  0.0057  224 ALA A C   
1600 O O   . ALA A 225 ? 1.0479 0.6079 0.7061 -0.0484 0.0347  0.0032  224 ALA A O   
1601 C CB  . ALA A 225 ? 1.0688 0.6177 0.7358 -0.0509 0.0414  0.0030  224 ALA A CB  
1602 N N   . LEU A 226 ? 0.9864 0.5612 0.6599 -0.0524 0.0301  0.0113  225 LEU A N   
1603 C CA  . LEU A 226 ? 1.1316 0.7198 0.8085 -0.0491 0.0283  0.0147  225 LEU A CA  
1604 C C   . LEU A 226 ? 1.1402 0.7248 0.8094 -0.0513 0.0243  0.0142  225 LEU A C   
1605 O O   . LEU A 226 ? 0.9948 0.5821 0.6612 -0.0471 0.0251  0.0136  225 LEU A O   
1606 C CB  . LEU A 226 ? 1.0088 0.6125 0.6975 -0.0498 0.0256  0.0215  225 LEU A CB  
1607 C CG  . LEU A 226 ? 1.0054 0.6191 0.7029 -0.0458 0.0296  0.0235  225 LEU A CG  
1608 C CD1 . LEU A 226 ? 1.0374 0.6652 0.7462 -0.0479 0.0265  0.0305  225 LEU A CD1 
1609 C CD2 . LEU A 226 ? 0.8102 0.4300 0.5064 -0.0392 0.0330  0.0221  225 LEU A CD2 
1610 N N   . ILE A 227 ? 1.1034 0.6817 0.7689 -0.0581 0.0198  0.0146  226 ILE A N   
1611 C CA  . ILE A 227 ? 1.1160 0.6910 0.7735 -0.0614 0.0155  0.0144  226 ILE A CA  
1612 C C   . ILE A 227 ? 1.1013 0.6637 0.7475 -0.0594 0.0188  0.0081  226 ILE A C   
1613 O O   . ILE A 227 ? 1.0414 0.6052 0.6831 -0.0582 0.0173  0.0084  226 ILE A O   
1614 C CB  . ILE A 227 ? 1.0649 0.6342 0.7192 -0.0705 0.0099  0.0156  226 ILE A CB  
1615 C CG1 . ILE A 227 ? 1.0692 0.6532 0.7357 -0.0727 0.0060  0.0233  226 ILE A CG1 
1616 C CG2 . ILE A 227 ? 1.1382 0.7032 0.7825 -0.0749 0.0054  0.0152  226 ILE A CG2 
1617 C CD1 . ILE A 227 ? 1.0879 0.6881 0.7597 -0.0716 0.0019  0.0302  226 ILE A CD1 
1618 N N   . THR A 228 ? 1.1030 0.6538 0.7453 -0.0586 0.0236  0.0030  227 THR A N   
1619 C CA  . THR A 228 ? 1.0517 0.5919 0.6842 -0.0562 0.0272  -0.0025 227 THR A CA  
1620 C C   . THR A 228 ? 1.0838 0.6314 0.7190 -0.0494 0.0300  -0.0020 227 THR A C   
1621 O O   . THR A 228 ? 1.1877 0.7307 0.8156 -0.0479 0.0306  -0.0042 227 THR A O   
1622 C CB  . THR A 228 ? 1.0643 0.5922 0.6936 -0.0563 0.0322  -0.0069 227 THR A CB  
1623 O OG1 . THR A 228 ? 1.1762 0.6963 0.8036 -0.0624 0.0300  -0.0073 227 THR A OG1 
1624 C CG2 . THR A 228 ? 0.9684 0.4847 0.5865 -0.0549 0.0355  -0.0121 227 THR A CG2 
1625 N N   . SER A 229 ? 1.0680 0.6266 0.7131 -0.0455 0.0318  0.0010  228 SER A N   
1626 C CA  . SER A 229 ? 1.1081 0.6713 0.7544 -0.0393 0.0352  0.0004  228 SER A CA  
1627 C C   . SER A 229 ? 1.0106 0.5814 0.6574 -0.0367 0.0327  0.0033  228 SER A C   
1628 O O   . SER A 229 ? 0.9642 0.5321 0.6066 -0.0331 0.0346  0.0014  228 SER A O   
1629 C CB  . SER A 229 ? 1.0488 0.6207 0.7042 -0.0365 0.0382  0.0022  228 SER A CB  
1630 O OG  . SER A 229 ? 1.1169 0.6824 0.7729 -0.0384 0.0409  0.0005  228 SER A OG  
1631 N N   . VAL A 230 ? 1.0100 0.5907 0.6628 -0.0384 0.0286  0.0085  229 VAL A N   
1632 C CA  . VAL A 230 ? 0.9765 0.5669 0.6324 -0.0350 0.0269  0.0127  229 VAL A CA  
1633 C C   . VAL A 230 ? 1.0371 0.6240 0.6868 -0.0386 0.0224  0.0139  229 VAL A C   
1634 O O   . VAL A 230 ? 1.0195 0.6155 0.6728 -0.0370 0.0199  0.0191  229 VAL A O   
1635 C CB  . VAL A 230 ? 1.0172 0.6231 0.6843 -0.0339 0.0253  0.0190  229 VAL A CB  
1636 C CG1 . VAL A 230 ? 1.0020 0.6189 0.6736 -0.0284 0.0253  0.0237  229 VAL A CG1 
1637 C CG2 . VAL A 230 ? 0.9341 0.5431 0.6065 -0.0318 0.0293  0.0178  229 VAL A CG2 
1638 N N   . THR A 231 ? 1.0226 0.5966 0.6629 -0.0433 0.0217  0.0095  230 THR A N   
1639 C CA  . THR A 231 ? 1.0189 0.5896 0.6520 -0.0473 0.0175  0.0104  230 THR A CA  
1640 C C   . THR A 231 ? 1.0733 0.6340 0.6972 -0.0452 0.0201  0.0059  230 THR A C   
1641 O O   . THR A 231 ? 0.9993 0.5637 0.6243 -0.0402 0.0212  0.0075  230 THR A O   
1642 C CB  . THR A 231 ? 1.0381 0.6024 0.6662 -0.0560 0.0134  0.0095  230 THR A CB  
1643 O OG1 . THR A 231 ? 1.1116 0.6651 0.7367 -0.0569 0.0172  0.0040  230 THR A OG1 
1644 C CG2 . THR A 231 ? 1.0047 0.5811 0.6415 -0.0595 0.0085  0.0162  230 THR A CG2 
1645 N N   . LEU A 232 ? 1.1245 0.6722 0.7391 -0.0489 0.0213  0.0005  231 LEU A N   
1646 C CA  . LEU A 232 ? 0.9511 0.4899 0.5569 -0.0473 0.0237  -0.0033 231 LEU A CA  
1647 C C   . LEU A 232 ? 1.0637 0.6027 0.6722 -0.0403 0.0288  -0.0049 231 LEU A C   
1648 O O   . LEU A 232 ? 1.1458 0.6829 0.7505 -0.0378 0.0294  -0.0050 231 LEU A O   
1649 C CB  . LEU A 232 ? 0.9295 0.4546 0.5250 -0.0520 0.0249  -0.0088 231 LEU A CB  
1650 C CG  . LEU A 232 ? 1.0220 0.5428 0.6092 -0.0596 0.0198  -0.0087 231 LEU A CG  
1651 C CD1 . LEU A 232 ? 1.0603 0.5669 0.6344 -0.0620 0.0223  -0.0146 231 LEU A CD1 
1652 C CD2 . LEU A 232 ? 1.0164 0.5470 0.6051 -0.0605 0.0147  -0.0031 231 LEU A CD2 
1653 N N   . PRO A 233 ? 1.0271 0.5681 0.6415 -0.0376 0.0324  -0.0059 232 PRO A N   
1654 C CA  . PRO A 233 ? 1.0910 0.6324 0.7071 -0.0319 0.0366  -0.0072 232 PRO A CA  
1655 C C   . PRO A 233 ? 1.0234 0.5725 0.6434 -0.0273 0.0359  -0.0038 232 PRO A C   
1656 O O   . PRO A 233 ? 1.0019 0.5469 0.6180 -0.0243 0.0375  -0.0050 232 PRO A O   
1657 C CB  . PRO A 233 ? 1.1022 0.6468 0.7247 -0.0311 0.0395  -0.0077 232 PRO A CB  
1658 C CG  . PRO A 233 ? 1.1082 0.6473 0.7286 -0.0362 0.0385  -0.0090 232 PRO A CG  
1659 C CD  . PRO A 233 ? 1.0013 0.5416 0.6193 -0.0402 0.0332  -0.0068 232 PRO A CD  
1660 N N   . VAL A 234 ? 0.9497 0.5096 0.5775 -0.0265 0.0337  0.0008  233 VAL A N   
1661 C CA  . VAL A 234 ? 1.0704 0.6375 0.7022 -0.0213 0.0337  0.0045  233 VAL A CA  
1662 C C   . VAL A 234 ? 1.0410 0.6063 0.6686 -0.0222 0.0306  0.0068  233 VAL A C   
1663 O O   . VAL A 234 ? 1.1187 0.6862 0.7477 -0.0172 0.0316  0.0091  233 VAL A O   
1664 C CB  . VAL A 234 ? 0.9526 0.5332 0.5944 -0.0200 0.0324  0.0097  233 VAL A CB  
1665 C CG1 . VAL A 234 ? 1.0118 0.5947 0.6578 -0.0202 0.0348  0.0078  233 VAL A CG1 
1666 C CG2 . VAL A 234 ? 1.0641 0.6500 0.7077 -0.0253 0.0266  0.0143  233 VAL A CG2 
1667 N N   . ALA A 235 ? 1.0591 0.6201 0.6810 -0.0284 0.0270  0.0063  234 ALA A N   
1668 C CA  . ALA A 235 ? 1.0525 0.6118 0.6693 -0.0301 0.0240  0.0084  234 ALA A CA  
1669 C C   . ALA A 235 ? 1.1549 0.7047 0.7651 -0.0272 0.0272  0.0048  234 ALA A C   
1670 O O   . ALA A 235 ? 1.1474 0.6987 0.7582 -0.0236 0.0272  0.0076  234 ALA A O   
1671 C CB  . ALA A 235 ? 1.0461 0.6018 0.6565 -0.0383 0.0196  0.0079  234 ALA A CB  
1672 N N   . TYR A 236 ? 1.1374 0.6777 0.7418 -0.0287 0.0301  -0.0010 235 TYR A N   
1673 C CA  . TYR A 236 ? 1.1887 0.7206 0.7870 -0.0267 0.0330  -0.0040 235 TYR A CA  
1674 C C   . TYR A 236 ? 1.1416 0.6751 0.7442 -0.0202 0.0361  -0.0033 235 TYR A C   
1675 O O   . TYR A 236 ? 1.1818 0.7109 0.7811 -0.0180 0.0369  -0.0032 235 TYR A O   
1676 C CB  . TYR A 236 ? 1.2084 0.7318 0.8014 -0.0290 0.0360  -0.0092 235 TYR A CB  
1677 C CG  . TYR A 236 ? 1.3082 0.8252 0.8927 -0.0345 0.0343  -0.0112 235 TYR A CG  
1678 C CD1 . TYR A 236 ? 1.3158 0.8355 0.8977 -0.0386 0.0294  -0.0085 235 TYR A CD1 
1679 C CD2 . TYR A 236 ? 1.3725 0.8809 0.9511 -0.0359 0.0377  -0.0155 235 TYR A CD2 
1680 C CE1 . TYR A 236 ? 1.3011 0.8140 0.8735 -0.0442 0.0280  -0.0109 235 TYR A CE1 
1681 C CE2 . TYR A 236 ? 1.4642 0.9656 1.0339 -0.0405 0.0369  -0.0179 235 TYR A CE2 
1682 C CZ  . TYR A 236 ? 1.4212 0.9244 0.9871 -0.0449 0.0320  -0.0159 235 TYR A CZ  
1683 O OH  . TYR A 236 ? 1.4426 0.9380 0.9979 -0.0500 0.0313  -0.0188 235 TYR A OH  
1684 N N   . ILE A 237 ? 1.0871 0.6265 0.6966 -0.0174 0.0378  -0.0029 236 ILE A N   
1685 C CA  . ILE A 237 ? 1.0650 0.6047 0.6771 -0.0115 0.0412  -0.0031 236 ILE A CA  
1686 C C   . ILE A 237 ? 1.0464 0.5897 0.6612 -0.0075 0.0401  0.0015  236 ILE A C   
1687 O O   . ILE A 237 ? 1.1006 0.6382 0.7128 -0.0038 0.0421  0.0009  236 ILE A O   
1688 C CB  . ILE A 237 ? 1.0628 0.6091 0.6812 -0.0097 0.0434  -0.0035 236 ILE A CB  
1689 C CG1 . ILE A 237 ? 1.0525 0.5950 0.6689 -0.0132 0.0451  -0.0074 236 ILE A CG1 
1690 C CG2 . ILE A 237 ? 0.9023 0.4486 0.5221 -0.0038 0.0469  -0.0040 236 ILE A CG2 
1691 C CD1 . ILE A 237 ? 1.0538 0.6037 0.6767 -0.0123 0.0468  -0.0072 236 ILE A CD1 
1692 N N   . MET A 238 ? 1.0065 0.5593 0.6267 -0.0081 0.0367  0.0066  237 MET A N   
1693 C CA  . MET A 238 ? 1.1421 0.6999 0.7662 -0.0040 0.0357  0.0124  237 MET A CA  
1694 C C   . MET A 238 ? 1.1028 0.6541 0.7210 -0.0054 0.0340  0.0132  237 MET A C   
1695 O O   . MET A 238 ? 1.0524 0.6028 0.6721 -0.0005 0.0352  0.0161  237 MET A O   
1696 C CB  . MET A 238 ? 1.0271 0.5979 0.6585 -0.0056 0.0318  0.0189  237 MET A CB  
1697 C CG  . MET A 238 ? 0.9769 0.5570 0.6165 -0.0021 0.0338  0.0206  237 MET A CG  
1698 S SD  . MET A 238 ? 1.2289 0.8230 0.8755 -0.0073 0.0282  0.0271  237 MET A SD  
1699 C CE  . MET A 238 ? 1.1097 0.7166 0.7657 -0.0010 0.0278  0.0369  237 MET A CE  
1700 N N   . MET A 239 ? 1.1078 0.6543 0.7191 -0.0118 0.0315  0.0107  238 MET A N   
1701 C CA  . MET A 239 ? 1.1350 0.6764 0.7402 -0.0137 0.0297  0.0117  238 MET A CA  
1702 C C   . MET A 239 ? 1.1371 0.6681 0.7376 -0.0107 0.0335  0.0079  238 MET A C   
1703 O O   . MET A 239 ? 1.1635 0.6916 0.7624 -0.0089 0.0331  0.0104  238 MET A O   
1704 C CB  . MET A 239 ? 1.1506 0.6898 0.7487 -0.0214 0.0263  0.0099  238 MET A CB  
1705 C CG  . MET A 239 ? 1.2225 0.7714 0.8236 -0.0256 0.0212  0.0152  238 MET A CG  
1706 S SD  . MET A 239 ? 1.4839 1.0286 1.0750 -0.0355 0.0172  0.0122  238 MET A SD  
1707 C CE  . MET A 239 ? 1.1721 0.7027 0.7539 -0.0354 0.0220  0.0041  238 MET A CE  
1708 N N   . ARG A 240 ? 1.0936 0.6193 0.6923 -0.0104 0.0369  0.0024  239 ARG A N   
1709 C CA  . ARG A 240 ? 1.0881 0.6046 0.6827 -0.0081 0.0401  -0.0007 239 ARG A CA  
1710 C C   . ARG A 240 ? 1.0547 0.5710 0.6536 -0.0016 0.0427  0.0008  239 ARG A C   
1711 O O   . ARG A 240 ? 1.0977 0.6061 0.6933 0.0006  0.0444  0.0001  239 ARG A O   
1712 C CB  . ARG A 240 ? 1.0351 0.5472 0.6266 -0.0104 0.0428  -0.0060 239 ARG A CB  
1713 C CG  . ARG A 240 ? 0.9705 0.4814 0.5577 -0.0159 0.0415  -0.0080 239 ARG A CG  
1714 C CD  . ARG A 240 ? 1.0223 0.5274 0.6060 -0.0171 0.0448  -0.0121 239 ARG A CD  
1715 N NE  . ARG A 240 ? 1.1386 0.6433 0.7203 -0.0211 0.0450  -0.0142 239 ARG A NE  
1716 C CZ  . ARG A 240 ? 1.2139 0.7234 0.7998 -0.0224 0.0445  -0.0144 239 ARG A CZ  
1717 N NH1 . ARG A 240 ? 1.1001 0.6168 0.6930 -0.0200 0.0438  -0.0124 239 ARG A NH1 
1718 N NH2 . ARG A 240 ? 1.2606 0.7674 0.8437 -0.0259 0.0451  -0.0164 239 ARG A NH2 
1719 N N   . LYS A 241 ? 1.0672 0.5915 0.6730 0.0016  0.0434  0.0029  240 LYS A N   
1720 C CA  . LYS A 241 ? 1.0146 0.5385 0.6241 0.0086  0.0465  0.0043  240 LYS A CA  
1721 C C   . LYS A 241 ? 1.0232 0.5488 0.6356 0.0119  0.0451  0.0105  240 LYS A C   
1722 O O   . LYS A 241 ? 0.9617 0.4801 0.5731 0.0166  0.0477  0.0108  240 LYS A O   
1723 C CB  . LYS A 241 ? 0.9485 0.4815 0.5646 0.0114  0.0481  0.0050  240 LYS A CB  
1724 C CG  . LYS A 241 ? 1.0817 0.6109 0.6953 0.0118  0.0518  -0.0007 240 LYS A CG  
1725 C CD  . LYS A 241 ? 1.1030 0.6385 0.7220 0.0176  0.0551  0.0004  240 LYS A CD  
1726 C CE  . LYS A 241 ? 1.1144 0.6642 0.7421 0.0177  0.0526  0.0060  240 LYS A CE  
1727 N NZ  . LYS A 241 ? 1.1385 0.6957 0.7719 0.0238  0.0561  0.0078  240 LYS A NZ  
1728 N N   . LEU A 242 ? 0.9987 0.5334 0.6145 0.0092  0.0408  0.0157  241 LEU A N   
1729 C CA  . LEU A 242 ? 1.0250 0.5628 0.6439 0.0113  0.0389  0.0226  241 LEU A CA  
1730 C C   . LEU A 242 ? 1.0645 0.5924 0.6764 0.0092  0.0381  0.0215  241 LEU A C   
1731 O O   . LEU A 242 ? 1.0542 0.5799 0.6680 0.0132  0.0386  0.0258  241 LEU A O   
1732 C CB  . LEU A 242 ? 1.0070 0.5573 0.6300 0.0071  0.0337  0.0286  241 LEU A CB  
1733 C CG  . LEU A 242 ? 0.9862 0.5421 0.6124 0.0074  0.0304  0.0369  241 LEU A CG  
1734 C CD1 . LEU A 242 ? 1.0136 0.5735 0.6486 0.0165  0.0337  0.0428  241 LEU A CD1 
1735 C CD2 . LEU A 242 ? 1.0599 0.6271 0.6874 0.0007  0.0245  0.0416  241 LEU A CD2 
1736 N N   . LEU A 243 ? 1.0869 0.6091 0.6912 0.0033  0.0372  0.0163  242 LEU A N   
1737 C CA  . LEU A 243 ? 1.0282 0.5420 0.6258 0.0010  0.0365  0.0155  242 LEU A CA  
1738 C C   . LEU A 243 ? 1.0789 0.5818 0.6743 0.0050  0.0405  0.0124  242 LEU A C   
1739 O O   . LEU A 243 ? 1.1068 0.6038 0.7002 0.0061  0.0403  0.0146  242 LEU A O   
1740 C CB  . LEU A 243 ? 0.9474 0.4591 0.5377 -0.0060 0.0348  0.0112  242 LEU A CB  
1741 C CG  . LEU A 243 ? 0.9945 0.4981 0.5772 -0.0088 0.0347  0.0098  242 LEU A CG  
1742 C CD1 . LEU A 243 ? 1.0781 0.5862 0.6584 -0.0126 0.0305  0.0143  242 LEU A CD1 
1743 C CD2 . LEU A 243 ? 1.0224 0.5213 0.5992 -0.0126 0.0364  0.0037  242 LEU A CD2 
1744 N N   . ALA A 244 ? 1.0513 0.5511 0.6465 0.0068  0.0439  0.0075  243 ALA A N   
1745 C CA  . ALA A 244 ? 1.0783 0.5672 0.6705 0.0099  0.0476  0.0042  243 ALA A CA  
1746 C C   . ALA A 244 ? 1.0523 0.5396 0.6492 0.0173  0.0502  0.0074  243 ALA A C   
1747 O O   . ALA A 244 ? 1.0232 0.4995 0.6167 0.0200  0.0530  0.0051  243 ALA A O   
1748 C CB  . ALA A 244 ? 1.0264 0.5134 0.6161 0.0084  0.0501  -0.0019 243 ALA A CB  
1749 N N   . ALA A 245 ? 1.0648 0.5625 0.6693 0.0207  0.0494  0.0127  244 ALA A N   
1750 C CA  . ALA A 245 ? 0.9892 0.4865 0.5992 0.0288  0.0525  0.0167  244 ALA A CA  
1751 C C   . ALA A 245 ? 1.1298 0.6253 0.7419 0.0305  0.0509  0.0232  244 ALA A C   
1752 O O   . ALA A 245 ? 1.1613 0.6480 0.7739 0.0363  0.0542  0.0243  244 ALA A O   
1753 C CB  . ALA A 245 ? 0.8652 0.3762 0.4837 0.0321  0.0528  0.0206  244 ALA A CB  
1754 N N   . GLN A 246 ? 1.2199 0.7231 0.8327 0.0255  0.0458  0.0276  245 GLN A N   
1755 C CA  . GLN A 246 ? 1.3189 0.8214 0.9332 0.0261  0.0437  0.0341  245 GLN A CA  
1756 C C   . GLN A 246 ? 1.2586 0.7480 0.8649 0.0231  0.0438  0.0304  245 GLN A C   
1757 O O   . GLN A 246 ? 1.2367 0.7184 0.8437 0.0268  0.0452  0.0334  245 GLN A O   
1758 C CB  . GLN A 246 ? 1.2566 0.7724 0.8733 0.0207  0.0380  0.0399  245 GLN A CB  
1759 C CG  . GLN A 246 ? 1.2755 0.8053 0.8997 0.0218  0.0369  0.0438  245 GLN A CG  
1760 C CD  . GLN A 246 ? 1.4079 0.9466 1.0423 0.0278  0.0370  0.0540  245 GLN A CD  
1761 O OE1 . GLN A 246 ? 1.4051 0.9422 1.0408 0.0290  0.0359  0.0596  245 GLN A OE1 
1762 N NE2 . GLN A 246 ? 1.5242 1.0731 1.1666 0.0318  0.0383  0.0573  245 GLN A NE2 
1763 N N   . TYR A 247 ? 1.1935 0.6805 0.7925 0.0166  0.0424  0.0245  246 TYR A N   
1764 C CA  . TYR A 247 ? 1.1840 0.6603 0.7754 0.0130  0.0424  0.0213  246 TYR A CA  
1765 C C   . TYR A 247 ? 1.1829 0.6499 0.7698 0.0132  0.0460  0.0137  246 TYR A C   
1766 O O   . TYR A 247 ? 1.3093 0.7754 0.8988 0.0178  0.0493  0.0116  246 TYR A O   
1767 C CB  . TYR A 247 ? 1.1543 0.6357 0.7411 0.0057  0.0384  0.0214  246 TYR A CB  
1768 C CG  . TYR A 247 ? 1.1820 0.6725 0.7720 0.0046  0.0344  0.0290  246 TYR A CG  
1769 C CD1 . TYR A 247 ? 1.1687 0.6713 0.7640 0.0044  0.0322  0.0326  246 TYR A CD1 
1770 C CD2 . TYR A 247 ? 1.2418 0.7296 0.8298 0.0032  0.0325  0.0333  246 TYR A CD2 
1771 C CE1 . TYR A 247 ? 1.1994 0.7111 0.7974 0.0026  0.0281  0.0402  246 TYR A CE1 
1772 C CE2 . TYR A 247 ? 1.2160 0.7131 0.8068 0.0016  0.0287  0.0408  246 TYR A CE2 
1773 C CZ  . TYR A 247 ? 1.1644 0.6735 0.7601 0.0012  0.0264  0.0442  246 TYR A CZ  
1774 O OH  . TYR A 247 ? 1.1510 0.6703 0.7492 -0.0012 0.0221  0.0523  246 TYR A OH  
1775 N N   . SER A 248 ? 1.1621 0.6231 0.7421 0.0081  0.0455  0.0099  247 SER A N   
1776 C CA  . SER A 248 ? 1.1327 0.5856 0.7079 0.0070  0.0483  0.0036  247 SER A CA  
1777 C C   . SER A 248 ? 1.0649 0.5243 0.6388 0.0029  0.0481  -0.0005 247 SER A C   
1778 O O   . SER A 248 ? 1.1222 0.5903 0.6975 0.0004  0.0458  0.0009  247 SER A O   
1779 C CB  . SER A 248 ? 1.0647 0.5072 0.6339 0.0039  0.0479  0.0031  247 SER A CB  
1780 O OG  . SER A 248 ? 1.1000 0.5468 0.6667 -0.0011 0.0449  0.0051  247 SER A OG  
1781 N N   . TRP A 249 ? 1.0616 0.5163 0.6326 0.0022  0.0506  -0.0054 248 TRP A N   
1782 C CA  . TRP A 249 ? 0.9271 0.3867 0.4967 -0.0022 0.0507  -0.0088 248 TRP A CA  
1783 C C   . TRP A 249 ? 0.9675 0.4254 0.5324 -0.0074 0.0492  -0.0085 248 TRP A C   
1784 O O   . TRP A 249 ? 0.9924 0.4555 0.5568 -0.0107 0.0491  -0.0099 248 TRP A O   
1785 C CB  . TRP A 249 ? 1.0093 0.4653 0.5772 -0.0020 0.0536  -0.0133 248 TRP A CB  
1786 C CG  . TRP A 249 ? 0.9431 0.4050 0.5158 0.0020  0.0554  -0.0143 248 TRP A CG  
1787 C CD1 . TRP A 249 ? 0.9595 0.4172 0.5326 0.0068  0.0581  -0.0155 248 TRP A CD1 
1788 C CD2 . TRP A 249 ? 1.0263 0.4993 0.6039 0.0015  0.0548  -0.0141 248 TRP A CD2 
1789 N NE1 . TRP A 249 ? 0.9313 0.3980 0.5096 0.0096  0.0593  -0.0156 248 TRP A NE1 
1790 C CE2 . TRP A 249 ? 0.9603 0.4366 0.5418 0.0061  0.0570  -0.0146 248 TRP A CE2 
1791 C CE3 . TRP A 249 ? 0.9932 0.4732 0.5721 -0.0024 0.0527  -0.0135 248 TRP A CE3 
1792 C CZ2 . TRP A 249 ? 0.8661 0.3534 0.4533 0.0066  0.0568  -0.0139 248 TRP A CZ2 
1793 C CZ3 . TRP A 249 ? 1.0020 0.4912 0.5860 -0.0021 0.0525  -0.0133 248 TRP A CZ3 
1794 C CH2 . TRP A 249 ? 0.9943 0.4877 0.5829 0.0022  0.0543  -0.0132 248 TRP A CH2 
1795 N N   . ASP A 250 ? 1.0720 0.5228 0.6336 -0.0081 0.0484  -0.0065 249 ASP A N   
1796 C CA  . ASP A 250 ? 1.0745 0.5251 0.6320 -0.0126 0.0469  -0.0051 249 ASP A CA  
1797 C C   . ASP A 250 ? 1.0462 0.5045 0.6046 -0.0136 0.0447  -0.0025 249 ASP A C   
1798 O O   . ASP A 250 ? 0.9213 0.3823 0.4764 -0.0172 0.0445  -0.0031 249 ASP A O   
1799 C CB  . ASP A 250 ? 1.0266 0.4684 0.5811 -0.0130 0.0462  -0.0026 249 ASP A CB  
1800 C CG  . ASP A 250 ? 1.0346 0.4669 0.5874 -0.0120 0.0480  -0.0052 249 ASP A CG  
1801 O OD1 . ASP A 250 ? 1.0237 0.4540 0.5790 -0.0076 0.0496  -0.0065 249 ASP A OD1 
1802 O OD2 . ASP A 250 ? 1.0971 0.5238 0.6455 -0.0159 0.0480  -0.0057 249 ASP A OD2 
1803 N N   . GLU A 251 ? 1.0362 0.4981 0.5986 -0.0105 0.0432  0.0005  250 GLU A N   
1804 C CA  . GLU A 251 ? 0.9773 0.4469 0.5400 -0.0123 0.0406  0.0030  250 GLU A CA  
1805 C C   . GLU A 251 ? 0.9957 0.4714 0.5590 -0.0142 0.0410  -0.0002 250 GLU A C   
1806 O O   . GLU A 251 ? 1.0891 0.5684 0.6491 -0.0177 0.0394  -0.0001 250 GLU A O   
1807 C CB  . GLU A 251 ? 1.0105 0.4838 0.5785 -0.0087 0.0387  0.0082  250 GLU A CB  
1808 C CG  . GLU A 251 ? 1.0298 0.5109 0.5971 -0.0116 0.0351  0.0122  250 GLU A CG  
1809 C CD  . GLU A 251 ? 1.0722 0.5511 0.6343 -0.0146 0.0333  0.0149  250 GLU A CD  
1810 O OE1 . GLU A 251 ? 1.1552 0.6266 0.7146 -0.0147 0.0349  0.0139  250 GLU A OE1 
1811 O OE2 . GLU A 251 ? 1.0586 0.5437 0.6190 -0.0175 0.0302  0.0183  250 GLU A OE2 
1812 N N   . VAL A 252 ? 1.0031 0.4793 0.5699 -0.0120 0.0431  -0.0031 251 VAL A N   
1813 C CA  . VAL A 252 ? 0.9652 0.4466 0.5330 -0.0139 0.0437  -0.0060 251 VAL A CA  
1814 C C   . VAL A 252 ? 1.0130 0.4918 0.5758 -0.0178 0.0452  -0.0088 251 VAL A C   
1815 O O   . VAL A 252 ? 1.0488 0.5305 0.6100 -0.0205 0.0450  -0.0101 251 VAL A O   
1816 C CB  . VAL A 252 ? 1.0688 0.5521 0.6418 -0.0107 0.0457  -0.0079 251 VAL A CB  
1817 C CG1 . VAL A 252 ? 0.9193 0.4094 0.4950 -0.0125 0.0456  -0.0094 251 VAL A CG1 
1818 C CG2 . VAL A 252 ? 1.0065 0.4910 0.5842 -0.0058 0.0453  -0.0047 251 VAL A CG2 
1819 N N   . GLY A 253 ? 0.9654 0.4384 0.5256 -0.0181 0.0469  -0.0095 252 GLY A N   
1820 C CA  . GLY A 253 ? 1.0060 0.4776 0.5623 -0.0213 0.0486  -0.0109 252 GLY A CA  
1821 C C   . GLY A 253 ? 0.9805 0.4521 0.5316 -0.0238 0.0475  -0.0094 252 GLY A C   
1822 O O   . GLY A 253 ? 1.0240 0.4957 0.5720 -0.0260 0.0495  -0.0106 252 GLY A O   
1823 N N   . ILE A 254 ? 1.0681 0.5397 0.6181 -0.0234 0.0448  -0.0063 253 ILE A N   
1824 C CA  . ILE A 254 ? 1.0503 0.5228 0.5946 -0.0261 0.0435  -0.0047 253 ILE A CA  
1825 C C   . ILE A 254 ? 1.0587 0.5350 0.6011 -0.0281 0.0430  -0.0067 253 ILE A C   
1826 O O   . ILE A 254 ? 1.1575 0.6330 0.6941 -0.0307 0.0444  -0.0083 253 ILE A O   
1827 C CB  . ILE A 254 ? 1.0570 0.5293 0.6013 -0.0254 0.0405  -0.0001 253 ILE A CB  
1828 C CG1 . ILE A 254 ? 0.9858 0.4524 0.5298 -0.0247 0.0412  0.0017  253 ILE A CG1 
1829 C CG2 . ILE A 254 ? 1.1261 0.6014 0.6644 -0.0287 0.0385  0.0017  253 ILE A CG2 
1830 C CD1 . ILE A 254 ? 1.0017 0.4667 0.5405 -0.0276 0.0430  0.0014  253 ILE A CD1 
1831 N N   . TRP A 255 ? 1.0325 0.5127 0.5797 -0.0270 0.0411  -0.0064 254 TRP A N   
1832 C CA  . TRP A 255 ? 1.0960 0.5794 0.6414 -0.0296 0.0400  -0.0081 254 TRP A CA  
1833 C C   . TRP A 255 ? 1.1214 0.6036 0.6677 -0.0300 0.0433  -0.0123 254 TRP A C   
1834 O O   . TRP A 255 ? 1.2320 0.7130 0.7735 -0.0328 0.0440  -0.0146 254 TRP A O   
1835 C CB  . TRP A 255 ? 1.0586 0.5479 0.6097 -0.0286 0.0366  -0.0053 254 TRP A CB  
1836 C CG  . TRP A 255 ? 1.0695 0.5622 0.6196 -0.0318 0.0349  -0.0066 254 TRP A CG  
1837 C CD1 . TRP A 255 ? 1.1620 0.6525 0.7041 -0.0365 0.0344  -0.0089 254 TRP A CD1 
1838 C CD2 . TRP A 255 ? 1.1586 0.6570 0.7157 -0.0310 0.0335  -0.0058 254 TRP A CD2 
1839 N NE1 . TRP A 255 ? 1.0975 0.5910 0.6407 -0.0391 0.0325  -0.0097 254 TRP A NE1 
1840 C CE2 . TRP A 255 ? 1.1007 0.5998 0.6536 -0.0358 0.0317  -0.0074 254 TRP A CE2 
1841 C CE3 . TRP A 255 ? 1.1356 0.6383 0.7016 -0.0266 0.0337  -0.0039 254 TRP A CE3 
1842 C CZ2 . TRP A 255 ? 1.1319 0.6366 0.6901 -0.0368 0.0296  -0.0065 254 TRP A CZ2 
1843 C CZ3 . TRP A 255 ? 1.1174 0.6265 0.6887 -0.0270 0.0321  -0.0029 254 TRP A CZ3 
1844 C CH2 . TRP A 255 ? 1.1566 0.6670 0.7244 -0.0322 0.0298  -0.0039 254 TRP A CH2 
1845 N N   . GLN A 256 ? 1.1033 0.5854 0.6552 -0.0273 0.0454  -0.0132 255 GLN A N   
1846 C CA  . GLN A 256 ? 1.0992 0.5812 0.6528 -0.0276 0.0486  -0.0162 255 GLN A CA  
1847 C C   . GLN A 256 ? 1.1251 0.6032 0.6734 -0.0291 0.0518  -0.0174 255 GLN A C   
1848 O O   . GLN A 256 ? 1.1858 0.6635 0.7340 -0.0299 0.0545  -0.0195 255 GLN A O   
1849 C CB  . GLN A 256 ? 1.0586 0.5422 0.6188 -0.0249 0.0500  -0.0164 255 GLN A CB  
1850 C CG  . GLN A 256 ? 1.1528 0.6390 0.7171 -0.0252 0.0522  -0.0185 255 GLN A CG  
1851 C CD  . GLN A 256 ? 1.2316 0.7219 0.7988 -0.0259 0.0502  -0.0187 255 GLN A CD  
1852 O OE1 . GLN A 256 ? 1.2694 0.7625 0.8380 -0.0252 0.0470  -0.0168 255 GLN A OE1 
1853 N NE2 . GLN A 256 ? 1.2702 0.7610 0.8387 -0.0273 0.0520  -0.0204 255 GLN A NE2 
1854 N N   . GLY A 257 ? 0.9657 0.4413 0.5100 -0.0293 0.0519  -0.0156 256 GLY A N   
1855 C CA  . GLY A 257 ? 1.0632 0.5364 0.6028 -0.0304 0.0553  -0.0159 256 GLY A CA  
1856 C C   . GLY A 257 ? 1.1958 0.6672 0.7285 -0.0325 0.0561  -0.0178 256 GLY A C   
1857 O O   . GLY A 257 ? 1.1751 0.6447 0.7056 -0.0326 0.0602  -0.0193 256 GLY A O   
1858 N N   . VAL A 258 ? 1.1586 0.6304 0.6874 -0.0343 0.0525  -0.0175 257 VAL A N   
1859 C CA  . VAL A 258 ? 1.2183 0.6874 0.7385 -0.0371 0.0530  -0.0198 257 VAL A CA  
1860 C C   . VAL A 258 ? 1.1679 0.6356 0.6897 -0.0378 0.0543  -0.0232 257 VAL A C   
1861 O O   . VAL A 258 ? 1.1154 0.5784 0.6306 -0.0394 0.0571  -0.0262 257 VAL A O   
1862 C CB  . VAL A 258 ? 1.2418 0.7127 0.7572 -0.0398 0.0481  -0.0179 257 VAL A CB  
1863 C CG1 . VAL A 258 ? 1.1519 0.6245 0.6680 -0.0387 0.0465  -0.0137 257 VAL A CG1 
1864 C CG2 . VAL A 258 ? 1.2307 0.7055 0.7512 -0.0406 0.0439  -0.0172 257 VAL A CG2 
1865 N N   . SER A 259 ? 1.1677 0.6392 0.6982 -0.0365 0.0525  -0.0228 258 SER A N   
1866 C CA  . SER A 259 ? 1.2321 0.7028 0.7654 -0.0371 0.0538  -0.0253 258 SER A CA  
1867 C C   . SER A 259 ? 1.1908 0.6596 0.7268 -0.0350 0.0594  -0.0264 258 SER A C   
1868 O O   . SER A 259 ? 1.2537 0.7186 0.7880 -0.0357 0.0623  -0.0289 258 SER A O   
1869 C CB  . SER A 259 ? 1.1904 0.6670 0.7325 -0.0362 0.0505  -0.0238 258 SER A CB  
1870 O OG  . SER A 259 ? 1.2293 0.7093 0.7706 -0.0374 0.0456  -0.0213 258 SER A OG  
1871 N N   . SER A 260 ? 1.1916 0.6626 0.7315 -0.0326 0.0611  -0.0243 259 SER A N   
1872 C CA  . SER A 260 ? 1.1878 0.6587 0.7310 -0.0309 0.0661  -0.0240 259 SER A CA  
1873 C C   . SER A 260 ? 1.0961 0.5621 0.6319 -0.0311 0.0705  -0.0250 259 SER A C   
1874 O O   . SER A 260 ? 1.1947 0.6595 0.7325 -0.0299 0.0752  -0.0254 259 SER A O   
1875 C CB  . SER A 260 ? 1.1830 0.6576 0.7309 -0.0295 0.0661  -0.0211 259 SER A CB  
1876 O OG  . SER A 260 ? 1.1783 0.6511 0.7210 -0.0297 0.0673  -0.0193 259 SER A OG  
1877 N N   . ILE A 261 ? 1.2155 0.6791 0.7430 -0.0324 0.0694  -0.0249 260 ILE A N   
1878 C CA  . ILE A 261 ? 1.2185 0.6776 0.7379 -0.0323 0.0740  -0.0259 260 ILE A CA  
1879 C C   . ILE A 261 ? 1.2363 0.6889 0.7495 -0.0338 0.0754  -0.0303 260 ILE A C   
1880 O O   . ILE A 261 ? 1.1775 0.6255 0.6881 -0.0323 0.0813  -0.0318 260 ILE A O   
1881 C CB  . ILE A 261 ? 1.0609 0.5202 0.5731 -0.0335 0.0721  -0.0241 260 ILE A CB  
1882 C CG1 . ILE A 261 ? 1.1300 0.5931 0.6461 -0.0317 0.0739  -0.0198 260 ILE A CG1 
1883 C CG2 . ILE A 261 ? 1.0774 0.5310 0.5777 -0.0348 0.0748  -0.0268 260 ILE A CG2 
1884 C CD1 . ILE A 261 ? 1.0552 0.5192 0.5659 -0.0329 0.0716  -0.0171 260 ILE A CD1 
1885 N N   . SER A 262 ? 1.3135 0.7654 0.8242 -0.0369 0.0703  -0.0320 261 SER A N   
1886 C CA  . SER A 262 ? 1.3443 0.7892 0.8481 -0.0396 0.0708  -0.0363 261 SER A CA  
1887 C C   . SER A 262 ? 1.3470 0.7900 0.8578 -0.0380 0.0740  -0.0376 261 SER A C   
1888 O O   . SER A 262 ? 1.3928 0.8276 0.8978 -0.0387 0.0776  -0.0411 261 SER A O   
1889 C CB  . SER A 262 ? 1.3323 0.7789 0.8335 -0.0439 0.0637  -0.0365 261 SER A CB  
1890 O OG  . SER A 262 ? 1.3936 0.8456 0.9055 -0.0435 0.0604  -0.0350 261 SER A OG  
1891 N N   . ASP A 263 ? 1.3018 0.7519 0.8246 -0.0359 0.0729  -0.0348 262 ASP A N   
1892 C CA  . ASP A 263 ? 1.3191 0.7692 0.8499 -0.0345 0.0758  -0.0350 262 ASP A CA  
1893 C C   . ASP A 263 ? 1.3134 0.7601 0.8444 -0.0312 0.0834  -0.0346 262 ASP A C   
1894 O O   . ASP A 263 ? 1.3971 0.8428 0.9342 -0.0299 0.0865  -0.0346 262 ASP A O   
1895 C CB  . ASP A 263 ? 1.3408 0.8003 0.8836 -0.0331 0.0731  -0.0317 262 ASP A CB  
1896 C CG  . ASP A 263 ? 1.4438 0.9071 0.9883 -0.0354 0.0665  -0.0316 262 ASP A CG  
1897 O OD1 . ASP A 263 ? 1.4085 0.8790 0.9617 -0.0341 0.0645  -0.0293 262 ASP A OD1 
1898 O OD2 . ASP A 263 ? 1.4360 0.8955 0.9727 -0.0386 0.0635  -0.0334 262 ASP A OD2 
1899 N N   . ALA A 264 ? 1.3062 0.7519 0.8317 -0.0298 0.0865  -0.0337 263 ALA A N   
1900 C CA  . ALA A 264 ? 1.2666 0.7105 0.7931 -0.0262 0.0942  -0.0323 263 ALA A CA  
1901 C C   . ALA A 264 ? 1.2662 0.6988 0.7847 -0.0260 0.0990  -0.0366 263 ALA A C   
1902 O O   . ALA A 264 ? 1.3291 0.7593 0.8531 -0.0236 0.1038  -0.0363 263 ALA A O   
1903 C CB  . ALA A 264 ? 1.2461 0.6930 0.7691 -0.0248 0.0960  -0.0294 263 ALA A CB  
1904 N N   . TYR A 265 ? 1.3676 0.7929 0.8729 -0.0288 0.0978  -0.0407 264 TYR A N   
1905 C CA  . TYR A 265 ? 1.3247 0.7372 0.8196 -0.0291 0.1026  -0.0457 264 TYR A CA  
1906 C C   . TYR A 265 ? 1.3200 0.7264 0.8144 -0.0329 0.0991  -0.0494 264 TYR A C   
1907 O O   . TYR A 265 ? 1.4054 0.8005 0.8946 -0.0326 0.1037  -0.0531 264 TYR A O   
1908 C CB  . TYR A 265 ? 1.2837 0.6905 0.7628 -0.0311 0.1030  -0.0487 264 TYR A CB  
1909 C CG  . TYR A 265 ? 1.2032 0.6120 0.6762 -0.0369 0.0943  -0.0501 264 TYR A CG  
1910 C CD1 . TYR A 265 ? 1.2510 0.6534 0.7181 -0.0421 0.0900  -0.0542 264 TYR A CD1 
1911 C CD2 . TYR A 265 ? 1.1696 0.5869 0.6429 -0.0374 0.0904  -0.0465 264 TYR A CD2 
1912 C CE1 . TYR A 265 ? 1.2623 0.6681 0.7246 -0.0475 0.0820  -0.0542 264 TYR A CE1 
1913 C CE2 . TYR A 265 ? 1.1799 0.5999 0.6487 -0.0423 0.0828  -0.0467 264 TYR A CE2 
1914 C CZ  . TYR A 265 ? 1.2498 0.6646 0.7134 -0.0473 0.0787  -0.0503 264 TYR A CZ  
1915 O OH  . TYR A 265 ? 1.1046 0.5236 0.5646 -0.0522 0.0711  -0.0493 264 TYR A OH  
1916 N N   . LEU A 266 ? 1.2984 0.7118 0.7982 -0.0362 0.0912  -0.0481 265 LEU A N   
1917 C CA  . LEU A 266 ? 1.4307 0.8396 0.9295 -0.0407 0.0869  -0.0509 265 LEU A CA  
1918 C C   . LEU A 266 ? 1.5783 0.9847 1.0864 -0.0385 0.0905  -0.0504 265 LEU A C   
1919 O O   . LEU A 266 ? 1.6536 1.0506 1.1573 -0.0416 0.0903  -0.0539 265 LEU A O   
1920 C CB  . LEU A 266 ? 1.4176 0.8367 0.9219 -0.0438 0.0781  -0.0483 265 LEU A CB  
1921 C CG  . LEU A 266 ? 1.2451 0.6644 0.7388 -0.0481 0.0728  -0.0492 265 LEU A CG  
1922 C CD1 . LEU A 266 ? 1.3370 0.7675 0.8388 -0.0498 0.0651  -0.0454 265 LEU A CD1 
1923 C CD2 . LEU A 266 ? 1.3109 0.7185 0.7906 -0.0536 0.0720  -0.0544 265 LEU A CD2 
1924 N N   . GLN A 267 ? 1.6259 1.0408 1.1468 -0.0338 0.0937  -0.0459 266 GLN A N   
1925 C CA  . GLN A 267 ? 1.6054 1.0199 1.1366 -0.0319 0.0967  -0.0443 266 GLN A CA  
1926 C C   . GLN A 267 ? 1.6901 1.0930 1.2171 -0.0286 0.1055  -0.0463 266 GLN A C   
1927 O O   . GLN A 267 ? 1.6546 1.0509 1.1847 -0.0288 0.1075  -0.0473 266 GLN A O   
1928 C CB  . GLN A 267 ? 1.5496 0.9781 1.0957 -0.0287 0.0965  -0.0383 266 GLN A CB  
1929 C CG  . GLN A 267 ? 1.5797 1.0192 1.1283 -0.0298 0.0904  -0.0361 266 GLN A CG  
1930 C CD  . GLN A 267 ? 1.6772 1.1170 1.2216 -0.0344 0.0827  -0.0382 266 GLN A CD  
1931 O OE1 . GLN A 267 ? 1.8023 1.2368 1.3445 -0.0376 0.0806  -0.0406 266 GLN A OE1 
1932 N NE2 . GLN A 267 ? 1.6352 1.0815 1.1787 -0.0349 0.0785  -0.0368 266 GLN A NE2 
1933 N N   . PHE A 268 ? 1.8064 1.2065 1.3267 -0.0254 0.1111  -0.0464 267 PHE A N   
1934 C CA  . PHE A 268 ? 1.7757 1.1630 1.2894 -0.0221 0.1200  -0.0490 267 PHE A CA  
1935 C C   . PHE A 268 ? 1.8032 1.1743 1.3016 -0.0267 0.1190  -0.0565 267 PHE A C   
1936 O O   . PHE A 268 ? 1.9176 1.2753 1.4116 -0.0251 0.1254  -0.0595 267 PHE A O   
1937 C CB  . PHE A 268 ? 1.7423 1.1313 1.2514 -0.0178 0.1260  -0.0472 267 PHE A CB  
1938 C CG  . PHE A 268 ? 1.8440 1.2253 1.3531 -0.0117 0.1369  -0.0465 267 PHE A CG  
1939 C CD1 . PHE A 268 ? 1.8214 1.2004 1.3409 -0.0090 0.1408  -0.0444 267 PHE A CD1 
1940 C CD2 . PHE A 268 ? 1.9062 1.2829 1.4054 -0.0083 0.1436  -0.0474 267 PHE A CD2 
1941 C CE1 . PHE A 268 ? 1.8091 1.1810 1.3297 -0.0028 0.1514  -0.0431 267 PHE A CE1 
1942 C CE2 . PHE A 268 ? 1.8450 1.2149 1.3447 -0.0019 0.1544  -0.0462 267 PHE A CE2 
1943 C CZ  . PHE A 268 ? 1.8360 1.2032 1.3467 0.0011  0.1584  -0.0440 267 PHE A CZ  
1944 N N   . ILE A 269 ? 1.7204 1.0924 1.2104 -0.0327 0.1111  -0.0592 268 ILE A N   
1945 C CA  . ILE A 269 ? 1.7012 1.0593 1.1766 -0.0388 0.1086  -0.0658 268 ILE A CA  
1946 C C   . ILE A 269 ? 1.7530 1.1087 1.2353 -0.0423 0.1045  -0.0660 268 ILE A C   
1947 O O   . ILE A 269 ? 1.7467 1.0872 1.2207 -0.0450 0.1065  -0.0708 268 ILE A O   
1948 C CB  . ILE A 269 ? 1.6216 0.9833 1.0865 -0.0443 0.1013  -0.0673 268 ILE A CB  
1949 C CG1 . ILE A 269 ? 1.5533 0.9071 1.0022 -0.0434 0.1064  -0.0709 268 ILE A CG1 
1950 C CG2 . ILE A 269 ? 1.6047 0.9613 1.0631 -0.0526 0.0935  -0.0706 268 ILE A CG2 
1951 C CD1 . ILE A 269 ? 1.5861 0.9439 1.0400 -0.0354 0.1149  -0.0675 268 ILE A CD1 
1952 N N   . THR A 270 ? 1.7261 1.0965 1.2235 -0.0424 0.0990  -0.0607 269 THR A N   
1953 C CA  . THR A 270 ? 1.7613 1.1319 1.2670 -0.0454 0.0952  -0.0598 269 THR A CA  
1954 C C   . THR A 270 ? 1.8378 1.2029 1.3521 -0.0408 0.1025  -0.0584 269 THR A C   
1955 O O   . THR A 270 ? 1.8023 1.1641 1.3216 -0.0435 0.1004  -0.0582 269 THR A O   
1956 C CB  . THR A 270 ? 1.5860 0.9744 1.1050 -0.0462 0.0879  -0.0544 269 THR A CB  
1957 O OG1 . THR A 270 ? 1.5614 0.9613 1.0918 -0.0401 0.0913  -0.0495 269 THR A OG1 
1958 C CG2 . THR A 270 ? 1.5738 0.9671 1.0853 -0.0510 0.0803  -0.0551 269 THR A CG2 
1959 N N   . ALA A 271 ? 1.9585 1.3234 1.4753 -0.0340 0.1109  -0.0566 270 ALA A N   
1960 C CA  . ALA A 271 ? 1.8396 1.1978 1.3635 -0.0293 0.1189  -0.0551 270 ALA A CA  
1961 C C   . ALA A 271 ? 1.7913 1.1277 1.3017 -0.0314 0.1228  -0.0618 270 ALA A C   
1962 O O   . ALA A 271 ? 1.8487 1.1773 1.3650 -0.0292 0.1277  -0.0611 270 ALA A O   
1963 C CB  . ALA A 271 ? 1.8497 1.2135 1.3790 -0.0216 0.1271  -0.0508 270 ALA A CB  
1964 N N   . SER A 272 ? 1.7291 1.0551 1.2212 -0.0359 0.1210  -0.0683 271 SER A N   
1965 C CA  . SER A 272 ? 1.8029 1.1071 1.2793 -0.0399 0.1231  -0.0757 271 SER A CA  
1966 C C   . SER A 272 ? 1.7894 1.0910 1.2649 -0.0487 0.1139  -0.0774 271 SER A C   
1967 O O   . SER A 272 ? 1.6626 0.9466 1.1228 -0.0544 0.1132  -0.0839 271 SER A O   
1968 C CB  . SER A 272 ? 1.6463 0.9412 1.1022 -0.0416 0.1249  -0.0819 271 SER A CB  
1969 O OG  . SER A 272 ? 1.7367 1.0095 1.1753 -0.0464 0.1268  -0.0898 271 SER A OG  
1970 N N   . PHE A 273 ? 1.8478 1.1664 1.3390 -0.0500 0.1068  -0.0714 272 PHE A N   
1971 C CA  . PHE A 273 ? 1.7818 1.1016 1.2743 -0.0580 0.0975  -0.0714 272 PHE A CA  
1972 C C   . PHE A 273 ? 1.7170 1.0389 1.2254 -0.0565 0.0983  -0.0670 272 PHE A C   
1973 O O   . PHE A 273 ? 1.7048 1.0112 1.2088 -0.0599 0.0994  -0.0700 272 PHE A O   
1974 C CB  . PHE A 273 ? 1.6786 1.0170 1.1756 -0.0612 0.0883  -0.0677 272 PHE A CB  
1975 C CG  . PHE A 273 ? 1.7163 1.0509 1.1963 -0.0669 0.0838  -0.0721 272 PHE A CG  
1976 C CD1 . PHE A 273 ? 1.7067 1.0316 1.1749 -0.0761 0.0777  -0.0759 272 PHE A CD1 
1977 C CD2 . PHE A 273 ? 1.6378 0.9791 1.1137 -0.0636 0.0852  -0.0717 272 PHE A CD2 
1978 C CE1 . PHE A 273 ? 1.5744 0.8970 1.0270 -0.0819 0.0732  -0.0791 272 PHE A CE1 
1979 C CE2 . PHE A 273 ? 1.5701 0.9090 1.0310 -0.0690 0.0809  -0.0749 272 PHE A CE2 
1980 C CZ  . PHE A 273 ? 1.5042 0.8341 0.9534 -0.0782 0.0749  -0.0786 272 PHE A CZ  
1981 N N   . SER A 274 ? 1.6732 1.0136 1.1998 -0.0519 0.0978  -0.0599 273 SER A N   
1982 C CA  . SER A 274 ? 1.7258 1.0717 1.2683 -0.0515 0.0969  -0.0549 273 SER A CA  
1983 C C   . SER A 274 ? 1.7092 1.0404 1.2536 -0.0473 0.1061  -0.0554 273 SER A C   
1984 O O   . SER A 274 ? 1.6713 0.9985 1.2228 -0.0495 0.1050  -0.0537 273 SER A O   
1985 C CB  . SER A 274 ? 1.7479 1.1164 1.3076 -0.0472 0.0953  -0.0475 273 SER A CB  
1986 O OG  . SER A 274 ? 1.9028 1.2757 1.4627 -0.0407 0.1013  -0.0464 273 SER A OG  
1987 N N   . VAL A 275 ? 1.7320 1.0553 1.2707 -0.0410 0.1153  -0.0573 274 VAL A N   
1988 C CA  . VAL A 275 ? 1.7558 1.0666 1.2984 -0.0356 0.1250  -0.0567 274 VAL A CA  
1989 C C   . VAL A 275 ? 1.7690 1.0534 1.2943 -0.0395 0.1277  -0.0649 274 VAL A C   
1990 O O   . VAL A 275 ? 1.7946 1.0664 1.3237 -0.0382 0.1324  -0.0646 274 VAL A O   
1991 C CB  . VAL A 275 ? 1.7122 1.0278 1.2585 -0.0265 0.1344  -0.0537 274 VAL A CB  
1992 C CG1 . VAL A 275 ? 1.6299 0.9704 1.1898 -0.0243 0.1305  -0.0467 274 VAL A CG1 
1993 C CG2 . VAL A 275 ? 1.7830 1.0852 1.3098 -0.0255 0.1391  -0.0607 274 VAL A CG2 
1994 N N   . TYR A 276 ? 1.6891 0.9641 1.1950 -0.0447 0.1247  -0.0721 275 TYR A N   
1995 C CA  . TYR A 276 ? 1.6963 0.9450 1.1829 -0.0491 0.1274  -0.0807 275 TYR A CA  
1996 C C   . TYR A 276 ? 1.6288 0.8726 1.1058 -0.0608 0.1165  -0.0845 275 TYR A C   
1997 O O   . TYR A 276 ? 1.5954 0.8235 1.0668 -0.0655 0.1163  -0.0880 275 TYR A O   
1998 C CB  . TYR A 276 ? 1.7603 0.9991 1.2290 -0.0461 0.1340  -0.0868 275 TYR A CB  
1999 C CG  . TYR A 276 ? 1.8279 1.0511 1.2898 -0.0422 0.1436  -0.0910 275 TYR A CG  
2000 C CD1 . TYR A 276 ? 1.8785 1.0983 1.3338 -0.0345 0.1536  -0.0926 275 TYR A CD1 
2001 C CD2 . TYR A 276 ? 1.8308 1.0427 1.2930 -0.0461 0.1428  -0.0931 275 TYR A CD2 
2002 C CE1 . TYR A 276 ? 1.9420 1.1476 1.3912 -0.0304 0.1630  -0.0963 275 TYR A CE1 
2003 C CE2 . TYR A 276 ? 1.8650 1.0622 1.3211 -0.0423 0.1518  -0.0971 275 TYR A CE2 
2004 C CZ  . TYR A 276 ? 1.9013 1.0953 1.3507 -0.0342 0.1621  -0.0987 275 TYR A CZ  
2005 O OH  . TYR A 276 ? 1.8353 1.0142 1.2783 -0.0299 0.1718  -0.1025 275 TYR A OH  
2006 N N   . LEU A 277 ? 1.5982 0.8584 1.0752 -0.0657 0.1070  -0.0828 276 LEU A N   
2007 C CA  . LEU A 277 ? 1.5383 0.7962 1.0066 -0.0770 0.0963  -0.0851 276 LEU A CA  
2008 C C   . LEU A 277 ? 1.5979 0.8627 1.0818 -0.0805 0.0905  -0.0796 276 LEU A C   
2009 O O   . LEU A 277 ? 1.5371 0.7855 1.0152 -0.0864 0.0893  -0.0825 276 LEU A O   
2010 C CB  . LEU A 277 ? 1.5345 0.8092 0.9998 -0.0802 0.0885  -0.0838 276 LEU A CB  
2011 C CG  . LEU A 277 ? 1.3998 0.6698 0.8504 -0.0921 0.0787  -0.0873 276 LEU A CG  
2012 C CD1 . LEU A 277 ? 1.3205 0.5697 0.7463 -0.0955 0.0825  -0.0963 276 LEU A CD1 
2013 C CD2 . LEU A 277 ? 1.4802 0.7733 0.9374 -0.0944 0.0697  -0.0819 276 LEU A CD2 
2014 N N   . LEU A 278 ? 1.6368 0.9253 1.1400 -0.0770 0.0870  -0.0715 277 LEU A N   
2015 C CA  . LEU A 278 ? 1.5893 0.8888 1.1078 -0.0806 0.0803  -0.0653 277 LEU A CA  
2016 C C   . LEU A 278 ? 1.5695 0.8535 1.0915 -0.0815 0.0838  -0.0655 277 LEU A C   
2017 O O   . LEU A 278 ? 1.5349 0.8162 1.0570 -0.0898 0.0765  -0.0647 277 LEU A O   
2018 C CB  . LEU A 278 ? 1.4865 0.8112 1.0251 -0.0738 0.0799  -0.0573 277 LEU A CB  
2019 C CG  . LEU A 278 ? 1.5126 0.8550 1.0670 -0.0771 0.0719  -0.0502 277 LEU A CG  
2020 C CD1 . LEU A 278 ? 1.4888 0.8297 1.0575 -0.0748 0.0753  -0.0457 277 LEU A CD1 
2021 C CD2 . LEU A 278 ? 1.4672 0.8080 1.0130 -0.0875 0.0619  -0.0515 277 LEU A CD2 
2022 N N   . PRO A 279 ? 1.5837 0.8576 1.1094 -0.0737 0.0944  -0.0658 278 PRO A N   
2023 C CA  . PRO A 279 ? 1.6420 0.8993 1.1706 -0.0750 0.0976  -0.0660 278 PRO A CA  
2024 C C   . PRO A 279 ? 1.6474 0.8783 1.1547 -0.0837 0.0961  -0.0746 278 PRO A C   
2025 O O   . PRO A 279 ? 1.5944 0.8133 1.1032 -0.0887 0.0943  -0.0744 278 PRO A O   
2026 C CB  . PRO A 279 ? 1.6183 0.8709 1.1538 -0.0638 0.1103  -0.0644 278 PRO A CB  
2027 C CG  . PRO A 279 ? 1.6117 0.8698 1.1395 -0.0586 0.1141  -0.0669 278 PRO A CG  
2028 C CD  . PRO A 279 ? 1.5410 0.8196 1.0705 -0.0633 0.1037  -0.0647 278 PRO A CD  
2029 N N   . THR A 280 ? 1.6533 0.8745 1.1403 -0.0861 0.0965  -0.0821 279 THR A N   
2030 C CA  . THR A 280 ? 1.6412 0.8468 1.1113 -0.0937 0.0946  -0.0895 279 THR A CA  
2031 C C   . THR A 280 ? 1.6638 0.8690 1.1280 -0.1071 0.0816  -0.0892 279 THR A C   
2032 O O   . THR A 280 ? 1.7350 0.9298 1.1974 -0.1138 0.0785  -0.0904 279 THR A O   
2033 C CB  . THR A 280 ? 1.5512 0.7522 1.0037 -0.0918 0.0988  -0.0963 279 THR A CB  
2034 O OG1 . THR A 280 ? 1.4866 0.6816 0.9415 -0.0811 0.1115  -0.0977 279 THR A OG1 
2035 C CG2 . THR A 280 ? 1.6379 0.8262 1.0702 -0.1028 0.0931  -0.1034 279 THR A CG2 
2036 N N   . LEU A 281 ? 1.6547 0.8762 1.1188 -0.1107 0.0736  -0.0865 280 LEU A N   
2037 C CA  . LEU A 281 ? 1.6635 0.8911 1.1245 -0.1229 0.0610  -0.0847 280 LEU A CA  
2038 C C   . LEU A 281 ? 1.6905 0.9245 1.1687 -0.1259 0.0562  -0.0777 280 LEU A C   
2039 O O   . LEU A 281 ? 1.6898 0.9190 1.1627 -0.1371 0.0475  -0.0775 280 LEU A O   
2040 C CB  . LEU A 281 ? 1.6128 0.8655 1.0779 -0.1234 0.0537  -0.0803 280 LEU A CB  
2041 C CG  . LEU A 281 ? 1.4978 0.7535 0.9527 -0.1187 0.0575  -0.0839 280 LEU A CG  
2042 C CD1 . LEU A 281 ? 1.4719 0.7453 0.9446 -0.1065 0.0634  -0.0786 280 LEU A CD1 
2043 C CD2 . LEU A 281 ? 1.5198 0.7877 0.9673 -0.1268 0.0472  -0.0827 280 LEU A CD2 
2044 N N   . SER A 282 ? 1.6680 0.9138 1.1668 -0.1165 0.0613  -0.0714 281 SER A N   
2045 C CA  . SER A 282 ? 1.7117 0.9652 1.2277 -0.1189 0.0570  -0.0641 281 SER A CA  
2046 C C   . SER A 282 ? 1.6840 0.9105 1.1925 -0.1240 0.0594  -0.0681 281 SER A C   
2047 O O   . SER A 282 ? 1.7507 0.9770 1.2634 -0.1325 0.0518  -0.0646 281 SER A O   
2048 C CB  . SER A 282 ? 1.7303 1.0028 1.2691 -0.1078 0.0623  -0.0565 281 SER A CB  
2049 O OG  . SER A 282 ? 1.7694 1.0275 1.3080 -0.0991 0.0742  -0.0592 281 SER A OG  
2050 N N   . ARG A 283 ? 1.7174 0.9206 1.2147 -0.1188 0.0701  -0.0752 282 ARG A N   
2051 C CA  . ARG A 283 ? 1.7333 0.9198 1.2292 -0.1208 0.0731  -0.0780 282 ARG A CA  
2052 C C   . ARG A 283 ? 1.8122 0.9865 1.2894 -0.1339 0.0650  -0.0840 282 ARG A C   
2053 O O   . ARG A 283 ? 1.9160 1.0847 1.3954 -0.1426 0.0585  -0.0818 282 ARG A O   
2054 C CB  . ARG A 283 ? 1.7475 0.9257 1.2428 -0.1091 0.0865  -0.0821 282 ARG A CB  
2055 C CG  . ARG A 283 ? 1.7642 0.9537 1.2786 -0.0967 0.0949  -0.0754 282 ARG A CG  
2056 C CD  . ARG A 283 ? 1.9029 1.0830 1.4288 -0.0905 0.1031  -0.0733 282 ARG A CD  
2057 N NE  . ARG A 283 ? 1.8670 1.0581 1.4108 -0.0789 0.1113  -0.0662 282 ARG A NE  
2058 C CZ  . ARG A 283 ? 1.8095 1.0008 1.3708 -0.0744 0.1155  -0.0595 282 ARG A CZ  
2059 N NH1 . ARG A 283 ? 1.6992 0.8798 1.2632 -0.0801 0.1126  -0.0591 282 ARG A NH1 
2060 N NH2 . ARG A 283 ? 1.6739 0.8763 1.2504 -0.0643 0.1228  -0.0526 282 ARG A NH2 
2061 N N   . LEU A 284 ? 1.7852 0.9554 1.2435 -0.1359 0.0651  -0.0911 283 LEU A N   
2062 C CA  . LEU A 284 ? 1.8241 0.9826 1.2630 -0.1485 0.0579  -0.0970 283 LEU A CA  
2063 C C   . LEU A 284 ? 1.7996 0.9663 1.2387 -0.1616 0.0438  -0.0917 283 LEU A C   
2064 O O   . LEU A 284 ? 1.7206 0.9029 1.1703 -0.1605 0.0396  -0.0851 283 LEU A O   
2065 C CB  . LEU A 284 ? 1.7621 0.9168 1.1812 -0.1479 0.0609  -0.1046 283 LEU A CB  
2066 C CG  . LEU A 284 ? 1.6900 0.8345 1.1036 -0.1369 0.0744  -0.1107 283 LEU A CG  
2067 C CD1 . LEU A 284 ? 1.7191 0.8455 1.1322 -0.1369 0.0793  -0.1139 283 LEU A CD1 
2068 C CD2 . LEU A 284 ? 1.5401 0.6964 0.9688 -0.1225 0.0836  -0.1067 283 LEU A CD2 
2069 N N   . THR A 285 ? 1.9376 1.0932 1.3644 -0.1743 0.0364  -0.0945 284 THR A N   
2070 C CA  . THR A 285 ? 1.8754 1.0373 1.3026 -0.1882 0.0225  -0.0888 284 THR A CA  
2071 C C   . THR A 285 ? 1.9596 1.1155 1.3644 -0.2019 0.0138  -0.0935 284 THR A C   
2072 O O   . THR A 285 ? 1.9593 1.1262 1.3615 -0.2107 0.0035  -0.0890 284 THR A O   
2073 C CB  . THR A 285 ? 1.9344 1.0910 1.3742 -0.1921 0.0199  -0.0840 284 THR A CB  
2074 O OG1 . THR A 285 ? 2.0255 1.1942 1.4880 -0.1831 0.0234  -0.0760 284 THR A OG1 
2075 C CG2 . THR A 285 ? 1.8269 0.9850 1.2615 -0.2093 0.0054  -0.0798 284 THR A CG2 
2076 N N   . GLU A 286 ? 2.0278 1.1665 1.4161 -0.2041 0.0178  -0.1021 285 GLU A N   
2077 C CA  . GLU A 286 ? 2.0999 1.2319 1.4659 -0.2182 0.0093  -0.1064 285 GLU A CA  
2078 C C   . GLU A 286 ? 2.0680 1.2111 1.4240 -0.2188 0.0067  -0.1071 285 GLU A C   
2079 O O   . GLU A 286 ? 1.9983 1.1473 1.3583 -0.2064 0.0153  -0.1085 285 GLU A O   
2080 C CB  . GLU A 286 ? 2.1573 1.2680 1.5072 -0.2184 0.0162  -0.1160 285 GLU A CB  
2081 C CG  . GLU A 286 ? 2.1087 1.2105 1.4352 -0.2344 0.0071  -0.1203 285 GLU A CG  
2082 C CD  . GLU A 286 ? 2.1688 1.2481 1.4787 -0.2341 0.0148  -0.1301 285 GLU A CD  
2083 O OE1 . GLU A 286 ? 2.2623 1.3330 1.5797 -0.2212 0.0270  -0.1332 285 GLU A OE1 
2084 O OE2 . GLU A 286 ? 2.1623 1.2326 1.4514 -0.2469 0.0085  -0.1344 285 GLU A OE2 
2085 N N   . LYS A 287 ? 1.9980 1.1443 1.3414 -0.2338 -0.0056 -0.1056 286 LYS A N   
2086 C CA  . LYS A 287 ? 1.8777 1.0349 1.2113 -0.2364 -0.0097 -0.1054 286 LYS A CA  
2087 C C   . LYS A 287 ? 1.9540 1.1030 1.2720 -0.2293 0.0000  -0.1145 286 LYS A C   
2088 O O   . LYS A 287 ? 1.8610 1.0188 1.1817 -0.2197 0.0055  -0.1147 286 LYS A O   
2089 C CB  . LYS A 287 ? 1.8129 0.9735 1.1345 -0.2553 -0.0248 -0.1020 286 LYS A CB  
2090 C CG  . LYS A 287 ? 1.6760 0.8598 0.9998 -0.2569 -0.0318 -0.0959 286 LYS A CG  
2091 C CD  . LYS A 287 ? 1.6977 0.9121 1.0532 -0.2451 -0.0316 -0.0844 286 LYS A CD  
2092 C CE  . LYS A 287 ? 1.6299 0.8563 1.0013 -0.2527 -0.0412 -0.0745 286 LYS A CE  
2093 N NZ  . LYS A 287 ? 1.6234 0.8769 1.0005 -0.2610 -0.0537 -0.0642 286 LYS A NZ  
2094 N N   . ARG A 288 ? 2.0791 1.2110 1.3802 -0.2344 0.0023  -0.1218 287 ARG A N   
2095 C CA  . ARG A 288 ? 2.0735 1.1967 1.3587 -0.2286 0.0116  -0.1302 287 ARG A CA  
2096 C C   . ARG A 288 ? 2.0679 1.1922 1.3658 -0.2099 0.0259  -0.1317 287 ARG A C   
2097 O O   . ARG A 288 ? 1.9570 1.0835 1.2477 -0.2029 0.0324  -0.1352 287 ARG A O   
2098 C CB  . ARG A 288 ? 2.1175 1.2200 1.3844 -0.2362 0.0128  -0.1377 287 ARG A CB  
2099 C CG  . ARG A 288 ? 2.1301 1.2309 1.3758 -0.2539 0.0012  -0.1388 287 ARG A CG  
2100 C CD  . ARG A 288 ? 2.1245 1.2305 1.3760 -0.2681 -0.0128 -0.1315 287 ARG A CD  
2101 N NE  . ARG A 288 ? 1.9822 1.0842 1.2126 -0.2859 -0.0236 -0.1327 287 ARG A NE  
2102 C CZ  . ARG A 288 ? 2.0658 1.1507 1.2832 -0.2952 -0.0254 -0.1371 287 ARG A CZ  
2103 N NH1 . ARG A 288 ? 2.0951 1.1642 1.3180 -0.2884 -0.0171 -0.1412 287 ARG A NH1 
2104 N NH2 . ARG A 288 ? 2.1337 1.2172 1.3319 -0.3120 -0.0358 -0.1373 287 ARG A NH2 
2105 N N   . ASP A 289 ? 2.2355 1.3589 1.5524 -0.2021 0.0306  -0.1285 288 ASP A N   
2106 C CA  . ASP A 289 ? 2.1310 1.2575 1.4618 -0.1850 0.0434  -0.1284 288 ASP A CA  
2107 C C   . ASP A 289 ? 2.0316 1.1777 1.3740 -0.1787 0.0423  -0.1226 288 ASP A C   
2108 O O   . ASP A 289 ? 2.0459 1.1962 1.3909 -0.1669 0.0515  -0.1239 288 ASP A O   
2109 C CB  . ASP A 289 ? 2.1745 1.2955 1.5229 -0.1794 0.0479  -0.1256 288 ASP A CB  
2110 C CG  . ASP A 289 ? 2.2758 1.3756 1.6133 -0.1838 0.0507  -0.1318 288 ASP A CG  
2111 O OD1 . ASP A 289 ? 2.2005 1.2895 1.5161 -0.1913 0.0493  -0.1385 288 ASP A OD1 
2112 O OD2 . ASP A 289 ? 2.3023 1.3958 1.6530 -0.1800 0.0542  -0.1298 288 ASP A OD2 
2113 N N   . ILE A 290 ? 1.9261 1.0841 1.2753 -0.1866 0.0310  -0.1159 289 ILE A N   
2114 C CA  . ILE A 290 ? 1.8013 0.9769 1.1618 -0.1809 0.0297  -0.1102 289 ILE A CA  
2115 C C   . ILE A 290 ? 1.6940 0.8740 1.0390 -0.1822 0.0286  -0.1134 289 ILE A C   
2116 O O   . ILE A 290 ? 1.5948 0.7833 0.9450 -0.1719 0.0347  -0.1128 289 ILE A O   
2117 C CB  . ILE A 290 ? 1.7253 0.9149 1.0992 -0.1885 0.0181  -0.1011 289 ILE A CB  
2118 C CG1 . ILE A 290 ? 1.7184 0.9060 1.1107 -0.1845 0.0207  -0.0968 289 ILE A CG1 
2119 C CG2 . ILE A 290 ? 1.5623 0.7836 0.9522 -0.1816 0.0153  -0.0931 289 ILE A CG2 
2120 C CD1 . ILE A 290 ? 1.6785 0.8655 1.0835 -0.1686 0.0335  -0.0972 289 ILE A CD1 
2121 N N   . THR A 291 ? 1.7468 0.9215 1.0727 -0.1954 0.0207  -0.1164 290 THR A N   
2122 C CA  . THR A 291 ? 1.6190 0.7982 0.9296 -0.1979 0.0190  -0.1190 290 THR A CA  
2123 C C   . THR A 291 ? 1.6485 0.8213 0.9524 -0.1866 0.0319  -0.1255 290 THR A C   
2124 O O   . THR A 291 ? 1.6396 0.8207 0.9408 -0.1813 0.0345  -0.1256 290 THR A O   
2125 C CB  . THR A 291 ? 1.6483 0.8223 0.9392 -0.2151 0.0082  -0.1208 290 THR A CB  
2126 O OG1 . THR A 291 ? 1.6824 0.8652 0.9815 -0.2257 -0.0043 -0.1133 290 THR A OG1 
2127 C CG2 . THR A 291 ? 1.4165 0.5961 0.6914 -0.2184 0.0059  -0.1228 290 THR A CG2 
2128 N N   . ARG A 292 ? 1.7113 0.8695 1.0128 -0.1826 0.0403  -0.1305 291 ARG A N   
2129 C CA  . ARG A 292 ? 1.6685 0.8200 0.9639 -0.1720 0.0529  -0.1362 291 ARG A CA  
2130 C C   . ARG A 292 ? 1.6284 0.7912 0.9413 -0.1568 0.0612  -0.1324 291 ARG A C   
2131 O O   . ARG A 292 ? 1.5213 0.6865 0.8292 -0.1495 0.0683  -0.1345 291 ARG A O   
2132 C CB  . ARG A 292 ? 1.5647 0.6974 0.8554 -0.1706 0.0602  -0.1417 291 ARG A CB  
2133 C CG  . ARG A 292 ? 1.5442 0.6629 0.8124 -0.1842 0.0548  -0.1476 291 ARG A CG  
2134 C CD  . ARG A 292 ? 1.7415 0.8406 1.0006 -0.1793 0.0658  -0.1551 291 ARG A CD  
2135 N NE  . ARG A 292 ? 1.8670 0.9509 1.1054 -0.1929 0.0604  -0.1606 291 ARG A NE  
2136 C CZ  . ARG A 292 ? 1.7048 0.7838 0.9211 -0.1997 0.0592  -0.1659 291 ARG A CZ  
2137 N NH1 . ARG A 292 ? 1.4427 0.5308 0.6544 -0.1943 0.0628  -0.1663 291 ARG A NH1 
2138 N NH2 . ARG A 292 ? 1.5009 0.5655 0.6991 -0.2124 0.0541  -0.1706 291 ARG A NH2 
2139 N N   . GLU A 293 ? 1.6050 0.7752 0.9385 -0.1524 0.0604  -0.1263 292 GLU A N   
2140 C CA  . GLU A 293 ? 1.5876 0.7686 0.9381 -0.1387 0.0681  -0.1222 292 GLU A CA  
2141 C C   . GLU A 293 ? 1.5645 0.7612 0.9171 -0.1386 0.0628  -0.1182 292 GLU A C   
2142 O O   . GLU A 293 ? 1.4728 0.6772 0.8321 -0.1281 0.0696  -0.1167 292 GLU A O   
2143 C CB  . GLU A 293 ? 1.6282 0.8113 0.9997 -0.1342 0.0694  -0.1168 292 GLU A CB  
2144 C CG  . GLU A 293 ? 1.7302 0.9018 1.1067 -0.1255 0.0808  -0.1193 292 GLU A CG  
2145 C CD  . GLU A 293 ? 1.7820 0.9577 1.1634 -0.1118 0.0926  -0.1193 292 GLU A CD  
2146 O OE1 . GLU A 293 ? 1.8308 1.0206 1.2183 -0.1076 0.0918  -0.1155 292 GLU A OE1 
2147 O OE2 . GLU A 293 ? 1.8046 0.9691 1.1837 -0.1053 0.1027  -0.1227 292 GLU A OE2 
2148 N N   . VAL A 294 ? 1.5855 0.7869 0.9326 -0.1502 0.0507  -0.1160 293 VAL A N   
2149 C CA  . VAL A 294 ? 1.4698 0.6951 0.8241 -0.1488 0.0453  -0.1100 293 VAL A CA  
2150 C C   . VAL A 294 ? 1.4993 0.7196 0.8338 -0.1494 0.0480  -0.1156 293 VAL A C   
2151 O O   . VAL A 294 ? 1.4358 0.6709 0.7769 -0.1417 0.0506  -0.1124 293 VAL A O   
2152 C CB  . VAL A 294 ? 1.4138 0.6553 0.7747 -0.1592 0.0316  -0.1029 293 VAL A CB  
2153 C CG1 . VAL A 294 ? 1.3676 0.6264 0.7245 -0.1622 0.0251  -0.0995 293 VAL A CG1 
2154 C CG2 . VAL A 294 ? 1.4851 0.7444 0.8726 -0.1534 0.0298  -0.0941 293 VAL A CG2 
2155 N N   . VAL A 295 ? 1.4873 0.6892 0.7990 -0.1584 0.0474  -0.1231 294 VAL A N   
2156 C CA  . VAL A 295 ? 1.4043 0.6048 0.6980 -0.1597 0.0493  -0.1275 294 VAL A CA  
2157 C C   . VAL A 295 ? 1.4596 0.6584 0.7563 -0.1457 0.0629  -0.1299 294 VAL A C   
2158 O O   . VAL A 295 ? 1.4952 0.7005 0.7869 -0.1417 0.0654  -0.1300 294 VAL A O   
2159 C CB  . VAL A 295 ? 1.4522 0.6401 0.7255 -0.1722 0.0450  -0.1329 294 VAL A CB  
2160 C CG1 . VAL A 295 ? 1.5134 0.6981 0.7683 -0.1720 0.0494  -0.1380 294 VAL A CG1 
2161 C CG2 . VAL A 295 ? 1.4367 0.6295 0.7056 -0.1872 0.0303  -0.1292 294 VAL A CG2 
2162 N N   . LYS A 296 ? 1.4484 0.6388 0.7537 -0.1381 0.0718  -0.1313 295 LYS A N   
2163 C CA  . LYS A 296 ? 1.4377 0.6258 0.7452 -0.1253 0.0848  -0.1332 295 LYS A CA  
2164 C C   . LYS A 296 ? 1.4637 0.6665 0.7876 -0.1150 0.0879  -0.1273 295 LYS A C   
2165 O O   . LYS A 296 ? 1.4989 0.7044 0.8205 -0.1072 0.0954  -0.1279 295 LYS A O   
2166 C CB  . LYS A 296 ? 1.5322 0.7074 0.8449 -0.1199 0.0935  -0.1356 295 LYS A CB  
2167 C CG  . LYS A 296 ? 1.6092 0.7883 0.9429 -0.1170 0.0922  -0.1302 295 LYS A CG  
2168 C CD  . LYS A 296 ? 1.6775 0.8473 1.0199 -0.1070 0.1039  -0.1310 295 LYS A CD  
2169 C CE  . LYS A 296 ? 1.6933 0.8635 1.0340 -0.0955 0.1158  -0.1322 295 LYS A CE  
2170 N NZ  . LYS A 296 ? 1.7047 0.8724 1.0610 -0.0839 0.1265  -0.1294 295 LYS A NZ  
2171 N N   . SER A 297 ? 1.4651 0.6772 0.8052 -0.1152 0.0822  -0.1215 296 SER A N   
2172 C CA  . SER A 297 ? 1.4923 0.7190 0.8475 -0.1064 0.0841  -0.1157 296 SER A CA  
2173 C C   . SER A 297 ? 1.3694 0.6125 0.7208 -0.1084 0.0785  -0.1131 296 SER A C   
2174 O O   . SER A 297 ? 1.3131 0.5667 0.6707 -0.1000 0.0833  -0.1104 296 SER A O   
2175 C CB  . SER A 297 ? 1.4310 0.6726 0.8096 -0.1056 0.0786  -0.1079 296 SER A CB  
2176 O OG  . SER A 297 ? 1.4464 0.6970 0.8249 -0.1161 0.0662  -0.1050 296 SER A OG  
2177 N N   . LEU A 298 ? 1.3608 0.6067 0.7026 -0.1198 0.0681  -0.1132 297 LEU A N   
2178 C CA  . LEU A 298 ? 1.3828 0.6432 0.7200 -0.1224 0.0626  -0.1105 297 LEU A CA  
2179 C C   . LEU A 298 ? 1.3967 0.6465 0.7150 -0.1201 0.0701  -0.1168 297 LEU A C   
2180 O O   . LEU A 298 ? 1.3641 0.6271 0.6853 -0.1154 0.0710  -0.1134 297 LEU A O   
2181 C CB  . LEU A 298 ? 1.3336 0.5981 0.6636 -0.1358 0.0502  -0.1090 297 LEU A CB  
2182 C CG  . LEU A 298 ? 1.3888 0.6711 0.7403 -0.1369 0.0420  -0.1003 297 LEU A CG  
2183 C CD1 . LEU A 298 ? 1.4548 0.7445 0.8004 -0.1496 0.0296  -0.0972 297 LEU A CD1 
2184 C CD2 . LEU A 298 ? 1.2732 0.5769 0.6445 -0.1266 0.0433  -0.0930 297 LEU A CD2 
2185 N N   . LYS A 299 ? 1.4178 0.6432 0.7162 -0.1233 0.0758  -0.1258 298 LYS A N   
2186 C CA  . LYS A 299 ? 1.4844 0.7041 0.7685 -0.1197 0.0838  -0.1304 298 LYS A CA  
2187 C C   . LYS A 299 ? 1.3746 0.5980 0.6699 -0.1055 0.0952  -0.1285 298 LYS A C   
2188 O O   . LYS A 299 ? 1.2382 0.4599 0.5236 -0.1014 0.1019  -0.1308 298 LYS A O   
2189 C CB  . LYS A 299 ? 1.5427 0.7464 0.8137 -0.1241 0.0873  -0.1369 298 LYS A CB  
2190 C CG  . LYS A 299 ? 1.4395 0.6389 0.6951 -0.1395 0.0762  -0.1393 298 LYS A CG  
2191 C CD  . LYS A 299 ? 1.4412 0.6238 0.6876 -0.1440 0.0788  -0.1451 298 LYS A CD  
2192 C CE  . LYS A 299 ? 1.4704 0.6429 0.7158 -0.1330 0.0930  -0.1491 298 LYS A CE  
2193 N NZ  . LYS A 299 ? 1.4602 0.6154 0.6999 -0.1359 0.0961  -0.1542 298 LYS A NZ  
2194 N N   . PHE A 300 ? 1.4932 0.7218 0.8084 -0.0984 0.0974  -0.1238 299 PHE A N   
2195 C CA  . PHE A 300 ? 1.5730 0.8072 0.9004 -0.0857 0.1070  -0.1205 299 PHE A CA  
2196 C C   . PHE A 300 ? 1.5709 0.8312 0.9171 -0.0822 0.1015  -0.1114 299 PHE A C   
2197 O O   . PHE A 300 ? 1.6136 0.8822 0.9599 -0.0767 0.1053  -0.1092 299 PHE A O   
2198 C CB  . PHE A 300 ? 1.5809 0.8102 0.9235 -0.0790 0.1135  -0.1190 299 PHE A CB  
2199 C CG  . PHE A 300 ? 1.6614 0.8949 1.0155 -0.0664 0.1241  -0.1154 299 PHE A CG  
2200 C CD1 . PHE A 300 ? 1.6050 0.8593 0.9797 -0.0612 0.1217  -0.1070 299 PHE A CD1 
2201 C CD2 . PHE A 300 ? 1.6970 0.9213 1.0467 -0.0594 0.1357  -0.1181 299 PHE A CD2 
2202 C CE1 . PHE A 300 ? 1.5461 0.8069 0.9324 -0.0505 0.1306  -0.1026 299 PHE A CE1 
2203 C CE2 . PHE A 300 ? 1.7945 1.0225 1.1543 -0.0482 0.1455  -0.1141 299 PHE A CE2 
2204 C CZ  . PHE A 300 ? 1.8163 1.0619 1.1937 -0.0441 0.1428  -0.1065 299 PHE A CZ  
2205 N N   . VAL A 301 ? 1.3845 0.6575 0.7461 -0.0852 0.0928  -0.1058 300 VAL A N   
2206 C CA  . VAL A 301 ? 1.4692 0.7651 0.8501 -0.0804 0.0893  -0.0974 300 VAL A CA  
2207 C C   . VAL A 301 ? 1.3755 0.6833 0.7505 -0.0849 0.0822  -0.0952 300 VAL A C   
2208 O O   . VAL A 301 ? 1.3657 0.6878 0.7500 -0.0794 0.0826  -0.0901 300 VAL A O   
2209 C CB  . VAL A 301 ? 1.3123 0.6177 0.7120 -0.0811 0.0835  -0.0923 300 VAL A CB  
2210 C CG1 . VAL A 301 ? 1.4809 0.7750 0.8871 -0.0764 0.0909  -0.0937 300 VAL A CG1 
2211 C CG2 . VAL A 301 ? 1.2809 0.5871 0.6754 -0.0921 0.0727  -0.0925 300 VAL A CG2 
2212 N N   . LEU A 302 ? 1.3204 0.6229 0.6800 -0.0950 0.0754  -0.0984 301 LEU A N   
2213 C CA  . LEU A 302 ? 1.2257 0.5404 0.5803 -0.0994 0.0686  -0.0954 301 LEU A CA  
2214 C C   . LEU A 302 ? 1.2540 0.5673 0.5981 -0.0950 0.0751  -0.0972 301 LEU A C   
2215 O O   . LEU A 302 ? 1.3141 0.6431 0.6663 -0.0919 0.0729  -0.0914 301 LEU A O   
2216 C CB  . LEU A 302 ? 1.2211 0.5309 0.5613 -0.1120 0.0597  -0.0979 301 LEU A CB  
2217 C CG  . LEU A 302 ? 1.2732 0.5959 0.6268 -0.1173 0.0493  -0.0917 301 LEU A CG  
2218 C CD1 . LEU A 302 ? 1.0938 0.4129 0.4319 -0.1305 0.0404  -0.0933 301 LEU A CD1 
2219 C CD2 . LEU A 302 ? 1.1522 0.4970 0.5236 -0.1121 0.0456  -0.0829 301 LEU A CD2 
2220 N N   . PRO A 303 ? 1.2694 0.5651 0.5963 -0.0943 0.0834  -0.1046 302 PRO A N   
2221 C CA  . PRO A 303 ? 1.2755 0.5722 0.5952 -0.0886 0.0905  -0.1052 302 PRO A CA  
2222 C C   . PRO A 303 ? 1.2854 0.5904 0.6227 -0.0770 0.0978  -0.1002 302 PRO A C   
2223 O O   . PRO A 303 ? 1.2201 0.5335 0.5576 -0.0726 0.1007  -0.0973 302 PRO A O   
2224 C CB  . PRO A 303 ? 1.2582 0.5321 0.5549 -0.0906 0.0981  -0.1148 302 PRO A CB  
2225 C CG  . PRO A 303 ? 1.2364 0.4967 0.5348 -0.0930 0.0984  -0.1185 302 PRO A CG  
2226 C CD  . PRO A 303 ? 1.3027 0.5762 0.6146 -0.0990 0.0865  -0.1129 302 PRO A CD  
2227 N N   . ALA A 304 ? 1.2749 0.5786 0.6270 -0.0724 0.1005  -0.0988 303 ALA A N   
2228 C CA  . ALA A 304 ? 1.3289 0.6414 0.6979 -0.0621 0.1069  -0.0935 303 ALA A CA  
2229 C C   . ALA A 304 ? 1.3578 0.6913 0.7427 -0.0609 0.1001  -0.0854 303 ALA A C   
2230 O O   . ALA A 304 ? 1.3195 0.6620 0.7103 -0.0550 0.1037  -0.0813 303 ALA A O   
2231 C CB  . ALA A 304 ? 1.1748 0.4806 0.5551 -0.0582 0.1113  -0.0937 303 ALA A CB  
2232 N N   . VAL A 305 ? 1.3891 0.7303 0.7811 -0.0664 0.0904  -0.0829 304 VAL A N   
2233 C CA  . VAL A 305 ? 1.3079 0.6675 0.7142 -0.0650 0.0843  -0.0757 304 VAL A CA  
2234 C C   . VAL A 305 ? 1.3021 0.6679 0.6990 -0.0680 0.0808  -0.0743 304 VAL A C   
2235 O O   . VAL A 305 ? 1.2936 0.6719 0.6996 -0.0646 0.0793  -0.0687 304 VAL A O   
2236 C CB  . VAL A 305 ? 1.2806 0.6470 0.6978 -0.0692 0.0759  -0.0730 304 VAL A CB  
2237 C CG1 . VAL A 305 ? 1.3490 0.7105 0.7530 -0.0790 0.0687  -0.0759 304 VAL A CG1 
2238 C CG2 . VAL A 305 ? 1.3103 0.6943 0.7431 -0.0663 0.0711  -0.0657 304 VAL A CG2 
2239 N N   . ALA A 306 ? 1.3089 0.6655 0.6869 -0.0747 0.0793  -0.0793 305 ALA A N   
2240 C CA  . ALA A 306 ? 1.1357 0.4987 0.5043 -0.0780 0.0758  -0.0776 305 ALA A CA  
2241 C C   . ALA A 306 ? 1.0428 0.4061 0.4080 -0.0715 0.0839  -0.0771 305 ALA A C   
2242 O O   . ALA A 306 ? 1.0993 0.4741 0.4675 -0.0705 0.0815  -0.0721 305 ALA A O   
2243 C CB  . ALA A 306 ? 1.0494 0.4027 0.3977 -0.0877 0.0720  -0.0830 305 ALA A CB  
2244 N N   . ALA A 307 ? 1.0519 0.4029 0.4114 -0.0668 0.0937  -0.0817 306 ALA A N   
2245 C CA  . ALA A 307 ? 1.1294 0.4817 0.4869 -0.0600 0.1020  -0.0804 306 ALA A CA  
2246 C C   . ALA A 307 ? 1.2110 0.5774 0.5889 -0.0532 0.1026  -0.0727 306 ALA A C   
2247 O O   . ALA A 307 ? 1.1543 0.5299 0.5338 -0.0506 0.1034  -0.0682 306 ALA A O   
2248 C CB  . ALA A 307 ? 1.1647 0.5006 0.5124 -0.0560 0.1130  -0.0866 306 ALA A CB  
2249 N N   . ALA A 308 ? 1.1724 0.5408 0.5655 -0.0506 0.1019  -0.0709 307 ALA A N   
2250 C CA  . ALA A 308 ? 1.1716 0.5530 0.5831 -0.0452 0.1018  -0.0639 307 ALA A CA  
2251 C C   . ALA A 308 ? 1.2268 0.6213 0.6441 -0.0482 0.0929  -0.0588 307 ALA A C   
2252 O O   . ALA A 308 ? 1.1979 0.6017 0.6218 -0.0449 0.0934  -0.0536 307 ALA A O   
2253 C CB  . ALA A 308 ? 1.0179 0.3989 0.4435 -0.0427 0.1025  -0.0632 307 ALA A CB  
2254 N N   . SER A 309 ? 1.2463 0.6416 0.6614 -0.0545 0.0848  -0.0598 308 SER A N   
2255 C CA  . SER A 309 ? 1.1020 0.5093 0.5229 -0.0569 0.0767  -0.0546 308 SER A CA  
2256 C C   . SER A 309 ? 1.0675 0.4783 0.4791 -0.0577 0.0769  -0.0527 308 SER A C   
2257 O O   . SER A 309 ? 1.1974 0.6175 0.6171 -0.0549 0.0758  -0.0471 308 SER A O   
2258 C CB  . SER A 309 ? 1.0412 0.4489 0.4601 -0.0638 0.0686  -0.0555 308 SER A CB  
2259 O OG  . SER A 309 ? 1.1476 0.5544 0.5769 -0.0630 0.0677  -0.0560 308 SER A OG  
2260 N N   . PHE A 310 ? 1.0592 0.4619 0.4532 -0.0618 0.0785  -0.0573 309 PHE A N   
2261 C CA  . PHE A 310 ? 1.1326 0.5390 0.5168 -0.0630 0.0787  -0.0555 309 PHE A CA  
2262 C C   . PHE A 310 ? 1.1115 0.5216 0.5009 -0.0559 0.0856  -0.0521 309 PHE A C   
2263 O O   . PHE A 310 ? 1.1989 0.6172 0.5881 -0.0557 0.0841  -0.0474 309 PHE A O   
2264 C CB  . PHE A 310 ? 1.1321 0.5276 0.4950 -0.0682 0.0807  -0.0621 309 PHE A CB  
2265 C CG  . PHE A 310 ? 1.0827 0.4837 0.4344 -0.0720 0.0781  -0.0599 309 PHE A CG  
2266 C CD1 . PHE A 310 ? 1.0232 0.4307 0.3722 -0.0792 0.0687  -0.0573 309 PHE A CD1 
2267 C CD2 . PHE A 310 ? 1.0290 0.4298 0.3735 -0.0682 0.0850  -0.0596 309 PHE A CD2 
2268 C CE1 . PHE A 310 ? 1.0367 0.4503 0.3760 -0.0829 0.0661  -0.0546 309 PHE A CE1 
2269 C CE2 . PHE A 310 ? 1.0370 0.4437 0.3714 -0.0718 0.0826  -0.0572 309 PHE A CE2 
2270 C CZ  . PHE A 310 ? 1.1029 0.5159 0.4347 -0.0793 0.0730  -0.0547 309 PHE A CZ  
2271 N N   . THR A 311 ? 1.0954 0.5004 0.4901 -0.0502 0.0931  -0.0537 310 THR A N   
2272 C CA  . THR A 311 ? 1.0913 0.5009 0.4914 -0.0438 0.0998  -0.0497 310 THR A CA  
2273 C C   . THR A 311 ? 1.1742 0.5959 0.5915 -0.0415 0.0957  -0.0424 310 THR A C   
2274 O O   . THR A 311 ? 1.1739 0.6029 0.5940 -0.0393 0.0968  -0.0373 310 THR A O   
2275 C CB  . THR A 311 ? 1.1042 0.5053 0.5050 -0.0384 0.1093  -0.0528 310 THR A CB  
2276 O OG1 . THR A 311 ? 1.2491 0.6363 0.6334 -0.0411 0.1126  -0.0605 310 THR A OG1 
2277 C CG2 . THR A 311 ? 0.9798 0.3856 0.3829 -0.0323 0.1171  -0.0484 310 THR A CG2 
2278 N N   . VAL A 312 ? 1.0962 0.5200 0.5249 -0.0422 0.0909  -0.0419 311 VAL A N   
2279 C CA  . VAL A 312 ? 1.2028 0.6367 0.6460 -0.0405 0.0869  -0.0358 311 VAL A CA  
2280 C C   . VAL A 312 ? 1.2248 0.6651 0.6664 -0.0442 0.0795  -0.0324 311 VAL A C   
2281 O O   . VAL A 312 ? 1.2377 0.6853 0.6875 -0.0427 0.0773  -0.0269 311 VAL A O   
2282 C CB  . VAL A 312 ? 1.1569 0.5914 0.6126 -0.0396 0.0847  -0.0362 311 VAL A CB  
2283 C CG1 . VAL A 312 ? 1.1563 0.5834 0.6122 -0.0368 0.0916  -0.0399 311 VAL A CG1 
2284 C CG2 . VAL A 312 ? 1.0970 0.5319 0.5522 -0.0443 0.0770  -0.0376 311 VAL A CG2 
2285 N N   . TRP A 313 ? 1.1544 0.5919 0.5854 -0.0493 0.0755  -0.0352 312 TRP A N   
2286 C CA  . TRP A 313 ? 1.1630 0.6072 0.5916 -0.0528 0.0692  -0.0311 312 TRP A CA  
2287 C C   . TRP A 313 ? 1.1346 0.5814 0.5563 -0.0518 0.0726  -0.0284 312 TRP A C   
2288 O O   . TRP A 313 ? 1.1363 0.5906 0.5621 -0.0521 0.0689  -0.0226 312 TRP A O   
2289 C CB  . TRP A 313 ? 1.1528 0.5946 0.5715 -0.0592 0.0639  -0.0340 312 TRP A CB  
2290 C CG  . TRP A 313 ? 1.1428 0.5925 0.5590 -0.0630 0.0575  -0.0290 312 TRP A CG  
2291 C CD1 . TRP A 313 ? 1.1267 0.5838 0.5522 -0.0644 0.0503  -0.0241 312 TRP A CD1 
2292 C CD2 . TRP A 313 ? 1.2730 0.7243 0.6769 -0.0657 0.0580  -0.0279 312 TRP A CD2 
2293 N NE1 . TRP A 313 ? 1.1485 0.6118 0.5690 -0.0677 0.0462  -0.0196 312 TRP A NE1 
2294 C CE2 . TRP A 313 ? 1.2331 0.6933 0.6402 -0.0689 0.0505  -0.0218 312 TRP A CE2 
2295 C CE3 . TRP A 313 ? 1.2096 0.6559 0.6000 -0.0655 0.0643  -0.0311 312 TRP A CE3 
2296 C CZ2 . TRP A 313 ? 1.2216 0.6865 0.6193 -0.0723 0.0487  -0.0187 312 TRP A CZ2 
2297 C CZ3 . TRP A 313 ? 1.2002 0.6511 0.5805 -0.0688 0.0627  -0.0285 312 TRP A CZ3 
2298 C CH2 . TRP A 313 ? 1.1626 0.6229 0.5467 -0.0725 0.0547  -0.0222 312 TRP A CH2 
2299 N N   . LEU A 314 ? 1.1711 0.6116 0.5825 -0.0504 0.0799  -0.0322 313 LEU A N   
2300 C CA  . LEU A 314 ? 1.3025 0.7461 0.7070 -0.0491 0.0838  -0.0295 313 LEU A CA  
2301 C C   . LEU A 314 ? 1.2835 0.7343 0.7008 -0.0444 0.0858  -0.0230 313 LEU A C   
2302 O O   . LEU A 314 ? 1.3863 0.8434 0.8023 -0.0444 0.0855  -0.0179 313 LEU A O   
2303 C CB  . LEU A 314 ? 1.1065 0.5409 0.4971 -0.0478 0.0923  -0.0353 313 LEU A CB  
2304 C CG  . LEU A 314 ? 1.1573 0.5894 0.5294 -0.0525 0.0920  -0.0380 313 LEU A CG  
2305 C CD1 . LEU A 314 ? 1.1858 0.6062 0.5435 -0.0507 0.1012  -0.0450 313 LEU A CD1 
2306 C CD2 . LEU A 314 ? 1.0442 0.4867 0.4163 -0.0524 0.0907  -0.0310 313 LEU A CD2 
2307 N N   . LEU A 315 ? 1.1279 0.5782 0.5573 -0.0409 0.0874  -0.0227 314 LEU A N   
2308 C CA  . LEU A 315 ? 1.2368 0.6935 0.6782 -0.0373 0.0889  -0.0167 314 LEU A CA  
2309 C C   . LEU A 315 ? 1.2418 0.7018 0.6962 -0.0378 0.0827  -0.0144 314 LEU A C   
2310 O O   . LEU A 315 ? 1.1606 0.6229 0.6257 -0.0351 0.0842  -0.0121 314 LEU A O   
2311 C CB  . LEU A 315 ? 1.1596 0.6139 0.6036 -0.0325 0.0975  -0.0176 314 LEU A CB  
2312 C CG  . LEU A 315 ? 1.0921 0.5419 0.5234 -0.0306 0.1055  -0.0201 314 LEU A CG  
2313 C CD1 . LEU A 315 ? 1.1635 0.6124 0.6004 -0.0249 0.1142  -0.0192 314 LEU A CD1 
2314 C CD2 . LEU A 315 ? 1.2280 0.6841 0.6530 -0.0316 0.1053  -0.0155 314 LEU A CD2 
2315 N N   . ARG A 316 ? 1.2970 0.7577 0.7506 -0.0413 0.0757  -0.0147 315 ARG A N   
2316 C CA  . ARG A 316 ? 1.1688 0.6321 0.6339 -0.0413 0.0702  -0.0128 315 ARG A CA  
2317 C C   . ARG A 316 ? 1.1311 0.5994 0.6049 -0.0397 0.0693  -0.0068 315 ARG A C   
2318 O O   . ARG A 316 ? 1.0977 0.5666 0.5814 -0.0382 0.0682  -0.0058 315 ARG A O   
2319 C CB  . ARG A 316 ? 1.1564 0.6208 0.6191 -0.0450 0.0633  -0.0128 315 ARG A CB  
2320 C CG  . ARG A 316 ? 1.1897 0.6577 0.6448 -0.0478 0.0606  -0.0093 315 ARG A CG  
2321 C CD  . ARG A 316 ? 1.1541 0.6227 0.6035 -0.0523 0.0551  -0.0104 315 ARG A CD  
2322 N NE  . ARG A 316 ? 1.2676 0.7425 0.7182 -0.0542 0.0497  -0.0042 315 ARG A NE  
2323 C CZ  . ARG A 316 ? 1.2831 0.7608 0.7235 -0.0577 0.0484  -0.0025 315 ARG A CZ  
2324 N NH1 . ARG A 316 ? 1.3044 0.7784 0.7315 -0.0598 0.0523  -0.0070 315 ARG A NH1 
2325 N NH2 . ARG A 316 ? 1.3104 0.7945 0.7540 -0.0592 0.0433  0.0041  315 ARG A NH2 
2326 N N   . ASP A 317 ? 1.1794 0.6510 0.6489 -0.0404 0.0696  -0.0025 316 ASP A N   
2327 C CA  . ASP A 317 ? 1.1003 0.5759 0.5772 -0.0394 0.0690  0.0035  316 ASP A CA  
2328 C C   . ASP A 317 ? 1.0781 0.5542 0.5604 -0.0367 0.0745  0.0039  316 ASP A C   
2329 O O   . ASP A 317 ? 1.2649 0.7424 0.7562 -0.0362 0.0731  0.0066  316 ASP A O   
2330 C CB  . ASP A 317 ? 1.0333 0.5130 0.5043 -0.0410 0.0686  0.0083  316 ASP A CB  
2331 C CG  . ASP A 317 ? 1.1269 0.6080 0.5956 -0.0439 0.0622  0.0102  316 ASP A CG  
2332 O OD1 . ASP A 317 ? 1.0196 0.4988 0.4927 -0.0443 0.0580  0.0084  316 ASP A OD1 
2333 O OD2 . ASP A 317 ? 1.1814 0.6662 0.6444 -0.0456 0.0614  0.0140  316 ASP A OD2 
2334 N N   . PHE A 318 ? 1.0617 0.5365 0.5383 -0.0349 0.0810  0.0015  317 PHE A N   
2335 C CA  . PHE A 318 ? 1.0576 0.5338 0.5401 -0.0318 0.0867  0.0028  317 PHE A CA  
2336 C C   . PHE A 318 ? 1.0999 0.5734 0.5899 -0.0309 0.0863  -0.0007 317 PHE A C   
2337 O O   . PHE A 318 ? 1.0097 0.4862 0.5084 -0.0296 0.0878  0.0021  317 PHE A O   
2338 C CB  . PHE A 318 ? 0.9261 0.4012 0.4007 -0.0293 0.0945  0.0014  317 PHE A CB  
2339 C CG  . PHE A 318 ? 0.9279 0.4072 0.4091 -0.0259 0.1008  0.0056  317 PHE A CG  
2340 C CD1 . PHE A 318 ? 1.0664 0.5534 0.5522 -0.0262 0.1006  0.0133  317 PHE A CD1 
2341 C CD2 . PHE A 318 ? 1.0959 0.5720 0.5794 -0.0227 0.1066  0.0027  317 PHE A CD2 
2342 C CE1 . PHE A 318 ? 1.1111 0.6036 0.6036 -0.0235 0.1061  0.0183  317 PHE A CE1 
2343 C CE2 . PHE A 318 ? 1.0787 0.5601 0.5693 -0.0195 0.1124  0.0077  317 PHE A CE2 
2344 C CZ  . PHE A 318 ? 1.1007 0.5908 0.5959 -0.0200 0.1121  0.0157  317 PHE A CZ  
2345 N N   . ALA A 319 ? 1.0818 0.5503 0.5686 -0.0319 0.0840  -0.0063 318 ALA A N   
2346 C CA  . ALA A 319 ? 1.0468 0.5132 0.5405 -0.0311 0.0835  -0.0094 318 ALA A CA  
2347 C C   . ALA A 319 ? 1.0703 0.5400 0.5738 -0.0317 0.0786  -0.0067 318 ALA A C   
2348 O O   . ALA A 319 ? 0.9862 0.4576 0.4977 -0.0305 0.0801  -0.0060 318 ALA A O   
2349 C CB  . ALA A 319 ? 1.0279 0.4889 0.5158 -0.0328 0.0814  -0.0152 318 ALA A CB  
2350 N N   . ILE A 320 ? 1.0884 0.5588 0.5911 -0.0337 0.0731  -0.0049 319 ILE A N   
2351 C CA  . ILE A 320 ? 0.9584 0.4301 0.4690 -0.0340 0.0689  -0.0026 319 ILE A CA  
2352 C C   . ILE A 320 ? 0.8621 0.3370 0.3774 -0.0339 0.0709  0.0020  319 ILE A C   
2353 O O   . ILE A 320 ? 0.8817 0.3573 0.4038 -0.0338 0.0703  0.0025  319 ILE A O   
2354 C CB  . ILE A 320 ? 0.9644 0.4357 0.4731 -0.0356 0.0633  -0.0009 319 ILE A CB  
2355 C CG1 . ILE A 320 ? 1.0704 0.5402 0.5755 -0.0364 0.0607  -0.0045 319 ILE A CG1 
2356 C CG2 . ILE A 320 ? 0.9068 0.3777 0.4227 -0.0355 0.0599  0.0013  319 ILE A CG2 
2357 C CD1 . ILE A 320 ? 1.0825 0.5534 0.5840 -0.0382 0.0561  -0.0019 319 ILE A CD1 
2358 N N   . TRP A 321 ? 0.9383 0.4156 0.4495 -0.0342 0.0731  0.0058  320 TRP A N   
2359 C CA  . TRP A 321 ? 0.9324 0.4138 0.4480 -0.0348 0.0745  0.0113  320 TRP A CA  
2360 C C   . TRP A 321 ? 0.8455 0.3298 0.3660 -0.0330 0.0797  0.0116  320 TRP A C   
2361 O O   . TRP A 321 ? 0.9690 0.4571 0.4955 -0.0341 0.0797  0.0157  320 TRP A O   
2362 C CB  . TRP A 321 ? 0.8702 0.3547 0.3806 -0.0355 0.0758  0.0160  320 TRP A CB  
2363 C CG  . TRP A 321 ? 0.8544 0.3444 0.3692 -0.0364 0.0773  0.0227  320 TRP A CG  
2364 C CD1 . TRP A 321 ? 0.8530 0.3438 0.3712 -0.0395 0.0730  0.0275  320 TRP A CD1 
2365 C CD2 . TRP A 321 ? 0.9795 0.4750 0.4961 -0.0346 0.0836  0.0259  320 TRP A CD2 
2366 N NE1 . TRP A 321 ? 0.8895 0.3866 0.4113 -0.0403 0.0757  0.0336  320 TRP A NE1 
2367 C CE2 . TRP A 321 ? 0.9406 0.4415 0.4620 -0.0371 0.0823  0.0332  320 TRP A CE2 
2368 C CE3 . TRP A 321 ? 0.9211 0.4172 0.4356 -0.0310 0.0904  0.0236  320 TRP A CE3 
2369 C CZ2 . TRP A 321 ? 0.9830 0.4916 0.5081 -0.0361 0.0874  0.0390  320 TRP A CZ2 
2370 C CZ3 . TRP A 321 ? 0.8567 0.3595 0.3750 -0.0292 0.0961  0.0291  320 TRP A CZ3 
2371 C CH2 . TRP A 321 ? 0.9559 0.4658 0.4799 -0.0317 0.0944  0.0371  320 TRP A CH2 
2372 N N   . LEU A 322 ? 0.9363 0.4188 0.4543 -0.0306 0.0840  0.0075  321 LEU A N   
2373 C CA  . LEU A 322 ? 0.9243 0.4095 0.4474 -0.0283 0.0896  0.0084  321 LEU A CA  
2374 C C   . LEU A 322 ? 0.9136 0.3982 0.4438 -0.0284 0.0879  0.0057  321 LEU A C   
2375 O O   . LEU A 322 ? 0.9660 0.4552 0.5036 -0.0292 0.0878  0.0092  321 LEU A O   
2376 C CB  . LEU A 322 ? 0.9401 0.4223 0.4568 -0.0253 0.0959  0.0054  321 LEU A CB  
2377 C CG  . LEU A 322 ? 1.0126 0.4965 0.5350 -0.0221 0.1024  0.0060  321 LEU A CG  
2378 C CD1 . LEU A 322 ? 0.9279 0.4198 0.4548 -0.0209 0.1067  0.0138  321 LEU A CD1 
2379 C CD2 . LEU A 322 ? 0.9824 0.4591 0.4975 -0.0195 0.1074  0.0005  321 LEU A CD2 
2380 N N   . LEU A 323 ? 0.8713 0.3508 0.3993 -0.0281 0.0863  -0.0002 322 LEU A N   
2381 C CA  . LEU A 323 ? 0.8894 0.3689 0.4240 -0.0278 0.0852  -0.0026 322 LEU A CA  
2382 C C   . LEU A 323 ? 0.9533 0.4336 0.4919 -0.0299 0.0794  -0.0022 322 LEU A C   
2383 O O   . LEU A 323 ? 0.9458 0.4286 0.4911 -0.0300 0.0790  -0.0021 322 LEU A O   
2384 C CB  . LEU A 323 ? 0.8673 0.3415 0.3982 -0.0271 0.0854  -0.0085 322 LEU A CB  
2385 C CG  . LEU A 323 ? 0.9990 0.4697 0.5241 -0.0250 0.0916  -0.0100 322 LEU A CG  
2386 C CD1 . LEU A 323 ? 0.8880 0.3521 0.4080 -0.0256 0.0908  -0.0161 322 LEU A CD1 
2387 C CD2 . LEU A 323 ? 0.9055 0.3798 0.4374 -0.0224 0.0977  -0.0068 322 LEU A CD2 
2388 N N   . LEU A 324 ? 0.8277 0.3059 0.3624 -0.0313 0.0752  -0.0017 323 LEU A N   
2389 C CA  . LEU A 324 ? 0.9293 0.4067 0.4671 -0.0327 0.0704  -0.0014 323 LEU A CA  
2390 C C   . LEU A 324 ? 0.8705 0.3484 0.4071 -0.0348 0.0688  0.0035  323 LEU A C   
2391 O O   . LEU A 324 ? 0.9178 0.3995 0.4547 -0.0353 0.0718  0.0074  323 LEU A O   
2392 C CB  . LEU A 324 ? 0.8820 0.3558 0.4175 -0.0323 0.0665  -0.0047 323 LEU A CB  
2393 C CG  . LEU A 324 ? 0.8322 0.3058 0.3695 -0.0311 0.0669  -0.0090 323 LEU A CG  
2394 C CD1 . LEU A 324 ? 0.9556 0.4276 0.4934 -0.0309 0.0624  -0.0107 323 LEU A CD1 
2395 C CD2 . LEU A 324 ? 0.8490 0.3255 0.3931 -0.0305 0.0693  -0.0093 323 LEU A CD2 
2396 N N   . SER A 325 ? 0.8411 0.3154 0.3769 -0.0358 0.0643  0.0036  324 SER A N   
2397 C CA  . SER A 325 ? 0.9896 0.4630 0.5242 -0.0382 0.0623  0.0082  324 SER A CA  
2398 C C   . SER A 325 ? 0.8988 0.3697 0.4288 -0.0381 0.0597  0.0092  324 SER A C   
2399 O O   . SER A 325 ? 0.8715 0.3411 0.3994 -0.0366 0.0586  0.0063  324 SER A O   
2400 C CB  . SER A 325 ? 1.0612 0.5312 0.5989 -0.0399 0.0593  0.0081  324 SER A CB  
2401 O OG  . SER A 325 ? 0.8349 0.2990 0.3712 -0.0391 0.0557  0.0067  324 SER A OG  
2402 N N   . ASN A 326 ? 0.9589 0.4298 0.4873 -0.0403 0.0584  0.0141  325 ASN A N   
2403 C CA  . ASN A 326 ? 0.9452 0.4142 0.4699 -0.0407 0.0555  0.0163  325 ASN A CA  
2404 C C   . ASN A 326 ? 1.0016 0.4649 0.5280 -0.0398 0.0514  0.0147  325 ASN A C   
2405 O O   . ASN A 326 ? 0.9897 0.4522 0.5139 -0.0393 0.0492  0.0157  325 ASN A O   
2406 C CB  . ASN A 326 ? 1.0395 0.5101 0.5631 -0.0434 0.0548  0.0226  325 ASN A CB  
2407 C CG  . ASN A 326 ? 1.1403 0.6163 0.6593 -0.0432 0.0574  0.0252  325 ASN A CG  
2408 O OD1 . ASN A 326 ? 0.9753 0.4517 0.4902 -0.0417 0.0578  0.0226  325 ASN A OD1 
2409 N ND2 . ASN A 326 ? 1.0521 0.5327 0.5713 -0.0449 0.0591  0.0306  325 ASN A ND2 
2410 N N   . LYS A 327 ? 0.9959 0.4553 0.5259 -0.0397 0.0507  0.0125  326 LYS A N   
2411 C CA  . LYS A 327 ? 0.9159 0.3698 0.4476 -0.0378 0.0480  0.0106  326 LYS A CA  
2412 C C   . LYS A 327 ? 0.9848 0.4412 0.5172 -0.0349 0.0481  0.0073  326 LYS A C   
2413 O O   . LYS A 327 ? 0.9383 0.3918 0.4727 -0.0328 0.0460  0.0066  326 LYS A O   
2414 C CB  . LYS A 327 ? 0.8930 0.3424 0.4274 -0.0382 0.0481  0.0083  326 LYS A CB  
2415 C CG  . LYS A 327 ? 0.9093 0.3547 0.4424 -0.0420 0.0469  0.0117  326 LYS A CG  
2416 C CD  . LYS A 327 ? 1.2073 0.6436 0.7394 -0.0419 0.0439  0.0133  326 LYS A CD  
2417 C CE  . LYS A 327 ? 0.9304 0.3676 0.4607 -0.0434 0.0422  0.0189  326 LYS A CE  
2418 N NZ  . LYS A 327 ? 1.0186 0.4487 0.5493 -0.0414 0.0395  0.0204  326 LYS A NZ  
2419 N N   . PHE A 328 ? 1.0567 0.5181 0.5874 -0.0349 0.0505  0.0054  327 PHE A N   
2420 C CA  . PHE A 328 ? 1.0240 0.4876 0.5541 -0.0334 0.0502  0.0026  327 PHE A CA  
2421 C C   . PHE A 328 ? 1.0323 0.4982 0.5569 -0.0345 0.0492  0.0046  327 PHE A C   
2422 O O   . PHE A 328 ? 1.0394 0.5075 0.5608 -0.0347 0.0500  0.0021  327 PHE A O   
2423 C CB  . PHE A 328 ? 0.9755 0.4417 0.5066 -0.0329 0.0535  -0.0012 327 PHE A CB  
2424 C CG  . PHE A 328 ? 0.9772 0.4427 0.5139 -0.0318 0.0539  -0.0035 327 PHE A CG  
2425 C CD1 . PHE A 328 ? 0.9796 0.4442 0.5183 -0.0329 0.0550  -0.0023 327 PHE A CD1 
2426 C CD2 . PHE A 328 ? 0.9548 0.4214 0.4945 -0.0301 0.0532  -0.0064 327 PHE A CD2 
2427 C CE1 . PHE A 328 ? 0.9722 0.4366 0.5150 -0.0324 0.0554  -0.0045 327 PHE A CE1 
2428 C CE2 . PHE A 328 ? 0.9471 0.4139 0.4916 -0.0290 0.0538  -0.0084 327 PHE A CE2 
2429 C CZ  . PHE A 328 ? 0.9729 0.4385 0.5186 -0.0301 0.0550  -0.0077 327 PHE A CZ  
2430 N N   . THR A 329 ? 1.1419 0.6070 0.6645 -0.0357 0.0475  0.0091  328 THR A N   
2431 C CA  . THR A 329 ? 1.0526 0.5210 0.5694 -0.0372 0.0468  0.0113  328 THR A CA  
2432 C C   . THR A 329 ? 0.9812 0.4511 0.4972 -0.0370 0.0436  0.0110  328 THR A C   
2433 O O   . THR A 329 ? 1.0378 0.5108 0.5475 -0.0388 0.0434  0.0111  328 THR A O   
2434 C CB  . THR A 329 ? 1.0240 0.4920 0.5397 -0.0387 0.0454  0.0170  328 THR A CB  
2435 O OG1 . THR A 329 ? 1.2005 0.6724 0.7108 -0.0402 0.0440  0.0196  328 THR A OG1 
2436 C CG2 . THR A 329 ? 0.9667 0.4299 0.4878 -0.0378 0.0422  0.0194  328 THR A CG2 
2437 N N   . ALA A 330 ? 1.0501 0.5184 0.5720 -0.0350 0.0413  0.0109  329 ALA A N   
2438 C CA  . ALA A 330 ? 0.9968 0.4680 0.5196 -0.0347 0.0380  0.0121  329 ALA A CA  
2439 C C   . ALA A 330 ? 1.0554 0.5295 0.5760 -0.0356 0.0385  0.0078  329 ALA A C   
2440 O O   . ALA A 330 ? 1.0624 0.5399 0.5844 -0.0357 0.0354  0.0091  329 ALA A O   
2441 C CB  . ALA A 330 ? 0.9990 0.4678 0.5295 -0.0314 0.0363  0.0138  329 ALA A CB  
2442 N N   . MET A 331 ? 1.1525 0.6256 0.6700 -0.0362 0.0421  0.0033  330 MET A N   
2443 C CA  . MET A 331 ? 1.1803 0.6548 0.6950 -0.0376 0.0423  -0.0006 330 MET A CA  
2444 C C   . MET A 331 ? 1.0969 0.5725 0.6015 -0.0411 0.0421  -0.0009 330 MET A C   
2445 O O   . MET A 331 ? 1.1065 0.5824 0.6073 -0.0432 0.0415  -0.0040 330 MET A O   
2446 C CB  . MET A 331 ? 1.1758 0.6480 0.6919 -0.0365 0.0466  -0.0051 330 MET A CB  
2447 C CG  . MET A 331 ? 1.0987 0.5693 0.6216 -0.0340 0.0484  -0.0048 330 MET A CG  
2448 S SD  . MET A 331 ? 1.2131 0.6835 0.7402 -0.0328 0.0518  -0.0092 330 MET A SD  
2449 C CE  . MET A 331 ? 1.0244 0.4937 0.5469 -0.0335 0.0570  -0.0094 330 MET A CE  
2450 N N   . ARG A 332 ? 1.1146 0.5908 0.6145 -0.0422 0.0425  0.0021  331 ARG A N   
2451 C CA  . ARG A 332 ? 1.1416 0.6183 0.6304 -0.0454 0.0435  0.0010  331 ARG A CA  
2452 C C   . ARG A 332 ? 1.1196 0.5989 0.6037 -0.0489 0.0393  0.0008  331 ARG A C   
2453 O O   . ARG A 332 ? 1.1657 0.6432 0.6402 -0.0519 0.0406  -0.0030 331 ARG A O   
2454 C CB  . ARG A 332 ? 1.2667 0.7451 0.7524 -0.0459 0.0438  0.0057  331 ARG A CB  
2455 C CG  . ARG A 332 ? 1.2181 0.7010 0.7038 -0.0478 0.0386  0.0114  331 ARG A CG  
2456 C CD  . ARG A 332 ? 1.3354 0.8201 0.8201 -0.0480 0.0388  0.0167  331 ARG A CD  
2457 N NE  . ARG A 332 ? 1.3406 0.8279 0.8140 -0.0511 0.0401  0.0167  331 ARG A NE  
2458 C CZ  . ARG A 332 ? 1.2433 0.7300 0.7117 -0.0506 0.0449  0.0160  331 ARG A CZ  
2459 N NH1 . ARG A 332 ? 1.2616 0.7458 0.7356 -0.0478 0.0483  0.0157  331 ARG A NH1 
2460 N NH2 . ARG A 332 ? 1.2858 0.7747 0.7429 -0.0533 0.0463  0.0158  331 ARG A NH2 
2461 N N   . ASP A 333 ? 1.1763 0.6597 0.6669 -0.0487 0.0344  0.0052  332 ASP A N   
2462 C CA  . ASP A 333 ? 1.1251 0.6131 0.6122 -0.0526 0.0298  0.0068  332 ASP A CA  
2463 C C   . ASP A 333 ? 1.0932 0.5809 0.5830 -0.0532 0.0287  0.0033  332 ASP A C   
2464 O O   . ASP A 333 ? 1.1449 0.6355 0.6296 -0.0577 0.0252  0.0034  332 ASP A O   
2465 C CB  . ASP A 333 ? 1.1209 0.6147 0.6143 -0.0520 0.0251  0.0145  332 ASP A CB  
2466 C CG  . ASP A 333 ? 1.0801 0.5764 0.5676 -0.0541 0.0243  0.0189  332 ASP A CG  
2467 O OD1 . ASP A 333 ? 1.1255 0.6190 0.6043 -0.0555 0.0278  0.0158  332 ASP A OD1 
2468 O OD2 . ASP A 333 ? 1.0218 0.5233 0.5137 -0.0542 0.0204  0.0258  332 ASP A OD2 
2469 N N   . LEU A 334 ? 1.2210 0.7058 0.7187 -0.0492 0.0313  0.0007  333 LEU A N   
2470 C CA  . LEU A 334 ? 1.1155 0.6001 0.6159 -0.0497 0.0308  -0.0027 333 LEU A CA  
2471 C C   . LEU A 334 ? 1.0951 0.5740 0.5868 -0.0522 0.0343  -0.0091 333 LEU A C   
2472 O O   . LEU A 334 ? 1.0657 0.5439 0.5578 -0.0540 0.0334  -0.0119 333 LEU A O   
2473 C CB  . LEU A 334 ? 1.0738 0.5581 0.5858 -0.0446 0.0325  -0.0029 333 LEU A CB  
2474 C CG  . LEU A 334 ? 1.1377 0.6258 0.6592 -0.0410 0.0300  0.0026  333 LEU A CG  
2475 C CD1 . LEU A 334 ? 1.1592 0.6443 0.6813 -0.0386 0.0317  0.0048  333 LEU A CD1 
2476 C CD2 . LEU A 334 ? 1.1417 0.6306 0.6725 -0.0374 0.0307  0.0014  333 LEU A CD2 
2477 N N   . PHE A 335 ? 1.1022 0.5768 0.5863 -0.0523 0.0385  -0.0112 334 PHE A N   
2478 C CA  . PHE A 335 ? 1.1010 0.5689 0.5770 -0.0535 0.0430  -0.0172 334 PHE A CA  
2479 C C   . PHE A 335 ? 1.1848 0.6509 0.6508 -0.0593 0.0403  -0.0200 334 PHE A C   
2480 O O   . PHE A 335 ? 1.2109 0.6725 0.6755 -0.0606 0.0413  -0.0243 334 PHE A O   
2481 C CB  . PHE A 335 ? 1.1085 0.5735 0.5780 -0.0522 0.0481  -0.0177 334 PHE A CB  
2482 C CG  . PHE A 335 ? 1.2049 0.6685 0.6820 -0.0473 0.0530  -0.0179 334 PHE A CG  
2483 C CD1 . PHE A 335 ? 1.1540 0.6213 0.6422 -0.0444 0.0514  -0.0141 334 PHE A CD1 
2484 C CD2 . PHE A 335 ? 1.2863 0.7449 0.7592 -0.0459 0.0594  -0.0215 334 PHE A CD2 
2485 C CE1 . PHE A 335 ? 1.1742 0.6406 0.6684 -0.0410 0.0554  -0.0140 334 PHE A CE1 
2486 C CE2 . PHE A 335 ? 1.2615 0.7204 0.7420 -0.0419 0.0636  -0.0205 334 PHE A CE2 
2487 C CZ  . PHE A 335 ? 1.2400 0.7032 0.7309 -0.0399 0.0613  -0.0168 334 PHE A CZ  
2488 N N   . ALA A 336 ? 1.2135 0.6831 0.6720 -0.0634 0.0364  -0.0172 335 ALA A N   
2489 C CA  . ALA A 336 ? 0.9762 0.4437 0.4226 -0.0702 0.0336  -0.0198 335 ALA A CA  
2490 C C   . ALA A 336 ? 1.0089 0.4787 0.4610 -0.0727 0.0290  -0.0196 335 ALA A C   
2491 O O   . ALA A 336 ? 1.0793 0.5431 0.5240 -0.0768 0.0292  -0.0246 335 ALA A O   
2492 C CB  . ALA A 336 ? 0.9308 0.4043 0.3702 -0.0744 0.0294  -0.0152 335 ALA A CB  
2493 N N   . TRP A 337 ? 1.0491 0.5273 0.5142 -0.0703 0.0251  -0.0138 336 TRP A N   
2494 C CA  . TRP A 337 ? 1.1066 0.5892 0.5777 -0.0726 0.0204  -0.0122 336 TRP A CA  
2495 C C   . TRP A 337 ? 1.1922 0.6693 0.6680 -0.0704 0.0238  -0.0172 336 TRP A C   
2496 O O   . TRP A 337 ? 1.1193 0.5958 0.5937 -0.0746 0.0211  -0.0187 336 TRP A O   
2497 C CB  . TRP A 337 ? 1.0337 0.5268 0.5180 -0.0694 0.0164  -0.0044 336 TRP A CB  
2498 C CG  . TRP A 337 ? 1.0868 0.5861 0.5684 -0.0713 0.0129  0.0017  336 TRP A CG  
2499 C CD1 . TRP A 337 ? 1.0509 0.5493 0.5308 -0.0687 0.0152  0.0033  336 TRP A CD1 
2500 C CD2 . TRP A 337 ? 1.0728 0.5812 0.5535 -0.0766 0.0062  0.0078  336 TRP A CD2 
2501 N NE1 . TRP A 337 ? 1.1247 0.6306 0.6030 -0.0717 0.0105  0.0099  336 TRP A NE1 
2502 C CE2 . TRP A 337 ? 1.0498 0.5623 0.5286 -0.0766 0.0049  0.0129  336 TRP A CE2 
2503 C CE3 . TRP A 337 ? 1.1424 0.6565 0.6241 -0.0817 0.0009  0.0101  336 TRP A CE3 
2504 C CZ2 . TRP A 337 ? 1.0419 0.5644 0.5201 -0.0813 -0.0013 0.0204  336 TRP A CZ2 
2505 C CZ3 . TRP A 337 ? 1.0276 0.5519 0.5086 -0.0866 -0.0055 0.0177  336 TRP A CZ3 
2506 C CH2 . TRP A 337 ? 1.1347 0.6632 0.6140 -0.0863 -0.0064 0.0228  336 TRP A CH2 
2507 N N   . GLN A 338 ? 1.1366 0.6102 0.6180 -0.0643 0.0294  -0.0192 337 GLN A N   
2508 C CA  . GLN A 338 ? 1.1033 0.5730 0.5904 -0.0619 0.0326  -0.0229 337 GLN A CA  
2509 C C   . GLN A 338 ? 1.1732 0.6328 0.6492 -0.0651 0.0361  -0.0294 337 GLN A C   
2510 O O   . GLN A 338 ? 1.1414 0.5980 0.6188 -0.0669 0.0359  -0.0320 337 GLN A O   
2511 C CB  . GLN A 338 ? 1.1767 0.6466 0.6730 -0.0551 0.0372  -0.0224 337 GLN A CB  
2512 C CG  . GLN A 338 ? 1.2098 0.6787 0.7146 -0.0523 0.0398  -0.0246 337 GLN A CG  
2513 C CD  . GLN A 338 ? 1.1196 0.5966 0.6365 -0.0501 0.0363  -0.0207 337 GLN A CD  
2514 O OE1 . GLN A 338 ? 1.1833 0.6664 0.7022 -0.0510 0.0317  -0.0163 337 GLN A OE1 
2515 N NE2 . GLN A 338 ? 1.2078 0.6854 0.7330 -0.0470 0.0387  -0.0218 337 GLN A NE2 
2516 N N   . LEU A 339 ? 1.1332 0.5870 0.5979 -0.0658 0.0396  -0.0320 338 LEU A N   
2517 C CA  . LEU A 339 ? 1.1535 0.5960 0.6071 -0.0676 0.0445  -0.0385 338 LEU A CA  
2518 C C   . LEU A 339 ? 1.1233 0.5615 0.5667 -0.0753 0.0403  -0.0413 338 LEU A C   
2519 O O   . LEU A 339 ? 1.1833 0.6118 0.6215 -0.0769 0.0432  -0.0466 338 LEU A O   
2520 C CB  . LEU A 339 ? 1.0690 0.5075 0.5128 -0.0662 0.0495  -0.0399 338 LEU A CB  
2521 C CG  . LEU A 339 ? 1.0196 0.4617 0.4726 -0.0593 0.0539  -0.0370 338 LEU A CG  
2522 C CD1 . LEU A 339 ? 0.9957 0.4335 0.4386 -0.0581 0.0595  -0.0386 338 LEU A CD1 
2523 C CD2 . LEU A 339 ? 1.1345 0.5752 0.5986 -0.0549 0.0576  -0.0382 338 LEU A CD2 
2524 N N   . VAL A 340 ? 0.9989 0.4440 0.4394 -0.0805 0.0333  -0.0375 339 VAL A N   
2525 C CA  . VAL A 340 ? 1.0981 0.5406 0.5294 -0.0889 0.0282  -0.0392 339 VAL A CA  
2526 C C   . VAL A 340 ? 1.2073 0.6513 0.6490 -0.0894 0.0257  -0.0386 339 VAL A C   
2527 O O   . VAL A 340 ? 1.2587 0.6944 0.6932 -0.0945 0.0252  -0.0430 339 VAL A O   
2528 C CB  . VAL A 340 ? 1.0969 0.5490 0.5245 -0.0944 0.0209  -0.0335 339 VAL A CB  
2529 C CG1 . VAL A 340 ? 1.0931 0.5475 0.5177 -0.1028 0.0137  -0.0323 339 VAL A CG1 
2530 C CG2 . VAL A 340 ? 1.0045 0.4522 0.4163 -0.0970 0.0230  -0.0358 339 VAL A CG2 
2531 N N   . GLY A 341 ? 1.1051 0.5593 0.5634 -0.0841 0.0244  -0.0334 340 GLY A N   
2532 C CA  . GLY A 341 ? 1.1521 0.6088 0.6210 -0.0836 0.0227  -0.0325 340 GLY A CA  
2533 C C   . GLY A 341 ? 1.1183 0.5649 0.5879 -0.0806 0.0292  -0.0382 340 GLY A C   
2534 O O   . GLY A 341 ? 1.1356 0.5798 0.6079 -0.0831 0.0279  -0.0395 340 GLY A O   
2535 N N   . ASP A 342 ? 1.0418 0.4830 0.5097 -0.0753 0.0361  -0.0409 341 ASP A N   
2536 C CA  . ASP A 342 ? 1.0767 0.5088 0.5455 -0.0720 0.0428  -0.0455 341 ASP A CA  
2537 C C   . ASP A 342 ? 1.2108 0.6295 0.6655 -0.0778 0.0440  -0.0515 341 ASP A C   
2538 O O   . ASP A 342 ? 1.1429 0.5555 0.6002 -0.0782 0.0457  -0.0540 341 ASP A O   
2539 C CB  . ASP A 342 ? 1.0882 0.5185 0.5572 -0.0657 0.0497  -0.0461 341 ASP A CB  
2540 C CG  . ASP A 342 ? 1.2841 0.7247 0.7676 -0.0598 0.0497  -0.0412 341 ASP A CG  
2541 O OD1 . ASP A 342 ? 1.2917 0.7409 0.7846 -0.0601 0.0447  -0.0375 341 ASP A OD1 
2542 O OD2 . ASP A 342 ? 1.3184 0.7584 0.8034 -0.0552 0.0548  -0.0410 341 ASP A OD2 
2543 N N   . VAL A 343 ? 1.2532 0.6666 0.6923 -0.0823 0.0434  -0.0541 342 VAL A N   
2544 C CA  . VAL A 343 ? 1.1976 0.5967 0.6205 -0.0886 0.0444  -0.0605 342 VAL A CA  
2545 C C   . VAL A 343 ? 1.1419 0.5413 0.5666 -0.0955 0.0376  -0.0599 342 VAL A C   
2546 O O   . VAL A 343 ? 1.2104 0.5980 0.6306 -0.0979 0.0397  -0.0645 342 VAL A O   
2547 C CB  . VAL A 343 ? 1.0958 0.4918 0.5015 -0.0932 0.0435  -0.0624 342 VAL A CB  
2548 C CG1 . VAL A 343 ? 1.0408 0.4250 0.4294 -0.1028 0.0406  -0.0678 342 VAL A CG1 
2549 C CG2 . VAL A 343 ? 1.1275 0.5179 0.5278 -0.0870 0.0522  -0.0651 342 VAL A CG2 
2550 N N   . LEU A 344 ? 1.1087 0.5218 0.5406 -0.0985 0.0296  -0.0535 343 LEU A N   
2551 C CA  . LEU A 344 ? 1.1394 0.5550 0.5732 -0.1057 0.0224  -0.0516 343 LEU A CA  
2552 C C   . LEU A 344 ? 1.2370 0.6556 0.6867 -0.1015 0.0235  -0.0499 343 LEU A C   
2553 O O   . LEU A 344 ? 1.2463 0.6608 0.6955 -0.1069 0.0205  -0.0508 343 LEU A O   
2554 C CB  . LEU A 344 ? 1.1950 0.6259 0.6325 -0.1096 0.0140  -0.0441 343 LEU A CB  
2555 C CG  . LEU A 344 ? 1.2898 0.7201 0.7112 -0.1177 0.0094  -0.0442 343 LEU A CG  
2556 C CD1 . LEU A 344 ? 1.1910 0.6089 0.5964 -0.1168 0.0159  -0.0509 343 LEU A CD1 
2557 C CD2 . LEU A 344 ? 1.2435 0.6911 0.6740 -0.1165 0.0041  -0.0354 343 LEU A CD2 
2558 N N   . LYS A 345 ? 1.1866 0.6124 0.6501 -0.0925 0.0277  -0.0473 344 LYS A N   
2559 C CA  . LYS A 345 ? 1.2533 0.6820 0.7313 -0.0883 0.0294  -0.0458 344 LYS A CA  
2560 C C   . LYS A 345 ? 1.1875 0.6010 0.6604 -0.0879 0.0356  -0.0520 344 LYS A C   
2561 O O   . LYS A 345 ? 1.2020 0.6132 0.6798 -0.0902 0.0344  -0.0520 344 LYS A O   
2562 C CB  . LYS A 345 ? 1.1661 0.6051 0.6577 -0.0794 0.0326  -0.0421 344 LYS A CB  
2563 C CG  . LYS A 345 ? 1.2274 0.6720 0.7343 -0.0752 0.0338  -0.0398 344 LYS A CG  
2564 C CD  . LYS A 345 ? 1.1240 0.5780 0.6422 -0.0674 0.0365  -0.0365 344 LYS A CD  
2565 C CE  . LYS A 345 ? 1.2210 0.6679 0.7365 -0.0624 0.0442  -0.0398 344 LYS A CE  
2566 N NZ  . LYS A 345 ? 1.1047 0.5601 0.6311 -0.0558 0.0464  -0.0365 344 LYS A NZ  
2567 N N   . VAL A 346 ? 1.1542 0.5576 0.6179 -0.0847 0.0426  -0.0566 345 VAL A N   
2568 C CA  . VAL A 346 ? 1.2344 0.6224 0.6928 -0.0836 0.0496  -0.0623 345 VAL A CA  
2569 C C   . VAL A 346 ? 1.2390 0.6138 0.6831 -0.0926 0.0466  -0.0670 345 VAL A C   
2570 O O   . VAL A 346 ? 1.1888 0.5525 0.6325 -0.0935 0.0494  -0.0701 345 VAL A O   
2571 C CB  . VAL A 346 ? 1.2602 0.6419 0.7122 -0.0777 0.0580  -0.0653 345 VAL A CB  
2572 C CG1 . VAL A 346 ? 1.2585 0.6210 0.6970 -0.0788 0.0645  -0.0723 345 VAL A CG1 
2573 C CG2 . VAL A 346 ? 1.0668 0.4574 0.5346 -0.0689 0.0627  -0.0613 345 VAL A CG2 
2574 N N   . GLY A 347 ? 1.2352 0.6104 0.6670 -0.0999 0.0407  -0.0674 346 GLY A N   
2575 C CA  . GLY A 347 ? 1.2565 0.6201 0.6743 -0.1100 0.0364  -0.0714 346 GLY A CA  
2576 C C   . GLY A 347 ? 1.2327 0.6021 0.6612 -0.1146 0.0298  -0.0674 346 GLY A C   
2577 O O   . GLY A 347 ? 1.2749 0.6315 0.6980 -0.1195 0.0298  -0.0711 346 GLY A O   
2578 N N   . ALA A 348 ? 1.2377 0.6263 0.6815 -0.1128 0.0243  -0.0596 347 ALA A N   
2579 C CA  . ALA A 348 ? 1.2290 0.6256 0.6853 -0.1157 0.0187  -0.0547 347 ALA A CA  
2580 C C   . ALA A 348 ? 1.2600 0.6545 0.7293 -0.1089 0.0245  -0.0550 347 ALA A C   
2581 O O   . ALA A 348 ? 1.2604 0.6600 0.7397 -0.1113 0.0207  -0.0514 347 ALA A O   
2582 C CB  . ALA A 348 ? 1.1675 0.5855 0.6365 -0.1146 0.0122  -0.0461 347 ALA A CB  
2583 N N   . TYR A 349 ? 1.2294 0.6176 0.6992 -0.1009 0.0334  -0.0583 348 TYR A N   
2584 C CA  . TYR A 349 ? 1.2206 0.6066 0.7022 -0.0950 0.0391  -0.0582 348 TYR A CA  
2585 C C   . TYR A 349 ? 1.3331 0.7026 0.8080 -0.1003 0.0400  -0.0625 348 TYR A C   
2586 O O   . TYR A 349 ? 1.3720 0.7435 0.8587 -0.0995 0.0399  -0.0599 348 TYR A O   
2587 C CB  . TYR A 349 ? 1.1480 0.5309 0.6305 -0.0859 0.0483  -0.0603 348 TYR A CB  
2588 C CG  . TYR A 349 ? 1.1034 0.5031 0.5999 -0.0787 0.0488  -0.0548 348 TYR A CG  
2589 C CD1 . TYR A 349 ? 1.2516 0.6674 0.7595 -0.0794 0.0423  -0.0489 348 TYR A CD1 
2590 C CD2 . TYR A 349 ? 1.1240 0.5232 0.6219 -0.0714 0.0561  -0.0556 348 TYR A CD2 
2591 C CE1 . TYR A 349 ? 1.1931 0.6222 0.7123 -0.0728 0.0432  -0.0447 348 TYR A CE1 
2592 C CE2 . TYR A 349 ? 1.1959 0.6090 0.7053 -0.0656 0.0563  -0.0509 348 TYR A CE2 
2593 C CZ  . TYR A 349 ? 1.1497 0.5768 0.6691 -0.0664 0.0500  -0.0460 348 TYR A CZ  
2594 O OH  . TYR A 349 ? 1.1008 0.5398 0.6302 -0.0608 0.0505  -0.0421 348 TYR A OH  
2595 N N   . VAL A 350 ? 1.2894 0.6421 0.7449 -0.1062 0.0408  -0.0690 349 VAL A N   
2596 C CA  . VAL A 350 ? 1.3545 0.6884 0.8017 -0.1114 0.0422  -0.0739 349 VAL A CA  
2597 C C   . VAL A 350 ? 1.3182 0.6572 0.7696 -0.1205 0.0326  -0.0701 349 VAL A C   
2598 O O   . VAL A 350 ? 1.2996 0.6293 0.7536 -0.1231 0.0329  -0.0709 349 VAL A O   
2599 C CB  . VAL A 350 ? 1.4177 0.7314 0.8411 -0.1158 0.0456  -0.0825 349 VAL A CB  
2600 C CG1 . VAL A 350 ? 1.3588 0.6712 0.7785 -0.1069 0.0543  -0.0850 349 VAL A CG1 
2601 C CG2 . VAL A 350 ? 1.3777 0.6929 0.7875 -0.1270 0.0362  -0.0828 349 VAL A CG2 
2602 N N   . PHE A 351 ? 1.2615 0.6155 0.7140 -0.1254 0.0239  -0.0652 350 PHE A N   
2603 C CA  . PHE A 351 ? 1.3182 0.6802 0.7768 -0.1336 0.0145  -0.0599 350 PHE A CA  
2604 C C   . PHE A 351 ? 1.4316 0.8091 0.9128 -0.1275 0.0144  -0.0528 350 PHE A C   
2605 O O   . PHE A 351 ? 1.4819 0.8609 0.9698 -0.1325 0.0099  -0.0496 350 PHE A O   
2606 C CB  . PHE A 351 ? 1.2090 0.5838 0.6629 -0.1403 0.0056  -0.0556 350 PHE A CB  
2607 C CG  . PHE A 351 ? 1.3834 0.7440 0.8141 -0.1485 0.0042  -0.0619 350 PHE A CG  
2608 C CD1 . PHE A 351 ? 1.3794 0.7233 0.7954 -0.1594 0.0009  -0.0664 350 PHE A CD1 
2609 C CD2 . PHE A 351 ? 1.4798 0.8436 0.9027 -0.1457 0.0060  -0.0631 350 PHE A CD2 
2610 C CE1 . PHE A 351 ? 1.5008 0.8312 0.8938 -0.1675 -0.0004 -0.0726 350 PHE A CE1 
2611 C CE2 . PHE A 351 ? 1.4146 0.7663 0.8156 -0.1535 0.0047  -0.0688 350 PHE A CE2 
2612 C CZ  . PHE A 351 ? 1.4058 0.7407 0.7914 -0.1645 0.0016  -0.0737 350 PHE A CZ  
2613 N N   . GLY A 352 ? 1.3207 0.7100 0.8137 -0.1171 0.0191  -0.0503 351 GLY A N   
2614 C CA  . GLY A 352 ? 1.3067 0.7101 0.8199 -0.1112 0.0198  -0.0442 351 GLY A CA  
2615 C C   . GLY A 352 ? 1.3460 0.7382 0.8639 -0.1081 0.0261  -0.0466 351 GLY A C   
2616 O O   . GLY A 352 ? 1.3780 0.7770 0.9088 -0.1085 0.0241  -0.0421 351 GLY A O   
2617 N N   . TYR A 353 ? 1.2735 0.6491 0.7816 -0.1047 0.0341  -0.0532 352 TYR A N   
2618 C CA  . TYR A 353 ? 1.3665 0.7303 0.8787 -0.1015 0.0408  -0.0552 352 TYR A CA  
2619 C C   . TYR A 353 ? 1.4602 0.8104 0.9667 -0.1105 0.0371  -0.0570 352 TYR A C   
2620 O O   . TYR A 353 ? 1.5458 0.8908 1.0608 -0.1088 0.0403  -0.0559 352 TYR A O   
2621 C CB  . TYR A 353 ? 1.2982 0.6476 0.8009 -0.0955 0.0507  -0.0613 352 TYR A CB  
2622 C CG  . TYR A 353 ? 1.3205 0.6824 0.8346 -0.0852 0.0564  -0.0582 352 TYR A CG  
2623 C CD1 . TYR A 353 ? 1.4131 0.7838 0.9447 -0.0794 0.0595  -0.0533 352 TYR A CD1 
2624 C CD2 . TYR A 353 ? 1.3178 0.6830 0.8252 -0.0820 0.0582  -0.0597 352 TYR A CD2 
2625 C CE1 . TYR A 353 ? 1.4907 0.8729 1.0319 -0.0711 0.0642  -0.0503 352 TYR A CE1 
2626 C CE2 . TYR A 353 ? 1.4459 0.8221 0.9633 -0.0735 0.0629  -0.0566 352 TYR A CE2 
2627 C CZ  . TYR A 353 ? 1.4818 0.8662 1.0157 -0.0683 0.0658  -0.0521 352 TYR A CZ  
2628 O OH  . TYR A 353 ? 1.3039 0.6991 0.8468 -0.0609 0.0699  -0.0489 352 TYR A OH  
2629 N N   . LEU A 354 ? 1.4217 0.7661 0.9140 -0.1204 0.0302  -0.0593 353 LEU A N   
2630 C CA  . LEU A 354 ? 1.3871 0.7213 0.8750 -0.1305 0.0246  -0.0596 353 LEU A CA  
2631 C C   . LEU A 354 ? 1.4614 0.8149 0.9680 -0.1323 0.0177  -0.0505 353 LEU A C   
2632 O O   . LEU A 354 ? 1.5723 0.9204 1.0850 -0.1352 0.0169  -0.0488 353 LEU A O   
2633 C CB  . LEU A 354 ? 1.4516 0.7772 0.9196 -0.1417 0.0180  -0.0635 353 LEU A CB  
2634 C CG  . LEU A 354 ? 1.4793 0.7830 0.9333 -0.1525 0.0154  -0.0684 353 LEU A CG  
2635 C CD1 . LEU A 354 ? 1.4912 0.7797 0.9204 -0.1599 0.0143  -0.0759 353 LEU A CD1 
2636 C CD2 . LEU A 354 ? 1.4495 0.7642 0.9126 -0.1615 0.0048  -0.0610 353 LEU A CD2 
2637 N N   . VAL A 355 ? 1.4291 0.8048 0.9446 -0.1305 0.0127  -0.0443 354 VAL A N   
2638 C CA  . VAL A 355 ? 1.5940 0.9897 1.1272 -0.1313 0.0066  -0.0352 354 VAL A CA  
2639 C C   . VAL A 355 ? 1.5049 0.9065 1.0552 -0.1225 0.0127  -0.0322 354 VAL A C   
2640 O O   . VAL A 355 ? 1.4553 0.8640 1.0178 -0.1246 0.0096  -0.0268 354 VAL A O   
2641 C CB  . VAL A 355 ? 1.5663 0.9833 1.1044 -0.1300 0.0014  -0.0295 354 VAL A CB  
2642 C CG1 . VAL A 355 ? 1.5105 0.9498 1.0691 -0.1266 -0.0017 -0.0203 354 VAL A CG1 
2643 C CG2 . VAL A 355 ? 1.4080 0.8228 0.9323 -0.1410 -0.0069 -0.0296 354 VAL A CG2 
2644 N N   . ILE A 356 ? 1.4993 0.8990 1.0510 -0.1130 0.0212  -0.0353 355 ILE A N   
2645 C CA  . ILE A 356 ? 1.4959 0.9009 1.0629 -0.1050 0.0272  -0.0324 355 ILE A CA  
2646 C C   . ILE A 356 ? 1.5416 0.9306 1.1087 -0.1079 0.0298  -0.0341 355 ILE A C   
2647 O O   . ILE A 356 ? 1.6421 1.0389 1.2240 -0.1065 0.0297  -0.0287 355 ILE A O   
2648 C CB  . ILE A 356 ? 1.4407 0.8456 1.0073 -0.0954 0.0356  -0.0352 355 ILE A CB  
2649 C CG1 . ILE A 356 ? 1.2921 0.7146 0.8619 -0.0919 0.0329  -0.0323 355 ILE A CG1 
2650 C CG2 . ILE A 356 ? 1.4359 0.8437 1.0165 -0.0882 0.0422  -0.0326 355 ILE A CG2 
2651 C CD1 . ILE A 356 ? 1.2277 0.6515 0.7979 -0.0832 0.0402  -0.0343 355 ILE A CD1 
2652 N N   . ALA A 357 ? 1.5372 0.9029 1.0872 -0.1121 0.0323  -0.0415 356 ALA A N   
2653 C CA  . ALA A 357 ? 1.6403 0.9878 1.1888 -0.1152 0.0349  -0.0437 356 ALA A CA  
2654 C C   . ALA A 357 ? 1.6846 1.0359 1.2378 -0.1248 0.0258  -0.0389 356 ALA A C   
2655 O O   . ALA A 357 ? 1.7274 1.0752 1.2902 -0.1253 0.0267  -0.0359 356 ALA A O   
2656 C CB  . ALA A 357 ? 1.5499 0.8706 1.0769 -0.1180 0.0396  -0.0534 356 ALA A CB  
2657 N N   . LYS A 358 ? 1.8135 1.1727 1.3608 -0.1326 0.0167  -0.0372 357 LYS A N   
2658 C CA  . LYS A 358 ? 1.7991 1.1655 1.3520 -0.1420 0.0072  -0.0312 357 LYS A CA  
2659 C C   . LYS A 358 ? 1.7934 1.1863 1.3687 -0.1374 0.0046  -0.0212 357 LYS A C   
2660 O O   . LYS A 358 ? 1.8842 1.2840 1.4676 -0.1437 -0.0020 -0.0151 357 LYS A O   
2661 C CB  . LYS A 358 ? 1.8096 1.1772 1.3489 -0.1520 -0.0017 -0.0318 357 LYS A CB  
2662 C CG  . LYS A 358 ? 1.7714 1.1365 1.3090 -0.1649 -0.0112 -0.0281 357 LYS A CG  
2663 C CD  . LYS A 358 ? 1.8433 1.2084 1.3656 -0.1755 -0.0196 -0.0289 357 LYS A CD  
2664 C CE  . LYS A 358 ? 1.7159 1.1025 1.2426 -0.1700 -0.0210 -0.0252 357 LYS A CE  
2665 N NZ  . LYS A 358 ? 1.6199 1.0056 1.1309 -0.1798 -0.0284 -0.0261 357 LYS A NZ  
2666 N N   . ALA A 359 ? 1.7150 1.1224 1.2997 -0.1269 0.0095  -0.0195 358 ALA A N   
2667 C CA  . ALA A 359 ? 1.6725 1.1045 1.2770 -0.1216 0.0082  -0.0109 358 ALA A CA  
2668 C C   . ALA A 359 ? 1.5808 1.0307 1.1900 -0.1277 -0.0016 -0.0039 358 ALA A C   
2669 O O   . ALA A 359 ? 1.3971 0.8653 1.0221 -0.1263 -0.0042 0.0041  358 ALA A O   
2670 C CB  . ALA A 359 ? 1.6431 1.0746 1.2611 -0.1196 0.0114  -0.0073 358 ALA A CB  
2671 N N   . SER A 360 ? 1.5960 1.0416 1.1915 -0.1345 -0.0069 -0.0061 359 SER A N   
2672 C CA  . SER A 360 ? 1.4635 0.9263 1.0630 -0.1406 -0.0162 0.0013  359 SER A CA  
2673 C C   . SER A 360 ? 1.4245 0.9090 1.0336 -0.1317 -0.0150 0.0056  359 SER A C   
2674 O O   . SER A 360 ? 1.4156 0.8995 1.0161 -0.1293 -0.0139 0.0024  359 SER A O   
2675 C CB  . SER A 360 ? 1.4416 0.8929 1.0230 -0.1512 -0.0222 -0.0022 359 SER A CB  
2676 O OG  . SER A 360 ? 1.3988 0.8679 0.9852 -0.1576 -0.0316 0.0063  359 SER A OG  
2677 N N   . LEU A 361 ? 1.3869 0.8902 1.0136 -0.1268 -0.0150 0.0129  360 LEU A N   
2678 C CA  . LEU A 361 ? 1.2222 0.7456 0.8580 -0.1186 -0.0138 0.0172  360 LEU A CA  
2679 C C   . LEU A 361 ? 1.2480 0.7821 0.8804 -0.1227 -0.0206 0.0215  360 LEU A C   
2680 O O   . LEU A 361 ? 1.3219 0.8665 0.9563 -0.1160 -0.0188 0.0226  360 LEU A O   
2681 C CB  . LEU A 361 ? 1.2030 0.7445 0.8572 -0.1139 -0.0131 0.0246  360 LEU A CB  
2682 C CG  . LEU A 361 ? 1.1318 0.6771 0.7932 -0.1031 -0.0047 0.0226  360 LEU A CG  
2683 C CD1 . LEU A 361 ? 1.2472 0.7722 0.9019 -0.1021 0.0015  0.0151  360 LEU A CD1 
2684 C CD2 . LEU A 361 ? 1.2418 0.8060 0.9205 -0.0999 -0.0049 0.0304  360 LEU A CD2 
2685 N N   . ARG A 362 ? 1.2843 0.8158 0.9115 -0.1338 -0.0284 0.0243  361 ARG A N   
2686 C CA  . ARG A 362 ? 1.3305 0.8718 0.9537 -0.1387 -0.0354 0.0289  361 ARG A CA  
2687 C C   . ARG A 362 ? 1.3424 0.8713 0.9497 -0.1384 -0.0333 0.0215  361 ARG A C   
2688 O O   . ARG A 362 ? 1.3106 0.8507 0.9185 -0.1348 -0.0341 0.0243  361 ARG A O   
2689 C CB  . ARG A 362 ? 1.3122 0.8526 0.9327 -0.1520 -0.0446 0.0336  361 ARG A CB  
2690 C CG  . ARG A 362 ? 1.3089 0.8562 0.9430 -0.1538 -0.0463 0.0395  361 ARG A CG  
2691 C CD  . ARG A 362 ? 1.3506 0.8777 0.9751 -0.1650 -0.0496 0.0357  361 ARG A CD  
2692 N NE  . ARG A 362 ? 1.2696 0.7984 0.9068 -0.1640 -0.0481 0.0389  361 ARG A NE  
2693 C CZ  . ARG A 362 ? 1.3172 0.8338 0.9559 -0.1577 -0.0402 0.0330  361 ARG A CZ  
2694 N NH1 . ARG A 362 ? 1.2261 0.7276 0.8545 -0.1518 -0.0328 0.0235  361 ARG A NH1 
2695 N NH2 . ARG A 362 ? 1.3033 0.8240 0.9548 -0.1573 -0.0397 0.0375  361 ARG A NH2 
2696 N N   . PHE A 363 ? 1.4783 0.9838 1.0711 -0.1419 -0.0302 0.0122  362 PHE A N   
2697 C CA  . PHE A 363 ? 1.4618 0.9551 1.0385 -0.1420 -0.0280 0.0050  362 PHE A CA  
2698 C C   . PHE A 363 ? 1.4326 0.9290 1.0131 -0.1295 -0.0198 0.0020  362 PHE A C   
2699 O O   . PHE A 363 ? 1.4321 0.9308 1.0065 -0.1273 -0.0196 0.0010  362 PHE A O   
2700 C CB  . PHE A 363 ? 1.5157 0.9827 1.0756 -0.1486 -0.0261 -0.0042 362 PHE A CB  
2701 C CG  . PHE A 363 ? 1.6145 1.0745 1.1617 -0.1626 -0.0348 -0.0037 362 PHE A CG  
2702 C CD1 . PHE A 363 ? 1.6128 1.0779 1.1664 -0.1710 -0.0419 0.0025  362 PHE A CD1 
2703 C CD2 . PHE A 363 ? 1.5435 0.9923 1.0720 -0.1679 -0.0361 -0.0093 362 PHE A CD2 
2704 C CE1 . PHE A 363 ? 1.5897 1.0482 1.1308 -0.1850 -0.0504 0.0032  362 PHE A CE1 
2705 C CE2 . PHE A 363 ? 1.5616 1.0039 1.0772 -0.1818 -0.0444 -0.0089 362 PHE A CE2 
2706 C CZ  . PHE A 363 ? 1.6827 1.1297 1.2044 -0.1906 -0.0517 -0.0027 362 PHE A CZ  
2707 N N   . TYR A 364 ? 1.2912 0.7880 0.8818 -0.1218 -0.0134 0.0011  363 TYR A N   
2708 C CA  . TYR A 364 ? 1.3466 0.8468 0.9410 -0.1107 -0.0061 -0.0012 363 TYR A CA  
2709 C C   . TYR A 364 ? 1.2457 0.7667 0.8498 -0.1057 -0.0083 0.0055  363 TYR A C   
2710 O O   . TYR A 364 ? 1.1467 0.6687 0.7472 -0.1003 -0.0054 0.0035  363 TYR A O   
2711 C CB  . TYR A 364 ? 1.3092 0.8079 0.9135 -0.1046 0.0003  -0.0023 363 TYR A CB  
2712 C CG  . TYR A 364 ? 1.3267 0.8233 0.9311 -0.0951 0.0083  -0.0064 363 TYR A CG  
2713 C CD1 . TYR A 364 ? 1.3355 0.8175 0.9262 -0.0944 0.0120  -0.0133 363 TYR A CD1 
2714 C CD2 . TYR A 364 ? 1.1442 0.6538 0.7620 -0.0872 0.0119  -0.0030 363 TYR A CD2 
2715 C CE1 . TYR A 364 ? 1.2361 0.7171 0.8274 -0.0862 0.0189  -0.0162 363 TYR A CE1 
2716 C CE2 . TYR A 364 ? 1.1383 0.6463 0.7559 -0.0795 0.0185  -0.0063 363 TYR A CE2 
2717 C CZ  . TYR A 364 ? 1.2320 0.7259 0.8368 -0.0791 0.0219  -0.0126 363 TYR A CZ  
2718 O OH  . TYR A 364 ? 1.1567 0.6496 0.7616 -0.0720 0.0282  -0.0152 363 TYR A OH  
2719 N N   . ILE A 365 ? 1.1823 0.7197 0.7986 -0.1071 -0.0130 0.0138  364 ILE A N   
2720 C CA  . ILE A 365 ? 1.2407 0.7976 0.8660 -0.1023 -0.0149 0.0208  364 ILE A CA  
2721 C C   . ILE A 365 ? 1.2109 0.7678 0.8265 -0.1062 -0.0192 0.0215  364 ILE A C   
2722 O O   . ILE A 365 ? 1.1636 0.7267 0.7801 -0.0998 -0.0171 0.0223  364 ILE A O   
2723 C CB  . ILE A 365 ? 1.1691 0.7436 0.8085 -0.1042 -0.0196 0.0302  364 ILE A CB  
2724 C CG1 . ILE A 365 ? 1.1736 0.7558 0.8258 -0.0960 -0.0141 0.0313  364 ILE A CG1 
2725 C CG2 . ILE A 365 ? 1.1799 0.7723 0.8246 -0.1037 -0.0244 0.0386  364 ILE A CG2 
2726 C CD1 . ILE A 365 ? 1.1916 0.7920 0.8581 -0.0972 -0.0180 0.0407  364 ILE A CD1 
2727 N N   . LEU A 366 ? 1.1874 0.7368 0.7931 -0.1171 -0.0253 0.0212  365 LEU A N   
2728 C CA  . LEU A 366 ? 1.1378 0.6880 0.7338 -0.1222 -0.0302 0.0226  365 LEU A CA  
2729 C C   . LEU A 366 ? 1.1101 0.6473 0.6940 -0.1182 -0.0249 0.0146  365 LEU A C   
2730 O O   . LEU A 366 ? 1.0743 0.6178 0.6560 -0.1165 -0.0260 0.0169  365 LEU A O   
2731 C CB  . LEU A 366 ? 1.1588 0.7019 0.7450 -0.1359 -0.0379 0.0232  365 LEU A CB  
2732 C CG  . LEU A 366 ? 1.1939 0.7514 0.7803 -0.1430 -0.0466 0.0321  365 LEU A CG  
2733 C CD1 . LEU A 366 ? 1.0445 0.6265 0.6502 -0.1373 -0.0483 0.0433  365 LEU A CD1 
2734 C CD2 . LEU A 366 ? 1.1097 0.6590 0.6859 -0.1576 -0.0545 0.0323  365 LEU A CD2 
2735 N N   . ALA A 367 ? 1.0784 0.5983 0.6553 -0.1166 -0.0188 0.0058  366 ALA A N   
2736 C CA  . ALA A 367 ? 1.0811 0.5889 0.6468 -0.1128 -0.0134 -0.0014 366 ALA A CA  
2737 C C   . ALA A 367 ? 1.1404 0.6586 0.7150 -0.1018 -0.0087 0.0004  366 ALA A C   
2738 O O   . ALA A 367 ? 1.0186 0.5375 0.5877 -0.0999 -0.0084 -0.0001 366 ALA A O   
2739 C CB  . ALA A 367 ? 0.9774 0.4658 0.5355 -0.1126 -0.0074 -0.0100 366 ALA A CB  
2740 N N   . GLU A 368 ? 1.1294 0.6553 0.7174 -0.0949 -0.0051 0.0025  367 GLU A N   
2741 C CA  . GLU A 368 ? 1.0448 0.5785 0.6401 -0.0849 -0.0003 0.0033  367 GLU A CA  
2742 C C   . GLU A 368 ? 1.0806 0.6304 0.6824 -0.0829 -0.0043 0.0110  367 GLU A C   
2743 O O   . GLU A 368 ? 1.0578 0.6097 0.6590 -0.0773 -0.0019 0.0109  367 GLU A O   
2744 C CB  . GLU A 368 ? 1.0727 0.6104 0.6794 -0.0789 0.0044  0.0035  367 GLU A CB  
2745 C CG  . GLU A 368 ? 1.0022 0.5249 0.6042 -0.0796 0.0092  -0.0030 367 GLU A CG  
2746 C CD  . GLU A 368 ? 1.1272 0.6417 0.7241 -0.0735 0.0159  -0.0085 367 GLU A CD  
2747 O OE1 . GLU A 368 ? 1.1243 0.6441 0.7212 -0.0691 0.0166  -0.0076 367 GLU A OE1 
2748 O OE2 . GLU A 368 ? 1.0886 0.5913 0.6818 -0.0732 0.0205  -0.0133 367 GLU A OE2 
2749 N N   . VAL A 369 ? 1.0371 0.5987 0.6458 -0.0874 -0.0103 0.0181  368 VAL A N   
2750 C CA  . VAL A 369 ? 1.0020 0.5800 0.6179 -0.0854 -0.0138 0.0266  368 VAL A CA  
2751 C C   . VAL A 369 ? 1.0169 0.5917 0.6222 -0.0895 -0.0172 0.0267  368 VAL A C   
2752 O O   . VAL A 369 ? 1.0728 0.6555 0.6813 -0.0843 -0.0166 0.0306  368 VAL A O   
2753 C CB  . VAL A 369 ? 1.0480 0.6402 0.6739 -0.0899 -0.0197 0.0351  368 VAL A CB  
2754 C CG1 . VAL A 369 ? 0.9653 0.5717 0.5941 -0.0923 -0.0256 0.0442  368 VAL A CG1 
2755 C CG2 . VAL A 369 ? 1.0797 0.6824 0.7198 -0.0823 -0.0157 0.0379  368 VAL A CG2 
2756 N N   . SER A 370 ? 1.0517 0.6144 0.6438 -0.0989 -0.0205 0.0225  369 SER A N   
2757 C CA  . SER A 370 ? 1.0506 0.6102 0.6313 -0.1038 -0.0239 0.0225  369 SER A CA  
2758 C C   . SER A 370 ? 1.0178 0.5705 0.5936 -0.0965 -0.0179 0.0175  369 SER A C   
2759 O O   . SER A 370 ? 1.0248 0.5838 0.5999 -0.0950 -0.0194 0.0214  369 SER A O   
2760 C CB  . SER A 370 ? 1.0523 0.5980 0.6178 -0.1153 -0.0277 0.0175  369 SER A CB  
2761 O OG  . SER A 370 ? 1.0482 0.6004 0.6176 -0.1234 -0.0343 0.0229  369 SER A OG  
2762 N N   . GLN A 371 ? 1.0159 0.5564 0.5889 -0.0920 -0.0111 0.0097  370 GLN A N   
2763 C CA  . GLN A 371 ? 1.0188 0.5532 0.5877 -0.0854 -0.0055 0.0053  370 GLN A CA  
2764 C C   . GLN A 371 ? 1.1161 0.6627 0.6970 -0.0763 -0.0034 0.0105  370 GLN A C   
2765 O O   . GLN A 371 ? 1.1606 0.7082 0.7393 -0.0731 -0.0026 0.0115  370 GLN A O   
2766 C CB  . GLN A 371 ? 1.0133 0.5338 0.5783 -0.0827 0.0012  -0.0029 370 GLN A CB  
2767 C CG  . GLN A 371 ? 1.0198 0.5248 0.5707 -0.0902 0.0010  -0.0092 370 GLN A CG  
2768 C CD  . GLN A 371 ? 1.0240 0.5164 0.5729 -0.0863 0.0084  -0.0161 370 GLN A CD  
2769 O OE1 . GLN A 371 ? 1.0226 0.5110 0.5693 -0.0807 0.0137  -0.0192 370 GLN A OE1 
2770 N NE2 . GLN A 371 ? 0.9717 0.4587 0.5221 -0.0893 0.0087  -0.0179 370 GLN A NE2 
2771 N N   . PHE A 372 ? 1.0532 0.6088 0.6467 -0.0719 -0.0022 0.0136  371 PHE A N   
2772 C CA  . PHE A 372 ? 1.0696 0.6357 0.6738 -0.0630 0.0004  0.0180  371 PHE A CA  
2773 C C   . PHE A 372 ? 1.0645 0.6421 0.6718 -0.0634 -0.0041 0.0261  371 PHE A C   
2774 O O   . PHE A 372 ? 1.0872 0.6671 0.6965 -0.0572 -0.0018 0.0278  371 PHE A O   
2775 C CB  . PHE A 372 ? 1.1048 0.6792 0.7210 -0.0593 0.0021  0.0203  371 PHE A CB  
2776 C CG  . PHE A 372 ? 1.1237 0.7111 0.7510 -0.0512 0.0038  0.0262  371 PHE A CG  
2777 C CD1 . PHE A 372 ? 1.1233 0.7257 0.7589 -0.0519 -0.0006 0.0352  371 PHE A CD1 
2778 C CD2 . PHE A 372 ? 1.1591 0.7437 0.7885 -0.0430 0.0100  0.0229  371 PHE A CD2 
2779 C CE1 . PHE A 372 ? 1.1877 0.8013 0.8334 -0.0436 0.0019  0.0406  371 PHE A CE1 
2780 C CE2 . PHE A 372 ? 1.1745 0.7691 0.8127 -0.0354 0.0121  0.0276  371 PHE A CE2 
2781 C CZ  . PHE A 372 ? 1.1579 0.7668 0.8043 -0.0352 0.0084  0.0363  371 PHE A CZ  
2782 N N   . THR A 373 ? 1.0189 0.6042 0.6271 -0.0708 -0.0108 0.0317  372 THR A N   
2783 C CA  . THR A 373 ? 0.9890 0.5874 0.6016 -0.0715 -0.0155 0.0410  372 THR A CA  
2784 C C   . THR A 373 ? 1.0933 0.6856 0.6954 -0.0739 -0.0166 0.0397  372 THR A C   
2785 O O   . THR A 373 ? 1.2424 0.8418 0.8489 -0.0689 -0.0163 0.0451  372 THR A O   
2786 C CB  . THR A 373 ? 1.0086 0.6168 0.6239 -0.0804 -0.0229 0.0477  372 THR A CB  
2787 O OG1 . THR A 373 ? 1.1315 0.7462 0.7573 -0.0780 -0.0218 0.0495  372 THR A OG1 
2788 C CG2 . THR A 373 ? 0.9081 0.5322 0.5295 -0.0810 -0.0278 0.0589  372 THR A CG2 
2789 N N   . LEU A 374 ? 1.1636 0.7426 0.7516 -0.0812 -0.0177 0.0328  373 LEU A N   
2790 C CA  . LEU A 374 ? 1.1740 0.7471 0.7509 -0.0838 -0.0186 0.0312  373 LEU A CA  
2791 C C   . LEU A 374 ? 1.2065 0.7748 0.7845 -0.0743 -0.0121 0.0282  373 LEU A C   
2792 O O   . LEU A 374 ? 1.2761 0.8470 0.8526 -0.0729 -0.0128 0.0315  373 LEU A O   
2793 C CB  . LEU A 374 ? 1.0756 0.6339 0.6363 -0.0926 -0.0196 0.0233  373 LEU A CB  
2794 C CG  . LEU A 374 ? 1.1363 0.6965 0.6913 -0.1044 -0.0271 0.0258  373 LEU A CG  
2795 C CD1 . LEU A 374 ? 1.2192 0.7615 0.7562 -0.1120 -0.0266 0.0164  373 LEU A CD1 
2796 C CD2 . LEU A 374 ? 1.2101 0.7848 0.7672 -0.1087 -0.0340 0.0358  373 LEU A CD2 
2797 N N   . LEU A 375 ? 1.1370 0.6985 0.7179 -0.0683 -0.0060 0.0223  374 LEU A N   
2798 C CA  . LEU A 375 ? 1.0926 0.6494 0.6746 -0.0601 -0.0001 0.0194  374 LEU A CA  
2799 C C   . LEU A 375 ? 1.2070 0.7751 0.8005 -0.0527 0.0004  0.0268  374 LEU A C   
2800 O O   . LEU A 375 ? 1.2934 0.8597 0.8859 -0.0486 0.0022  0.0277  374 LEU A O   
2801 C CB  . LEU A 375 ? 1.0922 0.6408 0.6753 -0.0563 0.0057  0.0125  374 LEU A CB  
2802 C CG  . LEU A 375 ? 1.1213 0.6554 0.6926 -0.0596 0.0086  0.0042  374 LEU A CG  
2803 C CD1 . LEU A 375 ? 1.2076 0.7369 0.7829 -0.0554 0.0140  -0.0005 374 LEU A CD1 
2804 C CD2 . LEU A 375 ? 1.1547 0.6827 0.7181 -0.0581 0.0104  0.0024  374 LEU A CD2 
2805 N N   . MET A 376 ? 1.1553 0.7350 0.7599 -0.0508 -0.0010 0.0323  375 MET A N   
2806 C CA  . MET A 376 ? 1.1675 0.7574 0.7833 -0.0426 0.0007  0.0391  375 MET A CA  
2807 C C   . MET A 376 ? 1.2317 0.8293 0.8483 -0.0439 -0.0034 0.0472  375 MET A C   
2808 O O   . MET A 376 ? 1.2653 0.8629 0.8847 -0.0373 -0.0007 0.0496  375 MET A O   
2809 C CB  . MET A 376 ? 1.1502 0.7517 0.7773 -0.0406 0.0003  0.0437  375 MET A CB  
2810 C CG  . MET A 376 ? 1.1792 0.7774 0.8108 -0.0336 0.0065  0.0387  375 MET A CG  
2811 S SD  . MET A 376 ? 1.3888 0.9774 1.0182 -0.0248 0.0132  0.0344  375 MET A SD  
2812 C CE  . MET A 376 ? 1.1287 0.7036 0.7507 -0.0264 0.0172  0.0236  375 MET A CE  
2813 N N   . VAL A 377 ? 1.2195 0.8238 0.8336 -0.0526 -0.0102 0.0519  376 VAL A N   
2814 C CA  . VAL A 377 ? 1.2905 0.9049 0.9066 -0.0544 -0.0147 0.0612  376 VAL A CA  
2815 C C   . VAL A 377 ? 1.2796 0.8847 0.8858 -0.0552 -0.0140 0.0581  376 VAL A C   
2816 O O   . VAL A 377 ? 1.2821 0.8928 0.8927 -0.0513 -0.0142 0.0646  376 VAL A O   
2817 C CB  . VAL A 377 ? 1.1671 0.7909 0.7819 -0.0650 -0.0227 0.0669  376 VAL A CB  
2818 C CG1 . VAL A 377 ? 1.0987 0.7095 0.6981 -0.0750 -0.0250 0.0582  376 VAL A CG1 
2819 C CG2 . VAL A 377 ? 1.1192 0.7558 0.7372 -0.0673 -0.0278 0.0780  376 VAL A CG2 
2820 N N   . PHE A 378 ? 1.3118 0.9029 0.9052 -0.0599 -0.0129 0.0485  377 PHE A N   
2821 C CA  . PHE A 378 ? 1.3180 0.9009 0.9013 -0.0612 -0.0122 0.0456  377 PHE A CA  
2822 C C   . PHE A 378 ? 1.2393 0.8160 0.8261 -0.0516 -0.0059 0.0433  377 PHE A C   
2823 O O   . PHE A 378 ? 1.2690 0.8442 0.8529 -0.0504 -0.0058 0.0453  377 PHE A O   
2824 C CB  . PHE A 378 ? 1.2685 0.8386 0.8368 -0.0688 -0.0124 0.0364  377 PHE A CB  
2825 C CG  . PHE A 378 ? 1.3651 0.9387 0.9256 -0.0800 -0.0194 0.0387  377 PHE A CG  
2826 C CD1 . PHE A 378 ? 1.3701 0.9317 0.9167 -0.0875 -0.0197 0.0305  377 PHE A CD1 
2827 C CD2 . PHE A 378 ? 1.4855 1.0742 1.0523 -0.0833 -0.0256 0.0493  377 PHE A CD2 
2828 C CE1 . PHE A 378 ? 1.4185 0.9819 0.9563 -0.0985 -0.0262 0.0320  377 PHE A CE1 
2829 C CE2 . PHE A 378 ? 1.5536 1.1458 1.1125 -0.0947 -0.0326 0.0517  377 PHE A CE2 
2830 C CZ  . PHE A 378 ? 1.4114 0.9902 0.9550 -0.1027 -0.0331 0.0426  377 PHE A CZ  
2831 N N   . ALA A 379 ? 1.1899 0.7632 0.7825 -0.0451 -0.0008 0.0392  378 ALA A N   
2832 C CA  . ALA A 379 ? 1.2596 0.8275 0.8558 -0.0363 0.0049  0.0376  378 ALA A CA  
2833 C C   . ALA A 379 ? 1.2473 0.8250 0.8543 -0.0299 0.0047  0.0468  378 ALA A C   
2834 O O   . ALA A 379 ? 1.1872 0.7616 0.7940 -0.0261 0.0063  0.0486  378 ALA A O   
2835 C CB  . ALA A 379 ? 1.1915 0.7540 0.7904 -0.0320 0.0100  0.0311  378 ALA A CB  
2836 N N   . HIS A 380 ? 1.2201 0.8101 0.8368 -0.0287 0.0029  0.0532  379 HIS A N   
2837 C CA  . HIS A 380 ? 1.2524 0.8528 0.8805 -0.0218 0.0034  0.0628  379 HIS A CA  
2838 C C   . HIS A 380 ? 1.2747 0.8792 0.9014 -0.0243 -0.0005 0.0699  379 HIS A C   
2839 O O   . HIS A 380 ? 1.3106 0.9175 0.9441 -0.0173 0.0017  0.0759  379 HIS A O   
2840 C CB  . HIS A 380 ? 1.2722 0.8872 0.9105 -0.0217 0.0011  0.0696  379 HIS A CB  
2841 C CG  . HIS A 380 ? 1.5218 1.1487 1.1728 -0.0139 0.0022  0.0803  379 HIS A CG  
2842 N ND1 . HIS A 380 ? 1.5679 1.2119 1.2274 -0.0164 -0.0026 0.0914  379 HIS A ND1 
2843 C CD2 . HIS A 380 ? 1.4886 1.1124 1.1453 -0.0036 0.0080  0.0819  379 HIS A CD2 
2844 C CE1 . HIS A 380 ? 1.4447 1.0965 1.1154 -0.0072 0.0005  0.0998  379 HIS A CE1 
2845 N NE2 . HIS A 380 ? 1.4280 1.0670 1.0969 0.0008  0.0071  0.0939  379 HIS A NE2 
2846 N N   . TRP A 381 ? 1.4179 1.0229 1.0354 -0.0343 -0.0060 0.0695  380 TRP A N   
2847 C CA  . TRP A 381 ? 1.4934 1.1031 1.1084 -0.0379 -0.0101 0.0763  380 TRP A CA  
2848 C C   . TRP A 381 ? 1.4855 1.0822 1.0918 -0.0367 -0.0072 0.0707  380 TRP A C   
2849 O O   . TRP A 381 ? 1.5278 1.1275 1.1362 -0.0351 -0.0081 0.0771  380 TRP A O   
2850 C CB  . TRP A 381 ? 1.5349 1.1509 1.1425 -0.0499 -0.0175 0.0784  380 TRP A CB  
2851 C CG  . TRP A 381 ? 1.7146 1.3411 1.3225 -0.0542 -0.0230 0.0885  380 TRP A CG  
2852 C CD1 . TRP A 381 ? 1.7133 1.3355 1.3101 -0.0601 -0.0254 0.0872  380 TRP A CD1 
2853 C CD2 . TRP A 381 ? 1.7996 1.4441 1.4201 -0.0530 -0.0267 0.1022  380 TRP A CD2 
2854 N NE1 . TRP A 381 ? 1.7475 1.3838 1.3488 -0.0631 -0.0307 0.0992  380 TRP A NE1 
2855 C CE2 . TRP A 381 ? 1.7870 1.4373 1.4032 -0.0588 -0.0316 0.1089  380 TRP A CE2 
2856 C CE3 . TRP A 381 ? 1.8057 1.4628 1.4408 -0.0475 -0.0261 0.1101  380 TRP A CE3 
2857 C CZ2 . TRP A 381 ? 1.8055 1.4740 1.4322 -0.0594 -0.0361 0.1235  380 TRP A CZ2 
2858 C CZ3 . TRP A 381 ? 1.7909 1.4659 1.4364 -0.0476 -0.0303 0.1246  380 TRP A CZ3 
2859 C CH2 . TRP A 381 ? 1.7936 1.4743 1.4352 -0.0536 -0.0353 0.1313  380 TRP A CH2 
2860 N N   . LEU A 382 ? 1.2389 0.8221 0.8365 -0.0375 -0.0037 0.0597  381 LEU A N   
2861 C CA  . LEU A 382 ? 1.1793 0.7511 0.7675 -0.0380 -0.0016 0.0545  381 LEU A CA  
2862 C C   . LEU A 382 ? 1.1983 0.7597 0.7890 -0.0298 0.0049  0.0495  381 LEU A C   
2863 O O   . LEU A 382 ? 1.2524 0.8073 0.8396 -0.0282 0.0065  0.0490  381 LEU A O   
2864 C CB  . LEU A 382 ? 1.1933 0.7575 0.7678 -0.0464 -0.0028 0.0463  381 LEU A CB  
2865 C CG  . LEU A 382 ? 1.1741 0.7452 0.7416 -0.0564 -0.0094 0.0496  381 LEU A CG  
2866 C CD1 . LEU A 382 ? 1.1105 0.6714 0.6643 -0.0633 -0.0091 0.0400  381 LEU A CD1 
2867 C CD2 . LEU A 382 ? 1.1408 0.7171 0.7061 -0.0585 -0.0127 0.0566  381 LEU A CD2 
2868 N N   . ILE A 383 ? 1.2625 0.8224 0.8589 -0.0249 0.0086  0.0460  382 ILE A N   
2869 C CA  . ILE A 383 ? 1.1803 0.7300 0.7778 -0.0180 0.0145  0.0410  382 ILE A CA  
2870 C C   . ILE A 383 ? 1.1159 0.6655 0.7199 -0.0110 0.0163  0.0470  382 ILE A C   
2871 O O   . ILE A 383 ? 1.0458 0.5859 0.6456 -0.0096 0.0185  0.0446  382 ILE A O   
2872 C CB  . ILE A 383 ? 1.1709 0.7205 0.7727 -0.0150 0.0177  0.0365  382 ILE A CB  
2873 C CG1 . ILE A 383 ? 1.1258 0.6700 0.7196 -0.0210 0.0177  0.0286  382 ILE A CG1 
2874 C CG2 . ILE A 383 ? 1.1126 0.6545 0.7176 -0.0071 0.0234  0.0338  382 ILE A CG2 
2875 C CD1 . ILE A 383 ? 1.0419 0.5738 0.6290 -0.0202 0.0218  0.0214  382 ILE A CD1 
2876 N N   . PRO A 384 ? 1.1634 0.7231 0.7779 -0.0065 0.0157  0.0553  383 PRO A N   
2877 C CA  . PRO A 384 ? 1.1896 0.7473 0.8103 0.0011  0.0183  0.0609  383 PRO A CA  
2878 C C   . PRO A 384 ? 1.1342 0.6910 0.7514 -0.0019 0.0155  0.0654  383 PRO A C   
2879 O O   . PRO A 384 ? 1.2028 0.7530 0.8223 0.0035  0.0182  0.0675  383 PRO A O   
2880 C CB  . PRO A 384 ? 1.1597 0.7310 0.7927 0.0058  0.0179  0.0699  383 PRO A CB  
2881 C CG  . PRO A 384 ? 1.2124 0.7901 0.8456 0.0021  0.0164  0.0669  383 PRO A CG  
2882 C CD  . PRO A 384 ? 1.1969 0.7702 0.8185 -0.0076 0.0128  0.0606  383 PRO A CD  
2883 N N   . ALA A 385 ? 1.1235 0.6863 0.7347 -0.0105 0.0101  0.0669  384 ALA A N   
2884 C CA  . ALA A 385 ? 1.0897 0.6533 0.6970 -0.0140 0.0069  0.0717  384 ALA A CA  
2885 C C   . ALA A 385 ? 1.1568 0.7077 0.7529 -0.0170 0.0086  0.0637  384 ALA A C   
2886 O O   . ALA A 385 ? 1.1723 0.7162 0.7686 -0.0136 0.0106  0.0648  384 ALA A O   
2887 C CB  . ALA A 385 ? 1.1534 0.7300 0.7585 -0.0224 0.0002  0.0774  384 ALA A CB  
2888 N N   . HIS A 386 ? 1.1600 0.7077 0.7466 -0.0232 0.0079  0.0559  385 HIS A N   
2889 C CA  . HIS A 386 ? 1.1999 0.7377 0.7755 -0.0267 0.0092  0.0495  385 HIS A CA  
2890 C C   . HIS A 386 ? 1.1340 0.6604 0.7078 -0.0234 0.0145  0.0408  385 HIS A C   
2891 O O   . HIS A 386 ? 1.0638 0.5825 0.6299 -0.0254 0.0161  0.0362  385 HIS A O   
2892 C CB  . HIS A 386 ? 1.1515 0.6921 0.7166 -0.0358 0.0056  0.0468  385 HIS A CB  
2893 C CG  . HIS A 386 ? 1.2007 0.7523 0.7652 -0.0409 -0.0002 0.0551  385 HIS A CG  
2894 N ND1 . HIS A 386 ? 1.2389 0.8024 0.8112 -0.0414 -0.0038 0.0621  385 HIS A ND1 
2895 C CD2 . HIS A 386 ? 1.2404 0.7941 0.7974 -0.0461 -0.0031 0.0580  385 HIS A CD2 
2896 C CE1 . HIS A 386 ? 1.1445 0.7170 0.7143 -0.0470 -0.0090 0.0693  385 HIS A CE1 
2897 N NE2 . HIS A 386 ? 1.2756 0.8422 0.8358 -0.0500 -0.0087 0.0667  385 HIS A NE2 
2898 N N   . GLY A 387 ? 1.0792 0.6055 0.6598 -0.0185 0.0172  0.0389  386 GLY A N   
2899 C CA  . GLY A 387 ? 1.0514 0.5676 0.6304 -0.0156 0.0220  0.0314  386 GLY A CA  
2900 C C   . GLY A 387 ? 1.0531 0.5663 0.6243 -0.0208 0.0225  0.0240  386 GLY A C   
2901 O O   . GLY A 387 ? 1.1474 0.6662 0.7178 -0.0245 0.0204  0.0233  386 GLY A O   
2902 N N   . ALA A 388 ? 0.9934 0.4977 0.5591 -0.0211 0.0255  0.0190  387 ALA A N   
2903 C CA  . ALA A 388 ? 1.0386 0.5395 0.5979 -0.0249 0.0271  0.0124  387 ALA A CA  
2904 C C   . ALA A 388 ? 1.1874 0.6911 0.7388 -0.0313 0.0241  0.0124  387 ALA A C   
2905 O O   . ALA A 388 ? 1.0888 0.5926 0.6368 -0.0346 0.0242  0.0084  387 ALA A O   
2906 C CB  . ALA A 388 ? 1.0256 0.5178 0.5810 -0.0240 0.0307  0.0086  387 ALA A CB  
2907 N N   . LEU A 389 ? 1.2447 0.7502 0.7926 -0.0334 0.0215  0.0168  388 LEU A N   
2908 C CA  . LEU A 389 ? 1.2615 0.7702 0.8009 -0.0399 0.0183  0.0170  388 LEU A CA  
2909 C C   . LEU A 389 ? 1.2811 0.7978 0.8235 -0.0426 0.0144  0.0195  388 LEU A C   
2910 O O   . LEU A 389 ? 1.3250 0.8415 0.8601 -0.0483 0.0129  0.0164  388 LEU A O   
2911 C CB  . LEU A 389 ? 1.2911 0.8017 0.8269 -0.0416 0.0160  0.0223  388 LEU A CB  
2912 C CG  . LEU A 389 ? 1.2744 0.7875 0.7991 -0.0489 0.0130  0.0221  388 LEU A CG  
2913 C CD1 . LEU A 389 ? 1.2747 0.7798 0.7893 -0.0515 0.0167  0.0140  388 LEU A CD1 
2914 C CD2 . LEU A 389 ? 1.2776 0.7939 0.7999 -0.0502 0.0108  0.0282  388 LEU A CD2 
2915 N N   . GLY A 390 ? 1.2439 0.7672 0.7968 -0.0386 0.0129  0.0254  389 GLY A N   
2916 C CA  . GLY A 390 ? 1.2427 0.7751 0.8000 -0.0409 0.0092  0.0288  389 GLY A CA  
2917 C C   . GLY A 390 ? 1.2637 0.7939 0.8211 -0.0417 0.0109  0.0228  389 GLY A C   
2918 O O   . GLY A 390 ? 1.3303 0.8658 0.8871 -0.0465 0.0074  0.0237  389 GLY A O   
2919 N N   . ALA A 391 ? 1.1065 0.6291 0.6650 -0.0376 0.0159  0.0171  390 ALA A N   
2920 C CA  . ALA A 391 ? 1.1226 0.6430 0.6813 -0.0385 0.0178  0.0116  390 ALA A CA  
2921 C C   . ALA A 391 ? 1.1650 0.6795 0.7123 -0.0450 0.0176  0.0062  390 ALA A C   
2922 O O   . ALA A 391 ? 1.1368 0.6519 0.6828 -0.0487 0.0163  0.0041  390 ALA A O   
2923 C CB  . ALA A 391 ? 1.1213 0.6361 0.6841 -0.0327 0.0230  0.0077  390 ALA A CB  
2924 N N   . ALA A 392 ? 1.1692 0.6775 0.7081 -0.0462 0.0193  0.0041  391 ALA A N   
2925 C CA  . ALA A 392 ? 1.1005 0.6029 0.6275 -0.0519 0.0197  -0.0007 391 ALA A CA  
2926 C C   . ALA A 392 ? 1.1700 0.6771 0.6911 -0.0588 0.0140  0.0020  391 ALA A C   
2927 O O   . ALA A 392 ? 1.1697 0.6727 0.6828 -0.0642 0.0134  -0.0022 391 ALA A O   
2928 C CB  . ALA A 392 ? 1.0680 0.5643 0.5878 -0.0511 0.0228  -0.0025 391 ALA A CB  
2929 N N   . GLN A 393 ? 1.1644 0.6799 0.6891 -0.0591 0.0098  0.0093  392 GLN A N   
2930 C CA  . GLN A 393 ? 1.1899 0.7121 0.7103 -0.0662 0.0037  0.0133  392 GLN A CA  
2931 C C   . GLN A 393 ? 1.0904 0.6172 0.6163 -0.0683 0.0011  0.0140  392 GLN A C   
2932 O O   . GLN A 393 ? 1.2349 0.7622 0.7534 -0.0761 -0.0029 0.0132  392 GLN A O   
2933 C CB  . GLN A 393 ? 1.1356 0.6675 0.6613 -0.0652 0.0000  0.0224  392 GLN A CB  
2934 C CG  . GLN A 393 ? 1.0992 0.6276 0.6192 -0.0643 0.0016  0.0229  392 GLN A CG  
2935 C CD  . GLN A 393 ? 1.1552 0.6920 0.6842 -0.0606 -0.0007 0.0322  392 GLN A CD  
2936 O OE1 . GLN A 393 ? 1.1504 0.6952 0.6907 -0.0575 -0.0025 0.0380  392 GLN A OE1 
2937 N NE2 . GLN A 393 ? 1.1366 0.6719 0.6610 -0.0607 -0.0003 0.0340  392 GLN A NE2 
2938 N N   . ALA A 394 ? 1.0842 0.6145 0.6227 -0.0618 0.0031  0.0154  393 ALA A N   
2939 C CA  . ALA A 394 ? 1.1844 0.7194 0.7289 -0.0633 0.0012  0.0160  393 ALA A CA  
2940 C C   . ALA A 394 ? 1.2499 0.7748 0.7863 -0.0673 0.0033  0.0078  393 ALA A C   
2941 O O   . ALA A 394 ? 1.3054 0.8306 0.8368 -0.0744 -0.0005 0.0073  393 ALA A O   
2942 C CB  . ALA A 394 ? 1.0903 0.6301 0.6488 -0.0548 0.0041  0.0185  393 ALA A CB  
2943 N N   . TYR A 395 ? 1.1722 0.6880 0.7071 -0.0629 0.0094  0.0017  394 TYR A N   
2944 C CA  . TYR A 395 ? 1.0484 0.5544 0.5771 -0.0653 0.0125  -0.0056 394 TYR A CA  
2945 C C   . TYR A 395 ? 1.2154 0.7153 0.7298 -0.0739 0.0099  -0.0087 394 TYR A C   
2946 O O   . TYR A 395 ? 1.3437 0.8391 0.8546 -0.0783 0.0092  -0.0119 394 TYR A O   
2947 C CB  . TYR A 395 ? 1.0721 0.5702 0.5998 -0.0599 0.0192  -0.0103 394 TYR A CB  
2948 C CG  . TYR A 395 ? 1.1720 0.6602 0.6944 -0.0611 0.0234  -0.0171 394 TYR A CG  
2949 C CD1 . TYR A 395 ? 1.3134 0.8020 0.8438 -0.0589 0.0254  -0.0184 394 TYR A CD1 
2950 C CD2 . TYR A 395 ? 1.1524 0.6311 0.6619 -0.0641 0.0259  -0.0217 394 TYR A CD2 
2951 C CE1 . TYR A 395 ? 1.2740 0.7536 0.8005 -0.0597 0.0296  -0.0238 394 TYR A CE1 
2952 C CE2 . TYR A 395 ? 1.2031 0.6723 0.7081 -0.0644 0.0305  -0.0274 394 TYR A CE2 
2953 C CZ  . TYR A 395 ? 1.2217 0.6914 0.7357 -0.0622 0.0323  -0.0283 394 TYR A CZ  
2954 O OH  . TYR A 395 ? 1.1657 0.6260 0.6762 -0.0621 0.0372  -0.0332 394 TYR A OH  
2955 N N   . MET A 396 ? 1.2515 0.7507 0.7569 -0.0765 0.0085  -0.0077 395 MET A N   
2956 C CA  . MET A 396 ? 1.1483 0.6418 0.6386 -0.0851 0.0059  -0.0107 395 MET A CA  
2957 C C   . MET A 396 ? 1.1560 0.6569 0.6467 -0.0925 -0.0015 -0.0063 395 MET A C   
2958 O O   . MET A 396 ? 1.2534 0.7477 0.7357 -0.0992 -0.0031 -0.0103 395 MET A O   
2959 C CB  . MET A 396 ? 1.0685 0.5617 0.5497 -0.0864 0.0057  -0.0096 395 MET A CB  
2960 C CG  . MET A 396 ? 1.2184 0.7128 0.6869 -0.0963 -0.0002 -0.0085 395 MET A CG  
2961 S SD  . MET A 396 ? 1.1676 0.6649 0.6260 -0.0989 -0.0018 -0.0054 395 MET A SD  
2962 C CE  . MET A 396 ? 0.9927 0.4791 0.4473 -0.0917 0.0074  -0.0118 395 MET A CE  
2963 N N   . ALA A 397 ? 1.1012 0.6158 0.6020 -0.0912 -0.0060 0.0025  396 ALA A N   
2964 C CA  . ALA A 397 ? 1.2319 0.7559 0.7326 -0.0990 -0.0138 0.0085  396 ALA A CA  
2965 C C   . ALA A 397 ? 1.2822 0.8072 0.7887 -0.1013 -0.0155 0.0081  396 ALA A C   
2966 O O   . ALA A 397 ? 1.3069 0.8336 0.8076 -0.1105 -0.0214 0.0096  396 ALA A O   
2967 C CB  . ALA A 397 ? 1.1337 0.6730 0.6457 -0.0959 -0.0174 0.0191  396 ALA A CB  
2968 N N   . THR A 398 ? 1.4828 1.0071 1.0003 -0.0937 -0.0109 0.0064  397 THR A N   
2969 C CA  . THR A 398 ? 1.4922 1.0170 1.0149 -0.0959 -0.0121 0.0058  397 THR A CA  
2970 C C   . THR A 398 ? 1.4894 0.9992 0.9982 -0.1027 -0.0111 -0.0026 397 THR A C   
2971 O O   . THR A 398 ? 1.5110 1.0204 1.0161 -0.1108 -0.0160 -0.0020 397 THR A O   
2972 C CB  . THR A 398 ? 1.4768 1.0037 1.0132 -0.0863 -0.0068 0.0054  397 THR A CB  
2973 O OG1 . THR A 398 ? 1.4727 0.9860 1.0038 -0.0835 -0.0003 -0.0032 397 THR A OG1 
2974 C CG2 . THR A 398 ? 1.4498 0.9857 0.9961 -0.0781 -0.0053 0.0108  397 THR A CG2 
2975 N N   . TYR A 399 ? 1.3199 0.8168 0.8208 -0.0994 -0.0046 -0.0102 398 TYR A N   
2976 C CA  . TYR A 399 ? 1.3720 0.8531 0.8598 -0.1044 -0.0021 -0.0185 398 TYR A CA  
2977 C C   . TYR A 399 ? 1.3307 0.8057 0.8007 -0.1141 -0.0060 -0.0206 398 TYR A C   
2978 O O   . TYR A 399 ? 1.3574 0.8189 0.8150 -0.1198 -0.0050 -0.0272 398 TYR A O   
2979 C CB  . TYR A 399 ? 1.3585 0.8293 0.8451 -0.0969 0.0068  -0.0249 398 TYR A CB  
2980 C CG  . TYR A 399 ? 1.4276 0.9022 0.9295 -0.0893 0.0105  -0.0239 398 TYR A CG  
2981 C CD1 . TYR A 399 ? 1.3336 0.8149 0.8454 -0.0908 0.0071  -0.0205 398 TYR A CD1 
2982 C CD2 . TYR A 399 ? 1.3822 0.8548 0.8887 -0.0811 0.0171  -0.0259 398 TYR A CD2 
2983 C CE1 . TYR A 399 ? 1.3618 0.8474 0.8871 -0.0842 0.0105  -0.0195 398 TYR A CE1 
2984 C CE2 . TYR A 399 ? 1.3811 0.8577 0.9007 -0.0749 0.0202  -0.0249 398 TYR A CE2 
2985 C CZ  . TYR A 399 ? 1.3981 0.8811 0.9268 -0.0764 0.0170  -0.0219 398 TYR A CZ  
2986 O OH  . TYR A 399 ? 1.2466 0.7344 0.7879 -0.0705 0.0201  -0.0208 398 TYR A OH  
2987 N N   . ILE A 400 ? 1.2324 0.7168 0.7004 -0.1162 -0.0103 -0.0151 399 ILE A N   
2988 C CA  . ILE A 400 ? 1.2273 0.7100 0.6801 -0.1272 -0.0162 -0.0150 399 ILE A CA  
2989 C C   . ILE A 400 ? 1.2484 0.7365 0.7035 -0.1357 -0.0237 -0.0110 399 ILE A C   
2990 O O   . ILE A 400 ? 1.2439 0.7214 0.6851 -0.1451 -0.0261 -0.0158 399 ILE A O   
2991 C CB  . ILE A 400 ? 1.1929 0.6866 0.6450 -0.1273 -0.0194 -0.0086 399 ILE A CB  
2992 C CG1 . ILE A 400 ? 1.1844 0.6699 0.6284 -0.1224 -0.0128 -0.0136 399 ILE A CG1 
2993 C CG2 . ILE A 400 ? 1.0755 0.5731 0.5159 -0.1397 -0.0277 -0.0053 399 ILE A CG2 
2994 C CD1 . ILE A 400 ? 1.1284 0.6235 0.5700 -0.1236 -0.0160 -0.0075 399 ILE A CD1 
2995 N N   . VAL A 401 ? 1.1406 0.6451 0.6131 -0.1325 -0.0273 -0.0019 400 VAL A N   
2996 C CA  . VAL A 401 ? 1.2523 0.7645 0.7295 -0.1398 -0.0344 0.0034  400 VAL A CA  
2997 C C   . VAL A 401 ? 1.2680 0.7691 0.7460 -0.1401 -0.0316 -0.0027 400 VAL A C   
2998 O O   . VAL A 401 ? 1.2281 0.7256 0.7001 -0.1498 -0.0367 -0.0031 400 VAL A O   
2999 C CB  . VAL A 401 ? 1.1744 0.7077 0.6710 -0.1346 -0.0377 0.0151  400 VAL A CB  
3000 C CG1 . VAL A 401 ? 1.1971 0.7407 0.6992 -0.1426 -0.0456 0.0222  400 VAL A CG1 
3001 C CG2 . VAL A 401 ? 1.0586 0.6018 0.5551 -0.1335 -0.0398 0.0214  400 VAL A CG2 
3002 N N   . TYR A 402 ? 1.2097 0.7053 0.6951 -0.1300 -0.0237 -0.0071 401 TYR A N   
3003 C CA  . TYR A 402 ? 1.2754 0.7622 0.7638 -0.1294 -0.0207 -0.0117 401 TYR A CA  
3004 C C   . TYR A 402 ? 1.2768 0.7434 0.7466 -0.1368 -0.0191 -0.0210 401 TYR A C   
3005 O O   . TYR A 402 ? 1.2196 0.6801 0.6867 -0.1437 -0.0221 -0.0224 401 TYR A O   
3006 C CB  . TYR A 402 ? 1.2372 0.7235 0.7372 -0.1172 -0.0125 -0.0139 401 TYR A CB  
3007 C CG  . TYR A 402 ? 1.2112 0.6923 0.7179 -0.1158 -0.0098 -0.0165 401 TYR A CG  
3008 C CD1 . TYR A 402 ? 1.1380 0.6283 0.6541 -0.1197 -0.0152 -0.0108 401 TYR A CD1 
3009 C CD2 . TYR A 402 ? 1.1342 0.6021 0.6384 -0.1107 -0.0019 -0.0238 401 TYR A CD2 
3010 C CE1 . TYR A 402 ? 1.0243 0.5104 0.5470 -0.1186 -0.0130 -0.0126 401 TYR A CE1 
3011 C CE2 . TYR A 402 ? 1.0699 0.5336 0.5809 -0.1095 0.0006  -0.0254 401 TYR A CE2 
3012 C CZ  . TYR A 402 ? 1.0763 0.5489 0.5964 -0.1135 -0.0051 -0.0199 401 TYR A CZ  
3013 O OH  . TYR A 402 ? 1.1452 0.6143 0.6726 -0.1125 -0.0028 -0.0210 401 TYR A OH  
3014 N N   . PHE A 403 ? 1.2349 0.6903 0.6914 -0.1354 -0.0143 -0.0274 402 PHE A N   
3015 C CA  . PHE A 403 ? 1.3090 0.7443 0.7462 -0.1419 -0.0120 -0.0366 402 PHE A CA  
3016 C C   . PHE A 403 ? 1.2787 0.7127 0.7033 -0.1558 -0.0208 -0.0354 402 PHE A C   
3017 O O   . PHE A 403 ? 1.2547 0.6748 0.6697 -0.1630 -0.0217 -0.0405 402 PHE A O   
3018 C CB  . PHE A 403 ? 1.2294 0.6558 0.6547 -0.1379 -0.0055 -0.0424 402 PHE A CB  
3019 C CG  . PHE A 403 ? 1.3231 0.7274 0.7307 -0.1408 0.0001  -0.0527 402 PHE A CG  
3020 C CD1 . PHE A 403 ? 1.3040 0.6978 0.7151 -0.1323 0.0093  -0.0580 402 PHE A CD1 
3021 C CD2 . PHE A 403 ? 1.4227 0.8166 0.8101 -0.1519 -0.0036 -0.0569 402 PHE A CD2 
3022 C CE1 . PHE A 403 ? 1.3391 0.7122 0.7344 -0.1341 0.0153  -0.0671 402 PHE A CE1 
3023 C CE2 . PHE A 403 ? 1.4770 0.8489 0.8471 -0.1541 0.0023  -0.0669 402 PHE A CE2 
3024 C CZ  . PHE A 403 ? 1.4123 0.7737 0.7867 -0.1447 0.0121  -0.0719 402 PHE A CZ  
3025 N N   . SER A 404 ? 1.2110 0.6592 0.6354 -0.1601 -0.0275 -0.0283 403 SER A N   
3026 C CA  . SER A 404 ? 1.1991 0.6487 0.6122 -0.1741 -0.0369 -0.0256 403 SER A CA  
3027 C C   . SER A 404 ? 1.2946 0.7495 0.7176 -0.1792 -0.0426 -0.0209 403 SER A C   
3028 O O   . SER A 404 ? 1.4691 0.9133 0.8796 -0.1905 -0.0470 -0.0241 403 SER A O   
3029 C CB  . SER A 404 ? 1.1877 0.6553 0.6028 -0.1763 -0.0429 -0.0167 403 SER A CB  
3030 O OG  . SER A 404 ? 1.2191 0.6842 0.6287 -0.1700 -0.0373 -0.0197 403 SER A OG  
3031 N N   . LEU A 405 ? 1.2728 0.7438 0.7176 -0.1712 -0.0427 -0.0132 404 LEU A N   
3032 C CA  . LEU A 405 ? 1.3006 0.7790 0.7565 -0.1754 -0.0480 -0.0076 404 LEU A CA  
3033 C C   . LEU A 405 ? 1.3620 0.8221 0.8143 -0.1759 -0.0436 -0.0158 404 LEU A C   
3034 O O   . LEU A 405 ? 1.4111 0.8682 0.8615 -0.1851 -0.0491 -0.0147 404 LEU A O   
3035 C CB  . LEU A 405 ? 1.2681 0.7677 0.7477 -0.1654 -0.0478 0.0020  404 LEU A CB  
3036 C CG  . LEU A 405 ? 1.2812 0.8033 0.7697 -0.1685 -0.0558 0.0146  404 LEU A CG  
3037 C CD1 . LEU A 405 ? 1.2536 0.7837 0.7462 -0.1787 -0.0643 0.0214  404 LEU A CD1 
3038 C CD2 . LEU A 405 ? 1.1430 0.6655 0.6176 -0.1742 -0.0590 0.0152  404 LEU A CD2 
3039 N N   . CYS A 406 ? 1.3909 0.8391 0.8428 -0.1662 -0.0338 -0.0235 405 CYS A N   
3040 C CA  . CYS A 406 ? 1.4464 0.8771 0.8958 -0.1657 -0.0287 -0.0308 405 CYS A CA  
3041 C C   . CYS A 406 ? 1.4889 0.8989 0.9158 -0.1775 -0.0307 -0.0385 405 CYS A C   
3042 O O   . CYS A 406 ? 1.5826 0.9823 1.0077 -0.1833 -0.0322 -0.0407 405 CYS A O   
3043 C CB  . CYS A 406 ? 1.4454 0.8688 0.8986 -0.1530 -0.0178 -0.0365 405 CYS A CB  
3044 S SG  . CYS A 406 ? 1.5044 0.9462 0.9839 -0.1400 -0.0144 -0.0296 405 CYS A SG  
3045 N N   . CYS A 407 ? 1.4385 0.8415 0.8477 -0.1815 -0.0305 -0.0428 406 CYS A N   
3046 C CA  . CYS A 407 ? 1.4770 0.8597 0.8625 -0.1934 -0.0324 -0.0507 406 CYS A CA  
3047 C C   . CYS A 407 ? 1.5010 0.8900 0.8835 -0.2078 -0.0442 -0.0447 406 CYS A C   
3048 O O   . CYS A 407 ? 1.5037 0.8756 0.8728 -0.2178 -0.0465 -0.0500 406 CYS A O   
3049 C CB  . CYS A 407 ? 1.4276 0.8037 0.7950 -0.1942 -0.0297 -0.0559 406 CYS A CB  
3050 S SG  . CYS A 407 ? 1.3867 0.7531 0.7546 -0.1788 -0.0157 -0.0633 406 CYS A SG  
3051 N N   . GLY A 408 ? 1.5529 0.9663 0.9479 -0.2090 -0.0517 -0.0333 407 GLY A N   
3052 C CA  . GLY A 408 ? 1.5425 0.9649 0.9363 -0.2227 -0.0633 -0.0259 407 GLY A CA  
3053 C C   . GLY A 408 ? 1.4875 0.9091 0.8924 -0.2251 -0.0657 -0.0234 407 GLY A C   
3054 O O   . GLY A 408 ? 1.5525 0.9640 0.9463 -0.2382 -0.0719 -0.0248 407 GLY A O   
3055 N N   . VAL A 409 ? 1.5480 0.9801 0.9747 -0.2128 -0.0610 -0.0195 408 VAL A N   
3056 C CA  . VAL A 409 ? 1.5722 1.0042 1.0105 -0.2140 -0.0626 -0.0169 408 VAL A CA  
3057 C C   . VAL A 409 ? 1.5272 0.9310 0.9524 -0.2163 -0.0570 -0.0284 408 VAL A C   
3058 O O   . VAL A 409 ? 1.5385 0.9367 0.9663 -0.2224 -0.0602 -0.0274 408 VAL A O   
3059 C CB  . VAL A 409 ? 1.5156 0.9655 0.9793 -0.2001 -0.0582 -0.0104 408 VAL A CB  
3060 C CG1 . VAL A 409 ? 1.4352 0.9107 0.9109 -0.1963 -0.0622 0.0002  408 VAL A CG1 
3061 C CG2 . VAL A 409 ? 1.4023 0.8402 0.8672 -0.1870 -0.0464 -0.0188 408 VAL A CG2 
3062 N N   . PHE A 410 ? 1.5503 0.9362 0.9616 -0.2113 -0.0484 -0.0389 409 PHE A N   
3063 C CA  . PHE A 410 ? 1.5925 0.9503 0.9901 -0.2131 -0.0423 -0.0499 409 PHE A CA  
3064 C C   . PHE A 410 ? 1.6105 0.9522 0.9861 -0.2300 -0.0495 -0.0539 409 PHE A C   
3065 O O   . PHE A 410 ? 1.7039 1.0311 1.0762 -0.2365 -0.0508 -0.0566 409 PHE A O   
3066 C CB  . PHE A 410 ? 1.6128 0.9571 1.0014 -0.2030 -0.0310 -0.0591 409 PHE A CB  
3067 C CG  . PHE A 410 ? 1.7057 1.0235 1.0853 -0.2010 -0.0225 -0.0692 409 PHE A CG  
3068 C CD1 . PHE A 410 ? 1.6992 1.0167 1.0957 -0.1921 -0.0168 -0.0680 409 PHE A CD1 
3069 C CD2 . PHE A 410 ? 1.7211 1.0141 1.0750 -0.2079 -0.0199 -0.0795 409 PHE A CD2 
3070 C CE1 . PHE A 410 ? 1.7173 1.0107 1.1067 -0.1897 -0.0086 -0.0764 409 PHE A CE1 
3071 C CE2 . PHE A 410 ? 1.7595 1.0272 1.1053 -0.2052 -0.0112 -0.0886 409 PHE A CE2 
3072 C CZ  . PHE A 410 ? 1.7339 1.0020 1.0981 -0.1959 -0.0056 -0.0866 409 PHE A CZ  
3073 N N   . LEU A 411 ? 1.5305 0.8745 0.8905 -0.2380 -0.0545 -0.0542 410 LEU A N   
3074 C CA  . LEU A 411 ? 1.5129 0.8427 0.8505 -0.2554 -0.0622 -0.0577 410 LEU A CA  
3075 C C   . LEU A 411 ? 1.6213 0.9651 0.9688 -0.2665 -0.0741 -0.0473 410 LEU A C   
3076 O O   . LEU A 411 ? 1.6627 0.9911 0.9956 -0.2806 -0.0798 -0.0504 410 LEU A O   
3077 C CB  . LEU A 411 ? 1.4269 0.7592 0.7468 -0.2612 -0.0650 -0.0591 410 LEU A CB  
3078 C CG  . LEU A 411 ? 1.4901 0.8082 0.7975 -0.2518 -0.0538 -0.0694 410 LEU A CG  
3079 C CD1 . LEU A 411 ? 1.4508 0.7684 0.7368 -0.2609 -0.0579 -0.0714 410 LEU A CD1 
3080 C CD2 . LEU A 411 ? 1.6153 0.9028 0.9105 -0.2495 -0.0444 -0.0819 410 LEU A CD2 
3081 N N   . LEU A 412 ? 1.5745 0.9470 0.9462 -0.2607 -0.0779 -0.0347 411 LEU A N   
3082 C CA  . LEU A 412 ? 1.6171 1.0047 1.0015 -0.2692 -0.0881 -0.0238 411 LEU A CA  
3083 C C   . LEU A 412 ? 1.6194 0.9947 1.0118 -0.2674 -0.0849 -0.0264 411 LEU A C   
3084 O O   . LEU A 412 ? 1.6821 1.0494 1.0689 -0.2803 -0.0920 -0.0253 411 LEU A O   
3085 C CB  . LEU A 412 ? 1.5429 0.9640 0.9517 -0.2614 -0.0913 -0.0100 411 LEU A CB  
3086 C CG  . LEU A 412 ? 1.3985 0.8400 0.8055 -0.2712 -0.1019 0.0002  411 LEU A CG  
3087 C CD1 . LEU A 412 ? 1.3244 0.7978 0.7583 -0.2626 -0.1043 0.0146  411 LEU A CD1 
3088 C CD2 . LEU A 412 ? 1.5534 0.9884 0.9465 -0.2909 -0.1130 0.0021  411 LEU A CD2 
3089 N N   . TRP A 413 ? 1.5943 0.9680 0.9999 -0.2518 -0.0744 -0.0295 412 TRP A N   
3090 C CA  . TRP A 413 ? 1.5700 0.9322 0.9840 -0.2488 -0.0703 -0.0318 412 TRP A CA  
3091 C C   . TRP A 413 ? 1.5857 0.9134 0.9767 -0.2558 -0.0666 -0.0446 412 TRP A C   
3092 O O   . TRP A 413 ? 1.5397 0.8551 0.9327 -0.2600 -0.0671 -0.0456 412 TRP A O   
3093 C CB  . TRP A 413 ? 1.5056 0.8762 0.9387 -0.2305 -0.0601 -0.0314 412 TRP A CB  
3094 C CG  . TRP A 413 ? 1.6514 1.0060 1.0899 -0.2246 -0.0524 -0.0365 412 TRP A CG  
3095 C CD1 . TRP A 413 ? 1.6399 1.0055 1.0993 -0.2203 -0.0526 -0.0297 412 TRP A CD1 
3096 C CD2 . TRP A 413 ? 1.6843 1.0106 1.1085 -0.2214 -0.0428 -0.0487 412 TRP A CD2 
3097 N NE1 . TRP A 413 ? 1.6161 0.9620 1.0752 -0.2152 -0.0442 -0.0366 412 TRP A NE1 
3098 C CE2 . TRP A 413 ? 1.5828 0.9042 1.0207 -0.2155 -0.0379 -0.0482 412 TRP A CE2 
3099 C CE3 . TRP A 413 ? 1.6444 0.9493 1.0455 -0.2228 -0.0377 -0.0597 412 TRP A CE3 
3100 C CZ2 . TRP A 413 ? 1.5305 0.8266 0.9605 -0.2107 -0.0280 -0.0577 412 TRP A CZ2 
3101 C CZ3 . TRP A 413 ? 1.6513 0.9307 1.0440 -0.2178 -0.0275 -0.0695 412 TRP A CZ3 
3102 C CH2 . TRP A 413 ? 1.6323 0.9075 1.0399 -0.2116 -0.0227 -0.0683 412 TRP A CH2 
3103 N N   . ARG A 414 ? 1.5994 0.9112 0.9686 -0.2571 -0.0626 -0.0541 413 ARG A N   
3104 C CA  . ARG A 414 ? 1.7325 1.0104 1.0772 -0.2644 -0.0589 -0.0667 413 ARG A CA  
3105 C C   . ARG A 414 ? 1.7870 1.0568 1.1171 -0.2841 -0.0706 -0.0656 413 ARG A C   
3106 O O   . ARG A 414 ? 1.7171 0.9603 1.0338 -0.2912 -0.0693 -0.0732 413 ARG A O   
3107 C CB  . ARG A 414 ? 1.6812 0.9461 1.0060 -0.2607 -0.0516 -0.0766 413 ARG A CB  
3108 C CG  . ARG A 414 ? 1.6775 0.9063 0.9788 -0.2634 -0.0439 -0.0907 413 ARG A CG  
3109 C CD  . ARG A 414 ? 1.7771 0.9958 1.0580 -0.2607 -0.0375 -0.0995 413 ARG A CD  
3110 N NE  . ARG A 414 ? 1.9647 1.1910 1.2300 -0.2740 -0.0475 -0.0975 413 ARG A NE  
3111 C CZ  . ARG A 414 ? 1.9720 1.1778 1.2080 -0.2835 -0.0472 -0.1071 413 ARG A CZ  
3112 N NH1 . ARG A 414 ? 1.8169 0.9966 1.0386 -0.2793 -0.0365 -0.1186 413 ARG A NH1 
3113 N NH2 . ARG A 414 ? 1.9011 1.1177 1.1252 -0.2960 -0.0572 -0.1034 413 ARG A NH2 
3114 N N   . ARG A 415 ? 1.8398 1.1318 1.1720 -0.2934 -0.0820 -0.0559 414 ARG A N   
3115 C CA  . ARG A 415 ? 1.8750 1.1639 1.1953 -0.3131 -0.0946 -0.0525 414 ARG A CA  
3116 C C   . ARG A 415 ? 1.9911 1.3005 1.3345 -0.3164 -0.1029 -0.0393 414 ARG A C   
3117 O O   . ARG A 415 ? 2.0547 1.3737 1.3949 -0.3316 -0.1153 -0.0315 414 ARG A O   
3118 C CB  . ARG A 415 ? 1.8647 1.1654 1.1714 -0.3229 -0.1025 -0.0494 414 ARG A CB  
3119 C CG  . ARG A 415 ? 1.8820 1.1632 1.1639 -0.3215 -0.0953 -0.0620 414 ARG A CG  
3120 C CD  . ARG A 415 ? 1.9494 1.2382 1.2136 -0.3359 -0.1051 -0.0593 414 ARG A CD  
3121 N NE  . ARG A 415 ? 1.9935 1.3188 1.2781 -0.3335 -0.1122 -0.0441 414 ARG A NE  
3122 C CZ  . ARG A 415 ? 1.9958 1.3408 1.2874 -0.3459 -0.1251 -0.0317 414 ARG A CZ  
3123 N NH1 . ARG A 415 ? 1.9745 1.3069 1.2543 -0.3627 -0.1335 -0.0322 414 ARG A NH1 
3124 N NH2 . ARG A 415 ? 2.0318 1.4097 1.3429 -0.3413 -0.1297 -0.0180 414 ARG A NH2 
3125 N N   . ARG A 416 ? 2.0793 1.3964 1.4458 -0.3026 -0.0965 -0.0361 415 ARG A N   
3126 C CA  . ARG A 416 ? 1.9678 1.3041 1.3574 -0.3038 -0.1027 -0.0239 415 ARG A CA  
3127 C C   . ARG A 416 ? 2.0361 1.4068 1.4390 -0.3074 -0.1128 -0.0092 415 ARG A C   
3128 O O   . ARG A 416 ? 2.1346 1.5132 1.5349 -0.3226 -0.1247 -0.0014 415 ARG A O   
3129 C CB  . ARG A 416 ? 1.9958 1.3118 1.3758 -0.3186 -0.1086 -0.0260 415 ARG A CB  
3130 C CG  . ARG A 416 ? 1.9957 1.2733 1.3564 -0.3179 -0.0994 -0.0415 415 ARG A CG  
3131 C CD  . ARG A 416 ? 1.9717 1.2247 1.3080 -0.3380 -0.1073 -0.0467 415 ARG A CD  
3132 N NE  . ARG A 416 ? 2.0272 1.2885 1.3477 -0.3516 -0.1173 -0.0442 415 ARG A NE  
3133 C CZ  . ARG A 416 ? 2.1013 1.3499 1.4023 -0.3717 -0.1276 -0.0450 415 ARG A CZ  
3134 N NH1 . ARG A 416 ? 2.0594 1.2849 1.3537 -0.3809 -0.1296 -0.0488 415 ARG A NH1 
3135 N NH2 . ARG A 416 ? 2.0148 1.2741 1.3027 -0.3832 -0.1365 -0.0417 415 ARG A NH2 
3136 N N   . ALA A 417 ? 1.8318 1.2230 1.2493 -0.2930 -0.1077 -0.0051 416 ALA A N   
3137 C CA  . ALA A 417 ? 1.7883 1.2128 1.2208 -0.2931 -0.1152 0.0091  416 ALA A CA  
3138 C C   . ALA A 417 ? 1.7114 1.1575 1.1692 -0.2912 -0.1194 0.0218  416 ALA A C   
3139 O O   . ALA A 417 ? 1.5964 1.0641 1.0620 -0.2998 -0.1297 0.0344  416 ALA A O   
3140 C CB  . ALA A 417 ? 1.7082 1.1453 1.1478 -0.2779 -0.1077 0.0089  416 ALA A CB  
3141 N N   . ALA B 2   ? 1.1961 0.8573 0.7297 0.3277  -0.1106 -0.1067 0   ALA B N   
3142 C CA  . ALA B 2   ? 1.1542 0.7851 0.6222 0.3629  -0.1158 -0.1006 0   ALA B CA  
3143 C C   . ALA B 2   ? 1.2723 0.8775 0.6548 0.3748  -0.1021 -0.0722 0   ALA B C   
3144 O O   . ALA B 2   ? 1.3042 0.8916 0.6242 0.4177  -0.1114 -0.0712 0   ALA B O   
3145 C CB  . ALA B 2   ? 1.1149 0.7743 0.6095 0.4100  -0.1518 -0.1421 0   ALA B CB  
3146 N N   . GLN B 3   ? 1.4920 1.0940 0.8725 0.3385  -0.0786 -0.0499 1   GLN B N   
3147 C CA  . GLN B 3   ? 1.5459 1.1169 0.8551 0.3390  -0.0541 -0.0193 1   GLN B CA  
3148 C C   . GLN B 3   ? 1.5573 1.0769 0.8340 0.3159  -0.0251 0.0116  1   GLN B C   
3149 O O   . GLN B 3   ? 1.6036 1.0814 0.8121 0.3361  -0.0096 0.0329  1   GLN B O   
3150 C CB  . GLN B 3   ? 1.5408 1.1379 0.8734 0.3126  -0.0444 -0.0166 1   GLN B CB  
3151 C CG  . GLN B 3   ? 1.6604 1.2246 0.9445 0.2946  -0.0092 0.0155  1   GLN B CG  
3152 C CD  . GLN B 3   ? 1.7079 1.2379 0.9071 0.3339  0.0031  0.0319  1   GLN B CD  
3153 O OE1 . GLN B 3   ? 1.5800 1.0599 0.7332 0.3301  0.0304  0.0593  1   GLN B OE1 
3154 N NE2 . GLN B 3   ? 1.7291 1.2836 0.9056 0.3739  -0.0163 0.0149  1   GLN B NE2 
3155 N N   . VAL B 4   ? 1.3310 0.8508 0.6544 0.2760  -0.0169 0.0138  2   VAL B N   
3156 C CA  . VAL B 4   ? 1.3432 0.8200 0.6482 0.2531  0.0064  0.0360  2   VAL B CA  
3157 C C   . VAL B 4   ? 1.2887 0.7676 0.6313 0.2497  -0.0060 0.0212  2   VAL B C   
3158 O O   . VAL B 4   ? 1.2070 0.7095 0.6038 0.2253  -0.0100 0.0095  2   VAL B O   
3159 C CB  . VAL B 4   ? 1.2613 0.7351 0.5835 0.2099  0.0285  0.0500  2   VAL B CB  
3160 C CG1 . VAL B 4   ? 1.1239 0.5599 0.4409 0.1866  0.0468  0.0644  2   VAL B CG1 
3161 C CG2 . VAL B 4   ? 1.3968 0.8647 0.6850 0.2127  0.0467  0.0643  2   VAL B CG2 
3162 N N   . GLN B 5   ? 1.2022 0.6542 0.5148 0.2758  -0.0104 0.0218  3   GLN B N   
3163 C CA  . GLN B 5   ? 1.1810 0.6331 0.5288 0.2754  -0.0200 0.0060  3   GLN B CA  
3164 C C   . GLN B 5   ? 1.3016 0.7133 0.6341 0.2493  0.0031  0.0264  3   GLN B C   
3165 O O   . GLN B 5   ? 1.3279 0.7008 0.6104 0.2503  0.0213  0.0502  3   GLN B O   
3166 C CB  . GLN B 5   ? 1.1133 0.5645 0.4449 0.3234  -0.0441 -0.0124 3   GLN B CB  
3167 C CG  . GLN B 5   ? 1.1567 0.6576 0.5296 0.3492  -0.0740 -0.0466 3   GLN B CG  
3168 C CD  . GLN B 5   ? 1.2463 0.7493 0.5636 0.3867  -0.0850 -0.0445 3   GLN B CD  
3169 O OE1 . GLN B 5   ? 1.2187 0.7131 0.5019 0.3730  -0.0661 -0.0213 3   GLN B OE1 
3170 N NE2 . GLN B 5   ? 1.2359 0.7510 0.5443 0.4365  -0.1158 -0.0711 3   GLN B NE2 
3171 N N   . LEU B 6   ? 1.1493 0.5687 0.5263 0.2267  0.0046  0.0162  4   LEU B N   
3172 C CA  . LEU B 6   ? 1.0465 0.4340 0.4156 0.2004  0.0241  0.0302  4   LEU B CA  
3173 C C   . LEU B 6   ? 1.0537 0.4309 0.4380 0.2111  0.0187  0.0169  4   LEU B C   
3174 O O   . LEU B 6   ? 1.0304 0.4357 0.4581 0.2216  0.0046  -0.0072 4   LEU B O   
3175 C CB  . LEU B 6   ? 1.0045 0.4067 0.4039 0.1634  0.0335  0.0315  4   LEU B CB  
3176 C CG  . LEU B 6   ? 1.0887 0.5094 0.4867 0.1526  0.0350  0.0383  4   LEU B CG  
3177 C CD1 . LEU B 6   ? 1.0503 0.4838 0.4762 0.1218  0.0395  0.0370  4   LEU B CD1 
3178 C CD2 . LEU B 6   ? 1.0293 0.4214 0.3838 0.1528  0.0508  0.0586  4   LEU B CD2 
3179 N N   . VAL B 7   ? 1.2313 0.5685 0.5864 0.2076  0.0315  0.0303  5   VAL B N   
3180 C CA  . VAL B 7   ? 1.3081 0.6315 0.6746 0.2174  0.0280  0.0183  5   VAL B CA  
3181 C C   . VAL B 7   ? 1.2916 0.5925 0.6600 0.1859  0.0474  0.0269  5   VAL B C   
3182 O O   . VAL B 7   ? 1.2589 0.5296 0.5971 0.1741  0.0621  0.0461  5   VAL B O   
3183 C CB  . VAL B 7   ? 1.2200 0.5123 0.5438 0.2549  0.0195  0.0230  5   VAL B CB  
3184 C CG1 . VAL B 7   ? 1.1711 0.4426 0.5052 0.2597  0.0193  0.0134  5   VAL B CG1 
3185 C CG2 . VAL B 7   ? 1.1638 0.4827 0.4888 0.2936  -0.0066 0.0052  5   VAL B CG2 
3186 N N   . GLU B 8   ? 1.3498 0.6650 0.7557 0.1736  0.0490  0.0109  6   GLU B N   
3187 C CA  . GLU B 8   ? 1.3581 0.6534 0.7627 0.1496  0.0647  0.0143  6   GLU B CA  
3188 C C   . GLU B 8   ? 1.3681 0.6320 0.7602 0.1633  0.0659  0.0120  6   GLU B C   
3189 O O   . GLU B 8   ? 1.4547 0.7141 0.8427 0.1929  0.0530  0.0052  6   GLU B O   
3190 C CB  . GLU B 8   ? 1.3712 0.6891 0.8120 0.1340  0.0704  0.0005  6   GLU B CB  
3191 C CG  . GLU B 8   ? 1.4311 0.7644 0.8733 0.1122  0.0753  0.0081  6   GLU B CG  
3192 C CD  . GLU B 8   ? 1.4091 0.7714 0.8660 0.1204  0.0638  0.0072  6   GLU B CD  
3193 O OE1 . GLU B 8   ? 1.3855 0.7708 0.8786 0.1336  0.0569  -0.0090 6   GLU B OE1 
3194 O OE2 . GLU B 8   ? 1.3947 0.7586 0.8328 0.1135  0.0620  0.0196  6   GLU B OE2 
3195 N N   . SER B 9   ? 1.2622 0.5042 0.6482 0.1439  0.0792  0.0152  7   SER B N   
3196 C CA  . SER B 9   ? 1.3729 0.5843 0.7516 0.1535  0.0817  0.0115  7   SER B CA  
3197 C C   . SER B 9   ? 1.2679 0.4694 0.6518 0.1290  0.0950  0.0069  7   SER B C   
3198 O O   . SER B 9   ? 1.1501 0.3534 0.5275 0.1073  0.1018  0.0135  7   SER B O   
3199 C CB  . SER B 9   ? 1.3649 0.5380 0.7066 0.1681  0.0835  0.0304  7   SER B CB  
3200 O OG  . SER B 9   ? 1.4567 0.6200 0.7831 0.1480  0.0962  0.0480  7   SER B OG  
3201 N N   . GLY B 10  ? 1.2195 0.4119 0.6157 0.1351  0.0967  -0.0075 8   GLY B N   
3202 C CA  . GLY B 10  ? 1.2334 0.4157 0.6310 0.1171  0.1081  -0.0153 8   GLY B CA  
3203 C C   . GLY B 10  ? 1.3056 0.5131 0.7228 0.1095  0.1154  -0.0298 8   GLY B C   
3204 O O   . GLY B 10  ? 1.4035 0.6354 0.8454 0.1180  0.1135  -0.0373 8   GLY B O   
3205 N N   . GLY B 11  ? 1.2316 0.4311 0.6381 0.0945  0.1254  -0.0349 9   GLY B N   
3206 C CA  . GLY B 11  ? 1.2863 0.4999 0.6985 0.0886  0.1383  -0.0448 9   GLY B CA  
3207 C C   . GLY B 11  ? 1.2744 0.4893 0.7126 0.0992  0.1475  -0.0627 9   GLY B C   
3208 O O   . GLY B 11  ? 1.2467 0.4566 0.7031 0.1142  0.1388  -0.0697 9   GLY B O   
3209 N N   . GLY B 12  ? 1.2042 0.4240 0.6427 0.0933  0.1666  -0.0708 10  GLY B N   
3210 C CA  . GLY B 12  ? 1.1822 0.4048 0.6505 0.1007  0.1819  -0.0900 10  GLY B CA  
3211 C C   . GLY B 12  ? 1.2955 0.5074 0.7396 0.0937  0.2050  -0.0960 10  GLY B C   
3212 O O   . GLY B 12  ? 1.4065 0.6193 0.8258 0.0865  0.2178  -0.0862 10  GLY B O   
3213 N N   . LEU B 13  ? 1.2131 0.4126 0.6598 0.0984  0.2100  -0.1120 11  LEU B N   
3214 C CA  . LEU B 13  ? 1.3763 0.5643 0.7950 0.0958  0.2319  -0.1205 11  LEU B CA  
3215 C C   . LEU B 13  ? 1.3944 0.5645 0.7676 0.0920  0.2176  -0.1191 11  LEU B C   
3216 O O   . LEU B 13  ? 1.4191 0.5808 0.7982 0.0918  0.1965  -0.1190 11  LEU B O   
3217 C CB  . LEU B 13  ? 1.4238 0.6115 0.8762 0.1037  0.2474  -0.1437 11  LEU B CB  
3218 C CG  . LEU B 13  ? 1.4207 0.6172 0.8929 0.1032  0.2845  -0.1515 11  LEU B CG  
3219 C CD1 . LEU B 13  ? 1.2866 0.4947 0.7969 0.1080  0.2958  -0.1742 11  LEU B CD1 
3220 C CD2 . LEU B 13  ? 1.3108 0.4928 0.7228 0.0983  0.3059  -0.1374 11  LEU B CD2 
3221 N N   . VAL B 14  ? 1.4058 0.5682 0.7342 0.0910  0.2300  -0.1193 12  VAL B N   
3222 C CA  . VAL B 14  ? 1.3245 0.4741 0.6133 0.0902  0.2142  -0.1249 12  VAL B CA  
3223 C C   . VAL B 14  ? 1.4663 0.6061 0.7047 0.0982  0.2334  -0.1324 12  VAL B C   
3224 O O   . VAL B 14  ? 1.4733 0.6132 0.6935 0.1010  0.2566  -0.1209 12  VAL B O   
3225 C CB  . VAL B 14  ? 1.3036 0.4583 0.5826 0.0824  0.1917  -0.1099 12  VAL B CB  
3226 C CG1 . VAL B 14  ? 1.2924 0.4575 0.5582 0.0811  0.2013  -0.0918 12  VAL B CG1 
3227 C CG2 . VAL B 14  ? 1.3314 0.4767 0.5785 0.0824  0.1750  -0.1223 12  VAL B CG2 
3228 N N   . GLN B 15  ? 1.5274 0.6561 0.7425 0.1040  0.2252  -0.1520 13  GLN B N   
3229 C CA  . GLN B 15  ? 1.4594 0.5811 0.6197 0.1164  0.2385  -0.1599 13  GLN B CA  
3230 C C   . GLN B 15  ? 1.4787 0.5974 0.5878 0.1213  0.2210  -0.1533 13  GLN B C   
3231 O O   . GLN B 15  ? 1.4530 0.5754 0.5746 0.1135  0.1945  -0.1522 13  GLN B O   
3232 C CB  . GLN B 15  ? 1.4953 0.6194 0.6621 0.1222  0.2308  -0.1853 13  GLN B CB  
3233 C CG  . GLN B 15  ? 1.4548 0.5827 0.6838 0.1157  0.2293  -0.1950 13  GLN B CG  
3234 C CD  . GLN B 15  ? 1.6276 0.7588 0.8634 0.1232  0.2307  -0.2201 13  GLN B CD  
3235 O OE1 . GLN B 15  ? 1.7177 0.8528 0.9357 0.1316  0.2552  -0.2254 13  GLN B OE1 
3236 N NE2 . GLN B 15  ? 1.4780 0.6065 0.7420 0.1201  0.2066  -0.2358 13  GLN B NE2 
3237 N N   . ALA B 16  ? 1.5262 0.6417 0.5829 0.1354  0.2355  -0.1475 14  ALA B N   
3238 C CA  . ALA B 16  ? 1.5521 0.6672 0.5593 0.1456  0.2158  -0.1416 14  ALA B CA  
3239 C C   . ALA B 16  ? 1.5584 0.6823 0.5681 0.1488  0.1770  -0.1686 14  ALA B C   
3240 O O   . ALA B 16  ? 1.5777 0.7056 0.5960 0.1540  0.1721  -0.1920 14  ALA B O   
3241 C CB  . ALA B 16  ? 1.6142 0.7210 0.5645 0.1648  0.2380  -0.1302 14  ALA B CB  
3242 N N   . GLY B 17  ? 1.5424 0.6708 0.5511 0.1455  0.1500  -0.1682 15  GLY B N   
3243 C CA  . GLY B 17  ? 1.5436 0.6817 0.5705 0.1454  0.1145  -0.1968 15  GLY B CA  
3244 C C   . GLY B 17  ? 1.4970 0.6318 0.5874 0.1237  0.1064  -0.2046 15  GLY B C   
3245 O O   . GLY B 17  ? 1.4907 0.6306 0.6069 0.1182  0.0803  -0.2235 15  GLY B O   
3246 N N   . GLY B 18  ? 1.4767 0.6048 0.5993 0.1122  0.1284  -0.1900 16  GLY B N   
3247 C CA  . GLY B 18  ? 1.4541 0.5847 0.6418 0.0943  0.1217  -0.1883 16  GLY B CA  
3248 C C   . GLY B 18  ? 1.4689 0.6100 0.6820 0.0805  0.1151  -0.1648 16  GLY B C   
3249 O O   . GLY B 18  ? 1.5482 0.6972 0.7353 0.0829  0.1160  -0.1491 16  GLY B O   
3250 N N   . SER B 19  ? 1.5046 0.6428 0.7678 0.0671  0.1104  -0.1618 17  SER B N   
3251 C CA  . SER B 19  ? 1.3960 0.5419 0.6849 0.0545  0.1046  -0.1427 17  SER B CA  
3252 C C   . SER B 19  ? 1.2882 0.4328 0.5964 0.0520  0.1184  -0.1178 17  SER B C   
3253 O O   . SER B 19  ? 1.2927 0.4292 0.6070 0.0582  0.1297  -0.1189 17  SER B O   
3254 C CB  . SER B 19  ? 1.4627 0.6024 0.7920 0.0431  0.0924  -0.1570 17  SER B CB  
3255 O OG  . SER B 19  ? 1.5613 0.7136 0.8844 0.0431  0.0739  -0.1752 17  SER B OG  
3256 N N   . LEU B 20  ? 1.2885 0.4426 0.6079 0.0448  0.1151  -0.0985 18  LEU B N   
3257 C CA  . LEU B 20  ? 1.2335 0.3893 0.5690 0.0462  0.1228  -0.0774 18  LEU B CA  
3258 C C   . LEU B 20  ? 1.2191 0.3823 0.5666 0.0376  0.1163  -0.0619 18  LEU B C   
3259 O O   . LEU B 20  ? 1.2206 0.3982 0.5589 0.0323  0.1084  -0.0626 18  LEU B O   
3260 C CB  . LEU B 20  ? 1.2467 0.4160 0.5694 0.0545  0.1334  -0.0705 18  LEU B CB  
3261 C CG  . LEU B 20  ? 1.2938 0.4673 0.6402 0.0614  0.1390  -0.0597 18  LEU B CG  
3262 C CD1 . LEU B 20  ? 1.4501 0.6034 0.8147 0.0660  0.1363  -0.0623 18  LEU B CD1 
3263 C CD2 . LEU B 20  ? 1.3218 0.5041 0.6699 0.0690  0.1545  -0.0653 18  LEU B CD2 
3264 N N   . GLY B 21  ? 1.3079 0.4595 0.6728 0.0387  0.1200  -0.0483 19  GLY B N   
3265 C CA  . GLY B 21  ? 1.2489 0.4041 0.6224 0.0328  0.1186  -0.0320 19  GLY B CA  
3266 C C   . GLY B 21  ? 1.2648 0.4338 0.6337 0.0436  0.1189  -0.0152 19  GLY B C   
3267 O O   . GLY B 21  ? 1.3247 0.4912 0.6945 0.0569  0.1209  -0.0156 19  GLY B O   
3268 N N   . LEU B 22  ? 1.2163 0.4022 0.5854 0.0388  0.1151  -0.0044 20  LEU B N   
3269 C CA  . LEU B 22  ? 1.1677 0.3703 0.5363 0.0497  0.1126  0.0081  20  LEU B CA  
3270 C C   . LEU B 22  ? 1.2128 0.4111 0.5814 0.0487  0.1140  0.0234  20  LEU B C   
3271 O O   . LEU B 22  ? 1.1812 0.3771 0.5561 0.0338  0.1167  0.0232  20  LEU B O   
3272 C CB  . LEU B 22  ? 1.1545 0.3856 0.5222 0.0471  0.1082  0.0053  20  LEU B CB  
3273 C CG  . LEU B 22  ? 1.1666 0.4019 0.5342 0.0533  0.1140  -0.0045 20  LEU B CG  
3274 C CD1 . LEU B 22  ? 1.1291 0.3878 0.5010 0.0537  0.1147  -0.0013 20  LEU B CD1 
3275 C CD2 . LEU B 22  ? 1.1099 0.3370 0.4908 0.0678  0.1169  -0.0081 20  LEU B CD2 
3276 N N   . SER B 23  ? 1.2107 0.4087 0.5732 0.0664  0.1124  0.0342  21  SER B N   
3277 C CA  . SER B 23  ? 1.3122 0.5021 0.6646 0.0710  0.1169  0.0508  21  SER B CA  
3278 C C   . SER B 23  ? 1.1619 0.3774 0.5102 0.0887  0.1061  0.0545  21  SER B C   
3279 O O   . SER B 23  ? 1.1172 0.3440 0.4720 0.1045  0.0967  0.0453  21  SER B O   
3280 C CB  . SER B 23  ? 1.2819 0.4287 0.6190 0.0823  0.1283  0.0622  21  SER B CB  
3281 O OG  . SER B 23  ? 1.3471 0.4842 0.6791 0.1021  0.1212  0.0560  21  SER B OG  
3282 N N   . CYS B 24  ? 1.2318 0.4579 0.5751 0.0863  0.1076  0.0646  22  CYS B N   
3283 C CA  . CYS B 24  ? 1.2742 0.5269 0.6154 0.1034  0.0961  0.0657  22  CYS B CA  
3284 C C   . CYS B 24  ? 1.3377 0.5734 0.6513 0.1157  0.1048  0.0833  22  CYS B C   
3285 O O   . CYS B 24  ? 1.3572 0.5843 0.6710 0.0982  0.1197  0.0922  22  CYS B O   
3286 C CB  . CYS B 24  ? 1.2174 0.5077 0.5814 0.0881  0.0886  0.0577  22  CYS B CB  
3287 S SG  . CYS B 24  ? 1.4495 0.7769 0.8240 0.1079  0.0727  0.0528  22  CYS B SG  
3288 N N   . ALA B 25  ? 1.1782 0.4086 0.4685 0.1478  0.0963  0.0865  23  ALA B N   
3289 C CA  . ALA B 25  ? 1.2913 0.4988 0.5410 0.1678  0.1060  0.1053  23  ALA B CA  
3290 C C   . ALA B 25  ? 1.2870 0.5315 0.5347 0.1841  0.0910  0.0999  23  ALA B C   
3291 O O   . ALA B 25  ? 1.2421 0.5204 0.5132 0.1959  0.0683  0.0804  23  ALA B O   
3292 C CB  . ALA B 25  ? 1.3312 0.5034 0.5471 0.1994  0.1052  0.1117  23  ALA B CB  
3293 N N   . ALA B 26  ? 1.2159 0.4537 0.4400 0.1847  0.1057  0.1153  24  ALA B N   
3294 C CA  . ALA B 26  ? 1.3244 0.5985 0.5479 0.1970  0.0936  0.1095  24  ALA B CA  
3295 C C   . ALA B 26  ? 1.4017 0.6581 0.5737 0.2340  0.0981  0.1212  24  ALA B C   
3296 O O   . ALA B 26  ? 1.2939 0.5266 0.4525 0.2293  0.1251  0.1364  24  ALA B O   
3297 C CB  . ALA B 26  ? 1.1835 0.4786 0.4343 0.1638  0.1059  0.1109  24  ALA B CB  
3298 N N   . SER B 27  ? 1.4690 0.7451 0.6238 0.2704  0.0711  0.1087  25  SER B N   
3299 C CA  . SER B 27  ? 1.4176 0.6930 0.5325 0.3091  0.0690  0.1100  25  SER B CA  
3300 C C   . SER B 27  ? 1.4668 0.7796 0.5863 0.3116  0.0624  0.1037  25  SER B C   
3301 O O   . SER B 27  ? 1.5204 0.8660 0.6468 0.3348  0.0308  0.0825  25  SER B O   
3302 C CB  . SER B 27  ? 1.4102 0.6826 0.5042 0.3549  0.0382  0.0933  25  SER B CB  
3303 O OG  . SER B 27  ? 1.5325 0.8480 0.6482 0.3751  0.0031  0.0670  25  SER B OG  
3304 N N   . GLY B 28  ? 1.2924 0.6020 0.4137 0.2876  0.0917  0.1191  26  GLY B N   
3305 C CA  . GLY B 28  ? 1.2743 0.6175 0.3998 0.2879  0.0889  0.1139  26  GLY B CA  
3306 C C   . GLY B 28  ? 1.3023 0.6294 0.4212 0.2682  0.1275  0.1337  26  GLY B C   
3307 O O   . GLY B 28  ? 1.3734 0.6689 0.5008 0.2425  0.1558  0.1486  26  GLY B O   
3308 N N   . ARG B 29  ? 1.4232 0.7729 0.5298 0.2815  0.1287  0.1313  27  ARG B N   
3309 C CA  . ARG B 29  ? 1.4311 0.7655 0.5285 0.2679  0.1676  0.1489  27  ARG B CA  
3310 C C   . ARG B 29  ? 1.4433 0.7874 0.5812 0.2215  0.1832  0.1495  27  ARG B C   
3311 O O   . ARG B 29  ? 1.4996 0.8774 0.6636 0.2094  0.1588  0.1333  27  ARG B O   
3312 C CB  . ARG B 29  ? 1.4599 0.8153 0.5280 0.3004  0.1635  0.1446  27  ARG B CB  
3313 C CG  . ARG B 29  ? 1.5814 0.9898 0.6668 0.3138  0.1231  0.1179  27  ARG B CG  
3314 C CD  . ARG B 29  ? 1.7334 1.1696 0.8172 0.3139  0.1327  0.1145  27  ARG B CD  
3315 N NE  . ARG B 29  ? 1.8485 1.3364 0.9648 0.3118  0.0990  0.0877  27  ARG B NE  
3316 C CZ  . ARG B 29  ? 1.7779 1.2883 0.9515 0.2714  0.0950  0.0788  27  ARG B CZ  
3317 N NH1 . ARG B 29  ? 1.6153 1.1013 0.8122 0.2321  0.1206  0.0934  27  ARG B NH1 
3318 N NH2 . ARG B 29  ? 1.6539 1.2179 0.8815 0.2687  0.0621  0.0508  27  ARG B NH2 
3319 N N   . THR B 30  ? 1.3303 0.6430 0.4756 0.1968  0.2243  0.1661  28  THR B N   
3320 C CA  . THR B 30  ? 1.4045 0.7191 0.5887 0.1538  0.2448  0.1653  28  THR B CA  
3321 C C   . THR B 30  ? 1.3808 0.7153 0.6178 0.1275  0.2160  0.1473  28  THR B C   
3322 O O   . THR B 30  ? 1.3972 0.7793 0.6806 0.1128  0.1889  0.1255  28  THR B O   
3323 C CB  . THR B 30  ? 1.5662 0.9251 0.7687 0.1504  0.2420  0.1525  28  THR B CB  
3324 O OG1 . THR B 30  ? 1.4547 0.8073 0.6019 0.1878  0.2527  0.1628  28  THR B OG1 
3325 C CG2 . THR B 30  ? 1.5829 0.9455 0.8411 0.1097  0.2731  0.1488  28  THR B CG2 
3326 N N   . PHE B 31  ? 1.3853 0.6803 0.6137 0.1236  0.2237  0.1569  29  PHE B N   
3327 C CA  . PHE B 31  ? 1.2000 0.5089 0.4722 0.1019  0.1999  0.1406  29  PHE B CA  
3328 C C   . PHE B 31  ? 1.2408 0.5648 0.5741 0.0615  0.2085  0.1271  29  PHE B C   
3329 O O   . PHE B 31  ? 1.2061 0.5576 0.5764 0.0457  0.1824  0.1084  29  PHE B O   
3330 C CB  . PHE B 31  ? 1.2369 0.4995 0.4823 0.1115  0.2059  0.1528  29  PHE B CB  
3331 C CG  . PHE B 31  ? 1.3071 0.5751 0.5943 0.0868  0.1915  0.1379  29  PHE B CG  
3332 C CD1 . PHE B 31  ? 1.2662 0.5635 0.5658 0.0923  0.1573  0.1220  29  PHE B CD1 
3333 C CD2 . PHE B 31  ? 1.3067 0.5492 0.6221 0.0596  0.2140  0.1384  29  PHE B CD2 
3334 C CE1 . PHE B 31  ? 1.2127 0.5115 0.5418 0.0728  0.1474  0.1099  29  PHE B CE1 
3335 C CE2 . PHE B 31  ? 1.1797 0.4274 0.5274 0.0413  0.1988  0.1224  29  PHE B CE2 
3336 C CZ  . PHE B 31  ? 1.1364 0.4109 0.4856 0.0489  0.1662  0.1098  29  PHE B CZ  
3337 N N   . SER B 32  ? 1.2052 0.5109 0.5504 0.0466  0.2453  0.1348  30  SER B N   
3338 C CA  . SER B 32  ? 1.2014 0.5209 0.6126 0.0102  0.2536  0.1166  30  SER B CA  
3339 C C   . SER B 32  ? 1.2273 0.6016 0.6775 -0.0004 0.2314  0.0948  30  SER B C   
3340 O O   . SER B 32  ? 1.2347 0.6254 0.7415 -0.0269 0.2336  0.0753  30  SER B O   
3341 C CB  . SER B 32  ? 1.2338 0.5149 0.6559 -0.0029 0.3050  0.1292  30  SER B CB  
3342 O OG  . SER B 32  ? 1.4349 0.7063 0.8146 0.0170  0.3309  0.1484  30  SER B OG  
3343 N N   . ASN B 33  ? 1.3301 0.7334 0.7558 0.0211  0.2086  0.0946  31  ASN B N   
3344 C CA  . ASN B 33  ? 1.3541 0.8074 0.8158 0.0137  0.1861  0.0747  31  ASN B CA  
3345 C C   . ASN B 33  ? 1.2720 0.7524 0.7453 0.0160  0.1442  0.0609  31  ASN B C   
3346 O O   . ASN B 33  ? 1.2532 0.7715 0.7557 0.0113  0.1232  0.0453  31  ASN B O   
3347 C CB  . ASN B 33  ? 1.3452 0.8144 0.7794 0.0355  0.1931  0.0812  31  ASN B CB  
3348 C CG  . ASN B 33  ? 1.3282 0.7893 0.7753 0.0238  0.2339  0.0852  31  ASN B CG  
3349 O OD1 . ASN B 33  ? 1.3791 0.8246 0.8655 -0.0025 0.2572  0.0807  31  ASN B OD1 
3350 N ND2 . ASN B 33  ? 1.3524 0.8251 0.7706 0.0441  0.2437  0.0908  31  ASN B ND2 
3351 N N   . TYR B 34  ? 1.2184 0.6781 0.6710 0.0233  0.1343  0.0667  32  TYR B N   
3352 C CA  . TYR B 34  ? 1.0996 0.5786 0.5586 0.0283  0.1023  0.0571  32  TYR B CA  
3353 C C   . TYR B 34  ? 1.1120 0.5861 0.5954 0.0077  0.0933  0.0459  32  TYR B C   
3354 O O   . TYR B 34  ? 1.0199 0.4696 0.5099 -0.0061 0.1093  0.0460  32  TYR B O   
3355 C CB  . TYR B 34  ? 1.1056 0.5683 0.5289 0.0528  0.0966  0.0667  32  TYR B CB  
3356 C CG  . TYR B 34  ? 1.3037 0.7817 0.7043 0.0811  0.0909  0.0692  32  TYR B CG  
3357 C CD1 . TYR B 34  ? 1.3199 0.7891 0.6945 0.0916  0.1121  0.0798  32  TYR B CD1 
3358 C CD2 . TYR B 34  ? 1.2430 0.7438 0.6500 0.0990  0.0655  0.0587  32  TYR B CD2 
3359 C CE1 . TYR B 34  ? 1.3903 0.8737 0.7374 0.1225  0.1043  0.0794  32  TYR B CE1 
3360 C CE2 . TYR B 34  ? 1.3189 0.8374 0.7101 0.1280  0.0559  0.0546  32  TYR B CE2 
3361 C CZ  . TYR B 34  ? 1.3972 0.9072 0.7542 0.1413  0.0733  0.0648  32  TYR B CZ  
3362 O OH  . TYR B 34  ? 1.4158 0.9434 0.7500 0.1750  0.0614  0.0584  32  TYR B OH  
3363 N N   . VAL B 35  ? 1.1715 0.6672 0.6677 0.0077  0.0682  0.0357  33  VAL B N   
3364 C CA  . VAL B 35  ? 1.1764 0.6647 0.6813 -0.0037 0.0567  0.0261  33  VAL B CA  
3365 C C   . VAL B 35  ? 1.1641 0.6318 0.6441 0.0068  0.0554  0.0339  33  VAL B C   
3366 O O   . VAL B 35  ? 1.1639 0.6424 0.6396 0.0200  0.0458  0.0361  33  VAL B O   
3367 C CB  . VAL B 35  ? 1.0813 0.5965 0.6059 -0.0063 0.0339  0.0137  33  VAL B CB  
3368 C CG1 . VAL B 35  ? 1.1420 0.6434 0.6564 -0.0080 0.0215  0.0084  33  VAL B CG1 
3369 C CG2 . VAL B 35  ? 1.0631 0.5976 0.6193 -0.0189 0.0333  0.0000  33  VAL B CG2 
3370 N N   . MET B 36  ? 1.0602 0.4994 0.5306 0.0007  0.0659  0.0353  34  MET B N   
3371 C CA  . MET B 36  ? 1.0544 0.4729 0.5040 0.0098  0.0666  0.0405  34  MET B CA  
3372 C C   . MET B 36  ? 1.0927 0.5087 0.5419 0.0040  0.0550  0.0305  34  MET B C   
3373 O O   . MET B 36  ? 1.1079 0.5251 0.5672 -0.0074 0.0492  0.0187  34  MET B O   
3374 C CB  . MET B 36  ? 1.1696 0.5550 0.6062 0.0092  0.0857  0.0483  34  MET B CB  
3375 C CG  . MET B 36  ? 1.1123 0.4893 0.5346 0.0205  0.1014  0.0626  34  MET B CG  
3376 S SD  . MET B 36  ? 1.1711 0.5732 0.5801 0.0465  0.0873  0.0662  34  MET B SD  
3377 C CE  . MET B 36  ? 1.0010 0.3806 0.3894 0.0654  0.0839  0.0689  34  MET B CE  
3378 N N   . ALA B 37  ? 0.9389 0.3508 0.3766 0.0142  0.0521  0.0334  35  ALA B N   
3379 C CA  . ALA B 37  ? 0.9631 0.3675 0.3907 0.0126  0.0462  0.0274  35  ALA B CA  
3380 C C   . ALA B 37  ? 1.0370 0.4246 0.4526 0.0213  0.0550  0.0308  35  ALA B C   
3381 O O   . ALA B 37  ? 0.9820 0.3702 0.4026 0.0307  0.0601  0.0356  35  ALA B O   
3382 C CB  . ALA B 37  ? 1.0492 0.4722 0.4829 0.0151  0.0347  0.0262  35  ALA B CB  
3383 N N   . TRP B 38  ? 0.9902 0.3628 0.3887 0.0205  0.0559  0.0262  36  TRP B N   
3384 C CA  . TRP B 38  ? 1.0243 0.3815 0.4137 0.0275  0.0668  0.0270  36  TRP B CA  
3385 C C   . TRP B 38  ? 1.0912 0.4481 0.4730 0.0320  0.0703  0.0290  36  TRP B C   
3386 O O   . TRP B 38  ? 1.0623 0.4147 0.4239 0.0310  0.0634  0.0275  36  TRP B O   
3387 C CB  . TRP B 38  ? 1.0185 0.3520 0.3904 0.0242  0.0710  0.0200  36  TRP B CB  
3388 C CG  . TRP B 38  ? 1.0239 0.3470 0.4042 0.0233  0.0763  0.0216  36  TRP B CG  
3389 C CD1 . TRP B 38  ? 1.0477 0.3645 0.4347 0.0143  0.0762  0.0196  36  TRP B CD1 
3390 C CD2 . TRP B 38  ? 1.0192 0.3335 0.4030 0.0335  0.0842  0.0252  36  TRP B CD2 
3391 N NE1 . TRP B 38  ? 1.0382 0.3376 0.4261 0.0188  0.0862  0.0262  36  TRP B NE1 
3392 C CE2 . TRP B 38  ? 1.0348 0.3330 0.4181 0.0323  0.0883  0.0290  36  TRP B CE2 
3393 C CE3 . TRP B 38  ? 1.0134 0.3311 0.4044 0.0446  0.0888  0.0238  36  TRP B CE3 
3394 C CZ2 . TRP B 38  ? 1.0483 0.3311 0.4288 0.0450  0.0937  0.0334  36  TRP B CZ2 
3395 C CZ3 . TRP B 38  ? 1.0386 0.3470 0.4350 0.0564  0.0915  0.0233  36  TRP B CZ3 
3396 C CH2 . TRP B 38  ? 1.0751 0.3649 0.4615 0.0581  0.0923  0.0291  36  TRP B CH2 
3397 N N   . PHE B 39  ? 1.0164 0.3761 0.4155 0.0388  0.0817  0.0312  37  PHE B N   
3398 C CA  . PHE B 39  ? 0.9998 0.3540 0.3984 0.0424  0.0939  0.0349  37  PHE B CA  
3399 C C   . PHE B 39  ? 1.1012 0.4408 0.5039 0.0468  0.1141  0.0315  37  PHE B C   
3400 O O   . PHE B 39  ? 1.1387 0.4854 0.5659 0.0502  0.1149  0.0247  37  PHE B O   
3401 C CB  . PHE B 39  ? 1.0931 0.4704 0.5293 0.0447  0.0916  0.0370  37  PHE B CB  
3402 C CG  . PHE B 39  ? 1.0530 0.4462 0.4883 0.0410  0.0733  0.0393  37  PHE B CG  
3403 C CD1 . PHE B 39  ? 0.9847 0.3979 0.4341 0.0394  0.0600  0.0359  37  PHE B CD1 
3404 C CD2 . PHE B 39  ? 0.9596 0.3456 0.3781 0.0414  0.0708  0.0449  37  PHE B CD2 
3405 C CE1 . PHE B 39  ? 1.0148 0.4445 0.4683 0.0353  0.0458  0.0358  37  PHE B CE1 
3406 C CE2 . PHE B 39  ? 0.9457 0.3484 0.3685 0.0389  0.0523  0.0439  37  PHE B CE2 
3407 C CZ  . PHE B 39  ? 1.0184 0.4450 0.4622 0.0344  0.0404  0.0382  37  PHE B CZ  
3408 N N   . ARG B 40  ? 1.1072 0.4249 0.4836 0.0490  0.1309  0.0355  38  ARG B N   
3409 C CA  . ARG B 40  ? 1.1300 0.4332 0.5126 0.0525  0.1559  0.0318  38  ARG B CA  
3410 C C   . ARG B 40  ? 1.0654 0.3640 0.4691 0.0546  0.1803  0.0384  38  ARG B C   
3411 O O   . ARG B 40  ? 1.0674 0.3656 0.4647 0.0548  0.1775  0.0485  38  ARG B O   
3412 C CB  . ARG B 40  ? 1.2414 0.5172 0.5719 0.0552  0.1624  0.0302  38  ARG B CB  
3413 C CG  . ARG B 40  ? 1.2073 0.4641 0.4836 0.0604  0.1597  0.0386  38  ARG B CG  
3414 C CD  . ARG B 40  ? 1.3130 0.5391 0.5394 0.0696  0.1785  0.0374  38  ARG B CD  
3415 N NE  . ARG B 40  ? 1.5095 0.7148 0.6740 0.0814  0.1717  0.0438  38  ARG B NE  
3416 C CZ  . ARG B 40  ? 1.4624 0.6559 0.5784 0.0900  0.1550  0.0328  38  ARG B CZ  
3417 N NH1 . ARG B 40  ? 1.3356 0.5344 0.4604 0.0854  0.1465  0.0162  38  ARG B NH1 
3418 N NH2 . ARG B 40  ? 1.4129 0.5884 0.4716 0.1059  0.1448  0.0364  38  ARG B NH2 
3419 N N   . GLN B 41  ? 1.0731 0.3670 0.5069 0.0561  0.2061  0.0314  39  GLN B N   
3420 C CA  . GLN B 41  ? 1.1101 0.3981 0.5784 0.0562  0.2365  0.0352  39  GLN B CA  
3421 C C   . GLN B 41  ? 1.1126 0.3837 0.5924 0.0574  0.2712  0.0281  39  GLN B C   
3422 O O   . GLN B 41  ? 1.0949 0.3799 0.6050 0.0583  0.2664  0.0107  39  GLN B O   
3423 C CB  . GLN B 41  ? 1.1565 0.4791 0.7003 0.0550  0.2265  0.0241  39  GLN B CB  
3424 C CG  . GLN B 41  ? 1.2444 0.5706 0.8586 0.0543  0.2590  0.0130  39  GLN B CG  
3425 C CD  . GLN B 41  ? 1.3583 0.7174 1.0454 0.0549  0.2475  0.0010  39  GLN B CD  
3426 O OE1 . GLN B 41  ? 1.3121 0.6809 0.9863 0.0545  0.2262  0.0098  39  GLN B OE1 
3427 N NE2 . GLN B 41  ? 1.3744 0.7533 1.1432 0.0570  0.2602  -0.0231 39  GLN B NE2 
3428 N N   . ALA B 42  ? 1.1937 0.4321 0.6466 0.0594  0.3077  0.0419  40  ALA B N   
3429 C CA  . ALA B 42  ? 1.2106 0.4276 0.6725 0.0603  0.3511  0.0383  40  ALA B CA  
3430 C C   . ALA B 42  ? 1.4700 0.6959 1.0187 0.0549  0.3837  0.0313  40  ALA B C   
3431 O O   . ALA B 42  ? 1.4510 0.6860 1.0301 0.0524  0.3791  0.0374  40  ALA B O   
3432 C CB  . ALA B 42  ? 1.2763 0.4464 0.6487 0.0692  0.3761  0.0595  40  ALA B CB  
3433 N N   . PRO B 43  ? 1.5595 0.7849 1.1575 0.0528  0.4169  0.0151  41  PRO B N   
3434 C CA  . PRO B 43  ? 1.5432 0.7810 1.2415 0.0466  0.4491  0.0013  41  PRO B CA  
3435 C C   . PRO B 43  ? 1.6579 0.8598 1.3425 0.0445  0.4893  0.0273  41  PRO B C   
3436 O O   . PRO B 43  ? 1.7787 0.9338 1.3966 0.0487  0.5281  0.0494  41  PRO B O   
3437 C CB  . PRO B 43  ? 1.5313 0.7669 1.2679 0.0456  0.4818  -0.0193 41  PRO B CB  
3438 C CG  . PRO B 43  ? 1.6586 0.8993 1.3384 0.0517  0.4475  -0.0249 41  PRO B CG  
3439 C CD  . PRO B 43  ? 1.6174 0.8365 1.1944 0.0557  0.4233  0.0029  41  PRO B CD  
3440 N N   . GLY B 44  ? 1.6935 0.9150 1.4388 0.0404  0.4802  0.0244  42  GLY B N   
3441 C CA  . GLY B 44  ? 1.7047 0.8924 1.4477 0.0387  0.5161  0.0484  42  GLY B CA  
3442 C C   . GLY B 44  ? 1.7003 0.8684 1.3538 0.0461  0.4886  0.0776  42  GLY B C   
3443 O O   . GLY B 44  ? 1.7890 0.9388 1.4420 0.0475  0.5090  0.0962  42  GLY B O   
3444 N N   . LYS B 45  ? 1.4441 0.6253 1.0300 0.0517  0.4404  0.0783  43  LYS B N   
3445 C CA  . LYS B 45  ? 1.4743 0.6411 0.9799 0.0596  0.4105  0.0999  43  LYS B CA  
3446 C C   . LYS B 45  ? 1.3766 0.5913 0.9225 0.0554  0.3595  0.0862  43  LYS B C   
3447 O O   . LYS B 45  ? 1.3419 0.5986 0.9600 0.0498  0.3427  0.0610  43  LYS B O   
3448 C CB  . LYS B 45  ? 1.4708 0.6161 0.8734 0.0697  0.3955  0.1078  43  LYS B CB  
3449 C CG  . LYS B 45  ? 1.5538 0.6542 0.8820 0.0841  0.4299  0.1273  43  LYS B CG  
3450 C CD  . LYS B 45  ? 1.5529 0.6476 0.7880 0.1002  0.3907  0.1314  43  LYS B CD  
3451 C CE  . LYS B 45  ? 1.6058 0.6977 0.8187 0.1113  0.3752  0.1442  43  LYS B CE  
3452 N NZ  . LYS B 45  ? 1.5104 0.5869 0.6360 0.1324  0.3473  0.1458  43  LYS B NZ  
3453 N N   . GLU B 46  ? 1.4160 0.6228 0.9110 0.0608  0.3348  0.1020  44  GLU B N   
3454 C CA  . GLU B 46  ? 1.3582 0.6070 0.8818 0.0576  0.2891  0.0911  44  GLU B CA  
3455 C C   . GLU B 46  ? 1.3322 0.6001 0.8142 0.0581  0.2505  0.0821  44  GLU B C   
3456 O O   . GLU B 46  ? 1.4855 0.7300 0.9028 0.0627  0.2526  0.0874  44  GLU B O   
3457 C CB  . GLU B 46  ? 1.5393 0.7731 1.0356 0.0628  0.2800  0.1092  44  GLU B CB  
3458 C CG  . GLU B 46  ? 1.6922 0.8901 1.0839 0.0754  0.2697  0.1276  44  GLU B CG  
3459 C CD  . GLU B 46  ? 1.9230 1.1156 1.2958 0.0835  0.2549  0.1400  44  GLU B CD  
3460 O OE1 . GLU B 46  ? 1.8837 1.0890 1.3177 0.0776  0.2547  0.1389  44  GLU B OE1 
3461 O OE2 . GLU B 46  ? 1.9764 1.1545 1.2783 0.0976  0.2411  0.1468  44  GLU B OE2 
3462 N N   . ARG B 47  ? 1.2606 0.5701 0.7819 0.0542  0.2170  0.0676  45  ARG B N   
3463 C CA  . ARG B 47  ? 1.0420 0.3674 0.5317 0.0536  0.1845  0.0606  45  ARG B CA  
3464 C C   . ARG B 47  ? 1.1286 0.4365 0.5487 0.0569  0.1668  0.0726  45  ARG B C   
3465 O O   . ARG B 47  ? 1.1245 0.4334 0.5407 0.0590  0.1566  0.0801  45  ARG B O   
3466 C CB  . ARG B 47  ? 0.9960 0.3642 0.5367 0.0519  0.1573  0.0460  45  ARG B CB  
3467 C CG  . ARG B 47  ? 1.2301 0.6114 0.7538 0.0519  0.1355  0.0376  45  ARG B CG  
3468 C CD  . ARG B 47  ? 1.1385 0.5529 0.7165 0.0571  0.1231  0.0207  45  ARG B CD  
3469 N NE  . ARG B 47  ? 1.1423 0.5632 0.7795 0.0608  0.1425  0.0076  45  ARG B NE  
3470 C CZ  . ARG B 47  ? 1.2272 0.6798 0.9256 0.0690  0.1319  -0.0121 45  ARG B CZ  
3471 N NH1 . ARG B 47  ? 1.1068 0.5853 0.8066 0.0762  0.1034  -0.0178 45  ARG B NH1 
3472 N NH2 . ARG B 47  ? 1.3148 0.7737 1.0763 0.0716  0.1510  -0.0288 45  ARG B NH2 
3473 N N   . GLU B 48  ? 1.2228 0.5157 0.5921 0.0589  0.1614  0.0710  46  GLU B N   
3474 C CA  . GLU B 48  ? 1.2126 0.4906 0.5203 0.0650  0.1420  0.0751  46  GLU B CA  
3475 C C   . GLU B 48  ? 1.0824 0.3832 0.3916 0.0585  0.1120  0.0615  46  GLU B C   
3476 O O   . GLU B 48  ? 1.0575 0.3712 0.3920 0.0523  0.1122  0.0529  46  GLU B O   
3477 C CB  . GLU B 48  ? 1.3312 0.5688 0.5736 0.0765  0.1605  0.0817  46  GLU B CB  
3478 C CG  . GLU B 48  ? 1.3565 0.5852 0.6067 0.0742  0.1860  0.0764  46  GLU B CG  
3479 C CD  . GLU B 48  ? 1.4856 0.6742 0.6640 0.0881  0.2042  0.0821  46  GLU B CD  
3480 O OE1 . GLU B 48  ? 1.5878 0.7527 0.7072 0.1025  0.1977  0.0918  46  GLU B OE1 
3481 O OE2 . GLU B 48  ? 1.3911 0.5714 0.5692 0.0873  0.2239  0.0758  46  GLU B OE2 
3482 N N   . PHE B 49  ? 1.0911 0.3942 0.3746 0.0613  0.0877  0.0590  47  PHE B N   
3483 C CA  . PHE B 49  ? 1.0683 0.3916 0.3608 0.0536  0.0629  0.0450  47  PHE B CA  
3484 C C   . PHE B 49  ? 1.1929 0.4992 0.4517 0.0558  0.0609  0.0344  47  PHE B C   
3485 O O   . PHE B 49  ? 1.1877 0.4681 0.3970 0.0685  0.0641  0.0348  47  PHE B O   
3486 C CB  . PHE B 49  ? 1.0664 0.4016 0.3555 0.0558  0.0381  0.0412  47  PHE B CB  
3487 C CG  . PHE B 49  ? 1.0507 0.4045 0.3537 0.0473  0.0166  0.0241  47  PHE B CG  
3488 C CD1 . PHE B 49  ? 1.0621 0.4420 0.4096 0.0347  0.0153  0.0216  47  PHE B CD1 
3489 C CD2 . PHE B 49  ? 1.1572 0.5015 0.4303 0.0538  -0.0011 0.0090  47  PHE B CD2 
3490 C CE1 . PHE B 49  ? 1.1241 0.5167 0.4884 0.0256  0.0030  0.0074  47  PHE B CE1 
3491 C CE2 . PHE B 49  ? 1.1679 0.5301 0.4674 0.0441  -0.0175 -0.0104 47  PHE B CE2 
3492 C CZ  . PHE B 49  ? 1.1514 0.5362 0.4978 0.0284  -0.0124 -0.0095 47  PHE B CZ  
3493 N N   . VAL B 50  ? 1.1090 0.4276 0.3926 0.0455  0.0564  0.0248  48  VAL B N   
3494 C CA  . VAL B 50  ? 1.2146 0.5202 0.4792 0.0454  0.0530  0.0114  48  VAL B CA  
3495 C C   . VAL B 50  ? 1.2041 0.5237 0.4854 0.0377  0.0310  -0.0047 48  VAL B C   
3496 O O   . VAL B 50  ? 1.1950 0.5082 0.4538 0.0442  0.0150  -0.0208 48  VAL B O   
3497 C CB  . VAL B 50  ? 1.1001 0.4007 0.3823 0.0408  0.0703  0.0124  48  VAL B CB  
3498 C CG1 . VAL B 50  ? 1.1890 0.4817 0.4690 0.0364  0.0635  -0.0030 48  VAL B CG1 
3499 C CG2 . VAL B 50  ? 1.1203 0.4027 0.3835 0.0493  0.0930  0.0196  48  VAL B CG2 
3500 N N   . ALA B 51  ? 1.0555 0.3938 0.3774 0.0256  0.0309  -0.0028 49  ALA B N   
3501 C CA  . ALA B 51  ? 1.1510 0.5014 0.4986 0.0155  0.0181  -0.0176 49  ALA B CA  
3502 C C   . ALA B 51  ? 1.0824 0.4538 0.4645 0.0071  0.0218  -0.0082 49  ALA B C   
3503 O O   . ALA B 51  ? 0.9940 0.3688 0.3806 0.0099  0.0329  0.0068  49  ALA B O   
3504 C CB  . ALA B 51  ? 1.0652 0.4014 0.4208 0.0093  0.0238  -0.0294 49  ALA B CB  
3505 N N   . ARG B 52  ? 1.0146 0.4011 0.4231 -0.0017 0.0120  -0.0203 50  ARG B N   
3506 C CA  . ARG B 52  ? 1.1070 0.5119 0.5455 -0.0093 0.0183  -0.0130 50  ARG B CA  
3507 C C   . ARG B 52  ? 1.1083 0.5169 0.5804 -0.0229 0.0205  -0.0286 50  ARG B C   
3508 O O   . ARG B 52  ? 1.0898 0.4973 0.5710 -0.0256 0.0079  -0.0508 50  ARG B O   
3509 C CB  . ARG B 52  ? 1.1385 0.5661 0.5820 -0.0045 0.0062  -0.0097 50  ARG B CB  
3510 C CG  . ARG B 52  ? 1.1231 0.5680 0.5869 -0.0088 -0.0123 -0.0288 50  ARG B CG  
3511 C CD  . ARG B 52  ? 1.1201 0.5894 0.5980 -0.0059 -0.0209 -0.0244 50  ARG B CD  
3512 N NE  . ARG B 52  ? 1.2715 0.7586 0.7720 -0.0083 -0.0408 -0.0456 50  ARG B NE  
3513 C CZ  . ARG B 52  ? 1.1879 0.6709 0.6692 0.0034  -0.0636 -0.0573 50  ARG B CZ  
3514 N NH1 . ARG B 52  ? 1.0854 0.5440 0.5200 0.0175  -0.0651 -0.0468 50  ARG B NH1 
3515 N NH2 . ARG B 52  ? 1.1829 0.6852 0.6913 0.0029  -0.0844 -0.0810 50  ARG B NH2 
3516 N N   . ILE B 53  ? 1.0552 0.4670 0.5468 -0.0298 0.0378  -0.0184 51  ILE B N   
3517 C CA  . ILE B 53  ? 1.0651 0.4773 0.5949 -0.0445 0.0496  -0.0298 51  ILE B CA  
3518 C C   . ILE B 53  ? 1.0952 0.5313 0.6455 -0.0479 0.0541  -0.0253 51  ILE B C   
3519 O O   . ILE B 53  ? 1.0849 0.5278 0.6161 -0.0380 0.0574  -0.0071 51  ILE B O   
3520 C CB  . ILE B 53  ? 1.1553 0.5367 0.6839 -0.0487 0.0755  -0.0192 51  ILE B CB  
3521 C CG1 . ILE B 53  ? 1.1139 0.4901 0.6900 -0.0662 0.0924  -0.0336 51  ILE B CG1 
3522 C CG2 . ILE B 53  ? 1.1882 0.5611 0.6901 -0.0376 0.0910  0.0082  51  ILE B CG2 
3523 C CD1 . ILE B 53  ? 1.2673 0.6122 0.8533 -0.0723 0.1058  -0.0396 51  ILE B CD1 
3524 N N   . SER B 54  ? 1.0544 0.5058 0.6481 -0.0606 0.0531  -0.0459 52  SER B N   
3525 C CA  . SER B 54  ? 1.0446 0.5211 0.6621 -0.0644 0.0580  -0.0456 52  SER B CA  
3526 C C   . SER B 54  ? 1.1932 0.6542 0.8123 -0.0688 0.0941  -0.0267 52  SER B C   
3527 O O   . SER B 54  ? 1.2120 0.6416 0.8265 -0.0727 0.1162  -0.0187 52  SER B O   
3528 C CB  . SER B 54  ? 1.0870 0.5873 0.7568 -0.0757 0.0444  -0.0782 52  SER B CB  
3529 O OG  . SER B 54  ? 1.0835 0.6097 0.7800 -0.0799 0.0506  -0.0795 52  SER B OG  
3530 N N   . GLU B 55  ? 1.1051 0.5858 0.7270 -0.0656 0.1007  -0.0193 53  GLU B N   
3531 C CA  . GLU B 55  ? 1.0954 0.5606 0.7075 -0.0642 0.1356  0.0002  53  GLU B CA  
3532 C C   . GLU B 55  ? 1.1379 0.6026 0.8018 -0.0840 0.1639  -0.0127 53  GLU B C   
3533 O O   . GLU B 55  ? 1.3334 0.7806 0.9880 -0.0830 0.1998  0.0049  53  GLU B O   
3534 C CB  . GLU B 55  ? 1.1033 0.5908 0.6904 -0.0475 0.1293  0.0124  53  GLU B CB  
3535 C CG  . GLU B 55  ? 1.1567 0.6804 0.7828 -0.0553 0.1262  -0.0037 53  GLU B CG  
3536 C CD  . GLU B 55  ? 1.1820 0.7335 0.8406 -0.0622 0.0911  -0.0294 53  GLU B CD  
3537 O OE1 . GLU B 55  ? 1.1675 0.7365 0.8763 -0.0769 0.0912  -0.0528 53  GLU B OE1 
3538 O OE2 . GLU B 55  ? 1.0654 0.6194 0.6997 -0.0512 0.0645  -0.0269 53  GLU B OE2 
3539 N N   . SER B 56  ? 1.1291 0.6107 0.8477 -0.1001 0.1501  -0.0443 54  SER B N   
3540 C CA  . SER B 56  ? 1.2293 0.7201 1.0136 -0.1199 0.1745  -0.0643 54  SER B CA  
3541 C C   . SER B 56  ? 1.3548 0.8196 1.1792 -0.1357 0.1908  -0.0793 54  SER B C   
3542 O O   . SER B 56  ? 1.4282 0.8544 1.2457 -0.1403 0.2319  -0.0590 54  SER B O   
3543 C CB  . SER B 56  ? 1.1889 0.7267 1.0167 -0.1234 0.1434  -0.0955 54  SER B CB  
3544 O OG  . SER B 56  ? 1.2488 0.8001 1.1506 -0.1430 0.1670  -0.1199 54  SER B OG  
3545 N N   . ARG B 57  ? 1.2630 0.7446 1.1285 -0.1420 0.1603  -0.1154 55  ARG B N   
3546 C CA  . ARG B 57  ? 1.3307 0.7935 1.2471 -0.1567 0.1721  -0.1384 55  ARG B CA  
3547 C C   . ARG B 57  ? 1.2991 0.7360 1.1704 -0.1461 0.1552  -0.1311 55  ARG B C   
3548 O O   . ARG B 57  ? 1.2423 0.6682 1.1545 -0.1550 0.1547  -0.1562 55  ARG B O   
3549 C CB  . ARG B 57  ? 1.2532 0.7525 1.2505 -0.1672 0.1468  -0.1911 55  ARG B CB  
3550 C CG  . ARG B 57  ? 1.3282 0.8553 1.3902 -0.1815 0.1666  -0.2073 55  ARG B CG  
3551 C CD  . ARG B 57  ? 1.3919 0.9566 1.4275 -0.1674 0.1325  -0.2075 55  ARG B CD  
3552 N NE  . ARG B 57  ? 1.4563 1.0627 1.5726 -0.1764 0.1177  -0.2520 55  ARG B NE  
3553 C CZ  . ARG B 57  ? 1.4244 1.0527 1.5728 -0.1843 0.1386  -0.2525 55  ARG B CZ  
3554 N NH1 . ARG B 57  ? 1.4463 1.0578 1.5496 -0.1830 0.1759  -0.2110 55  ARG B NH1 
3555 N NH2 . ARG B 57  ? 1.3184 0.9872 1.5450 -0.1910 0.1201  -0.2980 55  ARG B NH2 
3556 N N   . GLY B 58  ? 1.3844 0.8129 1.1789 -0.1271 0.1418  -0.1008 56  GLY B N   
3557 C CA  . GLY B 58  ? 1.3652 0.7718 1.1185 -0.1166 0.1268  -0.0953 56  GLY B CA  
3558 C C   . GLY B 58  ? 1.3908 0.8184 1.1377 -0.1072 0.0821  -0.1224 56  GLY B C   
3559 O O   . GLY B 58  ? 1.4076 0.8192 1.1430 -0.1029 0.0715  -0.1326 56  GLY B O   
3560 N N   . THR B 59  ? 1.3340 0.7947 1.0844 -0.1014 0.0561  -0.1344 57  THR B N   
3561 C CA  . THR B 59  ? 1.1840 0.6589 0.9175 -0.0871 0.0141  -0.1573 57  THR B CA  
3562 C C   . THR B 59  ? 1.1582 0.6152 0.8167 -0.0692 0.0048  -0.1309 57  THR B C   
3563 O O   . THR B 59  ? 1.0923 0.5454 0.7168 -0.0643 0.0166  -0.0993 57  THR B O   
3564 C CB  . THR B 59  ? 1.1434 0.6534 0.8960 -0.0829 -0.0100 -0.1733 57  THR B CB  
3565 O OG1 . THR B 59  ? 1.2824 0.8104 1.1090 -0.1017 0.0076  -0.1933 57  THR B OG1 
3566 C CG2 . THR B 59  ? 1.1604 0.6808 0.9029 -0.0660 -0.0535 -0.2046 57  THR B CG2 
3567 N N   . THR B 60  ? 1.1194 0.5663 0.7552 -0.0583 -0.0161 -0.1470 58  THR B N   
3568 C CA  . THR B 60  ? 1.1158 0.5419 0.6867 -0.0431 -0.0188 -0.1253 58  THR B CA  
3569 C C   . THR B 60  ? 1.1541 0.5870 0.6848 -0.0227 -0.0504 -0.1336 58  THR B C   
3570 O O   . THR B 60  ? 1.1538 0.6024 0.7033 -0.0168 -0.0768 -0.1643 58  THR B O   
3571 C CB  . THR B 60  ? 1.0640 0.4647 0.6312 -0.0447 -0.0100 -0.1326 58  THR B CB  
3572 O OG1 . THR B 60  ? 1.0925 0.5015 0.7058 -0.0492 -0.0250 -0.1736 58  THR B OG1 
3573 C CG2 . THR B 60  ? 1.1299 0.5113 0.7110 -0.0578 0.0252  -0.1098 58  THR B CG2 
3574 N N   . ASP B 61  ? 1.1165 0.5353 0.5928 -0.0103 -0.0465 -0.1068 59  ASP B N   
3575 C CA  . ASP B 61  ? 1.1788 0.5921 0.6055 0.0112  -0.0676 -0.1067 59  ASP B CA  
3576 C C   . ASP B 61  ? 1.1933 0.5791 0.5685 0.0209  -0.0529 -0.0861 59  ASP B C   
3577 O O   . ASP B 61  ? 1.1635 0.5434 0.5413 0.0131  -0.0293 -0.0634 59  ASP B O   
3578 C CB  . ASP B 61  ? 1.2676 0.6972 0.6933 0.0153  -0.0744 -0.0931 59  ASP B CB  
3579 C CG  . ASP B 61  ? 1.3394 0.7549 0.7099 0.0392  -0.0915 -0.0883 59  ASP B CG  
3580 O OD1 . ASP B 61  ? 1.4317 0.8374 0.7754 0.0553  -0.1131 -0.1099 59  ASP B OD1 
3581 O OD2 . ASP B 61  ? 1.3247 0.7368 0.6779 0.0438  -0.0828 -0.0637 59  ASP B OD2 
3582 N N   . TYR B 62  ? 1.2288 0.5976 0.5568 0.0403  -0.0671 -0.0962 60  TYR B N   
3583 C CA  . TYR B 62  ? 1.3164 0.6579 0.5954 0.0504  -0.0508 -0.0805 60  TYR B CA  
3584 C C   . TYR B 62  ? 1.3846 0.7092 0.6034 0.0737  -0.0566 -0.0686 60  TYR B C   
3585 O O   . TYR B 62  ? 1.3802 0.7109 0.5876 0.0863  -0.0802 -0.0780 60  TYR B O   
3586 C CB  . TYR B 62  ? 1.1863 0.5154 0.4587 0.0535  -0.0547 -0.1037 60  TYR B CB  
3587 C CG  . TYR B 62  ? 1.1608 0.4994 0.4939 0.0313  -0.0461 -0.1156 60  TYR B CG  
3588 C CD1 . TYR B 62  ? 1.1589 0.5159 0.5418 0.0231  -0.0631 -0.1458 60  TYR B CD1 
3589 C CD2 . TYR B 62  ? 1.1437 0.4706 0.4867 0.0199  -0.0195 -0.0973 60  TYR B CD2 
3590 C CE1 . TYR B 62  ? 1.1770 0.5366 0.6176 0.0021  -0.0483 -0.1542 60  TYR B CE1 
3591 C CE2 . TYR B 62  ? 1.1309 0.4583 0.5227 0.0024  -0.0084 -0.1041 60  TYR B CE2 
3592 C CZ  . TYR B 62  ? 1.1600 0.5019 0.6003 -0.0074 -0.0201 -0.1309 60  TYR B CZ  
3593 O OH  . TYR B 62  ? 1.1266 0.4632 0.6177 -0.0256 -0.0023 -0.1355 60  TYR B OH  
3594 N N   . ALA B 63  ? 1.4084 0.7091 0.5896 0.0803  -0.0328 -0.0476 61  ALA B N   
3595 C CA  . ALA B 63  ? 1.3462 0.6212 0.4656 0.1028  -0.0283 -0.0323 61  ALA B CA  
3596 C C   . ALA B 63  ? 1.4539 0.7081 0.5130 0.1283  -0.0467 -0.0523 61  ALA B C   
3597 O O   . ALA B 63  ? 1.4785 0.7375 0.5474 0.1266  -0.0576 -0.0777 61  ALA B O   
3598 C CB  . ALA B 63  ? 1.2862 0.5428 0.3951 0.0999  0.0088  -0.0058 61  ALA B CB  
3599 N N   . ASP B 64  ? 1.5719 0.8004 0.5664 0.1548  -0.0501 -0.0412 62  ASP B N   
3600 C CA  . ASP B 64  ? 1.6036 0.8125 0.5381 0.1850  -0.0634 -0.0547 62  ASP B CA  
3601 C C   . ASP B 64  ? 1.6271 0.8184 0.5412 0.1860  -0.0341 -0.0475 62  ASP B C   
3602 O O   . ASP B 64  ? 1.7072 0.8932 0.5907 0.2072  -0.0449 -0.0625 62  ASP B O   
3603 C CB  . ASP B 64  ? 1.5654 0.7586 0.4614 0.2125  -0.0663 -0.0365 62  ASP B CB  
3604 C CG  . ASP B 64  ? 1.7148 0.9251 0.6319 0.2130  -0.0952 -0.0431 62  ASP B CG  
3605 O OD1 . ASP B 64  ? 1.8373 1.0730 0.8005 0.1908  -0.1114 -0.0622 62  ASP B OD1 
3606 O OD2 . ASP B 64  ? 1.6943 0.8904 0.5827 0.2359  -0.1004 -0.0304 62  ASP B OD2 
3607 N N   . SER B 65  ? 1.5895 0.7742 0.5230 0.1649  0.0011  -0.0274 63  SER B N   
3608 C CA  . SER B 65  ? 1.5164 0.6855 0.4368 0.1651  0.0304  -0.0219 63  SER B CA  
3609 C C   . SER B 65  ? 1.6054 0.7850 0.5508 0.1511  0.0217  -0.0489 63  SER B C   
3610 O O   . SER B 65  ? 1.6301 0.8006 0.5548 0.1607  0.0272  -0.0598 63  SER B O   
3611 C CB  . SER B 65  ? 1.5628 0.7227 0.5035 0.1511  0.0717  0.0078  63  SER B CB  
3612 O OG  . SER B 65  ? 1.7029 0.8573 0.6540 0.1407  0.0955  0.0048  63  SER B OG  
3613 N N   . VAL B 66  ? 1.4907 0.7016 0.5088 0.1267  0.0092  -0.0567 64  VAL B N   
3614 C CA  . VAL B 66  ? 1.4663 0.6903 0.5333 0.1088  0.0091  -0.0737 64  VAL B CA  
3615 C C   . VAL B 66  ? 1.4210 0.6639 0.5202 0.1057  -0.0239 -0.1073 64  VAL B C   
3616 O O   . VAL B 66  ? 1.3207 0.5691 0.4597 0.0926  -0.0234 -0.1239 64  VAL B O   
3617 C CB  . VAL B 66  ? 1.3878 0.6261 0.5137 0.0841  0.0293  -0.0544 64  VAL B CB  
3618 C CG1 . VAL B 66  ? 1.2907 0.5129 0.4012 0.0862  0.0625  -0.0324 64  VAL B CG1 
3619 C CG2 . VAL B 66  ? 1.3158 0.5754 0.4736 0.0749  0.0193  -0.0445 64  VAL B CG2 
3620 N N   . LYS B 67  ? 1.3508 0.6029 0.4394 0.1177  -0.0518 -0.1198 65  LYS B N   
3621 C CA  . LYS B 67  ? 1.3427 0.6180 0.4795 0.1123  -0.0821 -0.1560 65  LYS B CA  
3622 C C   . LYS B 67  ? 1.4008 0.6700 0.5316 0.1225  -0.0948 -0.1908 65  LYS B C   
3623 O O   . LYS B 67  ? 1.5553 0.8054 0.6175 0.1512  -0.1037 -0.1998 65  LYS B O   
3624 C CB  . LYS B 67  ? 1.3632 0.6483 0.4831 0.1301  -0.1133 -0.1680 65  LYS B CB  
3625 C CG  . LYS B 67  ? 1.3357 0.6531 0.5303 0.1166  -0.1387 -0.2017 65  LYS B CG  
3626 C CD  . LYS B 67  ? 1.3976 0.7259 0.5768 0.1365  -0.1714 -0.2146 65  LYS B CD  
3627 C CE  . LYS B 67  ? 1.3292 0.6928 0.5930 0.1224  -0.1951 -0.2531 65  LYS B CE  
3628 N NZ  . LYS B 67  ? 1.3590 0.7345 0.6083 0.1477  -0.2349 -0.2764 65  LYS B NZ  
3629 N N   . GLY B 68  ? 1.3514 0.6347 0.5533 0.1002  -0.0940 -0.2102 66  GLY B N   
3630 C CA  . GLY B 68  ? 1.3821 0.6613 0.5945 0.1059  -0.1041 -0.2454 66  GLY B CA  
3631 C C   . GLY B 68  ? 1.3691 0.6318 0.5893 0.0922  -0.0731 -0.2293 66  GLY B C   
3632 O O   . GLY B 68  ? 1.3646 0.6287 0.6357 0.0797  -0.0722 -0.2515 66  GLY B O   
3633 N N   . ARG B 69  ? 1.3650 0.6112 0.5403 0.0949  -0.0470 -0.1924 67  ARG B N   
3634 C CA  . ARG B 69  ? 1.3541 0.5857 0.5362 0.0850  -0.0189 -0.1781 67  ARG B CA  
3635 C C   . ARG B 69  ? 1.3436 0.5805 0.5762 0.0599  0.0025  -0.1511 67  ARG B C   
3636 O O   . ARG B 69  ? 1.3974 0.6254 0.6587 0.0489  0.0177  -0.1492 67  ARG B O   
3637 C CB  . ARG B 69  ? 1.3871 0.5981 0.4989 0.1035  -0.0002 -0.1587 67  ARG B CB  
3638 C CG  . ARG B 69  ? 1.4530 0.6533 0.4923 0.1351  -0.0183 -0.1743 67  ARG B CG  
3639 C CD  . ARG B 69  ? 1.5071 0.6846 0.4813 0.1510  0.0100  -0.1467 67  ARG B CD  
3640 N NE  . ARG B 69  ? 1.4736 0.6482 0.4463 0.1428  0.0291  -0.1116 67  ARG B NE  
3641 C CZ  . ARG B 69  ? 1.4369 0.6040 0.4196 0.1325  0.0636  -0.0853 67  ARG B CZ  
3642 N NH1 . ARG B 69  ? 1.4405 0.5994 0.4306 0.1289  0.0838  -0.0890 67  ARG B NH1 
3643 N NH2 . ARG B 69  ? 1.4116 0.5810 0.4027 0.1264  0.0769  -0.0582 67  ARG B NH2 
3644 N N   . PHE B 70  ? 1.3291 0.5788 0.5699 0.0536  0.0029  -0.1311 68  PHE B N   
3645 C CA  . PHE B 70  ? 1.2203 0.4760 0.5016 0.0350  0.0202  -0.1072 68  PHE B CA  
3646 C C   . PHE B 70  ? 1.1996 0.4713 0.5346 0.0194  0.0103  -0.1187 68  PHE B C   
3647 O O   . PHE B 70  ? 1.2095 0.4952 0.5504 0.0233  -0.0118 -0.1393 68  PHE B O   
3648 C CB  . PHE B 70  ? 1.2836 0.5440 0.5434 0.0386  0.0305  -0.0781 68  PHE B CB  
3649 C CG  . PHE B 70  ? 1.3121 0.5571 0.5414 0.0473  0.0516  -0.0629 68  PHE B CG  
3650 C CD1 . PHE B 70  ? 1.2502 0.4777 0.4479 0.0586  0.0558  -0.0758 68  PHE B CD1 
3651 C CD2 . PHE B 70  ? 1.3400 0.5899 0.5778 0.0449  0.0676  -0.0392 68  PHE B CD2 
3652 C CE1 . PHE B 70  ? 1.2740 0.4883 0.4499 0.0655  0.0792  -0.0636 68  PHE B CE1 
3653 C CE2 . PHE B 70  ? 1.3715 0.6098 0.5941 0.0517  0.0890  -0.0297 68  PHE B CE2 
3654 C CZ  . PHE B 70  ? 1.3851 0.6049 0.5771 0.0611  0.0966  -0.0411 68  PHE B CZ  
3655 N N   . THR B 71  ? 1.2515 0.5192 0.6251 0.0038  0.0280  -0.1059 69  THR B N   
3656 C CA  . THR B 71  ? 1.2555 0.5332 0.6817 -0.0126 0.0289  -0.1122 69  THR B CA  
3657 C C   . THR B 71  ? 1.3154 0.5902 0.7505 -0.0201 0.0502  -0.0806 69  THR B C   
3658 O O   . THR B 71  ? 1.3798 0.6354 0.8081 -0.0186 0.0665  -0.0656 69  THR B O   
3659 C CB  . THR B 71  ? 1.2538 0.5199 0.7232 -0.0221 0.0311  -0.1382 69  THR B CB  
3660 O OG1 . THR B 71  ? 1.3115 0.5820 0.7691 -0.0101 0.0073  -0.1722 69  THR B OG1 
3661 C CG2 . THR B 71  ? 1.2320 0.5073 0.7626 -0.0403 0.0375  -0.1465 69  THR B CG2 
3662 N N   . ILE B 72  ? 1.1548 0.4489 0.6036 -0.0252 0.0480  -0.0726 70  ILE B N   
3663 C CA  . ILE B 72  ? 1.1291 0.4231 0.5824 -0.0284 0.0653  -0.0457 70  ILE B CA  
3664 C C   . ILE B 72  ? 1.1553 0.4449 0.6527 -0.0438 0.0803  -0.0486 70  ILE B C   
3665 O O   . ILE B 72  ? 1.1032 0.4037 0.6379 -0.0541 0.0730  -0.0731 70  ILE B O   
3666 C CB  . ILE B 72  ? 1.2200 0.5377 0.6572 -0.0219 0.0561  -0.0333 70  ILE B CB  
3667 C CG1 . ILE B 72  ? 1.1952 0.5113 0.6241 -0.0166 0.0703  -0.0076 70  ILE B CG1 
3668 C CG2 . ILE B 72  ? 1.1368 0.4776 0.6029 -0.0304 0.0453  -0.0462 70  ILE B CG2 
3669 C CD1 . ILE B 72  ? 1.0289 0.3710 0.4568 -0.0127 0.0626  0.0011  70  ILE B CD1 
3670 N N   . SER B 73  ? 1.1315 0.4032 0.6255 -0.0434 0.1027  -0.0249 71  SER B N   
3671 C CA  . SER B 73  ? 1.1578 0.4164 0.6856 -0.0560 0.1263  -0.0204 71  SER B CA  
3672 C C   . SER B 73  ? 1.1194 0.3691 0.6203 -0.0458 0.1432  0.0110  71  SER B C   
3673 O O   . SER B 73  ? 1.1103 0.3600 0.5741 -0.0291 0.1360  0.0252  71  SER B O   
3674 C CB  . SER B 73  ? 1.3351 0.5608 0.8878 -0.0640 0.1424  -0.0296 71  SER B CB  
3675 O OG  . SER B 73  ? 1.1942 0.3938 0.7122 -0.0508 0.1470  -0.0144 71  SER B OG  
3676 N N   . ARG B 74  ? 1.1347 0.3769 0.6565 -0.0544 0.1664  0.0193  72  ARG B N   
3677 C CA  . ARG B 74  ? 1.2278 0.4607 0.7187 -0.0412 0.1829  0.0475  72  ARG B CA  
3678 C C   . ARG B 74  ? 1.2287 0.4188 0.7270 -0.0456 0.2213  0.0631  72  ARG B C   
3679 O O   . ARG B 74  ? 1.2137 0.3920 0.7599 -0.0657 0.2377  0.0485  72  ARG B O   
3680 C CB  . ARG B 74  ? 1.1168 0.3867 0.6144 -0.0426 0.1752  0.0462  72  ARG B CB  
3681 C CG  . ARG B 74  ? 1.1220 0.4010 0.6715 -0.0641 0.1906  0.0316  72  ARG B CG  
3682 C CD  . ARG B 74  ? 1.1367 0.4504 0.6907 -0.0632 0.1855  0.0321  72  ARG B CD  
3683 N NE  . ARG B 74  ? 1.3602 0.6785 0.8639 -0.0403 0.1795  0.0541  72  ARG B NE  
3684 C CZ  . ARG B 74  ? 1.2227 0.5777 0.7212 -0.0329 0.1570  0.0502  72  ARG B CZ  
3685 N NH1 . ARG B 74  ? 1.1706 0.5581 0.7031 -0.0451 0.1380  0.0287  72  ARG B NH1 
3686 N NH2 . ARG B 74  ? 1.1727 0.5314 0.6329 -0.0108 0.1520  0.0660  72  ARG B NH2 
3687 N N   . ASP B 75  ? 1.3470 0.5121 0.7981 -0.0246 0.2359  0.0917  73  ASP B N   
3688 C CA  . ASP B 75  ? 1.2912 0.4075 0.7326 -0.0221 0.2770  0.1146  73  ASP B CA  
3689 C C   . ASP B 75  ? 1.3041 0.4293 0.7013 0.0012  0.2833  0.1366  73  ASP B C   
3690 O O   . ASP B 75  ? 1.3681 0.4983 0.7220 0.0306  0.2678  0.1468  73  ASP B O   
3691 C CB  . ASP B 75  ? 1.3203 0.4117 0.7514 -0.0100 0.2799  0.1207  73  ASP B CB  
3692 C CG  . ASP B 75  ? 1.4162 0.4805 0.8658 -0.0125 0.3184  0.1338  73  ASP B CG  
3693 O OD1 . ASP B 75  ? 1.4072 0.4703 0.8875 -0.0286 0.3461  0.1345  73  ASP B OD1 
3694 O OD2 . ASP B 75  ? 1.5170 0.5599 0.9521 0.0017  0.3225  0.1428  73  ASP B OD2 
3695 N N   . ASN B 76  ? 1.3290 0.4597 0.7423 -0.0110 0.3044  0.1389  74  ASN B N   
3696 C CA  . ASN B 76  ? 1.3583 0.5023 0.7314 0.0119  0.3098  0.1557  74  ASN B CA  
3697 C C   . ASN B 76  ? 1.3794 0.5008 0.7170 0.0393  0.3302  0.1761  74  ASN B C   
3698 O O   . ASN B 76  ? 1.4784 0.6094 0.7693 0.0698  0.3216  0.1864  74  ASN B O   
3699 C CB  . ASN B 76  ? 1.3220 0.4813 0.7294 -0.0089 0.3314  0.1501  74  ASN B CB  
3700 C CG  . ASN B 76  ? 1.3023 0.5193 0.7653 -0.0302 0.2967  0.1164  74  ASN B CG  
3701 O OD1 . ASN B 76  ? 1.2337 0.4813 0.6833 -0.0204 0.2573  0.1070  74  ASN B OD1 
3702 N ND2 . ASN B 76  ? 1.3488 0.5790 0.8760 -0.0580 0.3122  0.0973  74  ASN B ND2 
3703 N N   . ALA B 77  ? 1.4214 0.5114 0.7804 0.0309  0.3554  0.1802  75  ALA B N   
3704 C CA  . ALA B 77  ? 1.4871 0.5475 0.8082 0.0578  0.3766  0.2010  75  ALA B CA  
3705 C C   . ALA B 77  ? 1.4884 0.5499 0.7578 0.0926  0.3437  0.2044  75  ALA B C   
3706 O O   . ALA B 77  ? 1.5450 0.5942 0.7638 0.1262  0.3470  0.2186  75  ALA B O   
3707 C CB  . ALA B 77  ? 1.5289 0.5550 0.8900 0.0396  0.4099  0.2032  75  ALA B CB  
3708 N N   . LYS B 78  ? 1.4416 0.5157 0.7236 0.0865  0.3125  0.1895  76  LYS B N   
3709 C CA  . LYS B 78  ? 1.4401 0.5162 0.6845 0.1166  0.2824  0.1881  76  LYS B CA  
3710 C C   . LYS B 78  ? 1.3857 0.5003 0.6186 0.1269  0.2463  0.1757  76  LYS B C   
3711 O O   . LYS B 78  ? 1.3793 0.4987 0.5903 0.1503  0.2201  0.1698  76  LYS B O   
3712 C CB  . LYS B 78  ? 1.4344 0.4943 0.7006 0.1060  0.2757  0.1798  76  LYS B CB  
3713 C CG  . LYS B 78  ? 1.4899 0.5112 0.7728 0.0970  0.3096  0.1905  76  LYS B CG  
3714 C CD  . LYS B 78  ? 1.5922 0.5953 0.8790 0.1011  0.2979  0.1851  76  LYS B CD  
3715 C CE  . LYS B 78  ? 1.6655 0.6682 1.0115 0.0657  0.3016  0.1677  76  LYS B CE  
3716 N NZ  . LYS B 78  ? 1.4367 0.4727 0.8007 0.0491  0.2763  0.1475  76  LYS B NZ  
3717 N N   . ASN B 79  ? 1.3498 0.4901 0.6000 0.1102  0.2453  0.1705  77  ASN B N   
3718 C CA  . ASN B 79  ? 1.3295 0.5064 0.5740 0.1179  0.2132  0.1589  77  ASN B CA  
3719 C C   . ASN B 79  ? 1.2862 0.4706 0.5457 0.1117  0.1869  0.1439  77  ASN B C   
3720 O O   . ASN B 79  ? 1.2557 0.4582 0.5021 0.1313  0.1604  0.1360  77  ASN B O   
3721 C CB  . ASN B 79  ? 1.3221 0.5095 0.5237 0.1578  0.1999  0.1630  77  ASN B CB  
3722 C CG  . ASN B 79  ? 1.3463 0.5397 0.5339 0.1629  0.2192  0.1728  77  ASN B CG  
3723 O OD1 . ASN B 79  ? 1.4732 0.6480 0.6747 0.1432  0.2531  0.1830  77  ASN B OD1 
3724 N ND2 . ASN B 79  ? 1.3405 0.5597 0.5037 0.1900  0.1987  0.1678  77  ASN B ND2 
3725 N N   . THR B 80  ? 1.2775 0.4461 0.5665 0.0852  0.1955  0.1382  78  THR B N   
3726 C CA  . THR B 80  ? 1.2949 0.4652 0.5957 0.0792  0.1755  0.1239  78  THR B CA  
3727 C C   . THR B 80  ? 1.2528 0.4402 0.5948 0.0466  0.1728  0.1072  78  THR B C   
3728 O O   . THR B 80  ? 1.2083 0.3900 0.5745 0.0263  0.1912  0.1064  78  THR B O   
3729 C CB  . THR B 80  ? 1.2685 0.4102 0.5661 0.0866  0.1816  0.1254  78  THR B CB  
3730 O OG1 . THR B 80  ? 1.2908 0.4075 0.6072 0.0698  0.2103  0.1323  78  THR B OG1 
3731 C CG2 . THR B 80  ? 1.2881 0.4233 0.5485 0.1235  0.1743  0.1340  78  THR B CG2 
3732 N N   . ILE B 81  ? 1.2447 0.4589 0.5997 0.0435  0.1494  0.0902  79  ILE B N   
3733 C CA  . ILE B 81  ? 1.3056 0.5383 0.6924 0.0200  0.1412  0.0709  79  ILE B CA  
3734 C C   . ILE B 81  ? 1.2265 0.4472 0.6123 0.0210  0.1339  0.0603  79  ILE B C   
3735 O O   . ILE B 81  ? 1.1634 0.3780 0.5312 0.0389  0.1284  0.0639  79  ILE B O   
3736 C CB  . ILE B 81  ? 1.1560 0.4319 0.5532 0.0167  0.1224  0.0618  79  ILE B CB  
3737 C CG1 . ILE B 81  ? 1.0812 0.3733 0.4635 0.0363  0.1076  0.0633  79  ILE B CG1 
3738 C CG2 . ILE B 81  ? 1.1529 0.4428 0.5592 0.0116  0.1302  0.0674  79  ILE B CG2 
3739 C CD1 . ILE B 81  ? 1.1397 0.4665 0.5359 0.0316  0.0912  0.0531  79  ILE B CD1 
3740 N N   . TYR B 82  ? 1.2281 0.4472 0.6359 0.0034  0.1328  0.0436  80  TYR B N   
3741 C CA  . TYR B 82  ? 1.3138 0.5202 0.7200 0.0039  0.1278  0.0310  80  TYR B CA  
3742 C C   . TYR B 82  ? 1.2515 0.4828 0.6622 -0.0032 0.1106  0.0116  80  TYR B C   
3743 O O   . TYR B 82  ? 1.2767 0.5284 0.7011 -0.0128 0.1031  0.0036  80  TYR B O   
3744 C CB  . TYR B 82  ? 1.3580 0.5305 0.7825 -0.0056 0.1435  0.0266  80  TYR B CB  
3745 C CG  . TYR B 82  ? 1.3837 0.5206 0.7960 0.0039  0.1649  0.0496  80  TYR B CG  
3746 C CD1 . TYR B 82  ? 1.4234 0.5433 0.8054 0.0264  0.1634  0.0621  80  TYR B CD1 
3747 C CD2 . TYR B 82  ? 1.3510 0.4692 0.7815 -0.0072 0.1879  0.0581  80  TYR B CD2 
3748 C CE1 . TYR B 82  ? 1.4728 0.5653 0.8383 0.0411  0.1794  0.0825  80  TYR B CE1 
3749 C CE2 . TYR B 82  ? 1.4523 0.5368 0.8645 0.0052  0.2106  0.0823  80  TYR B CE2 
3750 C CZ  . TYR B 82  ? 1.4707 0.5521 0.8510 0.0310  0.2028  0.0933  80  TYR B CZ  
3751 O OH  . TYR B 82  ? 1.4611 0.5256 0.8248 0.0482  0.2194  0.1132  80  TYR B OH  
3752 N N   . LEU B 83  ? 1.2055 0.4329 0.6017 0.0041  0.1051  0.0038  81  LEU B N   
3753 C CA  . LEU B 83  ? 1.2538 0.4952 0.6410 0.0027  0.0922  -0.0126 81  LEU B CA  
3754 C C   . LEU B 83  ? 1.2334 0.4553 0.6150 0.0049  0.0939  -0.0273 81  LEU B C   
3755 O O   . LEU B 83  ? 1.1569 0.3697 0.5259 0.0149  0.0998  -0.0233 81  LEU B O   
3756 C CB  . LEU B 83  ? 1.0909 0.3507 0.4601 0.0125  0.0878  -0.0045 81  LEU B CB  
3757 C CG  . LEU B 83  ? 1.1453 0.4118 0.4937 0.0150  0.0791  -0.0158 81  LEU B CG  
3758 C CD1 . LEU B 83  ? 1.1228 0.4034 0.4768 0.0083  0.0644  -0.0252 81  LEU B CD1 
3759 C CD2 . LEU B 83  ? 1.1030 0.3782 0.4385 0.0245  0.0841  -0.0053 81  LEU B CD2 
3760 N N   . GLN B 84  ? 1.2862 0.5038 0.6824 -0.0034 0.0879  -0.0480 82  GLN B N   
3761 C CA  . GLN B 84  ? 1.2618 0.4636 0.6550 -0.0005 0.0866  -0.0673 82  GLN B CA  
3762 C C   . GLN B 84  ? 1.2623 0.4754 0.6214 0.0097  0.0736  -0.0810 82  GLN B C   
3763 O O   . GLN B 84  ? 1.2809 0.5081 0.6368 0.0096  0.0579  -0.0948 82  GLN B O   
3764 C CB  . GLN B 84  ? 1.2524 0.4436 0.6853 -0.0128 0.0864  -0.0873 82  GLN B CB  
3765 C CG  . GLN B 84  ? 1.3543 0.5290 0.7913 -0.0093 0.0845  -0.1102 82  GLN B CG  
3766 C CD  . GLN B 84  ? 1.3858 0.5369 0.8133 -0.0025 0.0995  -0.0953 82  GLN B CD  
3767 O OE1 . GLN B 84  ? 1.3480 0.4978 0.7492 0.0088  0.0977  -0.1007 82  GLN B OE1 
3768 N NE2 . GLN B 84  ? 1.5486 0.6789 0.9960 -0.0073 0.1153  -0.0769 82  GLN B NE2 
3769 N N   . MET B 85  ? 1.2456 0.4506 0.5778 0.0207  0.0813  -0.0775 83  MET B N   
3770 C CA  . MET B 85  ? 1.2743 0.4815 0.5651 0.0333  0.0770  -0.0865 83  MET B CA  
3771 C C   . MET B 85  ? 1.4286 0.6219 0.7117 0.0391  0.0739  -0.1119 83  MET B C   
3772 O O   . MET B 85  ? 1.6167 0.7963 0.9103 0.0394  0.0856  -0.1125 83  MET B O   
3773 C CB  . MET B 85  ? 1.2755 0.4831 0.5471 0.0410  0.0934  -0.0673 83  MET B CB  
3774 C CG  . MET B 85  ? 1.2734 0.4962 0.5623 0.0362  0.0957  -0.0457 83  MET B CG  
3775 S SD  . MET B 85  ? 1.1949 0.4202 0.4935 0.0428  0.1147  -0.0306 83  MET B SD  
3776 C CE  . MET B 85  ? 1.2648 0.4758 0.5305 0.0532  0.1302  -0.0408 83  MET B CE  
3777 N N   . ASN B 86  ? 1.4530 0.6505 0.7182 0.0464  0.0556  -0.1356 84  ASN B N   
3778 C CA  . ASN B 86  ? 1.5073 0.6954 0.7726 0.0528  0.0473  -0.1667 84  ASN B CA  
3779 C C   . ASN B 86  ? 1.6202 0.7992 0.8255 0.0737  0.0518  -0.1729 84  ASN B C   
3780 O O   . ASN B 86  ? 1.6976 0.8647 0.8982 0.0762  0.0696  -0.1695 84  ASN B O   
3781 C CB  . ASN B 86  ? 1.5173 0.7170 0.8069 0.0513  0.0214  -0.1977 84  ASN B CB  
3782 C CG  . ASN B 86  ? 1.4903 0.6886 0.8517 0.0300  0.0247  -0.2040 84  ASN B CG  
3783 O OD1 . ASN B 86  ? 1.5059 0.7170 0.9055 0.0228  0.0098  -0.2245 84  ASN B OD1 
3784 N ND2 . ASN B 86  ? 1.5069 0.6877 0.8882 0.0213  0.0459  -0.1870 84  ASN B ND2 
3785 N N   . SER B 87  ? 1.5638 0.7462 0.7212 0.0911  0.0366  -0.1830 85  SER B N   
3786 C CA  . SER B 87  ? 1.5588 0.7267 0.6470 0.1145  0.0457  -0.1846 85  SER B CA  
3787 C C   . SER B 87  ? 1.4875 0.6492 0.5487 0.1151  0.0727  -0.1481 85  SER B C   
3788 O O   . SER B 87  ? 1.5876 0.7571 0.6469 0.1121  0.0686  -0.1304 85  SER B O   
3789 C CB  . SER B 87  ? 1.5006 0.6725 0.5433 0.1384  0.0176  -0.2089 85  SER B CB  
3790 O OG  . SER B 87  ? 1.5051 0.6902 0.5914 0.1361  -0.0100 -0.2478 85  SER B OG  
3791 N N   . LEU B 88  ? 1.4499 0.5987 0.4978 0.1183  0.1010  -0.1394 86  LEU B N   
3792 C CA  . LEU B 88  ? 1.4320 0.5774 0.4790 0.1144  0.1308  -0.1093 86  LEU B CA  
3793 C C   . LEU B 88  ? 1.5352 0.6596 0.5187 0.1346  0.1566  -0.1045 86  LEU B C   
3794 O O   . LEU B 88  ? 1.5135 0.6344 0.4962 0.1397  0.1699  -0.1150 86  LEU B O   
3795 C CB  . LEU B 88  ? 1.4072 0.5592 0.5145 0.0980  0.1450  -0.1035 86  LEU B CB  
3796 C CG  . LEU B 88  ? 1.3918 0.5603 0.5489 0.0816  0.1390  -0.0861 86  LEU B CG  
3797 C CD1 . LEU B 88  ? 1.4644 0.6421 0.6383 0.0739  0.1105  -0.0956 86  LEU B CD1 
3798 C CD2 . LEU B 88  ? 1.3961 0.5666 0.6010 0.0736  0.1501  -0.0836 86  LEU B CD2 
3799 N N   . ASN B 89  ? 1.6433 0.7642 0.5926 0.1443  0.1626  -0.0833 87  ASN B N   
3800 C CA  . ASN B 89  ? 1.5600 0.6668 0.4721 0.1594  0.1930  -0.0664 87  ASN B CA  
3801 C C   . ASN B 89  ? 1.5351 0.6338 0.4768 0.1465  0.2337  -0.0472 87  ASN B C   
3802 O O   . ASN B 89  ? 1.4900 0.5990 0.4758 0.1297  0.2314  -0.0422 87  ASN B O   
3803 C CB  . ASN B 89  ? 1.6010 0.7024 0.4668 0.1785  0.1808  -0.0527 87  ASN B CB  
3804 C CG  . ASN B 89  ? 1.5608 0.6684 0.4446 0.1683  0.1696  -0.0381 87  ASN B CG  
3805 O OD1 . ASN B 89  ? 1.5462 0.6475 0.4487 0.1585  0.1968  -0.0161 87  ASN B OD1 
3806 N ND2 . ASN B 89  ? 1.5511 0.6732 0.4344 0.1708  0.1294  -0.0532 87  ASN B ND2 
3807 N N   . PRO B 90  ? 1.5745 0.6589 0.5027 0.1541  0.2711  -0.0380 88  PRO B N   
3808 C CA  . PRO B 90  ? 1.6156 0.6945 0.5840 0.1418  0.3128  -0.0257 88  PRO B CA  
3809 C C   . PRO B 90  ? 1.5330 0.6096 0.5118 0.1362  0.3208  -0.0030 88  PRO B C   
3810 O O   . PRO B 90  ? 1.4924 0.5788 0.5309 0.1220  0.3418  0.0014  88  PRO B O   
3811 C CB  . PRO B 90  ? 1.6133 0.6747 0.5593 0.1534  0.3514  -0.0206 88  PRO B CB  
3812 C CG  . PRO B 90  ? 1.6509 0.7150 0.5571 0.1682  0.3264  -0.0389 88  PRO B CG  
3813 C CD  . PRO B 90  ? 1.6415 0.7156 0.5245 0.1739  0.2786  -0.0436 88  PRO B CD  
3814 N N   . GLY B 91  ? 1.5543 0.6272 0.4958 0.1471  0.2986  0.0094  89  GLY B N   
3815 C CA  . GLY B 91  ? 1.5337 0.6068 0.4902 0.1420  0.3019  0.0295  89  GLY B CA  
3816 C C   . GLY B 91  ? 1.4731 0.5728 0.4784 0.1235  0.2767  0.0245  89  GLY B C   
3817 O O   . GLY B 91  ? 1.6017 0.7092 0.6358 0.1168  0.2786  0.0395  89  GLY B O   
3818 N N   . ASP B 92  ? 1.4623 0.5841 0.4980 0.1147  0.2490  0.0044  90  ASP B N   
3819 C CA  . ASP B 92  ? 1.4047 0.5583 0.5037 0.0976  0.2222  0.0012  90  ASP B CA  
3820 C C   . ASP B 92  ? 1.3430 0.5136 0.5134 0.0855  0.2391  0.0005  90  ASP B C   
3821 O O   . ASP B 92  ? 1.2769 0.4714 0.4948 0.0755  0.2190  -0.0014 90  ASP B O   
3822 C CB  . ASP B 92  ? 1.3391 0.5024 0.4382 0.0949  0.1887  -0.0185 90  ASP B CB  
3823 C CG  . ASP B 92  ? 1.4004 0.5555 0.4446 0.1074  0.1635  -0.0256 90  ASP B CG  
3824 O OD1 . ASP B 92  ? 1.4721 0.6248 0.4946 0.1131  0.1581  -0.0126 90  ASP B OD1 
3825 O OD2 . ASP B 92  ? 1.4005 0.5521 0.4266 0.1132  0.1472  -0.0470 90  ASP B OD2 
3826 N N   . THR B 93  ? 1.3272 0.4858 0.5062 0.0885  0.2756  0.0000  91  THR B N   
3827 C CA  . THR B 93  ? 1.2873 0.4645 0.5413 0.0801  0.2901  -0.0066 91  THR B CA  
3828 C C   . THR B 93  ? 1.3557 0.5500 0.6547 0.0739  0.2904  0.0043  91  THR B C   
3829 O O   . THR B 93  ? 1.2756 0.4556 0.5650 0.0760  0.3163  0.0182  91  THR B O   
3830 C CB  . THR B 93  ? 1.3252 0.4862 0.5846 0.0843  0.3333  -0.0124 91  THR B CB  
3831 O OG1 . THR B 93  ? 1.3873 0.5367 0.6117 0.0905  0.3303  -0.0265 91  THR B OG1 
3832 C CG2 . THR B 93  ? 1.2839 0.4682 0.6319 0.0773  0.3461  -0.0250 91  THR B CG2 
3833 N N   . ALA B 94  ? 1.2073 0.4297 0.5536 0.0681  0.2630  -0.0020 92  ALA B N   
3834 C CA  . ALA B 94  ? 1.1582 0.4018 0.5497 0.0642  0.2574  0.0038  92  ALA B CA  
3835 C C   . ALA B 94  ? 1.1519 0.4232 0.5905 0.0637  0.2304  -0.0085 92  ALA B C   
3836 O O   . ALA B 94  ? 1.2398 0.5091 0.6689 0.0656  0.2158  -0.0167 92  ALA B O   
3837 C CB  . ALA B 94  ? 1.1889 0.4280 0.5403 0.0636  0.2421  0.0205  92  ALA B CB  
3838 N N   . VAL B 95  ? 1.1795 0.4744 0.6671 0.0635  0.2241  -0.0098 93  VAL B N   
3839 C CA  . VAL B 95  ? 1.0574 0.3773 0.5783 0.0685  0.1960  -0.0193 93  VAL B CA  
3840 C C   . VAL B 95  ? 1.0678 0.3922 0.5557 0.0649  0.1708  -0.0056 93  VAL B C   
3841 O O   . VAL B 95  ? 1.0238 0.3551 0.5129 0.0612  0.1701  0.0035  93  VAL B O   
3842 C CB  . VAL B 95  ? 1.0121 0.3588 0.6068 0.0740  0.1996  -0.0343 93  VAL B CB  
3843 C CG1 . VAL B 95  ? 1.0862 0.4579 0.6977 0.0831  0.1664  -0.0394 93  VAL B CG1 
3844 C CG2 . VAL B 95  ? 1.0206 0.3688 0.6606 0.0796  0.2176  -0.0559 93  VAL B CG2 
3845 N N   . TYR B 96  ? 1.1125 0.4316 0.5748 0.0656  0.1524  -0.0049 94  TYR B N   
3846 C CA  . TYR B 96  ? 1.0903 0.4111 0.5248 0.0602  0.1332  0.0056  94  TYR B CA  
3847 C C   . TYR B 96  ? 0.9927 0.3345 0.4520 0.0670  0.1157  0.0049  94  TYR B C   
3848 O O   . TYR B 96  ? 1.0477 0.3901 0.5204 0.0779  0.1104  -0.0026 94  TYR B O   
3849 C CB  . TYR B 96  ? 1.1787 0.4787 0.5766 0.0559  0.1281  0.0056  94  TYR B CB  
3850 C CG  . TYR B 96  ? 1.1191 0.4001 0.4807 0.0525  0.1386  0.0050  94  TYR B CG  
3851 C CD1 . TYR B 96  ? 1.1751 0.4446 0.5349 0.0568  0.1609  0.0003  94  TYR B CD1 
3852 C CD2 . TYR B 96  ? 1.1567 0.4312 0.4856 0.0475  0.1264  0.0066  94  TYR B CD2 
3853 C CE1 . TYR B 96  ? 1.2439 0.4927 0.5598 0.0584  0.1716  0.0005  94  TYR B CE1 
3854 C CE2 . TYR B 96  ? 1.1998 0.4564 0.4885 0.0507  0.1318  0.0031  94  TYR B CE2 
3855 C CZ  . TYR B 96  ? 1.2702 0.5124 0.5470 0.0572  0.1549  0.0016  94  TYR B CZ  
3856 O OH  . TYR B 96  ? 1.2938 0.5151 0.5203 0.0649  0.1615  -0.0011 94  TYR B OH  
3857 N N   . SER B 97  ? 1.0352 0.3927 0.4968 0.0635  0.1062  0.0119  95  SER B N   
3858 C CA  . SER B 97  ? 0.9533 0.3319 0.4331 0.0720  0.0906  0.0109  95  SER B CA  
3859 C C   . SER B 97  ? 0.9902 0.3693 0.4449 0.0637  0.0803  0.0215  95  SER B C   
3860 O O   . SER B 97  ? 0.9528 0.3299 0.3940 0.0526  0.0807  0.0263  95  SER B O   
3861 C CB  . SER B 97  ? 0.9984 0.4031 0.5220 0.0775  0.0899  0.0033  95  SER B CB  
3862 O OG  . SER B 97  ? 1.0218 0.4290 0.5824 0.0845  0.1017  -0.0110 95  SER B OG  
3863 N N   . CYS B 98  ? 1.1552 0.5351 0.6031 0.0712  0.0722  0.0244  96  CYS B N   
3864 C CA  . CYS B 98  ? 1.1521 0.5344 0.5853 0.0636  0.0672  0.0330  96  CYS B CA  
3865 C C   . CYS B 98  ? 1.1332 0.5443 0.5845 0.0723  0.0570  0.0318  96  CYS B C   
3866 O O   . CYS B 98  ? 1.1106 0.5345 0.5782 0.0901  0.0510  0.0245  96  CYS B O   
3867 C CB  . CYS B 98  ? 1.1826 0.5411 0.5940 0.0662  0.0719  0.0398  96  CYS B CB  
3868 S SG  . CYS B 98  ? 1.5390 0.9029 0.9399 0.0830  0.0683  0.0483  96  CYS B SG  
3869 N N   . ALA B 99  ? 0.9527 0.3762 0.4046 0.0613  0.0530  0.0353  97  ALA B N   
3870 C CA  . ALA B 99  ? 1.0240 0.4767 0.4952 0.0679  0.0430  0.0324  97  ALA B CA  
3871 C C   . ALA B 99  ? 1.0721 0.5285 0.5309 0.0621  0.0427  0.0386  97  ALA B C   
3872 O O   . ALA B 99  ? 1.0734 0.5135 0.5195 0.0477  0.0497  0.0427  97  ALA B O   
3873 C CB  . ALA B 99  ? 0.9711 0.4392 0.4662 0.0612  0.0396  0.0280  97  ALA B CB  
3874 N N   . ALA B 100 ? 0.9589 0.4384 0.4263 0.0740  0.0354  0.0363  98  ALA B N   
3875 C CA  . ALA B 100 ? 0.9779 0.4635 0.4363 0.0704  0.0389  0.0414  98  ALA B CA  
3876 C C   . ALA B 100 ? 0.9386 0.4588 0.4236 0.0697  0.0266  0.0331  98  ALA B C   
3877 O O   . ALA B 100 ? 0.8895 0.4299 0.3974 0.0809  0.0152  0.0238  98  ALA B O   
3878 C CB  . ALA B 100 ? 0.9609 0.4350 0.3906 0.0910  0.0456  0.0487  98  ALA B CB  
3879 N N   . THR B 101 ? 0.8667 0.3943 0.3553 0.0562  0.0294  0.0338  99  THR B N   
3880 C CA  . THR B 101 ? 0.8411 0.4012 0.3555 0.0554  0.0175  0.0252  99  THR B CA  
3881 C C   . THR B 101 ? 0.8765 0.4417 0.3918 0.0439  0.0263  0.0256  99  THR B C   
3882 O O   . THR B 101 ? 0.9638 0.5071 0.4698 0.0310  0.0405  0.0302  99  THR B O   
3883 C CB  . THR B 101 ? 0.9361 0.5026 0.4727 0.0462  0.0058  0.0194  99  THR B CB  
3884 O OG1 . THR B 101 ? 0.7947 0.3918 0.3604 0.0530  -0.0071 0.0106  99  THR B OG1 
3885 C CG2 . THR B 101 ? 0.9447 0.5022 0.4794 0.0280  0.0057  0.0181  99  THR B CG2 
3886 N N   . LEU B 102 ? 0.9012 0.4965 0.4341 0.0486  0.0191  0.0182  100 LEU B N   
3887 C CA  . LEU B 102 ? 0.8930 0.4986 0.4362 0.0373  0.0285  0.0149  100 LEU B CA  
3888 C C   . LEU B 102 ? 0.9272 0.5425 0.5003 0.0187  0.0162  0.0034  100 LEU B C   
3889 O O   . LEU B 102 ? 0.8246 0.4436 0.4066 0.0198  -0.0014 -0.0002 100 LEU B O   
3890 C CB  . LEU B 102 ? 1.0504 0.6854 0.5983 0.0525  0.0256  0.0095  100 LEU B CB  
3891 C CG  . LEU B 102 ? 1.0195 0.6423 0.5284 0.0719  0.0443  0.0202  100 LEU B CG  
3892 C CD1 . LEU B 102 ? 0.9502 0.5404 0.4410 0.0584  0.0754  0.0333  100 LEU B CD1 
3893 C CD2 . LEU B 102 ? 1.0628 0.6740 0.5458 0.0960  0.0354  0.0242  100 LEU B CD2 
3894 N N   . PRO B 103 ? 0.9127 0.5300 0.5025 0.0033  0.0260  -0.0034 101 PRO B N   
3895 C CA  . PRO B 103 ? 0.8394 0.4656 0.4571 -0.0100 0.0093  -0.0192 101 PRO B CA  
3896 C C   . PRO B 103 ? 0.8750 0.5299 0.5138 -0.0039 -0.0146 -0.0288 101 PRO B C   
3897 O O   . PRO B 103 ? 0.8980 0.5512 0.5435 -0.0060 -0.0338 -0.0365 101 PRO B O   
3898 C CB  . PRO B 103 ? 0.8769 0.5067 0.5208 -0.0258 0.0268  -0.0297 101 PRO B CB  
3899 C CG  . PRO B 103 ? 0.9199 0.5255 0.5384 -0.0235 0.0583  -0.0127 101 PRO B CG  
3900 C CD  . PRO B 103 ? 0.9662 0.5737 0.5512 -0.0015 0.0547  0.0017  101 PRO B CD  
3901 N N   . ALA B 104 ? 0.9606 0.6396 0.6075 0.0062  -0.0144 -0.0291 102 ALA B N   
3902 C CA  . ALA B 104 ? 0.8454 0.5513 0.5181 0.0122  -0.0366 -0.0393 102 ALA B CA  
3903 C C   . ALA B 104 ? 0.8420 0.5359 0.5069 0.0212  -0.0499 -0.0324 102 ALA B C   
3904 O O   . ALA B 104 ? 0.8844 0.5874 0.5684 0.0235  -0.0675 -0.0385 102 ALA B O   
3905 C CB  . ALA B 104 ? 0.9276 0.6630 0.6116 0.0230  -0.0331 -0.0440 102 ALA B CB  
3906 N N   . TRP B 105 ? 0.8655 0.5372 0.5050 0.0267  -0.0398 -0.0200 103 TRP B N   
3907 C CA  . TRP B 105 ? 0.8255 0.4836 0.4632 0.0333  -0.0458 -0.0143 103 TRP B CA  
3908 C C   . TRP B 105 ? 0.8684 0.4998 0.4894 0.0259  -0.0500 -0.0105 103 TRP B C   
3909 O O   . TRP B 105 ? 0.8843 0.5038 0.5053 0.0311  -0.0548 -0.0059 103 TRP B O   
3910 C CB  . TRP B 105 ? 0.8254 0.4705 0.4466 0.0425  -0.0340 -0.0065 103 TRP B CB  
3911 C CG  . TRP B 105 ? 0.7496 0.4191 0.3816 0.0581  -0.0351 -0.0128 103 TRP B CG  
3912 C CD1 . TRP B 105 ? 0.7728 0.4593 0.3991 0.0625  -0.0313 -0.0164 103 TRP B CD1 
3913 C CD2 . TRP B 105 ? 0.7592 0.4383 0.4092 0.0743  -0.0402 -0.0190 103 TRP B CD2 
3914 N NE1 . TRP B 105 ? 0.8406 0.5459 0.4713 0.0838  -0.0365 -0.0238 103 TRP B NE1 
3915 C CE2 . TRP B 105 ? 0.7991 0.5026 0.4493 0.0913  -0.0443 -0.0281 103 TRP B CE2 
3916 C CE3 . TRP B 105 ? 0.7315 0.4009 0.4006 0.0771  -0.0402 -0.0199 103 TRP B CE3 
3917 C CZ2 . TRP B 105 ? 0.7619 0.4837 0.4327 0.1130  -0.0543 -0.0420 103 TRP B CZ2 
3918 C CZ3 . TRP B 105 ? 0.7216 0.4097 0.4207 0.0947  -0.0463 -0.0339 103 TRP B CZ3 
3919 C CH2 . TRP B 105 ? 0.7206 0.4362 0.4212 0.1134  -0.0562 -0.0467 103 TRP B CH2 
3920 N N   . THR B 106 ? 0.8784 0.4984 0.4850 0.0159  -0.0470 -0.0133 104 THR B N   
3921 C CA  . THR B 106 ? 0.9375 0.5330 0.5233 0.0137  -0.0545 -0.0139 104 THR B CA  
3922 C C   . THR B 106 ? 0.8787 0.4840 0.4768 0.0165  -0.0763 -0.0250 104 THR B C   
3923 O O   . THR B 106 ? 0.9384 0.5213 0.5125 0.0244  -0.0857 -0.0215 104 THR B O   
3924 C CB  . THR B 106 ? 0.8810 0.4631 0.4556 0.0036  -0.0463 -0.0190 104 THR B CB  
3925 O OG1 . THR B 106 ? 0.8372 0.4417 0.4419 -0.0060 -0.0473 -0.0337 104 THR B OG1 
3926 C CG2 . THR B 106 ? 0.9054 0.4726 0.4639 0.0034  -0.0254 -0.0066 104 THR B CG2 
3927 N N   . GLY B 107 ? 0.8456 0.4816 0.4772 0.0125  -0.0840 -0.0384 105 GLY B N   
3928 C CA  . GLY B 107 ? 0.8731 0.5198 0.5200 0.0169  -0.1078 -0.0520 105 GLY B CA  
3929 C C   . GLY B 107 ? 0.9410 0.5773 0.5792 0.0145  -0.1203 -0.0677 105 GLY B C   
3930 O O   . GLY B 107 ? 0.9439 0.5857 0.5958 0.0022  -0.1106 -0.0784 105 GLY B O   
3931 N N   . ILE B 108 ? 0.9228 0.5418 0.5382 0.0284  -0.1419 -0.0704 106 ILE B N   
3932 C CA  . ILE B 108 ? 0.9380 0.5476 0.5417 0.0334  -0.1617 -0.0904 106 ILE B CA  
3933 C C   . ILE B 108 ? 0.9870 0.5546 0.5304 0.0468  -0.1613 -0.0770 106 ILE B C   
3934 O O   . ILE B 108 ? 1.1051 0.6617 0.6348 0.0448  -0.1616 -0.0878 106 ILE B O   
3935 C CB  . ILE B 108 ? 0.9298 0.5557 0.5535 0.0451  -0.1939 -0.1120 106 ILE B CB  
3936 C CG1 . ILE B 108 ? 0.9067 0.5754 0.5959 0.0290  -0.1951 -0.1387 106 ILE B CG1 
3937 C CG2 . ILE B 108 ? 0.9383 0.5408 0.5251 0.0644  -0.2212 -0.1269 106 ILE B CG2 
3938 C CD1 . ILE B 108 ? 0.9898 0.6783 0.7077 0.0399  -0.2296 -0.1684 106 ILE B CD1 
3939 N N   . ILE B 109 ? 0.9893 0.5321 0.4987 0.0607  -0.1577 -0.0543 107 ILE B N   
3940 C CA  . ILE B 109 ? 0.9834 0.4827 0.4313 0.0751  -0.1514 -0.0386 107 ILE B CA  
3941 C C   . ILE B 109 ? 0.9706 0.4549 0.4096 0.0674  -0.1185 -0.0141 107 ILE B C   
3942 O O   . ILE B 109 ? 1.0080 0.4573 0.3998 0.0765  -0.1069 -0.0014 107 ILE B O   
3943 C CB  . ILE B 109 ? 1.0308 0.5014 0.4379 0.1007  -0.1675 -0.0301 107 ILE B CB  
3944 C CG1 . ILE B 109 ? 1.0141 0.4799 0.4366 0.1007  -0.1506 -0.0068 107 ILE B CG1 
3945 C CG2 . ILE B 109 ? 1.0431 0.5320 0.4644 0.1117  -0.2051 -0.0582 107 ILE B CG2 
3946 C CD1 . ILE B 109 ? 1.0551 0.4737 0.4301 0.1118  -0.1246 0.0222  107 ILE B CD1 
3947 N N   . GLY B 110 ? 0.9956 0.5056 0.4778 0.0535  -0.1040 -0.0095 108 GLY B N   
3948 C CA  . GLY B 110 ? 0.9297 0.4294 0.4114 0.0499  -0.0775 0.0086  108 GLY B CA  
3949 C C   . GLY B 110 ? 0.8984 0.4016 0.3822 0.0382  -0.0627 0.0069  108 GLY B C   
3950 O O   . GLY B 110 ? 0.9624 0.4739 0.4649 0.0341  -0.0466 0.0141  108 GLY B O   
3951 N N   . GLY B 111 ? 0.9176 0.4137 0.3842 0.0350  -0.0692 -0.0047 109 GLY B N   
3952 C CA  . GLY B 111 ? 0.9120 0.4053 0.3797 0.0247  -0.0539 -0.0053 109 GLY B CA  
3953 C C   . GLY B 111 ? 0.9801 0.4441 0.4157 0.0293  -0.0364 0.0081  109 GLY B C   
3954 O O   . GLY B 111 ? 1.0328 0.4951 0.4739 0.0228  -0.0215 0.0112  109 GLY B O   
3955 N N   . ARG B 112 ? 1.0587 0.4972 0.4597 0.0420  -0.0359 0.0167  110 ARG B N   
3956 C CA  . ARG B 112 ? 1.0704 0.4793 0.4399 0.0471  -0.0160 0.0281  110 ARG B CA  
3957 C C   . ARG B 112 ? 1.0555 0.4597 0.4405 0.0496  0.0046  0.0438  110 ARG B C   
3958 O O   . ARG B 112 ? 1.0193 0.3993 0.3851 0.0535  0.0252  0.0526  110 ARG B O   
3959 C CB  . ARG B 112 ? 1.0469 0.4244 0.3605 0.0623  -0.0234 0.0268  110 ARG B CB  
3960 C CG  . ARG B 112 ? 1.0623 0.4457 0.3668 0.0628  -0.0471 0.0039  110 ARG B CG  
3961 C CD  . ARG B 112 ? 1.1729 0.5255 0.4155 0.0851  -0.0593 -0.0002 110 ARG B CD  
3962 N NE  . ARG B 112 ? 1.2425 0.6035 0.4839 0.0878  -0.0848 -0.0292 110 ARG B NE  
3963 C CZ  . ARG B 112 ? 1.2795 0.6170 0.4694 0.1068  -0.0961 -0.0409 110 ARG B CZ  
3964 N NH1 . ARG B 112 ? 1.3907 0.6911 0.5174 0.1252  -0.0808 -0.0224 110 ARG B NH1 
3965 N NH2 . ARG B 112 ? 1.2094 0.5608 0.4137 0.1083  -0.1219 -0.0740 110 ARG B NH2 
3966 N N   . ARG B 113 ? 1.0021 0.4303 0.4271 0.0476  0.0002  0.0444  111 ARG B N   
3967 C CA  . ARG B 113 ? 0.9382 0.3643 0.3904 0.0505  0.0182  0.0538  111 ARG B CA  
3968 C C   . ARG B 113 ? 0.9026 0.3503 0.3931 0.0450  0.0272  0.0480  111 ARG B C   
3969 O O   . ARG B 113 ? 0.8728 0.3487 0.3837 0.0409  0.0147  0.0391  111 ARG B O   
3970 C CB  . ARG B 113 ? 1.0066 0.4476 0.4869 0.0537  0.0071  0.0540  111 ARG B CB  
3971 C CG  . ARG B 113 ? 1.0254 0.4564 0.5360 0.0576  0.0277  0.0630  111 ARG B CG  
3972 C CD  . ARG B 113 ? 1.2568 0.6399 0.7218 0.0679  0.0447  0.0808  111 ARG B CD  
3973 N NE  . ARG B 113 ? 1.3700 0.7349 0.8623 0.0679  0.0786  0.0898  111 ARG B NE  
3974 C CZ  . ARG B 113 ? 1.4071 0.7343 0.8650 0.0718  0.1069  0.1017  111 ARG B CZ  
3975 N NH1 . ARG B 113 ? 1.1546 0.4582 0.5444 0.0779  0.1029  0.1059  111 ARG B NH1 
3976 N NH2 . ARG B 113 ? 1.4493 0.7632 0.9465 0.0699  0.1409  0.1070  111 ARG B NH2 
3977 N N   . PRO B 114 ? 0.9099 0.3443 0.4101 0.0470  0.0491  0.0518  112 PRO B N   
3978 C CA  . PRO B 114 ? 0.9627 0.4175 0.4978 0.0468  0.0527  0.0423  112 PRO B CA  
3979 C C   . PRO B 114 ? 0.9366 0.4263 0.5241 0.0503  0.0425  0.0321  112 PRO B C   
3980 O O   . PRO B 114 ? 0.9665 0.4786 0.5687 0.0541  0.0338  0.0225  112 PRO B O   
3981 C CB  . PRO B 114 ? 0.9333 0.3658 0.4739 0.0491  0.0788  0.0451  112 PRO B CB  
3982 C CG  . PRO B 114 ? 0.9341 0.3398 0.4599 0.0510  0.0932  0.0580  112 PRO B CG  
3983 C CD  . PRO B 114 ? 0.9499 0.3487 0.4298 0.0518  0.0728  0.0636  112 PRO B CD  
3984 N N   . GLY B 115 ? 0.9164 0.4094 0.5299 0.0517  0.0433  0.0337  113 GLY B N   
3985 C CA  . GLY B 115 ? 0.8543 0.3828 0.5219 0.0561  0.0315  0.0204  113 GLY B CA  
3986 C C   . GLY B 115 ? 0.8545 0.4108 0.5148 0.0560  0.0084  0.0142  113 GLY B C   
3987 O O   . GLY B 115 ? 0.7682 0.3568 0.4673 0.0626  -0.0028 0.0008  113 GLY B O   
3988 N N   . ASN B 116 ? 0.8196 0.3646 0.4350 0.0496  0.0022  0.0211  114 ASN B N   
3989 C CA  . ASN B 116 ? 0.9182 0.4864 0.5296 0.0472  -0.0129 0.0150  114 ASN B CA  
3990 C C   . ASN B 116 ? 0.8032 0.3765 0.4024 0.0499  -0.0094 0.0126  114 ASN B C   
3991 O O   . ASN B 116 ? 0.8671 0.4536 0.4589 0.0479  -0.0147 0.0101  114 ASN B O   
3992 C CB  . ASN B 116 ? 0.9362 0.4914 0.5169 0.0392  -0.0207 0.0186  114 ASN B CB  
3993 C CG  . ASN B 116 ? 0.8413 0.4021 0.4354 0.0412  -0.0331 0.0172  114 ASN B CG  
3994 O OD1 . ASN B 116 ? 0.9261 0.4968 0.5534 0.0465  -0.0326 0.0160  114 ASN B OD1 
3995 N ND2 . ASN B 116 ? 0.8241 0.3786 0.3968 0.0382  -0.0456 0.0147  114 ASN B ND2 
3996 N N   . TYR B 117 ? 0.8406 0.4012 0.4376 0.0554  0.0012  0.0135  115 TYR B N   
3997 C CA  . TYR B 117 ? 0.9999 0.5581 0.5795 0.0619  0.0043  0.0129  115 TYR B CA  
3998 C C   . TYR B 117 ? 0.9692 0.5458 0.5794 0.0796  0.0006  0.0004  115 TYR B C   
3999 O O   . TYR B 117 ? 1.0048 0.5735 0.6344 0.0831  0.0080  -0.0042 115 TYR B O   
4000 C CB  . TYR B 117 ? 0.9863 0.5117 0.5340 0.0554  0.0166  0.0211  115 TYR B CB  
4001 C CG  . TYR B 117 ? 0.9924 0.5018 0.5124 0.0414  0.0166  0.0269  115 TYR B CG  
4002 C CD1 . TYR B 117 ? 0.9310 0.4327 0.4464 0.0357  0.0131  0.0285  115 TYR B CD1 
4003 C CD2 . TYR B 117 ? 0.9214 0.4218 0.4217 0.0360  0.0201  0.0290  115 TYR B CD2 
4004 C CE1 . TYR B 117 ? 0.8980 0.3884 0.3909 0.0274  0.0076  0.0275  115 TYR B CE1 
4005 C CE2 . TYR B 117 ? 0.9985 0.4884 0.4863 0.0236  0.0184  0.0274  115 TYR B CE2 
4006 C CZ  . TYR B 117 ? 1.0016 0.4890 0.4863 0.0204  0.0094  0.0244  115 TYR B CZ  
4007 O OH  . TYR B 117 ? 0.9287 0.4086 0.4034 0.0124  0.0024  0.0168  115 TYR B OH  
4008 N N   . PRO B 118 ? 0.8151 0.4170 0.4322 0.0933  -0.0109 -0.0083 116 PRO B N   
4009 C CA  . PRO B 118 ? 0.8731 0.4969 0.5233 0.1152  -0.0205 -0.0269 116 PRO B CA  
4010 C C   . PRO B 118 ? 1.0023 0.6108 0.6323 0.1301  -0.0182 -0.0288 116 PRO B C   
4011 O O   . PRO B 118 ? 1.0611 0.6780 0.7275 0.1424  -0.0218 -0.0457 116 PRO B O   
4012 C CB  . PRO B 118 ? 0.9235 0.5770 0.5752 0.1282  -0.0348 -0.0354 116 PRO B CB  
4013 C CG  . PRO B 118 ? 0.9199 0.5582 0.5254 0.1159  -0.0262 -0.0175 116 PRO B CG  
4014 C CD  . PRO B 118 ? 0.8680 0.4814 0.4665 0.0913  -0.0153 -0.0047 116 PRO B CD  
4015 N N   . TYR B 119 ? 1.0750 0.6603 0.6531 0.1299  -0.0114 -0.0137 117 TYR B N   
4016 C CA  . TYR B 119 ? 1.0604 0.6271 0.6131 0.1474  -0.0104 -0.0138 117 TYR B CA  
4017 C C   . TYR B 119 ? 0.9914 0.5278 0.5360 0.1316  0.0043  -0.0051 117 TYR B C   
4018 O O   . TYR B 119 ? 0.8889 0.4067 0.4137 0.1097  0.0157  0.0093  117 TYR B O   
4019 C CB  . TYR B 119 ? 1.1070 0.6593 0.6064 0.1585  -0.0070 -0.0003 117 TYR B CB  
4020 C CG  . TYR B 119 ? 1.0289 0.6093 0.5281 0.1723  -0.0173 -0.0067 117 TYR B CG  
4021 C CD1 . TYR B 119 ? 1.0329 0.6374 0.5424 0.2053  -0.0369 -0.0269 117 TYR B CD1 
4022 C CD2 . TYR B 119 ? 0.8824 0.4676 0.3745 0.1543  -0.0091 0.0034  117 TYR B CD2 
4023 C CE1 . TYR B 119 ? 1.1465 0.7780 0.6533 0.2205  -0.0472 -0.0350 117 TYR B CE1 
4024 C CE2 . TYR B 119 ? 0.9529 0.5649 0.4457 0.1671  -0.0169 -0.0038 117 TYR B CE2 
4025 C CZ  . TYR B 119 ? 1.1534 0.7879 0.6506 0.2005  -0.0356 -0.0221 117 TYR B CZ  
4026 O OH  . TYR B 119 ? 0.9513 0.6135 0.4464 0.2158  -0.0441 -0.0314 117 TYR B OH  
4027 N N   . TRP B 120 ? 0.9981 0.5314 0.5606 0.1447  0.0026  -0.0174 118 TRP B N   
4028 C CA  . TRP B 120 ? 0.9916 0.5003 0.5539 0.1320  0.0170  -0.0137 118 TRP B CA  
4029 C C   . TRP B 120 ? 1.0448 0.5355 0.5874 0.1508  0.0149  -0.0172 118 TRP B C   
4030 O O   . TRP B 120 ? 1.1288 0.6248 0.6569 0.1769  0.0010  -0.0229 118 TRP B O   
4031 C CB  . TRP B 120 ? 0.9953 0.5173 0.6125 0.1260  0.0231  -0.0277 118 TRP B CB  
4032 C CG  . TRP B 120 ? 1.1089 0.6364 0.7375 0.1072  0.0292  -0.0198 118 TRP B CG  
4033 C CD1 . TRP B 120 ? 0.9697 0.5248 0.6314 0.1097  0.0195  -0.0277 118 TRP B CD1 
4034 C CD2 . TRP B 120 ? 1.0865 0.5896 0.6906 0.0867  0.0443  -0.0037 118 TRP B CD2 
4035 N NE1 . TRP B 120 ? 1.0249 0.5719 0.6840 0.0915  0.0282  -0.0155 118 TRP B NE1 
4036 C CE2 . TRP B 120 ? 1.1060 0.6208 0.7268 0.0789  0.0426  -0.0009 118 TRP B CE2 
4037 C CE3 . TRP B 120 ? 1.0561 0.5284 0.6244 0.0771  0.0571  0.0065  118 TRP B CE3 
4038 C CZ2 . TRP B 120 ? 1.0720 0.5662 0.6691 0.0647  0.0521  0.0128  118 TRP B CZ2 
4039 C CZ3 . TRP B 120 ? 1.1249 0.5798 0.6708 0.0629  0.0660  0.0179  118 TRP B CZ3 
4040 C CH2 . TRP B 120 ? 1.1188 0.5835 0.6762 0.0583  0.0629  0.0215  118 TRP B CH2 
4041 N N   . GLY B 121 ? 1.1235 0.5906 0.6619 0.1401  0.0283  -0.0141 119 GLY B N   
4042 C CA  . GLY B 121 ? 1.0935 0.5436 0.6232 0.1569  0.0265  -0.0207 119 GLY B CA  
4043 C C   . GLY B 121 ? 1.1060 0.5649 0.6860 0.1570  0.0323  -0.0408 119 GLY B C   
4044 O O   . GLY B 121 ? 1.1408 0.6110 0.7551 0.1410  0.0438  -0.0443 119 GLY B O   
4045 N N   . GLN B 122 ? 1.1403 0.5914 0.7251 0.1765  0.0264  -0.0541 120 GLN B N   
4046 C CA  . GLN B 122 ? 1.1626 0.6245 0.8042 0.1787  0.0330  -0.0781 120 GLN B CA  
4047 C C   . GLN B 122 ? 1.1990 0.6382 0.8352 0.1534  0.0600  -0.0684 120 GLN B C   
4048 O O   . GLN B 122 ? 1.1192 0.5647 0.8028 0.1511  0.0736  -0.0859 120 GLN B O   
4049 C CB  . GLN B 122 ? 1.1573 0.6190 0.8071 0.2103  0.0150  -0.0990 120 GLN B CB  
4050 C CG  . GLN B 122 ? 1.3780 0.8027 0.9872 0.2095  0.0227  -0.0878 120 GLN B CG  
4051 C CD  . GLN B 122 ? 1.3850 0.7798 0.9219 0.2144  0.0180  -0.0604 120 GLN B CD  
4052 O OE1 . GLN B 122 ? 1.3499 0.7326 0.8560 0.1909  0.0307  -0.0371 120 GLN B OE1 
4053 N NE2 . GLN B 122 ? 1.4603 0.8413 0.9713 0.2468  0.0007  -0.0642 120 GLN B NE2 
4054 N N   . GLY B 123 ? 1.1841 0.5978 0.7667 0.1361  0.0686  -0.0438 121 GLY B N   
4055 C CA  . GLY B 123 ? 1.1647 0.5569 0.7335 0.1163  0.0906  -0.0363 121 GLY B CA  
4056 C C   . GLY B 123 ? 1.2787 0.6519 0.8443 0.1231  0.0959  -0.0452 121 GLY B C   
4057 O O   . GLY B 123 ? 1.2610 0.6416 0.8517 0.1436  0.0847  -0.0626 121 GLY B O   
4058 N N   . THR B 124 ? 1.2643 0.6130 0.7983 0.1079  0.1109  -0.0355 122 THR B N   
4059 C CA  . THR B 124 ? 1.2367 0.5659 0.7662 0.1117  0.1181  -0.0441 122 THR B CA  
4060 C C   . THR B 124 ? 1.1379 0.4566 0.6639 0.0972  0.1435  -0.0451 122 THR B C   
4061 O O   . THR B 124 ? 1.1632 0.4772 0.6643 0.0841  0.1519  -0.0323 122 THR B O   
4062 C CB  . THR B 124 ? 1.2222 0.5253 0.7078 0.1126  0.1087  -0.0323 122 THR B CB  
4063 O OG1 . THR B 124 ? 1.3334 0.6223 0.8263 0.1258  0.1075  -0.0445 122 THR B OG1 
4064 C CG2 . THR B 124 ? 1.2008 0.4864 0.6505 0.0925  0.1184  -0.0207 122 THR B CG2 
4065 N N   . GLN B 125 ? 1.0584 0.3721 0.6071 0.1025  0.1557  -0.0615 123 GLN B N   
4066 C CA  . GLN B 125 ? 1.1110 0.4139 0.6578 0.0928  0.1850  -0.0645 123 GLN B CA  
4067 C C   . GLN B 125 ? 1.2255 0.5012 0.7196 0.0868  0.1877  -0.0583 123 GLN B C   
4068 O O   . GLN B 125 ? 1.2034 0.4686 0.6929 0.0933  0.1767  -0.0651 123 GLN B O   
4069 C CB  . GLN B 125 ? 1.0676 0.3814 0.6735 0.1009  0.2005  -0.0892 123 GLN B CB  
4070 C CG  . GLN B 125 ? 1.0940 0.3942 0.6991 0.0920  0.2380  -0.0920 123 GLN B CG  
4071 C CD  . GLN B 125 ? 1.2603 0.5570 0.8539 0.0813  0.2600  -0.0755 123 GLN B CD  
4072 O OE1 . GLN B 125 ? 1.2970 0.5750 0.8283 0.0751  0.2602  -0.0556 123 GLN B OE1 
4073 N NE2 . GLN B 125 ? 1.2947 0.6084 0.9518 0.0808  0.2781  -0.0856 123 GLN B NE2 
4074 N N   . VAL B 126 ? 1.2413 0.5045 0.6958 0.0771  0.2008  -0.0471 124 VAL B N   
4075 C CA  . VAL B 126 ? 1.2345 0.4748 0.6404 0.0740  0.2024  -0.0466 124 VAL B CA  
4076 C C   . VAL B 126 ? 1.2634 0.4909 0.6525 0.0743  0.2339  -0.0493 124 VAL B C   
4077 O O   . VAL B 126 ? 1.2943 0.5201 0.6715 0.0722  0.2492  -0.0379 124 VAL B O   
4078 C CB  . VAL B 126 ? 1.2413 0.4768 0.6067 0.0674  0.1838  -0.0339 124 VAL B CB  
4079 C CG1 . VAL B 126 ? 1.1865 0.4016 0.5086 0.0668  0.1832  -0.0404 124 VAL B CG1 
4080 C CG2 . VAL B 126 ? 1.1212 0.3653 0.5023 0.0669  0.1601  -0.0294 124 VAL B CG2 
4081 N N   . THR B 127 ? 1.2304 0.4461 0.6164 0.0783  0.2456  -0.0636 125 THR B N   
4082 C CA  . THR B 127 ? 1.3434 0.5445 0.7117 0.0809  0.2806  -0.0675 125 THR B CA  
4083 C C   . THR B 127 ? 1.3812 0.5616 0.6933 0.0849  0.2769  -0.0738 125 THR B C   
4084 O O   . THR B 127 ? 1.3180 0.4973 0.6404 0.0864  0.2620  -0.0879 125 THR B O   
4085 C CB  . THR B 127 ? 1.3502 0.5611 0.7798 0.0836  0.3030  -0.0855 125 THR B CB  
4086 O OG1 . THR B 127 ? 1.2799 0.5156 0.7712 0.0831  0.2943  -0.0877 125 THR B OG1 
4087 C CG2 . THR B 127 ? 1.2835 0.4791 0.7021 0.0843  0.3492  -0.0852 125 THR B CG2 
4088 N N   . VAL B 128 ? 1.3297 0.4923 0.5819 0.0894  0.2897  -0.0649 126 VAL B N   
4089 C CA  . VAL B 128 ? 1.3747 0.5194 0.5677 0.0977  0.2820  -0.0742 126 VAL B CA  
4090 C C   . VAL B 128 ? 1.4293 0.5553 0.5944 0.1076  0.3210  -0.0800 126 VAL B C   
4091 O O   . VAL B 128 ? 1.6793 0.7896 0.8102 0.1136  0.3500  -0.0650 126 VAL B O   
4092 C CB  . VAL B 128 ? 1.4191 0.5570 0.5570 0.1018  0.2612  -0.0639 126 VAL B CB  
4093 C CG1 . VAL B 128 ? 1.4320 0.5585 0.5233 0.1116  0.2427  -0.0824 126 VAL B CG1 
4094 C CG2 . VAL B 128 ? 1.3493 0.5071 0.5219 0.0903  0.2323  -0.0551 126 VAL B CG2 
4095 N N   . SER B 129 ? 1.4402 0.5648 0.6181 0.1104  0.3246  -0.1010 127 SER B N   
4096 C CA  . SER B 129 ? 1.4936 0.6045 0.6479 0.1198  0.3611  -0.1082 127 SER B CA  
4097 C C   . SER B 129 ? 1.6253 0.7239 0.7014 0.1340  0.3547  -0.1025 127 SER B C   
4098 O O   . SER B 129 ? 1.7941 0.8801 0.8364 0.1435  0.3857  -0.0914 127 SER B O   
4099 C CB  . SER B 129 ? 1.4826 0.6059 0.6829 0.1183  0.3583  -0.1323 127 SER B CB  
4100 O OG  . SER B 129 ? 1.5745 0.7128 0.8435 0.1096  0.3427  -0.1388 127 SER B OG  
4101 N N   . VAL C 4   ? 1.8507 0.8181 0.6209 0.0607  0.0560  -0.0158 2   VAL C N   
4102 C CA  . VAL C 4   ? 1.9261 0.9088 0.7225 0.0631  0.0794  -0.0117 2   VAL C CA  
4103 C C   . VAL C 4   ? 1.8300 0.8093 0.6227 0.0627  0.0597  0.0075  2   VAL C C   
4104 O O   . VAL C 4   ? 1.7520 0.7372 0.5535 0.0693  0.0238  0.0174  2   VAL C O   
4105 C CB  . VAL C 4   ? 1.7863 0.8032 0.6363 0.0780  0.0794  -0.0163 2   VAL C CB  
4106 C CG1 . VAL C 4   ? 1.6106 0.6508 0.4872 0.0910  0.0382  -0.0035 2   VAL C CG1 
4107 C CG2 . VAL C 4   ? 1.8217 0.8468 0.6930 0.0787  0.1037  -0.0133 2   VAL C CG2 
4108 N N   . GLN C 5   ? 1.8514 0.8201 0.6336 0.0545  0.0839  0.0115  3   GLN C N   
4109 C CA  . GLN C 5   ? 1.8944 0.8561 0.6720 0.0527  0.0675  0.0273  3   GLN C CA  
4110 C C   . GLN C 5   ? 1.7918 0.7770 0.6127 0.0638  0.0721  0.0329  3   GLN C C   
4111 O O   . GLN C 5   ? 1.7119 0.7030 0.5467 0.0637  0.1015  0.0267  3   GLN C O   
4112 C CB  . GLN C 5   ? 1.9500 0.8768 0.6766 0.0327  0.0873  0.0302  3   GLN C CB  
4113 C CG  . GLN C 5   ? 2.1956 1.1015 0.8949 0.0257  0.0555  0.0446  3   GLN C CG  
4114 C CD  . GLN C 5   ? 2.2499 1.1520 0.9545 0.0227  0.0586  0.0571  3   GLN C CD  
4115 O OE1 . GLN C 5   ? 2.2475 1.1539 0.9625 0.0206  0.0901  0.0557  3   GLN C OE1 
4116 N NE2 . GLN C 5   ? 2.1661 1.0585 0.8651 0.0221  0.0249  0.0701  3   GLN C NE2 
4117 N N   . LEU C 6   ? 1.7425 0.7384 0.5843 0.0731  0.0433  0.0436  4   LEU C N   
4118 C CA  . LEU C 6   ? 1.7048 0.7214 0.5859 0.0845  0.0424  0.0481  4   LEU C CA  
4119 C C   . LEU C 6   ? 1.5977 0.5967 0.4678 0.0798  0.0371  0.0591  4   LEU C C   
4120 O O   . LEU C 6   ? 1.6728 0.6586 0.5263 0.0770  0.0139  0.0659  4   LEU C O   
4121 C CB  . LEU C 6   ? 1.6284 0.6765 0.5496 0.1014  0.0159  0.0484  4   LEU C CB  
4122 C CG  . LEU C 6   ? 1.5996 0.6641 0.5304 0.1054  0.0113  0.0407  4   LEU C CG  
4123 C CD1 . LEU C 6   ? 1.4105 0.5036 0.3768 0.1196  -0.0164 0.0447  4   LEU C CD1 
4124 C CD2 . LEU C 6   ? 1.4881 0.5614 0.4305 0.1050  0.0362  0.0326  4   LEU C CD2 
4125 N N   . VAL C 7   ? 1.5331 0.5292 0.4130 0.0781  0.0562  0.0622  5   VAL C N   
4126 C CA  . VAL C 7   ? 1.6371 0.6171 0.5120 0.0742  0.0503  0.0733  5   VAL C CA  
4127 C C   . VAL C 7   ? 1.5103 0.5051 0.4247 0.0861  0.0482  0.0747  5   VAL C C   
4128 O O   . VAL C 7   ? 1.5593 0.5670 0.4947 0.0895  0.0627  0.0701  5   VAL C O   
4129 C CB  . VAL C 7   ? 1.6090 0.5597 0.4465 0.0539  0.0775  0.0788  5   VAL C CB  
4130 C CG1 . VAL C 7   ? 1.6470 0.5972 0.5017 0.0507  0.1097  0.0797  5   VAL C CG1 
4131 C CG2 . VAL C 7   ? 1.7222 0.6521 0.5417 0.0462  0.0594  0.0922  5   VAL C CG2 
4132 N N   . GLU C 8   ? 1.6095 0.5991 0.5333 0.0917  0.0281  0.0813  6   GLU C N   
4133 C CA  . GLU C 8   ? 1.6065 0.6068 0.5645 0.1040  0.0207  0.0803  6   GLU C CA  
4134 C C   . GLU C 8   ? 1.5335 0.5133 0.4942 0.0950  0.0298  0.0889  6   GLU C C   
4135 O O   . GLU C 8   ? 1.6277 0.5856 0.5635 0.0804  0.0374  0.0982  6   GLU C O   
4136 C CB  . GLU C 8   ? 1.5074 0.5143 0.4785 0.1194  -0.0075 0.0793  6   GLU C CB  
4137 C CG  . GLU C 8   ? 1.4778 0.5136 0.4702 0.1341  -0.0147 0.0707  6   GLU C CG  
4138 C CD  . GLU C 8   ? 1.4886 0.5313 0.4707 0.1334  -0.0249 0.0706  6   GLU C CD  
4139 O OE1 . GLU C 8   ? 1.6906 0.7146 0.6433 0.1194  -0.0226 0.0750  6   GLU C OE1 
4140 O OE2 . GLU C 8   ? 1.5292 0.5938 0.5312 0.1459  -0.0357 0.0671  6   GLU C OE2 
4141 N N   . SER C 9   ? 1.5200 0.5067 0.5123 0.1023  0.0273  0.0862  7   SER C N   
4142 C CA  . SER C 9   ? 1.6109 0.5809 0.6183 0.0943  0.0312  0.0935  7   SER C CA  
4143 C C   . SER C 9   ? 1.5909 0.5708 0.6318 0.1054  0.0180  0.0856  7   SER C C   
4144 O O   . SER C 9   ? 1.5138 0.5126 0.5630 0.1160  0.0135  0.0761  7   SER C O   
4145 C CB  . SER C 9   ? 1.4962 0.4561 0.5048 0.0775  0.0613  0.1003  7   SER C CB  
4146 O OG  . SER C 9   ? 1.5484 0.4883 0.5620 0.0650  0.0659  0.1124  7   SER C OG  
4147 N N   . GLY C 10  ? 1.4744 0.4401 0.5323 0.1012  0.0108  0.0897  8   GLY C N   
4148 C CA  . GLY C 10  ? 1.5816 0.5514 0.6676 0.1068  -0.0012 0.0814  8   GLY C CA  
4149 C C   . GLY C 10  ? 1.5129 0.4752 0.5938 0.1222  -0.0232 0.0726  8   GLY C C   
4150 O O   . GLY C 10  ? 1.4472 0.4066 0.5416 0.1260  -0.0330 0.0638  8   GLY C O   
4151 N N   . GLY C 11  ? 1.4692 0.4251 0.5317 0.1307  -0.0317 0.0742  9   GLY C N   
4152 C CA  . GLY C 11  ? 1.6038 0.5497 0.6679 0.1477  -0.0502 0.0649  9   GLY C CA  
4153 C C   . GLY C 11  ? 1.6152 0.5384 0.6921 0.1448  -0.0642 0.0667  9   GLY C C   
4154 O O   . GLY C 11  ? 1.6107 0.5292 0.7009 0.1302  -0.0607 0.0733  9   GLY C O   
4155 N N   . GLY C 12  ? 1.7266 0.6359 0.8062 0.1589  -0.0811 0.0612  10  GLY C N   
4156 C CA  . GLY C 12  ? 1.8492 0.7361 0.9439 0.1577  -0.0978 0.0622  10  GLY C CA  
4157 C C   . GLY C 12  ? 1.7525 0.6290 0.8556 0.1772  -0.1084 0.0413  10  GLY C C   
4158 O O   . GLY C 12  ? 1.7395 0.6254 0.8350 0.1918  -0.1008 0.0264  10  GLY C O   
4159 N N   . LEU C 13  ? 1.8105 0.6658 0.9295 0.1768  -0.1248 0.0396  11  LEU C N   
4160 C CA  . LEU C 13  ? 1.7113 0.5520 0.8384 0.1942  -0.1342 0.0169  11  LEU C CA  
4161 C C   . LEU C 13  ? 1.6359 0.4718 0.7533 0.1879  -0.1312 0.0051  11  LEU C C   
4162 O O   . LEU C 13  ? 1.6727 0.5057 0.7975 0.1693  -0.1350 0.0174  11  LEU C O   
4163 C CB  . LEU C 13  ? 1.6444 0.4629 0.7961 0.1966  -0.1563 0.0198  11  LEU C CB  
4164 C CG  . LEU C 13  ? 1.7051 0.5043 0.8681 0.2105  -0.1663 -0.0048 11  LEU C CG  
4165 C CD1 . LEU C 13  ? 1.7040 0.5054 0.8820 0.2357  -0.1645 -0.0240 11  LEU C CD1 
4166 C CD2 . LEU C 13  ? 1.7724 0.5489 0.9580 0.2011  -0.1885 0.0038  11  LEU C CD2 
4167 N N   . VAL C 14  ? 1.6560 0.4906 0.7582 0.2021  -0.1245 -0.0182 12  VAL C N   
4168 C CA  . VAL C 14  ? 1.7030 0.5280 0.7865 0.1951  -0.1246 -0.0305 12  VAL C CA  
4169 C C   . VAL C 14  ? 1.7106 0.5194 0.7833 0.2122  -0.1256 -0.0596 12  VAL C C   
4170 O O   . VAL C 14  ? 1.7811 0.5959 0.8657 0.2314  -0.1191 -0.0715 12  VAL C O   
4171 C CB  . VAL C 14  ? 1.6406 0.4850 0.7044 0.1876  -0.1090 -0.0274 12  VAL C CB  
4172 C CG1 . VAL C 14  ? 1.5963 0.4504 0.6399 0.2053  -0.0935 -0.0472 12  VAL C CG1 
4173 C CG2 . VAL C 14  ? 1.6847 0.5181 0.7408 0.1693  -0.1178 -0.0262 12  VAL C CG2 
4174 N N   . GLN C 15  ? 1.6891 0.4774 0.7425 0.2042  -0.1339 -0.0713 13  GLN C N   
4175 C CA  . GLN C 15  ? 1.8106 0.5841 0.8462 0.2175  -0.1306 -0.1014 13  GLN C CA  
4176 C C   . GLN C 15  ? 1.8145 0.6053 0.8165 0.2207  -0.1080 -0.1159 13  GLN C C   
4177 O O   . GLN C 15  ? 1.8158 0.6256 0.8087 0.2124  -0.0994 -0.1024 13  GLN C O   
4178 C CB  . GLN C 15  ? 1.9445 0.6841 0.9678 0.2059  -0.1520 -0.1081 13  GLN C CB  
4179 C CG  . GLN C 15  ? 1.8811 0.6031 0.9405 0.2068  -0.1734 -0.1012 13  GLN C CG  
4180 C CD  . GLN C 15  ? 1.9533 0.6421 1.0028 0.1940  -0.1972 -0.1058 13  GLN C CD  
4181 O OE1 . GLN C 15  ? 2.0281 0.7076 1.0494 0.1784  -0.2030 -0.1037 13  GLN C OE1 
4182 N NE2 . GLN C 15  ? 2.0943 0.7631 1.1692 0.1997  -0.2143 -0.1109 13  GLN C NE2 
4183 N N   . ALA C 16  ? 1.9018 0.6882 0.8876 0.2316  -0.0967 -0.1441 14  ALA C N   
4184 C CA  . ALA C 16  ? 1.7969 0.6048 0.7518 0.2323  -0.0723 -0.1581 14  ALA C CA  
4185 C C   . ALA C 16  ? 1.8716 0.6624 0.7795 0.2088  -0.0822 -0.1552 14  ALA C C   
4186 O O   . ALA C 16  ? 1.8301 0.5861 0.7195 0.1994  -0.1013 -0.1613 14  ALA C O   
4187 C CB  . ALA C 16  ? 1.9090 0.7221 0.8675 0.2501  -0.0520 -0.1894 14  ALA C CB  
4188 N N   . GLY C 17  ? 1.8627 0.6761 0.7534 0.1985  -0.0725 -0.1449 15  GLY C N   
4189 C CA  . GLY C 17  ? 1.8109 0.6097 0.6606 0.1746  -0.0843 -0.1399 15  GLY C CA  
4190 C C   . GLY C 17  ? 1.8805 0.6656 0.7417 0.1571  -0.1072 -0.1146 15  GLY C C   
4191 O O   . GLY C 17  ? 1.9286 0.7053 0.7638 0.1367  -0.1182 -0.1077 15  GLY C O   
4192 N N   . ASP C 18  ? 1.8647 0.6492 0.7689 0.1624  -0.1145 -0.0993 16  ASP C N   
4193 C CA  . ASP C 18  ? 1.8281 0.6095 0.7590 0.1450  -0.1301 -0.0732 16  ASP C CA  
4194 C C   . ASP C 18  ? 1.6899 0.5208 0.6434 0.1423  -0.1130 -0.0571 16  ASP C C   
4195 O O   . ASP C 18  ? 1.6088 0.4716 0.5561 0.1545  -0.0922 -0.0651 16  ASP C O   
4196 C CB  . ASP C 18  ? 1.7035 0.4838 0.6791 0.1468  -0.1404 -0.0592 16  ASP C CB  
4197 C CG  . ASP C 18  ? 1.9705 0.7232 0.9387 0.1550  -0.1527 -0.0760 16  ASP C CG  
4198 O OD1 . ASP C 18  ? 2.2008 0.9316 1.1801 0.1418  -0.1762 -0.0694 16  ASP C OD1 
4199 O OD2 . ASP C 18  ? 2.0255 0.7814 0.9831 0.1745  -0.1388 -0.0960 16  ASP C OD2 
4200 N N   . SER C 19  ? 1.7656 0.6058 0.7522 0.1258  -0.1216 -0.0342 17  SER C N   
4201 C CA  . SER C 19  ? 1.7627 0.6484 0.7760 0.1209  -0.1074 -0.0191 17  SER C CA  
4202 C C   . SER C 19  ? 1.7023 0.6004 0.7497 0.1266  -0.0971 -0.0043 17  SER C C   
4203 O O   . SER C 19  ? 1.8081 0.6852 0.8686 0.1271  -0.1046 0.0006  17  SER C O   
4204 C CB  . SER C 19  ? 1.7216 0.6103 0.7518 0.0975  -0.1219 -0.0056 17  SER C CB  
4205 O OG  . SER C 19  ? 1.8392 0.7089 0.9070 0.0860  -0.1350 0.0100  17  SER C OG  
4206 N N   . LEU C 20  ? 1.5292 0.4663 0.5907 0.1284  -0.0804 0.0032  18  LEU C N   
4207 C CA  . LEU C 20  ? 1.4815 0.4294 0.5636 0.1314  -0.0688 0.0165  18  LEU C CA  
4208 C C   . LEU C 20  ? 1.4636 0.4500 0.5623 0.1253  -0.0552 0.0244  18  LEU C C   
4209 O O   . LEU C 20  ? 1.5034 0.5133 0.5941 0.1269  -0.0527 0.0177  18  LEU C O   
4210 C CB  . LEU C 20  ? 1.4806 0.4238 0.5480 0.1510  -0.0643 0.0096  18  LEU C CB  
4211 C CG  . LEU C 20  ? 1.4617 0.4003 0.5381 0.1518  -0.0597 0.0246  18  LEU C CG  
4212 C CD1 . LEU C 20  ? 1.4683 0.3989 0.5694 0.1354  -0.0662 0.0355  18  LEU C CD1 
4213 C CD2 . LEU C 20  ? 1.4796 0.4086 0.5460 0.1705  -0.0633 0.0180  18  LEU C CD2 
4214 N N   . THR C 21  ? 1.4564 0.4475 0.5775 0.1175  -0.0456 0.0382  19  THR C N   
4215 C CA  . THR C 21  ? 1.3723 0.3953 0.5116 0.1116  -0.0318 0.0436  19  THR C CA  
4216 C C   . THR C 21  ? 1.4407 0.4682 0.5681 0.1180  -0.0173 0.0488  19  THR C C   
4217 O O   . THR C 21  ? 1.4296 0.4357 0.5544 0.1142  -0.0133 0.0576  19  THR C O   
4218 C CB  . THR C 21  ? 1.3498 0.3741 0.5303 0.0935  -0.0308 0.0532  19  THR C CB  
4219 O OG1 . THR C 21  ? 1.5876 0.6152 0.7787 0.0855  -0.0475 0.0498  19  THR C OG1 
4220 C CG2 . THR C 21  ? 1.3247 0.3746 0.5264 0.0890  -0.0105 0.0579  19  THR C CG2 
4221 N N   . LEU C 22  ? 1.4586 0.5111 0.5765 0.1258  -0.0117 0.0447  20  LEU C N   
4222 C CA  . LEU C 22  ? 1.4609 0.5153 0.5626 0.1302  -0.0025 0.0496  20  LEU C CA  
4223 C C   . LEU C 22  ? 1.4471 0.5192 0.5638 0.1194  0.0129  0.0531  20  LEU C C   
4224 O O   . LEU C 22  ? 1.4194 0.5153 0.5597 0.1155  0.0130  0.0490  20  LEU C O   
4225 C CB  . LEU C 22  ? 1.3410 0.4091 0.4275 0.1460  -0.0088 0.0433  20  LEU C CB  
4226 C CG  . LEU C 22  ? 1.3953 0.4423 0.4670 0.1598  -0.0195 0.0411  20  LEU C CG  
4227 C CD1 . LEU C 22  ? 1.3876 0.4112 0.4617 0.1600  -0.0275 0.0357  20  LEU C CD1 
4228 C CD2 . LEU C 22  ? 1.3571 0.4263 0.4307 0.1750  -0.0229 0.0332  20  LEU C CD2 
4229 N N   . SER C 23  ? 1.3485 0.4067 0.4499 0.1136  0.0258  0.0601  21  SER C N   
4230 C CA  . SER C 23  ? 1.4972 0.5668 0.6085 0.1036  0.0453  0.0601  21  SER C CA  
4231 C C   . SER C 23  ? 1.5705 0.6342 0.6414 0.1068  0.0492  0.0611  21  SER C C   
4232 O O   . SER C 23  ? 1.5887 0.6283 0.6245 0.1100  0.0414  0.0680  21  SER C O   
4233 C CB  . SER C 23  ? 1.4975 0.5524 0.6274 0.0887  0.0635  0.0667  21  SER C CB  
4234 O OG  . SER C 23  ? 1.3380 0.4021 0.5166 0.0830  0.0584  0.0661  21  SER C OG  
4235 N N   . CYS C 24  ? 1.4565 0.5391 0.5335 0.1051  0.0579  0.0548  22  CYS C N   
4236 C CA  . CYS C 24  ? 1.4616 0.5360 0.4987 0.1064  0.0588  0.0546  22  CYS C CA  
4237 C C   . CYS C 24  ? 1.4931 0.5701 0.5349 0.0951  0.0837  0.0478  22  CYS C C   
4238 O O   . CYS C 24  ? 1.5011 0.6043 0.5798 0.0960  0.0858  0.0392  22  CYS C O   
4239 C CB  . CYS C 24  ? 1.5767 0.6723 0.6164 0.1195  0.0383  0.0513  22  CYS C CB  
4240 S SG  . CYS C 24  ? 1.7045 0.7928 0.7063 0.1198  0.0327  0.0507  22  CYS C SG  
4241 N N   . ALA C 25  ? 1.6569 0.7054 0.6618 0.0838  0.1032  0.0513  23  ALA C N   
4242 C CA  . ALA C 25  ? 1.5176 0.5644 0.5234 0.0725  0.1341  0.0419  23  ALA C CA  
4243 C C   . ALA C 25  ? 1.6038 0.6422 0.5652 0.0738  0.1309  0.0345  23  ALA C C   
4244 O O   . ALA C 25  ? 1.7018 0.7178 0.6095 0.0759  0.1119  0.0423  23  ALA C O   
4245 C CB  . ALA C 25  ? 1.4943 0.5127 0.4755 0.0574  0.1614  0.0488  23  ALA C CB  
4246 N N   . ALA C 26  ? 1.6621 0.7164 0.6499 0.0719  0.1468  0.0196  24  ALA C N   
4247 C CA  . ALA C 26  ? 1.7388 0.7855 0.6911 0.0731  0.1421  0.0100  24  ALA C CA  
4248 C C   . ALA C 26  ? 1.8574 0.8825 0.7829 0.0599  0.1802  -0.0040 24  ALA C C   
4249 O O   . ALA C 26  ? 1.7541 0.7880 0.7219 0.0533  0.2119  -0.0105 24  ALA C O   
4250 C CB  . ALA C 26  ? 1.7232 0.8066 0.7299 0.0836  0.1235  0.0027  24  ALA C CB  
4251 N N   . SER C 27  ? 2.1903 1.1852 1.0454 0.0556  0.1772  -0.0089 25  SER C N   
4252 C CA  . SER C 27  ? 2.2360 1.2079 1.0576 0.0428  0.2139  -0.0260 25  SER C CA  
4253 C C   . SER C 27  ? 2.2769 1.2767 1.1648 0.0481  0.2307  -0.0480 25  SER C C   
4254 O O   . SER C 27  ? 2.2203 1.2520 1.1621 0.0602  0.2030  -0.0485 25  SER C O   
4255 C CB  . SER C 27  ? 2.2308 1.1846 1.0055 0.0352  0.1912  -0.0234 25  SER C CB  
4256 O OG  . SER C 27  ? 2.3136 1.2540 1.0686 0.0254  0.2202  -0.0433 25  SER C OG  
4257 N N   . GLY C 28  ? 2.1164 1.1052 1.0059 0.0380  0.2767  -0.0657 26  GLY C N   
4258 C CA  . GLY C 28  ? 2.1365 1.1526 1.1050 0.0425  0.2954  -0.0873 26  GLY C CA  
4259 C C   . GLY C 28  ? 2.1002 1.0999 1.0369 0.0439  0.2953  -0.1097 26  GLY C C   
4260 O O   . GLY C 28  ? 2.1609 1.1407 1.0777 0.0354  0.3360  -0.1316 26  GLY C O   
4261 N N   . ARG C 29  ? 2.1008 1.1103 1.0365 0.0541  0.2500  -0.1045 27  ARG C N   
4262 C CA  . ARG C 29  ? 2.1329 1.1295 1.0505 0.0566  0.2420  -0.1246 27  ARG C CA  
4263 C C   . ARG C 29  ? 1.9687 1.0006 0.9419 0.0696  0.1936  -0.1144 27  ARG C C   
4264 O O   . ARG C 29  ? 1.9442 0.9750 0.8849 0.0737  0.1566  -0.0946 27  ARG C O   
4265 C CB  . ARG C 29  ? 2.2348 1.2030 1.0701 0.0445  0.2304  -0.1175 27  ARG C CB  
4266 C CG  . ARG C 29  ? 2.2325 1.1904 1.0562 0.0434  0.2254  -0.1381 27  ARG C CG  
4267 C CD  . ARG C 29  ? 2.3366 1.2997 1.2025 0.0407  0.2746  -0.1686 27  ARG C CD  
4268 N NE  . ARG C 29  ? 2.3708 1.3333 1.2542 0.0458  0.2642  -0.1914 27  ARG C NE  
4269 C CZ  . ARG C 29  ? 2.3039 1.2876 1.2706 0.0558  0.2746  -0.2129 27  ARG C CZ  
4270 N NH1 . ARG C 29  ? 2.3129 1.3194 1.3563 0.0617  0.2949  -0.2139 27  ARG C NH1 
4271 N NH2 . ARG C 29  ? 2.3309 1.3102 1.3092 0.0597  0.2612  -0.2330 27  ARG C NH2 
4272 N N   . THR C 30  ? 1.9386 1.0019 0.9993 0.0752  0.1947  -0.1271 28  THR C N   
4273 C CA  . THR C 30  ? 1.8104 0.9083 0.9298 0.0847  0.1519  -0.1180 28  THR C CA  
4274 C C   . THR C 30  ? 1.7168 0.8401 0.8479 0.0895  0.1215  -0.0891 28  THR C C   
4275 O O   . THR C 30  ? 1.6750 0.8182 0.8217 0.0958  0.0844  -0.0769 28  THR C O   
4276 C CB  . THR C 30  ? 1.7318 0.8091 0.8088 0.0869  0.1270  -0.1271 28  THR C CB  
4277 O OG1 . THR C 30  ? 1.7205 0.8325 0.8757 0.0935  0.0986  -0.1263 28  THR C OG1 
4278 C CG2 . THR C 30  ? 1.8278 0.8832 0.8251 0.0872  0.0957  -0.1081 28  THR C CG2 
4279 N N   . ALA C 31  ? 1.7022 0.8259 0.8312 0.0862  0.1389  -0.0789 29  ALA C N   
4280 C CA  . ALA C 31  ? 1.6411 0.7830 0.7757 0.0908  0.1142  -0.0552 29  ALA C CA  
4281 C C   . ALA C 31  ? 1.4847 0.6689 0.6996 0.0952  0.0915  -0.0473 29  ALA C C   
4282 O O   . ALA C 31  ? 1.4866 0.6870 0.7018 0.1000  0.0667  -0.0303 29  ALA C O   
4283 C CB  . ALA C 31  ? 1.6984 0.8281 0.8174 0.0853  0.1376  -0.0478 29  ALA C CB  
4284 N N   . TYR C 32  ? 1.4766 0.6772 0.7594 0.0928  0.0993  -0.0593 30  TYR C N   
4285 C CA  . TYR C 32  ? 1.4669 0.7032 0.8228 0.0933  0.0739  -0.0492 30  TYR C CA  
4286 C C   . TYR C 32  ? 1.3345 0.5864 0.6912 0.0979  0.0394  -0.0429 30  TYR C C   
4287 O O   . TYR C 32  ? 1.4620 0.7423 0.8642 0.0967  0.0151  -0.0298 30  TYR C O   
4288 C CB  . TYR C 32  ? 1.4018 0.6490 0.8395 0.0881  0.0889  -0.0619 30  TYR C CB  
4289 C CG  . TYR C 32  ? 1.4783 0.7108 0.9213 0.0888  0.1074  -0.0867 30  TYR C CG  
4290 C CD1 . TYR C 32  ? 1.5330 0.7373 0.9431 0.0860  0.1498  -0.1052 30  TYR C CD1 
4291 C CD2 . TYR C 32  ? 1.3736 0.6186 0.8531 0.0912  0.0834  -0.0922 30  TYR C CD2 
4292 C CE1 . TYR C 32  ? 1.5371 0.7241 0.9459 0.0863  0.1703  -0.1316 30  TYR C CE1 
4293 C CE2 . TYR C 32  ? 1.5291 0.7571 1.0131 0.0925  0.0996  -0.1178 30  TYR C CE2 
4294 C CZ  . TYR C 32  ? 1.6513 0.8494 1.0978 0.0904  0.1443  -0.1390 30  TYR C CZ  
4295 O OH  . TYR C 32  ? 1.5606 0.7379 1.0053 0.0914  0.1639  -0.1681 30  TYR C OH  
4296 N N   . ARG C 33  ? 1.3845 0.6167 0.6909 0.1014  0.0354  -0.0504 31  ARG C N   
4297 C CA  . ARG C 33  ? 1.2752 0.5207 0.5816 0.1055  0.0013  -0.0419 31  ARG C CA  
4298 C C   . ARG C 33  ? 1.2959 0.5391 0.5511 0.1108  -0.0153 -0.0245 31  ARG C C   
4299 O O   . ARG C 33  ? 1.2082 0.4608 0.4608 0.1144  -0.0421 -0.0160 31  ARG C O   
4300 C CB  . ARG C 33  ? 1.2491 0.4728 0.5397 0.1056  0.0004  -0.0604 31  ARG C CB  
4301 C CG  . ARG C 33  ? 1.3991 0.6234 0.7468 0.1021  0.0190  -0.0817 31  ARG C CG  
4302 C CD  . ARG C 33  ? 1.4483 0.6414 0.7648 0.1027  0.0241  -0.1051 31  ARG C CD  
4303 N NE  . ARG C 33  ? 1.3864 0.5643 0.7270 0.0998  0.0628  -0.1321 31  ARG C NE  
4304 C CZ  . ARG C 33  ? 1.4738 0.6458 0.8536 0.1006  0.0658  -0.1550 31  ARG C CZ  
4305 N NH1 . ARG C 33  ? 1.5946 0.7725 0.9916 0.1033  0.0292  -0.1533 31  ARG C NH1 
4306 N NH2 . ARG C 33  ? 1.5938 0.7535 1.0002 0.0987  0.1072  -0.1808 31  ARG C NH2 
4307 N N   . TYR C 34  ? 1.4234 0.6551 0.6452 0.1114  -0.0008 -0.0187 32  TYR C N   
4308 C CA  . TYR C 34  ? 1.3640 0.5903 0.5432 0.1173  -0.0146 -0.0042 32  TYR C CA  
4309 C C   . TYR C 34  ? 1.3646 0.6209 0.5755 0.1202  -0.0227 0.0102  32  TYR C C   
4310 O O   . TYR C 34  ? 1.2343 0.4976 0.4710 0.1160  -0.0097 0.0095  32  TYR C O   
4311 C CB  . TYR C 34  ? 1.3002 0.4877 0.4161 0.1152  0.0042  -0.0070 32  TYR C CB  
4312 C CG  . TYR C 34  ? 1.4860 0.6365 0.5399 0.1132  -0.0017 -0.0127 32  TYR C CG  
4313 C CD1 . TYR C 34  ? 1.4851 0.6093 0.5159 0.1057  0.0187  -0.0318 32  TYR C CD1 
4314 C CD2 . TYR C 34  ? 1.4307 0.5696 0.4495 0.1178  -0.0281 0.0007  32  TYR C CD2 
4315 C CE1 . TYR C 34  ? 1.4491 0.5325 0.4118 0.1015  0.0117  -0.0378 32  TYR C CE1 
4316 C CE2 . TYR C 34  ? 1.4503 0.5496 0.4088 0.1135  -0.0396 -0.0025 32  TYR C CE2 
4317 C CZ  . TYR C 34  ? 1.4819 0.5514 0.4066 0.1045  -0.0201 -0.0219 32  TYR C CZ  
4318 O OH  . TYR C 34  ? 1.5342 0.5590 0.3904 0.0977  -0.0327 -0.0258 32  TYR C OH  
4319 N N   . GLY C 35  ? 1.3116 0.5839 0.5211 0.1268  -0.0440 0.0228  33  GLY C N   
4320 C CA  . GLY C 35  ? 1.2228 0.5193 0.4507 0.1299  -0.0483 0.0341  33  GLY C CA  
4321 C C   . GLY C 35  ? 1.3058 0.5832 0.4953 0.1366  -0.0422 0.0378  33  GLY C C   
4322 O O   . GLY C 35  ? 1.3148 0.5691 0.4683 0.1408  -0.0475 0.0390  33  GLY C O   
4323 N N   . MET C 36  ? 1.2854 0.5692 0.4829 0.1366  -0.0342 0.0400  34  MET C N   
4324 C CA  . MET C 36  ? 1.2306 0.4931 0.3973 0.1420  -0.0274 0.0415  34  MET C CA  
4325 C C   . MET C 36  ? 1.2723 0.5532 0.4488 0.1500  -0.0336 0.0473  34  MET C C   
4326 O O   . MET C 36  ? 1.2446 0.5541 0.4481 0.1479  -0.0381 0.0501  34  MET C O   
4327 C CB  . MET C 36  ? 1.2360 0.4803 0.3992 0.1344  -0.0094 0.0363  34  MET C CB  
4328 C CG  . MET C 36  ? 1.3321 0.5691 0.5056 0.1249  0.0030  0.0279  34  MET C CG  
4329 S SD  . MET C 36  ? 1.4866 0.6875 0.6071 0.1235  0.0112  0.0223  34  MET C SD  
4330 C CE  . MET C 36  ? 1.4091 0.5837 0.4837 0.1292  0.0070  0.0322  34  MET C CE  
4331 N N   . GLY C 37  ? 1.3087 0.5710 0.4622 0.1584  -0.0332 0.0487  35  GLY C N   
4332 C CA  . GLY C 37  ? 1.3948 0.6701 0.5573 0.1680  -0.0349 0.0502  35  GLY C CA  
4333 C C   . GLY C 37  ? 1.4396 0.6857 0.5795 0.1750  -0.0325 0.0490  35  GLY C C   
4334 O O   . GLY C 37  ? 1.4824 0.6994 0.5968 0.1733  -0.0349 0.0515  35  GLY C O   
4335 N N   . TRP C 38  ? 1.4456 0.6972 0.5923 0.1817  -0.0282 0.0451  36  TRP C N   
4336 C CA  . TRP C 38  ? 1.2443 0.4688 0.3766 0.1895  -0.0277 0.0425  36  TRP C CA  
4337 C C   . TRP C 38  ? 1.3487 0.5836 0.4993 0.2055  -0.0327 0.0417  36  TRP C C   
4338 O O   . TRP C 38  ? 1.4093 0.6746 0.5817 0.2097  -0.0272 0.0386  36  TRP C O   
4339 C CB  . TRP C 38  ? 1.2747 0.4897 0.4007 0.1845  -0.0186 0.0354  36  TRP C CB  
4340 C CG  . TRP C 38  ? 1.3205 0.5168 0.4361 0.1706  -0.0141 0.0373  36  TRP C CG  
4341 C CD1 . TRP C 38  ? 1.3435 0.5520 0.4722 0.1578  -0.0100 0.0372  36  TRP C CD1 
4342 C CD2 . TRP C 38  ? 1.4079 0.5706 0.5043 0.1674  -0.0124 0.0407  36  TRP C CD2 
4343 N NE1 . TRP C 38  ? 1.3425 0.5294 0.4670 0.1481  -0.0033 0.0388  36  TRP C NE1 
4344 C CE2 . TRP C 38  ? 1.4234 0.5822 0.5249 0.1530  -0.0033 0.0414  36  TRP C CE2 
4345 C CE3 . TRP C 38  ? 1.3527 0.4878 0.4314 0.1741  -0.0187 0.0445  36  TRP C CE3 
4346 C CZ2 . TRP C 38  ? 1.4047 0.5355 0.4929 0.1450  0.0042  0.0455  36  TRP C CZ2 
4347 C CZ3 . TRP C 38  ? 1.3496 0.4543 0.4091 0.1647  -0.0148 0.0502  36  TRP C CZ3 
4348 C CH2 . TRP C 38  ? 1.3529 0.4567 0.4164 0.1502  -0.0012 0.0505  36  TRP C CH2 
4349 N N   . PHE C 39  ? 1.4459 0.6550 0.5906 0.2134  -0.0430 0.0454  37  PHE C N   
4350 C CA  . PHE C 39  ? 1.4893 0.7042 0.6621 0.2298  -0.0496 0.0446  37  PHE C CA  
4351 C C   . PHE C 39  ? 1.5300 0.7116 0.6953 0.2369  -0.0528 0.0406  37  PHE C C   
4352 O O   . PHE C 39  ? 1.5764 0.7262 0.7114 0.2278  -0.0566 0.0449  37  PHE C O   
4353 C CB  . PHE C 39  ? 1.4867 0.7018 0.6724 0.2328  -0.0698 0.0572  37  PHE C CB  
4354 C CG  . PHE C 39  ? 1.4024 0.6536 0.6092 0.2299  -0.0701 0.0610  37  PHE C CG  
4355 C CD1 . PHE C 39  ? 1.3967 0.6507 0.5821 0.2156  -0.0688 0.0632  37  PHE C CD1 
4356 C CD2 . PHE C 39  ? 1.3603 0.6426 0.6139 0.2415  -0.0712 0.0624  37  PHE C CD2 
4357 C CE1 . PHE C 39  ? 1.3007 0.5859 0.5084 0.2126  -0.0724 0.0674  37  PHE C CE1 
4358 C CE2 . PHE C 39  ? 1.3927 0.7082 0.6685 0.2374  -0.0731 0.0684  37  PHE C CE2 
4359 C CZ  . PHE C 39  ? 1.3172 0.6330 0.5687 0.2228  -0.0756 0.0712  37  PHE C CZ  
4360 N N   . ARG C 40  ? 1.5730 0.7623 0.7694 0.2529  -0.0499 0.0319  38  ARG C N   
4361 C CA  . ARG C 40  ? 1.4903 0.6478 0.6895 0.2622  -0.0563 0.0271  38  ARG C CA  
4362 C C   . ARG C 40  ? 1.5246 0.6857 0.7708 0.2793  -0.0695 0.0294  38  ARG C C   
4363 O O   . ARG C 40  ? 1.5431 0.7374 0.8247 0.2858  -0.0669 0.0307  38  ARG C O   
4364 C CB  . ARG C 40  ? 1.6292 0.7839 0.8217 0.2656  -0.0383 0.0085  38  ARG C CB  
4365 C CG  . ARG C 40  ? 1.5572 0.7431 0.7776 0.2777  -0.0192 -0.0073 38  ARG C CG  
4366 C CD  . ARG C 40  ? 1.5201 0.6920 0.7174 0.2774  -0.0039 -0.0263 38  ARG C CD  
4367 N NE  . ARG C 40  ? 1.5056 0.7067 0.7110 0.2823  0.0197  -0.0415 38  ARG C NE  
4368 C CZ  . ARG C 40  ? 1.5545 0.7486 0.7267 0.2757  0.0343  -0.0564 38  ARG C CZ  
4369 N NH1 . ARG C 40  ? 1.5496 0.7105 0.6862 0.2649  0.0254  -0.0579 38  ARG C NH1 
4370 N NH2 . ARG C 40  ? 1.6384 0.8579 0.8122 0.2782  0.0576  -0.0692 38  ARG C NH2 
4371 N N   . GLN C 41  ? 1.5511 0.6775 0.8035 0.2859  -0.0856 0.0314  39  GLN C N   
4372 C CA  . GLN C 41  ? 1.5917 0.7138 0.8938 0.3002  -0.1061 0.0376  39  GLN C CA  
4373 C C   . GLN C 41  ? 1.6019 0.6960 0.9260 0.3133  -0.1113 0.0275  39  GLN C C   
4374 O O   . GLN C 41  ? 1.5559 0.6128 0.8445 0.3048  -0.1204 0.0313  39  GLN C O   
4375 C CB  . GLN C 41  ? 1.6356 0.7335 0.9186 0.2884  -0.1378 0.0621  39  GLN C CB  
4376 C CG  . GLN C 41  ? 1.6658 0.7475 0.9975 0.2997  -0.1690 0.0732  39  GLN C CG  
4377 C CD  . GLN C 41  ? 1.6876 0.7524 0.9999 0.2866  -0.2007 0.0971  39  GLN C CD  
4378 O OE1 . GLN C 41  ? 1.7891 0.8403 1.0452 0.2625  -0.2046 0.1048  39  GLN C OE1 
4379 N NE2 . GLN C 41  ? 1.7135 0.7951 1.0834 0.2964  -0.2192 0.1047  39  GLN C NE2 
4380 N N   . HIS C 42  ? 1.6381 0.7501 1.0247 0.3339  -0.1048 0.0143  40  HIS C N   
4381 C CA  . HIS C 42  ? 1.4850 0.5705 0.9062 0.3494  -0.1122 0.0029  40  HIS C CA  
4382 C C   . HIS C 42  ? 1.5634 0.6181 1.0132 0.3504  -0.1542 0.0251  40  HIS C C   
4383 O O   . HIS C 42  ? 1.6232 0.6853 1.0813 0.3442  -0.1740 0.0450  40  HIS C O   
4384 C CB  . HIS C 42  ? 1.5539 0.6711 1.0353 0.3715  -0.0846 -0.0223 40  HIS C CB  
4385 C CG  . HIS C 42  ? 1.5762 0.7134 1.0210 0.3688  -0.0457 -0.0450 40  HIS C CG  
4386 N ND1 . HIS C 42  ? 1.5442 0.6678 0.9175 0.3501  -0.0410 -0.0434 40  HIS C ND1 
4387 C CD2 . HIS C 42  ? 1.5359 0.7035 1.0046 0.3807  -0.0107 -0.0689 40  HIS C CD2 
4388 C CE1 . HIS C 42  ? 1.5886 0.7305 0.9417 0.3497  -0.0097 -0.0638 40  HIS C CE1 
4389 N NE2 . HIS C 42  ? 1.6589 0.8266 1.0632 0.3674  0.0106  -0.0799 40  HIS C NE2 
4390 N N   . PRO C 43  ? 1.6593 0.6748 1.1222 0.3565  -0.1722 0.0233  41  PRO C N   
4391 C CA  . PRO C 43  ? 1.5760 0.5656 1.0692 0.3518  -0.2157 0.0466  41  PRO C CA  
4392 C C   . PRO C 43  ? 1.5961 0.6073 1.1701 0.3673  -0.2304 0.0520  41  PRO C C   
4393 O O   . PRO C 43  ? 1.5786 0.5996 1.2270 0.3929  -0.2209 0.0332  41  PRO C O   
4394 C CB  . PRO C 43  ? 1.6047 0.5712 1.1223 0.3560  -0.2232 0.0363  41  PRO C CB  
4395 C CG  . PRO C 43  ? 1.5993 0.5665 1.0988 0.3708  -0.1855 0.0047  41  PRO C CG  
4396 C CD  . PRO C 43  ? 1.6003 0.5962 1.0469 0.3615  -0.1564 0.0019  41  PRO C CD  
4397 N N   . GLY C 44  ? 1.6363 0.6563 1.1998 0.3508  -0.2525 0.0763  42  GLY C N   
4398 C CA  . GLY C 44  ? 1.6773 0.7196 1.3186 0.3610  -0.2707 0.0858  42  GLY C CA  
4399 C C   . GLY C 44  ? 1.6628 0.7477 1.3267 0.3748  -0.2412 0.0748  42  GLY C C   
4400 O O   . GLY C 44  ? 1.6022 0.7084 1.3341 0.3822  -0.2565 0.0850  42  GLY C O   
4401 N N   . LYS C 45  ? 1.5962 0.7068 1.2136 0.3717  -0.1980 0.0556  43  LYS C N   
4402 C CA  . LYS C 45  ? 1.6472 0.8125 1.2858 0.3760  -0.1646 0.0454  43  LYS C CA  
4403 C C   . LYS C 45  ? 1.7054 0.8779 1.2784 0.3541  -0.1686 0.0613  43  LYS C C   
4404 O O   . LYS C 45  ? 1.7479 0.8835 1.2574 0.3364  -0.1921 0.0773  43  LYS C O   
4405 C CB  . LYS C 45  ? 1.6296 0.8165 1.2610 0.3857  -0.1165 0.0139  43  LYS C CB  
4406 C CG  . LYS C 45  ? 1.5237 0.7055 1.2236 0.4095  -0.1067 -0.0076 43  LYS C CG  
4407 C CD  . LYS C 45  ? 1.5376 0.7516 1.3436 0.4272  -0.1096 -0.0052 43  LYS C CD  
4408 C CE  . LYS C 45  ? 1.6936 0.8729 1.5649 0.4376  -0.1534 0.0071  43  LYS C CE  
4409 N NZ  . LYS C 45  ? 1.6175 0.8293 1.6087 0.4571  -0.1549 0.0073  43  LYS C NZ  
4410 N N   . GLU C 46  ? 1.7133 0.9333 1.3029 0.3548  -0.1438 0.0564  44  GLU C N   
4411 C CA  . GLU C 46  ? 1.7517 0.9822 1.2949 0.3364  -0.1493 0.0705  44  GLU C CA  
4412 C C   . GLU C 46  ? 1.6835 0.9073 1.1455 0.3215  -0.1265 0.0612  44  GLU C C   
4413 O O   . GLU C 46  ? 1.6578 0.8752 1.1018 0.3254  -0.1039 0.0434  44  GLU C O   
4414 C CB  . GLU C 46  ? 1.6452 0.9289 1.2436 0.3416  -0.1347 0.0714  44  GLU C CB  
4415 C CG  . GLU C 46  ? 1.7487 1.0451 1.4434 0.3572  -0.1545 0.0805  44  GLU C CG  
4416 C CD  . GLU C 46  ? 1.8480 1.1151 1.5421 0.3472  -0.2066 0.1083  44  GLU C CD  
4417 O OE1 . GLU C 46  ? 1.9212 1.1687 1.5409 0.3280  -0.2198 0.1186  44  GLU C OE1 
4418 O OE2 . GLU C 46  ? 1.8530 1.1139 1.6214 0.3579  -0.2351 0.1192  44  GLU C OE2 
4419 N N   . ARG C 47  ? 1.6520 0.8753 1.0679 0.3041  -0.1344 0.0731  45  ARG C N   
4420 C CA  . ARG C 47  ? 1.6359 0.8566 0.9869 0.2891  -0.1150 0.0664  45  ARG C CA  
4421 C C   . ARG C 47  ? 1.5656 0.8341 0.9318 0.2891  -0.0864 0.0567  45  ARG C C   
4422 O O   . ARG C 47  ? 1.5253 0.8198 0.9079 0.2845  -0.0917 0.0662  45  ARG C O   
4423 C CB  . ARG C 47  ? 1.5365 0.7314 0.8343 0.2706  -0.1352 0.0816  45  ARG C CB  
4424 C CG  . ARG C 47  ? 1.7131 0.8774 1.0177 0.2697  -0.1739 0.1002  45  ARG C CG  
4425 C CD  . ARG C 47  ? 1.7057 0.8445 0.9488 0.2487  -0.1892 0.1113  45  ARG C CD  
4426 N NE  . ARG C 47  ? 1.7354 0.8475 0.9282 0.2314  -0.1839 0.1077  45  ARG C NE  
4427 C CZ  . ARG C 47  ? 1.7560 0.8416 0.9402 0.2206  -0.2057 0.1155  45  ARG C CZ  
4428 N NH1 . ARG C 47  ? 1.7676 0.8496 0.9935 0.2249  -0.2366 0.1270  45  ARG C NH1 
4429 N NH2 . ARG C 47  ? 1.7329 0.7956 0.8695 0.2040  -0.1970 0.1132  45  ARG C NH2 
4430 N N   . GLU C 48  ? 1.5557 0.8328 0.9139 0.2927  -0.0584 0.0388  46  GLU C N   
4431 C CA  . GLU C 48  ? 1.5384 0.8554 0.9021 0.2899  -0.0313 0.0302  46  GLU C CA  
4432 C C   . GLU C 48  ? 1.5178 0.8299 0.8258 0.2712  -0.0245 0.0295  46  GLU C C   
4433 O O   . GLU C 48  ? 1.5278 0.8063 0.7961 0.2635  -0.0318 0.0298  46  GLU C O   
4434 C CB  . GLU C 48  ? 1.5630 0.8901 0.9487 0.3037  -0.0042 0.0097  46  GLU C CB  
4435 C CG  . GLU C 48  ? 1.6064 0.8957 0.9553 0.3052  0.0006  -0.0051 46  GLU C CG  
4436 C CD  . GLU C 48  ? 1.7550 1.0508 1.0657 0.2972  0.0272  -0.0211 46  GLU C CD  
4437 O OE1 . GLU C 48  ? 1.7522 1.0837 1.0699 0.2929  0.0458  -0.0226 46  GLU C OE1 
4438 O OE2 . GLU C 48  ? 1.7618 1.0250 1.0352 0.2939  0.0276  -0.0310 46  GLU C OE2 
4439 N N   . PHE C 49  ? 1.4158 0.7624 0.7268 0.2632  -0.0110 0.0300  47  PHE C N   
4440 C CA  . PHE C 49  ? 1.3875 0.7340 0.6598 0.2447  -0.0092 0.0323  47  PHE C CA  
4441 C C   . PHE C 49  ? 1.4222 0.7513 0.6590 0.2396  0.0057  0.0184  47  PHE C C   
4442 O O   . PHE C 49  ? 1.5337 0.8653 0.7735 0.2479  0.0226  0.0047  47  PHE C O   
4443 C CB  . PHE C 49  ? 1.4252 0.8127 0.7164 0.2366  -0.0039 0.0396  47  PHE C CB  
4444 C CG  . PHE C 49  ? 1.4023 0.7904 0.6661 0.2177  -0.0080 0.0444  47  PHE C CG  
4445 C CD1 . PHE C 49  ? 1.3731 0.7361 0.6167 0.2105  -0.0229 0.0489  47  PHE C CD1 
4446 C CD2 . PHE C 49  ? 1.2882 0.7003 0.5477 0.2060  0.0034  0.0443  47  PHE C CD2 
4447 C CE1 . PHE C 49  ? 1.2360 0.6008 0.4660 0.1945  -0.0253 0.0516  47  PHE C CE1 
4448 C CE2 . PHE C 49  ? 1.2842 0.6959 0.5280 0.1885  -0.0045 0.0498  47  PHE C CE2 
4449 C CZ  . PHE C 49  ? 1.2469 0.6363 0.4812 0.1840  -0.0183 0.0525  47  PHE C CZ  
4450 N N   . VAL C 50  ? 1.3337 0.6437 0.5382 0.2252  -0.0007 0.0212  48  VAL C N   
4451 C CA  . VAL C 50  ? 1.4539 0.7463 0.6274 0.2167  0.0076  0.0115  48  VAL C CA  
4452 C C   . VAL C 50  ? 1.4452 0.7540 0.6095 0.1979  0.0068  0.0175  48  VAL C C   
4453 O O   . VAL C 50  ? 1.4604 0.7826 0.6152 0.1910  0.0162  0.0133  48  VAL C O   
4454 C CB  . VAL C 50  ? 1.4595 0.7113 0.6127 0.2158  -0.0008 0.0105  48  VAL C CB  
4455 C CG1 . VAL C 50  ? 1.4244 0.6601 0.5519 0.2012  0.0011  0.0065  48  VAL C CG1 
4456 C CG2 . VAL C 50  ? 1.5261 0.7574 0.6862 0.2328  -0.0005 0.0018  48  VAL C CG2 
4457 N N   . ALA C 51  ? 1.3334 0.6394 0.5002 0.1886  -0.0044 0.0273  49  ALA C N   
4458 C CA  . ALA C 51  ? 1.3926 0.7108 0.5601 0.1711  -0.0084 0.0330  49  ALA C CA  
4459 C C   . ALA C 51  ? 1.3145 0.6350 0.4955 0.1666  -0.0180 0.0413  49  ALA C C   
4460 O O   . ALA C 51  ? 1.2674 0.5658 0.4402 0.1714  -0.0203 0.0413  49  ALA C O   
4461 C CB  . ALA C 51  ? 1.2833 0.5771 0.4304 0.1595  -0.0088 0.0283  49  ALA C CB  
4462 N N   . SER C 52  ? 1.2299 0.5746 0.4289 0.1562  -0.0239 0.0481  50  SER C N   
4463 C CA  . SER C 52  ? 1.3398 0.6860 0.5527 0.1515  -0.0324 0.0527  50  SER C CA  
4464 C C   . SER C 52  ? 1.2173 0.5731 0.4474 0.1350  -0.0380 0.0559  50  SER C C   
4465 O O   . SER C 52  ? 1.2120 0.5810 0.4446 0.1261  -0.0402 0.0592  50  SER C O   
4466 C CB  . SER C 52  ? 1.2716 0.6386 0.5020 0.1586  -0.0407 0.0593  50  SER C CB  
4467 O OG  . SER C 52  ? 1.1914 0.5917 0.4430 0.1531  -0.0431 0.0662  50  SER C OG  
4468 N N   . ILE C 53  ? 1.1363 0.4832 0.3780 0.1300  -0.0407 0.0546  51  ILE C N   
4469 C CA  . ILE C 53  ? 1.1327 0.4880 0.4040 0.1156  -0.0480 0.0569  51  ILE C CA  
4470 C C   . ILE C 53  ? 1.2030 0.5721 0.4963 0.1156  -0.0568 0.0588  51  ILE C C   
4471 O O   . ILE C 53  ? 1.1907 0.5471 0.4700 0.1237  -0.0537 0.0542  51  ILE C O   
4472 C CB  . ILE C 53  ? 1.0996 0.4308 0.3763 0.1092  -0.0403 0.0509  51  ILE C CB  
4473 C CG1 . ILE C 53  ? 1.0824 0.4230 0.4033 0.0950  -0.0498 0.0533  51  ILE C CG1 
4474 C CG2 . ILE C 53  ? 1.1444 0.4536 0.4032 0.1166  -0.0274 0.0436  51  ILE C CG2 
4475 C CD1 . ILE C 53  ? 1.1218 0.4424 0.4625 0.0893  -0.0399 0.0472  51  ILE C CD1 
4476 N N   . TRP C 54  ? 1.2795 0.6714 0.6040 0.1053  -0.0705 0.0664  52  TRP C N   
4477 C CA  . TRP C 54  ? 1.2990 0.7022 0.6503 0.1039  -0.0822 0.0677  52  TRP C CA  
4478 C C   . TRP C 54  ? 1.2602 0.6424 0.6235 0.1022  -0.0753 0.0553  52  TRP C C   
4479 O O   . TRP C 54  ? 1.2804 0.6493 0.6517 0.0968  -0.0659 0.0502  52  TRP C O   
4480 C CB  . TRP C 54  ? 1.2923 0.7226 0.6779 0.0907  -0.1005 0.0804  52  TRP C CB  
4481 C CG  . TRP C 54  ? 1.2719 0.7170 0.6884 0.0895  -0.1168 0.0843  52  TRP C CG  
4482 C CD1 . TRP C 54  ? 1.2184 0.6729 0.6790 0.0775  -0.1342 0.0884  52  TRP C CD1 
4483 C CD2 . TRP C 54  ? 1.2495 0.6993 0.6587 0.1000  -0.1215 0.0852  52  TRP C CD2 
4484 N NE1 . TRP C 54  ? 1.1678 0.6321 0.6469 0.0804  -0.1480 0.0905  52  TRP C NE1 
4485 C CE2 . TRP C 54  ? 1.2405 0.7016 0.6875 0.0937  -0.1412 0.0890  52  TRP C CE2 
4486 C CE3 . TRP C 54  ? 1.2584 0.7018 0.6373 0.1136  -0.1143 0.0841  52  TRP C CE3 
4487 C CZ2 . TRP C 54  ? 1.2556 0.7206 0.7069 0.1001  -0.1541 0.0916  52  TRP C CZ2 
4488 C CZ3 . TRP C 54  ? 1.2477 0.6953 0.6337 0.1194  -0.1283 0.0880  52  TRP C CZ3 
4489 C CH2 . TRP C 54  ? 1.2588 0.7166 0.6788 0.1125  -0.1480 0.0916  52  TRP C CH2 
4490 N N   . TRP C 55  ? 1.1646 0.5426 0.5301 0.1065  -0.0792 0.0497  53  TRP C N   
4491 C CA  . TRP C 55  ? 1.1367 0.4906 0.5023 0.1062  -0.0658 0.0340  53  TRP C CA  
4492 C C   . TRP C 55  ? 1.1855 0.5453 0.6057 0.0957  -0.0669 0.0296  53  TRP C C   
4493 O O   . TRP C 55  ? 1.1158 0.4570 0.5444 0.0947  -0.0487 0.0153  53  TRP C O   
4494 C CB  . TRP C 55  ? 1.1608 0.5036 0.5087 0.1118  -0.0721 0.0276  53  TRP C CB  
4495 C CG  . TRP C 55  ? 1.2336 0.5950 0.6238 0.1075  -0.0936 0.0301  53  TRP C CG  
4496 C CD1 . TRP C 55  ? 1.2117 0.5971 0.6153 0.1080  -0.1165 0.0448  53  TRP C CD1 
4497 C CD2 . TRP C 55  ? 1.1816 0.5386 0.6112 0.1020  -0.0942 0.0175  53  TRP C CD2 
4498 N NE1 . TRP C 55  ? 1.2268 0.6221 0.6731 0.1022  -0.1342 0.0439  53  TRP C NE1 
4499 C CE2 . TRP C 55  ? 1.1255 0.5029 0.5891 0.0992  -0.1216 0.0261  53  TRP C CE2 
4500 C CE3 . TRP C 55  ? 1.1637 0.5024 0.6087 0.0994  -0.0730 -0.0006 53  TRP C CE3 
4501 C CZ2 . TRP C 55  ? 1.1008 0.4783 0.6124 0.0944  -0.1315 0.0166  53  TRP C CZ2 
4502 C CZ3 . TRP C 55  ? 1.1202 0.4606 0.6158 0.0955  -0.0793 -0.0119 53  TRP C CZ3 
4503 C CH2 . TRP C 55  ? 1.1066 0.4651 0.6344 0.0934  -0.1098 -0.0036 53  TRP C CH2 
4504 N N   . THR C 56  ? 1.1310 0.5151 0.5906 0.0867  -0.0876 0.0421  54  THR C N   
4505 C CA  . THR C 56  ? 1.0664 0.4546 0.5848 0.0751  -0.0944 0.0412  54  THR C CA  
4506 C C   . THR C 56  ? 1.1193 0.5013 0.6422 0.0678  -0.0896 0.0463  54  THR C C   
4507 O O   . THR C 56  ? 1.1133 0.4919 0.6877 0.0592  -0.0916 0.0437  54  THR C O   
4508 C CB  . THR C 56  ? 1.0745 0.4875 0.6341 0.0652  -0.1248 0.0553  54  THR C CB  
4509 O OG1 . THR C 56  ? 1.1899 0.6157 0.7403 0.0552  -0.1376 0.0737  54  THR C OG1 
4510 C CG2 . THR C 56  ? 1.1605 0.5829 0.7049 0.0724  -0.1346 0.0571  54  THR C CG2 
4511 N N   . GLY C 57  ? 1.1632 0.5421 0.6383 0.0710  -0.0847 0.0529  55  GLY C N   
4512 C CA  . GLY C 57  ? 1.2421 0.6107 0.7148 0.0638  -0.0836 0.0574  55  GLY C CA  
4513 C C   . GLY C 57  ? 1.2231 0.6037 0.7066 0.0489  -0.1085 0.0737  55  GLY C C   
4514 O O   . GLY C 57  ? 1.2719 0.6395 0.7547 0.0399  -0.1132 0.0780  55  GLY C O   
4515 N N   . THR C 58  ? 1.0546 0.4569 0.5454 0.0442  -0.1260 0.0839  56  THR C N   
4516 C CA  . THR C 58  ? 1.2717 0.6835 0.7648 0.0264  -0.1498 0.1016  56  THR C CA  
4517 C C   . THR C 58  ? 1.2422 0.6600 0.6755 0.0287  -0.1431 0.1075  56  THR C C   
4518 O O   . THR C 58  ? 1.2885 0.6996 0.6991 0.0147  -0.1529 0.1166  56  THR C O   
4519 C CB  . THR C 58  ? 1.2176 0.6499 0.7569 0.0163  -0.1740 0.1123  56  THR C CB  
4520 O OG1 . THR C 58  ? 1.1203 0.5706 0.6438 0.0275  -0.1685 0.1119  56  THR C OG1 
4521 C CG2 . THR C 58  ? 1.0900 0.5158 0.6966 0.0151  -0.1794 0.1033  56  THR C CG2 
4522 N N   . THR C 59  ? 1.1930 0.6209 0.6011 0.0453  -0.1271 0.1019  57  THR C N   
4523 C CA  . THR C 59  ? 1.2481 0.6862 0.6125 0.0498  -0.1175 0.1059  57  THR C CA  
4524 C C   . THR C 59  ? 1.2632 0.6833 0.5915 0.0675  -0.0948 0.0920  57  THR C C   
4525 O O   . THR C 59  ? 1.1797 0.5900 0.5128 0.0802  -0.0859 0.0824  57  THR C O   
4526 C CB  . THR C 59  ? 1.2285 0.6956 0.6056 0.0539  -0.1213 0.1140  57  THR C CB  
4527 O OG1 . THR C 59  ? 1.2227 0.7032 0.6428 0.0388  -0.1452 0.1258  57  THR C OG1 
4528 C CG2 . THR C 59  ? 1.1763 0.6597 0.5214 0.0531  -0.1116 0.1213  57  THR C CG2 
4529 N N   . THR C 60  ? 1.4156 0.8280 0.7053 0.0670  -0.0862 0.0907  58  THR C N   
4530 C CA  . THR C 60  ? 1.2251 0.6204 0.4830 0.0836  -0.0673 0.0784  58  THR C CA  
4531 C C   . THR C 60  ? 1.1318 0.5422 0.3642 0.0903  -0.0552 0.0785  58  THR C C   
4532 O O   . THR C 60  ? 1.1933 0.6150 0.4129 0.0771  -0.0578 0.0858  58  THR C O   
4533 C CB  . THR C 60  ? 1.2377 0.6016 0.4776 0.0782  -0.0668 0.0723  58  THR C CB  
4534 O OG1 . THR C 60  ? 1.3024 0.6625 0.5199 0.0619  -0.0757 0.0780  58  THR C OG1 
4535 C CG2 . THR C 60  ? 1.2549 0.6068 0.5309 0.0714  -0.0750 0.0723  58  THR C CG2 
4536 N N   . TYR C 61  ? 1.1783 0.5876 0.4046 0.1099  -0.0417 0.0707  59  TYR C N   
4537 C CA  . TYR C 61  ? 1.2554 0.6805 0.4708 0.1199  -0.0269 0.0685  59  TYR C CA  
4538 C C   . TYR C 61  ? 1.3153 0.7144 0.5031 0.1329  -0.0129 0.0539  59  TYR C C   
4539 O O   . TYR C 61  ? 1.3587 0.7339 0.5446 0.1410  -0.0149 0.0484  59  TYR C O   
4540 C CB  . TYR C 61  ? 1.3012 0.7501 0.5478 0.1322  -0.0281 0.0742  59  TYR C CB  
4541 C CG  . TYR C 61  ? 1.3670 0.8423 0.6438 0.1203  -0.0434 0.0886  59  TYR C CG  
4542 C CD1 . TYR C 61  ? 1.2399 0.7068 0.5334 0.1129  -0.0600 0.0912  59  TYR C CD1 
4543 C CD2 . TYR C 61  ? 1.3137 0.8223 0.6060 0.1162  -0.0400 0.0993  59  TYR C CD2 
4544 C CE1 . TYR C 61  ? 1.2499 0.7385 0.5749 0.1027  -0.0763 0.1032  59  TYR C CE1 
4545 C CE2 . TYR C 61  ? 1.2249 0.7565 0.5475 0.1044  -0.0569 0.1143  59  TYR C CE2 
4546 C CZ  . TYR C 61  ? 1.3066 0.8269 0.6456 0.0980  -0.0768 0.1158  59  TYR C CZ  
4547 O OH  . TYR C 61  ? 1.2943 0.8353 0.6673 0.0868  -0.0959 0.1296  59  TYR C OH  
4548 N N   . TYR C 62  ? 1.3896 0.7917 0.5548 0.1341  0.0023  0.0474  60  TYR C N   
4549 C CA  . TYR C 62  ? 1.3835 0.7602 0.5243 0.1469  0.0156  0.0312  60  TYR C CA  
4550 C C   . TYR C 62  ? 1.3394 0.7364 0.4865 0.1604  0.0373  0.0240  60  TYR C C   
4551 O O   . TYR C 62  ? 1.3823 0.8099 0.5373 0.1533  0.0455  0.0311  60  TYR C O   
4552 C CB  . TYR C 62  ? 1.3879 0.7347 0.4868 0.1327  0.0132  0.0244  60  TYR C CB  
4553 C CG  . TYR C 62  ? 1.4792 0.8043 0.5816 0.1201  -0.0070 0.0307  60  TYR C CG  
4554 C CD1 . TYR C 62  ? 1.3894 0.7259 0.5058 0.1007  -0.0233 0.0446  60  TYR C CD1 
4555 C CD2 . TYR C 62  ? 1.3729 0.6664 0.4708 0.1271  -0.0096 0.0235  60  TYR C CD2 
4556 C CE1 . TYR C 62  ? 1.3544 0.6731 0.4861 0.0901  -0.0398 0.0493  60  TYR C CE1 
4557 C CE2 . TYR C 62  ? 1.3870 0.6635 0.4962 0.1154  -0.0242 0.0295  60  TYR C CE2 
4558 C CZ  . TYR C 62  ? 1.3876 0.6775 0.5165 0.0976  -0.0382 0.0415  60  TYR C CZ  
4559 O OH  . TYR C 62  ? 1.3098 0.5847 0.4616 0.0869  -0.0509 0.0465  60  TYR C OH  
4560 N N   . ALA C 63  ? 1.4326 0.8127 0.5810 0.1794  0.0469  0.0103  61  ALA C N   
4561 C CA  . ALA C 63  ? 1.2822 0.6783 0.4438 0.1942  0.0705  -0.0005 61  ALA C CA  
4562 C C   . ALA C 63  ? 1.4426 0.8234 0.5573 0.1872  0.0899  -0.0168 61  ALA C C   
4563 O O   . ALA C 63  ? 1.5540 0.9031 0.6261 0.1744  0.0802  -0.0208 61  ALA C O   
4564 C CB  . ALA C 63  ? 1.3637 0.7457 0.5528 0.2175  0.0695  -0.0084 61  ALA C CB  
4565 N N   . ASP C 64  ? 1.5141 0.9166 0.6375 0.1952  0.1181  -0.0265 62  ASP C N   
4566 C CA  . ASP C 64  ? 1.5396 0.9264 0.6099 0.1870  0.1411  -0.0441 62  ASP C CA  
4567 C C   . ASP C 64  ? 1.5704 0.9101 0.6110 0.1971  0.1405  -0.0660 62  ASP C C   
4568 O O   . ASP C 64  ? 1.6410 0.9488 0.6215 0.1829  0.1408  -0.0762 62  ASP C O   
4569 C CB  . ASP C 64  ? 1.5502 0.9712 0.6419 0.1954  0.1779  -0.0524 62  ASP C CB  
4570 C CG  . ASP C 64  ? 1.7945 1.2523 0.8836 0.1743  0.1832  -0.0330 62  ASP C CG  
4571 O OD1 . ASP C 64  ? 1.8064 1.2593 0.8735 0.1528  0.1565  -0.0148 62  ASP C OD1 
4572 O OD2 . ASP C 64  ? 1.9679 1.4598 1.0820 0.1788  0.2140  -0.0352 62  ASP C OD2 
4573 N N   . SER C 65  ? 1.4860 0.8178 0.5674 0.2200  0.1359  -0.0719 63  SER C N   
4574 C CA  . SER C 65  ? 1.5270 0.8134 0.5886 0.2300  0.1304  -0.0897 63  SER C CA  
4575 C C   . SER C 65  ? 1.5632 0.8185 0.6010 0.2165  0.0992  -0.0783 63  SER C C   
4576 O O   . SER C 65  ? 1.7258 0.9433 0.7530 0.2232  0.0895  -0.0881 63  SER C O   
4577 C CB  . SER C 65  ? 1.5862 0.8745 0.7049 0.2573  0.1322  -0.0962 63  SER C CB  
4578 O OG  . SER C 65  ? 1.5696 0.8894 0.7396 0.2613  0.1192  -0.0746 63  SER C OG  
4579 N N   . VAL C 66  ? 1.5740 0.8448 0.6087 0.1975  0.0838  -0.0576 64  VAL C N   
4580 C CA  . VAL C 66  ? 1.5736 0.8232 0.6033 0.1857  0.0571  -0.0448 64  VAL C CA  
4581 C C   . VAL C 66  ? 1.5303 0.7718 0.5237 0.1593  0.0457  -0.0372 64  VAL C C   
4582 O O   . VAL C 66  ? 1.4113 0.6202 0.3868 0.1488  0.0280  -0.0360 64  VAL C O   
4583 C CB  . VAL C 66  ? 1.5476 0.8203 0.6218 0.1899  0.0449  -0.0265 64  VAL C CB  
4584 C CG1 . VAL C 66  ? 1.5761 0.8304 0.6473 0.1764  0.0240  -0.0148 64  VAL C CG1 
4585 C CG2 . VAL C 66  ? 1.5274 0.7988 0.6340 0.2131  0.0480  -0.0310 64  VAL C CG2 
4586 N N   . LYS C 67  ? 1.5716 0.8411 0.5568 0.1469  0.0536  -0.0304 65  LYS C N   
4587 C CA  . LYS C 67  ? 1.5524 0.8161 0.5103 0.1193  0.0366  -0.0179 65  LYS C CA  
4588 C C   . LYS C 67  ? 1.5474 0.7695 0.4558 0.1061  0.0302  -0.0297 65  LYS C C   
4589 O O   . LYS C 67  ? 1.6173 0.8275 0.4991 0.1132  0.0495  -0.0492 65  LYS C O   
4590 C CB  . LYS C 67  ? 1.4884 0.7886 0.4438 0.1077  0.0475  -0.0080 65  LYS C CB  
4591 C CG  . LYS C 67  ? 1.5123 0.8300 0.4890 0.0876  0.0231  0.0159  65  LYS C CG  
4592 C CD  . LYS C 67  ? 1.5938 0.9417 0.5595 0.0717  0.0314  0.0272  65  LYS C CD  
4593 C CE  . LYS C 67  ? 1.6207 1.0083 0.6200 0.0908  0.0585  0.0244  65  LYS C CE  
4594 N NZ  . LYS C 67  ? 1.7527 1.1766 0.7592 0.0743  0.0618  0.0422  65  LYS C NZ  
4595 N N   . GLY C 68  ? 1.4603 0.6632 0.3685 0.0862  0.0018  -0.0176 66  GLY C N   
4596 C CA  . GLY C 68  ? 1.5219 0.6852 0.3944 0.0698  -0.0131 -0.0239 66  GLY C CA  
4597 C C   . GLY C 68  ? 1.5146 0.6356 0.3846 0.0793  -0.0261 -0.0307 66  GLY C C   
4598 O O   . GLY C 68  ? 1.5424 0.6267 0.3920 0.0622  -0.0504 -0.0275 66  GLY C O   
4599 N N   . ARG C 69  ? 1.4944 0.6164 0.3830 0.1049  -0.0131 -0.0386 67  ARG C N   
4600 C CA  . ARG C 69  ? 1.4977 0.5865 0.3969 0.1133  -0.0238 -0.0435 67  ARG C CA  
4601 C C   . ARG C 69  ? 1.4968 0.6000 0.4502 0.1161  -0.0327 -0.0268 67  ARG C C   
4602 O O   . ARG C 69  ? 1.5752 0.6530 0.5402 0.1085  -0.0495 -0.0208 67  ARG C O   
4603 C CB  . ARG C 69  ? 1.6597 0.7373 0.5515 0.1379  -0.0043 -0.0650 67  ARG C CB  
4604 C CG  . ARG C 69  ? 1.6288 0.7128 0.4889 0.1399  0.0178  -0.0829 67  ARG C CG  
4605 C CD  . ARG C 69  ? 1.5997 0.6651 0.4600 0.1632  0.0332  -0.1064 67  ARG C CD  
4606 N NE  . ARG C 69  ? 1.5709 0.6631 0.4680 0.1881  0.0518  -0.1096 67  ARG C NE  
4607 C CZ  . ARG C 69  ? 1.5416 0.6312 0.4808 0.2034  0.0432  -0.1042 67  ARG C CZ  
4608 N NH1 . ARG C 69  ? 1.5416 0.5982 0.4806 0.1987  0.0211  -0.0982 67  ARG C NH1 
4609 N NH2 . ARG C 69  ? 1.5156 0.6351 0.4986 0.2222  0.0556  -0.1030 67  ARG C NH2 
4610 N N   . PHE C 70  ? 1.5121 0.6538 0.4982 0.1257  -0.0214 -0.0194 68  PHE C N   
4611 C CA  . PHE C 70  ? 1.4298 0.5816 0.4577 0.1288  -0.0259 -0.0068 68  PHE C CA  
4612 C C   . PHE C 70  ? 1.3848 0.5616 0.4378 0.1128  -0.0348 0.0087  68  PHE C C   
4613 O O   . PHE C 70  ? 1.3372 0.5368 0.3836 0.1055  -0.0339 0.0121  68  PHE C O   
4614 C CB  . PHE C 70  ? 1.4760 0.6453 0.5216 0.1502  -0.0118 -0.0095 68  PHE C CB  
4615 C CG  . PHE C 70  ? 1.6101 0.7550 0.6424 0.1672  -0.0055 -0.0241 68  PHE C CG  
4616 C CD1 . PHE C 70  ? 1.6666 0.7719 0.6833 0.1641  -0.0151 -0.0297 68  PHE C CD1 
4617 C CD2 . PHE C 70  ? 1.5632 0.7243 0.6061 0.1862  0.0079  -0.0317 68  PHE C CD2 
4618 C CE1 . PHE C 70  ? 1.7187 0.7993 0.7271 0.1798  -0.0119 -0.0438 68  PHE C CE1 
4619 C CE2 . PHE C 70  ? 1.6772 0.8149 0.7170 0.2026  0.0119  -0.0459 68  PHE C CE2 
4620 C CZ  . PHE C 70  ? 1.7456 0.8423 0.7666 0.1995  0.0019  -0.0525 68  PHE C CZ  
4621 N N   . THR C 71  ? 1.5305 0.7022 0.6148 0.1069  -0.0425 0.0181  69  THR C N   
4622 C CA  . THR C 71  ? 1.3228 0.5145 0.4415 0.0929  -0.0512 0.0306  69  THR C CA  
4623 C C   . THR C 71  ? 1.3217 0.5248 0.4713 0.1013  -0.0414 0.0341  69  THR C C   
4624 O O   . THR C 71  ? 1.2526 0.4352 0.4071 0.1047  -0.0370 0.0334  69  THR C O   
4625 C CB  . THR C 71  ? 1.2773 0.4471 0.4089 0.0729  -0.0711 0.0374  69  THR C CB  
4626 O OG1 . THR C 71  ? 1.3784 0.5416 0.4785 0.0590  -0.0849 0.0381  69  THR C OG1 
4627 C CG2 . THR C 71  ? 1.2421 0.4287 0.4279 0.0630  -0.0767 0.0484  69  THR C CG2 
4628 N N   . ILE C 72  ? 1.3518 0.5846 0.5183 0.1032  -0.0382 0.0383  70  ILE C N   
4629 C CA  . ILE C 72  ? 1.2926 0.5329 0.4816 0.1083  -0.0302 0.0404  70  ILE C CA  
4630 C C   . ILE C 72  ? 1.2480 0.4988 0.4779 0.0937  -0.0373 0.0464  70  ILE C C   
4631 O O   . ILE C 72  ? 1.1563 0.4238 0.3994 0.0835  -0.0502 0.0519  70  ILE C O   
4632 C CB  . ILE C 72  ? 1.2276 0.4891 0.4094 0.1215  -0.0245 0.0396  70  ILE C CB  
4633 C CG1 . ILE C 72  ? 1.2221 0.4846 0.4175 0.1238  -0.0190 0.0409  70  ILE C CG1 
4634 C CG2 . ILE C 72  ? 1.2182 0.5089 0.4070 0.1164  -0.0315 0.0440  70  ILE C CG2 
4635 C CD1 . ILE C 72  ? 1.2378 0.5189 0.4307 0.1336  -0.0202 0.0424  70  ILE C CD1 
4636 N N   . SER C 73  ? 1.1627 0.4027 0.4150 0.0918  -0.0285 0.0457  71  SER C N   
4637 C CA  . SER C 73  ? 1.1446 0.3936 0.4464 0.0801  -0.0312 0.0485  71  SER C CA  
4638 C C   . SER C 73  ? 1.2141 0.4602 0.5236 0.0856  -0.0108 0.0429  71  SER C C   
4639 O O   . SER C 73  ? 1.3012 0.5375 0.5731 0.0963  0.0004  0.0397  71  SER C O   
4640 C CB  . SER C 73  ? 1.1520 0.3851 0.4833 0.0660  -0.0419 0.0533  71  SER C CB  
4641 O OG  . SER C 73  ? 1.1691 0.3789 0.4962 0.0683  -0.0288 0.0514  71  SER C OG  
4642 N N   . ARG C 74  ? 1.2687 0.5210 0.6271 0.0772  -0.0064 0.0415  72  ARG C N   
4643 C CA  . ARG C 74  ? 1.2755 0.5233 0.6382 0.0804  0.0167  0.0332  72  ARG C CA  
4644 C C   . ARG C 74  ? 1.2955 0.5416 0.7201 0.0698  0.0272  0.0309  72  ARG C C   
4645 O O   . ARG C 74  ? 1.4038 0.6624 0.8817 0.0607  0.0102  0.0350  72  ARG C O   
4646 C CB  . ARG C 74  ? 1.2867 0.5509 0.6440 0.0859  0.0139  0.0285  72  ARG C CB  
4647 C CG  . ARG C 74  ? 1.3214 0.5819 0.6990 0.0845  0.0342  0.0170  72  ARG C CG  
4648 C CD  . ARG C 74  ? 1.3768 0.6449 0.7330 0.0912  0.0291  0.0119  72  ARG C CD  
4649 N NE  . ARG C 74  ? 1.5327 0.8116 0.9394 0.0868  0.0305  0.0028  72  ARG C NE  
4650 C CZ  . ARG C 74  ? 1.5263 0.8199 0.9420 0.0890  0.0140  0.0017  72  ARG C CZ  
4651 N NH1 . ARG C 74  ? 1.4753 0.7773 0.8558 0.0951  -0.0038 0.0102  72  ARG C NH1 
4652 N NH2 . ARG C 74  ? 1.5812 0.8817 1.0488 0.0851  0.0151  -0.0081 72  ARG C NH2 
4653 N N   . ASP C 75  ? 1.3622 0.5922 0.7819 0.0697  0.0551  0.0253  73  ASP C N   
4654 C CA  . ASP C 75  ? 1.3926 0.6222 0.8757 0.0608  0.0742  0.0210  73  ASP C CA  
4655 C C   . ASP C 75  ? 1.4771 0.7055 0.9527 0.0640  0.1031  0.0061  73  ASP C C   
4656 O O   . ASP C 75  ? 1.5787 0.7880 0.9973 0.0669  0.1248  0.0023  73  ASP C O   
4657 C CB  . ASP C 75  ? 1.4800 0.6904 0.9661 0.0554  0.0864  0.0276  73  ASP C CB  
4658 C CG  . ASP C 75  ? 1.4365 0.6509 1.0057 0.0450  0.1027  0.0262  73  ASP C CG  
4659 O OD1 . ASP C 75  ? 1.3268 0.5407 0.9092 0.0445  0.1372  0.0147  73  ASP C OD1 
4660 O OD2 . ASP C 75  ? 1.5511 0.7673 1.1729 0.0366  0.0810  0.0361  73  ASP C OD2 
4661 N N   . ASP C 76  ? 1.4097 0.6549 0.9404 0.0622  0.1017  -0.0025 74  ASP C N   
4662 C CA  . ASP C 76  ? 1.5326 0.7743 1.0514 0.0659  0.1259  -0.0200 74  ASP C CA  
4663 C C   . ASP C 76  ? 1.4779 0.7067 1.0187 0.0605  0.1695  -0.0319 74  ASP C C   
4664 O O   . ASP C 76  ? 1.5441 0.7561 1.0359 0.0622  0.1974  -0.0455 74  ASP C O   
4665 C CB  . ASP C 76  ? 1.4620 0.7247 1.0357 0.0663  0.1075  -0.0262 74  ASP C CB  
4666 C CG  . ASP C 76  ? 1.4517 0.7280 0.9991 0.0700  0.0690  -0.0142 74  ASP C CG  
4667 O OD1 . ASP C 76  ? 1.4341 0.7169 0.9873 0.0661  0.0454  0.0013  74  ASP C OD1 
4668 O OD2 . ASP C 76  ? 1.5443 0.8232 1.0639 0.0760  0.0630  -0.0205 74  ASP C OD2 
4669 N N   . VAL C 77  ? 1.3988 0.6334 1.0118 0.0528  0.1763  -0.0266 75  VAL C N   
4670 C CA  . VAL C 77  ? 1.4127 0.6389 1.0567 0.0470  0.2221  -0.0372 75  VAL C CA  
4671 C C   . VAL C 77  ? 1.5696 0.7707 1.1375 0.0441  0.2451  -0.0308 75  VAL C C   
4672 O O   . VAL C 77  ? 1.6687 0.8571 1.2290 0.0387  0.2893  -0.0408 75  VAL C O   
4673 C CB  . VAL C 77  ? 1.2804 0.5220 1.0388 0.0389  0.2197  -0.0314 75  VAL C CB  
4674 C CG1 . VAL C 77  ? 1.5031 0.7365 1.2588 0.0327  0.2040  -0.0101 75  VAL C CG1 
4675 C CG2 . VAL C 77  ? 1.4533 0.6960 1.2716 0.0350  0.2702  -0.0493 75  VAL C CG2 
4676 N N   . LYS C 78  ? 1.5706 0.7629 1.0816 0.0470  0.2172  -0.0145 76  LYS C N   
4677 C CA  . LYS C 78  ? 1.5932 0.7595 1.0312 0.0445  0.2313  -0.0063 76  LYS C CA  
4678 C C   . LYS C 78  ? 1.6189 0.7689 0.9600 0.0518  0.2205  -0.0073 76  LYS C C   
4679 O O   . LYS C 78  ? 1.6186 0.7435 0.8944 0.0492  0.2284  0.0003  76  LYS C O   
4680 C CB  . LYS C 78  ? 1.6366 0.7998 1.0885 0.0419  0.2080  0.0127  76  LYS C CB  
4681 C CG  . LYS C 78  ? 1.6196 0.7933 1.1674 0.0324  0.2139  0.0178  76  LYS C CG  
4682 C CD  . LYS C 78  ? 1.6218 0.7949 1.2074 0.0244  0.2641  0.0074  76  LYS C CD  
4683 C CE  . LYS C 78  ? 1.6344 0.8204 1.3300 0.0152  0.2683  0.0142  76  LYS C CE  
4684 N NZ  . LYS C 78  ? 1.7557 0.9252 1.4472 0.0061  0.2787  0.0304  76  LYS C NZ  
4685 N N   . ASN C 79  ? 1.6782 0.8410 1.0131 0.0600  0.1998  -0.0146 77  ASN C N   
4686 C CA  . ASN C 79  ? 1.6825 0.8313 0.9369 0.0668  0.1862  -0.0150 77  ASN C CA  
4687 C C   . ASN C 79  ? 1.7255 0.8643 0.9346 0.0715  0.1618  0.0017  77  ASN C C   
4688 O O   . ASN C 79  ? 1.7469 0.8607 0.8859 0.0721  0.1617  0.0058  77  ASN C O   
4689 C CB  . ASN C 79  ? 1.7503 0.8705 0.9451 0.0610  0.2187  -0.0267 77  ASN C CB  
4690 C CG  . ASN C 79  ? 1.8426 0.9687 1.0542 0.0624  0.2296  -0.0473 77  ASN C CG  
4691 O OD1 . ASN C 79  ? 1.9394 1.0530 1.0973 0.0663  0.2170  -0.0527 77  ASN C OD1 
4692 N ND2 . ASN C 79  ? 1.8765 1.0201 1.1680 0.0592  0.2508  -0.0588 77  ASN C ND2 
4693 N N   . MET C 80  ? 1.5876 0.7428 0.8364 0.0740  0.1394  0.0110  78  MET C N   
4694 C CA  . MET C 80  ? 1.4130 0.5581 0.6279 0.0792  0.1189  0.0235  78  MET C CA  
4695 C C   . MET C 80  ? 1.4174 0.5852 0.6507 0.0870  0.0877  0.0265  78  MET C C   
4696 O O   . MET C 80  ? 1.4170 0.6064 0.7021 0.0839  0.0797  0.0243  78  MET C O   
4697 C CB  . MET C 80  ? 1.4115 0.5436 0.6455 0.0716  0.1278  0.0320  78  MET C CB  
4698 C CG  . MET C 80  ? 1.4815 0.5834 0.6672 0.0652  0.1502  0.0366  78  MET C CG  
4699 S SD  . MET C 80  ? 1.5773 0.6623 0.7815 0.0574  0.1515  0.0509  78  MET C SD  
4700 C CE  . MET C 80  ? 1.4158 0.5154 0.7014 0.0444  0.1823  0.0464  78  MET C CE  
4701 N N   . VAL C 81  ? 1.4729 0.6343 0.6642 0.0962  0.0705  0.0320  79  VAL C N   
4702 C CA  . VAL C 81  ? 1.4027 0.5831 0.6018 0.1035  0.0461  0.0345  79  VAL C CA  
4703 C C   . VAL C 81  ? 1.4107 0.5766 0.5975 0.1061  0.0374  0.0399  79  VAL C C   
4704 O O   . VAL C 81  ? 1.4618 0.6038 0.6156 0.1089  0.0417  0.0433  79  VAL C O   
4705 C CB  . VAL C 81  ? 1.3641 0.5527 0.5335 0.1137  0.0350  0.0338  79  VAL C CB  
4706 C CG1 . VAL C 81  ? 1.3066 0.5165 0.4853 0.1204  0.0158  0.0364  79  VAL C CG1 
4707 C CG2 . VAL C 81  ? 1.2227 0.4210 0.4023 0.1107  0.0409  0.0272  79  VAL C CG2 
4708 N N   . TYR C 82  ? 1.3997 0.5762 0.6101 0.1039  0.0234  0.0409  80  TYR C N   
4709 C CA  . TYR C 82  ? 1.3089 0.4679 0.5090 0.1048  0.0142  0.0432  80  TYR C CA  
4710 C C   . TYR C 82  ? 1.3060 0.4736 0.4843 0.1146  0.0000  0.0402  80  TYR C C   
4711 O O   . TYR C 82  ? 1.3298 0.5220 0.5143 0.1159  -0.0055 0.0390  80  TYR C O   
4712 C CB  . TYR C 82  ? 1.2354 0.3906 0.4755 0.0913  0.0087  0.0464  80  TYR C CB  
4713 C CG  . TYR C 82  ? 1.3129 0.4641 0.5893 0.0812  0.0266  0.0488  80  TYR C CG  
4714 C CD1 . TYR C 82  ? 1.3582 0.4879 0.6180 0.0806  0.0437  0.0518  80  TYR C CD1 
4715 C CD2 . TYR C 82  ? 1.2724 0.4410 0.6027 0.0716  0.0274  0.0485  80  TYR C CD2 
4716 C CE1 . TYR C 82  ? 1.3190 0.4463 0.6121 0.0703  0.0661  0.0533  80  TYR C CE1 
4717 C CE2 . TYR C 82  ? 1.3011 0.4678 0.6727 0.0634  0.0486  0.0483  80  TYR C CE2 
4718 C CZ  . TYR C 82  ? 1.3387 0.4856 0.6901 0.0627  0.0704  0.0502  80  TYR C CZ  
4719 O OH  . TYR C 82  ? 1.4501 0.5965 0.8428 0.0535  0.0972  0.0494  80  TYR C OH  
4720 N N   . LEU C 83  ? 1.4176 0.5642 0.5725 0.1212  -0.0046 0.0385  81  LEU C N   
4721 C CA  . LEU C 83  ? 1.4097 0.5596 0.5461 0.1298  -0.0136 0.0322  81  LEU C CA  
4722 C C   . LEU C 83  ? 1.3601 0.4823 0.4898 0.1254  -0.0220 0.0296  81  LEU C C   
4723 O O   . LEU C 83  ? 1.3195 0.4165 0.4361 0.1316  -0.0220 0.0287  81  LEU C O   
4724 C CB  . LEU C 83  ? 1.3653 0.5153 0.4813 0.1466  -0.0112 0.0292  81  LEU C CB  
4725 C CG  . LEU C 83  ? 1.3096 0.4652 0.4131 0.1580  -0.0140 0.0199  81  LEU C CG  
4726 C CD1 . LEU C 83  ? 1.3323 0.5076 0.4381 0.1491  -0.0164 0.0174  81  LEU C CD1 
4727 C CD2 . LEU C 83  ? 1.2793 0.4486 0.3832 0.1732  -0.0119 0.0196  81  LEU C CD2 
4728 N N   . GLN C 84  ? 1.3992 0.5229 0.5376 0.1132  -0.0325 0.0297  82  GLN C N   
4729 C CA  . GLN C 84  ? 1.3443 0.4375 0.4731 0.1066  -0.0454 0.0273  82  GLN C CA  
4730 C C   . GLN C 84  ? 1.3769 0.4611 0.4662 0.1169  -0.0476 0.0142  82  GLN C C   
4731 O O   . GLN C 84  ? 1.4199 0.5216 0.4949 0.1152  -0.0477 0.0102  82  GLN C O   
4732 C CB  . GLN C 84  ? 1.3486 0.4420 0.5024 0.0869  -0.0604 0.0344  82  GLN C CB  
4733 C CG  . GLN C 84  ? 1.5454 0.6024 0.6998 0.0765  -0.0777 0.0360  82  GLN C CG  
4734 C CD  . GLN C 84  ? 1.6726 0.7181 0.8089 0.0622  -0.1002 0.0351  82  GLN C CD  
4735 O OE1 . GLN C 84  ? 1.6132 0.6760 0.7246 0.0622  -0.0994 0.0312  82  GLN C OE1 
4736 N NE2 . GLN C 84  ? 1.6241 0.6382 0.7710 0.0481  -0.1217 0.0403  82  GLN C NE2 
4737 N N   . MET C 85  ? 1.4985 0.5548 0.5716 0.1270  -0.0481 0.0073  83  MET C N   
4738 C CA  . MET C 85  ? 1.5838 0.6272 0.6239 0.1387  -0.0471 -0.0090 83  MET C CA  
4739 C C   . MET C 85  ? 1.5363 0.5430 0.5550 0.1277  -0.0635 -0.0152 83  MET C C   
4740 O O   . MET C 85  ? 1.5577 0.5413 0.5931 0.1177  -0.0763 -0.0065 83  MET C O   
4741 C CB  . MET C 85  ? 1.5046 0.5371 0.5453 0.1578  -0.0408 -0.0139 83  MET C CB  
4742 C CG  . MET C 85  ? 1.4766 0.5292 0.5386 0.1626  -0.0331 -0.0015 83  MET C CG  
4743 S SD  . MET C 85  ? 1.4859 0.5422 0.5487 0.1858  -0.0277 -0.0072 83  MET C SD  
4744 C CE  . MET C 85  ? 1.6019 0.7039 0.6708 0.1908  -0.0163 -0.0105 83  MET C CE  
4745 N N   . ASN C 86  ? 1.5199 0.5193 0.5007 0.1283  -0.0629 -0.0300 84  ASN C N   
4746 C CA  . ASN C 86  ? 1.5563 0.5176 0.5055 0.1136  -0.0817 -0.0361 84  ASN C CA  
4747 C C   . ASN C 86  ? 1.7162 0.6438 0.6248 0.1260  -0.0785 -0.0596 84  ASN C C   
4748 O O   . ASN C 86  ? 1.8541 0.7390 0.7524 0.1220  -0.0961 -0.0638 84  ASN C O   
4749 C CB  . ASN C 86  ? 1.5450 0.5188 0.4741 0.0947  -0.0884 -0.0315 84  ASN C CB  
4750 C CG  . ASN C 86  ? 1.6149 0.5854 0.5767 0.0724  -0.1118 -0.0113 84  ASN C CG  
4751 O OD1 . ASN C 86  ? 1.5505 0.5046 0.5455 0.0698  -0.1221 -0.0029 84  ASN C OD1 
4752 N ND2 . ASN C 86  ? 1.5607 0.5474 0.5187 0.0555  -0.1204 -0.0024 84  ASN C ND2 
4753 N N   . SER C 87  ? 1.6957 0.6404 0.5844 0.1410  -0.0561 -0.0760 85  SER C N   
4754 C CA  . SER C 87  ? 1.6650 0.5798 0.5201 0.1553  -0.0474 -0.1028 85  SER C CA  
4755 C C   . SER C 87  ? 1.6857 0.6236 0.5737 0.1819  -0.0268 -0.1100 85  SER C C   
4756 O O   . SER C 87  ? 1.6748 0.6416 0.5613 0.1923  -0.0036 -0.1200 85  SER C O   
4757 C CB  . SER C 87  ? 1.6885 0.6089 0.5020 0.1441  -0.0377 -0.1144 85  SER C CB  
4758 O OG  . SER C 87  ? 1.8792 0.7823 0.6658 0.1167  -0.0609 -0.1017 85  SER C OG  
4759 N N   . LEU C 88  ? 1.6262 0.5502 0.5466 0.1915  -0.0370 -0.1033 86  LEU C N   
4760 C CA  . LEU C 88  ? 1.6064 0.5473 0.5615 0.2142  -0.0253 -0.1058 86  LEU C CA  
4761 C C   . LEU C 88  ? 1.6461 0.5696 0.5941 0.2328  -0.0139 -0.1339 86  LEU C C   
4762 O O   . LEU C 88  ? 1.6871 0.5822 0.6196 0.2282  -0.0237 -0.1452 86  LEU C O   
4763 C CB  . LEU C 88  ? 1.6945 0.6222 0.6809 0.2148  -0.0418 -0.0871 86  LEU C CB  
4764 C CG  . LEU C 88  ? 1.5528 0.5103 0.5612 0.2034  -0.0431 -0.0610 86  LEU C CG  
4765 C CD1 . LEU C 88  ? 1.5802 0.5246 0.5831 0.1808  -0.0565 -0.0480 86  LEU C CD1 
4766 C CD2 . LEU C 88  ? 1.8699 0.8246 0.9055 0.2124  -0.0478 -0.0480 86  LEU C CD2 
4767 N N   . LYS C 89  ? 1.6418 0.5923 0.6142 0.2520  0.0062  -0.1426 87  LYS C N   
4768 C CA  . LYS C 89  ? 1.6733 0.6250 0.6622 0.2703  0.0223  -0.1677 87  LYS C CA  
4769 C C   . LYS C 89  ? 1.7279 0.6848 0.7702 0.2938  0.0213  -0.1652 87  LYS C C   
4770 O O   . LYS C 89  ? 1.7712 0.7551 0.8386 0.2932  0.0173  -0.1431 87  LYS C O   
4771 C CB  . LYS C 89  ? 1.6894 0.6712 0.6592 0.2692  0.0530  -0.1834 87  LYS C CB  
4772 C CG  . LYS C 89  ? 1.6994 0.6947 0.6281 0.2437  0.0513  -0.1690 87  LYS C CG  
4773 C CD  . LYS C 89  ? 1.7400 0.7583 0.6420 0.2363  0.0785  -0.1836 87  LYS C CD  
4774 C CE  . LYS C 89  ? 1.7255 0.7832 0.6582 0.2544  0.1083  -0.1891 87  LYS C CE  
4775 N NZ  . LYS C 89  ? 1.7239 0.8057 0.6291 0.2439  0.1379  -0.2012 87  LYS C NZ  
4776 N N   . PRO C 90  ? 1.7607 0.7035 0.8338 0.3101  0.0212  -0.1831 88  PRO C N   
4777 C CA  . PRO C 90  ? 1.6783 0.6209 0.8094 0.3302  0.0116  -0.1773 88  PRO C CA  
4778 C C   . PRO C 90  ? 1.6423 0.6225 0.8070 0.3408  0.0233  -0.1668 88  PRO C C   
4779 O O   . PRO C 90  ? 1.7137 0.6975 0.9216 0.3477  0.0052  -0.1486 88  PRO C O   
4780 C CB  . PRO C 90  ? 1.7247 0.6578 0.8858 0.3463  0.0210  -0.2072 88  PRO C CB  
4781 C CG  . PRO C 90  ? 1.7612 0.6716 0.8734 0.3299  0.0190  -0.2204 88  PRO C CG  
4782 C CD  . PRO C 90  ? 1.7406 0.6592 0.7963 0.3068  0.0209  -0.2056 88  PRO C CD  
4783 N N   . GLU C 91  ? 1.6330 0.6495 0.7841 0.3371  0.0504  -0.1737 89  GLU C N   
4784 C CA  . GLU C 91  ? 1.5920 0.6570 0.7840 0.3415  0.0595  -0.1591 89  GLU C CA  
4785 C C   . GLU C 91  ? 1.5899 0.6695 0.7727 0.3235  0.0392  -0.1259 89  GLU C C   
4786 O O   . GLU C 91  ? 1.5097 0.6193 0.7292 0.3271  0.0356  -0.1096 89  GLU C O   
4787 C CB  . GLU C 91  ? 1.6009 0.7003 0.7805 0.3408  0.0954  -0.1749 89  GLU C CB  
4788 C CG  . GLU C 91  ? 1.8364 0.9211 1.0083 0.3549  0.1257  -0.2130 89  GLU C CG  
4789 C CD  . GLU C 91  ? 1.9043 0.9390 1.0183 0.3463  0.1181  -0.2310 89  GLU C CD  
4790 O OE1 . GLU C 91  ? 1.7815 0.8104 0.9061 0.3545  0.1355  -0.2590 89  GLU C OE1 
4791 O OE2 . GLU C 91  ? 1.8766 0.8926 0.9511 0.3258  0.0930  -0.2131 89  GLU C OE2 
4792 N N   . ASP C 92  ? 1.6077 0.6656 0.7447 0.3040  0.0262  -0.1166 90  ASP C N   
4793 C CA  . ASP C 92  ? 1.5824 0.6497 0.7127 0.2874  0.0099  -0.0885 90  ASP C CA  
4794 C C   . ASP C 92  ? 1.6395 0.6839 0.7901 0.2904  -0.0141 -0.0716 90  ASP C C   
4795 O O   . ASP C 92  ? 1.5648 0.6163 0.7106 0.2782  -0.0246 -0.0494 90  ASP C O   
4796 C CB  . ASP C 92  ? 1.6237 0.6764 0.7083 0.2655  0.0059  -0.0849 90  ASP C CB  
4797 C CG  . ASP C 92  ? 1.6722 0.7428 0.7279 0.2572  0.0243  -0.0971 90  ASP C CG  
4798 O OD1 . ASP C 92  ? 1.6723 0.7823 0.7419 0.2588  0.0387  -0.0942 90  ASP C OD1 
4799 O OD2 . ASP C 92  ? 1.5961 0.6389 0.6135 0.2473  0.0222  -0.1082 90  ASP C OD2 
4800 N N   . THR C 93  ? 1.7050 0.7199 0.8759 0.3051  -0.0232 -0.0817 91  THR C N   
4801 C CA  . THR C 93  ? 1.6124 0.6018 0.8007 0.3060  -0.0491 -0.0633 91  THR C CA  
4802 C C   . THR C 93  ? 1.5298 0.5439 0.7491 0.3102  -0.0565 -0.0460 91  THR C C   
4803 O O   . THR C 93  ? 1.5181 0.5505 0.7815 0.3278  -0.0513 -0.0550 91  THR C O   
4804 C CB  . THR C 93  ? 1.6515 0.6054 0.8644 0.3225  -0.0595 -0.0786 91  THR C CB  
4805 O OG1 . THR C 93  ? 1.6325 0.5560 0.8117 0.3161  -0.0585 -0.0924 91  THR C OG1 
4806 C CG2 . THR C 93  ? 1.5889 0.5159 0.8210 0.3215  -0.0900 -0.0558 91  THR C CG2 
4807 N N   . ALA C 94  ? 1.5999 0.6130 0.7977 0.2937  -0.0684 -0.0219 92  ALA C N   
4808 C CA  . ALA C 94  ? 1.5234 0.5518 0.7384 0.2935  -0.0804 -0.0035 92  ALA C CA  
4809 C C   . ALA C 94  ? 1.4799 0.4891 0.6548 0.2723  -0.0928 0.0194  92  ALA C C   
4810 O O   . ALA C 94  ? 1.4914 0.4762 0.6377 0.2606  -0.0925 0.0217  92  ALA C O   
4811 C CB  . ALA C 94  ? 1.6064 0.6821 0.8363 0.2966  -0.0624 -0.0083 92  ALA C CB  
4812 N N   . VAL C 95  ? 1.5944 0.6131 0.7674 0.2669  -0.1028 0.0359  93  VAL C N   
4813 C CA  . VAL C 95  ? 1.5437 0.5462 0.6732 0.2462  -0.1088 0.0547  93  VAL C CA  
4814 C C   . VAL C 95  ? 1.4390 0.4768 0.5569 0.2381  -0.0911 0.0526  93  VAL C C   
4815 O O   . VAL C 95  ? 1.4200 0.4863 0.5609 0.2455  -0.0916 0.0517  93  VAL C O   
4816 C CB  . VAL C 95  ? 1.5013 0.4904 0.6344 0.2399  -0.1356 0.0726  93  VAL C CB  
4817 C CG1 . VAL C 95  ? 1.5155 0.4941 0.6088 0.2123  -0.1362 0.0843  93  VAL C CG1 
4818 C CG2 . VAL C 95  ? 1.5284 0.5000 0.7023 0.2535  -0.1562 0.0715  93  VAL C CG2 
4819 N N   . TYR C 96  ? 1.4295 0.4653 0.5183 0.2227  -0.0770 0.0528  94  TYR C N   
4820 C CA  . TYR C 96  ? 1.4204 0.4881 0.5050 0.2148  -0.0608 0.0491  94  TYR C CA  
4821 C C   . TYR C 96  ? 1.4221 0.4838 0.4802 0.2011  -0.0636 0.0622  94  TYR C C   
4822 O O   . TYR C 96  ? 1.4155 0.4624 0.4562 0.1850  -0.0613 0.0665  94  TYR C O   
4823 C CB  . TYR C 96  ? 1.4028 0.4715 0.4807 0.2061  -0.0459 0.0409  94  TYR C CB  
4824 C CG  . TYR C 96  ? 1.6662 0.7393 0.7597 0.2175  -0.0420 0.0250  94  TYR C CG  
4825 C CD1 . TYR C 96  ? 1.7167 0.8208 0.8298 0.2285  -0.0349 0.0143  94  TYR C CD1 
4826 C CD2 . TYR C 96  ? 1.6287 0.6728 0.7152 0.2162  -0.0445 0.0201  94  TYR C CD2 
4827 C CE1 . TYR C 96  ? 1.6791 0.7838 0.7979 0.2376  -0.0271 -0.0027 94  TYR C CE1 
4828 C CE2 . TYR C 96  ? 1.6551 0.6976 0.7482 0.2260  -0.0408 0.0027  94  TYR C CE2 
4829 C CZ  . TYR C 96  ? 1.6749 0.7469 0.7809 0.2365  -0.0305 -0.0097 94  TYR C CZ  
4830 O OH  . TYR C 96  ? 1.7593 0.8264 0.8636 0.2449  -0.0227 -0.0294 94  TYR C OH  
4831 N N   . TYR C 97  ? 1.5038 0.5914 0.5720 0.2034  -0.0656 0.0629  95  TYR C N   
4832 C CA  . TYR C 97  ? 1.5237 0.6195 0.5799 0.1882  -0.0664 0.0665  95  TYR C CA  
4833 C C   . TYR C 97  ? 1.4520 0.5747 0.5133 0.1824  -0.0504 0.0604  95  TYR C C   
4834 O O   . TYR C 97  ? 1.4716 0.6170 0.5516 0.1912  -0.0458 0.0561  95  TYR C O   
4835 C CB  . TYR C 97  ? 1.5561 0.6567 0.6244 0.1938  -0.0880 0.0735  95  TYR C CB  
4836 C CG  . TYR C 97  ? 1.6009 0.6771 0.6758 0.1997  -0.1097 0.0814  95  TYR C CG  
4837 C CD1 . TYR C 97  ? 1.6444 0.6931 0.6950 0.1852  -0.1152 0.0865  95  TYR C CD1 
4838 C CD2 . TYR C 97  ? 1.6534 0.7340 0.7645 0.2199  -0.1246 0.0844  95  TYR C CD2 
4839 C CE1 . TYR C 97  ? 1.5650 0.5923 0.6264 0.1885  -0.1389 0.0953  95  TYR C CE1 
4840 C CE2 . TYR C 97  ? 1.7162 0.7759 0.8459 0.2255  -0.1469 0.0912  95  TYR C CE2 
4841 C CZ  . TYR C 97  ? 1.6742 0.7077 0.7782 0.2088  -0.1559 0.0972  95  TYR C CZ  
4842 O OH  . TYR C 97  ? 1.8183 0.8318 0.9447 0.2122  -0.1815 0.1057  95  TYR C OH  
4843 N N   . CYS C 98  ? 1.4908 0.6116 0.5384 0.1665  -0.0414 0.0591  96  CYS C N   
4844 C CA  . CYS C 98  ? 1.5238 0.6669 0.5808 0.1609  -0.0306 0.0542  96  CYS C CA  
4845 C C   . CYS C 98  ? 1.5034 0.6500 0.5546 0.1565  -0.0402 0.0553  96  CYS C C   
4846 O O   . CYS C 98  ? 1.5597 0.6822 0.5853 0.1486  -0.0459 0.0581  96  CYS C O   
4847 C CB  . CYS C 98  ? 1.5458 0.6772 0.5925 0.1484  -0.0106 0.0515  96  CYS C CB  
4848 S SG  . CYS C 98  ? 1.7554 0.8511 0.7639 0.1328  0.0003  0.0545  96  CYS C SG  
4849 N N   . ALA C 99  ? 1.3747 0.5483 0.4468 0.1603  -0.0441 0.0539  97  ALA C N   
4850 C CA  . ALA C 99  ? 1.4836 0.6598 0.5532 0.1578  -0.0581 0.0556  97  ALA C CA  
4851 C C   . ALA C 99  ? 1.4255 0.6139 0.4997 0.1519  -0.0498 0.0502  97  ALA C C   
4852 O O   . ALA C 99  ? 1.4424 0.6495 0.5360 0.1530  -0.0405 0.0486  97  ALA C O   
4853 C CB  . ALA C 99  ? 1.4638 0.6585 0.5598 0.1706  -0.0789 0.0633  97  ALA C CB  
4854 N N   . ALA C 100 ? 1.5055 0.6786 0.5585 0.1449  -0.0559 0.0479  98  ALA C N   
4855 C CA  . ALA C 100 ? 1.4111 0.5847 0.4593 0.1399  -0.0490 0.0415  98  ALA C CA  
4856 C C   . ALA C 100 ? 1.4695 0.6539 0.5292 0.1427  -0.0728 0.0446  98  ALA C C   
4857 O O   . ALA C 100 ? 1.3658 0.5448 0.4233 0.1441  -0.0930 0.0502  98  ALA C O   
4858 C CB  . ALA C 100 ? 1.3547 0.4914 0.3574 0.1280  -0.0295 0.0324  98  ALA C CB  
4859 N N   . LYS C 101 ? 1.4314 0.6335 0.5132 0.1418  -0.0725 0.0408  99  LYS C N   
4860 C CA  . LYS C 101 ? 1.3906 0.6033 0.4887 0.1429  -0.0959 0.0437  99  LYS C CA  
4861 C C   . LYS C 101 ? 1.4803 0.7026 0.6012 0.1359  -0.0880 0.0312  99  LYS C C   
4862 O O   . LYS C 101 ? 1.3888 0.6380 0.5505 0.1340  -0.0758 0.0288  99  LYS C O   
4863 C CB  . LYS C 101 ? 1.3755 0.6281 0.5218 0.1517  -0.1122 0.0573  99  LYS C CB  
4864 C CG  . LYS C 101 ? 1.4103 0.6638 0.5657 0.1547  -0.1416 0.0666  99  LYS C CG  
4865 C CD  . LYS C 101 ? 1.4474 0.7027 0.6133 0.1498  -0.1568 0.0641  99  LYS C CD  
4866 C CE  . LYS C 101 ? 1.5043 0.7770 0.7042 0.1530  -0.1875 0.0775  99  LYS C CE  
4867 N NZ  . LYS C 101 ? 1.5052 0.7549 0.6862 0.1518  -0.2024 0.0797  99  LYS C NZ  
4868 N N   . PHE C 102 ? 1.4547 0.6519 0.5501 0.1316  -0.0975 0.0232  100 PHE C N   
4869 C CA  . PHE C 102 ? 1.4086 0.6110 0.5291 0.1262  -0.0913 0.0086  100 PHE C CA  
4870 C C   . PHE C 102 ? 1.3678 0.6137 0.5534 0.1286  -0.1126 0.0182  100 PHE C C   
4871 O O   . PHE C 102 ? 1.4375 0.6931 0.6313 0.1325  -0.1393 0.0313  100 PHE C O   
4872 C CB  . PHE C 102 ? 1.4738 0.6323 0.5421 0.1210  -0.0965 -0.0048 100 PHE C CB  
4873 C CG  . PHE C 102 ? 1.3745 0.5350 0.4713 0.1171  -0.0915 -0.0230 100 PHE C CG  
4874 C CD1 . PHE C 102 ? 1.3679 0.5189 0.4682 0.1123  -0.0569 -0.0426 100 PHE C CD1 
4875 C CD2 . PHE C 102 ? 1.3704 0.5426 0.4974 0.1183  -0.1218 -0.0203 100 PHE C CD2 
4876 C CE1 . PHE C 102 ? 1.4537 0.6064 0.5896 0.1100  -0.0520 -0.0613 100 PHE C CE1 
4877 C CE2 . PHE C 102 ? 1.3598 0.5320 0.5179 0.1153  -0.1196 -0.0379 100 PHE C CE2 
4878 C CZ  . PHE C 102 ? 1.3920 0.5541 0.5556 0.1117  -0.0843 -0.0595 100 PHE C CZ  
4879 N N   . TYR C 103 ? 1.2026 0.4740 0.4374 0.1248  -0.1022 0.0137  101 TYR C N   
4880 C CA  . TYR C 103 ? 1.2434 0.5550 0.5387 0.1233  -0.1218 0.0250  101 TYR C CA  
4881 C C   . TYR C 103 ? 1.3367 0.6773 0.6432 0.1280  -0.1322 0.0455  101 TYR C C   
4882 O O   . TYR C 103 ? 1.2961 0.6648 0.6378 0.1274  -0.1526 0.0587  101 TYR C O   
4883 C CB  . TYR C 103 ? 1.3363 0.6431 0.6452 0.1217  -0.1459 0.0216  101 TYR C CB  
4884 C CG  . TYR C 103 ? 1.1805 0.4786 0.5159 0.1162  -0.1388 0.0026  101 TYR C CG  
4885 C CD1 . TYR C 103 ? 1.2011 0.4940 0.5464 0.1130  -0.1100 -0.0107 101 TYR C CD1 
4886 C CD2 . TYR C 103 ? 1.1786 0.4733 0.5358 0.1144  -0.1617 -0.0025 101 TYR C CD2 
4887 C CE1 . TYR C 103 ? 1.2202 0.5065 0.6014 0.1091  -0.1019 -0.0293 101 TYR C CE1 
4888 C CE2 . TYR C 103 ? 1.1857 0.4713 0.5737 0.1107  -0.1548 -0.0225 101 TYR C CE2 
4889 C CZ  . TYR C 103 ? 1.1844 0.4668 0.5868 0.1085  -0.1237 -0.0363 101 TYR C CZ  
4890 O OH  . TYR C 103 ? 1.1905 0.4654 0.6349 0.1059  -0.1153 -0.0573 101 TYR C OH  
4891 N N   . GLY C 104 ? 1.4379 0.7717 0.7167 0.1326  -0.1168 0.0478  102 GLY C N   
4892 C CA  . GLY C 104 ? 1.3296 0.6861 0.6163 0.1389  -0.1211 0.0625  102 GLY C CA  
4893 C C   . GLY C 104 ? 1.2667 0.6327 0.5551 0.1377  -0.1017 0.0624  102 GLY C C   
4894 O O   . GLY C 104 ? 1.2248 0.5929 0.5279 0.1296  -0.0925 0.0566  102 GLY C O   
4895 N N   . GLY C 105 ? 1.3144 0.6843 0.5911 0.1458  -0.0976 0.0684  103 GLY C N   
4896 C CA  . GLY C 105 ? 1.2550 0.6297 0.5275 0.1456  -0.0816 0.0673  103 GLY C CA  
4897 C C   . GLY C 105 ? 1.1260 0.5357 0.4238 0.1438  -0.0822 0.0766  103 GLY C C   
4898 O O   . GLY C 105 ? 1.0759 0.4883 0.3704 0.1379  -0.0724 0.0748  103 GLY C O   
4899 N N   . ASN C 106 ? 1.1392 0.5738 0.4605 0.1472  -0.0934 0.0870  104 ASN C N   
4900 C CA  . ASN C 106 ? 1.2104 0.6796 0.5532 0.1438  -0.0896 0.0965  104 ASN C CA  
4901 C C   . ASN C 106 ? 1.2354 0.7201 0.5919 0.1565  -0.0877 0.1025  104 ASN C C   
4902 O O   . ASN C 106 ? 1.2340 0.7520 0.6162 0.1539  -0.0844 0.1123  104 ASN C O   
4903 C CB  . ASN C 106 ? 1.2983 0.7921 0.6731 0.1302  -0.1045 0.1070  104 ASN C CB  
4904 C CG  . ASN C 106 ? 1.3024 0.8059 0.7038 0.1338  -0.1241 0.1151  104 ASN C CG  
4905 O OD1 . ASN C 106 ? 1.2200 0.6991 0.6082 0.1421  -0.1317 0.1092  104 ASN C OD1 
4906 N ND2 . ASN C 106 ? 1.2408 0.7775 0.6773 0.1257  -0.1344 0.1300  104 ASN C ND2 
4907 N N   . SER C 107 ? 1.1012 0.5623 0.4444 0.1691  -0.0898 0.0980  105 SER C N   
4908 C CA  . SER C 107 ? 1.1517 0.6242 0.5180 0.1824  -0.0911 0.1036  105 SER C CA  
4909 C C   . SER C 107 ? 1.2897 0.7474 0.6381 0.1930  -0.0732 0.0937  105 SER C C   
4910 O O   . SER C 107 ? 1.2923 0.7190 0.6041 0.1920  -0.0679 0.0841  105 SER C O   
4911 C CB  . SER C 107 ? 1.2048 0.6577 0.5752 0.1874  -0.1161 0.1091  105 SER C CB  
4912 O OG  . SER C 107 ? 1.3706 0.8374 0.7778 0.1993  -0.1226 0.1178  105 SER C OG  
4913 N N   . LYS C 108 ? 1.2968 0.7775 0.6760 0.2033  -0.0630 0.0958  106 LYS C N   
4914 C CA  . LYS C 108 ? 1.2051 0.6717 0.5775 0.2164  -0.0479 0.0851  106 LYS C CA  
4915 C C   . LYS C 108 ? 1.3119 0.7529 0.6937 0.2288  -0.0662 0.0879  106 LYS C C   
4916 O O   . LYS C 108 ? 1.2980 0.7101 0.6590 0.2360  -0.0625 0.0793  106 LYS C O   
4917 C CB  . LYS C 108 ? 1.1349 0.6367 0.5393 0.2223  -0.0245 0.0830  106 LYS C CB  
4918 C CG  . LYS C 108 ? 1.2381 0.7660 0.6317 0.2065  -0.0097 0.0849  106 LYS C CG  
4919 C CD  . LYS C 108 ? 1.1414 0.6470 0.4844 0.1996  0.0053  0.0710  106 LYS C CD  
4920 C CE  . LYS C 108 ? 1.2717 0.7997 0.6005 0.1823  0.0184  0.0742  106 LYS C CE  
4921 N NZ  . LYS C 108 ? 1.2609 0.7630 0.5435 0.1674  0.0143  0.0692  106 LYS C NZ  
4922 N N   . ARG C 109 ? 1.3651 0.8129 0.7769 0.2299  -0.0895 0.1012  107 ARG C N   
4923 C CA  . ARG C 109 ? 1.3488 0.7698 0.7710 0.2394  -0.1129 0.1072  107 ARG C CA  
4924 C C   . ARG C 109 ? 1.3245 0.6956 0.6855 0.2323  -0.1261 0.1040  107 ARG C C   
4925 O O   . ARG C 109 ? 1.3581 0.7206 0.6837 0.2196  -0.1254 0.1013  107 ARG C O   
4926 C CB  . ARG C 109 ? 1.3695 0.8063 0.8366 0.2394  -0.1395 0.1237  107 ARG C CB  
4927 C CG  . ARG C 109 ? 1.4178 0.9077 0.9504 0.2437  -0.1255 0.1301  107 ARG C CG  
4928 C CD  . ARG C 109 ? 1.4042 0.9120 0.9679 0.2358  -0.1504 0.1467  107 ARG C CD  
4929 N NE  . ARG C 109 ? 1.4360 0.9186 1.0193 0.2403  -0.1882 0.1588  107 ARG C NE  
4930 C CZ  . ARG C 109 ? 1.4757 0.9820 1.1305 0.2459  -0.2056 0.1745  107 ARG C CZ  
4931 N NH1 . ARG C 109 ? 1.5000 1.0592 1.2156 0.2482  -0.1844 0.1799  107 ARG C NH1 
4932 N NH2 . ARG C 109 ? 1.5037 0.9783 1.1691 0.2478  -0.2460 0.1863  107 ARG C NH2 
4933 N N   . PRO C 110 ? 1.3996 0.7368 0.7498 0.2394  -0.1374 0.1046  108 PRO C N   
4934 C CA  . PRO C 110 ? 1.4535 0.7415 0.7420 0.2299  -0.1498 0.1046  108 PRO C CA  
4935 C C   . PRO C 110 ? 1.4323 0.6997 0.7031 0.2208  -0.1796 0.1155  108 PRO C C   
4936 O O   . PRO C 110 ? 1.3567 0.6043 0.5836 0.2043  -0.1778 0.1077  108 PRO C O   
4937 C CB  . PRO C 110 ? 1.3116 0.5710 0.6005 0.2395  -0.1566 0.1053  108 PRO C CB  
4938 C CG  . PRO C 110 ? 1.2939 0.5896 0.6436 0.2555  -0.1397 0.0994  108 PRO C CG  
4939 C CD  . PRO C 110 ? 1.3258 0.6668 0.7200 0.2556  -0.1369 0.1045  108 PRO C CD  
4940 N N   . GLY C 111 ? 1.4836 0.7682 0.8031 0.2260  -0.2023 0.1277  109 GLY C N   
4941 C CA  . GLY C 111 ? 1.3398 0.6176 0.6574 0.2114  -0.2297 0.1329  109 GLY C CA  
4942 C C   . GLY C 111 ? 1.3222 0.6100 0.6175 0.1982  -0.2216 0.1249  109 GLY C C   
4943 O O   . GLY C 111 ? 1.4065 0.6762 0.6781 0.1836  -0.2372 0.1214  109 GLY C O   
4944 N N   . ASP C 112 ? 1.2940 0.6061 0.5947 0.2032  -0.1989 0.1219  110 ASP C N   
4945 C CA  . ASP C 112 ? 1.3767 0.6978 0.6629 0.1913  -0.1914 0.1143  110 ASP C CA  
4946 C C   . ASP C 112 ? 1.3404 0.6370 0.5751 0.1820  -0.1696 0.0983  110 ASP C C   
4947 O O   . ASP C 112 ? 1.2844 0.5904 0.5138 0.1764  -0.1563 0.0919  110 ASP C O   
4948 C CB  . ASP C 112 ? 1.4011 0.7698 0.7313 0.1941  -0.1775 0.1179  110 ASP C CB  
4949 C CG  . ASP C 112 ? 1.4286 0.8291 0.8190 0.1984  -0.1966 0.1334  110 ASP C CG  
4950 O OD1 . ASP C 112 ? 1.3502 0.7328 0.7408 0.1951  -0.2273 0.1413  110 ASP C OD1 
4951 O OD2 . ASP C 112 ? 1.4355 0.8773 0.8719 0.2040  -0.1804 0.1375  110 ASP C OD2 
4952 N N   . TYR C 113 ? 1.2997 0.5653 0.5017 0.1802  -0.1668 0.0937  111 TYR C N   
4953 C CA  . TYR C 113 ? 1.3152 0.5548 0.4711 0.1707  -0.1463 0.0807  111 TYR C CA  
4954 C C   . TYR C 113 ? 1.3854 0.5853 0.5021 0.1606  -0.1595 0.0792  111 TYR C C   
4955 O O   . TYR C 113 ? 1.4949 0.6824 0.6128 0.1635  -0.1724 0.0864  111 TYR C O   
4956 C CB  . TYR C 113 ? 1.3720 0.6132 0.5252 0.1774  -0.1248 0.0781  111 TYR C CB  
4957 C CG  . TYR C 113 ? 1.3623 0.6339 0.5379 0.1825  -0.1087 0.0774  111 TYR C CG  
4958 C CD1 . TYR C 113 ? 1.3720 0.6794 0.5918 0.1912  -0.1133 0.0847  111 TYR C CD1 
4959 C CD2 . TYR C 113 ? 1.3089 0.5783 0.4704 0.1751  -0.0880 0.0684  111 TYR C CD2 
4960 C CE1 . TYR C 113 ? 1.2686 0.6106 0.5132 0.1891  -0.0968 0.0813  111 TYR C CE1 
4961 C CE2 . TYR C 113 ? 1.3572 0.6581 0.5464 0.1741  -0.0765 0.0664  111 TYR C CE2 
4962 C CZ  . TYR C 113 ? 1.2901 0.6265 0.5166 0.1800  -0.0810 0.0727  111 TYR C CZ  
4963 O OH  . TYR C 113 ? 1.2191 0.5843 0.4656 0.1752  -0.0700 0.0715  111 TYR C OH  
4964 N N   . ALA C 114 ? 1.3998 0.5758 0.4789 0.1487  -0.1567 0.0703  112 ALA C N   
4965 C CA  . ALA C 114 ? 1.5587 0.6929 0.5932 0.1367  -0.1716 0.0695  112 ALA C CA  
4966 C C   . ALA C 114 ? 1.5593 0.6630 0.5521 0.1289  -0.1541 0.0659  112 ALA C C   
4967 O O   . ALA C 114 ? 1.5139 0.5926 0.4874 0.1228  -0.1711 0.0728  112 ALA C O   
4968 C CB  . ALA C 114 ? 1.4909 0.6039 0.4936 0.1274  -0.1745 0.0603  112 ALA C CB  
4969 N N   . TYR C 115 ? 1.5782 0.6830 0.5598 0.1277  -0.1224 0.0570  113 TYR C N   
4970 C CA  . TYR C 115 ? 1.5872 0.6640 0.5322 0.1183  -0.1032 0.0545  113 TYR C CA  
4971 C C   . TYR C 115 ? 1.5598 0.6539 0.5326 0.1277  -0.0958 0.0594  113 TYR C C   
4972 O O   . TYR C 115 ? 1.5114 0.6379 0.5225 0.1393  -0.0898 0.0588  113 TYR C O   
4973 C CB  . TYR C 115 ? 1.5822 0.6459 0.4995 0.1098  -0.0718 0.0423  113 TYR C CB  
4974 C CG  . TYR C 115 ? 1.7358 0.7725 0.6139 0.0996  -0.0739 0.0341  113 TYR C CG  
4975 C CD1 . TYR C 115 ? 1.9138 0.9411 0.7859 0.0987  -0.1066 0.0383  113 TYR C CD1 
4976 C CD2 . TYR C 115 ? 1.8371 0.8563 0.6854 0.0908  -0.0428 0.0213  113 TYR C CD2 
4977 C CE1 . TYR C 115 ? 1.9666 0.9639 0.7980 0.0891  -0.1102 0.0296  113 TYR C CE1 
4978 C CE2 . TYR C 115 ? 1.9295 0.9221 0.7398 0.0819  -0.0419 0.0108  113 TYR C CE2 
4979 C CZ  . TYR C 115 ? 1.9264 0.9059 0.7250 0.0811  -0.0768 0.0149  113 TYR C CZ  
4980 O OH  . TYR C 115 ? 1.7730 0.7216 0.5298 0.0719  -0.0776 0.0035  113 TYR C OH  
4981 N N   . TRP C 116 ? 1.5548 0.6240 0.5047 0.1216  -0.0975 0.0645  114 TRP C N   
4982 C CA  . TRP C 116 ? 1.4887 0.5653 0.4592 0.1304  -0.0948 0.0692  114 TRP C CA  
4983 C C   . TRP C 116 ? 1.5840 0.6340 0.5220 0.1186  -0.0756 0.0687  114 TRP C C   
4984 O O   . TRP C 116 ? 1.7191 0.7420 0.6156 0.1027  -0.0673 0.0673  114 TRP C O   
4985 C CB  . TRP C 116 ? 1.4646 0.5382 0.4525 0.1381  -0.1257 0.0807  114 TRP C CB  
4986 C CG  . TRP C 116 ? 1.4702 0.5738 0.5012 0.1522  -0.1421 0.0841  114 TRP C CG  
4987 C CD1 . TRP C 116 ? 1.4407 0.5464 0.4778 0.1495  -0.1646 0.0884  114 TRP C CD1 
4988 C CD2 . TRP C 116 ? 1.4673 0.6009 0.5408 0.1707  -0.1369 0.0847  114 TRP C CD2 
4989 N NE1 . TRP C 116 ? 1.4722 0.6115 0.5595 0.1650  -0.1734 0.0931  114 TRP C NE1 
4990 C CE2 . TRP C 116 ? 1.4837 0.6394 0.5911 0.1785  -0.1549 0.0908  114 TRP C CE2 
4991 C CE3 . TRP C 116 ? 1.5029 0.6434 0.5861 0.1808  -0.1188 0.0809  114 TRP C CE3 
4992 C CZ2 . TRP C 116 ? 1.3804 0.5652 0.5300 0.1965  -0.1520 0.0939  114 TRP C CZ2 
4993 C CZ3 . TRP C 116 ? 1.4808 0.6459 0.5988 0.1985  -0.1168 0.0822  114 TRP C CZ3 
4994 C CH2 . TRP C 116 ? 1.3260 0.5131 0.4761 0.2066  -0.1316 0.0890  114 TRP C CH2 
4995 N N   . GLY C 117 ? 1.5131 0.5692 0.4690 0.1261  -0.0682 0.0704  115 GLY C N   
4996 C CA  . GLY C 117 ? 1.4927 0.5250 0.4254 0.1161  -0.0542 0.0731  115 GLY C CA  
4997 C C   . GLY C 117 ? 1.5196 0.5341 0.4512 0.1180  -0.0770 0.0840  115 GLY C C   
4998 O O   . GLY C 117 ? 1.5996 0.6209 0.5531 0.1291  -0.1020 0.0887  115 GLY C O   
4999 N N   . GLN C 118 ? 1.5605 0.5510 0.4694 0.1067  -0.0685 0.0892  116 GLN C N   
5000 C CA  . GLN C 118 ? 1.5838 0.5532 0.4905 0.1058  -0.0918 0.1011  116 GLN C CA  
5001 C C   . GLN C 118 ? 1.6291 0.6094 0.5753 0.1250  -0.0991 0.1005  116 GLN C C   
5002 O O   . GLN C 118 ? 1.6684 0.6370 0.6285 0.1312  -0.1245 0.1087  116 GLN C O   
5003 C CB  . GLN C 118 ? 1.6324 0.5719 0.5009 0.0854  -0.0807 0.1089  116 GLN C CB  
5004 C CG  . GLN C 118 ? 1.6194 0.5579 0.5016 0.0876  -0.0648 0.1098  116 GLN C CG  
5005 C CD  . GLN C 118 ? 1.5943 0.5451 0.4772 0.0847  -0.0300 0.1006  116 GLN C CD  
5006 O OE1 . GLN C 118 ? 1.6384 0.6034 0.5189 0.0852  -0.0181 0.0916  116 GLN C OE1 
5007 N NE2 . GLN C 118 ? 1.5939 0.5378 0.4839 0.0814  -0.0158 0.1041  116 GLN C NE2 
5008 N N   . GLY C 119 ? 1.5863 0.5853 0.5508 0.1342  -0.0786 0.0910  117 GLY C N   
5009 C CA  . GLY C 119 ? 1.5344 0.5391 0.5293 0.1524  -0.0833 0.0877  117 GLY C CA  
5010 C C   . GLY C 119 ? 1.5887 0.5731 0.5812 0.1483  -0.0787 0.0904  117 GLY C C   
5011 O O   . GLY C 119 ? 1.6306 0.5918 0.6035 0.1339  -0.0845 0.1006  117 GLY C O   
5012 N N   . THR C 120 ? 1.4847 0.4759 0.4960 0.1596  -0.0699 0.0820  118 THR C N   
5013 C CA  . THR C 120 ? 1.4981 0.4703 0.5140 0.1574  -0.0691 0.0830  118 THR C CA  
5014 C C   . THR C 120 ? 1.5521 0.5199 0.5931 0.1789  -0.0815 0.0743  118 THR C C   
5015 O O   . THR C 120 ? 1.6483 0.6316 0.6998 0.1933  -0.0753 0.0638  118 THR C O   
5016 C CB  . THR C 120 ? 1.4959 0.4736 0.5102 0.1472  -0.0465 0.0797  118 THR C CB  
5017 O OG1 . THR C 120 ? 1.5156 0.4772 0.5428 0.1476  -0.0501 0.0790  118 THR C OG1 
5018 C CG2 . THR C 120 ? 1.5776 0.5812 0.6023 0.1556  -0.0359 0.0692  118 THR C CG2 
5019 N N   . GLN C 121 ? 1.6471 0.5923 0.6980 0.1808  -0.0981 0.0782  119 GLN C N   
5020 C CA  . GLN C 121 ? 1.5922 0.5292 0.6710 0.2022  -0.1092 0.0669  119 GLN C CA  
5021 C C   . GLN C 121 ? 1.5249 0.4549 0.6065 0.2040  -0.0991 0.0544  119 GLN C C   
5022 O O   . GLN C 121 ? 1.5334 0.4529 0.6079 0.1879  -0.0972 0.0611  119 GLN C O   
5023 C CB  . GLN C 121 ? 1.5646 0.4808 0.6610 0.2032  -0.1350 0.0759  119 GLN C CB  
5024 C CG  . GLN C 121 ? 1.5776 0.4804 0.7078 0.2221  -0.1444 0.0617  119 GLN C CG  
5025 C CD  . GLN C 121 ? 1.5772 0.4878 0.7440 0.2459  -0.1528 0.0524  119 GLN C CD  
5026 O OE1 . GLN C 121 ? 1.5864 0.4990 0.7668 0.2450  -0.1705 0.0653  119 GLN C OE1 
5027 N NE2 . GLN C 121 ? 1.5703 0.4854 0.7552 0.2662  -0.1394 0.0291  119 GLN C NE2 
5028 N N   . VAL C 122 ? 1.5158 0.4503 0.6076 0.2224  -0.0928 0.0362  120 VAL C N   
5029 C CA  . VAL C 122 ? 1.5201 0.4444 0.6110 0.2242  -0.0869 0.0209  120 VAL C CA  
5030 C C   . VAL C 122 ? 1.6108 0.5240 0.7241 0.2458  -0.0932 0.0015  120 VAL C C   
5031 O O   . VAL C 122 ? 1.6374 0.5715 0.7670 0.2616  -0.0855 -0.0103 120 VAL C O   
5032 C CB  . VAL C 122 ? 1.7258 0.6763 0.8057 0.2189  -0.0685 0.0123  120 VAL C CB  
5033 C CG1 . VAL C 122 ? 1.6412 0.5812 0.7177 0.2215  -0.0664 -0.0067 120 VAL C CG1 
5034 C CG2 . VAL C 122 ? 1.6791 0.6350 0.7454 0.1981  -0.0615 0.0286  120 VAL C CG2 
5035 N N   . THR C 123 ? 1.6377 0.5300 0.7617 0.2440  -0.1053 -0.0027 121 THR C N   
5036 C CA  . THR C 123 ? 1.6907 0.5720 0.8387 0.2630  -0.1094 -0.0250 121 THR C CA  
5037 C C   . THR C 123 ? 1.6066 0.4771 0.7363 0.2593  -0.1026 -0.0433 121 THR C C   
5038 O O   . THR C 123 ? 1.6072 0.4666 0.7237 0.2410  -0.1094 -0.0328 121 THR C O   
5039 C CB  . THR C 123 ? 1.6204 0.4833 0.7992 0.2638  -0.1335 -0.0161 121 THR C CB  
5040 O OG1 . THR C 123 ? 1.7499 0.6026 0.9144 0.2403  -0.1440 0.0067  121 THR C OG1 
5041 C CG2 . THR C 123 ? 1.6242 0.4957 0.8313 0.2744  -0.1436 -0.0067 121 THR C CG2 
5042 N N   . VAL C 124 ? 1.6200 0.4947 0.7496 0.2749  -0.0888 -0.0704 122 VAL C N   
5043 C CA  . VAL C 124 ? 1.6587 0.5207 0.7644 0.2703  -0.0840 -0.0901 122 VAL C CA  
5044 C C   . VAL C 124 ? 1.6821 0.5330 0.8114 0.2879  -0.0839 -0.1161 122 VAL C C   
5045 O O   . VAL C 124 ? 1.6849 0.5512 0.8419 0.3072  -0.0716 -0.1294 122 VAL C O   
5046 C CB  . VAL C 124 ? 1.8246 0.7042 0.8952 0.2656  -0.0632 -0.0993 122 VAL C CB  
5047 C CG1 . VAL C 124 ? 1.7886 0.6960 0.8720 0.2835  -0.0423 -0.1110 122 VAL C CG1 
5048 C CG2 . VAL C 124 ? 1.7329 0.5962 0.7738 0.2583  -0.0618 -0.1189 122 VAL C CG2 
5049 N N   . SER C 125 ? 1.7369 0.5611 0.8611 0.2813  -0.0980 -0.1234 123 SER C N   
5050 C CA  . SER C 125 ? 1.8860 0.6938 1.0388 0.2961  -0.1030 -0.1460 123 SER C CA  
5051 C C   . SER C 125 ? 1.8994 0.6969 1.0196 0.2961  -0.0895 -0.1760 123 SER C C   
5052 O O   . SER C 125 ? 1.9363 0.7378 1.0108 0.2826  -0.0802 -0.1763 123 SER C O   
5053 C CB  . SER C 125 ? 1.9793 0.7615 1.1555 0.2881  -0.1333 -0.1299 123 SER C CB  
5054 O OG  . SER C 125 ? 1.9470 0.7094 1.0927 0.2689  -0.1451 -0.1245 123 SER C OG  
5055 N N   . SER C 126 ? 2.0164 0.7989 1.1613 0.3099  -0.0897 -0.2012 124 SER C N   
5056 C CA  . SER C 126 ? 2.1410 0.9096 1.2552 0.3102  -0.0764 -0.2332 124 SER C CA  
5057 C C   . SER C 126 ? 2.1339 0.9305 1.2158 0.3112  -0.0417 -0.2485 124 SER C C   
5058 O O   . SER C 126 ? 2.1768 0.9954 1.2873 0.3294  -0.0155 -0.2688 124 SER C O   
5059 C CB  . SER C 126 ? 2.2195 0.9552 1.2922 0.2886  -0.1000 -0.2254 124 SER C CB  
5060 O OG  . SER C 126 ? 2.3282 1.0399 1.3776 0.2900  -0.0957 -0.2564 124 SER C OG  
# 
